data_1HL5
# 
_entry.id   1HL5 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   1HL5         
PDBE  EBI-12308    
WWPDB D_1290012308 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
_pdbx_database_related.details 
PDB 1AZV unspecified 'FAMILIAL ALS MUTANT G37R CUZNSOD (HUMAN)' 
PDB 1BA9 unspecified 'THE SOLUTION STRUCTURE OF REDUCED MONOMERIC SUPEROXIDE DISMUTASE, NMR, 36 STRUCTURES' 
PDB 1DSW unspecified 
;THE SOLUTION STRUCTURE OF A MONOMERIC, REDUCED FORM OFHUMAN COPPER, ZINC SUPEROXIDE DISMUTASE BEARING THE SAMECHARGE AS THE NATIVE PROTEIN
;
PDB 1FUN unspecified 
'SUPEROXIDE DISMUTASE MUTANT WITH LYS 136 REPLACED BY GLU, CYS 6 REPLACED BY ALA AND CYS 111 REPLACED BY SER (K136E, C6A, C111S)' 
PDB 1HL4 unspecified 'THE STRUCTURE OF APO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE' 
PDB 1KMG unspecified 'THE SOLUTION STRUCTURE OF MONOMERIC COPPER- FREE SUPEROXIDEDISMUTASE' 
PDB 1L3N unspecified 'THE SOLUTION STRUCTURE OF REDUCED DIMERIC COPPER ZINC SOD:THE STRUCTURAL EFFECTS OF DIMERIZATION' 
PDB 1MFM unspecified 'MONOMERIC HUMAN SOD MUTANT F50E/G51E/E133Q AT ATOMIC RESOLUTION' 
PDB 1N18 unspecified 'THERMOSTABLE MUTANT OF HUMAN SUPEROXIDE DISMUTASE, C6A,C111S' 
PDB 1N19 unspecified 'STRUCTURE OF THE HSOD A4V MUTANT' 
PDB 1SOS unspecified 'SUPEROXIDE DISMUTASE MUTANT WITH CYS 6 REPLACED BY ALA AND CYS 111 REPLACED BY SER (C6A, C111S)' 
PDB 1SPD unspecified 'SUPEROXIDE DISMUTASE' 
PDB 4SOD unspecified 
;CU,ZN SUPEROXIDE DISMUTASE MUTANT WITH CYS 6 REPLACED BY ALA AND CYS 111 REPLACED BY SER (C6A,C111S) WITH AN 18-RESIDUE HEPARIN-BINDING PEPTIDE FUSED TO THE C- TERMINUS (THEORETICAL MODEL)
;
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1HL5 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.recvd_initial_deposition_date   2003-03-13 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Strange, R.W.'   1 
'Antonyuk, S.'    2 
'Hough, M.A.'     3 
'Doucette, P.'    4 
'Rodriguez, J.'   5 
'Hart, P.J.'      6 
'Hayward, L.J.'   7 
'Valentine, J.S.' 8 
'Hasnain, S.S.'   9 
# 
_citation.id                        primary 
_citation.title                     
;The Structure of Holo and Metal-Deficient Wild-Type Human Cu, Zn Superoxide Dismutase and its Relevance to Familial Amyotrophic Lateral Sclerosis
;
_citation.journal_abbrev            J.Mol.Biol. 
_citation.journal_volume            328 
_citation.page_first                877 
_citation.page_last                 ? 
_citation.year                      2003 
_citation.journal_id_ASTM           JMOBAK 
_citation.country                   UK 
_citation.journal_id_ISSN           0022-2836 
_citation.journal_id_CSD            0070 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   12729761 
_citation.pdbx_database_id_DOI      '10.1016/S0022-2836(03)00355-3' 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Strange, R.W.'   1 
primary 'Antonyuk, S.'    2 
primary 'Hough, M.A.'     3 
primary 'Doucette, P.'    4 
primary 'Rodriguez, J.'   5 
primary 'Hart, P.J.'      6 
primary 'Hayward, L.J.'   7 
primary 'Valentine, J.S.' 8 
primary 'Hasnain, S.S.'   9 
# 
_cell.entry_id           1HL5 
_cell.length_a           76.871 
_cell.length_b           172.380 
_cell.length_c           112.450 
_cell.angle_alpha        90.00 
_cell.angle_beta         93.45 
_cell.angle_gamma        90.00 
_cell.Z_PDB              36 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1HL5 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'SUPEROXIDE DISMUTASE' 15827.561 18   1.15.1.1 ? ? ? 
2 non-polymer syn 'COPPER (II) ION'      63.546    18   ?        ? ? ? 
3 non-polymer syn 'ZINC ION'             65.409    18   ?        ? ? ? 
4 non-polymer syn 'CALCIUM ION'          40.078    3    ?        ? ? ? 
5 water       nat water                  18.015    1763 ?        ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,S 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   THR n 
1 3   LYS n 
1 4   ALA n 
1 5   VAL n 
1 6   CYS n 
1 7   VAL n 
1 8   LEU n 
1 9   LYS n 
1 10  GLY n 
1 11  ASP n 
1 12  GLY n 
1 13  PRO n 
1 14  VAL n 
1 15  GLN n 
1 16  GLY n 
1 17  ILE n 
1 18  ILE n 
1 19  ASN n 
1 20  PHE n 
1 21  GLU n 
1 22  GLN n 
1 23  LYS n 
1 24  GLU n 
1 25  SER n 
1 26  ASN n 
1 27  GLY n 
1 28  PRO n 
1 29  VAL n 
1 30  LYS n 
1 31  VAL n 
1 32  TRP n 
1 33  GLY n 
1 34  SER n 
1 35  ILE n 
1 36  LYS n 
1 37  GLY n 
1 38  LEU n 
1 39  THR n 
1 40  GLU n 
1 41  GLY n 
1 42  LEU n 
1 43  HIS n 
1 44  GLY n 
1 45  PHE n 
1 46  HIS n 
1 47  VAL n 
1 48  HIS n 
1 49  GLU n 
1 50  PHE n 
1 51  GLY n 
1 52  ASP n 
1 53  ASN n 
1 54  THR n 
1 55  ALA n 
1 56  GLY n 
1 57  CYS n 
1 58  THR n 
1 59  SER n 
1 60  ALA n 
1 61  GLY n 
1 62  PRO n 
1 63  HIS n 
1 64  PHE n 
1 65  ASN n 
1 66  PRO n 
1 67  LEU n 
1 68  SER n 
1 69  ARG n 
1 70  LYS n 
1 71  HIS n 
1 72  GLY n 
1 73  GLY n 
1 74  PRO n 
1 75  LYS n 
1 76  ASP n 
1 77  GLU n 
1 78  GLU n 
1 79  ARG n 
1 80  HIS n 
1 81  VAL n 
1 82  GLY n 
1 83  ASP n 
1 84  LEU n 
1 85  GLY n 
1 86  ASN n 
1 87  VAL n 
1 88  THR n 
1 89  ALA n 
1 90  ASP n 
1 91  LYS n 
1 92  ASP n 
1 93  GLY n 
1 94  VAL n 
1 95  ALA n 
1 96  ASP n 
1 97  VAL n 
1 98  SER n 
1 99  ILE n 
1 100 GLU n 
1 101 ASP n 
1 102 SER n 
1 103 VAL n 
1 104 ILE n 
1 105 SER n 
1 106 LEU n 
1 107 SER n 
1 108 GLY n 
1 109 ASP n 
1 110 HIS n 
1 111 CYS n 
1 112 ILE n 
1 113 ILE n 
1 114 GLY n 
1 115 ARG n 
1 116 THR n 
1 117 LEU n 
1 118 VAL n 
1 119 VAL n 
1 120 HIS n 
1 121 GLU n 
1 122 LYS n 
1 123 ALA n 
1 124 ASP n 
1 125 ASP n 
1 126 LEU n 
1 127 GLY n 
1 128 LYS n 
1 129 GLY n 
1 130 GLY n 
1 131 ASN n 
1 132 GLU n 
1 133 GLU n 
1 134 SER n 
1 135 THR n 
1 136 LYS n 
1 137 THR n 
1 138 GLY n 
1 139 ASN n 
1 140 ALA n 
1 141 GLY n 
1 142 SER n 
1 143 ARG n 
1 144 LEU n 
1 145 ALA n 
1 146 CYS n 
1 147 GLY n 
1 148 VAL n 
1 149 ILE n 
1 150 GLY n 
1 151 ILE n 
1 152 ALA n 
1 153 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               HUMAN 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'HOMO SAPIENS' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'SACCHAROMYCES CEREVISIAE' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     4932 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               EG118 
_entity_src_gen.pdbx_host_org_variant              YEP351 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SODC_HUMAN 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           ? 
_struct_ref.pdbx_db_accession          P00441 
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1  1 1HL5 A 1 ? 153 ? P00441 2 ? 154 ? 1 153 
2  1 1HL5 B 1 ? 153 ? P00441 2 ? 154 ? 1 153 
3  1 1HL5 C 1 ? 153 ? P00441 2 ? 154 ? 1 153 
4  1 1HL5 D 1 ? 153 ? P00441 2 ? 154 ? 1 153 
5  1 1HL5 E 1 ? 153 ? P00441 2 ? 154 ? 1 153 
6  1 1HL5 F 1 ? 153 ? P00441 2 ? 154 ? 1 153 
7  1 1HL5 G 1 ? 153 ? P00441 2 ? 154 ? 1 153 
8  1 1HL5 H 1 ? 153 ? P00441 2 ? 154 ? 1 153 
9  1 1HL5 I 1 ? 153 ? P00441 2 ? 154 ? 1 153 
10 1 1HL5 J 1 ? 153 ? P00441 2 ? 154 ? 1 153 
11 1 1HL5 K 1 ? 153 ? P00441 2 ? 154 ? 1 153 
12 1 1HL5 L 1 ? 153 ? P00441 2 ? 154 ? 1 153 
13 1 1HL5 M 1 ? 153 ? P00441 2 ? 154 ? 1 153 
14 1 1HL5 N 1 ? 153 ? P00441 2 ? 154 ? 1 153 
15 1 1HL5 O 1 ? 153 ? P00441 2 ? 154 ? 1 153 
16 1 1HL5 P 1 ? 153 ? P00441 2 ? 154 ? 1 153 
17 1 1HL5 Q 1 ? 153 ? P00441 2 ? 154 ? 1 153 
18 1 1HL5 S 1 ? 153 ? P00441 2 ? 154 ? 1 153 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE           ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE          ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE        ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'   ? 'C4 H7 N O4'     133.103 
CA  non-polymer         . 'CALCIUM ION'     ? 'Ca 2'           40.078  
CU  non-polymer         . 'COPPER (II) ION' ? 'Cu 2'           63.546  
CYS 'L-peptide linking' y CYSTEINE          ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE         ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'   ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE           ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE         ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER             ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE        ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE           ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE            ? 'C6 H15 N2 O2 1' 147.195 
PHE 'L-peptide linking' y PHENYLALANINE     ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE           ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE            ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE         ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN        ? 'C11 H12 N2 O2'  204.225 
VAL 'L-peptide linking' y VALINE            ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'        ? 'Zn 2'           65.409  
# 
_exptl.entry_id          1HL5 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.6 
_exptl_crystal.density_percent_sol   52.2 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              8.00 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    '0.2 M CA ACETATE, 15% PEG 3350, 0.1 M TRIS PH 8.0' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100.0 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC CCD' 
_diffrn_detector.pdbx_collection_date   2002-01-15 
_diffrn_detector.details                MIRRORS 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'SI 111' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SRS BEAMLINE PX14.2' 
_diffrn_source.pdbx_synchrotron_site       SRS 
_diffrn_source.pdbx_synchrotron_beamline   PX14.2 
_diffrn_source.pdbx_wavelength             0.97 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     1HL5 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             50.000 
_reflns.d_resolution_high            1.800 
_reflns.number_obs                   265996 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         98.6 
_reflns.pdbx_Rmerge_I_obs            0.05200 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        20.0000 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              3.400 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             1.80 
_reflns_shell.d_res_low              1.86 
_reflns_shell.percent_possible_all   96.3 
_reflns_shell.Rmerge_I_obs           0.35000 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    2.700 
_reflns_shell.pdbx_redundancy        3.00 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 1HL5 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               'LIKELY RESIDUAL' 
_refine.ls_number_reflns_obs                     252571 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             50.00 
_refine.ls_d_res_high                            1.80 
_refine.ls_percent_reflns_obs                    98.5 
_refine.ls_R_factor_obs                          0.187 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.185 
_refine.ls_R_factor_R_free                       0.222 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.000 
_refine.ls_number_reflns_R_free                  13373 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.957 
_refine.correlation_coeff_Fo_to_Fc_free          0.942 
_refine.B_iso_mean                               20.08 
_refine.aniso_B[1][1]                            0.30000 
_refine.aniso_B[2][2]                            -0.20000 
_refine.aniso_B[3][3]                            -0.13000 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.30000 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    'BABINET MODEL WITH MASK' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.40 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'DISORDERED REGIONS IN MONOMERS O AND G WERE MODELED STEREOCHEMICALLY' 
_refine.pdbx_starting_model                      'PDB ENTRY 1SOS' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.125 
_refine.pdbx_overall_ESU_R_Free                  0.120 
_refine.overall_SU_ML                            0.086 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             2.732 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        19783 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         39 
_refine_hist.number_atoms_solvent             1763 
_refine_hist.number_atoms_total               21585 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        50.00 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.014  0.021  ? 20321 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.604  1.945  ? 27413 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       4.679  3.000  ? 2736  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       18.312 15.000 ? 3480  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.128  0.200  ? 3024  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.006  0.020  ? 15516 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbd_refined                0.221  0.300  ? 9366  'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        0.164  0.500  ? 2918  'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          0.086  0.500  ? 65    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       0.410  0.300  ? 121   'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     0.282  0.500  ? 62    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_mcbond_it                  0.835  1.500  ? 13410 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_mcangle_it                 1.537  2.000  ? 21294 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scbond_it                  2.558  3.000  ? 6911  'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scangle_it                 4.276  4.500  ? 6119  'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_long_range_B_other         ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.80 
_refine_ls_shell.d_res_low                        1.84 
_refine_ls_shell.number_reflns_R_work             17869 
_refine_ls_shell.R_factor_R_work                  0.2480 
_refine_ls_shell.percent_reflns_obs               ? 
_refine_ls_shell.R_factor_R_free                  0.2880 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             969 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
loop_
_struct_ncs_oper.id 
_struct_ncs_oper.code 
_struct_ncs_oper.details 
_struct_ncs_oper.matrix[1][1] 
_struct_ncs_oper.matrix[1][2] 
_struct_ncs_oper.matrix[1][3] 
_struct_ncs_oper.matrix[2][1] 
_struct_ncs_oper.matrix[2][2] 
_struct_ncs_oper.matrix[2][3] 
_struct_ncs_oper.matrix[3][1] 
_struct_ncs_oper.matrix[3][2] 
_struct_ncs_oper.matrix[3][3] 
_struct_ncs_oper.vector[1] 
_struct_ncs_oper.vector[2] 
_struct_ncs_oper.vector[3] 
1  given ? 0.895050  -0.368850 0.250680  -0.372240 -0.927450 -0.035590 0.245620  -0.061460 -0.967420 3.40235   183.62323 171.62170 
2  given ? -0.986350 0.057530  -0.154280 -0.057730 -0.998330 -0.003230 -0.154210 0.005720  0.988020  41.97392  173.66074 59.29191  
3  given ? -0.915130 0.389020  0.105830  0.392310  0.919760  0.011510  -0.092860 0.052050  -0.994320 4.91064   4.10431   115.60555 
4  given ? 0.956450  -0.194120 -0.218000 -0.084730 0.530050  -0.843720 0.279340  0.825450  0.490520  23.65226  71.57378  -10.01044 
5  given ? 0.957930  -0.190040 0.215050  -0.280800 -0.465950 0.839070  -0.059250 -0.864160 -0.499710 8.83297   110.49805 183.51767 
6  given ? -0.925350 0.224510  -0.305480 0.146330  -0.531820 -0.834120 -0.349720 -0.816560 0.459270  46.64627  204.50653 120.70108 
7  given ? -0.964170 0.227780  0.135960  0.228470  0.452630  0.861930  0.134790  0.862120  -0.488450 8.10633   -27.88937 56.90441  
8  given ? 0.911560  -0.356640 -0.204620 -0.350000 -0.411870 -0.841350 0.215780  0.838550  -0.500260 53.72966  211.35992 -2.85196  
9  given ? 0.999010  0.029030  -0.033620 0.015690  0.477480  0.878500  0.041560  -0.878160 0.476560  -13.08864 -33.34248 175.54706 
10 given ? 0.977310  -0.039520 0.208080  0.163110  -0.486220 -0.858480 0.135100  0.872940  -0.468740 22.31427  242.66022 31.64304  
11 given ? 0.862630  0.368500  0.346530  -0.487130 0.420620  0.765360  0.136280  -0.829030 0.542350  -44.52737 -52.29001 133.84116 
12 given ? -0.932870 0.360180  0.005670  0.191420  0.508970  -0.839230 -0.305160 -0.781810 -0.543740 1.61367   66.00793  231.29517 
13 given ? -0.983110 -0.024850 0.181300  0.163560  -0.563660 0.809650  0.082070  0.825630  0.558210  43.37927  111.04368 -56.49068 
14 given ? -0.915630 -0.365090 -0.168290 0.054550  -0.527580 0.847750  -0.398290 0.767050  0.502990  137.16948 60.40010  -44.98087 
15 given ? -0.950280 0.006510  -0.311320 0.257450  0.578810  -0.773760 0.175150  -0.815440 -0.551710 107.06050 86.02035  243.48880 
16 given ? 0.539870  0.661280  0.520810  -0.544850 -0.197090 0.815040  0.641620  -0.723780 0.253890  -87.03172 116.28680 146.14423 
17 given ? 0.844560  0.480970  0.235360  0.284100  -0.029920 -0.958330 -0.453880 0.876230  -0.161910 -70.59261 101.88297 1.33548   
# 
_struct.entry_id                  1HL5 
_struct.title                     'The Structure of Holo Type Human Cu, Zn Superoxide Dismutase' 
_struct.pdbx_descriptor           'SUPEROXIDE DISMUTASE (E.C.1.15.1.1)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1HL5 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            
'OXIDOREDUCTASE, HUMAN CU, ZN SUPEROXIDE DISMUTASE, ANTIOXIDANT, METAL-BINDING, AMYOTROPHIC LATERAL SCLEROSIS, DISEASE MUTATION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 1 ? 
D  N N 1 ? 
E  N N 1 ? 
F  N N 1 ? 
G  N N 1 ? 
H  N N 1 ? 
I  N N 1 ? 
J  N N 1 ? 
K  N N 1 ? 
L  N N 1 ? 
M  N N 1 ? 
N  N N 1 ? 
O  N N 1 ? 
P  N N 1 ? 
Q  N N 1 ? 
R  N N 1 ? 
S  N N 2 ? 
T  N N 3 ? 
U  N N 2 ? 
V  N N 3 ? 
W  N N 2 ? 
X  N N 3 ? 
Y  N N 4 ? 
Z  N N 2 ? 
AA N N 3 ? 
BA N N 4 ? 
CA N N 2 ? 
DA N N 3 ? 
EA N N 2 ? 
FA N N 3 ? 
GA N N 2 ? 
HA N N 3 ? 
IA N N 2 ? 
JA N N 3 ? 
KA N N 2 ? 
LA N N 3 ? 
MA N N 2 ? 
NA N N 3 ? 
OA N N 2 ? 
PA N N 3 ? 
QA N N 2 ? 
RA N N 3 ? 
SA N N 2 ? 
TA N N 3 ? 
UA N N 2 ? 
VA N N 3 ? 
WA N N 2 ? 
XA N N 3 ? 
YA N N 4 ? 
ZA N N 2 ? 
AB N N 3 ? 
BB N N 2 ? 
CB N N 3 ? 
DB N N 2 ? 
EB N N 3 ? 
FB N N 5 ? 
GB N N 5 ? 
HB N N 5 ? 
IB N N 5 ? 
JB N N 5 ? 
KB N N 5 ? 
LB N N 5 ? 
MB N N 5 ? 
NB N N 5 ? 
OB N N 5 ? 
PB N N 5 ? 
QB N N 5 ? 
RB N N 5 ? 
SB N N 5 ? 
TB N N 5 ? 
UB N N 5 ? 
VB N N 5 ? 
WB N N 5 ? 
# 
_struct_biol.id   1 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  ALA A 55  ? GLY A 61  ? ALA A 55  GLY A 61  5 ? 7 
HELX_P HELX_P2  2  GLU A 133 ? GLY A 138 ? GLU A 133 GLY A 138 1 ? 6 
HELX_P HELX_P3  3  ALA B 55  ? ALA B 60  ? ALA B 55  ALA B 60  5 ? 6 
HELX_P HELX_P4  4  GLU B 133 ? GLY B 138 ? GLU B 133 GLY B 138 1 ? 6 
HELX_P HELX_P5  5  ALA C 55  ? GLY C 61  ? ALA C 55  GLY C 61  5 ? 7 
HELX_P HELX_P6  6  GLU C 133 ? GLY C 138 ? GLU C 133 GLY C 138 1 ? 6 
HELX_P HELX_P7  7  ALA D 55  ? GLY D 61  ? ALA D 55  GLY D 61  5 ? 7 
HELX_P HELX_P8  8  GLU D 133 ? GLY D 138 ? GLU D 133 GLY D 138 1 ? 6 
HELX_P HELX_P9  9  ALA E 55  ? GLY E 61  ? ALA E 55  GLY E 61  5 ? 7 
HELX_P HELX_P10 10 GLU E 133 ? GLY E 138 ? GLU E 133 GLY E 138 1 ? 6 
HELX_P HELX_P11 11 ALA F 55  ? GLY F 61  ? ALA F 55  GLY F 61  5 ? 7 
HELX_P HELX_P12 12 GLU F 133 ? GLY F 138 ? GLU F 133 GLY F 138 1 ? 6 
HELX_P HELX_P13 13 ALA G 55  ? GLY G 61  ? ALA G 55  GLY G 61  5 ? 7 
HELX_P HELX_P14 14 SER G 107 ? HIS G 110 ? SER G 107 HIS G 110 5 ? 4 
HELX_P HELX_P15 15 ASN G 131 ? THR G 137 ? ASN G 131 THR G 137 1 ? 7 
HELX_P HELX_P16 16 ALA H 55  ? GLY H 61  ? ALA H 55  GLY H 61  5 ? 7 
HELX_P HELX_P17 17 SER H 107 ? HIS H 110 ? SER H 107 HIS H 110 5 ? 4 
HELX_P HELX_P18 18 GLU H 133 ? GLY H 138 ? GLU H 133 GLY H 138 1 ? 6 
HELX_P HELX_P19 19 ALA I 55  ? GLY I 61  ? ALA I 55  GLY I 61  5 ? 7 
HELX_P HELX_P20 20 GLU I 133 ? GLY I 138 ? GLU I 133 GLY I 138 1 ? 6 
HELX_P HELX_P21 21 ALA J 55  ? GLY J 61  ? ALA J 55  GLY J 61  5 ? 7 
HELX_P HELX_P22 22 SER J 107 ? HIS J 110 ? SER J 107 HIS J 110 5 ? 4 
HELX_P HELX_P23 23 GLU J 133 ? GLY J 138 ? GLU J 133 GLY J 138 1 ? 6 
HELX_P HELX_P24 24 ALA K 55  ? GLY K 61  ? ALA K 55  GLY K 61  5 ? 7 
HELX_P HELX_P25 25 GLU K 133 ? GLY K 138 ? GLU K 133 GLY K 138 1 ? 6 
HELX_P HELX_P26 26 ALA L 55  ? GLY L 61  ? ALA L 55  GLY L 61  5 ? 7 
HELX_P HELX_P27 27 GLU L 133 ? GLY L 138 ? GLU L 133 GLY L 138 1 ? 6 
HELX_P HELX_P28 28 GLY M 56  ? GLY M 61  ? GLY M 56  GLY M 61  5 ? 6 
HELX_P HELX_P29 29 GLU M 133 ? GLY M 138 ? GLU M 133 GLY M 138 1 ? 6 
HELX_P HELX_P30 30 ALA N 55  ? GLY N 61  ? ALA N 55  GLY N 61  5 ? 7 
HELX_P HELX_P31 31 GLU N 133 ? GLY N 138 ? GLU N 133 GLY N 138 1 ? 6 
HELX_P HELX_P32 32 ALA O 55  ? GLY O 61  ? ALA O 55  GLY O 61  5 ? 7 
HELX_P HELX_P33 33 GLU O 133 ? GLY O 138 ? GLU O 133 GLY O 138 1 ? 6 
HELX_P HELX_P34 34 ALA P 55  ? GLY P 61  ? ALA P 55  GLY P 61  5 ? 7 
HELX_P HELX_P35 35 GLU P 133 ? GLY P 138 ? GLU P 133 GLY P 138 1 ? 6 
HELX_P HELX_P36 36 ALA Q 55  ? GLY Q 61  ? ALA Q 55  GLY Q 61  5 ? 7 
HELX_P HELX_P37 37 GLU Q 133 ? GLY Q 138 ? GLU Q 133 GLY Q 138 1 ? 6 
HELX_P HELX_P38 38 ALA R 55  ? GLY R 61  ? ALA S 55  GLY S 61  5 ? 7 
HELX_P HELX_P39 39 GLU R 133 ? GLY R 138 ? GLU S 133 GLY S 138 1 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1   disulf ? ? A  CYS 57 SG ? ? ? 1_555 A  CYS 146 SG  ? ? A CYS 57  A CYS 146  1_555 ? ? ? ? ? ? ? 2.129 ? 
disulf2   disulf ? ? B  CYS 57 SG ? ? ? 1_555 B  CYS 146 SG  ? ? B CYS 57  B CYS 146  1_555 ? ? ? ? ? ? ? 2.208 ? 
disulf3   disulf ? ? C  CYS 57 SG ? ? ? 1_555 C  CYS 146 SG  ? ? C CYS 57  C CYS 146  1_555 ? ? ? ? ? ? ? 2.214 ? 
disulf4   disulf ? ? D  CYS 57 SG ? ? ? 1_555 D  CYS 146 SG  ? ? D CYS 57  D CYS 146  1_555 ? ? ? ? ? ? ? 2.160 ? 
disulf5   disulf ? ? E  CYS 57 SG ? ? ? 1_555 E  CYS 146 SG  ? ? E CYS 57  E CYS 146  1_555 ? ? ? ? ? ? ? 2.170 ? 
disulf6   disulf ? ? F  CYS 57 SG ? ? ? 1_555 F  CYS 146 SG  ? ? F CYS 57  F CYS 146  1_555 ? ? ? ? ? ? ? 2.159 ? 
disulf7   disulf ? ? G  CYS 57 SG ? ? ? 1_555 G  CYS 146 SG  ? ? G CYS 57  G CYS 146  1_555 ? ? ? ? ? ? ? 2.118 ? 
disulf8   disulf ? ? H  CYS 57 SG ? ? ? 1_555 H  CYS 146 SG  ? ? H CYS 57  H CYS 146  1_555 ? ? ? ? ? ? ? 2.115 ? 
disulf9   disulf ? ? I  CYS 57 SG ? ? ? 1_555 I  CYS 146 SG  ? ? I CYS 57  I CYS 146  1_555 ? ? ? ? ? ? ? 2.171 ? 
disulf10  disulf ? ? J  CYS 57 SG ? ? ? 1_555 J  CYS 146 SG  ? ? J CYS 57  J CYS 146  1_555 ? ? ? ? ? ? ? 2.175 ? 
disulf11  disulf ? ? K  CYS 57 SG ? ? ? 1_555 K  CYS 146 SG  ? ? K CYS 57  K CYS 146  1_555 ? ? ? ? ? ? ? 2.185 ? 
disulf12  disulf ? ? L  CYS 57 SG ? ? ? 1_555 L  CYS 146 SG  ? ? L CYS 57  L CYS 146  1_555 ? ? ? ? ? ? ? 2.140 ? 
disulf13  disulf ? ? M  CYS 57 SG ? ? ? 1_555 M  CYS 146 SG  ? ? M CYS 57  M CYS 146  1_555 ? ? ? ? ? ? ? 2.153 ? 
disulf14  disulf ? ? N  CYS 57 SG ? ? ? 1_555 N  CYS 146 SG  ? ? N CYS 57  N CYS 146  1_555 ? ? ? ? ? ? ? 2.155 ? 
disulf15  disulf ? ? O  CYS 57 SG ? ? ? 1_555 O  CYS 146 SG  ? ? O CYS 57  O CYS 146  1_555 ? ? ? ? ? ? ? 2.106 ? 
disulf16  disulf ? ? P  CYS 57 SG ? ? ? 1_555 P  CYS 146 SG  ? ? P CYS 57  P CYS 146  1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf17  disulf ? ? Q  CYS 57 SG ? ? ? 1_555 Q  CYS 146 SG  ? ? Q CYS 57  Q CYS 146  1_555 ? ? ? ? ? ? ? 2.133 ? 
disulf18  disulf ? ? R  CYS 57 SG ? ? ? 1_555 R  CYS 146 SG  ? ? S CYS 57  S CYS 146  1_555 ? ? ? ? ? ? ? 2.056 ? 
metalc1   metalc ? ? S  CU  .  CU ? ? ? 1_555 A  HIS 120 NE2 ? ? A CU  154 A HIS 120  1_555 ? ? ? ? ? ? ? 2.116 ? 
metalc2   metalc ? ? S  CU  .  CU ? ? ? 1_555 A  HIS 46  ND1 ? ? A CU  154 A HIS 46   1_555 ? ? ? ? ? ? ? 2.136 ? 
metalc3   metalc ? ? S  CU  .  CU ? ? ? 1_555 A  HIS 48  NE2 ? ? A CU  154 A HIS 48   1_555 ? ? ? ? ? ? ? 2.132 ? 
metalc4   metalc ? ? S  CU  .  CU ? ? ? 1_555 A  HIS 63  NE2 ? ? A CU  154 A HIS 63   1_555 ? ? ? ? ? ? ? 2.455 ? 
metalc5   metalc ? ? S  CU  .  CU ? ? ? 1_555 FB HOH .   O   ? ? A CU  154 A HOH 2047 1_555 ? ? ? ? ? ? ? 2.653 ? 
metalc6   metalc ? ? T  ZN  .  ZN ? ? ? 1_555 A  HIS 63  ND1 ? ? A ZN  155 A HIS 63   1_555 ? ? ? ? ? ? ? 2.020 ? 
metalc7   metalc ? ? T  ZN  .  ZN ? ? ? 1_555 A  ASP 83  OD1 ? ? A ZN  155 A ASP 83   1_555 ? ? ? ? ? ? ? 1.899 ? 
metalc8   metalc ? ? T  ZN  .  ZN ? ? ? 1_555 A  HIS 71  ND1 ? ? A ZN  155 A HIS 71   1_555 ? ? ? ? ? ? ? 1.990 ? 
metalc9   metalc ? ? T  ZN  .  ZN ? ? ? 1_555 A  HIS 80  ND1 ? ? A ZN  155 A HIS 80   1_555 ? ? ? ? ? ? ? 2.000 ? 
metalc10  metalc ? ? U  CU  .  CU ? ? ? 1_555 B  HIS 120 NE2 ? ? B CU  154 B HIS 120  1_555 ? ? ? ? ? ? ? 2.120 ? 
metalc11  metalc ? ? U  CU  .  CU ? ? ? 1_555 B  HIS 46  ND1 ? ? B CU  154 B HIS 46   1_555 ? ? ? ? ? ? ? 2.121 ? 
metalc12  metalc ? ? U  CU  .  CU ? ? ? 1_555 B  HIS 63  NE2 ? ? B CU  154 B HIS 63   1_555 ? ? ? ? ? ? ? 2.603 ? 
metalc13  metalc ? ? U  CU  .  CU ? ? ? 1_555 GB HOH .   O   ? ? B CU  154 B HOH 2083 1_555 ? ? ? ? ? ? ? 2.470 ? 
metalc14  metalc ? ? U  CU  .  CU ? ? ? 1_555 B  HIS 48  NE2 ? ? B CU  154 B HIS 48   1_555 ? ? ? ? ? ? ? 2.109 ? 
metalc15  metalc ? ? V  ZN  .  ZN ? ? ? 1_555 B  HIS 71  ND1 ? ? B ZN  155 B HIS 71   1_555 ? ? ? ? ? ? ? 2.016 ? 
metalc16  metalc ? ? V  ZN  .  ZN ? ? ? 1_555 B  HIS 80  ND1 ? ? B ZN  155 B HIS 80   1_555 ? ? ? ? ? ? ? 2.014 ? 
metalc17  metalc ? ? V  ZN  .  ZN ? ? ? 1_555 B  ASP 83  OD1 ? ? B ZN  155 B ASP 83   1_555 ? ? ? ? ? ? ? 1.942 ? 
metalc18  metalc ? ? V  ZN  .  ZN ? ? ? 1_555 B  HIS 63  ND1 ? ? B ZN  155 B HIS 63   1_555 ? ? ? ? ? ? ? 1.985 ? 
metalc19  metalc ? ? W  CU  .  CU ? ? ? 1_555 C  HIS 46  ND1 ? ? C CU  154 C HIS 46   1_555 ? ? ? ? ? ? ? 2.131 ? 
metalc20  metalc ? ? W  CU  .  CU ? ? ? 1_555 C  HIS 48  NE2 ? ? C CU  154 C HIS 48   1_555 ? ? ? ? ? ? ? 2.106 ? 
metalc21  metalc ? ? W  CU  .  CU ? ? ? 1_555 C  HIS 120 NE2 ? ? C CU  154 C HIS 120  1_555 ? ? ? ? ? ? ? 2.187 ? 
metalc22  metalc ? ? W  CU  .  CU ? ? ? 1_555 HB HOH .   O   ? ? C CU  154 C HOH 2074 1_555 ? ? ? ? ? ? ? 2.521 ? 
metalc23  metalc ? ? W  CU  .  CU ? ? ? 1_555 C  HIS 63  NE2 ? ? C CU  154 C HIS 63   1_555 ? ? ? ? ? ? ? 2.717 ? 
metalc24  metalc ? ? X  ZN  .  ZN ? ? ? 1_555 C  HIS 71  ND1 ? ? C ZN  155 C HIS 71   1_555 ? ? ? ? ? ? ? 2.051 ? 
metalc25  metalc ? ? X  ZN  .  ZN ? ? ? 1_555 C  HIS 63  ND1 ? ? C ZN  155 C HIS 63   1_555 ? ? ? ? ? ? ? 1.937 ? 
metalc26  metalc ? ? X  ZN  .  ZN ? ? ? 1_555 C  ASP 83  OD1 ? ? C ZN  155 C ASP 83   1_555 ? ? ? ? ? ? ? 1.967 ? 
metalc27  metalc ? ? X  ZN  .  ZN ? ? ? 1_555 C  HIS 80  ND1 ? ? C ZN  155 C HIS 80   1_555 ? ? ? ? ? ? ? 2.077 ? 
metalc28  metalc ? ? Y  CA  .  CA ? ? ? 1_555 HB HOH .   O   ? ? C CA  156 C HOH 2037 1_555 ? ? ? ? ? ? ? 2.196 ? 
metalc29  metalc ? ? Y  CA  .  CA ? ? ? 1_555 HB HOH .   O   ? ? C CA  156 C HOH 2106 1_555 ? ? ? ? ? ? ? 2.688 ? 
metalc30  metalc ? ? Y  CA  .  CA ? ? ? 1_555 HB HOH .   O   ? ? C CA  156 C HOH 2038 1_555 ? ? ? ? ? ? ? 2.430 ? 
metalc31  metalc ? ? Y  CA  .  CA ? ? ? 1_555 HB HOH .   O   ? ? C CA  156 C HOH 2035 1_555 ? ? ? ? ? ? ? 2.347 ? 
metalc32  metalc ? ? Y  CA  .  CA ? ? ? 1_555 C  SER 102 O   ? ? C CA  156 C SER 102  1_555 ? ? ? ? ? ? ? 2.493 ? 
metalc33  metalc ? ? Y  CA  .  CA ? ? ? 1_555 C  ASN 26  O   ? ? C CA  156 C ASN 26   1_555 ? ? ? ? ? ? ? 2.496 ? 
metalc34  metalc ? ? Y  CA  .  CA ? ? ? 1_555 C  ASN 26  OD1 ? ? C CA  156 C ASN 26   1_555 ? ? ? ? ? ? ? 2.439 ? 
metalc35  metalc ? ? Z  CU  .  CU ? ? ? 1_555 D  HIS 48  NE2 ? ? D CU  154 D HIS 48   1_555 ? ? ? ? ? ? ? 2.070 ? 
metalc36  metalc ? ? Z  CU  .  CU ? ? ? 1_555 D  HIS 120 NE2 ? ? D CU  154 D HIS 120  1_555 ? ? ? ? ? ? ? 2.141 ? 
metalc37  metalc ? ? Z  CU  .  CU ? ? ? 1_555 D  HIS 63  NE2 ? ? D CU  154 D HIS 63   1_555 ? ? ? ? ? ? ? 2.601 ? 
metalc38  metalc ? ? Z  CU  .  CU ? ? ? 1_555 IB HOH .   O   ? ? D CU  154 D HOH 2049 1_555 ? ? ? ? ? ? ? 2.698 ? 
metalc39  metalc ? ? Z  CU  .  CU ? ? ? 1_555 D  HIS 46  ND1 ? ? D CU  154 D HIS 46   1_555 ? ? ? ? ? ? ? 2.174 ? 
metalc40  metalc ? ? AA ZN  .  ZN ? ? ? 1_555 D  HIS 71  ND1 ? ? D ZN  155 D HIS 71   1_555 ? ? ? ? ? ? ? 2.057 ? 
metalc41  metalc ? ? AA ZN  .  ZN ? ? ? 1_555 D  HIS 80  ND1 ? ? D ZN  155 D HIS 80   1_555 ? ? ? ? ? ? ? 1.993 ? 
metalc42  metalc ? ? AA ZN  .  ZN ? ? ? 1_555 D  HIS 63  ND1 ? ? D ZN  155 D HIS 63   1_555 ? ? ? ? ? ? ? 2.022 ? 
metalc43  metalc ? ? AA ZN  .  ZN ? ? ? 1_555 D  ASP 83  OD1 ? ? D ZN  155 D ASP 83   1_555 ? ? ? ? ? ? ? 1.891 ? 
metalc44  metalc ? ? BA CA  .  CA ? ? ? 1_555 D  SER 102 O   ? ? D CA  156 D SER 102  1_555 ? ? ? ? ? ? ? 2.586 ? 
metalc45  metalc ? ? BA CA  .  CA ? ? ? 1_555 IB HOH .   O   ? ? D CA  156 D HOH 2072 1_555 ? ? ? ? ? ? ? 2.336 ? 
metalc46  metalc ? ? BA CA  .  CA ? ? ? 1_555 D  ASN 26  O   ? ? D CA  156 D ASN 26   1_555 ? ? ? ? ? ? ? 2.729 ? 
metalc47  metalc ? ? BA CA  .  CA ? ? ? 1_555 D  ASN 26  OD1 ? ? D CA  156 D ASN 26   1_555 ? ? ? ? ? ? ? 2.451 ? 
metalc48  metalc ? ? BA CA  .  CA ? ? ? 1_555 IB HOH .   O   ? ? D CA  156 D HOH 2024 1_555 ? ? ? ? ? ? ? 2.431 ? 
metalc49  metalc ? ? BA CA  .  CA ? ? ? 1_555 FB HOH .   O   ? ? D CA  156 A HOH 2063 1_455 ? ? ? ? ? ? ? 2.428 ? 
metalc50  metalc ? ? CA CU  .  CU ? ? ? 1_555 JB HOH .   O   ? ? E CU  154 E HOH 2052 1_555 ? ? ? ? ? ? ? 2.659 ? 
metalc51  metalc ? ? CA CU  .  CU ? ? ? 1_555 E  HIS 46  ND1 ? ? E CU  154 E HIS 46   1_555 ? ? ? ? ? ? ? 2.151 ? 
metalc52  metalc ? ? CA CU  .  CU ? ? ? 1_555 E  HIS 120 NE2 ? ? E CU  154 E HIS 120  1_555 ? ? ? ? ? ? ? 2.161 ? 
metalc53  metalc ? ? CA CU  .  CU ? ? ? 1_555 E  HIS 63  NE2 ? ? E CU  154 E HIS 63   1_555 ? ? ? ? ? ? ? 2.520 ? 
metalc54  metalc ? ? CA CU  .  CU ? ? ? 1_555 E  HIS 48  NE2 ? ? E CU  154 E HIS 48   1_555 ? ? ? ? ? ? ? 2.098 ? 
metalc55  metalc ? ? DA ZN  .  ZN ? ? ? 1_555 E  HIS 71  ND1 ? ? E ZN  155 E HIS 71   1_555 ? ? ? ? ? ? ? 1.999 ? 
metalc56  metalc ? ? DA ZN  .  ZN ? ? ? 1_555 E  HIS 80  ND1 ? ? E ZN  155 E HIS 80   1_555 ? ? ? ? ? ? ? 2.003 ? 
metalc57  metalc ? ? DA ZN  .  ZN ? ? ? 1_555 E  ASP 83  OD1 ? ? E ZN  155 E ASP 83   1_555 ? ? ? ? ? ? ? 1.954 ? 
metalc58  metalc ? ? DA ZN  .  ZN ? ? ? 1_555 E  HIS 63  ND1 ? ? E ZN  155 E HIS 63   1_555 ? ? ? ? ? ? ? 2.025 ? 
metalc59  metalc ? ? EA CU  .  CU ? ? ? 1_555 F  HIS 63  NE2 ? ? F CU  154 F HIS 63   1_555 ? ? ? ? ? ? ? 2.506 ? 
metalc60  metalc ? ? EA CU  .  CU ? ? ? 1_555 F  HIS 120 NE2 ? ? F CU  154 F HIS 120  1_555 ? ? ? ? ? ? ? 2.142 ? 
metalc61  metalc ? ? EA CU  .  CU ? ? ? 1_555 F  HIS 48  NE2 ? ? F CU  154 F HIS 48   1_555 ? ? ? ? ? ? ? 2.095 ? 
metalc62  metalc ? ? EA CU  .  CU ? ? ? 1_555 KB HOH .   O   ? ? F CU  154 F HOH 2040 1_555 ? ? ? ? ? ? ? 2.720 ? 
metalc63  metalc ? ? EA CU  .  CU ? ? ? 1_555 F  HIS 46  ND1 ? ? F CU  154 F HIS 46   1_555 ? ? ? ? ? ? ? 2.037 ? 
metalc64  metalc ? ? FA ZN  .  ZN ? ? ? 1_555 F  HIS 63  ND1 ? ? F ZN  155 F HIS 63   1_555 ? ? ? ? ? ? ? 2.025 ? 
metalc65  metalc ? ? FA ZN  .  ZN ? ? ? 1_555 F  HIS 71  ND1 ? ? F ZN  155 F HIS 71   1_555 ? ? ? ? ? ? ? 2.081 ? 
metalc66  metalc ? ? FA ZN  .  ZN ? ? ? 1_555 F  HIS 80  ND1 ? ? F ZN  155 F HIS 80   1_555 ? ? ? ? ? ? ? 1.952 ? 
metalc67  metalc ? ? FA ZN  .  ZN ? ? ? 1_555 F  ASP 83  OD1 ? ? F ZN  155 F ASP 83   1_555 ? ? ? ? ? ? ? 1.930 ? 
metalc68  metalc ? ? GA CU  .  CU ? ? ? 1_555 G  HIS 63  NE2 ? ? G CU  154 G HIS 63   1_555 ? ? ? ? ? ? ? 2.702 ? 
metalc69  metalc ? ? GA CU  .  CU ? ? ? 1_555 G  HIS 48  NE2 ? ? G CU  154 G HIS 48   1_555 ? ? ? ? ? ? ? 2.144 ? 
metalc70  metalc ? ? GA CU  .  CU ? ? ? 1_555 LB HOH .   O   ? ? G CU  154 G HOH 2022 1_555 ? ? ? ? ? ? ? 2.009 ? 
metalc71  metalc ? ? GA CU  .  CU ? ? ? 1_555 G  HIS 46  ND1 ? ? G CU  154 G HIS 46   1_555 ? ? ? ? ? ? ? 2.055 ? 
metalc72  metalc ? ? GA CU  .  CU ? ? ? 1_555 G  HIS 120 NE2 ? ? G CU  154 G HIS 120  1_555 ? ? ? ? ? ? ? 1.955 ? 
metalc73  metalc ? ? GA CU  .  CU ? ? ? 1_555 LB HOH .   O   ? ? G CU  154 G HOH 2010 1_555 ? ? ? ? ? ? ? 1.960 ? 
metalc74  metalc ? ? HA ZN  .  ZN ? ? ? 1_555 G  ASP 83  OD1 ? ? G ZN  155 G ASP 83   1_555 ? ? ? ? ? ? ? 1.856 ? 
metalc75  metalc ? ? HA ZN  .  ZN ? ? ? 1_555 G  HIS 71  ND1 ? ? G ZN  155 G HIS 71   1_555 ? ? ? ? ? ? ? 2.101 ? 
metalc76  metalc ? ? HA ZN  .  ZN ? ? ? 1_555 G  HIS 80  ND1 ? ? G ZN  155 G HIS 80   1_555 ? ? ? ? ? ? ? 1.949 ? 
metalc77  metalc ? ? HA ZN  .  ZN ? ? ? 1_555 G  HIS 63  ND1 ? ? G ZN  155 G HIS 63   1_555 ? ? ? ? ? ? ? 2.098 ? 
metalc78  metalc ? ? HA ZN  .  ZN ? ? ? 1_555 G  ASP 83  OD2 ? ? G ZN  155 G ASP 83   1_555 ? ? ? ? ? ? ? 2.673 ? 
metalc79  metalc ? ? IA CU  .  CU ? ? ? 1_555 H  HIS 46  ND1 ? ? H CU  154 H HIS 46   1_555 ? ? ? ? ? ? ? 2.132 ? 
metalc80  metalc ? ? IA CU  .  CU ? ? ? 1_555 H  HIS 120 NE2 ? ? H CU  154 H HIS 120  1_555 ? ? ? ? ? ? ? 2.113 ? 
metalc81  metalc ? ? IA CU  .  CU ? ? ? 1_555 H  HIS 63  NE2 ? ? H CU  154 H HIS 63   1_555 ? ? ? ? ? ? ? 2.521 ? 
metalc82  metalc ? ? IA CU  .  CU ? ? ? 1_555 H  HIS 48  NE2 ? ? H CU  154 H HIS 48   1_555 ? ? ? ? ? ? ? 2.102 ? 
metalc83  metalc ? ? IA CU  .  CU ? ? ? 1_555 MB HOH .   O   ? ? H CU  154 H HOH 2050 1_555 ? ? ? ? ? ? ? 2.736 ? 
metalc84  metalc ? ? JA ZN  .  ZN ? ? ? 1_555 H  ASP 83  OD1 ? ? H ZN  155 H ASP 83   1_555 ? ? ? ? ? ? ? 1.976 ? 
metalc85  metalc ? ? JA ZN  .  ZN ? ? ? 1_555 H  HIS 71  ND1 ? ? H ZN  155 H HIS 71   1_555 ? ? ? ? ? ? ? 2.056 ? 
metalc86  metalc ? ? JA ZN  .  ZN ? ? ? 1_555 H  HIS 80  ND1 ? ? H ZN  155 H HIS 80   1_555 ? ? ? ? ? ? ? 1.861 ? 
metalc87  metalc ? ? JA ZN  .  ZN ? ? ? 1_555 H  HIS 63  ND1 ? ? H ZN  155 H HIS 63   1_555 ? ? ? ? ? ? ? 2.032 ? 
metalc88  metalc ? ? KA CU  .  CU ? ? ? 1_555 I  HIS 63  NE2 ? ? I CU  154 I HIS 63   1_555 ? ? ? ? ? ? ? 2.665 ? 
metalc89  metalc ? ? KA CU  .  CU ? ? ? 1_555 I  HIS 46  ND1 ? ? I CU  154 I HIS 46   1_555 ? ? ? ? ? ? ? 2.124 ? 
metalc90  metalc ? ? KA CU  .  CU ? ? ? 1_555 I  HIS 120 NE2 ? ? I CU  154 I HIS 120  1_555 ? ? ? ? ? ? ? 2.035 ? 
metalc91  metalc ? ? KA CU  .  CU ? ? ? 1_555 I  HIS 48  NE2 ? ? I CU  154 I HIS 48   1_555 ? ? ? ? ? ? ? 2.109 ? 
metalc92  metalc ? ? LA ZN  .  ZN ? ? ? 1_555 I  HIS 80  ND1 ? ? I ZN  155 I HIS 80   1_555 ? ? ? ? ? ? ? 2.095 ? 
metalc93  metalc ? ? LA ZN  .  ZN ? ? ? 1_555 I  HIS 71  ND1 ? ? I ZN  155 I HIS 71   1_555 ? ? ? ? ? ? ? 2.056 ? 
metalc94  metalc ? ? LA ZN  .  ZN ? ? ? 1_555 I  ASP 83  OD1 ? ? I ZN  155 I ASP 83   1_555 ? ? ? ? ? ? ? 2.006 ? 
metalc95  metalc ? ? LA ZN  .  ZN ? ? ? 1_555 I  HIS 63  ND1 ? ? I ZN  155 I HIS 63   1_555 ? ? ? ? ? ? ? 1.943 ? 
metalc96  metalc ? ? MA CU  .  CU ? ? ? 1_555 J  HIS 63  NE2 ? ? J CU  154 J HIS 63   1_555 ? ? ? ? ? ? ? 2.614 ? 
metalc97  metalc ? ? MA CU  .  CU ? ? ? 1_555 J  HIS 46  ND1 ? ? J CU  154 J HIS 46   1_555 ? ? ? ? ? ? ? 2.149 ? 
metalc98  metalc ? ? MA CU  .  CU ? ? ? 1_555 J  HIS 48  NE2 ? ? J CU  154 J HIS 48   1_555 ? ? ? ? ? ? ? 2.088 ? 
metalc99  metalc ? ? MA CU  .  CU ? ? ? 1_555 OB HOH .   O   ? ? J CU  154 J HOH 2064 1_555 ? ? ? ? ? ? ? 2.631 ? 
metalc100 metalc ? ? MA CU  .  CU ? ? ? 1_555 J  HIS 120 NE2 ? ? J CU  154 J HIS 120  1_555 ? ? ? ? ? ? ? 2.142 ? 
metalc101 metalc ? ? NA ZN  .  ZN ? ? ? 1_555 J  ASP 83  OD1 ? ? J ZN  155 J ASP 83   1_555 ? ? ? ? ? ? ? 2.010 ? 
metalc102 metalc ? ? NA ZN  .  ZN ? ? ? 1_555 J  HIS 63  ND1 ? ? J ZN  155 J HIS 63   1_555 ? ? ? ? ? ? ? 1.951 ? 
metalc103 metalc ? ? NA ZN  .  ZN ? ? ? 1_555 J  HIS 71  ND1 ? ? J ZN  155 J HIS 71   1_555 ? ? ? ? ? ? ? 2.065 ? 
metalc104 metalc ? ? NA ZN  .  ZN ? ? ? 1_555 J  HIS 80  ND1 ? ? J ZN  155 J HIS 80   1_555 ? ? ? ? ? ? ? 1.999 ? 
metalc105 metalc ? ? OA CU  .  CU ? ? ? 1_555 PB HOH .   O   ? ? K CU  154 K HOH 2063 1_555 ? ? ? ? ? ? ? 2.650 ? 
metalc106 metalc ? ? OA CU  .  CU ? ? ? 1_555 K  HIS 120 NE2 ? ? K CU  154 K HIS 120  1_555 ? ? ? ? ? ? ? 2.146 ? 
metalc107 metalc ? ? OA CU  .  CU ? ? ? 1_555 K  HIS 63  NE2 ? ? K CU  154 K HIS 63   1_555 ? ? ? ? ? ? ? 2.485 ? 
metalc108 metalc ? ? OA CU  .  CU ? ? ? 1_555 K  HIS 46  ND1 ? ? K CU  154 K HIS 46   1_555 ? ? ? ? ? ? ? 2.114 ? 
metalc109 metalc ? ? OA CU  .  CU ? ? ? 1_555 K  HIS 48  NE2 ? ? K CU  154 K HIS 48   1_555 ? ? ? ? ? ? ? 2.114 ? 
metalc110 metalc ? ? PA ZN  .  ZN ? ? ? 1_555 K  HIS 63  ND1 ? ? K ZN  155 K HIS 63   1_555 ? ? ? ? ? ? ? 1.975 ? 
metalc111 metalc ? ? PA ZN  .  ZN ? ? ? 1_555 K  HIS 71  ND1 ? ? K ZN  155 K HIS 71   1_555 ? ? ? ? ? ? ? 2.124 ? 
metalc112 metalc ? ? PA ZN  .  ZN ? ? ? 1_555 K  HIS 80  ND1 ? ? K ZN  155 K HIS 80   1_555 ? ? ? ? ? ? ? 2.032 ? 
metalc113 metalc ? ? PA ZN  .  ZN ? ? ? 1_555 K  ASP 83  OD1 ? ? K ZN  155 K ASP 83   1_555 ? ? ? ? ? ? ? 1.905 ? 
metalc114 metalc ? ? QA CU  .  CU ? ? ? 1_555 L  HIS 48  NE2 ? ? L CU  154 L HIS 48   1_555 ? ? ? ? ? ? ? 2.049 ? 
metalc115 metalc ? ? QA CU  .  CU ? ? ? 1_555 L  HIS 46  ND1 ? ? L CU  154 L HIS 46   1_555 ? ? ? ? ? ? ? 2.087 ? 
metalc116 metalc ? ? QA CU  .  CU ? ? ? 1_555 L  HIS 120 NE2 ? ? L CU  154 L HIS 120  1_555 ? ? ? ? ? ? ? 2.022 ? 
metalc117 metalc ? ? RA ZN  .  ZN ? ? ? 1_555 L  HIS 63  ND1 ? ? L ZN  155 L HIS 63   1_555 ? ? ? ? ? ? ? 2.005 ? 
metalc118 metalc ? ? RA ZN  .  ZN ? ? ? 1_555 L  HIS 71  ND1 ? ? L ZN  155 L HIS 71   1_555 ? ? ? ? ? ? ? 2.064 ? 
metalc119 metalc ? ? RA ZN  .  ZN ? ? ? 1_555 L  ASP 83  OD1 ? ? L ZN  155 L ASP 83   1_555 ? ? ? ? ? ? ? 1.902 ? 
metalc120 metalc ? ? RA ZN  .  ZN ? ? ? 1_555 L  HIS 80  ND1 ? ? L ZN  155 L HIS 80   1_555 ? ? ? ? ? ? ? 1.978 ? 
metalc121 metalc ? ? SA CU  .  CU ? ? ? 1_555 M  HIS 63  NE2 ? ? M CU  154 M HIS 63   1_555 ? ? ? ? ? ? ? 2.532 ? 
metalc122 metalc ? ? SA CU  .  CU ? ? ? 1_555 M  HIS 46  ND1 ? ? M CU  154 M HIS 46   1_555 ? ? ? ? ? ? ? 2.110 ? 
metalc123 metalc ? ? SA CU  .  CU ? ? ? 1_555 M  HIS 48  NE2 ? ? M CU  154 M HIS 48   1_555 ? ? ? ? ? ? ? 2.108 ? 
metalc124 metalc ? ? SA CU  .  CU ? ? ? 1_555 RB HOH .   O   ? ? M CU  154 M HOH 2041 1_555 ? ? ? ? ? ? ? 2.620 ? 
metalc125 metalc ? ? SA CU  .  CU ? ? ? 1_555 M  HIS 120 NE2 ? ? M CU  154 M HIS 120  1_555 ? ? ? ? ? ? ? 2.096 ? 
metalc126 metalc ? ? TA ZN  .  ZN ? ? ? 1_555 M  HIS 63  ND1 ? ? M ZN  155 M HIS 63   1_555 ? ? ? ? ? ? ? 1.953 ? 
metalc127 metalc ? ? TA ZN  .  ZN ? ? ? 1_555 M  HIS 71  ND1 ? ? M ZN  155 M HIS 71   1_555 ? ? ? ? ? ? ? 2.055 ? 
metalc128 metalc ? ? TA ZN  .  ZN ? ? ? 1_555 M  HIS 80  ND1 ? ? M ZN  155 M HIS 80   1_555 ? ? ? ? ? ? ? 2.051 ? 
metalc129 metalc ? ? TA ZN  .  ZN ? ? ? 1_555 M  ASP 83  OD1 ? ? M ZN  155 M ASP 83   1_555 ? ? ? ? ? ? ? 1.909 ? 
metalc130 metalc ? ? UA CU  .  CU ? ? ? 1_555 SB HOH .   O   ? ? N CU  154 N HOH 2038 1_555 ? ? ? ? ? ? ? 2.649 ? 
metalc131 metalc ? ? UA CU  .  CU ? ? ? 1_555 N  HIS 120 NE2 ? ? N CU  154 N HIS 120  1_555 ? ? ? ? ? ? ? 2.038 ? 
metalc132 metalc ? ? UA CU  .  CU ? ? ? 1_555 N  HIS 63  NE2 ? ? N CU  154 N HIS 63   1_555 ? ? ? ? ? ? ? 2.723 ? 
metalc133 metalc ? ? UA CU  .  CU ? ? ? 1_555 N  HIS 48  NE2 ? ? N CU  154 N HIS 48   1_555 ? ? ? ? ? ? ? 2.065 ? 
metalc134 metalc ? ? UA CU  .  CU ? ? ? 1_555 N  HIS 46  ND1 ? ? N CU  154 N HIS 46   1_555 ? ? ? ? ? ? ? 2.115 ? 
metalc135 metalc ? ? VA ZN  .  ZN ? ? ? 1_555 N  HIS 71  ND1 ? ? N ZN  155 N HIS 71   1_555 ? ? ? ? ? ? ? 1.990 ? 
metalc136 metalc ? ? VA ZN  .  ZN ? ? ? 1_555 N  ASP 83  OD1 ? ? N ZN  155 N ASP 83   1_555 ? ? ? ? ? ? ? 2.019 ? 
metalc137 metalc ? ? VA ZN  .  ZN ? ? ? 1_555 N  HIS 63  ND1 ? ? N ZN  155 N HIS 63   1_555 ? ? ? ? ? ? ? 1.958 ? 
metalc138 metalc ? ? VA ZN  .  ZN ? ? ? 1_555 N  HIS 80  ND1 ? ? N ZN  155 N HIS 80   1_555 ? ? ? ? ? ? ? 2.181 ? 
metalc139 metalc ? ? WA CU  .  CU ? ? ? 1_555 O  HIS 48  NE2 ? ? O CU  154 O HIS 48   1_555 ? ? ? ? ? ? ? 2.176 ? 
metalc140 metalc ? ? WA CU  .  CU ? ? ? 1_555 O  HIS 120 NE2 ? ? O CU  154 O HIS 120  1_555 ? ? ? ? ? ? ? 2.104 ? 
metalc141 metalc ? ? WA CU  .  CU ? ? ? 1_555 O  HIS 46  ND1 ? ? O CU  154 O HIS 46   1_555 ? ? ? ? ? ? ? 2.190 ? 
metalc142 metalc ? ? WA CU  .  CU ? ? ? 1_555 O  HIS 63  NE2 ? ? O CU  154 O HIS 63   1_555 ? ? ? ? ? ? ? 2.595 ? 
metalc143 metalc ? ? XA ZN  .  ZN ? ? ? 1_555 O  ASP 83  OD1 ? ? O ZN  155 O ASP 83   1_555 ? ? ? ? ? ? ? 1.917 ? 
metalc144 metalc ? ? XA ZN  .  ZN ? ? ? 1_555 O  HIS 63  ND1 ? ? O ZN  155 O HIS 63   1_555 ? ? ? ? ? ? ? 2.033 ? 
metalc145 metalc ? ? XA ZN  .  ZN ? ? ? 1_555 O  HIS 80  ND1 ? ? O ZN  155 O HIS 80   1_555 ? ? ? ? ? ? ? 2.192 ? 
metalc146 metalc ? ? XA ZN  .  ZN ? ? ? 1_555 O  HIS 71  ND1 ? ? O ZN  155 O HIS 71   1_555 ? ? ? ? ? ? ? 1.952 ? 
metalc147 metalc ? ? YA CA  .  CA ? ? ? 1_555 H  SER 102 O   ? ? O CA  156 H SER 102  1_555 ? ? ? ? ? ? ? 2.454 ? 
metalc148 metalc ? ? YA CA  .  CA ? ? ? 1_555 MB HOH .   O   ? ? O CA  156 H HOH 2085 1_555 ? ? ? ? ? ? ? 2.401 ? 
metalc149 metalc ? ? YA CA  .  CA ? ? ? 1_555 H  ASN 26  OD1 ? ? O CA  156 H ASN 26   1_555 ? ? ? ? ? ? ? 2.611 ? 
metalc150 metalc ? ? YA CA  .  CA ? ? ? 1_555 MB HOH .   O   ? ? O CA  156 H HOH 2081 1_555 ? ? ? ? ? ? ? 2.442 ? 
metalc151 metalc ? ? YA CA  .  CA ? ? ? 1_555 MB HOH .   O   ? ? O CA  156 H HOH 2084 1_555 ? ? ? ? ? ? ? 2.396 ? 
metalc152 metalc ? ? YA CA  .  CA ? ? ? 1_555 H  ASN 26  O   ? ? O CA  156 H ASN 26   1_555 ? ? ? ? ? ? ? 2.694 ? 
metalc153 metalc ? ? ZA CU  .  CU ? ? ? 1_555 P  HIS 63  NE2 ? ? P CU  154 P HIS 63   1_555 ? ? ? ? ? ? ? 2.331 ? 
metalc154 metalc ? ? ZA CU  .  CU ? ? ? 1_555 P  HIS 120 NE2 ? ? P CU  154 P HIS 120  1_555 ? ? ? ? ? ? ? 2.574 ? 
metalc155 metalc ? ? ZA CU  .  CU ? ? ? 1_555 P  HIS 46  ND1 ? ? P CU  154 P HIS 46   1_555 ? ? ? ? ? ? ? 2.072 ? 
metalc156 metalc ? ? ZA CU  .  CU ? ? ? 1_555 P  HIS 48  NE2 ? ? P CU  154 P HIS 48   1_555 ? ? ? ? ? ? ? 2.117 ? 
metalc157 metalc ? ? AB ZN  .  ZN ? ? ? 1_555 P  ASP 83  OD2 ? ? P ZN  155 P ASP 83   1_555 ? ? ? ? ? ? ? 2.716 ? 
metalc158 metalc ? ? AB ZN  .  ZN ? ? ? 1_555 P  ASP 83  OD1 ? ? P ZN  155 P ASP 83   1_555 ? ? ? ? ? ? ? 1.809 ? 
metalc159 metalc ? ? AB ZN  .  ZN ? ? ? 1_555 P  HIS 71  ND1 ? ? P ZN  155 P HIS 71   1_555 ? ? ? ? ? ? ? 2.078 ? 
metalc160 metalc ? ? AB ZN  .  ZN ? ? ? 1_555 P  HIS 80  ND1 ? ? P ZN  155 P HIS 80   1_555 ? ? ? ? ? ? ? 2.183 ? 
metalc161 metalc ? ? AB ZN  .  ZN ? ? ? 1_555 P  HIS 63  ND1 ? ? P ZN  155 P HIS 63   1_555 ? ? ? ? ? ? ? 2.154 ? 
metalc162 metalc ? ? BB CU  .  CU ? ? ? 1_555 Q  HIS 120 NE2 ? ? Q CU  154 Q HIS 120  1_555 ? ? ? ? ? ? ? 2.120 ? 
metalc163 metalc ? ? BB CU  .  CU ? ? ? 1_555 VB HOH .   O   ? ? Q CU  154 Q HOH 2040 1_555 ? ? ? ? ? ? ? 2.737 ? 
metalc164 metalc ? ? BB CU  .  CU ? ? ? 1_555 Q  HIS 63  NE2 ? ? Q CU  154 Q HIS 63   1_555 ? ? ? ? ? ? ? 2.628 ? 
metalc165 metalc ? ? BB CU  .  CU ? ? ? 1_555 Q  HIS 46  ND1 ? ? Q CU  154 Q HIS 46   1_555 ? ? ? ? ? ? ? 2.081 ? 
metalc166 metalc ? ? BB CU  .  CU ? ? ? 1_555 Q  HIS 48  NE2 ? ? Q CU  154 Q HIS 48   1_555 ? ? ? ? ? ? ? 2.059 ? 
metalc167 metalc ? ? CB ZN  .  ZN ? ? ? 1_555 Q  HIS 63  ND1 ? ? Q ZN  155 Q HIS 63   1_555 ? ? ? ? ? ? ? 1.922 ? 
metalc168 metalc ? ? CB ZN  .  ZN ? ? ? 1_555 Q  ASP 83  OD1 ? ? Q ZN  155 Q ASP 83   1_555 ? ? ? ? ? ? ? 1.935 ? 
metalc169 metalc ? ? CB ZN  .  ZN ? ? ? 1_555 Q  HIS 80  ND1 ? ? Q ZN  155 Q HIS 80   1_555 ? ? ? ? ? ? ? 2.078 ? 
metalc170 metalc ? ? CB ZN  .  ZN ? ? ? 1_555 Q  HIS 71  ND1 ? ? Q ZN  155 Q HIS 71   1_555 ? ? ? ? ? ? ? 2.029 ? 
metalc171 metalc ? ? DB CU  .  CU ? ? ? 1_555 R  HIS 63  NE2 ? ? S CU  154 S HIS 63   1_555 ? ? ? ? ? ? ? 2.524 ? 
metalc172 metalc ? ? DB CU  .  CU ? ? ? 1_555 R  HIS 46  ND1 ? ? S CU  154 S HIS 46   1_555 ? ? ? ? ? ? ? 2.179 ? 
metalc173 metalc ? ? DB CU  .  CU ? ? ? 1_555 R  HIS 48  NE2 ? ? S CU  154 S HIS 48   1_555 ? ? ? ? ? ? ? 2.025 ? 
metalc174 metalc ? ? DB CU  .  CU ? ? ? 1_555 R  HIS 120 NE2 ? ? S CU  154 S HIS 120  1_555 ? ? ? ? ? ? ? 2.203 ? 
metalc175 metalc ? ? EB ZN  .  ZN ? ? ? 1_555 R  HIS 80  ND1 ? ? S ZN  155 S HIS 80   1_555 ? ? ? ? ? ? ? 2.051 ? 
metalc176 metalc ? ? EB ZN  .  ZN ? ? ? 1_555 R  ASP 83  OD1 ? ? S ZN  155 S ASP 83   1_555 ? ? ? ? ? ? ? 2.005 ? 
metalc177 metalc ? ? EB ZN  .  ZN ? ? ? 1_555 R  HIS 71  ND1 ? ? S ZN  155 S HIS 71   1_555 ? ? ? ? ? ? ? 2.115 ? 
metalc178 metalc ? ? EB ZN  .  ZN ? ? ? 1_555 R  HIS 63  ND1 ? ? S ZN  155 S HIS 63   1_555 ? ? ? ? ? ? ? 2.102 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA ? 5 ? 
AB ? 4 ? 
BA ? 5 ? 
BB ? 4 ? 
CA ? 5 ? 
CB ? 4 ? 
DA ? 5 ? 
DB ? 4 ? 
EA ? 5 ? 
EB ? 4 ? 
FA ? 9 ? 
GA ? 5 ? 
GB ? 4 ? 
HA ? 5 ? 
HB ? 4 ? 
IA ? 5 ? 
IB ? 4 ? 
JA ? 5 ? 
JB ? 4 ? 
KA ? 5 ? 
KB ? 4 ? 
LA ? 5 ? 
LB ? 4 ? 
MA ? 5 ? 
MB ? 4 ? 
NA ? 5 ? 
NB ? 4 ? 
OA ? 5 ? 
OB ? 4 ? 
PA ? 9 ? 
QA ? 5 ? 
QB ? 4 ? 
SA ? 5 ? 
SB ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA 1 2 ? anti-parallel 
AA 2 3 ? anti-parallel 
AA 3 4 ? anti-parallel 
AA 4 5 ? anti-parallel 
AB 1 2 ? anti-parallel 
AB 2 3 ? anti-parallel 
AB 3 4 ? anti-parallel 
BA 1 2 ? anti-parallel 
BA 2 3 ? anti-parallel 
BA 3 4 ? anti-parallel 
BA 4 5 ? anti-parallel 
BB 1 2 ? anti-parallel 
BB 2 3 ? anti-parallel 
BB 3 4 ? anti-parallel 
CA 1 2 ? anti-parallel 
CA 2 3 ? anti-parallel 
CA 3 4 ? anti-parallel 
CA 4 5 ? anti-parallel 
CB 1 2 ? anti-parallel 
CB 2 3 ? anti-parallel 
CB 3 4 ? anti-parallel 
DA 1 2 ? anti-parallel 
DA 2 3 ? anti-parallel 
DA 3 4 ? anti-parallel 
DA 4 5 ? anti-parallel 
DB 1 2 ? anti-parallel 
DB 2 3 ? anti-parallel 
DB 3 4 ? anti-parallel 
EA 1 2 ? anti-parallel 
EA 2 3 ? anti-parallel 
EA 3 4 ? anti-parallel 
EA 4 5 ? anti-parallel 
EB 1 2 ? anti-parallel 
EB 2 3 ? anti-parallel 
EB 3 4 ? anti-parallel 
FA 1 2 ? anti-parallel 
FA 2 3 ? anti-parallel 
FA 3 4 ? anti-parallel 
FA 4 5 ? anti-parallel 
FA 5 6 ? anti-parallel 
FA 6 7 ? anti-parallel 
FA 7 8 ? anti-parallel 
FA 8 9 ? anti-parallel 
GA 1 2 ? anti-parallel 
GA 2 3 ? anti-parallel 
GA 3 4 ? anti-parallel 
GA 4 5 ? anti-parallel 
GB 1 2 ? anti-parallel 
GB 2 3 ? anti-parallel 
GB 3 4 ? anti-parallel 
HA 1 2 ? anti-parallel 
HA 2 3 ? anti-parallel 
HA 3 4 ? anti-parallel 
HA 4 5 ? anti-parallel 
HB 1 2 ? anti-parallel 
HB 2 3 ? anti-parallel 
HB 3 4 ? anti-parallel 
IA 1 2 ? anti-parallel 
IA 2 3 ? anti-parallel 
IA 3 4 ? anti-parallel 
IA 4 5 ? anti-parallel 
IB 1 2 ? anti-parallel 
IB 2 3 ? anti-parallel 
IB 3 4 ? anti-parallel 
JA 1 2 ? anti-parallel 
JA 2 3 ? anti-parallel 
JA 3 4 ? anti-parallel 
JA 4 5 ? anti-parallel 
JB 1 2 ? anti-parallel 
JB 2 3 ? anti-parallel 
JB 3 4 ? anti-parallel 
KA 1 2 ? anti-parallel 
KA 2 3 ? anti-parallel 
KA 3 4 ? anti-parallel 
KA 4 5 ? anti-parallel 
KB 1 2 ? anti-parallel 
KB 2 3 ? anti-parallel 
KB 3 4 ? anti-parallel 
LA 1 2 ? anti-parallel 
LA 2 3 ? anti-parallel 
LA 3 4 ? anti-parallel 
LA 4 5 ? anti-parallel 
LB 1 2 ? anti-parallel 
LB 2 3 ? anti-parallel 
LB 3 4 ? anti-parallel 
MA 1 2 ? anti-parallel 
MA 2 3 ? anti-parallel 
MA 3 4 ? anti-parallel 
MA 4 5 ? anti-parallel 
MB 1 2 ? anti-parallel 
MB 2 3 ? anti-parallel 
MB 3 4 ? anti-parallel 
NA 1 2 ? anti-parallel 
NA 2 3 ? anti-parallel 
NA 3 4 ? anti-parallel 
NA 4 5 ? anti-parallel 
NB 1 2 ? anti-parallel 
NB 2 3 ? anti-parallel 
NB 3 4 ? anti-parallel 
OA 1 2 ? anti-parallel 
OA 2 3 ? anti-parallel 
OA 3 4 ? anti-parallel 
OA 4 5 ? anti-parallel 
OB 1 2 ? anti-parallel 
OB 2 3 ? anti-parallel 
OB 3 4 ? anti-parallel 
PA 1 2 ? anti-parallel 
PA 2 3 ? anti-parallel 
PA 3 4 ? anti-parallel 
PA 4 5 ? anti-parallel 
PA 5 6 ? anti-parallel 
PA 6 7 ? anti-parallel 
PA 7 8 ? anti-parallel 
PA 8 9 ? anti-parallel 
QA 1 2 ? anti-parallel 
QA 2 3 ? anti-parallel 
QA 3 4 ? anti-parallel 
QA 4 5 ? anti-parallel 
QB 1 2 ? anti-parallel 
QB 2 3 ? anti-parallel 
QB 3 4 ? anti-parallel 
SA 1 2 ? anti-parallel 
SA 2 3 ? anti-parallel 
SA 3 4 ? anti-parallel 
SA 4 5 ? anti-parallel 
SB 1 2 ? anti-parallel 
SB 2 3 ? anti-parallel 
SB 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA 1 ALA A 95  ? ASP A 101 ? ALA A 95  ASP A 101 
AA 2 VAL A 29  ? LYS A 36  ? VAL A 29  LYS A 36  
AA 3 GLN A 15  ? GLN A 22  ? GLN A 15  GLN A 22  
AA 4 THR A 2   ? LYS A 9   ? THR A 2   LYS A 9   
AA 5 GLY A 150 ? ILE A 151 ? GLY A 150 ILE A 151 
AB 1 ASP A 83  ? ALA A 89  ? ASP A 83  ALA A 89  
AB 2 GLY A 41  ? HIS A 48  ? GLY A 41  HIS A 48  
AB 3 THR A 116 ? HIS A 120 ? THR A 116 HIS A 120 
AB 4 ARG A 143 ? VAL A 148 ? ARG A 143 VAL A 148 
BA 1 ALA B 95  ? ASP B 101 ? ALA B 95  ASP B 101 
BA 2 VAL B 29  ? LYS B 36  ? VAL B 29  LYS B 36  
BA 3 GLN B 15  ? GLN B 22  ? GLN B 15  GLN B 22  
BA 4 THR B 2   ? LEU B 8   ? THR B 2   LEU B 8   
BA 5 GLY B 150 ? ILE B 151 ? GLY B 150 ILE B 151 
BB 1 ASP B 83  ? ALA B 89  ? ASP B 83  ALA B 89  
BB 2 GLY B 41  ? HIS B 48  ? GLY B 41  HIS B 48  
BB 3 THR B 116 ? HIS B 120 ? THR B 116 HIS B 120 
BB 4 ARG B 143 ? VAL B 148 ? ARG B 143 VAL B 148 
CA 1 ALA C 95  ? ASP C 101 ? ALA C 95  ASP C 101 
CA 2 VAL C 29  ? LYS C 36  ? VAL C 29  LYS C 36  
CA 3 GLN C 15  ? GLN C 22  ? GLN C 15  GLN C 22  
CA 4 THR C 2   ? LEU C 8   ? THR C 2   LEU C 8   
CA 5 GLY C 150 ? ILE C 151 ? GLY C 150 ILE C 151 
CB 1 ASP C 83  ? ALA C 89  ? ASP C 83  ALA C 89  
CB 2 GLY C 41  ? HIS C 48  ? GLY C 41  HIS C 48  
CB 3 THR C 116 ? HIS C 120 ? THR C 116 HIS C 120 
CB 4 ARG C 143 ? VAL C 148 ? ARG C 143 VAL C 148 
DA 1 ALA D 95  ? ASP D 101 ? ALA D 95  ASP D 101 
DA 2 VAL D 29  ? LYS D 36  ? VAL D 29  LYS D 36  
DA 3 GLN D 15  ? GLN D 22  ? GLN D 15  GLN D 22  
DA 4 THR D 2   ? LEU D 8   ? THR D 2   LEU D 8   
DA 5 GLY D 150 ? ILE D 151 ? GLY D 150 ILE D 151 
DB 1 ASP D 83  ? ALA D 89  ? ASP D 83  ALA D 89  
DB 2 GLY D 41  ? HIS D 48  ? GLY D 41  HIS D 48  
DB 3 THR D 116 ? HIS D 120 ? THR D 116 HIS D 120 
DB 4 ARG D 143 ? VAL D 148 ? ARG D 143 VAL D 148 
EA 1 ALA E 95  ? ASP E 101 ? ALA E 95  ASP E 101 
EA 2 VAL E 29  ? LYS E 36  ? VAL E 29  LYS E 36  
EA 3 GLN E 15  ? GLN E 22  ? GLN E 15  GLN E 22  
EA 4 THR E 2   ? LEU E 8   ? THR E 2   LEU E 8   
EA 5 GLY E 150 ? ILE E 151 ? GLY E 150 ILE E 151 
EB 1 ASP E 83  ? ALA E 89  ? ASP E 83  ALA E 89  
EB 2 GLY E 41  ? HIS E 48  ? GLY E 41  HIS E 48  
EB 3 THR E 116 ? HIS E 120 ? THR E 116 HIS E 120 
EB 4 ARG E 143 ? VAL E 148 ? ARG E 143 VAL E 148 
FA 1 LYS F 3   ? LYS F 9   ? LYS F 3   LYS F 9   
FA 2 GLN F 15  ? GLU F 21  ? GLN F 15  GLU F 21  
FA 3 VAL F 29  ? LYS F 36  ? VAL F 29  LYS F 36  
FA 4 ALA F 95  ? ASP F 101 ? ALA F 95  ASP F 101 
FA 5 ASP F 83  ? ALA F 89  ? ASP F 83  ALA F 89  
FA 6 GLY F 41  ? HIS F 48  ? GLY F 41  HIS F 48  
FA 7 THR F 116 ? HIS F 120 ? THR F 116 HIS F 120 
FA 8 ARG F 143 ? ILE F 151 ? ARG F 143 ILE F 151 
FA 9 LYS F 3   ? LYS F 9   ? LYS F 3   LYS F 9   
GA 1 ALA G 95  ? ASP G 101 ? ALA G 95  ASP G 101 
GA 2 VAL G 29  ? LYS G 36  ? VAL G 29  LYS G 36  
GA 3 GLN G 15  ? GLN G 22  ? GLN G 15  GLN G 22  
GA 4 THR G 2   ? LEU G 8   ? THR G 2   LEU G 8   
GA 5 GLY G 150 ? ALA G 152 ? GLY G 150 ALA G 152 
GB 1 ASP G 83  ? ALA G 89  ? ASP G 83  ALA G 89  
GB 2 GLY G 41  ? HIS G 48  ? GLY G 41  HIS G 48  
GB 3 THR G 116 ? HIS G 120 ? THR G 116 HIS G 120 
GB 4 ARG G 143 ? VAL G 148 ? ARG G 143 VAL G 148 
HA 1 ALA H 95  ? ASP H 101 ? ALA H 95  ASP H 101 
HA 2 VAL H 29  ? LYS H 36  ? VAL H 29  LYS H 36  
HA 3 GLN H 15  ? GLN H 22  ? GLN H 15  GLN H 22  
HA 4 THR H 2   ? LEU H 8   ? THR H 2   LEU H 8   
HA 5 GLY H 150 ? ILE H 151 ? GLY H 150 ILE H 151 
HB 1 ASP H 83  ? ALA H 89  ? ASP H 83  ALA H 89  
HB 2 GLY H 41  ? HIS H 48  ? GLY H 41  HIS H 48  
HB 3 THR H 116 ? HIS H 120 ? THR H 116 HIS H 120 
HB 4 ARG H 143 ? VAL H 148 ? ARG H 143 VAL H 148 
IA 1 ALA I 95  ? ASP I 101 ? ALA I 95  ASP I 101 
IA 2 VAL I 29  ? LYS I 36  ? VAL I 29  LYS I 36  
IA 3 GLN I 15  ? GLN I 22  ? GLN I 15  GLN I 22  
IA 4 THR I 2   ? LEU I 8   ? THR I 2   LEU I 8   
IA 5 GLY I 150 ? ILE I 151 ? GLY I 150 ILE I 151 
IB 1 ASP I 83  ? ALA I 89  ? ASP I 83  ALA I 89  
IB 2 GLY I 41  ? HIS I 48  ? GLY I 41  HIS I 48  
IB 3 THR I 116 ? HIS I 120 ? THR I 116 HIS I 120 
IB 4 ARG I 143 ? VAL I 148 ? ARG I 143 VAL I 148 
JA 1 ALA J 95  ? ASP J 101 ? ALA J 95  ASP J 101 
JA 2 VAL J 29  ? LYS J 36  ? VAL J 29  LYS J 36  
JA 3 GLN J 15  ? GLN J 22  ? GLN J 15  GLN J 22  
JA 4 THR J 2   ? LEU J 8   ? THR J 2   LEU J 8   
JA 5 GLY J 150 ? ILE J 151 ? GLY J 150 ILE J 151 
JB 1 ASP J 83  ? ALA J 89  ? ASP J 83  ALA J 89  
JB 2 GLY J 41  ? HIS J 48  ? GLY J 41  HIS J 48  
JB 3 THR J 116 ? HIS J 120 ? THR J 116 HIS J 120 
JB 4 ARG J 143 ? VAL J 148 ? ARG J 143 VAL J 148 
KA 1 ALA K 95  ? ASP K 101 ? ALA K 95  ASP K 101 
KA 2 VAL K 29  ? LYS K 36  ? VAL K 29  LYS K 36  
KA 3 GLN K 15  ? GLN K 22  ? GLN K 15  GLN K 22  
KA 4 THR K 2   ? LYS K 9   ? THR K 2   LYS K 9   
KA 5 GLY K 150 ? ILE K 151 ? GLY K 150 ILE K 151 
KB 1 ASP K 83  ? ALA K 89  ? ASP K 83  ALA K 89  
KB 2 GLY K 41  ? HIS K 48  ? GLY K 41  HIS K 48  
KB 3 THR K 116 ? HIS K 120 ? THR K 116 HIS K 120 
KB 4 ARG K 143 ? VAL K 148 ? ARG K 143 VAL K 148 
LA 1 ALA L 95  ? ASP L 101 ? ALA L 95  ASP L 101 
LA 2 VAL L 29  ? LYS L 36  ? VAL L 29  LYS L 36  
LA 3 GLN L 15  ? GLN L 22  ? GLN L 15  GLN L 22  
LA 4 LYS L 3   ? LEU L 8   ? LYS L 3   LEU L 8   
LA 5 GLY L 150 ? ILE L 151 ? GLY L 150 ILE L 151 
LB 1 ASP L 83  ? ALA L 89  ? ASP L 83  ALA L 89  
LB 2 GLY L 41  ? HIS L 48  ? GLY L 41  HIS L 48  
LB 3 THR L 116 ? HIS L 120 ? THR L 116 HIS L 120 
LB 4 ARG L 143 ? VAL L 148 ? ARG L 143 VAL L 148 
MA 1 ALA M 95  ? ASP M 101 ? ALA M 95  ASP M 101 
MA 2 VAL M 29  ? LYS M 36  ? VAL M 29  LYS M 36  
MA 3 GLN M 15  ? GLN M 22  ? GLN M 15  GLN M 22  
MA 4 THR M 2   ? LEU M 8   ? THR M 2   LEU M 8   
MA 5 GLY M 150 ? ILE M 151 ? GLY M 150 ILE M 151 
MB 1 ASP M 83  ? ALA M 89  ? ASP M 83  ALA M 89  
MB 2 GLY M 41  ? HIS M 48  ? GLY M 41  HIS M 48  
MB 3 THR M 116 ? HIS M 120 ? THR M 116 HIS M 120 
MB 4 ARG M 143 ? VAL M 148 ? ARG M 143 VAL M 148 
NA 1 ALA N 95  ? ASP N 101 ? ALA N 95  ASP N 101 
NA 2 VAL N 29  ? LYS N 36  ? VAL N 29  LYS N 36  
NA 3 GLN N 15  ? GLN N 22  ? GLN N 15  GLN N 22  
NA 4 LYS N 3   ? LEU N 8   ? LYS N 3   LEU N 8   
NA 5 GLY N 150 ? ILE N 151 ? GLY N 150 ILE N 151 
NB 1 ASP N 83  ? ALA N 89  ? ASP N 83  ALA N 89  
NB 2 GLY N 41  ? HIS N 48  ? GLY N 41  HIS N 48  
NB 3 THR N 116 ? HIS N 120 ? THR N 116 HIS N 120 
NB 4 ARG N 143 ? VAL N 148 ? ARG N 143 VAL N 148 
OA 1 ALA O 95  ? ASP O 101 ? ALA O 95  ASP O 101 
OA 2 VAL O 29  ? LYS O 36  ? VAL O 29  LYS O 36  
OA 3 GLN O 15  ? GLU O 21  ? GLN O 15  GLU O 21  
OA 4 LYS O 3   ? LEU O 8   ? LYS O 3   LEU O 8   
OA 5 GLY O 150 ? ILE O 151 ? GLY O 150 ILE O 151 
OB 1 ASP O 83  ? ALA O 89  ? ASP O 83  ALA O 89  
OB 2 GLY O 41  ? HIS O 48  ? GLY O 41  HIS O 48  
OB 3 THR O 116 ? HIS O 120 ? THR O 116 HIS O 120 
OB 4 ARG O 143 ? VAL O 148 ? ARG O 143 VAL O 148 
PA 1 THR P 2   ? LYS P 9   ? THR P 2   LYS P 9   
PA 2 GLN P 15  ? GLN P 22  ? GLN P 15  GLN P 22  
PA 3 VAL P 29  ? LYS P 36  ? VAL P 29  LYS P 36  
PA 4 ALA P 95  ? ASP P 101 ? ALA P 95  ASP P 101 
PA 5 ASP P 83  ? ALA P 89  ? ASP P 83  ALA P 89  
PA 6 GLY P 41  ? HIS P 48  ? GLY P 41  HIS P 48  
PA 7 THR P 116 ? HIS P 120 ? THR P 116 HIS P 120 
PA 8 ARG P 143 ? ILE P 151 ? ARG P 143 ILE P 151 
PA 9 THR P 2   ? LYS P 9   ? THR P 2   LYS P 9   
QA 1 ALA Q 95  ? ASP Q 101 ? ALA Q 95  ASP Q 101 
QA 2 VAL Q 29  ? LYS Q 36  ? VAL Q 29  LYS Q 36  
QA 3 GLN Q 15  ? GLU Q 21  ? GLN Q 15  GLU Q 21  
QA 4 LYS Q 3   ? LEU Q 8   ? LYS Q 3   LEU Q 8   
QA 5 GLY Q 150 ? ILE Q 151 ? GLY Q 150 ILE Q 151 
QB 1 ASP Q 83  ? ALA Q 89  ? ASP Q 83  ALA Q 89  
QB 2 GLY Q 41  ? HIS Q 48  ? GLY Q 41  HIS Q 48  
QB 3 THR Q 116 ? HIS Q 120 ? THR Q 116 HIS Q 120 
QB 4 ARG Q 143 ? VAL Q 148 ? ARG Q 143 VAL Q 148 
SA 1 ALA R 95  ? ASP R 101 ? ALA S 95  ASP S 101 
SA 2 VAL R 29  ? LYS R 36  ? VAL S 29  LYS S 36  
SA 3 GLN R 15  ? GLN R 22  ? GLN S 15  GLN S 22  
SA 4 THR R 2   ? LEU R 8   ? THR S 2   LEU S 8   
SA 5 GLY R 150 ? ALA R 152 ? GLY S 150 ALA S 152 
SB 1 ASP R 83  ? ALA R 89  ? ASP S 83  ALA S 89  
SB 2 GLY R 41  ? HIS R 48  ? GLY S 41  HIS S 48  
SB 3 THR R 116 ? HIS R 120 ? THR S 116 HIS S 120 
SB 4 ARG R 143 ? VAL R 148 ? ARG S 143 VAL S 148 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA 1 2 N ASP A 101 ? N ASP A 101 O VAL A 29  ? O VAL A 29  
AA 2 3 N LYS A 36  ? N LYS A 36  O GLN A 15  ? O GLN A 15  
AA 3 4 N GLN A 22  ? N GLN A 22  O THR A 2   ? O THR A 2   
AA 4 5 N VAL A 5   ? N VAL A 5   O GLY A 150 ? O GLY A 150 
AB 1 2 N ALA A 89  ? N ALA A 89  O GLY A 41  ? O GLY A 41  
AB 2 3 N HIS A 48  ? N HIS A 48  O THR A 116 ? O THR A 116 
AB 3 4 O VAL A 119 ? O VAL A 119 N LEU A 144 ? N LEU A 144 
BA 1 2 N ASP B 101 ? N ASP B 101 O VAL B 29  ? O VAL B 29  
BA 2 3 N LYS B 36  ? N LYS B 36  O GLN B 15  ? O GLN B 15  
BA 3 4 N GLN B 22  ? N GLN B 22  O THR B 2   ? O THR B 2   
BA 4 5 N VAL B 5   ? N VAL B 5   O GLY B 150 ? O GLY B 150 
BB 1 2 N ALA B 89  ? N ALA B 89  O GLY B 41  ? O GLY B 41  
BB 2 3 N HIS B 48  ? N HIS B 48  O THR B 116 ? O THR B 116 
BB 3 4 O VAL B 119 ? O VAL B 119 N LEU B 144 ? N LEU B 144 
CA 1 2 N ASP C 101 ? N ASP C 101 O VAL C 29  ? O VAL C 29  
CA 2 3 N LYS C 36  ? N LYS C 36  O GLN C 15  ? O GLN C 15  
CA 3 4 N GLN C 22  ? N GLN C 22  O THR C 2   ? O THR C 2   
CA 4 5 N VAL C 5   ? N VAL C 5   O GLY C 150 ? O GLY C 150 
CB 1 2 N ALA C 89  ? N ALA C 89  O GLY C 41  ? O GLY C 41  
CB 2 3 N HIS C 48  ? N HIS C 48  O THR C 116 ? O THR C 116 
CB 3 4 O VAL C 119 ? O VAL C 119 N LEU C 144 ? N LEU C 144 
DA 1 2 N ASP D 101 ? N ASP D 101 O VAL D 29  ? O VAL D 29  
DA 2 3 N LYS D 36  ? N LYS D 36  O GLN D 15  ? O GLN D 15  
DA 3 4 N GLN D 22  ? N GLN D 22  O THR D 2   ? O THR D 2   
DA 4 5 N VAL D 5   ? N VAL D 5   O GLY D 150 ? O GLY D 150 
DB 1 2 N ALA D 89  ? N ALA D 89  O GLY D 41  ? O GLY D 41  
DB 2 3 N HIS D 48  ? N HIS D 48  O THR D 116 ? O THR D 116 
DB 3 4 O VAL D 119 ? O VAL D 119 N LEU D 144 ? N LEU D 144 
EA 1 2 N ASP E 101 ? N ASP E 101 O VAL E 29  ? O VAL E 29  
EA 2 3 N LYS E 36  ? N LYS E 36  O GLN E 15  ? O GLN E 15  
EA 3 4 N GLN E 22  ? N GLN E 22  O THR E 2   ? O THR E 2   
EA 4 5 N VAL E 5   ? N VAL E 5   O GLY E 150 ? O GLY E 150 
EB 1 2 N ALA E 89  ? N ALA E 89  O GLY E 41  ? O GLY E 41  
EB 2 3 N HIS E 48  ? N HIS E 48  O THR E 116 ? O THR E 116 
EB 3 4 O VAL E 119 ? O VAL E 119 N LEU E 144 ? N LEU E 144 
FA 1 2 N LEU F 8   ? N LEU F 8   O GLY F 16  ? O GLY F 16  
FA 2 3 N GLU F 21  ? N GLU F 21  O LYS F 30  ? O LYS F 30  
FA 3 4 N ILE F 35  ? N ILE F 35  O ALA F 95  ? O ALA F 95  
FA 4 5 N ASP F 96  ? N ASP F 96  O THR F 88  ? O THR F 88  
FA 5 6 N ALA F 89  ? N ALA F 89  O GLY F 41  ? O GLY F 41  
FA 6 7 N HIS F 48  ? N HIS F 48  O THR F 116 ? O THR F 116 
FA 7 8 O VAL F 119 ? O VAL F 119 N LEU F 144 ? N LEU F 144 
FA 8 9 N GLY F 150 ? N GLY F 150 O VAL F 5   ? O VAL F 5   
GA 1 2 N ASP G 101 ? N ASP G 101 O VAL G 29  ? O VAL G 29  
GA 2 3 N LYS G 36  ? N LYS G 36  O GLN G 15  ? O GLN G 15  
GA 3 4 N GLN G 22  ? N GLN G 22  O THR G 2   ? O THR G 2   
GA 4 5 N VAL G 5   ? N VAL G 5   O GLY G 150 ? O GLY G 150 
GB 1 2 N ALA G 89  ? N ALA G 89  O GLY G 41  ? O GLY G 41  
GB 2 3 N HIS G 48  ? N HIS G 48  O THR G 116 ? O THR G 116 
GB 3 4 O VAL G 119 ? O VAL G 119 N LEU G 144 ? N LEU G 144 
HA 1 2 N ASP H 101 ? N ASP H 101 O VAL H 29  ? O VAL H 29  
HA 2 3 N LYS H 36  ? N LYS H 36  O GLN H 15  ? O GLN H 15  
HA 3 4 N GLN H 22  ? N GLN H 22  O THR H 2   ? O THR H 2   
HA 4 5 N VAL H 5   ? N VAL H 5   O GLY H 150 ? O GLY H 150 
HB 1 2 N ALA H 89  ? N ALA H 89  O GLY H 41  ? O GLY H 41  
HB 2 3 N HIS H 48  ? N HIS H 48  O THR H 116 ? O THR H 116 
HB 3 4 O VAL H 119 ? O VAL H 119 N LEU H 144 ? N LEU H 144 
IA 1 2 N ASP I 101 ? N ASP I 101 O VAL I 29  ? O VAL I 29  
IA 2 3 N LYS I 36  ? N LYS I 36  O GLN I 15  ? O GLN I 15  
IA 3 4 N GLN I 22  ? N GLN I 22  O THR I 2   ? O THR I 2   
IA 4 5 N VAL I 5   ? N VAL I 5   O GLY I 150 ? O GLY I 150 
IB 1 2 N ALA I 89  ? N ALA I 89  O GLY I 41  ? O GLY I 41  
IB 2 3 N HIS I 48  ? N HIS I 48  O THR I 116 ? O THR I 116 
IB 3 4 O VAL I 119 ? O VAL I 119 N LEU I 144 ? N LEU I 144 
JA 1 2 N ASP J 101 ? N ASP J 101 O VAL J 29  ? O VAL J 29  
JA 2 3 N LYS J 36  ? N LYS J 36  O GLN J 15  ? O GLN J 15  
JA 3 4 N GLN J 22  ? N GLN J 22  O THR J 2   ? O THR J 2   
JA 4 5 N VAL J 5   ? N VAL J 5   O GLY J 150 ? O GLY J 150 
JB 1 2 N ALA J 89  ? N ALA J 89  O GLY J 41  ? O GLY J 41  
JB 2 3 N HIS J 48  ? N HIS J 48  O THR J 116 ? O THR J 116 
JB 3 4 O VAL J 119 ? O VAL J 119 N LEU J 144 ? N LEU J 144 
KA 1 2 N ASP K 101 ? N ASP K 101 O VAL K 29  ? O VAL K 29  
KA 2 3 N LYS K 36  ? N LYS K 36  O GLN K 15  ? O GLN K 15  
KA 3 4 N GLN K 22  ? N GLN K 22  O THR K 2   ? O THR K 2   
KA 4 5 N VAL K 5   ? N VAL K 5   O GLY K 150 ? O GLY K 150 
KB 1 2 N ALA K 89  ? N ALA K 89  O GLY K 41  ? O GLY K 41  
KB 2 3 N HIS K 48  ? N HIS K 48  O THR K 116 ? O THR K 116 
KB 3 4 O VAL K 119 ? O VAL K 119 N LEU K 144 ? N LEU K 144 
LA 1 2 N ASP L 101 ? N ASP L 101 O VAL L 29  ? O VAL L 29  
LA 2 3 N LYS L 36  ? N LYS L 36  O GLN L 15  ? O GLN L 15  
LA 3 4 N PHE L 20  ? N PHE L 20  O ALA L 4   ? O ALA L 4   
LA 4 5 N VAL L 5   ? N VAL L 5   O GLY L 150 ? O GLY L 150 
LB 1 2 N ALA L 89  ? N ALA L 89  O GLY L 41  ? O GLY L 41  
LB 2 3 N HIS L 48  ? N HIS L 48  O THR L 116 ? O THR L 116 
LB 3 4 O VAL L 119 ? O VAL L 119 N LEU L 144 ? N LEU L 144 
MA 1 2 N ASP M 101 ? N ASP M 101 O VAL M 29  ? O VAL M 29  
MA 2 3 N LYS M 36  ? N LYS M 36  O GLN M 15  ? O GLN M 15  
MA 3 4 N GLN M 22  ? N GLN M 22  O THR M 2   ? O THR M 2   
MA 4 5 N VAL M 5   ? N VAL M 5   O GLY M 150 ? O GLY M 150 
MB 1 2 N ALA M 89  ? N ALA M 89  O GLY M 41  ? O GLY M 41  
MB 2 3 N HIS M 48  ? N HIS M 48  O THR M 116 ? O THR M 116 
MB 3 4 O VAL M 119 ? O VAL M 119 N LEU M 144 ? N LEU M 144 
NA 1 2 N ASP N 101 ? N ASP N 101 O VAL N 29  ? O VAL N 29  
NA 2 3 N LYS N 36  ? N LYS N 36  O GLN N 15  ? O GLN N 15  
NA 3 4 N PHE N 20  ? N PHE N 20  O ALA N 4   ? O ALA N 4   
NA 4 5 N VAL N 5   ? N VAL N 5   O GLY N 150 ? O GLY N 150 
NB 1 2 N ALA N 89  ? N ALA N 89  O GLY N 41  ? O GLY N 41  
NB 2 3 N HIS N 48  ? N HIS N 48  O THR N 116 ? O THR N 116 
NB 3 4 O VAL N 119 ? O VAL N 119 N LEU N 144 ? N LEU N 144 
OA 1 2 N ASP O 101 ? N ASP O 101 O VAL O 29  ? O VAL O 29  
OA 2 3 N LYS O 36  ? N LYS O 36  O GLN O 15  ? O GLN O 15  
OA 3 4 N PHE O 20  ? N PHE O 20  O ALA O 4   ? O ALA O 4   
OA 4 5 N VAL O 5   ? N VAL O 5   O GLY O 150 ? O GLY O 150 
OB 1 2 N ALA O 89  ? N ALA O 89  O GLY O 41  ? O GLY O 41  
OB 2 3 N HIS O 48  ? N HIS O 48  O THR O 116 ? O THR O 116 
OB 3 4 O VAL O 119 ? O VAL O 119 N LEU O 144 ? N LEU O 144 
PA 1 2 N LEU P 8   ? N LEU P 8   O GLY P 16  ? O GLY P 16  
PA 2 3 N GLU P 21  ? N GLU P 21  O LYS P 30  ? O LYS P 30  
PA 3 4 N ILE P 35  ? N ILE P 35  O ALA P 95  ? O ALA P 95  
PA 4 5 N ASP P 96  ? N ASP P 96  O THR P 88  ? O THR P 88  
PA 5 6 N ALA P 89  ? N ALA P 89  O GLY P 41  ? O GLY P 41  
PA 6 7 N HIS P 48  ? N HIS P 48  O THR P 116 ? O THR P 116 
PA 7 8 O VAL P 119 ? O VAL P 119 N LEU P 144 ? N LEU P 144 
PA 8 9 N GLY P 150 ? N GLY P 150 O VAL P 5   ? O VAL P 5   
QA 1 2 N ASP Q 101 ? N ASP Q 101 O VAL Q 29  ? O VAL Q 29  
QA 2 3 N LYS Q 36  ? N LYS Q 36  O GLN Q 15  ? O GLN Q 15  
QA 3 4 N PHE Q 20  ? N PHE Q 20  O ALA Q 4   ? O ALA Q 4   
QA 4 5 N VAL Q 5   ? N VAL Q 5   O GLY Q 150 ? O GLY Q 150 
QB 1 2 N ALA Q 89  ? N ALA Q 89  O GLY Q 41  ? O GLY Q 41  
QB 2 3 N HIS Q 48  ? N HIS Q 48  O THR Q 116 ? O THR Q 116 
QB 3 4 O VAL Q 119 ? O VAL Q 119 N LEU Q 144 ? N LEU Q 144 
SA 1 2 N ASP R 101 ? N ASP S 101 O VAL R 29  ? O VAL S 29  
SA 2 3 N LYS R 36  ? N LYS S 36  O GLN R 15  ? O GLN S 15  
SA 3 4 N GLN R 22  ? N GLN S 22  O THR R 2   ? O THR S 2   
SA 4 5 N VAL R 5   ? N VAL S 5   O GLY R 150 ? O GLY S 150 
SB 1 2 N ALA R 89  ? N ALA S 89  O GLY R 41  ? O GLY S 41  
SB 2 3 N HIS R 48  ? N HIS S 48  O THR R 116 ? O THR S 116 
SB 3 4 O VAL R 119 ? O VAL S 119 N LEU R 144 ? N LEU S 144 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU A 154' 
AC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN A 155' 
AC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU B 154' 
AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN B 155' 
AC5 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU C 154' 
AC6 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN C 155' 
AC7 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE CA C 156' 
AC8 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU D 154' 
AC9 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN D 155' 
BC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CA D 156' 
BC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU E 154' 
BC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN E 155' 
BC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU F 154' 
BC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN F 155' 
BC6 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE CU G 154' 
BC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN G 155' 
BC8 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU H 154' 
BC9 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN H 155' 
CC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU I 154' 
CC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN I 155' 
CC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU J 154' 
CC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN J 155' 
CC5 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU K 154' 
CC6 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN K 155' 
CC7 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU L 154' 
CC8 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN L 155' 
CC9 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU M 154' 
DC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN M 155' 
DC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU N 154' 
DC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN N 155' 
DC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU O 154' 
DC5 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN O 155' 
DC6 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CA O 156' 
DC7 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU P 154' 
DC8 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN P 155' 
DC9 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CU Q 154' 
EC1 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN Q 155' 
EC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU S 154' 
EC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN S 155' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 5 HIS A  46  ? HIS A 46   . ? 1_555 ? 
2   AC1 5 HIS A  48  ? HIS A 48   . ? 1_555 ? 
3   AC1 5 HIS A  63  ? HIS A 63   . ? 1_555 ? 
4   AC1 5 HIS A  120 ? HIS A 120  . ? 1_555 ? 
5   AC1 5 HOH FB .   ? HOH A 2047 . ? 1_555 ? 
6   AC2 5 HIS A  63  ? HIS A 63   . ? 1_555 ? 
7   AC2 5 HIS A  71  ? HIS A 71   . ? 1_555 ? 
8   AC2 5 HIS A  80  ? HIS A 80   . ? 1_555 ? 
9   AC2 5 ASP A  83  ? ASP A 83   . ? 1_555 ? 
10  AC2 5 LYS A  136 ? LYS A 136  . ? 1_555 ? 
11  AC3 5 HIS B  46  ? HIS B 46   . ? 1_555 ? 
12  AC3 5 HIS B  48  ? HIS B 48   . ? 1_555 ? 
13  AC3 5 HIS B  63  ? HIS B 63   . ? 1_555 ? 
14  AC3 5 HIS B  120 ? HIS B 120  . ? 1_555 ? 
15  AC3 5 HOH GB .   ? HOH B 2083 . ? 1_555 ? 
16  AC4 4 HIS B  63  ? HIS B 63   . ? 1_555 ? 
17  AC4 4 HIS B  71  ? HIS B 71   . ? 1_555 ? 
18  AC4 4 HIS B  80  ? HIS B 80   . ? 1_555 ? 
19  AC4 4 ASP B  83  ? ASP B 83   . ? 1_555 ? 
20  AC5 5 HIS C  46  ? HIS C 46   . ? 1_555 ? 
21  AC5 5 HIS C  48  ? HIS C 48   . ? 1_555 ? 
22  AC5 5 HIS C  63  ? HIS C 63   . ? 1_555 ? 
23  AC5 5 HIS C  120 ? HIS C 120  . ? 1_555 ? 
24  AC5 5 HOH HB .   ? HOH C 2074 . ? 1_555 ? 
25  AC6 4 HIS C  63  ? HIS C 63   . ? 1_555 ? 
26  AC6 4 HIS C  71  ? HIS C 71   . ? 1_555 ? 
27  AC6 4 HIS C  80  ? HIS C 80   . ? 1_555 ? 
28  AC6 4 ASP C  83  ? ASP C 83   . ? 1_555 ? 
29  AC7 6 ASN C  26  ? ASN C 26   . ? 1_555 ? 
30  AC7 6 SER C  102 ? SER C 102  . ? 1_555 ? 
31  AC7 6 HOH HB .   ? HOH C 2035 . ? 1_555 ? 
32  AC7 6 HOH HB .   ? HOH C 2037 . ? 1_555 ? 
33  AC7 6 HOH HB .   ? HOH C 2038 . ? 1_555 ? 
34  AC7 6 HOH HB .   ? HOH C 2106 . ? 1_555 ? 
35  AC8 5 HIS D  46  ? HIS D 46   . ? 1_555 ? 
36  AC8 5 HIS D  48  ? HIS D 48   . ? 1_555 ? 
37  AC8 5 HIS D  63  ? HIS D 63   . ? 1_555 ? 
38  AC8 5 HIS D  120 ? HIS D 120  . ? 1_555 ? 
39  AC8 5 HOH IB .   ? HOH D 2049 . ? 1_555 ? 
40  AC9 4 HIS D  63  ? HIS D 63   . ? 1_555 ? 
41  AC9 4 HIS D  71  ? HIS D 71   . ? 1_555 ? 
42  AC9 4 HIS D  80  ? HIS D 80   . ? 1_555 ? 
43  AC9 4 ASP D  83  ? ASP D 83   . ? 1_555 ? 
44  BC1 5 HOH FB .   ? HOH A 2063 . ? 1_555 ? 
45  BC1 5 ASN D  26  ? ASN D 26   . ? 1_555 ? 
46  BC1 5 SER D  102 ? SER D 102  . ? 1_555 ? 
47  BC1 5 HOH IB .   ? HOH D 2024 . ? 1_555 ? 
48  BC1 5 HOH IB .   ? HOH D 2072 . ? 1_555 ? 
49  BC2 5 HIS E  46  ? HIS E 46   . ? 1_555 ? 
50  BC2 5 HIS E  48  ? HIS E 48   . ? 1_555 ? 
51  BC2 5 HIS E  63  ? HIS E 63   . ? 1_555 ? 
52  BC2 5 HIS E  120 ? HIS E 120  . ? 1_555 ? 
53  BC2 5 HOH JB .   ? HOH E 2052 . ? 1_555 ? 
54  BC3 4 HIS E  63  ? HIS E 63   . ? 1_555 ? 
55  BC3 4 HIS E  71  ? HIS E 71   . ? 1_555 ? 
56  BC3 4 HIS E  80  ? HIS E 80   . ? 1_555 ? 
57  BC3 4 ASP E  83  ? ASP E 83   . ? 1_555 ? 
58  BC4 5 HIS F  46  ? HIS F 46   . ? 1_555 ? 
59  BC4 5 HIS F  48  ? HIS F 48   . ? 1_555 ? 
60  BC4 5 HIS F  63  ? HIS F 63   . ? 1_555 ? 
61  BC4 5 HIS F  120 ? HIS F 120  . ? 1_555 ? 
62  BC4 5 HOH KB .   ? HOH F 2040 . ? 1_555 ? 
63  BC5 4 HIS F  63  ? HIS F 63   . ? 1_555 ? 
64  BC5 4 HIS F  71  ? HIS F 71   . ? 1_555 ? 
65  BC5 4 HIS F  80  ? HIS F 80   . ? 1_555 ? 
66  BC5 4 ASP F  83  ? ASP F 83   . ? 1_555 ? 
67  BC6 6 HIS G  46  ? HIS G 46   . ? 1_555 ? 
68  BC6 6 HIS G  48  ? HIS G 48   . ? 1_555 ? 
69  BC6 6 HIS G  63  ? HIS G 63   . ? 1_555 ? 
70  BC6 6 HIS G  120 ? HIS G 120  . ? 1_555 ? 
71  BC6 6 HOH LB .   ? HOH G 2010 . ? 1_555 ? 
72  BC6 6 HOH LB .   ? HOH G 2022 . ? 1_555 ? 
73  BC7 5 HIS G  63  ? HIS G 63   . ? 1_555 ? 
74  BC7 5 HIS G  71  ? HIS G 71   . ? 1_555 ? 
75  BC7 5 HIS G  80  ? HIS G 80   . ? 1_555 ? 
76  BC7 5 ASP G  83  ? ASP G 83   . ? 1_555 ? 
77  BC7 5 LYS G  136 ? LYS G 136  . ? 1_555 ? 
78  BC8 5 HIS H  46  ? HIS H 46   . ? 1_555 ? 
79  BC8 5 HIS H  48  ? HIS H 48   . ? 1_555 ? 
80  BC8 5 HIS H  63  ? HIS H 63   . ? 1_555 ? 
81  BC8 5 HIS H  120 ? HIS H 120  . ? 1_555 ? 
82  BC8 5 HOH MB .   ? HOH H 2050 . ? 1_555 ? 
83  BC9 4 HIS H  63  ? HIS H 63   . ? 1_555 ? 
84  BC9 4 HIS H  71  ? HIS H 71   . ? 1_555 ? 
85  BC9 4 HIS H  80  ? HIS H 80   . ? 1_555 ? 
86  BC9 4 ASP H  83  ? ASP H 83   . ? 1_555 ? 
87  CC1 5 HIS I  46  ? HIS I 46   . ? 1_555 ? 
88  CC1 5 HIS I  48  ? HIS I 48   . ? 1_555 ? 
89  CC1 5 HIS I  63  ? HIS I 63   . ? 1_555 ? 
90  CC1 5 HIS I  120 ? HIS I 120  . ? 1_555 ? 
91  CC1 5 HOH NB .   ? HOH I 2069 . ? 1_555 ? 
92  CC2 4 HIS I  63  ? HIS I 63   . ? 1_555 ? 
93  CC2 4 HIS I  71  ? HIS I 71   . ? 1_555 ? 
94  CC2 4 HIS I  80  ? HIS I 80   . ? 1_555 ? 
95  CC2 4 ASP I  83  ? ASP I 83   . ? 1_555 ? 
96  CC3 5 HIS J  46  ? HIS J 46   . ? 1_555 ? 
97  CC3 5 HIS J  48  ? HIS J 48   . ? 1_555 ? 
98  CC3 5 HIS J  63  ? HIS J 63   . ? 1_555 ? 
99  CC3 5 HIS J  120 ? HIS J 120  . ? 1_555 ? 
100 CC3 5 HOH OB .   ? HOH J 2064 . ? 1_555 ? 
101 CC4 4 HIS J  63  ? HIS J 63   . ? 1_555 ? 
102 CC4 4 HIS J  71  ? HIS J 71   . ? 1_555 ? 
103 CC4 4 HIS J  80  ? HIS J 80   . ? 1_555 ? 
104 CC4 4 ASP J  83  ? ASP J 83   . ? 1_555 ? 
105 CC5 5 HIS K  46  ? HIS K 46   . ? 1_555 ? 
106 CC5 5 HIS K  48  ? HIS K 48   . ? 1_555 ? 
107 CC5 5 HIS K  63  ? HIS K 63   . ? 1_555 ? 
108 CC5 5 HIS K  120 ? HIS K 120  . ? 1_555 ? 
109 CC5 5 HOH PB .   ? HOH K 2063 . ? 1_555 ? 
110 CC6 5 HIS K  63  ? HIS K 63   . ? 1_555 ? 
111 CC6 5 HIS K  71  ? HIS K 71   . ? 1_555 ? 
112 CC6 5 HIS K  80  ? HIS K 80   . ? 1_555 ? 
113 CC6 5 ASP K  83  ? ASP K 83   . ? 1_555 ? 
114 CC6 5 LYS K  136 ? LYS K 136  . ? 1_555 ? 
115 CC7 4 HIS L  46  ? HIS L 46   . ? 1_555 ? 
116 CC7 4 HIS L  48  ? HIS L 48   . ? 1_555 ? 
117 CC7 4 HIS L  63  ? HIS L 63   . ? 1_555 ? 
118 CC7 4 HIS L  120 ? HIS L 120  . ? 1_555 ? 
119 CC8 4 HIS L  63  ? HIS L 63   . ? 1_555 ? 
120 CC8 4 HIS L  71  ? HIS L 71   . ? 1_555 ? 
121 CC8 4 HIS L  80  ? HIS L 80   . ? 1_555 ? 
122 CC8 4 ASP L  83  ? ASP L 83   . ? 1_555 ? 
123 CC9 5 HIS M  46  ? HIS M 46   . ? 1_555 ? 
124 CC9 5 HIS M  48  ? HIS M 48   . ? 1_555 ? 
125 CC9 5 HIS M  63  ? HIS M 63   . ? 1_555 ? 
126 CC9 5 HIS M  120 ? HIS M 120  . ? 1_555 ? 
127 CC9 5 HOH RB .   ? HOH M 2041 . ? 1_555 ? 
128 DC1 5 HIS M  63  ? HIS M 63   . ? 1_555 ? 
129 DC1 5 HIS M  71  ? HIS M 71   . ? 1_555 ? 
130 DC1 5 HIS M  80  ? HIS M 80   . ? 1_555 ? 
131 DC1 5 ASP M  83  ? ASP M 83   . ? 1_555 ? 
132 DC1 5 LYS M  136 ? LYS M 136  . ? 1_555 ? 
133 DC2 5 HIS N  46  ? HIS N 46   . ? 1_555 ? 
134 DC2 5 HIS N  48  ? HIS N 48   . ? 1_555 ? 
135 DC2 5 HIS N  63  ? HIS N 63   . ? 1_555 ? 
136 DC2 5 HIS N  120 ? HIS N 120  . ? 1_555 ? 
137 DC2 5 HOH SB .   ? HOH N 2038 . ? 1_555 ? 
138 DC3 4 HIS N  63  ? HIS N 63   . ? 1_555 ? 
139 DC3 4 HIS N  71  ? HIS N 71   . ? 1_555 ? 
140 DC3 4 HIS N  80  ? HIS N 80   . ? 1_555 ? 
141 DC3 4 ASP N  83  ? ASP N 83   . ? 1_555 ? 
142 DC4 4 HIS O  46  ? HIS O 46   . ? 1_555 ? 
143 DC4 4 HIS O  48  ? HIS O 48   . ? 1_555 ? 
144 DC4 4 HIS O  63  ? HIS O 63   . ? 1_555 ? 
145 DC4 4 HIS O  120 ? HIS O 120  . ? 1_555 ? 
146 DC5 5 HIS O  63  ? HIS O 63   . ? 1_555 ? 
147 DC5 5 HIS O  71  ? HIS O 71   . ? 1_555 ? 
148 DC5 5 HIS O  80  ? HIS O 80   . ? 1_555 ? 
149 DC5 5 ASP O  83  ? ASP O 83   . ? 1_555 ? 
150 DC5 5 LYS O  136 ? LYS O 136  . ? 1_555 ? 
151 DC6 5 ASN H  26  ? ASN H 26   . ? 1_555 ? 
152 DC6 5 SER H  102 ? SER H 102  . ? 1_555 ? 
153 DC6 5 HOH MB .   ? HOH H 2081 . ? 1_555 ? 
154 DC6 5 HOH MB .   ? HOH H 2084 . ? 1_555 ? 
155 DC6 5 HOH MB .   ? HOH H 2085 . ? 1_555 ? 
156 DC7 4 HIS P  46  ? HIS P 46   . ? 1_555 ? 
157 DC7 4 HIS P  48  ? HIS P 48   . ? 1_555 ? 
158 DC7 4 HIS P  63  ? HIS P 63   . ? 1_555 ? 
159 DC7 4 HIS P  120 ? HIS P 120  . ? 1_555 ? 
160 DC8 4 HIS P  63  ? HIS P 63   . ? 1_555 ? 
161 DC8 4 HIS P  71  ? HIS P 71   . ? 1_555 ? 
162 DC8 4 HIS P  80  ? HIS P 80   . ? 1_555 ? 
163 DC8 4 ASP P  83  ? ASP P 83   . ? 1_555 ? 
164 DC9 5 HIS Q  46  ? HIS Q 46   . ? 1_555 ? 
165 DC9 5 HIS Q  48  ? HIS Q 48   . ? 1_555 ? 
166 DC9 5 HIS Q  63  ? HIS Q 63   . ? 1_555 ? 
167 DC9 5 HIS Q  120 ? HIS Q 120  . ? 1_555 ? 
168 DC9 5 HOH VB .   ? HOH Q 2040 . ? 1_555 ? 
169 EC1 4 HIS Q  63  ? HIS Q 63   . ? 1_555 ? 
170 EC1 4 HIS Q  71  ? HIS Q 71   . ? 1_555 ? 
171 EC1 4 HIS Q  80  ? HIS Q 80   . ? 1_555 ? 
172 EC1 4 ASP Q  83  ? ASP Q 83   . ? 1_555 ? 
173 EC2 4 HIS R  46  ? HIS S 46   . ? 1_555 ? 
174 EC2 4 HIS R  48  ? HIS S 48   . ? 1_555 ? 
175 EC2 4 HIS R  63  ? HIS S 63   . ? 1_555 ? 
176 EC2 4 HIS R  120 ? HIS S 120  . ? 1_555 ? 
177 EC3 4 HIS R  63  ? HIS S 63   . ? 1_555 ? 
178 EC3 4 HIS R  71  ? HIS S 71   . ? 1_555 ? 
179 EC3 4 HIS R  80  ? HIS S 80   . ? 1_555 ? 
180 EC3 4 ASP R  83  ? ASP S 83   . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          1HL5 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    1HL5 
_atom_sites.fract_transf_matrix[1][1]   0.013009 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000784 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.005801 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.008909 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CA 
CU 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . ALA A  1 1   ? 51.772  73.156  80.900  1.00 24.48 ? 1    ALA A N   1 
ATOM   2     C  CA  . ALA A  1 1   ? 50.944  74.285  80.381  1.00 24.66 ? 1    ALA A CA  1 
ATOM   3     C  C   . ALA A  1 1   ? 50.036  74.831  81.463  1.00 24.12 ? 1    ALA A C   1 
ATOM   4     O  O   . ALA A  1 1   ? 49.705  74.138  82.419  1.00 24.68 ? 1    ALA A O   1 
ATOM   5     C  CB  . ALA A  1 1   ? 50.106  73.837  79.179  1.00 25.01 ? 1    ALA A CB  1 
ATOM   6     N  N   . THR A  1 2   ? 49.626  76.076  81.313  1.00 22.95 ? 2    THR A N   1 
ATOM   7     C  CA  . THR A  1 2   ? 48.726  76.671  82.268  1.00 22.16 ? 2    THR A CA  1 
ATOM   8     C  C   . THR A  1 2   ? 47.525  77.209  81.496  1.00 20.09 ? 2    THR A C   1 
ATOM   9     O  O   . THR A  1 2   ? 47.640  77.647  80.332  1.00 20.24 ? 2    THR A O   1 
ATOM   10    C  CB  . THR A  1 2   ? 49.494  77.703  83.117  1.00 22.55 ? 2    THR A CB  1 
ATOM   11    O  OG1 . THR A  1 2   ? 48.602  78.689  83.654  1.00 26.07 ? 2    THR A OG1 1 
ATOM   12    C  CG2 . THR A  1 2   ? 50.434  78.485  82.236  1.00 24.87 ? 2    THR A CG2 1 
ATOM   13    N  N   . LYS A  1 3   ? 46.364  77.104  82.119  1.00 17.81 ? 3    LYS A N   1 
ATOM   14    C  CA  . LYS A  1 3   ? 45.115  77.482  81.502  1.00 16.01 ? 3    LYS A CA  1 
ATOM   15    C  C   . LYS A  1 3   ? 44.342  78.424  82.402  1.00 14.67 ? 3    LYS A C   1 
ATOM   16    O  O   . LYS A  1 3   ? 44.330  78.245  83.619  1.00 14.24 ? 3    LYS A O   1 
ATOM   17    C  CB  . LYS A  1 3   ? 44.254  76.243  81.308  1.00 16.41 ? 3    LYS A CB  1 
ATOM   18    C  CG  . LYS A  1 3   ? 44.863  75.188  80.406  1.00 19.64 ? 3    LYS A CG  1 
ATOM   19    C  CD  . LYS A  1 3   ? 43.784  74.266  79.860  1.00 23.50 ? 3    LYS A CD  1 
ATOM   20    C  CE  . LYS A  1 3   ? 44.390  73.006  79.315  1.00 26.01 ? 3    LYS A CE  1 
ATOM   21    N  NZ  . LYS A  1 3   ? 44.818  73.184  77.902  1.00 28.55 ? 3    LYS A NZ  1 
ATOM   22    N  N   . ALA A  1 4   ? 43.669  79.397  81.807  1.00 13.29 ? 4    ALA A N   1 
ATOM   23    C  CA  . ALA A  1 4   ? 42.829  80.318  82.572  1.00 11.52 ? 4    ALA A CA  1 
ATOM   24    C  C   . ALA A  1 4   ? 41.562  80.605  81.793  1.00 11.91 ? 4    ALA A C   1 
ATOM   25    O  O   . ALA A  1 4   ? 41.482  80.314  80.593  1.00 10.43 ? 4    ALA A O   1 
ATOM   26    C  CB  . ALA A  1 4   ? 43.576  81.598  82.902  1.00 10.77 ? 4    ALA A CB  1 
ATOM   27    N  N   . VAL A  1 5   ? 40.580  81.194  82.467  1.00 11.17 ? 5    VAL A N   1 
ATOM   28    C  CA  . VAL A  1 5   ? 39.308  81.470  81.840  1.00 10.78 ? 5    VAL A CA  1 
ATOM   29    C  C   . VAL A  1 5   ? 38.732  82.720  82.480  1.00 10.78 ? 5    VAL A C   1 
ATOM   30    O  O   . VAL A  1 5   ? 39.032  83.044  83.646  1.00 10.20 ? 5    VAL A O   1 
ATOM   31    C  CB  . VAL A  1 5   ? 38.356  80.267  82.035  1.00 11.47 ? 5    VAL A CB  1 
ATOM   32    C  CG1 . VAL A  1 5   ? 37.938  80.131  83.513  1.00 11.97 ? 5    VAL A CG1 1 
ATOM   33    C  CG2 . VAL A  1 5   ? 37.133  80.370  81.127  1.00 11.68 ? 5    VAL A CG2 1 
ATOM   34    N  N   . CYS A  1 6   ? 37.858  83.389  81.751  1.00 10.19 ? 6    CYS A N   1 
ATOM   35    C  CA  . CYS A  1 6   ? 37.257  84.617  82.227  1.00 10.66 ? 6    CYS A CA  1 
ATOM   36    C  C   . CYS A  1 6   ? 35.815  84.679  81.738  1.00 10.89 ? 6    CYS A C   1 
ATOM   37    O  O   . CYS A  1 6   ? 35.547  84.520  80.530  1.00 10.12 ? 6    CYS A O   1 
ATOM   38    C  CB  . CYS A  1 6   ? 38.015  85.807  81.664  1.00 12.08 ? 6    CYS A CB  1 
ATOM   39    S  SG  . CYS A  1 6   ? 37.407  87.367  82.343  1.00 12.36 ? 6    CYS A SG  1 
ATOM   40    N  N   . VAL A  1 7   ? 34.886  84.894  82.665  1.00 9.03  ? 7    VAL A N   1 
ATOM   41    C  CA  . VAL A  1 7   ? 33.501  85.115  82.285  1.00 9.06  ? 7    VAL A CA  1 
ATOM   42    C  C   . VAL A  1 7   ? 33.244  86.603  82.307  1.00 9.43  ? 7    VAL A C   1 
ATOM   43    O  O   . VAL A  1 7   ? 33.359  87.234  83.366  1.00 9.64  ? 7    VAL A O   1 
ATOM   44    C  CB  . VAL A  1 7   ? 32.537  84.386  83.258  1.00 9.36  ? 7    VAL A CB  1 
ATOM   45    C  CG1 . VAL A  1 7   ? 31.068  84.660  82.861  1.00 8.75  ? 7    VAL A CG1 1 
ATOM   46    C  CG2 . VAL A  1 7   ? 32.836  82.937  83.194  1.00 10.69 ? 7    VAL A CG2 1 
ATOM   47    N  N   . LEU A  1 8   ? 32.904  87.179  81.154  1.00 10.21 ? 8    LEU A N   1 
ATOM   48    C  CA  . LEU A  1 8   ? 32.633  88.611  81.098  1.00 11.50 ? 8    LEU A CA  1 
ATOM   49    C  C   . LEU A  1 8   ? 31.150  88.889  81.302  1.00 11.76 ? 8    LEU A C   1 
ATOM   50    O  O   . LEU A  1 8   ? 30.317  88.253  80.662  1.00 10.98 ? 8    LEU A O   1 
ATOM   51    C  CB  . LEU A  1 8   ? 33.008  89.184  79.729  1.00 12.51 ? 8    LEU A CB  1 
ATOM   52    C  CG  . LEU A  1 8   ? 34.417  89.563  79.251  1.00 16.83 ? 8    LEU A CG  1 
ATOM   53    C  CD1 . LEU A  1 8   ? 35.480  88.867  79.962  1.00 21.31 ? 8    LEU A CD1 1 
ATOM   54    C  CD2 . LEU A  1 8   ? 34.534  89.354  77.716  1.00 18.09 ? 8    LEU A CD2 1 
ATOM   55    N  N   . LYS A  1 9   ? 30.850  89.848  82.184  1.00 11.35 ? 9    LYS A N   1 
ATOM   56    C  CA  . LYS A  1 9   ? 29.496  90.313  82.457  1.00 12.46 ? 9    LYS A CA  1 
ATOM   57    C  C   . LYS A  1 9   ? 29.493  91.812  82.715  1.00 12.13 ? 9    LYS A C   1 
ATOM   58    O  O   . LYS A  1 9   ? 30.482  92.331  83.202  1.00 11.56 ? 9    LYS A O   1 
ATOM   59    C  CB  . LYS A  1 9   ? 28.960  89.620  83.724  1.00 12.98 ? 9    LYS A CB  1 
ATOM   60    C  CG  . LYS A  1 9   ? 28.722  88.140  83.572  1.00 17.22 ? 9    LYS A CG  1 
ATOM   61    C  CD  . LYS A  1 9   ? 27.957  87.587  84.794  1.00 21.40 ? 9    LYS A CD  1 
ATOM   62    C  CE  . LYS A  1 9   ? 26.819  86.696  84.341  1.00 25.55 ? 9    LYS A CE  1 
ATOM   63    N  NZ  . LYS A  1 9   ? 27.247  85.725  83.276  1.00 27.78 ? 9    LYS A NZ  1 
ATOM   64    N  N   . GLY A  1 10  ? 28.364  92.492  82.467  1.00 13.04 ? 10   GLY A N   1 
ATOM   65    C  CA  . GLY A  1 10  ? 28.226  93.925  82.762  1.00 14.45 ? 10   GLY A CA  1 
ATOM   66    C  C   . GLY A  1 10  ? 26.797  94.354  83.124  1.00 15.84 ? 10   GLY A C   1 
ATOM   67    O  O   . GLY A  1 10  ? 25.957  93.518  83.467  1.00 13.89 ? 10   GLY A O   1 
ATOM   68    N  N   . ASP A  1 11  ? 26.517  95.654  83.044  1.00 16.66 ? 11   ASP A N   1 
ATOM   69    C  CA  . ASP A  1 11  ? 25.174  96.153  83.338  1.00 18.57 ? 11   ASP A CA  1 
ATOM   70    C  C   . ASP A  1 11  ? 24.218  96.088  82.140  1.00 18.16 ? 11   ASP A C   1 
ATOM   71    O  O   . ASP A  1 11  ? 23.012  96.362  82.280  1.00 17.47 ? 11   ASP A O   1 
ATOM   72    C  CB  . ASP A  1 11  ? 25.252  97.590  83.855  1.00 20.15 ? 11   ASP A CB  1 
ATOM   73    C  CG  . ASP A  1 11  ? 26.114  97.712  85.097  1.00 24.39 ? 11   ASP A CG  1 
ATOM   74    O  OD1 . ASP A  1 11  ? 26.123  96.751  85.902  1.00 27.75 ? 11   ASP A OD1 1 
ATOM   75    O  OD2 . ASP A  1 11  ? 26.823  98.723  85.346  1.00 28.78 ? 11   ASP A OD2 1 
ATOM   76    N  N   . GLY A  1 12  ? 24.742  95.744  80.966  1.00 16.24 ? 12   GLY A N   1 
ATOM   77    C  CA  . GLY A  1 12  ? 23.915  95.653  79.774  1.00 16.22 ? 12   GLY A CA  1 
ATOM   78    C  C   . GLY A  1 12  ? 23.893  94.252  79.206  1.00 15.63 ? 12   GLY A C   1 
ATOM   79    O  O   . GLY A  1 12  ? 24.167  93.298  79.917  1.00 16.52 ? 12   GLY A O   1 
ATOM   80    N  N   . PRO A  1 13  ? 23.649  94.142  77.912  1.00 15.58 ? 13   PRO A N   1 
ATOM   81    C  CA  . PRO A  1 13  ? 23.503  92.848  77.239  1.00 15.59 ? 13   PRO A CA  1 
ATOM   82    C  C   . PRO A  1 13  ? 24.834  92.144  76.908  1.00 15.35 ? 13   PRO A C   1 
ATOM   83    O  O   . PRO A  1 13  ? 24.800  91.001  76.435  1.00 15.50 ? 13   PRO A O   1 
ATOM   84    C  CB  . PRO A  1 13  ? 22.823  93.211  75.920  1.00 15.91 ? 13   PRO A CB  1 
ATOM   85    C  CG  . PRO A  1 13  ? 22.921  94.685  75.768  1.00 16.43 ? 13   PRO A CG  1 
ATOM   86    C  CD  . PRO A  1 13  ? 23.581  95.271  76.977  1.00 15.79 ? 13   PRO A CD  1 
ATOM   87    N  N   . VAL A  1 14  ? 25.967  92.786  77.152  1.00 13.85 ? 14   VAL A N   1 
ATOM   88    C  CA  . VAL A  1 14  ? 27.249  92.172  76.770  1.00 12.73 ? 14   VAL A CA  1 
ATOM   89    C  C   . VAL A  1 14  ? 27.717  91.056  77.689  1.00 13.00 ? 14   VAL A C   1 
ATOM   90    O  O   . VAL A  1 14  ? 27.828  91.226  78.901  1.00 12.39 ? 14   VAL A O   1 
ATOM   91    C  CB  . VAL A  1 14  ? 28.370  93.208  76.628  1.00 12.59 ? 14   VAL A CB  1 
ATOM   92    C  CG1 . VAL A  1 14  ? 29.673  92.495  76.228  1.00 11.36 ? 14   VAL A CG1 1 
ATOM   93    C  CG2 . VAL A  1 14  ? 27.976  94.228  75.597  1.00 11.15 ? 14   VAL A CG2 1 
ATOM   94    N  N   . GLN A  1 15  ? 27.955  89.884  77.127  1.00 13.16 ? 15   GLN A N   1 
ATOM   95    C  CA  . GLN A  1 15  ? 28.466  88.804  77.965  1.00 13.95 ? 15   GLN A CA  1 
ATOM   96    C  C   . GLN A  1 15  ? 29.335  87.874  77.131  1.00 12.64 ? 15   GLN A C   1 
ATOM   97    O  O   . GLN A  1 15  ? 29.154  87.779  75.935  1.00 13.41 ? 15   GLN A O   1 
ATOM   98    C  CB  . GLN A  1 15  ? 27.342  88.062  78.724  1.00 15.16 ? 15   GLN A CB  1 
ATOM   99    C  CG  . GLN A  1 15  ? 26.383  87.317  77.887  1.00 17.71 ? 15   GLN A CG  1 
ATOM   100   C  CD  . GLN A  1 15  ? 25.019  87.018  78.591  1.00 20.95 ? 15   GLN A CD  1 
ATOM   101   O  OE1 . GLN A  1 15  ? 24.094  86.590  77.933  1.00 24.10 ? 15   GLN A OE1 1 
ATOM   102   N  NE2 . GLN A  1 15  ? 24.914  87.253  79.889  1.00 25.99 ? 15   GLN A NE2 1 
ATOM   103   N  N   . GLY A  1 16  ? 30.263  87.185  77.760  1.00 11.91 ? 16   GLY A N   1 
ATOM   104   C  CA  . GLY A  1 16  ? 31.146  86.333  77.005  1.00 11.62 ? 16   GLY A CA  1 
ATOM   105   C  C   . GLY A  1 16  ? 31.955  85.423  77.875  1.00 10.82 ? 16   GLY A C   1 
ATOM   106   O  O   . GLY A  1 16  ? 31.862  85.471  79.109  1.00 10.02 ? 16   GLY A O   1 
ATOM   107   N  N   . ILE A  1 17  ? 32.709  84.558  77.211  1.00 9.89  ? 17   ILE A N   1 
ATOM   108   C  CA  . ILE A  1 17  ? 33.624  83.643  77.866  1.00 9.90  ? 17   ILE A CA  1 
ATOM   109   C  C   . ILE A  1 17  ? 34.944  83.654  77.075  1.00 9.02  ? 17   ILE A C   1 
ATOM   110   O  O   . ILE A  1 17  ? 34.964  83.381  75.865  1.00 9.65  ? 17   ILE A O   1 
ATOM   111   C  CB  . ILE A  1 17  ? 33.045  82.239  77.868  1.00 9.65  ? 17   ILE A CB  1 
ATOM   112   C  CG1 . ILE A  1 17  ? 31.757  82.203  78.704  1.00 9.04  ? 17   ILE A CG1 1 
ATOM   113   C  CG2 . ILE A  1 17  ? 34.070  81.256  78.392  1.00 10.87 ? 17   ILE A CG2 1 
ATOM   114   C  CD1 . ILE A  1 17  ? 31.070  80.821  78.742  1.00 13.62 ? 17   ILE A CD1 1 
ATOM   115   N  N   . ILE A  1 18  ? 36.044  83.949  77.752  1.00 8.57  ? 18   ILE A N   1 
ATOM   116   C  CA  . ILE A  1 18  ? 37.346  83.977  77.095  1.00 9.95  ? 18   ILE A CA  1 
ATOM   117   C  C   . ILE A  1 18  ? 38.306  83.023  77.764  1.00 10.31 ? 18   ILE A C   1 
ATOM   118   O  O   . ILE A  1 18  ? 38.464  83.034  78.996  1.00 10.94 ? 18   ILE A O   1 
ATOM   119   C  CB  . ILE A  1 18  ? 37.924  85.408  77.146  1.00 10.66 ? 18   ILE A CB  1 
ATOM   120   C  CG1 . ILE A  1 18  ? 37.005  86.406  76.420  1.00 10.45 ? 18   ILE A CG1 1 
ATOM   121   C  CG2 . ILE A  1 18  ? 39.368  85.439  76.639  1.00 10.20 ? 18   ILE A CG2 1 
ATOM   122   C  CD1 . ILE A  1 18  ? 36.912  86.179  74.883  1.00 9.37  ? 18   ILE A CD1 1 
ATOM   123   N  N   . ASN A  1 19  ? 38.993  82.231  76.947  1.00 9.85  ? 19   ASN A N   1 
ATOM   124   C  CA  . ASN A  1 19  ? 39.951  81.251  77.436  1.00 10.64 ? 19   ASN A CA  1 
ATOM   125   C  C   . ASN A  1 19  ? 41.362  81.728  77.197  1.00 10.14 ? 19   ASN A C   1 
ATOM   126   O  O   . ASN A  1 19  ? 41.604  82.469  76.253  1.00 9.69  ? 19   ASN A O   1 
ATOM   127   C  CB  . ASN A  1 19  ? 39.746  79.923  76.697  1.00 11.52 ? 19   ASN A CB  1 
ATOM   128   C  CG  . ASN A  1 19  ? 38.309  79.454  76.756  1.00 13.45 ? 19   ASN A CG  1 
ATOM   129   O  OD1 . ASN A  1 19  ? 37.540  79.644  75.812  1.00 17.25 ? 19   ASN A OD1 1 
ATOM   130   N  ND2 . ASN A  1 19  ? 37.920  78.885  77.889  1.00 9.08  ? 19   ASN A ND2 1 
ATOM   131   N  N   . PHE A  1 20  ? 42.290  81.266  78.038  1.00 10.73 ? 20   PHE A N   1 
ATOM   132   C  CA  . PHE A  1 20  ? 43.695  81.608  77.931  1.00 11.85 ? 20   PHE A CA  1 
ATOM   133   C  C   . PHE A  1 20  ? 44.511  80.329  78.048  1.00 13.09 ? 20   PHE A C   1 
ATOM   134   O  O   . PHE A  1 20  ? 44.270  79.514  78.925  1.00 12.04 ? 20   PHE A O   1 
ATOM   135   C  CB  . PHE A  1 20  ? 44.133  82.509  79.089  1.00 12.00 ? 20   PHE A CB  1 
ATOM   136   C  CG  . PHE A  1 20  ? 43.415  83.831  79.158  1.00 10.70 ? 20   PHE A CG  1 
ATOM   137   C  CD1 . PHE A  1 20  ? 42.177  83.920  79.774  1.00 11.75 ? 20   PHE A CD1 1 
ATOM   138   C  CD2 . PHE A  1 20  ? 43.986  84.978  78.643  1.00 11.43 ? 20   PHE A CD2 1 
ATOM   139   C  CE1 . PHE A  1 20  ? 41.514  85.105  79.854  1.00 12.98 ? 20   PHE A CE1 1 
ATOM   140   C  CE2 . PHE A  1 20  ? 43.318  86.208  78.736  1.00 11.85 ? 20   PHE A CE2 1 
ATOM   141   C  CZ  . PHE A  1 20  ? 42.082  86.265  79.351  1.00 12.88 ? 20   PHE A CZ  1 
ATOM   142   N  N   . GLU A  1 21  ? 45.511  80.158  77.199  1.00 13.34 ? 21   GLU A N   1 
ATOM   143   C  CA  . GLU A  1 21  ? 46.332  78.953  77.305  1.00 14.17 ? 21   GLU A CA  1 
ATOM   144   C  C   . GLU A  1 21  ? 47.786  79.304  77.060  1.00 14.25 ? 21   GLU A C   1 
ATOM   145   O  O   . GLU A  1 21  ? 48.105  80.030  76.135  1.00 12.68 ? 21   GLU A O   1 
ATOM   146   C  CB  . GLU A  1 21  ? 45.905  77.881  76.294  1.00 15.14 ? 21   GLU A CB  1 
ATOM   147   C  CG  . GLU A  1 21  ? 46.319  76.488  76.747  1.00 19.05 ? 21   GLU A CG  1 
ATOM   148   C  CD  . GLU A  1 21  ? 46.051  75.377  75.738  1.00 26.34 ? 21   GLU A CD  1 
ATOM   149   O  OE1 . GLU A  1 21  ? 45.237  75.543  74.790  1.00 29.25 ? 21   GLU A OE1 1 
ATOM   150   O  OE2 . GLU A  1 21  ? 46.694  74.323  75.886  1.00 29.41 ? 21   GLU A OE2 1 
ATOM   151   N  N   . GLN A  1 22  ? 48.670  78.801  77.899  1.00 14.30 ? 22   GLN A N   1 
ATOM   152   C  CA  . GLN A  1 22  ? 50.089  79.070  77.742  1.00 16.33 ? 22   GLN A CA  1 
ATOM   153   C  C   . GLN A  1 22  ? 50.782  77.725  77.904  1.00 18.57 ? 22   GLN A C   1 
ATOM   154   O  O   . GLN A  1 22  ? 50.590  77.024  78.904  1.00 18.23 ? 22   GLN A O   1 
ATOM   155   C  CB  . GLN A  1 22  ? 50.577  80.090  78.779  1.00 15.59 ? 22   GLN A CB  1 
ATOM   156   C  CG  . GLN A  1 22  ? 51.921  80.732  78.440  1.00 15.92 ? 22   GLN A CG  1 
ATOM   157   C  CD  . GLN A  1 22  ? 52.421  81.682  79.539  1.00 16.09 ? 22   GLN A CD  1 
ATOM   158   O  OE1 . GLN A  1 22  ? 52.021  81.568  80.699  1.00 16.50 ? 22   GLN A OE1 1 
ATOM   159   N  NE2 . GLN A  1 22  ? 53.284  82.606  79.171  1.00 14.68 ? 22   GLN A NE2 1 
ATOM   160   N  N   . LYS A  1 23  ? 51.552  77.347  76.898  1.00 21.24 ? 23   LYS A N   1 
ATOM   161   C  CA  . LYS A  1 23  ? 52.171  76.039  76.906  1.00 24.16 ? 23   LYS A CA  1 
ATOM   162   C  C   . LYS A  1 23  ? 53.488  76.054  77.661  1.00 25.59 ? 23   LYS A C   1 
ATOM   163   O  O   . LYS A  1 23  ? 53.851  75.076  78.325  1.00 25.60 ? 23   LYS A O   1 
ATOM   164   C  CB  . LYS A  1 23  ? 52.339  75.552  75.471  1.00 24.51 ? 23   LYS A CB  1 
ATOM   165   C  CG  . LYS A  1 23  ? 51.019  75.559  74.742  1.00 27.09 ? 23   LYS A CG  1 
ATOM   166   C  CD  . LYS A  1 23  ? 51.032  74.737  73.465  1.00 31.57 ? 23   LYS A CD  1 
ATOM   167   C  CE  . LYS A  1 23  ? 49.601  74.442  73.029  1.00 33.44 ? 23   LYS A CE  1 
ATOM   168   N  NZ  . LYS A  1 23  ? 49.540  73.861  71.657  1.00 35.43 ? 23   LYS A NZ  1 
ATOM   169   N  N   . GLU A  1 24  ? 54.200  77.172  77.572  1.00 27.43 ? 24   GLU A N   1 
ATOM   170   C  CA  . GLU A  1 24  ? 55.497  77.258  78.219  1.00 29.43 ? 24   GLU A CA  1 
ATOM   171   C  C   . GLU A  1 24  ? 55.688  78.535  78.997  1.00 29.66 ? 24   GLU A C   1 
ATOM   172   O  O   . GLU A  1 24  ? 54.987  79.519  78.774  1.00 29.49 ? 24   GLU A O   1 
ATOM   173   C  CB  . GLU A  1 24  ? 56.610  77.137  77.177  1.00 29.82 ? 24   GLU A CB  1 
ATOM   174   C  CG  . GLU A  1 24  ? 56.848  75.710  76.698  1.00 33.60 ? 24   GLU A CG  1 
ATOM   175   C  CD  . GLU A  1 24  ? 57.329  74.786  77.808  1.00 36.63 ? 24   GLU A CD  1 
ATOM   176   O  OE1 . GLU A  1 24  ? 56.596  74.616  78.818  1.00 38.72 ? 24   GLU A OE1 1 
ATOM   177   O  OE2 . GLU A  1 24  ? 58.441  74.219  77.671  1.00 38.16 ? 24   GLU A OE2 1 
ATOM   178   N  N   . SER A  1 25  ? 56.652  78.504  79.911  1.00 29.96 ? 25   SER A N   1 
ATOM   179   C  CA  . SER A  1 25  ? 57.028  79.688  80.664  1.00 30.28 ? 25   SER A CA  1 
ATOM   180   C  C   . SER A  1 25  ? 57.544  80.704  79.649  1.00 29.91 ? 25   SER A C   1 
ATOM   181   O  O   . SER A  1 25  ? 58.322  80.362  78.761  1.00 29.87 ? 25   SER A O   1 
ATOM   182   C  CB  . SER A  1 25  ? 58.115  79.344  81.686  1.00 30.54 ? 25   SER A CB  1 
ATOM   183   O  OG  . SER A  1 25  ? 57.740  79.762  82.992  1.00 31.78 ? 25   SER A OG  1 
ATOM   184   N  N   . ASN A  1 26  ? 57.085  81.946  79.767  1.00 29.52 ? 26   ASN A N   1 
ATOM   185   C  CA  . ASN A  1 26  ? 57.426  82.982  78.796  1.00 28.79 ? 26   ASN A CA  1 
ATOM   186   C  C   . ASN A  1 26  ? 56.923  82.743  77.375  1.00 27.35 ? 26   ASN A C   1 
ATOM   187   O  O   . ASN A  1 26  ? 57.276  83.479  76.478  1.00 27.85 ? 26   ASN A O   1 
ATOM   188   C  CB  . ASN A  1 26  ? 58.929  83.213  78.739  1.00 29.58 ? 26   ASN A CB  1 
ATOM   189   C  CG  . ASN A  1 26  ? 59.336  84.510  79.388  1.00 31.09 ? 26   ASN A CG  1 
ATOM   190   O  OD1 . ASN A  1 26  ? 60.091  85.301  78.808  1.00 34.51 ? 26   ASN A OD1 1 
ATOM   191   N  ND2 . ASN A  1 26  ? 58.843  84.743  80.598  1.00 30.33 ? 26   ASN A ND2 1 
ATOM   192   N  N   . GLY A  1 27  ? 56.122  81.710  77.158  1.00 25.49 ? 27   GLY A N   1 
ATOM   193   C  CA  . GLY A  1 27  ? 55.628  81.457  75.819  1.00 22.39 ? 27   GLY A CA  1 
ATOM   194   C  C   . GLY A  1 27  ? 54.439  82.342  75.491  1.00 20.33 ? 27   GLY A C   1 
ATOM   195   O  O   . GLY A  1 27  ? 53.966  83.112  76.333  1.00 19.97 ? 27   GLY A O   1 
ATOM   196   N  N   . PRO A  1 28  ? 53.960  82.235  74.250  1.00 18.46 ? 28   PRO A N   1 
ATOM   197   C  CA  . PRO A  1 28  ? 52.796  82.996  73.805  1.00 16.52 ? 28   PRO A CA  1 
ATOM   198   C  C   . PRO A  1 28  ? 51.587  82.501  74.575  1.00 14.99 ? 28   PRO A C   1 
ATOM   199   O  O   . PRO A  1 28  ? 51.535  81.343  74.981  1.00 14.53 ? 28   PRO A O   1 
ATOM   200   C  CB  . PRO A  1 28  ? 52.635  82.600  72.337  1.00 16.40 ? 28   PRO A CB  1 
ATOM   201   C  CG  . PRO A  1 28  ? 53.848  81.791  71.979  1.00 18.08 ? 28   PRO A CG  1 
ATOM   202   C  CD  . PRO A  1 28  ? 54.494  81.334  73.213  1.00 18.14 ? 28   PRO A CD  1 
ATOM   203   N  N   . VAL A  1 29  ? 50.619  83.376  74.777  1.00 13.28 ? 29   VAL A N   1 
ATOM   204   C  CA  . VAL A  1 29  ? 49.381  82.992  75.419  1.00 11.91 ? 29   VAL A CA  1 
ATOM   205   C  C   . VAL A  1 29  ? 48.331  83.132  74.327  1.00 11.71 ? 29   VAL A C   1 
ATOM   206   O  O   . VAL A  1 29  ? 48.257  84.171  73.657  1.00 11.51 ? 29   VAL A O   1 
ATOM   207   C  CB  . VAL A  1 29  ? 49.021  83.949  76.597  1.00 11.92 ? 29   VAL A CB  1 
ATOM   208   C  CG1 . VAL A  1 29  ? 47.673  83.587  77.221  1.00 11.56 ? 29   VAL A CG1 1 
ATOM   209   C  CG2 . VAL A  1 29  ? 50.132  83.959  77.677  1.00 12.35 ? 29   VAL A CG2 1 
ATOM   210   N  N   . LYS A  1 30  ? 47.559  82.074  74.112  1.00 11.47 ? 30   LYS A N   1 
ATOM   211   C  CA  . LYS A  1 30  ? 46.446  82.130  73.178  1.00 11.87 ? 30   LYS A CA  1 
ATOM   212   C  C   . LYS A  1 30  ? 45.269  82.578  73.994  1.00 12.00 ? 30   LYS A C   1 
ATOM   213   O  O   . LYS A  1 30  ? 45.042  82.070  75.115  1.00 11.17 ? 30   LYS A O   1 
ATOM   214   C  CB  . LYS A  1 30  ? 46.101  80.732  72.627  1.00 13.85 ? 30   LYS A CB  1 
ATOM   215   C  CG  . LYS A  1 30  ? 47.211  79.958  71.974  1.00 18.39 ? 30   LYS A CG  1 
ATOM   216   C  CD  . LYS A  1 30  ? 46.623  78.698  71.266  1.00 24.67 ? 30   LYS A CD  1 
ATOM   217   C  CE  . LYS A  1 30  ? 47.468  78.243  70.060  1.00 28.62 ? 30   LYS A CE  1 
ATOM   218   N  NZ  . LYS A  1 30  ? 46.705  77.354  69.093  1.00 30.42 ? 30   LYS A NZ  1 
ATOM   219   N  N   . VAL A  1 31  ? 44.533  83.530  73.451  1.00 11.15 ? 31   VAL A N   1 
ATOM   220   C  CA  . VAL A  1 31  ? 43.367  84.076  74.073  1.00 11.79 ? 31   VAL A CA  1 
ATOM   221   C  C   . VAL A  1 31  ? 42.263  83.869  73.055  1.00 11.76 ? 31   VAL A C   1 
ATOM   222   O  O   . VAL A  1 31  ? 42.326  84.402  71.946  1.00 11.62 ? 31   VAL A O   1 
ATOM   223   C  CB  . VAL A  1 31  ? 43.561  85.574  74.329  1.00 11.60 ? 31   VAL A CB  1 
ATOM   224   C  CG1 . VAL A  1 31  ? 42.378  86.165  75.084  1.00 12.45 ? 31   VAL A CG1 1 
ATOM   225   C  CG2 . VAL A  1 31  ? 44.875  85.817  75.100  1.00 11.87 ? 31   VAL A CG2 1 
ATOM   226   N  N   . TRP A  1 32  ? 41.242  83.117  73.429  1.00 10.55 ? 32   TRP A N   1 
ATOM   227   C  CA  . TRP A  1 32  ? 40.161  82.855  72.495  1.00 10.36 ? 32   TRP A CA  1 
ATOM   228   C  C   . TRP A  1 32  ? 38.843  82.609  73.172  1.00 9.81  ? 32   TRP A C   1 
ATOM   229   O  O   . TRP A  1 32  ? 38.766  82.100  74.295  1.00 9.40  ? 32   TRP A O   1 
ATOM   230   C  CB  . TRP A  1 32  ? 40.497  81.657  71.621  1.00 11.44 ? 32   TRP A CB  1 
ATOM   231   C  CG  . TRP A  1 32  ? 40.225  80.315  72.251  1.00 10.63 ? 32   TRP A CG  1 
ATOM   232   C  CD1 . TRP A  1 32  ? 39.156  79.501  72.012  1.00 14.04 ? 32   TRP A CD1 1 
ATOM   233   C  CD2 . TRP A  1 32  ? 41.058  79.612  73.170  1.00 13.98 ? 32   TRP A CD2 1 
ATOM   234   N  NE1 . TRP A  1 32  ? 39.258  78.341  72.748  1.00 14.07 ? 32   TRP A NE1 1 
ATOM   235   C  CE2 . TRP A  1 32  ? 40.425  78.381  73.462  1.00 14.86 ? 32   TRP A CE2 1 
ATOM   236   C  CE3 . TRP A  1 32  ? 42.269  79.901  73.800  1.00 17.06 ? 32   TRP A CE3 1 
ATOM   237   C  CZ2 . TRP A  1 32  ? 40.950  77.458  74.371  1.00 18.11 ? 32   TRP A CZ2 1 
ATOM   238   C  CZ3 . TRP A  1 32  ? 42.804  78.970  74.682  1.00 17.53 ? 32   TRP A CZ3 1 
ATOM   239   C  CH2 . TRP A  1 32  ? 42.142  77.760  74.956  1.00 17.37 ? 32   TRP A CH2 1 
ATOM   240   N  N   . GLY A  1 33  ? 37.781  82.949  72.469  1.00 10.14 ? 33   GLY A N   1 
ATOM   241   C  CA  . GLY A  1 33  ? 36.457  82.735  73.005  1.00 10.08 ? 33   GLY A CA  1 
ATOM   242   C  C   . GLY A  1 33  ? 35.451  83.534  72.226  1.00 10.87 ? 33   GLY A C   1 
ATOM   243   O  O   . GLY A  1 33  ? 35.662  83.847  71.047  1.00 9.73  ? 33   GLY A O   1 
ATOM   244   N  N   . SER A  1 34  ? 34.367  83.904  72.890  1.00 11.07 ? 34   SER A N   1 
ATOM   245   C  CA  . SER A  1 34  ? 33.268  84.547  72.201  1.00 12.39 ? 34   SER A CA  1 
ATOM   246   C  C   . SER A  1 34  ? 32.575  85.555  73.096  1.00 12.45 ? 34   SER A C   1 
ATOM   247   O  O   . SER A  1 34  ? 32.371  85.302  74.279  1.00 10.56 ? 34   SER A O   1 
ATOM   248   C  CB  . SER A  1 34  ? 32.265  83.463  71.795  1.00 14.04 ? 34   SER A CB  1 
ATOM   249   O  OG  . SER A  1 34  ? 31.096  84.045  71.253  1.00 18.64 ? 34   SER A OG  1 
ATOM   250   N  N   . ILE A  1 35  ? 32.210  86.693  72.526  1.00 11.84 ? 35   ILE A N   1 
ATOM   251   C  CA  . ILE A  1 35  ? 31.517  87.727  73.285  1.00 12.56 ? 35   ILE A CA  1 
ATOM   252   C  C   . ILE A  1 35  ? 30.295  88.114  72.479  1.00 12.68 ? 35   ILE A C   1 
ATOM   253   O  O   . ILE A  1 35  ? 30.404  88.329  71.256  1.00 13.52 ? 35   ILE A O   1 
ATOM   254   C  CB  . ILE A  1 35  ? 32.388  88.978  73.506  1.00 12.19 ? 35   ILE A CB  1 
ATOM   255   C  CG1 . ILE A  1 35  ? 33.720  88.660  74.165  1.00 12.56 ? 35   ILE A CG1 1 
ATOM   256   C  CG2 . ILE A  1 35  ? 31.665  90.006  74.405  1.00 10.65 ? 35   ILE A CG2 1 
ATOM   257   C  CD1 . ILE A  1 35  ? 34.627  89.909  74.154  1.00 12.32 ? 35   ILE A CD1 1 
ATOM   258   N  N   . LYS A  1 36  ? 29.126  88.177  73.128  1.00 12.61 ? 36   LYS A N   1 
ATOM   259   C  CA  . LYS A  1 36  ? 27.911  88.561  72.399  1.00 12.28 ? 36   LYS A CA  1 
ATOM   260   C  C   . LYS A  1 36  ? 27.311  89.849  72.972  1.00 11.72 ? 36   LYS A C   1 
ATOM   261   O  O   . LYS A  1 36  ? 27.758  90.312  74.009  1.00 11.63 ? 36   LYS A O   1 
ATOM   262   C  CB  . LYS A  1 36  ? 26.874  87.431  72.396  1.00 13.33 ? 36   LYS A CB  1 
ATOM   263   C  CG  . LYS A  1 36  ? 26.333  87.085  73.776  1.00 15.11 ? 36   LYS A CG  1 
ATOM   264   C  CD  . LYS A  1 36  ? 25.343  85.903  73.718  1.00 20.34 ? 36   LYS A CD  1 
ATOM   265   C  CE  . LYS A  1 36  ? 25.183  85.257  75.100  1.00 21.76 ? 36   LYS A CE  1 
ATOM   266   N  NZ  . LYS A  1 36  ? 24.108  84.195  75.166  1.00 21.24 ? 36   LYS A NZ  1 
ATOM   267   N  N   . GLY A  1 37  ? 26.355  90.450  72.262  1.00 11.13 ? 37   GLY A N   1 
ATOM   268   C  CA  . GLY A  1 37  ? 25.673  91.657  72.714  1.00 11.02 ? 37   GLY A CA  1 
ATOM   269   C  C   . GLY A  1 37  ? 26.356  92.975  72.375  1.00 11.02 ? 37   GLY A C   1 
ATOM   270   O  O   . GLY A  1 37  ? 25.944  94.046  72.823  1.00 9.49  ? 37   GLY A O   1 
ATOM   271   N  N   . LEU A  1 38  ? 27.378  92.894  71.530  1.00 10.93 ? 38   LEU A N   1 
ATOM   272   C  CA  . LEU A  1 38  ? 28.167  94.056  71.142  1.00 11.63 ? 38   LEU A CA  1 
ATOM   273   C  C   . LEU A  1 38  ? 27.622  94.742  69.912  1.00 12.21 ? 38   LEU A C   1 
ATOM   274   O  O   . LEU A  1 38  ? 26.888  94.122  69.123  1.00 12.44 ? 38   LEU A O   1 
ATOM   275   C  CB  . LEU A  1 38  ? 29.608  93.620  70.867  1.00 10.86 ? 38   LEU A CB  1 
ATOM   276   C  CG  . LEU A  1 38  ? 30.439  93.109  72.056  1.00 12.09 ? 38   LEU A CG  1 
ATOM   277   C  CD1 . LEU A  1 38  ? 31.663  92.355  71.549  1.00 12.07 ? 38   LEU A CD1 1 
ATOM   278   C  CD2 . LEU A  1 38  ? 30.853  94.258  72.965  1.00 9.32  ? 38   LEU A CD2 1 
ATOM   279   N  N   . THR A  1 39  ? 27.933  96.032  69.765  1.00 12.65 ? 39   THR A N   1 
ATOM   280   C  CA  . THR A  1 39  ? 27.590  96.716  68.512  1.00 13.92 ? 39   THR A CA  1 
ATOM   281   C  C   . THR A  1 39  ? 28.557  96.213  67.464  1.00 13.96 ? 39   THR A C   1 
ATOM   282   O  O   . THR A  1 39  ? 29.694  95.832  67.777  1.00 13.41 ? 39   THR A O   1 
ATOM   283   C  CB  . THR A  1 39  ? 27.671  98.257  68.591  1.00 13.72 ? 39   THR A CB  1 
ATOM   284   O  OG1 . THR A  1 39  ? 28.932  98.677  69.147  1.00 15.19 ? 39   THR A OG1 1 
ATOM   285   C  CG2 . THR A  1 39  ? 26.616  98.825  69.554  1.00 14.66 ? 39   THR A CG2 1 
ATOM   286   N  N   . GLU A  1 40  ? 28.127  96.230  66.207  1.00 13.29 ? 40   GLU A N   1 
ATOM   287   C  CA  . GLU A  1 40  ? 28.980  95.741  65.135  1.00 13.29 ? 40   GLU A CA  1 
ATOM   288   C  C   . GLU A  1 40  ? 30.217  96.602  65.034  1.00 12.49 ? 40   GLU A C   1 
ATOM   289   O  O   . GLU A  1 40  ? 30.114  97.824  65.077  1.00 12.93 ? 40   GLU A O   1 
ATOM   290   C  CB  . GLU A  1 40  ? 28.223  95.728  63.792  1.00 14.21 ? 40   GLU A CB  1 
ATOM   291   C  CG  . GLU A  1 40  ? 29.032  95.095  62.661  1.00 17.17 ? 40   GLU A CG  1 
ATOM   292   C  CD  . GLU A  1 40  ? 28.306  95.154  61.319  1.00 22.36 ? 40   GLU A CD  1 
ATOM   293   O  OE1 . GLU A  1 40  ? 27.087  95.441  61.313  1.00 24.47 ? 40   GLU A OE1 1 
ATOM   294   O  OE2 . GLU A  1 40  ? 28.957  94.908  60.270  1.00 22.41 ? 40   GLU A OE2 1 
ATOM   295   N  N   . GLY A  1 41  ? 31.392  95.989  64.915  1.00 11.59 ? 41   GLY A N   1 
ATOM   296   C  CA  . GLY A  1 41  ? 32.603  96.803  64.783  1.00 11.98 ? 41   GLY A CA  1 
ATOM   297   C  C   . GLY A  1 41  ? 33.672  96.504  65.830  1.00 11.12 ? 41   GLY A C   1 
ATOM   298   O  O   . GLY A  1 41  ? 33.599  95.518  66.523  1.00 10.37 ? 41   GLY A O   1 
ATOM   299   N  N   . LEU A  1 42  ? 34.674  97.368  65.928  1.00 11.50 ? 42   LEU A N   1 
ATOM   300   C  CA  . LEU A  1 42  ? 35.824  97.119  66.803  1.00 10.89 ? 42   LEU A CA  1 
ATOM   301   C  C   . LEU A  1 42  ? 35.559  97.534  68.217  1.00 10.53 ? 42   LEU A C   1 
ATOM   302   O  O   . LEU A  1 42  ? 34.934  98.557  68.447  1.00 9.74  ? 42   LEU A O   1 
ATOM   303   C  CB  . LEU A  1 42  ? 36.979  97.980  66.327  1.00 12.24 ? 42   LEU A CB  1 
ATOM   304   C  CG  . LEU A  1 42  ? 38.169  97.504  65.497  1.00 16.01 ? 42   LEU A CG  1 
ATOM   305   C  CD1 . LEU A  1 42  ? 38.055  96.110  64.965  1.00 15.04 ? 42   LEU A CD1 1 
ATOM   306   C  CD2 . LEU A  1 42  ? 38.600  98.584  64.470  1.00 18.54 ? 42   LEU A CD2 1 
ATOM   307   N  N   . HIS A  1 43  ? 36.106  96.771  69.166  1.00 8.55  ? 43   HIS A N   1 
ATOM   308   C  CA  . HIS A  1 43  ? 35.920  97.056  70.578  1.00 7.58  ? 43   HIS A CA  1 
ATOM   309   C  C   . HIS A  1 43  ? 37.231  96.824  71.317  1.00 6.05  ? 43   HIS A C   1 
ATOM   310   O  O   . HIS A  1 43  ? 37.852  95.774  71.177  1.00 6.67  ? 43   HIS A O   1 
ATOM   311   C  CB  . HIS A  1 43  ? 34.825  96.165  71.196  1.00 7.91  ? 43   HIS A CB  1 
ATOM   312   C  CG  . HIS A  1 43  ? 33.447  96.507  70.732  1.00 9.53  ? 43   HIS A CG  1 
ATOM   313   N  ND1 . HIS A  1 43  ? 32.679  97.482  71.333  1.00 9.67  ? 43   HIS A ND1 1 
ATOM   314   C  CD2 . HIS A  1 43  ? 32.723  96.042  69.691  1.00 11.11 ? 43   HIS A CD2 1 
ATOM   315   C  CE1 . HIS A  1 43  ? 31.530  97.590  70.688  1.00 12.32 ? 43   HIS A CE1 1 
ATOM   316   N  NE2 . HIS A  1 43  ? 31.540  96.740  69.676  1.00 12.49 ? 43   HIS A NE2 1 
ATOM   317   N  N   . GLY A  1 44  ? 37.636  97.804  72.121  1.00 6.42  ? 44   GLY A N   1 
ATOM   318   C  CA  . GLY A  1 44  ? 38.876  97.700  72.872  1.00 7.35  ? 44   GLY A CA  1 
ATOM   319   C  C   . GLY A  1 44  ? 38.806  96.509  73.835  1.00 8.54  ? 44   GLY A C   1 
ATOM   320   O  O   . GLY A  1 44  ? 37.739  96.177  74.381  1.00 9.80  ? 44   GLY A O   1 
ATOM   321   N  N   . PHE A  1 45  ? 39.950  95.901  74.086  1.00 7.82  ? 45   PHE A N   1 
ATOM   322   C  CA  . PHE A  1 45  ? 39.972  94.630  74.788  1.00 7.44  ? 45   PHE A CA  1 
ATOM   323   C  C   . PHE A  1 45  ? 41.277  94.656  75.536  1.00 7.43  ? 45   PHE A C   1 
ATOM   324   O  O   . PHE A  1 45  ? 42.363  94.565  74.925  1.00 7.73  ? 45   PHE A O   1 
ATOM   325   C  CB  . PHE A  1 45  ? 39.974  93.544  73.711  1.00 8.69  ? 45   PHE A CB  1 
ATOM   326   C  CG  . PHE A  1 45  ? 39.847  92.123  74.209  1.00 8.39  ? 45   PHE A CG  1 
ATOM   327   C  CD1 . PHE A  1 45  ? 38.681  91.694  74.833  1.00 10.16 ? 45   PHE A CD1 1 
ATOM   328   C  CD2 . PHE A  1 45  ? 40.852  91.201  73.940  1.00 7.54  ? 45   PHE A CD2 1 
ATOM   329   C  CE1 . PHE A  1 45  ? 38.542  90.359  75.248  1.00 10.39 ? 45   PHE A CE1 1 
ATOM   330   C  CE2 . PHE A  1 45  ? 40.717  89.843  74.344  1.00 10.05 ? 45   PHE A CE2 1 
ATOM   331   C  CZ  . PHE A  1 45  ? 39.562  89.438  74.973  1.00 10.02 ? 45   PHE A CZ  1 
ATOM   332   N  N   . HIS A  1 46  ? 41.175  94.759  76.868  1.00 5.79  ? 46   HIS A N   1 
ATOM   333   C  CA  . HIS A  1 46  ? 42.353  94.930  77.703  1.00 6.36  ? 46   HIS A CA  1 
ATOM   334   C  C   . HIS A  1 46  ? 42.312  94.179  79.024  1.00 5.94  ? 46   HIS A C   1 
ATOM   335   O  O   . HIS A  1 46  ? 41.231  93.921  79.574  1.00 8.22  ? 46   HIS A O   1 
ATOM   336   C  CB  . HIS A  1 46  ? 42.510  96.398  78.124  1.00 6.06  ? 46   HIS A CB  1 
ATOM   337   C  CG  . HIS A  1 46  ? 42.294  97.381  77.025  1.00 6.17  ? 46   HIS A CG  1 
ATOM   338   N  ND1 . HIS A  1 46  ? 41.373  98.386  77.097  1.00 6.19  ? 46   HIS A ND1 1 
ATOM   339   C  CD2 . HIS A  1 46  ? 42.880  97.498  75.808  1.00 6.99  ? 46   HIS A CD2 1 
ATOM   340   C  CE1 . HIS A  1 46  ? 41.394  99.100  75.996  1.00 10.04 ? 46   HIS A CE1 1 
ATOM   341   N  NE2 . HIS A  1 46  ? 42.304  98.584  75.194  1.00 6.27  ? 46   HIS A NE2 1 
ATOM   342   N  N   . VAL A  1 47  ? 43.506  93.930  79.556  1.00 6.54  ? 47   VAL A N   1 
ATOM   343   C  CA  . VAL A  1 47  ? 43.644  93.382  80.916  1.00 7.20  ? 47   VAL A CA  1 
ATOM   344   C  C   . VAL A  1 47  ? 43.879  94.613  81.790  1.00 6.80  ? 47   VAL A C   1 
ATOM   345   O  O   . VAL A  1 47  ? 44.840  95.369  81.601  1.00 6.11  ? 47   VAL A O   1 
ATOM   346   C  CB  . VAL A  1 47  ? 44.834  92.409  81.044  1.00 7.17  ? 47   VAL A CB  1 
ATOM   347   C  CG1 . VAL A  1 47  ? 45.012  91.952  82.512  1.00 9.61  ? 47   VAL A CG1 1 
ATOM   348   C  CG2 . VAL A  1 47  ? 44.575  91.157  80.215  1.00 8.28  ? 47   VAL A CG2 1 
ATOM   349   N  N   . HIS A  1 48  ? 42.981  94.837  82.737  1.00 7.62  ? 48   HIS A N   1 
ATOM   350   C  CA  . HIS A  1 48  ? 43.121  95.912  83.689  1.00 6.63  ? 48   HIS A CA  1 
ATOM   351   C  C   . HIS A  1 48  ? 43.752  95.360  84.935  1.00 7.29  ? 48   HIS A C   1 
ATOM   352   O  O   . HIS A  1 48  ? 43.704  94.144  85.153  1.00 7.64  ? 48   HIS A O   1 
ATOM   353   C  CB  . HIS A  1 48  ? 41.765  96.517  83.986  1.00 7.31  ? 48   HIS A CB  1 
ATOM   354   C  CG  . HIS A  1 48  ? 41.252  97.347  82.846  1.00 6.78  ? 48   HIS A CG  1 
ATOM   355   N  ND1 . HIS A  1 48  ? 40.906  98.676  82.978  1.00 6.55  ? 48   HIS A ND1 1 
ATOM   356   C  CD2 . HIS A  1 48  ? 41.077  97.037  81.542  1.00 7.12  ? 48   HIS A CD2 1 
ATOM   357   C  CE1 . HIS A  1 48  ? 40.535  99.152  81.796  1.00 6.69  ? 48   HIS A CE1 1 
ATOM   358   N  NE2 . HIS A  1 48  ? 40.610  98.170  80.922  1.00 7.27  ? 48   HIS A NE2 1 
ATOM   359   N  N   . GLU A  1 49  ? 44.334  96.265  85.719  1.00 6.26  ? 49   GLU A N   1 
ATOM   360   C  CA  . GLU A  1 49  ? 45.188  95.925  86.837  1.00 7.51  ? 49   GLU A CA  1 
ATOM   361   C  C   . GLU A  1 49  ? 44.553  95.074  87.929  1.00 6.87  ? 49   GLU A C   1 
ATOM   362   O  O   . GLU A  1 49  ? 45.127  94.087  88.364  1.00 7.25  ? 49   GLU A O   1 
ATOM   363   C  CB  . GLU A  1 49  ? 45.757  97.199  87.490  1.00 8.41  ? 49   GLU A CB  1 
ATOM   364   C  CG  . GLU A  1 49  ? 46.920  96.897  88.436  1.00 8.56  ? 49   GLU A CG  1 
ATOM   365   C  CD  . GLU A  1 49  ? 47.642  98.141  88.926  1.00 11.58 ? 49   GLU A CD  1 
ATOM   366   O  OE1 . GLU A  1 49  ? 47.283  99.250  88.486  1.00 9.27  ? 49   GLU A OE1 1 
ATOM   367   O  OE2 . GLU A  1 49  ? 48.529  97.990  89.797  1.00 11.66 ? 49   GLU A OE2 1 
ATOM   368   N  N   . PHE A  1 50  ? 43.400  95.463  88.404  1.00 6.51  ? 50   PHE A N   1 
ATOM   369   C  CA  . PHE A  1 50  ? 42.893  94.737  89.560  1.00 7.86  ? 50   PHE A CA  1 
ATOM   370   C  C   . PHE A  1 50  ? 41.741  93.797  89.259  1.00 7.92  ? 50   PHE A C   1 
ATOM   371   O  O   . PHE A  1 50  ? 40.855  94.132  88.466  1.00 7.71  ? 50   PHE A O   1 
ATOM   372   C  CB  . PHE A  1 50  ? 42.467  95.723  90.645  1.00 7.81  ? 50   PHE A CB  1 
ATOM   373   C  CG  . PHE A  1 50  ? 43.518  96.741  90.968  1.00 10.87 ? 50   PHE A CG  1 
ATOM   374   C  CD1 . PHE A  1 50  ? 44.695  96.360  91.592  1.00 14.06 ? 50   PHE A CD1 1 
ATOM   375   C  CD2 . PHE A  1 50  ? 43.339  98.071  90.624  1.00 11.25 ? 50   PHE A CD2 1 
ATOM   376   C  CE1 . PHE A  1 50  ? 45.689  97.304  91.861  1.00 13.16 ? 50   PHE A CE1 1 
ATOM   377   C  CE2 . PHE A  1 50  ? 44.322  99.007  90.919  1.00 13.36 ? 50   PHE A CE2 1 
ATOM   378   C  CZ  . PHE A  1 50  ? 45.490  98.617  91.525  1.00 11.48 ? 50   PHE A CZ  1 
ATOM   379   N  N   . GLY A  1 51  ? 41.713  92.675  90.003  1.00 7.33  ? 51   GLY A N   1 
ATOM   380   C  CA  . GLY A  1 51  ? 40.661  91.686  89.861  1.00 7.02  ? 51   GLY A CA  1 
ATOM   381   C  C   . GLY A  1 51  ? 39.572  92.037  90.847  1.00 6.96  ? 51   GLY A C   1 
ATOM   382   O  O   . GLY A  1 51  ? 39.168  91.199  91.625  1.00 7.43  ? 51   GLY A O   1 
ATOM   383   N  N   . ASP A  1 52  ? 39.190  93.311  90.874  1.00 7.21  ? 52   ASP A N   1 
ATOM   384   C  CA  . ASP A  1 52  ? 38.285  93.881  91.839  1.00 8.52  ? 52   ASP A CA  1 
ATOM   385   C  C   . ASP A  1 52  ? 37.028  94.329  91.139  1.00 10.39 ? 52   ASP A C   1 
ATOM   386   O  O   . ASP A  1 52  ? 37.068  95.257  90.302  1.00 9.18  ? 52   ASP A O   1 
ATOM   387   C  CB  . ASP A  1 52  ? 38.961  95.087  92.490  1.00 8.45  ? 52   ASP A CB  1 
ATOM   388   C  CG  . ASP A  1 52  ? 38.149  95.690  93.621  1.00 8.38  ? 52   ASP A CG  1 
ATOM   389   O  OD1 . ASP A  1 52  ? 36.895  95.570  93.654  1.00 10.87 ? 52   ASP A OD1 1 
ATOM   390   O  OD2 . ASP A  1 52  ? 38.725  96.354  94.503  1.00 10.53 ? 52   ASP A OD2 1 
ATOM   391   N  N   . ASN A  1 53  ? 35.923  93.664  91.470  1.00 11.25 ? 53   ASN A N   1 
ATOM   392   C  CA  . ASN A  1 53  ? 34.641  93.972  90.855  1.00 12.88 ? 53   ASN A CA  1 
ATOM   393   C  C   . ASN A  1 53  ? 33.651  94.503  91.888  1.00 12.89 ? 53   ASN A C   1 
ATOM   394   O  O   . ASN A  1 53  ? 32.454  94.477  91.668  1.00 12.37 ? 53   ASN A O   1 
ATOM   395   C  CB  . ASN A  1 53  ? 34.078  92.718  90.185  1.00 13.78 ? 53   ASN A CB  1 
ATOM   396   C  CG  . ASN A  1 53  ? 32.952  93.021  89.213  1.00 17.72 ? 53   ASN A CG  1 
ATOM   397   O  OD1 . ASN A  1 53  ? 33.057  93.928  88.380  1.00 19.73 ? 53   ASN A OD1 1 
ATOM   398   N  ND2 . ASN A  1 53  ? 31.878  92.249  89.299  1.00 18.10 ? 53   ASN A ND2 1 
ATOM   399   N  N   . THR A  1 54  ? 34.150  95.002  93.007  1.00 13.20 ? 54   THR A N   1 
ATOM   400   C  CA  . THR A  1 54  ? 33.257  95.435  94.086  1.00 14.54 ? 54   THR A CA  1 
ATOM   401   C  C   . THR A  1 54  ? 32.304  96.533  93.668  1.00 15.71 ? 54   THR A C   1 
ATOM   402   O  O   . THR A  1 54  ? 31.163  96.600  94.153  1.00 16.07 ? 54   THR A O   1 
ATOM   403   C  CB  . THR A  1 54  ? 34.029  95.864  95.324  1.00 15.06 ? 54   THR A CB  1 
ATOM   404   O  OG1 . THR A  1 54  ? 35.050  96.791  94.975  1.00 15.57 ? 54   THR A OG1 1 
ATOM   405   C  CG2 . THR A  1 54  ? 34.799  94.663  95.888  1.00 15.98 ? 54   THR A CG2 1 
ATOM   406   N  N   . ALA A  1 55  ? 32.767  97.377  92.762  1.00 14.88 ? 55   ALA A N   1 
ATOM   407   C  CA  . ALA A  1 55  ? 31.928  98.415  92.224  1.00 15.98 ? 55   ALA A CA  1 
ATOM   408   C  C   . ALA A  1 55  ? 31.754  98.210  90.734  1.00 15.14 ? 55   ALA A C   1 
ATOM   409   O  O   . ALA A  1 55  ? 31.712  99.148  89.969  1.00 16.95 ? 55   ALA A O   1 
ATOM   410   C  CB  . ALA A  1 55  ? 32.512  99.786  92.532  1.00 15.96 ? 55   ALA A CB  1 
ATOM   411   N  N   . GLY A  1 56  ? 31.676  96.967  90.301  1.00 14.93 ? 56   GLY A N   1 
ATOM   412   C  CA  . GLY A  1 56  ? 31.504  96.729  88.888  1.00 13.74 ? 56   GLY A CA  1 
ATOM   413   C  C   . GLY A  1 56  ? 32.839  96.889  88.143  1.00 13.11 ? 56   GLY A C   1 
ATOM   414   O  O   . GLY A  1 56  ? 33.908  96.930  88.753  1.00 12.27 ? 56   GLY A O   1 
ATOM   415   N  N   . CYS A  1 57  ? 32.769  97.060  86.830  1.00 13.24 ? 57   CYS A N   1 
ATOM   416   C  CA  . CYS A  1 57  ? 33.989  97.133  86.017  1.00 13.08 ? 57   CYS A CA  1 
ATOM   417   C  C   . CYS A  1 57  ? 34.901  98.329  86.398  1.00 12.73 ? 57   CYS A C   1 
ATOM   418   O  O   . CYS A  1 57  ? 36.127  98.282  86.206  1.00 11.62 ? 57   CYS A O   1 
ATOM   419   C  CB  . CYS A  1 57  ? 33.625  97.106  84.510  1.00 12.56 ? 57   CYS A CB  1 
ATOM   420   S  SG  . CYS A  1 57  ? 32.853  95.528  84.053  1.00 18.44 ? 57   CYS A SG  1 
ATOM   421   N  N   . THR A  1 58  ? 34.317  99.375  86.973  1.00 12.48 ? 58   THR A N   1 
ATOM   422   C  CA  . THR A  1 58  ? 35.092  100.541 87.384  1.00 13.64 ? 58   THR A CA  1 
ATOM   423   C  C   . THR A  1 58  ? 36.232  100.268 88.369  1.00 12.83 ? 58   THR A C   1 
ATOM   424   O  O   . THR A  1 58  ? 37.282  100.896 88.278  1.00 13.67 ? 58   THR A O   1 
ATOM   425   C  CB  . THR A  1 58  ? 34.165  101.642 87.948  1.00 14.11 ? 58   THR A CB  1 
ATOM   426   O  OG1 . THR A  1 58  ? 33.424  102.206 86.856  1.00 18.93 ? 58   THR A OG1 1 
ATOM   427   C  CG2 . THR A  1 58  ? 35.000  102.845 88.409  1.00 15.76 ? 58   THR A CG2 1 
ATOM   428   N  N   . SER A  1 59  ? 36.025  99.367  89.336  1.00 11.80 ? 59   SER A N   1 
ATOM   429   C  CA  . SER A  1 59  ? 37.076  99.079  90.302  1.00 10.86 ? 59   SER A CA  1 
ATOM   430   C  C   . SER A  1 59  ? 38.225  98.202  89.796  1.00 9.81  ? 59   SER A C   1 
ATOM   431   O  O   . SER A  1 59  ? 39.139  97.905  90.550  1.00 9.36  ? 59   SER A O   1 
ATOM   432   C  CB  . SER A  1 59  ? 36.524  98.465  91.618  1.00 12.11 ? 59   SER A CB  1 
ATOM   433   O  OG  . SER A  1 59  ? 35.245  97.958  91.467  1.00 13.05 ? 59   SER A OG  1 
ATOM   434   N  N   . ALA A  1 60  ? 38.194  97.786  88.541  1.00 8.33  ? 60   ALA A N   1 
ATOM   435   C  CA  . ALA A  1 60  ? 39.333  97.041  87.991  1.00 8.81  ? 60   ALA A CA  1 
ATOM   436   C  C   . ALA A  1 60  ? 40.553  97.945  87.788  1.00 8.72  ? 60   ALA A C   1 
ATOM   437   O  O   . ALA A  1 60  ? 41.631  97.463  87.428  1.00 8.67  ? 60   ALA A O   1 
ATOM   438   C  CB  . ALA A  1 60  ? 38.961  96.406  86.659  1.00 8.41  ? 60   ALA A CB  1 
ATOM   439   N  N   . GLY A  1 61  ? 40.359  99.256  87.951  1.00 8.05  ? 61   GLY A N   1 
ATOM   440   C  CA  . GLY A  1 61  ? 41.474  100.180 87.812  1.00 8.06  ? 61   GLY A CA  1 
ATOM   441   C  C   . GLY A  1 61  ? 41.914  100.388 86.380  1.00 7.63  ? 61   GLY A C   1 
ATOM   442   O  O   . GLY A  1 61  ? 41.159  100.078 85.457  1.00 7.75  ? 61   GLY A O   1 
ATOM   443   N  N   . PRO A  1 62  ? 43.135  100.880 86.169  1.00 7.95  ? 62   PRO A N   1 
ATOM   444   C  CA  . PRO A  1 62  ? 43.585  101.142 84.800  1.00 8.73  ? 62   PRO A CA  1 
ATOM   445   C  C   . PRO A  1 62  ? 44.185  99.925  84.113  1.00 8.77  ? 62   PRO A C   1 
ATOM   446   O  O   . PRO A  1 62  ? 44.154  98.816  84.605  1.00 8.78  ? 62   PRO A O   1 
ATOM   447   C  CB  . PRO A  1 62  ? 44.655  102.233 84.993  1.00 9.24  ? 62   PRO A CB  1 
ATOM   448   C  CG  . PRO A  1 62  ? 45.370  101.818 86.302  1.00 9.97  ? 62   PRO A CG  1 
ATOM   449   C  CD  . PRO A  1 62  ? 44.183  101.219 87.172  1.00 8.05  ? 62   PRO A CD  1 
ATOM   450   N  N   . HIS A  1 63  ? 44.729  100.124 82.932  1.00 7.97  ? 63   HIS A N   1 
ATOM   451   C  CA  . HIS A  1 63  ? 45.336  98.995  82.241  1.00 9.03  ? 63   HIS A CA  1 
ATOM   452   C  C   . HIS A  1 63  ? 46.510  98.479  83.032  1.00 9.13  ? 63   HIS A C   1 
ATOM   453   O  O   . HIS A  1 63  ? 47.246  99.284  83.658  1.00 7.78  ? 63   HIS A O   1 
ATOM   454   C  CB  . HIS A  1 63  ? 45.812  99.457  80.853  1.00 9.71  ? 63   HIS A CB  1 
ATOM   455   C  CG  . HIS A  1 63  ? 44.685  99.786  79.936  1.00 11.54 ? 63   HIS A CG  1 
ATOM   456   N  ND1 . HIS A  1 63  ? 44.877  100.289 78.674  1.00 9.20  ? 63   HIS A ND1 1 
ATOM   457   C  CD2 . HIS A  1 63  ? 43.347  99.687  80.108  1.00 11.88 ? 63   HIS A CD2 1 
ATOM   458   C  CE1 . HIS A  1 63  ? 43.702  100.496 78.104  1.00 13.55 ? 63   HIS A CE1 1 
ATOM   459   N  NE2 . HIS A  1 63  ? 42.759  100.130 78.952  1.00 17.63 ? 63   HIS A NE2 1 
ATOM   460   N  N   . PHE A  1 64  ? 46.667  97.152  83.028  1.00 8.53  ? 64   PHE A N   1 
ATOM   461   C  CA  . PHE A  1 64  ? 47.800  96.469  83.677  1.00 8.68  ? 64   PHE A CA  1 
ATOM   462   C  C   . PHE A  1 64  ? 49.092  97.016  83.022  1.00 9.07  ? 64   PHE A C   1 
ATOM   463   O  O   . PHE A  1 64  ? 49.250  96.957  81.828  1.00 8.80  ? 64   PHE A O   1 
ATOM   464   C  CB  . PHE A  1 64  ? 47.656  94.939  83.554  1.00 9.65  ? 64   PHE A CB  1 
ATOM   465   C  CG  . PHE A  1 64  ? 48.766  94.148  84.234  1.00 8.29  ? 64   PHE A CG  1 
ATOM   466   C  CD1 . PHE A  1 64  ? 49.260  94.544  85.458  1.00 8.86  ? 64   PHE A CD1 1 
ATOM   467   C  CD2 . PHE A  1 64  ? 49.317  93.034  83.616  1.00 8.02  ? 64   PHE A CD2 1 
ATOM   468   C  CE1 . PHE A  1 64  ? 50.282  93.826  86.073  1.00 9.21  ? 64   PHE A CE1 1 
ATOM   469   C  CE2 . PHE A  1 64  ? 50.349  92.324  84.209  1.00 7.54  ? 64   PHE A CE2 1 
ATOM   470   C  CZ  . PHE A  1 64  ? 50.804  92.704  85.453  1.00 10.11 ? 64   PHE A CZ  1 
ATOM   471   N  N   . ASN A  1 65  ? 50.003  97.571  83.828  1.00 8.70  ? 65   ASN A N   1 
ATOM   472   C  CA  . ASN A  1 65  ? 51.147  98.338  83.282  1.00 9.58  ? 65   ASN A CA  1 
ATOM   473   C  C   . ASN A  1 65  ? 52.285  98.289  84.283  1.00 10.33 ? 65   ASN A C   1 
ATOM   474   O  O   . ASN A  1 65  ? 52.644  99.351  84.840  1.00 12.09 ? 65   ASN A O   1 
ATOM   475   C  CB  . ASN A  1 65  ? 50.683  99.802  83.175  1.00 8.63  ? 65   ASN A CB  1 
ATOM   476   C  CG  . ASN A  1 65  ? 51.679  100.727 82.453  1.00 11.81 ? 65   ASN A CG  1 
ATOM   477   O  OD1 . ASN A  1 65  ? 52.573  100.277 81.732  1.00 12.13 ? 65   ASN A OD1 1 
ATOM   478   N  ND2 . ASN A  1 65  ? 51.464  102.043 82.601  1.00 9.70  ? 65   ASN A ND2 1 
ATOM   479   N  N   . PRO A  1 66  ? 52.857  97.107  84.528  1.00 10.46 ? 66   PRO A N   1 
ATOM   480   C  CA  . PRO A  1 66  ? 53.932  96.975  85.531  1.00 11.68 ? 66   PRO A CA  1 
ATOM   481   C  C   . PRO A  1 66  ? 55.196  97.660  85.052  1.00 13.45 ? 66   PRO A C   1 
ATOM   482   O  O   . PRO A  1 66  ? 56.045  97.970  85.886  1.00 14.29 ? 66   PRO A O   1 
ATOM   483   C  CB  . PRO A  1 66  ? 54.155  95.461  85.627  1.00 11.60 ? 66   PRO A CB  1 
ATOM   484   C  CG  . PRO A  1 66  ? 53.733  94.943  84.246  1.00 11.63 ? 66   PRO A CG  1 
ATOM   485   C  CD  . PRO A  1 66  ? 52.507  95.816  83.908  1.00 11.23 ? 66   PRO A CD  1 
ATOM   486   N  N   . LEU A  1 67  ? 55.300  97.936  83.746  1.00 14.23 ? 67   LEU A N   1 
ATOM   487   C  CA  . LEU A  1 67  ? 56.502  98.599  83.226  1.00 14.55 ? 67   LEU A CA  1 
ATOM   488   C  C   . LEU A  1 67  ? 56.359  100.113 83.108  1.00 14.72 ? 67   LEU A C   1 
ATOM   489   O  O   . LEU A  1 67  ? 57.286  100.812 82.677  1.00 14.15 ? 67   LEU A O   1 
ATOM   490   C  CB  . LEU A  1 67  ? 56.932  98.001  81.897  1.00 14.42 ? 67   LEU A CB  1 
ATOM   491   C  CG  . LEU A  1 67  ? 57.346  96.535  81.943  1.00 15.37 ? 67   LEU A CG  1 
ATOM   492   C  CD1 . LEU A  1 67  ? 57.747  96.068  80.584  1.00 16.81 ? 67   LEU A CD1 1 
ATOM   493   C  CD2 . LEU A  1 67  ? 58.481  96.282  82.963  1.00 18.00 ? 67   LEU A CD2 1 
ATOM   494   N  N   . SER A  1 68  ? 55.197  100.628 83.496  1.00 14.75 ? 68   SER A N   1 
ATOM   495   C  CA  . SER A  1 68  ? 54.962  102.077 83.497  1.00 15.61 ? 68   SER A CA  1 
ATOM   496   C  C   . SER A  1 68  ? 55.196  102.704 82.129  1.00 15.87 ? 68   SER A C   1 
ATOM   497   O  O   . SER A  1 68  ? 55.895  103.708 81.995  1.00 16.23 ? 68   SER A O   1 
ATOM   498   C  CB  . SER A  1 68  ? 55.837  102.785 84.550  1.00 15.67 ? 68   SER A CB  1 
ATOM   499   O  OG  . SER A  1 68  ? 55.447  102.387 85.859  1.00 17.58 ? 68   SER A OG  1 
ATOM   500   N  N   . ARG A  1 69  ? 54.604  102.106 81.111  1.00 14.87 ? 69   ARG A N   1 
ATOM   501   C  CA  . ARG A  1 69  ? 54.725  102.625 79.774  1.00 14.30 ? 69   ARG A CA  1 
ATOM   502   C  C   . ARG A  1 69  ? 53.442  103.331 79.384  1.00 13.20 ? 69   ARG A C   1 
ATOM   503   O  O   . ARG A  1 69  ? 52.503  103.358 80.180  1.00 12.31 ? 69   ARG A O   1 
ATOM   504   C  CB  . ARG A  1 69  ? 55.048  101.471 78.837  1.00 14.92 ? 69   ARG A CB  1 
ATOM   505   C  CG  . ARG A  1 69  ? 56.484  101.029 79.033  1.00 16.81 ? 69   ARG A CG  1 
ATOM   506   C  CD  . ARG A  1 69  ? 56.988  100.063 78.014  1.00 20.19 ? 69   ARG A CD  1 
ATOM   507   N  NE  . ARG A  1 69  ? 58.290  99.531  78.413  1.00 18.47 ? 69   ARG A NE  1 
ATOM   508   C  CZ  . ARG A  1 69  ? 58.947  98.632  77.699  1.00 19.93 ? 69   ARG A CZ  1 
ATOM   509   N  NH1 . ARG A  1 69  ? 58.414  98.172  76.568  1.00 20.33 ? 69   ARG A NH1 1 
ATOM   510   N  NH2 . ARG A  1 69  ? 60.122  98.189  78.114  1.00 16.76 ? 69   ARG A NH2 1 
ATOM   511   N  N   . LYS A  1 70  ? 53.424  103.973 78.208  1.00 12.62 ? 70   LYS A N   1 
ATOM   512   C  CA  . LYS A  1 70  ? 52.168  104.537 77.696  1.00 11.63 ? 70   LYS A CA  1 
ATOM   513   C  C   . LYS A  1 70  ? 51.364  103.492 76.923  1.00 10.35 ? 70   LYS A C   1 
ATOM   514   O  O   . LYS A  1 70  ? 51.869  102.422 76.514  1.00 9.15  ? 70   LYS A O   1 
ATOM   515   C  CB  . LYS A  1 70  ? 52.406  105.743 76.757  1.00 12.52 ? 70   LYS A CB  1 
ATOM   516   C  CG  . LYS A  1 70  ? 53.423  106.749 77.279  1.00 18.03 ? 70   LYS A CG  1 
ATOM   517   C  CD  . LYS A  1 70  ? 52.851  107.687 78.297  1.00 24.23 ? 70   LYS A CD  1 
ATOM   518   C  CE  . LYS A  1 70  ? 53.691  108.971 78.375  1.00 26.05 ? 70   LYS A CE  1 
ATOM   519   N  NZ  . LYS A  1 70  ? 54.075  109.500 77.011  1.00 31.69 ? 70   LYS A NZ  1 
ATOM   520   N  N   . HIS A  1 71  ? 50.103  103.824 76.689  1.00 9.24  ? 71   HIS A N   1 
ATOM   521   C  CA  . HIS A  1 71  ? 49.199  102.920 75.974  1.00 8.96  ? 71   HIS A CA  1 
ATOM   522   C  C   . HIS A  1 71  ? 49.570  102.787 74.510  1.00 9.53  ? 71   HIS A C   1 
ATOM   523   O  O   . HIS A  1 71  ? 49.981  103.768 73.855  1.00 10.00 ? 71   HIS A O   1 
ATOM   524   C  CB  . HIS A  1 71  ? 47.777  103.430 76.069  1.00 6.94  ? 71   HIS A CB  1 
ATOM   525   C  CG  . HIS A  1 71  ? 46.758  102.550 75.391  1.00 8.76  ? 71   HIS A CG  1 
ATOM   526   N  ND1 . HIS A  1 71  ? 46.226  101.418 75.983  1.00 6.48  ? 71   HIS A ND1 1 
ATOM   527   C  CD2 . HIS A  1 71  ? 46.150  102.660 74.189  1.00 8.71  ? 71   HIS A CD2 1 
ATOM   528   C  CE1 . HIS A  1 71  ? 45.350  100.862 75.161  1.00 7.68  ? 71   HIS A CE1 1 
ATOM   529   N  NE2 . HIS A  1 71  ? 45.273  101.606 74.072  1.00 7.70  ? 71   HIS A NE2 1 
ATOM   530   N  N   . GLY A  1 72  ? 49.438  101.584 73.973  1.00 9.18  ? 72   GLY A N   1 
ATOM   531   C  CA  . GLY A  1 72  ? 49.667  101.420 72.541  1.00 10.39 ? 72   GLY A CA  1 
ATOM   532   C  C   . GLY A  1 72  ? 48.884  100.227 72.023  1.00 10.46 ? 72   GLY A C   1 
ATOM   533   O  O   . GLY A  1 72  ? 47.996  99.683  72.705  1.00 9.51  ? 72   GLY A O   1 
ATOM   534   N  N   . GLY A  1 73  ? 49.187  99.819  70.793  1.00 11.23 ? 73   GLY A N   1 
ATOM   535   C  CA  . GLY A  1 73  ? 48.583  98.606  70.261  1.00 10.07 ? 73   GLY A CA  1 
ATOM   536   C  C   . GLY A  1 73  ? 49.456  97.405  70.629  1.00 10.00 ? 73   GLY A C   1 
ATOM   537   O  O   . GLY A  1 73  ? 50.614  97.567  71.042  1.00 10.68 ? 73   GLY A O   1 
ATOM   538   N  N   . PRO A  1 74  ? 48.927  96.202  70.485  1.00 10.97 ? 74   PRO A N   1 
ATOM   539   C  CA  . PRO A  1 74  ? 49.631  94.995  70.947  1.00 12.40 ? 74   PRO A CA  1 
ATOM   540   C  C   . PRO A  1 74  ? 50.975  94.814  70.239  1.00 13.67 ? 74   PRO A C   1 
ATOM   541   O  O   . PRO A  1 74  ? 51.914  94.248  70.787  1.00 14.28 ? 74   PRO A O   1 
ATOM   542   C  CB  . PRO A  1 74  ? 48.668  93.838  70.615  1.00 12.46 ? 74   PRO A CB  1 
ATOM   543   C  CG  . PRO A  1 74  ? 47.518  94.433  69.866  1.00 10.28 ? 74   PRO A CG  1 
ATOM   544   C  CD  . PRO A  1 74  ? 47.601  95.905  69.941  1.00 12.11 ? 74   PRO A CD  1 
ATOM   545   N  N   . LYS A  1 75  ? 51.081  95.346  69.037  1.00 15.81 ? 75   LYS A N   1 
ATOM   546   C  CA  . LYS A  1 75  ? 52.329  95.193  68.287  1.00 17.69 ? 75   LYS A CA  1 
ATOM   547   C  C   . LYS A  1 75  ? 53.410  96.253  68.562  1.00 18.47 ? 75   LYS A C   1 
ATOM   548   O  O   . LYS A  1 75  ? 54.553  96.138  68.068  1.00 18.19 ? 75   LYS A O   1 
ATOM   549   C  CB  . LYS A  1 75  ? 51.997  95.049  66.801  1.00 18.44 ? 75   LYS A CB  1 
ATOM   550   C  CG  . LYS A  1 75  ? 51.130  93.800  66.511  1.00 22.34 ? 75   LYS A CG  1 
ATOM   551   C  CD  . LYS A  1 75  ? 50.070  94.006  65.405  1.00 28.97 ? 75   LYS A CD  1 
ATOM   552   C  CE  . LYS A  1 75  ? 49.072  92.795  65.271  1.00 32.32 ? 75   LYS A CE  1 
ATOM   553   N  NZ  . LYS A  1 75  ? 47.924  92.685  66.290  1.00 30.69 ? 75   LYS A NZ  1 
ATOM   554   N  N   . ASP A  1 76  ? 53.067  97.276  69.349  1.00 17.65 ? 76   ASP A N   1 
ATOM   555   C  CA  . ASP A  1 76  ? 53.999  98.355  69.702  1.00 18.29 ? 76   ASP A CA  1 
ATOM   556   C  C   . ASP A  1 76  ? 54.932  98.022  70.864  1.00 18.11 ? 76   ASP A C   1 
ATOM   557   O  O   . ASP A  1 76  ? 54.501  97.392  71.824  1.00 17.84 ? 76   ASP A O   1 
ATOM   558   C  CB  . ASP A  1 76  ? 53.209  99.599  70.103  1.00 17.54 ? 76   ASP A CB  1 
ATOM   559   C  CG  . ASP A  1 76  ? 52.319  100.115 68.985  1.00 20.23 ? 76   ASP A CG  1 
ATOM   560   O  OD1 . ASP A  1 76  ? 52.676  99.905  67.798  1.00 22.49 ? 76   ASP A OD1 1 
ATOM   561   O  OD2 . ASP A  1 76  ? 51.260  100.751 69.184  1.00 17.39 ? 76   ASP A OD2 1 
ATOM   562   N  N   . GLU A  1 77  ? 56.194  98.461  70.812  1.00 17.47 ? 77   GLU A N   1 
ATOM   563   C  CA  . GLU A  1 77  ? 57.068  98.325  71.985  1.00 17.45 ? 77   GLU A CA  1 
ATOM   564   C  C   . GLU A  1 77  ? 56.503  99.176  73.124  1.00 17.10 ? 77   GLU A C   1 
ATOM   565   O  O   . GLU A  1 77  ? 56.500  98.748  74.283  1.00 17.78 ? 77   GLU A O   1 
ATOM   566   C  CB  . GLU A  1 77  ? 58.518  98.754  71.696  1.00 18.91 ? 77   GLU A CB  1 
ATOM   567   C  CG  . GLU A  1 77  ? 59.488  98.466  72.848  1.00 19.72 ? 77   GLU A CG  1 
ATOM   568   C  CD  . GLU A  1 77  ? 60.836  99.128  72.648  1.00 24.54 ? 77   GLU A CD  1 
ATOM   569   O  OE1 . GLU A  1 77  ? 61.070  99.618  71.523  1.00 27.11 ? 77   GLU A OE1 1 
ATOM   570   O  OE2 . GLU A  1 77  ? 61.668  99.171  73.593  1.00 23.21 ? 77   GLU A OE2 1 
ATOM   571   N  N   . GLU A  1 78  ? 55.997  100.365 72.806  1.00 15.01 ? 78   GLU A N   1 
ATOM   572   C  CA  . GLU A  1 78  ? 55.422  101.208 73.844  1.00 14.69 ? 78   GLU A CA  1 
ATOM   573   C  C   . GLU A  1 78  ? 53.966  100.810 74.000  1.00 12.99 ? 78   GLU A C   1 
ATOM   574   O  O   . GLU A  1 78  ? 53.111  101.210 73.214  1.00 11.94 ? 78   GLU A O   1 
ATOM   575   C  CB  . GLU A  1 78  ? 55.541  102.702 73.506  1.00 14.71 ? 78   GLU A CB  1 
ATOM   576   C  CG  . GLU A  1 78  ? 55.142  103.643 74.638  1.00 17.12 ? 78   GLU A CG  1 
ATOM   577   C  CD  . GLU A  1 78  ? 56.136  103.665 75.806  1.00 18.92 ? 78   GLU A CD  1 
ATOM   578   O  OE1 . GLU A  1 78  ? 57.231  103.025 75.694  1.00 21.30 ? 78   GLU A OE1 1 
ATOM   579   O  OE2 . GLU A  1 78  ? 55.846  104.353 76.839  1.00 14.11 ? 78   GLU A OE2 1 
ATOM   580   N  N   . ARG A  1 79  ? 53.687  99.983  75.000  1.00 12.54 ? 79   ARG A N   1 
ATOM   581   C  CA  . ARG A  1 79  ? 52.324  99.547  75.240  1.00 11.45 ? 79   ARG A CA  1 
ATOM   582   C  C   . ARG A  1 79  ? 52.293  99.078  76.659  1.00 11.15 ? 79   ARG A C   1 
ATOM   583   O  O   . ARG A  1 79  ? 53.335  98.791  77.248  1.00 11.30 ? 79   ARG A O   1 
ATOM   584   C  CB  . ARG A  1 79  ? 51.917  98.367  74.327  1.00 11.95 ? 79   ARG A CB  1 
ATOM   585   C  CG  . ARG A  1 79  ? 52.793  97.083  74.507  1.00 12.12 ? 79   ARG A CG  1 
ATOM   586   C  CD  . ARG A  1 79  ? 52.244  95.808  73.834  1.00 10.88 ? 79   ARG A CD  1 
ATOM   587   N  NE  . ARG A  1 79  ? 51.351  95.059  74.754  1.00 7.93  ? 79   ARG A NE  1 
ATOM   588   C  CZ  . ARG A  1 79  ? 50.960  93.832  74.522  1.00 7.84  ? 79   ARG A CZ  1 
ATOM   589   N  NH1 . ARG A  1 79  ? 51.307  93.259  73.388  1.00 5.87  ? 79   ARG A NH1 1 
ATOM   590   N  NH2 . ARG A  1 79  ? 50.214  93.158  75.401  1.00 6.76  ? 79   ARG A NH2 1 
ATOM   591   N  N   . HIS A  1 80  ? 51.088  99.038  77.210  1.00 10.26 ? 80   HIS A N   1 
ATOM   592   C  CA  . HIS A  1 80  ? 50.859  98.448  78.517  1.00 8.59  ? 80   HIS A CA  1 
ATOM   593   C  C   . HIS A  1 80  ? 50.847  96.934  78.366  1.00 8.07  ? 80   HIS A C   1 
ATOM   594   O  O   . HIS A  1 80  ? 50.443  96.390  77.313  1.00 8.41  ? 80   HIS A O   1 
ATOM   595   C  CB  . HIS A  1 80  ? 49.476  98.878  78.994  1.00 8.55  ? 80   HIS A CB  1 
ATOM   596   C  CG  . HIS A  1 80  ? 49.315  100.360 79.148  1.00 7.48  ? 80   HIS A CG  1 
ATOM   597   N  ND1 . HIS A  1 80  ? 48.136  101.010 78.855  1.00 7.60  ? 80   HIS A ND1 1 
ATOM   598   C  CD2 . HIS A  1 80  ? 50.147  101.301 79.660  1.00 7.54  ? 80   HIS A CD2 1 
ATOM   599   C  CE1 . HIS A  1 80  ? 48.258  102.292 79.155  1.00 10.03 ? 80   HIS A CE1 1 
ATOM   600   N  NE2 . HIS A  1 80  ? 49.465  102.489 79.667  1.00 9.76  ? 80   HIS A NE2 1 
ATOM   601   N  N   . VAL A  1 81  ? 51.278  96.220  79.405  1.00 7.63  ? 81   VAL A N   1 
ATOM   602   C  CA  . VAL A  1 81  ? 51.154  94.765  79.317  1.00 7.62  ? 81   VAL A CA  1 
ATOM   603   C  C   . VAL A  1 81  ? 49.724  94.376  78.943  1.00 7.50  ? 81   VAL A C   1 
ATOM   604   O  O   . VAL A  1 81  ? 49.515  93.461  78.155  1.00 8.13  ? 81   VAL A O   1 
ATOM   605   C  CB  . VAL A  1 81  ? 51.578  94.066  80.604  1.00 7.16  ? 81   VAL A CB  1 
ATOM   606   C  CG1 . VAL A  1 81  ? 51.202  92.570  80.550  1.00 5.00  ? 81   VAL A CG1 1 
ATOM   607   C  CG2 . VAL A  1 81  ? 53.114  94.224  80.737  1.00 7.55  ? 81   VAL A CG2 1 
ATOM   608   N  N   . GLY A  1 82  ? 48.724  95.054  79.494  1.00 7.91  ? 82   GLY A N   1 
ATOM   609   C  CA  . GLY A  1 82  ? 47.373  94.599  79.220  1.00 7.86  ? 82   GLY A CA  1 
ATOM   610   C  C   . GLY A  1 82  ? 46.805  95.070  77.886  1.00 9.16  ? 82   GLY A C   1 
ATOM   611   O  O   . GLY A  1 82  ? 45.624  94.924  77.668  1.00 8.61  ? 82   GLY A O   1 
ATOM   612   N  N   . ASP A  1 83  ? 47.618  95.611  76.976  1.00 7.81  ? 83   ASP A N   1 
ATOM   613   C  CA  . ASP A  1 83  ? 47.042  96.177  75.755  1.00 8.36  ? 83   ASP A CA  1 
ATOM   614   C  C   . ASP A  1 83  ? 46.895  95.107  74.675  1.00 9.13  ? 83   ASP A C   1 
ATOM   615   O  O   . ASP A  1 83  ? 47.812  94.908  73.896  1.00 10.49 ? 83   ASP A O   1 
ATOM   616   C  CB  . ASP A  1 83  ? 47.919  97.337  75.197  1.00 8.09  ? 83   ASP A CB  1 
ATOM   617   C  CG  . ASP A  1 83  ? 47.843  98.605  76.054  1.00 7.72  ? 83   ASP A CG  1 
ATOM   618   O  OD1 . ASP A  1 83  ? 46.870  98.747  76.861  1.00 6.31  ? 83   ASP A OD1 1 
ATOM   619   O  OD2 . ASP A  1 83  ? 48.681  99.538  75.948  1.00 8.92  ? 83   ASP A OD2 1 
ATOM   620   N  N   . LEU A  1 84  ? 45.743  94.462  74.587  1.00 8.93  ? 84   LEU A N   1 
ATOM   621   C  CA  . LEU A  1 84  ? 45.528  93.434  73.601  1.00 9.99  ? 84   LEU A CA  1 
ATOM   622   C  C   . LEU A  1 84  ? 44.789  93.946  72.359  1.00 10.78 ? 84   LEU A C   1 
ATOM   623   O  O   . LEU A  1 84  ? 44.328  93.150  71.532  1.00 11.05 ? 84   LEU A O   1 
ATOM   624   C  CB  . LEU A  1 84  ? 44.764  92.264  74.222  1.00 9.78  ? 84   LEU A CB  1 
ATOM   625   C  CG  . LEU A  1 84  ? 45.507  91.698  75.423  1.00 9.61  ? 84   LEU A CG  1 
ATOM   626   C  CD1 . LEU A  1 84  ? 44.555  90.681  76.091  1.00 11.00 ? 84   LEU A CD1 1 
ATOM   627   C  CD2 . LEU A  1 84  ? 46.801  91.062  74.920  1.00 11.44 ? 84   LEU A CD2 1 
ATOM   628   N  N   . GLY A  1 85  ? 44.634  95.255  72.248  1.00 9.60  ? 85   GLY A N   1 
ATOM   629   C  CA  . GLY A  1 85  ? 44.027  95.829  71.050  1.00 9.29  ? 85   GLY A CA  1 
ATOM   630   C  C   . GLY A  1 85  ? 42.518  95.810  70.973  1.00 9.61  ? 85   GLY A C   1 
ATOM   631   O  O   . GLY A  1 85  ? 41.838  96.211  71.910  1.00 8.70  ? 85   GLY A O   1 
ATOM   632   N  N   . ASN A  1 86  ? 42.003  95.382  69.822  1.00 8.26  ? 86   ASN A N   1 
ATOM   633   C  CA  . ASN A  1 86  ? 40.593  95.336  69.588  1.00 8.38  ? 86   ASN A CA  1 
ATOM   634   C  C   . ASN A  1 86  ? 40.114  93.936  69.262  1.00 8.20  ? 86   ASN A C   1 
ATOM   635   O  O   . ASN A  1 86  ? 40.872  93.111  68.750  1.00 8.15  ? 86   ASN A O   1 
ATOM   636   C  CB  . ASN A  1 86  ? 40.209  96.226  68.386  1.00 7.88  ? 86   ASN A CB  1 
ATOM   637   C  CG  . ASN A  1 86  ? 40.321  97.695  68.712  1.00 10.61 ? 86   ASN A CG  1 
ATOM   638   O  OD1 . ASN A  1 86  ? 39.623  98.184  69.609  1.00 9.67  ? 86   ASN A OD1 1 
ATOM   639   N  ND2 . ASN A  1 86  ? 41.251  98.400  68.032  1.00 6.85  ? 86   ASN A ND2 1 
ATOM   640   N  N   . VAL A  1 87  ? 38.859  93.666  69.585  1.00 8.19  ? 87   VAL A N   1 
ATOM   641   C  CA  . VAL A  1 87  ? 38.193  92.498  69.029  1.00 8.34  ? 87   VAL A CA  1 
ATOM   642   C  C   . VAL A  1 87  ? 37.107  92.988  68.099  1.00 8.53  ? 87   VAL A C   1 
ATOM   643   O  O   . VAL A  1 87  ? 36.751  94.173  68.102  1.00 9.98  ? 87   VAL A O   1 
ATOM   644   C  CB  . VAL A  1 87  ? 37.565  91.579  70.112  1.00 8.30  ? 87   VAL A CB  1 
ATOM   645   C  CG1 . VAL A  1 87  ? 38.712  90.912  70.930  1.00 9.57  ? 87   VAL A CG1 1 
ATOM   646   C  CG2 . VAL A  1 87  ? 36.628  92.403  70.990  1.00 9.00  ? 87   VAL A CG2 1 
ATOM   647   N  N   . THR A  1 88  ? 36.587  92.093  67.260  1.00 8.92  ? 88   THR A N   1 
ATOM   648   C  CA  . THR A  1 88  ? 35.628  92.521  66.227  1.00 9.75  ? 88   THR A CA  1 
ATOM   649   C  C   . THR A  1 88  ? 34.284  91.828  66.413  1.00 10.16 ? 88   THR A C   1 
ATOM   650   O  O   . THR A  1 88  ? 34.245  90.605  66.422  1.00 10.11 ? 88   THR A O   1 
ATOM   651   C  CB  . THR A  1 88  ? 36.192  92.147  64.829  1.00 11.82 ? 88   THR A CB  1 
ATOM   652   O  OG1 . THR A  1 88  ? 37.433  92.855  64.598  1.00 9.53  ? 88   THR A OG1 1 
ATOM   653   C  CG2 . THR A  1 88  ? 35.246  92.646  63.697  1.00 11.56 ? 88   THR A CG2 1 
ATOM   654   N  N   . ALA A  1 89  ? 33.191  92.591  66.529  1.00 9.91  ? 89   ALA A N   1 
ATOM   655   C  CA  . ALA A  1 89  ? 31.853  91.981  66.602  1.00 11.07 ? 89   ALA A CA  1 
ATOM   656   C  C   . ALA A  1 89  ? 31.213  92.073  65.222  1.00 11.99 ? 89   ALA A C   1 
ATOM   657   O  O   . ALA A  1 89  ? 31.341  93.099  64.547  1.00 10.78 ? 89   ALA A O   1 
ATOM   658   C  CB  . ALA A  1 89  ? 30.979  92.693  67.618  1.00 11.25 ? 89   ALA A CB  1 
ATOM   659   N  N   . ASP A  1 90  ? 30.552  90.989  64.814  1.00 13.68 ? 90   ASP A N   1 
ATOM   660   C  CA  . ASP A  1 90  ? 29.934  90.892  63.501  1.00 15.26 ? 90   ASP A CA  1 
ATOM   661   C  C   . ASP A  1 90  ? 28.567  91.566  63.494  1.00 16.05 ? 90   ASP A C   1 
ATOM   662   O  O   . ASP A  1 90  ? 28.202  92.248  64.450  1.00 14.77 ? 90   ASP A O   1 
ATOM   663   C  CB  . ASP A  1 90  ? 29.838  89.431  63.034  1.00 15.69 ? 90   ASP A CB  1 
ATOM   664   C  CG  . ASP A  1 90  ? 28.996  88.532  63.979  1.00 17.88 ? 90   ASP A CG  1 
ATOM   665   O  OD1 . ASP A  1 90  ? 28.143  89.027  64.759  1.00 17.86 ? 90   ASP A OD1 1 
ATOM   666   O  OD2 . ASP A  1 90  ? 29.152  87.287  64.001  1.00 18.74 ? 90   ASP A OD2 1 
ATOM   667   N  N   . LYS A  1 91  ? 27.824  91.385  62.403  1.00 16.43 ? 91   LYS A N   1 
ATOM   668   C  CA  . LYS A  1 91  ? 26.543  92.041  62.266  1.00 17.77 ? 91   LYS A CA  1 
ATOM   669   C  C   . LYS A  1 91  ? 25.548  91.574  63.335  1.00 18.14 ? 91   LYS A C   1 
ATOM   670   O  O   . LYS A  1 91  ? 24.671  92.334  63.731  1.00 18.43 ? 91   LYS A O   1 
ATOM   671   C  CB  . LYS A  1 91  ? 25.986  91.874  60.832  1.00 17.96 ? 91   LYS A CB  1 
ATOM   672   C  CG  . LYS A  1 91  ? 25.906  90.419  60.346  1.00 20.65 ? 91   LYS A CG  1 
ATOM   673   C  CD  . LYS A  1 91  ? 25.406  90.312  58.877  1.00 25.10 ? 91   LYS A CD  1 
ATOM   674   C  CE  . LYS A  1 91  ? 25.752  88.952  58.249  1.00 27.94 ? 91   LYS A CE  1 
ATOM   675   N  NZ  . LYS A  1 91  ? 25.468  88.896  56.774  1.00 29.97 ? 91   LYS A NZ  1 
ATOM   676   N  N   . ASP A  1 92  ? 25.728  90.349  63.834  1.00 18.30 ? 92   ASP A N   1 
ATOM   677   C  CA  . ASP A  1 92  ? 24.857  89.786  64.872  1.00 18.39 ? 92   ASP A CA  1 
ATOM   678   C  C   . ASP A  1 92  ? 25.297  90.138  66.302  1.00 17.22 ? 92   ASP A C   1 
ATOM   679   O  O   . ASP A  1 92  ? 24.723  89.656  67.295  1.00 15.99 ? 92   ASP A O   1 
ATOM   680   C  CB  . ASP A  1 92  ? 24.792  88.274  64.707  1.00 19.18 ? 92   ASP A CB  1 
ATOM   681   C  CG  . ASP A  1 92  ? 24.096  87.870  63.426  1.00 22.15 ? 92   ASP A CG  1 
ATOM   682   O  OD1 . ASP A  1 92  ? 23.033  88.467  63.119  1.00 25.12 ? 92   ASP A OD1 1 
ATOM   683   O  OD2 . ASP A  1 92  ? 24.538  86.986  62.662  1.00 24.89 ? 92   ASP A OD2 1 
ATOM   684   N  N   . GLY A  1 93  ? 26.324  90.973  66.396  1.00 16.08 ? 93   GLY A N   1 
ATOM   685   C  CA  . GLY A  1 93  ? 26.834  91.409  67.685  1.00 15.08 ? 93   GLY A CA  1 
ATOM   686   C  C   . GLY A  1 93  ? 27.730  90.412  68.388  1.00 13.99 ? 93   GLY A C   1 
ATOM   687   O  O   . GLY A  1 93  ? 27.976  90.558  69.573  1.00 14.09 ? 93   GLY A O   1 
ATOM   688   N  N   . VAL A  1 94  ? 28.239  89.424  67.659  1.00 13.22 ? 94   VAL A N   1 
ATOM   689   C  CA  . VAL A  1 94  ? 29.083  88.402  68.247  1.00 12.89 ? 94   VAL A CA  1 
ATOM   690   C  C   . VAL A  1 94  ? 30.524  88.567  67.818  1.00 12.49 ? 94   VAL A C   1 
ATOM   691   O  O   . VAL A  1 94  ? 30.810  88.703  66.611  1.00 10.99 ? 94   VAL A O   1 
ATOM   692   C  CB  . VAL A  1 94  ? 28.662  87.005  67.806  1.00 14.02 ? 94   VAL A CB  1 
ATOM   693   C  CG1 . VAL A  1 94  ? 29.623  85.979  68.421  1.00 13.55 ? 94   VAL A CG1 1 
ATOM   694   C  CG2 . VAL A  1 94  ? 27.209  86.711  68.236  1.00 15.96 ? 94   VAL A CG2 1 
ATOM   695   N  N   . ALA A  1 95  ? 31.419  88.591  68.803  1.00 11.62 ? 95   ALA A N   1 
ATOM   696   C  CA  . ALA A  1 95  ? 32.835  88.684  68.532  1.00 12.29 ? 95   ALA A CA  1 
ATOM   697   C  C   . ALA A  1 95  ? 33.490  87.366  68.804  1.00 12.41 ? 95   ALA A C   1 
ATOM   698   O  O   . ALA A  1 95  ? 33.517  86.876  69.949  1.00 11.75 ? 95   ALA A O   1 
ATOM   699   C  CB  . ALA A  1 95  ? 33.514  89.791  69.355  1.00 11.31 ? 95   ALA A CB  1 
ATOM   700   N  N   . ASP A  1 96  ? 34.028  86.780  67.743  1.00 12.01 ? 96   ASP A N   1 
ATOM   701   C  CA  . ASP A  1 96  ? 34.771  85.562  67.922  1.00 13.36 ? 96   ASP A CA  1 
ATOM   702   C  C   . ASP A  1 96  ? 36.201  86.015  68.132  1.00 13.17 ? 96   ASP A C   1 
ATOM   703   O  O   . ASP A  1 96  ? 36.792  86.687  67.287  1.00 14.29 ? 96   ASP A O   1 
ATOM   704   C  CB  . ASP A  1 96  ? 34.522  84.633  66.736  1.00 14.99 ? 96   ASP A CB  1 
ATOM   705   C  CG  . ASP A  1 96  ? 33.133  83.977  66.834  1.00 18.68 ? 96   ASP A CG  1 
ATOM   706   O  OD1 . ASP A  1 96  ? 32.788  83.475  67.951  1.00 25.99 ? 96   ASP A OD1 1 
ATOM   707   O  OD2 . ASP A  1 96  ? 32.302  83.925  65.885  1.00 24.47 ? 96   ASP A OD2 1 
ATOM   708   N  N   . VAL A  1 97  ? 36.727  85.743  69.310  1.00 11.70 ? 97   VAL A N   1 
ATOM   709   C  CA  . VAL A  1 97  ? 38.031  86.264  69.649  1.00 10.19 ? 97   VAL A CA  1 
ATOM   710   C  C   . VAL A  1 97  ? 39.082  85.206  69.458  1.00 10.01 ? 97   VAL A C   1 
ATOM   711   O  O   . VAL A  1 97  ? 38.901  84.055  69.886  1.00 8.32  ? 97   VAL A O   1 
ATOM   712   C  CB  . VAL A  1 97  ? 38.037  86.698  71.142  1.00 10.57 ? 97   VAL A CB  1 
ATOM   713   C  CG1 . VAL A  1 97  ? 39.430  87.250  71.563  1.00 9.22  ? 97   VAL A CG1 1 
ATOM   714   C  CG2 . VAL A  1 97  ? 36.969  87.726  71.363  1.00 9.12  ? 97   VAL A CG2 1 
ATOM   715   N  N   . SER A  1 98  ? 40.166  85.576  68.787  1.00 9.23  ? 98   SER A N   1 
ATOM   716   C  CA  . SER A  1 98  ? 41.303  84.680  68.662  1.00 11.58 ? 98   SER A CA  1 
ATOM   717   C  C   . SER A  1 98  ? 42.581  85.496  68.479  1.00 11.84 ? 98   SER A C   1 
ATOM   718   O  O   . SER A  1 98  ? 42.827  86.052  67.430  1.00 11.25 ? 98   SER A O   1 
ATOM   719   C  CB  . SER A  1 98  ? 41.114  83.679  67.525  1.00 11.71 ? 98   SER A CB  1 
ATOM   720   O  OG  . SER A  1 98  ? 42.067  82.662  67.686  1.00 14.18 ? 98   SER A OG  1 
ATOM   721   N  N   . ILE A  1 99  ? 43.365  85.573  69.546  1.00 12.53 ? 99   ILE A N   1 
ATOM   722   C  CA  . ILE A  1 99  ? 44.536  86.422  69.616  1.00 13.72 ? 99   ILE A CA  1 
ATOM   723   C  C   . ILE A  1 99  ? 45.674  85.594  70.214  1.00 13.88 ? 99   ILE A C   1 
ATOM   724   O  O   . ILE A  1 99  ? 45.424  84.656  70.969  1.00 14.28 ? 99   ILE A O   1 
ATOM   725   C  CB  . ILE A  1 99  ? 44.126  87.577  70.563  1.00 14.87 ? 99   ILE A CB  1 
ATOM   726   C  CG1 . ILE A  1 99  ? 43.390  88.681  69.786  1.00 15.52 ? 99   ILE A CG1 1 
ATOM   727   C  CG2 . ILE A  1 99  ? 45.279  88.211  71.309  1.00 16.60 ? 99   ILE A CG2 1 
ATOM   728   C  CD1 . ILE A  1 99  ? 42.725  89.701  70.735  1.00 15.11 ? 99   ILE A CD1 1 
ATOM   729   N  N   . GLU A  1 100 ? 46.911  85.935  69.878  1.00 14.41 ? 100  GLU A N   1 
ATOM   730   C  CA  . GLU A  1 100 ? 48.080  85.362  70.540  1.00 14.82 ? 100  GLU A CA  1 
ATOM   731   C  C   . GLU A  1 100 ? 48.942  86.535  70.964  1.00 13.60 ? 100  GLU A C   1 
ATOM   732   O  O   . GLU A  1 100 ? 49.184  87.456  70.166  1.00 12.78 ? 100  GLU A O   1 
ATOM   733   C  CB  . GLU A  1 100 ? 48.846  84.463  69.598  1.00 17.56 ? 100  GLU A CB  1 
ATOM   734   C  CG  . GLU A  1 100 ? 49.423  83.241  70.289  1.00 24.35 ? 100  GLU A CG  1 
ATOM   735   C  CD  . GLU A  1 100 ? 49.963  82.225  69.303  1.00 31.34 ? 100  GLU A CD  1 
ATOM   736   O  OE1 . GLU A  1 100 ? 49.154  81.579  68.608  1.00 35.54 ? 100  GLU A OE1 1 
ATOM   737   O  OE2 . GLU A  1 100 ? 51.197  82.079  69.230  1.00 35.03 ? 100  GLU A OE2 1 
ATOM   738   N  N   . ASP A  1 101 ? 49.399  86.541  72.205  1.00 11.98 ? 101  ASP A N   1 
ATOM   739   C  CA  . ASP A  1 101 ? 50.202  87.655  72.686  1.00 11.51 ? 101  ASP A CA  1 
ATOM   740   C  C   . ASP A  1 101 ? 51.312  87.105  73.553  1.00 12.89 ? 101  ASP A C   1 
ATOM   741   O  O   . ASP A  1 101 ? 51.072  86.184  74.338  1.00 11.71 ? 101  ASP A O   1 
ATOM   742   C  CB  . ASP A  1 101 ? 49.339  88.594  73.519  1.00 11.21 ? 101  ASP A CB  1 
ATOM   743   C  CG  . ASP A  1 101 ? 50.017  89.884  73.830  1.00 10.63 ? 101  ASP A CG  1 
ATOM   744   O  OD1 . ASP A  1 101 ? 50.024  90.778  72.947  1.00 10.81 ? 101  ASP A OD1 1 
ATOM   745   O  OD2 . ASP A  1 101 ? 50.554  90.107  74.953  1.00 12.69 ? 101  ASP A OD2 1 
ATOM   746   N  N   . SER A  1 102 ? 52.510  87.678  73.425  1.00 13.13 ? 102  SER A N   1 
ATOM   747   C  CA  . SER A  1 102 ? 53.629  87.223  74.247  1.00 14.41 ? 102  SER A CA  1 
ATOM   748   C  C   . SER A  1 102 ? 54.077  88.253  75.248  1.00 13.94 ? 102  SER A C   1 
ATOM   749   O  O   . SER A  1 102 ? 55.171  88.138  75.813  1.00 15.37 ? 102  SER A O   1 
ATOM   750   C  CB  . SER A  1 102 ? 54.825  86.849  73.381  1.00 15.26 ? 102  SER A CB  1 
ATOM   751   O  OG  . SER A  1 102 ? 54.406  86.101  72.254  1.00 20.14 ? 102  SER A OG  1 
ATOM   752   N  N   . VAL A  1 103 ? 53.268  89.269  75.473  1.00 11.90 ? 103  VAL A N   1 
ATOM   753   C  CA  . VAL A  1 103 ? 53.645  90.261  76.464  1.00 11.35 ? 103  VAL A CA  1 
ATOM   754   C  C   . VAL A  1 103 ? 52.918  89.880  77.763  1.00 10.86 ? 103  VAL A C   1 
ATOM   755   O  O   . VAL A  1 103 ? 53.523  89.849  78.824  1.00 10.61 ? 103  VAL A O   1 
ATOM   756   C  CB  . VAL A  1 103 ? 53.363  91.676  75.973  1.00 11.08 ? 103  VAL A CB  1 
ATOM   757   C  CG1 . VAL A  1 103 ? 53.461  92.660  77.091  1.00 11.65 ? 103  VAL A CG1 1 
ATOM   758   C  CG2 . VAL A  1 103 ? 54.343  92.056  74.808  1.00 13.35 ? 103  VAL A CG2 1 
ATOM   759   N  N   . ILE A  1 104 ? 51.636  89.533  77.671  1.00 10.15 ? 104  ILE A N   1 
ATOM   760   C  CA  . ILE A  1 104 ? 50.935  88.967  78.842  1.00 10.02 ? 104  ILE A CA  1 
ATOM   761   C  C   . ILE A  1 104 ? 51.485  87.572  79.130  1.00 11.03 ? 104  ILE A C   1 
ATOM   762   O  O   . ILE A  1 104 ? 52.140  86.967  78.275  1.00 10.82 ? 104  ILE A O   1 
ATOM   763   C  CB  . ILE A  1 104 ? 49.417  88.863  78.593  1.00 9.83  ? 104  ILE A CB  1 
ATOM   764   C  CG1 . ILE A  1 104 ? 49.128  88.040  77.331  1.00 8.66  ? 104  ILE A CG1 1 
ATOM   765   C  CG2 . ILE A  1 104 ? 48.793  90.266  78.439  1.00 11.27 ? 104  ILE A CG2 1 
ATOM   766   C  CD1 . ILE A  1 104 ? 47.699  87.502  77.248  1.00 10.35 ? 104  ILE A CD1 1 
ATOM   767   N  N   . SER A  1 105 ? 51.212  87.072  80.329  1.00 11.26 ? 105  SER A N   1 
ATOM   768   C  CA  . SER A  1 105 ? 51.673  85.753  80.739  1.00 11.99 ? 105  SER A CA  1 
ATOM   769   C  C   . SER A  1 105 ? 50.704  85.178  81.727  1.00 11.87 ? 105  SER A C   1 
ATOM   770   O  O   . SER A  1 105 ? 49.919  85.920  82.331  1.00 11.53 ? 105  SER A O   1 
ATOM   771   C  CB  . SER A  1 105 ? 53.069  85.837  81.369  1.00 13.11 ? 105  SER A CB  1 
ATOM   772   O  OG  . SER A  1 105 ? 53.648  84.543  81.481  1.00 13.81 ? 105  SER A OG  1 
ATOM   773   N  N   . LEU A  1 106 ? 50.740  83.856  81.884  1.00 11.61 ? 106  LEU A N   1 
ATOM   774   C  CA  . LEU A  1 106 ? 49.915  83.195  82.886  1.00 12.80 ? 106  LEU A CA  1 
ATOM   775   C  C   . LEU A  1 106 ? 50.770  82.773  84.087  1.00 13.29 ? 106  LEU A C   1 
ATOM   776   O  O   . LEU A  1 106 ? 50.297  82.085  84.999  1.00 12.95 ? 106  LEU A O   1 
ATOM   777   C  CB  . LEU A  1 106 ? 49.130  82.027  82.298  1.00 12.61 ? 106  LEU A CB  1 
ATOM   778   C  CG  . LEU A  1 106 ? 48.162  82.336  81.161  1.00 13.30 ? 106  LEU A CG  1 
ATOM   779   C  CD1 . LEU A  1 106 ? 47.344  81.090  80.830  1.00 11.85 ? 106  LEU A CD1 1 
ATOM   780   C  CD2 . LEU A  1 106 ? 47.246  83.520  81.497  1.00 11.67 ? 106  LEU A CD2 1 
ATOM   781   N  N   . SER A  1 107 ? 52.023  83.197  84.097  1.00 14.36 ? 107  SER A N   1 
ATOM   782   C  CA  . SER A  1 107 ? 52.910  82.931  85.235  1.00 16.62 ? 107  SER A CA  1 
ATOM   783   C  C   . SER A  1 107 ? 53.982  84.013  85.233  1.00 17.20 ? 107  SER A C   1 
ATOM   784   O  O   . SER A  1 107 ? 54.186  84.642  84.210  1.00 18.07 ? 107  SER A O   1 
ATOM   785   C  CB  . SER A  1 107 ? 53.580  81.578  85.060  1.00 16.98 ? 107  SER A CB  1 
ATOM   786   O  OG  . SER A  1 107 ? 54.800  81.744  84.363  1.00 18.86 ? 107  SER A OG  1 
ATOM   787   N  N   . GLY A  1 108 ? 54.672  84.247  86.350  1.00 17.84 ? 108  GLY A N   1 
ATOM   788   C  CA  . GLY A  1 108 ? 55.772  85.212  86.332  1.00 18.48 ? 108  GLY A CA  1 
ATOM   789   C  C   . GLY A  1 108 ? 55.435  86.702  86.459  1.00 19.37 ? 108  GLY A C   1 
ATOM   790   O  O   . GLY A  1 108 ? 54.372  87.084  86.948  1.00 19.05 ? 108  GLY A O   1 
ATOM   791   N  N   . ASP A  1 109 ? 56.354  87.549  86.002  1.00 20.26 ? 109  ASP A N   1 
ATOM   792   C  CA  . ASP A  1 109 ? 56.234  89.009  86.140  1.00 21.11 ? 109  ASP A CA  1 
ATOM   793   C  C   . ASP A  1 109 ? 55.015  89.635  85.434  1.00 20.96 ? 109  ASP A C   1 
ATOM   794   O  O   . ASP A  1 109 ? 54.399  90.604  85.932  1.00 22.70 ? 109  ASP A O   1 
ATOM   795   C  CB  . ASP A  1 109 ? 57.510  89.675  85.594  1.00 21.65 ? 109  ASP A CB  1 
ATOM   796   C  CG  . ASP A  1 109 ? 58.788  89.190  86.298  1.00 22.69 ? 109  ASP A CG  1 
ATOM   797   O  OD1 . ASP A  1 109 ? 59.736  89.990  86.381  1.00 22.97 ? 109  ASP A OD1 1 
ATOM   798   O  OD2 . ASP A  1 109 ? 58.939  88.050  86.785  1.00 23.86 ? 109  ASP A OD2 1 
ATOM   799   N  N   . HIS A  1 110 ? 54.668  89.118  84.269  1.00 19.55 ? 110  HIS A N   1 
ATOM   800   C  CA  . HIS A  1 110 ? 53.561  89.719  83.535  1.00 17.38 ? 110  HIS A CA  1 
ATOM   801   C  C   . HIS A  1 110 ? 52.300  88.896  83.719  1.00 15.75 ? 110  HIS A C   1 
ATOM   802   O  O   . HIS A  1 110 ? 51.420  88.910  82.892  1.00 13.32 ? 110  HIS A O   1 
ATOM   803   C  CB  . HIS A  1 110 ? 53.906  89.854  82.058  1.00 18.30 ? 110  HIS A CB  1 
ATOM   804   C  CG  . HIS A  1 110 ? 54.957  90.887  81.785  1.00 19.13 ? 110  HIS A CG  1 
ATOM   805   N  ND1 . HIS A  1 110 ? 55.481  91.108  80.525  1.00 21.10 ? 110  HIS A ND1 1 
ATOM   806   C  CD2 . HIS A  1 110 ? 55.585  91.756  82.615  1.00 17.80 ? 110  HIS A CD2 1 
ATOM   807   C  CE1 . HIS A  1 110 ? 56.388  92.071  80.595  1.00 22.13 ? 110  HIS A CE1 1 
ATOM   808   N  NE2 . HIS A  1 110 ? 56.480  92.472  81.854  1.00 18.48 ? 110  HIS A NE2 1 
ATOM   809   N  N   . CYS A  1 111 ? 52.223  88.172  84.832  1.00 14.74 ? 111  CYS A N   1 
ATOM   810   C  CA  . CYS A  1 111 ? 51.070  87.329  85.098  1.00 13.86 ? 111  CYS A CA  1 
ATOM   811   C  C   . CYS A  1 111 ? 49.732  88.094  85.140  1.00 12.68 ? 111  CYS A C   1 
ATOM   812   O  O   . CYS A  1 111 ? 49.632  89.126  85.807  1.00 12.85 ? 111  CYS A O   1 
ATOM   813   C  CB  . CYS A  1 111 ? 51.283  86.575  86.406  1.00 14.66 ? 111  CYS A CB  1 
ATOM   814   S  SG  . CYS A  1 111 ? 50.101  85.239  86.536  1.00 17.73 ? 111  CYS A SG  1 
ATOM   815   N  N   . ILE A  1 112 ? 48.706  87.579  84.447  1.00 10.59 ? 112  ILE A N   1 
ATOM   816   C  CA  . ILE A  1 112 ? 47.396  88.223  84.466  1.00 9.37  ? 112  ILE A CA  1 
ATOM   817   C  C   . ILE A  1 112 ? 46.324  87.467  85.257  1.00 8.54  ? 112  ILE A C   1 
ATOM   818   O  O   . ILE A  1 112 ? 45.190  87.912  85.288  1.00 7.75  ? 112  ILE A O   1 
ATOM   819   C  CB  . ILE A  1 112 ? 46.876  88.510  83.034  1.00 8.60  ? 112  ILE A CB  1 
ATOM   820   C  CG1 . ILE A  1 112 ? 46.748  87.192  82.270  1.00 8.58  ? 112  ILE A CG1 1 
ATOM   821   C  CG2 . ILE A  1 112 ? 47.869  89.439  82.293  1.00 9.83  ? 112  ILE A CG2 1 
ATOM   822   C  CD1 . ILE A  1 112 ? 46.099  87.345  80.892  1.00 8.23  ? 112  ILE A CD1 1 
ATOM   823   N  N   . ILE A  1 113 ? 46.669  86.325  85.848  1.00 7.85  ? 113  ILE A N   1 
ATOM   824   C  CA  . ILE A  1 113 ? 45.742  85.597  86.713  1.00 8.25  ? 113  ILE A CA  1 
ATOM   825   C  C   . ILE A  1 113 ? 45.350  86.497  87.877  1.00 6.54  ? 113  ILE A C   1 
ATOM   826   O  O   . ILE A  1 113 ? 46.197  87.107  88.511  1.00 6.65  ? 113  ILE A O   1 
ATOM   827   C  CB  . ILE A  1 113 ? 46.407  84.344  87.310  1.00 7.89  ? 113  ILE A CB  1 
ATOM   828   C  CG1 . ILE A  1 113 ? 46.898  83.423  86.201  1.00 10.76 ? 113  ILE A CG1 1 
ATOM   829   C  CG2 . ILE A  1 113 ? 45.410  83.583  88.179  1.00 7.77  ? 113  ILE A CG2 1 
ATOM   830   C  CD1 . ILE A  1 113 ? 45.848  83.137  85.234  1.00 13.78 ? 113  ILE A CD1 1 
ATOM   831   N  N   . GLY A  1 114 ? 44.067  86.571  88.159  1.00 6.25  ? 114  GLY A N   1 
ATOM   832   C  CA  . GLY A  1 114 ? 43.582  87.382  89.257  1.00 5.64  ? 114  GLY A CA  1 
ATOM   833   C  C   . GLY A  1 114 ? 43.357  88.830  88.853  1.00 5.76  ? 114  GLY A C   1 
ATOM   834   O  O   . GLY A  1 114 ? 43.015  89.641  89.704  1.00 7.10  ? 114  GLY A O   1 
ATOM   835   N  N   . ARG A  1 115 ? 43.642  89.186  87.601  1.00 6.55  ? 115  ARG A N   1 
ATOM   836   C  CA  . ARG A  1 115 ? 43.391  90.554  87.132  1.00 7.49  ? 115  ARG A CA  1 
ATOM   837   C  C   . ARG A  1 115 ? 42.078  90.552  86.354  1.00 8.40  ? 115  ARG A C   1 
ATOM   838   O  O   . ARG A  1 115 ? 41.442  89.518  86.307  1.00 9.88  ? 115  ARG A O   1 
ATOM   839   C  CB  . ARG A  1 115 ? 44.574  91.061  86.299  1.00 7.85  ? 115  ARG A CB  1 
ATOM   840   C  CG  . ARG A  1 115 ? 45.864  90.981  87.135  1.00 7.65  ? 115  ARG A CG  1 
ATOM   841   C  CD  . ARG A  1 115 ? 47.068  91.745  86.566  1.00 8.19  ? 115  ARG A CD  1 
ATOM   842   N  NE  . ARG A  1 115 ? 48.274  91.502  87.378  1.00 7.25  ? 115  ARG A NE  1 
ATOM   843   C  CZ  . ARG A  1 115 ? 48.640  92.223  88.434  1.00 8.20  ? 115  ARG A CZ  1 
ATOM   844   N  NH1 . ARG A  1 115 ? 47.900  93.246  88.862  1.00 10.01 ? 115  ARG A NH1 1 
ATOM   845   N  NH2 . ARG A  1 115 ? 49.770  91.937  89.059  1.00 9.90  ? 115  ARG A NH2 1 
ATOM   846   N  N   . THR A  1 116 ? 41.709  91.661  85.695  1.00 7.62  ? 116  THR A N   1 
ATOM   847   C  CA  . THR A  1 116 ? 40.406  91.750  85.062  1.00 8.14  ? 116  THR A CA  1 
ATOM   848   C  C   . THR A  1 116 ? 40.472  91.960  83.580  1.00 8.96  ? 116  THR A C   1 
ATOM   849   O  O   . THR A  1 116 ? 41.170  92.875  83.102  1.00 9.44  ? 116  THR A O   1 
ATOM   850   C  CB  . THR A  1 116 ? 39.637  92.929  85.641  1.00 8.78  ? 116  THR A CB  1 
ATOM   851   O  OG1 . THR A  1 116 ? 39.233  92.603  86.974  1.00 6.78  ? 116  THR A OG1 1 
ATOM   852   C  CG2 . THR A  1 116 ? 38.313  93.171  84.878  1.00 7.86  ? 116  THR A CG2 1 
ATOM   853   N  N   . LEU A  1 117 ? 39.787  91.115  82.833  1.00 8.62  ? 117  LEU A N   1 
ATOM   854   C  CA  . LEU A  1 117 ? 39.649  91.398  81.385  1.00 7.68  ? 117  LEU A CA  1 
ATOM   855   C  C   . LEU A  1 117 ? 38.416  92.260  81.128  1.00 8.41  ? 117  LEU A C   1 
ATOM   856   O  O   . LEU A  1 117 ? 37.334  91.980  81.673  1.00 7.70  ? 117  LEU A O   1 
ATOM   857   C  CB  . LEU A  1 117 ? 39.493  90.078  80.632  1.00 7.18  ? 117  LEU A CB  1 
ATOM   858   C  CG  . LEU A  1 117 ? 39.406  90.075  79.096  1.00 7.75  ? 117  LEU A CG  1 
ATOM   859   C  CD1 . LEU A  1 117 ? 40.734  90.524  78.546  1.00 8.92  ? 117  LEU A CD1 1 
ATOM   860   C  CD2 . LEU A  1 117 ? 39.065  88.637  78.632  1.00 9.35  ? 117  LEU A CD2 1 
ATOM   861   N  N   . VAL A  1 118 ? 38.555  93.279  80.264  1.00 7.16  ? 118  VAL A N   1 
ATOM   862   C  CA  . VAL A  1 118 ? 37.494  94.204  79.976  1.00 7.66  ? 118  VAL A CA  1 
ATOM   863   C  C   . VAL A  1 118 ? 37.259  94.342  78.479  1.00 8.57  ? 118  VAL A C   1 
ATOM   864   O  O   . VAL A  1 118 ? 38.217  94.405  77.710  1.00 8.51  ? 118  VAL A O   1 
ATOM   865   C  CB  . VAL A  1 118 ? 37.839  95.600  80.531  1.00 8.09  ? 118  VAL A CB  1 
ATOM   866   C  CG1 . VAL A  1 118 ? 36.799  96.643  80.095  1.00 10.71 ? 118  VAL A CG1 1 
ATOM   867   C  CG2 . VAL A  1 118 ? 37.995  95.529  82.062  1.00 6.70  ? 118  VAL A CG2 1 
ATOM   868   N  N   . VAL A  1 119 ? 35.991  94.395  78.070  1.00 7.75  ? 119  VAL A N   1 
ATOM   869   C  CA  . VAL A  1 119 ? 35.669  94.686  76.674  1.00 8.86  ? 119  VAL A CA  1 
ATOM   870   C  C   . VAL A  1 119 ? 34.938  96.036  76.706  1.00 8.67  ? 119  VAL A C   1 
ATOM   871   O  O   . VAL A  1 119 ? 34.076  96.277  77.565  1.00 8.39  ? 119  VAL A O   1 
ATOM   872   C  CB  . VAL A  1 119 ? 34.868  93.557  75.975  1.00 9.26  ? 119  VAL A CB  1 
ATOM   873   C  CG1 . VAL A  1 119 ? 33.556  93.273  76.759  1.00 11.86 ? 119  VAL A CG1 1 
ATOM   874   C  CG2 . VAL A  1 119 ? 34.550  93.929  74.512  1.00 8.63  ? 119  VAL A CG2 1 
ATOM   875   N  N   . HIS A  1 120 ? 35.315  96.921  75.784  1.00 8.39  ? 120  HIS A N   1 
ATOM   876   C  CA  . HIS A  1 120 ? 34.913  98.326  75.790  1.00 8.70  ? 120  HIS A CA  1 
ATOM   877   C  C   . HIS A  1 120 ? 33.861  98.738  74.757  1.00 8.90  ? 120  HIS A C   1 
ATOM   878   O  O   . HIS A  1 120 ? 33.623  98.060  73.766  1.00 8.29  ? 120  HIS A O   1 
ATOM   879   C  CB  . HIS A  1 120 ? 36.163  99.197  75.528  1.00 8.51  ? 120  HIS A CB  1 
ATOM   880   C  CG  . HIS A  1 120 ? 37.037  99.355  76.722  1.00 8.38  ? 120  HIS A CG  1 
ATOM   881   N  ND1 . HIS A  1 120 ? 36.783  100.288 77.703  1.00 8.23  ? 120  HIS A ND1 1 
ATOM   882   C  CD2 . HIS A  1 120 ? 38.164  98.706  77.095  1.00 7.37  ? 120  HIS A CD2 1 
ATOM   883   C  CE1 . HIS A  1 120 ? 37.722  100.210 78.637  1.00 8.83  ? 120  HIS A CE1 1 
ATOM   884   N  NE2 . HIS A  1 120 ? 38.585  99.278  78.274  1.00 6.41  ? 120  HIS A NE2 1 
ATOM   885   N  N   . GLU A  1 121 ? 33.270  99.889  75.029  1.00 8.43  ? 121  GLU A N   1 
ATOM   886   C  CA  . GLU A  1 121 ? 32.234  100.508 74.242  1.00 10.01 ? 121  GLU A CA  1 
ATOM   887   C  C   . GLU A  1 121 ? 32.674  100.835 72.818  1.00 10.24 ? 121  GLU A C   1 
ATOM   888   O  O   . GLU A  1 121 ? 31.928  100.613 71.852  1.00 9.46  ? 121  GLU A O   1 
ATOM   889   C  CB  . GLU A  1 121 ? 31.867  101.807 74.973  1.00 9.86  ? 121  GLU A CB  1 
ATOM   890   C  CG  . GLU A  1 121 ? 30.884  102.729 74.275  1.00 14.57 ? 121  GLU A CG  1 
ATOM   891   C  CD  . GLU A  1 121 ? 30.870  104.159 74.854  1.00 19.06 ? 121  GLU A CD  1 
ATOM   892   O  OE1 . GLU A  1 121 ? 30.022  104.966 74.405  1.00 22.81 ? 121  GLU A OE1 1 
ATOM   893   O  OE2 . GLU A  1 121 ? 31.697  104.509 75.739  1.00 17.50 ? 121  GLU A OE2 1 
ATOM   894   N  N   . LYS A  1 122 ? 33.871  101.398 72.718  1.00 10.11 ? 122  LYS A N   1 
ATOM   895   C  CA  . LYS A  1 122 ? 34.419  101.906 71.446  1.00 11.47 ? 122  LYS A CA  1 
ATOM   896   C  C   . LYS A  1 122 ? 35.711  101.189 71.060  1.00 10.95 ? 122  LYS A C   1 
ATOM   897   O  O   . LYS A  1 122 ? 36.261  100.408 71.849  1.00 10.37 ? 122  LYS A O   1 
ATOM   898   C  CB  . LYS A  1 122 ? 34.741  103.400 71.565  1.00 12.38 ? 122  LYS A CB  1 
ATOM   899   C  CG  . LYS A  1 122 ? 33.605  104.284 72.043  1.00 17.21 ? 122  LYS A CG  1 
ATOM   900   C  CD  . LYS A  1 122 ? 34.084  105.727 72.144  1.00 22.63 ? 122  LYS A CD  1 
ATOM   901   C  CE  . LYS A  1 122 ? 33.090  106.594 72.889  1.00 27.51 ? 122  LYS A CE  1 
ATOM   902   N  NZ  . LYS A  1 122 ? 33.774  107.424 73.950  1.00 31.20 ? 122  LYS A NZ  1 
ATOM   903   N  N   . ALA A  1 123 ? 36.208  101.495 69.862  1.00 9.89  ? 123  ALA A N   1 
ATOM   904   C  CA  . ALA A  1 123 ? 37.449  100.913 69.405  1.00 9.09  ? 123  ALA A CA  1 
ATOM   905   C  C   . ALA A  1 123 ? 38.601  101.547 70.168  1.00 9.21  ? 123  ALA A C   1 
ATOM   906   O  O   . ALA A  1 123 ? 38.553  102.703 70.571  1.00 9.19  ? 123  ALA A O   1 
ATOM   907   C  CB  . ALA A  1 123 ? 37.637  101.158 67.897  1.00 10.53 ? 123  ALA A CB  1 
ATOM   908   N  N   . ASP A  1 124 ? 39.624  100.754 70.394  1.00 7.87  ? 124  ASP A N   1 
ATOM   909   C  CA  . ASP A  1 124 ? 40.866  101.249 70.958  1.00 8.31  ? 124  ASP A CA  1 
ATOM   910   C  C   . ASP A  1 124 ? 41.626  101.929 69.789  1.00 7.36  ? 124  ASP A C   1 
ATOM   911   O  O   . ASP A  1 124 ? 41.868  101.290 68.741  1.00 8.07  ? 124  ASP A O   1 
ATOM   912   C  CB  . ASP A  1 124 ? 41.603  100.016 71.506  1.00 7.05  ? 124  ASP A CB  1 
ATOM   913   C  CG  . ASP A  1 124 ? 42.898  100.347 72.187  1.00 9.61  ? 124  ASP A CG  1 
ATOM   914   O  OD1 . ASP A  1 124 ? 43.529  101.399 71.891  1.00 7.28  ? 124  ASP A OD1 1 
ATOM   915   O  OD2 . ASP A  1 124 ? 43.357  99.577  73.054  1.00 10.78 ? 124  ASP A OD2 1 
ATOM   916   N  N   . ASP A  1 125 ? 42.003  103.211 69.931  1.00 6.73  ? 125  ASP A N   1 
ATOM   917   C  CA  . ASP A  1 125 ? 42.780  103.875 68.850  1.00 6.39  ? 125  ASP A CA  1 
ATOM   918   C  C   . ASP A  1 125 ? 44.292  103.578 68.786  1.00 6.33  ? 125  ASP A C   1 
ATOM   919   O  O   . ASP A  1 125 ? 45.042  104.131 67.934  1.00 6.05  ? 125  ASP A O   1 
ATOM   920   C  CB  . ASP A  1 125 ? 42.487  105.382 68.807  1.00 5.25  ? 125  ASP A CB  1 
ATOM   921   C  CG  . ASP A  1 125 ? 43.030  106.132 69.999  1.00 8.14  ? 125  ASP A CG  1 
ATOM   922   O  OD1 . ASP A  1 125 ? 43.946  105.652 70.712  1.00 7.61  ? 125  ASP A OD1 1 
ATOM   923   O  OD2 . ASP A  1 125 ? 42.612  107.275 70.294  1.00 8.84  ? 125  ASP A OD2 1 
ATOM   924   N  N   . LEU A  1 126 ? 44.731  102.688 69.667  1.00 7.18  ? 126  LEU A N   1 
ATOM   925   C  CA  . LEU A  1 126 ? 46.104  102.185 69.671  1.00 7.34  ? 126  LEU A CA  1 
ATOM   926   C  C   . LEU A  1 126 ? 47.097  103.304 69.942  1.00 6.93  ? 126  LEU A C   1 
ATOM   927   O  O   . LEU A  1 126 ? 48.276  103.191 69.585  1.00 8.60  ? 126  LEU A O   1 
ATOM   928   C  CB  . LEU A  1 126 ? 46.404  101.416 68.379  1.00 7.69  ? 126  LEU A CB  1 
ATOM   929   C  CG  . LEU A  1 126 ? 45.290  100.440 67.953  1.00 10.03 ? 126  LEU A CG  1 
ATOM   930   C  CD1 . LEU A  1 126 ? 45.722  99.679  66.742  1.00 10.32 ? 126  LEU A CD1 1 
ATOM   931   C  CD2 . LEU A  1 126 ? 44.954  99.406  69.128  1.00 7.80  ? 126  LEU A CD2 1 
ATOM   932   N  N   . GLY A  1 127 ? 46.637  104.367 70.613  1.00 6.52  ? 127  GLY A N   1 
ATOM   933   C  CA  . GLY A  1 127 ? 47.523  105.474 70.954  1.00 6.02  ? 127  GLY A CA  1 
ATOM   934   C  C   . GLY A  1 127 ? 47.640  106.543 69.880  1.00 5.72  ? 127  GLY A C   1 
ATOM   935   O  O   . GLY A  1 127 ? 48.470  107.473 70.014  1.00 6.81  ? 127  GLY A O   1 
ATOM   936   N  N   . LYS A  1 128 ? 46.812  106.433 68.828  1.00 5.00  ? 128  LYS A N   1 
ATOM   937   C  CA  . LYS A  1 128 ? 46.898  107.319 67.676  1.00 6.12  ? 128  LYS A CA  1 
ATOM   938   C  C   . LYS A  1 128 ? 45.840  108.430 67.611  1.00 6.72  ? 128  LYS A C   1 
ATOM   939   O  O   . LYS A  1 128 ? 45.629  109.051 66.535  1.00 6.73  ? 128  LYS A O   1 
ATOM   940   C  CB  . LYS A  1 128 ? 46.826  106.485 66.384  1.00 5.66  ? 128  LYS A CB  1 
ATOM   941   C  CG  . LYS A  1 128 ? 47.982  105.462 66.275  1.00 10.93 ? 128  LYS A CG  1 
ATOM   942   C  CD  . LYS A  1 128 ? 47.792  104.498 65.049  1.00 16.02 ? 128  LYS A CD  1 
ATOM   943   C  CE  . LYS A  1 128 ? 47.852  105.197 63.696  1.00 20.99 ? 128  LYS A CE  1 
ATOM   944   N  NZ  . LYS A  1 128 ? 47.255  104.360 62.522  1.00 23.07 ? 128  LYS A NZ  1 
ATOM   945   N  N   . GLY A  1 129 ? 45.189  108.679 68.750  1.00 7.29  ? 129  GLY A N   1 
ATOM   946   C  CA  . GLY A  1 129 ? 44.089  109.630 68.791  1.00 8.41  ? 129  GLY A CA  1 
ATOM   947   C  C   . GLY A  1 129 ? 44.441  111.101 69.009  1.00 8.75  ? 129  GLY A C   1 
ATOM   948   O  O   . GLY A  1 129 ? 43.570  111.956 68.878  1.00 10.04 ? 129  GLY A O   1 
ATOM   949   N  N   . GLY A  1 130 ? 45.688  111.410 69.344  1.00 7.82  ? 130  GLY A N   1 
ATOM   950   C  CA  . GLY A  1 130 ? 46.081  112.819 69.392  1.00 7.36  ? 130  GLY A CA  1 
ATOM   951   C  C   . GLY A  1 130 ? 45.645  113.593 70.619  1.00 8.47  ? 130  GLY A C   1 
ATOM   952   O  O   . GLY A  1 130 ? 45.820  114.818 70.669  1.00 7.14  ? 130  GLY A O   1 
ATOM   953   N  N   . ASN A  1 131 ? 45.041  112.896 71.573  1.00 10.74 ? 131  ASN A N   1 
ATOM   954   C  CA  . ASN A  1 131 ? 44.705  113.499 72.869  1.00 11.77 ? 131  ASN A CA  1 
ATOM   955   C  C   . ASN A  1 131 ? 45.396  112.825 74.024  1.00 12.61 ? 131  ASN A C   1 
ATOM   956   O  O   . ASN A  1 131 ? 46.021  111.759 73.895  1.00 10.32 ? 131  ASN A O   1 
ATOM   957   C  CB  . ASN A  1 131 ? 43.181  113.606 73.089  1.00 11.97 ? 131  ASN A CB  1 
ATOM   958   C  CG  . ASN A  1 131 ? 42.485  112.246 73.170  1.00 13.24 ? 131  ASN A CG  1 
ATOM   959   O  OD1 . ASN A  1 131 ? 43.094  111.221 72.957  1.00 12.79 ? 131  ASN A OD1 1 
ATOM   960   N  ND2 . ASN A  1 131 ? 41.194  112.256 73.462  1.00 12.53 ? 131  ASN A ND2 1 
ATOM   961   N  N   . GLU A  1 132 ? 45.285  113.422 75.207  1.00 12.74 ? 132  GLU A N   1 
ATOM   962   C  CA  . GLU A  1 132 ? 45.916  112.829 76.339  1.00 13.83 ? 132  GLU A CA  1 
ATOM   963   C  C   . GLU A  1 132 ? 45.345  111.426 76.604  1.00 13.23 ? 132  GLU A C   1 
ATOM   964   O  O   . GLU A  1 132 ? 46.089  110.500 76.907  1.00 13.32 ? 132  GLU A O   1 
ATOM   965   C  CB  . GLU A  1 132 ? 45.757  113.772 77.571  1.00 14.63 ? 132  GLU A CB  1 
ATOM   966   C  CG  . GLU A  1 132 ? 45.718  115.250 77.146  1.00 17.96 ? 132  GLU A CG  1 
ATOM   967   C  CD  . GLU A  1 132 ? 45.530  116.260 78.291  1.00 21.50 ? 132  GLU A CD  1 
ATOM   968   O  OE1 . GLU A  1 132 ? 46.284  117.252 78.324  1.00 24.94 ? 132  GLU A OE1 1 
ATOM   969   O  OE2 . GLU A  1 132 ? 44.612  116.105 79.128  1.00 23.63 ? 132  GLU A OE2 1 
ATOM   970   N  N   . GLU A  1 133 ? 44.030  111.268 76.479  1.00 12.29 ? 133  GLU A N   1 
ATOM   971   C  CA  . GLU A  1 133 ? 43.391  109.981 76.735  1.00 12.61 ? 133  GLU A CA  1 
ATOM   972   C  C   . GLU A  1 133 ? 43.924  108.849 75.831  1.00 10.66 ? 133  GLU A C   1 
ATOM   973   O  O   . GLU A  1 133 ? 43.980  107.666 76.216  1.00 9.83  ? 133  GLU A O   1 
ATOM   974   C  CB  . GLU A  1 133 ? 41.900  110.143 76.478  1.00 12.85 ? 133  GLU A CB  1 
ATOM   975   C  CG  . GLU A  1 133 ? 41.056  109.038 77.062  1.00 15.00 ? 133  GLU A CG  1 
ATOM   976   C  CD  . GLU A  1 133 ? 41.228  108.896 78.572  1.00 18.31 ? 133  GLU A CD  1 
ATOM   977   O  OE1 . GLU A  1 133 ? 41.260  109.915 79.294  1.00 19.64 ? 133  GLU A OE1 1 
ATOM   978   O  OE2 . GLU A  1 133 ? 41.366  107.751 79.038  1.00 19.18 ? 133  GLU A OE2 1 
ATOM   979   N  N   . SER A  1 134 ? 44.353  109.206 74.637  1.00 10.28 ? 134  SER A N   1 
ATOM   980   C  CA  . SER A  1 134 ? 44.789  108.159 73.708  1.00 9.37  ? 134  SER A CA  1 
ATOM   981   C  C   . SER A  1 134 ? 45.956  107.350 74.270  1.00 10.49 ? 134  SER A C   1 
ATOM   982   O  O   . SER A  1 134 ? 46.035  106.133 74.063  1.00 9.92  ? 134  SER A O   1 
ATOM   983   C  CB  . SER A  1 134 ? 45.159  108.755 72.343  1.00 9.93  ? 134  SER A CB  1 
ATOM   984   O  OG  . SER A  1 134 ? 45.555  107.682 71.482  1.00 7.09  ? 134  SER A OG  1 
ATOM   985   N  N   . THR A  1 135 ? 46.879  108.026 74.960  1.00 11.28 ? 135  THR A N   1 
ATOM   986   C  CA  . THR A  1 135 ? 48.052  107.352 75.481  1.00 11.87 ? 135  THR A CA  1 
ATOM   987   C  C   . THR A  1 135 ? 47.810  106.736 76.860  1.00 11.48 ? 135  THR A C   1 
ATOM   988   O  O   . THR A  1 135 ? 48.752  106.267 77.496  1.00 10.64 ? 135  THR A O   1 
ATOM   989   C  CB  . THR A  1 135 ? 49.311  108.258 75.458  1.00 13.93 ? 135  THR A CB  1 
ATOM   990   O  OG1 . THR A  1 135 ? 48.980  109.545 75.941  1.00 17.36 ? 135  THR A OG1 1 
ATOM   991   C  CG2 . THR A  1 135 ? 49.710  108.600 74.012  1.00 15.60 ? 135  THR A CG2 1 
ATOM   992   N  N   . LYS A  1 136 ? 46.562  106.748 77.306  1.00 10.79 ? 136  LYS A N   1 
ATOM   993   C  CA  . LYS A  1 136 ? 46.153  106.077 78.532  1.00 11.00 ? 136  LYS A CA  1 
ATOM   994   C  C   . LYS A  1 136 ? 45.253  104.861 78.293  1.00 10.62 ? 136  LYS A C   1 
ATOM   995   O  O   . LYS A  1 136 ? 45.508  103.768 78.828  1.00 9.39  ? 136  LYS A O   1 
ATOM   996   C  CB  . LYS A  1 136 ? 45.386  107.049 79.442  1.00 12.77 ? 136  LYS A CB  1 
ATOM   997   C  CG  . LYS A  1 136 ? 46.151  108.280 79.891  1.00 16.55 ? 136  LYS A CG  1 
ATOM   998   C  CD  . LYS A  1 136 ? 45.228  109.117 80.774  1.00 23.69 ? 136  LYS A CD  1 
ATOM   999   C  CE  . LYS A  1 136 ? 45.874  110.381 81.328  1.00 27.70 ? 136  LYS A CE  1 
ATOM   1000  N  NZ  . LYS A  1 136 ? 44.772  111.315 81.773  1.00 29.76 ? 136  LYS A NZ  1 
ATOM   1001  N  N   . THR A  1 137 ? 44.187  105.055 77.520  1.00 10.62 ? 137  THR A N   1 
ATOM   1002  C  CA  . THR A  1 137 ? 43.175  104.030 77.314  1.00 10.39 ? 137  THR A CA  1 
ATOM   1003  C  C   . THR A  1 137 ? 42.844  103.765 75.853  1.00 10.23 ? 137  THR A C   1 
ATOM   1004  O  O   . THR A  1 137 ? 41.992  102.941 75.564  1.00 10.11 ? 137  THR A O   1 
ATOM   1005  C  CB  . THR A  1 137 ? 41.847  104.484 77.950  1.00 11.15 ? 137  THR A CB  1 
ATOM   1006  O  OG1 . THR A  1 137 ? 41.397  105.689 77.293  1.00 8.86  ? 137  THR A OG1 1 
ATOM   1007  C  CG2 . THR A  1 137 ? 42.008  104.886 79.446  1.00 14.03 ? 137  THR A CG2 1 
ATOM   1008  N  N   . GLY A  1 138 ? 43.485  104.476 74.927  1.00 8.78  ? 138  GLY A N   1 
ATOM   1009  C  CA  . GLY A  1 138 ? 43.088  104.371 73.533  1.00 8.65  ? 138  GLY A CA  1 
ATOM   1010  C  C   . GLY A  1 138 ? 41.720  104.968 73.221  1.00 8.76  ? 138  GLY A C   1 
ATOM   1011  O  O   . GLY A  1 138 ? 41.175  104.709 72.142  1.00 7.61  ? 138  GLY A O   1 
ATOM   1012  N  N   . ASN A  1 139 ? 41.150  105.769 74.144  1.00 8.96  ? 139  ASN A N   1 
ATOM   1013  C  CA  . ASN A  1 139 ? 39.797  106.350 73.967  1.00 9.93  ? 139  ASN A CA  1 
ATOM   1014  C  C   . ASN A  1 139 ? 38.729  105.279 73.781  1.00 10.63 ? 139  ASN A C   1 
ATOM   1015  O  O   . ASN A  1 139 ? 37.712  105.474 73.105  1.00 9.80  ? 139  ASN A O   1 
ATOM   1016  C  CB  . ASN A  1 139 ? 39.743  107.343 72.782  1.00 10.18 ? 139  ASN A CB  1 
ATOM   1017  C  CG  . ASN A  1 139 ? 40.508  108.645 73.079  1.00 12.12 ? 139  ASN A CG  1 
ATOM   1018  O  OD1 . ASN A  1 139 ? 40.067  109.454 73.916  1.00 10.53 ? 139  ASN A OD1 1 
ATOM   1019  N  ND2 . ASN A  1 139 ? 41.639  108.862 72.385  1.00 6.29  ? 139  ASN A ND2 1 
ATOM   1020  N  N   . ALA A  1 140 ? 38.962  104.126 74.374  1.00 9.96  ? 140  ALA A N   1 
ATOM   1021  C  CA  . ALA A  1 140 ? 38.031  103.030 74.163  1.00 10.09 ? 140  ALA A CA  1 
ATOM   1022  C  C   . ALA A  1 140 ? 36.726  103.213 74.945  1.00 9.80  ? 140  ALA A C   1 
ATOM   1023  O  O   . ALA A  1 140 ? 35.786  102.423 74.778  1.00 9.00  ? 140  ALA A O   1 
ATOM   1024  C  CB  . ALA A  1 140 ? 38.672  101.701 74.498  1.00 10.46 ? 140  ALA A CB  1 
ATOM   1025  N  N   . GLY A  1 141 ? 36.689  104.215 75.818  1.00 8.83  ? 141  GLY A N   1 
ATOM   1026  C  CA  . GLY A  1 141 ? 35.443  104.566 76.479  1.00 10.29 ? 141  GLY A CA  1 
ATOM   1027  C  C   . GLY A  1 141 ? 34.973  103.575 77.532  1.00 10.88 ? 141  GLY A C   1 
ATOM   1028  O  O   . GLY A  1 141 ? 35.775  102.924 78.196  1.00 9.86  ? 141  GLY A O   1 
ATOM   1029  N  N   . SER A  1 142 ? 33.659  103.471 77.700  1.00 10.46 ? 142  SER A N   1 
ATOM   1030  C  CA  . SER A  1 142 ? 33.138  102.720 78.832  1.00 11.03 ? 142  SER A CA  1 
ATOM   1031  C  C   . SER A  1 142 ? 33.432  101.238 78.837  1.00 11.65 ? 142  SER A C   1 
ATOM   1032  O  O   . SER A  1 142 ? 33.818  100.639 77.821  1.00 10.42 ? 142  SER A O   1 
ATOM   1033  C  CB  . SER A  1 142 ? 31.631  102.973 79.031  1.00 11.30 ? 142  SER A CB  1 
ATOM   1034  O  OG  . SER A  1 142 ? 30.910  102.199 78.100  1.00 13.99 ? 142  SER A OG  1 
ATOM   1035  N  N   . ARG A  1 143 ? 33.247  100.656 80.018  1.00 10.89 ? 143  ARG A N   1 
ATOM   1036  C  CA  . ARG A  1 143 ? 33.502  99.244  80.227  1.00 11.98 ? 143  ARG A CA  1 
ATOM   1037  C  C   . ARG A  1 143 ? 32.191  98.522  80.131  1.00 12.70 ? 143  ARG A C   1 
ATOM   1038  O  O   . ARG A  1 143 ? 31.347  98.624  81.034  1.00 13.34 ? 143  ARG A O   1 
ATOM   1039  C  CB  . ARG A  1 143 ? 34.166  99.049  81.588  1.00 12.30 ? 143  ARG A CB  1 
ATOM   1040  C  CG  . ARG A  1 143 ? 35.453  99.826  81.681  1.00 11.42 ? 143  ARG A CG  1 
ATOM   1041  C  CD  . ARG A  1 143 ? 36.075  99.903  83.104  1.00 9.96  ? 143  ARG A CD  1 
ATOM   1042  N  NE  . ARG A  1 143 ? 37.205  100.820 83.084  1.00 8.60  ? 143  ARG A NE  1 
ATOM   1043  C  CZ  . ARG A  1 143 ? 38.207  100.801 83.933  1.00 8.19  ? 143  ARG A CZ  1 
ATOM   1044  N  NH1 . ARG A  1 143 ? 38.229  99.905  84.909  1.00 10.86 ? 143  ARG A NH1 1 
ATOM   1045  N  NH2 . ARG A  1 143 ? 39.194  101.670 83.807  1.00 8.42  ? 143  ARG A NH2 1 
ATOM   1046  N  N   . LEU A  1 144 ? 31.994  97.796  79.032  1.00 11.89 ? 144  LEU A N   1 
ATOM   1047  C  CA  . LEU A  1 144 ? 30.712  97.131  78.797  1.00 12.30 ? 144  LEU A CA  1 
ATOM   1048  C  C   . LEU A  1 144 ? 30.544  95.861  79.585  1.00 11.80 ? 144  LEU A C   1 
ATOM   1049  O  O   . LEU A  1 144 ? 29.433  95.533  80.030  1.00 11.37 ? 144  LEU A O   1 
ATOM   1050  C  CB  . LEU A  1 144 ? 30.541  96.807  77.320  1.00 12.62 ? 144  LEU A CB  1 
ATOM   1051  C  CG  . LEU A  1 144 ? 30.486  98.015  76.382  1.00 13.75 ? 144  LEU A CG  1 
ATOM   1052  C  CD1 . LEU A  1 144 ? 30.399  97.510  74.935  1.00 14.17 ? 144  LEU A CD1 1 
ATOM   1053  C  CD2 . LEU A  1 144 ? 29.362  99.010  76.700  1.00 15.35 ? 144  LEU A CD2 1 
ATOM   1054  N  N   . ALA A  1 145 ? 31.636  95.124  79.731  1.00 11.00 ? 145  ALA A N   1 
ATOM   1055  C  CA  . ALA A  1 145 ? 31.629  93.869  80.487  1.00 10.77 ? 145  ALA A CA  1 
ATOM   1056  C  C   . ALA A  1 145 ? 33.033  93.538  80.917  1.00 10.15 ? 145  ALA A C   1 
ATOM   1057  O  O   . ALA A  1 145 ? 33.999  93.943  80.265  1.00 8.92  ? 145  ALA A O   1 
ATOM   1058  C  CB  . ALA A  1 145 ? 31.084  92.719  79.663  1.00 10.89 ? 145  ALA A CB  1 
ATOM   1059  N  N   . CYS A  1 146 ? 33.133  92.774  82.004  1.00 9.43  ? 146  CYS A N   1 
ATOM   1060  C  CA  . CYS A  1 146 ? 34.422  92.392  82.538  1.00 8.33  ? 146  CYS A CA  1 
ATOM   1061  C  C   . CYS A  1 146 ? 34.292  91.160  83.368  1.00 7.95  ? 146  CYS A C   1 
ATOM   1062  O  O   . CYS A  1 146 ? 33.156  90.733  83.719  1.00 9.37  ? 146  CYS A O   1 
ATOM   1063  C  CB  . CYS A  1 146 ? 35.024  93.538  83.378  1.00 9.41  ? 146  CYS A CB  1 
ATOM   1064  S  SG  . CYS A  1 146 ? 34.047  93.957  84.853  1.00 13.02 ? 146  CYS A SG  1 
ATOM   1065  N  N   . GLY A  1 147 ? 35.435  90.588  83.716  1.00 7.72  ? 147  GLY A N   1 
ATOM   1066  C  CA  . GLY A  1 147 ? 35.478  89.458  84.641  1.00 9.02  ? 147  GLY A CA  1 
ATOM   1067  C  C   . GLY A  1 147 ? 36.874  89.261  85.199  1.00 8.88  ? 147  GLY A C   1 
ATOM   1068  O  O   . GLY A  1 147 ? 37.898  89.731  84.632  1.00 8.96  ? 147  GLY A O   1 
ATOM   1069  N  N   . VAL A  1 148 ? 36.975  88.509  86.282  1.00 7.28  ? 148  VAL A N   1 
ATOM   1070  C  CA  . VAL A  1 148 ? 38.288  88.234  86.827  1.00 7.95  ? 148  VAL A CA  1 
ATOM   1071  C  C   . VAL A  1 148 ? 38.874  87.027  86.112  1.00 8.69  ? 148  VAL A C   1 
ATOM   1072  O  O   . VAL A  1 148 ? 38.152  86.077  85.833  1.00 10.00 ? 148  VAL A O   1 
ATOM   1073  C  CB  . VAL A  1 148 ? 38.191  87.995  88.335  1.00 8.74  ? 148  VAL A CB  1 
ATOM   1074  C  CG1 . VAL A  1 148 ? 39.555  87.702  88.898  1.00 9.49  ? 148  VAL A CG1 1 
ATOM   1075  C  CG2 . VAL A  1 148 ? 37.593  89.229  88.987  1.00 10.42 ? 148  VAL A CG2 1 
ATOM   1076  N  N   . ILE A  1 149 ? 40.163  87.055  85.788  1.00 7.90  ? 149  ILE A N   1 
ATOM   1077  C  CA  . ILE A  1 149 ? 40.785  85.962  85.054  1.00 8.81  ? 149  ILE A CA  1 
ATOM   1078  C  C   . ILE A  1 149 ? 41.149  84.884  86.062  1.00 9.46  ? 149  ILE A C   1 
ATOM   1079  O  O   . ILE A  1 149 ? 41.927  85.137  86.981  1.00 10.13 ? 149  ILE A O   1 
ATOM   1080  C  CB  . ILE A  1 149 ? 42.054  86.473  84.332  1.00 9.76  ? 149  ILE A CB  1 
ATOM   1081  C  CG1 . ILE A  1 149 ? 41.653  87.515  83.286  1.00 10.16 ? 149  ILE A CG1 1 
ATOM   1082  C  CG2 . ILE A  1 149 ? 42.842  85.307  83.715  1.00 8.28  ? 149  ILE A CG2 1 
ATOM   1083  C  CD1 . ILE A  1 149 ? 42.881  88.352  82.678  1.00 10.29 ? 149  ILE A CD1 1 
ATOM   1084  N  N   . GLY A  1 150 ? 40.571  83.698  85.890  1.00 9.47  ? 150  GLY A N   1 
ATOM   1085  C  CA  . GLY A  1 150 ? 40.755  82.609  86.849  1.00 10.29 ? 150  GLY A CA  1 
ATOM   1086  C  C   . GLY A  1 150 ? 41.498  81.378  86.334  1.00 10.94 ? 150  GLY A C   1 
ATOM   1087  O  O   . GLY A  1 150 ? 41.555  81.080  85.120  1.00 10.64 ? 150  GLY A O   1 
ATOM   1088  N  N   . ILE A  1 151 ? 42.100  80.656  87.270  1.00 10.30 ? 151  ILE A N   1 
ATOM   1089  C  CA  . ILE A  1 151 ? 42.798  79.421  86.935  1.00 10.74 ? 151  ILE A CA  1 
ATOM   1090  C  C   . ILE A  1 151 ? 41.782  78.405  86.398  1.00 11.66 ? 151  ILE A C   1 
ATOM   1091  O  O   . ILE A  1 151 ? 40.735  78.187  87.019  1.00 12.57 ? 151  ILE A O   1 
ATOM   1092  C  CB  . ILE A  1 151 ? 43.520  78.850  88.177  1.00 10.36 ? 151  ILE A CB  1 
ATOM   1093  C  CG1 . ILE A  1 151 ? 44.709  79.752  88.550  1.00 10.67 ? 151  ILE A CG1 1 
ATOM   1094  C  CG2 . ILE A  1 151 ? 43.953  77.384  87.890  1.00 8.90  ? 151  ILE A CG2 1 
ATOM   1095  C  CD1 . ILE A  1 151 ? 45.372  79.440  89.897  1.00 12.48 ? 151  ILE A CD1 1 
ATOM   1096  N  N   . ALA A  1 152 ? 42.096  77.778  85.264  1.00 11.64 ? 152  ALA A N   1 
ATOM   1097  C  CA  . ALA A  1 152 ? 41.185  76.805  84.636  1.00 12.89 ? 152  ALA A CA  1 
ATOM   1098  C  C   . ALA A  1 152 ? 41.723  75.387  84.745  1.00 13.76 ? 152  ALA A C   1 
ATOM   1099  O  O   . ALA A  1 152 ? 42.925  75.190  84.876  1.00 12.85 ? 152  ALA A O   1 
ATOM   1100  C  CB  . ALA A  1 152 ? 40.963  77.155  83.123  1.00 12.69 ? 152  ALA A CB  1 
ATOM   1101  N  N   . GLN A  1 153 ? 40.838  74.395  84.687  1.00 15.60 ? 153  GLN A N   1 
ATOM   1102  C  CA  . GLN A  1 153 ? 41.310  73.019  84.706  1.00 18.27 ? 153  GLN A CA  1 
ATOM   1103  C  C   . GLN A  1 153 ? 41.926  72.667  83.337  1.00 19.70 ? 153  GLN A C   1 
ATOM   1104  O  O   . GLN A  1 153 ? 41.315  72.943  82.275  1.00 19.19 ? 153  GLN A O   1 
ATOM   1105  C  CB  . GLN A  1 153 ? 40.193  72.049  85.066  1.00 18.77 ? 153  GLN A CB  1 
ATOM   1106  C  CG  . GLN A  1 153 ? 40.676  70.592  85.248  1.00 21.95 ? 153  GLN A CG  1 
ATOM   1107  C  CD  . GLN A  1 153 ? 39.564  69.659  85.688  1.00 25.51 ? 153  GLN A CD  1 
ATOM   1108  O  OE1 . GLN A  1 153 ? 38.398  69.855  85.329  1.00 26.99 ? 153  GLN A OE1 1 
ATOM   1109  N  NE2 . GLN A  1 153 ? 39.921  68.641  86.469  1.00 27.51 ? 153  GLN A NE2 1 
ATOM   1110  O  OXT . GLN A  1 153 ? 43.048  72.126  83.323  1.00 21.01 ? 153  GLN A OXT 1 
ATOM   1111  N  N   . ALA B  1 1   ? -8.209  100.173 20.406  1.00 19.54 ? 1    ALA B N   1 
ATOM   1112  C  CA  . ALA B  1 1   ? -6.923  99.529  19.913  1.00 19.27 ? 1    ALA B CA  1 
ATOM   1113  C  C   . ALA B  1 1   ? -6.065  99.020  21.053  1.00 17.87 ? 1    ALA B C   1 
ATOM   1114  O  O   . ALA B  1 1   ? -6.018  99.634  22.110  1.00 19.02 ? 1    ALA B O   1 
ATOM   1115  C  CB  . ALA B  1 1   ? -6.125  100.538 19.090  1.00 20.21 ? 1    ALA B CB  1 
ATOM   1116  N  N   . THR B  1 2   ? -5.357  97.913  20.844  1.00 16.02 ? 2    THR B N   1 
ATOM   1117  C  CA  . THR B  1 2   ? -4.525  97.360  21.899  1.00 14.45 ? 2    THR B CA  1 
ATOM   1118  C  C   . THR B  1 2   ? -3.292  96.708  21.295  1.00 11.55 ? 2    THR B C   1 
ATOM   1119  O  O   . THR B  1 2   ? -3.281  96.354  20.114  1.00 8.99  ? 2    THR B O   1 
ATOM   1120  C  CB  . THR B  1 2   ? -5.328  96.454  22.877  1.00 15.45 ? 2    THR B CB  1 
ATOM   1121  O  OG1 . THR B  1 2   ? -4.530  95.358  23.344  1.00 20.55 ? 2    THR B OG1 1 
ATOM   1122  C  CG2 . THR B  1 2   ? -6.461  95.773  22.172  1.00 18.87 ? 2    THR B CG2 1 
ATOM   1123  N  N   . LYS B  1 3   ? -2.247  96.631  22.109  1.00 8.75  ? 3    LYS B N   1 
ATOM   1124  C  CA  . LYS B  1 3   ? -0.964  96.164  21.653  1.00 7.28  ? 3    LYS B CA  1 
ATOM   1125  C  C   . LYS B  1 3   ? -0.455  95.217  22.715  1.00 5.97  ? 3    LYS B C   1 
ATOM   1126  O  O   . LYS B  1 3   ? -0.748  95.411  23.910  1.00 5.00  ? 3    LYS B O   1 
ATOM   1127  C  CB  . LYS B  1 3   ? 0.007   97.347  21.545  1.00 7.43  ? 3    LYS B CB  1 
ATOM   1128  C  CG  . LYS B  1 3   ? -0.391  98.362  20.447  1.00 12.32 ? 3    LYS B CG  1 
ATOM   1129  C  CD  . LYS B  1 3   ? 0.801   99.181  19.979  1.00 18.28 ? 3    LYS B CD  1 
ATOM   1130  C  CE  . LYS B  1 3   ? 0.351   100.169 18.881  1.00 22.67 ? 3    LYS B CE  1 
ATOM   1131  N  NZ  . LYS B  1 3   ? 1.377   101.252 18.632  1.00 25.32 ? 3    LYS B NZ  1 
ATOM   1132  N  N   . ALA B  1 4   ? 0.310   94.225  22.278  1.00 5.03  ? 4    ALA B N   1 
ATOM   1133  C  CA  . ALA B  1 4   ? 0.899   93.244  23.201  1.00 5.00  ? 4    ALA B CA  1 
ATOM   1134  C  C   . ALA B  1 4   ? 2.245   92.894  22.640  1.00 5.00  ? 4    ALA B C   1 
ATOM   1135  O  O   . ALA B  1 4   ? 2.557   93.258  21.507  1.00 5.00  ? 4    ALA B O   1 
ATOM   1136  C  CB  . ALA B  1 4   ? 0.048   92.005  23.305  1.00 5.00  ? 4    ALA B CB  1 
ATOM   1137  N  N   . VAL B  1 5   ? 3.068   92.238  23.446  1.00 5.00  ? 5    VAL B N   1 
ATOM   1138  C  CA  . VAL B  1 5   ? 4.409   91.912  22.982  1.00 5.00  ? 5    VAL B CA  1 
ATOM   1139  C  C   . VAL B  1 5   ? 4.853   90.633  23.696  1.00 5.00  ? 5    VAL B C   1 
ATOM   1140  O  O   . VAL B  1 5   ? 4.365   90.318  24.771  1.00 5.00  ? 5    VAL B O   1 
ATOM   1141  C  CB  . VAL B  1 5   ? 5.355   93.055  23.323  1.00 5.00  ? 5    VAL B CB  1 
ATOM   1142  C  CG1 . VAL B  1 5   ? 5.500   93.267  24.874  1.00 5.00  ? 5    VAL B CG1 1 
ATOM   1143  C  CG2 . VAL B  1 5   ? 6.744   92.923  22.589  1.00 5.00  ? 5    VAL B CG2 1 
ATOM   1144  N  N   . CYS B  1 6   ? 5.788   89.911  23.108  1.00 5.00  ? 6    CYS B N   1 
ATOM   1145  C  CA  . CYS B  1 6   ? 6.223   88.670  23.721  1.00 5.00  ? 6    CYS B CA  1 
ATOM   1146  C  C   . CYS B  1 6   ? 7.735   88.543  23.456  1.00 5.12  ? 6    CYS B C   1 
ATOM   1147  O  O   . CYS B  1 6   ? 8.157   88.700  22.313  1.00 5.21  ? 6    CYS B O   1 
ATOM   1148  C  CB  . CYS B  1 6   ? 5.487   87.530  23.044  1.00 5.00  ? 6    CYS B CB  1 
ATOM   1149  S  SG  . CYS B  1 6   ? 6.001   85.929  23.757  1.00 6.54  ? 6    CYS B SG  1 
ATOM   1150  N  N   . VAL B  1 7   ? 8.535   88.276  24.482  1.00 5.00  ? 7    VAL B N   1 
ATOM   1151  C  CA  . VAL B  1 7   ? 9.966   88.040  24.272  1.00 5.00  ? 7    VAL B CA  1 
ATOM   1152  C  C   . VAL B  1 7   ? 10.127  86.530  24.351  1.00 5.83  ? 7    VAL B C   1 
ATOM   1153  O  O   . VAL B  1 7   ? 9.804   85.939  25.378  1.00 5.00  ? 7    VAL B O   1 
ATOM   1154  C  CB  . VAL B  1 7   ? 10.768  88.670  25.376  1.00 5.00  ? 7    VAL B CB  1 
ATOM   1155  C  CG1 . VAL B  1 7   ? 12.302  88.284  25.216  1.00 8.27  ? 7    VAL B CG1 1 
ATOM   1156  C  CG2 . VAL B  1 7   ? 10.569  90.229  25.301  1.00 7.84  ? 7    VAL B CG2 1 
ATOM   1157  N  N   . LEU B  1 8   ? 10.612  85.920  23.273  1.00 5.00  ? 8    LEU B N   1 
ATOM   1158  C  CA  . LEU B  1 8   ? 10.778  84.476  23.234  1.00 5.21  ? 8    LEU B CA  1 
ATOM   1159  C  C   . LEU B  1 8   ? 12.199  84.117  23.648  1.00 5.00  ? 8    LEU B C   1 
ATOM   1160  O  O   . LEU B  1 8   ? 13.162  84.659  23.099  1.00 5.00  ? 8    LEU B O   1 
ATOM   1161  C  CB  . LEU B  1 8   ? 10.524  83.954  21.818  1.00 5.61  ? 8    LEU B CB  1 
ATOM   1162  C  CG  . LEU B  1 8   ? 9.118   84.139  21.204  1.00 8.04  ? 8    LEU B CG  1 
ATOM   1163  C  CD1 . LEU B  1 8   ? 9.216   83.990  19.635  1.00 15.14 ? 8    LEU B CD1 1 
ATOM   1164  C  CD2 . LEU B  1 8   ? 8.134   83.152  21.646  1.00 13.40 ? 8    LEU B CD2 1 
ATOM   1165  N  N   . LYS B  1 9   ? 12.313  83.230  24.620  1.00 5.00  ? 9    LYS B N   1 
ATOM   1166  C  CA  . LYS B  1 9   ? 13.639  82.742  25.044  1.00 7.02  ? 9    LYS B CA  1 
ATOM   1167  C  C   . LYS B  1 9   ? 13.536  81.234  25.306  1.00 6.05  ? 9    LYS B C   1 
ATOM   1168  O  O   . LYS B  1 9   ? 12.469  80.720  25.513  1.00 5.00  ? 9    LYS B O   1 
ATOM   1169  C  CB  . LYS B  1 9   ? 14.043  83.483  26.341  1.00 8.00  ? 9    LYS B CB  1 
ATOM   1170  C  CG  . LYS B  1 9   ? 14.508  84.907  26.117  1.00 14.08 ? 9    LYS B CG  1 
ATOM   1171  C  CD  . LYS B  1 9   ? 14.707  85.649  27.465  1.00 22.21 ? 9    LYS B CD  1 
ATOM   1172  C  CE  . LYS B  1 9   ? 15.631  86.871  27.337  1.00 27.22 ? 9    LYS B CE  1 
ATOM   1173  N  NZ  . LYS B  1 9   ? 15.787  87.397  25.953  1.00 29.37 ? 9    LYS B NZ  1 
ATOM   1174  N  N   . GLY B  1 10  ? 14.656  80.533  25.252  1.00 7.30  ? 10   GLY B N   1 
ATOM   1175  C  CA  . GLY B  1 10  ? 14.649  79.103  25.479  1.00 9.09  ? 10   GLY B CA  1 
ATOM   1176  C  C   . GLY B  1 10  ? 16.001  78.658  26.030  1.00 9.08  ? 10   GLY B C   1 
ATOM   1177  O  O   . GLY B  1 10  ? 16.786  79.462  26.527  1.00 8.62  ? 10   GLY B O   1 
ATOM   1178  N  N   . ASP B  1 11  ? 16.238  77.353  25.905  1.00 11.10 ? 11   ASP B N   1 
ATOM   1179  C  CA  . ASP B  1 11  ? 17.455  76.728  26.397  1.00 13.14 ? 11   ASP B CA  1 
ATOM   1180  C  C   . ASP B  1 11  ? 18.603  76.802  25.395  1.00 11.77 ? 11   ASP B C   1 
ATOM   1181  O  O   . ASP B  1 11  ? 19.736  76.584  25.772  1.00 13.49 ? 11   ASP B O   1 
ATOM   1182  C  CB  . ASP B  1 11  ? 17.191  75.245  26.673  1.00 15.60 ? 11   ASP B CB  1 
ATOM   1183  C  CG  . ASP B  1 11  ? 16.198  75.018  27.812  1.00 20.56 ? 11   ASP B CG  1 
ATOM   1184  O  OD1 . ASP B  1 11  ? 16.238  75.788  28.796  1.00 23.90 ? 11   ASP B OD1 1 
ATOM   1185  O  OD2 . ASP B  1 11  ? 15.371  74.064  27.807  1.00 27.62 ? 11   ASP B OD2 1 
ATOM   1186  N  N   . GLY B  1 12  ? 18.316  77.112  24.147  1.00 8.69  ? 12   GLY B N   1 
ATOM   1187  C  CA  . GLY B  1 12  ? 19.317  77.055  23.097  1.00 7.04  ? 12   GLY B CA  1 
ATOM   1188  C  C   . GLY B  1 12  ? 19.478  78.416  22.487  1.00 5.28  ? 12   GLY B C   1 
ATOM   1189  O  O   . GLY B  1 12  ? 19.374  79.405  23.170  1.00 5.00  ? 12   GLY B O   1 
ATOM   1190  N  N   . PRO B  1 13  ? 19.791  78.462  21.199  1.00 5.00  ? 13   PRO B N   1 
ATOM   1191  C  CA  . PRO B  1 13  ? 20.055  79.736  20.530  1.00 5.00  ? 13   PRO B CA  1 
ATOM   1192  C  C   . PRO B  1 13  ? 18.823  80.533  20.079  1.00 5.66  ? 13   PRO B C   1 
ATOM   1193  O  O   . PRO B  1 13  ? 19.011  81.646  19.548  1.00 5.00  ? 13   PRO B O   1 
ATOM   1194  C  CB  . PRO B  1 13  ? 20.820  79.292  19.284  1.00 5.00  ? 13   PRO B CB  1 
ATOM   1195  C  CG  . PRO B  1 13  ? 20.165  77.926  18.953  1.00 5.81  ? 13   PRO B CG  1 
ATOM   1196  C  CD  . PRO B  1 13  ? 19.900  77.307  20.281  1.00 5.31  ? 13   PRO B CD  1 
ATOM   1197  N  N   . VAL B  1 14  ? 17.622  79.983  20.218  1.00 5.00  ? 14   VAL B N   1 
ATOM   1198  C  CA  . VAL B  1 14  ? 16.450  80.657  19.657  1.00 5.00  ? 14   VAL B CA  1 
ATOM   1199  C  C   . VAL B  1 14  ? 16.008  81.777  20.542  1.00 5.00  ? 14   VAL B C   1 
ATOM   1200  O  O   . VAL B  1 14  ? 15.791  81.581  21.731  1.00 5.00  ? 14   VAL B O   1 
ATOM   1201  C  CB  . VAL B  1 14  ? 15.275  79.664  19.425  1.00 5.14  ? 14   VAL B CB  1 
ATOM   1202  C  CG1 . VAL B  1 14  ? 14.031  80.383  18.821  1.00 5.00  ? 14   VAL B CG1 1 
ATOM   1203  C  CG2 . VAL B  1 14  ? 15.759  78.525  18.490  1.00 5.00  ? 14   VAL B CG2 1 
ATOM   1204  N  N   . GLN B  1 15  ? 15.911  82.962  19.974  1.00 5.00  ? 15   GLN B N   1 
ATOM   1205  C  CA  . GLN B  1 15  ? 15.370  84.096  20.733  1.00 7.96  ? 15   GLN B CA  1 
ATOM   1206  C  C   . GLN B  1 15  ? 14.672  85.016  19.775  1.00 8.91  ? 15   GLN B C   1 
ATOM   1207  O  O   . GLN B  1 15  ? 15.071  85.123  18.598  1.00 7.64  ? 15   GLN B O   1 
ATOM   1208  C  CB  . GLN B  1 15  ? 16.386  84.897  21.563  1.00 9.68  ? 15   GLN B CB  1 
ATOM   1209  C  CG  . GLN B  1 15  ? 17.805  84.656  21.428  1.00 12.97 ? 15   GLN B CG  1 
ATOM   1210  C  CD  . GLN B  1 15  ? 18.620  85.699  22.256  1.00 20.84 ? 15   GLN B CD  1 
ATOM   1211  O  OE1 . GLN B  1 15  ? 19.015  86.722  21.723  1.00 21.47 ? 15   GLN B OE1 1 
ATOM   1212  N  NE2 . GLN B  1 15  ? 18.821  85.441  23.559  1.00 23.90 ? 15   GLN B NE2 1 
ATOM   1213  N  N   . GLY B  1 16  ? 13.646  85.679  20.278  1.00 7.87  ? 16   GLY B N   1 
ATOM   1214  C  CA  . GLY B  1 16  ? 12.921  86.606  19.413  1.00 8.45  ? 16   GLY B CA  1 
ATOM   1215  C  C   . GLY B  1 16  ? 12.050  87.577  20.172  1.00 6.87  ? 16   GLY B C   1 
ATOM   1216  O  O   . GLY B  1 16  ? 11.920  87.515  21.413  1.00 5.92  ? 16   GLY B O   1 
ATOM   1217  N  N   . ILE B  1 17  ? 11.450  88.479  19.406  1.00 6.34  ? 17   ILE B N   1 
ATOM   1218  C  CA  . ILE B  1 17  ? 10.511  89.449  19.926  1.00 5.77  ? 17   ILE B CA  1 
ATOM   1219  C  C   . ILE B  1 17  ? 9.380   89.473  18.928  1.00 5.90  ? 17   ILE B C   1 
ATOM   1220  O  O   . ILE B  1 17  ? 9.592   89.623  17.686  1.00 5.26  ? 17   ILE B O   1 
ATOM   1221  C  CB  . ILE B  1 17  ? 11.135  90.855  20.021  1.00 6.27  ? 17   ILE B CB  1 
ATOM   1222  C  CG1 . ILE B  1 17  ? 12.176  90.912  21.145  1.00 8.43  ? 17   ILE B CG1 1 
ATOM   1223  C  CG2 . ILE B  1 17  ? 10.040  91.868  20.350  1.00 7.25  ? 17   ILE B CG2 1 
ATOM   1224  C  CD1 . ILE B  1 17  ? 13.021  92.252  21.211  1.00 11.92 ? 17   ILE B CD1 1 
ATOM   1225  N  N   . ILE B  1 18  ? 8.171   89.316  19.448  1.00 5.00  ? 18   ILE B N   1 
ATOM   1226  C  CA  . ILE B  1 18  ? 6.973   89.321  18.604  1.00 5.00  ? 18   ILE B CA  1 
ATOM   1227  C  C   . ILE B  1 18  ? 5.981   90.321  19.140  1.00 5.00  ? 18   ILE B C   1 
ATOM   1228  O  O   . ILE B  1 18  ? 5.662   90.306  20.344  1.00 5.00  ? 18   ILE B O   1 
ATOM   1229  C  CB  . ILE B  1 18  ? 6.308   87.923  18.557  1.00 5.00  ? 18   ILE B CB  1 
ATOM   1230  C  CG1 . ILE B  1 18  ? 7.248   86.860  17.933  1.00 5.00  ? 18   ILE B CG1 1 
ATOM   1231  C  CG2 . ILE B  1 18  ? 4.926   87.956  17.773  1.00 5.00  ? 18   ILE B CG2 1 
ATOM   1232  C  CD1 . ILE B  1 18  ? 7.488   87.052  16.401  1.00 5.00  ? 18   ILE B CD1 1 
ATOM   1233  N  N   . ASN B  1 19  ? 5.466   91.176  18.240  1.00 5.00  ? 19   ASN B N   1 
ATOM   1234  C  CA  . ASN B  1 19  ? 4.530   92.249  18.598  1.00 5.20  ? 19   ASN B CA  1 
ATOM   1235  C  C   . ASN B  1 19  ? 3.140   91.866  18.115  1.00 5.68  ? 19   ASN B C   1 
ATOM   1236  O  O   . ASN B  1 19  ? 3.023   91.101  17.143  1.00 5.29  ? 19   ASN B O   1 
ATOM   1237  C  CB  . ASN B  1 19  ? 4.949   93.534  17.858  1.00 5.00  ? 19   ASN B CB  1 
ATOM   1238  C  CG  . ASN B  1 19  ? 6.386   93.909  18.144  1.00 8.05  ? 19   ASN B CG  1 
ATOM   1239  O  OD1 . ASN B  1 19  ? 7.287   93.759  17.282  1.00 10.94 ? 19   ASN B OD1 1 
ATOM   1240  N  ND2 . ASN B  1 19  ? 6.624   94.370  19.331  1.00 5.00  ? 19   ASN B ND2 1 
ATOM   1241  N  N   . PHE B  1 20  ? 2.113   92.325  18.835  1.00 5.00  ? 20   PHE B N   1 
ATOM   1242  C  CA  . PHE B  1 20  ? 0.727   92.110  18.452  1.00 5.00  ? 20   PHE B CA  1 
ATOM   1243  C  C   . PHE B  1 20  ? 0.031   93.415  18.454  1.00 5.69  ? 20   PHE B C   1 
ATOM   1244  O  O   . PHE B  1 20  ? 0.201   94.195  19.399  1.00 6.24  ? 20   PHE B O   1 
ATOM   1245  C  CB  . PHE B  1 20  ? -0.017  91.219  19.481  1.00 5.00  ? 20   PHE B CB  1 
ATOM   1246  C  CG  . PHE B  1 20  ? 0.614   89.866  19.668  1.00 5.07  ? 20   PHE B CG  1 
ATOM   1247  C  CD1 . PHE B  1 20  ? 1.751   89.710  20.448  1.00 5.00  ? 20   PHE B CD1 1 
ATOM   1248  C  CD2 . PHE B  1 20  ? 0.044   88.751  19.082  1.00 7.35  ? 20   PHE B CD2 1 
ATOM   1249  C  CE1 . PHE B  1 20  ? 2.337   88.422  20.624  1.00 7.43  ? 20   PHE B CE1 1 
ATOM   1250  C  CE2 . PHE B  1 20  ? 0.610   87.483  19.266  1.00 7.34  ? 20   PHE B CE2 1 
ATOM   1251  C  CZ  . PHE B  1 20  ? 1.748   87.321  20.044  1.00 9.24  ? 20   PHE B CZ  1 
ATOM   1252  N  N   . GLU B  1 21  ? -0.786  93.657  17.424  1.00 6.63  ? 21   GLU B N   1 
ATOM   1253  C  CA  . GLU B  1 21  ? -1.568  94.884  17.433  1.00 8.29  ? 21   GLU B CA  1 
ATOM   1254  C  C   . GLU B  1 21  ? -2.967  94.621  16.909  1.00 7.85  ? 21   GLU B C   1 
ATOM   1255  O  O   . GLU B  1 21  ? -3.134  93.928  15.899  1.00 7.38  ? 21   GLU B O   1 
ATOM   1256  C  CB  . GLU B  1 21  ? -0.910  95.978  16.587  1.00 9.20  ? 21   GLU B CB  1 
ATOM   1257  C  CG  . GLU B  1 21  ? -1.753  97.250  16.681  1.00 12.94 ? 21   GLU B CG  1 
ATOM   1258  C  CD  . GLU B  1 21  ? -1.193  98.418  15.907  1.00 21.69 ? 21   GLU B CD  1 
ATOM   1259  O  OE1 . GLU B  1 21  ? -0.478  98.192  14.902  1.00 27.75 ? 21   GLU B OE1 1 
ATOM   1260  O  OE2 . GLU B  1 21  ? -1.518  99.569  16.289  1.00 27.81 ? 21   GLU B OE2 1 
ATOM   1261  N  N   . GLN B  1 22  ? -3.966  95.153  17.606  1.00 7.48  ? 22   GLN B N   1 
ATOM   1262  C  CA  . GLN B  1 22  ? -5.350  94.962  17.215  1.00 9.17  ? 22   GLN B CA  1 
ATOM   1263  C  C   . GLN B  1 22  ? -6.055  96.308  17.214  1.00 11.14 ? 22   GLN B C   1 
ATOM   1264  O  O   . GLN B  1 22  ? -6.162  96.963  18.234  1.00 10.74 ? 22   GLN B O   1 
ATOM   1265  C  CB  . GLN B  1 22  ? -6.054  93.986  18.151  1.00 9.06  ? 22   GLN B CB  1 
ATOM   1266  C  CG  . GLN B  1 22  ? -7.428  93.536  17.680  1.00 8.51  ? 22   GLN B CG  1 
ATOM   1267  C  CD  . GLN B  1 22  ? -8.108  92.578  18.647  1.00 9.86  ? 22   GLN B CD  1 
ATOM   1268  O  OE1 . GLN B  1 22  ? -7.882  92.638  19.851  1.00 11.10 ? 22   GLN B OE1 1 
ATOM   1269  N  NE2 . GLN B  1 22  ? -8.941  91.701  18.127  1.00 9.20  ? 22   GLN B NE2 1 
ATOM   1270  N  N   . LYS B  1 23  ? -6.489  96.713  16.036  1.00 13.35 ? 23   LYS B N   1 
ATOM   1271  C  CA  . LYS B  1 23  ? -7.094  98.027  15.844  1.00 17.07 ? 23   LYS B CA  1 
ATOM   1272  C  C   . LYS B  1 23  ? -8.514  98.129  16.377  1.00 17.81 ? 23   LYS B C   1 
ATOM   1273  O  O   . LYS B  1 23  ? -8.897  99.154  16.937  1.00 18.06 ? 23   LYS B O   1 
ATOM   1274  C  CB  . LYS B  1 23  ? -7.077  98.371  14.357  1.00 17.31 ? 23   LYS B CB  1 
ATOM   1275  C  CG  . LYS B  1 23  ? -5.713  98.802  13.854  1.00 20.93 ? 23   LYS B CG  1 
ATOM   1276  C  CD  . LYS B  1 23  ? -5.761  99.157  12.378  1.00 27.05 ? 23   LYS B CD  1 
ATOM   1277  C  CE  . LYS B  1 23  ? -4.900  100.382 12.094  1.00 29.96 ? 23   LYS B CE  1 
ATOM   1278  N  NZ  . LYS B  1 23  ? -3.609  100.326 12.851  1.00 30.70 ? 23   LYS B NZ  1 
ATOM   1279  N  N   . GLU B  1 24  ? -9.288  97.061  16.213  1.00 19.35 ? 24   GLU B N   1 
ATOM   1280  C  CA  . GLU B  1 24  ? -10.711 97.080  16.565  1.00 21.65 ? 24   GLU B CA  1 
ATOM   1281  C  C   . GLU B  1 24  ? -11.106 95.870  17.383  1.00 22.11 ? 24   GLU B C   1 
ATOM   1282  O  O   . GLU B  1 24  ? -10.613 94.768  17.150  1.00 21.68 ? 24   GLU B O   1 
ATOM   1283  C  CB  . GLU B  1 24  ? -11.572 97.014  15.287  1.00 21.90 ? 24   GLU B CB  1 
ATOM   1284  C  CG  . GLU B  1 24  ? -11.683 98.277  14.447  1.00 26.13 ? 24   GLU B CG  1 
ATOM   1285  C  CD  . GLU B  1 24  ? -12.628 98.093  13.258  1.00 28.98 ? 24   GLU B CD  1 
ATOM   1286  O  OE1 . GLU B  1 24  ? -13.371 97.078  13.228  1.00 29.81 ? 24   GLU B OE1 1 
ATOM   1287  O  OE2 . GLU B  1 24  ? -12.639 98.960  12.353  1.00 33.30 ? 24   GLU B OE2 1 
ATOM   1288  N  N   . SER B  1 25  ? -12.033 96.072  18.309  1.00 22.93 ? 25   SER B N   1 
ATOM   1289  C  CA  . SER B  1 25  ? -12.602 94.966  19.059  1.00 23.66 ? 25   SER B CA  1 
ATOM   1290  C  C   . SER B  1 25  ? -12.968 93.828  18.097  1.00 23.51 ? 25   SER B C   1 
ATOM   1291  O  O   . SER B  1 25  ? -13.641 94.043  17.081  1.00 23.23 ? 25   SER B O   1 
ATOM   1292  C  CB  . SER B  1 25  ? -13.858 95.433  19.797  1.00 24.21 ? 25   SER B CB  1 
ATOM   1293  O  OG  . SER B  1 25  ? -14.219 94.502  20.806  1.00 26.62 ? 25   SER B OG  1 
ATOM   1294  N  N   . ASN B  1 26  ? -12.498 92.625  18.407  1.00 22.85 ? 26   ASN B N   1 
ATOM   1295  C  CA  . ASN B  1 26  ? -12.773 91.437  17.595  1.00 22.97 ? 26   ASN B CA  1 
ATOM   1296  C  C   . ASN B  1 26  ? -12.234 91.572  16.156  1.00 21.07 ? 26   ASN B C   1 
ATOM   1297  O  O   . ASN B  1 26  ? -12.520 90.747  15.301  1.00 21.32 ? 26   ASN B O   1 
ATOM   1298  C  CB  . ASN B  1 26  ? -14.284 91.124  17.621  1.00 24.39 ? 26   ASN B CB  1 
ATOM   1299  C  CG  . ASN B  1 26  ? -14.600 89.639  17.893  1.00 28.62 ? 26   ASN B CG  1 
ATOM   1300  O  OD1 . ASN B  1 26  ? -15.757 89.289  18.211  1.00 32.07 ? 26   ASN B OD1 1 
ATOM   1301  N  ND2 . ASN B  1 26  ? -13.593 88.762  17.749  1.00 32.07 ? 26   ASN B ND2 1 
ATOM   1302  N  N   . GLY B  1 27  ? -11.450 92.617  15.891  1.00 19.05 ? 27   GLY B N   1 
ATOM   1303  C  CA  . GLY B  1 27  ? -10.850 92.802  14.577  1.00 16.42 ? 27   GLY B CA  1 
ATOM   1304  C  C   . GLY B  1 27  ? -9.577  91.981  14.427  1.00 14.64 ? 27   GLY B C   1 
ATOM   1305  O  O   . GLY B  1 27  ? -9.129  91.350  15.384  1.00 13.70 ? 27   GLY B O   1 
ATOM   1306  N  N   . PRO B  1 28  ? -8.982  91.975  13.237  1.00 13.37 ? 28   PRO B N   1 
ATOM   1307  C  CA  . PRO B  1 28  ? -7.760  91.198  13.010  1.00 12.49 ? 28   PRO B CA  1 
ATOM   1308  C  C   . PRO B  1 28  ? -6.619  91.692  13.891  1.00 10.79 ? 28   PRO B C   1 
ATOM   1309  O  O   . PRO B  1 28  ? -6.539  92.892  14.224  1.00 9.33  ? 28   PRO B O   1 
ATOM   1310  C  CB  . PRO B  1 28  ? -7.428  91.473  11.543  1.00 12.87 ? 28   PRO B CB  1 
ATOM   1311  C  CG  . PRO B  1 28  ? -8.716  91.965  10.947  1.00 14.40 ? 28   PRO B CG  1 
ATOM   1312  C  CD  . PRO B  1 28  ? -9.433  92.695  12.030  1.00 14.62 ? 28   PRO B CD  1 
ATOM   1313  N  N   . VAL B  1 29  ? -5.753  90.746  14.241  1.00 8.49  ? 29   VAL B N   1 
ATOM   1314  C  CA  . VAL B  1 29  ? -4.583  91.007  15.031  1.00 6.71  ? 29   VAL B CA  1 
ATOM   1315  C  C   . VAL B  1 29  ? -3.390  90.851  14.115  1.00 6.87  ? 29   VAL B C   1 
ATOM   1316  O  O   . VAL B  1 29  ? -3.253  89.851  13.416  1.00 7.14  ? 29   VAL B O   1 
ATOM   1317  C  CB  . VAL B  1 29  ? -4.474  89.999  16.209  1.00 7.65  ? 29   VAL B CB  1 
ATOM   1318  C  CG1 . VAL B  1 29  ? -3.205  90.287  17.074  1.00 5.46  ? 29   VAL B CG1 1 
ATOM   1319  C  CG2 . VAL B  1 29  ? -5.788  89.973  17.033  1.00 6.01  ? 29   VAL B CG2 1 
ATOM   1320  N  N   . LYS B  1 30  ? -2.536  91.845  14.101  1.00 7.02  ? 30   LYS B N   1 
ATOM   1321  C  CA  . LYS B  1 30  ? -1.323  91.736  13.313  1.00 7.92  ? 30   LYS B CA  1 
ATOM   1322  C  C   . LYS B  1 30  ? -0.273  91.193  14.240  1.00 7.38  ? 30   LYS B C   1 
ATOM   1323  O  O   . LYS B  1 30  ? -0.139  91.678  15.341  1.00 7.11  ? 30   LYS B O   1 
ATOM   1324  C  CB  . LYS B  1 30  ? -0.863  93.109  12.847  1.00 8.45  ? 30   LYS B CB  1 
ATOM   1325  C  CG  . LYS B  1 30  ? -1.757  93.681  11.787  1.00 15.22 ? 30   LYS B CG  1 
ATOM   1326  C  CD  . LYS B  1 30  ? -1.153  94.980  11.208  1.00 21.69 ? 30   LYS B CD  1 
ATOM   1327  C  CE  . LYS B  1 30  ? -2.195  95.810  10.473  1.00 26.35 ? 30   LYS B CE  1 
ATOM   1328  N  NZ  . LYS B  1 30  ? -1.573  97.085  10.031  1.00 28.65 ? 30   LYS B NZ  1 
ATOM   1329  N  N   . VAL B  1 31  ? 0.434   90.163  13.800  1.00 7.35  ? 31   VAL B N   1 
ATOM   1330  C  CA  . VAL B  1 31  ? 1.494   89.602  14.610  1.00 7.32  ? 31   VAL B CA  1 
ATOM   1331  C  C   . VAL B  1 31  ? 2.794   89.631  13.837  1.00 7.70  ? 31   VAL B C   1 
ATOM   1332  O  O   . VAL B  1 31  ? 2.882   89.094  12.725  1.00 6.10  ? 31   VAL B O   1 
ATOM   1333  C  CB  . VAL B  1 31  ? 1.107   88.277  15.398  1.00 10.39 ? 31   VAL B CB  1 
ATOM   1334  C  CG1 . VAL B  1 31  ? -0.320  87.806  15.247  1.00 8.54  ? 31   VAL B CG1 1 
ATOM   1335  C  CG2 . VAL B  1 31  ? 2.269   87.280  15.725  1.00 5.81  ? 31   VAL B CG2 1 
ATOM   1336  N  N   . TRP B  1 32  ? 3.775   90.344  14.378  1.00 5.90  ? 32   TRP B N   1 
ATOM   1337  C  CA  . TRP B  1 32  ? 4.997   90.532  13.618  1.00 6.93  ? 32   TRP B CA  1 
ATOM   1338  C  C   . TRP B  1 32  ? 6.201   90.726  14.488  1.00 6.46  ? 32   TRP B C   1 
ATOM   1339  O  O   . TRP B  1 32  ? 6.121   91.246  15.597  1.00 5.12  ? 32   TRP B O   1 
ATOM   1340  C  CB  . TRP B  1 32  ? 4.889   91.726  12.650  1.00 6.80  ? 32   TRP B CB  1 
ATOM   1341  C  CG  . TRP B  1 32  ? 5.117   93.077  13.353  1.00 8.25  ? 32   TRP B CG  1 
ATOM   1342  C  CD1 . TRP B  1 32  ? 6.268   93.846  13.357  1.00 10.48 ? 32   TRP B CD1 1 
ATOM   1343  C  CD2 . TRP B  1 32  ? 4.170   93.783  14.127  1.00 10.43 ? 32   TRP B CD2 1 
ATOM   1344  N  NE1 . TRP B  1 32  ? 6.056   95.001  14.074  1.00 12.28 ? 32   TRP B NE1 1 
ATOM   1345  C  CE2 . TRP B  1 32  ? 4.777   94.981  14.565  1.00 9.98  ? 32   TRP B CE2 1 
ATOM   1346  C  CE3 . TRP B  1 32  ? 2.839   93.545  14.470  1.00 13.50 ? 32   TRP B CE3 1 
ATOM   1347  C  CZ2 . TRP B  1 32  ? 4.109   95.918  15.343  1.00 15.20 ? 32   TRP B CZ2 1 
ATOM   1348  C  CZ3 . TRP B  1 32  ? 2.185   94.461  15.267  1.00 14.55 ? 32   TRP B CZ3 1 
ATOM   1349  C  CH2 . TRP B  1 32  ? 2.813   95.645  15.685  1.00 14.69 ? 32   TRP B CH2 1 
ATOM   1350  N  N   . GLY B  1 33  ? 7.341   90.350  13.945  1.00 6.62  ? 33   GLY B N   1 
ATOM   1351  C  CA  . GLY B  1 33  ? 8.575   90.463  14.673  1.00 6.85  ? 33   GLY B CA  1 
ATOM   1352  C  C   . GLY B  1 33  ? 9.629   89.627  13.992  1.00 6.80  ? 33   GLY B C   1 
ATOM   1353  O  O   . GLY B  1 33  ? 9.588   89.377  12.785  1.00 7.21  ? 33   GLY B O   1 
ATOM   1354  N  N   . SER B  1 34  ? 10.592  89.218  14.786  1.00 7.20  ? 34   SER B N   1 
ATOM   1355  C  CA  . SER B  1 34  ? 11.734  88.503  14.280  1.00 7.92  ? 34   SER B CA  1 
ATOM   1356  C  C   . SER B  1 34  ? 12.150  87.478  15.310  1.00 7.63  ? 34   SER B C   1 
ATOM   1357  O  O   . SER B  1 34  ? 12.162  87.762  16.516  1.00 7.58  ? 34   SER B O   1 
ATOM   1358  C  CB  . SER B  1 34  ? 12.894  89.497  14.131  1.00 9.04  ? 34   SER B CB  1 
ATOM   1359  O  OG  . SER B  1 34  ? 13.961  88.890  13.435  1.00 13.93 ? 34   SER B OG  1 
ATOM   1360  N  N   . ILE B  1 35  ? 12.543  86.314  14.830  1.00 5.82  ? 35   ILE B N   1 
ATOM   1361  C  CA  . ILE B  1 35  ? 13.074  85.290  15.712  1.00 5.27  ? 35   ILE B CA  1 
ATOM   1362  C  C   . ILE B  1 35  ? 14.400  84.840  15.102  1.00 5.00  ? 35   ILE B C   1 
ATOM   1363  O  O   . ILE B  1 35  ? 14.473  84.605  13.883  1.00 5.61  ? 35   ILE B O   1 
ATOM   1364  C  CB  . ILE B  1 35  ? 12.120  84.113  15.768  1.00 5.00  ? 35   ILE B CB  1 
ATOM   1365  C  CG1 . ILE B  1 35  ? 10.708  84.602  16.177  1.00 5.58  ? 35   ILE B CG1 1 
ATOM   1366  C  CG2 . ILE B  1 35  ? 12.696  83.042  16.754  1.00 5.00  ? 35   ILE B CG2 1 
ATOM   1367  C  CD1 . ILE B  1 35  ? 9.629   83.423  16.224  1.00 5.98  ? 35   ILE B CD1 1 
ATOM   1368  N  N   . LYS B  1 36  ? 15.445  84.701  15.915  1.00 5.12  ? 36   LYS B N   1 
ATOM   1369  C  CA  . LYS B  1 36  ? 16.713  84.261  15.345  1.00 6.16  ? 36   LYS B CA  1 
ATOM   1370  C  C   . LYS B  1 36  ? 17.182  82.974  16.009  1.00 5.00  ? 36   LYS B C   1 
ATOM   1371  O  O   . LYS B  1 36  ? 16.613  82.533  16.991  1.00 5.00  ? 36   LYS B O   1 
ATOM   1372  C  CB  . LYS B  1 36  ? 17.790  85.347  15.506  1.00 7.15  ? 36   LYS B CB  1 
ATOM   1373  C  CG  . LYS B  1 36  ? 18.055  85.746  16.934  1.00 10.70 ? 36   LYS B CG  1 
ATOM   1374  C  CD  . LYS B  1 36  ? 19.140  86.864  16.929  1.00 17.55 ? 36   LYS B CD  1 
ATOM   1375  C  CE  . LYS B  1 36  ? 19.230  87.637  18.242  1.00 21.67 ? 36   LYS B CE  1 
ATOM   1376  N  NZ  . LYS B  1 36  ? 20.485  88.538  18.279  1.00 23.07 ? 36   LYS B NZ  1 
ATOM   1377  N  N   . GLY B  1 37  ? 18.212  82.366  15.421  1.00 5.00  ? 37   GLY B N   1 
ATOM   1378  C  CA  . GLY B  1 37  ? 18.787  81.167  15.977  1.00 5.44  ? 37   GLY B CA  1 
ATOM   1379  C  C   . GLY B  1 37  ? 18.071  79.917  15.521  1.00 5.00  ? 37   GLY B C   1 
ATOM   1380  O  O   . GLY B  1 37  ? 18.332  78.841  16.041  1.00 5.25  ? 37   GLY B O   1 
ATOM   1381  N  N   . LEU B  1 38  ? 17.181  80.023  14.530  1.00 5.64  ? 38   LEU B N   1 
ATOM   1382  C  CA  . LEU B  1 38  ? 16.437  78.841  14.095  1.00 5.79  ? 38   LEU B CA  1 
ATOM   1383  C  C   . LEU B  1 38  ? 17.134  78.072  12.952  1.00 6.78  ? 38   LEU B C   1 
ATOM   1384  O  O   . LEU B  1 38  ? 17.876  78.662  12.190  1.00 8.01  ? 38   LEU B O   1 
ATOM   1385  C  CB  . LEU B  1 38  ? 15.065  79.288  13.567  1.00 5.00  ? 38   LEU B CB  1 
ATOM   1386  C  CG  . LEU B  1 38  ? 14.065  79.810  14.619  1.00 5.06  ? 38   LEU B CG  1 
ATOM   1387  C  CD1 . LEU B  1 38  ? 12.974  80.664  13.980  1.00 5.61  ? 38   LEU B CD1 1 
ATOM   1388  C  CD2 . LEU B  1 38  ? 13.451  78.631  15.370  1.00 5.00  ? 38   LEU B CD2 1 
ATOM   1389  N  N   . THR B  1 39  ? 16.834  76.792  12.788  1.00 7.32  ? 39   THR B N   1 
ATOM   1390  C  CA  . THR B  1 39  ? 17.274  76.073  11.585  1.00 7.53  ? 39   THR B CA  1 
ATOM   1391  C  C   . THR B  1 39  ? 16.455  76.565  10.409  1.00 8.15  ? 39   THR B C   1 
ATOM   1392  O  O   . THR B  1 39  ? 15.251  76.834  10.529  1.00 7.11  ? 39   THR B O   1 
ATOM   1393  C  CB  . THR B  1 39  ? 17.105  74.548  11.701  1.00 8.13  ? 39   THR B CB  1 
ATOM   1394  O  OG1 . THR B  1 39  ? 15.747  74.249  12.070  1.00 5.16  ? 39   THR B OG1 1 
ATOM   1395  C  CG2 . THR B  1 39  ? 17.972  73.954  12.830  1.00 8.47  ? 39   THR B CG2 1 
ATOM   1396  N  N   . GLU B  1 40  ? 17.099  76.628  9.246   1.00 7.51  ? 40   GLU B N   1 
ATOM   1397  C  CA  . GLU B  1 40  ? 16.420  77.085  8.019   1.00 7.95  ? 40   GLU B CA  1 
ATOM   1398  C  C   . GLU B  1 40  ? 15.191  76.242  7.750   1.00 7.48  ? 40   GLU B C   1 
ATOM   1399  O  O   . GLU B  1 40  ? 15.245  75.037  7.855   1.00 7.21  ? 40   GLU B O   1 
ATOM   1400  C  CB  . GLU B  1 40  ? 17.391  77.030  6.810   1.00 9.04  ? 40   GLU B CB  1 
ATOM   1401  C  CG  . GLU B  1 40  ? 16.811  77.572  5.503   1.00 11.63 ? 40   GLU B CG  1 
ATOM   1402  C  CD  . GLU B  1 40  ? 17.763  77.428  4.302   1.00 18.48 ? 40   GLU B CD  1 
ATOM   1403  O  OE1 . GLU B  1 40  ? 18.849  76.807  4.451   1.00 17.72 ? 40   GLU B OE1 1 
ATOM   1404  O  OE2 . GLU B  1 40  ? 17.406  77.926  3.198   1.00 18.07 ? 40   GLU B OE2 1 
ATOM   1405  N  N   . GLY B  1 41  ? 14.079  76.889  7.438   1.00 6.95  ? 41   GLY B N   1 
ATOM   1406  C  CA  . GLY B  1 41  ? 12.856  76.157  7.119   1.00 6.86  ? 41   GLY B CA  1 
ATOM   1407  C  C   . GLY B  1 41  ? 11.693  76.523  8.015   1.00 6.88  ? 41   GLY B C   1 
ATOM   1408  O  O   . GLY B  1 41  ? 11.703  77.554  8.688   1.00 5.73  ? 41   GLY B O   1 
ATOM   1409  N  N   . LEU B  1 42  ? 10.662  75.680  7.998   1.00 5.99  ? 42   LEU B N   1 
ATOM   1410  C  CA  . LEU B  1 42  ? 9.426   75.960  8.727   1.00 6.97  ? 42   LEU B CA  1 
ATOM   1411  C  C   . LEU B  1 42  ? 9.441   75.534  10.189  1.00 6.06  ? 42   LEU B C   1 
ATOM   1412  O  O   . LEU B  1 42  ? 9.984   74.481  10.520  1.00 6.24  ? 42   LEU B O   1 
ATOM   1413  C  CB  . LEU B  1 42  ? 8.284   75.166  8.059   1.00 7.62  ? 42   LEU B CB  1 
ATOM   1414  C  CG  . LEU B  1 42  ? 7.380   75.719  6.944   1.00 13.00 ? 42   LEU B CG  1 
ATOM   1415  C  CD1 . LEU B  1 42  ? 7.724   77.056  6.320   1.00 12.78 ? 42   LEU B CD1 1 
ATOM   1416  C  CD2 . LEU B  1 42  ? 6.877   74.622  5.896   1.00 13.57 ? 42   LEU B CD2 1 
ATOM   1417  N  N   . HIS B  1 43  ? 8.814   76.335  11.057  1.00 5.06  ? 43   HIS B N   1 
ATOM   1418  C  CA  . HIS B  1 43  ? 8.737   76.013  12.479  1.00 5.00  ? 43   HIS B CA  1 
ATOM   1419  C  C   . HIS B  1 43  ? 7.353   76.312  12.975  1.00 5.00  ? 43   HIS B C   1 
ATOM   1420  O  O   . HIS B  1 43  ? 6.842   77.387  12.727  1.00 5.00  ? 43   HIS B O   1 
ATOM   1421  C  CB  . HIS B  1 43  ? 9.734   76.906  13.251  1.00 5.00  ? 43   HIS B CB  1 
ATOM   1422  C  CG  . HIS B  1 43  ? 11.155  76.571  12.931  1.00 5.73  ? 43   HIS B CG  1 
ATOM   1423  N  ND1 . HIS B  1 43  ? 11.857  75.605  13.627  1.00 5.00  ? 43   HIS B ND1 1 
ATOM   1424  C  CD2 . HIS B  1 43  ? 11.966  76.986  11.927  1.00 5.68  ? 43   HIS B CD2 1 
ATOM   1425  C  CE1 . HIS B  1 43  ? 13.061  75.473  13.084  1.00 5.00  ? 43   HIS B CE1 1 
ATOM   1426  N  NE2 . HIS B  1 43  ? 13.145  76.273  12.039  1.00 6.37  ? 43   HIS B NE2 1 
ATOM   1427  N  N   . GLY B  1 44  ? 6.743   75.383  13.717  1.00 5.00  ? 44   GLY B N   1 
ATOM   1428  C  CA  . GLY B  1 44  ? 5.397   75.641  14.170  1.00 5.00  ? 44   GLY B CA  1 
ATOM   1429  C  C   . GLY B  1 44  ? 5.368   76.816  15.139  1.00 5.18  ? 44   GLY B C   1 
ATOM   1430  O  O   . GLY B  1 44  ? 6.345   77.072  15.829  1.00 5.00  ? 44   GLY B O   1 
ATOM   1431  N  N   . PHE B  1 45  ? 4.246   77.514  15.181  1.00 5.00  ? 45   PHE B N   1 
ATOM   1432  C  CA  . PHE B  1 45  ? 4.174   78.774  15.912  1.00 5.00  ? 45   PHE B CA  1 
ATOM   1433  C  C   . PHE B  1 45  ? 2.775   78.830  16.483  1.00 5.00  ? 45   PHE B C   1 
ATOM   1434  O  O   . PHE B  1 45  ? 1.801   78.982  15.743  1.00 5.00  ? 45   PHE B O   1 
ATOM   1435  C  CB  . PHE B  1 45  ? 4.426   79.878  14.890  1.00 5.00  ? 45   PHE B CB  1 
ATOM   1436  C  CG  . PHE B  1 45  ? 4.579   81.302  15.451  1.00 5.00  ? 45   PHE B CG  1 
ATOM   1437  C  CD1 . PHE B  1 45  ? 5.618   81.660  16.301  1.00 5.77  ? 45   PHE B CD1 1 
ATOM   1438  C  CD2 . PHE B  1 45  ? 3.721   82.271  15.018  1.00 5.00  ? 45   PHE B CD2 1 
ATOM   1439  C  CE1 . PHE B  1 45  ? 5.790   83.007  16.707  1.00 5.62  ? 45   PHE B CE1 1 
ATOM   1440  C  CE2 . PHE B  1 45  ? 3.846   83.637  15.436  1.00 5.00  ? 45   PHE B CE2 1 
ATOM   1441  C  CZ  . PHE B  1 45  ? 4.903   83.990  16.265  1.00 5.00  ? 45   PHE B CZ  1 
ATOM   1442  N  N   . HIS B  1 46  ? 2.655   78.788  17.813  1.00 5.00  ? 46   HIS B N   1 
ATOM   1443  C  CA  . HIS B  1 46  ? 1.322   78.680  18.412  1.00 5.00  ? 46   HIS B CA  1 
ATOM   1444  C  C   . HIS B  1 46  ? 1.147   79.455  19.707  1.00 5.00  ? 46   HIS B C   1 
ATOM   1445  O  O   . HIS B  1 46  ? 2.128   79.643  20.441  1.00 5.00  ? 46   HIS B O   1 
ATOM   1446  C  CB  . HIS B  1 46  ? 1.094   77.217  18.847  1.00 5.15  ? 46   HIS B CB  1 
ATOM   1447  C  CG  . HIS B  1 46  ? 1.394   76.195  17.794  1.00 6.32  ? 46   HIS B CG  1 
ATOM   1448  N  ND1 . HIS B  1 46  ? 2.205   75.119  18.024  1.00 5.00  ? 46   HIS B ND1 1 
ATOM   1449  C  CD2 . HIS B  1 46  ? 0.988   76.083  16.506  1.00 5.00  ? 46   HIS B CD2 1 
ATOM   1450  C  CE1 . HIS B  1 46  ? 2.284   74.364  16.950  1.00 6.47  ? 46   HIS B CE1 1 
ATOM   1451  N  NE2 . HIS B  1 46  ? 1.583   74.947  15.994  1.00 7.26  ? 46   HIS B NE2 1 
ATOM   1452  N  N   . VAL B  1 47  ? -0.103  79.799  20.031  1.00 5.30  ? 47   VAL B N   1 
ATOM   1453  C  CA  . VAL B  1 47  ? -0.373  80.303  21.372  1.00 5.00  ? 47   VAL B CA  1 
ATOM   1454  C  C   . VAL B  1 47  ? -0.798  79.103  22.217  1.00 5.00  ? 47   VAL B C   1 
ATOM   1455  O  O   . VAL B  1 47  ? -1.762  78.419  21.886  1.00 5.00  ? 47   VAL B O   1 
ATOM   1456  C  CB  . VAL B  1 47  ? -1.473  81.337  21.392  1.00 5.00  ? 47   VAL B CB  1 
ATOM   1457  C  CG1 . VAL B  1 47  ? -1.750  81.775  22.847  1.00 5.00  ? 47   VAL B CG1 1 
ATOM   1458  C  CG2 . VAL B  1 47  ? -1.096  82.536  20.419  1.00 6.54  ? 47   VAL B CG2 1 
ATOM   1459  N  N   . HIS B  1 48  ? -0.038  78.822  23.274  1.00 5.00  ? 48   HIS B N   1 
ATOM   1460  C  CA  . HIS B  1 48  ? -0.389  77.761  24.210  1.00 5.00  ? 48   HIS B CA  1 
ATOM   1461  C  C   . HIS B  1 48  ? -1.179  78.328  25.382  1.00 5.00  ? 48   HIS B C   1 
ATOM   1462  O  O   . HIS B  1 48  ? -1.127  79.539  25.664  1.00 5.00  ? 48   HIS B O   1 
ATOM   1463  C  CB  . HIS B  1 48  ? 0.856   77.064  24.718  1.00 5.00  ? 48   HIS B CB  1 
ATOM   1464  C  CG  . HIS B  1 48  ? 1.489   76.214  23.667  1.00 5.00  ? 48   HIS B CG  1 
ATOM   1465  N  ND1 . HIS B  1 48  ? 1.732   74.863  23.823  1.00 5.00  ? 48   HIS B ND1 1 
ATOM   1466  C  CD2 . HIS B  1 48  ? 1.908   76.537  22.423  1.00 5.00  ? 48   HIS B CD2 1 
ATOM   1467  C  CE1 . HIS B  1 48  ? 2.277   74.391  22.706  1.00 5.00  ? 48   HIS B CE1 1 
ATOM   1468  N  NE2 . HIS B  1 48  ? 2.407   75.389  21.862  1.00 5.00  ? 48   HIS B NE2 1 
ATOM   1469  N  N   . GLU B  1 49  ? -1.875  77.445  26.076  1.00 5.00  ? 49   GLU B N   1 
ATOM   1470  C  CA  . GLU B  1 49  ? -2.927  77.871  26.994  1.00 5.00  ? 49   GLU B CA  1 
ATOM   1471  C  C   . GLU B  1 49  ? -2.480  78.720  28.190  1.00 5.00  ? 49   GLU B C   1 
ATOM   1472  O  O   . GLU B  1 49  ? -3.112  79.713  28.521  1.00 5.00  ? 49   GLU B O   1 
ATOM   1473  C  CB  . GLU B  1 49  ? -3.660  76.637  27.517  1.00 5.00  ? 49   GLU B CB  1 
ATOM   1474  C  CG  . GLU B  1 49  ? -4.951  76.996  28.280  1.00 7.22  ? 49   GLU B CG  1 
ATOM   1475  C  CD  . GLU B  1 49  ? -5.743  75.788  28.754  1.00 9.40  ? 49   GLU B CD  1 
ATOM   1476  O  OE1 . GLU B  1 49  ? -5.426  74.641  28.336  1.00 6.91  ? 49   GLU B OE1 1 
ATOM   1477  O  OE2 . GLU B  1 49  ? -6.692  75.987  29.568  1.00 8.66  ? 49   GLU B OE2 1 
ATOM   1478  N  N   . PHE B  1 50  ? -1.405  78.298  28.847  1.00 5.00  ? 50   PHE B N   1 
ATOM   1479  C  CA  . PHE B  1 50  ? -0.965  78.927  30.085  1.00 5.00  ? 50   PHE B CA  1 
ATOM   1480  C  C   . PHE B  1 50  ? 0.276   79.792  29.967  1.00 5.00  ? 50   PHE B C   1 
ATOM   1481  O  O   . PHE B  1 50  ? 1.240   79.382  29.312  1.00 5.00  ? 50   PHE B O   1 
ATOM   1482  C  CB  . PHE B  1 50  ? -0.674  77.843  31.148  1.00 5.00  ? 50   PHE B CB  1 
ATOM   1483  C  CG  . PHE B  1 50  ? -1.837  76.934  31.358  1.00 6.32  ? 50   PHE B CG  1 
ATOM   1484  C  CD1 . PHE B  1 50  ? -3.028  77.464  31.781  1.00 5.99  ? 50   PHE B CD1 1 
ATOM   1485  C  CD2 . PHE B  1 50  ? -1.741  75.576  31.062  1.00 8.81  ? 50   PHE B CD2 1 
ATOM   1486  C  CE1 . PHE B  1 50  ? -4.156  76.632  31.916  1.00 10.07 ? 50   PHE B CE1 1 
ATOM   1487  C  CE2 . PHE B  1 50  ? -2.838  74.734  31.210  1.00 11.43 ? 50   PHE B CE2 1 
ATOM   1488  C  CZ  . PHE B  1 50  ? -4.059  75.281  31.649  1.00 9.55  ? 50   PHE B CZ  1 
ATOM   1489  N  N   . GLY B  1 51  ? 0.250   80.949  30.645  1.00 5.00  ? 51   GLY B N   1 
ATOM   1490  C  CA  . GLY B  1 51  ? 1.384   81.851  30.709  1.00 5.00  ? 51   GLY B CA  1 
ATOM   1491  C  C   . GLY B  1 51  ? 2.256   81.429  31.880  1.00 5.00  ? 51   GLY B C   1 
ATOM   1492  O  O   . GLY B  1 51  ? 2.634   82.240  32.719  1.00 5.00  ? 51   GLY B O   1 
ATOM   1493  N  N   . ASP B  1 52  ? 2.601   80.136  31.896  1.00 5.00  ? 52   ASP B N   1 
ATOM   1494  C  CA  . ASP B  1 52  ? 3.324   79.511  33.024  1.00 5.00  ? 52   ASP B CA  1 
ATOM   1495  C  C   . ASP B  1 52  ? 4.675   78.999  32.536  1.00 5.00  ? 52   ASP B C   1 
ATOM   1496  O  O   . ASP B  1 52  ? 4.744   78.015  31.791  1.00 5.83  ? 52   ASP B O   1 
ATOM   1497  C  CB  . ASP B  1 52  ? 2.457   78.364  33.553  1.00 5.00  ? 52   ASP B CB  1 
ATOM   1498  C  CG  . ASP B  1 52  ? 3.073   77.680  34.762  1.00 5.00  ? 52   ASP B CG  1 
ATOM   1499  O  OD1 . ASP B  1 52  ? 4.325   77.774  34.965  1.00 5.00  ? 52   ASP B OD1 1 
ATOM   1500  O  OD2 . ASP B  1 52  ? 2.366   77.031  35.564  1.00 5.00  ? 52   ASP B OD2 1 
ATOM   1501  N  N   . ASN B  1 53  ? 5.739   79.689  32.925  1.00 5.00  ? 53   ASN B N   1 
ATOM   1502  C  CA  . ASN B  1 53  ? 7.085   79.357  32.484  1.00 6.55  ? 53   ASN B CA  1 
ATOM   1503  C  C   . ASN B  1 53  ? 7.869   78.716  33.646  1.00 5.06  ? 53   ASN B C   1 
ATOM   1504  O  O   . ASN B  1 53  ? 9.111   78.711  33.651  1.00 5.00  ? 53   ASN B O   1 
ATOM   1505  C  CB  . ASN B  1 53  ? 7.767   80.630  31.942  1.00 8.40  ? 53   ASN B CB  1 
ATOM   1506  C  CG  . ASN B  1 53  ? 9.097   80.342  31.258  1.00 16.63 ? 53   ASN B CG  1 
ATOM   1507  O  OD1 . ASN B  1 53  ? 10.166  80.801  31.709  1.00 23.50 ? 53   ASN B OD1 1 
ATOM   1508  N  ND2 . ASN B  1 53  ? 9.048   79.572  30.184  1.00 20.70 ? 53   ASN B ND2 1 
ATOM   1509  N  N   . THR B  1 54  ? 7.149   78.240  34.667  1.00 5.00  ? 54   THR B N   1 
ATOM   1510  C  CA  . THR B  1 54  ? 7.822   77.652  35.828  1.00 5.00  ? 54   THR B CA  1 
ATOM   1511  C  C   . THR B  1 54  ? 8.645   76.403  35.491  1.00 5.00  ? 54   THR B C   1 
ATOM   1512  O  O   . THR B  1 54  ? 9.602   76.101  36.228  1.00 5.00  ? 54   THR B O   1 
ATOM   1513  C  CB  . THR B  1 54  ? 6.883   77.288  36.968  1.00 5.00  ? 54   THR B CB  1 
ATOM   1514  O  OG1 . THR B  1 54  ? 5.874   76.353  36.514  1.00 5.00  ? 54   THR B OG1 1 
ATOM   1515  C  CG2 . THR B  1 54  ? 6.166   78.545  37.559  1.00 5.00  ? 54   THR B CG2 1 
ATOM   1516  N  N   . ALA B  1 55  ? 8.245   75.695  34.435  1.00 5.00  ? 55   ALA B N   1 
ATOM   1517  C  CA  . ALA B  1 55  ? 9.012   74.515  33.966  1.00 5.09  ? 55   ALA B CA  1 
ATOM   1518  C  C   . ALA B  1 55  ? 9.580   74.858  32.574  1.00 5.00  ? 55   ALA B C   1 
ATOM   1519  O  O   . ALA B  1 55  ? 9.614   74.028  31.656  1.00 5.00  ? 55   ALA B O   1 
ATOM   1520  C  CB  . ALA B  1 55  ? 8.104   73.259  33.909  1.00 5.00  ? 55   ALA B CB  1 
ATOM   1521  N  N   . GLY B  1 56  ? 10.046  76.097  32.419  1.00 5.00  ? 56   GLY B N   1 
ATOM   1522  C  CA  . GLY B  1 56  ? 10.373  76.597  31.080  1.00 5.00  ? 56   GLY B CA  1 
ATOM   1523  C  C   . GLY B  1 56  ? 9.139   76.504  30.159  1.00 5.24  ? 56   GLY B C   1 
ATOM   1524  O  O   . GLY B  1 56  ? 7.980   76.671  30.606  1.00 5.00  ? 56   GLY B O   1 
ATOM   1525  N  N   . CYS B  1 57  ? 9.366   76.196  28.874  1.00 5.00  ? 57   CYS B N   1 
ATOM   1526  C  CA  . CYS B  1 57  ? 8.260   76.093  27.923  1.00 6.27  ? 57   CYS B CA  1 
ATOM   1527  C  C   . CYS B  1 57  ? 7.333   74.918  28.194  1.00 5.33  ? 57   CYS B C   1 
ATOM   1528  O  O   . CYS B  1 57  ? 6.219   74.888  27.701  1.00 5.00  ? 57   CYS B O   1 
ATOM   1529  C  CB  . CYS B  1 57  ? 8.788   75.966  26.502  1.00 7.12  ? 57   CYS B CB  1 
ATOM   1530  S  SG  . CYS B  1 57  ? 9.694   77.504  26.085  1.00 14.02 ? 57   CYS B SG  1 
ATOM   1531  N  N   . THR B  1 58  ? 7.832   73.951  28.953  1.00 5.00  ? 58   THR B N   1 
ATOM   1532  C  CA  . THR B  1 58  ? 7.054   72.725  29.201  1.00 6.24  ? 58   THR B CA  1 
ATOM   1533  C  C   . THR B  1 58  ? 5.812   72.918  30.045  1.00 7.88  ? 58   THR B C   1 
ATOM   1534  O  O   . THR B  1 58  ? 4.928   72.056  30.005  1.00 10.47 ? 58   THR B O   1 
ATOM   1535  C  CB  . THR B  1 58  ? 7.906   71.558  29.757  1.00 6.53  ? 58   THR B CB  1 
ATOM   1536  O  OG1 . THR B  1 58  ? 8.323   71.802  31.129  1.00 7.30  ? 58   THR B OG1 1 
ATOM   1537  C  CG2 . THR B  1 58  ? 9.172   71.438  28.939  1.00 5.91  ? 58   THR B CG2 1 
ATOM   1538  N  N   . SER B  1 59  ? 5.719   73.985  30.826  1.00 5.08  ? 59   SER B N   1 
ATOM   1539  C  CA  . SER B  1 59  ? 4.510   74.179  31.639  1.00 5.00  ? 59   SER B CA  1 
ATOM   1540  C  C   . SER B  1 59  ? 3.438   75.064  30.923  1.00 5.00  ? 59   SER B C   1 
ATOM   1541  O  O   . SER B  1 59  ? 2.443   75.463  31.530  1.00 5.00  ? 59   SER B O   1 
ATOM   1542  C  CB  . SER B  1 59  ? 4.874   74.814  32.994  1.00 5.05  ? 59   SER B CB  1 
ATOM   1543  O  OG  . SER B  1 59  ? 5.848   75.832  32.747  1.00 5.00  ? 59   SER B OG  1 
ATOM   1544  N  N   . ALA B  1 60  ? 3.701   75.438  29.671  1.00 5.00  ? 60   ALA B N   1 
ATOM   1545  C  CA  . ALA B  1 60  ? 2.770   76.287  28.930  1.00 5.22  ? 60   ALA B CA  1 
ATOM   1546  C  C   . ALA B  1 60  ? 1.437   75.599  28.588  1.00 5.00  ? 60   ALA B C   1 
ATOM   1547  O  O   . ALA B  1 60  ? 0.530   76.253  28.109  1.00 5.00  ? 60   ALA B O   1 
ATOM   1548  C  CB  . ALA B  1 60  ? 3.427   76.792  27.642  1.00 5.00  ? 60   ALA B CB  1 
ATOM   1549  N  N   . GLY B  1 61  ? 1.331   74.285  28.816  1.00 5.36  ? 61   GLY B N   1 
ATOM   1550  C  CA  . GLY B  1 61  ? 0.095   73.583  28.461  1.00 5.00  ? 61   GLY B CA  1 
ATOM   1551  C  C   . GLY B  1 61  ? -0.018  73.291  26.969  1.00 5.00  ? 61   GLY B C   1 
ATOM   1552  O  O   . GLY B  1 61  ? 0.945   73.457  26.197  1.00 5.00  ? 61   GLY B O   1 
ATOM   1553  N  N   . PRO B  1 62  ? -1.194  72.836  26.563  1.00 5.00  ? 62   PRO B N   1 
ATOM   1554  C  CA  . PRO B  1 62  ? -1.472  72.534  25.149  1.00 5.00  ? 62   PRO B CA  1 
ATOM   1555  C  C   . PRO B  1 62  ? -1.842  73.822  24.411  1.00 5.00  ? 62   PRO B C   1 
ATOM   1556  O  O   . PRO B  1 62  ? -1.756  74.926  24.947  1.00 5.00  ? 62   PRO B O   1 
ATOM   1557  C  CB  . PRO B  1 62  ? -2.674  71.622  25.236  1.00 6.30  ? 62   PRO B CB  1 
ATOM   1558  C  CG  . PRO B  1 62  ? -3.455  72.116  26.468  1.00 5.99  ? 62   PRO B CG  1 
ATOM   1559  C  CD  . PRO B  1 62  ? -2.356  72.578  27.434  1.00 5.00  ? 62   PRO B CD  1 
ATOM   1560  N  N   . HIS B  1 63  ? -2.246  73.693  23.149  1.00 5.00  ? 63   HIS B N   1 
ATOM   1561  C  CA  . HIS B  1 63  ? -2.671  74.854  22.377  1.00 5.00  ? 63   HIS B CA  1 
ATOM   1562  C  C   . HIS B  1 63  ? -3.906  75.458  23.025  1.00 5.03  ? 63   HIS B C   1 
ATOM   1563  O  O   . HIS B  1 63  ? -4.772  74.739  23.503  1.00 5.00  ? 63   HIS B O   1 
ATOM   1564  C  CB  . HIS B  1 63  ? -2.945  74.377  20.931  1.00 5.00  ? 63   HIS B CB  1 
ATOM   1565  C  CG  . HIS B  1 63  ? -1.697  73.949  20.213  1.00 5.76  ? 63   HIS B CG  1 
ATOM   1566  N  ND1 . HIS B  1 63  ? -1.684  73.473  18.919  1.00 5.51  ? 63   HIS B ND1 1 
ATOM   1567  C  CD2 . HIS B  1 63  ? -0.406  73.933  20.628  1.00 9.80  ? 63   HIS B CD2 1 
ATOM   1568  C  CE1 . HIS B  1 63  ? -0.444  73.177  18.570  1.00 8.48  ? 63   HIS B CE1 1 
ATOM   1569  N  NE2 . HIS B  1 63  ? 0.348   73.456  19.589  1.00 13.23 ? 63   HIS B NE2 1 
ATOM   1570  N  N   . PHE B  1 64  ? -3.970  76.787  23.037  1.00 5.00  ? 64   PHE B N   1 
ATOM   1571  C  CA  . PHE B  1 64  ? -5.127  77.521  23.523  1.00 5.00  ? 64   PHE B CA  1 
ATOM   1572  C  C   . PHE B  1 64  ? -6.306  77.124  22.620  1.00 5.42  ? 64   PHE B C   1 
ATOM   1573  O  O   . PHE B  1 64  ? -6.264  77.302  21.403  1.00 5.00  ? 64   PHE B O   1 
ATOM   1574  C  CB  . PHE B  1 64  ? -4.840  79.025  23.460  1.00 5.23  ? 64   PHE B CB  1 
ATOM   1575  C  CG  . PHE B  1 64  ? -5.973  79.883  23.936  1.00 5.83  ? 64   PHE B CG  1 
ATOM   1576  C  CD1 . PHE B  1 64  ? -6.695  79.524  25.033  1.00 7.81  ? 64   PHE B CD1 1 
ATOM   1577  C  CD2 . PHE B  1 64  ? -6.309  81.054  23.239  1.00 6.26  ? 64   PHE B CD2 1 
ATOM   1578  C  CE1 . PHE B  1 64  ? -7.775  80.335  25.479  1.00 8.95  ? 64   PHE B CE1 1 
ATOM   1579  C  CE2 . PHE B  1 64  ? -7.342  81.846  23.676  1.00 9.04  ? 64   PHE B CE2 1 
ATOM   1580  C  CZ  . PHE B  1 64  ? -8.072  81.468  24.803  1.00 7.95  ? 64   PHE B CZ  1 
ATOM   1581  N  N   . ASN B  1 65  ? -7.326  76.556  23.254  1.00 5.00  ? 65   ASN B N   1 
ATOM   1582  C  CA  . ASN B  1 65  ? -8.432  75.923  22.532  1.00 6.73  ? 65   ASN B CA  1 
ATOM   1583  C  C   . ASN B  1 65  ? -9.759  76.050  23.285  1.00 7.90  ? 65   ASN B C   1 
ATOM   1584  O  O   . ASN B  1 65  ? -10.344 75.029  23.701  1.00 7.00  ? 65   ASN B O   1 
ATOM   1585  C  CB  . ASN B  1 65  ? -8.062  74.435  22.368  1.00 6.04  ? 65   ASN B CB  1 
ATOM   1586  C  CG  . ASN B  1 65  ? -9.044  73.665  21.458  1.00 7.23  ? 65   ASN B CG  1 
ATOM   1587  O  OD1 . ASN B  1 65  ? -9.702  74.243  20.606  1.00 7.68  ? 65   ASN B OD1 1 
ATOM   1588  N  ND2 . ASN B  1 65  ? -9.095  72.353  21.632  1.00 5.72  ? 65   ASN B ND2 1 
ATOM   1589  N  N   . PRO B  1 66  ? -10.213 77.285  23.485  1.00 8.78  ? 66   PRO B N   1 
ATOM   1590  C  CA  . PRO B  1 66  ? -11.440 77.545  24.241  1.00 10.52 ? 66   PRO B CA  1 
ATOM   1591  C  C   . PRO B  1 66  ? -12.673 76.991  23.514  1.00 11.94 ? 66   PRO B C   1 
ATOM   1592  O  O   . PRO B  1 66  ? -13.718 76.835  24.135  1.00 12.27 ? 66   PRO B O   1 
ATOM   1593  C  CB  . PRO B  1 66  ? -11.490 79.073  24.300  1.00 10.36 ? 66   PRO B CB  1 
ATOM   1594  C  CG  . PRO B  1 66  ? -10.789 79.477  23.064  1.00 9.44  ? 66   PRO B CG  1 
ATOM   1595  C  CD  . PRO B  1 66  ? -9.588  78.537  23.001  1.00 9.42  ? 66   PRO B CD  1 
ATOM   1596  N  N   . LEU B  1 67  ? -12.564 76.672  22.233  1.00 12.51 ? 67   LEU B N   1 
ATOM   1597  C  CA  . LEU B  1 67  ? -13.739 76.098  21.548  1.00 14.03 ? 67   LEU B CA  1 
ATOM   1598  C  C   . LEU B  1 67  ? -13.651 74.589  21.358  1.00 13.81 ? 67   LEU B C   1 
ATOM   1599  O  O   . LEU B  1 67  ? -14.450 74.014  20.613  1.00 14.92 ? 67   LEU B O   1 
ATOM   1600  C  CB  . LEU B  1 67  ? -14.008 76.800  20.223  1.00 14.32 ? 67   LEU B CB  1 
ATOM   1601  C  CG  . LEU B  1 67  ? -14.157 78.313  20.332  1.00 16.05 ? 67   LEU B CG  1 
ATOM   1602  C  CD1 . LEU B  1 67  ? -14.458 78.904  18.955  1.00 20.59 ? 67   LEU B CD1 1 
ATOM   1603  C  CD2 . LEU B  1 67  ? -15.227 78.703  21.339  1.00 19.65 ? 67   LEU B CD2 1 
ATOM   1604  N  N   . SER B  1 68  ? -12.688 73.950  22.019  1.00 14.14 ? 68   SER B N   1 
ATOM   1605  C  CA  . SER B  1 68  ? -12.567 72.482  22.005  1.00 14.32 ? 68   SER B CA  1 
ATOM   1606  C  C   . SER B  1 68  ? -12.548 71.850  20.609  1.00 14.87 ? 68   SER B C   1 
ATOM   1607  O  O   . SER B  1 68  ? -13.278 70.868  20.338  1.00 14.49 ? 68   SER B O   1 
ATOM   1608  C  CB  . SER B  1 68  ? -13.727 71.858  22.792  1.00 15.46 ? 68   SER B CB  1 
ATOM   1609  O  OG  . SER B  1 68  ? -13.809 72.430  24.089  1.00 15.13 ? 68   SER B OG  1 
ATOM   1610  N  N   . ARG B  1 69  ? -11.743 72.414  19.721  1.00 13.49 ? 69   ARG B N   1 
ATOM   1611  C  CA  . ARG B  1 69  ? -11.631 71.899  18.363  1.00 13.05 ? 69   ARG B CA  1 
ATOM   1612  C  C   . ARG B  1 69  ? -10.349 71.095  18.203  1.00 11.69 ? 69   ARG B C   1 
ATOM   1613  O  O   . ARG B  1 69  ? -9.538  70.989  19.112  1.00 11.00 ? 69   ARG B O   1 
ATOM   1614  C  CB  . ARG B  1 69  ? -11.597 73.056  17.365  1.00 12.88 ? 69   ARG B CB  1 
ATOM   1615  C  CG  . ARG B  1 69  ? -12.820 73.980  17.390  1.00 18.65 ? 69   ARG B CG  1 
ATOM   1616  C  CD  . ARG B  1 69  ? -14.009 73.441  16.592  1.00 25.08 ? 69   ARG B CD  1 
ATOM   1617  N  NE  . ARG B  1 69  ? -14.595 74.493  15.757  1.00 31.20 ? 69   ARG B NE  1 
ATOM   1618  C  CZ  . ARG B  1 69  ? -14.886 74.374  14.465  1.00 32.83 ? 69   ARG B CZ  1 
ATOM   1619  N  NH1 . ARG B  1 69  ? -14.677 73.237  13.806  1.00 34.11 ? 69   ARG B NH1 1 
ATOM   1620  N  NH2 . ARG B  1 69  ? -15.413 75.405  13.825  1.00 36.28 ? 69   ARG B NH2 1 
ATOM   1621  N  N   . LYS B  1 70  ? -10.170 70.519  17.030  1.00 10.93 ? 70   LYS B N   1 
ATOM   1622  C  CA  . LYS B  1 70  ? -8.958  69.778  16.763  1.00 10.72 ? 70   LYS B CA  1 
ATOM   1623  C  C   . LYS B  1 70  ? -7.952  70.742  16.128  1.00 9.23  ? 70   LYS B C   1 
ATOM   1624  O  O   . LYS B  1 70  ? -8.313  71.830  15.677  1.00 6.71  ? 70   LYS B O   1 
ATOM   1625  C  CB  . LYS B  1 70  ? -9.246  68.651  15.775  1.00 12.27 ? 70   LYS B CB  1 
ATOM   1626  C  CG  . LYS B  1 70  ? -10.014 67.478  16.395  1.00 16.11 ? 70   LYS B CG  1 
ATOM   1627  C  CD  . LYS B  1 70  ? -9.982  66.290  15.426  1.00 23.04 ? 70   LYS B CD  1 
ATOM   1628  C  CE  . LYS B  1 70  ? -11.102 65.296  15.677  1.00 25.72 ? 70   LYS B CE  1 
ATOM   1629  N  NZ  . LYS B  1 70  ? -10.889 64.108  14.793  1.00 30.26 ? 70   LYS B NZ  1 
ATOM   1630  N  N   . HIS B  1 71  ? -6.716  70.288  16.059  1.00 8.84  ? 71   HIS B N   1 
ATOM   1631  C  CA  . HIS B  1 71  ? -5.618  71.083  15.543  1.00 8.25  ? 71   HIS B CA  1 
ATOM   1632  C  C   . HIS B  1 71  ? -5.703  71.308  14.024  1.00 8.81  ? 71   HIS B C   1 
ATOM   1633  O  O   . HIS B  1 71  ? -6.049  70.375  13.287  1.00 9.84  ? 71   HIS B O   1 
ATOM   1634  C  CB  . HIS B  1 71  ? -4.260  70.464  15.961  1.00 6.99  ? 71   HIS B CB  1 
ATOM   1635  C  CG  . HIS B  1 71  ? -3.105  71.257  15.444  1.00 7.27  ? 71   HIS B CG  1 
ATOM   1636  N  ND1 . HIS B  1 71  ? -2.660  72.408  16.057  1.00 5.00  ? 71   HIS B ND1 1 
ATOM   1637  C  CD2 . HIS B  1 71  ? -2.357  71.101  14.328  1.00 5.72  ? 71   HIS B CD2 1 
ATOM   1638  C  CE1 . HIS B  1 71  ? -1.678  72.926  15.343  1.00 6.42  ? 71   HIS B CE1 1 
ATOM   1639  N  NE2 . HIS B  1 71  ? -1.478  72.158  14.286  1.00 5.60  ? 71   HIS B NE2 1 
ATOM   1640  N  N   . GLY B  1 72  ? -5.422  72.531  13.554  1.00 6.88  ? 72   GLY B N   1 
ATOM   1641  C  CA  . GLY B  1 72  ? -5.403  72.807  12.120  1.00 7.39  ? 72   GLY B CA  1 
ATOM   1642  C  C   . GLY B  1 72  ? -4.424  73.926  11.801  1.00 7.73  ? 72   GLY B C   1 
ATOM   1643  O  O   . GLY B  1 72  ? -3.639  74.322  12.673  1.00 7.34  ? 72   GLY B O   1 
ATOM   1644  N  N   . GLY B  1 73  ? -4.430  74.400  10.553  1.00 7.64  ? 73   GLY B N   1 
ATOM   1645  C  CA  . GLY B  1 73  ? -3.656  75.584  10.152  1.00 7.30  ? 73   GLY B CA  1 
ATOM   1646  C  C   . GLY B  1 73  ? -4.548  76.806  10.391  1.00 7.37  ? 73   GLY B C   1 
ATOM   1647  O  O   . GLY B  1 73  ? -5.752  76.648  10.568  1.00 7.56  ? 73   GLY B O   1 
ATOM   1648  N  N   . PRO B  1 74  ? -3.971  77.995  10.417  1.00 6.71  ? 74   PRO B N   1 
ATOM   1649  C  CA  . PRO B  1 74  ? -4.730  79.207  10.718  1.00 7.03  ? 74   PRO B CA  1 
ATOM   1650  C  C   . PRO B  1 74  ? -5.816  79.490  9.679   1.00 7.96  ? 74   PRO B C   1 
ATOM   1651  O  O   . PRO B  1 74  ? -6.767  80.182  9.979   1.00 8.08  ? 74   PRO B O   1 
ATOM   1652  C  CB  . PRO B  1 74  ? -3.643  80.310  10.734  1.00 7.93  ? 74   PRO B CB  1 
ATOM   1653  C  CG  . PRO B  1 74  ? -2.497  79.718  9.893   1.00 7.62  ? 74   PRO B CG  1 
ATOM   1654  C  CD  . PRO B  1 74  ? -2.524  78.256  10.240  1.00 6.06  ? 74   PRO B CD  1 
ATOM   1655  N  N   . LYS B  1 75  ? -5.665  78.984  8.465   1.00 9.02  ? 75   LYS B N   1 
ATOM   1656  C  CA  . LYS B  1 75  ? -6.680  79.244  7.431   1.00 10.50 ? 75   LYS B CA  1 
ATOM   1657  C  C   . LYS B  1 75  ? -7.850  78.252  7.521   1.00 10.78 ? 75   LYS B C   1 
ATOM   1658  O  O   . LYS B  1 75  ? -8.893  78.413  6.846   1.00 10.73 ? 75   LYS B O   1 
ATOM   1659  C  CB  . LYS B  1 75  ? -6.026  79.192  6.038   1.00 11.18 ? 75   LYS B CB  1 
ATOM   1660  C  CG  . LYS B  1 75  ? -4.813  80.133  5.921   1.00 14.74 ? 75   LYS B CG  1 
ATOM   1661  C  CD  . LYS B  1 75  ? -4.086  79.960  4.560   1.00 21.08 ? 75   LYS B CD  1 
ATOM   1662  C  CE  . LYS B  1 75  ? -2.908  80.951  4.373   1.00 20.49 ? 75   LYS B CE  1 
ATOM   1663  N  NZ  . LYS B  1 75  ? -3.304  82.382  4.274   1.00 23.36 ? 75   LYS B NZ  1 
ATOM   1664  N  N   . ASP B  1 76  ? -7.723  77.228  8.365   1.00 9.84  ? 76   ASP B N   1 
ATOM   1665  C  CA  . ASP B  1 76  ? -8.795  76.248  8.456   1.00 10.22 ? 76   ASP B CA  1 
ATOM   1666  C  C   . ASP B  1 76  ? -9.886  76.665  9.425   1.00 11.07 ? 76   ASP B C   1 
ATOM   1667  O  O   . ASP B  1 76  ? -9.594  77.291  10.453  1.00 10.05 ? 76   ASP B O   1 
ATOM   1668  C  CB  . ASP B  1 76  ? -8.273  74.881  8.907   1.00 10.49 ? 76   ASP B CB  1 
ATOM   1669  C  CG  . ASP B  1 76  ? -7.143  74.348  8.012   1.00 12.74 ? 76   ASP B CG  1 
ATOM   1670  O  OD1 . ASP B  1 76  ? -7.088  74.681  6.777   1.00 14.63 ? 76   ASP B OD1 1 
ATOM   1671  O  OD2 . ASP B  1 76  ? -6.234  73.607  8.468   1.00 12.81 ? 76   ASP B OD2 1 
ATOM   1672  N  N   . GLU B  1 77  ? -11.126 76.283  9.100   1.00 11.38 ? 77   GLU B N   1 
ATOM   1673  C  CA  . GLU B  1 77  ? -12.252 76.456  10.000  1.00 13.06 ? 77   GLU B CA  1 
ATOM   1674  C  C   . GLU B  1 77  ? -12.073 75.580  11.229  1.00 12.29 ? 77   GLU B C   1 
ATOM   1675  O  O   . GLU B  1 77  ? -12.388 76.011  12.344  1.00 13.36 ? 77   GLU B O   1 
ATOM   1676  C  CB  . GLU B  1 77  ? -13.573 76.082  9.294   1.00 14.12 ? 77   GLU B CB  1 
ATOM   1677  C  CG  . GLU B  1 77  ? -14.801 76.676  9.968   1.00 18.90 ? 77   GLU B CG  1 
ATOM   1678  C  CD  . GLU B  1 77  ? -15.173 75.939  11.238  1.00 24.61 ? 77   GLU B CD  1 
ATOM   1679  O  OE1 . GLU B  1 77  ? -14.869 74.725  11.321  1.00 26.57 ? 77   GLU B OE1 1 
ATOM   1680  O  OE2 . GLU B  1 77  ? -15.778 76.574  12.152  1.00 25.70 ? 77   GLU B OE2 1 
ATOM   1681  N  N   . GLU B  1 78  ? -11.584 74.352  11.042  1.00 10.83 ? 78   GLU B N   1 
ATOM   1682  C  CA  . GLU B  1 78  ? -11.305 73.502  12.192  1.00 9.65  ? 78   GLU B CA  1 
ATOM   1683  C  C   . GLU B  1 78  ? -9.850  73.778  12.661  1.00 8.37  ? 78   GLU B C   1 
ATOM   1684  O  O   . GLU B  1 78  ? -8.890  73.334  12.028  1.00 7.78  ? 78   GLU B O   1 
ATOM   1685  C  CB  . GLU B  1 78  ? -11.475 72.018  11.842  1.00 10.62 ? 78   GLU B CB  1 
ATOM   1686  C  CG  . GLU B  1 78  ? -11.286 71.047  13.002  1.00 12.39 ? 78   GLU B CG  1 
ATOM   1687  C  CD  . GLU B  1 78  ? -12.467 71.012  13.962  1.00 20.28 ? 78   GLU B CD  1 
ATOM   1688  O  OE1 . GLU B  1 78  ? -13.553 71.527  13.582  1.00 23.55 ? 78   GLU B OE1 1 
ATOM   1689  O  OE2 . GLU B  1 78  ? -12.337 70.446  15.084  1.00 19.55 ? 78   GLU B OE2 1 
ATOM   1690  N  N   . ARG B  1 79  ? -9.701  74.536  13.743  1.00 7.44  ? 79   ARG B N   1 
ATOM   1691  C  CA  . ARG B  1 79  ? -8.379  74.814  14.320  1.00 6.01  ? 79   ARG B CA  1 
ATOM   1692  C  C   . ARG B  1 79  ? -8.576  75.209  15.769  1.00 6.13  ? 79   ARG B C   1 
ATOM   1693  O  O   . ARG B  1 79  ? -9.699  75.503  16.208  1.00 6.77  ? 79   ARG B O   1 
ATOM   1694  C  CB  . ARG B  1 79  ? -7.706  75.986  13.605  1.00 7.20  ? 79   ARG B CB  1 
ATOM   1695  C  CG  . ARG B  1 79  ? -8.571  77.216  13.587  1.00 7.62  ? 79   ARG B CG  1 
ATOM   1696  C  CD  . ARG B  1 79  ? -7.880  78.464  13.033  1.00 9.36  ? 79   ARG B CD  1 
ATOM   1697  N  NE  . ARG B  1 79  ? -7.175  79.182  14.091  1.00 6.56  ? 79   ARG B NE  1 
ATOM   1698  C  CZ  . ARG B  1 79  ? -6.630  80.367  13.906  1.00 9.29  ? 79   ARG B CZ  1 
ATOM   1699  N  NH1 . ARG B  1 79  ? -6.698  80.948  12.708  1.00 7.30  ? 79   ARG B NH1 1 
ATOM   1700  N  NH2 . ARG B  1 79  ? -6.035  80.988  14.909  1.00 5.92  ? 79   ARG B NH2 1 
ATOM   1701  N  N   . HIS B  1 80  ? -7.479  75.184  16.516  1.00 5.19  ? 80   HIS B N   1 
ATOM   1702  C  CA  . HIS B  1 80  ? -7.442  75.738  17.842  1.00 5.67  ? 80   HIS B CA  1 
ATOM   1703  C  C   . HIS B  1 80  ? -7.282  77.256  17.672  1.00 5.22  ? 80   HIS B C   1 
ATOM   1704  O  O   . HIS B  1 80  ? -6.677  77.727  16.692  1.00 5.14  ? 80   HIS B O   1 
ATOM   1705  C  CB  . HIS B  1 80  ? -6.179  75.232  18.571  1.00 5.98  ? 80   HIS B CB  1 
ATOM   1706  C  CG  . HIS B  1 80  ? -6.123  73.750  18.732  1.00 5.99  ? 80   HIS B CG  1 
ATOM   1707  N  ND1 . HIS B  1 80  ? -4.952  73.028  18.629  1.00 5.00  ? 80   HIS B ND1 1 
ATOM   1708  C  CD2 . HIS B  1 80  ? -7.093  72.859  19.053  1.00 5.00  ? 80   HIS B CD2 1 
ATOM   1709  C  CE1 . HIS B  1 80  ? -5.211  71.755  18.859  1.00 6.07  ? 80   HIS B CE1 1 
ATOM   1710  N  NE2 . HIS B  1 80  ? -6.499  71.627  19.125  1.00 7.30  ? 80   HIS B NE2 1 
ATOM   1711  N  N   . VAL B  1 81  ? -7.791  78.014  18.637  1.00 5.51  ? 81   VAL B N   1 
ATOM   1712  C  CA  . VAL B  1 81  ? -7.593  79.468  18.588  1.00 5.00  ? 81   VAL B CA  1 
ATOM   1713  C  C   . VAL B  1 81  ? -6.096  79.757  18.462  1.00 5.00  ? 81   VAL B C   1 
ATOM   1714  O  O   . VAL B  1 81  ? -5.676  80.625  17.701  1.00 5.00  ? 81   VAL B O   1 
ATOM   1715  C  CB  . VAL B  1 81  ? -8.168  80.191  19.833  1.00 5.00  ? 81   VAL B CB  1 
ATOM   1716  C  CG1 . VAL B  1 81  ? -7.744  81.665  19.849  1.00 5.00  ? 81   VAL B CG1 1 
ATOM   1717  C  CG2 . VAL B  1 81  ? -9.736  80.100  19.831  1.00 5.26  ? 81   VAL B CG2 1 
ATOM   1718  N  N   . GLY B  1 82  ? -5.277  79.019  19.201  1.00 5.00  ? 82   GLY B N   1 
ATOM   1719  C  CA  . GLY B  1 82  ? -3.827  79.311  19.191  1.00 5.00  ? 82   GLY B CA  1 
ATOM   1720  C  C   . GLY B  1 82  ? -3.052  78.833  17.960  1.00 5.02  ? 82   GLY B C   1 
ATOM   1721  O  O   . GLY B  1 82  ? -1.812  78.912  17.931  1.00 5.00  ? 82   GLY B O   1 
ATOM   1722  N  N   . ASP B  1 83  ? -3.750  78.289  16.945  1.00 5.00  ? 83   ASP B N   1 
ATOM   1723  C  CA  . ASP B  1 83  ? -3.049  77.753  15.781  1.00 5.00  ? 83   ASP B CA  1 
ATOM   1724  C  C   . ASP B  1 83  ? -2.623  78.803  14.755  1.00 5.66  ? 83   ASP B C   1 
ATOM   1725  O  O   . ASP B  1 83  ? -3.407  79.149  13.861  1.00 7.32  ? 83   ASP B O   1 
ATOM   1726  C  CB  . ASP B  1 83  ? -3.921  76.701  15.072  1.00 5.00  ? 83   ASP B CB  1 
ATOM   1727  C  CG  . ASP B  1 83  ? -4.057  75.427  15.870  1.00 5.00  ? 83   ASP B CG  1 
ATOM   1728  O  OD1 . ASP B  1 83  ? -3.217  75.199  16.804  1.00 5.54  ? 83   ASP B OD1 1 
ATOM   1729  O  OD2 . ASP B  1 83  ? -4.967  74.587  15.629  1.00 5.00  ? 83   ASP B OD2 1 
ATOM   1730  N  N   . LEU B  1 84  ? -1.401  79.299  14.864  1.00 5.00  ? 84   LEU B N   1 
ATOM   1731  C  CA  . LEU B  1 84  ? -0.936  80.320  13.918  1.00 5.31  ? 84   LEU B CA  1 
ATOM   1732  C  C   . LEU B  1 84  ? -0.058  79.745  12.815  1.00 5.61  ? 84   LEU B C   1 
ATOM   1733  O  O   . LEU B  1 84  ? 0.621   80.494  12.115  1.00 6.72  ? 84   LEU B O   1 
ATOM   1734  C  CB  . LEU B  1 84  ? -0.229  81.447  14.650  1.00 5.00  ? 84   LEU B CB  1 
ATOM   1735  C  CG  . LEU B  1 84  ? -1.175  82.125  15.660  1.00 5.49  ? 84   LEU B CG  1 
ATOM   1736  C  CD1 . LEU B  1 84  ? -0.428  83.234  16.450  1.00 5.31  ? 84   LEU B CD1 1 
ATOM   1737  C  CD2 . LEU B  1 84  ? -2.379  82.725  14.938  1.00 8.13  ? 84   LEU B CD2 1 
ATOM   1738  N  N   . GLY B  1 85  ? -0.042  78.429  12.688  1.00 5.00  ? 85   GLY B N   1 
ATOM   1739  C  CA  . GLY B  1 85  ? 0.662   77.785  11.580  1.00 5.05  ? 85   GLY B CA  1 
ATOM   1740  C  C   . GLY B  1 85  ? 2.169   77.727  11.742  1.00 5.52  ? 85   GLY B C   1 
ATOM   1741  O  O   . GLY B  1 85  ? 2.679   77.409  12.809  1.00 5.44  ? 85   GLY B O   1 
ATOM   1742  N  N   . ASN B  1 86  ? 2.879   78.052  10.661  1.00 5.00  ? 86   ASN B N   1 
ATOM   1743  C  CA  . ASN B  1 86  ? 4.326   78.038  10.664  1.00 5.37  ? 86   ASN B CA  1 
ATOM   1744  C  C   . ASN B  1 86  ? 4.939   79.414  10.421  1.00 5.44  ? 86   ASN B C   1 
ATOM   1745  O  O   . ASN B  1 86  ? 4.330   80.248  9.782   1.00 5.00  ? 86   ASN B O   1 
ATOM   1746  C  CB  . ASN B  1 86  ? 4.811   77.130  9.516   1.00 5.00  ? 86   ASN B CB  1 
ATOM   1747  C  CG  . ASN B  1 86  ? 4.588   75.682  9.826   1.00 6.02  ? 86   ASN B CG  1 
ATOM   1748  O  OD1 . ASN B  1 86  ? 5.143   75.178  10.788  1.00 5.00  ? 86   ASN B OD1 1 
ATOM   1749  N  ND2 . ASN B  1 86  ? 3.774   75.015  9.022   1.00 5.80  ? 86   ASN B ND2 1 
ATOM   1750  N  N   . VAL B  1 87  ? 6.160   79.617  10.927  1.00 5.00  ? 87   VAL B N   1 
ATOM   1751  C  CA  . VAL B  1 87  ? 6.976   80.743  10.489  1.00 5.03  ? 87   VAL B CA  1 
ATOM   1752  C  C   . VAL B  1 87  ? 8.142   80.164  9.705   1.00 5.00  ? 87   VAL B C   1 
ATOM   1753  O  O   . VAL B  1 87  ? 8.400   78.963  9.779   1.00 5.00  ? 87   VAL B O   1 
ATOM   1754  C  CB  . VAL B  1 87  ? 7.448   81.610  11.649  1.00 5.26  ? 87   VAL B CB  1 
ATOM   1755  C  CG1 . VAL B  1 87  ? 6.236   82.197  12.319  1.00 6.40  ? 87   VAL B CG1 1 
ATOM   1756  C  CG2 . VAL B  1 87  ? 8.316   80.812  12.673  1.00 6.15  ? 87   VAL B CG2 1 
ATOM   1757  N  N   . THR B  1 88  ? 8.862   81.006  8.967   1.00 5.00  ? 88   THR B N   1 
ATOM   1758  C  CA  . THR B  1 88  ? 9.906   80.507  8.070   1.00 5.65  ? 88   THR B CA  1 
ATOM   1759  C  C   . THR B  1 88  ? 11.231  81.125  8.395   1.00 5.84  ? 88   THR B C   1 
ATOM   1760  O  O   . THR B  1 88  ? 11.339  82.336  8.355   1.00 5.86  ? 88   THR B O   1 
ATOM   1761  C  CB  . THR B  1 88  ? 9.544   80.952  6.642   1.00 7.50  ? 88   THR B CB  1 
ATOM   1762  O  OG1 . THR B  1 88  ? 8.304   80.318  6.267   1.00 7.80  ? 88   THR B OG1 1 
ATOM   1763  C  CG2 . THR B  1 88  ? 10.634  80.478  5.621   1.00 8.66  ? 88   THR B CG2 1 
ATOM   1764  N  N   . ALA B  1 89  ? 12.223  80.311  8.731   1.00 5.00  ? 89   ALA B N   1 
ATOM   1765  C  CA  . ALA B  1 89  ? 13.546  80.841  9.000   1.00 5.96  ? 89   ALA B CA  1 
ATOM   1766  C  C   . ALA B  1 89  ? 14.363  80.790  7.711   1.00 6.30  ? 89   ALA B C   1 
ATOM   1767  O  O   . ALA B  1 89  ? 14.281  79.806  6.982   1.00 6.43  ? 89   ALA B O   1 
ATOM   1768  C  CB  . ALA B  1 89  ? 14.203  80.017  10.086  1.00 6.53  ? 89   ALA B CB  1 
ATOM   1769  N  N   . ASP B  1 90  ? 15.136  81.847  7.445   1.00 8.77  ? 90   ASP B N   1 
ATOM   1770  C  CA  . ASP B  1 90  ? 15.985  81.907  6.235   1.00 10.46 ? 90   ASP B CA  1 
ATOM   1771  C  C   . ASP B  1 90  ? 17.306  81.172  6.454   1.00 11.18 ? 90   ASP B C   1 
ATOM   1772  O  O   . ASP B  1 90  ? 17.497  80.564  7.502   1.00 9.53  ? 90   ASP B O   1 
ATOM   1773  C  CB  . ASP B  1 90  ? 16.291  83.347  5.889   1.00 11.47 ? 90   ASP B CB  1 
ATOM   1774  C  CG  . ASP B  1 90  ? 17.201  84.003  6.914   1.00 13.94 ? 90   ASP B CG  1 
ATOM   1775  O  OD1 . ASP B  1 90  ? 17.888  83.288  7.705   1.00 14.80 ? 90   ASP B OD1 1 
ATOM   1776  O  OD2 . ASP B  1 90  ? 17.263  85.233  7.046   1.00 17.39 ? 90   ASP B OD2 1 
ATOM   1777  N  N   . LYS B  1 91  ? 18.219  81.234  5.458   1.00 12.34 ? 91   LYS B N   1 
ATOM   1778  C  CA  . LYS B  1 91  ? 19.499  80.522  5.543   1.00 13.55 ? 91   LYS B CA  1 
ATOM   1779  C  C   . LYS B  1 91  ? 20.325  80.920  6.758   1.00 13.44 ? 91   LYS B C   1 
ATOM   1780  O  O   . LYS B  1 91  ? 21.134  80.133  7.250   1.00 14.36 ? 91   LYS B O   1 
ATOM   1781  C  CB  . LYS B  1 91  ? 20.353  80.734  4.247   1.00 14.53 ? 91   LYS B CB  1 
ATOM   1782  C  CG  . LYS B  1 91  ? 20.997  82.137  4.156   1.00 18.93 ? 91   LYS B CG  1 
ATOM   1783  C  CD  . LYS B  1 91  ? 22.215  82.207  3.187   1.00 25.81 ? 91   LYS B CD  1 
ATOM   1784  C  CE  . LYS B  1 91  ? 23.271  83.228  3.682   1.00 28.82 ? 91   LYS B CE  1 
ATOM   1785  N  NZ  . LYS B  1 91  ? 22.741  84.614  3.945   1.00 30.81 ? 91   LYS B NZ  1 
ATOM   1786  N  N   . ASP B  1 92  ? 20.166  82.149  7.223   1.00 13.46 ? 92   ASP B N   1 
ATOM   1787  C  CA  . ASP B  1 92  ? 20.882  82.611  8.421   1.00 13.98 ? 92   ASP B CA  1 
ATOM   1788  C  C   . ASP B  1 92  ? 20.219  82.292  9.766   1.00 13.01 ? 92   ASP B C   1 
ATOM   1789  O  O   . ASP B  1 92  ? 20.697  82.721  10.825  1.00 13.32 ? 92   ASP B O   1 
ATOM   1790  C  CB  . ASP B  1 92  ? 21.102  84.111  8.336   1.00 14.54 ? 92   ASP B CB  1 
ATOM   1791  C  CG  . ASP B  1 92  ? 21.979  84.483  7.160   1.00 18.88 ? 92   ASP B CG  1 
ATOM   1792  O  OD1 . ASP B  1 92  ? 22.775  83.610  6.740   1.00 21.30 ? 92   ASP B OD1 1 
ATOM   1793  O  OD2 . ASP B  1 92  ? 21.905  85.585  6.578   1.00 22.62 ? 92   ASP B OD2 1 
ATOM   1794  N  N   . GLY B  1 93  ? 19.111  81.571  9.735   1.00 10.85 ? 93   GLY B N   1 
ATOM   1795  C  CA  . GLY B  1 93  ? 18.443  81.240  10.974  1.00 8.86  ? 93   GLY B CA  1 
ATOM   1796  C  C   . GLY B  1 93  ? 17.483  82.301  11.450  1.00 7.87  ? 93   GLY B C   1 
ATOM   1797  O  O   . GLY B  1 93  ? 16.992  82.225  12.589  1.00 7.03  ? 93   GLY B O   1 
ATOM   1798  N  N   . VAL B  1 94  ? 17.160  83.260  10.584  1.00 6.42  ? 94   VAL B N   1 
ATOM   1799  C  CA  . VAL B  1 94  ? 16.263  84.348  10.973  1.00 7.61  ? 94   VAL B CA  1 
ATOM   1800  C  C   . VAL B  1 94  ? 14.872  84.217  10.336  1.00 6.71  ? 94   VAL B C   1 
ATOM   1801  O  O   . VAL B  1 94  ? 14.761  84.080  9.128   1.00 7.02  ? 94   VAL B O   1 
ATOM   1802  C  CB  . VAL B  1 94  ? 16.876  85.729  10.611  1.00 7.25  ? 94   VAL B CB  1 
ATOM   1803  C  CG1 . VAL B  1 94  ? 15.945  86.859  11.019  1.00 10.42 ? 94   VAL B CG1 1 
ATOM   1804  C  CG2 . VAL B  1 94  ? 18.237  85.921  11.312  1.00 7.07  ? 94   VAL B CG2 1 
ATOM   1805  N  N   . ALA B  1 95  ? 13.837  84.243  11.177  1.00 5.24  ? 95   ALA B N   1 
ATOM   1806  C  CA  . ALA B  1 95  ? 12.446  84.223  10.757  1.00 6.75  ? 95   ALA B CA  1 
ATOM   1807  C  C   . ALA B  1 95  ? 11.866  85.616  10.914  1.00 7.26  ? 95   ALA B C   1 
ATOM   1808  O  O   . ALA B  1 95  ? 11.706  86.139  12.032  1.00 9.01  ? 95   ALA B O   1 
ATOM   1809  C  CB  . ALA B  1 95  ? 11.592  83.189  11.549  1.00 5.31  ? 95   ALA B CB  1 
ATOM   1810  N  N   . ASP B  1 96  ? 11.606  86.278  9.795   1.00 7.33  ? 96   ASP B N   1 
ATOM   1811  C  CA  . ASP B  1 96  ? 10.883  87.534  9.862   1.00 8.17  ? 96   ASP B CA  1 
ATOM   1812  C  C   . ASP B  1 96  ? 9.414   87.154  9.882   1.00 9.45  ? 96   ASP B C   1 
ATOM   1813  O  O   . ASP B  1 96  ? 8.899   86.481  8.958   1.00 10.92 ? 96   ASP B O   1 
ATOM   1814  C  CB  . ASP B  1 96  ? 11.298  88.429  8.686   1.00 10.90 ? 96   ASP B CB  1 
ATOM   1815  C  CG  . ASP B  1 96  ? 12.672  89.047  8.941   1.00 13.83 ? 96   ASP B CG  1 
ATOM   1816  O  OD1 . ASP B  1 96  ? 13.543  88.926  8.070   1.00 23.14 ? 96   ASP B OD1 1 
ATOM   1817  O  OD2 . ASP B  1 96  ? 13.003  89.598  10.055  1.00 20.65 ? 96   ASP B OD2 1 
ATOM   1818  N  N   . VAL B  1 97  ? 8.742   87.461  10.985  1.00 8.06  ? 97   VAL B N   1 
ATOM   1819  C  CA  . VAL B  1 97  ? 7.376   87.003  11.132  1.00 5.90  ? 97   VAL B CA  1 
ATOM   1820  C  C   . VAL B  1 97  ? 6.398   88.103  10.793  1.00 6.06  ? 97   VAL B C   1 
ATOM   1821  O  O   . VAL B  1 97  ? 6.593   89.253  11.217  1.00 6.36  ? 97   VAL B O   1 
ATOM   1822  C  CB  . VAL B  1 97  ? 7.123   86.521  12.600  1.00 6.40  ? 97   VAL B CB  1 
ATOM   1823  C  CG1 . VAL B  1 97  ? 5.643   86.159  12.815  1.00 5.66  ? 97   VAL B CG1 1 
ATOM   1824  C  CG2 . VAL B  1 97  ? 8.044   85.376  12.900  1.00 5.00  ? 97   VAL B CG2 1 
ATOM   1825  N  N   . SER B  1 98  ? 5.364   87.767  10.022  1.00 5.94  ? 98   SER B N   1 
ATOM   1826  C  CA  . SER B  1 98  ? 4.279   88.714  9.783   1.00 5.87  ? 98   SER B CA  1 
ATOM   1827  C  C   . SER B  1 98  ? 3.010   87.972  9.422   1.00 6.25  ? 98   SER B C   1 
ATOM   1828  O  O   . SER B  1 98  ? 2.885   87.408  8.334   1.00 6.79  ? 98   SER B O   1 
ATOM   1829  C  CB  . SER B  1 98  ? 4.639   89.778  8.702   1.00 5.68  ? 98   SER B CB  1 
ATOM   1830  O  OG  . SER B  1 98  ? 3.586   90.738  8.608   1.00 6.14  ? 98   SER B OG  1 
ATOM   1831  N  N   . ILE B  1 99  ? 2.057   87.961  10.341  1.00 5.57  ? 99   ILE B N   1 
ATOM   1832  C  CA  . ILE B  1 99  ? 0.846   87.194  10.163  1.00 7.18  ? 99   ILE B CA  1 
ATOM   1833  C  C   . ILE B  1 99  ? -0.309  88.092  10.526  1.00 7.80  ? 99   ILE B C   1 
ATOM   1834  O  O   . ILE B  1 99  ? -0.158  88.973  11.352  1.00 9.10  ? 99   ILE B O   1 
ATOM   1835  C  CB  . ILE B  1 99  ? 0.914   85.968  11.153  1.00 7.39  ? 99   ILE B CB  1 
ATOM   1836  C  CG1 . ILE B  1 99  ? 1.875   84.887  10.608  1.00 7.30  ? 99   ILE B CG1 1 
ATOM   1837  C  CG2 . ILE B  1 99  ? -0.460  85.337  11.429  1.00 10.17 ? 99   ILE B CG2 1 
ATOM   1838  C  CD1 . ILE B  1 99  ? 2.251   83.802  11.692  1.00 10.14 ? 99   ILE B CD1 1 
ATOM   1839  N  N   . GLU B  1 100 ? -1.451  87.897  9.885   1.00 7.27  ? 100  GLU B N   1 
ATOM   1840  C  CA  . GLU B  1 100 ? -2.649  88.584  10.319  1.00 8.59  ? 100  GLU B CA  1 
ATOM   1841  C  C   . GLU B  1 100 ? -3.638  87.461  10.677  1.00 7.98  ? 100  GLU B C   1 
ATOM   1842  O  O   . GLU B  1 100 ? -3.811  86.500  9.901   1.00 8.19  ? 100  GLU B O   1 
ATOM   1843  C  CB  . GLU B  1 100 ? -3.158  89.544  9.223   1.00 8.28  ? 100  GLU B CB  1 
ATOM   1844  C  CG  . GLU B  1 100 ? -4.340  90.381  9.683   1.00 14.02 ? 100  GLU B CG  1 
ATOM   1845  C  CD  . GLU B  1 100 ? -5.026  91.121  8.552   1.00 19.12 ? 100  GLU B CD  1 
ATOM   1846  O  OE1 . GLU B  1 100 ? -4.439  92.139  8.120   1.00 20.61 ? 100  GLU B OE1 1 
ATOM   1847  O  OE2 . GLU B  1 100 ? -6.141  90.687  8.112   1.00 20.07 ? 100  GLU B OE2 1 
ATOM   1848  N  N   . ASP B  1 101 ? -4.282  87.554  11.838  1.00 7.46  ? 101  ASP B N   1 
ATOM   1849  C  CA  . ASP B  1 101 ? -5.204  86.500  12.243  1.00 7.87  ? 101  ASP B CA  1 
ATOM   1850  C  C   . ASP B  1 101 ? -6.431  87.096  12.923  1.00 8.52  ? 101  ASP B C   1 
ATOM   1851  O  O   . ASP B  1 101 ? -6.319  88.025  13.742  1.00 6.59  ? 101  ASP B O   1 
ATOM   1852  C  CB  . ASP B  1 101 ? -4.508  85.503  13.189  1.00 7.75  ? 101  ASP B CB  1 
ATOM   1853  C  CG  . ASP B  1 101 ? -5.291  84.251  13.367  1.00 9.55  ? 101  ASP B CG  1 
ATOM   1854  O  OD1 . ASP B  1 101 ? -5.209  83.374  12.460  1.00 11.85 ? 101  ASP B OD1 1 
ATOM   1855  O  OD2 . ASP B  1 101 ? -6.056  84.057  14.341  1.00 9.01  ? 101  ASP B OD2 1 
ATOM   1856  N  N   . SER B  1 102 ? -7.589  86.546  12.596  1.00 7.32  ? 102  SER B N   1 
ATOM   1857  C  CA  . SER B  1 102 ? -8.843  87.053  13.122  1.00 9.30  ? 102  SER B CA  1 
ATOM   1858  C  C   . SER B  1 102 ? -9.491  86.153  14.146  1.00 8.92  ? 102  SER B C   1 
ATOM   1859  O  O   . SER B  1 102 ? -10.580 86.436  14.637  1.00 9.37  ? 102  SER B O   1 
ATOM   1860  C  CB  . SER B  1 102 ? -9.816  87.315  11.974  1.00 9.97  ? 102  SER B CB  1 
ATOM   1861  O  OG  . SER B  1 102 ? -9.524  88.594  11.477  1.00 12.76 ? 102  SER B OG  1 
ATOM   1862  N  N   . VAL B  1 103 ? -8.833  85.064  14.470  1.00 7.48  ? 103  VAL B N   1 
ATOM   1863  C  CA  . VAL B  1 103 ? -9.387  84.141  15.440  1.00 6.79  ? 103  VAL B CA  1 
ATOM   1864  C  C   . VAL B  1 103 ? -8.819  84.482  16.807  1.00 6.71  ? 103  VAL B C   1 
ATOM   1865  O  O   . VAL B  1 103 ? -9.562  84.537  17.796  1.00 6.77  ? 103  VAL B O   1 
ATOM   1866  C  CB  . VAL B  1 103 ? -9.119  82.682  15.044  1.00 7.24  ? 103  VAL B CB  1 
ATOM   1867  C  CG1 . VAL B  1 103 ? -9.575  81.722  16.177  1.00 6.80  ? 103  VAL B CG1 1 
ATOM   1868  C  CG2 . VAL B  1 103 ? -9.872  82.359  13.740  1.00 10.19 ? 103  VAL B CG2 1 
ATOM   1869  N  N   . ILE B  1 104 ? -7.511  84.728  16.879  1.00 6.01  ? 104  ILE B N   1 
ATOM   1870  C  CA  . ILE B  1 104 ? -6.985  85.195  18.156  1.00 6.21  ? 104  ILE B CA  1 
ATOM   1871  C  C   . ILE B  1 104 ? -7.522  86.616  18.388  1.00 6.92  ? 104  ILE B C   1 
ATOM   1872  O  O   . ILE B  1 104 ? -8.028  87.273  17.448  1.00 5.52  ? 104  ILE B O   1 
ATOM   1873  C  CB  . ILE B  1 104 ? -5.453  85.230  18.162  1.00 5.00  ? 104  ILE B CB  1 
ATOM   1874  C  CG1 . ILE B  1 104 ? -4.954  86.162  17.059  1.00 6.93  ? 104  ILE B CG1 1 
ATOM   1875  C  CG2 . ILE B  1 104 ? -4.864  83.811  18.034  1.00 5.78  ? 104  ILE B CG2 1 
ATOM   1876  C  CD1 . ILE B  1 104 ? -3.429  86.353  17.091  1.00 7.08  ? 104  ILE B CD1 1 
ATOM   1877  N  N   . SER B  1 105 ? -7.391  87.090  19.617  1.00 6.67  ? 105  SER B N   1 
ATOM   1878  C  CA  . SER B  1 105 ? -7.800  88.443  19.954  1.00 7.82  ? 105  SER B CA  1 
ATOM   1879  C  C   . SER B  1 105 ? -7.018  88.943  21.152  1.00 8.08  ? 105  SER B C   1 
ATOM   1880  O  O   . SER B  1 105 ? -6.424  88.128  21.922  1.00 8.43  ? 105  SER B O   1 
ATOM   1881  C  CB  . SER B  1 105 ? -9.326  88.523  20.205  1.00 7.40  ? 105  SER B CB  1 
ATOM   1882  O  OG  . SER B  1 105 ? -9.746  89.855  20.503  1.00 7.79  ? 105  SER B OG  1 
ATOM   1883  N  N   . LEU B  1 106 ? -6.935  90.270  21.260  1.00 8.20  ? 106  LEU B N   1 
ATOM   1884  C  CA  . LEU B  1 106 ? -6.279  90.898  22.406  1.00 10.42 ? 106  LEU B CA  1 
ATOM   1885  C  C   . LEU B  1 106 ? -7.317  91.345  23.459  1.00 11.84 ? 106  LEU B C   1 
ATOM   1886  O  O   . LEU B  1 106 ? -6.971  92.011  24.429  1.00 12.10 ? 106  LEU B O   1 
ATOM   1887  C  CB  . LEU B  1 106 ? -5.343  92.035  21.977  1.00 9.81  ? 106  LEU B CB  1 
ATOM   1888  C  CG  . LEU B  1 106 ? -4.242  91.657  20.975  1.00 10.45 ? 106  LEU B CG  1 
ATOM   1889  C  CD1 . LEU B  1 106 ? -3.273  92.830  20.729  1.00 8.03  ? 106  LEU B CD1 1 
ATOM   1890  C  CD2 . LEU B  1 106 ? -3.451  90.411  21.482  1.00 6.84  ? 106  LEU B CD2 1 
ATOM   1891  N  N   . SER B  1 107 ? -8.571  90.943  23.274  1.00 14.18 ? 107  SER B N   1 
ATOM   1892  C  CA  . SER B  1 107 ? -9.664  91.158  24.260  1.00 17.69 ? 107  SER B CA  1 
ATOM   1893  C  C   . SER B  1 107 ? -10.753 90.078  24.070  1.00 19.40 ? 107  SER B C   1 
ATOM   1894  O  O   . SER B  1 107 ? -10.780 89.431  23.029  1.00 19.16 ? 107  SER B O   1 
ATOM   1895  C  CB  . SER B  1 107 ? -10.267 92.553  24.124  1.00 17.65 ? 107  SER B CB  1 
ATOM   1896  O  OG  . SER B  1 107 ? -11.033 92.638  22.933  1.00 20.96 ? 107  SER B OG  1 
ATOM   1897  N  N   . GLY B  1 108 ? -11.598 89.826  25.082  1.00 21.55 ? 108  GLY B N   1 
ATOM   1898  C  CA  . GLY B  1 108 ? -12.679 88.843  24.938  1.00 23.53 ? 108  GLY B CA  1 
ATOM   1899  C  C   . GLY B  1 108 ? -12.421 87.378  25.317  1.00 25.27 ? 108  GLY B C   1 
ATOM   1900  O  O   . GLY B  1 108 ? -11.466 87.083  26.037  1.00 25.64 ? 108  GLY B O   1 
ATOM   1901  N  N   . ASP B  1 109 ? -13.275 86.461  24.829  1.00 26.07 ? 109  ASP B N   1 
ATOM   1902  C  CA  . ASP B  1 109 ? -13.189 85.003  25.111  1.00 26.39 ? 109  ASP B CA  1 
ATOM   1903  C  C   . ASP B  1 109 ? -11.970 84.359  24.407  1.00 25.19 ? 109  ASP B C   1 
ATOM   1904  O  O   . ASP B  1 109 ? -11.413 83.357  24.862  1.00 25.72 ? 109  ASP B O   1 
ATOM   1905  C  CB  . ASP B  1 109 ? -14.489 84.299  24.655  1.00 27.43 ? 109  ASP B CB  1 
ATOM   1906  C  CG  . ASP B  1 109 ? -14.947 83.161  25.601  1.00 31.10 ? 109  ASP B CG  1 
ATOM   1907  O  OD1 . ASP B  1 109 ? -15.779 83.426  26.508  1.00 34.41 ? 109  ASP B OD1 1 
ATOM   1908  O  OD2 . ASP B  1 109 ? -14.579 81.961  25.487  1.00 34.55 ? 109  ASP B OD2 1 
ATOM   1909  N  N   . HIS B  1 110 ? -11.555 84.936  23.287  1.00 22.92 ? 110  HIS B N   1 
ATOM   1910  C  CA  . HIS B  1 110 ? -10.401 84.398  22.581  1.00 20.09 ? 110  HIS B CA  1 
ATOM   1911  C  C   . HIS B  1 110 ? -9.129  85.163  22.905  1.00 16.34 ? 110  HIS B C   1 
ATOM   1912  O  O   . HIS B  1 110 ? -8.173  85.121  22.111  1.00 14.93 ? 110  HIS B O   1 
ATOM   1913  C  CB  . HIS B  1 110 ? -10.624 84.472  21.073  1.00 20.73 ? 110  HIS B CB  1 
ATOM   1914  C  CG  . HIS B  1 110 ? -11.577 83.444  20.553  1.00 23.88 ? 110  HIS B CG  1 
ATOM   1915  N  ND1 . HIS B  1 110 ? -11.620 83.077  19.223  1.00 27.81 ? 110  HIS B ND1 1 
ATOM   1916  C  CD2 . HIS B  1 110 ? -12.527 82.712  21.178  1.00 25.22 ? 110  HIS B CD2 1 
ATOM   1917  C  CE1 . HIS B  1 110 ? -12.554 82.157  19.054  1.00 27.00 ? 110  HIS B CE1 1 
ATOM   1918  N  NE2 . HIS B  1 110 ? -13.118 81.918  20.225  1.00 25.93 ? 110  HIS B NE2 1 
ATOM   1919  N  N   . CYS B  1 111 ? -9.122  85.863  24.035  1.00 13.36 ? 111  CYS B N   1 
ATOM   1920  C  CA  . CYS B  1 111 ? -8.015  86.742  24.380  1.00 12.33 ? 111  CYS B CA  1 
ATOM   1921  C  C   . CYS B  1 111 ? -6.727  85.946  24.721  1.00 9.54  ? 111  CYS B C   1 
ATOM   1922  O  O   . CYS B  1 111 ? -6.781  84.960  25.456  1.00 7.80  ? 111  CYS B O   1 
ATOM   1923  C  CB  . CYS B  1 111 ? -8.416  87.662  25.518  1.00 13.43 ? 111  CYS B CB  1 
ATOM   1924  S  SG  . CYS B  1 111 ? -7.143  88.828  25.936  1.00 20.93 ? 111  CYS B SG  1 
ATOM   1925  N  N   . ILE B  1 112 ? -5.597  86.382  24.177  1.00 6.81  ? 112  ILE B N   1 
ATOM   1926  C  CA  . ILE B  1 112 ? -4.344  85.643  24.367  1.00 6.25  ? 112  ILE B CA  1 
ATOM   1927  C  C   . ILE B  1 112 ? -3.351  86.345  25.297  1.00 5.75  ? 112  ILE B C   1 
ATOM   1928  O  O   . ILE B  1 112 ? -2.237  85.845  25.493  1.00 5.00  ? 112  ILE B O   1 
ATOM   1929  C  CB  . ILE B  1 112 ? -3.669  85.364  23.018  1.00 6.34  ? 112  ILE B CB  1 
ATOM   1930  C  CG1 . ILE B  1 112 ? -3.373  86.691  22.279  1.00 5.00  ? 112  ILE B CG1 1 
ATOM   1931  C  CG2 . ILE B  1 112 ? -4.551  84.430  22.157  1.00 5.83  ? 112  ILE B CG2 1 
ATOM   1932  C  CD1 . ILE B  1 112 ? -2.475  86.493  20.971  1.00 9.19  ? 112  ILE B CD1 1 
ATOM   1933  N  N   . ILE B  1 113 ? -3.729  87.511  25.823  1.00 5.00  ? 113  ILE B N   1 
ATOM   1934  C  CA  . ILE B  1 113 ? -2.866  88.176  26.791  1.00 6.09  ? 113  ILE B CA  1 
ATOM   1935  C  C   . ILE B  1 113 ? -2.682  87.261  27.999  1.00 5.11  ? 113  ILE B C   1 
ATOM   1936  O  O   . ILE B  1 113 ? -3.657  86.690  28.497  1.00 5.00  ? 113  ILE B O   1 
ATOM   1937  C  CB  . ILE B  1 113 ? -3.502  89.448  27.318  1.00 6.52  ? 113  ILE B CB  1 
ATOM   1938  C  CG1 . ILE B  1 113 ? -3.805  90.429  26.189  1.00 11.85 ? 113  ILE B CG1 1 
ATOM   1939  C  CG2 . ILE B  1 113 ? -2.579  90.095  28.393  1.00 6.53  ? 113  ILE B CG2 1 
ATOM   1940  C  CD1 . ILE B  1 113 ? -2.618  90.835  25.440  1.00 14.50 ? 113  ILE B CD1 1 
ATOM   1941  N  N   . GLY B  1 114 ? -1.446  87.103  28.475  1.00 5.00  ? 114  GLY B N   1 
ATOM   1942  C  CA  . GLY B  1 114 ? -1.259  86.272  29.662  1.00 5.00  ? 114  GLY B CA  1 
ATOM   1943  C  C   . GLY B  1 114 ? -1.063  84.806  29.298  1.00 5.15  ? 114  GLY B C   1 
ATOM   1944  O  O   . GLY B  1 114 ? -0.822  83.992  30.206  1.00 5.38  ? 114  GLY B O   1 
ATOM   1945  N  N   . ARG B  1 115 ? -1.124  84.476  28.002  1.00 5.00  ? 115  ARG B N   1 
ATOM   1946  C  CA  . ARG B  1 115 ? -0.871  83.100  27.540  1.00 5.13  ? 115  ARG B CA  1 
ATOM   1947  C  C   . ARG B  1 115 ? 0.536   82.994  26.983  1.00 5.00  ? 115  ARG B C   1 
ATOM   1948  O  O   . ARG B  1 115 ? 1.272   83.939  27.070  1.00 5.06  ? 115  ARG B O   1 
ATOM   1949  C  CB  . ARG B  1 115 ? -1.941  82.648  26.542  1.00 5.00  ? 115  ARG B CB  1 
ATOM   1950  C  CG  . ARG B  1 115 ? -3.315  82.787  27.251  1.00 5.68  ? 115  ARG B CG  1 
ATOM   1951  C  CD  . ARG B  1 115 ? -4.510  82.170  26.514  1.00 6.35  ? 115  ARG B CD  1 
ATOM   1952  N  NE  . ARG B  1 115 ? -5.787  82.475  27.190  1.00 6.99  ? 115  ARG B NE  1 
ATOM   1953  C  CZ  . ARG B  1 115 ? -6.340  81.747  28.154  1.00 7.40  ? 115  ARG B CZ  1 
ATOM   1954  N  NH1 . ARG B  1 115 ? -5.718  80.677  28.672  1.00 6.22  ? 115  ARG B NH1 1 
ATOM   1955  N  NH2 . ARG B  1 115 ? -7.525  82.101  28.658  1.00 7.85  ? 115  ARG B NH2 1 
ATOM   1956  N  N   . THR B  1 116 ? 0.944   81.847  26.454  1.00 5.00  ? 116  THR B N   1 
ATOM   1957  C  CA  . THR B  1 116 ? 2.349   81.715  26.028  1.00 5.00  ? 116  THR B CA  1 
ATOM   1958  C  C   . THR B  1 116 ? 2.483   81.519  24.528  1.00 5.07  ? 116  THR B C   1 
ATOM   1959  O  O   . THR B  1 116 ? 1.793   80.665  23.948  1.00 6.03  ? 116  THR B O   1 
ATOM   1960  C  CB  . THR B  1 116 ? 2.983   80.502  26.727  1.00 5.06  ? 116  THR B CB  1 
ATOM   1961  O  OG1 . THR B  1 116 ? 3.179   80.787  28.118  1.00 6.84  ? 116  THR B OG1 1 
ATOM   1962  C  CG2 . THR B  1 116 ? 4.366   80.211  26.177  1.00 6.68  ? 116  THR B CG2 1 
ATOM   1963  N  N   . LEU B  1 117 ? 3.377   82.277  23.905  1.00 5.00  ? 117  LEU B N   1 
ATOM   1964  C  CA  . LEU B  1 117 ? 3.660   82.062  22.485  1.00 5.00  ? 117  LEU B CA  1 
ATOM   1965  C  C   . LEU B  1 117 ? 4.877   81.120  22.418  1.00 5.00  ? 117  LEU B C   1 
ATOM   1966  O  O   . LEU B  1 117 ? 5.875   81.338  23.136  1.00 5.00  ? 117  LEU B O   1 
ATOM   1967  C  CB  . LEU B  1 117 ? 4.013   83.398  21.824  1.00 5.00  ? 117  LEU B CB  1 
ATOM   1968  C  CG  . LEU B  1 117 ? 4.363   83.345  20.319  1.00 5.00  ? 117  LEU B CG  1 
ATOM   1969  C  CD1 . LEU B  1 117 ? 3.094   82.990  19.561  1.00 5.00  ? 117  LEU B CD1 1 
ATOM   1970  C  CD2 . LEU B  1 117 ? 4.863   84.747  19.809  1.00 5.35  ? 117  LEU B CD2 1 
ATOM   1971  N  N   . VAL B  1 118 ? 4.808   80.118  21.550  1.00 5.00  ? 118  VAL B N   1 
ATOM   1972  C  CA  . VAL B  1 118 ? 5.863   79.098  21.433  1.00 5.00  ? 118  VAL B CA  1 
ATOM   1973  C  C   . VAL B  1 118 ? 6.288   78.965  19.984  1.00 5.00  ? 118  VAL B C   1 
ATOM   1974  O  O   . VAL B  1 118 ? 5.439   78.937  19.079  1.00 5.00  ? 118  VAL B O   1 
ATOM   1975  C  CB  . VAL B  1 118 ? 5.353   77.710  21.895  1.00 5.00  ? 118  VAL B CB  1 
ATOM   1976  C  CG1 . VAL B  1 118 ? 6.484   76.617  21.675  1.00 5.80  ? 118  VAL B CG1 1 
ATOM   1977  C  CG2 . VAL B  1 118 ? 4.867   77.833  23.351  1.00 5.00  ? 118  VAL B CG2 1 
ATOM   1978  N  N   . VAL B  1 119 ? 7.596   78.885  19.759  1.00 5.00  ? 119  VAL B N   1 
ATOM   1979  C  CA  . VAL B  1 119 ? 8.063   78.531  18.420  1.00 5.00  ? 119  VAL B CA  1 
ATOM   1980  C  C   . VAL B  1 119 ? 8.722   77.134  18.553  1.00 5.00  ? 119  VAL B C   1 
ATOM   1981  O  O   . VAL B  1 119 ? 9.451   76.851  19.518  1.00 5.00  ? 119  VAL B O   1 
ATOM   1982  C  CB  . VAL B  1 119 ? 9.050   79.561  17.835  1.00 5.00  ? 119  VAL B CB  1 
ATOM   1983  C  CG1 . VAL B  1 119 ? 10.321  79.698  18.745  1.00 5.00  ? 119  VAL B CG1 1 
ATOM   1984  C  CG2 . VAL B  1 119 ? 9.456   79.152  16.398  1.00 5.00  ? 119  VAL B CG2 1 
ATOM   1985  N  N   . HIS B  1 120 ? 8.455   76.264  17.582  1.00 5.00  ? 120  HIS B N   1 
ATOM   1986  C  CA  . HIS B  1 120 ? 8.834   74.853  17.698  1.00 5.00  ? 120  HIS B CA  1 
ATOM   1987  C  C   . HIS B  1 120 ? 10.003  74.369  16.878  1.00 5.06  ? 120  HIS B C   1 
ATOM   1988  O  O   . HIS B  1 120 ? 10.415  75.007  15.945  1.00 5.00  ? 120  HIS B O   1 
ATOM   1989  C  CB  . HIS B  1 120 ? 7.623   74.050  17.225  1.00 5.00  ? 120  HIS B CB  1 
ATOM   1990  C  CG  . HIS B  1 120 ? 6.541   73.969  18.241  1.00 5.70  ? 120  HIS B CG  1 
ATOM   1991  N  ND1 . HIS B  1 120 ? 6.518   73.000  19.225  1.00 5.00  ? 120  HIS B ND1 1 
ATOM   1992  C  CD2 . HIS B  1 120 ? 5.397   74.698  18.406  1.00 6.12  ? 120  HIS B CD2 1 
ATOM   1993  C  CE1 . HIS B  1 120 ? 5.429   73.147  19.971  1.00 5.00  ? 120  HIS B CE1 1 
ATOM   1994  N  NE2 . HIS B  1 120 ? 4.754   74.180  19.512  1.00 5.23  ? 120  HIS B NE2 1 
ATOM   1995  N  N   . GLU B  1 121 ? 10.459  73.176  17.208  1.00 5.00  ? 121  GLU B N   1 
ATOM   1996  C  CA  . GLU B  1 121 ? 11.573  72.503  16.565  1.00 5.43  ? 121  GLU B CA  1 
ATOM   1997  C  C   . GLU B  1 121 ? 11.349  72.200  15.085  1.00 6.10  ? 121  GLU B C   1 
ATOM   1998  O  O   . GLU B  1 121 ? 12.249  72.341  14.234  1.00 5.00  ? 121  GLU B O   1 
ATOM   1999  C  CB  . GLU B  1 121 ? 11.737  71.193  17.336  1.00 6.48  ? 121  GLU B CB  1 
ATOM   2000  C  CG  . GLU B  1 121 ? 12.717  70.177  16.754  1.00 9.28  ? 121  GLU B CG  1 
ATOM   2001  C  CD  . GLU B  1 121 ? 12.550  68.767  17.363  1.00 15.13 ? 121  GLU B CD  1 
ATOM   2002  O  OE1 . GLU B  1 121 ? 13.412  67.930  17.052  1.00 16.52 ? 121  GLU B OE1 1 
ATOM   2003  O  OE2 . GLU B  1 121 ? 11.563  68.460  18.108  1.00 12.16 ? 121  GLU B OE2 1 
ATOM   2004  N  N   . LYS B  1 122 ? 10.131  71.762  14.806  1.00 5.88  ? 122  LYS B N   1 
ATOM   2005  C  CA  . LYS B  1 122 ? 9.758   71.261  13.491  1.00 7.20  ? 122  LYS B CA  1 
ATOM   2006  C  C   . LYS B  1 122 ? 8.599   72.009  12.859  1.00 5.93  ? 122  LYS B C   1 
ATOM   2007  O  O   . LYS B  1 122 ? 7.921   72.811  13.500  1.00 5.56  ? 122  LYS B O   1 
ATOM   2008  C  CB  . LYS B  1 122 ? 9.318   69.788  13.665  1.00 6.96  ? 122  LYS B CB  1 
ATOM   2009  C  CG  . LYS B  1 122 ? 10.420  68.893  14.124  1.00 14.14 ? 122  LYS B CG  1 
ATOM   2010  C  CD  . LYS B  1 122 ? 9.858   67.471  14.083  1.00 23.40 ? 122  LYS B CD  1 
ATOM   2011  C  CE  . LYS B  1 122 ? 10.733  66.503  14.825  1.00 26.27 ? 122  LYS B CE  1 
ATOM   2012  N  NZ  . LYS B  1 122 ? 10.276  65.129  14.436  1.00 32.69 ? 122  LYS B NZ  1 
ATOM   2013  N  N   . ALA B  1 123 ? 8.341   71.705  11.596  1.00 5.67  ? 123  ALA B N   1 
ATOM   2014  C  CA  . ALA B  1 123 ? 7.175   72.300  10.953  1.00 6.71  ? 123  ALA B CA  1 
ATOM   2015  C  C   . ALA B  1 123 ? 5.874   71.733  11.572  1.00 5.24  ? 123  ALA B C   1 
ATOM   2016  O  O   . ALA B  1 123 ? 5.790   70.527  11.946  1.00 6.06  ? 123  ALA B O   1 
ATOM   2017  C  CB  . ALA B  1 123 ? 7.210   71.997  9.451   1.00 7.56  ? 123  ALA B CB  1 
ATOM   2018  N  N   . ASP B  1 124 ? 4.874   72.591  11.692  1.00 5.04  ? 124  ASP B N   1 
ATOM   2019  C  CA  . ASP B  1 124 ? 3.519   72.148  12.041  1.00 5.01  ? 124  ASP B CA  1 
ATOM   2020  C  C   . ASP B  1 124 ? 2.897   71.545  10.750  1.00 5.68  ? 124  ASP B C   1 
ATOM   2021  O  O   . ASP B  1 124 ? 2.844   72.244  9.726   1.00 5.29  ? 124  ASP B O   1 
ATOM   2022  C  CB  . ASP B  1 124 ? 2.761   73.436  12.389  1.00 5.03  ? 124  ASP B CB  1 
ATOM   2023  C  CG  . ASP B  1 124 ? 1.342   73.209  12.884  1.00 5.68  ? 124  ASP B CG  1 
ATOM   2024  O  OD1 . ASP B  1 124 ? 0.653   72.216  12.496  1.00 5.00  ? 124  ASP B OD1 1 
ATOM   2025  O  OD2 . ASP B  1 124 ? 0.840   74.044  13.681  1.00 6.68  ? 124  ASP B OD2 1 
ATOM   2026  N  N   . ASP B  1 125 ? 2.436   70.280  10.783  1.00 5.00  ? 125  ASP B N   1 
ATOM   2027  C  CA  . ASP B  1 125 ? 1.818   69.648  9.603   1.00 5.00  ? 125  ASP B CA  1 
ATOM   2028  C  C   . ASP B  1 125 ? 0.360   70.064  9.294   1.00 5.00  ? 125  ASP B C   1 
ATOM   2029  O  O   . ASP B  1 125 ? -0.280  69.552  8.356   1.00 5.00  ? 125  ASP B O   1 
ATOM   2030  C  CB  . ASP B  1 125 ? 1.967   68.118  9.644   1.00 5.00  ? 125  ASP B CB  1 
ATOM   2031  C  CG  . ASP B  1 125 ? 1.185   67.459  10.781  1.00 5.00  ? 125  ASP B CG  1 
ATOM   2032  O  OD1 . ASP B  1 125 ? 0.203   68.016  11.290  1.00 5.00  ? 125  ASP B OD1 1 
ATOM   2033  O  OD2 . ASP B  1 125 ? 1.510   66.303  11.217  1.00 6.03  ? 125  ASP B OD2 1 
ATOM   2034  N  N   . LEU B  1 126 ? -0.151  70.972  10.122  1.00 5.00  ? 126  LEU B N   1 
ATOM   2035  C  CA  . LEU B  1 126 ? -1.460  71.567  9.957   1.00 5.00  ? 126  LEU B CA  1 
ATOM   2036  C  C   . LEU B  1 126 ? -2.592  70.537  10.027  1.00 5.00  ? 126  LEU B C   1 
ATOM   2037  O  O   . LEU B  1 126 ? -3.671  70.727  9.447   1.00 5.09  ? 126  LEU B O   1 
ATOM   2038  C  CB  . LEU B  1 126 ? -1.557  72.402  8.663   1.00 5.52  ? 126  LEU B CB  1 
ATOM   2039  C  CG  . LEU B  1 126 ? -0.358  73.325  8.362   1.00 6.61  ? 126  LEU B CG  1 
ATOM   2040  C  CD1 . LEU B  1 126 ? -0.633  74.193  7.110   1.00 7.87  ? 126  LEU B CD1 1 
ATOM   2041  C  CD2 . LEU B  1 126 ? -0.105  74.263  9.569   1.00 6.60  ? 126  LEU B CD2 1 
ATOM   2042  N  N   . GLY B  1 127 ? -2.349  69.479  10.791  1.00 5.00  ? 127  GLY B N   1 
ATOM   2043  C  CA  . GLY B  1 127 ? -3.336  68.429  10.976  1.00 5.00  ? 127  GLY B CA  1 
ATOM   2044  C  C   . GLY B  1 127 ? -3.397  67.382  9.877   1.00 5.28  ? 127  GLY B C   1 
ATOM   2045  O  O   . GLY B  1 127 ? -4.313  66.529  9.858   1.00 5.00  ? 127  GLY B O   1 
ATOM   2046  N  N   . LYS B  1 128 ? -2.423  67.389  8.985   1.00 5.00  ? 128  LYS B N   1 
ATOM   2047  C  CA  . LYS B  1 128 ? -2.459  66.486  7.812   1.00 5.05  ? 128  LYS B CA  1 
ATOM   2048  C  C   . LYS B  1 128 ? -1.442  65.346  7.929   1.00 5.00  ? 128  LYS B C   1 
ATOM   2049  O  O   . LYS B  1 128 ? -1.097  64.704  6.931   1.00 5.00  ? 128  LYS B O   1 
ATOM   2050  C  CB  . LYS B  1 128 ? -2.156  67.314  6.573   1.00 5.00  ? 128  LYS B CB  1 
ATOM   2051  C  CG  . LYS B  1 128 ? -3.232  68.419  6.311   1.00 8.88  ? 128  LYS B CG  1 
ATOM   2052  C  CD  . LYS B  1 128 ? -2.930  69.230  4.999   1.00 13.67 ? 128  LYS B CD  1 
ATOM   2053  C  CE  . LYS B  1 128 ? -3.386  68.431  3.781   1.00 18.47 ? 128  LYS B CE  1 
ATOM   2054  N  NZ  . LYS B  1 128 ? -3.729  69.269  2.603   1.00 22.67 ? 128  LYS B NZ  1 
ATOM   2055  N  N   . GLY B  1 129 ? -1.001  65.070  9.151   1.00 5.00  ? 129  GLY B N   1 
ATOM   2056  C  CA  . GLY B  1 129 ? 0.034   64.069  9.333   1.00 5.70  ? 129  GLY B CA  1 
ATOM   2057  C  C   . GLY B  1 129 ? -0.418  62.612  9.530   1.00 5.98  ? 129  GLY B C   1 
ATOM   2058  O  O   . GLY B  1 129 ? 0.427   61.738  9.627   1.00 5.10  ? 129  GLY B O   1 
ATOM   2059  N  N   . GLY B  1 130 ? -1.718  62.356  9.641   1.00 5.00  ? 130  GLY B N   1 
ATOM   2060  C  CA  . GLY B  1 130 ? -2.175  60.964  9.692   1.00 5.00  ? 130  GLY B CA  1 
ATOM   2061  C  C   . GLY B  1 130 ? -1.966  60.219  11.009  1.00 6.53  ? 130  GLY B C   1 
ATOM   2062  O  O   . GLY B  1 130 ? -2.090  59.008  11.050  1.00 6.53  ? 130  GLY B O   1 
ATOM   2063  N  N   . ASN B  1 131 ? -1.597  60.939  12.066  1.00 7.70  ? 131  ASN B N   1 
ATOM   2064  C  CA  . ASN B  1 131 ? -1.537  60.346  13.402  1.00 8.45  ? 131  ASN B CA  1 
ATOM   2065  C  C   . ASN B  1 131 ? -2.386  61.124  14.384  1.00 9.77  ? 131  ASN B C   1 
ATOM   2066  O  O   . ASN B  1 131 ? -2.906  62.212  14.079  1.00 8.61  ? 131  ASN B O   1 
ATOM   2067  C  CB  . ASN B  1 131 ? -0.107  60.092  13.893  1.00 8.92  ? 131  ASN B CB  1 
ATOM   2068  C  CG  . ASN B  1 131 ? 0.724   61.347  13.982  1.00 10.15 ? 131  ASN B CG  1 
ATOM   2069  O  OD1 . ASN B  1 131 ? 0.242   62.445  13.684  1.00 10.57 ? 131  ASN B OD1 1 
ATOM   2070  N  ND2 . ASN B  1 131 ? 1.992   61.188  14.383  1.00 11.46 ? 131  ASN B ND2 1 
ATOM   2071  N  N   . GLU B  1 132 ? -2.560  60.591  15.593  1.00 10.51 ? 132  GLU B N   1 
ATOM   2072  C  CA  . GLU B  1 132 ? -3.351  61.354  16.532  1.00 12.28 ? 132  GLU B CA  1 
ATOM   2073  C  C   . GLU B  1 132 ? -2.613  62.606  16.927  1.00 11.00 ? 132  GLU B C   1 
ATOM   2074  O  O   . GLU B  1 132 ? -3.238  63.633  17.196  1.00 11.42 ? 132  GLU B O   1 
ATOM   2075  C  CB  . GLU B  1 132 ? -3.675  60.549  17.794  1.00 13.77 ? 132  GLU B CB  1 
ATOM   2076  C  CG  . GLU B  1 132 ? -4.791  61.220  18.586  1.00 20.79 ? 132  GLU B CG  1 
ATOM   2077  C  CD  . GLU B  1 132 ? -6.146  61.148  17.889  1.00 27.09 ? 132  GLU B CD  1 
ATOM   2078  O  OE1 . GLU B  1 132 ? -6.359  60.253  17.032  1.00 31.60 ? 132  GLU B OE1 1 
ATOM   2079  O  OE2 . GLU B  1 132 ? -7.012  61.997  18.201  1.00 32.36 ? 132  GLU B OE2 1 
ATOM   2080  N  N   . GLU B  1 133 ? -1.282  62.541  16.979  1.00 9.50  ? 133  GLU B N   1 
ATOM   2081  C  CA  . GLU B  1 133 ? -0.533  63.718  17.372  1.00 10.36 ? 133  GLU B CA  1 
ATOM   2082  C  C   . GLU B  1 133 ? -0.790  64.894  16.392  1.00 9.86  ? 133  GLU B C   1 
ATOM   2083  O  O   . GLU B  1 133 ? -0.769  66.077  16.794  1.00 10.80 ? 133  GLU B O   1 
ATOM   2084  C  CB  . GLU B  1 133 ? 0.963   63.405  17.402  1.00 10.56 ? 133  GLU B CB  1 
ATOM   2085  C  CG  . GLU B  1 133 ? 1.832   64.491  17.971  1.00 13.14 ? 133  GLU B CG  1 
ATOM   2086  C  CD  . GLU B  1 133 ? 1.544   64.781  19.442  1.00 19.68 ? 133  GLU B CD  1 
ATOM   2087  O  OE1 . GLU B  1 133 ? 1.147   63.850  20.184  1.00 16.83 ? 133  GLU B OE1 1 
ATOM   2088  O  OE2 . GLU B  1 133 ? 1.728   65.955  19.841  1.00 20.58 ? 133  GLU B OE2 1 
ATOM   2089  N  N   . SER B  1 134 ? -1.027  64.576  15.129  1.00 8.61  ? 134  SER B N   1 
ATOM   2090  C  CA  . SER B  1 134 ? -1.231  65.639  14.134  1.00 7.02  ? 134  SER B CA  1 
ATOM   2091  C  C   . SER B  1 134 ? -2.449  66.489  14.488  1.00 7.25  ? 134  SER B C   1 
ATOM   2092  O  O   . SER B  1 134 ? -2.419  67.716  14.293  1.00 6.03  ? 134  SER B O   1 
ATOM   2093  C  CB  . SER B  1 134 ? -1.387  65.060  12.714  1.00 5.57  ? 134  SER B CB  1 
ATOM   2094  O  OG  . SER B  1 134 ? -1.622  66.100  11.765  1.00 5.02  ? 134  SER B OG  1 
ATOM   2095  N  N   . THR B  1 135 ? -3.486  65.853  15.029  1.00 6.62  ? 135  THR B N   1 
ATOM   2096  C  CA  . THR B  1 135 ? -4.741  66.516  15.387  1.00 7.37  ? 135  THR B CA  1 
ATOM   2097  C  C   . THR B  1 135 ? -4.641  67.231  16.699  1.00 7.62  ? 135  THR B C   1 
ATOM   2098  O  O   . THR B  1 135 ? -5.627  67.845  17.127  1.00 7.98  ? 135  THR B O   1 
ATOM   2099  C  CB  . THR B  1 135 ? -5.941  65.497  15.514  1.00 9.01  ? 135  THR B CB  1 
ATOM   2100  O  OG1 . THR B  1 135 ? -5.879  64.875  16.803  1.00 13.00 ? 135  THR B OG1 1 
ATOM   2101  C  CG2 . THR B  1 135 ? -5.744  64.359  14.649  1.00 9.17  ? 135  THR B CG2 1 
ATOM   2102  N  N   . LYS B  1 136 ? -3.489  67.143  17.349  1.00 7.04  ? 136  LYS B N   1 
ATOM   2103  C  CA  . LYS B  1 136 ? -3.280  67.829  18.623  1.00 8.93  ? 136  LYS B CA  1 
ATOM   2104  C  C   . LYS B  1 136 ? -2.262  68.960  18.551  1.00 9.22  ? 136  LYS B C   1 
ATOM   2105  O  O   . LYS B  1 136 ? -2.517  70.057  19.026  1.00 8.69  ? 136  LYS B O   1 
ATOM   2106  C  CB  . LYS B  1 136 ? -2.791  66.829  19.704  1.00 10.17 ? 136  LYS B CB  1 
ATOM   2107  C  CG  . LYS B  1 136 ? -3.725  65.673  19.932  1.00 13.28 ? 136  LYS B CG  1 
ATOM   2108  C  CD  . LYS B  1 136 ? -3.191  64.778  21.067  1.00 18.36 ? 136  LYS B CD  1 
ATOM   2109  C  CE  . LYS B  1 136 ? -4.113  63.620  21.367  1.00 22.50 ? 136  LYS B CE  1 
ATOM   2110  N  NZ  . LYS B  1 136 ? -3.522  62.908  22.552  1.00 26.20 ? 136  LYS B NZ  1 
ATOM   2111  N  N   . THR B  1 137 ? -1.092  68.689  17.978  1.00 9.13  ? 137  THR B N   1 
ATOM   2112  C  CA  . THR B  1 137 ? -0.002  69.663  17.954  1.00 9.32  ? 137  THR B CA  1 
ATOM   2113  C  C   . THR B  1 137 ? 0.583   69.857  16.583  1.00 8.49  ? 137  THR B C   1 
ATOM   2114  O  O   . THR B  1 137 ? 1.496   70.678  16.388  1.00 9.09  ? 137  THR B O   1 
ATOM   2115  C  CB  . THR B  1 137 ? 1.169   69.154  18.826  1.00 10.27 ? 137  THR B CB  1 
ATOM   2116  O  OG1 . THR B  1 137 ? 1.739   67.993  18.194  1.00 8.82  ? 137  THR B OG1 1 
ATOM   2117  C  CG2 . THR B  1 137 ? 0.664   68.622  20.143  1.00 12.36 ? 137  THR B CG2 1 
ATOM   2118  N  N   . GLY B  1 138 ? 0.109   69.102  15.600  1.00 7.35  ? 138  GLY B N   1 
ATOM   2119  C  CA  . GLY B  1 138 ? 0.697   69.197  14.280  1.00 5.57  ? 138  GLY B CA  1 
ATOM   2120  C  C   . GLY B  1 138 ? 2.073   68.558  14.138  1.00 5.00  ? 138  GLY B C   1 
ATOM   2121  O  O   . GLY B  1 138 ? 2.734   68.815  13.160  1.00 5.00  ? 138  GLY B O   1 
ATOM   2122  N  N   . ASN B  1 139 ? 2.491   67.726  15.110  1.00 5.16  ? 139  ASN B N   1 
ATOM   2123  C  CA  . ASN B  1 139 ? 3.790   67.089  15.114  1.00 5.00  ? 139  ASN B CA  1 
ATOM   2124  C  C   . ASN B  1 139 ? 4.930   68.098  15.025  1.00 6.06  ? 139  ASN B C   1 
ATOM   2125  O  O   . ASN B  1 139 ? 5.943   67.815  14.440  1.00 6.33  ? 139  ASN B O   1 
ATOM   2126  C  CB  . ASN B  1 139 ? 3.901   66.112  13.937  1.00 5.41  ? 139  ASN B CB  1 
ATOM   2127  C  CG  . ASN B  1 139 ? 3.064   64.893  14.153  1.00 6.62  ? 139  ASN B CG  1 
ATOM   2128  O  OD1 . ASN B  1 139 ? 3.349   64.115  15.056  1.00 6.84  ? 139  ASN B OD1 1 
ATOM   2129  N  ND2 . ASN B  1 139 ? 1.999   64.726  13.362  1.00 5.00  ? 139  ASN B ND2 1 
ATOM   2130  N  N   . ALA B  1 140 ? 4.744   69.266  15.618  1.00 5.26  ? 140  ALA B N   1 
ATOM   2131  C  CA  . ALA B  1 140 ? 5.741   70.314  15.558  1.00 5.00  ? 140  ALA B CA  1 
ATOM   2132  C  C   . ALA B  1 140 ? 6.925   70.101  16.509  1.00 5.53  ? 140  ALA B C   1 
ATOM   2133  O  O   . ALA B  1 140 ? 7.911   70.848  16.468  1.00 5.00  ? 140  ALA B O   1 
ATOM   2134  C  CB  . ALA B  1 140 ? 5.073   71.672  15.797  1.00 5.42  ? 140  ALA B CB  1 
ATOM   2135  N  N   . GLY B  1 141 ? 6.825   69.094  17.377  1.00 5.45  ? 141  GLY B N   1 
ATOM   2136  C  CA  . GLY B  1 141 ? 8.017   68.708  18.127  1.00 5.42  ? 141  GLY B CA  1 
ATOM   2137  C  C   . GLY B  1 141 ? 8.252   69.636  19.301  1.00 5.35  ? 141  GLY B C   1 
ATOM   2138  O  O   . GLY B  1 141 ? 7.340   70.298  19.825  1.00 5.00  ? 141  GLY B O   1 
ATOM   2139  N  N   . SER B  1 142 ? 9.509   69.689  19.730  1.00 7.08  ? 142  SER B N   1 
ATOM   2140  C  CA  . SER B  1 142 ? 9.794   70.391  20.965  1.00 6.88  ? 142  SER B CA  1 
ATOM   2141  C  C   . SER B  1 142 ? 9.626   71.906  20.891  1.00 7.15  ? 142  SER B C   1 
ATOM   2142  O  O   . SER B  1 142 ? 9.582   72.512  19.814  1.00 7.82  ? 142  SER B O   1 
ATOM   2143  C  CB  . SER B  1 142 ? 11.228  70.035  21.454  1.00 7.75  ? 142  SER B CB  1 
ATOM   2144  O  OG  . SER B  1 142 ? 12.182  70.652  20.614  1.00 9.04  ? 142  SER B OG  1 
ATOM   2145  N  N   . ARG B  1 143 ? 9.607   72.516  22.062  1.00 5.00  ? 143  ARG B N   1 
ATOM   2146  C  CA  . ARG B  1 143 ? 9.340   73.945  22.199  1.00 5.41  ? 143  ARG B CA  1 
ATOM   2147  C  C   . ARG B  1 143 ? 10.697  74.608  22.321  1.00 5.05  ? 143  ARG B C   1 
ATOM   2148  O  O   . ARG B  1 143 ? 11.371  74.416  23.328  1.00 6.98  ? 143  ARG B O   1 
ATOM   2149  C  CB  . ARG B  1 143 ? 8.514   74.151  23.459  1.00 5.00  ? 143  ARG B CB  1 
ATOM   2150  C  CG  . ARG B  1 143 ? 7.178   73.343  23.366  1.00 5.00  ? 143  ARG B CG  1 
ATOM   2151  C  CD  . ARG B  1 143 ? 6.283   73.478  24.616  1.00 7.06  ? 143  ARG B CD  1 
ATOM   2152  N  NE  . ARG B  1 143 ? 5.102   72.621  24.454  1.00 7.03  ? 143  ARG B NE  1 
ATOM   2153  C  CZ  . ARG B  1 143 ? 4.110   72.521  25.324  1.00 8.96  ? 143  ARG B CZ  1 
ATOM   2154  N  NH1 . ARG B  1 143 ? 4.121   73.244  26.443  1.00 6.06  ? 143  ARG B NH1 1 
ATOM   2155  N  NH2 . ARG B  1 143 ? 3.093   71.717  25.050  1.00 5.00  ? 143  ARG B NH2 1 
ATOM   2156  N  N   . LEU B  1 144 ? 11.143  75.289  21.274  1.00 5.00  ? 144  LEU B N   1 
ATOM   2157  C  CA  . LEU B  1 144 ? 12.507  75.828  21.307  1.00 5.00  ? 144  LEU B CA  1 
ATOM   2158  C  C   . LEU B  1 144 ? 12.622  77.117  22.101  1.00 5.00  ? 144  LEU B C   1 
ATOM   2159  O  O   . LEU B  1 144 ? 13.662  77.384  22.677  1.00 5.00  ? 144  LEU B O   1 
ATOM   2160  C  CB  . LEU B  1 144 ? 13.026  76.140  19.917  1.00 5.44  ? 144  LEU B CB  1 
ATOM   2161  C  CG  . LEU B  1 144 ? 13.112  74.887  19.055  1.00 8.95  ? 144  LEU B CG  1 
ATOM   2162  C  CD1 . LEU B  1 144 ? 13.774  75.281  17.769  1.00 10.90 ? 144  LEU B CD1 1 
ATOM   2163  C  CD2 . LEU B  1 144 ? 13.857  73.782  19.774  1.00 9.90  ? 144  LEU B CD2 1 
ATOM   2164  N  N   . ALA B  1 145 ? 11.600  77.953  22.027  1.00 5.00  ? 145  ALA B N   1 
ATOM   2165  C  CA  . ALA B  1 145 ? 11.581  79.219  22.785  1.00 5.06  ? 145  ALA B CA  1 
ATOM   2166  C  C   . ALA B  1 145 ? 10.125  79.643  23.018  1.00 5.00  ? 145  ALA B C   1 
ATOM   2167  O  O   . ALA B  1 145 ? 9.227   79.226  22.287  1.00 5.00  ? 145  ALA B O   1 
ATOM   2168  C  CB  . ALA B  1 145 ? 12.380  80.347  22.087  1.00 5.00  ? 145  ALA B CB  1 
ATOM   2169  N  N   . CYS B  1 146 ? 9.889   80.414  24.068  1.00 5.00  ? 146  CYS B N   1 
ATOM   2170  C  CA  . CYS B  1 146 ? 8.546   80.804  24.407  1.00 5.00  ? 146  CYS B CA  1 
ATOM   2171  C  C   . CYS B  1 146 ? 8.606   82.022  25.272  1.00 5.00  ? 146  CYS B C   1 
ATOM   2172  O  O   . CYS B  1 146 ? 9.666   82.420  25.768  1.00 5.00  ? 146  CYS B O   1 
ATOM   2173  C  CB  . CYS B  1 146 ? 7.755   79.690  25.155  1.00 5.47  ? 146  CYS B CB  1 
ATOM   2174  S  SG  . CYS B  1 146 ? 8.525   79.264  26.727  1.00 8.32  ? 146  CYS B SG  1 
ATOM   2175  N  N   . GLY B  1 147 ? 7.464   82.653  25.422  1.00 5.00  ? 147  GLY B N   1 
ATOM   2176  C  CA  . GLY B  1 147 ? 7.375   83.764  26.376  1.00 5.00  ? 147  GLY B CA  1 
ATOM   2177  C  C   . GLY B  1 147 ? 5.923   84.060  26.692  1.00 5.00  ? 147  GLY B C   1 
ATOM   2178  O  O   . GLY B  1 147 ? 5.053   83.625  25.964  1.00 5.00  ? 147  GLY B O   1 
ATOM   2179  N  N   . VAL B  1 148 ? 5.653   84.838  27.743  1.00 5.00  ? 148  VAL B N   1 
ATOM   2180  C  CA  . VAL B  1 148 ? 4.273   85.167  28.072  1.00 5.00  ? 148  VAL B CA  1 
ATOM   2181  C  C   . VAL B  1 148 ? 3.891   86.425  27.282  1.00 5.00  ? 148  VAL B C   1 
ATOM   2182  O  O   . VAL B  1 148 ? 4.690   87.378  27.148  1.00 5.49  ? 148  VAL B O   1 
ATOM   2183  C  CB  . VAL B  1 148 ? 4.094   85.449  29.591  1.00 5.10  ? 148  VAL B CB  1 
ATOM   2184  C  CG1 . VAL B  1 148 ? 2.585   85.701  29.915  1.00 5.00  ? 148  VAL B CG1 1 
ATOM   2185  C  CG2 . VAL B  1 148 ? 4.624   84.269  30.395  1.00 5.00  ? 148  VAL B CG2 1 
ATOM   2186  N  N   . ILE B  1 149 ? 2.691   86.426  26.724  1.00 5.39  ? 149  ILE B N   1 
ATOM   2187  C  CA  . ILE B  1 149 ? 2.220   87.561  25.949  1.00 5.00  ? 149  ILE B CA  1 
ATOM   2188  C  C   . ILE B  1 149 ? 1.780   88.657  26.914  1.00 5.62  ? 149  ILE B C   1 
ATOM   2189  O  O   . ILE B  1 149 ? 0.843   88.466  27.701  1.00 5.97  ? 149  ILE B O   1 
ATOM   2190  C  CB  . ILE B  1 149 ? 1.084   87.128  25.013  1.00 6.01  ? 149  ILE B CB  1 
ATOM   2191  C  CG1 . ILE B  1 149 ? 1.635   86.053  24.077  1.00 5.00  ? 149  ILE B CG1 1 
ATOM   2192  C  CG2 . ILE B  1 149 ? 0.547   88.352  24.228  1.00 5.00  ? 149  ILE B CG2 1 
ATOM   2193  C  CD1 . ILE B  1 149 ? 0.498   85.229  23.343  1.00 5.11  ? 149  ILE B CD1 1 
ATOM   2194  N  N   . GLY B  1 150 ? 2.440   89.815  26.817  1.00 5.00  ? 150  GLY B N   1 
ATOM   2195  C  CA  . GLY B  1 150 ? 2.199   90.887  27.787  1.00 5.00  ? 150  GLY B CA  1 
ATOM   2196  C  C   . GLY B  1 150 ? 1.603   92.129  27.156  1.00 5.23  ? 150  GLY B C   1 
ATOM   2197  O  O   . GLY B  1 150 ? 1.757   92.346  25.955  1.00 5.00  ? 150  GLY B O   1 
ATOM   2198  N  N   . ILE B  1 151 ? 0.885   92.926  27.961  1.00 5.00  ? 151  ILE B N   1 
ATOM   2199  C  CA  . ILE B  1 151 ? 0.327   94.210  27.500  1.00 5.45  ? 151  ILE B CA  1 
ATOM   2200  C  C   . ILE B  1 151 ? 1.430   95.196  27.185  1.00 5.13  ? 151  ILE B C   1 
ATOM   2201  O  O   . ILE B  1 151 ? 2.344   95.365  27.993  1.00 6.25  ? 151  ILE B O   1 
ATOM   2202  C  CB  . ILE B  1 151 ? -0.582  94.800  28.611  1.00 5.02  ? 151  ILE B CB  1 
ATOM   2203  C  CG1 . ILE B  1 151 ? -1.816  93.907  28.781  1.00 6.11  ? 151  ILE B CG1 1 
ATOM   2204  C  CG2 . ILE B  1 151 ? -1.090  96.213  28.233  1.00 6.86  ? 151  ILE B CG2 1 
ATOM   2205  C  CD1 . ILE B  1 151 ? -2.617  94.172  30.072  1.00 7.93  ? 151  ILE B CD1 1 
ATOM   2206  N  N   . ALA B  1 152 ? 1.361   95.845  26.014  1.00 5.56  ? 152  ALA B N   1 
ATOM   2207  C  CA  . ALA B  1 152 ? 2.409   96.766  25.619  1.00 7.00  ? 152  ALA B CA  1 
ATOM   2208  C  C   . ALA B  1 152 ? 1.855   98.170  25.493  1.00 7.90  ? 152  ALA B C   1 
ATOM   2209  O  O   . ALA B  1 152 ? 0.662   98.346  25.332  1.00 6.01  ? 152  ALA B O   1 
ATOM   2210  C  CB  . ALA B  1 152 ? 3.017   96.324  24.238  1.00 6.62  ? 152  ALA B CB  1 
ATOM   2211  N  N   . GLN B  1 153 ? 2.732   99.156  25.567  1.00 9.55  ? 153  GLN B N   1 
ATOM   2212  C  CA  . GLN B  1 153 ? 2.316   100.559 25.454  1.00 12.02 ? 153  GLN B CA  1 
ATOM   2213  C  C   . GLN B  1 153 ? 1.825   100.923 24.053  1.00 14.38 ? 153  GLN B C   1 
ATOM   2214  O  O   . GLN B  1 153 ? 2.413   100.552 23.046  1.00 16.09 ? 153  GLN B O   1 
ATOM   2215  C  CB  . GLN B  1 153 ? 3.489   101.448 25.849  1.00 12.35 ? 153  GLN B CB  1 
ATOM   2216  C  CG  . GLN B  1 153 ? 3.196   102.957 25.825  1.00 14.91 ? 153  GLN B CG  1 
ATOM   2217  C  CD  . GLN B  1 153 ? 4.330   103.759 26.441  1.00 18.62 ? 153  GLN B CD  1 
ATOM   2218  O  OE1 . GLN B  1 153 ? 5.512   103.489 26.184  1.00 21.25 ? 153  GLN B OE1 1 
ATOM   2219  N  NE2 . GLN B  1 153 ? 3.982   104.718 27.267  1.00 21.20 ? 153  GLN B NE2 1 
ATOM   2220  O  OXT . GLN B  1 153 ? 0.824   101.617 23.873  1.00 15.74 ? 153  GLN B OXT 1 
ATOM   2221  N  N   . ALA C  1 1   ? 53.305  71.296  35.784  1.00 20.85 ? 1    ALA C N   1 
ATOM   2222  C  CA  . ALA C  1 1   ? 51.823  70.997  35.824  1.00 20.55 ? 1    ALA C CA  1 
ATOM   2223  C  C   . ALA C  1 1   ? 50.954  72.246  36.087  1.00 19.16 ? 1    ALA C C   1 
ATOM   2224  O  O   . ALA C  1 1   ? 51.023  72.811  37.175  1.00 20.65 ? 1    ALA C O   1 
ATOM   2225  C  CB  . ALA C  1 1   ? 51.565  69.935  36.893  1.00 20.96 ? 1    ALA C CB  1 
ATOM   2226  N  N   . THR C  1 2   ? 50.107  72.645  35.132  1.00 16.26 ? 2    THR C N   1 
ATOM   2227  C  CA  . THR C  1 2   ? 49.321  73.876  35.271  1.00 14.29 ? 2    THR C CA  1 
ATOM   2228  C  C   . THR C  1 2   ? 47.882  73.694  34.778  1.00 10.38 ? 2    THR C C   1 
ATOM   2229  O  O   . THR C  1 2   ? 47.624  72.906  33.887  1.00 7.07  ? 2    THR C O   1 
ATOM   2230  C  CB  . THR C  1 2   ? 49.964  75.040  34.432  1.00 13.85 ? 2    THR C CB  1 
ATOM   2231  O  OG1 . THR C  1 2   ? 51.286  75.326  34.897  1.00 20.97 ? 2    THR C OG1 1 
ATOM   2232  C  CG2 . THR C  1 2   ? 49.262  76.340  34.690  1.00 18.73 ? 2    THR C CG2 1 
ATOM   2233  N  N   . LYS C  1 3   ? 46.958  74.439  35.369  1.00 7.79  ? 3    LYS C N   1 
ATOM   2234  C  CA  . LYS C  1 3   ? 45.565  74.395  34.942  1.00 7.37  ? 3    LYS C CA  1 
ATOM   2235  C  C   . LYS C  1 3   ? 45.026  75.813  34.815  1.00 6.31  ? 3    LYS C C   1 
ATOM   2236  O  O   . LYS C  1 3   ? 45.471  76.712  35.550  1.00 5.00  ? 3    LYS C O   1 
ATOM   2237  C  CB  . LYS C  1 3   ? 44.722  73.683  35.995  1.00 9.80  ? 3    LYS C CB  1 
ATOM   2238  C  CG  . LYS C  1 3   ? 45.018  72.182  36.071  1.00 13.37 ? 3    LYS C CG  1 
ATOM   2239  C  CD  . LYS C  1 3   ? 44.263  71.560  37.236  1.00 19.40 ? 3    LYS C CD  1 
ATOM   2240  C  CE  . LYS C  1 3   ? 42.771  71.462  36.954  1.00 23.46 ? 3    LYS C CE  1 
ATOM   2241  N  NZ  . LYS C  1 3   ? 42.232  70.242  37.656  1.00 26.99 ? 3    LYS C NZ  1 
ATOM   2242  N  N   . ALA C  1 4   ? 44.141  76.022  33.840  1.00 5.00  ? 4    ALA C N   1 
ATOM   2243  C  CA  . ALA C  1 4   ? 43.503  77.332  33.688  1.00 5.00  ? 4    ALA C CA  1 
ATOM   2244  C  C   . ALA C  1 4   ? 42.007  77.114  33.399  1.00 5.54  ? 4    ALA C C   1 
ATOM   2245  O  O   . ALA C  1 4   ? 41.563  75.988  33.118  1.00 5.00  ? 4    ALA C O   1 
ATOM   2246  C  CB  . ALA C  1 4   ? 44.155  78.132  32.576  1.00 5.00  ? 4    ALA C CB  1 
ATOM   2247  N  N   . VAL C  1 5   ? 41.230  78.190  33.438  1.00 5.00  ? 5    VAL C N   1 
ATOM   2248  C  CA  . VAL C  1 5   ? 39.808  78.061  33.219  1.00 5.00  ? 5    VAL C CA  1 
ATOM   2249  C  C   . VAL C  1 5   ? 39.307  79.363  32.585  1.00 5.00  ? 5    VAL C C   1 
ATOM   2250  O  O   . VAL C  1 5   ? 39.910  80.409  32.756  1.00 5.00  ? 5    VAL C O   1 
ATOM   2251  C  CB  . VAL C  1 5   ? 39.040  77.727  34.559  1.00 5.00  ? 5    VAL C CB  1 
ATOM   2252  C  CG1 . VAL C  1 5   ? 39.094  78.955  35.566  1.00 5.00  ? 5    VAL C CG1 1 
ATOM   2253  C  CG2 . VAL C  1 5   ? 37.567  77.307  34.293  1.00 5.00  ? 5    VAL C CG2 1 
ATOM   2254  N  N   . CYS C  1 6   ? 38.181  79.291  31.889  1.00 5.00  ? 6    CYS C N   1 
ATOM   2255  C  CA  . CYS C  1 6   ? 37.648  80.501  31.274  1.00 5.00  ? 6    CYS C CA  1 
ATOM   2256  C  C   . CYS C  1 6   ? 36.138  80.393  31.259  1.00 5.00  ? 6    CYS C C   1 
ATOM   2257  O  O   . CYS C  1 6   ? 35.608  79.374  30.817  1.00 5.00  ? 6    CYS C O   1 
ATOM   2258  C  CB  . CYS C  1 6   ? 38.181  80.594  29.836  1.00 5.00  ? 6    CYS C CB  1 
ATOM   2259  S  SG  . CYS C  1 6   ? 37.542  82.042  28.948  1.00 6.34  ? 6    CYS C SG  1 
ATOM   2260  N  N   . VAL C  1 7   ? 35.464  81.424  31.730  1.00 5.00  ? 7    VAL C N   1 
ATOM   2261  C  CA  . VAL C  1 7   ? 34.007  81.499  31.698  1.00 5.00  ? 7    VAL C CA  1 
ATOM   2262  C  C   . VAL C  1 7   ? 33.641  82.362  30.510  1.00 5.08  ? 7    VAL C C   1 
ATOM   2263  O  O   . VAL C  1 7   ? 34.017  83.531  30.451  1.00 5.22  ? 7    VAL C O   1 
ATOM   2264  C  CB  . VAL C  1 7   ? 33.461  82.166  32.958  1.00 5.00  ? 7    VAL C CB  1 
ATOM   2265  C  CG1 . VAL C  1 7   ? 31.941  82.196  32.864  1.00 5.00  ? 7    VAL C CG1 1 
ATOM   2266  C  CG2 . VAL C  1 7   ? 33.918  81.360  34.162  1.00 6.82  ? 7    VAL C CG2 1 
ATOM   2267  N  N   . LEU C  1 8   ? 32.940  81.775  29.533  1.00 5.00  ? 8    LEU C N   1 
ATOM   2268  C  CA  . LEU C  1 8   ? 32.540  82.488  28.326  1.00 5.00  ? 8    LEU C CA  1 
ATOM   2269  C  C   . LEU C  1 8   ? 31.162  83.101  28.485  1.00 5.34  ? 8    LEU C C   1 
ATOM   2270  O  O   . LEU C  1 8   ? 30.213  82.397  28.829  1.00 5.74  ? 8    LEU C O   1 
ATOM   2271  C  CB  . LEU C  1 8   ? 32.448  81.474  27.141  1.00 5.00  ? 8    LEU C CB  1 
ATOM   2272  C  CG  . LEU C  1 8   ? 33.791  80.837  26.752  1.00 6.69  ? 8    LEU C CG  1 
ATOM   2273  C  CD1 . LEU C  1 8   ? 33.505  79.710  25.706  1.00 9.59  ? 8    LEU C CD1 1 
ATOM   2274  C  CD2 . LEU C  1 8   ? 34.636  81.864  26.104  1.00 8.49  ? 8    LEU C CD2 1 
ATOM   2275  N  N   . LYS C  1 9   ? 31.063  84.406  28.268  1.00 5.81  ? 9    LYS C N   1 
ATOM   2276  C  CA  . LYS C  1 9   ? 29.763  85.066  28.326  1.00 7.82  ? 9    LYS C CA  1 
ATOM   2277  C  C   . LYS C  1 9   ? 29.688  86.089  27.229  1.00 7.08  ? 9    LYS C C   1 
ATOM   2278  O  O   . LYS C  1 9   ? 30.724  86.551  26.751  1.00 5.65  ? 9    LYS C O   1 
ATOM   2279  C  CB  . LYS C  1 9   ? 29.594  85.801  29.664  1.00 8.88  ? 9    LYS C CB  1 
ATOM   2280  C  CG  . LYS C  1 9   ? 29.489  84.874  30.844  1.00 16.22 ? 9    LYS C CG  1 
ATOM   2281  C  CD  . LYS C  1 9   ? 29.027  85.631  32.083  1.00 22.26 ? 9    LYS C CD  1 
ATOM   2282  C  CE  . LYS C  1 9   ? 28.428  84.683  33.118  1.00 25.48 ? 9    LYS C CE  1 
ATOM   2283  N  NZ  . LYS C  1 9   ? 29.358  84.441  34.242  1.00 24.57 ? 9    LYS C NZ  1 
ATOM   2284  N  N   . GLY C  1 10  ? 28.461  86.496  26.883  1.00 8.02  ? 10   GLY C N   1 
ATOM   2285  C  CA  . GLY C  1 10  ? 28.267  87.435  25.799  1.00 9.08  ? 10   GLY C CA  1 
ATOM   2286  C  C   . GLY C  1 10  ? 26.938  88.169  25.941  1.00 10.22 ? 10   GLY C C   1 
ATOM   2287  O  O   . GLY C  1 10  ? 26.325  88.135  26.998  1.00 11.66 ? 10   GLY C O   1 
ATOM   2288  N  N   . ASP C  1 11  ? 26.496  88.792  24.862  1.00 10.92 ? 11   ASP C N   1 
ATOM   2289  C  CA  . ASP C  1 11  ? 25.248  89.546  24.893  1.00 13.33 ? 11   ASP C CA  1 
ATOM   2290  C  C   . ASP C  1 11  ? 24.043  88.690  24.566  1.00 12.38 ? 11   ASP C C   1 
ATOM   2291  O  O   . ASP C  1 11  ? 22.901  89.110  24.786  1.00 13.19 ? 11   ASP C O   1 
ATOM   2292  C  CB  . ASP C  1 11  ? 25.335  90.719  23.907  1.00 14.97 ? 11   ASP C CB  1 
ATOM   2293  C  CG  . ASP C  1 11  ? 26.340  91.799  24.362  1.00 18.69 ? 11   ASP C CG  1 
ATOM   2294  O  OD1 . ASP C  1 11  ? 26.502  92.012  25.588  1.00 20.95 ? 11   ASP C OD1 1 
ATOM   2295  O  OD2 . ASP C  1 11  ? 26.977  92.496  23.540  1.00 24.81 ? 11   ASP C OD2 1 
ATOM   2296  N  N   . GLY C  1 12  ? 24.295  87.503  24.032  1.00 10.11 ? 12   GLY C N   1 
ATOM   2297  C  CA  . GLY C  1 12  ? 23.248  86.599  23.598  1.00 10.08 ? 12   GLY C CA  1 
ATOM   2298  C  C   . GLY C  1 12  ? 23.199  85.401  24.512  1.00 9.61  ? 12   GLY C C   1 
ATOM   2299  O  O   . GLY C  1 12  ? 23.624  85.481  25.639  1.00 9.75  ? 12   GLY C O   1 
ATOM   2300  N  N   . PRO C  1 13  ? 22.636  84.294  24.047  1.00 8.10  ? 13   PRO C N   1 
ATOM   2301  C  CA  . PRO C  1 13  ? 22.483  83.101  24.885  1.00 7.86  ? 13   PRO C CA  1 
ATOM   2302  C  C   . PRO C  1 13  ? 23.706  82.181  25.018  1.00 7.26  ? 13   PRO C C   1 
ATOM   2303  O  O   . PRO C  1 13  ? 23.626  81.166  25.714  1.00 5.53  ? 13   PRO C O   1 
ATOM   2304  C  CB  . PRO C  1 13  ? 21.380  82.310  24.155  1.00 7.71  ? 13   PRO C CB  1 
ATOM   2305  C  CG  . PRO C  1 13  ? 21.516  82.701  22.745  1.00 9.10  ? 13   PRO C CG  1 
ATOM   2306  C  CD  . PRO C  1 13  ? 21.981  84.167  22.717  1.00 9.15  ? 13   PRO C CD  1 
ATOM   2307  N  N   . VAL C  1 14  ? 24.825  82.513  24.377  1.00 6.42  ? 14   VAL C N   1 
ATOM   2308  C  CA  . VAL C  1 14  ? 25.964  81.606  24.434  1.00 6.10  ? 14   VAL C CA  1 
ATOM   2309  C  C   . VAL C  1 14  ? 26.732  81.768  25.726  1.00 6.68  ? 14   VAL C C   1 
ATOM   2310  O  O   . VAL C  1 14  ? 27.067  82.895  26.113  1.00 6.10  ? 14   VAL C O   1 
ATOM   2311  C  CB  . VAL C  1 14  ? 26.900  81.846  23.265  1.00 5.63  ? 14   VAL C CB  1 
ATOM   2312  C  CG1 . VAL C  1 14  ? 28.172  80.996  23.382  1.00 5.56  ? 14   VAL C CG1 1 
ATOM   2313  C  CG2 . VAL C  1 14  ? 26.143  81.537  21.968  1.00 5.62  ? 14   VAL C CG2 1 
ATOM   2314  N  N   . GLN C  1 15  ? 26.947  80.663  26.408  1.00 6.59  ? 15   GLN C N   1 
ATOM   2315  C  CA  . GLN C  1 15  ? 27.740  80.688  27.625  1.00 7.64  ? 15   GLN C CA  1 
ATOM   2316  C  C   . GLN C  1 15  ? 28.363  79.342  27.841  1.00 7.27  ? 15   GLN C C   1 
ATOM   2317  O  O   . GLN C  1 15  ? 27.829  78.297  27.452  1.00 7.17  ? 15   GLN C O   1 
ATOM   2318  C  CB  . GLN C  1 15  ? 26.905  81.108  28.868  1.00 9.27  ? 15   GLN C CB  1 
ATOM   2319  C  CG  . GLN C  1 15  ? 25.558  80.419  28.992  1.00 12.67 ? 15   GLN C CG  1 
ATOM   2320  C  CD  . GLN C  1 15  ? 24.816  80.773  30.302  1.00 21.89 ? 15   GLN C CD  1 
ATOM   2321  O  OE1 . GLN C  1 15  ? 23.706  80.311  30.518  1.00 26.05 ? 15   GLN C OE1 1 
ATOM   2322  N  NE2 . GLN C  1 15  ? 25.446  81.568  31.167  1.00 26.49 ? 15   GLN C NE2 1 
ATOM   2323  N  N   . GLY C  1 16  ? 29.526  79.352  28.480  1.00 6.54  ? 16   GLY C N   1 
ATOM   2324  C  CA  . GLY C  1 16  ? 30.135  78.074  28.811  1.00 7.42  ? 16   GLY C CA  1 
ATOM   2325  C  C   . GLY C  1 16  ? 31.358  78.222  29.686  1.00 5.83  ? 16   GLY C C   1 
ATOM   2326  O  O   . GLY C  1 16  ? 31.707  79.322  30.128  1.00 5.00  ? 16   GLY C O   1 
ATOM   2327  N  N   . ILE C  1 17  ? 31.973  77.081  29.973  1.00 5.00  ? 17   ILE C N   1 
ATOM   2328  C  CA  . ILE C  1 17  ? 33.159  77.077  30.815  1.00 5.13  ? 17   ILE C CA  1 
ATOM   2329  C  C   . ILE C  1 17  ? 34.136  76.184  30.119  1.00 5.00  ? 17   ILE C C   1 
ATOM   2330  O  O   . ILE C  1 17  ? 33.776  75.029  29.751  1.00 5.00  ? 17   ILE C O   1 
ATOM   2331  C  CB  . ILE C  1 17  ? 32.819  76.425  32.175  1.00 5.18  ? 17   ILE C CB  1 
ATOM   2332  C  CG1 . ILE C  1 17  ? 31.860  77.319  32.973  1.00 8.10  ? 17   ILE C CG1 1 
ATOM   2333  C  CG2 . ILE C  1 17  ? 34.136  76.113  32.981  1.00 5.11  ? 17   ILE C CG2 1 
ATOM   2334  C  CD1 . ILE C  1 17  ? 31.426  76.684  34.327  1.00 7.88  ? 17   ILE C CD1 1 
ATOM   2335  N  N   . ILE C  1 18  ? 35.355  76.670  29.933  1.00 5.00  ? 18   ILE C N   1 
ATOM   2336  C  CA  . ILE C  1 18  ? 36.367  75.867  29.244  1.00 5.00  ? 18   ILE C CA  1 
ATOM   2337  C  C   . ILE C  1 18  ? 37.578  75.721  30.158  1.00 5.00  ? 18   ILE C C   1 
ATOM   2338  O  O   . ILE C  1 18  ? 38.015  76.703  30.778  1.00 5.00  ? 18   ILE C O   1 
ATOM   2339  C  CB  . ILE C  1 18  ? 36.808  76.557  27.938  1.00 5.00  ? 18   ILE C CB  1 
ATOM   2340  C  CG1 . ILE C  1 18  ? 35.634  76.593  26.935  1.00 5.00  ? 18   ILE C CG1 1 
ATOM   2341  C  CG2 . ILE C  1 18  ? 38.040  75.856  27.308  1.00 5.00  ? 18   ILE C CG2 1 
ATOM   2342  C  CD1 . ILE C  1 18  ? 35.161  75.151  26.463  1.00 5.00  ? 18   ILE C CD1 1 
ATOM   2343  N  N   . ASN C  1 19  ? 38.049  74.484  30.284  1.00 5.00  ? 19   ASN C N   1 
ATOM   2344  C  CA  . ASN C  1 19  ? 39.168  74.149  31.123  1.00 5.34  ? 19   ASN C CA  1 
ATOM   2345  C  C   . ASN C  1 19  ? 40.404  73.931  30.280  1.00 5.00  ? 19   ASN C C   1 
ATOM   2346  O  O   . ASN C  1 19  ? 40.316  73.487  29.128  1.00 6.01  ? 19   ASN C O   1 
ATOM   2347  C  CB  . ASN C  1 19  ? 38.859  72.825  31.852  1.00 5.00  ? 19   ASN C CB  1 
ATOM   2348  C  CG  . ASN C  1 19  ? 37.549  72.865  32.592  1.00 8.06  ? 19   ASN C CG  1 
ATOM   2349  O  OD1 . ASN C  1 19  ? 36.528  72.261  32.179  1.00 10.54 ? 19   ASN C OD1 1 
ATOM   2350  N  ND2 . ASN C  1 19  ? 37.546  73.587  33.689  1.00 5.00  ? 19   ASN C ND2 1 
ATOM   2351  N  N   . PHE C  1 20  ? 41.564  74.208  30.855  1.00 5.00  ? 20   PHE C N   1 
ATOM   2352  C  CA  . PHE C  1 20  ? 42.823  73.973  30.192  1.00 5.00  ? 20   PHE C CA  1 
ATOM   2353  C  C   . PHE C  1 20  ? 43.709  73.245  31.158  1.00 5.63  ? 20   PHE C C   1 
ATOM   2354  O  O   . PHE C  1 20  ? 43.748  73.606  32.340  1.00 5.25  ? 20   PHE C O   1 
ATOM   2355  C  CB  . PHE C  1 20  ? 43.541  75.294  29.860  1.00 5.00  ? 20   PHE C CB  1 
ATOM   2356  C  CG  . PHE C  1 20  ? 42.784  76.211  28.949  1.00 6.30  ? 20   PHE C CG  1 
ATOM   2357  C  CD1 . PHE C  1 20  ? 41.756  77.030  29.438  1.00 6.69  ? 20   PHE C CD1 1 
ATOM   2358  C  CD2 . PHE C  1 20  ? 43.116  76.277  27.607  1.00 5.31  ? 20   PHE C CD2 1 
ATOM   2359  C  CE1 . PHE C  1 20  ? 41.079  77.902  28.580  1.00 6.53  ? 20   PHE C CE1 1 
ATOM   2360  C  CE2 . PHE C  1 20  ? 42.448  77.145  26.749  1.00 6.57  ? 20   PHE C CE2 1 
ATOM   2361  C  CZ  . PHE C  1 20  ? 41.438  77.969  27.248  1.00 6.47  ? 20   PHE C CZ  1 
ATOM   2362  N  N   . GLU C  1 21  ? 44.447  72.237  30.682  1.00 6.61  ? 21   GLU C N   1 
ATOM   2363  C  CA  . GLU C  1 21  ? 45.359  71.497  31.574  1.00 7.06  ? 21   GLU C CA  1 
ATOM   2364  C  C   . GLU C  1 21  ? 46.619  71.192  30.817  1.00 6.48  ? 21   GLU C C   1 
ATOM   2365  O  O   . GLU C  1 21  ? 46.577  70.757  29.657  1.00 6.79  ? 21   GLU C O   1 
ATOM   2366  C  CB  . GLU C  1 21  ? 44.713  70.218  32.093  1.00 8.40  ? 21   GLU C CB  1 
ATOM   2367  C  CG  . GLU C  1 21  ? 45.611  69.348  32.993  1.00 13.78 ? 21   GLU C CG  1 
ATOM   2368  C  CD  . GLU C  1 21  ? 44.855  68.160  33.585  1.00 22.20 ? 21   GLU C CD  1 
ATOM   2369  O  OE1 . GLU C  1 21  ? 43.660  68.312  33.915  1.00 24.48 ? 21   GLU C OE1 1 
ATOM   2370  O  OE2 . GLU C  1 21  ? 45.441  67.064  33.709  1.00 28.23 ? 21   GLU C OE2 1 
ATOM   2371  N  N   . GLN C  1 22  ? 47.759  71.474  31.433  1.00 6.40  ? 22   GLN C N   1 
ATOM   2372  C  CA  . GLN C  1 22  ? 49.031  71.198  30.783  1.00 7.27  ? 22   GLN C CA  1 
ATOM   2373  C  C   . GLN C  1 22  ? 49.897  70.436  31.781  1.00 9.00  ? 22   GLN C C   1 
ATOM   2374  O  O   . GLN C  1 22  ? 50.296  70.975  32.814  1.00 8.80  ? 22   GLN C O   1 
ATOM   2375  C  CB  . GLN C  1 22  ? 49.724  72.491  30.362  1.00 8.20  ? 22   GLN C CB  1 
ATOM   2376  C  CG  . GLN C  1 22  ? 50.994  72.274  29.534  1.00 5.81  ? 22   GLN C CG  1 
ATOM   2377  C  CD  . GLN C  1 22  ? 51.636  73.582  29.106  1.00 6.26  ? 22   GLN C CD  1 
ATOM   2378  O  OE1 . GLN C  1 22  ? 51.571  74.592  29.827  1.00 7.66  ? 22   GLN C OE1 1 
ATOM   2379  N  NE2 . GLN C  1 22  ? 52.226  73.585  27.921  1.00 5.58  ? 22   GLN C NE2 1 
ATOM   2380  N  N   . LYS C  1 23  ? 50.171  69.185  31.451  1.00 11.11 ? 23   LYS C N   1 
ATOM   2381  C  CA  . LYS C  1 23  ? 50.901  68.292  32.361  1.00 13.69 ? 23   LYS C CA  1 
ATOM   2382  C  C   . LYS C  1 23  ? 52.386  68.575  32.486  1.00 14.59 ? 23   LYS C C   1 
ATOM   2383  O  O   . LYS C  1 23  ? 52.968  68.384  33.560  1.00 14.06 ? 23   LYS C O   1 
ATOM   2384  C  CB  . LYS C  1 23  ? 50.675  66.855  31.930  1.00 14.58 ? 23   LYS C CB  1 
ATOM   2385  C  CG  . LYS C  1 23  ? 49.325  66.290  32.371  1.00 19.91 ? 23   LYS C CG  1 
ATOM   2386  C  CD  . LYS C  1 23  ? 49.060  64.919  31.749  1.00 26.65 ? 23   LYS C CD  1 
ATOM   2387  C  CE  . LYS C  1 23  ? 47.721  64.319  32.223  1.00 30.67 ? 23   LYS C CE  1 
ATOM   2388  N  NZ  . LYS C  1 23  ? 46.591  64.471  31.233  1.00 31.23 ? 23   LYS C NZ  1 
ATOM   2389  N  N   . GLU C  1 24  ? 53.027  68.993  31.403  1.00 15.20 ? 24   GLU C N   1 
ATOM   2390  C  CA  . GLU C  1 24  ? 54.458  69.290  31.486  1.00 17.69 ? 24   GLU C CA  1 
ATOM   2391  C  C   . GLU C  1 24  ? 54.743  70.595  30.790  1.00 17.60 ? 24   GLU C C   1 
ATOM   2392  O  O   . GLU C  1 24  ? 54.060  70.952  29.821  1.00 17.53 ? 24   GLU C O   1 
ATOM   2393  C  CB  . GLU C  1 24  ? 55.286  68.228  30.773  1.00 18.10 ? 24   GLU C CB  1 
ATOM   2394  C  CG  . GLU C  1 24  ? 54.622  66.883  30.636  1.00 23.53 ? 24   GLU C CG  1 
ATOM   2395  C  CD  . GLU C  1 24  ? 55.412  65.963  29.725  1.00 29.43 ? 24   GLU C CD  1 
ATOM   2396  O  OE1 . GLU C  1 24  ? 56.646  66.162  29.587  1.00 33.13 ? 24   GLU C OE1 1 
ATOM   2397  O  OE2 . GLU C  1 24  ? 54.792  65.045  29.141  1.00 33.04 ? 24   GLU C OE2 1 
ATOM   2398  N  N   . SER C  1 25  ? 55.775  71.294  31.235  1.00 17.26 ? 25   SER C N   1 
ATOM   2399  C  CA  . SER C  1 25  ? 56.082  72.579  30.617  1.00 17.67 ? 25   SER C CA  1 
ATOM   2400  C  C   . SER C  1 25  ? 56.367  72.381  29.123  1.00 17.53 ? 25   SER C C   1 
ATOM   2401  O  O   . SER C  1 25  ? 56.985  71.389  28.716  1.00 16.23 ? 25   SER C O   1 
ATOM   2402  C  CB  . SER C  1 25  ? 57.235  73.276  31.336  1.00 19.07 ? 25   SER C CB  1 
ATOM   2403  O  OG  . SER C  1 25  ? 58.454  72.899  30.755  1.00 19.69 ? 25   SER C OG  1 
ATOM   2404  N  N   . ASN C  1 26  ? 55.859  73.312  28.314  1.00 17.35 ? 26   ASN C N   1 
ATOM   2405  C  CA  . ASN C  1 26  ? 55.965  73.253  26.856  1.00 17.56 ? 26   ASN C CA  1 
ATOM   2406  C  C   . ASN C  1 26  ? 55.161  72.092  26.247  1.00 16.25 ? 26   ASN C C   1 
ATOM   2407  O  O   . ASN C  1 26  ? 55.062  71.984  25.030  1.00 17.19 ? 26   ASN C O   1 
ATOM   2408  C  CB  . ASN C  1 26  ? 57.444  73.246  26.377  1.00 18.82 ? 26   ASN C CB  1 
ATOM   2409  C  CG  . ASN C  1 26  ? 57.612  73.859  24.983  1.00 23.24 ? 26   ASN C CG  1 
ATOM   2410  O  OD1 . ASN C  1 26  ? 56.660  73.895  24.185  1.00 26.88 ? 26   ASN C OD1 1 
ATOM   2411  N  ND2 . ASN C  1 26  ? 58.814  74.358  24.687  1.00 26.30 ? 26   ASN C ND2 1 
ATOM   2412  N  N   . GLY C  1 27  ? 54.565  71.238  27.081  1.00 14.41 ? 27   GLY C N   1 
ATOM   2413  C  CA  . GLY C  1 27  ? 53.787  70.105  26.599  1.00 12.39 ? 27   GLY C CA  1 
ATOM   2414  C  C   . GLY C  1 27  ? 52.403  70.413  26.021  1.00 10.93 ? 27   GLY C C   1 
ATOM   2415  O  O   . GLY C  1 27  ? 51.984  71.590  25.969  1.00 11.24 ? 27   GLY C O   1 
ATOM   2416  N  N   . PRO C  1 28  ? 51.690  69.383  25.564  1.00 9.64  ? 28   PRO C N   1 
ATOM   2417  C  CA  . PRO C  1 28  ? 50.323  69.561  25.042  1.00 9.10  ? 28   PRO C CA  1 
ATOM   2418  C  C   . PRO C  1 28  ? 49.410  70.166  26.086  1.00 7.40  ? 28   PRO C C   1 
ATOM   2419  O  O   . PRO C  1 28  ? 49.503  69.823  27.259  1.00 7.71  ? 28   PRO C O   1 
ATOM   2420  C  CB  . PRO C  1 28  ? 49.825  68.132  24.817  1.00 9.01  ? 28   PRO C CB  1 
ATOM   2421  C  CG  . PRO C  1 28  ? 51.022  67.289  24.786  1.00 11.17 ? 28   PRO C CG  1 
ATOM   2422  C  CD  . PRO C  1 28  ? 52.151  67.984  25.472  1.00 10.35 ? 28   PRO C CD  1 
ATOM   2423  N  N   . VAL C  1 29  ? 48.504  71.013  25.636  1.00 6.69  ? 29   VAL C N   1 
ATOM   2424  C  CA  . VAL C  1 29  ? 47.498  71.567  26.509  1.00 6.49  ? 29   VAL C CA  1 
ATOM   2425  C  C   . VAL C  1 29  ? 46.159  70.924  26.158  1.00 6.42  ? 29   VAL C C   1 
ATOM   2426  O  O   . VAL C  1 29  ? 45.746  70.947  24.988  1.00 6.88  ? 29   VAL C O   1 
ATOM   2427  C  CB  . VAL C  1 29  ? 47.399  73.065  26.325  1.00 6.28  ? 29   VAL C CB  1 
ATOM   2428  C  CG1 . VAL C  1 29  ? 46.241  73.651  27.242  1.00 6.12  ? 29   VAL C CG1 1 
ATOM   2429  C  CG2 . VAL C  1 29  ? 48.777  73.739  26.614  1.00 5.94  ? 29   VAL C CG2 1 
ATOM   2430  N  N   . LYS C  1 30  ? 45.503  70.319  27.144  1.00 6.66  ? 30   LYS C N   1 
ATOM   2431  C  CA  . LYS C  1 30  ? 44.152  69.779  26.923  1.00 6.68  ? 30   LYS C CA  1 
ATOM   2432  C  C   . LYS C  1 30  ? 43.120  70.888  27.176  1.00 6.10  ? 30   LYS C C   1 
ATOM   2433  O  O   . LYS C  1 30  ? 43.205  71.617  28.172  1.00 5.10  ? 30   LYS C O   1 
ATOM   2434  C  CB  . LYS C  1 30  ? 43.888  68.569  27.842  1.00 8.31  ? 30   LYS C CB  1 
ATOM   2435  C  CG  . LYS C  1 30  ? 44.652  67.334  27.420  1.00 11.58 ? 30   LYS C CG  1 
ATOM   2436  C  CD  . LYS C  1 30  ? 44.518  66.171  28.434  1.00 17.92 ? 30   LYS C CD  1 
ATOM   2437  C  CE  . LYS C  1 30  ? 45.310  64.942  27.977  1.00 21.66 ? 30   LYS C CE  1 
ATOM   2438  N  N   . VAL C  1 31  ? 42.148  71.011  26.266  1.00 5.39  ? 31   VAL C N   1 
ATOM   2439  C  CA  . VAL C  1 31  ? 41.136  72.063  26.342  1.00 5.09  ? 31   VAL C CA  1 
ATOM   2440  C  C   . VAL C  1 31  ? 39.777  71.395  26.275  1.00 5.67  ? 31   VAL C C   1 
ATOM   2441  O  O   . VAL C  1 31  ? 39.504  70.662  25.315  1.00 7.25  ? 31   VAL C O   1 
ATOM   2442  C  CB  . VAL C  1 31  ? 41.263  73.046  25.132  1.00 5.55  ? 31   VAL C CB  1 
ATOM   2443  C  CG1 . VAL C  1 31  ? 40.279  74.224  25.297  1.00 6.09  ? 31   VAL C CG1 1 
ATOM   2444  C  CG2 . VAL C  1 31  ? 42.738  73.578  25.033  1.00 5.00  ? 31   VAL C CG2 1 
ATOM   2445  N  N   . TRP C  1 32  ? 38.921  71.601  27.286  1.00 5.34  ? 32   TRP C N   1 
ATOM   2446  C  CA  . TRP C  1 32  ? 37.641  70.905  27.256  1.00 6.08  ? 32   TRP C CA  1 
ATOM   2447  C  C   . TRP C  1 32  ? 36.614  71.611  28.128  1.00 6.22  ? 32   TRP C C   1 
ATOM   2448  O  O   . TRP C  1 32  ? 36.965  72.331  29.065  1.00 5.37  ? 32   TRP C O   1 
ATOM   2449  C  CB  . TRP C  1 32  ? 37.810  69.458  27.740  1.00 6.99  ? 32   TRP C CB  1 
ATOM   2450  C  CG  . TRP C  1 32  ? 37.908  69.323  29.205  1.00 8.82  ? 32   TRP C CG  1 
ATOM   2451  C  CD1 . TRP C  1 32  ? 36.911  68.939  30.061  1.00 9.42  ? 32   TRP C CD1 1 
ATOM   2452  C  CD2 . TRP C  1 32  ? 39.059  69.561  30.009  1.00 11.41 ? 32   TRP C CD2 1 
ATOM   2453  N  NE1 . TRP C  1 32  ? 37.384  68.930  31.350  1.00 13.95 ? 32   TRP C NE1 1 
ATOM   2454  C  CE2 . TRP C  1 32  ? 38.703  69.290  31.345  1.00 12.28 ? 32   TRP C CE2 1 
ATOM   2455  C  CE3 . TRP C  1 32  ? 40.370  69.947  29.735  1.00 13.69 ? 32   TRP C CE3 1 
ATOM   2456  C  CZ2 . TRP C  1 32  ? 39.588  69.423  32.403  1.00 14.93 ? 32   TRP C CZ2 1 
ATOM   2457  C  CZ3 . TRP C  1 32  ? 41.259  70.099  30.797  1.00 12.63 ? 32   TRP C CZ3 1 
ATOM   2458  C  CH2 . TRP C  1 32  ? 40.862  69.819  32.119  1.00 14.83 ? 32   TRP C CH2 1 
ATOM   2459  N  N   . GLY C  1 33  ? 35.358  71.369  27.817  1.00 5.44  ? 33   GLY C N   1 
ATOM   2460  C  CA  . GLY C  1 33  ? 34.289  71.953  28.578  1.00 7.36  ? 33   GLY C CA  1 
ATOM   2461  C  C   . GLY C  1 33  ? 33.084  72.021  27.693  1.00 8.14  ? 33   GLY C C   1 
ATOM   2462  O  O   . GLY C  1 33  ? 33.059  71.458  26.638  1.00 10.61 ? 33   GLY C O   1 
ATOM   2463  N  N   . SER C  1 34  ? 32.048  72.672  28.159  1.00 8.29  ? 34   SER C N   1 
ATOM   2464  C  CA  . SER C  1 34  ? 30.801  72.692  27.423  1.00 8.43  ? 34   SER C CA  1 
ATOM   2465  C  C   . SER C  1 34  ? 30.389  74.125  27.146  1.00 6.65  ? 34   SER C C   1 
ATOM   2466  O  O   . SER C  1 34  ? 30.535  74.998  28.016  1.00 6.13  ? 34   SER C O   1 
ATOM   2467  C  CB  . SER C  1 34  ? 29.754  71.939  28.249  1.00 10.81 ? 34   SER C CB  1 
ATOM   2468  O  OG  . SER C  1 34  ? 28.431  72.335  27.937  1.00 16.13 ? 34   SER C OG  1 
ATOM   2469  N  N   . ILE C  1 35  ? 29.933  74.397  25.938  1.00 5.00  ? 35   ILE C N   1 
ATOM   2470  C  CA  . ILE C  1 35  ? 29.420  75.723  25.632  1.00 5.00  ? 35   ILE C CA  1 
ATOM   2471  C  C   . ILE C  1 35  ? 27.971  75.529  25.153  1.00 5.40  ? 35   ILE C C   1 
ATOM   2472  O  O   . ILE C  1 35  ? 27.725  74.650  24.317  1.00 6.33  ? 35   ILE C O   1 
ATOM   2473  C  CB  . ILE C  1 35  ? 30.230  76.389  24.508  1.00 5.00  ? 35   ILE C CB  1 
ATOM   2474  C  CG1 . ILE C  1 35  ? 31.704  76.514  24.920  1.00 5.10  ? 35   ILE C CG1 1 
ATOM   2475  C  CG2 . ILE C  1 35  ? 29.618  77.767  24.226  1.00 5.00  ? 35   ILE C CG2 1 
ATOM   2476  C  CD1 . ILE C  1 35  ? 32.594  76.965  23.707  1.00 7.89  ? 35   ILE C CD1 1 
ATOM   2477  N  N   . LYS C  1 36  ? 27.016  76.319  25.634  1.00 5.00  ? 36   LYS C N   1 
ATOM   2478  C  CA  . LYS C  1 36  ? 25.647  76.101  25.181  1.00 5.21  ? 36   LYS C CA  1 
ATOM   2479  C  C   . LYS C  1 36  ? 25.087  77.363  24.562  1.00 5.08  ? 36   LYS C C   1 
ATOM   2480  O  O   . LYS C  1 36  ? 25.756  78.398  24.560  1.00 5.00  ? 36   LYS C O   1 
ATOM   2481  C  CB  . LYS C  1 36  ? 24.728  75.662  26.309  1.00 7.42  ? 36   LYS C CB  1 
ATOM   2482  C  CG  . LYS C  1 36  ? 24.544  76.706  27.354  1.00 11.27 ? 36   LYS C CG  1 
ATOM   2483  C  CD  . LYS C  1 36  ? 23.648  76.148  28.504  1.00 20.02 ? 36   LYS C CD  1 
ATOM   2484  C  CE  . LYS C  1 36  ? 22.702  77.232  29.076  1.00 25.07 ? 36   LYS C CE  1 
ATOM   2485  N  NZ  . LYS C  1 36  ? 21.530  76.648  29.903  1.00 27.39 ? 36   LYS C NZ  1 
ATOM   2486  N  N   . GLY C  1 37  ? 23.891  77.249  23.989  1.00 5.00  ? 37   GLY C N   1 
ATOM   2487  C  CA  . GLY C  1 37  ? 23.225  78.392  23.378  1.00 5.00  ? 37   GLY C CA  1 
ATOM   2488  C  C   . GLY C  1 37  ? 23.654  78.684  21.938  1.00 5.00  ? 37   GLY C C   1 
ATOM   2489  O  O   . GLY C  1 37  ? 23.382  79.745  21.400  1.00 5.00  ? 37   GLY C O   1 
ATOM   2490  N  N   . LEU C  1 38  ? 24.366  77.748  21.347  1.00 5.00  ? 38   LEU C N   1 
ATOM   2491  C  CA  . LEU C  1 38  ? 24.881  77.948  19.989  1.00 5.00  ? 38   LEU C CA  1 
ATOM   2492  C  C   . LEU C  1 38  ? 23.982  77.331  18.876  1.00 5.03  ? 38   LEU C C   1 
ATOM   2493  O  O   . LEU C  1 38  ? 23.255  76.356  19.119  1.00 5.00  ? 38   LEU C O   1 
ATOM   2494  C  CB  . LEU C  1 38  ? 26.243  77.269  19.879  1.00 5.00  ? 38   LEU C CB  1 
ATOM   2495  C  CG  . LEU C  1 38  ? 27.433  77.827  20.691  1.00 5.00  ? 38   LEU C CG  1 
ATOM   2496  C  CD1 . LEU C  1 38  ? 28.539  76.725  20.833  1.00 5.10  ? 38   LEU C CD1 1 
ATOM   2497  C  CD2 . LEU C  1 38  ? 27.958  79.064  19.982  1.00 5.02  ? 38   LEU C CD2 1 
ATOM   2498  N  N   . THR C  1 39  ? 24.078  77.894  17.668  1.00 5.00  ? 39   THR C N   1 
ATOM   2499  C  CA  . THR C  1 39  ? 23.426  77.298  16.507  1.00 5.54  ? 39   THR C CA  1 
ATOM   2500  C  C   . THR C  1 39  ? 24.180  76.013  16.169  1.00 5.68  ? 39   THR C C   1 
ATOM   2501  O  O   . THR C  1 39  ? 25.402  75.904  16.332  1.00 5.33  ? 39   THR C O   1 
ATOM   2502  C  CB  . THR C  1 39  ? 23.423  78.219  15.292  1.00 6.85  ? 39   THR C CB  1 
ATOM   2503  O  OG1 . THR C  1 39  ? 24.743  78.699  15.046  1.00 6.01  ? 39   THR C OG1 1 
ATOM   2504  C  CG2 . THR C  1 39  ? 22.581  79.456  15.542  1.00 7.93  ? 39   THR C CG2 1 
ATOM   2505  N  N   . GLU C  1 40  ? 23.443  75.026  15.680  1.00 5.81  ? 40   GLU C N   1 
ATOM   2506  C  CA  . GLU C  1 40  ? 24.068  73.753  15.372  1.00 6.63  ? 40   GLU C CA  1 
ATOM   2507  C  C   . GLU C  1 40  ? 25.197  73.929  14.346  1.00 6.23  ? 40   GLU C C   1 
ATOM   2508  O  O   . GLU C  1 40  ? 25.075  74.695  13.409  1.00 8.79  ? 40   GLU C O   1 
ATOM   2509  C  CB  . GLU C  1 40  ? 22.990  72.789  14.811  1.00 6.70  ? 40   GLU C CB  1 
ATOM   2510  C  CG  . GLU C  1 40  ? 23.471  71.347  14.642  1.00 9.22  ? 40   GLU C CG  1 
ATOM   2511  C  CD  . GLU C  1 40  ? 22.355  70.402  14.166  1.00 16.63 ? 40   GLU C CD  1 
ATOM   2512  O  OE1 . GLU C  1 40  ? 21.178  70.851  14.046  1.00 18.49 ? 40   GLU C OE1 1 
ATOM   2513  O  OE2 . GLU C  1 40  ? 22.670  69.219  13.879  1.00 17.79 ? 40   GLU C OE2 1 
ATOM   2514  N  N   . GLY C  1 41  ? 26.304  73.220  14.495  1.00 5.74  ? 41   GLY C N   1 
ATOM   2515  C  CA  . GLY C  1 41  ? 27.356  73.289  13.476  1.00 5.61  ? 41   GLY C CA  1 
ATOM   2516  C  C   . GLY C  1 41  ? 28.649  73.908  13.984  1.00 5.70  ? 41   GLY C C   1 
ATOM   2517  O  O   . GLY C  1 41  ? 28.849  74.013  15.202  1.00 5.11  ? 41   GLY C O   1 
ATOM   2518  N  N   . LEU C  1 42  ? 29.515  74.328  13.052  1.00 5.88  ? 42   LEU C N   1 
ATOM   2519  C  CA  . LEU C  1 42  ? 30.852  74.801  13.402  1.00 5.00  ? 42   LEU C CA  1 
ATOM   2520  C  C   . LEU C  1 42  ? 30.874  76.236  13.881  1.00 5.00  ? 42   LEU C C   1 
ATOM   2521  O  O   . LEU C  1 42  ? 30.186  77.106  13.307  1.00 5.00  ? 42   LEU C O   1 
ATOM   2522  C  CB  . LEU C  1 42  ? 31.740  74.727  12.141  1.00 5.22  ? 42   LEU C CB  1 
ATOM   2523  C  CG  . LEU C  1 42  ? 32.019  73.338  11.591  1.00 8.50  ? 42   LEU C CG  1 
ATOM   2524  C  CD1 . LEU C  1 42  ? 32.733  73.495  10.209  1.00 9.30  ? 42   LEU C CD1 1 
ATOM   2525  C  CD2 . LEU C  1 42  ? 32.944  72.623  12.543  1.00 9.37  ? 42   LEU C CD2 1 
ATOM   2526  N  N   . HIS C  1 43  ? 31.705  76.482  14.890  1.00 5.00  ? 43   HIS C N   1 
ATOM   2527  C  CA  . HIS C  1 43  ? 31.932  77.821  15.419  1.00 5.00  ? 43   HIS C CA  1 
ATOM   2528  C  C   . HIS C  1 43  ? 33.414  78.040  15.634  1.00 5.00  ? 43   HIS C C   1 
ATOM   2529  O  O   . HIS C  1 43  ? 34.073  77.244  16.287  1.00 5.00  ? 43   HIS C O   1 
ATOM   2530  C  CB  . HIS C  1 43  ? 31.176  78.005  16.741  1.00 5.00  ? 43   HIS C CB  1 
ATOM   2531  C  CG  . HIS C  1 43  ? 29.700  77.997  16.555  1.00 5.00  ? 43   HIS C CG  1 
ATOM   2532  N  ND1 . HIS C  1 43  ? 28.989  79.138  16.237  1.00 5.00  ? 43   HIS C ND1 1 
ATOM   2533  C  CD2 . HIS C  1 43  ? 28.819  76.980  16.509  1.00 5.00  ? 43   HIS C CD2 1 
ATOM   2534  C  CE1 . HIS C  1 43  ? 27.716  78.837  16.099  1.00 5.00  ? 43   HIS C CE1 1 
ATOM   2535  N  NE2 . HIS C  1 43  ? 27.589  77.532  16.233  1.00 5.85  ? 43   HIS C NE2 1 
ATOM   2536  N  N   . GLY C  1 44  ? 33.956  79.123  15.110  1.00 5.00  ? 44   GLY C N   1 
ATOM   2537  C  CA  . GLY C  1 44  ? 35.376  79.380  15.264  1.00 5.00  ? 44   GLY C CA  1 
ATOM   2538  C  C   . GLY C  1 44  ? 35.691  79.564  16.756  1.00 5.00  ? 44   GLY C C   1 
ATOM   2539  O  O   . GLY C  1 44  ? 34.868  80.074  17.539  1.00 5.00  ? 44   GLY C O   1 
ATOM   2540  N  N   . PHE C  1 45  ? 36.906  79.196  17.143  1.00 5.00  ? 45   PHE C N   1 
ATOM   2541  C  CA  . PHE C  1 45  ? 37.275  79.161  18.558  1.00 5.00  ? 45   PHE C CA  1 
ATOM   2542  C  C   . PHE C  1 45  ? 38.744  79.552  18.637  1.00 5.00  ? 45   PHE C C   1 
ATOM   2543  O  O   . PHE C  1 45  ? 39.616  78.811  18.157  1.00 5.00  ? 45   PHE C O   1 
ATOM   2544  C  CB  . PHE C  1 45  ? 37.068  77.710  18.968  1.00 5.00  ? 45   PHE C CB  1 
ATOM   2545  C  CG  . PHE C  1 45  ? 37.185  77.406  20.463  1.00 5.00  ? 45   PHE C CG  1 
ATOM   2546  C  CD1 . PHE C  1 45  ? 36.267  77.917  21.393  1.00 5.43  ? 45   PHE C CD1 1 
ATOM   2547  C  CD2 . PHE C  1 45  ? 38.178  76.518  20.901  1.00 5.33  ? 45   PHE C CD2 1 
ATOM   2548  C  CE1 . PHE C  1 45  ? 36.355  77.555  22.770  1.00 6.52  ? 45   PHE C CE1 1 
ATOM   2549  C  CE2 . PHE C  1 45  ? 38.268  76.149  22.242  1.00 5.00  ? 45   PHE C CE2 1 
ATOM   2550  C  CZ  . PHE C  1 45  ? 37.350  76.667  23.175  1.00 5.77  ? 45   PHE C CZ  1 
ATOM   2551  N  N   . HIS C  1 46  ? 39.030  80.712  19.226  1.00 5.00  ? 46   HIS C N   1 
ATOM   2552  C  CA  . HIS C  1 46  ? 40.398  81.244  19.188  1.00 5.00  ? 46   HIS C CA  1 
ATOM   2553  C  C   . HIS C  1 46  ? 40.819  81.901  20.505  1.00 5.00  ? 46   HIS C C   1 
ATOM   2554  O  O   . HIS C  1 46  ? 39.980  82.421  21.234  1.00 5.00  ? 46   HIS C O   1 
ATOM   2555  C  CB  . HIS C  1 46  ? 40.441  82.398  18.159  1.00 5.25  ? 46   HIS C CB  1 
ATOM   2556  C  CG  . HIS C  1 46  ? 39.833  82.043  16.843  1.00 6.16  ? 46   HIS C CG  1 
ATOM   2557  N  ND1 . HIS C  1 46  ? 38.885  82.811  16.203  1.00 5.65  ? 46   HIS C ND1 1 
ATOM   2558  C  CD2 . HIS C  1 46  ? 40.061  80.982  16.036  1.00 6.04  ? 46   HIS C CD2 1 
ATOM   2559  C  CE1 . HIS C  1 46  ? 38.547  82.235  15.072  1.00 8.17  ? 46   HIS C CE1 1 
ATOM   2560  N  NE2 . HIS C  1 46  ? 39.241  81.118  14.947  1.00 5.19  ? 46   HIS C NE2 1 
ATOM   2561  N  N   . VAL C  1 47  ? 42.125  81.949  20.725  1.00 5.00  ? 47   VAL C N   1 
ATOM   2562  C  CA  . VAL C  1 47  ? 42.640  82.809  21.780  1.00 5.00  ? 47   VAL C CA  1 
ATOM   2563  C  C   . VAL C  1 47  ? 43.004  84.132  21.138  1.00 5.00  ? 47   VAL C C   1 
ATOM   2564  O  O   . VAL C  1 47  ? 43.863  84.182  20.211  1.00 5.00  ? 47   VAL C O   1 
ATOM   2565  C  CB  . VAL C  1 47  ? 43.862  82.205  22.419  1.00 5.00  ? 47   VAL C CB  1 
ATOM   2566  C  CG1 . VAL C  1 47  ? 44.311  83.133  23.523  1.00 5.00  ? 47   VAL C CG1 1 
ATOM   2567  C  CG2 . VAL C  1 47  ? 43.497  80.812  22.937  1.00 5.55  ? 47   VAL C CG2 1 
ATOM   2568  N  N   . HIS C  1 48  ? 42.380  85.197  21.642  1.00 5.00  ? 48   HIS C N   1 
ATOM   2569  C  CA  . HIS C  1 48  ? 42.675  86.553  21.164  1.00 5.00  ? 48   HIS C CA  1 
ATOM   2570  C  C   . HIS C  1 48  ? 43.690  87.188  22.070  1.00 5.00  ? 48   HIS C C   1 
ATOM   2571  O  O   . HIS C  1 48  ? 43.874  86.753  23.204  1.00 5.00  ? 48   HIS C O   1 
ATOM   2572  C  CB  . HIS C  1 48  ? 41.417  87.407  21.069  1.00 5.00  ? 48   HIS C CB  1 
ATOM   2573  C  CG  . HIS C  1 48  ? 40.561  87.016  19.918  1.00 5.00  ? 48   HIS C CG  1 
ATOM   2574  N  ND1 . HIS C  1 48  ? 40.172  87.896  18.927  1.00 5.00  ? 48   HIS C ND1 1 
ATOM   2575  C  CD2 . HIS C  1 48  ? 40.083  85.807  19.576  1.00 5.00  ? 48   HIS C CD2 1 
ATOM   2576  C  CE1 . HIS C  1 48  ? 39.451  87.227  18.032  1.00 6.31  ? 48   HIS C CE1 1 
ATOM   2577  N  NE2 . HIS C  1 48  ? 39.353  85.972  18.434  1.00 5.00  ? 48   HIS C NE2 1 
ATOM   2578  N  N   . GLU C  1 49  ? 44.340  88.225  21.573  1.00 5.00  ? 49   GLU C N   1 
ATOM   2579  C  CA  . GLU C  1 49  ? 45.557  88.751  22.211  1.00 5.00  ? 49   GLU C CA  1 
ATOM   2580  C  C   . GLU C  1 49  ? 45.419  89.340  23.621  1.00 5.00  ? 49   GLU C C   1 
ATOM   2581  O  O   . GLU C  1 49  ? 46.258  89.043  24.504  1.00 5.31  ? 49   GLU C O   1 
ATOM   2582  C  CB  . GLU C  1 49  ? 46.171  89.820  21.306  1.00 5.00  ? 49   GLU C CB  1 
ATOM   2583  C  CG  . GLU C  1 49  ? 47.502  90.316  21.849  1.00 6.14  ? 49   GLU C CG  1 
ATOM   2584  C  CD  . GLU C  1 49  ? 48.224  91.269  20.897  1.00 11.14 ? 49   GLU C CD  1 
ATOM   2585  O  OE1 . GLU C  1 49  ? 47.668  91.592  19.820  1.00 9.80  ? 49   GLU C OE1 1 
ATOM   2586  O  OE2 . GLU C  1 49  ? 49.354  91.681  21.271  1.00 7.00  ? 49   GLU C OE2 1 
ATOM   2587  N  N   . PHE C  1 50  ? 44.389  90.157  23.819  1.00 5.00  ? 50   PHE C N   1 
ATOM   2588  C  CA  . PHE C  1 50  ? 44.233  90.904  25.081  1.00 5.00  ? 50   PHE C CA  1 
ATOM   2589  C  C   . PHE C  1 50  ? 43.153  90.364  25.990  1.00 5.00  ? 50   PHE C C   1 
ATOM   2590  O  O   . PHE C  1 50  ? 42.061  90.024  25.516  1.00 6.45  ? 50   PHE C O   1 
ATOM   2591  C  CB  . PHE C  1 50  ? 43.948  92.375  24.781  1.00 5.00  ? 50   PHE C CB  1 
ATOM   2592  C  CG  . PHE C  1 50  ? 44.976  92.970  23.873  1.00 7.66  ? 50   PHE C CG  1 
ATOM   2593  C  CD1 . PHE C  1 50  ? 46.311  92.968  24.255  1.00 10.37 ? 50   PHE C CD1 1 
ATOM   2594  C  CD2 . PHE C  1 50  ? 44.622  93.459  22.611  1.00 9.07  ? 50   PHE C CD2 1 
ATOM   2595  C  CE1 . PHE C  1 50  ? 47.297  93.485  23.389  1.00 11.42 ? 50   PHE C CE1 1 
ATOM   2596  C  CE2 . PHE C  1 50  ? 45.590  93.960  21.754  1.00 12.49 ? 50   PHE C CE2 1 
ATOM   2597  C  CZ  . PHE C  1 50  ? 46.930  93.969  22.149  1.00 11.97 ? 50   PHE C CZ  1 
ATOM   2598  N  N   . GLY C  1 51  ? 43.470  90.311  27.278  1.00 5.00  ? 51   GLY C N   1 
ATOM   2599  C  CA  . GLY C  1 51  ? 42.523  89.855  28.309  1.00 5.00  ? 51   GLY C CA  1 
ATOM   2600  C  C   . GLY C  1 51  ? 41.763  91.110  28.721  1.00 5.15  ? 51   GLY C C   1 
ATOM   2601  O  O   . GLY C  1 51  ? 41.592  91.385  29.885  1.00 5.00  ? 51   GLY C O   1 
ATOM   2602  N  N   . ASP C  1 52  ? 41.259  91.854  27.730  1.00 5.08  ? 52   ASP C N   1 
ATOM   2603  C  CA  . ASP C  1 52  ? 40.647  93.149  27.989  1.00 5.58  ? 52   ASP C CA  1 
ATOM   2604  C  C   . ASP C  1 52  ? 39.166  93.099  27.563  1.00 6.18  ? 52   ASP C C   1 
ATOM   2605  O  O   . ASP C  1 52  ? 38.855  93.007  26.358  1.00 5.77  ? 52   ASP C O   1 
ATOM   2606  C  CB  . ASP C  1 52  ? 41.412  94.212  27.167  1.00 5.70  ? 52   ASP C CB  1 
ATOM   2607  C  CG  . ASP C  1 52  ? 40.870  95.611  27.359  1.00 7.89  ? 52   ASP C CG  1 
ATOM   2608  O  OD1 . ASP C  1 52  ? 39.692  95.765  27.730  1.00 6.70  ? 52   ASP C OD1 1 
ATOM   2609  O  OD2 . ASP C  1 52  ? 41.568  96.628  27.129  1.00 9.57  ? 52   ASP C OD2 1 
ATOM   2610  N  N   . ASN C  1 53  ? 38.258  93.135  28.537  1.00 6.67  ? 53   ASN C N   1 
ATOM   2611  C  CA  . ASN C  1 53  ? 36.834  93.006  28.191  1.00 7.75  ? 53   ASN C CA  1 
ATOM   2612  C  C   . ASN C  1 53  ? 36.114  94.325  28.476  1.00 7.13  ? 53   ASN C C   1 
ATOM   2613  O  O   . ASN C  1 53  ? 34.902  94.348  28.719  1.00 6.24  ? 53   ASN C O   1 
ATOM   2614  C  CB  . ASN C  1 53  ? 36.163  91.813  28.950  1.00 10.24 ? 53   ASN C CB  1 
ATOM   2615  C  CG  . ASN C  1 53  ? 36.619  90.377  28.426  1.00 17.13 ? 53   ASN C CG  1 
ATOM   2616  O  OD1 . ASN C  1 53  ? 37.403  90.227  27.460  1.00 24.64 ? 53   ASN C OD1 1 
ATOM   2617  N  ND2 . ASN C  1 53  ? 36.123  89.312  29.122  1.00 23.80 ? 53   ASN C ND2 1 
ATOM   2618  N  N   . THR C  1 54  ? 36.868  95.418  28.479  1.00 5.84  ? 54   THR C N   1 
ATOM   2619  C  CA  . THR C  1 54  ? 36.286  96.724  28.775  1.00 7.50  ? 54   THR C CA  1 
ATOM   2620  C  C   . THR C  1 54  ? 35.232  97.171  27.761  1.00 8.18  ? 54   THR C C   1 
ATOM   2621  O  O   . THR C  1 54  ? 34.343  97.970  28.084  1.00 8.45  ? 54   THR C O   1 
ATOM   2622  C  CB  . THR C  1 54  ? 37.330  97.828  28.901  1.00 7.87  ? 54   THR C CB  1 
ATOM   2623  O  OG1 . THR C  1 54  ? 38.099  97.915  27.693  1.00 7.16  ? 54   THR C OG1 1 
ATOM   2624  C  CG2 . THR C  1 54  ? 38.339  97.522  30.039  1.00 9.93  ? 54   THR C CG2 1 
ATOM   2625  N  N   . ALA C  1 55  ? 35.329  96.675  26.555  1.00 7.91  ? 55   ALA C N   1 
ATOM   2626  C  CA  . ALA C  1 55  ? 34.303  96.945  25.546  1.00 10.11 ? 55   ALA C CA  1 
ATOM   2627  C  C   . ALA C  1 55  ? 33.774  95.619  25.033  1.00 11.22 ? 55   ALA C C   1 
ATOM   2628  O  O   . ALA C  1 55  ? 33.643  95.404  23.811  1.00 13.37 ? 55   ALA C O   1 
ATOM   2629  C  CB  . ALA C  1 55  ? 34.882  97.771  24.403  1.00 11.18 ? 55   ALA C CB  1 
ATOM   2630  N  N   . GLY C  1 56  ? 33.520  94.703  25.957  1.00 10.15 ? 56   GLY C N   1 
ATOM   2631  C  CA  . GLY C  1 56  ? 33.024  93.389  25.592  1.00 10.00 ? 56   GLY C CA  1 
ATOM   2632  C  C   . GLY C  1 56  ? 34.101  92.629  24.802  1.00 9.44  ? 56   GLY C C   1 
ATOM   2633  O  O   . GLY C  1 56  ? 35.314  92.875  24.955  1.00 8.44  ? 56   GLY C O   1 
ATOM   2634  N  N   . CYS C  1 57  ? 33.657  91.749  23.908  1.00 7.65  ? 57   CYS C N   1 
ATOM   2635  C  CA  . CYS C  1 57  ? 34.612  90.910  23.206  1.00 8.70  ? 57   CYS C CA  1 
ATOM   2636  C  C   . CYS C  1 57  ? 35.481  91.697  22.221  1.00 7.42  ? 57   CYS C C   1 
ATOM   2637  O  O   . CYS C  1 57  ? 36.550  91.246  21.828  1.00 6.94  ? 57   CYS C O   1 
ATOM   2638  C  CB  . CYS C  1 57  ? 33.848  89.769  22.513  1.00 8.62  ? 57   CYS C CB  1 
ATOM   2639  S  SG  . CYS C  1 57  ? 33.118  88.675  23.780  1.00 15.83 ? 57   CYS C SG  1 
ATOM   2640  N  N   . THR C  1 58  ? 35.000  92.856  21.802  1.00 6.94  ? 58   THR C N   1 
ATOM   2641  C  CA  . THR C  1 58  ? 35.757  93.668  20.851  1.00 8.30  ? 58   THR C CA  1 
ATOM   2642  C  C   . THR C  1 58  ? 37.154  94.071  21.316  1.00 6.64  ? 58   THR C C   1 
ATOM   2643  O  O   . THR C  1 58  ? 38.111  94.059  20.552  1.00 5.82  ? 58   THR C O   1 
ATOM   2644  C  CB  . THR C  1 58  ? 34.923  94.882  20.462  1.00 9.53  ? 58   THR C CB  1 
ATOM   2645  O  OG1 . THR C  1 58  ? 33.739  94.387  19.822  1.00 14.86 ? 58   THR C OG1 1 
ATOM   2646  C  CG2 . THR C  1 58  ? 35.604  95.635  19.350  1.00 11.76 ? 58   THR C CG2 1 
ATOM   2647  N  N   . SER C  1 59  ? 37.266  94.415  22.588  1.00 5.74  ? 59   SER C N   1 
ATOM   2648  C  CA  . SER C  1 59  ? 38.534  94.878  23.146  1.00 5.65  ? 59   SER C CA  1 
ATOM   2649  C  C   . SER C  1 59  ? 39.595  93.790  23.333  1.00 5.00  ? 59   SER C C   1 
ATOM   2650  O  O   . SER C  1 59  ? 40.714  94.094  23.695  1.00 5.00  ? 59   SER C O   1 
ATOM   2651  C  CB  . SER C  1 59  ? 38.306  95.684  24.445  1.00 5.36  ? 59   SER C CB  1 
ATOM   2652  O  OG  . SER C  1 59  ? 37.274  95.136  25.233  1.00 9.70  ? 59   SER C OG  1 
ATOM   2653  N  N   . ALA C  1 60  ? 39.270  92.535  23.018  1.00 5.00  ? 60   ALA C N   1 
ATOM   2654  C  CA  . ALA C  1 60  ? 40.256  91.472  23.108  1.00 5.00  ? 60   ALA C CA  1 
ATOM   2655  C  C   . ALA C  1 60  ? 41.259  91.547  21.959  1.00 5.00  ? 60   ALA C C   1 
ATOM   2656  O  O   . ALA C  1 60  ? 42.217  90.789  21.929  1.00 5.02  ? 60   ALA C O   1 
ATOM   2657  C  CB  . ALA C  1 60  ? 39.564  90.123  23.023  1.00 5.00  ? 60   ALA C CB  1 
ATOM   2658  N  N   . GLY C  1 61  ? 40.992  92.362  20.956  1.00 5.00  ? 61   GLY C N   1 
ATOM   2659  C  CA  . GLY C  1 61  ? 41.971  92.488  19.908  1.00 5.00  ? 61   GLY C CA  1 
ATOM   2660  C  C   . GLY C  1 61  ? 41.940  91.323  18.932  1.00 5.00  ? 61   GLY C C   1 
ATOM   2661  O  O   . GLY C  1 61  ? 40.984  90.557  18.889  1.00 5.00  ? 61   GLY C O   1 
ATOM   2662  N  N   . PRO C  1 62  ? 42.997  91.183  18.148  1.00 5.19  ? 62   PRO C N   1 
ATOM   2663  C  CA  . PRO C  1 62  ? 43.052  90.141  17.108  1.00 5.61  ? 62   PRO C CA  1 
ATOM   2664  C  C   . PRO C  1 62  ? 43.519  88.818  17.690  1.00 5.50  ? 62   PRO C C   1 
ATOM   2665  O  O   . PRO C  1 62  ? 43.700  88.736  18.912  1.00 5.87  ? 62   PRO C O   1 
ATOM   2666  C  CB  . PRO C  1 62  ? 44.090  90.704  16.129  1.00 5.78  ? 62   PRO C CB  1 
ATOM   2667  C  CG  . PRO C  1 62  ? 45.117  91.325  17.072  1.00 7.09  ? 62   PRO C CG  1 
ATOM   2668  C  CD  . PRO C  1 62  ? 44.235  91.985  18.195  1.00 5.42  ? 62   PRO C CD  1 
ATOM   2669  N  N   . HIS C  1 63  ? 43.696  87.785  16.847  1.00 5.26  ? 63   HIS C N   1 
ATOM   2670  C  CA  . HIS C  1 63  ? 44.195  86.505  17.365  1.00 5.87  ? 63   HIS C CA  1 
ATOM   2671  C  C   . HIS C  1 63  ? 45.594  86.664  17.962  1.00 6.22  ? 63   HIS C C   1 
ATOM   2672  O  O   . HIS C  1 63  ? 46.415  87.435  17.447  1.00 5.53  ? 63   HIS C O   1 
ATOM   2673  C  CB  . HIS C  1 63  ? 44.241  85.448  16.245  1.00 6.24  ? 63   HIS C CB  1 
ATOM   2674  C  CG  . HIS C  1 63  ? 42.896  85.149  15.688  1.00 7.42  ? 63   HIS C CG  1 
ATOM   2675  N  ND1 . HIS C  1 63  ? 42.689  84.312  14.617  1.00 6.13  ? 63   HIS C ND1 1 
ATOM   2676  C  CD2 . HIS C  1 63  ? 41.673  85.620  16.049  1.00 9.72  ? 63   HIS C CD2 1 
ATOM   2677  C  CE1 . HIS C  1 63  ? 41.391  84.248  14.364  1.00 8.77  ? 63   HIS C CE1 1 
ATOM   2678  N  NE2 . HIS C  1 63  ? 40.759  85.049  15.205  1.00 11.69 ? 63   HIS C NE2 1 
ATOM   2679  N  N   . PHE C  1 64  ? 45.853  85.954  19.057  1.00 5.16  ? 64   PHE C N   1 
ATOM   2680  C  CA  . PHE C  1 64  ? 47.175  85.982  19.687  1.00 5.00  ? 64   PHE C CA  1 
ATOM   2681  C  C   . PHE C  1 64  ? 48.170  85.451  18.667  1.00 5.77  ? 64   PHE C C   1 
ATOM   2682  O  O   . PHE C  1 64  ? 48.035  84.300  18.231  1.00 5.72  ? 64   PHE C O   1 
ATOM   2683  C  CB  . PHE C  1 64  ? 47.136  85.069  20.915  1.00 5.22  ? 64   PHE C CB  1 
ATOM   2684  C  CG  . PHE C  1 64  ? 48.456  84.979  21.658  1.00 5.69  ? 64   PHE C CG  1 
ATOM   2685  C  CD1 . PHE C  1 64  ? 49.243  86.105  21.832  1.00 6.92  ? 64   PHE C CD1 1 
ATOM   2686  C  CD2 . PHE C  1 64  ? 48.861  83.770  22.214  1.00 5.45  ? 64   PHE C CD2 1 
ATOM   2687  C  CE1 . PHE C  1 64  ? 50.452  86.018  22.544  1.00 7.46  ? 64   PHE C CE1 1 
ATOM   2688  C  CE2 . PHE C  1 64  ? 50.085  83.679  22.926  1.00 5.58  ? 64   PHE C CE2 1 
ATOM   2689  C  CZ  . PHE C  1 64  ? 50.849  84.795  23.088  1.00 6.04  ? 64   PHE C CZ  1 
ATOM   2690  N  N   . ASN C  1 65  ? 49.176  86.256  18.311  1.00 5.33  ? 65   ASN C N   1 
ATOM   2691  C  CA  . ASN C  1 65  ? 50.029  85.915  17.157  1.00 6.72  ? 65   ASN C CA  1 
ATOM   2692  C  C   . ASN C  1 65  ? 51.452  86.472  17.373  1.00 7.83  ? 65   ASN C C   1 
ATOM   2693  O  O   . ASN C  1 65  ? 51.902  87.387  16.650  1.00 6.46  ? 65   ASN C O   1 
ATOM   2694  C  CB  . ASN C  1 65  ? 49.400  86.568  15.923  1.00 7.01  ? 65   ASN C CB  1 
ATOM   2695  C  CG  . ASN C  1 65  ? 50.149  86.275  14.636  1.00 8.64  ? 65   ASN C CG  1 
ATOM   2696  O  OD1 . ASN C  1 65  ? 50.854  85.274  14.509  1.00 8.51  ? 65   ASN C OD1 1 
ATOM   2697  N  ND2 . ASN C  1 65  ? 49.986  87.161  13.671  1.00 9.55  ? 65   ASN C ND2 1 
ATOM   2698  N  N   . PRO C  1 66  ? 52.143  85.945  18.380  1.00 8.27  ? 66   PRO C N   1 
ATOM   2699  C  CA  . PRO C  1 66  ? 53.475  86.468  18.731  1.00 9.52  ? 66   PRO C CA  1 
ATOM   2700  C  C   . PRO C  1 66  ? 54.515  86.216  17.654  1.00 10.60 ? 66   PRO C C   1 
ATOM   2701  O  O   . PRO C  1 66  ? 55.489  86.964  17.605  1.00 9.60  ? 66   PRO C O   1 
ATOM   2702  C  CB  . PRO C  1 66  ? 53.849  85.690  20.007  1.00 9.59  ? 66   PRO C CB  1 
ATOM   2703  C  CG  . PRO C  1 66  ? 52.997  84.411  19.967  1.00 9.61  ? 66   PRO C CG  1 
ATOM   2704  C  CD  . PRO C  1 66  ? 51.692  84.882  19.307  1.00 8.85  ? 66   PRO C CD  1 
ATOM   2705  N  N   . LEU C  1 67  ? 54.315  85.181  16.836  1.00 11.49 ? 67   LEU C N   1 
ATOM   2706  C  CA  . LEU C  1 67  ? 55.220  84.866  15.725  1.00 12.98 ? 67   LEU C CA  1 
ATOM   2707  C  C   . LEU C  1 67  ? 54.877  85.609  14.424  1.00 13.49 ? 67   LEU C C   1 
ATOM   2708  O  O   . LEU C  1 67  ? 55.512  85.367  13.380  1.00 12.56 ? 67   LEU C O   1 
ATOM   2709  C  CB  . LEU C  1 67  ? 55.255  83.356  15.466  1.00 13.24 ? 67   LEU C CB  1 
ATOM   2710  C  CG  . LEU C  1 67  ? 55.851  82.566  16.632  1.00 15.90 ? 67   LEU C CG  1 
ATOM   2711  C  CD1 . LEU C  1 67  ? 55.946  81.076  16.299  1.00 15.89 ? 67   LEU C CD1 1 
ATOM   2712  C  CD2 . LEU C  1 67  ? 57.230  83.137  17.041  1.00 18.44 ? 67   LEU C CD2 1 
ATOM   2713  N  N   . SER C  1 68  ? 53.890  86.505  14.475  1.00 12.34 ? 68   SER C N   1 
ATOM   2714  C  CA  . SER C  1 68  ? 53.505  87.285  13.287  1.00 13.57 ? 68   SER C CA  1 
ATOM   2715  C  C   . SER C  1 68  ? 53.289  86.421  12.026  1.00 13.82 ? 68   SER C C   1 
ATOM   2716  O  O   . SER C  1 68  ? 53.855  86.679  10.939  1.00 13.40 ? 68   SER C O   1 
ATOM   2717  C  CB  . SER C  1 68  ? 54.494  88.421  12.998  1.00 13.78 ? 68   SER C CB  1 
ATOM   2718  O  OG  . SER C  1 68  ? 54.719  89.231  14.148  1.00 14.90 ? 68   SER C OG  1 
ATOM   2719  N  N   . ARG C  1 69  ? 52.472  85.390  12.171  1.00 12.58 ? 69   ARG C N   1 
ATOM   2720  C  CA  . ARG C  1 69  ? 52.165  84.486  11.073  1.00 13.14 ? 69   ARG C CA  1 
ATOM   2721  C  C   . ARG C  1 69  ? 50.747  84.734  10.550  1.00 12.07 ? 69   ARG C C   1 
ATOM   2722  O  O   . ARG C  1 69  ? 50.020  85.553  11.126  1.00 12.49 ? 69   ARG C O   1 
ATOM   2723  C  CB  . ARG C  1 69  ? 52.417  83.017  11.512  1.00 12.87 ? 69   ARG C CB  1 
ATOM   2724  C  CG  . ARG C  1 69  ? 53.966  82.684  11.633  1.00 18.47 ? 69   ARG C CG  1 
ATOM   2725  C  CD  . ARG C  1 69  ? 54.326  81.181  11.723  1.00 24.13 ? 69   ARG C CD  1 
ATOM   2726  N  NE  . ARG C  1 69  ? 55.688  80.957  12.208  1.00 25.50 ? 69   ARG C NE  1 
ATOM   2727  C  CZ  . ARG C  1 69  ? 56.159  79.793  12.665  1.00 28.57 ? 69   ARG C CZ  1 
ATOM   2728  N  NH1 . ARG C  1 69  ? 55.380  78.713  12.697  1.00 28.37 ? 69   ARG C NH1 1 
ATOM   2729  N  NH2 . ARG C  1 69  ? 57.424  79.709  13.089  1.00 28.04 ? 69   ARG C NH2 1 
ATOM   2730  N  N   . LYS C  1 70  ? 50.365  84.067  9.458   1.00 10.87 ? 70   LYS C N   1 
ATOM   2731  C  CA  . LYS C  1 70  ? 49.013  84.192  8.922   1.00 10.77 ? 70   LYS C CA  1 
ATOM   2732  C  C   . LYS C  1 70  ? 48.079  83.200  9.615   1.00 9.20  ? 70   LYS C C   1 
ATOM   2733  O  O   . LYS C  1 70  ? 48.512  82.205  10.212  1.00 8.42  ? 70   LYS C O   1 
ATOM   2734  C  CB  . LYS C  1 70  ? 48.979  83.988  7.397   1.00 10.91 ? 70   LYS C CB  1 
ATOM   2735  C  CG  . LYS C  1 70  ? 49.804  85.044  6.630   1.00 16.19 ? 70   LYS C CG  1 
ATOM   2736  C  CD  . LYS C  1 70  ? 49.271  86.456  6.901   1.00 21.87 ? 70   LYS C CD  1 
ATOM   2737  C  CE  . LYS C  1 70  ? 49.981  87.581  6.101   1.00 21.64 ? 70   LYS C CE  1 
ATOM   2738  N  NZ  . LYS C  1 70  ? 49.833  87.445  4.617   1.00 27.09 ? 70   LYS C NZ  1 
ATOM   2739  N  N   . HIS C  1 71  ? 46.789  83.488  9.553   1.00 7.61  ? 71   HIS C N   1 
ATOM   2740  C  CA  . HIS C  1 71  ? 45.805  82.620  10.163  1.00 7.72  ? 71   HIS C CA  1 
ATOM   2741  C  C   . HIS C  1 71  ? 45.755  81.236  9.521   1.00 8.53  ? 71   HIS C C   1 
ATOM   2742  O  O   . HIS C  1 71  ? 45.948  81.074  8.304   1.00 7.66  ? 71   HIS C O   1 
ATOM   2743  C  CB  . HIS C  1 71  ? 44.426  83.273  10.075  1.00 7.44  ? 71   HIS C CB  1 
ATOM   2744  C  CG  . HIS C  1 71  ? 43.333  82.452  10.673  1.00 8.29  ? 71   HIS C CG  1 
ATOM   2745  N  ND1 . HIS C  1 71  ? 43.071  82.427  12.032  1.00 7.52  ? 71   HIS C ND1 1 
ATOM   2746  C  CD2 . HIS C  1 71  ? 42.416  81.638  10.089  1.00 7.18  ? 71   HIS C CD2 1 
ATOM   2747  C  CE1 . HIS C  1 71  ? 42.030  81.640  12.250  1.00 6.83  ? 71   HIS C CE1 1 
ATOM   2748  N  NE2 . HIS C  1 71  ? 41.624  81.145  11.094  1.00 8.08  ? 71   HIS C NE2 1 
ATOM   2749  N  N   . GLY C  1 72  ? 45.524  80.224  10.343  1.00 7.19  ? 72   GLY C N   1 
ATOM   2750  C  CA  . GLY C  1 72  ? 45.401  78.870  9.855   1.00 7.73  ? 72   GLY C CA  1 
ATOM   2751  C  C   . GLY C  1 72  ? 44.548  78.032  10.782  1.00 8.70  ? 72   GLY C C   1 
ATOM   2752  O  O   . GLY C  1 72  ? 43.936  78.564  11.717  1.00 7.28  ? 72   GLY C O   1 
ATOM   2753  N  N   . GLY C  1 73  ? 44.492  76.725  10.518  1.00 8.23  ? 73   GLY C N   1 
ATOM   2754  C  CA  . GLY C  1 73  ? 43.820  75.808  11.424  1.00 8.45  ? 73   GLY C CA  1 
ATOM   2755  C  C   . GLY C  1 73  ? 44.865  75.332  12.422  1.00 8.27  ? 73   GLY C C   1 
ATOM   2756  O  O   . GLY C  1 73  ? 46.047  75.542  12.182  1.00 8.93  ? 73   GLY C O   1 
ATOM   2757  N  N   . PRO C  1 74  ? 44.478  74.713  13.536  1.00 8.90  ? 74   PRO C N   1 
ATOM   2758  C  CA  . PRO C  1 74  ? 45.471  74.300  14.542  1.00 8.80  ? 74   PRO C CA  1 
ATOM   2759  C  C   . PRO C  1 74  ? 46.527  73.279  14.018  1.00 9.81  ? 74   PRO C C   1 
ATOM   2760  O  O   . PRO C  1 74  ? 47.618  73.194  14.565  1.00 8.01  ? 74   PRO C O   1 
ATOM   2761  C  CB  . PRO C  1 74  ? 44.620  73.641  15.646  1.00 10.39 ? 74   PRO C CB  1 
ATOM   2762  C  CG  . PRO C  1 74  ? 43.307  73.315  14.980  1.00 10.24 ? 74   PRO C CG  1 
ATOM   2763  C  CD  . PRO C  1 74  ? 43.098  74.482  13.996  1.00 8.96  ? 74   PRO C CD  1 
ATOM   2764  N  N   . LYS C  1 75  ? 46.204  72.535  12.981  1.00 10.71 ? 75   LYS C N   1 
ATOM   2765  C  CA  . LYS C  1 75  ? 47.163  71.551  12.433  1.00 12.89 ? 75   LYS C CA  1 
ATOM   2766  C  C   . LYS C  1 75  ? 48.173  72.118  11.418  1.00 13.91 ? 75   LYS C C   1 
ATOM   2767  O  O   . LYS C  1 75  ? 49.071  71.400  10.953  1.00 13.71 ? 75   LYS C O   1 
ATOM   2768  C  CB  . LYS C  1 75  ? 46.420  70.412  11.761  1.00 13.78 ? 75   LYS C CB  1 
ATOM   2769  C  CG  . LYS C  1 75  ? 45.411  69.665  12.611  1.00 18.65 ? 75   LYS C CG  1 
ATOM   2770  C  CD  . LYS C  1 75  ? 44.520  68.868  11.672  1.00 25.73 ? 75   LYS C CD  1 
ATOM   2771  C  CE  . LYS C  1 75  ? 43.834  67.679  12.355  1.00 29.01 ? 75   LYS C CE  1 
ATOM   2772  N  NZ  . LYS C  1 75  ? 44.003  66.445  11.495  1.00 32.65 ? 75   LYS C NZ  1 
ATOM   2773  N  N   . ASP C  1 76  ? 48.012  73.376  11.037  1.00 14.25 ? 76   ASP C N   1 
ATOM   2774  C  CA  . ASP C  1 76  ? 48.939  74.038  10.099  1.00 16.45 ? 76   ASP C CA  1 
ATOM   2775  C  C   . ASP C  1 76  ? 50.234  74.605  10.738  1.00 16.37 ? 76   ASP C C   1 
ATOM   2776  O  O   . ASP C  1 76  ? 50.181  75.069  11.861  1.00 16.58 ? 76   ASP C O   1 
ATOM   2777  C  CB  . ASP C  1 76  ? 48.211  75.208  9.432   1.00 15.96 ? 76   ASP C CB  1 
ATOM   2778  C  CG  . ASP C  1 76  ? 47.033  74.782  8.590   1.00 19.19 ? 76   ASP C CG  1 
ATOM   2779  O  OD1 . ASP C  1 76  ? 47.047  73.683  7.990   1.00 23.85 ? 76   ASP C OD1 1 
ATOM   2780  O  OD2 . ASP C  1 76  ? 46.033  75.518  8.425   1.00 23.35 ? 76   ASP C OD2 1 
ATOM   2781  N  N   . GLU C  1 77  ? 51.387  74.620  10.035  1.00 17.72 ? 77   GLU C N   1 
ATOM   2782  C  CA  . GLU C  1 77  ? 52.572  75.294  10.624  1.00 17.88 ? 77   GLU C CA  1 
ATOM   2783  C  C   . GLU C  1 77  ? 52.355  76.791  10.563  1.00 16.54 ? 77   GLU C C   1 
ATOM   2784  O  O   . GLU C  1 77  ? 52.650  77.527  11.539  1.00 17.03 ? 77   GLU C O   1 
ATOM   2785  C  CB  . GLU C  1 77  ? 53.909  74.962  9.949   1.00 19.63 ? 77   GLU C CB  1 
ATOM   2786  C  CG  . GLU C  1 77  ? 55.010  75.957  10.336  1.00 23.54 ? 77   GLU C CG  1 
ATOM   2787  C  CD  . GLU C  1 77  ? 55.342  75.935  11.826  1.00 30.41 ? 77   GLU C CD  1 
ATOM   2788  O  OE1 . GLU C  1 77  ? 54.531  75.382  12.606  1.00 33.21 ? 77   GLU C OE1 1 
ATOM   2789  O  OE2 . GLU C  1 77  ? 56.416  76.465  12.236  1.00 33.02 ? 77   GLU C OE2 1 
ATOM   2790  N  N   . GLU C  1 78  ? 51.791  77.237  9.439   1.00 13.85 ? 78   GLU C N   1 
ATOM   2791  C  CA  . GLU C  1 78  ? 51.383  78.641  9.333   1.00 12.32 ? 78   GLU C CA  1 
ATOM   2792  C  C   . GLU C  1 78  ? 50.027  78.810  10.046  1.00 10.03 ? 78   GLU C C   1 
ATOM   2793  O  O   . GLU C  1 78  ? 48.960  78.439  9.531   1.00 6.57  ? 78   GLU C O   1 
ATOM   2794  C  CB  . GLU C  1 78  ? 51.313  79.123  7.861   1.00 12.55 ? 78   GLU C CB  1 
ATOM   2795  C  CG  . GLU C  1 78  ? 51.138  80.633  7.681   1.00 15.18 ? 78   GLU C CG  1 
ATOM   2796  C  CD  . GLU C  1 78  ? 52.388  81.464  8.017   1.00 20.01 ? 78   GLU C CD  1 
ATOM   2797  O  OE1 . GLU C  1 78  ? 53.480  80.866  8.160   1.00 24.01 ? 78   GLU C OE1 1 
ATOM   2798  O  OE2 . GLU C  1 78  ? 52.294  82.725  8.118   1.00 17.23 ? 78   GLU C OE2 1 
ATOM   2799  N  N   . ARG C  1 79  ? 50.079  79.351  11.256  1.00 8.97  ? 79   ARG C N   1 
ATOM   2800  C  CA  . ARG C  1 79  ? 48.877  79.621  12.009  1.00 7.83  ? 79   ARG C CA  1 
ATOM   2801  C  C   . ARG C  1 79  ? 49.266  80.583  13.085  1.00 7.19  ? 79   ARG C C   1 
ATOM   2802  O  O   . ARG C  1 79  ? 50.456  80.747  13.427  1.00 6.87  ? 79   ARG C O   1 
ATOM   2803  C  CB  . ARG C  1 79  ? 48.327  78.365  12.702  1.00 7.84  ? 79   ARG C CB  1 
ATOM   2804  C  CG  . ARG C  1 79  ? 49.353  77.634  13.640  1.00 8.91  ? 79   ARG C CG  1 
ATOM   2805  C  CD  . ARG C  1 79  ? 48.698  76.592  14.547  1.00 10.22 ? 79   ARG C CD  1 
ATOM   2806  N  NE  . ARG C  1 79  ? 48.174  77.143  15.824  1.00 5.91  ? 79   ARG C NE  1 
ATOM   2807  C  CZ  . ARG C  1 79  ? 47.876  76.357  16.860  1.00 9.45  ? 79   ARG C CZ  1 
ATOM   2808  N  NH1 . ARG C  1 79  ? 47.976  75.032  16.735  1.00 6.64  ? 79   ARG C NH1 1 
ATOM   2809  N  NH2 . ARG C  1 79  ? 47.452  76.872  18.025  1.00 5.00  ? 79   ARG C NH2 1 
ATOM   2810  N  N   . HIS C  1 80  ? 48.252  81.222  13.646  1.00 7.32  ? 80   HIS C N   1 
ATOM   2811  C  CA  . HIS C  1 80  ? 48.475  82.056  14.821  1.00 6.16  ? 80   HIS C CA  1 
ATOM   2812  C  C   . HIS C  1 80  ? 48.558  81.149  16.034  1.00 5.58  ? 80   HIS C C   1 
ATOM   2813  O  O   . HIS C  1 80  ? 47.934  80.092  16.036  1.00 5.38  ? 80   HIS C O   1 
ATOM   2814  C  CB  . HIS C  1 80  ? 47.257  82.938  15.004  1.00 6.44  ? 80   HIS C CB  1 
ATOM   2815  C  CG  . HIS C  1 80  ? 47.042  83.897  13.868  1.00 5.81  ? 80   HIS C CG  1 
ATOM   2816  N  ND1 . HIS C  1 80  ? 45.793  84.285  13.445  1.00 5.00  ? 80   HIS C ND1 1 
ATOM   2817  C  CD2 . HIS C  1 80  ? 47.934  84.557  13.086  1.00 7.69  ? 80   HIS C CD2 1 
ATOM   2818  C  CE1 . HIS C  1 80  ? 45.920  85.186  12.484  1.00 7.28  ? 80   HIS C CE1 1 
ATOM   2819  N  NE2 . HIS C  1 80  ? 47.215  85.362  12.234  1.00 5.00  ? 80   HIS C NE2 1 
ATOM   2820  N  N   . VAL C  1 81  ? 49.255  81.592  17.089  1.00 5.00  ? 81   VAL C N   1 
ATOM   2821  C  CA  . VAL C  1 81  ? 49.270  80.760  18.295  1.00 5.23  ? 81   VAL C CA  1 
ATOM   2822  C  C   . VAL C  1 81  ? 47.838  80.524  18.761  1.00 5.00  ? 81   VAL C C   1 
ATOM   2823  O  O   . VAL C  1 81  ? 47.497  79.421  19.143  1.00 5.00  ? 81   VAL C O   1 
ATOM   2824  C  CB  . VAL C  1 81  ? 50.136  81.343  19.400  1.00 5.00  ? 81   VAL C CB  1 
ATOM   2825  C  CG1 . VAL C  1 81  ? 49.935  80.601  20.750  1.00 6.29  ? 81   VAL C CG1 1 
ATOM   2826  C  CG2 . VAL C  1 81  ? 51.604  81.246  18.924  1.00 6.81  ? 81   VAL C CG2 1 
ATOM   2827  N  N   . GLY C  1 82  ? 46.992  81.543  18.675  1.00 5.00  ? 82   GLY C N   1 
ATOM   2828  C  CA  . GLY C  1 82  ? 45.628  81.368  19.198  1.00 5.00  ? 82   GLY C CA  1 
ATOM   2829  C  C   . GLY C  1 82  ? 44.648  80.620  18.319  1.00 6.30  ? 82   GLY C C   1 
ATOM   2830  O  O   . GLY C  1 82  ? 43.453  80.530  18.661  1.00 5.35  ? 82   GLY C O   1 
ATOM   2831  N  N   . ASP C  1 83  ? 45.116  80.050  17.202  1.00 5.09  ? 83   ASP C N   1 
ATOM   2832  C  CA  . ASP C  1 83  ? 44.210  79.389  16.272  1.00 5.41  ? 83   ASP C CA  1 
ATOM   2833  C  C   . ASP C  1 83  ? 43.819  77.991  16.714  1.00 6.40  ? 83   ASP C C   1 
ATOM   2834  O  O   . ASP C  1 83  ? 44.521  77.013  16.388  1.00 6.82  ? 83   ASP C O   1 
ATOM   2835  C  CB  . ASP C  1 83  ? 44.814  79.327  14.853  1.00 6.03  ? 83   ASP C CB  1 
ATOM   2836  C  CG  . ASP C  1 83  ? 44.843  80.675  14.192  1.00 7.64  ? 83   ASP C CG  1 
ATOM   2837  O  OD1 . ASP C  1 83  ? 44.131  81.582  14.686  1.00 5.00  ? 83   ASP C OD1 1 
ATOM   2838  O  OD2 . ASP C  1 83  ? 45.569  80.933  13.189  1.00 7.73  ? 83   ASP C OD2 1 
ATOM   2839  N  N   . LEU C  1 84  ? 42.696  77.873  17.427  1.00 5.00  ? 84   LEU C N   1 
ATOM   2840  C  CA  . LEU C  1 84  ? 42.244  76.545  17.853  1.00 5.00  ? 84   LEU C CA  1 
ATOM   2841  C  C   . LEU C  1 84  ? 41.147  75.955  16.961  1.00 6.37  ? 84   LEU C C   1 
ATOM   2842  O  O   . LEU C  1 84  ? 40.500  74.978  17.347  1.00 7.55  ? 84   LEU C O   1 
ATOM   2843  C  CB  . LEU C  1 84  ? 41.769  76.539  19.331  1.00 5.00  ? 84   LEU C CB  1 
ATOM   2844  C  CG  . LEU C  1 84  ? 42.882  76.937  20.298  1.00 6.28  ? 84   LEU C CG  1 
ATOM   2845  C  CD1 . LEU C  1 84  ? 42.332  77.018  21.737  1.00 7.12  ? 84   LEU C CD1 1 
ATOM   2846  C  CD2 . LEU C  1 84  ? 44.081  75.982  20.255  1.00 7.25  ? 84   LEU C CD2 1 
ATOM   2847  N  N   . GLY C  1 85  ? 40.937  76.551  15.797  1.00 5.00  ? 85   GLY C N   1 
ATOM   2848  C  CA  . GLY C  1 85  ? 40.053  75.981  14.786  1.00 6.46  ? 85   GLY C CA  1 
ATOM   2849  C  C   . GLY C  1 85  ? 38.577  76.150  15.117  1.00 6.42  ? 85   GLY C C   1 
ATOM   2850  O  O   . GLY C  1 85  ? 38.142  77.247  15.486  1.00 7.12  ? 85   GLY C O   1 
ATOM   2851  N  N   . ASN C  1 86  ? 37.818  75.072  14.946  1.00 5.84  ? 86   ASN C N   1 
ATOM   2852  C  CA  . ASN C  1 86  ? 36.383  75.117  15.225  1.00 5.00  ? 86   ASN C CA  1 
ATOM   2853  C  C   . ASN C  1 86  ? 35.961  74.234  16.370  1.00 5.64  ? 86   ASN C C   1 
ATOM   2854  O  O   . ASN C  1 86  ? 36.634  73.246  16.676  1.00 5.69  ? 86   ASN C O   1 
ATOM   2855  C  CB  . ASN C  1 86  ? 35.597  74.637  14.006  1.00 5.37  ? 86   ASN C CB  1 
ATOM   2856  C  CG  . ASN C  1 86  ? 35.609  75.654  12.900  1.00 6.22  ? 86   ASN C CG  1 
ATOM   2857  O  OD1 . ASN C  1 86  ? 35.175  76.775  13.095  1.00 5.00  ? 86   ASN C OD1 1 
ATOM   2858  N  ND2 . ASN C  1 86  ? 36.180  75.283  11.746  1.00 7.69  ? 86   ASN C ND2 1 
ATOM   2859  N  N   . VAL C  1 87  ? 34.838  74.589  16.977  1.00 5.46  ? 87   VAL C N   1 
ATOM   2860  C  CA  . VAL C  1 87  ? 34.173  73.626  17.844  1.00 5.17  ? 87   VAL C CA  1 
ATOM   2861  C  C   . VAL C  1 87  ? 32.779  73.386  17.235  1.00 5.52  ? 87   VAL C C   1 
ATOM   2862  O  O   . VAL C  1 87  ? 32.199  74.264  16.581  1.00 6.14  ? 87   VAL C O   1 
ATOM   2863  C  CB  . VAL C  1 87  ? 34.030  74.106  19.304  1.00 5.41  ? 87   VAL C CB  1 
ATOM   2864  C  CG1 . VAL C  1 87  ? 35.444  74.258  19.932  1.00 5.86  ? 87   VAL C CG1 1 
ATOM   2865  C  CG2 . VAL C  1 87  ? 33.222  75.392  19.402  1.00 6.03  ? 87   VAL C CG2 1 
ATOM   2866  N  N   . THR C  1 88  ? 32.229  72.210  17.507  1.00 5.00  ? 88   THR C N   1 
ATOM   2867  C  CA  . THR C  1 88  ? 30.996  71.829  16.881  1.00 5.00  ? 88   THR C CA  1 
ATOM   2868  C  C   . THR C  1 88  ? 29.894  71.726  17.909  1.00 5.00  ? 88   THR C C   1 
ATOM   2869  O  O   . THR C  1 88  ? 30.043  71.037  18.932  1.00 5.00  ? 88   THR C O   1 
ATOM   2870  C  CB  . THR C  1 88  ? 31.208  70.456  16.223  1.00 5.00  ? 88   THR C CB  1 
ATOM   2871  O  OG1 . THR C  1 88  ? 32.148  70.581  15.148  1.00 6.00  ? 88   THR C OG1 1 
ATOM   2872  C  CG2 . THR C  1 88  ? 29.922  69.964  15.567  1.00 7.81  ? 88   THR C CG2 1 
ATOM   2873  N  N   . ALA C  1 89  ? 28.801  72.440  17.643  1.00 5.00  ? 89   ALA C N   1 
ATOM   2874  C  CA  . ALA C  1 89  ? 27.624  72.393  18.496  1.00 5.00  ? 89   ALA C CA  1 
ATOM   2875  C  C   . ALA C  1 89  ? 26.650  71.392  17.933  1.00 6.12  ? 89   ALA C C   1 
ATOM   2876  O  O   . ALA C  1 89  ? 26.445  71.331  16.705  1.00 5.79  ? 89   ALA C O   1 
ATOM   2877  C  CB  . ALA C  1 89  ? 26.951  73.764  18.581  1.00 6.02  ? 89   ALA C CB  1 
ATOM   2878  N  N   . ASP C  1 90  ? 26.068  70.607  18.835  1.00 5.49  ? 90   ASP C N   1 
ATOM   2879  C  CA  . ASP C  1 90  ? 25.142  69.554  18.427  1.00 6.52  ? 90   ASP C CA  1 
ATOM   2880  C  C   . ASP C  1 90  ? 23.761  70.126  18.166  1.00 6.24  ? 90   ASP C C   1 
ATOM   2881  O  O   . ASP C  1 90  ? 23.558  71.335  18.197  1.00 5.00  ? 90   ASP C O   1 
ATOM   2882  C  CB  . ASP C  1 90  ? 25.119  68.399  19.439  1.00 6.76  ? 90   ASP C CB  1 
ATOM   2883  C  CG  . ASP C  1 90  ? 24.608  68.820  20.822  1.00 8.91  ? 90   ASP C CG  1 
ATOM   2884  O  OD1 . ASP C  1 90  ? 23.928  69.854  20.941  1.00 8.37  ? 90   ASP C OD1 1 
ATOM   2885  O  OD2 . ASP C  1 90  ? 24.834  68.147  21.858  1.00 10.50 ? 90   ASP C OD2 1 
ATOM   2886  N  N   . LYS C  1 91  ? 22.790  69.258  17.907  1.00 7.14  ? 91   LYS C N   1 
ATOM   2887  C  CA  . LYS C  1 91  ? 21.453  69.766  17.621  1.00 7.77  ? 91   LYS C CA  1 
ATOM   2888  C  C   . LYS C  1 91  ? 20.776  70.526  18.758  1.00 8.39  ? 91   LYS C C   1 
ATOM   2889  O  O   . LYS C  1 91  ? 19.870  71.313  18.512  1.00 9.58  ? 91   LYS C O   1 
ATOM   2890  C  CB  . LYS C  1 91  ? 20.553  68.643  17.074  1.00 9.35  ? 91   LYS C CB  1 
ATOM   2891  C  CG  . LYS C  1 91  ? 19.568  68.045  18.031  1.00 14.81 ? 91   LYS C CG  1 
ATOM   2892  C  CD  . LYS C  1 91  ? 18.873  66.822  17.373  1.00 23.15 ? 91   LYS C CD  1 
ATOM   2893  C  CE  . LYS C  1 91  ? 17.552  67.165  16.676  1.00 27.45 ? 91   LYS C CE  1 
ATOM   2894  N  NZ  . LYS C  1 91  ? 16.914  65.935  16.099  1.00 29.33 ? 91   LYS C NZ  1 
ATOM   2895  N  N   . ASP C  1 92  ? 21.219  70.346  19.995  1.00 7.64  ? 92   ASP C N   1 
ATOM   2896  C  CA  . ASP C  1 92  ? 20.608  71.098  21.092  1.00 7.19  ? 92   ASP C CA  1 
ATOM   2897  C  C   . ASP C  1 92  ? 21.398  72.387  21.395  1.00 6.58  ? 92   ASP C C   1 
ATOM   2898  O  O   . ASP C  1 92  ? 21.133  73.046  22.383  1.00 7.70  ? 92   ASP C O   1 
ATOM   2899  C  CB  . ASP C  1 92  ? 20.578  70.277  22.375  1.00 7.75  ? 92   ASP C CB  1 
ATOM   2900  C  CG  . ASP C  1 92  ? 19.762  69.016  22.244  1.00 11.94 ? 92   ASP C CG  1 
ATOM   2901  O  OD1 . ASP C  1 92  ? 18.699  69.054  21.594  1.00 12.17 ? 92   ASP C OD1 1 
ATOM   2902  O  OD2 . ASP C  1 92  ? 20.120  67.949  22.770  1.00 15.84 ? 92   ASP C OD2 1 
ATOM   2903  N  N   . GLY C  1 93  ? 22.358  72.716  20.554  1.00 6.03  ? 93   GLY C N   1 
ATOM   2904  C  CA  . GLY C  1 93  ? 23.121  73.943  20.750  1.00 5.44  ? 93   GLY C CA  1 
ATOM   2905  C  C   . GLY C  1 93  ? 24.309  73.812  21.672  1.00 6.14  ? 93   GLY C C   1 
ATOM   2906  O  O   . GLY C  1 93  ? 24.879  74.819  22.071  1.00 5.32  ? 93   GLY C O   1 
ATOM   2907  N  N   . VAL C  1 94  ? 24.724  72.580  21.961  1.00 5.00  ? 94   VAL C N   1 
ATOM   2908  C  CA  . VAL C  1 94  ? 25.836  72.368  22.891  1.00 5.45  ? 94   VAL C CA  1 
ATOM   2909  C  C   . VAL C  1 94  ? 27.109  71.896  22.214  1.00 5.61  ? 94   VAL C C   1 
ATOM   2910  O  O   . VAL C  1 94  ? 27.097  70.947  21.432  1.00 5.93  ? 94   VAL C O   1 
ATOM   2911  C  CB  . VAL C  1 94  ? 25.466  71.313  23.942  1.00 5.70  ? 94   VAL C CB  1 
ATOM   2912  C  CG1 . VAL C  1 94  ? 26.637  71.096  24.916  1.00 8.24  ? 94   VAL C CG1 1 
ATOM   2913  C  CG2 . VAL C  1 94  ? 24.170  71.719  24.645  1.00 7.24  ? 94   VAL C CG2 1 
ATOM   2914  N  N   . ALA C  1 95  ? 28.210  72.569  22.510  1.00 5.00  ? 95   ALA C N   1 
ATOM   2915  C  CA  . ALA C  1 95  ? 29.499  72.171  22.004  1.00 5.06  ? 95   ALA C CA  1 
ATOM   2916  C  C   . ALA C  1 95  ? 30.262  71.556  23.166  1.00 5.01  ? 95   ALA C C   1 
ATOM   2917  O  O   . ALA C  1 95  ? 30.608  72.253  24.112  1.00 5.00  ? 95   ALA C O   1 
ATOM   2918  C  CB  . ALA C  1 95  ? 30.273  73.385  21.408  1.00 5.34  ? 95   ALA C CB  1 
ATOM   2919  N  N   . ASP C  1 96  ? 30.412  70.229  23.136  1.00 5.00  ? 96   ASP C N   1 
ATOM   2920  C  CA  . ASP C  1 96  ? 31.265  69.536  24.111  1.00 5.32  ? 96   ASP C CA  1 
ATOM   2921  C  C   . ASP C  1 96  ? 32.707  69.546  23.624  1.00 5.00  ? 96   ASP C C   1 
ATOM   2922  O  O   . ASP C  1 96  ? 33.177  68.627  22.976  1.00 5.00  ? 96   ASP C O   1 
ATOM   2923  C  CB  . ASP C  1 96  ? 30.777  68.126  24.318  1.00 5.55  ? 96   ASP C CB  1 
ATOM   2924  C  CG  . ASP C  1 96  ? 29.470  68.096  25.085  1.00 10.32 ? 96   ASP C CG  1 
ATOM   2925  O  OD1 . ASP C  1 96  ? 28.518  67.404  24.639  1.00 12.62 ? 96   ASP C OD1 1 
ATOM   2926  O  OD2 . ASP C  1 96  ? 29.320  68.738  26.144  1.00 10.05 ? 96   ASP C OD2 1 
ATOM   2927  N  N   . VAL C  1 97  ? 33.401  70.611  23.963  1.00 5.00  ? 97   VAL C N   1 
ATOM   2928  C  CA  . VAL C  1 97  ? 34.701  70.875  23.433  1.00 5.00  ? 97   VAL C CA  1 
ATOM   2929  C  C   . VAL C  1 97  ? 35.718  69.876  23.950  1.00 5.75  ? 97   VAL C C   1 
ATOM   2930  O  O   . VAL C  1 97  ? 35.726  69.555  25.147  1.00 6.21  ? 97   VAL C O   1 
ATOM   2931  C  CB  . VAL C  1 97  ? 35.121  72.301  23.845  1.00 5.37  ? 97   VAL C CB  1 
ATOM   2932  C  CG1 . VAL C  1 97  ? 36.556  72.598  23.371  1.00 5.00  ? 97   VAL C CG1 1 
ATOM   2933  C  CG2 . VAL C  1 97  ? 34.074  73.319  23.296  1.00 5.00  ? 97   VAL C CG2 1 
ATOM   2934  N  N   . SER C  1 98  ? 36.549  69.384  23.047  1.00 6.22  ? 98   SER C N   1 
ATOM   2935  C  CA  . SER C  1 98  ? 37.622  68.438  23.387  1.00 7.75  ? 98   SER C CA  1 
ATOM   2936  C  C   . SER C  1 98  ? 38.736  68.631  22.353  1.00 7.43  ? 98   SER C C   1 
ATOM   2937  O  O   . SER C  1 98  ? 38.657  68.148  21.192  1.00 8.44  ? 98   SER C O   1 
ATOM   2938  C  CB  . SER C  1 98  ? 37.098  66.993  23.361  1.00 9.25  ? 98   SER C CB  1 
ATOM   2939  O  OG  . SER C  1 98  ? 38.069  66.102  23.914  1.00 12.47 ? 98   SER C OG  1 
ATOM   2940  N  N   . ILE C  1 99  ? 39.765  69.364  22.743  1.00 6.79  ? 99   ILE C N   1 
ATOM   2941  C  CA  . ILE C  1 99  ? 40.856  69.765  21.845  1.00 6.53  ? 99   ILE C CA  1 
ATOM   2942  C  C   . ILE C  1 99  ? 42.169  69.531  22.604  1.00 7.75  ? 99   ILE C C   1 
ATOM   2943  O  O   . ILE C  1 99  ? 42.212  69.680  23.809  1.00 6.08  ? 99   ILE C O   1 
ATOM   2944  C  CB  . ILE C  1 99  ? 40.709  71.300  21.522  1.00 7.75  ? 99   ILE C CB  1 
ATOM   2945  C  CG1 . ILE C  1 99  ? 39.617  71.526  20.456  1.00 9.43  ? 99   ILE C CG1 1 
ATOM   2946  C  CG2 . ILE C  1 99  ? 42.012  71.927  21.013  1.00 7.67  ? 99   ILE C CG2 1 
ATOM   2947  C  CD1 . ILE C  1 99  ? 39.183  72.967  20.277  1.00 9.34  ? 99   ILE C CD1 1 
ATOM   2948  N  N   . GLU C  1 100 ? 43.222  69.138  21.893  1.00 7.50  ? 100  GLU C N   1 
ATOM   2949  C  CA  . GLU C  1 100 ? 44.550  69.076  22.469  1.00 8.22  ? 100  GLU C CA  1 
ATOM   2950  C  C   . GLU C  1 100 ? 45.443  69.847  21.499  1.00 7.74  ? 100  GLU C C   1 
ATOM   2951  O  O   . GLU C  1 100 ? 45.371  69.626  20.266  1.00 7.77  ? 100  GLU C O   1 
ATOM   2952  C  CB  . GLU C  1 100 ? 45.062  67.640  22.578  1.00 9.43  ? 100  GLU C CB  1 
ATOM   2953  C  CG  . GLU C  1 100 ? 46.480  67.572  23.131  1.00 12.01 ? 100  GLU C CG  1 
ATOM   2954  C  CD  . GLU C  1 100 ? 46.958  66.134  23.308  1.00 19.57 ? 100  GLU C CD  1 
ATOM   2955  O  OE1 . GLU C  1 100 ? 46.318  65.408  24.095  1.00 23.04 ? 100  GLU C OE1 1 
ATOM   2956  O  OE2 . GLU C  1 100 ? 47.952  65.733  22.655  1.00 21.50 ? 100  GLU C OE2 1 
ATOM   2957  N  N   . ASP C  1 101 ? 46.260  70.748  22.032  1.00 6.86  ? 101  ASP C N   1 
ATOM   2958  C  CA  . ASP C  1 101 ? 47.104  71.621  21.202  1.00 7.28  ? 101  ASP C CA  1 
ATOM   2959  C  C   . ASP C  1 101 ? 48.473  71.867  21.831  1.00 7.72  ? 101  ASP C C   1 
ATOM   2960  O  O   . ASP C  1 101 ? 48.569  72.145  23.033  1.00 8.01  ? 101  ASP C O   1 
ATOM   2961  C  CB  . ASP C  1 101 ? 46.371  72.938  20.946  1.00 7.73  ? 101  ASP C CB  1 
ATOM   2962  C  CG  . ASP C  1 101 ? 47.064  73.799  19.931  1.00 5.74  ? 101  ASP C CG  1 
ATOM   2963  O  OD1 . ASP C  1 101 ? 46.876  73.520  18.732  1.00 12.76 ? 101  ASP C OD1 1 
ATOM   2964  O  OD2 . ASP C  1 101 ? 47.841  74.737  20.213  1.00 7.25  ? 101  ASP C OD2 1 
ATOM   2965  N  N   . SER C  1 102 ? 49.532  71.767  21.030  1.00 7.61  ? 102  SER C N   1 
ATOM   2966  C  CA  . SER C  1 102 ? 50.859  71.949  21.584  1.00 9.29  ? 102  SER C CA  1 
ATOM   2967  C  C   . SER C  1 102 ? 51.505  73.250  21.151  1.00 8.44  ? 102  SER C C   1 
ATOM   2968  O  O   . SER C  1 102 ? 52.681  73.464  21.426  1.00 9.35  ? 102  SER C O   1 
ATOM   2969  C  CB  . SER C  1 102 ? 51.756  70.770  21.244  1.00 11.40 ? 102  SER C CB  1 
ATOM   2970  O  OG  . SER C  1 102 ? 51.240  69.601  21.832  1.00 15.24 ? 102  SER C OG  1 
ATOM   2971  N  N   . VAL C  1 103 ? 50.743  74.127  20.493  1.00 6.08  ? 103  VAL C N   1 
ATOM   2972  C  CA  . VAL C  1 103 ? 51.270  75.416  20.132  1.00 5.18  ? 103  VAL C CA  1 
ATOM   2973  C  C   . VAL C  1 103 ? 50.960  76.397  21.268  1.00 5.33  ? 103  VAL C C   1 
ATOM   2974  O  O   . VAL C  1 103 ? 51.826  77.141  21.698  1.00 5.00  ? 103  VAL C O   1 
ATOM   2975  C  CB  . VAL C  1 103 ? 50.797  75.893  18.720  1.00 5.00  ? 103  VAL C CB  1 
ATOM   2976  C  CG1 . VAL C  1 103 ? 51.279  77.312  18.441  1.00 5.57  ? 103  VAL C CG1 1 
ATOM   2977  C  CG2 . VAL C  1 103 ? 51.289  74.888  17.594  1.00 8.48  ? 103  VAL C CG2 1 
ATOM   2978  N  N   . ILE C  1 104 ? 49.716  76.399  21.754  1.00 5.30  ? 104  ILE C N   1 
ATOM   2979  C  CA  . ILE C  1 104 ? 49.419  77.230  22.924  1.00 5.64  ? 104  ILE C CA  1 
ATOM   2980  C  C   . ILE C  1 104 ? 50.129  76.618  24.114  1.00 5.77  ? 104  ILE C C   1 
ATOM   2981  O  O   . ILE C  1 104 ? 50.535  75.439  24.095  1.00 6.13  ? 104  ILE C O   1 
ATOM   2982  C  CB  . ILE C  1 104 ? 47.905  77.299  23.219  1.00 5.01  ? 104  ILE C CB  1 
ATOM   2983  C  CG1 . ILE C  1 104 ? 47.340  75.889  23.494  1.00 5.00  ? 104  ILE C CG1 1 
ATOM   2984  C  CG2 . ILE C  1 104 ? 47.149  78.091  22.094  1.00 5.63  ? 104  ILE C CG2 1 
ATOM   2985  C  CD1 . ILE C  1 104 ? 45.890  75.821  24.093  1.00 5.94  ? 104  ILE C CD1 1 
ATOM   2986  N  N   . SER C  1 105 ? 50.262  77.401  25.178  1.00 5.30  ? 105  SER C N   1 
ATOM   2987  C  CA  . SER C  1 105 ? 50.936  76.903  26.383  1.00 6.62  ? 105  SER C CA  1 
ATOM   2988  C  C   . SER C  1 105 ? 50.383  77.629  27.604  1.00 6.95  ? 105  SER C C   1 
ATOM   2989  O  O   . SER C  1 105 ? 49.786  78.714  27.458  1.00 7.47  ? 105  SER C O   1 
ATOM   2990  C  CB  . SER C  1 105 ? 52.447  77.131  26.311  1.00 7.02  ? 105  SER C CB  1 
ATOM   2991  O  OG  . SER C  1 105 ? 53.073  76.545  27.443  1.00 8.49  ? 105  SER C OG  1 
ATOM   2992  N  N   . LEU C  1 106 ? 50.548  77.043  28.779  1.00 7.24  ? 106  LEU C N   1 
ATOM   2993  C  CA  . LEU C  1 106 ? 50.095  77.690  30.018  1.00 8.12  ? 106  LEU C CA  1 
ATOM   2994  C  C   . LEU C  1 106 ? 51.294  78.284  30.754  1.00 10.27 ? 106  LEU C C   1 
ATOM   2995  O  O   . LEU C  1 106 ? 51.159  78.775  31.862  1.00 10.49 ? 106  LEU C O   1 
ATOM   2996  C  CB  . LEU C  1 106 ? 49.271  76.756  30.915  1.00 7.12  ? 106  LEU C CB  1 
ATOM   2997  C  CG  . LEU C  1 106 ? 48.046  76.135  30.256  1.00 6.50  ? 106  LEU C CG  1 
ATOM   2998  C  CD1 . LEU C  1 106 ? 47.256  75.270  31.255  1.00 9.78  ? 106  LEU C CD1 1 
ATOM   2999  C  CD2 . LEU C  1 106 ? 47.095  77.261  29.667  1.00 5.46  ? 106  LEU C CD2 1 
ATOM   3000  N  N   . SER C  1 107 ? 52.441  78.278  30.082  1.00 12.55 ? 107  SER C N   1 
ATOM   3001  C  CA  . SER C  1 107 ? 53.658  78.917  30.563  1.00 16.14 ? 107  SER C CA  1 
ATOM   3002  C  C   . SER C  1 107 ? 54.529  79.356  29.365  1.00 17.85 ? 107  SER C C   1 
ATOM   3003  O  O   . SER C  1 107 ? 54.237  79.033  28.224  1.00 18.59 ? 107  SER C O   1 
ATOM   3004  C  CB  . SER C  1 107 ? 54.436  77.926  31.427  1.00 17.13 ? 107  SER C CB  1 
ATOM   3005  O  OG  . SER C  1 107 ? 55.173  77.066  30.573  1.00 19.09 ? 107  SER C OG  1 
ATOM   3006  N  N   . GLY C  1 108 ? 55.594  80.108  29.613  1.00 20.00 ? 108  GLY C N   1 
ATOM   3007  C  CA  . GLY C  1 108 ? 56.524  80.470  28.544  1.00 20.88 ? 108  GLY C CA  1 
ATOM   3008  C  C   . GLY C  1 108 ? 56.034  81.436  27.478  1.00 21.54 ? 108  GLY C C   1 
ATOM   3009  O  O   . GLY C  1 108 ? 55.054  82.169  27.677  1.00 21.62 ? 108  GLY C O   1 
ATOM   3010  N  N   . ASP C  1 109 ? 56.700  81.401  26.320  1.00 21.92 ? 109  ASP C N   1 
ATOM   3011  C  CA  . ASP C  1 109 ? 56.438  82.321  25.194  1.00 22.17 ? 109  ASP C CA  1 
ATOM   3012  C  C   . ASP C  1 109 ? 54.999  82.355  24.660  1.00 20.78 ? 109  ASP C C   1 
ATOM   3013  O  O   . ASP C  1 109 ? 54.449  83.426  24.336  1.00 21.94 ? 109  ASP C O   1 
ATOM   3014  C  CB  . ASP C  1 109 ? 57.358  81.968  23.999  1.00 22.73 ? 109  ASP C CB  1 
ATOM   3015  C  CG  . ASP C  1 109 ? 58.797  82.405  24.225  1.00 26.64 ? 109  ASP C CG  1 
ATOM   3016  O  OD1 . ASP C  1 109 ? 59.517  82.734  23.232  1.00 30.79 ? 109  ASP C OD1 1 
ATOM   3017  O  OD2 . ASP C  1 109 ? 59.294  82.444  25.374  1.00 30.45 ? 109  ASP C OD2 1 
ATOM   3018  N  N   . HIS C  1 110 ? 54.433  81.176  24.493  1.00 17.68 ? 110  HIS C N   1 
ATOM   3019  C  CA  . HIS C  1 110 ? 53.119  81.054  23.874  1.00 15.32 ? 110  HIS C CA  1 
ATOM   3020  C  C   . HIS C  1 110 ? 52.040  80.966  24.953  1.00 13.69 ? 110  HIS C C   1 
ATOM   3021  O  O   . HIS C  1 110 ? 50.979  80.368  24.721  1.00 11.37 ? 110  HIS C O   1 
ATOM   3022  C  CB  . HIS C  1 110 ? 53.080  79.808  22.988  1.00 15.17 ? 110  HIS C CB  1 
ATOM   3023  C  CG  . HIS C  1 110 ? 53.926  79.923  21.751  1.00 16.14 ? 110  HIS C CG  1 
ATOM   3024  N  ND1 . HIS C  1 110 ? 53.993  78.926  20.798  1.00 15.87 ? 110  HIS C ND1 1 
ATOM   3025  C  CD2 . HIS C  1 110 ? 54.763  80.904  21.334  1.00 15.14 ? 110  HIS C CD2 1 
ATOM   3026  C  CE1 . HIS C  1 110 ? 54.808  79.308  19.829  1.00 17.40 ? 110  HIS C CE1 1 
ATOM   3027  N  NE2 . HIS C  1 110 ? 55.287  80.504  20.129  1.00 16.20 ? 110  HIS C NE2 1 
ATOM   3028  N  N   . CYS C  1 111 ? 52.346  81.536  26.122  1.00 11.46 ? 111  CYS C N   1 
ATOM   3029  C  CA  . CYS C  1 111 ? 51.444  81.519  27.275  1.00 10.85 ? 111  CYS C CA  1 
ATOM   3030  C  C   . CYS C  1 111 ? 50.143  82.260  26.941  1.00 9.26  ? 111  CYS C C   1 
ATOM   3031  O  O   . CYS C  1 111 ? 50.193  83.381  26.408  1.00 9.03  ? 111  CYS C O   1 
ATOM   3032  C  CB  . CYS C  1 111 ? 52.093  82.159  28.507  1.00 11.23 ? 111  CYS C CB  1 
ATOM   3033  S  SG  . CYS C  1 111 ? 51.130  81.742  29.988  1.00 18.10 ? 111  CYS C SG  1 
ATOM   3034  N  N   . ILE C  1 112 ? 49.005  81.625  27.241  1.00 6.56  ? 112  ILE C N   1 
ATOM   3035  C  CA  . ILE C  1 112 ? 47.682  82.204  26.973  1.00 5.73  ? 112  ILE C CA  1 
ATOM   3036  C  C   . ILE C  1 112 ? 46.957  82.679  28.231  1.00 5.24  ? 112  ILE C C   1 
ATOM   3037  O  O   . ILE C  1 112 ? 45.819  83.153  28.162  1.00 5.00  ? 112  ILE C O   1 
ATOM   3038  C  CB  . ILE C  1 112 ? 46.777  81.236  26.245  1.00 5.33  ? 112  ILE C CB  1 
ATOM   3039  C  CG1 . ILE C  1 112 ? 46.504  79.962  27.068  1.00 6.84  ? 112  ILE C CG1 1 
ATOM   3040  C  CG2 . ILE C  1 112 ? 47.340  80.922  24.819  1.00 5.57  ? 112  ILE C CG2 1 
ATOM   3041  C  CD1 . ILE C  1 112 ? 45.557  79.004  26.344  1.00 7.93  ? 112  ILE C CD1 1 
ATOM   3042  N  N   . ILE C  1 113 ? 47.618  82.542  29.378  1.00 5.00  ? 113  ILE C N   1 
ATOM   3043  C  CA  . ILE C  1 113 ? 46.976  82.977  30.605  1.00 5.39  ? 113  ILE C CA  1 
ATOM   3044  C  C   . ILE C  1 113 ? 46.825  84.498  30.549  1.00 5.00  ? 113  ILE C C   1 
ATOM   3045  O  O   . ILE C  1 113 ? 47.758  85.204  30.144  1.00 5.00  ? 113  ILE C O   1 
ATOM   3046  C  CB  . ILE C  1 113 ? 47.809  82.557  31.868  1.00 5.41  ? 113  ILE C CB  1 
ATOM   3047  C  CG1 . ILE C  1 113 ? 47.922  81.039  31.979  1.00 10.53 ? 113  ILE C CG1 1 
ATOM   3048  C  CG2 . ILE C  1 113 ? 47.199  83.151  33.156  1.00 5.03  ? 113  ILE C CG2 1 
ATOM   3049  C  CD1 . ILE C  1 113 ? 46.709  80.410  32.279  1.00 15.35 ? 113  ILE C CD1 1 
ATOM   3050  N  N   . GLY C  1 114 ? 45.647  85.016  30.931  1.00 5.00  ? 114  GLY C N   1 
ATOM   3051  C  CA  . GLY C  1 114 ? 45.464  86.450  30.882  1.00 5.00  ? 114  GLY C CA  1 
ATOM   3052  C  C   . GLY C  1 114 ? 45.015  86.980  29.512  1.00 5.00  ? 114  GLY C C   1 
ATOM   3053  O  O   . GLY C  1 114 ? 44.845  88.164  29.351  1.00 5.00  ? 114  GLY C O   1 
ATOM   3054  N  N   . ARG C  1 115 ? 44.842  86.090  28.548  1.00 5.00  ? 115  ARG C N   1 
ATOM   3055  C  CA  . ARG C  1 115 ? 44.372  86.509  27.222  1.00 5.00  ? 115  ARG C CA  1 
ATOM   3056  C  C   . ARG C  1 115 ? 42.906  86.101  27.142  1.00 5.00  ? 115  ARG C C   1 
ATOM   3057  O  O   . ARG C  1 115 ? 42.355  85.625  28.147  1.00 5.00  ? 115  ARG C O   1 
ATOM   3058  C  CB  . ARG C  1 115 ? 45.250  85.844  26.173  1.00 5.00  ? 115  ARG C CB  1 
ATOM   3059  C  CG  . ARG C  1 115 ? 46.725  86.222  26.418  1.00 5.01  ? 115  ARG C CG  1 
ATOM   3060  C  CD  . ARG C  1 115 ? 47.604  85.982  25.209  1.00 5.82  ? 115  ARG C CD  1 
ATOM   3061  N  NE  . ARG C  1 115 ? 49.007  86.258  25.511  1.00 6.08  ? 115  ARG C NE  1 
ATOM   3062  C  CZ  . ARG C  1 115 ? 49.601  87.411  25.313  1.00 7.04  ? 115  ARG C CZ  1 
ATOM   3063  N  NH1 . ARG C  1 115 ? 48.934  88.424  24.769  1.00 5.00  ? 115  ARG C NH1 1 
ATOM   3064  N  NH2 . ARG C  1 115 ? 50.893  87.539  25.627  1.00 6.61  ? 115  ARG C NH2 1 
ATOM   3065  N  N   . THR C  1 116 ? 42.258  86.236  25.984  1.00 5.00  ? 116  THR C N   1 
ATOM   3066  C  CA  . THR C  1 116 ? 40.813  86.017  25.939  1.00 5.00  ? 116  THR C CA  1 
ATOM   3067  C  C   . THR C  1 116 ? 40.454  84.874  25.016  1.00 5.51  ? 116  THR C C   1 
ATOM   3068  O  O   . THR C  1 116 ? 40.930  84.843  23.902  1.00 6.24  ? 116  THR C O   1 
ATOM   3069  C  CB  . THR C  1 116 ? 40.125  87.314  25.383  1.00 5.09  ? 116  THR C CB  1 
ATOM   3070  O  OG1 . THR C  1 116 ? 40.200  88.348  26.376  1.00 5.40  ? 116  THR C OG1 1 
ATOM   3071  C  CG2 . THR C  1 116 ? 38.631  87.139  25.186  1.00 5.00  ? 116  THR C CG2 1 
ATOM   3072  N  N   . LEU C  1 117 ? 39.602  83.964  25.465  1.00 5.00  ? 117  LEU C N   1 
ATOM   3073  C  CA  . LEU C  1 117 ? 39.107  82.906  24.598  1.00 5.00  ? 117  LEU C CA  1 
ATOM   3074  C  C   . LEU C  1 117 ? 37.780  83.415  24.009  1.00 5.00  ? 117  LEU C C   1 
ATOM   3075  O  O   . LEU C  1 117 ? 36.953  83.959  24.741  1.00 5.00  ? 117  LEU C O   1 
ATOM   3076  C  CB  . LEU C  1 117 ? 38.889  81.647  25.460  1.00 5.00  ? 117  LEU C CB  1 
ATOM   3077  C  CG  . LEU C  1 117 ? 38.329  80.440  24.737  1.00 5.00  ? 117  LEU C CG  1 
ATOM   3078  C  CD1 . LEU C  1 117 ? 39.379  79.938  23.780  1.00 5.59  ? 117  LEU C CD1 1 
ATOM   3079  C  CD2 . LEU C  1 117 ? 37.988  79.356  25.785  1.00 5.00  ? 117  LEU C CD2 1 
ATOM   3080  N  N   . VAL C  1 118 ? 37.582  83.238  22.695  1.00 5.00  ? 118  VAL C N   1 
ATOM   3081  C  CA  . VAL C  1 118 ? 36.381  83.719  21.998  1.00 5.00  ? 118  VAL C CA  1 
ATOM   3082  C  C   . VAL C  1 118 ? 35.739  82.592  21.208  1.00 5.00  ? 118  VAL C C   1 
ATOM   3083  O  O   . VAL C  1 118 ? 36.467  81.779  20.580  1.00 5.00  ? 118  VAL C O   1 
ATOM   3084  C  CB  . VAL C  1 118 ? 36.764  84.802  20.974  1.00 5.37  ? 118  VAL C CB  1 
ATOM   3085  C  CG1 . VAL C  1 118 ? 35.468  85.284  20.212  1.00 5.00  ? 118  VAL C CG1 1 
ATOM   3086  C  CG2 . VAL C  1 118 ? 37.391  86.030  21.722  1.00 5.00  ? 118  VAL C CG2 1 
ATOM   3087  N  N   . VAL C  1 119 ? 34.412  82.465  21.310  1.00 5.00  ? 119  VAL C N   1 
ATOM   3088  C  CA  . VAL C  1 119 ? 33.710  81.524  20.434  1.00 5.00  ? 119  VAL C CA  1 
ATOM   3089  C  C   . VAL C  1 119 ? 32.893  82.408  19.451  1.00 5.00  ? 119  VAL C C   1 
ATOM   3090  O  O   . VAL C  1 119 ? 32.278  83.422  19.830  1.00 5.00  ? 119  VAL C O   1 
ATOM   3091  C  CB  . VAL C  1 119 ? 32.832  80.503  21.172  1.00 5.24  ? 119  VAL C CB  1 
ATOM   3092  C  CG1 . VAL C  1 119 ? 31.767  81.206  22.051  1.00 5.00  ? 119  VAL C CG1 1 
ATOM   3093  C  CG2 . VAL C  1 119 ? 32.119  79.548  20.135  1.00 5.00  ? 119  VAL C CG2 1 
ATOM   3094  N  N   . HIS C  1 120 ? 32.900  82.023  18.185  1.00 5.00  ? 120  HIS C N   1 
ATOM   3095  C  CA  . HIS C  1 120 ? 32.342  82.881  17.135  1.00 5.00  ? 120  HIS C CA  1 
ATOM   3096  C  C   . HIS C  1 120 ? 31.023  82.446  16.539  1.00 5.00  ? 120  HIS C C   1 
ATOM   3097  O  O   . HIS C  1 120 ? 30.585  81.329  16.680  1.00 5.00  ? 120  HIS C O   1 
ATOM   3098  C  CB  . HIS C  1 120 ? 33.383  82.903  15.979  1.00 5.00  ? 120  HIS C CB  1 
ATOM   3099  C  CG  . HIS C  1 120 ? 34.533  83.814  16.247  1.00 5.00  ? 120  HIS C CG  1 
ATOM   3100  N  ND1 . HIS C  1 120 ? 34.515  85.142  15.867  1.00 5.34  ? 120  HIS C ND1 1 
ATOM   3101  C  CD2 . HIS C  1 120 ? 35.759  83.599  16.800  1.00 5.40  ? 120  HIS C CD2 1 
ATOM   3102  C  CE1 . HIS C  1 120 ? 35.667  85.704  16.182  1.00 5.24  ? 120  HIS C CE1 1 
ATOM   3103  N  NE2 . HIS C  1 120 ? 36.412  84.809  16.782  1.00 5.00  ? 120  HIS C NE2 1 
ATOM   3104  N  N   . GLU C  1 121 ? 30.450  83.372  15.779  1.00 5.00  ? 121  GLU C N   1 
ATOM   3105  C  CA  . GLU C  1 121 ? 29.187  83.225  15.104  1.00 5.00  ? 121  GLU C CA  1 
ATOM   3106  C  C   . GLU C  1 121 ? 29.187  82.116  14.056  1.00 5.00  ? 121  GLU C C   1 
ATOM   3107  O  O   . GLU C  1 121 ? 28.177  81.383  13.910  1.00 5.00  ? 121  GLU C O   1 
ATOM   3108  C  CB  . GLU C  1 121 ? 28.935  84.572  14.388  1.00 6.14  ? 121  GLU C CB  1 
ATOM   3109  C  CG  . GLU C  1 121 ? 27.633  84.660  13.599  1.00 7.50  ? 121  GLU C CG  1 
ATOM   3110  C  CD  . GLU C  1 121 ? 27.602  85.884  12.655  1.00 12.70 ? 121  GLU C CD  1 
ATOM   3111  O  OE1 . GLU C  1 121 ? 26.521  86.120  12.100  1.00 16.31 ? 121  GLU C OE1 1 
ATOM   3112  O  OE2 . GLU C  1 121 ? 28.640  86.600  12.440  1.00 8.07  ? 121  GLU C OE2 1 
ATOM   3113  N  N   . LYS C  1 122 ? 30.271  82.062  13.278  1.00 5.00  ? 122  LYS C N   1 
ATOM   3114  C  CA  . LYS C  1 122 ? 30.360  81.165  12.105  1.00 6.88  ? 122  LYS C CA  1 
ATOM   3115  C  C   . LYS C  1 122 ? 31.540  80.253  12.111  1.00 5.30  ? 122  LYS C C   1 
ATOM   3116  O  O   . LYS C  1 122 ? 32.448  80.353  12.960  1.00 5.05  ? 122  LYS C O   1 
ATOM   3117  C  CB  . LYS C  1 122 ? 30.537  81.996  10.782  1.00 7.72  ? 122  LYS C CB  1 
ATOM   3118  C  CG  . LYS C  1 122 ? 29.696  83.204  10.672  1.00 13.70 ? 122  LYS C CG  1 
ATOM   3119  C  CD  . LYS C  1 122 ? 29.408  83.525  9.209   1.00 19.69 ? 122  LYS C CD  1 
ATOM   3120  C  CE  . LYS C  1 122 ? 29.782  84.975  8.946   1.00 24.36 ? 122  LYS C CE  1 
ATOM   3121  N  NZ  . LYS C  1 122 ? 28.874  85.627  7.912   1.00 27.25 ? 122  LYS C NZ  1 
ATOM   3122  N  N   . ALA C  1 123 ? 31.568  79.362  11.124  1.00 5.56  ? 123  ALA C N   1 
ATOM   3123  C  CA  . ALA C  1 123 ? 32.738  78.484  10.999  1.00 5.00  ? 123  ALA C CA  1 
ATOM   3124  C  C   . ALA C  1 123 ? 33.995  79.276  10.647  1.00 5.09  ? 123  ALA C C   1 
ATOM   3125  O  O   . ALA C  1 123 ? 33.952  80.249  9.872   1.00 5.00  ? 123  ALA C O   1 
ATOM   3126  C  CB  . ALA C  1 123 ? 32.506  77.398  9.873   1.00 6.11  ? 123  ALA C CB  1 
ATOM   3127  N  N   . ASP C  1 124 ? 35.115  78.818  11.184  1.00 5.00  ? 124  ASP C N   1 
ATOM   3128  C  CA  . ASP C  1 124 ? 36.440  79.322  10.835  1.00 5.00  ? 124  ASP C CA  1 
ATOM   3129  C  C   . ASP C  1 124 ? 36.829  78.517  9.579   1.00 5.00  ? 124  ASP C C   1 
ATOM   3130  O  O   . ASP C  1 124 ? 36.799  77.290  9.614   1.00 5.00  ? 124  ASP C O   1 
ATOM   3131  C  CB  . ASP C  1 124 ? 37.383  78.949  11.987  1.00 5.47  ? 124  ASP C CB  1 
ATOM   3132  C  CG  . ASP C  1 124 ? 38.804  79.459  11.812  1.00 5.52  ? 124  ASP C CG  1 
ATOM   3133  O  OD1 . ASP C  1 124 ? 39.307  79.641  10.667  1.00 5.00  ? 124  ASP C OD1 1 
ATOM   3134  O  OD2 . ASP C  1 124 ? 39.537  79.706  12.810  1.00 8.11  ? 124  ASP C OD2 1 
ATOM   3135  N  N   . ASP C  1 125 ? 37.154  79.206  8.470   1.00 5.00  ? 125  ASP C N   1 
ATOM   3136  C  CA  . ASP C  1 125 ? 37.556  78.507  7.229   1.00 5.15  ? 125  ASP C CA  1 
ATOM   3137  C  C   . ASP C  1 125 ? 39.007  78.005  7.219   1.00 5.56  ? 125  ASP C C   1 
ATOM   3138  O  O   . ASP C  1 125 ? 39.518  77.514  6.176   1.00 5.00  ? 125  ASP C O   1 
ATOM   3139  C  CB  . ASP C  1 125 ? 37.265  79.374  5.977   1.00 5.89  ? 125  ASP C CB  1 
ATOM   3140  C  CG  . ASP C  1 125 ? 38.078  80.652  5.894   1.00 7.00  ? 125  ASP C CG  1 
ATOM   3141  O  OD1 . ASP C  1 125 ? 39.192  80.744  6.471   1.00 5.00  ? 125  ASP C OD1 1 
ATOM   3142  O  OD2 . ASP C  1 125 ? 37.696  81.638  5.170   1.00 5.00  ? 125  ASP C OD2 1 
ATOM   3143  N  N   . LEU C  1 126 ? 39.664  78.176  8.360   1.00 5.00  ? 126  LEU C N   1 
ATOM   3144  C  CA  . LEU C  1 126 ? 41.024  77.711  8.580   1.00 5.77  ? 126  LEU C CA  1 
ATOM   3145  C  C   . LEU C  1 126 ? 42.059  78.296  7.583   1.00 5.00  ? 126  LEU C C   1 
ATOM   3146  O  O   . LEU C  1 126 ? 43.102  77.651  7.304   1.00 5.00  ? 126  LEU C O   1 
ATOM   3147  C  CB  . LEU C  1 126 ? 41.043  76.184  8.538   1.00 5.00  ? 126  LEU C CB  1 
ATOM   3148  C  CG  . LEU C  1 126 ? 39.960  75.579  9.470   1.00 8.38  ? 126  LEU C CG  1 
ATOM   3149  C  CD1 . LEU C  1 126 ? 39.995  74.041  9.396   1.00 8.33  ? 126  LEU C CD1 1 
ATOM   3150  C  CD2 . LEU C  1 126 ? 40.117  76.101  10.904  1.00 6.27  ? 126  LEU C CD2 1 
ATOM   3151  N  N   . GLY C  1 127 ? 41.773  79.511  7.102   1.00 5.00  ? 127  GLY C N   1 
ATOM   3152  C  CA  . GLY C  1 127 ? 42.682  80.224  6.231   1.00 5.72  ? 127  GLY C CA  1 
ATOM   3153  C  C   . GLY C  1 127 ? 42.576  79.763  4.797   1.00 5.23  ? 127  GLY C C   1 
ATOM   3154  O  O   . GLY C  1 127 ? 43.419  80.132  3.975   1.00 5.00  ? 127  GLY C O   1 
ATOM   3155  N  N   . LYS C  1 128 ? 41.528  79.004  4.470   1.00 5.00  ? 128  LYS C N   1 
ATOM   3156  C  CA  . LYS C  1 128 ? 41.393  78.449  3.107   1.00 5.00  ? 128  LYS C CA  1 
ATOM   3157  C  C   . LYS C  1 128 ? 40.288  79.100  2.270   1.00 5.00  ? 128  LYS C C   1 
ATOM   3158  O  O   . LYS C  1 128 ? 39.846  78.548  1.249   1.00 6.35  ? 128  LYS C O   1 
ATOM   3159  C  CB  . LYS C  1 128 ? 41.189  76.920  3.180   1.00 5.00  ? 128  LYS C CB  1 
ATOM   3160  C  CG  . LYS C  1 128 ? 42.323  76.183  3.908   1.00 9.72  ? 128  LYS C CG  1 
ATOM   3161  C  CD  . LYS C  1 128 ? 42.134  74.679  3.785   1.00 16.83 ? 128  LYS C CD  1 
ATOM   3162  C  CE  . LYS C  1 128 ? 43.205  73.911  4.543   1.00 23.11 ? 128  LYS C CE  1 
ATOM   3163  N  NZ  . LYS C  1 128 ? 42.862  72.444  4.444   1.00 28.90 ? 128  LYS C NZ  1 
ATOM   3164  N  N   . GLY C  1 129 ? 39.857  80.283  2.650   1.00 5.00  ? 129  GLY C N   1 
ATOM   3165  C  CA  . GLY C  1 129 ? 38.741  80.908  1.981   1.00 5.00  ? 129  GLY C CA  1 
ATOM   3166  C  C   . GLY C  1 129 ? 39.132  81.716  0.743   1.00 5.00  ? 129  GLY C C   1 
ATOM   3167  O  O   . GLY C  1 129 ? 38.259  82.133  -0.012  1.00 5.00  ? 129  GLY C O   1 
ATOM   3168  N  N   . GLY C  1 130 ? 40.425  81.925  0.533   1.00 5.00  ? 130  GLY C N   1 
ATOM   3169  C  CA  . GLY C  1 130 ? 40.823  82.632  -0.700  1.00 5.00  ? 130  GLY C CA  1 
ATOM   3170  C  C   . GLY C  1 130 ? 40.604  84.150  -0.677  1.00 5.00  ? 130  GLY C C   1 
ATOM   3171  O  O   . GLY C  1 130 ? 40.590  84.783  -1.695  1.00 5.00  ? 130  GLY C O   1 
ATOM   3172  N  N   . ASN C  1 131 ? 40.448  84.736  0.503   1.00 5.00  ? 131  ASN C N   1 
ATOM   3173  C  CA  . ASN C  1 131 ? 40.373  86.191  0.616   1.00 5.00  ? 131  ASN C CA  1 
ATOM   3174  C  C   . ASN C  1 131 ? 41.236  86.670  1.762   1.00 5.00  ? 131  ASN C C   1 
ATOM   3175  O  O   . ASN C  1 131 ? 41.758  85.876  2.545   1.00 5.00  ? 131  ASN C O   1 
ATOM   3176  C  CB  . ASN C  1 131 ? 38.937  86.715  0.753   1.00 5.00  ? 131  ASN C CB  1 
ATOM   3177  C  CG  . ASN C  1 131 ? 38.170  86.047  1.910   1.00 5.94  ? 131  ASN C CG  1 
ATOM   3178  O  OD1 . ASN C  1 131 ? 38.721  85.773  2.955   1.00 6.30  ? 131  ASN C OD1 1 
ATOM   3179  N  ND2 . ASN C  1 131 ? 36.882  85.817  1.699   1.00 10.86 ? 131  ASN C ND2 1 
ATOM   3180  N  N   . GLU C  1 132 ? 41.396  87.984  1.861   1.00 5.23  ? 132  GLU C N   1 
ATOM   3181  C  CA  . GLU C  1 132 ? 42.246  88.524  2.916   1.00 6.89  ? 132  GLU C CA  1 
ATOM   3182  C  C   . GLU C  1 132 ? 41.741  88.203  4.302   1.00 7.20  ? 132  GLU C C   1 
ATOM   3183  O  O   . GLU C  1 132 ? 42.525  87.832  5.198   1.00 7.09  ? 132  GLU C O   1 
ATOM   3184  C  CB  . GLU C  1 132 ? 42.410  90.034  2.718   1.00 8.15  ? 132  GLU C CB  1 
ATOM   3185  C  CG  . GLU C  1 132 ? 43.516  90.685  3.539   1.00 14.76 ? 132  GLU C CG  1 
ATOM   3186  C  CD  . GLU C  1 132 ? 43.735  92.137  3.123   1.00 21.87 ? 132  GLU C CD  1 
ATOM   3187  O  OE1 . GLU C  1 132 ? 44.366  92.401  2.081   1.00 26.40 ? 132  GLU C OE1 1 
ATOM   3188  O  OE2 . GLU C  1 132 ? 43.251  93.025  3.829   1.00 26.79 ? 132  GLU C OE2 1 
ATOM   3189  N  N   . GLU C  1 133 ? 40.436  88.320  4.509   1.00 6.59  ? 133  GLU C N   1 
ATOM   3190  C  CA  . GLU C  1 133 ? 39.877  88.040  5.837   1.00 8.70  ? 133  GLU C CA  1 
ATOM   3191  C  C   . GLU C  1 133 ? 40.190  86.593  6.269   1.00 7.44  ? 133  GLU C C   1 
ATOM   3192  O  O   . GLU C  1 133 ? 40.411  86.310  7.462   1.00 7.91  ? 133  GLU C O   1 
ATOM   3193  C  CB  . GLU C  1 133 ? 38.361  88.320  5.830   1.00 9.66  ? 133  GLU C CB  1 
ATOM   3194  C  CG  . GLU C  1 133 ? 37.661  88.338  7.190   1.00 13.29 ? 133  GLU C CG  1 
ATOM   3195  C  CD  . GLU C  1 133 ? 38.057  89.493  8.094   1.00 17.89 ? 133  GLU C CD  1 
ATOM   3196  O  OE1 . GLU C  1 133 ? 38.430  90.584  7.615   1.00 22.18 ? 133  GLU C OE1 1 
ATOM   3197  O  OE2 . GLU C  1 133 ? 37.958  89.304  9.321   1.00 24.57 ? 133  GLU C OE2 1 
ATOM   3198  N  N   . SER C  1 134 ? 40.247  85.672  5.304   1.00 6.31  ? 134  SER C N   1 
ATOM   3199  C  CA  . SER C  1 134 ? 40.507  84.281  5.656   1.00 5.59  ? 134  SER C CA  1 
ATOM   3200  C  C   . SER C  1 134 ? 41.880  84.128  6.353   1.00 5.97  ? 134  SER C C   1 
ATOM   3201  O  O   . SER C  1 134 ? 42.027  83.341  7.306   1.00 5.00  ? 134  SER C O   1 
ATOM   3202  C  CB  . SER C  1 134 ? 40.433  83.381  4.397   1.00 5.00  ? 134  SER C CB  1 
ATOM   3203  O  OG  . SER C  1 134 ? 40.739  82.055  4.771   1.00 5.13  ? 134  SER C OG  1 
ATOM   3204  N  N   . THR C  1 135 ? 42.861  84.894  5.883   1.00 5.56  ? 135  THR C N   1 
ATOM   3205  C  CA  . THR C  1 135 ? 44.219  84.835  6.411   1.00 7.44  ? 135  THR C CA  1 
ATOM   3206  C  C   . THR C  1 135 ? 44.369  85.632  7.695   1.00 8.52  ? 135  THR C C   1 
ATOM   3207  O  O   . THR C  1 135 ? 45.456  85.648  8.294   1.00 8.97  ? 135  THR C O   1 
ATOM   3208  C  CB  . THR C  1 135 ? 45.277  85.423  5.415   1.00 8.13  ? 135  THR C CB  1 
ATOM   3209  O  OG1 . THR C  1 135 ? 45.120  86.870  5.357   1.00 12.96 ? 135  THR C OG1 1 
ATOM   3210  C  CG2 . THR C  1 135 ? 45.037  85.014  4.070   1.00 7.84  ? 135  THR C CG2 1 
ATOM   3211  N  N   . LYS C  1 136 ? 43.319  86.325  8.110   1.00 9.08  ? 136  LYS C N   1 
ATOM   3212  C  CA  . LYS C  1 136 ? 43.395  87.032  9.382   1.00 9.49  ? 136  LYS C CA  1 
ATOM   3213  C  C   . LYS C  1 136 ? 42.516  86.406  10.455  1.00 8.62  ? 136  LYS C C   1 
ATOM   3214  O  O   . LYS C  1 136 ? 42.970  86.169  11.576  1.00 8.37  ? 136  LYS C O   1 
ATOM   3215  C  CB  . LYS C  1 136 ? 42.959  88.497  9.214   1.00 10.51 ? 136  LYS C CB  1 
ATOM   3216  C  CG  . LYS C  1 136 ? 43.760  89.281  8.234   1.00 15.00 ? 136  LYS C CG  1 
ATOM   3217  C  CD  . LYS C  1 136 ? 43.345  90.775  8.369   1.00 22.91 ? 136  LYS C CD  1 
ATOM   3218  C  CE  . LYS C  1 136 ? 43.914  91.605  7.231   1.00 25.62 ? 136  LYS C CE  1 
ATOM   3219  N  NZ  . LYS C  1 136 ? 43.281  92.974  7.165   1.00 29.03 ? 136  LYS C NZ  1 
ATOM   3220  N  N   . THR C  1 137 ? 41.247  86.167  10.143  1.00 8.44  ? 137  THR C N   1 
ATOM   3221  C  CA  . THR C  1 137 ? 40.306  85.654  11.152  1.00 9.82  ? 137  THR C CA  1 
ATOM   3222  C  C   . THR C  1 137 ? 39.653  84.367  10.798  1.00 10.35 ? 137  THR C C   1 
ATOM   3223  O  O   . THR C  1 137 ? 38.840  83.825  11.565  1.00 9.79  ? 137  THR C O   1 
ATOM   3224  C  CB  . THR C  1 137 ? 39.162  86.668  11.348  1.00 10.59 ? 137  THR C CB  1 
ATOM   3225  O  OG1 . THR C  1 137 ? 38.436  86.808  10.106  1.00 7.99  ? 137  THR C OG1 1 
ATOM   3226  C  CG2 . THR C  1 137 ? 39.735  88.035  11.601  1.00 12.74 ? 137  THR C CG2 1 
ATOM   3227  N  N   . GLY C  1 138 ? 39.932  83.863  9.603   1.00 8.41  ? 138  GLY C N   1 
ATOM   3228  C  CA  . GLY C  1 138 ? 39.186  82.689  9.174   1.00 7.47  ? 138  GLY C CA  1 
ATOM   3229  C  C   . GLY C  1 138 ? 37.706  82.960  8.826   1.00 6.26  ? 138  GLY C C   1 
ATOM   3230  O  O   . GLY C  1 138 ? 36.963  82.025  8.595   1.00 5.32  ? 138  GLY C O   1 
ATOM   3231  N  N   . ASN C  1 139 ? 37.305  84.228  8.726   1.00 5.45  ? 139  ASN C N   1 
ATOM   3232  C  CA  . ASN C  1 139 ? 35.928  84.591  8.372   1.00 5.84  ? 139  ASN C CA  1 
ATOM   3233  C  C   . ASN C  1 139 ? 34.907  83.997  9.353   1.00 5.00  ? 139  ASN C C   1 
ATOM   3234  O  O   . ASN C  1 139 ? 33.832  83.605  8.970   1.00 5.00  ? 139  ASN C O   1 
ATOM   3235  C  CB  . ASN C  1 139 ? 35.569  84.126  6.943   1.00 5.22  ? 139  ASN C CB  1 
ATOM   3236  C  CG  . ASN C  1 139 ? 36.210  84.988  5.860   1.00 8.45  ? 139  ASN C CG  1 
ATOM   3237  O  OD1 . ASN C  1 139 ? 35.895  86.173  5.734   1.00 9.10  ? 139  ASN C OD1 1 
ATOM   3238  N  ND2 . ASN C  1 139 ? 37.138  84.392  5.082   1.00 6.25  ? 139  ASN C ND2 1 
ATOM   3239  N  N   . ALA C  1 140 ? 35.268  83.952  10.631  1.00 5.00  ? 140  ALA C N   1 
ATOM   3240  C  CA  . ALA C  1 140 ? 34.386  83.313  11.621  1.00 5.53  ? 140  ALA C CA  1 
ATOM   3241  C  C   . ALA C  1 140 ? 33.305  84.265  12.159  1.00 5.92  ? 140  ALA C C   1 
ATOM   3242  O  O   . ALA C  1 140 ? 32.466  83.883  12.987  1.00 5.00  ? 140  ALA C O   1 
ATOM   3243  C  CB  . ALA C  1 140 ? 35.235  82.769  12.752  1.00 6.10  ? 140  ALA C CB  1 
ATOM   3244  N  N   . GLY C  1 141 ? 33.276  85.471  11.621  1.00 5.85  ? 141  GLY C N   1 
ATOM   3245  C  CA  . GLY C  1 141 ? 32.219  86.416  11.979  1.00 5.71  ? 141  GLY C CA  1 
ATOM   3246  C  C   . GLY C  1 141 ? 32.288  86.929  13.413  1.00 5.41  ? 141  GLY C C   1 
ATOM   3247  O  O   . GLY C  1 141 ? 33.373  86.993  14.044  1.00 5.00  ? 141  GLY C O   1 
ATOM   3248  N  N   . SER C  1 142 ? 31.109  87.265  13.943  1.00 5.06  ? 142  SER C N   1 
ATOM   3249  C  CA  . SER C  1 142 ? 31.082  87.986  15.208  1.00 5.00  ? 142  SER C CA  1 
ATOM   3250  C  C   . SER C  1 142 ? 31.535  87.165  16.406  1.00 5.00  ? 142  SER C C   1 
ATOM   3251  O  O   . SER C  1 142 ? 31.621  85.931  16.339  1.00 5.00  ? 142  SER C O   1 
ATOM   3252  C  CB  . SER C  1 142 ? 29.693  88.592  15.470  1.00 5.66  ? 142  SER C CB  1 
ATOM   3253  O  OG  . SER C  1 142 ? 28.793  87.569  15.795  1.00 7.24  ? 142  SER C OG  1 
ATOM   3254  N  N   . ARG C  1 143 ? 31.819  87.874  17.497  1.00 5.00  ? 143  ARG C N   1 
ATOM   3255  C  CA  . ARG C  1 143 ? 32.272  87.221  18.729  1.00 5.00  ? 143  ARG C CA  1 
ATOM   3256  C  C   . ARG C  1 143 ? 31.031  87.051  19.609  1.00 5.08  ? 143  ARG C C   1 
ATOM   3257  O  O   . ARG C  1 143 ? 30.475  88.053  20.118  1.00 6.88  ? 143  ARG C O   1 
ATOM   3258  C  CB  . ARG C  1 143 ? 33.294  88.129  19.409  1.00 5.00  ? 143  ARG C CB  1 
ATOM   3259  C  CG  . ARG C  1 143 ? 34.472  88.407  18.460  1.00 6.11  ? 143  ARG C CG  1 
ATOM   3260  C  CD  . ARG C  1 143 ? 35.495  89.457  18.981  1.00 6.93  ? 143  ARG C CD  1 
ATOM   3261  N  NE  . ARG C  1 143 ? 36.494  89.708  17.932  1.00 6.92  ? 143  ARG C NE  1 
ATOM   3262  C  CZ  . ARG C  1 143 ? 37.663  90.270  18.149  1.00 7.15  ? 143  ARG C CZ  1 
ATOM   3263  N  NH1 . ARG C  1 143 ? 38.002  90.630  19.403  1.00 5.76  ? 143  ARG C NH1 1 
ATOM   3264  N  NH2 . ARG C  1 143 ? 38.515  90.420  17.122  1.00 5.11  ? 143  ARG C NH2 1 
ATOM   3265  N  N   . LEU C  1 144 ? 30.589  85.814  19.754  1.00 5.00  ? 144  LEU C N   1 
ATOM   3266  C  CA  . LEU C  1 144 ? 29.340  85.533  20.481  1.00 5.00  ? 144  LEU C CA  1 
ATOM   3267  C  C   . LEU C  1 144 ? 29.535  85.535  21.988  1.00 5.00  ? 144  LEU C C   1 
ATOM   3268  O  O   . LEU C  1 144 ? 28.622  85.932  22.718  1.00 5.00  ? 144  LEU C O   1 
ATOM   3269  C  CB  . LEU C  1 144 ? 28.753  84.187  20.101  1.00 5.00  ? 144  LEU C CB  1 
ATOM   3270  C  CG  . LEU C  1 144 ? 28.343  84.045  18.617  1.00 5.00  ? 144  LEU C CG  1 
ATOM   3271  C  CD1 . LEU C  1 144 ? 27.677  82.697  18.432  1.00 9.07  ? 144  LEU C CD1 1 
ATOM   3272  C  CD2 . LEU C  1 144 ? 27.396  85.119  18.204  1.00 7.70  ? 144  LEU C CD2 1 
ATOM   3273  N  N   . ALA C  1 145 ? 30.691  85.055  22.446  1.00 5.00  ? 145  ALA C N   1 
ATOM   3274  C  CA  . ALA C  1 145 ? 30.963  85.057  23.904  1.00 5.00  ? 145  ALA C CA  1 
ATOM   3275  C  C   . ALA C  1 145 ? 32.466  84.993  24.101  1.00 5.00  ? 145  ALA C C   1 
ATOM   3276  O  O   . ALA C  1 145 ? 33.190  84.498  23.234  1.00 5.00  ? 145  ALA C O   1 
ATOM   3277  C  CB  . ALA C  1 145 ? 30.281  83.872  24.581  1.00 5.00  ? 145  ALA C CB  1 
ATOM   3278  N  N   . CYS C  1 146 ? 32.939  85.502  25.233  1.00 5.00  ? 146  CYS C N   1 
ATOM   3279  C  CA  . CYS C  1 146 ? 34.378  85.438  25.480  1.00 5.00  ? 146  CYS C CA  1 
ATOM   3280  C  C   . CYS C  1 146 ? 34.593  85.504  26.964  1.00 5.00  ? 146  CYS C C   1 
ATOM   3281  O  O   . CYS C  1 146 ? 33.671  85.778  27.736  1.00 5.00  ? 146  CYS C O   1 
ATOM   3282  C  CB  . CYS C  1 146 ? 35.116  86.623  24.831  1.00 5.64  ? 146  CYS C CB  1 
ATOM   3283  S  SG  . CYS C  1 146 ? 34.541  88.252  25.422  1.00 9.04  ? 146  CYS C SG  1 
ATOM   3284  N  N   . GLY C  1 147 ? 35.838  85.267  27.351  1.00 5.00  ? 147  GLY C N   1 
ATOM   3285  C  CA  . GLY C  1 147 ? 36.215  85.456  28.763  1.00 5.00  ? 147  GLY C CA  1 
ATOM   3286  C  C   . GLY C  1 147 ? 37.721  85.507  28.876  1.00 5.00  ? 147  GLY C C   1 
ATOM   3287  O  O   . GLY C  1 147 ? 38.462  85.089  27.976  1.00 5.00  ? 147  GLY C O   1 
ATOM   3288  N  N   . VAL C  1 148 ? 38.209  85.977  30.012  1.00 5.00  ? 148  VAL C N   1 
ATOM   3289  C  CA  . VAL C  1 148 ? 39.652  85.976  30.189  1.00 5.00  ? 148  VAL C CA  1 
ATOM   3290  C  C   . VAL C  1 148 ? 40.088  84.634  30.767  1.00 5.12  ? 148  VAL C C   1 
ATOM   3291  O  O   . VAL C  1 148 ? 39.438  84.086  31.660  1.00 5.00  ? 148  VAL C O   1 
ATOM   3292  C  CB  . VAL C  1 148 ? 40.053  87.128  31.127  1.00 5.00  ? 148  VAL C CB  1 
ATOM   3293  C  CG1 . VAL C  1 148 ? 41.618  87.182  31.304  1.00 5.77  ? 148  VAL C CG1 1 
ATOM   3294  C  CG2 . VAL C  1 148 ? 39.432  88.468  30.567  1.00 5.00  ? 148  VAL C CG2 1 
ATOM   3295  N  N   . ILE C  1 149 ? 41.195  84.115  30.258  1.00 5.00  ? 149  ILE C N   1 
ATOM   3296  C  CA  . ILE C  1 149 ? 41.737  82.834  30.691  1.00 5.00  ? 149  ILE C CA  1 
ATOM   3297  C  C   . ILE C  1 149 ? 42.498  83.001  31.999  1.00 5.00  ? 149  ILE C C   1 
ATOM   3298  O  O   . ILE C  1 149 ? 43.504  83.724  32.066  1.00 5.00  ? 149  ILE C O   1 
ATOM   3299  C  CB  . ILE C  1 149 ? 42.641  82.264  29.596  1.00 5.00  ? 149  ILE C CB  1 
ATOM   3300  C  CG1 . ILE C  1 149 ? 41.829  82.056  28.332  1.00 5.00  ? 149  ILE C CG1 1 
ATOM   3301  C  CG2 . ILE C  1 149 ? 43.232  80.907  30.019  1.00 5.00  ? 149  ILE C CG2 1 
ATOM   3302  C  CD1 . ILE C  1 149 ? 42.714  81.748  27.065  1.00 5.08  ? 149  ILE C CD1 1 
ATOM   3303  N  N   . GLY C  1 150 ? 41.994  82.338  33.038  1.00 5.00  ? 150  GLY C N   1 
ATOM   3304  C  CA  . GLY C  1 150 ? 42.526  82.552  34.392  1.00 5.00  ? 150  GLY C CA  1 
ATOM   3305  C  C   . GLY C  1 150 ? 43.167  81.289  34.965  1.00 5.00  ? 150  GLY C C   1 
ATOM   3306  O  O   . GLY C  1 150 ? 42.866  80.176  34.546  1.00 5.00  ? 150  GLY C O   1 
ATOM   3307  N  N   . ILE C  1 151 ? 44.082  81.487  35.898  1.00 5.00  ? 151  ILE C N   1 
ATOM   3308  C  CA  . ILE C  1 151 ? 44.725  80.347  36.574  1.00 5.00  ? 151  ILE C CA  1 
ATOM   3309  C  C   . ILE C  1 151 ? 43.708  79.648  37.442  1.00 5.00  ? 151  ILE C C   1 
ATOM   3310  O  O   . ILE C  1 151 ? 42.974  80.307  38.134  1.00 5.00  ? 151  ILE C O   1 
ATOM   3311  C  CB  . ILE C  1 151 ? 45.858  80.861  37.467  1.00 5.00  ? 151  ILE C CB  1 
ATOM   3312  C  CG1 . ILE C  1 151 ? 46.976  81.430  36.583  1.00 5.64  ? 151  ILE C CG1 1 
ATOM   3313  C  CG2 . ILE C  1 151 ? 46.386  79.716  38.371  1.00 6.82  ? 151  ILE C CG2 1 
ATOM   3314  C  CD1 . ILE C  1 151 ? 48.042  82.233  37.373  1.00 11.33 ? 151  ILE C CD1 1 
ATOM   3315  N  N   . ALA C  1 152 ? 43.719  78.304  37.439  1.00 5.00  ? 152  ALA C N   1 
ATOM   3316  C  CA  . ALA C  1 152 ? 42.785  77.511  38.204  1.00 5.93  ? 152  ALA C CA  1 
ATOM   3317  C  C   . ALA C  1 152 ? 43.535  76.544  39.125  1.00 7.20  ? 152  ALA C C   1 
ATOM   3318  O  O   . ALA C  1 152 ? 44.705  76.262  38.911  1.00 6.60  ? 152  ALA C O   1 
ATOM   3319  C  CB  . ALA C  1 152 ? 41.863  76.700  37.211  1.00 6.64  ? 152  ALA C CB  1 
ATOM   3320  N  N   . GLN C  1 153 ? 42.849  76.072  40.136  1.00 8.32  ? 153  GLN C N   1 
ATOM   3321  C  CA  . GLN C  1 153 ? 43.467  75.135  41.074  1.00 12.05 ? 153  GLN C CA  1 
ATOM   3322  C  C   . GLN C  1 153 ? 43.558  73.770  40.422  1.00 14.22 ? 153  GLN C C   1 
ATOM   3323  O  O   . GLN C  1 153 ? 42.604  73.337  39.767  1.00 15.04 ? 153  GLN C O   1 
ATOM   3324  C  CB  . GLN C  1 153 ? 42.652  75.050  42.350  1.00 11.76 ? 153  GLN C CB  1 
ATOM   3325  C  CG  . GLN C  1 153 ? 43.357  74.162  43.394  1.00 13.65 ? 153  GLN C CG  1 
ATOM   3326  C  CD  . GLN C  1 153 ? 42.615  74.134  44.686  1.00 17.25 ? 153  GLN C CD  1 
ATOM   3327  O  OE1 . GLN C  1 153 ? 41.436  73.762  44.717  1.00 21.32 ? 153  GLN C OE1 1 
ATOM   3328  N  NE2 . GLN C  1 153 ? 43.290  74.527  45.771  1.00 18.05 ? 153  GLN C NE2 1 
ATOM   3329  O  OXT . GLN C  1 153 ? 44.614  73.146  40.562  1.00 18.09 ? 153  GLN C OXT 1 
ATOM   3330  N  N   . ALA D  1 1   ? -8.809  104.288 89.897  1.00 23.79 ? 1    ALA D N   1 
ATOM   3331  C  CA  . ALA D  1 1   ? -7.998  103.663 88.790  1.00 22.01 ? 1    ALA D CA  1 
ATOM   3332  C  C   . ALA D  1 1   ? -7.504  102.230 89.061  1.00 21.83 ? 1    ALA D C   1 
ATOM   3333  O  O   . ALA D  1 1   ? -6.981  101.914 90.145  1.00 22.41 ? 1    ALA D O   1 
ATOM   3334  C  CB  . ALA D  1 1   ? -6.793  104.550 88.417  1.00 22.71 ? 1    ALA D CB  1 
ATOM   3335  N  N   . THR D  1 2   ? -7.630  101.377 88.050  1.00 18.32 ? 2    THR D N   1 
ATOM   3336  C  CA  . THR D  1 2   ? -7.114  100.040 88.154  1.00 16.20 ? 2    THR D CA  1 
ATOM   3337  C  C   . THR D  1 2   ? -5.641  100.116 87.793  1.00 12.53 ? 2    THR D C   1 
ATOM   3338  O  O   . THR D  1 2   ? -5.245  100.886 86.930  1.00 9.67  ? 2    THR D O   1 
ATOM   3339  C  CB  . THR D  1 2   ? -7.899  99.095  87.236  1.00 17.98 ? 2    THR D CB  1 
ATOM   3340  O  OG1 . THR D  1 2   ? -9.289  99.158  87.599  1.00 21.60 ? 2    THR D OG1 1 
ATOM   3341  C  CG2 . THR D  1 2   ? -7.565  97.679  87.563  1.00 19.72 ? 2    THR D CG2 1 
ATOM   3342  N  N   . LYS D  1 3   ? -4.834  99.325  88.491  1.00 10.32 ? 3    LYS D N   1 
ATOM   3343  C  CA  . LYS D  1 3   ? -3.395  99.308  88.282  1.00 8.49  ? 3    LYS D CA  1 
ATOM   3344  C  C   . LYS D  1 3   ? -2.923  97.860  88.153  1.00 8.56  ? 3    LYS D C   1 
ATOM   3345  O  O   . LYS D  1 3   ? -3.485  96.954  88.792  1.00 7.16  ? 3    LYS D O   1 
ATOM   3346  C  CB  . LYS D  1 3   ? -2.709  99.933  89.492  1.00 9.61  ? 3    LYS D CB  1 
ATOM   3347  C  CG  . LYS D  1 3   ? -3.072  101.415 89.714  1.00 12.67 ? 3    LYS D CG  1 
ATOM   3348  C  CD  . LYS D  1 3   ? -2.339  101.980 90.956  1.00 19.12 ? 3    LYS D CD  1 
ATOM   3349  C  CE  . LYS D  1 3   ? -3.005  103.251 91.515  1.00 22.47 ? 3    LYS D CE  1 
ATOM   3350  N  NZ  . LYS D  1 3   ? -3.456  104.151 90.412  1.00 28.98 ? 3    LYS D NZ  1 
ATOM   3351  N  N   . ALA D  1 4   ? -1.923  97.651  87.299  1.00 6.97  ? 4    ALA D N   1 
ATOM   3352  C  CA  . ALA D  1 4   ? -1.343  96.330  87.121  1.00 6.51  ? 4    ALA D CA  1 
ATOM   3353  C  C   . ALA D  1 4   ? 0.167   96.494  86.940  1.00 5.95  ? 4    ALA D C   1 
ATOM   3354  O  O   . ALA D  1 4   ? 0.669   97.610  86.774  1.00 6.68  ? 4    ALA D O   1 
ATOM   3355  C  CB  . ALA D  1 4   ? -1.986  95.615  85.915  1.00 6.87  ? 4    ALA D CB  1 
ATOM   3356  N  N   . VAL D  1 5   ? 0.906   95.394  87.041  1.00 5.67  ? 5    VAL D N   1 
ATOM   3357  C  CA  . VAL D  1 5   ? 2.338   95.451  86.938  1.00 5.91  ? 5    VAL D CA  1 
ATOM   3358  C  C   . VAL D  1 5   ? 2.833   94.136  86.391  1.00 5.98  ? 5    VAL D C   1 
ATOM   3359  O  O   . VAL D  1 5   ? 2.179   93.121  86.551  1.00 6.31  ? 5    VAL D O   1 
ATOM   3360  C  CB  . VAL D  1 5   ? 2.973   95.751  88.293  1.00 7.75  ? 5    VAL D CB  1 
ATOM   3361  C  CG1 . VAL D  1 5   ? 2.709   94.560  89.256  1.00 7.63  ? 5    VAL D CG1 1 
ATOM   3362  C  CG2 . VAL D  1 5   ? 4.515   96.113  88.149  1.00 8.18  ? 5    VAL D CG2 1 
ATOM   3363  N  N   . CYS D  1 6   ? 3.983   94.175  85.733  1.00 5.49  ? 6    CYS D N   1 
ATOM   3364  C  CA  . CYS D  1 6   ? 4.569   92.981  85.177  1.00 6.54  ? 6    CYS D CA  1 
ATOM   3365  C  C   . CYS D  1 6   ? 6.076   93.048  85.293  1.00 6.93  ? 6    CYS D C   1 
ATOM   3366  O  O   . CYS D  1 6   ? 6.692   94.064  84.910  1.00 8.22  ? 6    CYS D O   1 
ATOM   3367  C  CB  . CYS D  1 6   ? 4.139   92.866  83.722  1.00 6.91  ? 6    CYS D CB  1 
ATOM   3368  S  SG  . CYS D  1 6   ? 4.817   91.425  82.854  1.00 8.30  ? 6    CYS D SG  1 
ATOM   3369  N  N   . VAL D  1 7   ? 6.658   91.982  85.835  1.00 7.18  ? 7    VAL D N   1 
ATOM   3370  C  CA  . VAL D  1 7   ? 8.109   91.809  85.895  1.00 7.43  ? 7    VAL D CA  1 
ATOM   3371  C  C   . VAL D  1 7   ? 8.550   90.905  84.738  1.00 8.36  ? 7    VAL D C   1 
ATOM   3372  O  O   . VAL D  1 7   ? 8.171   89.728  84.642  1.00 7.75  ? 7    VAL D O   1 
ATOM   3373  C  CB  . VAL D  1 7   ? 8.550   91.209  87.256  1.00 7.97  ? 7    VAL D CB  1 
ATOM   3374  C  CG1 . VAL D  1 7   ? 10.112  91.104  87.308  1.00 9.72  ? 7    VAL D CG1 1 
ATOM   3375  C  CG2 . VAL D  1 7   ? 7.989   92.079  88.371  1.00 8.52  ? 7    VAL D CG2 1 
ATOM   3376  N  N   . LEU D  1 8   ? 9.320   91.488  83.818  1.00 7.89  ? 8    LEU D N   1 
ATOM   3377  C  CA  . LEU D  1 8   ? 9.812   90.765  82.635  1.00 8.98  ? 8    LEU D CA  1 
ATOM   3378  C  C   . LEU D  1 8   ? 11.173  90.125  82.950  1.00 9.77  ? 8    LEU D C   1 
ATOM   3379  O  O   . LEU D  1 8   ? 12.099  90.810  83.376  1.00 9.61  ? 8    LEU D O   1 
ATOM   3380  C  CB  . LEU D  1 8   ? 10.000  91.769  81.484  1.00 9.63  ? 8    LEU D CB  1 
ATOM   3381  C  CG  . LEU D  1 8   ? 8.749   92.480  80.935  1.00 11.51 ? 8    LEU D CG  1 
ATOM   3382  C  CD1 . LEU D  1 8   ? 9.108   93.617  79.912  1.00 12.99 ? 8    LEU D CD1 1 
ATOM   3383  C  CD2 . LEU D  1 8   ? 7.863   91.467  80.287  1.00 13.24 ? 8    LEU D CD2 1 
ATOM   3384  N  N   . LYS D  1 9   ? 11.272  88.812  82.792  1.00 11.00 ? 9    LYS D N   1 
ATOM   3385  C  CA  . LYS D  1 9   ? 12.561  88.145  82.991  1.00 12.34 ? 9    LYS D CA  1 
ATOM   3386  C  C   . LYS D  1 9   ? 12.726  87.067  81.948  1.00 12.09 ? 9    LYS D C   1 
ATOM   3387  O  O   . LYS D  1 9   ? 11.756  86.601  81.387  1.00 10.72 ? 9    LYS D O   1 
ATOM   3388  C  CB  . LYS D  1 9   ? 12.590  87.496  84.364  1.00 14.61 ? 9    LYS D CB  1 
ATOM   3389  C  CG  . LYS D  1 9   ? 13.219  88.378  85.442  1.00 19.31 ? 9    LYS D CG  1 
ATOM   3390  C  CD  . LYS D  1 9   ? 12.573  88.135  86.813  1.00 28.39 ? 9    LYS D CD  1 
ATOM   3391  C  CE  . LYS D  1 9   ? 13.120  89.117  87.885  1.00 30.17 ? 9    LYS D CE  1 
ATOM   3392  N  NZ  . LYS D  1 9   ? 13.830  90.310  87.281  1.00 34.08 ? 9    LYS D NZ  1 
ATOM   3393  N  N   . GLY D  1 10  ? 13.955  86.641  81.690  1.00 12.80 ? 10   GLY D N   1 
ATOM   3394  C  CA  . GLY D  1 10  ? 14.141  85.550  80.760  1.00 13.55 ? 10   GLY D CA  1 
ATOM   3395  C  C   . GLY D  1 10  ? 15.454  84.853  81.024  1.00 14.42 ? 10   GLY D C   1 
ATOM   3396  O  O   . GLY D  1 10  ? 16.028  84.994  82.109  1.00 14.71 ? 10   GLY D O   1 
ATOM   3397  N  N   . ASP D  1 11  ? 15.926  84.107  80.038  1.00 15.41 ? 11   ASP D N   1 
ATOM   3398  C  CA  . ASP D  1 11  ? 17.185  83.367  80.178  1.00 17.25 ? 11   ASP D CA  1 
ATOM   3399  C  C   . ASP D  1 11  ? 18.423  84.243  80.002  1.00 17.68 ? 11   ASP D C   1 
ATOM   3400  O  O   . ASP D  1 11  ? 19.507  83.885  80.470  1.00 19.34 ? 11   ASP D O   1 
ATOM   3401  C  CB  . ASP D  1 11  ? 17.201  82.210  79.190  1.00 18.31 ? 11   ASP D CB  1 
ATOM   3402  N  N   . GLY D  1 12  ? 18.266  85.382  79.335  1.00 16.82 ? 12   GLY D N   1 
ATOM   3403  C  CA  . GLY D  1 12  ? 19.376  86.293  79.113  1.00 16.86 ? 12   GLY D CA  1 
ATOM   3404  C  C   . GLY D  1 12  ? 19.421  87.506  80.018  1.00 15.82 ? 12   GLY D C   1 
ATOM   3405  O  O   . GLY D  1 12  ? 18.913  87.483  81.145  1.00 16.07 ? 12   GLY D O   1 
ATOM   3406  N  N   . PRO D  1 13  ? 20.022  88.583  79.517  1.00 15.29 ? 13   PRO D N   1 
ATOM   3407  C  CA  . PRO D  1 13  ? 20.186  89.820  80.288  1.00 14.69 ? 13   PRO D CA  1 
ATOM   3408  C  C   . PRO D  1 13  ? 18.951  90.747  80.261  1.00 13.96 ? 13   PRO D C   1 
ATOM   3409  O  O   . PRO D  1 13  ? 18.955  91.750  80.970  1.00 13.98 ? 13   PRO D O   1 
ATOM   3410  C  CB  . PRO D  1 13  ? 21.327  90.543  79.547  1.00 14.64 ? 13   PRO D CB  1 
ATOM   3411  C  CG  . PRO D  1 13  ? 21.395  89.934  78.176  1.00 14.58 ? 13   PRO D CG  1 
ATOM   3412  C  CD  . PRO D  1 13  ? 20.592  88.683  78.160  1.00 15.27 ? 13   PRO D CD  1 
ATOM   3413  N  N   . VAL D  1 14  ? 17.941  90.450  79.453  1.00 13.69 ? 14   VAL D N   1 
ATOM   3414  C  CA  . VAL D  1 14  ? 16.790  91.354  79.346  1.00 14.05 ? 14   VAL D CA  1 
ATOM   3415  C  C   . VAL D  1 14  ? 15.905  91.227  80.569  1.00 14.40 ? 14   VAL D C   1 
ATOM   3416  O  O   . VAL D  1 14  ? 15.500  90.128  80.935  1.00 14.35 ? 14   VAL D O   1 
ATOM   3417  C  CB  . VAL D  1 14  ? 15.957  91.109  78.058  1.00 14.34 ? 14   VAL D CB  1 
ATOM   3418  C  CG1 . VAL D  1 14  ? 14.725  92.017  78.035  1.00 14.42 ? 14   VAL D CG1 1 
ATOM   3419  C  CG2 . VAL D  1 14  ? 16.823  91.364  76.781  1.00 13.15 ? 14   VAL D CG2 1 
ATOM   3420  N  N   . GLN D  1 15  ? 15.652  92.347  81.225  1.00 14.14 ? 15   GLN D N   1 
ATOM   3421  C  CA  . GLN D  1 15  ? 14.804  92.356  82.405  1.00 14.46 ? 15   GLN D CA  1 
ATOM   3422  C  C   . GLN D  1 15  ? 14.161  93.727  82.577  1.00 13.75 ? 15   GLN D C   1 
ATOM   3423  O  O   . GLN D  1 15  ? 14.761  94.768  82.265  1.00 13.76 ? 15   GLN D O   1 
ATOM   3424  C  CB  . GLN D  1 15  ? 15.573  91.927  83.673  1.00 15.20 ? 15   GLN D CB  1 
ATOM   3425  C  CG  . GLN D  1 15  ? 16.701  92.840  84.035  1.00 19.00 ? 15   GLN D CG  1 
ATOM   3426  C  CD  . GLN D  1 15  ? 17.425  92.510  85.351  1.00 25.59 ? 15   GLN D CD  1 
ATOM   3427  N  NE2 . GLN D  1 15  ? 16.684  92.042  86.349  1.00 28.44 ? 15   GLN D NE2 1 
ATOM   3428  N  N   . GLY D  1 16  ? 12.937  93.755  83.113  1.00 11.84 ? 16   GLY D N   1 
ATOM   3429  C  CA  . GLY D  1 16  ? 12.316  95.040  83.304  1.00 10.24 ? 16   GLY D CA  1 
ATOM   3430  C  C   . GLY D  1 16  ? 11.050  94.951  84.126  1.00 9.86  ? 16   GLY D C   1 
ATOM   3431  O  O   . GLY D  1 16  ? 10.667  93.868  84.572  1.00 9.98  ? 16   GLY D O   1 
ATOM   3432  N  N   . ILE D  1 17  ? 10.438  96.107  84.322  1.00 8.75  ? 17   ILE D N   1 
ATOM   3433  C  CA  . ILE D  1 17  ? 9.221   96.253  85.104  1.00 8.32  ? 17   ILE D CA  1 
ATOM   3434  C  C   . ILE D  1 17  ? 8.345   97.195  84.335  1.00 7.64  ? 17   ILE D C   1 
ATOM   3435  O  O   . ILE D  1 17  ? 8.766   98.318  83.976  1.00 6.84  ? 17   ILE D O   1 
ATOM   3436  C  CB  . ILE D  1 17  ? 9.549   96.885  86.416  1.00 9.05  ? 17   ILE D CB  1 
ATOM   3437  C  CG1 . ILE D  1 17  ? 10.372  95.900  87.269  1.00 8.76  ? 17   ILE D CG1 1 
ATOM   3438  C  CG2 . ILE D  1 17  ? 8.259   97.293  87.165  1.00 8.98  ? 17   ILE D CG2 1 
ATOM   3439  C  CD1 . ILE D  1 17  ? 10.845  96.558  88.645  1.00 11.59 ? 17   ILE D CD1 1 
ATOM   3440  N  N   . ILE D  1 18  ? 7.141   96.737  84.037  1.00 6.54  ? 18   ILE D N   1 
ATOM   3441  C  CA  . ILE D  1 18  ? 6.212   97.569  83.303  1.00 5.90  ? 18   ILE D CA  1 
ATOM   3442  C  C   . ILE D  1 18  ? 4.962   97.756  84.140  1.00 7.32  ? 18   ILE D C   1 
ATOM   3443  O  O   . ILE D  1 18  ? 4.411   96.781  84.665  1.00 5.92  ? 18   ILE D O   1 
ATOM   3444  C  CB  . ILE D  1 18  ? 5.846   96.855  81.985  1.00 6.18  ? 18   ILE D CB  1 
ATOM   3445  C  CG1 . ILE D  1 18  ? 7.071   96.725  81.047  1.00 5.72  ? 18   ILE D CG1 1 
ATOM   3446  C  CG2 . ILE D  1 18  ? 4.686   97.570  81.273  1.00 5.00  ? 18   ILE D CG2 1 
ATOM   3447  C  CD1 . ILE D  1 18  ? 7.690   98.089  80.633  1.00 10.37 ? 18   ILE D CD1 1 
ATOM   3448  N  N   . ASN D  1 19  ? 4.528   99.005  84.251  1.00 6.36  ? 19   ASN D N   1 
ATOM   3449  C  CA  . ASN D  1 19  ? 3.348   99.371  84.961  1.00 6.97  ? 19   ASN D CA  1 
ATOM   3450  C  C   . ASN D  1 19  ? 2.206   99.619  84.016  1.00 6.74  ? 19   ASN D C   1 
ATOM   3451  O  O   . ASN D  1 19  ? 2.427   100.050 82.875  1.00 5.65  ? 19   ASN D O   1 
ATOM   3452  C  CB  . ASN D  1 19  ? 3.610   100.663 85.743  1.00 6.62  ? 19   ASN D CB  1 
ATOM   3453  C  CG  . ASN D  1 19  ? 4.846   100.560 86.602  1.00 10.97 ? 19   ASN D CG  1 
ATOM   3454  O  OD1 . ASN D  1 19  ? 5.922   101.137 86.288  1.00 13.02 ? 19   ASN D OD1 1 
ATOM   3455  N  ND2 . ASN D  1 19  ? 4.736   99.796  87.670  1.00 5.66  ? 19   ASN D ND2 1 
ATOM   3456  N  N   . PHE D  1 20  ? 0.992   99.391  84.514  1.00 6.03  ? 20   PHE D N   1 
ATOM   3457  C  CA  . PHE D  1 20  ? -0.245  99.660  83.778  1.00 6.54  ? 20   PHE D CA  1 
ATOM   3458  C  C   . PHE D  1 20  ? -1.199  100.424 84.660  1.00 6.67  ? 20   PHE D C   1 
ATOM   3459  O  O   . PHE D  1 20  ? -1.324  100.141 85.862  1.00 7.47  ? 20   PHE D O   1 
ATOM   3460  C  CB  . PHE D  1 20  ? -0.979  98.367  83.383  1.00 6.38  ? 20   PHE D CB  1 
ATOM   3461  C  CG  . PHE D  1 20  ? -0.178  97.429  82.526  1.00 7.94  ? 20   PHE D CG  1 
ATOM   3462  C  CD1 . PHE D  1 20  ? 0.809   96.616  83.085  1.00 5.98  ? 20   PHE D CD1 1 
ATOM   3463  C  CD2 . PHE D  1 20  ? -0.437  97.342  81.162  1.00 9.31  ? 20   PHE D CD2 1 
ATOM   3464  C  CE1 . PHE D  1 20  ? 1.512   95.724  82.279  1.00 10.25 ? 20   PHE D CE1 1 
ATOM   3465  C  CE2 . PHE D  1 20  ? 0.282   96.482  80.352  1.00 11.51 ? 20   PHE D CE2 1 
ATOM   3466  C  CZ  . PHE D  1 20  ? 1.248   95.657  80.913  1.00 9.45  ? 20   PHE D CZ  1 
ATOM   3467  N  N   . GLU D  1 21  ? -1.892  101.405 84.079  1.00 6.94  ? 21   GLU D N   1 
ATOM   3468  C  CA  . GLU D  1 21  ? -2.858  102.169 84.855  1.00 8.91  ? 21   GLU D CA  1 
ATOM   3469  C  C   . GLU D  1 21  ? -4.041  102.560 83.984  1.00 8.70  ? 21   GLU D C   1 
ATOM   3470  O  O   . GLU D  1 21  ? -3.867  103.053 82.870  1.00 8.48  ? 21   GLU D O   1 
ATOM   3471  C  CB  . GLU D  1 21  ? -2.226  103.405 85.500  1.00 9.49  ? 21   GLU D CB  1 
ATOM   3472  C  CG  . GLU D  1 21  ? -3.236  104.183 86.332  1.00 16.05 ? 21   GLU D CG  1 
ATOM   3473  C  CD  . GLU D  1 21  ? -2.608  105.350 87.069  1.00 23.68 ? 21   GLU D CD  1 
ATOM   3474  O  OE1 . GLU D  1 21  ? -1.899  106.155 86.436  1.00 27.65 ? 21   GLU D OE1 1 
ATOM   3475  O  OE2 . GLU D  1 21  ? -2.841  105.464 88.280  1.00 28.75 ? 21   GLU D OE2 1 
ATOM   3476  N  N   . GLN D  1 22  ? -5.250  102.333 84.485  1.00 9.87  ? 22   GLN D N   1 
ATOM   3477  C  CA  . GLN D  1 22  ? -6.455  102.675 83.742  1.00 10.64 ? 22   GLN D CA  1 
ATOM   3478  C  C   . GLN D  1 22  ? -7.355  103.444 84.691  1.00 11.39 ? 22   GLN D C   1 
ATOM   3479  O  O   . GLN D  1 22  ? -7.892  102.890 85.668  1.00 11.60 ? 22   GLN D O   1 
ATOM   3480  C  CB  . GLN D  1 22  ? -7.153  101.424 83.205  1.00 9.68  ? 22   GLN D CB  1 
ATOM   3481  C  CG  . GLN D  1 22  ? -8.312  101.677 82.253  1.00 10.53 ? 22   GLN D CG  1 
ATOM   3482  C  CD  . GLN D  1 22  ? -8.981  100.382 81.785  1.00 12.16 ? 22   GLN D CD  1 
ATOM   3483  O  OE1 . GLN D  1 22  ? -9.042  99.388  82.547  1.00 11.60 ? 22   GLN D OE1 1 
ATOM   3484  N  NE2 . GLN D  1 22  ? -9.488  100.389 80.553  1.00 11.11 ? 22   GLN D NE2 1 
ATOM   3485  N  N   . LYS D  1 23  ? -7.509  104.728 84.405  1.00 13.48 ? 23   LYS D N   1 
ATOM   3486  C  CA  . LYS D  1 23  ? -8.281  105.569 85.315  1.00 15.68 ? 23   LYS D CA  1 
ATOM   3487  C  C   . LYS D  1 23  ? -9.786  105.398 85.198  1.00 15.78 ? 23   LYS D C   1 
ATOM   3488  O  O   . LYS D  1 23  ? -10.513 105.601 86.173  1.00 14.63 ? 23   LYS D O   1 
ATOM   3489  C  CB  . LYS D  1 23  ? -7.929  107.034 85.111  1.00 16.89 ? 23   LYS D CB  1 
ATOM   3490  C  CG  . LYS D  1 23  ? -6.660  107.427 85.846  1.00 21.86 ? 23   LYS D CG  1 
ATOM   3491  C  CD  . LYS D  1 23  ? -5.919  108.547 85.134  1.00 28.63 ? 23   LYS D CD  1 
ATOM   3492  C  CE  . LYS D  1 23  ? -4.932  109.237 86.092  1.00 32.59 ? 23   LYS D CE  1 
ATOM   3493  N  NZ  . LYS D  1 23  ? -4.659  108.392 87.312  1.00 33.98 ? 23   LYS D NZ  1 
ATOM   3494  N  N   . GLU D  1 24  ? -10.251 105.000 84.024  1.00 15.63 ? 24   GLU D N   1 
ATOM   3495  C  CA  . GLU D  1 24  ? -11.682 104.911 83.794  1.00 16.90 ? 24   GLU D CA  1 
ATOM   3496  C  C   . GLU D  1 24  ? -12.039 103.588 83.168  1.00 16.51 ? 24   GLU D C   1 
ATOM   3497  O  O   . GLU D  1 24  ? -11.318 103.113 82.308  1.00 16.73 ? 24   GLU D O   1 
ATOM   3498  C  CB  . GLU D  1 24  ? -12.131 106.039 82.836  1.00 17.07 ? 24   GLU D CB  1 
ATOM   3499  N  N   . SER D  1 25  ? -13.164 102.999 83.569  1.00 16.99 ? 25   SER D N   1 
ATOM   3500  C  CA  . SER D  1 25  ? -13.617 101.770 82.925  1.00 17.21 ? 25   SER D CA  1 
ATOM   3501  C  C   . SER D  1 25  ? -13.613 101.920 81.393  1.00 16.82 ? 25   SER D C   1 
ATOM   3502  O  O   . SER D  1 25  ? -14.092 102.920 80.837  1.00 16.72 ? 25   SER D O   1 
ATOM   3503  C  CB  . SER D  1 25  ? -15.009 101.349 83.435  1.00 17.96 ? 25   SER D CB  1 
ATOM   3504  O  OG  . SER D  1 25  ? -15.950 102.382 83.192  1.00 22.31 ? 25   SER D OG  1 
ATOM   3505  N  N   . ASN D  1 26  ? -13.073 100.910 80.724  1.00 16.48 ? 26   ASN D N   1 
ATOM   3506  C  CA  . ASN D  1 26  ? -12.951 100.901 79.250  1.00 16.91 ? 26   ASN D CA  1 
ATOM   3507  C  C   . ASN D  1 26  ? -12.139 102.066 78.655  1.00 16.24 ? 26   ASN D C   1 
ATOM   3508  O  O   . ASN D  1 26  ? -12.039 102.203 77.445  1.00 16.92 ? 26   ASN D O   1 
ATOM   3509  C  CB  . ASN D  1 26  ? -14.334 100.797 78.572  1.00 16.70 ? 26   ASN D CB  1 
ATOM   3510  C  CG  . ASN D  1 26  ? -14.249 100.345 77.112  1.00 18.61 ? 26   ASN D CG  1 
ATOM   3511  O  OD1 . ASN D  1 26  ? -13.420 99.501  76.763  1.00 21.14 ? 26   ASN D OD1 1 
ATOM   3512  N  ND2 . ASN D  1 26  ? -15.105 100.912 76.252  1.00 19.70 ? 26   ASN D ND2 1 
ATOM   3513  N  N   . GLY D  1 27  ? -11.552 102.902 79.510  1.00 15.77 ? 27   GLY D N   1 
ATOM   3514  C  CA  . GLY D  1 27  ? -10.755 104.027 79.041  1.00 13.62 ? 27   GLY D CA  1 
ATOM   3515  C  C   . GLY D  1 27  ? -9.332  103.630 78.690  1.00 12.89 ? 27   GLY D C   1 
ATOM   3516  O  O   . GLY D  1 27  ? -8.990  102.456 78.717  1.00 12.96 ? 27   GLY D O   1 
ATOM   3517  N  N   . PRO D  1 28  ? -8.508  104.602 78.299  1.00 11.95 ? 28   PRO D N   1 
ATOM   3518  C  CA  . PRO D  1 28  ? -7.123  104.313 77.905  1.00 11.51 ? 28   PRO D CA  1 
ATOM   3519  C  C   . PRO D  1 28  ? -6.330  103.685 79.040  1.00 10.37 ? 28   PRO D C   1 
ATOM   3520  O  O   . PRO D  1 28  ? -6.544  104.051 80.181  1.00 10.48 ? 28   PRO D O   1 
ATOM   3521  C  CB  . PRO D  1 28  ? -6.513  105.699 77.627  1.00 12.11 ? 28   PRO D CB  1 
ATOM   3522  C  CG  . PRO D  1 28  ? -7.639  106.616 77.477  1.00 12.08 ? 28   PRO D CG  1 
ATOM   3523  C  CD  . PRO D  1 28  ? -8.834  106.035 78.225  1.00 11.83 ? 28   PRO D CD  1 
ATOM   3524  N  N   . VAL D  1 29  ? -5.420  102.780 78.681  1.00 8.88  ? 29   VAL D N   1 
ATOM   3525  C  CA  . VAL D  1 29  ? -4.514  102.178 79.637  1.00 9.62  ? 29   VAL D CA  1 
ATOM   3526  C  C   . VAL D  1 29  ? -3.137  102.775 79.339  1.00 9.17  ? 29   VAL D C   1 
ATOM   3527  O  O   . VAL D  1 29  ? -2.665  102.728 78.193  1.00 11.20 ? 29   VAL D O   1 
ATOM   3528  C  CB  . VAL D  1 29  ? -4.454  100.667 79.504  1.00 9.34  ? 29   VAL D CB  1 
ATOM   3529  C  CG1 . VAL D  1 29  ? -3.423  100.077 80.492  1.00 7.60  ? 29   VAL D CG1 1 
ATOM   3530  C  CG2 . VAL D  1 29  ? -5.877  100.042 79.719  1.00 7.69  ? 29   VAL D CG2 1 
ATOM   3531  N  N   . LYS D  1 30  ? -2.530  103.353 80.365  1.00 9.91  ? 30   LYS D N   1 
ATOM   3532  C  CA  . LYS D  1 30  ? -1.177  103.874 80.271  1.00 9.94  ? 30   LYS D CA  1 
ATOM   3533  C  C   . LYS D  1 30  ? -0.247  102.731 80.648  1.00 9.96  ? 30   LYS D C   1 
ATOM   3534  O  O   . LYS D  1 30  ? -0.491  102.052 81.664  1.00 9.76  ? 30   LYS D O   1 
ATOM   3535  C  CB  . LYS D  1 30  ? -0.983  105.015 81.260  1.00 11.23 ? 30   LYS D CB  1 
ATOM   3536  C  CG  . LYS D  1 30  ? -1.647  106.323 80.850  1.00 15.64 ? 30   LYS D CG  1 
ATOM   3537  C  CD  . LYS D  1 30  ? -1.428  107.444 81.876  1.00 21.80 ? 30   LYS D CD  1 
ATOM   3538  C  CE  . LYS D  1 30  ? -2.260  108.692 81.511  1.00 23.72 ? 30   LYS D CE  1 
ATOM   3539  N  N   . VAL D  1 31  ? 0.788   102.537 79.833  1.00 8.71  ? 31   VAL D N   1 
ATOM   3540  C  CA  . VAL D  1 31  ? 1.779   101.508 80.056  1.00 9.66  ? 31   VAL D CA  1 
ATOM   3541  C  C   . VAL D  1 31  ? 3.154   102.110 80.032  1.00 9.50  ? 31   VAL D C   1 
ATOM   3542  O  O   . VAL D  1 31  ? 3.519   102.754 79.049  1.00 9.88  ? 31   VAL D O   1 
ATOM   3543  C  CB  . VAL D  1 31  ? 1.580   100.240 79.181  1.00 10.49 ? 31   VAL D CB  1 
ATOM   3544  C  CG1 . VAL D  1 31  ? 0.294   100.193 78.313  1.00 9.78  ? 31   VAL D CG1 1 
ATOM   3545  C  CG2 . VAL D  1 31  ? 2.830   99.379  78.851  1.00 11.14 ? 31   VAL D CG2 1 
ATOM   3546  N  N   . TRP D  1 32  ? 3.884   101.934 81.138  1.00 9.00  ? 32   TRP D N   1 
ATOM   3547  C  CA  . TRP D  1 32  ? 5.190   102.587 81.269  1.00 9.46  ? 32   TRP D CA  1 
ATOM   3548  C  C   . TRP D  1 32  ? 6.118   101.856 82.212  1.00 9.12  ? 32   TRP D C   1 
ATOM   3549  O  O   . TRP D  1 32  ? 5.683   101.153 83.117  1.00 8.21  ? 32   TRP D O   1 
ATOM   3550  C  CB  . TRP D  1 32  ? 5.018   104.009 81.744  1.00 9.97  ? 32   TRP D CB  1 
ATOM   3551  C  CG  . TRP D  1 32  ? 4.821   104.140 83.201  1.00 10.77 ? 32   TRP D CG  1 
ATOM   3552  C  CD1 . TRP D  1 32  ? 5.771   104.439 84.138  1.00 11.48 ? 32   TRP D CD1 1 
ATOM   3553  C  CD2 . TRP D  1 32  ? 3.597   103.970 83.910  1.00 9.79  ? 32   TRP D CD2 1 
ATOM   3554  N  NE1 . TRP D  1 32  ? 5.202   104.483 85.385  1.00 13.07 ? 32   TRP D NE1 1 
ATOM   3555  C  CE2 . TRP D  1 32  ? 3.863   104.216 85.274  1.00 11.91 ? 32   TRP D CE2 1 
ATOM   3556  C  CE3 . TRP D  1 32  ? 2.291   103.665 83.525  1.00 10.26 ? 32   TRP D CE3 1 
ATOM   3557  C  CZ2 . TRP D  1 32  ? 2.887   104.114 86.256  1.00 14.47 ? 32   TRP D CZ2 1 
ATOM   3558  C  CZ3 . TRP D  1 32  ? 1.312   103.561 84.507  1.00 12.17 ? 32   TRP D CZ3 1 
ATOM   3559  C  CH2 . TRP D  1 32  ? 1.615   103.805 85.855  1.00 16.23 ? 32   TRP D CH2 1 
ATOM   3560  N  N   . GLY D  1 33  ? 7.403   102.014 81.988  1.00 7.38  ? 33   GLY D N   1 
ATOM   3561  C  CA  . GLY D  1 33  ? 8.368   101.364 82.845  1.00 9.35  ? 33   GLY D CA  1 
ATOM   3562  C  C   . GLY D  1 33  ? 9.688   101.274 82.127  1.00 10.12 ? 33   GLY D C   1 
ATOM   3563  O  O   . GLY D  1 33  ? 9.874   101.942 81.143  1.00 9.72  ? 33   GLY D O   1 
ATOM   3564  N  N   . SER D  1 34  ? 10.617  100.497 82.648  1.00 11.11 ? 34   SER D N   1 
ATOM   3565  C  CA  . SER D  1 34  ? 11.920  100.438 82.028  1.00 12.48 ? 34   SER D CA  1 
ATOM   3566  C  C   . SER D  1 34  ? 12.305  99.000  81.741  1.00 12.91 ? 34   SER D C   1 
ATOM   3567  O  O   . SER D  1 34  ? 12.019  98.087  82.526  1.00 13.83 ? 34   SER D O   1 
ATOM   3568  C  CB  . SER D  1 34  ? 12.945  101.101 82.941  1.00 13.41 ? 34   SER D CB  1 
ATOM   3569  O  OG  . SER D  1 34  ? 14.200  101.065 82.295  1.00 18.22 ? 34   SER D OG  1 
ATOM   3570  N  N   . ILE D  1 35  ? 12.887  98.751  80.585  1.00 11.72 ? 35   ILE D N   1 
ATOM   3571  C  CA  . ILE D  1 35  ? 13.370  97.421  80.311  1.00 11.21 ? 35   ILE D CA  1 
ATOM   3572  C  C   . ILE D  1 35  ? 14.846  97.602  80.000  1.00 12.17 ? 35   ILE D C   1 
ATOM   3573  O  O   . ILE D  1 35  ? 15.201  98.492  79.228  1.00 12.11 ? 35   ILE D O   1 
ATOM   3574  C  CB  . ILE D  1 35  ? 12.700  96.818  79.083  1.00 10.67 ? 35   ILE D CB  1 
ATOM   3575  C  CG1 . ILE D  1 35  ? 11.161  96.792  79.253  1.00 10.49 ? 35   ILE D CG1 1 
ATOM   3576  C  CG2 . ILE D  1 35  ? 13.234  95.427  78.884  1.00 10.19 ? 35   ILE D CG2 1 
ATOM   3577  C  CD1 . ILE D  1 35  ? 10.417  96.234  78.007  1.00 13.37 ? 35   ILE D CD1 1 
ATOM   3578  N  N   . LYS D  1 36  ? 15.699  96.756  80.548  1.00 13.00 ? 36   LYS D N   1 
ATOM   3579  C  CA  . LYS D  1 36  ? 17.123  96.911  80.231  1.00 14.03 ? 36   LYS D CA  1 
ATOM   3580  C  C   . LYS D  1 36  ? 17.756  95.653  79.657  1.00 14.21 ? 36   LYS D C   1 
ATOM   3581  O  O   . LYS D  1 36  ? 17.133  94.598  79.604  1.00 13.35 ? 36   LYS D O   1 
ATOM   3582  C  CB  . LYS D  1 36  ? 17.899  97.358  81.471  1.00 14.34 ? 36   LYS D CB  1 
ATOM   3583  C  CG  . LYS D  1 36  ? 18.018  96.250  82.518  1.00 17.23 ? 36   LYS D CG  1 
ATOM   3584  C  CD  . LYS D  1 36  ? 18.604  96.760  83.817  1.00 23.21 ? 36   LYS D CD  1 
ATOM   3585  C  CE  . LYS D  1 36  ? 18.900  95.616  84.778  1.00 27.64 ? 36   LYS D CE  1 
ATOM   3586  N  NZ  . LYS D  1 36  ? 19.547  96.095  86.055  1.00 30.53 ? 36   LYS D NZ  1 
ATOM   3587  N  N   . GLY D  1 37  ? 19.027  95.780  79.249  1.00 14.05 ? 37   GLY D N   1 
ATOM   3588  C  CA  . GLY D  1 37  ? 19.755  94.679  78.657  1.00 13.73 ? 37   GLY D CA  1 
ATOM   3589  C  C   . GLY D  1 37  ? 19.365  94.364  77.232  1.00 12.76 ? 37   GLY D C   1 
ATOM   3590  O  O   . GLY D  1 37  ? 19.592  93.250  76.769  1.00 13.30 ? 37   GLY D O   1 
ATOM   3591  N  N   . LEU D  1 38  ? 18.780  95.321  76.518  1.00 12.72 ? 38   LEU D N   1 
ATOM   3592  C  CA  . LEU D  1 38  ? 18.339  95.090  75.135  1.00 12.29 ? 38   LEU D CA  1 
ATOM   3593  C  C   . LEU D  1 38  ? 19.317  95.651  74.077  1.00 12.46 ? 38   LEU D C   1 
ATOM   3594  O  O   . LEU D  1 38  ? 20.056  96.587  74.379  1.00 10.61 ? 38   LEU D O   1 
ATOM   3595  C  CB  . LEU D  1 38  ? 17.020  95.812  74.889  1.00 12.04 ? 38   LEU D CB  1 
ATOM   3596  C  CG  . LEU D  1 38  ? 15.743  95.282  75.566  1.00 11.51 ? 38   LEU D CG  1 
ATOM   3597  C  CD1 . LEU D  1 38  ? 14.726  96.404  75.632  1.00 11.28 ? 38   LEU D CD1 1 
ATOM   3598  C  CD2 . LEU D  1 38  ? 15.221  94.062  74.778  1.00 7.67  ? 38   LEU D CD2 1 
ATOM   3599  N  N   . THR D  1 39  ? 19.253  95.121  72.847  1.00 12.98 ? 39   THR D N   1 
ATOM   3600  C  CA  . THR D  1 39  ? 20.018  95.695  71.720  1.00 14.12 ? 39   THR D CA  1 
ATOM   3601  C  C   . THR D  1 39  ? 19.398  97.038  71.362  1.00 14.40 ? 39   THR D C   1 
ATOM   3602  O  O   . THR D  1 39  ? 18.182  97.208  71.441  1.00 13.58 ? 39   THR D O   1 
ATOM   3603  C  CB  . THR D  1 39  ? 20.014  94.788  70.446  1.00 14.64 ? 39   THR D CB  1 
ATOM   3604  O  OG1 . THR D  1 39  ? 18.672  94.398  70.091  1.00 16.54 ? 39   THR D OG1 1 
ATOM   3605  C  CG2 . THR D  1 39  ? 20.751  93.484  70.671  1.00 16.05 ? 39   THR D CG2 1 
ATOM   3606  N  N   . GLU D  1 40  ? 20.219  98.003  70.951  1.00 13.62 ? 40   GLU D N   1 
ATOM   3607  C  CA  . GLU D  1 40  ? 19.688  99.317  70.564  1.00 13.56 ? 40   GLU D CA  1 
ATOM   3608  C  C   . GLU D  1 40  ? 18.662  99.160  69.464  1.00 13.30 ? 40   GLU D C   1 
ATOM   3609  O  O   . GLU D  1 40  ? 18.848  98.362  68.537  1.00 13.07 ? 40   GLU D O   1 
ATOM   3610  C  CB  . GLU D  1 40  ? 20.822  100.247 70.052  1.00 13.74 ? 40   GLU D CB  1 
ATOM   3611  C  CG  . GLU D  1 40  ? 20.342  101.625 69.582  1.00 15.25 ? 40   GLU D CG  1 
ATOM   3612  C  CD  . GLU D  1 40  ? 21.489  102.580 69.197  1.00 21.01 ? 40   GLU D CD  1 
ATOM   3613  O  OE1 . GLU D  1 40  ? 22.679  102.149 69.230  1.00 18.26 ? 40   GLU D OE1 1 
ATOM   3614  O  OE2 . GLU D  1 40  ? 21.195  103.771 68.864  1.00 20.36 ? 40   GLU D OE2 1 
ATOM   3615  N  N   . GLY D  1 41  ? 17.604  99.963  69.511  1.00 13.05 ? 41   GLY D N   1 
ATOM   3616  C  CA  . GLY D  1 41  ? 16.636  99.915  68.444  1.00 13.56 ? 41   GLY D CA  1 
ATOM   3617  C  C   . GLY D  1 41  ? 15.308  99.315  68.840  1.00 14.24 ? 41   GLY D C   1 
ATOM   3618  O  O   . GLY D  1 41  ? 14.980  99.225  70.039  1.00 13.98 ? 41   GLY D O   1 
ATOM   3619  N  N   . LEU D  1 42  ? 14.525  98.938  67.837  1.00 14.31 ? 42   LEU D N   1 
ATOM   3620  C  CA  . LEU D  1 42  ? 13.150  98.492  68.084  1.00 13.33 ? 42   LEU D CA  1 
ATOM   3621  C  C   . LEU D  1 42  ? 13.050  97.057  68.549  1.00 12.76 ? 42   LEU D C   1 
ATOM   3622  O  O   . LEU D  1 42  ? 13.792  96.175  68.080  1.00 10.74 ? 42   LEU D O   1 
ATOM   3623  C  CB  . LEU D  1 42  ? 12.322  98.651  66.823  1.00 15.22 ? 42   LEU D CB  1 
ATOM   3624  C  CG  . LEU D  1 42  ? 11.610  99.960  66.471  1.00 17.56 ? 42   LEU D CG  1 
ATOM   3625  C  CD1 . LEU D  1 42  ? 12.031  101.129 67.329  1.00 20.83 ? 42   LEU D CD1 1 
ATOM   3626  C  CD2 . LEU D  1 42  ? 11.754  100.240 64.996  1.00 18.18 ? 42   LEU D CD2 1 
ATOM   3627  N  N   . HIS D  1 43  ? 12.104  96.832  69.469  1.00 9.57  ? 43   HIS D N   1 
ATOM   3628  C  CA  . HIS D  1 43  ? 11.809  95.486  69.973  1.00 10.76 ? 43   HIS D CA  1 
ATOM   3629  C  C   . HIS D  1 43  ? 10.309  95.314  70.042  1.00 9.45  ? 43   HIS D C   1 
ATOM   3630  O  O   . HIS D  1 43  ? 9.596   96.191  70.541  1.00 9.66  ? 43   HIS D O   1 
ATOM   3631  C  CB  . HIS D  1 43  ? 12.471  95.239  71.333  1.00 10.48 ? 43   HIS D CB  1 
ATOM   3632  C  CG  . HIS D  1 43  ? 13.966  95.132  71.256  1.00 13.69 ? 43   HIS D CG  1 
ATOM   3633  N  ND1 . HIS D  1 43  ? 14.614  93.957  70.929  1.00 15.03 ? 43   HIS D ND1 1 
ATOM   3634  C  CD2 . HIS D  1 43  ? 14.937  96.062  71.423  1.00 15.55 ? 43   HIS D CD2 1 
ATOM   3635  C  CE1 . HIS D  1 43  ? 15.919  94.167  70.904  1.00 17.01 ? 43   HIS D CE1 1 
ATOM   3636  N  NE2 . HIS D  1 43  ? 16.142  95.436  71.202  1.00 15.43 ? 43   HIS D NE2 1 
ATOM   3637  N  N   . GLY D  1 44  ? 9.815   94.201  69.518  1.00 8.66  ? 44   GLY D N   1 
ATOM   3638  C  CA  . GLY D  1 44  ? 8.390   93.950  69.537  1.00 8.86  ? 44   GLY D CA  1 
ATOM   3639  C  C   . GLY D  1 44  ? 7.955   93.834  71.004  1.00 8.12  ? 44   GLY D C   1 
ATOM   3640  O  O   . GLY D  1 44  ? 8.690   93.308  71.837  1.00 9.30  ? 44   GLY D O   1 
ATOM   3641  N  N   . PHE D  1 45  ? 6.747   94.280  71.282  1.00 8.18  ? 45   PHE D N   1 
ATOM   3642  C  CA  . PHE D  1 45  ? 6.188   94.345  72.648  1.00 8.45  ? 45   PHE D CA  1 
ATOM   3643  C  C   . PHE D  1 45  ? 4.701   94.025  72.577  1.00 8.66  ? 45   PHE D C   1 
ATOM   3644  O  O   . PHE D  1 45  ? 3.912   94.842  72.081  1.00 7.43  ? 45   PHE D O   1 
ATOM   3645  C  CB  . PHE D  1 45  ? 6.437   95.781  73.099  1.00 8.64  ? 45   PHE D CB  1 
ATOM   3646  C  CG  . PHE D  1 45  ? 6.126   96.076  74.554  1.00 9.46  ? 45   PHE D CG  1 
ATOM   3647  C  CD1 . PHE D  1 45  ? 6.903   95.548  75.582  1.00 7.32  ? 45   PHE D CD1 1 
ATOM   3648  C  CD2 . PHE D  1 45  ? 5.126   96.983  74.859  1.00 9.40  ? 45   PHE D CD2 1 
ATOM   3649  C  CE1 . PHE D  1 45  ? 6.620   95.918  76.930  1.00 9.92  ? 45   PHE D CE1 1 
ATOM   3650  C  CE2 . PHE D  1 45  ? 4.833   97.357  76.195  1.00 9.92  ? 45   PHE D CE2 1 
ATOM   3651  C  CZ  . PHE D  1 45  ? 5.564   96.804  77.219  1.00 8.37  ? 45   PHE D CZ  1 
ATOM   3652  N  N   . HIS D  1 46  ? 4.306   92.848  73.124  1.00 9.38  ? 46   HIS D N   1 
ATOM   3653  C  CA  . HIS D  1 46  ? 2.949   92.366  72.980  1.00 9.12  ? 46   HIS D CA  1 
ATOM   3654  C  C   . HIS D  1 46  ? 2.435   91.691  74.242  1.00 7.19  ? 46   HIS D C   1 
ATOM   3655  O  O   . HIS D  1 46  ? 3.199   91.156  75.048  1.00 7.60  ? 46   HIS D O   1 
ATOM   3656  C  CB  . HIS D  1 46  ? 2.892   91.269  71.901  1.00 10.21 ? 46   HIS D CB  1 
ATOM   3657  C  CG  . HIS D  1 46  ? 3.656   91.589  70.646  1.00 11.34 ? 46   HIS D CG  1 
ATOM   3658  N  ND1 . HIS D  1 46  ? 4.651   90.779  70.155  1.00 11.37 ? 46   HIS D ND1 1 
ATOM   3659  C  CD2 . HIS D  1 46  ? 3.561   92.627  69.779  1.00 12.63 ? 46   HIS D CD2 1 
ATOM   3660  C  CE1 . HIS D  1 46  ? 5.136   91.287  69.038  1.00 13.08 ? 46   HIS D CE1 1 
ATOM   3661  N  NE2 . HIS D  1 46  ? 4.481   92.404  68.778  1.00 12.51 ? 46   HIS D NE2 1 
ATOM   3662  N  N   . VAL D  1 47  ? 1.134   91.651  74.332  1.00 6.20  ? 47   VAL D N   1 
ATOM   3663  C  CA  . VAL D  1 47  ? 0.483   90.841  75.326  1.00 7.52  ? 47   VAL D CA  1 
ATOM   3664  C  C   . VAL D  1 47  ? 0.086   89.541  74.635  1.00 7.31  ? 47   VAL D C   1 
ATOM   3665  O  O   . VAL D  1 47  ? -0.645  89.563  73.630  1.00 7.14  ? 47   VAL D O   1 
ATOM   3666  C  CB  . VAL D  1 47  ? -0.772  91.492  75.845  1.00 5.69  ? 47   VAL D CB  1 
ATOM   3667  C  CG1 . VAL D  1 47  ? -1.439  90.536  76.824  1.00 6.58  ? 47   VAL D CG1 1 
ATOM   3668  C  CG2 . VAL D  1 47  ? -0.444  92.858  76.513  1.00 7.74  ? 47   VAL D CG2 1 
ATOM   3669  N  N   . HIS D  1 48  ? 0.597   88.425  75.154  1.00 7.46  ? 48   HIS D N   1 
ATOM   3670  C  CA  . HIS D  1 48  ? 0.344   87.112  74.607  1.00 7.87  ? 48   HIS D CA  1 
ATOM   3671  C  C   . HIS D  1 48  ? -0.780  86.494  75.406  1.00 7.56  ? 48   HIS D C   1 
ATOM   3672  O  O   . HIS D  1 48  ? -1.043  86.910  76.527  1.00 9.37  ? 48   HIS D O   1 
ATOM   3673  C  CB  . HIS D  1 48  ? 1.612   86.225  74.654  1.00 7.98  ? 48   HIS D CB  1 
ATOM   3674  C  CG  . HIS D  1 48  ? 2.616   86.558  73.586  1.00 8.93  ? 48   HIS D CG  1 
ATOM   3675  N  ND1 . HIS D  1 48  ? 3.058   85.640  72.657  1.00 6.66  ? 48   HIS D ND1 1 
ATOM   3676  C  CD2 . HIS D  1 48  ? 3.192   87.733  73.253  1.00 9.53  ? 48   HIS D CD2 1 
ATOM   3677  C  CE1 . HIS D  1 48  ? 3.901   86.234  71.818  1.00 11.90 ? 48   HIS D CE1 1 
ATOM   3678  N  NE2 . HIS D  1 48  ? 4.019   87.495  72.185  1.00 7.95  ? 48   HIS D NE2 1 
ATOM   3679  N  N   . GLU D  1 49  ? -1.432  85.500  74.829  1.00 7.94  ? 49   GLU D N   1 
ATOM   3680  C  CA  . GLU D  1 49  ? -2.691  84.999  75.358  1.00 8.50  ? 49   GLU D CA  1 
ATOM   3681  C  C   . GLU D  1 49  ? -2.640  84.377  76.750  1.00 7.79  ? 49   GLU D C   1 
ATOM   3682  O  O   . GLU D  1 49  ? -3.513  84.650  77.591  1.00 7.12  ? 49   GLU D O   1 
ATOM   3683  C  CB  . GLU D  1 49  ? -3.297  83.961  74.401  1.00 8.99  ? 49   GLU D CB  1 
ATOM   3684  C  CG  . GLU D  1 49  ? -4.707  83.596  74.787  1.00 12.86 ? 49   GLU D CG  1 
ATOM   3685  C  CD  . GLU D  1 49  ? -5.354  82.688  73.749  1.00 13.41 ? 49   GLU D CD  1 
ATOM   3686  O  OE1 . GLU D  1 49  ? -4.693  82.353  72.752  1.00 12.50 ? 49   GLU D OE1 1 
ATOM   3687  O  OE2 . GLU D  1 49  ? -6.490  82.267  73.973  1.00 15.40 ? 49   GLU D OE2 1 
ATOM   3688  N  N   . PHE D  1 50  ? -1.658  83.522  77.005  1.00 8.60  ? 50   PHE D N   1 
ATOM   3689  C  CA  . PHE D  1 50  ? -1.704  82.820  78.306  1.00 9.48  ? 50   PHE D CA  1 
ATOM   3690  C  C   . PHE D  1 50  ? -0.694  83.297  79.316  1.00 9.89  ? 50   PHE D C   1 
ATOM   3691  O  O   . PHE D  1 50  ? 0.447   83.594  78.933  1.00 10.01 ? 50   PHE D O   1 
ATOM   3692  C  CB  . PHE D  1 50  ? -1.529  81.317  78.110  1.00 9.88  ? 50   PHE D CB  1 
ATOM   3693  C  CG  . PHE D  1 50  ? -2.438  80.763  77.062  1.00 13.57 ? 50   PHE D CG  1 
ATOM   3694  C  CD1 . PHE D  1 50  ? -3.816  80.784  77.245  1.00 13.52 ? 50   PHE D CD1 1 
ATOM   3695  C  CD2 . PHE D  1 50  ? -1.926  80.286  75.871  1.00 13.98 ? 50   PHE D CD2 1 
ATOM   3696  C  CE1 . PHE D  1 50  ? -4.673  80.262  76.238  1.00 14.41 ? 50   PHE D CE1 1 
ATOM   3697  C  CE2 . PHE D  1 50  ? -2.763  79.820  74.850  1.00 16.57 ? 50   PHE D CE2 1 
ATOM   3698  C  CZ  . PHE D  1 50  ? -4.131  79.805  75.049  1.00 15.11 ? 50   PHE D CZ  1 
ATOM   3699  N  N   . GLY D  1 51  ? -1.105  83.319  80.601  1.00 8.69  ? 51   GLY D N   1 
ATOM   3700  C  CA  . GLY D  1 51  ? -0.201  83.705  81.685  1.00 9.31  ? 51   GLY D CA  1 
ATOM   3701  C  C   . GLY D  1 51  ? 0.427   82.431  82.214  1.00 10.07 ? 51   GLY D C   1 
ATOM   3702  O  O   . GLY D  1 51  ? 0.341   82.105  83.411  1.00 9.16  ? 51   GLY D O   1 
ATOM   3703  N  N   . ASP D  1 52  ? 1.025   81.685  81.276  1.00 9.83  ? 52   ASP D N   1 
ATOM   3704  C  CA  . ASP D  1 52  ? 1.594   80.373  81.557  1.00 10.63 ? 52   ASP D CA  1 
ATOM   3705  C  C   . ASP D  1 52  ? 3.094   80.391  81.269  1.00 10.36 ? 52   ASP D C   1 
ATOM   3706  O  O   . ASP D  1 52  ? 3.510   80.452  80.110  1.00 9.85  ? 52   ASP D O   1 
ATOM   3707  C  CB  . ASP D  1 52  ? 0.917   79.363  80.620  1.00 11.02 ? 52   ASP D CB  1 
ATOM   3708  C  CG  . ASP D  1 52  ? 1.300   77.937  80.917  1.00 10.60 ? 52   ASP D CG  1 
ATOM   3709  O  OD1 . ASP D  1 52  ? 2.383   77.711  81.499  1.00 10.79 ? 52   ASP D OD1 1 
ATOM   3710  O  OD2 . ASP D  1 52  ? 0.580   76.978  80.581  1.00 13.85 ? 52   ASP D OD2 1 
ATOM   3711  N  N   . ASN D  1 53  ? 3.889   80.341  82.325  1.00 10.23 ? 53   ASN D N   1 
ATOM   3712  C  CA  . ASN D  1 53  ? 5.341   80.370  82.226  1.00 11.52 ? 53   ASN D CA  1 
ATOM   3713  C  C   . ASN D  1 53  ? 5.931   78.982  82.477  1.00 10.74 ? 53   ASN D C   1 
ATOM   3714  O  O   . ASN D  1 53  ? 7.088   78.859  82.836  1.00 10.43 ? 53   ASN D O   1 
ATOM   3715  C  CB  . ASN D  1 53  ? 5.882   81.306  83.345  1.00 12.50 ? 53   ASN D CB  1 
ATOM   3716  C  CG  . ASN D  1 53  ? 7.362   81.678  83.148  1.00 16.62 ? 53   ASN D CG  1 
ATOM   3717  O  OD1 . ASN D  1 53  ? 8.153   81.680  84.108  1.00 24.06 ? 53   ASN D OD1 1 
ATOM   3718  N  ND2 . ASN D  1 53  ? 7.732   81.988  81.924  1.00 21.56 ? 53   ASN D ND2 1 
ATOM   3719  N  N   . THR D  1 54  ? 5.133   77.931  82.363  1.00 10.11 ? 54   THR D N   1 
ATOM   3720  C  CA  . THR D  1 54  ? 5.641   76.618  82.737  1.00 11.61 ? 54   THR D CA  1 
ATOM   3721  C  C   . THR D  1 54  ? 6.798   76.136  81.824  1.00 12.98 ? 54   THR D C   1 
ATOM   3722  O  O   . THR D  1 54  ? 7.618   75.322  82.255  1.00 12.56 ? 54   THR D O   1 
ATOM   3723  C  CB  . THR D  1 54  ? 4.511   75.558  82.760  1.00 11.38 ? 54   THR D CB  1 
ATOM   3724  O  OG1 . THR D  1 54  ? 3.843   75.517  81.487  1.00 11.08 ? 54   THR D OG1 1 
ATOM   3725  C  CG2 . THR D  1 54  ? 3.441   75.984  83.713  1.00 11.97 ? 54   THR D CG2 1 
ATOM   3726  N  N   . ALA D  1 55  ? 6.841   76.609  80.586  1.00 13.72 ? 55   ALA D N   1 
ATOM   3727  C  CA  . ALA D  1 55  ? 7.953   76.281  79.679  1.00 15.61 ? 55   ALA D CA  1 
ATOM   3728  C  C   . ALA D  1 55  ? 8.606   77.567  79.236  1.00 16.10 ? 55   ALA D C   1 
ATOM   3729  O  O   . ALA D  1 55  ? 8.898   77.743  78.050  1.00 17.51 ? 55   ALA D O   1 
ATOM   3730  C  CB  . ALA D  1 55  ? 7.455   75.539  78.446  1.00 16.34 ? 55   ALA D CB  1 
ATOM   3731  N  N   . GLY D  1 56  ? 8.797   78.488  80.165  1.00 15.62 ? 56   GLY D N   1 
ATOM   3732  C  CA  . GLY D  1 56  ? 9.346   79.791  79.809  1.00 15.53 ? 56   GLY D CA  1 
ATOM   3733  C  C   . GLY D  1 56  ? 8.365   80.623  78.999  1.00 14.90 ? 56   GLY D C   1 
ATOM   3734  O  O   . GLY D  1 56  ? 7.152   80.406  79.053  1.00 14.66 ? 56   GLY D O   1 
ATOM   3735  N  N   . CYS D  1 57  ? 8.888   81.558  78.208  1.00 14.85 ? 57   CYS D N   1 
ATOM   3736  C  CA  . CYS D  1 57  ? 8.022   82.436  77.443  1.00 14.86 ? 57   CYS D CA  1 
ATOM   3737  C  C   . CYS D  1 57  ? 7.246   81.677  76.361  1.00 13.88 ? 57   CYS D C   1 
ATOM   3738  O  O   . CYS D  1 57  ? 6.195   82.146  75.903  1.00 12.65 ? 57   CYS D O   1 
ATOM   3739  C  CB  . CYS D  1 57  ? 8.825   83.603  76.876  1.00 14.83 ? 57   CYS D CB  1 
ATOM   3740  S  SG  . CYS D  1 57  ? 9.553   84.655  78.171  1.00 19.77 ? 57   CYS D SG  1 
ATOM   3741  N  N   . THR D  1 58  ? 7.708   80.477  76.016  1.00 12.71 ? 58   THR D N   1 
ATOM   3742  C  CA  . THR D  1 58  ? 7.047   79.726  74.943  1.00 13.74 ? 58   THR D CA  1 
ATOM   3743  C  C   . THR D  1 58  ? 5.615   79.361  75.282  1.00 12.87 ? 58   THR D C   1 
ATOM   3744  O  O   . THR D  1 58  ? 4.738   79.372  74.411  1.00 13.50 ? 58   THR D O   1 
ATOM   3745  C  CB  . THR D  1 58  ? 7.819   78.429  74.617  1.00 14.05 ? 58   THR D CB  1 
ATOM   3746  O  OG1 . THR D  1 58  ? 9.125   78.763  74.147  1.00 17.72 ? 58   THR D OG1 1 
ATOM   3747  C  CG2 . THR D  1 58  ? 7.201   77.713  73.405  1.00 15.19 ? 58   THR D CG2 1 
ATOM   3748  N  N   . SER D  1 59  ? 5.361   79.022  76.546  1.00 11.42 ? 59   SER D N   1 
ATOM   3749  C  CA  . SER D  1 59  ? 4.032   78.577  76.893  1.00 10.39 ? 59   SER D CA  1 
ATOM   3750  C  C   . SER D  1 59  ? 3.008   79.724  77.008  1.00 10.37 ? 59   SER D C   1 
ATOM   3751  O  O   . SER D  1 59  ? 1.873   79.464  77.287  1.00 9.96  ? 59   SER D O   1 
ATOM   3752  C  CB  . SER D  1 59  ? 4.051   77.703  78.161  1.00 11.37 ? 59   SER D CB  1 
ATOM   3753  O  OG  . SER D  1 59  ? 4.967   78.242  79.067  1.00 12.69 ? 59   SER D OG  1 
ATOM   3754  N  N   . ALA D  1 60  ? 3.411   80.980  76.790  1.00 8.98  ? 60   ALA D N   1 
ATOM   3755  C  CA  . ALA D  1 60  ? 2.434   82.061  76.778  1.00 9.45  ? 60   ALA D CA  1 
ATOM   3756  C  C   . ALA D  1 60  ? 1.521   82.014  75.558  1.00 9.83  ? 60   ALA D C   1 
ATOM   3757  O  O   . ALA D  1 60  ? 0.550   82.754  75.468  1.00 9.15  ? 60   ALA D O   1 
ATOM   3758  C  CB  . ALA D  1 60  ? 3.146   83.460  76.839  1.00 9.27  ? 60   ALA D CB  1 
ATOM   3759  N  N   . GLY D  1 61  ? 1.850   81.195  74.562  1.00 10.67 ? 61   GLY D N   1 
ATOM   3760  C  CA  . GLY D  1 61  ? 0.969   81.146  73.406  1.00 9.95  ? 61   GLY D CA  1 
ATOM   3761  C  C   . GLY D  1 61  ? 1.158   82.316  72.453  1.00 9.86  ? 61   GLY D C   1 
ATOM   3762  O  O   . GLY D  1 61  ? 2.140   83.044  72.523  1.00 10.35 ? 61   GLY D O   1 
ATOM   3763  N  N   . PRO D  1 62  ? 0.212   82.506  71.551  1.00 9.59  ? 62   PRO D N   1 
ATOM   3764  C  CA  . PRO D  1 62  ? 0.315   83.561  70.522  1.00 9.91  ? 62   PRO D CA  1 
ATOM   3765  C  C   . PRO D  1 62  ? -0.183  84.885  71.049  1.00 10.08 ? 62   PRO D C   1 
ATOM   3766  O  O   . PRO D  1 62  ? -0.464  85.016  72.274  1.00 10.73 ? 62   PRO D O   1 
ATOM   3767  C  CB  . PRO D  1 62  ? -0.637  83.062  69.443  1.00 10.22 ? 62   PRO D CB  1 
ATOM   3768  C  CG  . PRO D  1 62  ? -1.704  82.365  70.250  1.00 11.11 ? 62   PRO D CG  1 
ATOM   3769  C  CD  . PRO D  1 62  ? -1.014  81.702  71.412  1.00 10.46 ? 62   PRO D CD  1 
ATOM   3770  N  N   . HIS D  1 63  ? -0.279  85.875  70.173  1.00 9.83  ? 63   HIS D N   1 
ATOM   3771  C  CA  . HIS D  1 63  ? -0.801  87.168  70.630  1.00 9.64  ? 63   HIS D CA  1 
ATOM   3772  C  C   . HIS D  1 63  ? -2.243  87.079  71.116  1.00 9.43  ? 63   HIS D C   1 
ATOM   3773  O  O   . HIS D  1 63  ? -3.037  86.313  70.542  1.00 9.75  ? 63   HIS D O   1 
ATOM   3774  C  CB  . HIS D  1 63  ? -0.661  88.220  69.531  1.00 9.01  ? 63   HIS D CB  1 
ATOM   3775  C  CG  . HIS D  1 63  ? 0.755   88.504  69.192  1.00 10.72 ? 63   HIS D CG  1 
ATOM   3776  N  ND1 . HIS D  1 63  ? 1.130   89.309  68.145  1.00 10.74 ? 63   HIS D ND1 1 
ATOM   3777  C  CD2 . HIS D  1 63  ? 1.898   88.033  69.737  1.00 11.61 ? 63   HIS D CD2 1 
ATOM   3778  C  CE1 . HIS D  1 63  ? 2.450   89.355  68.081  1.00 10.66 ? 63   HIS D CE1 1 
ATOM   3779  N  NE2 . HIS D  1 63  ? 2.940   88.583  69.039  1.00 12.56 ? 63   HIS D NE2 1 
ATOM   3780  N  N   . PHE D  1 64  ? -2.579  87.844  72.166  1.00 8.42  ? 64   PHE D N   1 
ATOM   3781  C  CA  . PHE D  1 64  ? -3.946  87.871  72.708  1.00 10.55 ? 64   PHE D CA  1 
ATOM   3782  C  C   . PHE D  1 64  ? -4.789  88.424  71.576  1.00 10.94 ? 64   PHE D C   1 
ATOM   3783  O  O   . PHE D  1 64  ? -4.515  89.503  71.098  1.00 11.04 ? 64   PHE D O   1 
ATOM   3784  C  CB  . PHE D  1 64  ? -4.002  88.774  73.948  1.00 10.94 ? 64   PHE D CB  1 
ATOM   3785  C  CG  . PHE D  1 64  ? -5.367  88.913  74.545  1.00 10.41 ? 64   PHE D CG  1 
ATOM   3786  C  CD1 . PHE D  1 64  ? -6.224  87.813  74.616  1.00 9.98  ? 64   PHE D CD1 1 
ATOM   3787  C  CD2 . PHE D  1 64  ? -5.777  90.132  75.083  1.00 10.24 ? 64   PHE D CD2 1 
ATOM   3788  C  CE1 . PHE D  1 64  ? -7.490  87.926  75.191  1.00 10.90 ? 64   PHE D CE1 1 
ATOM   3789  C  CE2 . PHE D  1 64  ? -7.029  90.261  75.643  1.00 10.18 ? 64   PHE D CE2 1 
ATOM   3790  C  CZ  . PHE D  1 64  ? -7.894  89.138  75.711  1.00 12.15 ? 64   PHE D CZ  1 
ATOM   3791  N  N   . ASN D  1 65  ? -5.783  87.670  71.135  1.00 11.91 ? 65   ASN D N   1 
ATOM   3792  C  CA  . ASN D  1 65  ? -6.519  88.008  69.901  1.00 13.05 ? 65   ASN D CA  1 
ATOM   3793  C  C   . ASN D  1 65  ? -7.941  87.481  69.976  1.00 14.23 ? 65   ASN D C   1 
ATOM   3794  O  O   . ASN D  1 65  ? -8.310  86.559  69.231  1.00 13.74 ? 65   ASN D O   1 
ATOM   3795  C  CB  . ASN D  1 65  ? -5.811  87.302  68.752  1.00 12.67 ? 65   ASN D CB  1 
ATOM   3796  C  CG  . ASN D  1 65  ? -6.431  87.596  67.390  1.00 13.86 ? 65   ASN D CG  1 
ATOM   3797  O  OD1 . ASN D  1 65  ? -7.050  88.638  67.189  1.00 15.56 ? 65   ASN D OD1 1 
ATOM   3798  N  ND2 . ASN D  1 65  ? -6.225  86.682  66.440  1.00 16.67 ? 65   ASN D ND2 1 
ATOM   3799  N  N   . PRO D  1 66  ? -8.733  88.020  70.893  1.00 13.80 ? 66   PRO D N   1 
ATOM   3800  C  CA  . PRO D  1 66  ? -10.110 87.546  71.087  1.00 15.38 ? 66   PRO D CA  1 
ATOM   3801  C  C   . PRO D  1 66  ? -11.028 87.789  69.907  1.00 16.10 ? 66   PRO D C   1 
ATOM   3802  O  O   . PRO D  1 66  ? -12.038 87.078  69.790  1.00 15.57 ? 66   PRO D O   1 
ATOM   3803  C  CB  . PRO D  1 66  ? -10.599 88.352  72.301  1.00 15.54 ? 66   PRO D CB  1 
ATOM   3804  C  CG  . PRO D  1 66  ? -9.692  89.536  72.310  1.00 14.83 ? 66   PRO D CG  1 
ATOM   3805  C  CD  . PRO D  1 66  ? -8.351  89.022  71.903  1.00 15.17 ? 66   PRO D CD  1 
ATOM   3806  N  N   . LEU D  1 67  ? -10.688 88.753  69.058  1.00 16.42 ? 67   LEU D N   1 
ATOM   3807  C  CA  . LEU D  1 67  ? -11.482 89.040  67.872  1.00 17.40 ? 67   LEU D CA  1 
ATOM   3808  C  C   . LEU D  1 67  ? -10.983 88.324  66.621  1.00 18.07 ? 67   LEU D C   1 
ATOM   3809  O  O   . LEU D  1 67  ? -11.463 88.590  65.514  1.00 18.64 ? 67   LEU D O   1 
ATOM   3810  C  CB  . LEU D  1 67  ? -11.578 90.541  67.635  1.00 17.37 ? 67   LEU D CB  1 
ATOM   3811  C  CG  . LEU D  1 67  ? -12.385 91.238  68.728  1.00 19.20 ? 67   LEU D CG  1 
ATOM   3812  C  CD1 . LEU D  1 67  ? -12.227 92.748  68.617  1.00 20.95 ? 67   LEU D CD1 1 
ATOM   3813  C  CD2 . LEU D  1 67  ? -13.867 90.828  68.678  1.00 22.40 ? 67   LEU D CD2 1 
ATOM   3814  N  N   . SER D  1 68  ? -10.026 87.415  66.790  1.00 18.41 ? 68   SER D N   1 
ATOM   3815  C  CA  . SER D  1 68  ? -9.539  86.607  65.673  1.00 19.32 ? 68   SER D CA  1 
ATOM   3816  C  C   . SER D  1 68  ? -9.180  87.487  64.482  1.00 19.42 ? 68   SER D C   1 
ATOM   3817  O  O   . SER D  1 68  ? -9.633  87.223  63.354  1.00 20.07 ? 68   SER D O   1 
ATOM   3818  C  CB  . SER D  1 68  ? -10.616 85.602  65.236  1.00 19.12 ? 68   SER D CB  1 
ATOM   3819  O  OG  . SER D  1 68  ? -10.969 84.677  66.265  1.00 19.79 ? 68   SER D OG  1 
ATOM   3820  N  N   . ARG D  1 69  ? -8.414  88.551  64.726  1.00 18.90 ? 69   ARG D N   1 
ATOM   3821  C  CA  . ARG D  1 69  ? -7.993  89.475  63.663  1.00 19.20 ? 69   ARG D CA  1 
ATOM   3822  C  C   . ARG D  1 69  ? -6.548  89.161  63.296  1.00 18.25 ? 69   ARG D C   1 
ATOM   3823  O  O   . ARG D  1 69  ? -5.942  88.299  63.924  1.00 18.39 ? 69   ARG D O   1 
ATOM   3824  C  CB  . ARG D  1 69  ? -8.134  90.946  64.105  1.00 19.76 ? 69   ARG D CB  1 
ATOM   3825  C  CG  . ARG D  1 69  ? -9.567  91.385  64.490  1.00 22.68 ? 69   ARG D CG  1 
ATOM   3826  C  CD  . ARG D  1 69  ? -10.124 92.587  63.690  1.00 27.47 ? 69   ARG D CD  1 
ATOM   3827  N  NE  . ARG D  1 69  ? -11.023 93.476  64.444  1.00 29.79 ? 69   ARG D NE  1 
ATOM   3828  C  CZ  . ARG D  1 69  ? -12.349 93.358  64.492  1.00 33.91 ? 69   ARG D CZ  1 
ATOM   3829  N  NH1 . ARG D  1 69  ? -12.958 92.373  63.842  1.00 35.82 ? 69   ARG D NH1 1 
ATOM   3830  N  NH2 . ARG D  1 69  ? -13.075 94.220  65.199  1.00 35.04 ? 69   ARG D NH2 1 
ATOM   3831  N  N   . LYS D  1 70  ? -6.008  89.805  62.263  1.00 17.41 ? 70   LYS D N   1 
ATOM   3832  C  CA  . LYS D  1 70  ? -4.619  89.570  61.882  1.00 16.45 ? 70   LYS D CA  1 
ATOM   3833  C  C   . LYS D  1 70  ? -3.701  90.553  62.624  1.00 15.36 ? 70   LYS D C   1 
ATOM   3834  O  O   . LYS D  1 70  ? -4.167  91.547  63.167  1.00 15.34 ? 70   LYS D O   1 
ATOM   3835  C  CB  . LYS D  1 70  ? -4.432  89.630  60.356  1.00 17.12 ? 70   LYS D CB  1 
ATOM   3836  C  CG  . LYS D  1 70  ? -5.231  88.551  59.609  1.00 17.16 ? 70   LYS D CG  1 
ATOM   3837  N  N   . HIS D  1 71  ? -2.408  90.251  62.679  1.00 14.51 ? 71   HIS D N   1 
ATOM   3838  C  CA  . HIS D  1 71  ? -1.449  91.122  63.360  1.00 13.69 ? 71   HIS D CA  1 
ATOM   3839  C  C   . HIS D  1 71  ? -1.307  92.510  62.756  1.00 14.48 ? 71   HIS D C   1 
ATOM   3840  O  O   . HIS D  1 71  ? -1.372  92.687  61.518  1.00 12.67 ? 71   HIS D O   1 
ATOM   3841  C  CB  . HIS D  1 71  ? -0.075  90.429  63.466  1.00 13.85 ? 71   HIS D CB  1 
ATOM   3842  C  CG  . HIS D  1 71  ? 0.959   91.218  64.210  1.00 14.61 ? 71   HIS D CG  1 
ATOM   3843  N  ND1 . HIS D  1 71  ? 1.053   91.240  65.593  1.00 11.79 ? 71   HIS D ND1 1 
ATOM   3844  C  CD2 . HIS D  1 71  ? 1.952   92.017  63.750  1.00 13.96 ? 71   HIS D CD2 1 
ATOM   3845  C  CE1 . HIS D  1 71  ? 2.070   92.011  65.941  1.00 10.95 ? 71   HIS D CE1 1 
ATOM   3846  N  NE2 . HIS D  1 71  ? 2.623   92.501  64.842  1.00 15.07 ? 71   HIS D NE2 1 
ATOM   3847  N  N   . GLY D  1 72  ? -1.131  93.516  63.613  1.00 13.35 ? 72   GLY D N   1 
ATOM   3848  C  CA  . GLY D  1 72  ? -0.927  94.864  63.115  1.00 13.97 ? 72   GLY D CA  1 
ATOM   3849  C  C   . GLY D  1 72  ? -0.209  95.711  64.132  1.00 14.33 ? 72   GLY D C   1 
ATOM   3850  O  O   . GLY D  1 72  ? 0.260   95.187  65.147  1.00 13.02 ? 72   GLY D O   1 
ATOM   3851  N  N   . GLY D  1 73  ? -0.104  97.010  63.858  1.00 14.12 ? 73   GLY D N   1 
ATOM   3852  C  CA  . GLY D  1 73  ? 0.426   97.944  64.838  1.00 14.85 ? 73   GLY D CA  1 
ATOM   3853  C  C   . GLY D  1 73  ? -0.710  98.405  65.742  1.00 14.43 ? 73   GLY D C   1 
ATOM   3854  O  O   . GLY D  1 73  ? -1.888  98.212  65.418  1.00 14.64 ? 73   GLY D O   1 
ATOM   3855  N  N   . PRO D  1 74  ? -0.380  98.988  66.877  1.00 15.34 ? 74   PRO D N   1 
ATOM   3856  C  CA  . PRO D  1 74  ? -1.412  99.480  67.802  1.00 15.85 ? 74   PRO D CA  1 
ATOM   3857  C  C   . PRO D  1 74  ? -2.364  100.502 67.176  1.00 16.73 ? 74   PRO D C   1 
ATOM   3858  O  O   . PRO D  1 74  ? -3.485  100.648 67.651  1.00 15.46 ? 74   PRO D O   1 
ATOM   3859  C  CB  . PRO D  1 74  ? -0.596  100.081 68.961  1.00 16.06 ? 74   PRO D CB  1 
ATOM   3860  C  CG  . PRO D  1 74  ? 0.784   100.287 68.385  1.00 16.30 ? 74   PRO D CG  1 
ATOM   3861  C  CD  . PRO D  1 74  ? 0.974   99.156  67.432  1.00 14.71 ? 74   PRO D CD  1 
ATOM   3862  N  N   . LYS D  1 75  ? -1.948  101.179 66.105  1.00 18.05 ? 75   LYS D N   1 
ATOM   3863  C  CA  . LYS D  1 75  ? -2.839  102.155 65.455  1.00 19.34 ? 75   LYS D CA  1 
ATOM   3864  C  C   . LYS D  1 75  ? -3.846  101.581 64.431  1.00 19.93 ? 75   LYS D C   1 
ATOM   3865  O  O   . LYS D  1 75  ? -4.764  102.288 63.993  1.00 19.14 ? 75   LYS D O   1 
ATOM   3866  C  CB  . LYS D  1 75  ? -2.019  103.256 64.776  1.00 20.66 ? 75   LYS D CB  1 
ATOM   3867  C  CG  . LYS D  1 75  ? -1.437  104.288 65.730  1.00 23.08 ? 75   LYS D CG  1 
ATOM   3868  C  CD  . LYS D  1 75  ? -0.074  103.896 66.229  1.00 29.34 ? 75   LYS D CD  1 
ATOM   3869  C  CE  . LYS D  1 75  ? 0.221   104.577 67.563  1.00 32.99 ? 75   LYS D CE  1 
ATOM   3870  N  NZ  . LYS D  1 75  ? 1.328   103.923 68.339  1.00 31.78 ? 75   LYS D NZ  1 
ATOM   3871  N  N   . ASP D  1 76  ? -3.688  100.312 64.051  1.00 20.32 ? 76   ASP D N   1 
ATOM   3872  C  CA  . ASP D  1 76  ? -4.538  99.705  63.025  1.00 20.50 ? 76   ASP D CA  1 
ATOM   3873  C  C   . ASP D  1 76  ? -5.849  99.151  63.563  1.00 20.66 ? 76   ASP D C   1 
ATOM   3874  O  O   . ASP D  1 76  ? -5.892  98.585  64.658  1.00 20.18 ? 76   ASP D O   1 
ATOM   3875  C  CB  . ASP D  1 76  ? -3.813  98.548  62.331  1.00 20.13 ? 76   ASP D CB  1 
ATOM   3876  C  CG  . ASP D  1 76  ? -2.450  98.942  61.780  1.00 22.50 ? 76   ASP D CG  1 
ATOM   3877  O  OD1 . ASP D  1 76  ? -2.267  100.121 61.410  1.00 23.91 ? 76   ASP D OD1 1 
ATOM   3878  O  OD2 . ASP D  1 76  ? -1.512  98.120  61.646  1.00 23.04 ? 76   ASP D OD2 1 
ATOM   3879  N  N   . GLU D  1 77  ? -6.901  99.276  62.752  1.00 20.58 ? 77   GLU D N   1 
ATOM   3880  C  CA  . GLU D  1 77  ? -8.203  98.702  63.083  1.00 20.99 ? 77   GLU D CA  1 
ATOM   3881  C  C   . GLU D  1 77  ? -8.005  97.193  63.068  1.00 19.85 ? 77   GLU D C   1 
ATOM   3882  O  O   . GLU D  1 77  ? -8.496  96.478  63.958  1.00 21.45 ? 77   GLU D O   1 
ATOM   3883  C  CB  . GLU D  1 77  ? -9.268  99.156  62.056  1.00 22.05 ? 77   GLU D CB  1 
ATOM   3884  C  CG  . GLU D  1 77  ? -10.726 99.148  62.525  1.00 26.83 ? 77   GLU D CG  1 
ATOM   3885  C  CD  . GLU D  1 77  ? -11.056 100.208 63.588  1.00 33.20 ? 77   GLU D CD  1 
ATOM   3886  O  OE1 . GLU D  1 77  ? -10.315 101.217 63.715  1.00 35.60 ? 77   GLU D OE1 1 
ATOM   3887  O  OE2 . GLU D  1 77  ? -12.070 100.030 64.312  1.00 35.76 ? 77   GLU D OE2 1 
ATOM   3888  N  N   . GLU D  1 78  ? -7.251  96.710  62.079  1.00 18.53 ? 78   GLU D N   1 
ATOM   3889  C  CA  . GLU D  1 78  ? -6.905  95.300  62.023  1.00 17.32 ? 78   GLU D CA  1 
ATOM   3890  C  C   . GLU D  1 78  ? -5.631  95.068  62.885  1.00 15.94 ? 78   GLU D C   1 
ATOM   3891  O  O   . GLU D  1 78  ? -4.526  95.342  62.459  1.00 14.38 ? 78   GLU D O   1 
ATOM   3892  C  CB  . GLU D  1 78  ? -6.684  94.854  60.559  1.00 17.38 ? 78   GLU D CB  1 
ATOM   3893  C  CG  . GLU D  1 78  ? -6.494  93.350  60.364  1.00 19.64 ? 78   GLU D CG  1 
ATOM   3894  C  CD  . GLU D  1 78  ? -7.775  92.513  60.509  1.00 23.32 ? 78   GLU D CD  1 
ATOM   3895  O  OE1 . GLU D  1 78  ? -8.899  93.081  60.560  1.00 26.46 ? 78   GLU D OE1 1 
ATOM   3896  O  OE2 . GLU D  1 78  ? -7.660  91.261  60.558  1.00 22.10 ? 78   GLU D OE2 1 
ATOM   3897  N  N   . ARG D  1 79  ? -5.815  94.630  64.129  1.00 14.89 ? 79   ARG D N   1 
ATOM   3898  C  CA  . ARG D  1 79  ? -4.671  94.269  65.008  1.00 14.03 ? 79   ARG D CA  1 
ATOM   3899  C  C   . ARG D  1 79  ? -5.164  93.263  66.010  1.00 12.17 ? 79   ARG D C   1 
ATOM   3900  O  O   . ARG D  1 79  ? -6.374  93.095  66.195  1.00 12.10 ? 79   ARG D O   1 
ATOM   3901  C  CB  . ARG D  1 79  ? -4.139  95.479  65.777  1.00 14.46 ? 79   ARG D CB  1 
ATOM   3902  C  CG  . ARG D  1 79  ? -5.115  95.985  66.814  1.00 14.29 ? 79   ARG D CG  1 
ATOM   3903  C  CD  . ARG D  1 79  ? -4.599  95.793  68.287  1.00 19.19 ? 79   ARG D CD  1 
ATOM   3904  N  NE  . ARG D  1 79  ? -4.373  97.140  68.705  1.00 18.40 ? 79   ARG D NE  1 
ATOM   3905  C  CZ  . ARG D  1 79  ? -4.134  97.602  69.887  1.00 15.36 ? 79   ARG D CZ  1 
ATOM   3906  N  NH1 . ARG D  1 79  ? -3.958  96.828  70.967  1.00 11.73 ? 79   ARG D NH1 1 
ATOM   3907  N  NH2 . ARG D  1 79  ? -4.032  98.922  69.948  1.00 13.80 ? 79   ARG D NH2 1 
ATOM   3908  N  N   . HIS D  1 80  ? -4.248  92.550  66.647  1.00 12.32 ? 80   HIS D N   1 
ATOM   3909  C  CA  . HIS D  1 80  ? -4.646  91.706  67.781  1.00 11.00 ? 80   HIS D CA  1 
ATOM   3910  C  C   . HIS D  1 80  ? -4.811  92.652  68.985  1.00 9.76  ? 80   HIS D C   1 
ATOM   3911  O  O   . HIS D  1 80  ? -4.128  93.653  69.054  1.00 8.64  ? 80   HIS D O   1 
ATOM   3912  C  CB  . HIS D  1 80  ? -3.515  90.722  68.090  1.00 11.55 ? 80   HIS D CB  1 
ATOM   3913  C  CG  . HIS D  1 80  ? -3.152  89.829  66.953  1.00 11.35 ? 80   HIS D CG  1 
ATOM   3914  N  ND1 . HIS D  1 80  ? -1.844  89.473  66.674  1.00 10.54 ? 80   HIS D ND1 1 
ATOM   3915  C  CD2 . HIS D  1 80  ? -3.928  89.181  66.050  1.00 10.56 ? 80   HIS D CD2 1 
ATOM   3916  C  CE1 . HIS D  1 80  ? -1.839  88.622  65.661  1.00 14.18 ? 80   HIS D CE1 1 
ATOM   3917  N  NE2 . HIS D  1 80  ? -3.085  88.445  65.252  1.00 14.04 ? 80   HIS D NE2 1 
ATOM   3918  N  N   . VAL D  1 81  ? -5.713  92.364  69.926  1.00 9.96  ? 81   VAL D N   1 
ATOM   3919  C  CA  . VAL D  1 81  ? -5.796  93.191  71.126  1.00 9.34  ? 81   VAL D CA  1 
ATOM   3920  C  C   . VAL D  1 81  ? -4.412  93.347  71.746  1.00 8.45  ? 81   VAL D C   1 
ATOM   3921  O  O   . VAL D  1 81  ? -4.077  94.406  72.241  1.00 7.98  ? 81   VAL D O   1 
ATOM   3922  C  CB  . VAL D  1 81  ? -6.746  92.558  72.168  1.00 9.73  ? 81   VAL D CB  1 
ATOM   3923  C  CG1 . VAL D  1 81  ? -6.648  93.319  73.557  1.00 10.42 ? 81   VAL D CG1 1 
ATOM   3924  C  CG2 . VAL D  1 81  ? -8.149  92.546  71.634  1.00 10.49 ? 81   VAL D CG2 1 
ATOM   3925  N  N   . GLY D  1 82  ? -3.599  92.291  71.714  1.00 8.20  ? 82   GLY D N   1 
ATOM   3926  C  CA  . GLY D  1 82  ? -2.281  92.336  72.370  1.00 9.15  ? 82   GLY D CA  1 
ATOM   3927  C  C   . GLY D  1 82  ? -1.185  93.097  71.611  1.00 9.85  ? 82   GLY D C   1 
ATOM   3928  O  O   . GLY D  1 82  ? -0.022  93.183  72.056  1.00 9.61  ? 82   GLY D O   1 
ATOM   3929  N  N   . ASP D  1 83  ? -1.534  93.688  70.478  1.00 10.45 ? 83   ASP D N   1 
ATOM   3930  C  CA  . ASP D  1 83  ? -0.499  94.338  69.668  1.00 11.20 ? 83   ASP D CA  1 
ATOM   3931  C  C   . ASP D  1 83  ? -0.111  95.743  70.161  1.00 11.35 ? 83   ASP D C   1 
ATOM   3932  O  O   . ASP D  1 83  ? -0.752  96.749  69.788  1.00 12.04 ? 83   ASP D O   1 
ATOM   3933  C  CB  . ASP D  1 83  ? -0.920  94.369  68.192  1.00 11.83 ? 83   ASP D CB  1 
ATOM   3934  C  CG  . ASP D  1 83  ? -0.979  92.998  67.557  1.00 12.41 ? 83   ASP D CG  1 
ATOM   3935  O  OD1 . ASP D  1 83  ? -0.340  92.042  68.053  1.00 9.43  ? 83   ASP D OD1 1 
ATOM   3936  O  OD2 . ASP D  1 83  ? -1.590  92.800  66.492  1.00 13.47 ? 83   ASP D OD2 1 
ATOM   3937  N  N   . LEU D  1 84  ? 0.942   95.841  70.981  1.00 9.20  ? 84   LEU D N   1 
ATOM   3938  C  CA  . LEU D  1 84  ? 1.329   97.140  71.501  1.00 9.88  ? 84   LEU D CA  1 
ATOM   3939  C  C   . LEU D  1 84  ? 2.500   97.746  70.717  1.00 10.42 ? 84   LEU D C   1 
ATOM   3940  O  O   . LEU D  1 84  ? 3.078   98.747  71.115  1.00 11.08 ? 84   LEU D O   1 
ATOM   3941  C  CB  . LEU D  1 84  ? 1.596   97.104  73.005  1.00 9.63  ? 84   LEU D CB  1 
ATOM   3942  C  CG  . LEU D  1 84  ? 0.361   96.741  73.829  1.00 10.00 ? 84   LEU D CG  1 
ATOM   3943  C  CD1 . LEU D  1 84  ? 0.758   96.635  75.324  1.00 11.41 ? 84   LEU D CD1 1 
ATOM   3944  C  CD2 . LEU D  1 84  ? -0.718  97.824  73.622  1.00 12.21 ? 84   LEU D CD2 1 
ATOM   3945  N  N   . GLY D  1 85  ? 2.831   97.123  69.600  1.00 10.66 ? 85   GLY D N   1 
ATOM   3946  C  CA  . GLY D  1 85  ? 3.870   97.654  68.723  1.00 9.98  ? 85   GLY D CA  1 
ATOM   3947  C  C   . GLY D  1 85  ? 5.289   97.363  69.134  1.00 10.15 ? 85   GLY D C   1 
ATOM   3948  O  O   . GLY D  1 85  ? 5.635   96.221  69.452  1.00 11.83 ? 85   GLY D O   1 
ATOM   3949  N  N   . ASN D  1 86  ? 6.133   98.400  69.054  1.00 10.87 ? 86   ASN D N   1 
ATOM   3950  C  CA  . ASN D  1 86  ? 7.529   98.327  69.443  1.00 10.57 ? 86   ASN D CA  1 
ATOM   3951  C  C   . ASN D  1 86  ? 7.867   99.228  70.621  1.00 10.38 ? 86   ASN D C   1 
ATOM   3952  O  O   . ASN D  1 86  ? 7.206   100.248 70.852  1.00 10.65 ? 86   ASN D O   1 
ATOM   3953  C  CB  . ASN D  1 86  ? 8.424   98.788  68.276  1.00 11.06 ? 86   ASN D CB  1 
ATOM   3954  C  CG  . ASN D  1 86  ? 8.455   97.769  67.160  1.00 12.08 ? 86   ASN D CG  1 
ATOM   3955  O  OD1 . ASN D  1 86  ? 8.889   96.645  67.372  1.00 11.96 ? 86   ASN D OD1 1 
ATOM   3956  N  ND2 . ASN D  1 86  ? 7.975   98.148  65.980  1.00 11.40 ? 86   ASN D ND2 1 
ATOM   3957  N  N   . VAL D  1 87  ? 8.902   98.826  71.354  1.00 9.90  ? 87   VAL D N   1 
ATOM   3958  C  CA  . VAL D  1 87  ? 9.552   99.729  72.280  1.00 10.00 ? 87   VAL D CA  1 
ATOM   3959  C  C   . VAL D  1 87  ? 10.952  99.957  71.691  1.00 10.81 ? 87   VAL D C   1 
ATOM   3960  O  O   . VAL D  1 87  ? 11.491  99.118  70.944  1.00 11.69 ? 87   VAL D O   1 
ATOM   3961  C  CB  . VAL D  1 87  ? 9.604   99.190  73.730  1.00 9.46  ? 87   VAL D CB  1 
ATOM   3962  C  CG1 . VAL D  1 87  ? 8.178   99.072  74.247  1.00 9.97  ? 87   VAL D CG1 1 
ATOM   3963  C  CG2 . VAL D  1 87  ? 10.297  97.825  73.759  1.00 11.05 ? 87   VAL D CG2 1 
ATOM   3964  N  N   . THR D  1 88  ? 11.515  101.116 72.005  1.00 10.49 ? 88   THR D N   1 
ATOM   3965  C  CA  . THR D  1 88  ? 12.791  101.500 71.472  1.00 11.56 ? 88   THR D CA  1 
ATOM   3966  C  C   . THR D  1 88  ? 13.807  101.524 72.565  1.00 11.71 ? 88   THR D C   1 
ATOM   3967  O  O   . THR D  1 88  ? 13.626  102.220 73.575  1.00 12.41 ? 88   THR D O   1 
ATOM   3968  C  CB  . THR D  1 88  ? 12.672  102.904 70.886  1.00 11.16 ? 88   THR D CB  1 
ATOM   3969  O  OG1 . THR D  1 88  ? 11.740  102.859 69.801  1.00 11.11 ? 88   THR D OG1 1 
ATOM   3970  C  CG2 . THR D  1 88  ? 14.015  103.352 70.243  1.00 13.85 ? 88   THR D CG2 1 
ATOM   3971  N  N   . ALA D  1 89  ? 14.865  100.748 72.386  1.00 11.72 ? 89   ALA D N   1 
ATOM   3972  C  CA  . ALA D  1 89  ? 15.952  100.722 73.348  1.00 12.15 ? 89   ALA D CA  1 
ATOM   3973  C  C   . ALA D  1 89  ? 16.994  101.725 72.881  1.00 14.06 ? 89   ALA D C   1 
ATOM   3974  O  O   . ALA D  1 89  ? 17.338  101.751 71.693  1.00 12.73 ? 89   ALA D O   1 
ATOM   3975  C  CB  . ALA D  1 89  ? 16.556  99.340  73.429  1.00 12.10 ? 89   ALA D CB  1 
ATOM   3976  N  N   . ASP D  1 90  ? 17.481  102.536 73.817  1.00 14.80 ? 90   ASP D N   1 
ATOM   3977  C  CA  . ASP D  1 90  ? 18.470  103.559 73.495  1.00 16.65 ? 90   ASP D CA  1 
ATOM   3978  C  C   . ASP D  1 90  ? 19.856  102.947 73.395  1.00 17.28 ? 90   ASP D C   1 
ATOM   3979  O  O   . ASP D  1 90  ? 20.025  101.740 73.547  1.00 17.63 ? 90   ASP D O   1 
ATOM   3980  C  CB  . ASP D  1 90  ? 18.445  104.726 74.496  1.00 16.00 ? 90   ASP D CB  1 
ATOM   3981  C  CG  . ASP D  1 90  ? 18.865  104.327 75.910  1.00 16.06 ? 90   ASP D CG  1 
ATOM   3982  O  OD1 . ASP D  1 90  ? 19.567  103.309 76.097  1.00 14.46 ? 90   ASP D OD1 1 
ATOM   3983  O  OD2 . ASP D  1 90  ? 18.539  105.009 76.914  1.00 16.71 ? 90   ASP D OD2 1 
ATOM   3984  N  N   . LYS D  1 91  ? 20.844  103.795 73.154  1.00 18.77 ? 91   LYS D N   1 
ATOM   3985  C  CA  . LYS D  1 91  ? 22.217  103.351 72.957  1.00 19.45 ? 91   LYS D CA  1 
ATOM   3986  C  C   . LYS D  1 91  ? 22.763  102.473 74.099  1.00 19.15 ? 91   LYS D C   1 
ATOM   3987  O  O   . LYS D  1 91  ? 23.645  101.628 73.876  1.00 19.48 ? 91   LYS D O   1 
ATOM   3988  C  CB  . LYS D  1 91  ? 23.118  104.573 72.703  1.00 19.98 ? 91   LYS D CB  1 
ATOM   3989  C  CG  . LYS D  1 91  ? 23.695  105.234 73.967  1.00 22.39 ? 91   LYS D CG  1 
ATOM   3990  C  CD  . LYS D  1 91  ? 25.236  105.130 73.982  1.00 27.20 ? 91   LYS D CD  1 
ATOM   3991  C  CE  . LYS D  1 91  ? 25.878  105.359 75.364  1.00 29.31 ? 91   LYS D CE  1 
ATOM   3992  N  NZ  . LYS D  1 91  ? 25.305  106.492 76.165  1.00 31.08 ? 91   LYS D NZ  1 
ATOM   3993  N  N   . ASP D  1 92  ? 22.245  102.676 75.305  1.00 18.30 ? 92   ASP D N   1 
ATOM   3994  C  CA  . ASP D  1 92  ? 22.653  101.897 76.474  1.00 18.70 ? 92   ASP D CA  1 
ATOM   3995  C  C   . ASP D  1 92  ? 21.808  100.639 76.708  1.00 17.89 ? 92   ASP D C   1 
ATOM   3996  O  O   . ASP D  1 92  ? 21.981  99.965  77.725  1.00 18.00 ? 92   ASP D O   1 
ATOM   3997  C  CB  . ASP D  1 92  ? 22.617  102.760 77.739  1.00 19.29 ? 92   ASP D CB  1 
ATOM   3998  C  CG  . ASP D  1 92  ? 23.583  103.919 77.671  1.00 21.81 ? 92   ASP D CG  1 
ATOM   3999  O  OD1 . ASP D  1 92  ? 24.746  103.703 77.238  1.00 22.87 ? 92   ASP D OD1 1 
ATOM   4000  O  OD2 . ASP D  1 92  ? 23.257  105.080 78.009  1.00 23.76 ? 92   ASP D OD2 1 
ATOM   4001  N  N   . GLY D  1 93  ? 20.907  100.335 75.776  1.00 17.05 ? 93   GLY D N   1 
ATOM   4002  C  CA  . GLY D  1 93  ? 20.110  99.118  75.841  1.00 15.41 ? 93   GLY D CA  1 
ATOM   4003  C  C   . GLY D  1 93  ? 18.905  99.220  76.749  1.00 15.02 ? 93   GLY D C   1 
ATOM   4004  O  O   . GLY D  1 93  ? 18.269  98.190  77.085  1.00 14.54 ? 93   GLY D O   1 
ATOM   4005  N  N   . VAL D  1 94  ? 18.593  100.444 77.159  1.00 13.65 ? 94   VAL D N   1 
ATOM   4006  C  CA  . VAL D  1 94  ? 17.447  100.693 78.020  1.00 13.45 ? 94   VAL D CA  1 
ATOM   4007  C  C   . VAL D  1 94  ? 16.266  101.230 77.230  1.00 12.79 ? 94   VAL D C   1 
ATOM   4008  O  O   . VAL D  1 94  ? 16.384  102.221 76.475  1.00 11.81 ? 94   VAL D O   1 
ATOM   4009  C  CB  . VAL D  1 94  ? 17.762  101.739 79.111  1.00 13.61 ? 94   VAL D CB  1 
ATOM   4010  C  CG1 . VAL D  1 94  ? 16.481  102.193 79.810  1.00 13.36 ? 94   VAL D CG1 1 
ATOM   4011  C  CG2 . VAL D  1 94  ? 18.745  101.195 80.111  1.00 13.93 ? 94   VAL D CG2 1 
ATOM   4012  N  N   . ALA D  1 95  ? 15.121  100.577 77.406  1.00 11.69 ? 95   ALA D N   1 
ATOM   4013  C  CA  . ALA D  1 95  ? 13.901  101.056 76.803  1.00 11.52 ? 95   ALA D CA  1 
ATOM   4014  C  C   . ALA D  1 95  ? 13.025  101.657 77.896  1.00 11.95 ? 95   ALA D C   1 
ATOM   4015  O  O   . ALA D  1 95  ? 12.589  100.947 78.819  1.00 11.15 ? 95   ALA D O   1 
ATOM   4016  C  CB  . ALA D  1 95  ? 13.173  99.908  76.082  1.00 11.12 ? 95   ALA D CB  1 
ATOM   4017  N  N   . ASP D  1 96  ? 12.814  102.971 77.803  1.00 11.80 ? 96   ASP D N   1 
ATOM   4018  C  CA  . ASP D  1 96  ? 11.918  103.696 78.681  1.00 12.16 ? 96   ASP D CA  1 
ATOM   4019  C  C   . ASP D  1 96  ? 10.554  103.713 78.047  1.00 11.72 ? 96   ASP D C   1 
ATOM   4020  O  O   . ASP D  1 96  ? 10.211  104.587 77.243  1.00 12.85 ? 96   ASP D O   1 
ATOM   4021  C  CB  . ASP D  1 96  ? 12.440  105.102 78.910  1.00 13.27 ? 96   ASP D CB  1 
ATOM   4022  C  CG  . ASP D  1 96  ? 13.655  105.102 79.797  1.00 15.48 ? 96   ASP D CG  1 
ATOM   4023  O  OD1 . ASP D  1 96  ? 14.602  105.851 79.496  1.00 20.00 ? 96   ASP D OD1 1 
ATOM   4024  O  OD2 . ASP D  1 96  ? 13.735  104.370 80.816  1.00 19.28 ? 96   ASP D OD2 1 
ATOM   4025  N  N   . VAL D  1 97  ? 9.748   102.726 78.413  1.00 10.11 ? 97   VAL D N   1 
ATOM   4026  C  CA  . VAL D  1 97  ? 8.500   102.501 77.726  1.00 9.41  ? 97   VAL D CA  1 
ATOM   4027  C  C   . VAL D  1 97  ? 7.462   103.512 78.129  1.00 9.03  ? 97   VAL D C   1 
ATOM   4028  O  O   . VAL D  1 97  ? 7.346   103.831 79.312  1.00 8.90  ? 97   VAL D O   1 
ATOM   4029  C  CB  . VAL D  1 97  ? 8.003   101.109 78.103  1.00 8.60  ? 97   VAL D CB  1 
ATOM   4030  C  CG1 . VAL D  1 97  ? 6.663   100.797 77.431  1.00 9.87  ? 97   VAL D CG1 1 
ATOM   4031  C  CG2 . VAL D  1 97  ? 9.092   100.100 77.771  1.00 9.87  ? 97   VAL D CG2 1 
ATOM   4032  N  N   . SER D  1 98  ? 6.698   104.000 77.161  1.00 10.55 ? 98   SER D N   1 
ATOM   4033  C  CA  . SER D  1 98  ? 5.605   104.917 77.434  1.00 12.37 ? 98   SER D CA  1 
ATOM   4034  C  C   . SER D  1 98  ? 4.606   104.794 76.295  1.00 13.43 ? 98   SER D C   1 
ATOM   4035  O  O   . SER D  1 98  ? 4.844   105.256 75.168  1.00 12.93 ? 98   SER D O   1 
ATOM   4036  C  CB  . SER D  1 98  ? 6.087   106.355 77.543  1.00 14.27 ? 98   SER D CB  1 
ATOM   4037  O  OG  . SER D  1 98  ? 5.060   107.142 78.131  1.00 16.16 ? 98   SER D OG  1 
ATOM   4038  N  N   . ILE D  1 99  ? 3.491   104.149 76.576  1.00 12.22 ? 99   ILE D N   1 
ATOM   4039  C  CA  . ILE D  1 99  ? 2.517   103.820 75.551  1.00 12.98 ? 99   ILE D CA  1 
ATOM   4040  C  C   . ILE D  1 99  ? 1.149   104.084 76.179  1.00 13.78 ? 99   ILE D C   1 
ATOM   4041  O  O   . ILE D  1 99  ? 0.986   103.921 77.396  1.00 12.87 ? 99   ILE D O   1 
ATOM   4042  C  CB  . ILE D  1 99  ? 2.654   102.308 75.214  1.00 13.98 ? 99   ILE D CB  1 
ATOM   4043  C  CG1 . ILE D  1 99  ? 3.857   102.043 74.300  1.00 14.69 ? 99   ILE D CG1 1 
ATOM   4044  C  CG2 . ILE D  1 99  ? 1.403   101.756 74.521  1.00 15.16 ? 99   ILE D CG2 1 
ATOM   4045  C  CD1 . ILE D  1 99  ? 4.171   100.554 74.095  1.00 13.78 ? 99   ILE D CD1 1 
ATOM   4046  N  N   . GLU D  1 100 ? 0.186   104.517 75.374  1.00 12.61 ? 100  GLU D N   1 
ATOM   4047  C  CA  . GLU D  1 100 ? -1.183  104.588 75.861  1.00 13.47 ? 100  GLU D CA  1 
ATOM   4048  C  C   . GLU D  1 100 ? -2.001  103.803 74.848  1.00 12.61 ? 100  GLU D C   1 
ATOM   4049  O  O   . GLU D  1 100 ? -1.808  103.975 73.633  1.00 11.62 ? 100  GLU D O   1 
ATOM   4050  C  CB  . GLU D  1 100 ? -1.652  106.035 76.024  1.00 13.58 ? 100  GLU D CB  1 
ATOM   4051  C  CG  . GLU D  1 100 ? -3.087  106.152 76.505  1.00 18.39 ? 100  GLU D CG  1 
ATOM   4052  C  CD  . GLU D  1 100 ? -3.595  107.577 76.380  1.00 25.13 ? 100  GLU D CD  1 
ATOM   4053  O  OE1 . GLU D  1 100 ? -3.147  108.405 77.211  1.00 25.61 ? 100  GLU D OE1 1 
ATOM   4054  O  OE2 . GLU D  1 100 ? -4.403  107.865 75.435  1.00 24.55 ? 100  GLU D OE2 1 
ATOM   4055  N  N   . ASP D  1 101 ? -2.908  102.950 75.323  1.00 11.84 ? 101  ASP D N   1 
ATOM   4056  C  CA  . ASP D  1 101 ? -3.680  102.131 74.422  1.00 11.86 ? 101  ASP D CA  1 
ATOM   4057  C  C   . ASP D  1 101 ? -5.093  101.925 74.920  1.00 12.75 ? 101  ASP D C   1 
ATOM   4058  O  O   . ASP D  1 101 ? -5.291  101.586 76.079  1.00 11.12 ? 101  ASP D O   1 
ATOM   4059  C  CB  . ASP D  1 101 ? -2.985  100.792 74.237  1.00 12.25 ? 101  ASP D CB  1 
ATOM   4060  C  CG  . ASP D  1 101 ? -3.547  100.017 73.122  1.00 11.77 ? 101  ASP D CG  1 
ATOM   4061  O  OD1 . ASP D  1 101 ? -3.244  100.339 71.942  1.00 14.65 ? 101  ASP D OD1 1 
ATOM   4062  O  OD2 . ASP D  1 101 ? -4.373  99.100  73.294  1.00 12.64 ? 101  ASP D OD2 1 
ATOM   4063  N  N   . SER D  1 102 ? -6.059  102.049 74.017  1.00 12.93 ? 102  SER D N   1 
ATOM   4064  C  CA  . SER D  1 102 ? -7.452  101.910 74.407  1.00 14.15 ? 102  SER D CA  1 
ATOM   4065  C  C   . SER D  1 102 ? -8.090  100.629 73.912  1.00 12.81 ? 102  SER D C   1 
ATOM   4066  O  O   . SER D  1 102 ? -9.291  100.398 74.122  1.00 14.72 ? 102  SER D O   1 
ATOM   4067  C  CB  . SER D  1 102 ? -8.236  103.131 73.942  1.00 16.15 ? 102  SER D CB  1 
ATOM   4068  O  OG  . SER D  1 102 ? -7.849  104.276 74.686  1.00 20.55 ? 102  SER D OG  1 
ATOM   4069  N  N   . VAL D  1 103 ? -7.312  99.779  73.256  1.00 11.30 ? 103  VAL D N   1 
ATOM   4070  C  CA  . VAL D  1 103 ? -7.853  98.506  72.838  1.00 9.85  ? 103  VAL D CA  1 
ATOM   4071  C  C   . VAL D  1 103 ? -7.671  97.501  73.996  1.00 9.78  ? 103  VAL D C   1 
ATOM   4072  O  O   . VAL D  1 103 ? -8.618  96.793  74.336  1.00 9.70  ? 103  VAL D O   1 
ATOM   4073  C  CB  . VAL D  1 103 ? -7.265  97.998  71.526  1.00 10.41 ? 103  VAL D CB  1 
ATOM   4074  C  CG1 . VAL D  1 103 ? -7.689  96.549  71.317  1.00 12.43 ? 103  VAL D CG1 1 
ATOM   4075  C  CG2 . VAL D  1 103 ? -7.780  98.903  70.356  1.00 10.08 ? 103  VAL D CG2 1 
ATOM   4076  N  N   . ILE D  1 104 ? -6.489  97.428  74.592  1.00 9.55  ? 104  ILE D N   1 
ATOM   4077  C  CA  . ILE D  1 104 ? -6.349  96.557  75.785  1.00 8.67  ? 104  ILE D CA  1 
ATOM   4078  C  C   . ILE D  1 104 ? -7.114  97.230  76.909  1.00 8.73  ? 104  ILE D C   1 
ATOM   4079  O  O   . ILE D  1 104 ? -7.442  98.410  76.813  1.00 8.62  ? 104  ILE D O   1 
ATOM   4080  C  CB  . ILE D  1 104 ? -4.876  96.453  76.251  1.00 9.69  ? 104  ILE D CB  1 
ATOM   4081  C  CG1 . ILE D  1 104 ? -4.316  97.861  76.563  1.00 8.28  ? 104  ILE D CG1 1 
ATOM   4082  C  CG2 . ILE D  1 104 ? -4.074  95.648  75.248  1.00 9.10  ? 104  ILE D CG2 1 
ATOM   4083  C  CD1 . ILE D  1 104 ? -2.976  97.908  77.308  1.00 8.90  ? 104  ILE D CD1 1 
ATOM   4084  N  N   . SER D  1 105 ? -7.402  96.483  77.978  1.00 7.02  ? 105  SER D N   1 
ATOM   4085  C  CA  . SER D  1 105 ? -8.116  97.034  79.139  1.00 7.72  ? 105  SER D CA  1 
ATOM   4086  C  C   . SER D  1 105 ? -7.654  96.272  80.388  1.00 8.05  ? 105  SER D C   1 
ATOM   4087  O  O   . SER D  1 105 ? -7.018  95.223  80.263  1.00 7.87  ? 105  SER D O   1 
ATOM   4088  C  CB  . SER D  1 105 ? -9.634  96.883  78.937  1.00 8.06  ? 105  SER D CB  1 
ATOM   4089  O  OG  . SER D  1 105 ? -10.385 97.426  80.017  1.00 8.00  ? 105  SER D OG  1 
ATOM   4090  N  N   . LEU D  1 106 ? -7.945  96.802  81.566  1.00 8.56  ? 106  LEU D N   1 
ATOM   4091  C  CA  . LEU D  1 106 ? -7.621  96.101  82.797  1.00 10.50 ? 106  LEU D CA  1 
ATOM   4092  C  C   . LEU D  1 106 ? -8.883  95.522  83.426  1.00 12.54 ? 106  LEU D C   1 
ATOM   4093  O  O   . LEU D  1 106 ? -8.853  95.087  84.597  1.00 11.86 ? 106  LEU D O   1 
ATOM   4094  C  CB  . LEU D  1 106 ? -6.909  97.014  83.810  1.00 11.10 ? 106  LEU D CB  1 
ATOM   4095  C  CG  . LEU D  1 106 ? -5.609  97.582  83.241  1.00 8.43  ? 106  LEU D CG  1 
ATOM   4096  C  CD1 . LEU D  1 106 ? -4.900  98.434  84.314  1.00 11.77 ? 106  LEU D CD1 1 
ATOM   4097  C  CD2 . LEU D  1 106 ? -4.677  96.486  82.673  1.00 10.77 ? 106  LEU D CD2 1 
ATOM   4098  N  N   . SER D  1 107 ? -9.961  95.468  82.633  1.00 14.74 ? 107  SER D N   1 
ATOM   4099  C  CA  . SER D  1 107 ? -11.217 94.811  83.053  1.00 17.93 ? 107  SER D CA  1 
ATOM   4100  C  C   . SER D  1 107 ? -12.006 94.447  81.792  1.00 18.43 ? 107  SER D C   1 
ATOM   4101  O  O   . SER D  1 107 ? -11.720 94.969  80.715  1.00 18.73 ? 107  SER D O   1 
ATOM   4102  C  CB  . SER D  1 107 ? -12.074 95.778  83.839  1.00 17.94 ? 107  SER D CB  1 
ATOM   4103  O  OG  . SER D  1 107 ? -12.836 96.488  82.874  1.00 21.93 ? 107  SER D OG  1 
ATOM   4104  N  N   . GLY D  1 108 ? -13.020 93.575  81.882  1.00 18.49 ? 108  GLY D N   1 
ATOM   4105  C  CA  . GLY D  1 108 ? -13.804 93.309  80.683  1.00 18.88 ? 108  GLY D CA  1 
ATOM   4106  C  C   . GLY D  1 108 ? -13.259 92.266  79.715  1.00 19.46 ? 108  GLY D C   1 
ATOM   4107  O  O   . GLY D  1 108 ? -12.355 91.502  80.049  1.00 18.87 ? 108  GLY D O   1 
ATOM   4108  N  N   . ASP D  1 109 ? -13.828 92.220  78.513  1.00 19.88 ? 109  ASP D N   1 
ATOM   4109  C  CA  . ASP D  1 109 ? -13.468 91.207  77.498  1.00 21.10 ? 109  ASP D CA  1 
ATOM   4110  C  C   . ASP D  1 109 ? -12.034 91.292  77.026  1.00 20.03 ? 109  ASP D C   1 
ATOM   4111  O  O   . ASP D  1 109 ? -11.408 90.270  76.695  1.00 21.62 ? 109  ASP D O   1 
ATOM   4112  C  CB  . ASP D  1 109 ? -14.301 91.389  76.234  1.00 22.06 ? 109  ASP D CB  1 
ATOM   4113  C  CG  . ASP D  1 109 ? -15.700 90.909  76.393  1.00 26.05 ? 109  ASP D CG  1 
ATOM   4114  O  OD1 . ASP D  1 109 ? -16.602 91.576  75.823  1.00 29.52 ? 109  ASP D OD1 1 
ATOM   4115  O  OD2 . ASP D  1 109 ? -15.984 89.872  77.036  1.00 29.93 ? 109  ASP D OD2 1 
ATOM   4116  N  N   . HIS D  1 110 ? -11.540 92.512  76.913  1.00 16.73 ? 110  HIS D N   1 
ATOM   4117  C  CA  . HIS D  1 110 ? -10.168 92.679  76.466  1.00 14.48 ? 110  HIS D CA  1 
ATOM   4118  C  C   . HIS D  1 110 ? -9.222  92.816  77.660  1.00 12.97 ? 110  HIS D C   1 
ATOM   4119  O  O   . HIS D  1 110 ? -8.137  93.389  77.514  1.00 10.79 ? 110  HIS D O   1 
ATOM   4120  C  CB  . HIS D  1 110 ? -10.058 93.887  75.563  1.00 14.60 ? 110  HIS D CB  1 
ATOM   4121  C  CG  . HIS D  1 110 ? -10.804 93.728  74.281  1.00 15.28 ? 110  HIS D CG  1 
ATOM   4122  N  ND1 . HIS D  1 110 ? -10.843 94.708  73.318  1.00 17.75 ? 110  HIS D ND1 1 
ATOM   4123  C  CD2 . HIS D  1 110 ? -11.562 92.705  73.815  1.00 16.27 ? 110  HIS D CD2 1 
ATOM   4124  C  CE1 . HIS D  1 110 ? -11.586 94.297  72.303  1.00 17.10 ? 110  HIS D CE1 1 
ATOM   4125  N  NE2 . HIS D  1 110 ? -12.027 93.082  72.577  1.00 18.32 ? 110  HIS D NE2 1 
ATOM   4126  N  N   . CYS D  1 111 ? -9.620  92.278  78.820  1.00 11.78 ? 111  CYS D N   1 
ATOM   4127  C  CA  . CYS D  1 111 ? -8.765  92.347  80.003  1.00 10.99 ? 111  CYS D CA  1 
ATOM   4128  C  C   . CYS D  1 111 ? -7.415  91.647  79.760  1.00 11.06 ? 111  CYS D C   1 
ATOM   4129  O  O   . CYS D  1 111 ? -7.384  90.543  79.202  1.00 10.54 ? 111  CYS D O   1 
ATOM   4130  C  CB  . CYS D  1 111 ? -9.471  91.742  81.221  1.00 13.40 ? 111  CYS D CB  1 
ATOM   4131  S  SG  . CYS D  1 111 ? -8.565  92.116  82.705  1.00 16.85 ? 111  CYS D SG  1 
ATOM   4132  N  N   . ILE D  1 112 ? -6.301  92.260  80.171  1.00 8.58  ? 112  ILE D N   1 
ATOM   4133  C  CA  . ILE D  1 112 ? -4.988  91.608  79.980  1.00 8.29  ? 112  ILE D CA  1 
ATOM   4134  C  C   . ILE D  1 112 ? -4.372  91.111  81.293  1.00 6.86  ? 112  ILE D C   1 
ATOM   4135  O  O   . ILE D  1 112 ? -3.290  90.545  81.304  1.00 7.14  ? 112  ILE D O   1 
ATOM   4136  C  CB  . ILE D  1 112 ? -4.016  92.525  79.267  1.00 8.15  ? 112  ILE D CB  1 
ATOM   4137  C  CG1 . ILE D  1 112 ? -3.751  93.778  80.097  1.00 8.78  ? 112  ILE D CG1 1 
ATOM   4138  C  CG2 . ILE D  1 112 ? -4.601  92.913  77.863  1.00 7.18  ? 112  ILE D CG2 1 
ATOM   4139  C  CD1 . ILE D  1 112 ? -2.633  94.683  79.469  1.00 9.22  ? 112  ILE D CD1 1 
ATOM   4140  N  N   . ILE D  1 113 ? -5.045  91.371  82.403  1.00 6.90  ? 113  ILE D N   1 
ATOM   4141  C  CA  . ILE D  1 113 ? -4.575  90.846  83.678  1.00 7.13  ? 113  ILE D CA  1 
ATOM   4142  C  C   . ILE D  1 113 ? -4.566  89.329  83.665  1.00 6.67  ? 113  ILE D C   1 
ATOM   4143  O  O   . ILE D  1 113 ? -5.520  88.692  83.171  1.00 8.10  ? 113  ILE D O   1 
ATOM   4144  C  CB  . ILE D  1 113 ? -5.435  91.436  84.841  1.00 7.71  ? 113  ILE D CB  1 
ATOM   4145  C  CG1 . ILE D  1 113 ? -4.966  92.902  85.041  1.00 9.63  ? 113  ILE D CG1 1 
ATOM   4146  C  CG2 . ILE D  1 113 ? -5.195  90.650  86.172  1.00 8.52  ? 113  ILE D CG2 1 
ATOM   4147  C  CD1 . ILE D  1 113 ? -5.888  93.744  85.845  1.00 13.39 ? 113  ILE D CD1 1 
ATOM   4148  N  N   . GLY D  1 114 ? -3.461  88.726  84.103  1.00 6.35  ? 114  GLY D N   1 
ATOM   4149  C  CA  . GLY D  1 114 ? -3.382  87.252  84.076  1.00 5.70  ? 114  GLY D CA  1 
ATOM   4150  C  C   . GLY D  1 114 ? -2.857  86.748  82.728  1.00 6.16  ? 114  GLY D C   1 
ATOM   4151  O  O   . GLY D  1 114 ? -2.680  85.546  82.517  1.00 6.22  ? 114  GLY D O   1 
ATOM   4152  N  N   . ARG D  1 115 ? -2.565  87.668  81.809  1.00 5.37  ? 115  ARG D N   1 
ATOM   4153  C  CA  . ARG D  1 115 ? -1.931  87.277  80.546  1.00 5.92  ? 115  ARG D CA  1 
ATOM   4154  C  C   . ARG D  1 115 ? -0.438  87.588  80.574  1.00 6.93  ? 115  ARG D C   1 
ATOM   4155  O  O   . ARG D  1 115 ? 0.045   88.025  81.598  1.00 7.31  ? 115  ARG D O   1 
ATOM   4156  C  CB  . ARG D  1 115 ? -2.650  87.937  79.367  1.00 7.04  ? 115  ARG D CB  1 
ATOM   4157  C  CG  . ARG D  1 115 ? -4.151  87.524  79.395  1.00 8.75  ? 115  ARG D CG  1 
ATOM   4158  C  CD  . ARG D  1 115 ? -4.926  87.857  78.126  1.00 10.86 ? 115  ARG D CD  1 
ATOM   4159  N  NE  . ARG D  1 115 ? -6.359  87.610  78.332  1.00 11.19 ? 115  ARG D NE  1 
ATOM   4160  C  CZ  . ARG D  1 115 ? -6.948  86.446  78.114  1.00 10.22 ? 115  ARG D CZ  1 
ATOM   4161  N  NH1 . ARG D  1 115 ? -6.255  85.408  77.657  1.00 10.91 ? 115  ARG D NH1 1 
ATOM   4162  N  NH2 . ARG D  1 115 ? -8.240  86.332  78.321  1.00 11.05 ? 115  ARG D NH2 1 
ATOM   4163  N  N   . THR D  1 116 ? 0.297   87.404  79.472  1.00 7.08  ? 116  THR D N   1 
ATOM   4164  C  CA  . THR D  1 116 ? 1.762   87.544  79.538  1.00 7.48  ? 116  THR D CA  1 
ATOM   4165  C  C   . THR D  1 116 ? 2.250   88.652  78.652  1.00 7.04  ? 116  THR D C   1 
ATOM   4166  O  O   . THR D  1 116 ? 1.888   88.692  77.500  1.00 6.59  ? 116  THR D O   1 
ATOM   4167  C  CB  . THR D  1 116 ? 2.415   86.238  79.062  1.00 8.53  ? 116  THR D CB  1 
ATOM   4168  O  OG1 . THR D  1 116 ? 2.163   85.215  80.040  1.00 6.66  ? 116  THR D OG1 1 
ATOM   4169  C  CG2 . THR D  1 116 ? 3.955   86.351  79.034  1.00 7.97  ? 116  THR D CG2 1 
ATOM   4170  N  N   . LEU D  1 117 ? 3.086   89.524  79.189  1.00 6.43  ? 117  LEU D N   1 
ATOM   4171  C  CA  . LEU D  1 117 ? 3.675   90.611  78.388  1.00 6.33  ? 117  LEU D CA  1 
ATOM   4172  C  C   . LEU D  1 117 ? 4.998   90.072  77.925  1.00 6.81  ? 117  LEU D C   1 
ATOM   4173  O  O   . LEU D  1 117 ? 5.713   89.418  78.698  1.00 6.62  ? 117  LEU D O   1 
ATOM   4174  C  CB  . LEU D  1 117 ? 3.851   91.862  79.269  1.00 6.92  ? 117  LEU D CB  1 
ATOM   4175  C  CG  . LEU D  1 117 ? 4.452   93.075  78.604  1.00 7.32  ? 117  LEU D CG  1 
ATOM   4176  C  CD1 . LEU D  1 117 ? 3.530   93.643  77.516  1.00 6.62  ? 117  LEU D CD1 1 
ATOM   4177  C  CD2 . LEU D  1 117 ? 4.813   94.097  79.675  1.00 6.32  ? 117  LEU D CD2 1 
ATOM   4178  N  N   . VAL D  1 118 ? 5.325   90.277  76.656  1.00 6.64  ? 118  VAL D N   1 
ATOM   4179  C  CA  . VAL D  1 118 ? 6.568   89.724  76.108  1.00 6.39  ? 118  VAL D CA  1 
ATOM   4180  C  C   . VAL D  1 118 ? 7.350   90.816  75.404  1.00 7.42  ? 118  VAL D C   1 
ATOM   4181  O  O   . VAL D  1 118 ? 6.756   91.608  74.703  1.00 7.06  ? 118  VAL D O   1 
ATOM   4182  C  CB  . VAL D  1 118 ? 6.234   88.649  75.076  1.00 7.20  ? 118  VAL D CB  1 
ATOM   4183  C  CG1 . VAL D  1 118 ? 7.478   88.202  74.317  1.00 8.32  ? 118  VAL D CG1 1 
ATOM   4184  C  CG2 . VAL D  1 118 ? 5.513   87.458  75.736  1.00 6.10  ? 118  VAL D CG2 1 
ATOM   4185  N  N   . VAL D  1 119 ? 8.663   90.882  75.624  1.00 6.51  ? 119  VAL D N   1 
ATOM   4186  C  CA  . VAL D  1 119 ? 9.515   91.738  74.800  1.00 7.60  ? 119  VAL D CA  1 
ATOM   4187  C  C   . VAL D  1 119 ? 10.370  90.829  73.911  1.00 8.50  ? 119  VAL D C   1 
ATOM   4188  O  O   . VAL D  1 119 ? 10.914  89.827  74.348  1.00 7.67  ? 119  VAL D O   1 
ATOM   4189  C  CB  . VAL D  1 119 ? 10.344  92.741  75.592  1.00 6.74  ? 119  VAL D CB  1 
ATOM   4190  C  CG1 . VAL D  1 119 ? 11.311  92.042  76.541  1.00 8.78  ? 119  VAL D CG1 1 
ATOM   4191  C  CG2 . VAL D  1 119 ? 11.078  93.753  74.662  1.00 7.20  ? 119  VAL D CG2 1 
ATOM   4192  N  N   . HIS D  1 120 ? 10.505  91.246  72.667  1.00 8.75  ? 120  HIS D N   1 
ATOM   4193  C  CA  . HIS D  1 120 ? 11.067  90.383  71.624  1.00 10.30 ? 120  HIS D CA  1 
ATOM   4194  C  C   . HIS D  1 120 ? 12.468  90.753  71.148  1.00 10.40 ? 120  HIS D C   1 
ATOM   4195  O  O   . HIS D  1 120 ? 12.957  91.845  71.387  1.00 9.49  ? 120  HIS D O   1 
ATOM   4196  C  CB  . HIS D  1 120 ? 10.135  90.438  70.415  1.00 9.90  ? 120  HIS D CB  1 
ATOM   4197  C  CG  . HIS D  1 120 ? 8.967   89.516  70.497  1.00 12.03 ? 120  HIS D CG  1 
ATOM   4198  N  ND1 . HIS D  1 120 ? 9.047   88.187  70.132  1.00 11.07 ? 120  HIS D ND1 1 
ATOM   4199  C  CD2 . HIS D  1 120 ? 7.686   89.723  70.896  1.00 14.57 ? 120  HIS D CD2 1 
ATOM   4200  C  CE1 . HIS D  1 120 ? 7.868   87.616  70.303  1.00 13.92 ? 120  HIS D CE1 1 
ATOM   4201  N  NE2 . HIS D  1 120 ? 7.029   88.520  70.776  1.00 16.54 ? 120  HIS D NE2 1 
ATOM   4202  N  N   . GLU D  1 121 ? 13.078  89.793  70.449  1.00 11.41 ? 121  GLU D N   1 
ATOM   4203  C  CA  . GLU D  1 121 ? 14.408  89.888  69.890  1.00 12.52 ? 121  GLU D CA  1 
ATOM   4204  C  C   . GLU D  1 121 ? 14.523  90.962  68.828  1.00 12.88 ? 121  GLU D C   1 
ATOM   4205  O  O   . GLU D  1 121 ? 15.483  91.709  68.810  1.00 13.68 ? 121  GLU D O   1 
ATOM   4206  C  CB  . GLU D  1 121 ? 14.713  88.536  69.246  1.00 12.89 ? 121  GLU D CB  1 
ATOM   4207  C  CG  . GLU D  1 121 ? 15.972  88.494  68.390  1.00 15.93 ? 121  GLU D CG  1 
ATOM   4208  C  CD  . GLU D  1 121 ? 16.138  87.135  67.749  1.00 21.03 ? 121  GLU D CD  1 
ATOM   4209  O  OE1 . GLU D  1 121 ? 17.315  86.694  67.619  1.00 24.85 ? 121  GLU D OE1 1 
ATOM   4210  O  OE2 . GLU D  1 121 ? 15.093  86.503  67.392  1.00 19.82 ? 121  GLU D OE2 1 
ATOM   4211  N  N   . LYS D  1 122 ? 13.530  91.048  67.956  1.00 12.92 ? 122  LYS D N   1 
ATOM   4212  C  CA  . LYS D  1 122 ? 13.605  91.964  66.829  1.00 14.60 ? 122  LYS D CA  1 
ATOM   4213  C  C   . LYS D  1 122 ? 12.455  92.945  66.766  1.00 13.45 ? 122  LYS D C   1 
ATOM   4214  O  O   . LYS D  1 122 ? 11.506  92.873  67.542  1.00 13.48 ? 122  LYS D O   1 
ATOM   4215  C  CB  . LYS D  1 122 ? 13.630  91.182  65.497  1.00 14.13 ? 122  LYS D CB  1 
ATOM   4216  C  CG  . LYS D  1 122 ? 14.711  90.127  65.375  1.00 19.20 ? 122  LYS D CG  1 
ATOM   4217  C  CD  . LYS D  1 122 ? 14.645  89.379  63.994  1.00 20.87 ? 122  LYS D CD  1 
ATOM   4218  N  N   . ALA D  1 123 ? 12.530  93.869  65.816  1.00 13.37 ? 123  ALA D N   1 
ATOM   4219  C  CA  . ALA D  1 123 ? 11.422  94.809  65.647  1.00 12.06 ? 123  ALA D CA  1 
ATOM   4220  C  C   . ALA D  1 123 ? 10.192  94.080  65.123  1.00 12.36 ? 123  ALA D C   1 
ATOM   4221  O  O   . ALA D  1 123 ? 10.278  93.073  64.394  1.00 11.42 ? 123  ALA D O   1 
ATOM   4222  C  CB  . ALA D  1 123 ? 11.803  95.947  64.682  1.00 12.93 ? 123  ALA D CB  1 
ATOM   4223  N  N   . ASP D  1 124 ? 9.044   94.604  65.510  1.00 11.48 ? 124  ASP D N   1 
ATOM   4224  C  CA  . ASP D  1 124 ? 7.764   94.143  65.042  1.00 11.94 ? 124  ASP D CA  1 
ATOM   4225  C  C   . ASP D  1 124 ? 7.504   94.928  63.749  1.00 11.10 ? 124  ASP D C   1 
ATOM   4226  O  O   . ASP D  1 124 ? 7.561   96.166  63.736  1.00 10.95 ? 124  ASP D O   1 
ATOM   4227  C  CB  . ASP D  1 124 ? 6.754   94.506  66.133  1.00 11.37 ? 124  ASP D CB  1 
ATOM   4228  C  CG  . ASP D  1 124 ? 5.363   94.081  65.819  1.00 14.17 ? 124  ASP D CG  1 
ATOM   4229  O  OD1 . ASP D  1 124 ? 5.052   93.872  64.628  1.00 12.54 ? 124  ASP D OD1 1 
ATOM   4230  O  OD2 . ASP D  1 124 ? 4.464   93.955  66.699  1.00 14.21 ? 124  ASP D OD2 1 
ATOM   4231  N  N   . ASP D  1 125 ? 7.233   94.235  62.641  1.00 11.18 ? 125  ASP D N   1 
ATOM   4232  C  CA  . ASP D  1 125 ? 7.062   94.976  61.371  1.00 10.73 ? 125  ASP D CA  1 
ATOM   4233  C  C   . ASP D  1 125 ? 5.642   95.501  61.174  1.00 11.19 ? 125  ASP D C   1 
ATOM   4234  O  O   . ASP D  1 125 ? 5.272   95.969  60.086  1.00 10.14 ? 125  ASP D O   1 
ATOM   4235  C  CB  . ASP D  1 125 ? 7.530   94.152  60.146  1.00 11.13 ? 125  ASP D CB  1 
ATOM   4236  C  CG  . ASP D  1 125 ? 6.693   92.901  59.912  1.00 12.62 ? 125  ASP D CG  1 
ATOM   4237  O  OD1 . ASP D  1 125 ? 5.503   92.837  60.352  1.00 8.69  ? 125  ASP D OD1 1 
ATOM   4238  O  OD2 . ASP D  1 125 ? 7.161   91.901  59.301  1.00 12.98 ? 125  ASP D OD2 1 
ATOM   4239  N  N   . LEU D  1 126 ? 4.864   95.422  62.260  1.00 10.47 ? 126  LEU D N   1 
ATOM   4240  C  CA  . LEU D  1 126 ? 3.469   95.870  62.293  1.00 10.61 ? 126  LEU D CA  1 
ATOM   4241  C  C   . LEU D  1 126 ? 2.561   95.289  61.178  1.00 8.79  ? 126  LEU D C   1 
ATOM   4242  O  O   . LEU D  1 126 ? 1.573   95.900  60.801  1.00 8.13  ? 126  LEU D O   1 
ATOM   4243  C  CB  . LEU D  1 126 ? 3.403   97.394  62.338  1.00 11.19 ? 126  LEU D CB  1 
ATOM   4244  C  CG  . LEU D  1 126 ? 4.477   98.044  63.219  1.00 11.24 ? 126  LEU D CG  1 
ATOM   4245  C  CD1 . LEU D  1 126 ? 4.353   99.546  63.185  1.00 11.90 ? 126  LEU D CD1 1 
ATOM   4246  C  CD2 . LEU D  1 126 ? 4.275   97.502  64.658  1.00 11.93 ? 126  LEU D CD2 1 
ATOM   4247  N  N   . GLY D  1 127 ? 2.873   94.077  60.737  1.00 7.48  ? 127  GLY D N   1 
ATOM   4248  C  CA  . GLY D  1 127 ? 2.083   93.397  59.735  1.00 7.58  ? 127  GLY D CA  1 
ATOM   4249  C  C   . GLY D  1 127 ? 2.408   93.783  58.316  1.00 7.63  ? 127  GLY D C   1 
ATOM   4250  O  O   . GLY D  1 127 ? 1.649   93.450  57.389  1.00 7.66  ? 127  GLY D O   1 
ATOM   4251  N  N   . LYS D  1 128 ? 3.511   94.510  58.135  1.00 6.50  ? 128  LYS D N   1 
ATOM   4252  C  CA  . LYS D  1 128 ? 3.838   95.054  56.822  1.00 6.29  ? 128  LYS D CA  1 
ATOM   4253  C  C   . LYS D  1 128 ? 5.009   94.400  56.105  1.00 5.50  ? 128  LYS D C   1 
ATOM   4254  O  O   . LYS D  1 128 ? 5.545   94.963  55.158  1.00 5.00  ? 128  LYS D O   1 
ATOM   4255  C  CB  . LYS D  1 128 ? 4.082   96.572  56.936  1.00 7.21  ? 128  LYS D CB  1 
ATOM   4256  C  CG  . LYS D  1 128 ? 2.931   97.298  57.606  1.00 9.68  ? 128  LYS D CG  1 
ATOM   4257  C  CD  . LYS D  1 128 ? 2.881   98.760  57.236  1.00 17.64 ? 128  LYS D CD  1 
ATOM   4258  C  CE  . LYS D  1 128 ? 4.039   99.510  57.840  1.00 22.59 ? 128  LYS D CE  1 
ATOM   4259  N  NZ  . LYS D  1 128 ? 4.137   100.945 57.343  1.00 27.41 ? 128  LYS D NZ  1 
ATOM   4260  N  N   . GLY D  1 129 ? 5.386   93.223  56.567  1.00 5.00  ? 129  GLY D N   1 
ATOM   4261  C  CA  . GLY D  1 129 ? 6.550   92.543  56.076  1.00 5.00  ? 129  GLY D CA  1 
ATOM   4262  C  C   . GLY D  1 129 ? 6.331   91.737  54.805  1.00 5.00  ? 129  GLY D C   1 
ATOM   4263  O  O   . GLY D  1 129 ? 7.307   91.249  54.236  1.00 5.00  ? 129  GLY D O   1 
ATOM   4264  N  N   . GLY D  1 130 ? 5.083   91.598  54.358  1.00 5.00  ? 130  GLY D N   1 
ATOM   4265  C  CA  . GLY D  1 130 ? 4.857   90.878  53.101  1.00 5.00  ? 130  GLY D CA  1 
ATOM   4266  C  C   . GLY D  1 130 ? 4.939   89.349  53.175  1.00 5.00  ? 130  GLY D C   1 
ATOM   4267  O  O   . GLY D  1 130 ? 5.118   88.703  52.138  1.00 5.00  ? 130  GLY D O   1 
ATOM   4268  N  N   . ASN D  1 131 ? 4.846   88.785  54.375  1.00 5.74  ? 131  ASN D N   1 
ATOM   4269  C  CA  . ASN D  1 131 ? 4.812   87.329  54.561  1.00 7.13  ? 131  ASN D CA  1 
ATOM   4270  C  C   . ASN D  1 131 ? 3.812   86.873  55.612  1.00 7.22  ? 131  ASN D C   1 
ATOM   4271  O  O   . ASN D  1 131 ? 3.302   87.676  56.391  1.00 7.69  ? 131  ASN D O   1 
ATOM   4272  C  CB  . ASN D  1 131 ? 6.203   86.709  54.802  1.00 7.42  ? 131  ASN D CB  1 
ATOM   4273  C  CG  . ASN D  1 131 ? 6.905   87.276  56.029  1.00 7.14  ? 131  ASN D CG  1 
ATOM   4274  O  OD1 . ASN D  1 131 ? 6.280   87.634  57.016  1.00 7.38  ? 131  ASN D OD1 1 
ATOM   4275  N  ND2 . ASN D  1 131 ? 8.224   87.301  55.977  1.00 9.90  ? 131  ASN D ND2 1 
ATOM   4276  N  N   . GLU D  1 132 ? 3.534   85.572  55.646  1.00 7.96  ? 132  GLU D N   1 
ATOM   4277  C  CA  . GLU D  1 132 ? 2.568   85.034  56.604  1.00 9.09  ? 132  GLU D CA  1 
ATOM   4278  C  C   . GLU D  1 132 ? 2.937   85.373  58.034  1.00 9.29  ? 132  GLU D C   1 
ATOM   4279  O  O   . GLU D  1 132 ? 2.098   85.830  58.827  1.00 9.01  ? 132  GLU D O   1 
ATOM   4280  C  CB  . GLU D  1 132 ? 2.396   83.516  56.429  1.00 9.52  ? 132  GLU D CB  1 
ATOM   4281  C  CG  . GLU D  1 132 ? 1.290   82.955  57.320  1.00 14.61 ? 132  GLU D CG  1 
ATOM   4282  C  CD  . GLU D  1 132 ? 1.050   81.463  57.146  1.00 20.47 ? 132  GLU D CD  1 
ATOM   4283  O  OE1 . GLU D  1 132 ? 0.142   80.958  57.838  1.00 22.11 ? 132  GLU D OE1 1 
ATOM   4284  O  OE2 . GLU D  1 132 ? 1.757   80.794  56.346  1.00 21.67 ? 132  GLU D OE2 1 
ATOM   4285  N  N   . GLU D  1 133 ? 4.200   85.185  58.373  1.00 9.64  ? 133  GLU D N   1 
ATOM   4286  C  CA  . GLU D  1 133 ? 4.648   85.451  59.735  1.00 11.31 ? 133  GLU D CA  1 
ATOM   4287  C  C   . GLU D  1 133 ? 4.374   86.919  60.117  1.00 10.42 ? 133  GLU D C   1 
ATOM   4288  O  O   . GLU D  1 133 ? 3.963   87.220  61.241  1.00 11.19 ? 133  GLU D O   1 
ATOM   4289  C  CB  . GLU D  1 133 ? 6.133   85.064  59.865  1.00 12.19 ? 133  GLU D CB  1 
ATOM   4290  C  CG  . GLU D  1 133 ? 6.739   85.137  61.265  1.00 17.15 ? 133  GLU D CG  1 
ATOM   4291  C  CD  . GLU D  1 133 ? 6.269   84.068  62.228  1.00 22.83 ? 133  GLU D CD  1 
ATOM   4292  O  OE1 . GLU D  1 133 ? 6.241   82.869  61.864  1.00 25.53 ? 133  GLU D OE1 1 
ATOM   4293  O  OE2 . GLU D  1 133 ? 5.964   84.435  63.381  1.00 24.16 ? 133  GLU D OE2 1 
ATOM   4294  N  N   . SER D  1 134 ? 4.575   87.839  59.182  1.00 9.63  ? 134  SER D N   1 
ATOM   4295  C  CA  . SER D  1 134 ? 4.284   89.224  59.472  1.00 9.23  ? 134  SER D CA  1 
ATOM   4296  C  C   . SER D  1 134 ? 2.847   89.398  59.951  1.00 10.27 ? 134  SER D C   1 
ATOM   4297  O  O   . SER D  1 134 ? 2.598   90.212  60.830  1.00 9.64  ? 134  SER D O   1 
ATOM   4298  C  CB  . SER D  1 134 ? 4.543   90.124  58.253  1.00 9.18  ? 134  SER D CB  1 
ATOM   4299  O  OG  . SER D  1 134 ? 4.212   91.443  58.578  1.00 8.73  ? 134  SER D OG  1 
ATOM   4300  N  N   . THR D  1 135 ? 1.913   88.647  59.367  1.00 10.37 ? 135  THR D N   1 
ATOM   4301  C  CA  . THR D  1 135 ? 0.496   88.745  59.745  1.00 11.60 ? 135  THR D CA  1 
ATOM   4302  C  C   . THR D  1 135 ? 0.138   88.021  61.050  1.00 12.25 ? 135  THR D C   1 
ATOM   4303  O  O   . THR D  1 135 ? -1.013  88.052  61.461  1.00 10.45 ? 135  THR D O   1 
ATOM   4304  C  CB  . THR D  1 135 ? -0.403  88.173  58.626  1.00 12.28 ? 135  THR D CB  1 
ATOM   4305  O  OG1 . THR D  1 135 ? -0.338  86.733  58.649  1.00 14.79 ? 135  THR D OG1 1 
ATOM   4306  C  CG2 . THR D  1 135 ? 0.129   88.526  57.331  1.00 13.38 ? 135  THR D CG2 1 
ATOM   4307  N  N   . LYS D  1 136 ? 1.115   87.367  61.672  1.00 12.30 ? 136  LYS D N   1 
ATOM   4308  C  CA  . LYS D  1 136 ? 0.873   86.627  62.916  1.00 12.68 ? 136  LYS D CA  1 
ATOM   4309  C  C   . LYS D  1 136 ? 1.622   87.207  64.101  1.00 12.70 ? 136  LYS D C   1 
ATOM   4310  O  O   . LYS D  1 136 ? 1.038   87.381  65.188  1.00 11.95 ? 136  LYS D O   1 
ATOM   4311  C  CB  . LYS D  1 136 ? 1.320   85.182  62.753  1.00 12.61 ? 136  LYS D CB  1 
ATOM   4312  C  CG  . LYS D  1 136 ? 0.524   84.427  61.725  1.00 17.11 ? 136  LYS D CG  1 
ATOM   4313  C  CD  . LYS D  1 136 ? 1.146   83.067  61.457  1.00 21.13 ? 136  LYS D CD  1 
ATOM   4314  N  N   . THR D  1 137 ? 2.922   87.460  63.903  1.00 12.54 ? 137  THR D N   1 
ATOM   4315  C  CA  . THR D  1 137 ? 3.810   87.938  64.973  1.00 12.76 ? 137  THR D CA  1 
ATOM   4316  C  C   . THR D  1 137 ? 4.574   89.206  64.658  1.00 13.21 ? 137  THR D C   1 
ATOM   4317  O  O   . THR D  1 137 ? 5.335   89.698  65.498  1.00 12.19 ? 137  THR D O   1 
ATOM   4318  C  CB  . THR D  1 137 ? 4.884   86.874  65.284  1.00 13.44 ? 137  THR D CB  1 
ATOM   4319  O  OG1 . THR D  1 137 ? 5.746   86.708  64.141  1.00 10.93 ? 137  THR D OG1 1 
ATOM   4320  C  CG2 . THR D  1 137 ? 4.269   85.528  65.485  1.00 14.13 ? 137  THR D CG2 1 
ATOM   4321  N  N   . GLY D  1 138 ? 4.437   89.715  63.436  1.00 10.90 ? 138  GLY D N   1 
ATOM   4322  C  CA  . GLY D  1 138 ? 5.228   90.854  63.028  1.00 11.00 ? 138  GLY D CA  1 
ATOM   4323  C  C   . GLY D  1 138 ? 6.700   90.534  62.809  1.00 10.36 ? 138  GLY D C   1 
ATOM   4324  O  O   . GLY D  1 138 ? 7.506   91.446  62.700  1.00 9.50  ? 138  GLY D O   1 
ATOM   4325  N  N   . ASN D  1 139 ? 7.061   89.252  62.772  1.00 10.90 ? 139  ASN D N   1 
ATOM   4326  C  CA  . ASN D  1 139 ? 8.469   88.851  62.601  1.00 10.57 ? 139  ASN D CA  1 
ATOM   4327  C  C   . ASN D  1 139 ? 9.357   89.377  63.709  1.00 11.03 ? 139  ASN D C   1 
ATOM   4328  O  O   . ASN D  1 139 ? 10.527  89.682  63.510  1.00 9.75  ? 139  ASN D O   1 
ATOM   4329  C  CB  . ASN D  1 139 ? 9.026   89.272  61.235  1.00 11.04 ? 139  ASN D CB  1 
ATOM   4330  C  CG  . ASN D  1 139 ? 8.503   88.385  60.116  1.00 13.54 ? 139  ASN D CG  1 
ATOM   4331  O  OD1 . ASN D  1 139 ? 8.780   87.189  60.071  1.00 13.54 ? 139  ASN D OD1 1 
ATOM   4332  N  ND2 . ASN D  1 139 ? 7.703   88.957  59.262  1.00 12.38 ? 139  ASN D ND2 1 
ATOM   4333  N  N   . ALA D  1 140 ? 8.812   89.446  64.914  1.00 10.96 ? 140  ALA D N   1 
ATOM   4334  C  CA  . ALA D  1 140 ? 9.571   90.022  66.000  1.00 12.56 ? 140  ALA D CA  1 
ATOM   4335  C  C   . ALA D  1 140 ? 10.580  89.057  66.599  1.00 12.87 ? 140  ALA D C   1 
ATOM   4336  O  O   . ALA D  1 140 ? 11.378  89.433  67.452  1.00 13.24 ? 140  ALA D O   1 
ATOM   4337  C  CB  . ALA D  1 140 ? 8.631   90.584  67.065  1.00 12.00 ? 140  ALA D CB  1 
ATOM   4338  N  N   . GLY D  1 141 ? 10.596  87.817  66.114  1.00 13.59 ? 141  GLY D N   1 
ATOM   4339  C  CA  . GLY D  1 141 ? 11.631  86.900  66.552  1.00 12.28 ? 141  GLY D CA  1 
ATOM   4340  C  C   . GLY D  1 141 ? 11.415  86.354  67.936  1.00 12.16 ? 141  GLY D C   1 
ATOM   4341  O  O   . GLY D  1 141 ? 10.280  86.313  68.406  1.00 12.07 ? 141  GLY D O   1 
ATOM   4342  N  N   . SER D  1 142 ? 12.500  85.975  68.600  1.00 11.84 ? 142  SER D N   1 
ATOM   4343  C  CA  . SER D  1 142 ? 12.380  85.241  69.845  1.00 12.55 ? 142  SER D CA  1 
ATOM   4344  C  C   . SER D  1 142 ? 11.898  86.074  71.015  1.00 11.49 ? 142  SER D C   1 
ATOM   4345  O  O   . SER D  1 142 ? 11.876  87.296  70.960  1.00 11.09 ? 142  SER D O   1 
ATOM   4346  C  CB  . SER D  1 142 ? 13.692  84.533  70.185  1.00 13.38 ? 142  SER D CB  1 
ATOM   4347  O  OG  . SER D  1 142 ? 14.683  85.468  70.583  1.00 16.41 ? 142  SER D OG  1 
ATOM   4348  N  N   . ARG D  1 143 ? 11.486  85.373  72.056  1.00 10.69 ? 143  ARG D N   1 
ATOM   4349  C  CA  . ARG D  1 143 ? 10.984  85.996  73.276  1.00 10.60 ? 143  ARG D CA  1 
ATOM   4350  C  C   . ARG D  1 143 ? 12.133  86.166  74.257  1.00 10.38 ? 143  ARG D C   1 
ATOM   4351  O  O   . ARG D  1 143 ? 12.619  85.183  74.834  1.00 11.70 ? 143  ARG D O   1 
ATOM   4352  C  CB  . ARG D  1 143 ? 9.863   85.104  73.832  1.00 10.98 ? 143  ARG D CB  1 
ATOM   4353  C  CG  . ARG D  1 143 ? 8.780   84.876  72.773  1.00 10.87 ? 143  ARG D CG  1 
ATOM   4354  C  CD  . ARG D  1 143 ? 7.611   83.947  73.184  1.00 12.74 ? 143  ARG D CD  1 
ATOM   4355  N  NE  . ARG D  1 143 ? 6.699   83.762  72.051  1.00 12.24 ? 143  ARG D NE  1 
ATOM   4356  C  CZ  . ARG D  1 143 ? 5.511   83.182  72.127  1.00 13.02 ? 143  ARG D CZ  1 
ATOM   4357  N  NH1 . ARG D  1 143 ? 5.077   82.706  73.301  1.00 11.79 ? 143  ARG D NH1 1 
ATOM   4358  N  NH2 . ARG D  1 143 ? 4.752   83.080  71.028  1.00 11.97 ? 143  ARG D NH2 1 
ATOM   4359  N  N   . LEU D  1 144 ? 12.606  87.395  74.424  1.00 9.39  ? 144  LEU D N   1 
ATOM   4360  C  CA  . LEU D  1 144 ? 13.767  87.628  75.288  1.00 9.77  ? 144  LEU D CA  1 
ATOM   4361  C  C   . LEU D  1 144 ? 13.409  87.627  76.746  1.00 9.45  ? 144  LEU D C   1 
ATOM   4362  O  O   . LEU D  1 144 ? 14.179  87.184  77.580  1.00 8.61  ? 144  LEU D O   1 
ATOM   4363  C  CB  . LEU D  1 144 ? 14.469  88.948  74.923  1.00 8.80  ? 144  LEU D CB  1 
ATOM   4364  C  CG  . LEU D  1 144 ? 14.951  88.905  73.467  1.00 12.32 ? 144  LEU D CG  1 
ATOM   4365  C  CD1 . LEU D  1 144 ? 15.753  90.149  73.213  1.00 14.83 ? 144  LEU D CD1 1 
ATOM   4366  C  CD2 . LEU D  1 144 ? 15.837  87.679  73.204  1.00 13.45 ? 144  LEU D CD2 1 
ATOM   4367  N  N   . ALA D  1 145 ? 12.233  88.147  77.062  1.00 9.27  ? 145  ALA D N   1 
ATOM   4368  C  CA  . ALA D  1 145 ? 11.818  88.218  78.456  1.00 9.13  ? 145  ALA D CA  1 
ATOM   4369  C  C   . ALA D  1 145 ? 10.318  88.321  78.494  1.00 8.77  ? 145  ALA D C   1 
ATOM   4370  O  O   . ALA D  1 145 ? 9.697   88.865  77.576  1.00 8.91  ? 145  ALA D O   1 
ATOM   4371  C  CB  . ALA D  1 145 ? 12.416  89.426  79.167  1.00 7.61  ? 145  ALA D CB  1 
ATOM   4372  N  N   . CYS D  1 146 ? 9.731   87.815  79.576  1.00 8.51  ? 146  CYS D N   1 
ATOM   4373  C  CA  . CYS D  1 146 ? 8.294   87.910  79.696  1.00 7.95  ? 146  CYS D CA  1 
ATOM   4374  C  C   . CYS D  1 146 ? 7.866   87.831  81.170  1.00 7.39  ? 146  CYS D C   1 
ATOM   4375  O  O   . CYS D  1 146 ? 8.652   87.461  82.071  1.00 6.34  ? 146  CYS D O   1 
ATOM   4376  C  CB  . CYS D  1 146 ? 7.634   86.747  78.956  1.00 9.74  ? 146  CYS D CB  1 
ATOM   4377  S  SG  . CYS D  1 146 ? 8.030   85.087  79.640  1.00 12.61 ? 146  CYS D SG  1 
ATOM   4378  N  N   . GLY D  1 147 ? 6.601   88.155  81.414  1.00 5.97  ? 147  GLY D N   1 
ATOM   4379  C  CA  . GLY D  1 147 ? 6.040   87.979  82.745  1.00 6.53  ? 147  GLY D CA  1 
ATOM   4380  C  C   . GLY D  1 147 ? 4.525   87.988  82.745  1.00 6.56  ? 147  GLY D C   1 
ATOM   4381  O  O   . GLY D  1 147 ? 3.897   88.453  81.807  1.00 6.89  ? 147  GLY D O   1 
ATOM   4382  N  N   . VAL D  1 148 ? 3.922   87.468  83.808  1.00 6.67  ? 148  VAL D N   1 
ATOM   4383  C  CA  . VAL D  1 148 ? 2.487   87.495  83.887  1.00 6.52  ? 148  VAL D CA  1 
ATOM   4384  C  C   . VAL D  1 148 ? 2.051   88.851  84.428  1.00 7.14  ? 148  VAL D C   1 
ATOM   4385  O  O   . VAL D  1 148 ? 2.681   89.379  85.352  1.00 8.19  ? 148  VAL D O   1 
ATOM   4386  C  CB  . VAL D  1 148 ? 1.968   86.373  84.789  1.00 7.84  ? 148  VAL D CB  1 
ATOM   4387  C  CG1 . VAL D  1 148 ? 0.433   86.348  84.747  1.00 7.54  ? 148  VAL D CG1 1 
ATOM   4388  C  CG2 . VAL D  1 148 ? 2.577   85.052  84.305  1.00 5.00  ? 148  VAL D CG2 1 
ATOM   4389  N  N   . ILE D  1 149 ? 1.026   89.430  83.805  1.00 5.13  ? 149  ILE D N   1 
ATOM   4390  C  CA  . ILE D  1 149 ? 0.520   90.731  84.232  1.00 5.63  ? 149  ILE D CA  1 
ATOM   4391  C  C   . ILE D  1 149 ? -0.320  90.573  85.495  1.00 5.02  ? 149  ILE D C   1 
ATOM   4392  O  O   . ILE D  1 149 ? -1.339  89.883  85.511  1.00 6.48  ? 149  ILE D O   1 
ATOM   4393  C  CB  . ILE D  1 149 ? -0.275  91.381  83.091  1.00 6.98  ? 149  ILE D CB  1 
ATOM   4394  C  CG1 . ILE D  1 149 ? 0.698   91.602  81.913  1.00 5.95  ? 149  ILE D CG1 1 
ATOM   4395  C  CG2 . ILE D  1 149 ? -0.899  92.697  83.524  1.00 7.02  ? 149  ILE D CG2 1 
ATOM   4396  C  CD1 . ILE D  1 149 ? -0.048  91.905  80.561  1.00 7.38  ? 149  ILE D CD1 1 
ATOM   4397  N  N   . GLY D  1 150 ? 0.088   91.239  86.563  1.00 5.50  ? 150  GLY D N   1 
ATOM   4398  C  CA  . GLY D  1 150 ? -0.653  91.083  87.828  1.00 5.39  ? 150  GLY D CA  1 
ATOM   4399  C  C   . GLY D  1 150 ? -1.294  92.348  88.331  1.00 5.82  ? 150  GLY D C   1 
ATOM   4400  O  O   . GLY D  1 150 ? -0.893  93.481  87.974  1.00 5.00  ? 150  GLY D O   1 
ATOM   4401  N  N   . ILE D  1 151 ? -2.229  92.164  89.258  1.00 5.13  ? 151  ILE D N   1 
ATOM   4402  C  CA  . ILE D  1 151 ? -2.901  93.310  89.870  1.00 5.00  ? 151  ILE D CA  1 
ATOM   4403  C  C   . ILE D  1 151 ? -1.934  93.997  90.804  1.00 5.30  ? 151  ILE D C   1 
ATOM   4404  O  O   . ILE D  1 151 ? -1.252  93.332  91.564  1.00 5.00  ? 151  ILE D O   1 
ATOM   4405  C  CB  . ILE D  1 151 ? -4.150  92.821  90.652  1.00 5.92  ? 151  ILE D CB  1 
ATOM   4406  C  CG1 . ILE D  1 151 ? -5.189  92.277  89.653  1.00 8.02  ? 151  ILE D CG1 1 
ATOM   4407  C  CG2 . ILE D  1 151 ? -4.723  93.933  91.503  1.00 9.52  ? 151  ILE D CG2 1 
ATOM   4408  C  CD1 . ILE D  1 151 ? -6.320  91.413  90.340  1.00 10.41 ? 151  ILE D CD1 1 
ATOM   4409  N  N   . ALA D  1 152 ? -1.841  95.324  90.721  1.00 5.54  ? 152  ALA D N   1 
ATOM   4410  C  CA  . ALA D  1 152 ? -0.899  96.094  91.526  1.00 6.53  ? 152  ALA D CA  1 
ATOM   4411  C  C   . ALA D  1 152 ? -1.637  96.920  92.564  1.00 8.20  ? 152  ALA D C   1 
ATOM   4412  O  O   . ALA D  1 152 ? -2.832  97.192  92.422  1.00 6.98  ? 152  ALA D O   1 
ATOM   4413  C  CB  . ALA D  1 152 ? -0.072  97.017  90.644  1.00 6.70  ? 152  ALA D CB  1 
ATOM   4414  N  N   . GLN D  1 153 ? -0.897  97.284  93.600  1.00 8.86  ? 153  GLN D N   1 
ATOM   4415  C  CA  . GLN D  1 153 ? -1.426  98.026  94.739  1.00 12.63 ? 153  GLN D CA  1 
ATOM   4416  C  C   . GLN D  1 153 ? -1.627  99.492  94.407  1.00 14.22 ? 153  GLN D C   1 
ATOM   4417  O  O   . GLN D  1 153 ? -0.735  100.086 93.771  1.00 15.27 ? 153  GLN D O   1 
ATOM   4418  C  CB  . GLN D  1 153 ? -0.455  97.882  95.904  1.00 12.67 ? 153  GLN D CB  1 
ATOM   4419  C  CG  . GLN D  1 153 ? -0.882  98.524  97.218  1.00 14.42 ? 153  GLN D CG  1 
ATOM   4420  C  CD  . GLN D  1 153 ? -0.087  97.960  98.363  1.00 15.64 ? 153  GLN D CD  1 
ATOM   4421  O  OE1 . GLN D  1 153 ? 1.030   97.414  98.174  1.00 15.10 ? 153  GLN D OE1 1 
ATOM   4422  N  NE2 . GLN D  1 153 ? -0.649  98.035  99.542  1.00 15.05 ? 153  GLN D NE2 1 
ATOM   4423  O  OXT . GLN D  1 153 ? -2.670  100.029 94.838  1.00 14.96 ? 153  GLN D OXT 1 
ATOM   4424  N  N   . ALA E  1 1   ? 64.723  127.312 73.971  1.00 26.29 ? 1    ALA E N   1 
ATOM   4425  C  CA  . ALA E  1 1   ? 63.308  126.836 74.231  1.00 25.31 ? 1    ALA E CA  1 
ATOM   4426  C  C   . ALA E  1 1   ? 62.211  127.719 73.633  1.00 24.66 ? 1    ALA E C   1 
ATOM   4427  O  O   . ALA E  1 1   ? 61.586  128.502 74.356  1.00 25.76 ? 1    ALA E O   1 
ATOM   4428  C  CB  . ALA E  1 1   ? 63.072  126.693 75.729  1.00 26.26 ? 1    ALA E CB  1 
ATOM   4429  N  N   . THR E  1 2   ? 61.914  127.532 72.346  1.00 22.01 ? 2    THR E N   1 
ATOM   4430  C  CA  . THR E  1 2   ? 60.957  128.375 71.644  1.00 20.02 ? 2    THR E CA  1 
ATOM   4431  C  C   . THR E  1 2   ? 59.505  127.971 71.924  1.00 17.23 ? 2    THR E C   1 
ATOM   4432  O  O   . THR E  1 2   ? 59.198  126.814 72.230  1.00 14.16 ? 2    THR E O   1 
ATOM   4433  C  CB  . THR E  1 2   ? 61.215  128.366 70.093  1.00 20.71 ? 2    THR E CB  1 
ATOM   4434  O  OG1 . THR E  1 2   ? 62.581  128.050 69.809  1.00 26.38 ? 2    THR E OG1 1 
ATOM   4435  C  CG2 . THR E  1 2   ? 61.085  129.770 69.526  1.00 23.75 ? 2    THR E CG2 1 
ATOM   4436  N  N   . LYS E  1 3   ? 58.618  128.953 71.840  1.00 14.52 ? 3    LYS E N   1 
ATOM   4437  C  CA  . LYS E  1 3   ? 57.197  128.696 72.026  1.00 13.53 ? 3    LYS E CA  1 
ATOM   4438  C  C   . LYS E  1 3   ? 56.407  129.385 70.924  1.00 11.28 ? 3    LYS E C   1 
ATOM   4439  O  O   . LYS E  1 3   ? 56.809  130.430 70.425  1.00 9.39  ? 3    LYS E O   1 
ATOM   4440  C  CB  . LYS E  1 3   ? 56.729  129.244 73.358  1.00 13.83 ? 3    LYS E CB  1 
ATOM   4441  C  CG  . LYS E  1 3   ? 57.232  128.447 74.564  1.00 15.94 ? 3    LYS E CG  1 
ATOM   4442  C  CD  . LYS E  1 3   ? 57.073  129.285 75.825  1.00 19.44 ? 3    LYS E CD  1 
ATOM   4443  N  N   . ALA E  1 4   ? 55.284  128.790 70.548  1.00 9.66  ? 4    ALA E N   1 
ATOM   4444  C  CA  . ALA E  1 4   ? 54.423  129.411 69.568  1.00 8.22  ? 4    ALA E CA  1 
ATOM   4445  C  C   . ALA E  1 4   ? 53.023  129.144 70.000  1.00 7.78  ? 4    ALA E C   1 
ATOM   4446  O  O   . ALA E  1 4   ? 52.797  128.318 70.870  1.00 7.82  ? 4    ALA E O   1 
ATOM   4447  C  CB  . ALA E  1 4   ? 54.627  128.781 68.182  1.00 7.58  ? 4    ALA E CB  1 
ATOM   4448  N  N   . VAL E  1 5   ? 52.073  129.797 69.342  1.00 6.15  ? 5    VAL E N   1 
ATOM   4449  C  CA  . VAL E  1 5   ? 50.686  129.636 69.707  1.00 6.11  ? 5    VAL E CA  1 
ATOM   4450  C  C   . VAL E  1 5   ? 49.818  129.886 68.466  1.00 6.97  ? 5    VAL E C   1 
ATOM   4451  O  O   . VAL E  1 5   ? 50.242  130.573 67.535  1.00 6.67  ? 5    VAL E O   1 
ATOM   4452  C  CB  . VAL E  1 5   ? 50.343  130.610 70.873  1.00 6.71  ? 5    VAL E CB  1 
ATOM   4453  C  CG1 . VAL E  1 5   ? 50.416  132.084 70.374  1.00 5.39  ? 5    VAL E CG1 1 
ATOM   4454  C  CG2 . VAL E  1 5   ? 48.998  130.285 71.481  1.00 6.72  ? 5    VAL E CG2 1 
ATOM   4455  N  N   . CYS E  1 6   ? 48.612  129.306 68.452  1.00 6.47  ? 6    CYS E N   1 
ATOM   4456  C  CA  . CYS E  1 6   ? 47.713  129.406 67.314  1.00 6.85  ? 6    CYS E CA  1 
ATOM   4457  C  C   . CYS E  1 6   ? 46.299  129.459 67.833  1.00 7.46  ? 6    CYS E C   1 
ATOM   4458  O  O   . CYS E  1 6   ? 45.927  128.648 68.637  1.00 8.15  ? 6    CYS E O   1 
ATOM   4459  C  CB  . CYS E  1 6   ? 47.847  128.135 66.466  1.00 5.77  ? 6    CYS E CB  1 
ATOM   4460  S  SG  . CYS E  1 6   ? 46.837  128.310 64.977  1.00 10.05 ? 6    CYS E SG  1 
ATOM   4461  N  N   . VAL E  1 7   ? 45.545  130.452 67.409  1.00 7.34  ? 7    VAL E N   1 
ATOM   4462  C  CA  . VAL E  1 7   ? 44.145  130.604 67.754  1.00 7.06  ? 7    VAL E CA  1 
ATOM   4463  C  C   . VAL E  1 7   ? 43.373  130.155 66.533  1.00 8.42  ? 7    VAL E C   1 
ATOM   4464  O  O   . VAL E  1 7   ? 43.528  130.740 65.453  1.00 7.25  ? 7    VAL E O   1 
ATOM   4465  C  CB  . VAL E  1 7   ? 43.806  132.071 68.058  1.00 6.57  ? 7    VAL E CB  1 
ATOM   4466  C  CG1 . VAL E  1 7   ? 42.277  132.229 68.300  1.00 8.81  ? 7    VAL E CG1 1 
ATOM   4467  C  CG2 . VAL E  1 7   ? 44.630  132.545 69.263  1.00 7.07  ? 7    VAL E CG2 1 
ATOM   4468  N  N   . LEU E  1 8   ? 42.597  129.067 66.679  1.00 7.50  ? 8    LEU E N   1 
ATOM   4469  C  CA  . LEU E  1 8   ? 41.856  128.510 65.545  1.00 8.85  ? 8    LEU E CA  1 
ATOM   4470  C  C   . LEU E  1 8   ? 40.434  129.058 65.530  1.00 8.32  ? 8    LEU E C   1 
ATOM   4471  O  O   . LEU E  1 8   ? 39.767  129.050 66.552  1.00 8.19  ? 8    LEU E O   1 
ATOM   4472  C  CB  . LEU E  1 8   ? 41.702  126.990 65.716  1.00 8.28  ? 8    LEU E CB  1 
ATOM   4473  C  CG  . LEU E  1 8   ? 42.976  126.120 65.731  1.00 13.12 ? 8    LEU E CG  1 
ATOM   4474  C  CD1 . LEU E  1 8   ? 43.936  126.474 66.817  1.00 15.21 ? 8    LEU E CD1 1 
ATOM   4475  C  CD2 . LEU E  1 8   ? 42.567  124.651 65.935  1.00 15.99 ? 8    LEU E CD2 1 
ATOM   4476  N  N   . LYS E  1 9   ? 39.994  129.527 64.380  1.00 8.43  ? 9    LYS E N   1 
ATOM   4477  C  CA  . LYS E  1 9   ? 38.644  130.055 64.225  1.00 10.33 ? 9    LYS E CA  1 
ATOM   4478  C  C   . LYS E  1 9   ? 38.174  129.688 62.856  1.00 10.29 ? 9    LYS E C   1 
ATOM   4479  O  O   . LYS E  1 9   ? 38.980  129.488 61.961  1.00 9.82  ? 9    LYS E O   1 
ATOM   4480  C  CB  . LYS E  1 9   ? 38.668  131.579 64.298  1.00 10.90 ? 9    LYS E CB  1 
ATOM   4481  C  CG  . LYS E  1 9   ? 39.149  132.100 65.643  1.00 16.99 ? 9    LYS E CG  1 
ATOM   4482  C  CD  . LYS E  1 9   ? 38.335  131.501 66.799  1.00 22.40 ? 9    LYS E CD  1 
ATOM   4483  C  CE  . LYS E  1 9   ? 39.061  131.781 68.125  1.00 22.55 ? 9    LYS E CE  1 
ATOM   4484  N  NZ  . LYS E  1 9   ? 39.178  130.659 69.114  1.00 25.17 ? 9    LYS E NZ  1 
ATOM   4485  N  N   . GLY E  1 10  ? 36.856  129.659 62.664  1.00 11.50 ? 10   GLY E N   1 
ATOM   4486  C  CA  . GLY E  1 10  ? 36.322  129.300 61.366  1.00 12.85 ? 10   GLY E CA  1 
ATOM   4487  C  C   . GLY E  1 10  ? 34.947  129.925 61.222  1.00 14.41 ? 10   GLY E C   1 
ATOM   4488  O  O   . GLY E  1 10  ? 34.602  130.792 62.008  1.00 15.03 ? 10   GLY E O   1 
ATOM   4489  N  N   . ASP E  1 11  ? 34.166  129.516 60.239  1.00 15.65 ? 11   ASP E N   1 
ATOM   4490  C  CA  . ASP E  1 11  ? 32.825  130.132 60.096  1.00 17.53 ? 11   ASP E CA  1 
ATOM   4491  C  C   . ASP E  1 11  ? 31.751  129.446 60.934  1.00 17.34 ? 11   ASP E C   1 
ATOM   4492  O  O   . ASP E  1 11  ? 30.589  129.897 60.994  1.00 17.34 ? 11   ASP E O   1 
ATOM   4493  C  CB  . ASP E  1 11  ? 32.377  130.125 58.645  1.00 18.85 ? 11   ASP E CB  1 
ATOM   4494  C  CG  . ASP E  1 11  ? 33.334  130.853 57.739  1.00 21.36 ? 11   ASP E CG  1 
ATOM   4495  O  OD1 . ASP E  1 11  ? 33.763  131.967 58.088  1.00 26.05 ? 11   ASP E OD1 1 
ATOM   4496  O  OD2 . ASP E  1 11  ? 33.701  130.377 56.643  1.00 27.07 ? 11   ASP E OD2 1 
ATOM   4497  N  N   . GLY E  1 12  ? 32.139  128.344 61.552  1.00 16.10 ? 12   GLY E N   1 
ATOM   4498  C  CA  . GLY E  1 12  ? 31.247  127.561 62.382  1.00 15.89 ? 12   GLY E CA  1 
ATOM   4499  C  C   . GLY E  1 12  ? 31.590  127.704 63.846  1.00 14.23 ? 12   GLY E C   1 
ATOM   4500  O  O   . GLY E  1 12  ? 32.226  128.662 64.247  1.00 14.89 ? 12   GLY E O   1 
ATOM   4501  N  N   . PRO E  1 13  ? 31.183  126.737 64.647  1.00 14.16 ? 13   PRO E N   1 
ATOM   4502  C  CA  . PRO E  1 13  ? 31.414  126.781 66.097  1.00 13.36 ? 13   PRO E CA  1 
ATOM   4503  C  C   . PRO E  1 13  ? 32.772  126.241 66.549  1.00 12.89 ? 13   PRO E C   1 
ATOM   4504  O  O   . PRO E  1 13  ? 33.065  126.230 67.751  1.00 12.79 ? 13   PRO E O   1 
ATOM   4505  C  CB  . PRO E  1 13  ? 30.333  125.851 66.627  1.00 14.35 ? 13   PRO E CB  1 
ATOM   4506  C  CG  . PRO E  1 13  ? 30.177  124.794 65.500  1.00 14.91 ? 13   PRO E CG  1 
ATOM   4507  C  CD  . PRO E  1 13  ? 30.492  125.505 64.208  1.00 14.36 ? 13   PRO E CD  1 
ATOM   4508  N  N   . VAL E  1 14  ? 33.590  125.772 65.620  1.00 10.62 ? 14   VAL E N   1 
ATOM   4509  C  CA  . VAL E  1 14  ? 34.861  125.191 66.026  1.00 9.38  ? 14   VAL E CA  1 
ATOM   4510  C  C   . VAL E  1 14  ? 35.884  126.288 66.312  1.00 8.91  ? 14   VAL E C   1 
ATOM   4511  O  O   . VAL E  1 14  ? 36.133  127.151 65.483  1.00 8.30  ? 14   VAL E O   1 
ATOM   4512  C  CB  . VAL E  1 14  ? 35.397  124.275 64.944  1.00 8.70  ? 14   VAL E CB  1 
ATOM   4513  C  CG1 . VAL E  1 14  ? 36.710  123.655 65.397  1.00 8.01  ? 14   VAL E CG1 1 
ATOM   4514  C  CG2 . VAL E  1 14  ? 34.368  123.198 64.619  1.00 8.57  ? 14   VAL E CG2 1 
ATOM   4515  N  N   . GLN E  1 15  ? 36.469  126.259 67.500  1.00 9.17  ? 15   GLN E N   1 
ATOM   4516  C  CA  . GLN E  1 15  ? 37.474  127.270 67.833  1.00 9.87  ? 15   GLN E CA  1 
ATOM   4517  C  C   . GLN E  1 15  ? 38.329  126.704 68.949  1.00 9.35  ? 15   GLN E C   1 
ATOM   4518  O  O   . GLN E  1 15  ? 37.890  125.865 69.743  1.00 8.17  ? 15   GLN E O   1 
ATOM   4519  C  CB  . GLN E  1 15  ? 36.807  128.613 68.250  1.00 10.84 ? 15   GLN E CB  1 
ATOM   4520  C  CG  . GLN E  1 15  ? 35.738  128.480 69.331  1.00 11.75 ? 15   GLN E CG  1 
ATOM   4521  C  CD  . GLN E  1 15  ? 35.199  129.854 69.851  1.00 17.24 ? 15   GLN E CD  1 
ATOM   4522  N  N   . GLY E  1 16  ? 39.545  127.185 69.046  1.00 9.02  ? 16   GLY E N   1 
ATOM   4523  C  CA  . GLY E  1 16  ? 40.357  126.765 70.166  1.00 8.98  ? 16   GLY E CA  1 
ATOM   4524  C  C   . GLY E  1 16  ? 41.715  127.419 70.101  1.00 8.21  ? 16   GLY E C   1 
ATOM   4525  O  O   . GLY E  1 16  ? 41.957  128.307 69.268  1.00 6.52  ? 16   GLY E O   1 
ATOM   4526  N  N   . ILE E  1 17  ? 42.564  126.980 71.013  1.00 7.00  ? 17   ILE E N   1 
ATOM   4527  C  CA  . ILE E  1 17  ? 43.907  127.527 71.146  1.00 8.47  ? 17   ILE E CA  1 
ATOM   4528  C  C   . ILE E  1 17  ? 44.853  126.363 71.209  1.00 8.17  ? 17   ILE E C   1 
ATOM   4529  O  O   . ILE E  1 17  ? 44.669  125.457 72.036  1.00 8.36  ? 17   ILE E O   1 
ATOM   4530  C  CB  . ILE E  1 17  ? 44.024  128.362 72.445  1.00 8.29  ? 17   ILE E CB  1 
ATOM   4531  C  CG1 . ILE E  1 17  ? 43.160  129.624 72.350  1.00 9.38  ? 17   ILE E CG1 1 
ATOM   4532  C  CG2 . ILE E  1 17  ? 45.520  128.732 72.758  1.00 9.12  ? 17   ILE E CG2 1 
ATOM   4533  C  CD1 . ILE E  1 17  ? 43.000  130.341 73.734  1.00 11.24 ? 17   ILE E CD1 1 
ATOM   4534  N  N   . ILE E  1 18  ? 45.887  126.391 70.372  1.00 6.99  ? 18   ILE E N   1 
ATOM   4535  C  CA  . ILE E  1 18  ? 46.903  125.344 70.391  1.00 6.31  ? 18   ILE E CA  1 
ATOM   4536  C  C   . ILE E  1 18  ? 48.267  125.979 70.662  1.00 6.75  ? 18   ILE E C   1 
ATOM   4537  O  O   . ILE E  1 18  ? 48.647  126.980 70.020  1.00 6.03  ? 18   ILE E O   1 
ATOM   4538  C  CB  . ILE E  1 18  ? 46.940  124.634 69.060  1.00 6.92  ? 18   ILE E CB  1 
ATOM   4539  C  CG1 . ILE E  1 18  ? 45.582  123.915 68.825  1.00 6.45  ? 18   ILE E CG1 1 
ATOM   4540  C  CG2 . ILE E  1 18  ? 48.114  123.664 69.014  1.00 6.60  ? 18   ILE E CG2 1 
ATOM   4541  C  CD1 . ILE E  1 18  ? 45.354  122.783 69.866  1.00 7.43  ? 18   ILE E CD1 1 
ATOM   4542  N  N   . ASN E  1 19  ? 48.998  125.354 71.573  1.00 7.10  ? 19   ASN E N   1 
ATOM   4543  C  CA  . ASN E  1 19  ? 50.297  125.834 72.004  1.00 8.30  ? 19   ASN E CA  1 
ATOM   4544  C  C   . ASN E  1 19  ? 51.368  124.911 71.430  1.00 8.10  ? 19   ASN E C   1 
ATOM   4545  O  O   . ASN E  1 19  ? 51.115  123.725 71.230  1.00 8.14  ? 19   ASN E O   1 
ATOM   4546  C  CB  . ASN E  1 19  ? 50.376  125.765 73.539  1.00 8.58  ? 19   ASN E CB  1 
ATOM   4547  C  CG  . ASN E  1 19  ? 49.307  126.584 74.216  1.00 11.44 ? 19   ASN E CG  1 
ATOM   4548  O  OD1 . ASN E  1 19  ? 48.363  126.032 74.796  1.00 15.41 ? 19   ASN E OD1 1 
ATOM   4549  N  ND2 . ASN E  1 19  ? 49.425  127.891 74.136  1.00 5.48  ? 19   ASN E ND2 1 
ATOM   4550  N  N   . PHE E  1 20  ? 52.548  125.468 71.159  1.00 7.76  ? 20   PHE E N   1 
ATOM   4551  C  CA  . PHE E  1 20  ? 53.679  124.674 70.724  1.00 8.22  ? 20   PHE E CA  1 
ATOM   4552  C  C   . PHE E  1 20  ? 54.870  125.024 71.604  1.00 9.52  ? 20   PHE E C   1 
ATOM   4553  O  O   . PHE E  1 20  ? 55.102  126.216 71.897  1.00 8.79  ? 20   PHE E O   1 
ATOM   4554  C  CB  . PHE E  1 20  ? 54.070  124.992 69.294  1.00 9.40  ? 20   PHE E CB  1 
ATOM   4555  C  CG  . PHE E  1 20  ? 52.953  124.814 68.288  1.00 8.38  ? 20   PHE E CG  1 
ATOM   4556  C  CD1 . PHE E  1 20  ? 51.947  125.773 68.167  1.00 10.51 ? 20   PHE E CD1 1 
ATOM   4557  C  CD2 . PHE E  1 20  ? 52.910  123.701 67.456  1.00 9.60  ? 20   PHE E CD2 1 
ATOM   4558  C  CE1 . PHE E  1 20  ? 50.935  125.628 67.220  1.00 10.50 ? 20   PHE E CE1 1 
ATOM   4559  C  CE2 . PHE E  1 20  ? 51.883  123.536 66.528  1.00 8.44  ? 20   PHE E CE2 1 
ATOM   4560  C  CZ  . PHE E  1 20  ? 50.906  124.503 66.396  1.00 9.63  ? 20   PHE E CZ  1 
ATOM   4561  N  N   . GLU E  1 21  ? 55.635  124.003 71.982  1.00 9.10  ? 21   GLU E N   1 
ATOM   4562  C  CA  . GLU E  1 21  ? 56.825  124.261 72.811  1.00 11.39 ? 21   GLU E CA  1 
ATOM   4563  C  C   . GLU E  1 21  ? 57.951  123.364 72.354  1.00 12.01 ? 21   GLU E C   1 
ATOM   4564  O  O   . GLU E  1 21  ? 57.779  122.149 72.205  1.00 10.79 ? 21   GLU E O   1 
ATOM   4565  C  CB  . GLU E  1 21  ? 56.559  124.037 74.299  1.00 11.95 ? 21   GLU E CB  1 
ATOM   4566  C  CG  . GLU E  1 21  ? 57.774  124.426 75.153  1.00 17.51 ? 21   GLU E CG  1 
ATOM   4567  C  CD  . GLU E  1 21  ? 57.510  124.398 76.649  1.00 26.31 ? 21   GLU E CD  1 
ATOM   4568  O  OE1 . GLU E  1 21  ? 56.763  123.502 77.126  1.00 30.99 ? 21   GLU E OE1 1 
ATOM   4569  O  OE2 . GLU E  1 21  ? 58.088  125.258 77.350  1.00 30.66 ? 21   GLU E OE2 1 
ATOM   4570  N  N   . GLN E  1 22  ? 59.105  123.966 72.121  1.00 12.32 ? 22   GLN E N   1 
ATOM   4571  C  CA  . GLN E  1 22  ? 60.253  123.191 71.675  1.00 14.30 ? 22   GLN E CA  1 
ATOM   4572  C  C   . GLN E  1 22  ? 61.431  123.529 72.578  1.00 15.53 ? 22   GLN E C   1 
ATOM   4573  O  O   . GLN E  1 22  ? 61.996  124.612 72.483  1.00 15.65 ? 22   GLN E O   1 
ATOM   4574  C  CB  . GLN E  1 22  ? 60.552  123.505 70.210  1.00 13.03 ? 22   GLN E CB  1 
ATOM   4575  C  CG  . GLN E  1 22  ? 61.675  122.651 69.641  1.00 15.63 ? 22   GLN E CG  1 
ATOM   4576  C  CD  . GLN E  1 22  ? 61.894  122.908 68.163  1.00 15.30 ? 22   GLN E CD  1 
ATOM   4577  O  OE1 . GLN E  1 22  ? 61.764  124.047 67.692  1.00 15.35 ? 22   GLN E OE1 1 
ATOM   4578  N  NE2 . GLN E  1 22  ? 62.263  121.870 67.438  1.00 13.96 ? 22   GLN E NE2 1 
ATOM   4579  N  N   . LYS E  1 23  ? 61.767  122.599 73.461  1.00 18.01 ? 23   LYS E N   1 
ATOM   4580  C  CA  . LYS E  1 23  ? 62.783  122.837 74.485  1.00 21.42 ? 23   LYS E CA  1 
ATOM   4581  C  C   . LYS E  1 23  ? 64.176  122.974 73.909  1.00 22.29 ? 23   LYS E C   1 
ATOM   4582  O  O   . LYS E  1 23  ? 64.981  123.774 74.397  1.00 23.53 ? 23   LYS E O   1 
ATOM   4583  C  CB  . LYS E  1 23  ? 62.761  121.700 75.513  1.00 22.44 ? 23   LYS E CB  1 
ATOM   4584  C  CG  . LYS E  1 23  ? 61.604  121.765 76.522  1.00 25.04 ? 23   LYS E CG  1 
ATOM   4585  C  CD  . LYS E  1 23  ? 61.978  120.965 77.781  1.00 28.88 ? 23   LYS E CD  1 
ATOM   4586  N  N   . GLU E  1 24  ? 64.475  122.176 72.892  1.00 23.92 ? 24   GLU E N   1 
ATOM   4587  C  CA  . GLU E  1 24  ? 65.789  122.210 72.260  1.00 25.79 ? 24   GLU E CA  1 
ATOM   4588  C  C   . GLU E  1 24  ? 65.657  122.485 70.771  1.00 25.97 ? 24   GLU E C   1 
ATOM   4589  O  O   . GLU E  1 24  ? 64.731  121.986 70.114  1.00 25.62 ? 24   GLU E O   1 
ATOM   4590  C  CB  . GLU E  1 24  ? 66.509  120.859 72.401  1.00 26.25 ? 24   GLU E CB  1 
ATOM   4591  C  CG  . GLU E  1 24  ? 66.505  120.198 73.774  1.00 29.18 ? 24   GLU E CG  1 
ATOM   4592  C  CD  . GLU E  1 24  ? 67.102  118.791 73.709  1.00 33.42 ? 24   GLU E CD  1 
ATOM   4593  O  OE1 . GLU E  1 24  ? 67.242  118.267 72.576  1.00 35.23 ? 24   GLU E OE1 1 
ATOM   4594  O  OE2 . GLU E  1 24  ? 67.443  118.208 74.771  1.00 35.34 ? 24   GLU E OE2 1 
ATOM   4595  N  N   . SER E  1 25  ? 66.610  123.236 70.225  1.00 25.85 ? 25   SER E N   1 
ATOM   4596  C  CA  . SER E  1 25  ? 66.629  123.462 68.781  1.00 25.87 ? 25   SER E CA  1 
ATOM   4597  C  C   . SER E  1 25  ? 66.575  122.121 68.067  1.00 25.82 ? 25   SER E C   1 
ATOM   4598  O  O   . SER E  1 25  ? 67.377  121.243 68.341  1.00 26.16 ? 25   SER E O   1 
ATOM   4599  C  CB  . SER E  1 25  ? 67.904  124.222 68.371  1.00 26.36 ? 25   SER E CB  1 
ATOM   4600  O  OG  . SER E  1 25  ? 68.392  123.781 67.109  1.00 26.17 ? 25   SER E OG  1 
ATOM   4601  N  N   . ASN E  1 26  ? 65.626  121.971 67.149  1.00 25.74 ? 26   ASN E N   1 
ATOM   4602  C  CA  . ASN E  1 26  ? 65.456  120.742 66.382  1.00 24.92 ? 26   ASN E CA  1 
ATOM   4603  C  C   . ASN E  1 26  ? 64.925  119.573 67.192  1.00 23.28 ? 26   ASN E C   1 
ATOM   4604  O  O   . ASN E  1 26  ? 64.728  118.482 66.649  1.00 22.98 ? 26   ASN E O   1 
ATOM   4605  C  CB  . ASN E  1 26  ? 66.759  120.347 65.677  1.00 26.70 ? 26   ASN E CB  1 
ATOM   4606  C  CG  . ASN E  1 26  ? 66.852  120.908 64.266  1.00 29.85 ? 26   ASN E CG  1 
ATOM   4607  O  OD1 . ASN E  1 26  ? 66.430  122.042 64.004  1.00 36.73 ? 26   ASN E OD1 1 
ATOM   4608  N  ND2 . ASN E  1 26  ? 67.394  120.116 63.350  1.00 32.55 ? 26   ASN E ND2 1 
ATOM   4609  N  N   . GLY E  1 27  ? 64.684  119.795 68.481  1.00 21.12 ? 27   GLY E N   1 
ATOM   4610  C  CA  . GLY E  1 27  ? 64.172  118.737 69.331  1.00 19.16 ? 27   GLY E CA  1 
ATOM   4611  C  C   . GLY E  1 27  ? 62.687  118.557 69.099  1.00 17.58 ? 27   GLY E C   1 
ATOM   4612  O  O   . GLY E  1 27  ? 62.092  119.287 68.307  1.00 17.95 ? 27   GLY E O   1 
ATOM   4613  N  N   . PRO E  1 28  ? 62.085  117.608 69.809  1.00 16.11 ? 28   PRO E N   1 
ATOM   4614  C  CA  . PRO E  1 28  ? 60.645  117.338 69.695  1.00 14.65 ? 28   PRO E CA  1 
ATOM   4615  C  C   . PRO E  1 28  ? 59.837  118.575 70.054  1.00 13.56 ? 28   PRO E C   1 
ATOM   4616  O  O   . PRO E  1 28  ? 60.254  119.340 70.939  1.00 11.99 ? 28   PRO E O   1 
ATOM   4617  C  CB  . PRO E  1 28  ? 60.382  116.303 70.776  1.00 14.85 ? 28   PRO E CB  1 
ATOM   4618  C  CG  . PRO E  1 28  ? 61.712  115.756 71.163  1.00 16.58 ? 28   PRO E CG  1 
ATOM   4619  C  CD  . PRO E  1 28  ? 62.756  116.773 70.818  1.00 16.12 ? 28   PRO E CD  1 
ATOM   4620  N  N   . VAL E  1 29  ? 58.690  118.741 69.392  1.00 10.70 ? 29   VAL E N   1 
ATOM   4621  C  CA  . VAL E  1 29  ? 57.806  119.855 69.666  1.00 10.56 ? 29   VAL E CA  1 
ATOM   4622  C  C   . VAL E  1 29  ? 56.556  119.322 70.365  1.00 10.00 ? 29   VAL E C   1 
ATOM   4623  O  O   . VAL E  1 29  ? 55.925  118.394 69.856  1.00 10.25 ? 29   VAL E O   1 
ATOM   4624  C  CB  . VAL E  1 29  ? 57.334  120.537 68.367  1.00 10.66 ? 29   VAL E CB  1 
ATOM   4625  C  CG1 . VAL E  1 29  ? 56.362  121.687 68.716  1.00 10.16 ? 29   VAL E CG1 1 
ATOM   4626  C  CG2 . VAL E  1 29  ? 58.509  121.069 67.551  1.00 10.06 ? 29   VAL E CG2 1 
ATOM   4627  N  N   . LYS E  1 30  ? 56.224  119.869 71.530  1.00 9.77  ? 30   LYS E N   1 
ATOM   4628  C  CA  . LYS E  1 30  ? 54.991  119.484 72.215  1.00 9.56  ? 30   LYS E CA  1 
ATOM   4629  C  C   . LYS E  1 30  ? 53.911  120.383 71.651  1.00 9.64  ? 30   LYS E C   1 
ATOM   4630  O  O   . LYS E  1 30  ? 54.113  121.582 71.544  1.00 8.81  ? 30   LYS E O   1 
ATOM   4631  C  CB  . LYS E  1 30  ? 55.076  119.712 73.738  1.00 11.01 ? 30   LYS E CB  1 
ATOM   4632  C  CG  . LYS E  1 30  ? 55.795  118.582 74.459  1.00 15.99 ? 30   LYS E CG  1 
ATOM   4633  C  CD  . LYS E  1 30  ? 56.017  118.819 75.956  1.00 22.19 ? 30   LYS E CD  1 
ATOM   4634  C  CE  . LYS E  1 30  ? 57.197  117.959 76.429  1.00 23.69 ? 30   LYS E CE  1 
ATOM   4635  N  NZ  . LYS E  1 30  ? 57.382  117.930 77.907  1.00 25.43 ? 30   LYS E NZ  1 
ATOM   4636  N  N   . VAL E  1 31  ? 52.757  119.797 71.358  1.00 9.31  ? 31   VAL E N   1 
ATOM   4637  C  CA  . VAL E  1 31  ? 51.608  120.511 70.788  1.00 8.57  ? 31   VAL E CA  1 
ATOM   4638  C  C   . VAL E  1 31  ? 50.423  120.148 71.644  1.00 8.67  ? 31   VAL E C   1 
ATOM   4639  O  O   . VAL E  1 31  ? 50.094  118.963 71.786  1.00 8.58  ? 31   VAL E O   1 
ATOM   4640  C  CB  . VAL E  1 31  ? 51.330  120.028 69.359  1.00 9.11  ? 31   VAL E CB  1 
ATOM   4641  C  CG1 . VAL E  1 31  ? 50.194  120.846 68.717  1.00 9.88  ? 31   VAL E CG1 1 
ATOM   4642  C  CG2 . VAL E  1 31  ? 52.592  120.157 68.499  1.00 10.78 ? 31   VAL E CG2 1 
ATOM   4643  N  N   . TRP E  1 32  ? 49.779  121.142 72.232  1.00 8.72  ? 32   TRP E N   1 
ATOM   4644  C  CA  . TRP E  1 32  ? 48.688  120.847 73.144  1.00 9.22  ? 32   TRP E CA  1 
ATOM   4645  C  C   . TRP E  1 32  ? 47.761  122.035 73.272  1.00 9.34  ? 32   TRP E C   1 
ATOM   4646  O  O   . TRP E  1 32  ? 48.162  123.183 73.108  1.00 8.31  ? 32   TRP E O   1 
ATOM   4647  C  CB  . TRP E  1 32  ? 49.203  120.466 74.536  1.00 9.69  ? 32   TRP E CB  1 
ATOM   4648  C  CG  . TRP E  1 32  ? 49.587  121.624 75.395  1.00 10.92 ? 32   TRP E CG  1 
ATOM   4649  C  CD1 . TRP E  1 32  ? 48.842  122.207 76.385  1.00 13.40 ? 32   TRP E CD1 1 
ATOM   4650  C  CD2 . TRP E  1 32  ? 50.809  122.337 75.340  1.00 12.24 ? 32   TRP E CD2 1 
ATOM   4651  N  NE1 . TRP E  1 32  ? 49.546  123.247 76.954  1.00 16.18 ? 32   TRP E NE1 1 
ATOM   4652  C  CE2 . TRP E  1 32  ? 50.758  123.347 76.326  1.00 15.38 ? 32   TRP E CE2 1 
ATOM   4653  C  CE3 . TRP E  1 32  ? 51.945  122.246 74.533  1.00 14.11 ? 32   TRP E CE3 1 
ATOM   4654  C  CZ2 . TRP E  1 32  ? 51.791  124.248 76.528  1.00 17.10 ? 32   TRP E CZ2 1 
ATOM   4655  C  CZ3 . TRP E  1 32  ? 52.984  123.127 74.745  1.00 18.30 ? 32   TRP E CZ3 1 
ATOM   4656  C  CH2 . TRP E  1 32  ? 52.902  124.120 75.743  1.00 20.06 ? 32   TRP E CH2 1 
ATOM   4657  N  N   . GLY E  1 33  ? 46.517  121.761 73.619  1.00 9.60  ? 33   GLY E N   1 
ATOM   4658  C  CA  . GLY E  1 33  ? 45.562  122.843 73.770  1.00 10.14 ? 33   GLY E CA  1 
ATOM   4659  C  C   . GLY E  1 33  ? 44.187  122.250 73.623  1.00 11.68 ? 33   GLY E C   1 
ATOM   4660  O  O   . GLY E  1 33  ? 44.020  121.035 73.620  1.00 13.05 ? 33   GLY E O   1 
ATOM   4661  N  N   . SER E  1 34  ? 43.179  123.090 73.511  1.00 11.23 ? 34   SER E N   1 
ATOM   4662  C  CA  . SER E  1 34  ? 41.831  122.577 73.500  1.00 11.83 ? 34   SER E CA  1 
ATOM   4663  C  C   . SER E  1 34  ? 41.092  123.183 72.319  1.00 11.39 ? 34   SER E C   1 
ATOM   4664  O  O   . SER E  1 34  ? 41.233  124.389 72.058  1.00 12.43 ? 34   SER E O   1 
ATOM   4665  C  CB  . SER E  1 34  ? 41.155  122.978 74.828  1.00 13.32 ? 34   SER E CB  1 
ATOM   4666  O  OG  . SER E  1 34  ? 39.780  122.680 74.842  1.00 16.04 ? 34   SER E OG  1 
ATOM   4667  N  N   . ILE E  1 35  ? 40.368  122.353 71.582  1.00 9.49  ? 35   ILE E N   1 
ATOM   4668  C  CA  . ILE E  1 35  ? 39.532  122.833 70.509  1.00 9.67  ? 35   ILE E CA  1 
ATOM   4669  C  C   . ILE E  1 35  ? 38.107  122.433 70.841  1.00 8.73  ? 35   ILE E C   1 
ATOM   4670  O  O   . ILE E  1 35  ? 37.850  121.271 71.166  1.00 9.60  ? 35   ILE E O   1 
ATOM   4671  C  CB  . ILE E  1 35  ? 39.938  122.198 69.155  1.00 8.89  ? 35   ILE E CB  1 
ATOM   4672  C  CG1 . ILE E  1 35  ? 41.418  122.468 68.872  1.00 9.94  ? 35   ILE E CG1 1 
ATOM   4673  C  CG2 . ILE E  1 35  ? 39.102  122.779 68.021  1.00 10.35 ? 35   ILE E CG2 1 
ATOM   4674  C  CD1 . ILE E  1 35  ? 41.971  121.534 67.731  1.00 12.47 ? 35   ILE E CD1 1 
ATOM   4675  N  N   . LYS E  1 36  ? 37.182  123.375 70.776  1.00 8.66  ? 36   LYS E N   1 
ATOM   4676  C  CA  . LYS E  1 36  ? 35.794  123.024 71.059  1.00 9.83  ? 36   LYS E CA  1 
ATOM   4677  C  C   . LYS E  1 36  ? 34.903  123.103 69.820  1.00 9.61  ? 36   LYS E C   1 
ATOM   4678  O  O   . LYS E  1 36  ? 35.330  123.576 68.773  1.00 9.13  ? 36   LYS E O   1 
ATOM   4679  C  CB  . LYS E  1 36  ? 35.238  123.871 72.215  1.00 10.37 ? 36   LYS E CB  1 
ATOM   4680  C  CG  . LYS E  1 36  ? 34.876  125.300 71.885  1.00 15.73 ? 36   LYS E CG  1 
ATOM   4681  C  CD  . LYS E  1 36  ? 34.653  126.111 73.173  1.00 21.21 ? 36   LYS E CD  1 
ATOM   4682  C  CE  . LYS E  1 36  ? 33.769  127.343 72.967  1.00 24.34 ? 36   LYS E CE  1 
ATOM   4683  N  NZ  . LYS E  1 36  ? 33.743  128.197 74.217  1.00 26.38 ? 36   LYS E NZ  1 
ATOM   4684  N  N   . GLY E  1 37  ? 33.662  122.618 69.941  1.00 9.09  ? 37   GLY E N   1 
ATOM   4685  C  CA  . GLY E  1 37  ? 32.695  122.717 68.870  1.00 9.56  ? 37   GLY E CA  1 
ATOM   4686  C  C   . GLY E  1 37  ? 32.796  121.643 67.804  1.00 10.73 ? 37   GLY E C   1 
ATOM   4687  O  O   . GLY E  1 37  ? 32.190  121.778 66.756  1.00 10.35 ? 37   GLY E O   1 
ATOM   4688  N  N   . LEU E  1 38  ? 33.530  120.566 68.078  1.00 10.11 ? 38   LEU E N   1 
ATOM   4689  C  CA  . LEU E  1 38  ? 33.726  119.519 67.077  1.00 10.27 ? 38   LEU E CA  1 
ATOM   4690  C  C   . LEU E  1 38  ? 32.734  118.387 67.268  1.00 10.64 ? 38   LEU E C   1 
ATOM   4691  O  O   . LEU E  1 38  ? 32.200  118.192 68.371  1.00 9.88  ? 38   LEU E O   1 
ATOM   4692  C  CB  . LEU E  1 38  ? 35.134  118.941 67.218  1.00 10.19 ? 38   LEU E CB  1 
ATOM   4693  C  CG  . LEU E  1 38  ? 36.320  119.845 66.864  1.00 10.96 ? 38   LEU E CG  1 
ATOM   4694  C  CD1 . LEU E  1 38  ? 37.642  119.343 67.542  1.00 10.73 ? 38   LEU E CD1 1 
ATOM   4695  C  CD2 . LEU E  1 38  ? 36.464  119.913 65.332  1.00 7.11  ? 38   LEU E CD2 1 
ATOM   4696  N  N   . THR E  1 39  ? 32.460  117.657 66.189  1.00 11.02 ? 39   THR E N   1 
ATOM   4697  C  CA  . THR E  1 39  ? 31.713  116.423 66.335  1.00 11.34 ? 39   THR E CA  1 
ATOM   4698  C  C   . THR E  1 39  ? 32.603  115.363 66.997  1.00 11.73 ? 39   THR E C   1 
ATOM   4699  O  O   . THR E  1 39  ? 33.832  115.279 66.774  1.00 10.58 ? 39   THR E O   1 
ATOM   4700  C  CB  . THR E  1 39  ? 31.241  115.890 64.980  1.00 11.75 ? 39   THR E CB  1 
ATOM   4701  O  OG1 . THR E  1 39  ? 32.378  115.699 64.126  1.00 11.47 ? 39   THR E OG1 1 
ATOM   4702  C  CG2 . THR E  1 39  ? 30.361  116.923 64.283  1.00 12.04 ? 39   THR E CG2 1 
ATOM   4703  N  N   . GLU E  1 40  ? 31.962  114.492 67.764  1.00 11.28 ? 40   GLU E N   1 
ATOM   4704  C  CA  . GLU E  1 40  ? 32.692  113.449 68.449  1.00 12.36 ? 40   GLU E CA  1 
ATOM   4705  C  C   . GLU E  1 40  ? 33.460  112.608 67.435  1.00 12.12 ? 40   GLU E C   1 
ATOM   4706  O  O   . GLU E  1 40  ? 32.946  112.259 66.381  1.00 13.02 ? 40   GLU E O   1 
ATOM   4707  C  CB  . GLU E  1 40  ? 31.723  112.578 69.273  1.00 13.16 ? 40   GLU E CB  1 
ATOM   4708  C  CG  . GLU E  1 40  ? 32.437  111.542 70.125  1.00 14.17 ? 40   GLU E CG  1 
ATOM   4709  C  CD  . GLU E  1 40  ? 31.475  110.705 70.938  1.00 17.62 ? 40   GLU E CD  1 
ATOM   4710  O  OE1 . GLU E  1 40  ? 30.259  110.884 70.769  1.00 14.71 ? 40   GLU E OE1 1 
ATOM   4711  O  OE2 . GLU E  1 40  ? 31.942  109.855 71.720  1.00 22.13 ? 40   GLU E OE2 1 
ATOM   4712  N  N   . GLY E  1 41  ? 34.694  112.284 67.747  1.00 11.12 ? 41   GLY E N   1 
ATOM   4713  C  CA  . GLY E  1 41  ? 35.463  111.441 66.855  1.00 12.71 ? 41   GLY E CA  1 
ATOM   4714  C  C   . GLY E  1 41  ? 36.752  112.078 66.371  1.00 11.88 ? 41   GLY E C   1 
ATOM   4715  O  O   . GLY E  1 41  ? 37.185  113.117 66.896  1.00 11.73 ? 41   GLY E O   1 
ATOM   4716  N  N   . LEU E  1 42  ? 37.357  111.448 65.357  1.00 11.78 ? 42   LEU E N   1 
ATOM   4717  C  CA  . LEU E  1 42  ? 38.651  111.843 64.827  1.00 11.07 ? 42   LEU E CA  1 
ATOM   4718  C  C   . LEU E  1 42  ? 38.537  112.965 63.814  1.00 10.78 ? 42   LEU E C   1 
ATOM   4719  O  O   . LEU E  1 42  ? 37.624  112.990 62.972  1.00 10.16 ? 42   LEU E O   1 
ATOM   4720  C  CB  . LEU E  1 42  ? 39.292  110.647 64.099  1.00 11.57 ? 42   LEU E CB  1 
ATOM   4721  C  CG  . LEU E  1 42  ? 39.598  109.393 64.924  1.00 11.91 ? 42   LEU E CG  1 
ATOM   4722  C  CD1 . LEU E  1 42  ? 39.824  108.243 63.958  1.00 12.79 ? 42   LEU E CD1 1 
ATOM   4723  C  CD2 . LEU E  1 42  ? 40.866  109.727 65.654  1.00 13.29 ? 42   LEU E CD2 1 
ATOM   4724  N  N   . HIS E  1 43  ? 39.496  113.878 63.865  1.00 8.76  ? 43   HIS E N   1 
ATOM   4725  C  CA  . HIS E  1 43  ? 39.521  115.019 62.960  1.00 7.78  ? 43   HIS E CA  1 
ATOM   4726  C  C   . HIS E  1 43  ? 40.973  115.234 62.512  1.00 8.47  ? 43   HIS E C   1 
ATOM   4727  O  O   . HIS E  1 43  ? 41.882  115.346 63.352  1.00 7.81  ? 43   HIS E O   1 
ATOM   4728  C  CB  . HIS E  1 43  ? 38.989  116.287 63.654  1.00 7.62  ? 43   HIS E CB  1 
ATOM   4729  C  CG  . HIS E  1 43  ? 37.540  116.196 64.038  1.00 8.41  ? 43   HIS E CG  1 
ATOM   4730  N  ND1 . HIS E  1 43  ? 36.534  116.618 63.202  1.00 11.50 ? 43   HIS E ND1 1 
ATOM   4731  C  CD2 . HIS E  1 43  ? 36.930  115.703 65.146  1.00 8.25  ? 43   HIS E CD2 1 
ATOM   4732  C  CE1 . HIS E  1 43  ? 35.360  116.404 63.780  1.00 12.47 ? 43   HIS E CE1 1 
ATOM   4733  N  NE2 . HIS E  1 43  ? 35.571  115.851 64.963  1.00 9.83  ? 43   HIS E NE2 1 
ATOM   4734  N  N   . GLY E  1 44  ? 41.174  115.337 61.196  1.00 6.87  ? 44   GLY E N   1 
ATOM   4735  C  CA  . GLY E  1 44  ? 42.497  115.607 60.633  1.00 6.45  ? 44   GLY E CA  1 
ATOM   4736  C  C   . GLY E  1 44  ? 43.084  116.900 61.202  1.00 7.10  ? 44   GLY E C   1 
ATOM   4737  O  O   . GLY E  1 44  ? 42.357  117.871 61.438  1.00 6.70  ? 44   GLY E O   1 
ATOM   4738  N  N   . PHE E  1 45  ? 44.401  116.932 61.403  1.00 6.04  ? 45   PHE E N   1 
ATOM   4739  C  CA  . PHE E  1 45  ? 45.019  118.061 62.113  1.00 7.06  ? 45   PHE E CA  1 
ATOM   4740  C  C   . PHE E  1 45  ? 46.382  118.273 61.473  1.00 6.57  ? 45   PHE E C   1 
ATOM   4741  O  O   . PHE E  1 45  ? 47.273  117.432 61.611  1.00 8.05  ? 45   PHE E O   1 
ATOM   4742  C  CB  . PHE E  1 45  ? 45.125  117.638 63.577  1.00 6.93  ? 45   PHE E CB  1 
ATOM   4743  C  CG  . PHE E  1 45  ? 45.615  118.720 64.544  1.00 6.94  ? 45   PHE E CG  1 
ATOM   4744  C  CD1 . PHE E  1 45  ? 44.871  119.872 64.756  1.00 9.19  ? 45   PHE E CD1 1 
ATOM   4745  C  CD2 . PHE E  1 45  ? 46.784  118.531 65.244  1.00 8.84  ? 45   PHE E CD2 1 
ATOM   4746  C  CE1 . PHE E  1 45  ? 45.287  120.845 65.687  1.00 10.89 ? 45   PHE E CE1 1 
ATOM   4747  C  CE2 . PHE E  1 45  ? 47.206  119.513 66.221  1.00 7.35  ? 45   PHE E CE2 1 
ATOM   4748  C  CZ  . PHE E  1 45  ? 46.462  120.650 66.392  1.00 10.43 ? 45   PHE E CZ  1 
ATOM   4749  N  N   . HIS E  1 46  ? 46.545  119.379 60.741  1.00 6.69  ? 46   HIS E N   1 
ATOM   4750  C  CA  . HIS E  1 46  ? 47.725  119.549 59.911  1.00 7.33  ? 46   HIS E CA  1 
ATOM   4751  C  C   . HIS E  1 46  ? 48.264  120.957 59.913  1.00 7.51  ? 46   HIS E C   1 
ATOM   4752  O  O   . HIS E  1 46  ? 47.496  121.925 60.078  1.00 7.63  ? 46   HIS E O   1 
ATOM   4753  C  CB  . HIS E  1 46  ? 47.363  119.278 58.437  1.00 8.46  ? 46   HIS E CB  1 
ATOM   4754  C  CG  . HIS E  1 46  ? 46.616  118.001 58.203  1.00 7.67  ? 46   HIS E CG  1 
ATOM   4755  N  ND1 . HIS E  1 46  ? 45.405  117.961 57.553  1.00 6.17  ? 46   HIS E ND1 1 
ATOM   4756  C  CD2 . HIS E  1 46  ? 46.903  116.719 58.532  1.00 8.50  ? 46   HIS E CD2 1 
ATOM   4757  C  CE1 . HIS E  1 46  ? 44.985  116.717 57.449  1.00 6.49  ? 46   HIS E CE1 1 
ATOM   4758  N  NE2 . HIS E  1 46  ? 45.858  115.939 58.069  1.00 7.08  ? 46   HIS E NE2 1 
ATOM   4759  N  N   . VAL E  1 47  ? 49.554  121.065 59.605  1.00 7.28  ? 47   VAL E N   1 
ATOM   4760  C  CA  . VAL E  1 47  ? 50.127  122.367 59.288  1.00 6.66  ? 47   VAL E CA  1 
ATOM   4761  C  C   . VAL E  1 47  ? 50.097  122.513 57.783  1.00 6.86  ? 47   VAL E C   1 
ATOM   4762  O  O   . VAL E  1 47  ? 50.652  121.675 57.056  1.00 6.44  ? 47   VAL E O   1 
ATOM   4763  C  CB  . VAL E  1 47  ? 51.560  122.534 59.803  1.00 7.16  ? 47   VAL E CB  1 
ATOM   4764  C  CG1 . VAL E  1 47  ? 52.122  123.908 59.413  1.00 6.40  ? 47   VAL E CG1 1 
ATOM   4765  C  CG2 . VAL E  1 47  ? 51.582  122.329 61.351  1.00 7.48  ? 47   VAL E CG2 1 
ATOM   4766  N  N   . HIS E  1 48  ? 49.417  123.564 57.342  1.00 7.12  ? 48   HIS E N   1 
ATOM   4767  C  CA  . HIS E  1 48  ? 49.333  123.932 55.929  1.00 6.98  ? 48   HIS E CA  1 
ATOM   4768  C  C   . HIS E  1 48  ? 50.403  124.945 55.616  1.00 7.95  ? 48   HIS E C   1 
ATOM   4769  O  O   . HIS E  1 48  ? 50.945  125.590 56.522  1.00 8.58  ? 48   HIS E O   1 
ATOM   4770  C  CB  . HIS E  1 48  ? 47.928  124.384 55.554  1.00 5.84  ? 48   HIS E CB  1 
ATOM   4771  C  CG  . HIS E  1 48  ? 46.948  123.238 55.512  1.00 5.00  ? 48   HIS E CG  1 
ATOM   4772  N  ND1 . HIS E  1 48  ? 46.215  122.923 54.395  1.00 5.96  ? 48   HIS E ND1 1 
ATOM   4773  C  CD2 . HIS E  1 48  ? 46.586  122.339 56.465  1.00 7.18  ? 48   HIS E CD2 1 
ATOM   4774  C  CE1 . HIS E  1 48  ? 45.450  121.865 54.648  1.00 8.98  ? 48   HIS E CE1 1 
ATOM   4775  N  NE2 . HIS E  1 48  ? 45.656  121.496 55.896  1.00 5.21  ? 48   HIS E NE2 1 
ATOM   4776  N  N   . GLU E  1 49  ? 50.700  125.070 54.328  1.00 7.75  ? 49   GLU E N   1 
ATOM   4777  C  CA  . GLU E  1 49  ? 51.880  125.795 53.856  1.00 8.72  ? 49   GLU E CA  1 
ATOM   4778  C  C   . GLU E  1 49  ? 51.899  127.285 54.127  1.00 8.52  ? 49   GLU E C   1 
ATOM   4779  O  O   . GLU E  1 49  ? 52.932  127.796 54.592  1.00 8.69  ? 49   GLU E O   1 
ATOM   4780  C  CB  . GLU E  1 49  ? 52.088  125.536 52.365  1.00 9.14  ? 49   GLU E CB  1 
ATOM   4781  C  CG  . GLU E  1 49  ? 53.402  126.146 51.873  1.00 10.30 ? 49   GLU E CG  1 
ATOM   4782  C  CD  . GLU E  1 49  ? 53.731  125.789 50.448  1.00 15.12 ? 49   GLU E CD  1 
ATOM   4783  O  OE1 . GLU E  1 49  ? 52.933  125.031 49.818  1.00 12.91 ? 49   GLU E OE1 1 
ATOM   4784  O  OE2 . GLU E  1 49  ? 54.774  126.297 49.976  1.00 13.23 ? 49   GLU E OE2 1 
ATOM   4785  N  N   . PHE E  1 50  ? 50.779  127.971 53.884  1.00 7.64  ? 50   PHE E N   1 
ATOM   4786  C  CA  . PHE E  1 50  ? 50.754  129.439 53.992  1.00 8.43  ? 50   PHE E CA  1 
ATOM   4787  C  C   . PHE E  1 50  ? 49.939  129.964 55.150  1.00 9.20  ? 50   PHE E C   1 
ATOM   4788  O  O   . PHE E  1 50  ? 48.884  129.438 55.439  1.00 9.77  ? 50   PHE E O   1 
ATOM   4789  C  CB  . PHE E  1 50  ? 50.181  130.023 52.705  1.00 8.65  ? 50   PHE E CB  1 
ATOM   4790  C  CG  . PHE E  1 50  ? 50.909  129.553 51.490  1.00 9.82  ? 50   PHE E CG  1 
ATOM   4791  C  CD1 . PHE E  1 50  ? 52.236  129.887 51.304  1.00 11.00 ? 50   PHE E CD1 1 
ATOM   4792  C  CD2 . PHE E  1 50  ? 50.285  128.728 50.565  1.00 12.89 ? 50   PHE E CD2 1 
ATOM   4793  C  CE1 . PHE E  1 50  ? 52.934  129.412 50.165  1.00 12.65 ? 50   PHE E CE1 1 
ATOM   4794  C  CE2 . PHE E  1 50  ? 50.976  128.260 49.441  1.00 13.15 ? 50   PHE E CE2 1 
ATOM   4795  C  CZ  . PHE E  1 50  ? 52.282  128.593 49.261  1.00 11.12 ? 50   PHE E CZ  1 
ATOM   4796  N  N   . GLY E  1 51  ? 50.452  131.002 55.797  1.00 9.62  ? 51   GLY E N   1 
ATOM   4797  C  CA  . GLY E  1 51  ? 49.762  131.665 56.887  1.00 9.62  ? 51   GLY E CA  1 
ATOM   4798  C  C   . GLY E  1 51  ? 48.907  132.771 56.291  1.00 10.35 ? 51   GLY E C   1 
ATOM   4799  O  O   . GLY E  1 51  ? 48.973  133.938 56.672  1.00 11.24 ? 51   GLY E O   1 
ATOM   4800  N  N   . ASP E  1 52  ? 48.098  132.397 55.311  1.00 10.27 ? 52   ASP E N   1 
ATOM   4801  C  CA  . ASP E  1 52  ? 47.336  133.361 54.542  1.00 10.95 ? 52   ASP E CA  1 
ATOM   4802  C  C   . ASP E  1 52  ? 45.869  133.082 54.779  1.00 11.39 ? 52   ASP E C   1 
ATOM   4803  O  O   . ASP E  1 52  ? 45.360  132.063 54.336  1.00 10.10 ? 52   ASP E O   1 
ATOM   4804  C  CB  . ASP E  1 52  ? 47.672  133.199 53.048  1.00 10.64 ? 52   ASP E CB  1 
ATOM   4805  C  CG  . ASP E  1 52  ? 46.886  134.130 52.164  1.00 11.80 ? 52   ASP E CG  1 
ATOM   4806  O  OD1 . ASP E  1 52  ? 45.826  134.655 52.569  1.00 12.81 ? 52   ASP E OD1 1 
ATOM   4807  O  OD2 . ASP E  1 52  ? 47.262  134.408 51.018  1.00 14.23 ? 52   ASP E OD2 1 
ATOM   4808  N  N   . ASN E  1 53  ? 45.200  133.983 55.486  1.00 12.06 ? 53   ASN E N   1 
ATOM   4809  C  CA  . ASN E  1 53  ? 43.803  133.791 55.843  1.00 13.05 ? 53   ASN E CA  1 
ATOM   4810  C  C   . ASN E  1 53  ? 42.892  134.723 55.059  1.00 13.36 ? 53   ASN E C   1 
ATOM   4811  O  O   . ASN E  1 53  ? 41.755  134.979 55.463  1.00 13.42 ? 53   ASN E O   1 
ATOM   4812  C  CB  . ASN E  1 53  ? 43.619  134.054 57.339  1.00 15.22 ? 53   ASN E CB  1 
ATOM   4813  C  CG  . ASN E  1 53  ? 42.279  133.564 57.855  1.00 18.47 ? 53   ASN E CG  1 
ATOM   4814  O  OD1 . ASN E  1 53  ? 41.891  132.429 57.613  1.00 23.36 ? 53   ASN E OD1 1 
ATOM   4815  N  ND2 . ASN E  1 53  ? 41.565  134.423 58.553  1.00 23.22 ? 53   ASN E ND2 1 
ATOM   4816  N  N   . THR E  1 54  ? 43.388  135.267 53.955  1.00 12.95 ? 54   THR E N   1 
ATOM   4817  C  CA  . THR E  1 54  ? 42.613  136.252 53.215  1.00 13.70 ? 54   THR E CA  1 
ATOM   4818  C  C   . THR E  1 54  ? 41.284  135.689 52.672  1.00 15.03 ? 54   THR E C   1 
ATOM   4819  O  O   . THR E  1 54  ? 40.351  136.428 52.431  1.00 16.15 ? 54   THR E O   1 
ATOM   4820  C  CB  . THR E  1 54  ? 43.449  136.868 52.065  1.00 14.13 ? 54   THR E CB  1 
ATOM   4821  O  OG1 . THR E  1 54  ? 43.939  135.833 51.196  1.00 10.58 ? 54   THR E OG1 1 
ATOM   4822  C  CG2 . THR E  1 54  ? 44.706  137.535 52.610  1.00 14.94 ? 54   THR E CG2 1 
ATOM   4823  N  N   . ALA E  1 55  ? 41.205  134.382 52.500  1.00 15.38 ? 55   ALA E N   1 
ATOM   4824  C  CA  . ALA E  1 55  ? 39.963  133.769 52.034  1.00 16.10 ? 55   ALA E CA  1 
ATOM   4825  C  C   . ALA E  1 55  ? 39.625  132.631 52.965  1.00 16.05 ? 55   ALA E C   1 
ATOM   4826  O  O   . ALA E  1 55  ? 39.285  131.524 52.518  1.00 17.78 ? 55   ALA E O   1 
ATOM   4827  C  CB  . ALA E  1 55  ? 40.112  133.276 50.586  1.00 16.11 ? 55   ALA E CB  1 
ATOM   4828  N  N   . GLY E  1 56  ? 39.738  132.881 54.266  1.00 15.51 ? 56   GLY E N   1 
ATOM   4829  C  CA  . GLY E  1 56  ? 39.469  131.862 55.266  1.00 15.14 ? 56   GLY E CA  1 
ATOM   4830  C  C   . GLY E  1 56  ? 40.524  130.751 55.198  1.00 14.53 ? 56   GLY E C   1 
ATOM   4831  O  O   . GLY E  1 56  ? 41.625  130.961 54.719  1.00 14.61 ? 56   GLY E O   1 
ATOM   4832  N  N   . CYS E  1 57  ? 40.153  129.541 55.587  1.00 13.57 ? 57   CYS E N   1 
ATOM   4833  C  CA  . CYS E  1 57  ? 41.124  128.471 55.636  1.00 13.33 ? 57   CYS E CA  1 
ATOM   4834  C  C   . CYS E  1 57  ? 41.588  128.010 54.260  1.00 11.87 ? 57   CYS E C   1 
ATOM   4835  O  O   . CYS E  1 57  ? 42.643  127.442 54.129  1.00 11.24 ? 57   CYS E O   1 
ATOM   4836  C  CB  . CYS E  1 57  ? 40.557  127.314 56.456  1.00 14.14 ? 57   CYS E CB  1 
ATOM   4837  S  SG  . CYS E  1 57  ? 40.215  127.919 58.098  1.00 19.17 ? 57   CYS E SG  1 
ATOM   4838  N  N   . THR E  1 58  ? 40.803  128.280 53.239  1.00 11.29 ? 58   THR E N   1 
ATOM   4839  C  CA  . THR E  1 58  ? 41.157  127.890 51.890  1.00 12.12 ? 58   THR E CA  1 
ATOM   4840  C  C   . THR E  1 58  ? 42.488  128.471 51.392  1.00 11.58 ? 58   THR E C   1 
ATOM   4841  O  O   . THR E  1 58  ? 43.246  127.786 50.687  1.00 10.67 ? 58   THR E O   1 
ATOM   4842  C  CB  . THR E  1 58  ? 40.002  128.287 50.960  1.00 12.59 ? 58   THR E CB  1 
ATOM   4843  O  OG1 . THR E  1 58  ? 38.897  127.417 51.254  1.00 17.26 ? 58   THR E OG1 1 
ATOM   4844  C  CG2 . THR E  1 58  ? 40.341  127.977 49.486  1.00 13.35 ? 58   THR E CG2 1 
ATOM   4845  N  N   . SER E  1 59  ? 42.796  129.712 51.779  1.00 9.96  ? 59   SER E N   1 
ATOM   4846  C  CA  . SER E  1 59  ? 44.032  130.346 51.318  1.00 10.85 ? 59   SER E CA  1 
ATOM   4847  C  C   . SER E  1 59  ? 45.298  129.825 52.015  1.00 10.64 ? 59   SER E C   1 
ATOM   4848  O  O   . SER E  1 59  ? 46.404  130.181 51.637  1.00 10.30 ? 59   SER E O   1 
ATOM   4849  C  CB  . SER E  1 59  ? 43.932  131.893 51.339  1.00 10.69 ? 59   SER E CB  1 
ATOM   4850  O  OG  . SER E  1 59  ? 43.352  132.317 52.542  1.00 14.64 ? 59   SER E OG  1 
ATOM   4851  N  N   . ALA E  1 60  ? 45.134  128.928 52.979  1.00 10.22 ? 60   ALA E N   1 
ATOM   4852  C  CA  . ALA E  1 60  ? 46.298  128.290 53.614  1.00 10.27 ? 60   ALA E CA  1 
ATOM   4853  C  C   . ALA E  1 60  ? 47.062  127.348 52.659  1.00 9.47  ? 60   ALA E C   1 
ATOM   4854  O  O   . ALA E  1 60  ? 48.191  126.951 52.930  1.00 8.08  ? 60   ALA E O   1 
ATOM   4855  C  CB  . ALA E  1 60  ? 45.865  127.528 54.866  1.00 10.38 ? 60   ALA E CB  1 
ATOM   4856  N  N   . GLY E  1 61  ? 46.472  127.007 51.520  1.00 8.83  ? 61   GLY E N   1 
ATOM   4857  C  CA  . GLY E  1 61  ? 47.203  126.134 50.609  1.00 9.15  ? 61   GLY E CA  1 
ATOM   4858  C  C   . GLY E  1 61  ? 47.169  124.685 51.115  1.00 10.16 ? 61   GLY E C   1 
ATOM   4859  O  O   . GLY E  1 61  ? 46.388  124.344 52.006  1.00 9.96  ? 61   GLY E O   1 
ATOM   4860  N  N   . PRO E  1 62  ? 48.053  123.859 50.582  1.00 9.28  ? 62   PRO E N   1 
ATOM   4861  C  CA  . PRO E  1 62  ? 48.110  122.435 50.911  1.00 9.52  ? 62   PRO E CA  1 
ATOM   4862  C  C   . PRO E  1 62  ? 48.974  122.186 52.136  1.00 9.97  ? 62   PRO E C   1 
ATOM   4863  O  O   . PRO E  1 62  ? 49.388  123.138 52.821  1.00 9.29  ? 62   PRO E O   1 
ATOM   4864  C  CB  . PRO E  1 62  ? 48.767  121.857 49.656  1.00 9.42  ? 62   PRO E CB  1 
ATOM   4865  C  CG  . PRO E  1 62  ? 49.758  122.929 49.302  1.00 9.83  ? 62   PRO E CG  1 
ATOM   4866  C  CD  . PRO E  1 62  ? 49.103  124.241 49.621  1.00 9.57  ? 62   PRO E CD  1 
ATOM   4867  N  N   . HIS E  1 63  ? 49.240  120.916 52.413  1.00 10.16 ? 63   HIS E N   1 
ATOM   4868  C  CA  . HIS E  1 63  ? 50.045  120.578 53.581  1.00 9.50  ? 63   HIS E CA  1 
ATOM   4869  C  C   . HIS E  1 63  ? 51.445  121.087 53.394  1.00 10.12 ? 63   HIS E C   1 
ATOM   4870  O  O   . HIS E  1 63  ? 51.969  121.085 52.264  1.00 9.92  ? 63   HIS E O   1 
ATOM   4871  C  CB  . HIS E  1 63  ? 50.016  119.060 53.860  1.00 9.27  ? 63   HIS E CB  1 
ATOM   4872  C  CG  . HIS E  1 63  ? 48.662  118.575 54.285  1.00 11.37 ? 63   HIS E CG  1 
ATOM   4873  N  ND1 . HIS E  1 63  ? 48.361  117.246 54.500  1.00 9.55  ? 63   HIS E ND1 1 
ATOM   4874  C  CD2 . HIS E  1 63  ? 47.510  119.264 54.468  1.00 11.70 ? 63   HIS E CD2 1 
ATOM   4875  C  CE1 . HIS E  1 63  ? 47.082  117.145 54.814  1.00 12.72 ? 63   HIS E CE1 1 
ATOM   4876  N  NE2 . HIS E  1 63  ? 46.545  118.353 54.801  1.00 15.44 ? 63   HIS E NE2 1 
ATOM   4877  N  N   . PHE E  1 64  ? 52.035  121.570 54.491  1.00 9.31  ? 64   PHE E N   1 
ATOM   4878  C  CA  . PHE E  1 64  ? 53.432  122.012 54.482  1.00 9.94  ? 64   PHE E CA  1 
ATOM   4879  C  C   . PHE E  1 64  ? 54.273  120.779 54.164  1.00 10.16 ? 64   PHE E C   1 
ATOM   4880  O  O   . PHE E  1 64  ? 54.235  119.798 54.878  1.00 10.29 ? 64   PHE E O   1 
ATOM   4881  C  CB  . PHE E  1 64  ? 53.803  122.618 55.856  1.00 9.80  ? 64   PHE E CB  1 
ATOM   4882  C  CG  . PHE E  1 64  ? 55.230  123.096 55.952  1.00 11.37 ? 64   PHE E CG  1 
ATOM   4883  C  CD1 . PHE E  1 64  ? 55.815  123.815 54.907  1.00 11.87 ? 64   PHE E CD1 1 
ATOM   4884  C  CD2 . PHE E  1 64  ? 55.974  122.855 57.107  1.00 13.76 ? 64   PHE E CD2 1 
ATOM   4885  C  CE1 . PHE E  1 64  ? 57.139  124.261 55.010  1.00 12.15 ? 64   PHE E CE1 1 
ATOM   4886  C  CE2 . PHE E  1 64  ? 57.308  123.313 57.230  1.00 13.42 ? 64   PHE E CE2 1 
ATOM   4887  C  CZ  . PHE E  1 64  ? 57.883  124.013 56.176  1.00 14.24 ? 64   PHE E CZ  1 
ATOM   4888  N  N   . ASN E  1 65  ? 55.050  120.851 53.090  1.00 10.80 ? 65   ASN E N   1 
ATOM   4889  C  CA  . ASN E  1 65  ? 55.724  119.678 52.540  1.00 11.34 ? 65   ASN E CA  1 
ATOM   4890  C  C   . ASN E  1 65  ? 57.007  120.095 51.836  1.00 12.29 ? 65   ASN E C   1 
ATOM   4891  O  O   . ASN E  1 65  ? 57.131  119.997 50.600  1.00 12.94 ? 65   ASN E O   1 
ATOM   4892  C  CB  . ASN E  1 65  ? 54.769  119.084 51.511  1.00 11.17 ? 65   ASN E CB  1 
ATOM   4893  C  CG  . ASN E  1 65  ? 55.250  117.765 50.917  1.00 11.87 ? 65   ASN E CG  1 
ATOM   4894  O  OD1 . ASN E  1 65  ? 56.030  117.017 51.516  1.00 10.24 ? 65   ASN E OD1 1 
ATOM   4895  N  ND2 . ASN E  1 65  ? 54.726  117.456 49.743  1.00 11.43 ? 65   ASN E ND2 1 
ATOM   4896  N  N   . PRO E  1 66  ? 57.967  120.569 52.608  1.00 12.64 ? 66   PRO E N   1 
ATOM   4897  C  CA  . PRO E  1 66  ? 59.230  121.035 52.037  1.00 14.07 ? 66   PRO E CA  1 
ATOM   4898  C  C   . PRO E  1 66  ? 60.029  119.902 51.391  1.00 14.58 ? 66   PRO E C   1 
ATOM   4899  O  O   . PRO E  1 66  ? 60.869  120.186 50.546  1.00 15.11 ? 66   PRO E O   1 
ATOM   4900  C  CB  . PRO E  1 66  ? 59.960  121.601 53.248  1.00 13.75 ? 66   PRO E CB  1 
ATOM   4901  C  CG  . PRO E  1 66  ? 59.390  120.831 54.376  1.00 14.57 ? 66   PRO E CG  1 
ATOM   4902  C  CD  . PRO E  1 66  ? 57.925  120.760 54.063  1.00 13.04 ? 66   PRO E CD  1 
ATOM   4903  N  N   . LEU E  1 67  ? 59.796  118.654 51.762  1.00 15.16 ? 67   LEU E N   1 
ATOM   4904  C  CA  . LEU E  1 67  ? 60.549  117.590 51.111  1.00 16.02 ? 67   LEU E CA  1 
ATOM   4905  C  C   . LEU E  1 67  ? 59.780  116.889 49.995  1.00 16.18 ? 67   LEU E C   1 
ATOM   4906  O  O   . LEU E  1 67  ? 60.179  115.824 49.566  1.00 15.69 ? 67   LEU E O   1 
ATOM   4907  C  CB  . LEU E  1 67  ? 61.039  116.576 52.131  1.00 16.58 ? 67   LEU E CB  1 
ATOM   4908  C  CG  . LEU E  1 67  ? 61.785  117.192 53.312  1.00 17.74 ? 67   LEU E CG  1 
ATOM   4909  C  CD1 . LEU E  1 67  ? 62.025  116.126 54.358  1.00 18.01 ? 67   LEU E CD1 1 
ATOM   4910  C  CD2 . LEU E  1 67  ? 63.090  117.845 52.871  1.00 20.96 ? 67   LEU E CD2 1 
ATOM   4911  N  N   . SER E  1 68  ? 58.678  117.475 49.537  1.00 16.03 ? 68   SER E N   1 
ATOM   4912  C  CA  . SER E  1 68  ? 57.913  116.911 48.420  1.00 16.67 ? 68   SER E CA  1 
ATOM   4913  C  C   . SER E  1 68  ? 57.612  115.422 48.555  1.00 16.43 ? 68   SER E C   1 
ATOM   4914  O  O   . SER E  1 68  ? 57.850  114.621 47.623  1.00 15.46 ? 68   SER E O   1 
ATOM   4915  C  CB  . SER E  1 68  ? 58.625  117.181 47.076  1.00 17.31 ? 68   SER E CB  1 
ATOM   4916  O  OG  . SER E  1 68  ? 59.058  118.535 46.992  1.00 18.51 ? 68   SER E OG  1 
ATOM   4917  N  N   . ARG E  1 69  ? 57.091  115.031 49.709  1.00 15.57 ? 69   ARG E N   1 
ATOM   4918  C  CA  . ARG E  1 69  ? 56.709  113.652 49.900  1.00 15.41 ? 69   ARG E CA  1 
ATOM   4919  C  C   . ARG E  1 69  ? 55.198  113.514 49.786  1.00 14.90 ? 69   ARG E C   1 
ATOM   4920  O  O   . ARG E  1 69  ? 54.475  114.505 49.592  1.00 14.32 ? 69   ARG E O   1 
ATOM   4921  C  CB  . ARG E  1 69  ? 57.191  113.150 51.259  1.00 15.75 ? 69   ARG E CB  1 
ATOM   4922  C  CG  . ARG E  1 69  ? 58.654  113.406 51.524  1.00 17.68 ? 69   ARG E CG  1 
ATOM   4923  C  CD  . ARG E  1 69  ? 59.299  112.412 52.474  1.00 20.60 ? 69   ARG E CD  1 
ATOM   4924  N  NE  . ARG E  1 69  ? 60.755  112.471 52.377  1.00 22.04 ? 69   ARG E NE  1 
ATOM   4925  C  CZ  . ARG E  1 69  ? 61.579  112.156 53.363  1.00 24.04 ? 69   ARG E CZ  1 
ATOM   4926  N  NH1 . ARG E  1 69  ? 61.095  111.733 54.531  1.00 24.12 ? 69   ARG E NH1 1 
ATOM   4927  N  NH2 . ARG E  1 69  ? 62.892  112.242 53.181  1.00 22.95 ? 69   ARG E NH2 1 
ATOM   4928  N  N   . LYS E  1 70  ? 54.723  112.285 49.917  1.00 13.36 ? 70   LYS E N   1 
ATOM   4929  C  CA  . LYS E  1 70  ? 53.301  112.038 49.895  1.00 13.17 ? 70   LYS E CA  1 
ATOM   4930  C  C   . LYS E  1 70  ? 52.749  112.132 51.303  1.00 12.25 ? 70   LYS E C   1 
ATOM   4931  O  O   . LYS E  1 70  ? 53.489  112.066 52.289  1.00 10.90 ? 70   LYS E O   1 
ATOM   4932  C  CB  . LYS E  1 70  ? 52.989  110.669 49.310  1.00 14.46 ? 70   LYS E CB  1 
ATOM   4933  C  CG  . LYS E  1 70  ? 53.196  110.606 47.808  1.00 16.81 ? 70   LYS E CG  1 
ATOM   4934  C  CD  . LYS E  1 70  ? 53.255  109.153 47.369  1.00 22.06 ? 70   LYS E CD  1 
ATOM   4935  C  CE  . LYS E  1 70  ? 53.137  109.028 45.841  1.00 25.68 ? 70   LYS E CE  1 
ATOM   4936  N  N   . HIS E  1 71  ? 51.433  112.296 51.385  1.00 11.32 ? 71   HIS E N   1 
ATOM   4937  C  CA  . HIS E  1 71  ? 50.749  112.349 52.665  1.00 10.61 ? 71   HIS E CA  1 
ATOM   4938  C  C   . HIS E  1 71  ? 50.830  111.055 53.476  1.00 10.52 ? 71   HIS E C   1 
ATOM   4939  O  O   . HIS E  1 71  ? 50.675  109.928 52.936  1.00 10.40 ? 71   HIS E O   1 
ATOM   4940  C  CB  . HIS E  1 71  ? 49.284  112.714 52.460  1.00 9.84  ? 71   HIS E CB  1 
ATOM   4941  C  CG  . HIS E  1 71  ? 48.530  112.917 53.742  1.00 10.12 ? 71   HIS E CG  1 
ATOM   4942  N  ND1 . HIS E  1 71  ? 48.676  114.048 54.516  1.00 9.88  ? 71   HIS E ND1 1 
ATOM   4943  C  CD2 . HIS E  1 71  ? 47.635  112.125 54.391  1.00 10.70 ? 71   HIS E CD2 1 
ATOM   4944  C  CE1 . HIS E  1 71  ? 47.888  113.951 55.581  1.00 7.05  ? 71   HIS E CE1 1 
ATOM   4945  N  NE2 . HIS E  1 71  ? 47.247  112.795 55.526  1.00 7.45  ? 71   HIS E NE2 1 
ATOM   4946  N  N   . GLY E  1 72  ? 51.033  111.216 54.779  1.00 9.88  ? 72   GLY E N   1 
ATOM   4947  C  CA  . GLY E  1 72  ? 51.115  110.101 55.707  1.00 10.34 ? 72   GLY E CA  1 
ATOM   4948  C  C   . GLY E  1 72  ? 50.589  110.436 57.088  1.00 10.98 ? 72   GLY E C   1 
ATOM   4949  O  O   . GLY E  1 72  ? 49.933  111.483 57.290  1.00 10.62 ? 72   GLY E O   1 
ATOM   4950  N  N   . GLY E  1 73  ? 50.821  109.515 58.022  1.00 10.77 ? 73   GLY E N   1 
ATOM   4951  C  CA  . GLY E  1 73  ? 50.502  109.759 59.421  1.00 11.57 ? 73   GLY E CA  1 
ATOM   4952  C  C   . GLY E  1 73  ? 51.801  110.219 60.061  1.00 11.32 ? 73   GLY E C   1 
ATOM   4953  O  O   . GLY E  1 73  ? 52.847  110.116 59.434  1.00 10.36 ? 73   GLY E O   1 
ATOM   4954  N  N   . PRO E  1 74  ? 51.742  110.783 61.258  1.00 12.25 ? 74   PRO E N   1 
ATOM   4955  C  CA  . PRO E  1 74  ? 52.946  111.324 61.899  1.00 13.17 ? 74   PRO E CA  1 
ATOM   4956  C  C   . PRO E  1 74  ? 54.022  110.262 62.121  1.00 14.21 ? 74   PRO E C   1 
ATOM   4957  O  O   . PRO E  1 74  ? 55.177  110.597 62.068  1.00 14.67 ? 74   PRO E O   1 
ATOM   4958  C  CB  . PRO E  1 74  ? 52.462  111.793 63.264  1.00 12.85 ? 74   PRO E CB  1 
ATOM   4959  C  CG  . PRO E  1 74  ? 50.992  111.567 63.320  1.00 14.46 ? 74   PRO E CG  1 
ATOM   4960  C  CD  . PRO E  1 74  ? 50.518  111.003 62.042  1.00 11.89 ? 74   PRO E CD  1 
ATOM   4961  N  N   . LYS E  1 75  ? 53.655  109.020 62.405  1.00 15.19 ? 75   LYS E N   1 
ATOM   4962  C  CA  . LYS E  1 75  ? 54.686  107.994 62.617  1.00 17.39 ? 75   LYS E CA  1 
ATOM   4963  C  C   . LYS E  1 75  ? 55.311  107.435 61.324  1.00 17.97 ? 75   LYS E C   1 
ATOM   4964  O  O   . LYS E  1 75  ? 56.276  106.645 61.371  1.00 17.88 ? 75   LYS E O   1 
ATOM   4965  C  CB  . LYS E  1 75  ? 54.128  106.859 63.477  1.00 18.00 ? 75   LYS E CB  1 
ATOM   4966  C  CG  . LYS E  1 75  ? 53.469  107.329 64.758  1.00 19.78 ? 75   LYS E CG  1 
ATOM   4967  C  CD  . LYS E  1 75  ? 54.539  107.790 65.744  1.00 24.53 ? 75   LYS E CD  1 
ATOM   4968  N  N   . ASP E  1 76  ? 54.792  107.831 60.161  1.00 17.46 ? 76   ASP E N   1 
ATOM   4969  C  CA  . ASP E  1 76  ? 55.345  107.343 58.899  1.00 17.08 ? 76   ASP E CA  1 
ATOM   4970  C  C   . ASP E  1 76  ? 56.579  108.092 58.437  1.00 16.52 ? 76   ASP E C   1 
ATOM   4971  O  O   . ASP E  1 76  ? 56.700  109.287 58.643  1.00 16.81 ? 76   ASP E O   1 
ATOM   4972  C  CB  . ASP E  1 76  ? 54.322  107.476 57.771  1.00 16.85 ? 76   ASP E CB  1 
ATOM   4973  C  CG  . ASP E  1 76  ? 53.138  106.557 57.932  1.00 19.12 ? 76   ASP E CG  1 
ATOM   4974  O  OD1 . ASP E  1 76  ? 53.322  105.348 58.261  1.00 19.95 ? 76   ASP E OD1 1 
ATOM   4975  O  OD2 . ASP E  1 76  ? 51.968  106.931 57.714  1.00 17.52 ? 76   ASP E OD2 1 
ATOM   4976  N  N   . GLU E  1 77  ? 57.479  107.407 57.740  1.00 16.02 ? 77   GLU E N   1 
ATOM   4977  C  CA  . GLU E  1 77  ? 58.637  108.095 57.189  1.00 15.31 ? 77   GLU E CA  1 
ATOM   4978  C  C   . GLU E  1 77  ? 58.211  108.902 55.960  1.00 14.33 ? 77   GLU E C   1 
ATOM   4979  O  O   . GLU E  1 77  ? 58.677  110.030 55.742  1.00 14.44 ? 77   GLU E O   1 
ATOM   4980  C  CB  . GLU E  1 77  ? 59.731  107.093 56.829  1.00 16.53 ? 77   GLU E CB  1 
ATOM   4981  C  CG  . GLU E  1 77  ? 61.018  107.756 56.382  1.00 19.34 ? 77   GLU E CG  1 
ATOM   4982  C  CD  . GLU E  1 77  ? 60.924  108.417 55.013  1.00 23.85 ? 77   GLU E CD  1 
ATOM   4983  N  N   . GLU E  1 78  ? 57.314  108.330 55.161  1.00 12.75 ? 78   GLU E N   1 
ATOM   4984  C  CA  . GLU E  1 78  ? 56.751  109.042 54.034  1.00 12.51 ? 78   GLU E CA  1 
ATOM   4985  C  C   . GLU E  1 78  ? 55.575  109.848 54.581  1.00 12.27 ? 78   GLU E C   1 
ATOM   4986  O  O   . GLU E  1 78  ? 54.491  109.303 54.826  1.00 11.84 ? 78   GLU E O   1 
ATOM   4987  C  CB  . GLU E  1 78  ? 56.266  108.099 52.931  1.00 13.41 ? 78   GLU E CB  1 
ATOM   4988  C  CG  . GLU E  1 78  ? 55.718  108.790 51.680  1.00 15.53 ? 78   GLU E CG  1 
ATOM   4989  C  CD  . GLU E  1 78  ? 56.792  109.426 50.790  1.00 19.41 ? 78   GLU E CD  1 
ATOM   4990  O  OE1 . GLU E  1 78  ? 57.997  109.189 51.046  1.00 24.09 ? 78   GLU E OE1 1 
ATOM   4991  O  OE2 . GLU E  1 78  ? 56.437  110.150 49.816  1.00 17.52 ? 78   GLU E OE2 1 
ATOM   4992  N  N   . ARG E  1 79  ? 55.817  111.137 54.799  1.00 11.06 ? 79   ARG E N   1 
ATOM   4993  C  CA  . ARG E  1 79  ? 54.774  112.033 55.293  1.00 11.00 ? 79   ARG E CA  1 
ATOM   4994  C  C   . ARG E  1 79  ? 55.181  113.440 54.951  1.00 10.91 ? 79   ARG E C   1 
ATOM   4995  O  O   . ARG E  1 79  ? 56.350  113.706 54.697  1.00 10.89 ? 79   ARG E O   1 
ATOM   4996  C  CB  . ARG E  1 79  ? 54.624  111.925 56.808  1.00 10.05 ? 79   ARG E CB  1 
ATOM   4997  C  CG  . ARG E  1 79  ? 55.893  112.353 57.606  1.00 11.99 ? 79   ARG E CG  1 
ATOM   4998  C  CD  . ARG E  1 79  ? 55.666  112.519 59.092  1.00 11.20 ? 79   ARG E CD  1 
ATOM   4999  N  NE  . ARG E  1 79  ? 55.303  113.906 59.461  1.00 9.41  ? 79   ARG E NE  1 
ATOM   5000  C  CZ  . ARG E  1 79  ? 55.252  114.322 60.717  1.00 9.00  ? 79   ARG E CZ  1 
ATOM   5001  N  NH1 . ARG E  1 79  ? 55.508  113.475 61.701  1.00 9.22  ? 79   ARG E NH1 1 
ATOM   5002  N  NH2 . ARG E  1 79  ? 54.985  115.603 60.998  1.00 11.01 ? 79   ARG E NH2 1 
ATOM   5003  N  N   . HIS E  1 80  ? 54.210  114.342 54.971  1.00 10.50 ? 80   HIS E N   1 
ATOM   5004  C  CA  . HIS E  1 80  ? 54.480  115.763 54.837  1.00 10.00 ? 80   HIS E CA  1 
ATOM   5005  C  C   . HIS E  1 80  ? 54.952  116.255 56.185  1.00 10.09 ? 80   HIS E C   1 
ATOM   5006  O  O   . HIS E  1 80  ? 54.536  115.715 57.215  1.00 10.00 ? 80   HIS E O   1 
ATOM   5007  C  CB  . HIS E  1 80  ? 53.173  116.485 54.544  1.00 10.36 ? 80   HIS E CB  1 
ATOM   5008  C  CG  . HIS E  1 80  ? 52.532  116.090 53.255  1.00 10.45 ? 80   HIS E CG  1 
ATOM   5009  N  ND1 . HIS E  1 80  ? 51.161  116.012 53.092  1.00 7.57  ? 80   HIS E ND1 1 
ATOM   5010  C  CD2 . HIS E  1 80  ? 53.076  115.761 52.059  1.00 11.98 ? 80   HIS E CD2 1 
ATOM   5011  C  CE1 . HIS E  1 80  ? 50.892  115.702 51.838  1.00 12.33 ? 80   HIS E CE1 1 
ATOM   5012  N  NE2 . HIS E  1 80  ? 52.035  115.523 51.196  1.00 12.54 ? 80   HIS E NE2 1 
ATOM   5013  N  N   . VAL E  1 81  ? 55.797  117.284 56.210  1.00 9.15  ? 81   VAL E N   1 
ATOM   5014  C  CA  . VAL E  1 81  ? 56.183  117.842 57.510  1.00 8.91  ? 81   VAL E CA  1 
ATOM   5015  C  C   . VAL E  1 81  ? 54.921  118.209 58.322  1.00 8.79  ? 81   VAL E C   1 
ATOM   5016  O  O   . VAL E  1 81  ? 54.858  117.958 59.519  1.00 8.13  ? 81   VAL E O   1 
ATOM   5017  C  CB  . VAL E  1 81  ? 57.139  119.048 57.384  1.00 9.43  ? 81   VAL E CB  1 
ATOM   5018  C  CG1 . VAL E  1 81  ? 57.297  119.783 58.725  1.00 10.18 ? 81   VAL E CG1 1 
ATOM   5019  C  CG2 . VAL E  1 81  ? 58.484  118.568 56.893  1.00 8.36  ? 81   VAL E CG2 1 
ATOM   5020  N  N   . GLY E  1 82  ? 53.894  118.740 57.663  1.00 7.76  ? 82   GLY E N   1 
ATOM   5021  C  CA  . GLY E  1 82  ? 52.733  119.202 58.415  1.00 8.60  ? 82   GLY E CA  1 
ATOM   5022  C  C   . GLY E  1 82  ? 51.746  118.104 58.839  1.00 9.16  ? 82   GLY E C   1 
ATOM   5023  O  O   . GLY E  1 82  ? 50.701  118.427 59.400  1.00 8.53  ? 82   GLY E O   1 
ATOM   5024  N  N   . ASP E  1 83  ? 52.091  116.828 58.622  1.00 7.95  ? 83   ASP E N   1 
ATOM   5025  C  CA  . ASP E  1 83  ? 51.157  115.739 58.928  1.00 8.28  ? 83   ASP E CA  1 
ATOM   5026  C  C   . ASP E  1 83  ? 51.153  115.315 60.383  1.00 8.81  ? 83   ASP E C   1 
ATOM   5027  O  O   . ASP E  1 83  ? 51.939  114.446 60.773  1.00 8.43  ? 83   ASP E O   1 
ATOM   5028  C  CB  . ASP E  1 83  ? 51.429  114.509 58.050  1.00 8.56  ? 83   ASP E CB  1 
ATOM   5029  C  CG  . ASP E  1 83  ? 51.079  114.733 56.622  1.00 8.59  ? 83   ASP E CG  1 
ATOM   5030  O  OD1 . ASP E  1 83  ? 50.368  115.729 56.308  1.00 8.42  ? 83   ASP E OD1 1 
ATOM   5031  O  OD2 . ASP E  1 83  ? 51.477  113.930 55.729  1.00 10.46 ? 83   ASP E OD2 1 
ATOM   5032  N  N   . LEU E  1 84  ? 50.281  115.929 61.190  1.00 7.47  ? 84   LEU E N   1 
ATOM   5033  C  CA  . LEU E  1 84  ? 50.211  115.607 62.613  1.00 8.61  ? 84   LEU E CA  1 
ATOM   5034  C  C   . LEU E  1 84  ? 49.110  114.590 62.953  1.00 9.18  ? 84   LEU E C   1 
ATOM   5035  O  O   . LEU E  1 84  ? 48.809  114.313 64.142  1.00 10.53 ? 84   LEU E O   1 
ATOM   5036  C  CB  . LEU E  1 84  ? 49.993  116.902 63.387  1.00 7.96  ? 84   LEU E CB  1 
ATOM   5037  C  CG  . LEU E  1 84  ? 51.190  117.845 63.264  1.00 8.00  ? 84   LEU E CG  1 
ATOM   5038  C  CD1 . LEU E  1 84  ? 50.797  119.120 63.984  1.00 10.76 ? 84   LEU E CD1 1 
ATOM   5039  C  CD2 . LEU E  1 84  ? 52.438  117.223 63.895  1.00 9.82  ? 84   LEU E CD2 1 
ATOM   5040  N  N   . GLY E  1 85  ? 48.492  114.048 61.915  1.00 8.96  ? 85   GLY E N   1 
ATOM   5041  C  CA  . GLY E  1 85  ? 47.523  112.991 62.114  1.00 9.00  ? 85   GLY E CA  1 
ATOM   5042  C  C   . GLY E  1 85  ? 46.152  113.457 62.540  1.00 8.73  ? 85   GLY E C   1 
ATOM   5043  O  O   . GLY E  1 85  ? 45.592  114.385 61.947  1.00 10.22 ? 85   GLY E O   1 
ATOM   5044  N  N   . ASN E  1 86  ? 45.586  112.788 63.547  1.00 8.24  ? 86   ASN E N   1 
ATOM   5045  C  CA  . ASN E  1 86  ? 44.235  113.123 63.975  1.00 7.76  ? 86   ASN E CA  1 
ATOM   5046  C  C   . ASN E  1 86  ? 44.246  113.599 65.411  1.00 7.42  ? 86   ASN E C   1 
ATOM   5047  O  O   . ASN E  1 86  ? 45.165  113.288 66.183  1.00 7.61  ? 86   ASN E O   1 
ATOM   5048  C  CB  . ASN E  1 86  ? 43.314  111.908 63.937  1.00 7.46  ? 86   ASN E CB  1 
ATOM   5049  C  CG  . ASN E  1 86  ? 42.960  111.493 62.513  1.00 9.95  ? 86   ASN E CG  1 
ATOM   5050  O  OD1 . ASN E  1 86  ? 42.317  112.237 61.793  1.00 8.41  ? 86   ASN E OD1 1 
ATOM   5051  N  ND2 . ASN E  1 86  ? 43.390  110.309 62.119  1.00 10.32 ? 86   ASN E ND2 1 
ATOM   5052  N  N   . VAL E  1 87  ? 43.236  114.383 65.745  1.00 8.42  ? 87   VAL E N   1 
ATOM   5053  C  CA  . VAL E  1 87  ? 42.973  114.716 67.133  1.00 8.18  ? 87   VAL E CA  1 
ATOM   5054  C  C   . VAL E  1 87  ? 41.583  114.178 67.382  1.00 8.71  ? 87   VAL E C   1 
ATOM   5055  O  O   . VAL E  1 87  ? 40.800  114.034 66.450  1.00 9.99  ? 87   VAL E O   1 
ATOM   5056  C  CB  . VAL E  1 87  ? 43.074  116.221 67.426  1.00 8.49  ? 87   VAL E CB  1 
ATOM   5057  C  CG1 . VAL E  1 87  ? 44.534  116.715 67.211  1.00 7.98  ? 87   VAL E CG1 1 
ATOM   5058  C  CG2 . VAL E  1 87  ? 42.065  116.982 66.577  1.00 9.12  ? 87   VAL E CG2 1 
ATOM   5059  N  N   . THR E  1 88  ? 41.260  113.859 68.640  1.00 7.59  ? 88   THR E N   1 
ATOM   5060  C  CA  . THR E  1 88  ? 39.981  113.215 68.938  1.00 8.42  ? 88   THR E CA  1 
ATOM   5061  C  C   . THR E  1 88  ? 39.118  114.123 69.772  1.00 8.44  ? 88   THR E C   1 
ATOM   5062  O  O   . THR E  1 88  ? 39.573  114.655 70.779  1.00 9.45  ? 88   THR E O   1 
ATOM   5063  C  CB  . THR E  1 88  ? 40.239  111.934 69.753  1.00 8.37  ? 88   THR E CB  1 
ATOM   5064  O  OG1 . THR E  1 88  ? 40.972  111.027 68.927  1.00 8.77  ? 88   THR E OG1 1 
ATOM   5065  C  CG2 . THR E  1 88  ? 38.883  111.169 70.075  1.00 8.77  ? 88   THR E CG2 1 
ATOM   5066  N  N   . ALA E  1 89  ? 37.876  114.312 69.366  1.00 8.68  ? 89   ALA E N   1 
ATOM   5067  C  CA  . ALA E  1 89  ? 36.960  115.073 70.190  1.00 9.17  ? 89   ALA E CA  1 
ATOM   5068  C  C   . ALA E  1 89  ? 36.029  114.126 70.952  1.00 9.90  ? 89   ALA E C   1 
ATOM   5069  O  O   . ALA E  1 89  ? 35.562  113.113 70.413  1.00 8.96  ? 89   ALA E O   1 
ATOM   5070  C  CB  . ALA E  1 89  ? 36.134  116.018 69.336  1.00 9.30  ? 89   ALA E CB  1 
ATOM   5071  N  N   . ASP E  1 90  ? 35.737  114.505 72.193  1.00 10.70 ? 90   ASP E N   1 
ATOM   5072  C  CA  . ASP E  1 90  ? 34.873  113.713 73.068  1.00 11.40 ? 90   ASP E CA  1 
ATOM   5073  C  C   . ASP E  1 90  ? 33.400  113.964 72.806  1.00 12.41 ? 90   ASP E C   1 
ATOM   5074  O  O   . ASP E  1 90  ? 33.059  114.634 71.847  1.00 12.36 ? 90   ASP E O   1 
ATOM   5075  C  CB  . ASP E  1 90  ? 35.270  113.910 74.541  1.00 11.36 ? 90   ASP E CB  1 
ATOM   5076  C  CG  . ASP E  1 90  ? 35.054  115.354 75.052  1.00 12.49 ? 90   ASP E CG  1 
ATOM   5077  O  OD1 . ASP E  1 90  ? 34.215  116.120 74.498  1.00 12.56 ? 90   ASP E OD1 1 
ATOM   5078  O  OD2 . ASP E  1 90  ? 35.701  115.796 76.039  1.00 14.25 ? 90   ASP E OD2 1 
ATOM   5079  N  N   . LYS E  1 91  ? 32.515  113.404 73.631  1.00 13.25 ? 91   LYS E N   1 
ATOM   5080  C  CA  . LYS E  1 91  ? 31.090  113.550 73.355  1.00 14.47 ? 91   LYS E CA  1 
ATOM   5081  C  C   . LYS E  1 91  ? 30.570  114.976 73.585  1.00 14.25 ? 91   LYS E C   1 
ATOM   5082  O  O   . LYS E  1 91  ? 29.483  115.312 73.143  1.00 14.45 ? 91   LYS E O   1 
ATOM   5083  C  CB  . LYS E  1 91  ? 30.265  112.522 74.140  1.00 15.15 ? 91   LYS E CB  1 
ATOM   5084  C  CG  . LYS E  1 91  ? 30.463  112.595 75.630  1.00 19.01 ? 91   LYS E CG  1 
ATOM   5085  C  CD  . LYS E  1 91  ? 29.875  113.867 76.228  1.00 25.07 ? 91   LYS E CD  1 
ATOM   5086  C  CE  . LYS E  1 91  ? 29.920  113.850 77.759  1.00 26.81 ? 91   LYS E CE  1 
ATOM   5087  N  N   . ASP E  1 92  ? 31.350  115.809 74.263  1.00 13.66 ? 92   ASP E N   1 
ATOM   5088  C  CA  . ASP E  1 92  ? 30.990  117.210 74.457  1.00 13.69 ? 92   ASP E CA  1 
ATOM   5089  C  C   . ASP E  1 92  ? 31.555  118.099 73.318  1.00 13.00 ? 92   ASP E C   1 
ATOM   5090  O  O   . ASP E  1 92  ? 31.415  119.329 73.350  1.00 12.42 ? 92   ASP E O   1 
ATOM   5091  C  CB  . ASP E  1 92  ? 31.493  117.726 75.804  1.00 13.53 ? 92   ASP E CB  1 
ATOM   5092  C  CG  . ASP E  1 92  ? 30.882  116.983 76.979  1.00 16.83 ? 92   ASP E CG  1 
ATOM   5093  O  OD1 . ASP E  1 92  ? 29.655  116.742 76.947  1.00 15.73 ? 92   ASP E OD1 1 
ATOM   5094  O  OD2 . ASP E  1 92  ? 31.552  116.602 77.973  1.00 20.08 ? 92   ASP E OD2 1 
ATOM   5095  N  N   . GLY E  1 93  ? 32.159  117.477 72.308  1.00 11.90 ? 93   GLY E N   1 
ATOM   5096  C  CA  . GLY E  1 93  ? 32.722  118.241 71.209  1.00 11.55 ? 93   GLY E CA  1 
ATOM   5097  C  C   . GLY E  1 93  ? 34.112  118.811 71.474  1.00 10.49 ? 93   GLY E C   1 
ATOM   5098  O  O   . GLY E  1 93  ? 34.616  119.625 70.698  1.00 11.30 ? 93   GLY E O   1 
ATOM   5099  N  N   . VAL E  1 94  ? 34.756  118.378 72.549  1.00 9.30  ? 94   VAL E N   1 
ATOM   5100  C  CA  . VAL E  1 94  ? 36.050  118.957 72.903  1.00 9.53  ? 94   VAL E CA  1 
ATOM   5101  C  C   . VAL E  1 94  ? 37.236  118.060 72.566  1.00 9.31  ? 94   VAL E C   1 
ATOM   5102  O  O   . VAL E  1 94  ? 37.245  116.899 72.937  1.00 8.58  ? 94   VAL E O   1 
ATOM   5103  C  CB  . VAL E  1 94  ? 36.078  119.313 74.404  1.00 9.89  ? 94   VAL E CB  1 
ATOM   5104  C  CG1 . VAL E  1 94  ? 37.452  119.822 74.836  1.00 11.40 ? 94   VAL E CG1 1 
ATOM   5105  C  CG2 . VAL E  1 94  ? 34.984  120.372 74.708  1.00 11.20 ? 94   VAL E CG2 1 
ATOM   5106  N  N   . ALA E  1 95  ? 38.211  118.582 71.825  1.00 8.80  ? 95   ALA E N   1 
ATOM   5107  C  CA  . ALA E  1 95  ? 39.452  117.850 71.591  1.00 9.82  ? 95   ALA E CA  1 
ATOM   5108  C  C   . ALA E  1 95  ? 40.557  118.424 72.482  1.00 10.33 ? 95   ALA E C   1 
ATOM   5109  O  O   . ALA E  1 95  ? 41.002  119.553 72.304  1.00 11.37 ? 95   ALA E O   1 
ATOM   5110  C  CB  . ALA E  1 95  ? 39.868  117.921 70.109  1.00 9.82  ? 95   ALA E CB  1 
ATOM   5111  N  N   . ASP E  1 96  ? 40.989  117.638 73.454  1.00 10.83 ? 96   ASP E N   1 
ATOM   5112  C  CA  . ASP E  1 96  ? 42.077  118.028 74.331  1.00 11.39 ? 96   ASP E CA  1 
ATOM   5113  C  C   . ASP E  1 96  ? 43.364  117.520 73.709  1.00 10.51 ? 96   ASP E C   1 
ATOM   5114  O  O   . ASP E  1 96  ? 43.795  116.404 73.932  1.00 11.72 ? 96   ASP E O   1 
ATOM   5115  C  CB  . ASP E  1 96  ? 41.825  117.486 75.739  1.00 12.23 ? 96   ASP E CB  1 
ATOM   5116  C  CG  . ASP E  1 96  ? 40.755  118.302 76.479  1.00 15.35 ? 96   ASP E CG  1 
ATOM   5117  O  OD1 . ASP E  1 96  ? 39.861  117.696 77.099  1.00 17.20 ? 96   ASP E OD1 1 
ATOM   5118  O  OD2 . ASP E  1 96  ? 40.730  119.569 76.476  1.00 16.14 ? 96   ASP E OD2 1 
ATOM   5119  N  N   . VAL E  1 97  ? 43.932  118.343 72.845  1.00 9.71  ? 97   VAL E N   1 
ATOM   5120  C  CA  . VAL E  1 97  ? 45.071  117.945 72.043  1.00 8.60  ? 97   VAL E CA  1 
ATOM   5121  C  C   . VAL E  1 97  ? 46.336  117.779 72.851  1.00 9.05  ? 97   VAL E C   1 
ATOM   5122  O  O   . VAL E  1 97  ? 46.648  118.629 73.679  1.00 9.56  ? 97   VAL E O   1 
ATOM   5123  C  CB  . VAL E  1 97  ? 45.309  119.009 70.960  1.00 7.59  ? 97   VAL E CB  1 
ATOM   5124  C  CG1 . VAL E  1 97  ? 46.529  118.653 70.084  1.00 8.49  ? 97   VAL E CG1 1 
ATOM   5125  C  CG2 . VAL E  1 97  ? 44.028  119.174 70.113  1.00 8.73  ? 97   VAL E CG2 1 
ATOM   5126  N  N   . SER E  1 98  ? 47.025  116.661 72.625  1.00 11.23 ? 98   SER E N   1 
ATOM   5127  C  CA  . SER E  1 98  ? 48.345  116.410 73.244  1.00 11.63 ? 98   SER E CA  1 
ATOM   5128  C  C   . SER E  1 98  ? 49.135  115.519 72.308  1.00 12.10 ? 98   SER E C   1 
ATOM   5129  O  O   . SER E  1 98  ? 48.835  114.326 72.168  1.00 12.58 ? 98   SER E O   1 
ATOM   5130  C  CB  . SER E  1 98  ? 48.228  115.733 74.606  1.00 12.59 ? 98   SER E CB  1 
ATOM   5131  O  OG  . SER E  1 98  ? 49.491  115.793 75.250  1.00 16.02 ? 98   SER E OG  1 
ATOM   5132  N  N   . ILE E  1 99  ? 50.101  116.116 71.621  1.00 10.89 ? 99   ILE E N   1 
ATOM   5133  C  CA  . ILE E  1 99  ? 50.904  115.418 70.617  1.00 11.98 ? 99   ILE E CA  1 
ATOM   5134  C  C   . ILE E  1 99  ? 52.352  115.845 70.819  1.00 11.73 ? 99   ILE E C   1 
ATOM   5135  O  O   . ILE E  1 99  ? 52.630  116.973 71.229  1.00 11.89 ? 99   ILE E O   1 
ATOM   5136  C  CB  . ILE E  1 99  ? 50.427  115.871 69.218  1.00 12.09 ? 99   ILE E CB  1 
ATOM   5137  C  CG1 . ILE E  1 99  ? 49.086  115.190 68.851  1.00 12.99 ? 99   ILE E CG1 1 
ATOM   5138  C  CG2 . ILE E  1 99  ? 51.499  115.650 68.117  1.00 14.11 ? 99   ILE E CG2 1 
ATOM   5139  C  CD1 . ILE E  1 99  ? 48.405  115.869 67.536  1.00 15.33 ? 99   ILE E CD1 1 
ATOM   5140  N  N   . GLU E  1 100 ? 53.287  114.944 70.580  1.00 11.83 ? 100  GLU E N   1 
ATOM   5141  C  CA  . GLU E  1 100 ? 54.679  115.370 70.501  1.00 12.24 ? 100  GLU E CA  1 
ATOM   5142  C  C   . GLU E  1 100 ? 55.150  114.978 69.109  1.00 12.39 ? 100  GLU E C   1 
ATOM   5143  O  O   . GLU E  1 100 ? 54.899  113.846 68.665  1.00 11.17 ? 100  GLU E O   1 
ATOM   5144  C  CB  . GLU E  1 100 ? 55.544  114.703 71.565  1.00 13.52 ? 100  GLU E CB  1 
ATOM   5145  C  CG  . GLU E  1 100 ? 57.023  114.870 71.273  1.00 17.28 ? 100  GLU E CG  1 
ATOM   5146  C  CD  . GLU E  1 100 ? 57.909  114.167 72.303  1.00 22.47 ? 100  GLU E CD  1 
ATOM   5147  O  OE1 . GLU E  1 100 ? 57.823  114.558 73.496  1.00 20.19 ? 100  GLU E OE1 1 
ATOM   5148  O  OE2 . GLU E  1 100 ? 58.678  113.231 71.912  1.00 23.08 ? 100  GLU E OE2 1 
ATOM   5149  N  N   . ASP E  1 101 ? 55.800  115.897 68.405  1.00 11.14 ? 101  ASP E N   1 
ATOM   5150  C  CA  . ASP E  1 101 ? 56.272  115.605 67.059  1.00 11.80 ? 101  ASP E CA  1 
ATOM   5151  C  C   . ASP E  1 101 ? 57.701  116.114 66.884  1.00 11.93 ? 101  ASP E C   1 
ATOM   5152  O  O   . ASP E  1 101 ? 58.035  117.212 67.312  1.00 10.76 ? 101  ASP E O   1 
ATOM   5153  C  CB  . ASP E  1 101 ? 55.350  116.235 66.018  1.00 11.89 ? 101  ASP E CB  1 
ATOM   5154  C  CG  . ASP E  1 101 ? 55.590  115.688 64.642  1.00 12.71 ? 101  ASP E CG  1 
ATOM   5155  O  OD1 . ASP E  1 101 ? 55.127  114.548 64.373  1.00 11.74 ? 101  ASP E OD1 1 
ATOM   5156  O  OD2 . ASP E  1 101 ? 56.252  116.303 63.784  1.00 10.53 ? 101  ASP E OD2 1 
ATOM   5157  N  N   . SER E  1 102 ? 58.557  115.295 66.272  1.00 12.08 ? 102  SER E N   1 
ATOM   5158  C  CA  . SER E  1 102 ? 59.942  115.693 66.079  1.00 13.69 ? 102  SER E CA  1 
ATOM   5159  C  C   . SER E  1 102 ? 60.219  115.996 64.622  1.00 13.21 ? 102  SER E C   1 
ATOM   5160  O  O   . SER E  1 102 ? 61.370  116.163 64.233  1.00 13.54 ? 102  SER E O   1 
ATOM   5161  C  CB  . SER E  1 102 ? 60.899  114.606 66.563  1.00 13.87 ? 102  SER E CB  1 
ATOM   5162  O  OG  . SER E  1 102 ? 60.792  114.436 67.970  1.00 19.13 ? 102  SER E OG  1 
ATOM   5163  N  N   . VAL E  1 103 ? 59.167  116.038 63.802  1.00 12.13 ? 103  VAL E N   1 
ATOM   5164  C  CA  . VAL E  1 103 ? 59.362  116.376 62.406  1.00 11.78 ? 103  VAL E CA  1 
ATOM   5165  C  C   . VAL E  1 103 ? 59.080  117.868 62.153  1.00 11.36 ? 103  VAL E C   1 
ATOM   5166  O  O   . VAL E  1 103 ? 59.824  118.549 61.441  1.00 11.77 ? 103  VAL E O   1 
ATOM   5167  C  CB  . VAL E  1 103 ? 58.522  115.456 61.484  1.00 11.19 ? 103  VAL E CB  1 
ATOM   5168  C  CG1 . VAL E  1 103 ? 58.510  115.996 60.051  1.00 12.75 ? 103  VAL E CG1 1 
ATOM   5169  C  CG2 . VAL E  1 103 ? 59.065  114.039 61.537  1.00 13.21 ? 103  VAL E CG2 1 
ATOM   5170  N  N   . ILE E  1 104 ? 58.031  118.398 62.757  1.00 10.15 ? 104  ILE E N   1 
ATOM   5171  C  CA  . ILE E  1 104 ? 57.840  119.849 62.675  1.00 10.16 ? 104  ILE E CA  1 
ATOM   5172  C  C   . ILE E  1 104 ? 58.919  120.461 63.567  1.00 10.01 ? 104  ILE E C   1 
ATOM   5173  O  O   . ILE E  1 104 ? 59.554  119.749 64.343  1.00 10.54 ? 104  ILE E O   1 
ATOM   5174  C  CB  . ILE E  1 104 ? 56.430  120.251 63.178  1.00 9.39  ? 104  ILE E CB  1 
ATOM   5175  C  CG1 . ILE E  1 104 ? 56.166  119.636 64.548  1.00 10.39 ? 104  ILE E CG1 1 
ATOM   5176  C  CG2 . ILE E  1 104 ? 55.392  119.729 62.190  1.00 10.40 ? 104  ILE E CG2 1 
ATOM   5177  C  CD1 . ILE E  1 104 ? 55.040  120.280 65.361  1.00 5.50  ? 104  ILE E CD1 1 
ATOM   5178  N  N   . SER E  1 105 ? 59.132  121.762 63.452  1.00 10.28 ? 105  SER E N   1 
ATOM   5179  C  CA  . SER E  1 105 ? 60.065  122.478 64.311  1.00 9.49  ? 105  SER E CA  1 
ATOM   5180  C  C   . SER E  1 105 ? 59.662  123.938 64.417  1.00 10.41 ? 105  SER E C   1 
ATOM   5181  O  O   . SER E  1 105 ? 58.952  124.447 63.557  1.00 8.36  ? 105  SER E O   1 
ATOM   5182  C  CB  . SER E  1 105 ? 61.498  122.389 63.745  1.00 10.61 ? 105  SER E CB  1 
ATOM   5183  O  OG  . SER E  1 105 ? 62.442  122.903 64.669  1.00 11.61 ? 105  SER E OG  1 
ATOM   5184  N  N   . LEU E  1 106 ? 60.141  124.603 65.464  1.00 10.76 ? 106  LEU E N   1 
ATOM   5185  C  CA  . LEU E  1 106 ? 59.937  126.044 65.633  1.00 12.68 ? 106  LEU E CA  1 
ATOM   5186  C  C   . LEU E  1 106 ? 61.165  126.853 65.192  1.00 13.90 ? 106  LEU E C   1 
ATOM   5187  O  O   . LEU E  1 106 ? 61.200  128.073 65.361  1.00 13.94 ? 106  LEU E O   1 
ATOM   5188  C  CB  . LEU E  1 106 ? 59.574  126.393 67.078  1.00 12.19 ? 106  LEU E CB  1 
ATOM   5189  C  CG  . LEU E  1 106 ? 58.344  125.640 67.587  1.00 12.16 ? 106  LEU E CG  1 
ATOM   5190  C  CD1 . LEU E  1 106 ? 57.969  126.106 69.012  1.00 12.18 ? 106  LEU E CD1 1 
ATOM   5191  C  CD2 . LEU E  1 106 ? 57.146  125.800 66.639  1.00 13.73 ? 106  LEU E CD2 1 
ATOM   5192  N  N   . SER E  1 107 ? 62.161  126.199 64.609  1.00 15.63 ? 107  SER E N   1 
ATOM   5193  C  CA  . SER E  1 107 ? 63.341  126.933 64.149  1.00 17.90 ? 107  SER E CA  1 
ATOM   5194  C  C   . SER E  1 107 ? 64.007  126.238 62.992  1.00 18.41 ? 107  SER E C   1 
ATOM   5195  O  O   . SER E  1 107 ? 64.015  125.007 62.922  1.00 19.62 ? 107  SER E O   1 
ATOM   5196  C  CB  . SER E  1 107 ? 64.350  127.127 65.287  1.00 17.67 ? 107  SER E CB  1 
ATOM   5197  N  N   . HIS E  1 110 ? 62.239  123.117 58.573  1.00 15.67 ? 110  HIS E N   1 
ATOM   5198  C  CA  . HIS E  1 110 ? 60.917  122.519 58.896  1.00 14.91 ? 110  HIS E CA  1 
ATOM   5199  C  C   . HIS E  1 110 ? 60.132  123.440 59.832  1.00 14.11 ? 110  HIS E C   1 
ATOM   5200  O  O   . HIS E  1 110 ? 59.187  122.990 60.508  1.00 14.34 ? 110  HIS E O   1 
ATOM   5201  C  CB  . HIS E  1 110 ? 60.993  121.142 59.565  1.00 15.05 ? 110  HIS E CB  1 
ATOM   5202  C  CG  . HIS E  1 110 ? 61.578  120.062 58.716  1.00 17.36 ? 110  HIS E CG  1 
ATOM   5203  N  ND1 . HIS E  1 110 ? 61.495  118.724 59.059  1.00 18.42 ? 110  HIS E ND1 1 
ATOM   5204  C  CD2 . HIS E  1 110 ? 62.294  120.116 57.570  1.00 16.82 ? 110  HIS E CD2 1 
ATOM   5205  C  CE1 . HIS E  1 110 ? 62.130  118.004 58.150  1.00 20.24 ? 110  HIS E CE1 1 
ATOM   5206  N  NE2 . HIS E  1 110 ? 62.625  118.824 57.238  1.00 19.46 ? 110  HIS E NE2 1 
ATOM   5207  N  N   . CYS E  1 111 ? 60.563  124.703 59.913  1.00 12.99 ? 111  CYS E N   1 
ATOM   5208  C  CA  . CYS E  1 111 ? 59.957  125.699 60.785  1.00 12.29 ? 111  CYS E CA  1 
ATOM   5209  C  C   . CYS E  1 111 ? 58.508  125.975 60.397  1.00 11.16 ? 111  CYS E C   1 
ATOM   5210  O  O   . CYS E  1 111 ? 58.212  126.175 59.229  1.00 10.88 ? 111  CYS E O   1 
ATOM   5211  C  CB  . CYS E  1 111 ? 60.778  126.992 60.752  1.00 12.27 ? 111  CYS E CB  1 
ATOM   5212  S  SG  . CYS E  1 111 ? 60.210  128.099 62.026  1.00 17.52 ? 111  CYS E SG  1 
ATOM   5213  N  N   . ILE E  1 112 ? 57.600  125.970 61.369  1.00 9.93  ? 112  ILE E N   1 
ATOM   5214  C  CA  . ILE E  1 112 ? 56.173  126.127 61.054  1.00 9.20  ? 112  ILE E CA  1 
ATOM   5215  C  C   . ILE E  1 112 ? 55.631  127.470 61.487  1.00 9.34  ? 112  ILE E C   1 
ATOM   5216  O  O   . ILE E  1 112 ? 54.449  127.740 61.317  1.00 8.74  ? 112  ILE E O   1 
ATOM   5217  C  CB  . ILE E  1 112 ? 55.302  124.998 61.687  1.00 10.20 ? 112  ILE E CB  1 
ATOM   5218  C  CG1 . ILE E  1 112 ? 55.411  124.955 63.227  1.00 9.34  ? 112  ILE E CG1 1 
ATOM   5219  C  CG2 . ILE E  1 112 ? 55.657  123.628 61.038  1.00 8.42  ? 112  ILE E CG2 1 
ATOM   5220  C  CD1 . ILE E  1 112 ? 54.395  123.922 63.907  1.00 8.45  ? 112  ILE E CD1 1 
ATOM   5221  N  N   . ILE E  1 113 ? 56.504  128.319 62.030  1.00 8.37  ? 113  ILE E N   1 
ATOM   5222  C  CA  . ILE E  1 113 ? 56.049  129.623 62.467  1.00 8.87  ? 113  ILE E CA  1 
ATOM   5223  C  C   . ILE E  1 113 ? 55.616  130.395 61.222  1.00 8.20  ? 113  ILE E C   1 
ATOM   5224  O  O   . ILE E  1 113 ? 56.338  130.396 60.210  1.00 8.31  ? 113  ILE E O   1 
ATOM   5225  C  CB  . ILE E  1 113 ? 57.208  130.386 63.101  1.00 10.15 ? 113  ILE E CB  1 
ATOM   5226  C  CG1 . ILE E  1 113 ? 57.693  129.684 64.367  1.00 13.74 ? 113  ILE E CG1 1 
ATOM   5227  C  CG2 . ILE E  1 113 ? 56.832  131.860 63.336  1.00 10.25 ? 113  ILE E CG2 1 
ATOM   5228  C  CD1 . ILE E  1 113 ? 56.647  129.501 65.342  1.00 16.85 ? 113  ILE E CD1 1 
ATOM   5229  N  N   . GLY E  1 114 ? 54.481  131.080 61.266  1.00 6.05  ? 114  GLY E N   1 
ATOM   5230  C  CA  . GLY E  1 114 ? 54.039  131.825 60.098  1.00 7.12  ? 114  GLY E CA  1 
ATOM   5231  C  C   . GLY E  1 114 ? 53.189  131.019 59.103  1.00 6.93  ? 114  GLY E C   1 
ATOM   5232  O  O   . GLY E  1 114 ? 52.739  131.527 58.078  1.00 7.60  ? 114  GLY E O   1 
ATOM   5233  N  N   . ARG E  1 115 ? 52.962  129.767 59.422  1.00 7.22  ? 115  ARG E N   1 
ATOM   5234  C  CA  . ARG E  1 115 ? 52.179  128.888 58.566  1.00 8.09  ? 115  ARG E CA  1 
ATOM   5235  C  C   . ARG E  1 115 ? 50.851  128.692 59.260  1.00 8.75  ? 115  ARG E C   1 
ATOM   5236  O  O   . ARG E  1 115 ? 50.607  129.374 60.243  1.00 9.39  ? 115  ARG E O   1 
ATOM   5237  C  CB  . ARG E  1 115 ? 52.934  127.592 58.347  1.00 8.36  ? 115  ARG E CB  1 
ATOM   5238  C  CG  . ARG E  1 115 ? 54.354  127.914 57.775  1.00 8.63  ? 115  ARG E CG  1 
ATOM   5239  C  CD  . ARG E  1 115 ? 55.059  126.721 57.146  1.00 12.30 ? 115  ARG E CD  1 
ATOM   5240  N  NE  . ARG E  1 115 ? 56.389  127.039 56.652  1.00 11.55 ? 115  ARG E NE  1 
ATOM   5241  C  CZ  . ARG E  1 115 ? 56.672  127.424 55.422  1.00 12.13 ? 115  ARG E CZ  1 
ATOM   5242  N  NH1 . ARG E  1 115 ? 55.712  127.590 54.517  1.00 11.92 ? 115  ARG E NH1 1 
ATOM   5243  N  NH2 . ARG E  1 115 ? 57.942  127.649 55.092  1.00 15.23 ? 115  ARG E NH2 1 
ATOM   5244  N  N   . THR E  1 116 ? 49.985  127.816 58.734  1.00 8.22  ? 116  THR E N   1 
ATOM   5245  C  CA  . THR E  1 116 ? 48.625  127.684 59.260  1.00 8.92  ? 116  THR E CA  1 
ATOM   5246  C  C   . THR E  1 116 ? 48.318  126.313 59.825  1.00 8.76  ? 116  THR E C   1 
ATOM   5247  O  O   . THR E  1 116 ? 48.609  125.292 59.188  1.00 9.86  ? 116  THR E O   1 
ATOM   5248  C  CB  . THR E  1 116 ? 47.585  127.994 58.163  1.00 9.71  ? 116  THR E CB  1 
ATOM   5249  O  OG1 . THR E  1 116 ? 47.668  129.379 57.815  1.00 10.41 ? 116  THR E OG1 1 
ATOM   5250  C  CG2 . THR E  1 116 ? 46.109  127.777 58.653  1.00 8.35  ? 116  THR E CG2 1 
ATOM   5251  N  N   . LEU E  1 117 ? 47.732  126.301 61.020  1.00 7.53  ? 117  LEU E N   1 
ATOM   5252  C  CA  . LEU E  1 117 ? 47.275  125.056 61.598  1.00 6.83  ? 117  LEU E CA  1 
ATOM   5253  C  C   . LEU E  1 117 ? 45.805  124.928 61.241  1.00 7.31  ? 117  LEU E C   1 
ATOM   5254  O  O   . LEU E  1 117 ? 45.075  125.920 61.366  1.00 6.45  ? 117  LEU E O   1 
ATOM   5255  C  CB  . LEU E  1 117 ? 47.480  125.082 63.111  1.00 6.44  ? 117  LEU E CB  1 
ATOM   5256  C  CG  . LEU E  1 117 ? 47.085  123.829 63.868  1.00 7.00  ? 117  LEU E CG  1 
ATOM   5257  C  CD1 . LEU E  1 117 ? 48.013  122.659 63.514  1.00 6.87  ? 117  LEU E CD1 1 
ATOM   5258  C  CD2 . LEU E  1 117 ? 47.159  124.133 65.420  1.00 8.92  ? 117  LEU E CD2 1 
ATOM   5259  N  N   . VAL E  1 118 ? 45.388  123.737 60.783  1.00 5.89  ? 118  VAL E N   1 
ATOM   5260  C  CA  . VAL E  1 118 ? 44.005  123.506 60.338  1.00 6.72  ? 118  VAL E CA  1 
ATOM   5261  C  C   . VAL E  1 118 ? 43.439  122.251 60.996  1.00 7.13  ? 118  VAL E C   1 
ATOM   5262  O  O   . VAL E  1 118 ? 44.146  121.254 61.088  1.00 7.47  ? 118  VAL E O   1 
ATOM   5263  C  CB  . VAL E  1 118 ? 43.959  123.252 58.825  1.00 5.00  ? 118  VAL E CB  1 
ATOM   5264  C  CG1 . VAL E  1 118 ? 42.490  122.949 58.370  1.00 6.52  ? 118  VAL E CG1 1 
ATOM   5265  C  CG2 . VAL E  1 118 ? 44.527  124.447 58.058  1.00 6.78  ? 118  VAL E CG2 1 
ATOM   5266  N  N   . VAL E  1 119 ? 42.206  122.333 61.478  1.00 7.30  ? 119  VAL E N   1 
ATOM   5267  C  CA  . VAL E  1 119 ? 41.507  121.141 61.987  1.00 6.85  ? 119  VAL E CA  1 
ATOM   5268  C  C   . VAL E  1 119 ? 40.357  120.890 61.017  1.00 7.55  ? 119  VAL E C   1 
ATOM   5269  O  O   . VAL E  1 119 ? 39.716  121.823 60.528  1.00 6.56  ? 119  VAL E O   1 
ATOM   5270  C  CB  . VAL E  1 119 ? 41.038  121.271 63.424  1.00 5.90  ? 119  VAL E CB  1 
ATOM   5271  C  CG1 . VAL E  1 119 ? 40.119  122.499 63.637  1.00 6.91  ? 119  VAL E CG1 1 
ATOM   5272  C  CG2 . VAL E  1 119 ? 40.325  119.960 63.914  1.00 5.57  ? 119  VAL E CG2 1 
ATOM   5273  N  N   . HIS E  1 120 ? 40.179  119.608 60.691  1.00 7.31  ? 120  HIS E N   1 
ATOM   5274  C  CA  . HIS E  1 120 ? 39.295  119.206 59.608  1.00 7.79  ? 120  HIS E CA  1 
ATOM   5275  C  C   . HIS E  1 120 ? 37.979  118.582 60.018  1.00 8.35  ? 120  HIS E C   1 
ATOM   5276  O  O   . HIS E  1 120 ? 37.772  118.147 61.151  1.00 7.87  ? 120  HIS E O   1 
ATOM   5277  C  CB  . HIS E  1 120 ? 40.041  118.169 58.754  1.00 6.55  ? 120  HIS E CB  1 
ATOM   5278  C  CG  . HIS E  1 120 ? 41.038  118.771 57.844  1.00 6.23  ? 120  HIS E CG  1 
ATOM   5279  N  ND1 . HIS E  1 120 ? 40.699  119.251 56.597  1.00 6.93  ? 120  HIS E ND1 1 
ATOM   5280  C  CD2 . HIS E  1 120 ? 42.372  118.969 57.978  1.00 7.52  ? 120  HIS E CD2 1 
ATOM   5281  C  CE1 . HIS E  1 120 ? 41.782  119.710 55.999  1.00 8.35  ? 120  HIS E CE1 1 
ATOM   5282  N  NE2 . HIS E  1 120 ? 42.797  119.577 56.826  1.00 10.03 ? 120  HIS E NE2 1 
ATOM   5283  N  N   . GLU E  1 121 ? 37.120  118.475 59.024  1.00 7.20  ? 121  GLU E N   1 
ATOM   5284  C  CA  . GLU E  1 121 ? 35.798  117.945 59.184  1.00 9.78  ? 121  GLU E CA  1 
ATOM   5285  C  C   . GLU E  1 121 ? 35.784  116.453 59.504  1.00 9.35  ? 121  GLU E C   1 
ATOM   5286  O  O   . GLU E  1 121 ? 34.976  116.007 60.322  1.00 9.59  ? 121  GLU E O   1 
ATOM   5287  C  CB  . GLU E  1 121 ? 35.051  118.199 57.868  1.00 10.47 ? 121  GLU E CB  1 
ATOM   5288  C  CG  . GLU E  1 121 ? 33.658  117.565 57.798  1.00 15.83 ? 121  GLU E CG  1 
ATOM   5289  C  CD  . GLU E  1 121 ? 33.121  117.508 56.369  1.00 21.61 ? 121  GLU E CD  1 
ATOM   5290  O  OE1 . GLU E  1 121 ? 31.877  117.522 56.225  1.00 25.62 ? 121  GLU E OE1 1 
ATOM   5291  O  OE2 . GLU E  1 121 ? 33.929  117.433 55.394  1.00 20.27 ? 121  GLU E OE2 1 
ATOM   5292  N  N   . LYS E  1 122 ? 36.666  115.691 58.861  1.00 9.28  ? 122  LYS E N   1 
ATOM   5293  C  CA  . LYS E  1 122 ? 36.638  114.226 58.960  1.00 10.84 ? 122  LYS E CA  1 
ATOM   5294  C  C   . LYS E  1 122 ? 37.981  113.705 59.412  1.00 10.80 ? 122  LYS E C   1 
ATOM   5295  O  O   . LYS E  1 122 ? 38.949  114.463 59.521  1.00 9.75  ? 122  LYS E O   1 
ATOM   5296  C  CB  . LYS E  1 122 ? 36.355  113.580 57.585  1.00 10.88 ? 122  LYS E CB  1 
ATOM   5297  C  CG  . LYS E  1 122 ? 35.275  114.180 56.746  1.00 16.91 ? 122  LYS E CG  1 
ATOM   5298  C  CD  . LYS E  1 122 ? 34.914  113.187 55.627  1.00 20.65 ? 122  LYS E CD  1 
ATOM   5299  C  CE  . LYS E  1 122 ? 35.591  113.494 54.293  1.00 22.47 ? 122  LYS E CE  1 
ATOM   5300  N  NZ  . LYS E  1 122 ? 35.087  112.502 53.240  1.00 26.65 ? 122  LYS E NZ  1 
ATOM   5301  N  N   . ALA E  1 123 ? 38.061  112.386 59.573  1.00 10.74 ? 123  ALA E N   1 
ATOM   5302  C  CA  . ALA E  1 123 ? 39.306  111.782 60.007  1.00 10.77 ? 123  ALA E CA  1 
ATOM   5303  C  C   . ALA E  1 123 ? 40.274  111.780 58.837  1.00 11.77 ? 123  ALA E C   1 
ATOM   5304  O  O   . ALA E  1 123 ? 39.858  111.697 57.660  1.00 11.31 ? 123  ALA E O   1 
ATOM   5305  C  CB  . ALA E  1 123 ? 39.056  110.372 60.483  1.00 12.79 ? 123  ALA E CB  1 
ATOM   5306  N  N   . ASP E  1 124 ? 41.552  111.889 59.176  1.00 10.46 ? 124  ASP E N   1 
ATOM   5307  C  CA  . ASP E  1 124 ? 42.643  111.779 58.201  1.00 10.01 ? 124  ASP E CA  1 
ATOM   5308  C  C   . ASP E  1 124 ? 42.930  110.267 58.093  1.00 8.64  ? 124  ASP E C   1 
ATOM   5309  O  O   . ASP E  1 124 ? 43.132  109.604 59.123  1.00 7.50  ? 124  ASP E O   1 
ATOM   5310  C  CB  . ASP E  1 124 ? 43.804  112.539 58.813  1.00 10.58 ? 124  ASP E CB  1 
ATOM   5311  C  CG  . ASP E  1 124 ? 45.051  112.488 58.009  1.00 10.59 ? 124  ASP E CG  1 
ATOM   5312  O  OD1 . ASP E  1 124 ? 45.228  111.595 57.159  1.00 8.38  ? 124  ASP E OD1 1 
ATOM   5313  O  OD2 . ASP E  1 124 ? 45.919  113.360 58.161  1.00 9.11  ? 124  ASP E OD2 1 
ATOM   5314  N  N   . ASP E  1 125 ? 42.943  109.706 56.874  1.00 6.97  ? 125  ASP E N   1 
ATOM   5315  C  CA  . ASP E  1 125 ? 43.170  108.252 56.730  1.00 7.48  ? 125  ASP E CA  1 
ATOM   5316  C  C   . ASP E  1 125 ? 44.639  107.869 56.750  1.00 8.27  ? 125  ASP E C   1 
ATOM   5317  O  O   . ASP E  1 125 ? 45.035  106.682 56.548  1.00 8.04  ? 125  ASP E O   1 
ATOM   5318  C  CB  . ASP E  1 125 ? 42.431  107.677 55.487  1.00 8.35  ? 125  ASP E CB  1 
ATOM   5319  C  CG  . ASP E  1 125 ? 42.908  108.250 54.174  1.00 8.56  ? 125  ASP E CG  1 
ATOM   5320  O  OD1 . ASP E  1 125 ? 44.027  108.788 54.107  1.00 7.89  ? 125  ASP E OD1 1 
ATOM   5321  O  OD2 . ASP E  1 125 ? 42.216  108.168 53.126  1.00 7.20  ? 125  ASP E OD2 1 
ATOM   5322  N  N   . LEU E  1 126 ? 45.450  108.881 57.013  1.00 7.14  ? 126  LEU E N   1 
ATOM   5323  C  CA  . LEU E  1 126 ? 46.890  108.700 57.154  1.00 8.01  ? 126  LEU E CA  1 
ATOM   5324  C  C   . LEU E  1 126 ? 47.569  108.137 55.903  1.00 7.56  ? 126  LEU E C   1 
ATOM   5325  O  O   . LEU E  1 126 ? 48.589  107.438 55.998  1.00 7.59  ? 126  LEU E O   1 
ATOM   5326  C  CB  . LEU E  1 126 ? 47.177  107.815 58.392  1.00 9.13  ? 126  LEU E CB  1 
ATOM   5327  C  CG  . LEU E  1 126 ? 46.460  108.240 59.706  1.00 10.17 ? 126  LEU E CG  1 
ATOM   5328  C  CD1 . LEU E  1 126 ? 46.933  107.423 60.913  1.00 11.64 ? 126  LEU E CD1 1 
ATOM   5329  C  CD2 . LEU E  1 126 ? 46.615  109.774 60.012  1.00 11.00 ? 126  LEU E CD2 1 
ATOM   5330  N  N   . GLY E  1 127 ? 47.019  108.440 54.726  1.00 5.73  ? 127  GLY E N   1 
ATOM   5331  C  CA  . GLY E  1 127 ? 47.613  107.969 53.486  1.00 5.60  ? 127  GLY E CA  1 
ATOM   5332  C  C   . GLY E  1 127 ? 47.233  106.540 53.101  1.00 6.19  ? 127  GLY E C   1 
ATOM   5333  O  O   . GLY E  1 127 ? 47.743  105.998 52.105  1.00 5.86  ? 127  GLY E O   1 
ATOM   5334  N  N   . LYS E  1 128 ? 46.300  105.937 53.836  1.00 5.74  ? 128  LYS E N   1 
ATOM   5335  C  CA  . LYS E  1 128 ? 45.960  104.534 53.612  1.00 5.66  ? 128  LYS E CA  1 
ATOM   5336  C  C   . LYS E  1 128 ? 44.628  104.282 52.891  1.00 5.93  ? 128  LYS E C   1 
ATOM   5337  O  O   . LYS E  1 128 ? 44.107  103.164 52.932  1.00 6.21  ? 128  LYS E O   1 
ATOM   5338  C  CB  . LYS E  1 128 ? 45.978  103.772 54.973  1.00 7.27  ? 128  LYS E CB  1 
ATOM   5339  C  CG  . LYS E  1 128 ? 47.365  103.872 55.625  1.00 8.79  ? 128  LYS E CG  1 
ATOM   5340  C  CD  . LYS E  1 128 ? 47.357  103.385 57.074  1.00 15.65 ? 128  LYS E CD  1 
ATOM   5341  C  CE  . LYS E  1 128 ? 47.008  101.937 57.211  1.00 19.60 ? 128  LYS E CE  1 
ATOM   5342  N  NZ  . LYS E  1 128 ? 47.185  101.477 58.671  1.00 23.53 ? 128  LYS E NZ  1 
ATOM   5343  N  N   . GLY E  1 129 ? 44.095  105.331 52.266  1.00 6.27  ? 129  GLY E N   1 
ATOM   5344  C  CA  . GLY E  1 129 ? 42.784  105.317 51.641  1.00 6.28  ? 129  GLY E CA  1 
ATOM   5345  C  C   . GLY E  1 129 ? 42.667  104.714 50.248  1.00 6.45  ? 129  GLY E C   1 
ATOM   5346  O  O   . GLY E  1 129 ? 41.531  104.429 49.791  1.00 6.82  ? 129  GLY E O   1 
ATOM   5347  N  N   . GLY E  1 130 ? 43.800  104.494 49.584  1.00 5.25  ? 130  GLY E N   1 
ATOM   5348  C  CA  . GLY E  1 130 ? 43.801  103.854 48.265  1.00 5.13  ? 130  GLY E CA  1 
ATOM   5349  C  C   . GLY E  1 130 ? 43.355  104.721 47.078  1.00 7.01  ? 130  GLY E C   1 
ATOM   5350  O  O   . GLY E  1 130 ? 42.998  104.194 46.012  1.00 5.78  ? 130  GLY E O   1 
ATOM   5351  N  N   . ASN E  1 131 ? 43.375  106.040 47.268  1.00 8.39  ? 131  ASN E N   1 
ATOM   5352  C  CA  . ASN E  1 131 ? 43.082  106.989 46.165  1.00 10.10 ? 131  ASN E CA  1 
ATOM   5353  C  C   . ASN E  1 131 ? 44.083  108.135 46.146  1.00 10.39 ? 131  ASN E C   1 
ATOM   5354  O  O   . ASN E  1 131 ? 44.849  108.282 47.070  1.00 9.05  ? 131  ASN E O   1 
ATOM   5355  C  CB  . ASN E  1 131 ? 41.603  107.454 46.152  1.00 10.63 ? 131  ASN E CB  1 
ATOM   5356  C  CG  . ASN E  1 131 ? 41.163  108.192 47.423  1.00 12.50 ? 131  ASN E CG  1 
ATOM   5357  O  OD1 . ASN E  1 131 ? 41.980  108.599 48.255  1.00 10.73 ? 131  ASN E OD1 1 
ATOM   5358  N  ND2 . ASN E  1 131 ? 39.852  108.415 47.544  1.00 13.78 ? 131  ASN E ND2 1 
ATOM   5359  N  N   . GLU E  1 132 ? 44.136  108.921 45.061  1.00 10.93 ? 132  GLU E N   1 
ATOM   5360  C  CA  . GLU E  1 132 ? 45.109  110.002 45.018  1.00 11.93 ? 132  GLU E CA  1 
ATOM   5361  C  C   . GLU E  1 132 ? 44.854  111.006 46.133  1.00 10.60 ? 132  GLU E C   1 
ATOM   5362  O  O   . GLU E  1 132 ? 45.792  111.561 46.702  1.00 11.40 ? 132  GLU E O   1 
ATOM   5363  C  CB  . GLU E  1 132 ? 45.205  110.682 43.625  1.00 12.43 ? 132  GLU E CB  1 
ATOM   5364  C  CG  . GLU E  1 132 ? 46.482  111.517 43.488  1.00 16.03 ? 132  GLU E CG  1 
ATOM   5365  N  N   . GLU E  1 133 ? 43.599  111.214 46.492  1.00 10.56 ? 133  GLU E N   1 
ATOM   5366  C  CA  . GLU E  1 133 ? 43.304  112.188 47.545  1.00 10.28 ? 133  GLU E CA  1 
ATOM   5367  C  C   . GLU E  1 133 ? 43.945  111.748 48.881  1.00 10.00 ? 133  GLU E C   1 
ATOM   5368  O  O   . GLU E  1 133 ? 44.471  112.574 49.639  1.00 8.77  ? 133  GLU E O   1 
ATOM   5369  C  CB  . GLU E  1 133 ? 41.794  112.364 47.721  1.00 11.79 ? 133  GLU E CB  1 
ATOM   5370  C  CG  . GLU E  1 133 ? 41.400  113.511 48.667  1.00 11.93 ? 133  GLU E CG  1 
ATOM   5371  C  CD  . GLU E  1 133 ? 41.727  114.870 48.099  1.00 16.44 ? 133  GLU E CD  1 
ATOM   5372  O  OE1 . GLU E  1 133 ? 41.380  115.134 46.939  1.00 18.08 ? 133  GLU E OE1 1 
ATOM   5373  O  OE2 . GLU E  1 133 ? 42.322  115.683 48.817  1.00 18.00 ? 133  GLU E OE2 1 
ATOM   5374  N  N   . SER E  1 134 ? 43.925  110.452 49.162  1.00 8.66  ? 134  SER E N   1 
ATOM   5375  C  CA  . SER E  1 134 ? 44.540  109.973 50.405  1.00 8.27  ? 134  SER E CA  1 
ATOM   5376  C  C   . SER E  1 134 ? 46.018  110.357 50.480  1.00 8.77  ? 134  SER E C   1 
ATOM   5377  O  O   . SER E  1 134 ? 46.481  110.731 51.564  1.00 8.32  ? 134  SER E O   1 
ATOM   5378  C  CB  . SER E  1 134 ? 44.423  108.436 50.513  1.00 8.81  ? 134  SER E CB  1 
ATOM   5379  O  OG  . SER E  1 134 ? 44.967  108.030 51.751  1.00 7.35  ? 134  SER E OG  1 
ATOM   5380  N  N   . THR E  1 135 ? 46.737  110.265 49.345  1.00 7.66  ? 135  THR E N   1 
ATOM   5381  C  CA  . THR E  1 135 ? 48.155  110.634 49.289  1.00 10.07 ? 135  THR E CA  1 
ATOM   5382  C  C   . THR E  1 135 ? 48.412  112.130 49.311  1.00 10.02 ? 135  THR E C   1 
ATOM   5383  O  O   . THR E  1 135 ? 49.574  112.545 49.347  1.00 8.58  ? 135  THR E O   1 
ATOM   5384  C  CB  . THR E  1 135 ? 48.852  110.108 48.002  1.00 10.24 ? 135  THR E CB  1 
ATOM   5385  O  OG1 . THR E  1 135 ? 48.292  110.788 46.859  1.00 14.72 ? 135  THR E OG1 1 
ATOM   5386  C  CG2 . THR E  1 135 ? 48.558  108.714 47.760  1.00 11.71 ? 135  THR E CG2 1 
ATOM   5387  N  N   . LYS E  1 136 ? 47.349  112.937 49.253  1.00 11.14 ? 136  LYS E N   1 
ATOM   5388  C  CA  . LYS E  1 136 ? 47.467  114.402 49.324  1.00 12.34 ? 136  LYS E CA  1 
ATOM   5389  C  C   . LYS E  1 136 ? 47.011  115.033 50.644  1.00 11.65 ? 136  LYS E C   1 
ATOM   5390  O  O   . LYS E  1 136 ? 47.766  115.811 51.260  1.00 11.53 ? 136  LYS E O   1 
ATOM   5391  C  CB  . LYS E  1 136 ? 46.618  115.044 48.215  1.00 13.41 ? 136  LYS E CB  1 
ATOM   5392  C  CG  . LYS E  1 136 ? 47.150  114.841 46.808  1.00 18.11 ? 136  LYS E CG  1 
ATOM   5393  C  CD  . LYS E  1 136 ? 46.060  115.235 45.810  1.00 24.60 ? 136  LYS E CD  1 
ATOM   5394  C  CE  . LYS E  1 136 ? 46.608  116.045 44.672  1.00 28.45 ? 136  LYS E CE  1 
ATOM   5395  N  NZ  . LYS E  1 136 ? 45.533  116.889 44.067  1.00 31.26 ? 136  LYS E NZ  1 
ATOM   5396  N  N   . THR E  1 137 ? 45.784  114.705 51.057  1.00 10.88 ? 137  THR E N   1 
ATOM   5397  C  CA  . THR E  1 137 ? 45.149  115.277 52.258  1.00 11.74 ? 137  THR E CA  1 
ATOM   5398  C  C   . THR E  1 137 ? 44.670  114.258 53.270  1.00 12.03 ? 137  THR E C   1 
ATOM   5399  O  O   . THR E  1 137 ? 44.147  114.643 54.314  1.00 11.35 ? 137  THR E O   1 
ATOM   5400  C  CB  . THR E  1 137 ? 43.884  116.065 51.845  1.00 11.55 ? 137  THR E CB  1 
ATOM   5401  O  OG1 . THR E  1 137 ? 42.926  115.148 51.269  1.00 12.32 ? 137  THR E OG1 1 
ATOM   5402  C  CG2 . THR E  1 137 ? 44.186  117.050 50.684  1.00 11.97 ? 137  THR E CG2 1 
ATOM   5403  N  N   . GLY E  1 138 ? 44.815  112.962 52.985  1.00 9.65  ? 138  GLY E N   1 
ATOM   5404  C  CA  . GLY E  1 138 ? 44.228  111.965 53.887  1.00 9.75  ? 138  GLY E CA  1 
ATOM   5405  C  C   . GLY E  1 138 ? 42.691  111.909 53.876  1.00 8.94  ? 138  GLY E C   1 
ATOM   5406  O  O   . GLY E  1 138 ? 42.046  111.323 54.756  1.00 8.64  ? 138  GLY E O   1 
ATOM   5407  N  N   . ASN E  1 139 ? 42.084  112.545 52.901  1.00 8.68  ? 139  ASN E N   1 
ATOM   5408  C  CA  . ASN E  1 139 ? 40.619  112.540 52.802  1.00 8.88  ? 139  ASN E CA  1 
ATOM   5409  C  C   . ASN E  1 139 ? 39.996  113.146 54.043  1.00 9.44  ? 139  ASN E C   1 
ATOM   5410  O  O   . ASN E  1 139 ? 38.896  112.750 54.458  1.00 9.31  ? 139  ASN E O   1 
ATOM   5411  C  CB  . ASN E  1 139 ? 40.090  111.107 52.569  1.00 8.72  ? 139  ASN E CB  1 
ATOM   5412  C  CG  . ASN E  1 139 ? 40.343  110.633 51.138  1.00 13.33 ? 139  ASN E CG  1 
ATOM   5413  O  OD1 . ASN E  1 139 ? 39.765  111.182 50.206  1.00 11.85 ? 139  ASN E OD1 1 
ATOM   5414  N  ND2 . ASN E  1 139 ? 41.242  109.661 50.950  1.00 14.32 ? 139  ASN E ND2 1 
ATOM   5415  N  N   . ALA E  1 140 ? 40.680  114.125 54.628  1.00 8.17  ? 140  ALA E N   1 
ATOM   5416  C  CA  . ALA E  1 140 ? 40.162  114.728 55.873  1.00 8.94  ? 140  ALA E CA  1 
ATOM   5417  C  C   . ALA E  1 140 ? 39.020  115.740 55.670  1.00 9.26  ? 140  ALA E C   1 
ATOM   5418  O  O   . ALA E  1 140 ? 38.422  116.238 56.618  1.00 9.85  ? 140  ALA E O   1 
ATOM   5419  C  CB  . ALA E  1 140 ? 41.307  115.347 56.673  1.00 9.04  ? 140  ALA E CB  1 
ATOM   5420  N  N   . GLY E  1 141 ? 38.673  116.013 54.416  1.00 9.86  ? 141  GLY E N   1 
ATOM   5421  C  CA  . GLY E  1 141 ? 37.518  116.849 54.180  1.00 10.46 ? 141  GLY E CA  1 
ATOM   5422  C  C   . GLY E  1 141 ? 37.738  118.317 54.448  1.00 9.80  ? 141  GLY E C   1 
ATOM   5423  O  O   . GLY E  1 141 ? 38.870  118.803 54.473  1.00 9.25  ? 141  GLY E O   1 
ATOM   5424  N  N   . SER E  1 142 ? 36.655  119.012 54.760  1.00 9.98  ? 142  SER E N   1 
ATOM   5425  C  CA  . SER E  1 142 ? 36.719  120.460 54.799  1.00 10.50 ? 142  SER E CA  1 
ATOM   5426  C  C   . SER E  1 142 ? 37.465  121.003 56.007  1.00 9.62  ? 142  SER E C   1 
ATOM   5427  O  O   . SER E  1 142 ? 37.649  120.295 57.013  1.00 8.38  ? 142  SER E O   1 
ATOM   5428  C  CB  . SER E  1 142 ? 35.302  121.054 54.692  1.00 12.24 ? 142  SER E CB  1 
ATOM   5429  O  OG  . SER E  1 142 ? 34.658  120.923 55.931  1.00 15.88 ? 142  SER E OG  1 
ATOM   5430  N  N   . ARG E  1 143 ? 37.914  122.245 55.881  1.00 8.21  ? 143  ARG E N   1 
ATOM   5431  C  CA  . ARG E  1 143 ? 38.702  122.899 56.924  1.00 8.88  ? 143  ARG E CA  1 
ATOM   5432  C  C   . ARG E  1 143 ? 37.743  123.618 57.860  1.00 9.19  ? 143  ARG E C   1 
ATOM   5433  O  O   . ARG E  1 143 ? 37.168  124.623 57.477  1.00 9.77  ? 143  ARG E O   1 
ATOM   5434  C  CB  . ARG E  1 143 ? 39.661  123.889 56.270  1.00 8.51  ? 143  ARG E CB  1 
ATOM   5435  C  CG  . ARG E  1 143 ? 40.510  123.225 55.157  1.00 9.35  ? 143  ARG E CG  1 
ATOM   5436  C  CD  . ARG E  1 143 ? 41.362  124.170 54.313  1.00 10.56 ? 143  ARG E CD  1 
ATOM   5437  N  NE  . ARG E  1 143 ? 42.115  123.362 53.343  1.00 10.03 ? 143  ARG E NE  1 
ATOM   5438  C  CZ  . ARG E  1 143 ? 43.164  123.792 52.656  1.00 11.11 ? 143  ARG E CZ  1 
ATOM   5439  N  NH1 . ARG E  1 143 ? 43.632  125.025 52.852  1.00 11.54 ? 143  ARG E NH1 1 
ATOM   5440  N  NH2 . ARG E  1 143 ? 43.766  122.970 51.801  1.00 8.22  ? 143  ARG E NH2 1 
ATOM   5441  N  N   . LEU E  1 144 ? 37.559  123.110 59.074  1.00 7.42  ? 144  LEU E N   1 
ATOM   5442  C  CA  . LEU E  1 144 ? 36.593  123.733 59.945  1.00 8.96  ? 144  LEU E CA  1 
ATOM   5443  C  C   . LEU E  1 144 ? 37.107  124.974 60.654  1.00 7.88  ? 144  LEU E C   1 
ATOM   5444  O  O   . LEU E  1 144 ? 36.316  125.866 60.936  1.00 8.53  ? 144  LEU E O   1 
ATOM   5445  C  CB  . LEU E  1 144 ? 36.106  122.754 60.998  1.00 9.06  ? 144  LEU E CB  1 
ATOM   5446  C  CG  . LEU E  1 144 ? 35.518  121.457 60.412  1.00 11.39 ? 144  LEU E CG  1 
ATOM   5447  C  CD1 . LEU E  1 144 ? 35.111  120.590 61.584  1.00 16.81 ? 144  LEU E CD1 1 
ATOM   5448  C  CD2 . LEU E  1 144 ? 34.341  121.706 59.447  1.00 14.13 ? 144  LEU E CD2 1 
ATOM   5449  N  N   . ALA E  1 145 ? 38.393  125.005 60.998  1.00 7.49  ? 145  ALA E N   1 
ATOM   5450  C  CA  . ALA E  1 145 ? 38.934  126.154 61.754  1.00 7.35  ? 145  ALA E CA  1 
ATOM   5451  C  C   . ALA E  1 145 ? 40.420  126.175 61.517  1.00 7.46  ? 145  ALA E C   1 
ATOM   5452  O  O   . ALA E  1 145 ? 41.010  125.124 61.251  1.00 6.94  ? 145  ALA E O   1 
ATOM   5453  C  CB  . ALA E  1 145 ? 38.627  126.076 63.268  1.00 8.10  ? 145  ALA E CB  1 
ATOM   5454  N  N   . CYS E  1 146 ? 41.019  127.359 61.532  1.00 7.77  ? 146  CYS E N   1 
ATOM   5455  C  CA  . CYS E  1 146 ? 42.443  127.443 61.272  1.00 8.01  ? 146  CYS E CA  1 
ATOM   5456  C  C   . CYS E  1 146 ? 42.970  128.722 61.900  1.00 7.59  ? 146  CYS E C   1 
ATOM   5457  O  O   . CYS E  1 146 ? 42.195  129.563 62.367  1.00 7.26  ? 146  CYS E O   1 
ATOM   5458  C  CB  . CYS E  1 146 ? 42.738  127.471 59.756  1.00 9.08  ? 146  CYS E CB  1 
ATOM   5459  S  SG  . CYS E  1 146 ? 41.970  128.884 58.933  1.00 12.73 ? 146  CYS E SG  1 
ATOM   5460  N  N   . GLY E  1 147 ? 44.292  128.824 61.957  1.00 6.79  ? 147  GLY E N   1 
ATOM   5461  C  CA  . GLY E  1 147 ? 44.922  130.050 62.418  1.00 6.92  ? 147  GLY E CA  1 
ATOM   5462  C  C   . GLY E  1 147 ? 46.405  130.072 62.039  1.00 8.07  ? 147  GLY E C   1 
ATOM   5463  O  O   . GLY E  1 147 ? 47.021  129.021 61.743  1.00 7.55  ? 147  GLY E O   1 
ATOM   5464  N  N   . VAL E  1 148 ? 46.991  131.277 62.054  1.00 8.47  ? 148  VAL E N   1 
ATOM   5465  C  CA  . VAL E  1 148 ? 48.408  131.398 61.762  1.00 8.68  ? 148  VAL E CA  1 
ATOM   5466  C  C   . VAL E  1 148 ? 49.173  131.062 63.026  1.00 9.03  ? 148  VAL E C   1 
ATOM   5467  O  O   . VAL E  1 148 ? 48.754  131.430 64.133  1.00 8.40  ? 148  VAL E O   1 
ATOM   5468  C  CB  . VAL E  1 148 ? 48.781  132.854 61.282  1.00 8.45  ? 148  VAL E CB  1 
ATOM   5469  C  CG1 . VAL E  1 148 ? 50.257  132.933 60.946  1.00 9.02  ? 148  VAL E CG1 1 
ATOM   5470  C  CG2 . VAL E  1 148 ? 47.893  133.273 60.090  1.00 10.30 ? 148  VAL E CG2 1 
ATOM   5471  N  N   . ILE E  1 149 ? 50.287  130.373 62.880  1.00 7.36  ? 149  ILE E N   1 
ATOM   5472  C  CA  . ILE E  1 149 ? 51.086  129.997 64.019  1.00 7.35  ? 149  ILE E CA  1 
ATOM   5473  C  C   . ILE E  1 149 ? 52.025  131.160 64.343  1.00 8.00  ? 149  ILE E C   1 
ATOM   5474  O  O   . ILE E  1 149 ? 52.858  131.559 63.518  1.00 8.57  ? 149  ILE E O   1 
ATOM   5475  C  CB  . ILE E  1 149 ? 51.866  128.674 63.696  1.00 7.77  ? 149  ILE E CB  1 
ATOM   5476  C  CG1 . ILE E  1 149 ? 50.865  127.545 63.365  1.00 7.86  ? 149  ILE E CG1 1 
ATOM   5477  C  CG2 . ILE E  1 149 ? 52.814  128.325 64.811  1.00 7.41  ? 149  ILE E CG2 1 
ATOM   5478  C  CD1 . ILE E  1 149 ? 51.521  126.221 62.748  1.00 6.94  ? 149  ILE E CD1 1 
ATOM   5479  N  N   . GLY E  1 150 ? 51.888  131.698 65.546  1.00 7.56  ? 150  GLY E N   1 
ATOM   5480  C  CA  . GLY E  1 150 ? 52.708  132.854 65.885  1.00 7.47  ? 150  GLY E CA  1 
ATOM   5481  C  C   . GLY E  1 150 ? 53.692  132.592 66.995  1.00 8.27  ? 150  GLY E C   1 
ATOM   5482  O  O   . GLY E  1 150 ? 53.515  131.654 67.808  1.00 9.42  ? 150  GLY E O   1 
ATOM   5483  N  N   . ILE E  1 151 ? 54.704  133.468 67.073  1.00 6.85  ? 151  ILE E N   1 
ATOM   5484  C  CA  . ILE E  1 151 ? 55.718  133.430 68.129  1.00 7.06  ? 151  ILE E CA  1 
ATOM   5485  C  C   . ILE E  1 151 ? 55.061  133.782 69.454  1.00 7.87  ? 151  ILE E C   1 
ATOM   5486  O  O   . ILE E  1 151 ? 54.353  134.802 69.538  1.00 7.44  ? 151  ILE E O   1 
ATOM   5487  C  CB  . ILE E  1 151 ? 56.847  134.456 67.811  1.00 7.38  ? 151  ILE E CB  1 
ATOM   5488  C  CG1 . ILE E  1 151 ? 57.611  134.026 66.537  1.00 7.76  ? 151  ILE E CG1 1 
ATOM   5489  C  CG2 . ILE E  1 151 ? 57.806  134.661 69.029  1.00 7.86  ? 151  ILE E CG2 1 
ATOM   5490  C  CD1 . ILE E  1 151 ? 58.584  135.080 66.018  1.00 11.92 ? 151  ILE E CD1 1 
ATOM   5491  N  N   . ALA E  1 152 ? 55.303  132.979 70.506  1.00 7.00  ? 152  ALA E N   1 
ATOM   5492  C  CA  . ALA E  1 152 ? 54.685  133.281 71.782  1.00 8.23  ? 152  ALA E CA  1 
ATOM   5493  C  C   . ALA E  1 152 ? 55.772  133.617 72.811  1.00 9.21  ? 152  ALA E C   1 
ATOM   5494  O  O   . ALA E  1 152 ? 56.943  133.317 72.590  1.00 8.88  ? 152  ALA E O   1 
ATOM   5495  C  CB  . ALA E  1 152 ? 53.826  132.117 72.274  1.00 8.74  ? 152  ALA E CB  1 
ATOM   5496  N  N   . GLN E  1 153 ? 55.363  134.262 73.894  1.00 10.78 ? 153  GLN E N   1 
ATOM   5497  C  CA  . GLN E  1 153 ? 56.295  134.742 74.922  1.00 13.76 ? 153  GLN E CA  1 
ATOM   5498  C  C   . GLN E  1 153 ? 56.912  133.596 75.690  1.00 15.54 ? 153  GLN E C   1 
ATOM   5499  O  O   . GLN E  1 153 ? 56.142  132.718 76.049  1.00 16.39 ? 153  GLN E O   1 
ATOM   5500  C  CB  . GLN E  1 153 ? 55.589  135.647 75.921  1.00 13.52 ? 153  GLN E CB  1 
ATOM   5501  C  CG  . GLN E  1 153 ? 56.550  136.189 76.975  1.00 16.67 ? 153  GLN E CG  1 
ATOM   5502  C  CD  . GLN E  1 153 ? 56.012  137.397 77.699  1.00 19.48 ? 153  GLN E CD  1 
ATOM   5503  O  OE1 . GLN E  1 153 ? 54.882  137.374 78.202  1.00 23.27 ? 153  GLN E OE1 1 
ATOM   5504  N  NE2 . GLN E  1 153 ? 56.800  138.464 77.736  1.00 20.44 ? 153  GLN E NE2 1 
ATOM   5505  O  OXT . GLN E  1 153 ? 58.122  133.606 75.964  1.00 17.69 ? 153  GLN E OXT 1 
ATOM   5506  C  C   . LYS F  1 3   ? 1.841   123.126 121.757 1.00 18.32 ? 3    LYS F C   1 
ATOM   5507  O  O   . LYS F  1 3   ? 2.051   124.253 121.289 1.00 16.89 ? 3    LYS F O   1 
ATOM   5508  N  N   . ALA F  1 4   ? 1.221   122.165 121.079 1.00 16.15 ? 4    ALA F N   1 
ATOM   5509  C  CA  . ALA F  1 4   ? 0.627   122.430 119.765 1.00 15.04 ? 4    ALA F CA  1 
ATOM   5510  C  C   . ALA F  1 4   ? -0.677  121.678 119.609 1.00 14.38 ? 4    ALA F C   1 
ATOM   5511  O  O   . ALA F  1 4   ? -1.023  120.778 120.412 1.00 14.30 ? 4    ALA F O   1 
ATOM   5512  C  CB  . ALA F  1 4   ? 1.583   122.114 118.650 1.00 14.27 ? 4    ALA F CB  1 
ATOM   5513  N  N   . VAL F  1 5   ? -1.402  122.020 118.561 1.00 13.33 ? 5    VAL F N   1 
ATOM   5514  C  CA  . VAL F  1 5   ? -2.701  121.449 118.380 1.00 13.34 ? 5    VAL F CA  1 
ATOM   5515  C  C   . VAL F  1 5   ? -3.015  121.430 116.898 1.00 12.72 ? 5    VAL F C   1 
ATOM   5516  O  O   . VAL F  1 5   ? -2.516  122.273 116.126 1.00 12.78 ? 5    VAL F O   1 
ATOM   5517  C  CB  . VAL F  1 5   ? -3.735  122.261 119.148 1.00 13.43 ? 5    VAL F CB  1 
ATOM   5518  C  CG1 . VAL F  1 5   ? -3.927  123.640 118.488 1.00 14.22 ? 5    VAL F CG1 1 
ATOM   5519  C  CG2 . VAL F  1 5   ? -5.063  121.479 119.258 1.00 15.56 ? 5    VAL F CG2 1 
ATOM   5520  N  N   . CYS F  1 6   ? -3.835  120.470 116.494 1.00 12.65 ? 6    CYS F N   1 
ATOM   5521  C  CA  . CYS F  1 6   ? -4.203  120.353 115.083 1.00 12.66 ? 6    CYS F CA  1 
ATOM   5522  C  C   . CYS F  1 6   ? -5.654  119.932 114.981 1.00 12.60 ? 6    CYS F C   1 
ATOM   5523  O  O   . CYS F  1 6   ? -6.086  118.996 115.656 1.00 12.90 ? 6    CYS F O   1 
ATOM   5524  C  CB  . CYS F  1 6   ? -3.323  119.316 114.382 1.00 13.55 ? 6    CYS F CB  1 
ATOM   5525  S  SG  . CYS F  1 6   ? -3.748  119.108 112.623 1.00 14.46 ? 6    CYS F SG  1 
ATOM   5526  N  N   . VAL F  1 7   ? -6.403  120.635 114.140 1.00 12.92 ? 7    VAL F N   1 
ATOM   5527  C  CA  . VAL F  1 7   ? -7.790  120.274 113.886 1.00 12.25 ? 7    VAL F CA  1 
ATOM   5528  C  C   . VAL F  1 7   ? -7.851  119.604 112.538 1.00 12.61 ? 7    VAL F C   1 
ATOM   5529  O  O   . VAL F  1 7   ? -7.561  120.231 111.523 1.00 11.71 ? 7    VAL F O   1 
ATOM   5530  C  CB  . VAL F  1 7   ? -8.691  121.513 113.869 1.00 12.54 ? 7    VAL F CB  1 
ATOM   5531  C  CG1 . VAL F  1 7   ? -10.150 121.126 113.530 1.00 14.24 ? 7    VAL F CG1 1 
ATOM   5532  C  CG2 . VAL F  1 7   ? -8.642  122.186 115.230 1.00 13.26 ? 7    VAL F CG2 1 
ATOM   5533  N  N   . LEU F  1 8   ? -8.236  118.329 112.515 1.00 12.96 ? 8    LEU F N   1 
ATOM   5534  C  CA  . LEU F  1 8   ? -8.326  117.601 111.258 1.00 14.51 ? 8    LEU F CA  1 
ATOM   5535  C  C   . LEU F  1 8   ? -9.714  117.680 110.645 1.00 14.10 ? 8    LEU F C   1 
ATOM   5536  O  O   . LEU F  1 8   ? -10.705 117.380 111.304 1.00 14.51 ? 8    LEU F O   1 
ATOM   5537  C  CB  . LEU F  1 8   ? -7.975  116.130 111.486 1.00 14.49 ? 8    LEU F CB  1 
ATOM   5538  C  CG  . LEU F  1 8   ? -6.546  115.566 111.382 1.00 19.61 ? 8    LEU F CG  1 
ATOM   5539  C  CD1 . LEU F  1 8   ? -5.470  116.574 111.395 1.00 24.69 ? 8    LEU F CD1 1 
ATOM   5540  C  CD2 . LEU F  1 8   ? -6.323  114.494 112.461 1.00 24.92 ? 8    LEU F CD2 1 
ATOM   5541  N  N   . LYS F  1 9   ? -9.773  118.026 109.361 1.00 14.36 ? 9    LYS F N   1 
ATOM   5542  C  CA  . LYS F  1 9   ? -11.011 118.063 108.601 1.00 14.59 ? 9    LYS F CA  1 
ATOM   5543  C  C   . LYS F  1 9   ? -10.705 117.658 107.188 1.00 14.62 ? 9    LYS F C   1 
ATOM   5544  O  O   . LYS F  1 9   ? -9.553  117.794 106.721 1.00 13.92 ? 9    LYS F O   1 
ATOM   5545  C  CB  . LYS F  1 9   ? -11.582 119.491 108.537 1.00 15.42 ? 9    LYS F CB  1 
ATOM   5546  C  CG  . LYS F  1 9   ? -12.184 119.959 109.829 1.00 18.41 ? 9    LYS F CG  1 
ATOM   5547  C  CD  . LYS F  1 9   ? -12.687 121.396 109.684 1.00 23.16 ? 9    LYS F CD  1 
ATOM   5548  C  CE  . LYS F  1 9   ? -13.660 121.720 110.802 1.00 25.60 ? 9    LYS F CE  1 
ATOM   5549  N  NZ  . LYS F  1 9   ? -13.922 123.187 110.852 1.00 27.39 ? 9    LYS F NZ  1 
ATOM   5550  N  N   . GLY F  1 10  ? -11.741 117.205 106.477 1.00 15.85 ? 10   GLY F N   1 
ATOM   5551  C  CA  . GLY F  1 10  ? -11.603 116.888 105.068 1.00 16.02 ? 10   GLY F CA  1 
ATOM   5552  C  C   . GLY F  1 10  ? -12.875 117.133 104.279 1.00 16.85 ? 10   GLY F C   1 
ATOM   5553  O  O   . GLY F  1 10  ? -13.721 117.948 104.679 1.00 15.76 ? 10   GLY F O   1 
ATOM   5554  N  N   . ASP F  1 11  ? -13.016 116.420 103.159 1.00 16.50 ? 11   ASP F N   1 
ATOM   5555  C  CA  . ASP F  1 11  ? -14.193 116.600 102.324 1.00 17.01 ? 11   ASP F CA  1 
ATOM   5556  C  C   . ASP F  1 11  ? -15.277 115.625 102.734 1.00 15.46 ? 11   ASP F C   1 
ATOM   5557  O  O   . ASP F  1 11  ? -16.403 115.703 102.233 1.00 15.71 ? 11   ASP F O   1 
ATOM   5558  C  CB  . ASP F  1 11  ? -13.858 116.418 100.838 1.00 18.07 ? 11   ASP F CB  1 
ATOM   5559  C  CG  . ASP F  1 11  ? -12.985 117.541 100.301 1.00 23.00 ? 11   ASP F CG  1 
ATOM   5560  O  OD1 . ASP F  1 11  ? -13.106 118.691 100.798 1.00 24.43 ? 11   ASP F OD1 1 
ATOM   5561  O  OD2 . ASP F  1 11  ? -12.132 117.347 99.405  1.00 30.42 ? 11   ASP F OD2 1 
ATOM   5562  N  N   . GLY F  1 12  ? -14.936 114.702 103.638 1.00 14.07 ? 12   GLY F N   1 
ATOM   5563  C  CA  . GLY F  1 12  ? -15.869 113.668 104.066 1.00 12.69 ? 12   GLY F CA  1 
ATOM   5564  C  C   . GLY F  1 12  ? -16.271 113.765 105.530 1.00 11.79 ? 12   GLY F C   1 
ATOM   5565  O  O   . GLY F  1 12  ? -16.316 114.858 106.079 1.00 10.45 ? 12   GLY F O   1 
ATOM   5566  N  N   . PRO F  1 13  ? -16.563 112.631 106.161 1.00 11.81 ? 13   PRO F N   1 
ATOM   5567  C  CA  . PRO F  1 13  ? -16.994 112.609 107.569 1.00 12.10 ? 13   PRO F CA  1 
ATOM   5568  C  C   . PRO F  1 13  ? -15.898 112.693 108.634 1.00 12.15 ? 13   PRO F C   1 
ATOM   5569  O  O   . PRO F  1 13  ? -16.221 112.817 109.824 1.00 11.59 ? 13   PRO F O   1 
ATOM   5570  C  CB  . PRO F  1 13  ? -17.661 111.246 107.682 1.00 11.25 ? 13   PRO F CB  1 
ATOM   5571  C  CG  . PRO F  1 13  ? -16.795 110.357 106.763 1.00 12.57 ? 13   PRO F CG  1 
ATOM   5572  C  CD  . PRO F  1 13  ? -16.490 111.273 105.578 1.00 11.24 ? 13   PRO F CD  1 
ATOM   5573  N  N   . VAL F  1 14  ? -14.637 112.604 108.238 1.00 12.14 ? 14   VAL F N   1 
ATOM   5574  C  CA  . VAL F  1 14  ? -13.566 112.486 109.213 1.00 12.69 ? 14   VAL F CA  1 
ATOM   5575  C  C   . VAL F  1 14  ? -13.281 113.806 109.898 1.00 13.51 ? 14   VAL F C   1 
ATOM   5576  O  O   . VAL F  1 14  ? -13.047 114.815 109.244 1.00 14.15 ? 14   VAL F O   1 
ATOM   5577  C  CB  . VAL F  1 14  ? -12.292 111.865 108.586 1.00 12.08 ? 14   VAL F CB  1 
ATOM   5578  C  CG1 . VAL F  1 14  ? -11.229 111.624 109.643 1.00 11.91 ? 14   VAL F CG1 1 
ATOM   5579  C  CG2 . VAL F  1 14  ? -12.663 110.500 107.929 1.00 11.48 ? 14   VAL F CG2 1 
ATOM   5580  N  N   . GLN F  1 15  ? -13.364 113.800 111.220 1.00 14.44 ? 15   GLN F N   1 
ATOM   5581  C  CA  . GLN F  1 15  ? -13.023 114.988 112.001 1.00 15.63 ? 15   GLN F CA  1 
ATOM   5582  C  C   . GLN F  1 15  ? -12.274 114.637 113.269 1.00 14.97 ? 15   GLN F C   1 
ATOM   5583  O  O   . GLN F  1 15  ? -12.591 113.665 113.954 1.00 15.40 ? 15   GLN F O   1 
ATOM   5584  C  CB  . GLN F  1 15  ? -14.211 115.912 112.263 1.00 16.17 ? 15   GLN F CB  1 
ATOM   5585  C  CG  . GLN F  1 15  ? -15.418 115.343 112.910 1.00 20.63 ? 15   GLN F CG  1 
ATOM   5586  N  N   . GLY F  1 16  ? -11.215 115.368 113.540 1.00 13.89 ? 16   GLY F N   1 
ATOM   5587  C  CA  . GLY F  1 16  ? -10.437 115.011 114.713 1.00 13.11 ? 16   GLY F CA  1 
ATOM   5588  C  C   . GLY F  1 16  ? -9.796  116.226 115.331 1.00 12.85 ? 16   GLY F C   1 
ATOM   5589  O  O   . GLY F  1 16  ? -9.752  117.283 114.712 1.00 12.15 ? 16   GLY F O   1 
ATOM   5590  N  N   . ILE F  1 17  ? -9.342  116.084 116.572 1.00 12.09 ? 17   ILE F N   1 
ATOM   5591  C  CA  . ILE F  1 17  ? -8.528  117.121 117.200 1.00 13.09 ? 17   ILE F CA  1 
ATOM   5592  C  C   . ILE F  1 17  ? -7.383  116.379 117.810 1.00 12.87 ? 17   ILE F C   1 
ATOM   5593  O  O   . ILE F  1 17  ? -7.603  115.376 118.505 1.00 12.06 ? 17   ILE F O   1 
ATOM   5594  C  CB  . ILE F  1 17  ? -9.273  117.848 118.332 1.00 13.95 ? 17   ILE F CB  1 
ATOM   5595  C  CG1 . ILE F  1 17  ? -10.366 118.747 117.758 1.00 14.28 ? 17   ILE F CG1 1 
ATOM   5596  C  CG2 . ILE F  1 17  ? -8.270  118.703 119.153 1.00 13.02 ? 17   ILE F CG2 1 
ATOM   5597  C  CD1 . ILE F  1 17  ? -11.222 119.470 118.821 1.00 15.46 ? 17   ILE F CD1 1 
ATOM   5598  N  N   . ILE F  1 18  ? -6.172  116.843 117.557 1.00 12.47 ? 18   ILE F N   1 
ATOM   5599  C  CA  . ILE F  1 18  ? -4.995  116.173 118.077 1.00 13.10 ? 18   ILE F CA  1 
ATOM   5600  C  C   . ILE F  1 18  ? -4.136  117.199 118.762 1.00 13.84 ? 18   ILE F C   1 
ATOM   5601  O  O   . ILE F  1 18  ? -3.882  118.265 118.216 1.00 13.03 ? 18   ILE F O   1 
ATOM   5602  C  CB  . ILE F  1 18  ? -4.173  115.490 116.955 1.00 12.83 ? 18   ILE F CB  1 
ATOM   5603  C  CG1 . ILE F  1 18  ? -5.004  114.452 116.197 1.00 12.63 ? 18   ILE F CG1 1 
ATOM   5604  C  CG2 . ILE F  1 18  ? -2.855  114.915 117.507 1.00 14.26 ? 18   ILE F CG2 1 
ATOM   5605  C  CD1 . ILE F  1 18  ? -5.267  113.100 116.955 1.00 12.88 ? 18   ILE F CD1 1 
ATOM   5606  N  N   . ASN F  1 19  ? -3.658  116.837 119.954 1.00 14.02 ? 19   ASN F N   1 
ATOM   5607  C  CA  . ASN F  1 19  ? -2.832  117.709 120.777 1.00 14.89 ? 19   ASN F CA  1 
ATOM   5608  C  C   . ASN F  1 19  ? -1.382  117.239 120.781 1.00 15.02 ? 19   ASN F C   1 
ATOM   5609  O  O   . ASN F  1 19  ? -1.141  116.047 120.635 1.00 13.99 ? 19   ASN F O   1 
ATOM   5610  C  CB  . ASN F  1 19  ? -3.353  117.652 122.219 1.00 14.41 ? 19   ASN F CB  1 
ATOM   5611  C  CG  . ASN F  1 19  ? -4.832  117.952 122.301 1.00 16.37 ? 19   ASN F CG  1 
ATOM   5612  O  OD1 . ASN F  1 19  ? -5.658  117.054 122.518 1.00 19.10 ? 19   ASN F OD1 1 
ATOM   5613  N  ND2 . ASN F  1 19  ? -5.183  119.215 122.081 1.00 11.90 ? 19   ASN F ND2 1 
ATOM   5614  N  N   . PHE F  1 20  ? -0.437  118.175 120.932 1.00 14.65 ? 20   PHE F N   1 
ATOM   5615  C  CA  . PHE F  1 20  ? 0.996   117.856 121.051 1.00 15.22 ? 20   PHE F CA  1 
ATOM   5616  C  C   . PHE F  1 20  ? 1.585   118.549 122.282 1.00 16.84 ? 20   PHE F C   1 
ATOM   5617  O  O   . PHE F  1 20  ? 1.228   119.682 122.596 1.00 16.23 ? 20   PHE F O   1 
ATOM   5618  C  CB  . PHE F  1 20  ? 1.793   118.301 119.820 1.00 14.76 ? 20   PHE F CB  1 
ATOM   5619  C  CG  . PHE F  1 20  ? 1.294   117.707 118.510 1.00 13.84 ? 20   PHE F CG  1 
ATOM   5620  C  CD1 . PHE F  1 20  ? 0.164   118.232 117.893 1.00 13.67 ? 20   PHE F CD1 1 
ATOM   5621  C  CD2 . PHE F  1 20  ? 1.975   116.682 117.892 1.00 15.35 ? 20   PHE F CD2 1 
ATOM   5622  C  CE1 . PHE F  1 20  ? -0.292  117.727 116.693 1.00 15.88 ? 20   PHE F CE1 1 
ATOM   5623  C  CE2 . PHE F  1 20  ? 1.510   116.149 116.680 1.00 15.21 ? 20   PHE F CE2 1 
ATOM   5624  C  CZ  . PHE F  1 20  ? 0.382   116.679 116.082 1.00 16.35 ? 20   PHE F CZ  1 
ATOM   5625  N  N   . GLU F  1 21  ? 2.521   117.882 122.954 1.00 18.73 ? 21   GLU F N   1 
ATOM   5626  C  CA  . GLU F  1 21  ? 3.110   118.453 124.169 1.00 22.62 ? 21   GLU F CA  1 
ATOM   5627  C  CB  . GLU F  1 21  ? 2.283   118.125 125.423 1.00 22.37 ? 21   GLU F CB  1 
ATOM   5628  C  CG  . GLU F  1 21  ? 2.773   118.824 126.691 1.00 24.47 ? 21   GLU F CG  1 
ATOM   5629  N  N   . PRO F  1 28  ? 10.735  113.822 124.379 1.00 34.67 ? 28   PRO F N   1 
ATOM   5630  C  CA  . PRO F  1 28  ? 9.632   113.158 123.691 1.00 32.47 ? 28   PRO F CA  1 
ATOM   5631  C  C   . PRO F  1 28  ? 8.481   114.100 123.478 1.00 30.36 ? 28   PRO F C   1 
ATOM   5632  O  O   . PRO F  1 28  ? 8.235   114.987 124.309 1.00 28.90 ? 28   PRO F O   1 
ATOM   5633  C  CB  . PRO F  1 28  ? 9.185   112.084 124.685 1.00 33.22 ? 28   PRO F CB  1 
ATOM   5634  C  CG  . PRO F  1 28  ? 10.338  111.883 125.594 1.00 34.24 ? 28   PRO F CG  1 
ATOM   5635  C  CD  . PRO F  1 28  ? 11.047  113.198 125.675 1.00 34.81 ? 28   PRO F CD  1 
ATOM   5636  N  N   . VAL F  1 29  ? 7.790   113.918 122.356 1.00 27.13 ? 29   VAL F N   1 
ATOM   5637  C  CA  . VAL F  1 29  ? 6.582   114.655 122.138 1.00 24.46 ? 29   VAL F CA  1 
ATOM   5638  C  C   . VAL F  1 29  ? 5.457   113.694 122.337 1.00 23.04 ? 29   VAL F C   1 
ATOM   5639  O  O   . VAL F  1 29  ? 5.407   112.618 121.734 1.00 22.13 ? 29   VAL F O   1 
ATOM   5640  C  CB  . VAL F  1 29  ? 6.433   115.198 120.734 1.00 25.07 ? 29   VAL F CB  1 
ATOM   5641  C  CG1 . VAL F  1 29  ? 5.095   115.948 120.631 1.00 24.52 ? 29   VAL F CG1 1 
ATOM   5642  C  CG2 . VAL F  1 29  ? 7.609   116.071 120.370 1.00 24.39 ? 29   VAL F CG2 1 
ATOM   5643  N  N   . LYS F  1 30  ? 4.558   114.096 123.211 1.00 20.66 ? 30   LYS F N   1 
ATOM   5644  C  CA  . LYS F  1 30  ? 3.342   113.365 123.458 1.00 19.54 ? 30   LYS F CA  1 
ATOM   5645  C  C   . LYS F  1 30  ? 2.259   113.807 122.488 1.00 18.57 ? 30   LYS F C   1 
ATOM   5646  O  O   . LYS F  1 30  ? 2.022   114.996 122.327 1.00 17.17 ? 30   LYS F O   1 
ATOM   5647  C  CB  . LYS F  1 30  ? 2.852   113.666 124.870 1.00 20.63 ? 30   LYS F CB  1 
ATOM   5648  C  CG  . LYS F  1 30  ? 3.658   113.003 125.977 1.00 22.61 ? 30   LYS F CG  1 
ATOM   5649  C  CD  . LYS F  1 30  ? 3.040   113.344 127.340 1.00 26.88 ? 30   LYS F CD  1 
ATOM   5650  C  CE  . LYS F  1 30  ? 3.905   112.891 128.523 1.00 28.86 ? 30   LYS F CE  1 
ATOM   5651  N  NZ  . LYS F  1 30  ? 3.445   113.533 129.820 1.00 29.72 ? 30   LYS F NZ  1 
ATOM   5652  N  N   . VAL F  1 31  ? 1.595   112.864 121.841 1.00 16.59 ? 31   VAL F N   1 
ATOM   5653  C  CA  . VAL F  1 31  ? 0.506   113.270 120.973 1.00 16.81 ? 31   VAL F CA  1 
ATOM   5654  C  C   . VAL F  1 31  ? -0.770  112.516 121.303 1.00 16.79 ? 31   VAL F C   1 
ATOM   5655  O  O   . VAL F  1 31  ? -0.753  111.286 121.515 1.00 17.83 ? 31   VAL F O   1 
ATOM   5656  C  CB  . VAL F  1 31  ? 0.944   113.328 119.482 1.00 17.13 ? 31   VAL F CB  1 
ATOM   5657  C  CG1 . VAL F  1 31  ? 2.313   112.806 119.252 1.00 14.78 ? 31   VAL F CG1 1 
ATOM   5658  C  CG2 . VAL F  1 31  ? -0.147  112.959 118.462 1.00 16.90 ? 31   VAL F CG2 1 
ATOM   5659  N  N   . TRP F  1 32  ? -1.866  113.254 121.438 1.00 16.23 ? 32   TRP F N   1 
ATOM   5660  C  CA  . TRP F  1 32  ? -3.093  112.584 121.835 1.00 16.69 ? 32   TRP F CA  1 
ATOM   5661  C  C   . TRP F  1 32  ? -4.342  113.301 121.389 1.00 17.16 ? 32   TRP F C   1 
ATOM   5662  O  O   . TRP F  1 32  ? -4.345  114.520 121.196 1.00 16.64 ? 32   TRP F O   1 
ATOM   5663  C  CB  . TRP F  1 32  ? -3.126  112.430 123.354 1.00 16.48 ? 32   TRP F CB  1 
ATOM   5664  C  CG  . TRP F  1 32  ? -3.460  113.661 124.098 1.00 17.83 ? 32   TRP F CG  1 
ATOM   5665  C  CD1 . TRP F  1 32  ? -4.669  114.000 124.620 1.00 17.89 ? 32   TRP F CD1 1 
ATOM   5666  C  CD2 . TRP F  1 32  ? -2.568  114.728 124.432 1.00 17.84 ? 32   TRP F CD2 1 
ATOM   5667  N  NE1 . TRP F  1 32  ? -4.584  115.215 125.262 1.00 20.46 ? 32   TRP F NE1 1 
ATOM   5668  C  CE2 . TRP F  1 32  ? -3.299  115.677 125.161 1.00 19.02 ? 32   TRP F CE2 1 
ATOM   5669  C  CE3 . TRP F  1 32  ? -1.213  114.970 124.192 1.00 20.37 ? 32   TRP F CE3 1 
ATOM   5670  C  CZ2 . TRP F  1 32  ? -2.729  116.853 125.644 1.00 21.31 ? 32   TRP F CZ2 1 
ATOM   5671  C  CZ3 . TRP F  1 32  ? -0.646  116.125 124.670 1.00 20.17 ? 32   TRP F CZ3 1 
ATOM   5672  C  CH2 . TRP F  1 32  ? -1.402  117.059 125.384 1.00 21.35 ? 32   TRP F CH2 1 
ATOM   5673  N  N   . GLY F  1 33  ? -5.413  112.535 121.233 1.00 17.40 ? 33   GLY F N   1 
ATOM   5674  C  CA  . GLY F  1 33  ? -6.664  113.135 120.819 1.00 18.01 ? 33   GLY F CA  1 
ATOM   5675  C  C   . GLY F  1 33  ? -7.667  112.101 120.392 1.00 17.97 ? 33   GLY F C   1 
ATOM   5676  O  O   . GLY F  1 33  ? -7.616  110.951 120.811 1.00 18.00 ? 33   GLY F O   1 
ATOM   5677  N  N   . SER F  1 34  ? -8.574  112.523 119.532 1.00 17.64 ? 34   SER F N   1 
ATOM   5678  C  CA  . SER F  1 34  ? -9.614  111.647 119.071 1.00 17.29 ? 34   SER F CA  1 
ATOM   5679  C  C   . SER F  1 34  ? -9.907  112.016 117.629 1.00 16.93 ? 34   SER F C   1 
ATOM   5680  O  O   . SER F  1 34  ? -9.948  113.182 117.293 1.00 15.43 ? 34   SER F O   1 
ATOM   5681  C  CB  . SER F  1 34  ? -10.870 111.879 119.920 1.00 17.57 ? 34   SER F CB  1 
ATOM   5682  O  OG  . SER F  1 34  ? -11.888 110.969 119.562 1.00 19.20 ? 34   SER F OG  1 
ATOM   5683  N  N   . ILE F  1 35  ? -10.092 111.017 116.775 1.00 15.48 ? 35   ILE F N   1 
ATOM   5684  C  CA  . ILE F  1 35  ? -10.504 111.261 115.408 1.00 14.93 ? 35   ILE F CA  1 
ATOM   5685  C  C   . ILE F  1 35  ? -11.755 110.399 115.231 1.00 15.18 ? 35   ILE F C   1 
ATOM   5686  O  O   . ILE F  1 35  ? -11.768 109.239 115.645 1.00 15.11 ? 35   ILE F O   1 
ATOM   5687  C  CB  . ILE F  1 35  ? -9.426  110.816 114.452 1.00 14.55 ? 35   ILE F CB  1 
ATOM   5688  C  CG1 . ILE F  1 35  ? -8.103  111.510 114.780 1.00 15.31 ? 35   ILE F CG1 1 
ATOM   5689  C  CG2 . ILE F  1 35  ? -9.832  111.092 112.989 1.00 14.56 ? 35   ILE F CG2 1 
ATOM   5690  C  CD1 . ILE F  1 35  ? -6.961  110.975 113.959 1.00 17.03 ? 35   ILE F CD1 1 
ATOM   5691  N  N   . LYS F  1 36  ? -12.785 110.948 114.599 1.00 14.50 ? 36   LYS F N   1 
ATOM   5692  C  CA  . LYS F  1 36  ? -14.039 110.215 114.449 1.00 14.65 ? 36   LYS F CA  1 
ATOM   5693  C  C   . LYS F  1 36  ? -14.439 110.146 112.993 1.00 14.22 ? 36   LYS F C   1 
ATOM   5694  O  O   . LYS F  1 36  ? -13.823 110.815 112.163 1.00 14.74 ? 36   LYS F O   1 
ATOM   5695  C  CB  . LYS F  1 36  ? -15.128 110.851 115.332 1.00 15.61 ? 36   LYS F CB  1 
ATOM   5696  N  N   . GLY F  1 37  ? -15.447 109.340 112.673 1.00 13.65 ? 37   GLY F N   1 
ATOM   5697  C  CA  . GLY F  1 37  ? -15.909 109.230 111.305 1.00 13.90 ? 37   GLY F CA  1 
ATOM   5698  C  C   . GLY F  1 37  ? -15.053 108.312 110.447 1.00 13.50 ? 37   GLY F C   1 
ATOM   5699  O  O   . GLY F  1 37  ? -15.159 108.328 109.231 1.00 13.83 ? 37   GLY F O   1 
ATOM   5700  N  N   . LEU F  1 38  ? -14.226 107.493 111.081 1.00 14.21 ? 38   LEU F N   1 
ATOM   5701  C  CA  . LEU F  1 38  ? -13.319 106.581 110.365 1.00 13.93 ? 38   LEU F CA  1 
ATOM   5702  C  C   . LEU F  1 38  ? -13.870 105.170 110.177 1.00 14.45 ? 38   LEU F C   1 
ATOM   5703  O  O   . LEU F  1 38  ? -14.684 104.739 110.974 1.00 14.53 ? 38   LEU F O   1 
ATOM   5704  C  CB  . LEU F  1 38  ? -12.024 106.453 111.172 1.00 14.18 ? 38   LEU F CB  1 
ATOM   5705  C  CG  . LEU F  1 38  ? -11.125 107.694 111.151 1.00 13.88 ? 38   LEU F CG  1 
ATOM   5706  C  CD1 . LEU F  1 38  ? -10.127 107.564 112.259 1.00 15.30 ? 38   LEU F CD1 1 
ATOM   5707  C  CD2 . LEU F  1 38  ? -10.438 107.872 109.786 1.00 16.15 ? 38   LEU F CD2 1 
ATOM   5708  N  N   . THR F  1 39  ? -13.432 104.456 109.135 1.00 14.34 ? 39   THR F N   1 
ATOM   5709  C  CA  . THR F  1 39  ? -13.751 103.017 109.043 1.00 15.85 ? 39   THR F CA  1 
ATOM   5710  C  C   . THR F  1 39  ? -12.982 102.246 110.116 1.00 15.96 ? 39   THR F C   1 
ATOM   5711  O  O   . THR F  1 39  ? -11.817 102.537 110.387 1.00 15.82 ? 39   THR F O   1 
ATOM   5712  C  CB  . THR F  1 39  ? -13.422 102.398 107.656 1.00 16.13 ? 39   THR F CB  1 
ATOM   5713  O  OG1 . THR F  1 39  ? -12.067 102.690 107.289 1.00 16.63 ? 39   THR F OG1 1 
ATOM   5714  C  CG2 . THR F  1 39  ? -14.278 103.010 106.537 1.00 17.29 ? 39   THR F CG2 1 
ATOM   5715  N  N   . GLU F  1 40  ? -13.644 101.257 110.722 1.00 16.14 ? 40   GLU F N   1 
ATOM   5716  C  CA  . GLU F  1 40  ? -13.019 100.431 111.749 1.00 16.43 ? 40   GLU F CA  1 
ATOM   5717  C  C   . GLU F  1 40  ? -11.673 99.900  111.230 1.00 16.03 ? 40   GLU F C   1 
ATOM   5718  O  O   . GLU F  1 40  ? -11.572 99.471  110.082 1.00 16.51 ? 40   GLU F O   1 
ATOM   5719  C  CB  . GLU F  1 40  ? -13.936 99.236  112.107 1.00 16.71 ? 40   GLU F CB  1 
ATOM   5720  C  CG  . GLU F  1 40  ? -13.463 98.467  113.331 1.00 18.00 ? 40   GLU F CG  1 
ATOM   5721  C  CD  . GLU F  1 40  ? -14.273 97.220  113.634 1.00 21.15 ? 40   GLU F CD  1 
ATOM   5722  O  OE1 . GLU F  1 40  ? -15.332 97.000  112.994 1.00 20.83 ? 40   GLU F OE1 1 
ATOM   5723  O  OE2 . GLU F  1 40  ? -13.830 96.449  114.523 1.00 20.17 ? 40   GLU F OE2 1 
ATOM   5724  N  N   . GLY F  1 41  ? -10.637 99.919  112.058 1.00 15.70 ? 41   GLY F N   1 
ATOM   5725  C  CA  . GLY F  1 41  ? -9.347  99.414  111.603 1.00 15.34 ? 41   GLY F CA  1 
ATOM   5726  C  C   . GLY F  1 41  ? -8.207  100.429 111.622 1.00 14.95 ? 41   GLY F C   1 
ATOM   5727  O  O   . GLY F  1 41  ? -8.328  101.501 112.230 1.00 15.08 ? 41   GLY F O   1 
ATOM   5728  N  N   . LEU F  1 42  ? -7.099  100.092 110.960 1.00 14.53 ? 42   LEU F N   1 
ATOM   5729  C  CA  . LEU F  1 42  ? -5.903  100.939 110.978 1.00 14.64 ? 42   LEU F CA  1 
ATOM   5730  C  C   . LEU F  1 42  ? -5.939  102.024 109.924 1.00 14.15 ? 42   LEU F C   1 
ATOM   5731  O  O   . LEU F  1 42  ? -6.368  101.774 108.785 1.00 13.56 ? 42   LEU F O   1 
ATOM   5732  C  CB  . LEU F  1 42  ? -4.664  100.091 110.696 1.00 15.80 ? 42   LEU F CB  1 
ATOM   5733  C  CG  . LEU F  1 42  ? -3.872  99.398  111.811 1.00 16.74 ? 42   LEU F CG  1 
ATOM   5734  C  CD1 . LEU F  1 42  ? -4.719  99.219  113.016 1.00 20.93 ? 42   LEU F CD1 1 
ATOM   5735  C  CD2 . LEU F  1 42  ? -3.326  98.047  111.283 1.00 19.23 ? 42   LEU F CD2 1 
ATOM   5736  N  N   . HIS F  1 43  ? -5.423  103.200 110.286 1.00 13.24 ? 43   HIS F N   1 
ATOM   5737  C  CA  . HIS F  1 43  ? -5.311  104.327 109.349 1.00 12.82 ? 43   HIS F CA  1 
ATOM   5738  C  C   . HIS F  1 43  ? -3.966  105.015 109.493 1.00 12.00 ? 43   HIS F C   1 
ATOM   5739  O  O   . HIS F  1 43  ? -3.587  105.375 110.595 1.00 12.22 ? 43   HIS F O   1 
ATOM   5740  C  CB  . HIS F  1 43  ? -6.425  105.341 109.627 1.00 12.93 ? 43   HIS F CB  1 
ATOM   5741  C  CG  . HIS F  1 43  ? -7.788  104.797 109.345 1.00 12.57 ? 43   HIS F CG  1 
ATOM   5742  N  ND1 . HIS F  1 43  ? -8.375  104.892 108.103 1.00 13.99 ? 43   HIS F ND1 1 
ATOM   5743  C  CD2 . HIS F  1 43  ? -8.683  104.160 110.142 1.00 13.06 ? 43   HIS F CD2 1 
ATOM   5744  C  CE1 . HIS F  1 43  ? -9.578  104.345 108.146 1.00 14.04 ? 43   HIS F CE1 1 
ATOM   5745  N  NE2 . HIS F  1 43  ? -9.787  103.884 109.367 1.00 11.63 ? 43   HIS F NE2 1 
ATOM   5746  N  N   . GLY F  1 44  ? -3.225  105.152 108.389 1.00 11.96 ? 44   GLY F N   1 
ATOM   5747  C  CA  . GLY F  1 44  ? -1.944  105.831 108.410 1.00 10.16 ? 44   GLY F CA  1 
ATOM   5748  C  C   . GLY F  1 44  ? -2.067  107.258 109.011 1.00 11.44 ? 44   GLY F C   1 
ATOM   5749  O  O   . GLY F  1 44  ? -3.057  107.965 108.796 1.00 9.93  ? 44   GLY F O   1 
ATOM   5750  N  N   . PHE F  1 45  ? -1.034  107.661 109.728 1.00 10.80 ? 45   PHE F N   1 
ATOM   5751  C  CA  . PHE F  1 45  ? -1.045  108.905 110.515 1.00 12.01 ? 45   PHE F CA  1 
ATOM   5752  C  C   . PHE F  1 45  ? 0.341   109.508 110.394 1.00 11.23 ? 45   PHE F C   1 
ATOM   5753  O  O   . PHE F  1 45  ? 1.301   108.965 110.940 1.00 11.02 ? 45   PHE F O   1 
ATOM   5754  C  CB  . PHE F  1 45  ? -1.344  108.498 111.950 1.00 11.61 ? 45   PHE F CB  1 
ATOM   5755  C  CG  . PHE F  1 45  ? -1.610  109.638 112.885 1.00 13.31 ? 45   PHE F CG  1 
ATOM   5756  C  CD1 . PHE F  1 45  ? -2.619  110.558 112.621 1.00 14.06 ? 45   PHE F CD1 1 
ATOM   5757  C  CD2 . PHE F  1 45  ? -0.897  109.736 114.060 1.00 12.27 ? 45   PHE F CD2 1 
ATOM   5758  C  CE1 . PHE F  1 45  ? -2.888  111.590 113.528 1.00 15.05 ? 45   PHE F CE1 1 
ATOM   5759  C  CE2 . PHE F  1 45  ? -1.143  110.739 114.956 1.00 12.91 ? 45   PHE F CE2 1 
ATOM   5760  C  CZ  . PHE F  1 45  ? -2.143  111.678 114.693 1.00 12.39 ? 45   PHE F CZ  1 
ATOM   5761  N  N   . HIS F  1 46  ? 0.436   110.598 109.620 1.00 11.80 ? 46   HIS F N   1 
ATOM   5762  C  CA  . HIS F  1 46  ? 1.708   111.216 109.294 1.00 10.70 ? 46   HIS F CA  1 
ATOM   5763  C  C   . HIS F  1 46  ? 1.706   112.742 109.360 1.00 11.07 ? 46   HIS F C   1 
ATOM   5764  O  O   . HIS F  1 46  ? 0.663   113.384 109.160 1.00 11.78 ? 46   HIS F O   1 
ATOM   5765  C  CB  . HIS F  1 46  ? 2.080   110.891 107.845 1.00 12.17 ? 46   HIS F CB  1 
ATOM   5766  C  CG  . HIS F  1 46  ? 1.854   109.464 107.451 1.00 8.26  ? 46   HIS F CG  1 
ATOM   5767  N  ND1 . HIS F  1 46  ? 1.203   109.105 106.299 1.00 9.40  ? 46   HIS F ND1 1 
ATOM   5768  C  CD2 . HIS F  1 46  ? 2.235   108.303 108.040 1.00 13.68 ? 46   HIS F CD2 1 
ATOM   5769  C  CE1 . HIS F  1 46  ? 1.183   107.791 106.180 1.00 10.18 ? 46   HIS F CE1 1 
ATOM   5770  N  NE2 . HIS F  1 46  ? 1.778   107.276 107.241 1.00 10.62 ? 46   HIS F NE2 1 
ATOM   5771  N  N   . VAL F  1 47  ? 2.901   113.297 109.558 1.00 11.06 ? 47   VAL F N   1 
ATOM   5772  C  CA  . VAL F  1 47  ? 3.131   114.705 109.345 1.00 11.18 ? 47   VAL F CA  1 
ATOM   5773  C  C   . VAL F  1 47  ? 3.724   114.856 107.944 1.00 11.28 ? 47   VAL F C   1 
ATOM   5774  O  O   . VAL F  1 47  ? 4.754   114.255 107.607 1.00 10.76 ? 47   VAL F O   1 
ATOM   5775  C  CB  . VAL F  1 47  ? 4.126   115.322 110.318 1.00 11.63 ? 47   VAL F CB  1 
ATOM   5776  C  CG1 . VAL F  1 47  ? 4.312   116.824 109.989 1.00 10.81 ? 47   VAL F CG1 1 
ATOM   5777  C  CG2 . VAL F  1 47  ? 3.689   115.084 111.779 1.00 11.87 ? 47   VAL F CG2 1 
ATOM   5778  N  N   . HIS F  1 48  ? 3.034   115.641 107.129 1.00 9.90  ? 48   HIS F N   1 
ATOM   5779  C  CA  . HIS F  1 48  ? 3.441   115.973 105.773 1.00 10.10 ? 48   HIS F CA  1 
ATOM   5780  C  C   . HIS F  1 48  ? 4.095   117.320 105.782 1.00 10.09 ? 48   HIS F C   1 
ATOM   5781  O  O   . HIS F  1 48  ? 3.869   118.145 106.700 1.00 10.73 ? 48   HIS F O   1 
ATOM   5782  C  CB  . HIS F  1 48  ? 2.243   115.951 104.794 1.00 9.48  ? 48   HIS F CB  1 
ATOM   5783  C  CG  . HIS F  1 48  ? 1.735   114.568 104.507 1.00 11.17 ? 48   HIS F CG  1 
ATOM   5784  N  ND1 . HIS F  1 48  ? 1.660   114.039 103.234 1.00 10.46 ? 48   HIS F ND1 1 
ATOM   5785  C  CD2 . HIS F  1 48  ? 1.307   113.596 105.348 1.00 10.63 ? 48   HIS F CD2 1 
ATOM   5786  C  CE1 . HIS F  1 48  ? 1.184   112.806 103.300 1.00 11.23 ? 48   HIS F CE1 1 
ATOM   5787  N  NE2 . HIS F  1 48  ? 0.953   112.519 104.571 1.00 10.22 ? 48   HIS F NE2 1 
ATOM   5788  N  N   . GLU F  1 49  ? 4.863   117.579 104.730 1.00 9.82  ? 49   GLU F N   1 
ATOM   5789  C  CA  . GLU F  1 49  ? 5.810   118.678 104.750 1.00 10.89 ? 49   GLU F CA  1 
ATOM   5790  C  C   . GLU F  1 49  ? 5.256   120.101 104.846 1.00 11.34 ? 49   GLU F C   1 
ATOM   5791  O  O   . GLU F  1 49  ? 5.752   120.899 105.631 1.00 10.67 ? 49   GLU F O   1 
ATOM   5792  C  CB  . GLU F  1 49  ? 6.693   118.585 103.504 1.00 10.95 ? 49   GLU F CB  1 
ATOM   5793  C  CG  . GLU F  1 49  ? 7.879   119.539 103.510 1.00 13.93 ? 49   GLU F CG  1 
ATOM   5794  C  CD  . GLU F  1 49  ? 8.777   119.395 102.284 1.00 17.30 ? 49   GLU F CD  1 
ATOM   5795  O  OE1 . GLU F  1 49  ? 8.557   118.474 101.459 1.00 17.13 ? 49   GLU F OE1 1 
ATOM   5796  O  OE2 . GLU F  1 49  ? 9.714   120.208 102.141 1.00 20.33 ? 49   GLU F OE2 1 
ATOM   5797  N  N   . PHE F  1 50  ? 4.262   120.421 104.021 1.00 11.62 ? 50   PHE F N   1 
ATOM   5798  C  CA  . PHE F  1 50  ? 3.759   121.792 103.927 1.00 12.02 ? 50   PHE F CA  1 
ATOM   5799  C  C   . PHE F  1 50  ? 2.442   121.990 104.662 1.00 12.19 ? 50   PHE F C   1 
ATOM   5800  O  O   . PHE F  1 50  ? 1.559   121.108 104.639 1.00 12.25 ? 50   PHE F O   1 
ATOM   5801  C  CB  . PHE F  1 50  ? 3.542   122.143 102.460 1.00 12.81 ? 50   PHE F CB  1 
ATOM   5802  C  CG  . PHE F  1 50  ? 4.741   121.851 101.592 1.00 15.78 ? 50   PHE F CG  1 
ATOM   5803  C  CD1 . PHE F  1 50  ? 5.939   122.503 101.818 1.00 18.45 ? 50   PHE F CD1 1 
ATOM   5804  C  CD2 . PHE F  1 50  ? 4.679   120.892 100.569 1.00 18.38 ? 50   PHE F CD2 1 
ATOM   5805  C  CE1 . PHE F  1 50  ? 7.071   122.212 101.035 1.00 20.56 ? 50   PHE F CE1 1 
ATOM   5806  C  CE2 . PHE F  1 50  ? 5.790   120.621 99.790  1.00 19.07 ? 50   PHE F CE2 1 
ATOM   5807  C  CZ  . PHE F  1 50  ? 6.993   121.281 100.028 1.00 17.47 ? 50   PHE F CZ  1 
ATOM   5808  N  N   . GLY F  1 51  ? 2.312   123.136 105.313 1.00 12.37 ? 51   GLY F N   1 
ATOM   5809  C  CA  . GLY F  1 51  ? 1.079   123.475 106.010 1.00 12.87 ? 51   GLY F CA  1 
ATOM   5810  C  C   . GLY F  1 51  ? 0.210   124.256 105.036 1.00 12.73 ? 51   GLY F C   1 
ATOM   5811  O  O   . GLY F  1 51  ? -0.257  125.393 105.313 1.00 13.02 ? 51   GLY F O   1 
ATOM   5812  N  N   . ASP F  1 52  ? 0.011   123.648 103.879 1.00 12.38 ? 52   ASP F N   1 
ATOM   5813  C  CA  . ASP F  1 52  ? -0.671  124.279 102.775 1.00 13.87 ? 52   ASP F CA  1 
ATOM   5814  C  C   . ASP F  1 52  ? -1.910  123.489 102.433 1.00 14.40 ? 52   ASP F C   1 
ATOM   5815  O  O   . ASP F  1 52  ? -1.822  122.354 101.956 1.00 14.82 ? 52   ASP F O   1 
ATOM   5816  C  CB  . ASP F  1 52  ? 0.280   124.345 101.580 1.00 14.11 ? 52   ASP F CB  1 
ATOM   5817  C  CG  . ASP F  1 52  ? -0.345  125.025 100.380 1.00 15.80 ? 52   ASP F CG  1 
ATOM   5818  O  OD1 . ASP F  1 52  ? -1.601  125.148 100.350 1.00 13.88 ? 52   ASP F OD1 1 
ATOM   5819  O  OD2 . ASP F  1 52  ? 0.349   125.463 99.428  1.00 14.46 ? 52   ASP F OD2 1 
ATOM   5820  N  N   . ASN F  1 53  ? -3.066  124.081 102.693 1.00 14.24 ? 53   ASN F N   1 
ATOM   5821  C  CA  . ASN F  1 53  ? -4.340  123.413 102.465 1.00 15.77 ? 53   ASN F CA  1 
ATOM   5822  C  C   . ASN F  1 53  ? -5.101  124.037 101.317 1.00 13.88 ? 53   ASN F C   1 
ATOM   5823  O  O   . ASN F  1 53  ? -6.313  123.846 101.212 1.00 14.39 ? 53   ASN F O   1 
ATOM   5824  C  CB  . ASN F  1 53  ? -5.217  123.547 103.722 1.00 16.88 ? 53   ASN F CB  1 
ATOM   5825  C  CG  . ASN F  1 53  ? -6.338  122.519 103.765 1.00 21.13 ? 53   ASN F CG  1 
ATOM   5826  O  OD1 . ASN F  1 53  ? -6.126  121.339 103.493 1.00 24.40 ? 53   ASN F OD1 1 
ATOM   5827  N  ND2 . ASN F  1 53  ? -7.554  122.975 104.097 1.00 25.17 ? 53   ASN F ND2 1 
ATOM   5828  N  N   . THR F  1 54  ? -4.434  124.831 100.491 1.00 13.59 ? 54   THR F N   1 
ATOM   5829  C  CA  . THR F  1 54  ? -5.155  125.546 99.422  1.00 14.28 ? 54   THR F CA  1 
ATOM   5830  C  C   . THR F  1 54  ? -5.916  124.629 98.476  1.00 15.74 ? 54   THR F C   1 
ATOM   5831  O  O   . THR F  1 54  ? -6.948  125.019 97.953  1.00 16.16 ? 54   THR F O   1 
ATOM   5832  C  CB  . THR F  1 54  ? -4.245  126.450 98.618  1.00 14.76 ? 54   THR F CB  1 
ATOM   5833  O  OG1 . THR F  1 54  ? -3.117  125.688 98.166  1.00 14.96 ? 54   THR F OG1 1 
ATOM   5834  C  CG2 . THR F  1 54  ? -3.624  127.543 99.528  1.00 13.48 ? 54   THR F CG2 1 
ATOM   5835  N  N   . ALA F  1 55  ? -5.380  123.440 98.234  1.00 16.22 ? 55   ALA F N   1 
ATOM   5836  C  CA  . ALA F  1 55  ? -6.056  122.440 97.389  1.00 17.53 ? 55   ALA F CA  1 
ATOM   5837  C  C   . ALA F  1 55  ? -6.437  121.254 98.243  1.00 17.76 ? 55   ALA F C   1 
ATOM   5838  O  O   . ALA F  1 55  ? -6.267  120.095 97.838  1.00 20.37 ? 55   ALA F O   1 
ATOM   5839  C  CB  . ALA F  1 55  ? -5.135  121.980 96.285  1.00 17.60 ? 55   ALA F CB  1 
ATOM   5840  N  N   . GLY F  1 56  ? -6.904  121.519 99.451  1.00 17.24 ? 56   GLY F N   1 
ATOM   5841  C  CA  . GLY F  1 56  ? -7.207  120.443 100.380 1.00 16.43 ? 56   GLY F CA  1 
ATOM   5842  C  C   . GLY F  1 56  ? -5.930  119.736 100.855 1.00 16.50 ? 56   GLY F C   1 
ATOM   5843  O  O   . GLY F  1 56  ? -4.819  120.305 100.787 1.00 15.64 ? 56   GLY F O   1 
ATOM   5844  N  N   . CYS F  1 57  ? -6.074  118.475 101.257 1.00 15.84 ? 57   CYS F N   1 
ATOM   5845  C  CA  . CYS F  1 57  ? -4.945  117.719 101.823 1.00 16.86 ? 57   CYS F CA  1 
ATOM   5846  C  C   . CYS F  1 57  ? -3.829  117.442 100.828 1.00 15.89 ? 57   CYS F C   1 
ATOM   5847  O  O   . CYS F  1 57  ? -2.682  117.169 101.210 1.00 14.19 ? 57   CYS F O   1 
ATOM   5848  C  CB  . CYS F  1 57  ? -5.448  116.412 102.435 1.00 17.25 ? 57   CYS F CB  1 
ATOM   5849  S  SG  . CYS F  1 57  ? -6.502  116.724 103.885 1.00 22.05 ? 57   CYS F SG  1 
ATOM   5850  N  N   . THR F  1 58  ? -4.181  117.518 99.549  1.00 15.14 ? 58   THR F N   1 
ATOM   5851  C  CA  . THR F  1 58  ? -3.222  117.263 98.479  1.00 15.72 ? 58   THR F CA  1 
ATOM   5852  C  C   . THR F  1 58  ? -2.055  118.241 98.489  1.00 14.58 ? 58   THR F C   1 
ATOM   5853  O  O   . THR F  1 58  ? -0.911  117.865 98.253  1.00 13.59 ? 58   THR F O   1 
ATOM   5854  C  CB  . THR F  1 58  ? -3.963  117.355 97.134  1.00 16.47 ? 58   THR F CB  1 
ATOM   5855  O  OG1 . THR F  1 58  ? -4.847  116.224 97.036  1.00 18.61 ? 58   THR F OG1 1 
ATOM   5856  C  CG2 . THR F  1 58  ? -2.982  117.176 95.957  1.00 18.13 ? 58   THR F CG2 1 
ATOM   5857  N  N   . SER F  1 59  ? -2.329  119.512 98.773  1.00 12.74 ? 59   SER F N   1 
ATOM   5858  C  CA  . SER F  1 59  ? -1.245  120.479 98.758  1.00 13.37 ? 59   SER F CA  1 
ATOM   5859  C  C   . SER F  1 59  ? -0.287  120.387 99.959  1.00 12.45 ? 59   SER F C   1 
ATOM   5860  O  O   . SER F  1 59  ? 0.646   121.148 100.044 1.00 12.50 ? 59   SER F O   1 
ATOM   5861  C  CB  . SER F  1 59  ? -1.805  121.907 98.592  1.00 13.99 ? 59   SER F CB  1 
ATOM   5862  O  OG  . SER F  1 59  ? -2.990  122.001 99.348  1.00 17.36 ? 59   SER F OG  1 
ATOM   5863  N  N   . ALA F  1 60  ? -0.504  119.457 100.878 1.00 12.19 ? 60   ALA F N   1 
ATOM   5864  C  CA  . ALA F  1 60  ? 0.420   119.273 101.998 1.00 12.02 ? 60   ALA F CA  1 
ATOM   5865  C  C   . ALA F  1 60  ? 1.725   118.615 101.560 1.00 12.99 ? 60   ALA F C   1 
ATOM   5866  O  O   . ALA F  1 60  ? 2.694   118.576 102.306 1.00 12.45 ? 60   ALA F O   1 
ATOM   5867  C  CB  . ALA F  1 60  ? -0.234  118.433 103.094 1.00 11.83 ? 60   ALA F CB  1 
ATOM   5868  N  N   . GLY F  1 61  ? 1.757   118.092 100.341 1.00 12.65 ? 61   GLY F N   1 
ATOM   5869  C  CA  . GLY F  1 61  ? 2.981   117.482 99.854  1.00 12.42 ? 61   GLY F CA  1 
ATOM   5870  C  C   . GLY F  1 61  ? 3.229   116.114 100.457 1.00 11.23 ? 61   GLY F C   1 
ATOM   5871  O  O   . GLY F  1 61  ? 2.302   115.475 100.990 1.00 11.77 ? 61   GLY F O   1 
ATOM   5872  N  N   . PRO F  1 62  ? 4.478   115.662 100.397 1.00 10.75 ? 62   PRO F N   1 
ATOM   5873  C  CA  . PRO F  1 62  ? 4.835   114.321 100.884 1.00 10.95 ? 62   PRO F CA  1 
ATOM   5874  C  C   . PRO F  1 62  ? 5.144   114.329 102.378 1.00 11.14 ? 62   PRO F C   1 
ATOM   5875  O  O   . PRO F  1 62  ? 4.947   115.332 103.055 1.00 10.53 ? 62   PRO F O   1 
ATOM   5876  C  CB  . PRO F  1 62  ? 6.090   113.957 100.063 1.00 11.00 ? 62   PRO F CB  1 
ATOM   5877  C  CG  . PRO F  1 62  ? 6.678   115.295 99.636  1.00 13.14 ? 62   PRO F CG  1 
ATOM   5878  C  CD  . PRO F  1 62  ? 5.649   116.390 99.888  1.00 11.27 ? 62   PRO F CD  1 
ATOM   5879  N  N   . HIS F  1 63  ? 5.662   113.220 102.886 1.00 11.33 ? 63   HIS F N   1 
ATOM   5880  C  CA  . HIS F  1 63  ? 5.958   113.121 104.294 1.00 11.68 ? 63   HIS F CA  1 
ATOM   5881  C  C   . HIS F  1 63  ? 7.096   114.068 104.604 1.00 12.71 ? 63   HIS F C   1 
ATOM   5882  O  O   . HIS F  1 63  ? 8.000   114.245 103.773 1.00 12.98 ? 63   HIS F O   1 
ATOM   5883  C  CB  . HIS F  1 63  ? 6.315   111.645 104.642 1.00 12.63 ? 63   HIS F CB  1 
ATOM   5884  C  CG  . HIS F  1 63  ? 5.129   110.732 104.547 1.00 14.55 ? 63   HIS F CG  1 
ATOM   5885  N  ND1 . HIS F  1 63  ? 5.183   109.371 104.778 1.00 15.45 ? 63   HIS F ND1 1 
ATOM   5886  C  CD2 . HIS F  1 63  ? 3.835   111.016 104.251 1.00 14.53 ? 63   HIS F CD2 1 
ATOM   5887  C  CE1 . HIS F  1 63  ? 3.973   108.856 104.618 1.00 17.49 ? 63   HIS F CE1 1 
ATOM   5888  N  NE2 . HIS F  1 63  ? 3.137   109.834 104.296 1.00 17.39 ? 63   HIS F NE2 1 
ATOM   5889  N  N   . PHE F  1 64  ? 7.024   114.702 105.777 1.00 12.23 ? 64   PHE F N   1 
ATOM   5890  C  CA  . PHE F  1 64  ? 8.095   115.544 106.249 1.00 12.75 ? 64   PHE F CA  1 
ATOM   5891  C  C   . PHE F  1 64  ? 9.304   114.626 106.404 1.00 13.32 ? 64   PHE F C   1 
ATOM   5892  O  O   . PHE F  1 64  ? 9.249   113.671 107.182 1.00 12.41 ? 64   PHE F O   1 
ATOM   5893  C  CB  . PHE F  1 64  ? 7.707   116.133 107.594 1.00 12.63 ? 64   PHE F CB  1 
ATOM   5894  C  CG  . PHE F  1 64  ? 8.743   117.058 108.178 1.00 13.98 ? 64   PHE F CG  1 
ATOM   5895  C  CD1 . PHE F  1 64  ? 9.499   117.891 107.363 1.00 13.48 ? 64   PHE F CD1 1 
ATOM   5896  C  CD2 . PHE F  1 64  ? 8.953   117.083 109.551 1.00 15.45 ? 64   PHE F CD2 1 
ATOM   5897  C  CE1 . PHE F  1 64  ? 10.449  118.750 107.917 1.00 15.51 ? 64   PHE F CE1 1 
ATOM   5898  C  CE2 . PHE F  1 64  ? 9.912   117.948 110.125 1.00 15.19 ? 64   PHE F CE2 1 
ATOM   5899  C  CZ  . PHE F  1 64  ? 10.655  118.775 109.297 1.00 15.08 ? 64   PHE F CZ  1 
ATOM   5900  N  N   . ASN F  1 65  ? 10.384  114.946 105.693 1.00 13.14 ? 65   ASN F N   1 
ATOM   5901  C  CA  . ASN F  1 65  ? 11.542  114.052 105.600 1.00 14.67 ? 65   ASN F CA  1 
ATOM   5902  C  C   . ASN F  1 65  ? 12.840  114.850 105.422 1.00 15.30 ? 65   ASN F C   1 
ATOM   5903  O  O   . ASN F  1 65  ? 13.499  114.764 104.386 1.00 15.76 ? 65   ASN F O   1 
ATOM   5904  C  CB  . ASN F  1 65  ? 11.315  113.150 104.381 1.00 13.96 ? 65   ASN F CB  1 
ATOM   5905  C  CG  . ASN F  1 65  ? 12.348  112.081 104.233 1.00 14.11 ? 65   ASN F CG  1 
ATOM   5906  O  OD1 . ASN F  1 65  ? 12.955  111.659 105.210 1.00 11.28 ? 65   ASN F OD1 1 
ATOM   5907  N  ND2 . ASN F  1 65  ? 12.526  111.600 103.000 1.00 13.46 ? 65   ASN F ND2 1 
ATOM   5908  N  N   . PRO F  1 66  ? 13.195  115.652 106.411 1.00 15.40 ? 66   PRO F N   1 
ATOM   5909  C  CA  . PRO F  1 66  ? 14.380  116.501 106.295 1.00 16.21 ? 66   PRO F CA  1 
ATOM   5910  C  C   . PRO F  1 66  ? 15.691  115.696 106.191 1.00 17.24 ? 66   PRO F C   1 
ATOM   5911  O  O   . PRO F  1 66  ? 16.635  116.211 105.616 1.00 17.30 ? 66   PRO F O   1 
ATOM   5912  C  CB  . PRO F  1 66  ? 14.338  117.319 107.580 1.00 15.68 ? 66   PRO F CB  1 
ATOM   5913  C  CG  . PRO F  1 66  ? 13.646  116.449 108.519 1.00 15.32 ? 66   PRO F CG  1 
ATOM   5914  C  CD  . PRO F  1 66  ? 12.510  115.850 107.698 1.00 16.10 ? 66   PRO F CD  1 
ATOM   5915  N  N   . LEU F  1 67  ? 15.737  114.469 106.701 1.00 17.84 ? 67   LEU F N   1 
ATOM   5916  C  CA  . LEU F  1 67  ? 16.946  113.643 106.596 1.00 19.45 ? 67   LEU F CA  1 
ATOM   5917  C  C   . LEU F  1 67  ? 16.986  112.767 105.346 1.00 19.79 ? 67   LEU F C   1 
ATOM   5918  O  O   . LEU F  1 67  ? 17.818  111.857 105.235 1.00 19.43 ? 67   LEU F O   1 
ATOM   5919  C  CB  . LEU F  1 67  ? 17.106  112.767 107.844 1.00 19.87 ? 67   LEU F CB  1 
ATOM   5920  C  CG  . LEU F  1 67  ? 17.177  113.602 109.133 1.00 22.35 ? 67   LEU F CG  1 
ATOM   5921  C  CD1 . LEU F  1 67  ? 17.491  112.758 110.373 1.00 23.69 ? 67   LEU F CD1 1 
ATOM   5922  C  CD2 . LEU F  1 67  ? 18.221  114.698 108.967 1.00 24.08 ? 67   LEU F CD2 1 
ATOM   5923  N  N   . SER F  1 68  ? 16.071  113.025 104.414 1.00 19.86 ? 68   SER F N   1 
ATOM   5924  C  CA  . SER F  1 68  ? 16.019  112.269 103.167 1.00 20.50 ? 68   SER F CA  1 
ATOM   5925  C  C   . SER F  1 68  ? 16.099  110.743 103.358 1.00 19.93 ? 68   SER F C   1 
ATOM   5926  O  O   . SER F  1 68  ? 16.849  110.031 102.674 1.00 19.69 ? 68   SER F O   1 
ATOM   5927  C  CB  . SER F  1 68  ? 17.090  112.808 102.216 1.00 21.01 ? 68   SER F CB  1 
ATOM   5928  O  OG  . SER F  1 68  ? 16.858  114.201 102.037 1.00 21.11 ? 68   SER F OG  1 
ATOM   5929  N  N   . ARG F  1 69  ? 15.309  110.229 104.301 1.00 19.28 ? 69   ARG F N   1 
ATOM   5930  C  CA  . ARG F  1 69  ? 15.295  108.789 104.557 1.00 17.94 ? 69   ARG F CA  1 
ATOM   5931  C  C   . ARG F  1 69  ? 14.140  108.096 103.813 1.00 17.87 ? 69   ARG F C   1 
ATOM   5932  O  O   . ARG F  1 69  ? 13.333  108.751 103.120 1.00 17.26 ? 69   ARG F O   1 
ATOM   5933  C  CB  . ARG F  1 69  ? 15.189  108.501 106.061 1.00 18.43 ? 69   ARG F CB  1 
ATOM   5934  C  CG  . ARG F  1 69  ? 16.303  109.127 106.964 1.00 18.09 ? 69   ARG F CG  1 
ATOM   5935  C  CD  . ARG F  1 69  ? 17.439  108.215 107.348 1.00 23.43 ? 69   ARG F CD  1 
ATOM   5936  N  NE  . ARG F  1 69  ? 18.211  108.720 108.490 1.00 24.26 ? 69   ARG F NE  1 
ATOM   5937  C  CZ  . ARG F  1 69  ? 19.303  109.458 108.377 1.00 26.96 ? 69   ARG F CZ  1 
ATOM   5938  N  NH1 . ARG F  1 69  ? 19.753  109.807 107.172 1.00 27.49 ? 69   ARG F NH1 1 
ATOM   5939  N  NH2 . ARG F  1 69  ? 19.941  109.869 109.470 1.00 27.94 ? 69   ARG F NH2 1 
ATOM   5940  N  N   . LYS F  1 70  ? 14.063  106.772 103.968 1.00 16.45 ? 70   LYS F N   1 
ATOM   5941  C  CA  . LYS F  1 70  ? 12.947  105.996 103.449 1.00 16.01 ? 70   LYS F CA  1 
ATOM   5942  C  C   . LYS F  1 70  ? 11.816  105.968 104.459 1.00 14.70 ? 70   LYS F C   1 
ATOM   5943  O  O   . LYS F  1 70  ? 12.040  106.196 105.647 1.00 14.54 ? 70   LYS F O   1 
ATOM   5944  C  CB  . LYS F  1 70  ? 13.376  104.560 103.154 1.00 17.08 ? 70   LYS F CB  1 
ATOM   5945  C  CG  . LYS F  1 70  ? 14.423  104.447 102.062 1.00 19.91 ? 70   LYS F CG  1 
ATOM   5946  N  N   . HIS F  1 71  ? 10.600  105.701 103.980 1.00 12.82 ? 71   HIS F N   1 
ATOM   5947  C  CA  . HIS F  1 71  ? 9.440   105.616 104.846 1.00 12.59 ? 71   HIS F CA  1 
ATOM   5948  C  C   . HIS F  1 71  ? 9.570   104.405 105.768 1.00 13.35 ? 71   HIS F C   1 
ATOM   5949  O  O   . HIS F  1 71  ? 10.042  103.338 105.332 1.00 12.69 ? 71   HIS F O   1 
ATOM   5950  C  CB  . HIS F  1 71  ? 8.156   105.456 104.004 1.00 12.53 ? 71   HIS F CB  1 
ATOM   5951  C  CG  . HIS F  1 71  ? 6.923   105.312 104.838 1.00 11.03 ? 71   HIS F CG  1 
ATOM   5952  N  ND1 . HIS F  1 71  ? 6.351   106.369 105.506 1.00 12.06 ? 71   HIS F ND1 1 
ATOM   5953  C  CD2 . HIS F  1 71  ? 6.168   104.235 105.131 1.00 13.57 ? 71   HIS F CD2 1 
ATOM   5954  C  CE1 . HIS F  1 71  ? 5.293   105.951 106.179 1.00 12.26 ? 71   HIS F CE1 1 
ATOM   5955  N  NE2 . HIS F  1 71  ? 5.162   104.653 105.968 1.00 14.95 ? 71   HIS F NE2 1 
ATOM   5956  N  N   . GLY F  1 72  ? 9.159   104.554 107.029 1.00 13.38 ? 72   GLY F N   1 
ATOM   5957  C  CA  . GLY F  1 72  ? 9.182   103.429 107.959 1.00 13.01 ? 72   GLY F CA  1 
ATOM   5958  C  C   . GLY F  1 72  ? 8.086   103.578 109.004 1.00 12.95 ? 72   GLY F C   1 
ATOM   5959  O  O   . GLY F  1 72  ? 7.240   104.455 108.872 1.00 12.23 ? 72   GLY F O   1 
ATOM   5960  N  N   . GLY F  1 73  ? 8.052   102.674 109.978 1.00 12.75 ? 73   GLY F N   1 
ATOM   5961  C  CA  . GLY F  1 73  ? 7.162   102.796 111.123 1.00 13.83 ? 73   GLY F CA  1 
ATOM   5962  C  C   . GLY F  1 73  ? 7.835   103.710 112.152 1.00 14.51 ? 73   GLY F C   1 
ATOM   5963  O  O   . GLY F  1 73  ? 9.025   103.954 112.062 1.00 14.38 ? 73   GLY F O   1 
ATOM   5964  N  N   . PRO F  1 74  ? 7.085   104.205 113.132 1.00 15.74 ? 74   PRO F N   1 
ATOM   5965  C  CA  . PRO F  1 74  ? 7.641   105.099 114.157 1.00 16.74 ? 74   PRO F CA  1 
ATOM   5966  C  C   . PRO F  1 74  ? 8.817   104.487 114.929 1.00 17.97 ? 74   PRO F C   1 
ATOM   5967  O  O   . PRO F  1 74  ? 9.705   105.215 115.393 1.00 17.41 ? 74   PRO F O   1 
ATOM   5968  C  CB  . PRO F  1 74  ? 6.469   105.329 115.126 1.00 17.64 ? 74   PRO F CB  1 
ATOM   5969  C  CG  . PRO F  1 74  ? 5.373   104.371 114.726 1.00 18.09 ? 74   PRO F CG  1 
ATOM   5970  C  CD  . PRO F  1 74  ? 5.652   103.921 113.314 1.00 16.64 ? 74   PRO F CD  1 
ATOM   5971  N  N   . LYS F  1 75  ? 8.855   103.166 115.036 1.00 19.21 ? 75   LYS F N   1 
ATOM   5972  C  CA  . LYS F  1 75  ? 9.896   102.529 115.829 1.00 21.53 ? 75   LYS F CA  1 
ATOM   5973  C  C   . LYS F  1 75  ? 11.122  102.149 115.017 1.00 22.00 ? 75   LYS F C   1 
ATOM   5974  O  O   . LYS F  1 75  ? 12.093  101.627 115.569 1.00 21.61 ? 75   LYS F O   1 
ATOM   5975  C  CB  . LYS F  1 75  ? 9.334   101.298 116.547 1.00 21.56 ? 75   LYS F CB  1 
ATOM   5976  C  CG  . LYS F  1 75  ? 8.347   101.668 117.640 1.00 25.32 ? 75   LYS F CG  1 
ATOM   5977  C  CD  . LYS F  1 75  ? 7.677   100.450 118.283 1.00 30.07 ? 75   LYS F CD  1 
ATOM   5978  C  CE  . LYS F  1 75  ? 6.653   100.903 119.344 1.00 33.60 ? 75   LYS F CE  1 
ATOM   5979  N  NZ  . LYS F  1 75  ? 5.769   102.047 118.875 1.00 36.57 ? 75   LYS F NZ  1 
ATOM   5980  N  N   . ASP F  1 76  ? 11.078  102.404 113.714 1.00 22.21 ? 76   ASP F N   1 
ATOM   5981  C  CA  . ASP F  1 76  ? 12.198  102.060 112.850 1.00 22.87 ? 76   ASP F CA  1 
ATOM   5982  C  C   . ASP F  1 76  ? 13.255  103.144 112.877 1.00 23.12 ? 76   ASP F C   1 
ATOM   5983  O  O   . ASP F  1 76  ? 12.937  104.329 112.996 1.00 23.70 ? 76   ASP F O   1 
ATOM   5984  C  CB  . ASP F  1 76  ? 11.740  101.849 111.410 1.00 22.39 ? 76   ASP F CB  1 
ATOM   5985  C  CG  . ASP F  1 76  ? 10.840  100.650 111.261 1.00 24.27 ? 76   ASP F CG  1 
ATOM   5986  O  OD1 . ASP F  1 76  ? 11.111  99.607  111.904 1.00 26.81 ? 76   ASP F OD1 1 
ATOM   5987  O  OD2 . ASP F  1 76  ? 9.836   100.642 110.524 1.00 23.37 ? 76   ASP F OD2 1 
ATOM   5988  N  N   . GLU F  1 77  ? 14.515  102.723 112.776 1.00 23.50 ? 77   GLU F N   1 
ATOM   5989  C  CA  . GLU F  1 77  ? 15.614  103.664 112.663 1.00 23.61 ? 77   GLU F CA  1 
ATOM   5990  C  C   . GLU F  1 77  ? 15.420  104.399 111.349 1.00 22.38 ? 77   GLU F C   1 
ATOM   5991  O  O   . GLU F  1 77  ? 15.486  105.627 111.295 1.00 22.69 ? 77   GLU F O   1 
ATOM   5992  C  CB  . GLU F  1 77  ? 16.950  102.937 112.667 1.00 24.60 ? 77   GLU F CB  1 
ATOM   5993  C  CG  . GLU F  1 77  ? 18.144  103.868 112.769 1.00 28.68 ? 77   GLU F CG  1 
ATOM   5994  C  CD  . GLU F  1 77  ? 18.399  104.662 111.499 1.00 33.89 ? 77   GLU F CD  1 
ATOM   5995  O  OE1 . GLU F  1 77  ? 17.840  104.298 110.438 1.00 36.19 ? 77   GLU F OE1 1 
ATOM   5996  O  OE2 . GLU F  1 77  ? 19.169  105.653 111.566 1.00 35.93 ? 77   GLU F OE2 1 
ATOM   5997  N  N   . GLU F  1 78  ? 15.131  103.638 110.297 1.00 19.89 ? 78   GLU F N   1 
ATOM   5998  C  CA  . GLU F  1 78  ? 14.885  104.218 108.987 1.00 18.64 ? 78   GLU F CA  1 
ATOM   5999  C  C   . GLU F  1 78  ? 13.417  104.636 108.853 1.00 16.70 ? 78   GLU F C   1 
ATOM   6000  O  O   . GLU F  1 78  ? 12.530  103.805 108.666 1.00 14.95 ? 78   GLU F O   1 
ATOM   6001  C  CB  . GLU F  1 78  ? 15.238  103.227 107.878 1.00 18.94 ? 78   GLU F CB  1 
ATOM   6002  C  CG  . GLU F  1 78  ? 15.162  103.810 106.472 1.00 20.98 ? 78   GLU F CG  1 
ATOM   6003  C  CD  . GLU F  1 78  ? 16.356  104.681 106.080 1.00 24.98 ? 78   GLU F CD  1 
ATOM   6004  O  OE1 . GLU F  1 78  ? 17.338  104.763 106.867 1.00 25.91 ? 78   GLU F OE1 1 
ATOM   6005  O  OE2 . GLU F  1 78  ? 16.315  105.273 104.963 1.00 23.09 ? 78   GLU F OE2 1 
ATOM   6006  N  N   . ARG F  1 79  ? 13.178  105.933 108.959 1.00 15.73 ? 79   ARG F N   1 
ATOM   6007  C  CA  . ARG F  1 79  ? 11.831  106.480 108.843 1.00 14.51 ? 79   ARG F CA  1 
ATOM   6008  C  C   . ARG F  1 79  ? 11.921  107.947 108.507 1.00 13.99 ? 79   ARG F C   1 
ATOM   6009  O  O   . ARG F  1 79  ? 12.972  108.572 108.699 1.00 12.94 ? 79   ARG F O   1 
ATOM   6010  C  CB  . ARG F  1 79  ? 11.090  106.339 110.179 1.00 15.81 ? 79   ARG F CB  1 
ATOM   6011  C  CG  . ARG F  1 79  ? 11.701  107.178 111.341 1.00 13.66 ? 79   ARG F CG  1 
ATOM   6012  C  CD  . ARG F  1 79  ? 10.768  108.329 111.823 1.00 23.46 ? 79   ARG F CD  1 
ATOM   6013  N  NE  . ARG F  1 79  ? 10.224  107.905 113.094 1.00 26.06 ? 79   ARG F NE  1 
ATOM   6014  C  CZ  . ARG F  1 79  ? 9.383   108.547 113.887 1.00 20.91 ? 79   ARG F CZ  1 
ATOM   6015  N  NH1 . ARG F  1 79  ? 8.845   109.743 113.586 1.00 20.16 ? 79   ARG F NH1 1 
ATOM   6016  N  NH2 . ARG F  1 79  ? 9.085   107.931 115.030 1.00 18.30 ? 79   ARG F NH2 1 
ATOM   6017  N  N   . HIS F  1 80  ? 10.818  108.498 107.991 1.00 13.55 ? 80   HIS F N   1 
ATOM   6018  C  CA  . HIS F  1 80  ? 10.694  109.933 107.757 1.00 13.68 ? 80   HIS F CA  1 
ATOM   6019  C  C   . HIS F  1 80  ? 10.410  110.544 109.122 1.00 13.16 ? 80   HIS F C   1 
ATOM   6020  O  O   . HIS F  1 80  ? 9.772   109.884 109.956 1.00 12.97 ? 80   HIS F O   1 
ATOM   6021  C  CB  . HIS F  1 80  ? 9.462   110.211 106.878 1.00 13.86 ? 80   HIS F CB  1 
ATOM   6022  C  CG  . HIS F  1 80  ? 9.519   109.619 105.498 1.00 13.90 ? 80   HIS F CG  1 
ATOM   6023  N  ND1 . HIS F  1 80  ? 8.402   109.144 104.825 1.00 9.71  ? 80   HIS F ND1 1 
ATOM   6024  C  CD2 . HIS F  1 80  ? 10.566  109.445 104.657 1.00 13.19 ? 80   HIS F CD2 1 
ATOM   6025  C  CE1 . HIS F  1 80  ? 8.768   108.725 103.633 1.00 13.09 ? 80   HIS F CE1 1 
ATOM   6026  N  NE2 . HIS F  1 80  ? 10.076  108.878 103.514 1.00 13.13 ? 80   HIS F NE2 1 
ATOM   6027  N  N   . VAL F  1 81  ? 10.836  111.782 109.376 1.00 12.53 ? 81   VAL F N   1 
ATOM   6028  C  CA  . VAL F  1 81  ? 10.474  112.426 110.635 1.00 12.28 ? 81   VAL F CA  1 
ATOM   6029  C  C   . VAL F  1 81  ? 8.980   112.354 110.832 1.00 12.04 ? 81   VAL F C   1 
ATOM   6030  O  O   . VAL F  1 81  ? 8.492   112.094 111.937 1.00 10.98 ? 81   VAL F O   1 
ATOM   6031  C  CB  . VAL F  1 81  ? 10.927  113.917 110.703 1.00 13.69 ? 81   VAL F CB  1 
ATOM   6032  C  CG1 . VAL F  1 81  ? 10.185  114.689 111.835 1.00 11.51 ? 81   VAL F CG1 1 
ATOM   6033  C  CG2 . VAL F  1 81  ? 12.463  113.979 110.883 1.00 13.32 ? 81   VAL F CG2 1 
ATOM   6034  N  N   . GLY F  1 82  ? 8.233   112.551 109.749 1.00 11.89 ? 82   GLY F N   1 
ATOM   6035  C  CA  . GLY F  1 82  ? 6.778   112.540 109.870 1.00 12.62 ? 82   GLY F CA  1 
ATOM   6036  C  C   . GLY F  1 82  ? 6.055   111.204 110.004 1.00 13.02 ? 82   GLY F C   1 
ATOM   6037  O  O   . GLY F  1 82  ? 4.823   111.174 109.985 1.00 11.66 ? 82   GLY F O   1 
ATOM   6038  N  N   . ASP F  1 83  ? 6.796   110.101 110.191 1.00 12.60 ? 83   ASP F N   1 
ATOM   6039  C  CA  . ASP F  1 83  ? 6.178   108.772 110.254 1.00 13.44 ? 83   ASP F CA  1 
ATOM   6040  C  C   . ASP F  1 83  ? 5.625   108.340 111.622 1.00 13.85 ? 83   ASP F C   1 
ATOM   6041  O  O   . ASP F  1 83  ? 6.340   107.741 112.429 1.00 14.19 ? 83   ASP F O   1 
ATOM   6042  C  CB  . ASP F  1 83  ? 7.152   107.703 109.704 1.00 12.65 ? 83   ASP F CB  1 
ATOM   6043  C  CG  . ASP F  1 83  ? 7.376   107.831 108.192 1.00 14.01 ? 83   ASP F CG  1 
ATOM   6044  O  OD1 . ASP F  1 83  ? 6.582   108.529 107.509 1.00 11.35 ? 83   ASP F OD1 1 
ATOM   6045  O  OD2 . ASP F  1 83  ? 8.323   107.273 107.592 1.00 13.36 ? 83   ASP F OD2 1 
ATOM   6046  N  N   . LEU F  1 84  ? 4.347   108.593 111.870 1.00 13.46 ? 84   LEU F N   1 
ATOM   6047  C  CA  . LEU F  1 84  ? 3.768   108.266 113.170 1.00 14.54 ? 84   LEU F CA  1 
ATOM   6048  C  C   . LEU F  1 84  ? 2.936   106.992 113.147 1.00 15.00 ? 84   LEU F C   1 
ATOM   6049  O  O   . LEU F  1 84  ? 2.108   106.767 114.033 1.00 16.32 ? 84   LEU F O   1 
ATOM   6050  C  CB  . LEU F  1 84  ? 2.906   109.419 113.656 1.00 13.54 ? 84   LEU F CB  1 
ATOM   6051  C  CG  . LEU F  1 84  ? 3.738   110.652 113.970 1.00 15.77 ? 84   LEU F CG  1 
ATOM   6052  C  CD1 . LEU F  1 84  ? 2.813   111.796 114.388 1.00 13.07 ? 84   LEU F CD1 1 
ATOM   6053  C  CD2 . LEU F  1 84  ? 4.783   110.327 115.067 1.00 13.86 ? 84   LEU F CD2 1 
ATOM   6054  N  N   . GLY F  1 85  ? 3.143   106.169 112.132 1.00 15.67 ? 85   GLY F N   1 
ATOM   6055  C  CA  . GLY F  1 85  ? 2.460   104.880 112.041 1.00 15.05 ? 85   GLY F CA  1 
ATOM   6056  C  C   . GLY F  1 85  ? 0.975   104.911 111.718 1.00 15.26 ? 85   GLY F C   1 
ATOM   6057  O  O   . GLY F  1 85  ? 0.523   105.526 110.738 1.00 13.68 ? 85   GLY F O   1 
ATOM   6058  N  N   . ASN F  1 86  ? 0.220   104.184 112.535 1.00 15.44 ? 86   ASN F N   1 
ATOM   6059  C  CA  . ASN F  1 86  ? -1.217  104.070 112.364 1.00 15.32 ? 86   ASN F CA  1 
ATOM   6060  C  C   . ASN F  1 86  ? -2.006  104.421 113.625 1.00 16.44 ? 86   ASN F C   1 
ATOM   6061  O  O   . ASN F  1 86  ? -1.541  104.210 114.763 1.00 16.31 ? 86   ASN F O   1 
ATOM   6062  C  CB  . ASN F  1 86  ? -1.567  102.619 112.051 1.00 15.63 ? 86   ASN F CB  1 
ATOM   6063  C  CG  . ASN F  1 86  ? -1.143  102.184 110.656 1.00 15.59 ? 86   ASN F CG  1 
ATOM   6064  O  OD1 . ASN F  1 86  ? -1.692  102.657 109.663 1.00 14.19 ? 86   ASN F OD1 1 
ATOM   6065  N  ND2 . ASN F  1 86  ? -0.228  101.209 110.580 1.00 14.28 ? 86   ASN F ND2 1 
ATOM   6066  N  N   . VAL F  1 87  ? -3.212  104.939 113.428 1.00 15.70 ? 87   VAL F N   1 
ATOM   6067  C  CA  . VAL F  1 87  ? -4.147  105.039 114.532 1.00 16.16 ? 87   VAL F CA  1 
ATOM   6068  C  C   . VAL F  1 87  ? -5.202  103.963 114.267 1.00 16.42 ? 87   VAL F C   1 
ATOM   6069  O  O   . VAL F  1 87  ? -5.346  103.483 113.138 1.00 16.23 ? 87   VAL F O   1 
ATOM   6070  C  CB  . VAL F  1 87  ? -4.749  106.416 114.647 1.00 16.13 ? 87   VAL F CB  1 
ATOM   6071  C  CG1 . VAL F  1 87  ? -3.610  107.444 114.810 1.00 15.57 ? 87   VAL F CG1 1 
ATOM   6072  C  CG2 . VAL F  1 87  ? -5.593  106.756 113.407 1.00 15.39 ? 87   VAL F CG2 1 
ATOM   6073  N  N   . THR F  1 88  ? -5.904  103.557 115.314 1.00 16.27 ? 88   THR F N   1 
ATOM   6074  C  CA  . THR F  1 88  ? -6.891  102.501 115.202 1.00 15.96 ? 88   THR F CA  1 
ATOM   6075  C  C   . THR F  1 88  ? -8.284  102.984 115.574 1.00 15.56 ? 88   THR F C   1 
ATOM   6076  O  O   . THR F  1 88  ? -8.489  103.441 116.687 1.00 15.40 ? 88   THR F O   1 
ATOM   6077  C  CB  . THR F  1 88  ? -6.499  101.359 116.170 1.00 16.60 ? 88   THR F CB  1 
ATOM   6078  O  OG1 . THR F  1 88  ? -5.287  100.742 115.708 1.00 16.45 ? 88   THR F OG1 1 
ATOM   6079  C  CG2 . THR F  1 88  ? -7.529  100.226 116.109 1.00 17.50 ? 88   THR F CG2 1 
ATOM   6080  N  N   . ALA F  1 89  ? -9.230  102.870 114.648 1.00 14.96 ? 89   ALA F N   1 
ATOM   6081  C  CA  . ALA F  1 89  ? -10.617 103.242 114.900 1.00 14.96 ? 89   ALA F CA  1 
ATOM   6082  C  C   . ALA F  1 89  ? -11.358 101.976 115.338 1.00 15.36 ? 89   ALA F C   1 
ATOM   6083  O  O   . ALA F  1 89  ? -11.136 100.914 114.776 1.00 15.28 ? 89   ALA F O   1 
ATOM   6084  C  CB  . ALA F  1 89  ? -11.250 103.782 113.639 1.00 14.85 ? 89   ALA F CB  1 
ATOM   6085  N  N   . ASP F  1 90  ? -12.226 102.116 116.331 1.00 15.44 ? 90   ASP F N   1 
ATOM   6086  C  CA  . ASP F  1 90  ? -13.013 101.005 116.845 1.00 17.15 ? 90   ASP F CA  1 
ATOM   6087  C  C   . ASP F  1 90  ? -14.260 100.817 116.005 1.00 17.49 ? 90   ASP F C   1 
ATOM   6088  O  O   . ASP F  1 90  ? -14.453 101.472 114.975 1.00 16.60 ? 90   ASP F O   1 
ATOM   6089  C  CB  . ASP F  1 90  ? -13.383 101.225 118.310 1.00 17.16 ? 90   ASP F CB  1 
ATOM   6090  C  CG  . ASP F  1 90  ? -14.272 102.455 118.530 1.00 19.05 ? 90   ASP F CG  1 
ATOM   6091  O  OD1 . ASP F  1 90  ? -14.915 102.943 117.567 1.00 20.55 ? 90   ASP F OD1 1 
ATOM   6092  O  OD2 . ASP F  1 90  ? -14.398 102.999 119.653 1.00 20.26 ? 90   ASP F OD2 1 
ATOM   6093  N  N   . LYS F  1 91  ? -15.132 99.943  116.477 1.00 18.01 ? 91   LYS F N   1 
ATOM   6094  C  CA  . LYS F  1 91  ? -16.302 99.577  115.707 1.00 19.50 ? 91   LYS F CA  1 
ATOM   6095  C  C   . LYS F  1 91  ? -17.152 100.803 115.434 1.00 19.16 ? 91   LYS F C   1 
ATOM   6096  O  O   . LYS F  1 91  ? -17.834 100.863 114.414 1.00 19.82 ? 91   LYS F O   1 
ATOM   6097  C  CB  . LYS F  1 91  ? -17.099 98.452  116.421 1.00 19.49 ? 91   LYS F CB  1 
ATOM   6098  C  CG  . LYS F  1 91  ? -17.903 98.935  117.632 1.00 22.92 ? 91   LYS F CG  1 
ATOM   6099  C  CD  . LYS F  1 91  ? -19.332 99.371  117.244 1.00 26.70 ? 91   LYS F CD  1 
ATOM   6100  C  CE  . LYS F  1 91  ? -20.169 99.756  118.463 1.00 28.44 ? 91   LYS F CE  1 
ATOM   6101  N  NZ  . LYS F  1 91  ? -20.075 98.753  119.568 1.00 29.66 ? 91   LYS F NZ  1 
ATOM   6102  N  N   . ASP F  1 92  ? -17.068 101.794 116.321 1.00 18.86 ? 92   ASP F N   1 
ATOM   6103  C  CA  . ASP F  1 92  ? -17.840 103.021 116.207 1.00 18.66 ? 92   ASP F CA  1 
ATOM   6104  C  C   . ASP F  1 92  ? -17.166 104.128 115.399 1.00 17.53 ? 92   ASP F C   1 
ATOM   6105  O  O   . ASP F  1 92  ? -17.647 105.267 115.385 1.00 16.89 ? 92   ASP F O   1 
ATOM   6106  C  CB  . ASP F  1 92  ? -18.184 103.560 117.589 1.00 19.26 ? 92   ASP F CB  1 
ATOM   6107  C  CG  . ASP F  1 92  ? -19.187 102.691 118.312 1.00 22.61 ? 92   ASP F CG  1 
ATOM   6108  O  OD1 . ASP F  1 92  ? -20.286 102.466 117.755 1.00 25.74 ? 92   ASP F OD1 1 
ATOM   6109  O  OD2 . ASP F  1 92  ? -18.953 102.174 119.426 1.00 25.19 ? 92   ASP F OD2 1 
ATOM   6110  N  N   . GLY F  1 93  ? -16.045 103.824 114.757 1.00 16.55 ? 93   GLY F N   1 
ATOM   6111  C  CA  . GLY F  1 93  ? -15.423 104.800 113.877 1.00 16.52 ? 93   GLY F CA  1 
ATOM   6112  C  C   . GLY F  1 93  ? -14.543 105.818 114.567 1.00 16.35 ? 93   GLY F C   1 
ATOM   6113  O  O   . GLY F  1 93  ? -14.055 106.790 113.948 1.00 15.74 ? 93   GLY F O   1 
ATOM   6114  N  N   . VAL F  1 94  ? -14.315 105.572 115.851 1.00 16.45 ? 94   VAL F N   1 
ATOM   6115  C  CA  . VAL F  1 94  ? -13.518 106.464 116.673 1.00 16.88 ? 94   VAL F CA  1 
ATOM   6116  C  C   . VAL F  1 94  ? -12.134 105.941 116.985 1.00 17.05 ? 94   VAL F C   1 
ATOM   6117  O  O   . VAL F  1 94  ? -11.966 104.827 117.477 1.00 16.50 ? 94   VAL F O   1 
ATOM   6118  C  CB  . VAL F  1 94  ? -14.177 106.707 118.024 1.00 17.72 ? 94   VAL F CB  1 
ATOM   6119  C  CG1 . VAL F  1 94  ? -13.333 107.682 118.846 1.00 15.92 ? 94   VAL F CG1 1 
ATOM   6120  C  CG2 . VAL F  1 94  ? -15.620 107.204 117.841 1.00 18.04 ? 94   VAL F CG2 1 
ATOM   6121  N  N   . ALA F  1 95  ? -11.140 106.771 116.711 1.00 16.78 ? 95   ALA F N   1 
ATOM   6122  C  CA  . ALA F  1 95  ? -9.782  106.433 117.046 1.00 17.90 ? 95   ALA F CA  1 
ATOM   6123  C  C   . ALA F  1 95  ? -9.318  107.309 118.202 1.00 18.88 ? 95   ALA F C   1 
ATOM   6124  O  O   . ALA F  1 95  ? -9.206  108.544 118.081 1.00 19.26 ? 95   ALA F O   1 
ATOM   6125  C  CB  . ALA F  1 95  ? -8.856  106.611 115.824 1.00 17.88 ? 95   ALA F CB  1 
ATOM   6126  N  N   . ASP F  1 96  ? -9.082  106.672 119.342 1.00 19.46 ? 96   ASP F N   1 
ATOM   6127  C  CA  . ASP F  1 96  ? -8.491  107.373 120.466 1.00 20.22 ? 96   ASP F CA  1 
ATOM   6128  C  C   . ASP F  1 96  ? -6.988  107.298 120.247 1.00 20.06 ? 96   ASP F C   1 
ATOM   6129  O  O   . ASP F  1 96  ? -6.406  106.218 120.096 1.00 19.89 ? 96   ASP F O   1 
ATOM   6130  C  CB  . ASP F  1 96  ? -8.935  106.778 121.810 1.00 21.04 ? 96   ASP F CB  1 
ATOM   6131  C  CG  . ASP F  1 96  ? -10.253 107.375 122.299 1.00 23.90 ? 96   ASP F CG  1 
ATOM   6132  O  OD1 . ASP F  1 96  ? -11.042 106.626 122.914 1.00 26.32 ? 96   ASP F OD1 1 
ATOM   6133  O  OD2 . ASP F  1 96  ? -10.596 108.583 122.097 1.00 27.41 ? 96   ASP F OD2 1 
ATOM   6134  N  N   . VAL F  1 97  ? -6.364  108.462 120.162 1.00 20.19 ? 97   VAL F N   1 
ATOM   6135  C  CA  . VAL F  1 97  ? -4.949  108.539 119.867 1.00 20.68 ? 97   VAL F CA  1 
ATOM   6136  C  C   . VAL F  1 97  ? -4.144  108.881 121.108 1.00 21.48 ? 97   VAL F C   1 
ATOM   6137  O  O   . VAL F  1 97  ? -4.441  109.849 121.810 1.00 21.49 ? 97   VAL F O   1 
ATOM   6138  C  CB  . VAL F  1 97  ? -4.664  109.620 118.779 1.00 20.17 ? 97   VAL F CB  1 
ATOM   6139  C  CG1 . VAL F  1 97  ? -3.168  109.745 118.534 1.00 20.68 ? 97   VAL F CG1 1 
ATOM   6140  C  CG2 . VAL F  1 97  ? -5.417  109.306 117.484 1.00 19.86 ? 97   VAL F CG2 1 
ATOM   6141  N  N   . SER F  1 98  ? -3.136  108.059 121.390 1.00 22.94 ? 98   SER F N   1 
ATOM   6142  C  CA  . SER F  1 98  ? -2.218  108.335 122.483 1.00 24.00 ? 98   SER F CA  1 
ATOM   6143  C  C   . SER F  1 98  ? -0.877  107.738 122.130 1.00 23.98 ? 98   SER F C   1 
ATOM   6144  O  O   . SER F  1 98  ? -0.650  106.529 122.266 1.00 24.83 ? 98   SER F O   1 
ATOM   6145  C  CB  . SER F  1 98  ? -2.720  107.782 123.803 1.00 24.98 ? 98   SER F CB  1 
ATOM   6146  O  OG  . SER F  1 98  ? -1.739  108.007 124.804 1.00 28.15 ? 98   SER F OG  1 
ATOM   6147  N  N   . ILE F  1 99  ? 0.020   108.612 121.716 1.00 23.07 ? 99   ILE F N   1 
ATOM   6148  C  CA  . ILE F  1 99  ? 1.300   108.239 121.162 1.00 22.98 ? 99   ILE F CA  1 
ATOM   6149  C  C   . ILE F  1 99  ? 2.385   109.059 121.827 1.00 21.99 ? 99   ILE F C   1 
ATOM   6150  O  O   . ILE F  1 99  ? 2.149   110.185 122.253 1.00 21.82 ? 99   ILE F O   1 
ATOM   6151  C  CB  . ILE F  1 99  ? 1.267   108.601 119.631 1.00 23.50 ? 99   ILE F CB  1 
ATOM   6152  C  CG1 . ILE F  1 99  ? 0.549   107.524 118.820 1.00 26.33 ? 99   ILE F CG1 1 
ATOM   6153  C  CG2 . ILE F  1 99  ? 2.648   108.812 119.065 1.00 24.02 ? 99   ILE F CG2 1 
ATOM   6154  C  CD1 . ILE F  1 99  ? 0.159   108.025 117.414 1.00 28.34 ? 99   ILE F CD1 1 
ATOM   6155  N  N   . GLU F  1 100 ? 3.580   108.502 121.911 1.00 20.81 ? 100  GLU F N   1 
ATOM   6156  C  CA  . GLU F  1 100 ? 4.722   109.281 122.345 1.00 20.28 ? 100  GLU F CA  1 
ATOM   6157  C  C   . GLU F  1 100 ? 5.774   109.109 121.264 1.00 19.27 ? 100  GLU F C   1 
ATOM   6158  O  O   . GLU F  1 100 ? 5.993   108.000 120.808 1.00 19.34 ? 100  GLU F O   1 
ATOM   6159  C  CB  . GLU F  1 100 ? 5.253   108.788 123.688 1.00 21.20 ? 100  GLU F CB  1 
ATOM   6160  C  CG  . GLU F  1 100 ? 6.136   109.813 124.367 1.00 22.98 ? 100  GLU F CG  1 
ATOM   6161  C  CD  . GLU F  1 100 ? 6.581   109.383 125.755 1.00 26.23 ? 100  GLU F CD  1 
ATOM   6162  O  OE1 . GLU F  1 100 ? 5.969   109.866 126.735 1.00 24.56 ? 100  GLU F OE1 1 
ATOM   6163  O  OE2 . GLU F  1 100 ? 7.541   108.565 125.845 1.00 25.97 ? 100  GLU F OE2 1 
ATOM   6164  N  N   . ASP F  1 101 ? 6.405   110.192 120.825 1.00 18.24 ? 101  ASP F N   1 
ATOM   6165  C  CA  . ASP F  1 101 ? 7.386   110.067 119.749 1.00 18.11 ? 101  ASP F CA  1 
ATOM   6166  C  C   . ASP F  1 101 ? 8.570   110.953 120.011 1.00 17.79 ? 101  ASP F C   1 
ATOM   6167  O  O   . ASP F  1 101 ? 8.419   112.100 120.450 1.00 18.16 ? 101  ASP F O   1 
ATOM   6168  C  CB  . ASP F  1 101 ? 6.781   110.393 118.359 1.00 17.89 ? 101  ASP F CB  1 
ATOM   6169  C  CG  . ASP F  1 101 ? 7.751   110.082 117.209 1.00 18.24 ? 101  ASP F CG  1 
ATOM   6170  O  OD1 . ASP F  1 101 ? 7.952   108.887 116.912 1.00 22.17 ? 101  ASP F OD1 1 
ATOM   6171  O  OD2 . ASP F  1 101 ? 8.408   110.933 116.575 1.00 19.59 ? 101  ASP F OD2 1 
ATOM   6172  N  N   . SER F  1 102 ? 9.746   110.445 119.675 1.00 17.59 ? 102  SER F N   1 
ATOM   6173  C  CA  . SER F  1 102 ? 10.983  111.156 119.970 1.00 17.71 ? 102  SER F CA  1 
ATOM   6174  C  C   . SER F  1 102 ? 11.746  111.669 118.753 1.00 16.69 ? 102  SER F C   1 
ATOM   6175  O  O   . SER F  1 102 ? 12.816  112.271 118.898 1.00 16.00 ? 102  SER F O   1 
ATOM   6176  C  CB  . SER F  1 102 ? 11.889  110.280 120.861 1.00 18.82 ? 102  SER F CB  1 
ATOM   6177  O  OG  . SER F  1 102 ? 11.398  110.298 122.196 1.00 21.02 ? 102  SER F OG  1 
ATOM   6178  N  N   . VAL F  1 103 ? 11.183  111.466 117.568 1.00 15.40 ? 103  VAL F N   1 
ATOM   6179  C  CA  . VAL F  1 103 ? 11.790  111.953 116.328 1.00 14.54 ? 103  VAL F CA  1 
ATOM   6180  C  C   . VAL F  1 103 ? 11.175  113.295 115.922 1.00 14.36 ? 103  VAL F C   1 
ATOM   6181  O  O   . VAL F  1 103 ? 11.906  114.246 115.574 1.00 14.34 ? 103  VAL F O   1 
ATOM   6182  C  CB  . VAL F  1 103 ? 11.677  110.917 115.203 1.00 14.76 ? 103  VAL F CB  1 
ATOM   6183  C  CG1 . VAL F  1 103 ? 12.239  111.461 113.909 1.00 14.23 ? 103  VAL F CG1 1 
ATOM   6184  C  CG2 . VAL F  1 103 ? 12.442  109.658 115.622 1.00 14.46 ? 103  VAL F CG2 1 
ATOM   6185  N  N   . ILE F  1 104 ? 9.852   113.405 116.001 1.00 13.81 ? 104  ILE F N   1 
ATOM   6186  C  CA  . ILE F  1 104 ? 9.242   114.715 115.727 1.00 12.96 ? 104  ILE F CA  1 
ATOM   6187  C  C   . ILE F  1 104 ? 9.642   115.629 116.866 1.00 13.99 ? 104  ILE F C   1 
ATOM   6188  O  O   . ILE F  1 104 ? 10.038  115.146 117.916 1.00 13.89 ? 104  ILE F O   1 
ATOM   6189  C  CB  . ILE F  1 104 ? 7.721   114.658 115.649 1.00 12.33 ? 104  ILE F CB  1 
ATOM   6190  C  CG1 . ILE F  1 104 ? 7.127   114.070 116.928 1.00 11.61 ? 104  ILE F CG1 1 
ATOM   6191  C  CG2 . ILE F  1 104 ? 7.309   113.814 114.432 1.00 12.32 ? 104  ILE F CG2 1 
ATOM   6192  C  CD1 . ILE F  1 104 ? 5.608   114.207 117.063 1.00 10.59 ? 104  ILE F CD1 1 
ATOM   6193  N  N   . SER F  1 105 ? 9.521   116.941 116.666 1.00 13.77 ? 105  SER F N   1 
ATOM   6194  C  CA  . SER F  1 105 ? 9.833   117.913 117.722 1.00 15.45 ? 105  SER F CA  1 
ATOM   6195  C  C   . SER F  1 105 ? 8.949   119.143 117.561 1.00 15.80 ? 105  SER F C   1 
ATOM   6196  O  O   . SER F  1 105 ? 8.365   119.351 116.495 1.00 14.44 ? 105  SER F O   1 
ATOM   6197  C  CB  . SER F  1 105 ? 11.313  118.330 117.689 1.00 15.40 ? 105  SER F CB  1 
ATOM   6198  O  OG  . SER F  1 105 ? 11.681  119.045 118.867 1.00 17.50 ? 105  SER F OG  1 
ATOM   6199  N  N   . LEU F  1 106 ? 8.829   119.940 118.625 1.00 16.34 ? 106  LEU F N   1 
ATOM   6200  C  CA  . LEU F  1 106 ? 8.104   121.208 118.529 1.00 17.47 ? 106  LEU F CA  1 
ATOM   6201  C  C   . LEU F  1 106 ? 9.054   122.406 118.463 1.00 19.16 ? 106  LEU F C   1 
ATOM   6202  O  O   . LEU F  1 106 ? 8.638   123.539 118.645 1.00 18.47 ? 106  LEU F O   1 
ATOM   6203  C  CB  . LEU F  1 106 ? 7.089   121.381 119.649 1.00 16.96 ? 106  LEU F CB  1 
ATOM   6204  C  CG  . LEU F  1 106 ? 6.025   120.284 119.728 1.00 15.67 ? 106  LEU F CG  1 
ATOM   6205  C  CD1 . LEU F  1 106 ? 5.074   120.619 120.858 1.00 16.89 ? 106  LEU F CD1 1 
ATOM   6206  C  CD2 . LEU F  1 106 ? 5.245   120.030 118.401 1.00 13.65 ? 106  LEU F CD2 1 
ATOM   6207  N  N   . SER F  1 107 ? 10.328  122.141 118.191 1.00 20.94 ? 107  SER F N   1 
ATOM   6208  C  CA  . SER F  1 107 ? 11.309  123.190 117.912 1.00 22.70 ? 107  SER F CA  1 
ATOM   6209  C  C   . SER F  1 107 ? 12.510  122.469 117.301 1.00 24.17 ? 107  SER F C   1 
ATOM   6210  O  O   . SER F  1 107 ? 12.560  121.230 117.320 1.00 23.29 ? 107  SER F O   1 
ATOM   6211  C  CB  . SER F  1 107 ? 11.748  123.915 119.176 1.00 23.60 ? 107  SER F CB  1 
ATOM   6212  O  OG  . SER F  1 107 ? 12.876  123.268 119.713 1.00 24.43 ? 107  SER F OG  1 
ATOM   6213  N  N   . GLY F  1 108 ? 13.470  123.218 116.756 1.00 24.76 ? 108  GLY F N   1 
ATOM   6214  C  CA  . GLY F  1 108 ? 14.637  122.584 116.160 1.00 26.31 ? 108  GLY F CA  1 
ATOM   6215  C  C   . GLY F  1 108 ? 14.459  122.213 114.698 1.00 27.35 ? 108  GLY F C   1 
ATOM   6216  O  O   . GLY F  1 108 ? 13.545  122.728 114.021 1.00 27.88 ? 108  GLY F O   1 
ATOM   6217  N  N   . ASP F  1 109 ? 15.284  121.296 114.191 1.00 27.59 ? 109  ASP F N   1 
ATOM   6218  C  CA  . ASP F  1 109 ? 15.179  121.002 112.761 1.00 27.83 ? 109  ASP F CA  1 
ATOM   6219  C  C   . ASP F  1 109 ? 14.139  119.968 112.378 1.00 26.43 ? 109  ASP F C   1 
ATOM   6220  O  O   . ASP F  1 109 ? 13.733  119.874 111.214 1.00 27.02 ? 109  ASP F O   1 
ATOM   6221  C  CB  . ASP F  1 109 ? 16.535  120.805 112.075 1.00 28.68 ? 109  ASP F CB  1 
ATOM   6222  C  CG  . ASP F  1 109 ? 16.714  121.763 110.891 1.00 31.53 ? 109  ASP F CG  1 
ATOM   6223  O  OD1 . ASP F  1 109 ? 17.229  122.887 111.094 1.00 33.97 ? 109  ASP F OD1 1 
ATOM   6224  O  OD2 . ASP F  1 109 ? 16.318  121.498 109.731 1.00 37.62 ? 109  ASP F OD2 1 
ATOM   6225  N  N   . HIS F  1 110 ? 13.676  119.212 113.362 1.00 24.30 ? 110  HIS F N   1 
ATOM   6226  C  CA  . HIS F  1 110 ? 12.587  118.279 113.112 1.00 22.44 ? 110  HIS F CA  1 
ATOM   6227  C  C   . HIS F  1 110 ? 11.274  118.899 113.573 1.00 20.87 ? 110  HIS F C   1 
ATOM   6228  O  O   . HIS F  1 110 ? 10.336  118.188 113.921 1.00 20.55 ? 110  HIS F O   1 
ATOM   6229  C  CB  . HIS F  1 110 ? 12.843  116.991 113.858 1.00 22.55 ? 110  HIS F CB  1 
ATOM   6230  C  CG  . HIS F  1 110 ? 14.047  116.258 113.369 1.00 23.41 ? 110  HIS F CG  1 
ATOM   6231  N  ND1 . HIS F  1 110 ? 14.323  114.958 113.732 1.00 23.89 ? 110  HIS F ND1 1 
ATOM   6232  C  CD2 . HIS F  1 110 ? 15.047  116.642 112.539 1.00 23.71 ? 110  HIS F CD2 1 
ATOM   6233  C  CE1 . HIS F  1 110 ? 15.445  114.572 113.147 1.00 23.91 ? 110  HIS F CE1 1 
ATOM   6234  N  NE2 . HIS F  1 110 ? 15.901  115.574 112.415 1.00 25.17 ? 110  HIS F NE2 1 
ATOM   6235  N  N   . CYS F  1 111 ? 11.235  120.232 113.606 1.00 18.77 ? 111  CYS F N   1 
ATOM   6236  C  CA  . CYS F  1 111 ? 10.056  120.964 114.081 1.00 17.79 ? 111  CYS F CA  1 
ATOM   6237  C  C   . CYS F  1 111 ? 8.866   120.783 113.133 1.00 16.17 ? 111  CYS F C   1 
ATOM   6238  O  O   . CYS F  1 111 ? 9.028   120.929 111.925 1.00 16.22 ? 111  CYS F O   1 
ATOM   6239  C  CB  . CYS F  1 111 ? 10.396  122.439 114.295 1.00 17.45 ? 111  CYS F CB  1 
ATOM   6240  S  SG  . CYS F  1 111 ? 9.006   123.333 114.986 1.00 22.88 ? 111  CYS F SG  1 
ATOM   6241  N  N   . ILE F  1 112 ? 7.690   120.450 113.681 1.00 14.47 ? 112  ILE F N   1 
ATOM   6242  C  CA  . ILE F  1 112 ? 6.507   120.128 112.868 1.00 14.07 ? 112  ILE F CA  1 
ATOM   6243  C  C   . ILE F  1 112 ? 5.444   121.220 112.903 1.00 13.88 ? 112  ILE F C   1 
ATOM   6244  O  O   . ILE F  1 112 ? 4.405   121.102 112.244 1.00 15.11 ? 112  ILE F O   1 
ATOM   6245  C  CB  . ILE F  1 112 ? 5.883   118.774 113.289 1.00 14.63 ? 112  ILE F CB  1 
ATOM   6246  C  CG1 . ILE F  1 112 ? 5.374   118.798 114.737 1.00 13.57 ? 112  ILE F CG1 1 
ATOM   6247  C  CG2 . ILE F  1 112 ? 6.885   117.617 113.048 1.00 13.48 ? 112  ILE F CG2 1 
ATOM   6248  C  CD1 . ILE F  1 112 ? 4.584   117.484 115.142 1.00 13.21 ? 112  ILE F CD1 1 
ATOM   6249  N  N   . ILE F  1 113 ? 5.705   122.289 113.651 1.00 13.13 ? 113  ILE F N   1 
ATOM   6250  C  CA  . ILE F  1 113 ? 4.766   123.402 113.714 1.00 12.97 ? 113  ILE F CA  1 
ATOM   6251  C  C   . ILE F  1 113 ? 4.644   124.011 112.339 1.00 12.40 ? 113  ILE F C   1 
ATOM   6252  O  O   . ILE F  1 113 ? 5.655   124.294 111.674 1.00 12.60 ? 113  ILE F O   1 
ATOM   6253  C  CB  . ILE F  1 113 ? 5.271   124.511 114.648 1.00 13.84 ? 113  ILE F CB  1 
ATOM   6254  C  CG1 . ILE F  1 113 ? 5.534   123.972 116.053 1.00 16.26 ? 113  ILE F CG1 1 
ATOM   6255  C  CG2 . ILE F  1 113 ? 4.263   125.691 114.664 1.00 13.85 ? 113  ILE F CG2 1 
ATOM   6256  C  CD1 . ILE F  1 113 ? 4.318   123.597 116.782 1.00 16.45 ? 113  ILE F CD1 1 
ATOM   6257  N  N   . GLY F  1 114 ? 3.424   124.285 111.911 1.00 11.63 ? 114  GLY F N   1 
ATOM   6258  C  CA  . GLY F  1 114 ? 3.277   124.901 110.616 1.00 11.24 ? 114  GLY F CA  1 
ATOM   6259  C  C   . GLY F  1 114 ? 3.243   123.888 109.502 1.00 11.36 ? 114  GLY F C   1 
ATOM   6260  O  O   . GLY F  1 114 ? 3.158   124.275 108.342 1.00 11.18 ? 114  GLY F O   1 
ATOM   6261  N  N   . ARG F  1 115 ? 3.323   122.598 109.836 1.00 9.58  ? 115  ARG F N   1 
ATOM   6262  C  CA  . ARG F  1 115 ? 3.209   121.560 108.809 1.00 10.10 ? 115  ARG F CA  1 
ATOM   6263  C  C   . ARG F  1 115 ? 1.852   120.916 108.962 1.00 10.39 ? 115  ARG F C   1 
ATOM   6264  O  O   . ARG F  1 115 ? 1.021   121.397 109.742 1.00 11.35 ? 115  ARG F O   1 
ATOM   6265  C  CB  . ARG F  1 115 ? 4.357   120.515 108.914 1.00 10.08 ? 115  ARG F CB  1 
ATOM   6266  C  CG  . ARG F  1 115 ? 5.716   121.256 109.079 1.00 9.55  ? 115  ARG F CG  1 
ATOM   6267  C  CD  . ARG F  1 115 ? 6.932   120.411 108.716 1.00 14.72 ? 115  ARG F CD  1 
ATOM   6268  N  NE  . ARG F  1 115 ? 8.195   121.149 108.808 1.00 13.35 ? 115  ARG F NE  1 
ATOM   6269  C  CZ  . ARG F  1 115 ? 8.823   121.696 107.769 1.00 16.42 ? 115  ARG F CZ  1 
ATOM   6270  N  NH1 . ARG F  1 115 ? 8.292   121.609 106.556 1.00 15.23 ? 115  ARG F NH1 1 
ATOM   6271  N  NH2 . ARG F  1 115 ? 9.984   122.332 107.944 1.00 13.05 ? 115  ARG F NH2 1 
ATOM   6272  N  N   . THR F  1 116 ? 1.590   119.858 108.184 1.00 10.84 ? 116  THR F N   1 
ATOM   6273  C  CA  . THR F  1 116 ? 0.250   119.299 108.156 1.00 11.75 ? 116  THR F CA  1 
ATOM   6274  C  C   . THR F  1 116 ? 0.170   117.883 108.708 1.00 12.86 ? 116  THR F C   1 
ATOM   6275  O  O   . THR F  1 116 ? 0.940   117.023 108.274 1.00 12.30 ? 116  THR F O   1 
ATOM   6276  C  CB  . THR F  1 116 ? -0.197  119.228 106.707 1.00 13.21 ? 116  THR F CB  1 
ATOM   6277  O  OG1 . THR F  1 116 ? -0.477  120.548 106.228 1.00 11.90 ? 116  THR F OG1 1 
ATOM   6278  C  CG2 . THR F  1 116 ? -1.536  118.500 106.586 1.00 13.69 ? 116  THR F CG2 1 
ATOM   6279  N  N   . LEU F  1 117 ? -0.755  117.645 109.643 1.00 12.14 ? 117  LEU F N   1 
ATOM   6280  C  CA  . LEU F  1 117 ? -1.019  116.287 110.121 1.00 12.36 ? 117  LEU F CA  1 
ATOM   6281  C  C   . LEU F  1 117 ? -2.080  115.671 109.225 1.00 12.10 ? 117  LEU F C   1 
ATOM   6282  O  O   . LEU F  1 117 ? -3.066  116.317 108.932 1.00 10.50 ? 117  LEU F O   1 
ATOM   6283  C  CB  . LEU F  1 117 ? -1.528  116.330 111.567 1.00 13.76 ? 117  LEU F CB  1 
ATOM   6284  C  CG  . LEU F  1 117 ? -1.721  114.961 112.214 1.00 12.56 ? 117  LEU F CG  1 
ATOM   6285  C  CD1 . LEU F  1 117 ? -0.348  114.272 112.272 1.00 13.90 ? 117  LEU F CD1 1 
ATOM   6286  C  CD2 . LEU F  1 117 ? -2.305  115.225 113.591 1.00 12.82 ? 117  LEU F CD2 1 
ATOM   6287  N  N   . VAL F  1 118 ? -1.871  114.431 108.768 1.00 11.88 ? 118  VAL F N   1 
ATOM   6288  C  CA  . VAL F  1 118 ? -2.811  113.764 107.883 1.00 11.62 ? 118  VAL F CA  1 
ATOM   6289  C  C   . VAL F  1 118 ? -3.229  112.384 108.405 1.00 12.38 ? 118  VAL F C   1 
ATOM   6290  O  O   . VAL F  1 118 ? -2.415  111.659 108.932 1.00 12.18 ? 118  VAL F O   1 
ATOM   6291  C  CB  . VAL F  1 118 ? -2.184  113.561 106.481 1.00 12.08 ? 118  VAL F CB  1 
ATOM   6292  C  CG1 . VAL F  1 118 ? -3.161  112.826 105.547 1.00 13.21 ? 118  VAL F CG1 1 
ATOM   6293  C  CG2 . VAL F  1 118 ? -1.681  114.922 105.879 1.00 11.06 ? 118  VAL F CG2 1 
ATOM   6294  N  N   . VAL F  1 119 ? -4.509  112.061 108.281 1.00 12.60 ? 119  VAL F N   1 
ATOM   6295  C  CA  . VAL F  1 119 ? -4.980  110.728 108.589 1.00 12.38 ? 119  VAL F CA  1 
ATOM   6296  C  C   . VAL F  1 119 ? -5.472  110.104 107.276 1.00 12.70 ? 119  VAL F C   1 
ATOM   6297  O  O   . VAL F  1 119 ? -6.216  110.725 106.501 1.00 11.94 ? 119  VAL F O   1 
ATOM   6298  C  CB  . VAL F  1 119 ? -6.039  110.691 109.676 1.00 12.47 ? 119  VAL F CB  1 
ATOM   6299  C  CG1 . VAL F  1 119 ? -7.275  111.491 109.280 1.00 14.42 ? 119  VAL F CG1 1 
ATOM   6300  C  CG2 . VAL F  1 119 ? -6.417  109.222 110.014 1.00 14.32 ? 119  VAL F CG2 1 
ATOM   6301  N  N   . HIS F  1 120 ? -5.076  108.854 107.075 1.00 12.49 ? 120  HIS F N   1 
ATOM   6302  C  CA  . HIS F  1 120 ? -5.251  108.196 105.798 1.00 12.60 ? 120  HIS F CA  1 
ATOM   6303  C  C   . HIS F  1 120 ? -6.394  107.189 105.662 1.00 12.42 ? 120  HIS F C   1 
ATOM   6304  O  O   . HIS F  1 120 ? -6.884  106.676 106.636 1.00 13.64 ? 120  HIS F O   1 
ATOM   6305  C  CB  . HIS F  1 120 ? -3.944  107.492 105.444 1.00 11.57 ? 120  HIS F CB  1 
ATOM   6306  C  CG  . HIS F  1 120 ? -2.909  108.424 104.906 1.00 13.71 ? 120  HIS F CG  1 
ATOM   6307  N  ND1 . HIS F  1 120 ? -2.879  108.802 103.581 1.00 11.81 ? 120  HIS F ND1 1 
ATOM   6308  C  CD2 . HIS F  1 120 ? -1.869  109.058 105.502 1.00 10.30 ? 120  HIS F CD2 1 
ATOM   6309  C  CE1 . HIS F  1 120 ? -1.865  109.621 103.380 1.00 10.11 ? 120  HIS F CE1 1 
ATOM   6310  N  NE2 . HIS F  1 120 ? -1.252  109.804 104.531 1.00 10.90 ? 120  HIS F NE2 1 
ATOM   6311  N  N   . GLU F  1 121 ? -6.749  106.920 104.413 1.00 12.59 ? 121  GLU F N   1 
ATOM   6312  C  CA  . GLU F  1 121 ? -7.762  105.961 103.990 1.00 13.37 ? 121  GLU F CA  1 
ATOM   6313  C  C   . GLU F  1 121 ? -7.428  104.577 104.474 1.00 13.87 ? 121  GLU F C   1 
ATOM   6314  O  O   . GLU F  1 121 ? -8.319  103.849 104.926 1.00 14.50 ? 121  GLU F O   1 
ATOM   6315  C  CB  . GLU F  1 121 ? -7.787  105.941 102.466 1.00 13.93 ? 121  GLU F CB  1 
ATOM   6316  C  CG  . GLU F  1 121 ? -8.742  104.943 101.819 1.00 15.10 ? 121  GLU F CG  1 
ATOM   6317  C  CD  . GLU F  1 121 ? -8.455  104.760 100.334 1.00 19.46 ? 121  GLU F CD  1 
ATOM   6318  O  OE1 . GLU F  1 121 ? -9.274  104.102 99.653  1.00 21.03 ? 121  GLU F OE1 1 
ATOM   6319  O  OE2 . GLU F  1 121 ? -7.415  105.257 99.831  1.00 17.69 ? 121  GLU F OE2 1 
ATOM   6320  N  N   . LYS F  1 122 ? -6.152  104.207 104.388 1.00 14.17 ? 122  LYS F N   1 
ATOM   6321  C  CA  . LYS F  1 122 ? -5.748  102.846 104.738 1.00 15.07 ? 122  LYS F CA  1 
ATOM   6322  C  C   . LYS F  1 122 ? -4.573  102.723 105.683 1.00 14.01 ? 122  LYS F C   1 
ATOM   6323  O  O   . LYS F  1 122 ? -3.926  103.689 106.059 1.00 14.04 ? 122  LYS F O   1 
ATOM   6324  C  CB  . LYS F  1 122 ? -5.403  102.009 103.495 1.00 15.02 ? 122  LYS F CB  1 
ATOM   6325  C  CG  . LYS F  1 122 ? -6.198  102.257 102.252 1.00 18.93 ? 122  LYS F CG  1 
ATOM   6326  C  CD  . LYS F  1 122 ? -5.616  101.429 101.105 1.00 23.20 ? 122  LYS F CD  1 
ATOM   6327  C  CE  . LYS F  1 122 ? -5.679  102.183 99.779  1.00 25.47 ? 122  LYS F CE  1 
ATOM   6328  N  NZ  . LYS F  1 122 ? -5.722  101.262 98.590  1.00 26.73 ? 122  LYS F NZ  1 
ATOM   6329  N  N   . ALA F  1 123 ? -4.276  101.476 106.022 1.00 13.76 ? 123  ALA F N   1 
ATOM   6330  C  CA  . ALA F  1 123 ? -3.202  101.212 106.932 1.00 13.94 ? 123  ALA F CA  1 
ATOM   6331  C  C   . ALA F  1 123 ? -1.884  101.562 106.272 1.00 14.21 ? 123  ALA F C   1 
ATOM   6332  O  O   . ALA F  1 123 ? -1.691  101.361 105.047 1.00 14.50 ? 123  ALA F O   1 
ATOM   6333  C  CB  . ALA F  1 123 ? -3.207  99.725  107.353 1.00 14.11 ? 123  ALA F CB  1 
ATOM   6334  N  N   . ASP F  1 124 ? -0.997  102.101 107.099 1.00 13.20 ? 124  ASP F N   1 
ATOM   6335  C  CA  . ASP F  1 124 ? 0.378   102.347 106.742 1.00 12.93 ? 124  ASP F CA  1 
ATOM   6336  C  C   . ASP F  1 124 ? 1.066   100.986 106.915 1.00 12.27 ? 124  ASP F C   1 
ATOM   6337  O  O   . ASP F  1 124 ? 1.046   100.404 108.009 1.00 12.05 ? 124  ASP F O   1 
ATOM   6338  C  CB  . ASP F  1 124 ? 0.941   103.379 107.720 1.00 13.17 ? 124  ASP F CB  1 
ATOM   6339  C  CG  . ASP F  1 124 ? 2.389   103.761 107.438 1.00 14.16 ? 124  ASP F CG  1 
ATOM   6340  O  OD1 . ASP F  1 124 ? 3.140   102.982 106.794 1.00 11.03 ? 124  ASP F OD1 1 
ATOM   6341  O  OD2 . ASP F  1 124 ? 2.874   104.853 107.835 1.00 16.21 ? 124  ASP F OD2 1 
ATOM   6342  N  N   . ASP F  1 125 ? 1.683   100.471 105.853 1.00 12.34 ? 125  ASP F N   1 
ATOM   6343  C  CA  . ASP F  1 125 ? 2.391   99.175  105.965 1.00 12.32 ? 125  ASP F CA  1 
ATOM   6344  C  C   . ASP F  1 125 ? 3.803   99.274  106.554 1.00 12.46 ? 125  ASP F C   1 
ATOM   6345  O  O   . ASP F  1 125 ? 4.589   98.310  106.512 1.00 11.28 ? 125  ASP F O   1 
ATOM   6346  C  CB  . ASP F  1 125 ? 2.388   98.408  104.644 1.00 12.16 ? 125  ASP F CB  1 
ATOM   6347  C  CG  . ASP F  1 125 ? 3.267   99.031  103.577 1.00 13.17 ? 125  ASP F CG  1 
ATOM   6348  O  OD1 . ASP F  1 125 ? 4.196   99.809  103.875 1.00 13.35 ? 125  ASP F OD1 1 
ATOM   6349  O  OD2 . ASP F  1 125 ? 3.139   98.726  102.373 1.00 13.70 ? 125  ASP F OD2 1 
ATOM   6350  N  N   . LEU F  1 126 ? 4.101   100.447 107.099 1.00 12.81 ? 126  LEU F N   1 
ATOM   6351  C  CA  . LEU F  1 126 ? 5.372   100.738 107.775 1.00 12.55 ? 126  LEU F CA  1 
ATOM   6352  C  C   . LEU F  1 126 ? 6.628   100.540 106.921 1.00 12.10 ? 126  LEU F C   1 
ATOM   6353  O  O   . LEU F  1 126 ? 7.716   100.352 107.447 1.00 12.75 ? 126  LEU F O   1 
ATOM   6354  C  CB  . LEU F  1 126 ? 5.453   100.031 109.139 1.00 12.72 ? 126  LEU F CB  1 
ATOM   6355  C  CG  . LEU F  1 126 ? 4.103   100.109 109.884 1.00 14.55 ? 126  LEU F CG  1 
ATOM   6356  C  CD1 . LEU F  1 126 ? 4.140   99.275  111.171 1.00 17.90 ? 126  LEU F CD1 1 
ATOM   6357  C  CD2 . LEU F  1 126 ? 3.644   101.561 110.136 1.00 15.21 ? 126  LEU F CD2 1 
ATOM   6358  N  N   . GLY F  1 127 ? 6.462   100.594 105.606 1.00 11.01 ? 127  GLY F N   1 
ATOM   6359  C  CA  . GLY F  1 127 ? 7.584   100.547 104.696 1.00 11.91 ? 127  GLY F CA  1 
ATOM   6360  C  C   . GLY F  1 127 ? 8.013   99.121  104.392 1.00 11.76 ? 127  GLY F C   1 
ATOM   6361  O  O   . GLY F  1 127 ? 9.071   98.899  103.810 1.00 12.44 ? 127  GLY F O   1 
ATOM   6362  N  N   . LYS F  1 128 ? 7.178   98.168  104.773 1.00 11.23 ? 128  LYS F N   1 
ATOM   6363  C  CA  . LYS F  1 128 ? 7.535   96.757  104.597 1.00 11.53 ? 128  LYS F CA  1 
ATOM   6364  C  C   . LYS F  1 128 ? 6.718   96.055  103.488 1.00 11.01 ? 128  LYS F C   1 
ATOM   6365  O  O   . LYS F  1 128 ? 6.674   94.830  103.432 1.00 11.18 ? 128  LYS F O   1 
ATOM   6366  C  CB  . LYS F  1 128 ? 7.417   96.044  105.952 1.00 12.02 ? 128  LYS F CB  1 
ATOM   6367  C  CG  . LYS F  1 128 ? 8.449   96.612  106.949 1.00 16.45 ? 128  LYS F CG  1 
ATOM   6368  C  CD  . LYS F  1 128 ? 8.241   96.223  108.387 1.00 23.69 ? 128  LYS F CD  1 
ATOM   6369  C  CE  . LYS F  1 128 ? 9.212   97.007  109.271 1.00 26.07 ? 128  LYS F CE  1 
ATOM   6370  N  NZ  . LYS F  1 128 ? 10.542  97.209  108.582 1.00 29.01 ? 128  LYS F NZ  1 
ATOM   6371  N  N   . GLY F  1 129 ? 6.115   96.835  102.599 1.00 11.33 ? 129  GLY F N   1 
ATOM   6372  C  CA  . GLY F  1 129 ? 5.253   96.315  101.550 1.00 11.49 ? 129  GLY F CA  1 
ATOM   6373  C  C   . GLY F  1 129 ? 5.953   95.832  100.286 1.00 12.20 ? 129  GLY F C   1 
ATOM   6374  O  O   . GLY F  1 129 ? 5.293   95.303  99.402  1.00 11.79 ? 129  GLY F O   1 
ATOM   6375  N  N   . GLY F  1 130 ? 7.265   96.000  100.191 1.00 11.65 ? 130  GLY F N   1 
ATOM   6376  C  CA  . GLY F  1 130 ? 7.990   95.519  99.018  1.00 14.02 ? 130  GLY F CA  1 
ATOM   6377  C  C   . GLY F  1 130 ? 7.938   96.492  97.831  1.00 15.08 ? 130  GLY F C   1 
ATOM   6378  O  O   . GLY F  1 130 ? 8.966   96.733  97.196  1.00 16.41 ? 130  GLY F O   1 
ATOM   6379  N  N   . ASN F  1 131 ? 6.774   97.048  97.517  1.00 15.14 ? 131  ASN F N   1 
ATOM   6380  C  CA  . ASN F  1 131 ? 6.680   97.968  96.364  1.00 14.97 ? 131  ASN F CA  1 
ATOM   6381  C  C   . ASN F  1 131 ? 7.342   99.333  96.635  1.00 15.92 ? 131  ASN F C   1 
ATOM   6382  O  O   . ASN F  1 131 ? 7.604   99.709  97.779  1.00 15.68 ? 131  ASN F O   1 
ATOM   6383  C  CB  . ASN F  1 131 ? 5.229   98.129  95.835  1.00 14.19 ? 131  ASN F CB  1 
ATOM   6384  C  CG  . ASN F  1 131 ? 4.281   98.704  96.868  1.00 15.71 ? 131  ASN F CG  1 
ATOM   6385  O  OD1 . ASN F  1 131 ? 4.603   98.739  98.039  1.00 19.80 ? 131  ASN F OD1 1 
ATOM   6386  N  ND2 . ASN F  1 131 ? 3.099   99.172  96.428  1.00 18.12 ? 131  ASN F ND2 1 
ATOM   6387  N  N   . GLU F  1 132 ? 7.644   100.057 95.573  1.00 15.63 ? 132  GLU F N   1 
ATOM   6388  C  CA  . GLU F  1 132 ? 8.238   101.385 95.712  1.00 16.92 ? 132  GLU F CA  1 
ATOM   6389  C  C   . GLU F  1 132 ? 7.397   102.308 96.607  1.00 16.19 ? 132  GLU F C   1 
ATOM   6390  O  O   . GLU F  1 132 ? 7.917   103.063 97.461  1.00 16.09 ? 132  GLU F O   1 
ATOM   6391  C  CB  . GLU F  1 132 ? 8.406   102.000 94.321  1.00 17.45 ? 132  GLU F CB  1 
ATOM   6392  C  CG  . GLU F  1 132 ? 9.486   103.068 94.249  1.00 23.66 ? 132  GLU F CG  1 
ATOM   6393  C  CD  . GLU F  1 132 ? 9.426   103.951 93.004  1.00 29.30 ? 132  GLU F CD  1 
ATOM   6394  O  OE1 . GLU F  1 132 ? 9.899   105.115 93.097  1.00 31.95 ? 132  GLU F OE1 1 
ATOM   6395  O  OE2 . GLU F  1 132 ? 8.920   103.504 91.941  1.00 32.14 ? 132  GLU F OE2 1 
ATOM   6396  N  N   . GLU F  1 133 ? 6.089   102.245 96.428  1.00 14.99 ? 133  GLU F N   1 
ATOM   6397  C  CA  . GLU F  1 133 ? 5.224   103.122 97.175  1.00 15.10 ? 133  GLU F CA  1 
ATOM   6398  C  C   . GLU F  1 133 ? 5.340   102.865 98.678  1.00 14.58 ? 133  GLU F C   1 
ATOM   6399  O  O   . GLU F  1 133 ? 5.226   103.797 99.486  1.00 13.86 ? 133  GLU F O   1 
ATOM   6400  C  CB  . GLU F  1 133 ? 3.783   103.009 96.695  1.00 16.18 ? 133  GLU F CB  1 
ATOM   6401  C  CG  . GLU F  1 133 ? 2.835   104.043 97.277  1.00 17.06 ? 133  GLU F CG  1 
ATOM   6402  C  CD  . GLU F  1 133 ? 3.060   105.459 96.745  1.00 25.01 ? 133  GLU F CD  1 
ATOM   6403  O  OE1 . GLU F  1 133 ? 3.744   105.633 95.718  1.00 26.67 ? 133  GLU F OE1 1 
ATOM   6404  O  OE2 . GLU F  1 133 ? 2.547   106.397 97.372  1.00 26.64 ? 133  GLU F OE2 1 
ATOM   6405  N  N   . SER F  1 134 ? 5.567   101.611 99.056  1.00 13.79 ? 134  SER F N   1 
ATOM   6406  C  CA  . SER F  1 134 ? 5.732   101.324 100.468 1.00 12.97 ? 134  SER F CA  1 
ATOM   6407  C  C   . SER F  1 134 ? 6.835   102.172 101.070 1.00 13.05 ? 134  SER F C   1 
ATOM   6408  O  O   . SER F  1 134 ? 6.721   102.649 102.200 1.00 12.02 ? 134  SER F O   1 
ATOM   6409  C  CB  . SER F  1 134 ? 6.124   99.865  100.684 1.00 13.00 ? 134  SER F CB  1 
ATOM   6410  O  OG  . SER F  1 134 ? 6.176   99.615  102.090 1.00 10.94 ? 134  SER F OG  1 
ATOM   6411  N  N   . THR F  1 135 ? 7.930   102.311 100.329 1.00 13.20 ? 135  THR F N   1 
ATOM   6412  C  CA  . THR F  1 135 ? 9.083   103.076 100.792 1.00 15.37 ? 135  THR F CA  1 
ATOM   6413  C  C   . THR F  1 135 ? 8.829   104.572 100.753 1.00 15.72 ? 135  THR F C   1 
ATOM   6414  O  O   . THR F  1 135 ? 9.697   105.345 101.169 1.00 15.30 ? 135  THR F O   1 
ATOM   6415  C  CB  . THR F  1 135 ? 10.318  102.826 99.887  1.00 16.05 ? 135  THR F CB  1 
ATOM   6416  O  OG1 . THR F  1 135 ? 10.095  103.452 98.602  1.00 19.97 ? 135  THR F OG1 1 
ATOM   6417  C  CG2 . THR F  1 135 ? 10.454  101.400 99.558  1.00 17.78 ? 135  THR F CG2 1 
ATOM   6418  N  N   . LYS F  1 136 ? 7.672   104.992 100.247 1.00 15.32 ? 136  LYS F N   1 
ATOM   6419  C  CA  . LYS F  1 136 ? 7.360   106.440 100.226 1.00 16.67 ? 136  LYS F CA  1 
ATOM   6420  C  C   . LYS F  1 136 ? 6.271   106.862 101.182 1.00 16.20 ? 136  LYS F C   1 
ATOM   6421  O  O   . LYS F  1 136 ? 6.446   107.826 101.941 1.00 15.71 ? 136  LYS F O   1 
ATOM   6422  C  CB  . LYS F  1 136 ? 7.008   106.923 98.817  1.00 17.67 ? 136  LYS F CB  1 
ATOM   6423  C  CG  . LYS F  1 136 ? 8.151   106.731 97.848  1.00 19.94 ? 136  LYS F CG  1 
ATOM   6424  C  CD  . LYS F  1 136 ? 7.636   106.584 96.443  1.00 26.85 ? 136  LYS F CD  1 
ATOM   6425  C  CE  . LYS F  1 136 ? 8.455   107.399 95.458  1.00 31.43 ? 136  LYS F CE  1 
ATOM   6426  N  NZ  . LYS F  1 136 ? 7.607   107.816 94.273  1.00 32.90 ? 136  LYS F NZ  1 
ATOM   6427  N  N   . THR F  1 137 ? 5.163   106.135 101.169 1.00 15.93 ? 137  THR F N   1 
ATOM   6428  C  CA  . THR F  1 137 ? 3.978   106.506 101.935 1.00 16.27 ? 137  THR F CA  1 
ATOM   6429  C  C   . THR F  1 137 ? 3.446   105.373 102.790 1.00 16.13 ? 137  THR F C   1 
ATOM   6430  O  O   . THR F  1 137 ? 2.443   105.529 103.506 1.00 16.50 ? 137  THR F O   1 
ATOM   6431  C  CB  . THR F  1 137 ? 2.864   106.889 100.954 1.00 17.06 ? 137  THR F CB  1 
ATOM   6432  O  OG1 . THR F  1 137 ? 2.493   105.731 100.185 1.00 16.10 ? 137  THR F OG1 1 
ATOM   6433  C  CG2 . THR F  1 137 ? 3.382   107.868 99.883  1.00 19.41 ? 137  THR F CG2 1 
ATOM   6434  N  N   . GLY F  1 138 ? 4.078   104.207 102.710 1.00 14.15 ? 138  GLY F N   1 
ATOM   6435  C  CA  . GLY F  1 138 ? 3.512   103.064 103.394 1.00 13.49 ? 138  GLY F CA  1 
ATOM   6436  C  C   . GLY F  1 138 ? 2.226   102.545 102.736 1.00 12.79 ? 138  GLY F C   1 
ATOM   6437  O  O   . GLY F  1 138 ? 1.483   101.807 103.367 1.00 12.72 ? 138  GLY F O   1 
ATOM   6438  N  N   . ASN F  1 139 ? 1.954   102.927 101.490 1.00 11.44 ? 139  ASN F N   1 
ATOM   6439  C  CA  . ASN F  1 139 ? 0.713   102.501 100.808 1.00 11.99 ? 139  ASN F CA  1 
ATOM   6440  C  C   . ASN F  1 139 ? -0.590  102.870 101.559 1.00 11.93 ? 139  ASN F C   1 
ATOM   6441  O  O   . ASN F  1 139 ? -1.616  102.180 101.478 1.00 12.15 ? 139  ASN F O   1 
ATOM   6442  C  CB  . ASN F  1 139 ? 0.751   100.996 100.462 1.00 11.66 ? 139  ASN F CB  1 
ATOM   6443  C  CG  . ASN F  1 139 ? 1.782   100.664 99.371  1.00 14.56 ? 139  ASN F CG  1 
ATOM   6444  O  OD1 . ASN F  1 139 ? 1.648   101.091 98.217  1.00 16.25 ? 139  ASN F OD1 1 
ATOM   6445  N  ND2 . ASN F  1 139 ? 2.780   99.839  99.723  1.00 13.10 ? 139  ASN F ND2 1 
ATOM   6446  N  N   . ALA F  1 140 ? -0.543  103.969 102.294 1.00 10.93 ? 140  ALA F N   1 
ATOM   6447  C  CA  . ALA F  1 140 ? -1.675  104.355 103.135 1.00 12.49 ? 140  ALA F CA  1 
ATOM   6448  C  C   . ALA F  1 140 ? -2.888  104.957 102.409 1.00 12.87 ? 140  ALA F C   1 
ATOM   6449  O  O   . ALA F  1 140 ? -3.927  105.222 103.017 1.00 12.93 ? 140  ALA F O   1 
ATOM   6450  C  CB  . ALA F  1 140 ? -1.204  105.259 104.243 1.00 12.26 ? 140  ALA F CB  1 
ATOM   6451  N  N   . GLY F  1 141 ? -2.783  105.125 101.101 1.00 13.55 ? 141  GLY F N   1 
ATOM   6452  C  CA  . GLY F  1 141 ? -3.935  105.563 100.348 1.00 13.22 ? 141  GLY F CA  1 
ATOM   6453  C  C   . GLY F  1 141 ? -4.221  107.051 100.455 1.00 14.43 ? 141  GLY F C   1 
ATOM   6454  O  O   . GLY F  1 141 ? -3.337  107.884 100.676 1.00 14.16 ? 141  GLY F O   1 
ATOM   6455  N  N   . SER F  1 142 ? -5.487  107.387 100.297 1.00 13.80 ? 142  SER F N   1 
ATOM   6456  C  CA  . SER F  1 142 ? -5.851  108.785 100.197 1.00 13.81 ? 142  SER F CA  1 
ATOM   6457  C  C   . SER F  1 142 ? -5.844  109.482 101.539 1.00 13.11 ? 142  SER F C   1 
ATOM   6458  O  O   . SER F  1 142 ? -5.717  108.858 102.593 1.00 12.90 ? 142  SER F O   1 
ATOM   6459  C  CB  . SER F  1 142 ? -7.207  108.937 99.492  1.00 14.53 ? 142  SER F CB  1 
ATOM   6460  O  OG  . SER F  1 142 ? -8.279  108.674 100.380 1.00 17.42 ? 142  SER F OG  1 
ATOM   6461  N  N   . ARG F  1 143 ? -5.980  110.794 101.483 1.00 12.99 ? 143  ARG F N   1 
ATOM   6462  C  CA  . ARG F  1 143 ? -5.945  111.616 102.693 1.00 13.65 ? 143  ARG F CA  1 
ATOM   6463  C  C   . ARG F  1 143 ? -7.370  111.975 103.074 1.00 13.48 ? 143  ARG F C   1 
ATOM   6464  O  O   . ARG F  1 143 ? -8.027  112.732 102.366 1.00 13.80 ? 143  ARG F O   1 
ATOM   6465  C  CB  . ARG F  1 143 ? -5.092  112.857 102.423 1.00 14.11 ? 143  ARG F CB  1 
ATOM   6466  C  CG  . ARG F  1 143 ? -3.704  112.530 101.840 1.00 14.45 ? 143  ARG F CG  1 
ATOM   6467  C  CD  . ARG F  1 143 ? -2.836  113.757 101.369 1.00 15.86 ? 143  ARG F CD  1 
ATOM   6468  N  NE  . ARG F  1 143 ? -1.613  113.260 100.734 1.00 13.92 ? 143  ARG F NE  1 
ATOM   6469  C  CZ  . ARG F  1 143 ? -0.518  113.961 100.439 1.00 14.07 ? 143  ARG F CZ  1 
ATOM   6470  N  NH1 . ARG F  1 143 ? -0.456  115.269 100.690 1.00 12.63 ? 143  ARG F NH1 1 
ATOM   6471  N  NH2 . ARG F  1 143 ? 0.532   113.333 99.860  1.00 12.91 ? 143  ARG F NH2 1 
ATOM   6472  N  N   . LEU F  1 144 ? -7.851  111.437 104.184 1.00 12.76 ? 144  LEU F N   1 
ATOM   6473  C  CA  . LEU F  1 144 ? -9.253  111.645 104.539 1.00 12.54 ? 144  LEU F CA  1 
ATOM   6474  C  C   . LEU F  1 144 ? -9.455  112.957 105.222 1.00 11.76 ? 144  LEU F C   1 
ATOM   6475  O  O   . LEU F  1 144 ? -10.493 113.550 105.069 1.00 12.45 ? 144  LEU F O   1 
ATOM   6476  C  CB  . LEU F  1 144 ? -9.756  110.541 105.450 1.00 12.19 ? 144  LEU F CB  1 
ATOM   6477  C  CG  . LEU F  1 144 ? -9.530  109.146 104.859 1.00 13.81 ? 144  LEU F CG  1 
ATOM   6478  C  CD1 . LEU F  1 144 ? -9.919  108.073 105.857 1.00 16.16 ? 144  LEU F CD1 1 
ATOM   6479  C  CD2 . LEU F  1 144 ? -10.317 108.979 103.552 1.00 14.37 ? 144  LEU F CD2 1 
ATOM   6480  N  N   . ALA F  1 145 ? -8.496  113.344 106.047 1.00 12.40 ? 145  ALA F N   1 
ATOM   6481  C  CA  . ALA F  1 145 ? -8.576  114.611 106.796 1.00 12.64 ? 145  ALA F CA  1 
ATOM   6482  C  C   . ALA F  1 145 ? -7.179  115.108 107.118 1.00 12.49 ? 145  ALA F C   1 
ATOM   6483  O  O   . ALA F  1 145 ? -6.235  114.324 107.218 1.00 11.61 ? 145  ALA F O   1 
ATOM   6484  C  CB  . ALA F  1 145 ? -9.373  114.456 108.097 1.00 12.14 ? 145  ALA F CB  1 
ATOM   6485  N  N   . CYS F  1 146 ? -7.056  116.421 107.314 1.00 12.25 ? 146  CYS F N   1 
ATOM   6486  C  CA  . CYS F  1 146 ? -5.773  116.988 107.659 1.00 13.15 ? 146  CYS F CA  1 
ATOM   6487  C  C   . CYS F  1 146 ? -6.004  118.344 108.323 1.00 13.17 ? 146  CYS F C   1 
ATOM   6488  O  O   . CYS F  1 146 ? -7.147  118.854 108.421 1.00 12.96 ? 146  CYS F O   1 
ATOM   6489  C  CB  . CYS F  1 146 ? -4.892  117.183 106.423 1.00 13.68 ? 146  CYS F CB  1 
ATOM   6490  S  SG  . CYS F  1 146 ? -5.691  118.244 105.187 1.00 17.23 ? 146  CYS F SG  1 
ATOM   6491  N  N   . GLY F  1 147 ? -4.913  118.910 108.794 1.00 12.87 ? 147  GLY F N   1 
ATOM   6492  C  CA  . GLY F  1 147 ? -4.983  120.218 109.425 1.00 13.43 ? 147  GLY F CA  1 
ATOM   6493  C  C   . GLY F  1 147 ? -3.572  120.700 109.641 1.00 13.44 ? 147  GLY F C   1 
ATOM   6494  O  O   . GLY F  1 147 ? -2.625  119.920 109.666 1.00 13.90 ? 147  GLY F O   1 
ATOM   6495  N  N   . VAL F  1 148 ? -3.434  122.013 109.779 1.00 12.77 ? 148  VAL F N   1 
ATOM   6496  C  CA  . VAL F  1 148 ? -2.142  122.583 109.997 1.00 12.36 ? 148  VAL F CA  1 
ATOM   6497  C  C   . VAL F  1 148 ? -1.882  122.540 111.494 1.00 13.08 ? 148  VAL F C   1 
ATOM   6498  O  O   . VAL F  1 148 ? -2.781  122.823 112.304 1.00 14.52 ? 148  VAL F O   1 
ATOM   6499  C  CB  . VAL F  1 148 ? -2.061  124.062 109.453 1.00 12.59 ? 148  VAL F CB  1 
ATOM   6500  C  CG1 . VAL F  1 148 ? -0.669  124.637 109.697 1.00 12.30 ? 148  VAL F CG1 1 
ATOM   6501  C  CG2 . VAL F  1 148 ? -2.315  124.072 107.952 1.00 12.32 ? 148  VAL F CG2 1 
ATOM   6502  N  N   . ILE F  1 149 ? -0.665  122.152 111.842 1.00 11.93 ? 149  ILE F N   1 
ATOM   6503  C  CA  . ILE F  1 149 ? -0.215  122.059 113.225 1.00 11.85 ? 149  ILE F CA  1 
ATOM   6504  C  C   . ILE F  1 149 ? 0.119   123.436 113.784 1.00 12.22 ? 149  ILE F C   1 
ATOM   6505  O  O   . ILE F  1 149 ? 1.051   124.114 113.333 1.00 13.43 ? 149  ILE F O   1 
ATOM   6506  C  CB  . ILE F  1 149 ? 0.973   121.100 113.349 1.00 11.77 ? 149  ILE F CB  1 
ATOM   6507  C  CG1 . ILE F  1 149 ? 0.566   119.708 112.845 1.00 11.31 ? 149  ILE F CG1 1 
ATOM   6508  C  CG2 . ILE F  1 149 ? 1.422   120.997 114.811 1.00 12.01 ? 149  ILE F CG2 1 
ATOM   6509  C  CD1 . ILE F  1 149 ? 1.762   118.729 112.771 1.00 12.69 ? 149  ILE F CD1 1 
ATOM   6510  N  N   . GLY F  1 150 ? -0.652  123.865 114.771 1.00 12.85 ? 150  GLY F N   1 
ATOM   6511  C  CA  . GLY F  1 150 ? -0.504  125.235 115.283 1.00 12.45 ? 150  GLY F CA  1 
ATOM   6512  C  C   . GLY F  1 150 ? -0.042  125.330 116.720 1.00 13.47 ? 150  GLY F C   1 
ATOM   6513  O  O   . GLY F  1 150 ? -0.205  124.402 117.513 1.00 13.23 ? 150  GLY F O   1 
ATOM   6514  N  N   . ILE F  1 151 ? 0.567   126.457 117.057 1.00 12.37 ? 151  ILE F N   1 
ATOM   6515  C  CA  . ILE F  1 151 ? 0.993   126.690 118.420 1.00 13.28 ? 151  ILE F CA  1 
ATOM   6516  C  C   . ILE F  1 151 ? -0.208  126.784 119.330 1.00 13.76 ? 151  ILE F C   1 
ATOM   6517  O  O   . ILE F  1 151 ? -1.170  127.480 119.022 1.00 14.32 ? 151  ILE F O   1 
ATOM   6518  C  CB  . ILE F  1 151 ? 1.788   127.979 118.462 1.00 13.35 ? 151  ILE F CB  1 
ATOM   6519  C  CG1 . ILE F  1 151 ? 3.141   127.750 117.773 1.00 14.03 ? 151  ILE F CG1 1 
ATOM   6520  C  CG2 . ILE F  1 151 ? 1.971   128.474 119.903 1.00 13.84 ? 151  ILE F CG2 1 
ATOM   6521  C  CD1 . ILE F  1 151 ? 3.901   129.052 117.503 1.00 15.16 ? 151  ILE F CD1 1 
ATOM   6522  N  N   . ALA F  1 152 ? -0.145  126.110 120.476 1.00 14.28 ? 152  ALA F N   1 
ATOM   6523  C  CA  . ALA F  1 152 ? -1.237  126.160 121.435 1.00 15.67 ? 152  ALA F CA  1 
ATOM   6524  C  C   . ALA F  1 152 ? -0.804  126.859 122.727 1.00 17.00 ? 152  ALA F C   1 
ATOM   6525  O  O   . ALA F  1 152 ? 0.386   127.034 122.976 1.00 16.84 ? 152  ALA F O   1 
ATOM   6526  C  CB  . ALA F  1 152 ? -1.728  124.738 121.751 1.00 16.13 ? 152  ALA F CB  1 
ATOM   6527  N  N   . GLN F  1 153 ? -1.781  127.245 123.539 1.00 18.24 ? 153  GLN F N   1 
ATOM   6528  C  CA  . GLN F  1 153 ? -1.518  127.914 124.812 1.00 20.29 ? 153  GLN F CA  1 
ATOM   6529  C  C   . GLN F  1 153 ? -1.078  126.879 125.843 1.00 21.13 ? 153  GLN F C   1 
ATOM   6530  O  O   . GLN F  1 153 ? -1.702  125.827 125.958 1.00 21.54 ? 153  GLN F O   1 
ATOM   6531  C  CB  . GLN F  1 153 ? -2.779  128.620 125.300 1.00 19.78 ? 153  GLN F CB  1 
ATOM   6532  C  CG  . GLN F  1 153 ? -2.608  129.339 126.655 1.00 24.43 ? 153  GLN F CG  1 
ATOM   6533  C  CD  . GLN F  1 153 ? -3.759  130.278 126.957 1.00 27.96 ? 153  GLN F CD  1 
ATOM   6534  O  OE1 . GLN F  1 153 ? -4.929  129.892 126.827 1.00 31.30 ? 153  GLN F OE1 1 
ATOM   6535  N  NE2 . GLN F  1 153 ? -3.439  131.513 127.351 1.00 28.18 ? 153  GLN F NE2 1 
ATOM   6536  O  OXT . GLN F  1 153 ? -0.112  127.065 126.601 1.00 23.03 ? 153  GLN F OXT 1 
ATOM   6537  N  N   . ALA G  1 1   ? 1.437   136.546 76.003  1.00 34.74 ? 1    ALA G N   1 
ATOM   6538  C  CA  . ALA G  1 1   ? 1.904   137.943 75.735  1.00 34.58 ? 1    ALA G CA  1 
ATOM   6539  C  C   . ALA G  1 1   ? 2.855   137.943 74.554  1.00 33.93 ? 1    ALA G C   1 
ATOM   6540  O  O   . ALA G  1 1   ? 3.680   137.018 74.405  1.00 34.91 ? 1    ALA G O   1 
ATOM   6541  C  CB  . ALA G  1 1   ? 2.566   138.546 76.975  1.00 35.00 ? 1    ALA G CB  1 
ATOM   6542  N  N   . THR G  1 2   ? 2.783   138.967 73.705  1.00 32.26 ? 2    THR G N   1 
ATOM   6543  C  CA  . THR G  1 2   ? 3.554   138.863 72.446  1.00 30.23 ? 2    THR G CA  1 
ATOM   6544  C  C   . THR G  1 2   ? 4.993   139.408 72.373  1.00 28.04 ? 2    THR G C   1 
ATOM   6545  O  O   . THR G  1 2   ? 5.256   140.609 72.504  1.00 27.31 ? 2    THR G O   1 
ATOM   6546  C  CB  . THR G  1 2   ? 2.670   139.211 71.206  1.00 30.70 ? 2    THR G CB  1 
ATOM   6547  O  OG1 . THR G  1 2   ? 2.583   138.064 70.351  1.00 31.92 ? 2    THR G OG1 1 
ATOM   6548  C  CG2 . THR G  1 2   ? 3.332   140.230 70.322  1.00 31.53 ? 2    THR G CG2 1 
ATOM   6549  N  N   . LYS G  1 3   ? 5.919   138.484 72.146  1.00 25.64 ? 3    LYS G N   1 
ATOM   6550  C  CA  . LYS G  1 3   ? 7.340   138.786 72.073  1.00 23.16 ? 3    LYS G CA  1 
ATOM   6551  C  C   . LYS G  1 3   ? 7.931   138.236 70.770  1.00 21.53 ? 3    LYS G C   1 
ATOM   6552  O  O   . LYS G  1 3   ? 7.425   137.251 70.227  1.00 19.85 ? 3    LYS G O   1 
ATOM   6553  C  CB  . LYS G  1 3   ? 8.035   138.147 73.276  1.00 23.82 ? 3    LYS G CB  1 
ATOM   6554  C  CG  . LYS G  1 3   ? 7.573   138.725 74.650  1.00 26.92 ? 3    LYS G CG  1 
ATOM   6555  C  CD  . LYS G  1 3   ? 7.546   137.658 75.756  1.00 30.36 ? 3    LYS G CD  1 
ATOM   6556  C  CE  . LYS G  1 3   ? 7.360   138.273 77.152  1.00 32.62 ? 3    LYS G CE  1 
ATOM   6557  N  NZ  . LYS G  1 3   ? 8.648   138.804 77.718  1.00 34.50 ? 3    LYS G NZ  1 
ATOM   6558  N  N   . ALA G  1 4   ? 8.985   138.897 70.283  1.00 19.55 ? 4    ALA G N   1 
ATOM   6559  C  CA  . ALA G  1 4   ? 9.698   138.483 69.080  1.00 19.14 ? 4    ALA G CA  1 
ATOM   6560  C  C   . ALA G  1 4   ? 11.185  138.723 69.277  1.00 18.42 ? 4    ALA G C   1 
ATOM   6561  O  O   . ALA G  1 4   ? 11.604  139.413 70.208  1.00 18.65 ? 4    ALA G O   1 
ATOM   6562  C  CB  . ALA G  1 4   ? 9.203   139.244 67.869  1.00 18.54 ? 4    ALA G CB  1 
ATOM   6563  N  N   . VAL G  1 5   ? 11.992  138.192 68.364  1.00 17.46 ? 5    VAL G N   1 
ATOM   6564  C  CA  . VAL G  1 5   ? 13.421  138.331 68.483  1.00 16.80 ? 5    VAL G CA  1 
ATOM   6565  C  C   . VAL G  1 5   ? 14.002  138.240 67.084  1.00 17.14 ? 5    VAL G C   1 
ATOM   6566  O  O   . VAL G  1 5   ? 13.377  137.648 66.185  1.00 16.33 ? 5    VAL G O   1 
ATOM   6567  C  CB  . VAL G  1 5   ? 14.007  137.209 69.364  1.00 17.61 ? 5    VAL G CB  1 
ATOM   6568  C  CG1 . VAL G  1 5   ? 13.850  135.831 68.692  1.00 16.77 ? 5    VAL G CG1 1 
ATOM   6569  C  CG2 . VAL G  1 5   ? 15.509  137.485 69.691  1.00 18.54 ? 5    VAL G CG2 1 
ATOM   6570  N  N   . CYS G  1 6   ? 15.166  138.849 66.887  1.00 16.15 ? 6    CYS G N   1 
ATOM   6571  C  CA  . CYS G  1 6   ? 15.827  138.838 65.599  1.00 16.36 ? 6    CYS G CA  1 
ATOM   6572  C  C   . CYS G  1 6   ? 17.340  138.812 65.766  1.00 15.84 ? 6    CYS G C   1 
ATOM   6573  O  O   . CYS G  1 6   ? 17.902  139.611 66.496  1.00 15.03 ? 6    CYS G O   1 
ATOM   6574  C  CB  . CYS G  1 6   ? 15.417  140.051 64.763  1.00 16.20 ? 6    CYS G CB  1 
ATOM   6575  S  SG  . CYS G  1 6   ? 16.283  140.214 63.174  1.00 19.37 ? 6    CYS G SG  1 
ATOM   6576  N  N   . VAL G  1 7   ? 17.987  137.849 65.103  1.00 15.06 ? 7    VAL G N   1 
ATOM   6577  C  CA  . VAL G  1 7   ? 19.434  137.737 65.172  1.00 16.28 ? 7    VAL G CA  1 
ATOM   6578  C  C   . VAL G  1 7   ? 19.933  138.343 63.883  1.00 16.19 ? 7    VAL G C   1 
ATOM   6579  O  O   . VAL G  1 7   ? 19.644  137.837 62.778  1.00 14.23 ? 7    VAL G O   1 
ATOM   6580  C  CB  . VAL G  1 7   ? 19.899  136.256 65.248  1.00 16.34 ? 7    VAL G CB  1 
ATOM   6581  C  CG1 . VAL G  1 7   ? 21.442  136.145 65.175  1.00 16.85 ? 7    VAL G CG1 1 
ATOM   6582  C  CG2 . VAL G  1 7   ? 19.382  135.608 66.525  1.00 17.71 ? 7    VAL G CG2 1 
ATOM   6583  N  N   . LEU G  1 8   ? 20.684  139.424 64.011  1.00 15.18 ? 8    LEU G N   1 
ATOM   6584  C  CA  . LEU G  1 8   ? 21.233  140.116 62.866  1.00 16.85 ? 8    LEU G CA  1 
ATOM   6585  C  C   . LEU G  1 8   ? 22.613  139.592 62.570  1.00 17.13 ? 8    LEU G C   1 
ATOM   6586  O  O   . LEU G  1 8   ? 23.475  139.547 63.455  1.00 17.27 ? 8    LEU G O   1 
ATOM   6587  C  CB  . LEU G  1 8   ? 21.384  141.607 63.167  1.00 17.33 ? 8    LEU G CB  1 
ATOM   6588  C  CG  . LEU G  1 8   ? 20.148  142.489 63.353  1.00 20.58 ? 8    LEU G CG  1 
ATOM   6589  C  CD1 . LEU G  1 8   ? 19.287  142.539 62.116  1.00 21.69 ? 8    LEU G CD1 1 
ATOM   6590  C  CD2 . LEU G  1 8   ? 19.363  142.013 64.564  1.00 23.29 ? 8    LEU G CD2 1 
ATOM   6591  N  N   . LYS G  1 9   ? 22.824  139.173 61.326  1.00 18.08 ? 9    LYS G N   1 
ATOM   6592  C  CA  . LYS G  1 9   ? 24.139  138.720 60.885  1.00 19.19 ? 9    LYS G CA  1 
ATOM   6593  C  C   . LYS G  1 9   ? 24.431  139.272 59.476  1.00 18.44 ? 9    LYS G C   1 
ATOM   6594  O  O   . LYS G  1 9   ? 23.506  139.620 58.744  1.00 18.45 ? 9    LYS G O   1 
ATOM   6595  C  CB  . LYS G  1 9   ? 24.159  137.184 60.864  1.00 20.63 ? 9    LYS G CB  1 
ATOM   6596  C  CG  . LYS G  1 9   ? 23.960  136.523 62.236  1.00 25.42 ? 9    LYS G CG  1 
ATOM   6597  C  CD  . LYS G  1 9   ? 24.324  135.031 62.189  1.00 30.86 ? 9    LYS G CD  1 
ATOM   6598  C  CE  . LYS G  1 9   ? 24.094  134.297 63.535  1.00 33.23 ? 9    LYS G CE  1 
ATOM   6599  N  NZ  . LYS G  1 9   ? 24.437  135.090 64.763  1.00 37.85 ? 9    LYS G NZ  1 
ATOM   6600  N  N   . GLY G  1 10  ? 25.706  139.354 59.084  1.00 19.11 ? 10   GLY G N   1 
ATOM   6601  C  CA  . GLY G  1 10  ? 26.050  139.909 57.770  1.00 19.65 ? 10   GLY G CA  1 
ATOM   6602  C  C   . GLY G  1 10  ? 27.331  139.307 57.185  1.00 20.62 ? 10   GLY G C   1 
ATOM   6603  O  O   . GLY G  1 10  ? 27.783  138.272 57.656  1.00 19.08 ? 10   GLY G O   1 
ATOM   6604  N  N   . ASP G  1 11  ? 27.906  139.956 56.172  1.00 20.85 ? 11   ASP G N   1 
ATOM   6605  C  CA  . ASP G  1 11  ? 29.136  139.480 55.558  1.00 22.94 ? 11   ASP G CA  1 
ATOM   6606  C  C   . ASP G  1 11  ? 30.354  139.976 56.339  1.00 22.86 ? 11   ASP G C   1 
ATOM   6607  O  O   . ASP G  1 11  ? 31.459  139.435 56.187  1.00 23.13 ? 11   ASP G O   1 
ATOM   6608  C  CB  . ASP G  1 11  ? 29.246  139.989 54.102  1.00 23.97 ? 11   ASP G CB  1 
ATOM   6609  C  CG  . ASP G  1 11  ? 28.114  139.495 53.215  1.00 25.82 ? 11   ASP G CG  1 
ATOM   6610  O  OD1 . ASP G  1 11  ? 27.668  138.358 53.411  1.00 26.45 ? 11   ASP G OD1 1 
ATOM   6611  O  OD2 . ASP G  1 11  ? 27.597  140.183 52.302  1.00 32.72 ? 11   ASP G OD2 1 
ATOM   6612  N  N   . GLY G  1 12  ? 30.157  141.020 57.144  1.00 21.98 ? 12   GLY G N   1 
ATOM   6613  C  CA  . GLY G  1 12  ? 31.238  141.598 57.920  1.00 21.92 ? 12   GLY G CA  1 
ATOM   6614  C  C   . GLY G  1 12  ? 31.151  141.320 59.410  1.00 21.44 ? 12   GLY G C   1 
ATOM   6615  O  O   . GLY G  1 12  ? 30.569  140.312 59.848  1.00 21.56 ? 12   GLY G O   1 
ATOM   6616  N  N   . PRO G  1 13  ? 31.699  142.241 60.193  1.00 20.51 ? 13   PRO G N   1 
ATOM   6617  C  CA  . PRO G  1 13  ? 31.782  142.083 61.649  1.00 20.23 ? 13   PRO G CA  1 
ATOM   6618  C  C   . PRO G  1 13  ? 30.472  142.446 62.371  1.00 19.51 ? 13   PRO G C   1 
ATOM   6619  O  O   . PRO G  1 13  ? 30.382  142.274 63.596  1.00 17.70 ? 13   PRO G O   1 
ATOM   6620  C  CB  . PRO G  1 13  ? 32.820  143.125 62.060  1.00 20.65 ? 13   PRO G CB  1 
ATOM   6621  C  CG  . PRO G  1 13  ? 32.982  144.047 60.897  1.00 21.10 ? 13   PRO G CG  1 
ATOM   6622  C  CD  . PRO G  1 13  ? 32.227  143.524 59.720  1.00 20.50 ? 13   PRO G CD  1 
ATOM   6623  N  N   . VAL G  1 14  ? 29.505  142.996 61.650  1.00 18.06 ? 14   VAL G N   1 
ATOM   6624  C  CA  . VAL G  1 14  ? 28.296  143.449 62.304  1.00 18.85 ? 14   VAL G CA  1 
ATOM   6625  C  C   . VAL G  1 14  ? 27.367  142.299 62.689  1.00 19.84 ? 14   VAL G C   1 
ATOM   6626  O  O   . VAL G  1 14  ? 27.022  141.441 61.846  1.00 19.07 ? 14   VAL G O   1 
ATOM   6627  C  CB  . VAL G  1 14  ? 27.539  144.476 61.429  1.00 18.49 ? 14   VAL G CB  1 
ATOM   6628  C  CG1 . VAL G  1 14  ? 26.262  144.955 62.112  1.00 19.21 ? 14   VAL G CG1 1 
ATOM   6629  C  CG2 . VAL G  1 14  ? 28.450  145.677 61.104  1.00 18.41 ? 14   VAL G CG2 1 
ATOM   6630  N  N   . GLN G  1 15  ? 26.991  142.264 63.962  1.00 19.60 ? 15   GLN G N   1 
ATOM   6631  C  CA  . GLN G  1 15  ? 26.088  141.219 64.433  1.00 21.23 ? 15   GLN G CA  1 
ATOM   6632  C  C   . GLN G  1 15  ? 25.400  141.676 65.689  1.00 20.07 ? 15   GLN G C   1 
ATOM   6633  O  O   . GLN G  1 15  ? 25.912  142.538 66.407  1.00 19.85 ? 15   GLN G O   1 
ATOM   6634  C  CB  . GLN G  1 15  ? 26.821  139.897 64.683  1.00 21.87 ? 15   GLN G CB  1 
ATOM   6635  C  CG  . GLN G  1 15  ? 28.018  139.972 65.601  1.00 26.47 ? 15   GLN G CG  1 
ATOM   6636  C  CD  . GLN G  1 15  ? 28.856  138.698 65.530  1.00 32.33 ? 15   GLN G CD  1 
ATOM   6637  O  OE1 . GLN G  1 15  ? 29.995  138.660 66.024  1.00 37.56 ? 15   GLN G OE1 1 
ATOM   6638  N  NE2 . GLN G  1 15  ? 28.313  137.667 64.885  1.00 35.71 ? 15   GLN G NE2 1 
ATOM   6639  N  N   . GLY G  1 16  ? 24.232  141.112 65.956  1.00 19.41 ? 16   GLY G N   1 
ATOM   6640  C  CA  . GLY G  1 16  ? 23.536  141.472 67.164  1.00 19.25 ? 16   GLY G CA  1 
ATOM   6641  C  C   . GLY G  1 16  ? 22.237  140.738 67.360  1.00 19.44 ? 16   GLY G C   1 
ATOM   6642  O  O   . GLY G  1 16  ? 21.871  139.850 66.576  1.00 19.10 ? 16   GLY G O   1 
ATOM   6643  N  N   . ILE G  1 17  ? 21.582  141.069 68.466  1.00 18.87 ? 17   ILE G N   1 
ATOM   6644  C  CA  . ILE G  1 17  ? 20.291  140.490 68.805  1.00 17.96 ? 17   ILE G CA  1 
ATOM   6645  C  C   . ILE G  1 17  ? 19.376  141.636 69.170  1.00 18.74 ? 17   ILE G C   1 
ATOM   6646  O  O   . ILE G  1 17  ? 19.769  142.535 69.947  1.00 16.51 ? 17   ILE G O   1 
ATOM   6647  C  CB  . ILE G  1 17  ? 20.476  139.493 69.960  1.00 18.51 ? 17   ILE G CB  1 
ATOM   6648  C  CG1 . ILE G  1 17  ? 21.280  138.286 69.457  1.00 20.42 ? 17   ILE G CG1 1 
ATOM   6649  C  CG2 . ILE G  1 17  ? 19.135  139.033 70.548  1.00 18.48 ? 17   ILE G CG2 1 
ATOM   6650  C  CD1 . ILE G  1 17  ? 21.576  137.247 70.514  1.00 25.90 ? 17   ILE G CD1 1 
ATOM   6651  N  N   . ILE G  1 18  ? 18.178  141.637 68.582  1.00 17.39 ? 18   ILE G N   1 
ATOM   6652  C  CA  . ILE G  1 18  ? 17.179  142.664 68.856  1.00 17.75 ? 18   ILE G CA  1 
ATOM   6653  C  C   . ILE G  1 18  ? 15.912  141.996 69.347  1.00 17.61 ? 18   ILE G C   1 
ATOM   6654  O  O   . ILE G  1 18  ? 15.373  141.094 68.701  1.00 16.93 ? 18   ILE G O   1 
ATOM   6655  C  CB  . ILE G  1 18  ? 16.892  143.504 67.606  1.00 17.07 ? 18   ILE G CB  1 
ATOM   6656  C  CG1 . ILE G  1 18  ? 18.190  144.124 67.068  1.00 16.92 ? 18   ILE G CG1 1 
ATOM   6657  C  CG2 . ILE G  1 18  ? 15.842  144.585 67.917  1.00 16.49 ? 18   ILE G CG2 1 
ATOM   6658  C  CD1 . ILE G  1 18  ? 18.794  145.223 67.987  1.00 21.85 ? 18   ILE G CD1 1 
ATOM   6659  N  N   . ASN G  1 19  ? 15.428  142.426 70.499  1.00 18.09 ? 19   ASN G N   1 
ATOM   6660  C  CA  . ASN G  1 19  ? 14.204  141.872 71.052  1.00 19.34 ? 19   ASN G CA  1 
ATOM   6661  C  C   . ASN G  1 19  ? 13.038  142.835 70.870  1.00 20.29 ? 19   ASN G C   1 
ATOM   6662  O  O   . ASN G  1 19  ? 13.225  144.051 70.814  1.00 20.07 ? 19   ASN G O   1 
ATOM   6663  C  CB  . ASN G  1 19  ? 14.390  141.634 72.539  1.00 20.00 ? 19   ASN G CB  1 
ATOM   6664  C  CG  . ASN G  1 19  ? 15.636  140.872 72.843  1.00 20.27 ? 19   ASN G CG  1 
ATOM   6665  O  OD1 . ASN G  1 19  ? 16.713  141.460 73.094  1.00 26.29 ? 19   ASN G OD1 1 
ATOM   6666  N  ND2 . ASN G  1 19  ? 15.516  139.558 72.859  1.00 18.02 ? 19   ASN G ND2 1 
ATOM   6667  N  N   . PHE G  1 20  ? 11.834  142.279 70.802  1.00 21.29 ? 20   PHE G N   1 
ATOM   6668  C  CA  . PHE G  1 20  ? 10.611  143.043 70.573  1.00 21.64 ? 20   PHE G CA  1 
ATOM   6669  C  C   . PHE G  1 20  ? 9.569   142.591 71.563  1.00 22.63 ? 20   PHE G C   1 
ATOM   6670  O  O   . PHE G  1 20  ? 9.449   141.401 71.851  1.00 22.13 ? 20   PHE G O   1 
ATOM   6671  C  CB  . PHE G  1 20  ? 10.014  142.721 69.192  1.00 21.93 ? 20   PHE G CB  1 
ATOM   6672  C  CG  . PHE G  1 20  ? 10.849  143.168 68.016  1.00 20.72 ? 20   PHE G CG  1 
ATOM   6673  C  CD1 . PHE G  1 20  ? 11.863  142.360 67.511  1.00 17.76 ? 20   PHE G CD1 1 
ATOM   6674  C  CD2 . PHE G  1 20  ? 10.557  144.371 67.374  1.00 20.28 ? 20   PHE G CD2 1 
ATOM   6675  C  CE1 . PHE G  1 20  ? 12.617  142.770 66.411  1.00 17.99 ? 20   PHE G CE1 1 
ATOM   6676  C  CE2 . PHE G  1 20  ? 11.288  144.785 66.285  1.00 20.05 ? 20   PHE G CE2 1 
ATOM   6677  C  CZ  . PHE G  1 20  ? 12.331  143.987 65.802  1.00 17.76 ? 20   PHE G CZ  1 
ATOM   6678  N  N   . GLU G  1 21  ? 8.762   143.536 72.042  1.00 23.99 ? 21   GLU G N   1 
ATOM   6679  C  CA  . GLU G  1 21  ? 7.670   143.191 72.924  1.00 26.29 ? 21   GLU G CA  1 
ATOM   6680  C  C   . GLU G  1 21  ? 6.530   144.223 72.818  1.00 26.64 ? 21   GLU G C   1 
ATOM   6681  O  O   . GLU G  1 21  ? 6.767   145.435 72.856  1.00 26.43 ? 21   GLU G O   1 
ATOM   6682  C  CB  . GLU G  1 21  ? 8.162   143.045 74.370  1.00 26.97 ? 21   GLU G CB  1 
ATOM   6683  C  CG  . GLU G  1 21  ? 7.051   142.697 75.354  1.00 30.33 ? 21   GLU G CG  1 
ATOM   6684  C  CD  . GLU G  1 21  ? 7.455   142.871 76.812  1.00 35.73 ? 21   GLU G CD  1 
ATOM   6685  O  OE1 . GLU G  1 21  ? 7.979   143.958 77.180  1.00 38.03 ? 21   GLU G OE1 1 
ATOM   6686  O  OE2 . GLU G  1 21  ? 7.214   141.928 77.605  1.00 38.14 ? 21   GLU G OE2 1 
ATOM   6687  N  N   . GLN G  1 22  ? 5.307   143.719 72.661  1.00 28.00 ? 22   GLN G N   1 
ATOM   6688  C  CA  . GLN G  1 22  ? 4.106   144.548 72.533  1.00 29.33 ? 22   GLN G CA  1 
ATOM   6689  C  C   . GLN G  1 22  ? 3.034   144.025 73.481  1.00 30.34 ? 22   GLN G C   1 
ATOM   6690  O  O   . GLN G  1 22  ? 2.673   142.855 73.429  1.00 30.21 ? 22   GLN G O   1 
ATOM   6691  C  CB  . GLN G  1 22  ? 3.593   144.502 71.098  1.00 29.44 ? 22   GLN G CB  1 
ATOM   6692  C  CG  . GLN G  1 22  ? 2.335   145.311 70.841  1.00 28.67 ? 22   GLN G CG  1 
ATOM   6693  C  CD  . GLN G  1 22  ? 1.903   145.198 69.403  1.00 28.36 ? 22   GLN G CD  1 
ATOM   6694  O  OE1 . GLN G  1 22  ? 1.969   144.122 68.820  1.00 28.97 ? 22   GLN G OE1 1 
ATOM   6695  N  NE2 . GLN G  1 22  ? 1.495   146.310 68.816  1.00 28.99 ? 22   GLN G NE2 1 
ATOM   6696  N  N   . LYS G  1 23  ? 2.535   144.895 74.351  1.00 31.74 ? 23   LYS G N   1 
ATOM   6697  C  CA  . LYS G  1 23  ? 1.540   144.510 75.361  1.00 33.30 ? 23   LYS G CA  1 
ATOM   6698  C  C   . LYS G  1 23  ? 0.105   144.444 74.847  1.00 33.92 ? 23   LYS G C   1 
ATOM   6699  O  O   . LYS G  1 23  ? -0.650  143.544 75.214  1.00 33.67 ? 23   LYS G O   1 
ATOM   6700  C  CB  . LYS G  1 23  ? 1.598   145.457 76.559  1.00 33.27 ? 23   LYS G CB  1 
ATOM   6701  C  CG  . LYS G  1 23  ? 2.749   145.207 77.539  1.00 34.84 ? 23   LYS G CG  1 
ATOM   6702  C  CD  . LYS G  1 23  ? 2.990   146.455 78.408  1.00 38.10 ? 23   LYS G CD  1 
ATOM   6703  C  CE  . LYS G  1 23  ? 3.863   146.174 79.637  1.00 39.53 ? 23   LYS G CE  1 
ATOM   6704  N  NZ  . LYS G  1 23  ? 5.235   145.689 79.293  1.00 40.22 ? 23   LYS G NZ  1 
ATOM   6705  N  N   . GLU G  1 24  ? -0.264  145.387 73.990  1.00 35.14 ? 24   GLU G N   1 
ATOM   6706  C  CA  . GLU G  1 24  ? -1.639  145.461 73.516  1.00 36.93 ? 24   GLU G CA  1 
ATOM   6707  C  C   . GLU G  1 24  ? -1.735  145.486 71.994  1.00 37.34 ? 24   GLU G C   1 
ATOM   6708  O  O   . GLU G  1 24  ? -0.861  146.031 71.316  1.00 37.51 ? 24   GLU G O   1 
ATOM   6709  C  CB  . GLU G  1 24  ? -2.335  146.704 74.099  1.00 37.02 ? 24   GLU G CB  1 
ATOM   6710  C  CG  . GLU G  1 24  ? -2.576  146.676 75.607  1.00 39.49 ? 24   GLU G CG  1 
ATOM   6711  C  CD  . GLU G  1 24  ? -3.326  147.910 76.122  1.00 42.55 ? 24   GLU G CD  1 
ATOM   6712  O  OE1 . GLU G  1 24  ? -3.837  148.694 75.292  1.00 44.23 ? 24   GLU G OE1 1 
ATOM   6713  O  OE2 . GLU G  1 24  ? -3.414  148.111 77.361  1.00 43.54 ? 24   GLU G OE2 1 
ATOM   6714  N  N   . SER G  1 25  ? -2.797  144.877 71.474  1.00 37.95 ? 25   SER G N   1 
ATOM   6715  C  CA  . SER G  1 25  ? -3.126  144.910 70.054  1.00 38.20 ? 25   SER G CA  1 
ATOM   6716  C  C   . SER G  1 25  ? -3.086  146.375 69.578  1.00 38.23 ? 25   SER G C   1 
ATOM   6717  O  O   . SER G  1 25  ? -3.699  147.249 70.204  1.00 38.13 ? 25   SER G O   1 
ATOM   6718  C  CB  . SER G  1 25  ? -4.532  144.333 69.863  1.00 38.19 ? 25   SER G CB  1 
ATOM   6719  O  OG  . SER G  1 25  ? -4.670  143.713 68.601  1.00 38.86 ? 25   SER G OG  1 
ATOM   6720  N  N   . ASN G  1 26  ? -2.357  146.638 68.488  1.00 38.06 ? 26   ASN G N   1 
ATOM   6721  C  CA  . ASN G  1 26  ? -2.149  148.009 67.978  1.00 37.79 ? 26   ASN G CA  1 
ATOM   6722  C  C   . ASN G  1 26  ? -1.378  148.939 68.921  1.00 36.52 ? 26   ASN G C   1 
ATOM   6723  O  O   . ASN G  1 26  ? -1.168  150.116 68.610  1.00 37.00 ? 26   ASN G O   1 
ATOM   6724  C  CB  . ASN G  1 26  ? -3.476  148.684 67.585  1.00 38.66 ? 26   ASN G CB  1 
ATOM   6725  C  CG  . ASN G  1 26  ? -3.533  149.053 66.107  1.00 40.83 ? 26   ASN G CG  1 
ATOM   6726  O  OD1 . ASN G  1 26  ? -4.453  148.650 65.384  1.00 42.85 ? 26   ASN G OD1 1 
ATOM   6727  N  ND2 . ASN G  1 26  ? -2.551  149.834 65.655  1.00 43.63 ? 26   ASN G ND2 1 
ATOM   6728  N  N   . GLY G  1 27  ? -0.969  148.421 70.076  1.00 34.74 ? 27   GLY G N   1 
ATOM   6729  C  CA  . GLY G  1 27  ? -0.286  149.228 71.076  1.00 32.04 ? 27   GLY G CA  1 
ATOM   6730  C  C   . GLY G  1 27  ? 1.217   149.285 70.862  1.00 30.04 ? 27   GLY G C   1 
ATOM   6731  O  O   . GLY G  1 27  ? 1.733   148.707 69.916  1.00 29.39 ? 27   GLY G O   1 
ATOM   6732  N  N   . PRO G  1 28  ? 1.904   150.019 71.731  1.00 28.31 ? 28   PRO G N   1 
ATOM   6733  C  CA  . PRO G  1 28  ? 3.359   150.219 71.657  1.00 26.83 ? 28   PRO G CA  1 
ATOM   6734  C  C   . PRO G  1 28  ? 4.246   148.972 71.591  1.00 25.50 ? 28   PRO G C   1 
ATOM   6735  O  O   . PRO G  1 28  ? 4.070   148.023 72.356  1.00 24.44 ? 28   PRO G O   1 
ATOM   6736  C  CB  . PRO G  1 28  ? 3.672   150.957 72.959  1.00 27.38 ? 28   PRO G CB  1 
ATOM   6737  C  CG  . PRO G  1 28  ? 2.415   151.652 73.306  1.00 27.78 ? 28   PRO G CG  1 
ATOM   6738  C  CD  . PRO G  1 28  ? 1.291   150.782 72.835  1.00 28.37 ? 28   PRO G CD  1 
ATOM   6739  N  N   . VAL G  1 29  ? 5.232   149.022 70.704  1.00 23.86 ? 29   VAL G N   1 
ATOM   6740  C  CA  . VAL G  1 29  ? 6.213   147.945 70.579  1.00 23.19 ? 29   VAL G CA  1 
ATOM   6741  C  C   . VAL G  1 29  ? 7.547   148.439 71.121  1.00 22.50 ? 29   VAL G C   1 
ATOM   6742  O  O   . VAL G  1 29  ? 8.118   149.406 70.610  1.00 22.16 ? 29   VAL G O   1 
ATOM   6743  C  CB  . VAL G  1 29  ? 6.400   147.521 69.108  1.00 23.32 ? 29   VAL G CB  1 
ATOM   6744  C  CG1 . VAL G  1 29  ? 7.576   146.542 68.952  1.00 23.37 ? 29   VAL G CG1 1 
ATOM   6745  C  CG2 . VAL G  1 29  ? 5.126   146.904 68.578  1.00 23.31 ? 29   VAL G CG2 1 
ATOM   6746  N  N   . LYS G  1 30  ? 8.038   147.814 72.179  1.00 21.69 ? 30   LYS G N   1 
ATOM   6747  C  CA  . LYS G  1 30  ? 9.361   148.174 72.656  1.00 21.93 ? 30   LYS G CA  1 
ATOM   6748  C  C   . LYS G  1 30  ? 10.365  147.370 71.831  1.00 21.69 ? 30   LYS G C   1 
ATOM   6749  O  O   . LYS G  1 30  ? 10.175  146.182 71.624  1.00 20.85 ? 30   LYS G O   1 
ATOM   6750  C  CB  . LYS G  1 30  ? 9.544   147.806 74.129  1.00 22.02 ? 30   LYS G CB  1 
ATOM   6751  C  CG  . LYS G  1 30  ? 8.579   148.488 75.098  1.00 25.53 ? 30   LYS G CG  1 
ATOM   6752  C  CD  . LYS G  1 30  ? 9.021   148.301 76.556  1.00 29.33 ? 30   LYS G CD  1 
ATOM   6753  C  CE  . LYS G  1 30  ? 7.875   148.588 77.537  1.00 31.27 ? 30   LYS G CE  1 
ATOM   6754  N  NZ  . LYS G  1 30  ? 8.289   148.518 78.969  1.00 31.91 ? 30   LYS G NZ  1 
ATOM   6755  N  N   . VAL G  1 31  ? 11.414  148.013 71.342  1.00 21.53 ? 31   VAL G N   1 
ATOM   6756  C  CA  . VAL G  1 31  ? 12.437  147.248 70.629  1.00 20.84 ? 31   VAL G CA  1 
ATOM   6757  C  C   . VAL G  1 31  ? 13.807  147.493 71.227  1.00 20.66 ? 31   VAL G C   1 
ATOM   6758  O  O   . VAL G  1 31  ? 14.257  148.634 71.348  1.00 21.79 ? 31   VAL G O   1 
ATOM   6759  C  CB  . VAL G  1 31  ? 12.356  147.326 69.063  1.00 22.01 ? 31   VAL G CB  1 
ATOM   6760  C  CG1 . VAL G  1 31  ? 11.446  148.400 68.511  1.00 21.84 ? 31   VAL G CG1 1 
ATOM   6761  C  CG2 . VAL G  1 31  ? 13.764  147.201 68.368  1.00 21.56 ? 31   VAL G CG2 1 
ATOM   6762  N  N   . TRP G  1 32  ? 14.459  146.425 71.665  1.00 20.26 ? 32   TRP G N   1 
ATOM   6763  C  CA  . TRP G  1 32  ? 15.716  146.604 72.368  1.00 19.11 ? 32   TRP G CA  1 
ATOM   6764  C  C   . TRP G  1 32  ? 16.719  145.474 72.229  1.00 19.17 ? 32   TRP G C   1 
ATOM   6765  O  O   . TRP G  1 32  ? 16.348  144.301 72.053  1.00 17.84 ? 32   TRP G O   1 
ATOM   6766  C  CB  . TRP G  1 32  ? 15.436  146.822 73.847  1.00 19.65 ? 32   TRP G CB  1 
ATOM   6767  C  CG  . TRP G  1 32  ? 15.419  145.558 74.626  1.00 20.48 ? 32   TRP G CG  1 
ATOM   6768  C  CD1 . TRP G  1 32  ? 16.480  144.957 75.253  1.00 23.36 ? 32   TRP G CD1 1 
ATOM   6769  C  CD2 . TRP G  1 32  ? 14.297  144.711 74.848  1.00 20.75 ? 32   TRP G CD2 1 
ATOM   6770  N  NE1 . TRP G  1 32  ? 16.076  143.791 75.857  1.00 21.46 ? 32   TRP G NE1 1 
ATOM   6771  C  CE2 . TRP G  1 32  ? 14.736  143.628 75.635  1.00 21.96 ? 32   TRP G CE2 1 
ATOM   6772  C  CE3 . TRP G  1 32  ? 12.950  144.773 74.488  1.00 22.08 ? 32   TRP G CE3 1 
ATOM   6773  C  CZ2 . TRP G  1 32  ? 13.890  142.623 76.054  1.00 22.41 ? 32   TRP G CZ2 1 
ATOM   6774  C  CZ3 . TRP G  1 32  ? 12.108  143.776 74.908  1.00 24.08 ? 32   TRP G CZ3 1 
ATOM   6775  C  CH2 . TRP G  1 32  ? 12.581  142.708 75.682  1.00 25.56 ? 32   TRP G CH2 1 
ATOM   6776  N  N   . GLY G  1 33  ? 17.988  145.858 72.331  1.00 18.60 ? 33   GLY G N   1 
ATOM   6777  C  CA  . GLY G  1 33  ? 19.103  144.939 72.285  1.00 19.39 ? 33   GLY G CA  1 
ATOM   6778  C  C   . GLY G  1 33  ? 20.410  145.666 71.990  1.00 19.84 ? 33   GLY G C   1 
ATOM   6779  O  O   . GLY G  1 33  ? 20.560  146.865 72.294  1.00 19.09 ? 33   GLY G O   1 
ATOM   6780  N  N   . SER G  1 34  ? 21.367  144.933 71.420  1.00 20.53 ? 34   SER G N   1 
ATOM   6781  C  CA  . SER G  1 34  ? 22.640  145.530 71.000  1.00 20.11 ? 34   SER G CA  1 
ATOM   6782  C  C   . SER G  1 34  ? 23.212  144.908 69.730  1.00 19.57 ? 34   SER G C   1 
ATOM   6783  O  O   . SER G  1 34  ? 22.965  143.731 69.401  1.00 19.23 ? 34   SER G O   1 
ATOM   6784  C  CB  . SER G  1 34  ? 23.685  145.523 72.112  1.00 21.41 ? 34   SER G CB  1 
ATOM   6785  O  OG  . SER G  1 34  ? 24.098  144.207 72.350  1.00 24.75 ? 34   SER G OG  1 
ATOM   6786  N  N   . ILE G  1 35  ? 23.923  145.753 68.997  1.00 18.59 ? 35   ILE G N   1 
ATOM   6787  C  CA  . ILE G  1 35  ? 24.596  145.407 67.757  1.00 17.71 ? 35   ILE G CA  1 
ATOM   6788  C  C   . ILE G  1 35  ? 26.045  145.812 67.924  1.00 17.58 ? 35   ILE G C   1 
ATOM   6789  O  O   . ILE G  1 35  ? 26.343  146.919 68.403  1.00 16.98 ? 35   ILE G O   1 
ATOM   6790  C  CB  . ILE G  1 35  ? 23.977  146.194 66.581  1.00 17.37 ? 35   ILE G CB  1 
ATOM   6791  C  CG1 . ILE G  1 35  ? 22.473  145.957 66.509  1.00 19.21 ? 35   ILE G CG1 1 
ATOM   6792  C  CG2 . ILE G  1 35  ? 24.608  145.773 65.243  1.00 15.84 ? 35   ILE G CG2 1 
ATOM   6793  C  CD1 . ILE G  1 35  ? 21.759  146.860 65.442  1.00 20.46 ? 35   ILE G CD1 1 
ATOM   6794  N  N   . LYS G  1 36  ? 26.967  144.914 67.578  1.00 16.48 ? 36   LYS G N   1 
ATOM   6795  C  CA  . LYS G  1 36  ? 28.386  145.257 67.660  1.00 17.02 ? 36   LYS G CA  1 
ATOM   6796  C  C   . LYS G  1 36  ? 28.983  145.259 66.263  1.00 16.77 ? 36   LYS G C   1 
ATOM   6797  O  O   . LYS G  1 36  ? 28.305  144.856 65.300  1.00 15.81 ? 36   LYS G O   1 
ATOM   6798  C  CB  . LYS G  1 36  ? 29.134  144.268 68.559  1.00 17.61 ? 36   LYS G CB  1 
ATOM   6799  C  CG  . LYS G  1 36  ? 29.131  142.807 68.090  1.00 21.24 ? 36   LYS G CG  1 
ATOM   6800  C  CD  . LYS G  1 36  ? 29.474  141.911 69.287  1.00 29.40 ? 36   LYS G CD  1 
ATOM   6801  C  CE  . LYS G  1 36  ? 30.325  140.717 68.889  1.00 32.40 ? 36   LYS G CE  1 
ATOM   6802  N  NZ  . LYS G  1 36  ? 30.930  140.058 70.095  1.00 35.94 ? 36   LYS G NZ  1 
ATOM   6803  N  N   . GLY G  1 37  ? 30.249  145.679 66.163  1.00 15.89 ? 37   GLY G N   1 
ATOM   6804  C  CA  . GLY G  1 37  ? 30.986  145.711 64.908  1.00 15.75 ? 37   GLY G CA  1 
ATOM   6805  C  C   . GLY G  1 37  ? 30.756  146.897 63.979  1.00 15.36 ? 37   GLY G C   1 
ATOM   6806  O  O   . GLY G  1 37  ? 31.161  146.890 62.813  1.00 15.37 ? 37   GLY G O   1 
ATOM   6807  N  N   . LEU G  1 38  ? 30.137  147.936 64.514  1.00 15.26 ? 38   LEU G N   1 
ATOM   6808  C  CA  . LEU G  1 38  ? 29.763  149.110 63.734  1.00 14.88 ? 38   LEU G CA  1 
ATOM   6809  C  C   . LEU G  1 38  ? 30.732  150.279 63.840  1.00 15.13 ? 38   LEU G C   1 
ATOM   6810  O  O   . LEU G  1 38  ? 31.410  150.463 64.884  1.00 15.40 ? 38   LEU G O   1 
ATOM   6811  C  CB  . LEU G  1 38  ? 28.417  149.618 64.254  1.00 14.47 ? 38   LEU G CB  1 
ATOM   6812  C  CG  . LEU G  1 38  ? 27.178  148.758 63.979  1.00 16.25 ? 38   LEU G CG  1 
ATOM   6813  C  CD1 . LEU G  1 38  ? 26.010  149.129 64.927  1.00 13.86 ? 38   LEU G CD1 1 
ATOM   6814  C  CD2 . LEU G  1 38  ? 26.795  148.860 62.503  1.00 13.92 ? 38   LEU G CD2 1 
ATOM   6815  N  N   . THR G  1 39  ? 30.798  151.087 62.783  1.00 14.59 ? 39   THR G N   1 
ATOM   6816  C  CA  . THR G  1 39  ? 31.528  152.354 62.897  1.00 15.92 ? 39   THR G CA  1 
ATOM   6817  C  C   . THR G  1 39  ? 30.776  153.259 63.884  1.00 16.27 ? 39   THR G C   1 
ATOM   6818  O  O   . THR G  1 39  ? 29.554  153.223 63.985  1.00 16.55 ? 39   THR G O   1 
ATOM   6819  C  CB  . THR G  1 39  ? 31.664  153.079 61.558  1.00 15.93 ? 39   THR G CB  1 
ATOM   6820  O  OG1 . THR G  1 39  ? 30.407  153.084 60.874  1.00 17.26 ? 39   THR G OG1 1 
ATOM   6821  C  CG2 . THR G  1 39  ? 32.615  152.329 60.607  1.00 16.54 ? 39   THR G CG2 1 
ATOM   6822  N  N   . GLU G  1 40  ? 31.518  154.096 64.587  1.00 17.20 ? 40   GLU G N   1 
ATOM   6823  C  CA  . GLU G  1 40  ? 30.930  154.916 65.618  1.00 18.18 ? 40   GLU G CA  1 
ATOM   6824  C  C   . GLU G  1 40  ? 29.920  155.835 64.955  1.00 18.52 ? 40   GLU G C   1 
ATOM   6825  O  O   . GLU G  1 40  ? 30.129  156.278 63.825  1.00 18.89 ? 40   GLU G O   1 
ATOM   6826  C  CB  . GLU G  1 40  ? 32.033  155.713 66.338  1.00 19.04 ? 40   GLU G CB  1 
ATOM   6827  C  CG  . GLU G  1 40  ? 31.529  156.614 67.448  1.00 22.14 ? 40   GLU G CG  1 
ATOM   6828  C  CD  . GLU G  1 40  ? 32.646  157.224 68.272  1.00 26.67 ? 40   GLU G CD  1 
ATOM   6829  O  OE1 . GLU G  1 40  ? 33.841  157.038 67.922  1.00 27.40 ? 40   GLU G OE1 1 
ATOM   6830  O  OE2 . GLU G  1 40  ? 32.318  157.900 69.279  1.00 28.68 ? 40   GLU G OE2 1 
ATOM   6831  N  N   . GLY G  1 41  ? 28.802  156.080 65.626  1.00 17.91 ? 41   GLY G N   1 
ATOM   6832  C  CA  . GLY G  1 41  ? 27.810  156.965 65.070  1.00 16.69 ? 41   GLY G CA  1 
ATOM   6833  C  C   . GLY G  1 41  ? 26.491  156.347 64.684  1.00 16.94 ? 41   GLY G C   1 
ATOM   6834  O  O   . GLY G  1 41  ? 26.109  155.242 65.145  1.00 15.63 ? 41   GLY G O   1 
ATOM   6835  N  N   . LEU G  1 42  ? 25.796  157.082 63.813  1.00 16.50 ? 42   LEU G N   1 
ATOM   6836  C  CA  . LEU G  1 42  ? 24.444  156.726 63.357  1.00 16.84 ? 42   LEU G CA  1 
ATOM   6837  C  C   . LEU G  1 42  ? 24.381  155.700 62.231  1.00 16.56 ? 42   LEU G C   1 
ATOM   6838  O  O   . LEU G  1 42  ? 25.100  155.790 61.239  1.00 16.52 ? 42   LEU G O   1 
ATOM   6839  C  CB  . LEU G  1 42  ? 23.680  157.973 62.895  1.00 17.40 ? 42   LEU G CB  1 
ATOM   6840  C  CG  . LEU G  1 42  ? 22.762  158.726 63.884  1.00 18.58 ? 42   LEU G CG  1 
ATOM   6841  C  CD1 . LEU G  1 42  ? 23.143  158.567 65.350  1.00 20.09 ? 42   LEU G CD1 1 
ATOM   6842  C  CD2 . LEU G  1 42  ? 22.590  160.182 63.472  1.00 19.64 ? 42   LEU G CD2 1 
ATOM   6843  N  N   . HIS G  1 43  ? 23.492  154.737 62.398  1.00 16.03 ? 43   HIS G N   1 
ATOM   6844  C  CA  . HIS G  1 43  ? 23.296  153.706 61.397  1.00 16.46 ? 43   HIS G CA  1 
ATOM   6845  C  C   . HIS G  1 43  ? 21.783  153.494 61.208  1.00 16.39 ? 43   HIS G C   1 
ATOM   6846  O  O   . HIS G  1 43  ? 21.062  153.331 62.176  1.00 15.89 ? 43   HIS G O   1 
ATOM   6847  C  CB  . HIS G  1 43  ? 23.972  152.405 61.856  1.00 17.08 ? 43   HIS G CB  1 
ATOM   6848  C  CG  . HIS G  1 43  ? 25.466  152.475 61.849  1.00 16.93 ? 43   HIS G CG  1 
ATOM   6849  N  ND1 . HIS G  1 43  ? 26.222  152.079 60.766  1.00 19.79 ? 43   HIS G ND1 1 
ATOM   6850  C  CD2 . HIS G  1 43  ? 26.341  152.917 62.778  1.00 16.72 ? 43   HIS G CD2 1 
ATOM   6851  C  CE1 . HIS G  1 43  ? 27.501  152.256 61.039  1.00 18.07 ? 43   HIS G CE1 1 
ATOM   6852  N  NE2 . HIS G  1 43  ? 27.598  152.778 62.249  1.00 19.96 ? 43   HIS G NE2 1 
ATOM   6853  N  N   . GLY G  1 44  ? 21.312  153.513 59.965  1.00 16.53 ? 44   GLY G N   1 
ATOM   6854  C  CA  . GLY G  1 44  ? 19.902  153.291 59.680  1.00 17.45 ? 44   GLY G CA  1 
ATOM   6855  C  C   . GLY G  1 44  ? 19.400  151.929 60.163  1.00 18.17 ? 44   GLY G C   1 
ATOM   6856  O  O   . GLY G  1 44  ? 20.134  150.947 60.114  1.00 16.81 ? 44   GLY G O   1 
ATOM   6857  N  N   . PHE G  1 45  ? 18.141  151.882 60.605  1.00 18.05 ? 45   PHE G N   1 
ATOM   6858  C  CA  . PHE G  1 45  ? 17.593  150.702 61.279  1.00 18.52 ? 45   PHE G CA  1 
ATOM   6859  C  C   . PHE G  1 45  ? 16.138  150.555 60.831  1.00 18.12 ? 45   PHE G C   1 
ATOM   6860  O  O   . PHE G  1 45  ? 15.251  151.313 61.275  1.00 17.88 ? 45   PHE G O   1 
ATOM   6861  C  CB  . PHE G  1 45  ? 17.726  150.953 62.803  1.00 18.92 ? 45   PHE G CB  1 
ATOM   6862  C  CG  . PHE G  1 45  ? 17.447  149.759 63.670  1.00 19.07 ? 45   PHE G CG  1 
ATOM   6863  C  CD1 . PHE G  1 45  ? 18.221  148.618 63.592  1.00 18.98 ? 45   PHE G CD1 1 
ATOM   6864  C  CD2 . PHE G  1 45  ? 16.441  149.822 64.627  1.00 18.24 ? 45   PHE G CD2 1 
ATOM   6865  C  CE1 . PHE G  1 45  ? 17.971  147.537 64.428  1.00 19.46 ? 45   PHE G CE1 1 
ATOM   6866  C  CE2 . PHE G  1 45  ? 16.186  148.752 65.455  1.00 18.51 ? 45   PHE G CE2 1 
ATOM   6867  C  CZ  . PHE G  1 45  ? 16.944  147.602 65.354  1.00 16.11 ? 45   PHE G CZ  1 
ATOM   6868  N  N   . HIS G  1 46  ? 15.888  149.574 59.958  1.00 18.14 ? 46   HIS G N   1 
ATOM   6869  C  CA  . HIS G  1 46  ? 14.575  149.418 59.342  1.00 18.42 ? 46   HIS G CA  1 
ATOM   6870  C  C   . HIS G  1 46  ? 14.036  148.008 59.296  1.00 18.23 ? 46   HIS G C   1 
ATOM   6871  O  O   . HIS G  1 46  ? 14.801  147.033 59.283  1.00 18.31 ? 46   HIS G O   1 
ATOM   6872  C  CB  . HIS G  1 46  ? 14.633  149.836 57.882  1.00 18.51 ? 46   HIS G CB  1 
ATOM   6873  C  CG  . HIS G  1 46  ? 15.373  151.105 57.636  1.00 18.52 ? 46   HIS G CG  1 
ATOM   6874  N  ND1 . HIS G  1 46  ? 16.308  151.231 56.633  1.00 17.35 ? 46   HIS G ND1 1 
ATOM   6875  C  CD2 . HIS G  1 46  ? 15.283  152.316 58.226  1.00 17.64 ? 46   HIS G CD2 1 
ATOM   6876  C  CE1 . HIS G  1 46  ? 16.775  152.463 56.625  1.00 19.26 ? 46   HIS G CE1 1 
ATOM   6877  N  NE2 . HIS G  1 46  ? 16.179  153.138 57.590  1.00 20.24 ? 46   HIS G NE2 1 
ATOM   6878  N  N   . VAL G  1 47  ? 12.708  147.923 59.211  1.00 18.11 ? 47   VAL G N   1 
ATOM   6879  C  CA  . VAL G  1 47  ? 12.069  146.660 58.925  1.00 17.23 ? 47   VAL G CA  1 
ATOM   6880  C  C   . VAL G  1 47  ? 11.753  146.646 57.440  1.00 17.65 ? 47   VAL G C   1 
ATOM   6881  O  O   . VAL G  1 47  ? 11.019  147.506 56.939  1.00 17.07 ? 47   VAL G O   1 
ATOM   6882  C  CB  . VAL G  1 47  ? 10.746  146.452 59.675  1.00 17.43 ? 47   VAL G CB  1 
ATOM   6883  C  CG1 . VAL G  1 47  ? 10.115  145.134 59.237  1.00 17.66 ? 47   VAL G CG1 1 
ATOM   6884  C  CG2 . VAL G  1 47  ? 10.988  146.456 61.161  1.00 18.11 ? 47   VAL G CG2 1 
ATOM   6885  N  N   . HIS G  1 48  ? 12.314  145.661 56.740  1.00 16.73 ? 48   HIS G N   1 
ATOM   6886  C  CA  . HIS G  1 48  ? 12.075  145.503 55.312  1.00 16.96 ? 48   HIS G CA  1 
ATOM   6887  C  C   . HIS G  1 48  ? 10.953  144.477 55.072  1.00 16.88 ? 48   HIS G C   1 
ATOM   6888  O  O   . HIS G  1 48  ? 10.631  143.673 55.939  1.00 16.52 ? 48   HIS G O   1 
ATOM   6889  C  CB  . HIS G  1 48  ? 13.369  145.108 54.598  1.00 17.22 ? 48   HIS G CB  1 
ATOM   6890  C  CG  . HIS G  1 48  ? 14.347  146.227 54.504  1.00 16.30 ? 48   HIS G CG  1 
ATOM   6891  N  ND1 . HIS G  1 48  ? 14.779  146.739 53.302  1.00 17.11 ? 48   HIS G ND1 1 
ATOM   6892  C  CD2 . HIS G  1 48  ? 14.960  146.955 55.470  1.00 15.91 ? 48   HIS G CD2 1 
ATOM   6893  C  CE1 . HIS G  1 48  ? 15.632  147.727 53.532  1.00 17.39 ? 48   HIS G CE1 1 
ATOM   6894  N  NE2 . HIS G  1 48  ? 15.757  147.874 54.836  1.00 10.93 ? 48   HIS G NE2 1 
ATOM   6895  N  N   . GLU G  1 49  ? 10.363  144.526 53.889  1.00 16.95 ? 49   GLU G N   1 
ATOM   6896  C  CA  . GLU G  1 49  ? 9.121   143.804 53.619  1.00 17.23 ? 49   GLU G CA  1 
ATOM   6897  C  C   . GLU G  1 49  ? 9.176   142.280 53.745  1.00 17.01 ? 49   GLU G C   1 
ATOM   6898  O  O   . GLU G  1 49  ? 8.329   141.699 54.417  1.00 16.71 ? 49   GLU G O   1 
ATOM   6899  C  CB  . GLU G  1 49  ? 8.580   144.182 52.233  1.00 17.01 ? 49   GLU G CB  1 
ATOM   6900  C  CG  . GLU G  1 49  ? 7.162   143.689 51.957  1.00 18.61 ? 49   GLU G CG  1 
ATOM   6901  C  CD  . GLU G  1 49  ? 6.656   144.062 50.571  1.00 21.77 ? 49   GLU G CD  1 
ATOM   6902  O  OE1 . GLU G  1 49  ? 7.258   144.948 49.942  1.00 22.93 ? 49   GLU G OE1 1 
ATOM   6903  O  OE2 . GLU G  1 49  ? 5.665   143.462 50.093  1.00 20.01 ? 49   GLU G OE2 1 
ATOM   6904  N  N   . PHE G  1 50  ? 10.185  141.658 53.139  1.00 17.20 ? 50   PHE G N   1 
ATOM   6905  C  CA  . PHE G  1 50  ? 10.255  140.191 53.032  1.00 17.06 ? 50   PHE G CA  1 
ATOM   6906  C  C   . PHE G  1 50  ? 11.259  139.552 53.981  1.00 17.32 ? 50   PHE G C   1 
ATOM   6907  O  O   . PHE G  1 50  ? 12.392  140.043 54.116  1.00 17.68 ? 50   PHE G O   1 
ATOM   6908  C  CB  . PHE G  1 50  ? 10.634  139.821 51.612  1.00 17.00 ? 50   PHE G CB  1 
ATOM   6909  C  CG  . PHE G  1 50  ? 9.729   140.419 50.598  1.00 17.98 ? 50   PHE G CG  1 
ATOM   6910  C  CD1 . PHE G  1 50  ? 8.379   140.137 50.625  1.00 20.11 ? 50   PHE G CD1 1 
ATOM   6911  C  CD2 . PHE G  1 50  ? 10.209  141.323 49.665  1.00 19.02 ? 50   PHE G CD2 1 
ATOM   6912  C  CE1 . PHE G  1 50  ? 7.514   140.727 49.717  1.00 20.95 ? 50   PHE G CE1 1 
ATOM   6913  C  CE2 . PHE G  1 50  ? 9.363   141.926 48.757  1.00 20.46 ? 50   PHE G CE2 1 
ATOM   6914  C  CZ  . PHE G  1 50  ? 8.009   141.625 48.773  1.00 21.95 ? 50   PHE G CZ  1 
ATOM   6915  N  N   . GLY G  1 51  ? 10.837  138.477 54.638  1.00 16.26 ? 51   GLY G N   1 
ATOM   6916  C  CA  . GLY G  1 51  ? 11.721  137.723 55.508  1.00 17.12 ? 51   GLY G CA  1 
ATOM   6917  C  C   . GLY G  1 51  ? 12.433  136.716 54.621  1.00 17.83 ? 51   GLY G C   1 
ATOM   6918  O  O   . GLY G  1 51  ? 12.419  135.522 54.886  1.00 18.10 ? 51   GLY G O   1 
ATOM   6919  N  N   . ASP G  1 52  ? 13.030  137.209 53.540  1.00 18.00 ? 52   ASP G N   1 
ATOM   6920  C  CA  . ASP G  1 52  ? 13.657  136.344 52.559  1.00 18.41 ? 52   ASP G CA  1 
ATOM   6921  C  C   . ASP G  1 52  ? 15.136  136.630 52.552  1.00 19.08 ? 52   ASP G C   1 
ATOM   6922  O  O   . ASP G  1 52  ? 15.571  137.677 52.085  1.00 18.11 ? 52   ASP G O   1 
ATOM   6923  C  CB  . ASP G  1 52  ? 13.062  136.628 51.181  1.00 18.03 ? 52   ASP G CB  1 
ATOM   6924  C  CG  . ASP G  1 52  ? 13.590  135.720 50.099  1.00 18.42 ? 52   ASP G CG  1 
ATOM   6925  O  OD1 . ASP G  1 52  ? 14.718  135.178 50.191  1.00 17.16 ? 52   ASP G OD1 1 
ATOM   6926  O  OD2 . ASP G  1 52  ? 12.896  135.467 49.076  1.00 19.31 ? 52   ASP G OD2 1 
ATOM   6927  N  N   . ASN G  1 53  ? 15.905  135.686 53.069  1.00 19.75 ? 53   ASN G N   1 
ATOM   6928  C  CA  . ASN G  1 53  ? 17.351  135.824 53.103  1.00 21.25 ? 53   ASN G CA  1 
ATOM   6929  C  C   . ASN G  1 53  ? 18.070  134.946 52.090  1.00 20.87 ? 53   ASN G C   1 
ATOM   6930  O  O   . ASN G  1 53  ? 19.250  134.633 52.258  1.00 20.38 ? 53   ASN G O   1 
ATOM   6931  C  CB  . ASN G  1 53  ? 17.869  135.453 54.483  1.00 22.13 ? 53   ASN G CB  1 
ATOM   6932  C  CG  . ASN G  1 53  ? 19.285  135.913 54.697  1.00 27.57 ? 53   ASN G CG  1 
ATOM   6933  O  OD1 . ASN G  1 53  ? 19.605  137.084 54.448  1.00 33.28 ? 53   ASN G OD1 1 
ATOM   6934  N  ND2 . ASN G  1 53  ? 20.147  135.008 55.154  1.00 30.77 ? 53   ASN G ND2 1 
ATOM   6935  N  N   . THR G  1 54  ? 17.383  134.534 51.039  1.00 20.06 ? 54   THR G N   1 
ATOM   6936  C  CA  . THR G  1 54  ? 18.029  133.612 50.107  1.00 20.88 ? 54   THR G CA  1 
ATOM   6937  C  C   . THR G  1 54  ? 19.225  134.234 49.373  1.00 21.45 ? 54   THR G C   1 
ATOM   6938  O  O   . THR G  1 54  ? 20.123  133.518 48.942  1.00 21.03 ? 54   THR G O   1 
ATOM   6939  C  CB  . THR G  1 54  ? 17.025  133.050 49.076  1.00 20.14 ? 54   THR G CB  1 
ATOM   6940  O  OG1 . THR G  1 54  ? 16.331  134.139 48.458  1.00 19.83 ? 54   THR G OG1 1 
ATOM   6941  C  CG2 . THR G  1 54  ? 15.931  132.299 49.788  1.00 20.19 ? 54   THR G CG2 1 
ATOM   6942  N  N   . ALA G  1 55  ? 19.200  135.549 49.191  1.00 21.81 ? 55   ALA G N   1 
ATOM   6943  C  CA  . ALA G  1 55  ? 20.324  136.244 48.569  1.00 22.64 ? 55   ALA G CA  1 
ATOM   6944  C  C   . ALA G  1 55  ? 20.839  137.260 49.543  1.00 22.86 ? 55   ALA G C   1 
ATOM   6945  O  O   . ALA G  1 55  ? 21.004  138.454 49.199  1.00 23.58 ? 55   ALA G O   1 
ATOM   6946  C  CB  . ALA G  1 55  ? 19.904  136.931 47.276  1.00 22.76 ? 55   ALA G CB  1 
ATOM   6947  N  N   . GLY G  1 56  ? 21.098  136.812 50.763  1.00 22.86 ? 56   GLY G N   1 
ATOM   6948  C  CA  . GLY G  1 56  ? 21.521  137.737 51.808  1.00 22.60 ? 56   GLY G CA  1 
ATOM   6949  C  C   . GLY G  1 56  ? 20.471  138.809 52.109  1.00 22.69 ? 56   GLY G C   1 
ATOM   6950  O  O   . GLY G  1 56  ? 19.281  138.624 51.899  1.00 22.43 ? 56   GLY G O   1 
ATOM   6951  N  N   . CYS G  1 57  ? 20.920  139.962 52.585  1.00 22.19 ? 57   CYS G N   1 
ATOM   6952  C  CA  . CYS G  1 57  ? 20.006  141.036 52.945  1.00 22.17 ? 57   CYS G CA  1 
ATOM   6953  C  C   . CYS G  1 57  ? 19.281  141.622 51.730  1.00 21.54 ? 57   CYS G C   1 
ATOM   6954  O  O   . CYS G  1 57  ? 18.251  142.274 51.863  1.00 21.31 ? 57   CYS G O   1 
ATOM   6955  C  CB  . CYS G  1 57  ? 20.780  142.133 53.672  1.00 22.20 ? 57   CYS G CB  1 
ATOM   6956  S  SG  . CYS G  1 57  ? 21.440  141.508 55.244  1.00 25.42 ? 57   CYS G SG  1 
ATOM   6957  N  N   . THR G  1 58  ? 19.826  141.384 50.552  1.00 21.34 ? 58   THR G N   1 
ATOM   6958  C  CA  . THR G  1 58  ? 19.243  141.902 49.318  1.00 21.82 ? 58   THR G CA  1 
ATOM   6959  C  C   . THR G  1 58  ? 17.801  141.461 49.042  1.00 20.56 ? 58   THR G C   1 
ATOM   6960  O  O   . THR G  1 58  ? 16.963  142.263 48.633  1.00 19.90 ? 58   THR G O   1 
ATOM   6961  C  CB  . THR G  1 58  ? 20.136  141.522 48.120  1.00 22.37 ? 58   THR G CB  1 
ATOM   6962  O  OG1 . THR G  1 58  ? 21.414  142.143 48.298  1.00 26.23 ? 58   THR G OG1 1 
ATOM   6963  C  CG2 . THR G  1 58  ? 19.621  142.197 46.833  1.00 22.68 ? 58   THR G CG2 1 
ATOM   6964  N  N   . SER G  1 59  ? 17.508  140.180 49.246  1.00 19.18 ? 59   SER G N   1 
ATOM   6965  C  CA  . SER G  1 59  ? 16.165  139.698 48.992  1.00 18.25 ? 59   SER G CA  1 
ATOM   6966  C  C   . SER G  1 59  ? 15.137  140.159 50.016  1.00 18.14 ? 59   SER G C   1 
ATOM   6967  O  O   . SER G  1 59  ? 13.960  139.840 49.882  1.00 18.49 ? 59   SER G O   1 
ATOM   6968  C  CB  . SER G  1 59  ? 16.171  138.175 48.911  1.00 18.17 ? 59   SER G CB  1 
ATOM   6969  O  OG  . SER G  1 59  ? 17.223  137.712 49.714  1.00 16.95 ? 59   SER G OG  1 
ATOM   6970  N  N   . ALA G  1 60  ? 15.559  140.935 51.018  1.00 18.02 ? 60   ALA G N   1 
ATOM   6971  C  CA  . ALA G  1 60  ? 14.623  141.397 52.029  1.00 17.74 ? 60   ALA G CA  1 
ATOM   6972  C  C   . ALA G  1 60  ? 13.657  142.383 51.392  1.00 18.49 ? 60   ALA G C   1 
ATOM   6973  O  O   . ALA G  1 60  ? 12.595  142.702 51.950  1.00 19.34 ? 60   ALA G O   1 
ATOM   6974  C  CB  . ALA G  1 60  ? 15.375  142.074 53.205  1.00 17.66 ? 60   ALA G CB  1 
ATOM   6975  N  N   . GLY G  1 61  ? 14.028  142.894 50.229  1.00 19.08 ? 61   GLY G N   1 
ATOM   6976  C  CA  . GLY G  1 61  ? 13.176  143.861 49.547  1.00 19.32 ? 61   GLY G CA  1 
ATOM   6977  C  C   . GLY G  1 61  ? 13.257  145.254 50.158  1.00 19.88 ? 61   GLY G C   1 
ATOM   6978  O  O   . GLY G  1 61  ? 14.271  145.601 50.806  1.00 20.06 ? 61   GLY G O   1 
ATOM   6979  N  N   . PRO G  1 62  ? 12.196  146.046 49.998  1.00 19.73 ? 62   PRO G N   1 
ATOM   6980  C  CA  . PRO G  1 62  ? 12.203  147.429 50.470  1.00 20.45 ? 62   PRO G CA  1 
ATOM   6981  C  C   . PRO G  1 62  ? 11.648  147.543 51.881  1.00 20.01 ? 62   PRO G C   1 
ATOM   6982  O  O   . PRO G  1 62  ? 11.376  146.547 52.527  1.00 20.09 ? 62   PRO G O   1 
ATOM   6983  C  CB  . PRO G  1 62  ? 11.244  148.116 49.503  1.00 20.88 ? 62   PRO G CB  1 
ATOM   6984  C  CG  . PRO G  1 62  ? 10.295  147.071 49.090  1.00 20.23 ? 62   PRO G CG  1 
ATOM   6985  C  CD  . PRO G  1 62  ? 10.897  145.696 49.400  1.00 20.50 ? 62   PRO G CD  1 
ATOM   6986  N  N   . HIS G  1 63  ? 11.435  148.767 52.346  1.00 20.20 ? 63   HIS G N   1 
ATOM   6987  C  CA  . HIS G  1 63  ? 10.921  148.944 53.687  1.00 20.17 ? 63   HIS G CA  1 
ATOM   6988  C  C   . HIS G  1 63  ? 9.484   148.462 53.743  1.00 20.41 ? 63   HIS G C   1 
ATOM   6989  O  O   . HIS G  1 63  ? 8.757   148.604 52.763  1.00 20.69 ? 63   HIS G O   1 
ATOM   6990  C  CB  . HIS G  1 63  ? 11.020  150.424 54.069  1.00 20.21 ? 63   HIS G CB  1 
ATOM   6991  C  CG  . HIS G  1 63  ? 12.431  150.910 54.150  1.00 20.97 ? 63   HIS G CG  1 
ATOM   6992  N  ND1 . HIS G  1 63  ? 12.760  152.220 54.427  1.00 21.20 ? 63   HIS G ND1 1 
ATOM   6993  C  CD2 . HIS G  1 63  ? 13.604  150.248 54.008  1.00 20.91 ? 63   HIS G CD2 1 
ATOM   6994  C  CE1 . HIS G  1 63  ? 14.077  152.344 54.453  1.00 20.93 ? 63   HIS G CE1 1 
ATOM   6995  N  NE2 . HIS G  1 63  ? 14.613  151.163 54.205  1.00 20.18 ? 63   HIS G NE2 1 
ATOM   6996  N  N   . PHE G  1 64  ? 9.093   147.862 54.868  1.00 20.62 ? 64   PHE G N   1 
ATOM   6997  C  CA  . PHE G  1 64  ? 7.711   147.423 55.070  1.00 20.83 ? 64   PHE G CA  1 
ATOM   6998  C  C   . PHE G  1 64  ? 6.861   148.688 55.026  1.00 21.11 ? 64   PHE G C   1 
ATOM   6999  O  O   . PHE G  1 64  ? 7.140   149.645 55.728  1.00 20.75 ? 64   PHE G O   1 
ATOM   7000  C  CB  . PHE G  1 64  ? 7.561   146.719 56.417  1.00 21.14 ? 64   PHE G CB  1 
ATOM   7001  C  CG  . PHE G  1 64  ? 6.164   146.268 56.725  1.00 20.93 ? 64   PHE G CG  1 
ATOM   7002  C  CD1 . PHE G  1 64  ? 5.360   145.728 55.738  1.00 22.88 ? 64   PHE G CD1 1 
ATOM   7003  C  CD2 . PHE G  1 64  ? 5.655   146.371 58.012  1.00 21.83 ? 64   PHE G CD2 1 
ATOM   7004  C  CE1 . PHE G  1 64  ? 4.070   145.301 56.027  1.00 24.08 ? 64   PHE G CE1 1 
ATOM   7005  C  CE2 . PHE G  1 64  ? 4.363   145.936 58.305  1.00 22.43 ? 64   PHE G CE2 1 
ATOM   7006  C  CZ  . PHE G  1 64  ? 3.578   145.411 57.316  1.00 22.53 ? 64   PHE G CZ  1 
ATOM   7007  N  N   . ASN G  1 65  ? 5.842   148.692 54.183  1.00 21.00 ? 65   ASN G N   1 
ATOM   7008  C  CA  . ASN G  1 65  ? 5.035   149.900 53.997  1.00 21.34 ? 65   ASN G CA  1 
ATOM   7009  C  C   . ASN G  1 65  ? 3.686   149.594 53.397  1.00 21.77 ? 65   ASN G C   1 
ATOM   7010  O  O   . ASN G  1 65  ? 3.438   149.887 52.225  1.00 21.56 ? 65   ASN G O   1 
ATOM   7011  C  CB  . ASN G  1 65  ? 5.750   150.826 53.041  1.00 20.61 ? 65   ASN G CB  1 
ATOM   7012  C  CG  . ASN G  1 65  ? 5.048   152.142 52.883  1.00 20.90 ? 65   ASN G CG  1 
ATOM   7013  O  OD1 . ASN G  1 65  ? 4.325   152.606 53.781  1.00 19.39 ? 65   ASN G OD1 1 
ATOM   7014  N  ND2 . ASN G  1 65  ? 5.281   152.778 51.749  1.00 20.75 ? 65   ASN G ND2 1 
ATOM   7015  N  N   . PRO G  1 66  ? 2.806   149.016 54.195  1.00 22.85 ? 66   PRO G N   1 
ATOM   7016  C  CA  . PRO G  1 66  ? 1.479   148.631 53.704  1.00 23.75 ? 66   PRO G CA  1 
ATOM   7017  C  C   . PRO G  1 66  ? 0.677   149.846 53.199  1.00 24.45 ? 66   PRO G C   1 
ATOM   7018  O  O   . PRO G  1 66  ? -0.203  149.699 52.350  1.00 24.59 ? 66   PRO G O   1 
ATOM   7019  C  CB  . PRO G  1 66  ? 0.795   148.033 54.939  1.00 23.75 ? 66   PRO G CB  1 
ATOM   7020  C  CG  . PRO G  1 66  ? 1.821   147.837 55.946  1.00 24.26 ? 66   PRO G CG  1 
ATOM   7021  C  CD  . PRO G  1 66  ? 3.025   148.665 55.607  1.00 22.44 ? 66   PRO G CD  1 
ATOM   7022  N  N   . LEU G  1 67  ? 1.016   151.023 53.702  1.00 24.85 ? 67   LEU G N   1 
ATOM   7023  C  CA  . LEU G  1 67  ? 0.274   152.249 53.396  1.00 25.61 ? 67   LEU G CA  1 
ATOM   7024  C  C   . LEU G  1 67  ? 0.834   153.132 52.281  1.00 26.09 ? 67   LEU G C   1 
ATOM   7025  O  O   . LEU G  1 67  ? 0.393   154.284 52.109  1.00 26.39 ? 67   LEU G O   1 
ATOM   7026  C  CB  . LEU G  1 67  ? 0.093   153.069 54.668  1.00 25.49 ? 67   LEU G CB  1 
ATOM   7027  C  CG  . LEU G  1 67  ? -0.693  152.289 55.718  1.00 25.40 ? 67   LEU G CG  1 
ATOM   7028  C  CD1 . LEU G  1 67  ? -0.704  153.036 57.033  1.00 26.13 ? 67   LEU G CD1 1 
ATOM   7029  C  CD2 . LEU G  1 67  ? -2.119  151.989 55.225  1.00 23.90 ? 67   LEU G CD2 1 
ATOM   7030  N  N   . SER G  1 68  ? 1.793   152.598 51.533  1.00 26.19 ? 68   SER G N   1 
ATOM   7031  C  CA  . SER G  1 68  ? 2.334   153.284 50.371  1.00 26.58 ? 68   SER G CA  1 
ATOM   7032  C  C   . SER G  1 68  ? 2.626   154.726 50.687  1.00 26.68 ? 68   SER G C   1 
ATOM   7033  O  O   . SER G  1 68  ? 2.163   155.625 49.987  1.00 26.53 ? 68   SER G O   1 
ATOM   7034  C  CB  . SER G  1 68  ? 1.333   153.218 49.202  1.00 26.27 ? 68   SER G CB  1 
ATOM   7035  O  OG  . SER G  1 68  ? 1.103   151.879 48.812  1.00 27.74 ? 68   SER G OG  1 
ATOM   7036  N  N   . ARG G  1 69  ? 3.370   154.944 51.765  1.00 27.17 ? 69   ARG G N   1 
ATOM   7037  C  CA  . ARG G  1 69  ? 3.771   156.279 52.173  1.00 27.40 ? 69   ARG G CA  1 
ATOM   7038  C  C   . ARG G  1 69  ? 5.230   156.491 51.802  1.00 26.98 ? 69   ARG G C   1 
ATOM   7039  O  O   . ARG G  1 69  ? 5.918   155.552 51.374  1.00 27.68 ? 69   ARG G O   1 
ATOM   7040  C  CB  . ARG G  1 69  ? 3.624   156.436 53.679  1.00 27.70 ? 69   ARG G CB  1 
ATOM   7041  C  CG  . ARG G  1 69  ? 2.216   156.361 54.214  1.00 30.67 ? 69   ARG G CG  1 
ATOM   7042  C  CD  . ARG G  1 69  ? 2.058   157.063 55.551  1.00 35.82 ? 69   ARG G CD  1 
ATOM   7043  N  NE  . ARG G  1 69  ? 0.901   156.597 56.304  1.00 38.40 ? 69   ARG G NE  1 
ATOM   7044  C  CZ  . ARG G  1 69  ? -0.330  157.029 56.116  1.00 39.15 ? 69   ARG G CZ  1 
ATOM   7045  N  NH1 . ARG G  1 69  ? -0.577  157.942 55.185  1.00 41.12 ? 69   ARG G NH1 1 
ATOM   7046  N  NH2 . ARG G  1 69  ? -1.317  156.545 56.856  1.00 39.87 ? 69   ARG G NH2 1 
ATOM   7047  N  N   . LYS G  1 70  ? 5.705   157.717 51.975  1.00 26.03 ? 70   LYS G N   1 
ATOM   7048  C  CA  . LYS G  1 70  ? 7.089   158.031 51.695  1.00 24.98 ? 70   LYS G CA  1 
ATOM   7049  C  C   . LYS G  1 70  ? 7.918   157.747 52.934  1.00 23.86 ? 70   LYS G C   1 
ATOM   7050  O  O   . LYS G  1 70  ? 7.402   157.673 54.056  1.00 22.56 ? 70   LYS G O   1 
ATOM   7051  C  CB  . LYS G  1 70  ? 7.256   159.487 51.272  1.00 25.66 ? 70   LYS G CB  1 
ATOM   7052  C  CG  . LYS G  1 70  ? 6.472   159.865 50.030  1.00 27.57 ? 70   LYS G CG  1 
ATOM   7053  C  CD  . LYS G  1 70  ? 6.629   158.814 48.947  1.00 30.41 ? 70   LYS G CD  1 
ATOM   7054  C  CE  . LYS G  1 70  ? 6.017   159.287 47.627  1.00 31.74 ? 70   LYS G CE  1 
ATOM   7055  N  NZ  . LYS G  1 70  ? 6.850   160.337 46.972  1.00 33.65 ? 70   LYS G NZ  1 
ATOM   7056  N  N   . HIS G  1 71  ? 9.216   157.600 52.734  1.00 22.92 ? 71   HIS G N   1 
ATOM   7057  C  CA  . HIS G  1 71  ? 10.061  157.264 53.853  1.00 22.62 ? 71   HIS G CA  1 
ATOM   7058  C  C   . HIS G  1 71  ? 10.125  158.432 54.822  1.00 22.15 ? 71   HIS G C   1 
ATOM   7059  O  O   . HIS G  1 71  ? 10.090  159.598 54.427  1.00 20.88 ? 71   HIS G O   1 
ATOM   7060  C  CB  . HIS G  1 71  ? 11.460  156.875 53.390  1.00 22.52 ? 71   HIS G CB  1 
ATOM   7061  C  CG  . HIS G  1 71  ? 12.427  156.676 54.515  1.00 22.85 ? 71   HIS G CG  1 
ATOM   7062  N  ND1 . HIS G  1 71  ? 12.515  155.496 55.223  1.00 22.21 ? 71   HIS G ND1 1 
ATOM   7063  C  CD2 . HIS G  1 71  ? 13.341  157.512 55.062  1.00 21.83 ? 71   HIS G CD2 1 
ATOM   7064  C  CE1 . HIS G  1 71  ? 13.445  155.615 56.156  1.00 21.24 ? 71   HIS G CE1 1 
ATOM   7065  N  NE2 . HIS G  1 71  ? 13.959  156.829 56.081  1.00 22.48 ? 71   HIS G NE2 1 
ATOM   7066  N  N   . GLY G  1 72  ? 10.203  158.119 56.103  1.00 21.81 ? 72   GLY G N   1 
ATOM   7067  C  CA  . GLY G  1 72  ? 10.354  159.175 57.089  1.00 21.36 ? 72   GLY G CA  1 
ATOM   7068  C  C   . GLY G  1 72  ? 11.120  158.672 58.292  1.00 20.95 ? 72   GLY G C   1 
ATOM   7069  O  O   . GLY G  1 72  ? 11.653  157.540 58.315  1.00 20.56 ? 72   GLY G O   1 
ATOM   7070  N  N   . GLY G  1 73  ? 11.186  159.523 59.295  1.00 20.85 ? 73   GLY G N   1 
ATOM   7071  C  CA  . GLY G  1 73  ? 11.757  159.150 60.562  1.00 21.39 ? 73   GLY G CA  1 
ATOM   7072  C  C   . GLY G  1 73  ? 10.621  158.549 61.351  1.00 21.68 ? 73   GLY G C   1 
ATOM   7073  O  O   . GLY G  1 73  ? 9.456   158.733 61.009  1.00 22.48 ? 73   GLY G O   1 
ATOM   7074  N  N   . PRO G  1 74  ? 10.953  157.868 62.432  1.00 21.97 ? 74   PRO G N   1 
ATOM   7075  C  CA  . PRO G  1 74  ? 9.953   157.187 63.251  1.00 22.15 ? 74   PRO G CA  1 
ATOM   7076  C  C   . PRO G  1 74  ? 8.887   158.171 63.753  1.00 22.35 ? 74   PRO G C   1 
ATOM   7077  O  O   . PRO G  1 74  ? 7.711   157.837 63.795  1.00 22.25 ? 74   PRO G O   1 
ATOM   7078  C  CB  . PRO G  1 74  ? 10.760  156.679 64.448  1.00 21.86 ? 74   PRO G CB  1 
ATOM   7079  C  CG  . PRO G  1 74  ? 12.185  156.730 64.024  1.00 23.11 ? 74   PRO G CG  1 
ATOM   7080  C  CD  . PRO G  1 74  ? 12.312  157.790 62.991  1.00 22.45 ? 74   PRO G CD  1 
ATOM   7081  N  N   . LYS G  1 75  ? 9.301   159.377 64.123  1.00 22.87 ? 75   LYS G N   1 
ATOM   7082  C  CA  . LYS G  1 75  ? 8.368   160.341 64.696  1.00 23.74 ? 75   LYS G CA  1 
ATOM   7083  C  C   . LYS G  1 75  ? 7.478   161.055 63.657  1.00 24.05 ? 75   LYS G C   1 
ATOM   7084  O  O   . LYS G  1 75  ? 6.522   161.742 64.029  1.00 24.38 ? 75   LYS G O   1 
ATOM   7085  C  CB  . LYS G  1 75  ? 9.125   161.361 65.575  1.00 23.94 ? 75   LYS G CB  1 
ATOM   7086  C  CG  . LYS G  1 75  ? 9.884   160.746 66.769  1.00 24.51 ? 75   LYS G CG  1 
ATOM   7087  C  CD  . LYS G  1 75  ? 10.798  161.770 67.491  1.00 30.37 ? 75   LYS G CD  1 
ATOM   7088  C  CE  . LYS G  1 75  ? 11.946  161.048 68.256  1.00 32.81 ? 75   LYS G CE  1 
ATOM   7089  N  NZ  . LYS G  1 75  ? 12.467  159.795 67.551  1.00 34.57 ? 75   LYS G NZ  1 
ATOM   7090  N  N   . ASP G  1 76  ? 7.786   160.906 62.368  1.00 24.19 ? 76   ASP G N   1 
ATOM   7091  C  CA  . ASP G  1 76  ? 7.013   161.584 61.325  1.00 24.89 ? 76   ASP G CA  1 
ATOM   7092  C  C   . ASP G  1 76  ? 5.673   160.913 61.066  1.00 25.03 ? 76   ASP G C   1 
ATOM   7093  O  O   . ASP G  1 76  ? 5.584   159.674 61.070  1.00 26.28 ? 76   ASP G O   1 
ATOM   7094  C  CB  . ASP G  1 76  ? 7.782   161.674 59.998  1.00 24.45 ? 76   ASP G CB  1 
ATOM   7095  C  CG  . ASP G  1 76  ? 9.111   162.411 60.122  1.00 24.75 ? 76   ASP G CG  1 
ATOM   7096  O  OD1 . ASP G  1 76  ? 9.143   163.517 60.707  1.00 24.62 ? 76   ASP G OD1 1 
ATOM   7097  O  OD2 . ASP G  1 76  ? 10.182  161.958 59.653  1.00 23.77 ? 76   ASP G OD2 1 
ATOM   7098  N  N   . GLU G  1 77  ? 4.636   161.729 60.853  1.00 25.57 ? 77   GLU G N   1 
ATOM   7099  C  CA  . GLU G  1 77  ? 3.318   161.216 60.465  1.00 25.88 ? 77   GLU G CA  1 
ATOM   7100  C  C   . GLU G  1 77  ? 3.558   160.430 59.208  1.00 25.19 ? 77   GLU G C   1 
ATOM   7101  O  O   . GLU G  1 77  ? 3.115   159.288 59.070  1.00 25.27 ? 77   GLU G O   1 
ATOM   7102  C  CB  . GLU G  1 77  ? 2.328   162.351 60.163  1.00 26.41 ? 77   GLU G CB  1 
ATOM   7103  C  CG  . GLU G  1 77  ? 0.926   161.861 59.792  1.00 28.35 ? 77   GLU G CG  1 
ATOM   7104  C  CD  . GLU G  1 77  ? 0.496   162.134 58.343  1.00 30.78 ? 77   GLU G CD  1 
ATOM   7105  O  OE1 . GLU G  1 77  ? 0.278   163.319 57.983  1.00 29.47 ? 77   GLU G OE1 1 
ATOM   7106  O  OE2 . GLU G  1 77  ? 0.331   161.156 57.572  1.00 31.51 ? 77   GLU G OE2 1 
ATOM   7107  N  N   . GLU G  1 78  ? 4.284   161.051 58.287  1.00 24.43 ? 78   GLU G N   1 
ATOM   7108  C  CA  . GLU G  1 78  ? 4.641   160.406 57.038  1.00 24.30 ? 78   GLU G CA  1 
ATOM   7109  C  C   . GLU G  1 78  ? 5.840   159.484 57.274  1.00 23.43 ? 78   GLU G C   1 
ATOM   7110  O  O   . GLU G  1 78  ? 6.931   159.955 57.553  1.00 23.44 ? 78   GLU G O   1 
ATOM   7111  C  CB  . GLU G  1 78  ? 4.990   161.462 55.983  1.00 24.32 ? 78   GLU G CB  1 
ATOM   7112  C  CG  . GLU G  1 78  ? 5.040   160.925 54.556  1.00 25.03 ? 78   GLU G CG  1 
ATOM   7113  C  CD  . GLU G  1 78  ? 3.665   160.564 54.008  1.00 27.55 ? 78   GLU G CD  1 
ATOM   7114  O  OE1 . GLU G  1 78  ? 2.657   161.098 54.527  1.00 29.13 ? 78   GLU G OE1 1 
ATOM   7115  O  OE2 . GLU G  1 78  ? 3.585   159.752 53.053  1.00 24.80 ? 78   GLU G OE2 1 
ATOM   7116  N  N   . ARG G  1 79  ? 5.623   158.177 57.196  1.00 22.58 ? 79   ARG G N   1 
ATOM   7117  C  CA  . ARG G  1 79  ? 6.715   157.219 57.325  1.00 21.57 ? 79   ARG G CA  1 
ATOM   7118  C  C   . ARG G  1 79  ? 6.256   155.858 56.859  1.00 22.02 ? 79   ARG G C   1 
ATOM   7119  O  O   . ARG G  1 79  ? 5.060   155.564 56.874  1.00 22.33 ? 79   ARG G O   1 
ATOM   7120  C  CB  . ARG G  1 79  ? 7.246   157.132 58.765  1.00 21.03 ? 79   ARG G CB  1 
ATOM   7121  C  CG  . ARG G  1 79  ? 6.223   156.715 59.819  1.00 19.29 ? 79   ARG G CG  1 
ATOM   7122  C  CD  . ARG G  1 79  ? 6.814   156.353 61.172  1.00 20.07 ? 79   ARG G CD  1 
ATOM   7123  N  NE  . ARG G  1 79  ? 6.994   154.902 61.322  1.00 16.95 ? 79   ARG G NE  1 
ATOM   7124  C  CZ  . ARG G  1 79  ? 7.306   154.305 62.469  1.00 19.91 ? 79   ARG G CZ  1 
ATOM   7125  N  NH1 . ARG G  1 79  ? 7.517   155.026 63.569  1.00 17.89 ? 79   ARG G NH1 1 
ATOM   7126  N  NH2 . ARG G  1 79  ? 7.423   152.980 62.520  1.00 18.86 ? 79   ARG G NH2 1 
ATOM   7127  N  N   . HIS G  1 80  ? 7.209   155.044 56.409  1.00 21.03 ? 80   HIS G N   1 
ATOM   7128  C  CA  . HIS G  1 80  ? 6.908   153.677 56.064  1.00 21.04 ? 80   HIS G CA  1 
ATOM   7129  C  C   . HIS G  1 80  ? 6.689   153.054 57.423  1.00 21.29 ? 80   HIS G C   1 
ATOM   7130  O  O   . HIS G  1 80  ? 7.245   153.524 58.417  1.00 21.43 ? 80   HIS G O   1 
ATOM   7131  C  CB  . HIS G  1 80  ? 8.133   152.987 55.461  1.00 20.87 ? 80   HIS G CB  1 
ATOM   7132  C  CG  . HIS G  1 80  ? 8.554   153.518 54.128  1.00 20.71 ? 80   HIS G CG  1 
ATOM   7133  N  ND1 . HIS G  1 80  ? 9.882   153.651 53.768  1.00 20.47 ? 80   HIS G ND1 1 
ATOM   7134  C  CD2 . HIS G  1 80  ? 7.830   153.936 53.065  1.00 19.48 ? 80   HIS G CD2 1 
ATOM   7135  C  CE1 . HIS G  1 80  ? 9.953   154.125 52.536  1.00 22.06 ? 80   HIS G CE1 1 
ATOM   7136  N  NE2 . HIS G  1 80  ? 8.722   154.307 52.089  1.00 21.75 ? 80   HIS G NE2 1 
ATOM   7137  N  N   . VAL G  1 81  ? 5.928   151.975 57.490  1.00 21.00 ? 81   VAL G N   1 
ATOM   7138  C  CA  . VAL G  1 81  ? 5.752   151.334 58.778  1.00 20.82 ? 81   VAL G CA  1 
ATOM   7139  C  C   . VAL G  1 81  ? 7.084   150.827 59.361  1.00 20.44 ? 81   VAL G C   1 
ATOM   7140  O  O   . VAL G  1 81  ? 7.295   150.872 60.573  1.00 20.21 ? 81   VAL G O   1 
ATOM   7141  C  CB  . VAL G  1 81  ? 4.731   150.208 58.678  1.00 21.31 ? 81   VAL G CB  1 
ATOM   7142  C  CG1 . VAL G  1 81  ? 4.798   149.302 59.900  1.00 20.25 ? 81   VAL G CG1 1 
ATOM   7143  C  CG2 . VAL G  1 81  ? 3.327   150.820 58.485  1.00 22.76 ? 81   VAL G CG2 1 
ATOM   7144  N  N   . GLY G  1 82  ? 7.995   150.376 58.505  1.00 19.81 ? 82   GLY G N   1 
ATOM   7145  C  CA  . GLY G  1 82  ? 9.260   149.832 58.979  1.00 19.66 ? 82   GLY G CA  1 
ATOM   7146  C  C   . GLY G  1 82  ? 10.348  150.843 59.294  1.00 19.48 ? 82   GLY G C   1 
ATOM   7147  O  O   . GLY G  1 82  ? 11.488  150.476 59.629  1.00 19.66 ? 82   GLY G O   1 
ATOM   7148  N  N   . ASP G  1 83  ? 10.006  152.134 59.256  1.00 19.08 ? 83   ASP G N   1 
ATOM   7149  C  CA  . ASP G  1 83  ? 10.999  153.180 59.488  1.00 18.60 ? 83   ASP G CA  1 
ATOM   7150  C  C   . ASP G  1 83  ? 11.304  153.412 60.971  1.00 18.69 ? 83   ASP G C   1 
ATOM   7151  O  O   . ASP G  1 83  ? 10.572  154.147 61.651  1.00 17.79 ? 83   ASP G O   1 
ATOM   7152  C  CB  . ASP G  1 83  ? 10.518  154.504 58.865  1.00 19.35 ? 83   ASP G CB  1 
ATOM   7153  C  CG  . ASP G  1 83  ? 10.569  154.480 57.348  1.00 19.52 ? 83   ASP G CG  1 
ATOM   7154  O  OD1 . ASP G  1 83  ? 11.118  153.501 56.797  1.00 15.43 ? 83   ASP G OD1 1 
ATOM   7155  O  OD2 . ASP G  1 83  ? 10.120  155.391 56.626  1.00 18.53 ? 83   ASP G OD2 1 
ATOM   7156  N  N   . LEU G  1 84  ? 12.397  152.828 61.460  1.00 18.46 ? 84   LEU G N   1 
ATOM   7157  C  CA  . LEU G  1 84  ? 12.747  152.946 62.866  1.00 18.86 ? 84   LEU G CA  1 
ATOM   7158  C  C   . LEU G  1 84  ? 13.923  153.886 63.077  1.00 19.65 ? 84   LEU G C   1 
ATOM   7159  O  O   . LEU G  1 84  ? 14.547  153.873 64.145  1.00 20.70 ? 84   LEU G O   1 
ATOM   7160  C  CB  . LEU G  1 84  ? 13.060  151.572 63.459  1.00 19.24 ? 84   LEU G CB  1 
ATOM   7161  C  CG  . LEU G  1 84  ? 11.885  150.594 63.376  1.00 18.17 ? 84   LEU G CG  1 
ATOM   7162  C  CD1 . LEU G  1 84  ? 12.327  149.192 63.770  1.00 19.60 ? 84   LEU G CD1 1 
ATOM   7163  C  CD2 . LEU G  1 84  ? 10.757  151.078 64.268  1.00 18.84 ? 84   LEU G CD2 1 
ATOM   7164  N  N   . GLY G  1 85  ? 14.234  154.689 62.062  1.00 19.56 ? 85   GLY G N   1 
ATOM   7165  C  CA  . GLY G  1 85  ? 15.263  155.709 62.179  1.00 19.17 ? 85   GLY G CA  1 
ATOM   7166  C  C   . GLY G  1 85  ? 16.686  155.196 62.310  1.00 19.38 ? 85   GLY G C   1 
ATOM   7167  O  O   . GLY G  1 85  ? 17.125  154.367 61.523  1.00 18.69 ? 85   GLY G O   1 
ATOM   7168  N  N   . ASN G  1 86  ? 17.405  155.686 63.311  1.00 18.92 ? 86   ASN G N   1 
ATOM   7169  C  CA  . ASN G  1 86  ? 18.812  155.337 63.481  1.00 19.46 ? 86   ASN G CA  1 
ATOM   7170  C  C   . ASN G  1 86  ? 19.145  154.743 64.830  1.00 19.39 ? 86   ASN G C   1 
ATOM   7171  O  O   . ASN G  1 86  ? 18.508  155.083 65.841  1.00 20.21 ? 86   ASN G O   1 
ATOM   7172  C  CB  . ASN G  1 86  ? 19.652  156.608 63.373  1.00 19.99 ? 86   ASN G CB  1 
ATOM   7173  C  CG  . ASN G  1 86  ? 19.777  157.102 61.967  1.00 20.46 ? 86   ASN G CG  1 
ATOM   7174  O  OD1 . ASN G  1 86  ? 20.382  156.448 61.126  1.00 20.99 ? 86   ASN G OD1 1 
ATOM   7175  N  ND2 . ASN G  1 86  ? 19.204  158.280 61.696  1.00 19.49 ? 86   ASN G ND2 1 
ATOM   7176  N  N   . VAL G  1 87  ? 20.171  153.891 64.866  1.00 18.75 ? 87   VAL G N   1 
ATOM   7177  C  CA  . VAL G  1 87  ? 20.739  153.498 66.152  1.00 18.09 ? 87   VAL G CA  1 
ATOM   7178  C  C   . VAL G  1 87  ? 22.135  154.114 66.209  1.00 17.30 ? 87   VAL G C   1 
ATOM   7179  O  O   . VAL G  1 87  ? 22.688  154.474 65.182  1.00 16.81 ? 87   VAL G O   1 
ATOM   7180  C  CB  . VAL G  1 87  ? 20.773  152.001 66.353  1.00 18.36 ? 87   VAL G CB  1 
ATOM   7181  C  CG1 . VAL G  1 87  ? 19.338  151.431 66.346  1.00 19.71 ? 87   VAL G CG1 1 
ATOM   7182  C  CG2 . VAL G  1 87  ? 21.595  151.330 65.255  1.00 17.30 ? 87   VAL G CG2 1 
ATOM   7183  N  N   . THR G  1 88  ? 22.691  154.267 67.408  1.00 16.27 ? 88   THR G N   1 
ATOM   7184  C  CA  . THR G  1 88  ? 23.968  154.935 67.553  1.00 15.25 ? 88   THR G CA  1 
ATOM   7185  C  C   . THR G  1 88  ? 25.013  154.001 68.088  1.00 15.05 ? 88   THR G C   1 
ATOM   7186  O  O   . THR G  1 88  ? 24.846  153.471 69.174  1.00 15.13 ? 88   THR G O   1 
ATOM   7187  C  CB  . THR G  1 88  ? 23.800  156.079 68.571  1.00 16.17 ? 88   THR G CB  1 
ATOM   7188  O  OG1 . THR G  1 88  ? 22.859  157.024 68.061  1.00 15.55 ? 88   THR G OG1 1 
ATOM   7189  C  CG2 . THR G  1 88  ? 25.089  156.890 68.702  1.00 15.81 ? 88   THR G CG2 1 
ATOM   7190  N  N   . ALA G  1 89  ? 26.091  153.802 67.345  1.00 14.83 ? 89   ALA G N   1 
ATOM   7191  C  CA  . ALA G  1 89  ? 27.196  152.975 67.822  1.00 14.87 ? 89   ALA G CA  1 
ATOM   7192  C  C   . ALA G  1 89  ? 28.177  153.837 68.598  1.00 16.19 ? 89   ALA G C   1 
ATOM   7193  O  O   . ALA G  1 89  ? 28.476  154.964 68.182  1.00 15.56 ? 89   ALA G O   1 
ATOM   7194  C  CB  . ALA G  1 89  ? 27.906  152.333 66.660  1.00 14.86 ? 89   ALA G CB  1 
ATOM   7195  N  N   . ASP G  1 90  ? 28.702  153.301 69.709  1.00 17.04 ? 90   ASP G N   1 
ATOM   7196  C  CA  . ASP G  1 90  ? 29.698  154.007 70.503  1.00 17.50 ? 90   ASP G CA  1 
ATOM   7197  C  C   . ASP G  1 90  ? 31.094  153.797 69.927  1.00 18.10 ? 90   ASP G C   1 
ATOM   7198  O  O   . ASP G  1 90  ? 31.244  153.188 68.861  1.00 17.72 ? 90   ASP G O   1 
ATOM   7199  C  CB  . ASP G  1 90  ? 29.627  153.641 72.000  1.00 17.76 ? 90   ASP G CB  1 
ATOM   7200  C  CG  . ASP G  1 90  ? 29.963  152.162 72.292  1.00 19.83 ? 90   ASP G CG  1 
ATOM   7201  O  OD1 . ASP G  1 90  ? 30.635  151.497 71.459  1.00 19.40 ? 90   ASP G OD1 1 
ATOM   7202  O  OD2 . ASP G  1 90  ? 29.595  151.584 73.355  1.00 19.75 ? 90   ASP G OD2 1 
ATOM   7203  N  N   . LYS G  1 91  ? 32.119  154.265 70.642  1.00 17.60 ? 91   LYS G N   1 
ATOM   7204  C  CA  . LYS G  1 91  ? 33.479  154.235 70.107  1.00 18.82 ? 91   LYS G CA  1 
ATOM   7205  C  C   . LYS G  1 91  ? 34.017  152.819 69.960  1.00 19.07 ? 91   LYS G C   1 
ATOM   7206  O  O   . LYS G  1 91  ? 34.972  152.575 69.193  1.00 20.87 ? 91   LYS G O   1 
ATOM   7207  C  CB  . LYS G  1 91  ? 34.414  155.115 70.980  1.00 18.91 ? 91   LYS G CB  1 
ATOM   7208  C  CG  . LYS G  1 91  ? 33.872  156.553 71.149  1.00 22.68 ? 91   LYS G CG  1 
ATOM   7209  C  CD  . LYS G  1 91  ? 34.540  157.355 72.289  1.00 29.18 ? 91   LYS G CD  1 
ATOM   7210  C  CE  . LYS G  1 91  ? 34.099  158.840 72.274  1.00 31.95 ? 91   LYS G CE  1 
ATOM   7211  N  NZ  . LYS G  1 91  ? 34.564  159.613 73.464  1.00 32.37 ? 91   LYS G NZ  1 
ATOM   7212  N  N   . ASP G  1 92  ? 33.417  151.894 70.708  1.00 17.82 ? 92   ASP G N   1 
ATOM   7213  C  CA  . ASP G  1 92  ? 33.801  150.477 70.668  1.00 18.21 ? 92   ASP G CA  1 
ATOM   7214  C  C   . ASP G  1 92  ? 32.993  149.699 69.618  1.00 17.09 ? 92   ASP G C   1 
ATOM   7215  O  O   . ASP G  1 92  ? 33.092  148.487 69.546  1.00 17.00 ? 92   ASP G O   1 
ATOM   7216  C  CB  . ASP G  1 92  ? 33.547  149.822 72.024  1.00 18.59 ? 92   ASP G CB  1 
ATOM   7217  C  CG  . ASP G  1 92  ? 34.447  150.375 73.120  1.00 21.74 ? 92   ASP G CG  1 
ATOM   7218  O  OD1 . ASP G  1 92  ? 35.624  150.683 72.839  1.00 23.40 ? 92   ASP G OD1 1 
ATOM   7219  O  OD2 . ASP G  1 92  ? 34.055  150.540 74.297  1.00 25.79 ? 92   ASP G OD2 1 
ATOM   7220  N  N   . GLY G  1 93  ? 32.160  150.390 68.853  1.00 16.48 ? 93   GLY G N   1 
ATOM   7221  C  CA  . GLY G  1 93  ? 31.376  149.751 67.801  1.00 16.05 ? 93   GLY G CA  1 
ATOM   7222  C  C   . GLY G  1 93  ? 30.070  149.145 68.263  1.00 16.01 ? 93   GLY G C   1 
ATOM   7223  O  O   . GLY G  1 93  ? 29.390  148.410 67.522  1.00 14.34 ? 93   GLY G O   1 
ATOM   7224  N  N   . VAL G  1 94  ? 29.695  149.447 69.495  1.00 15.48 ? 94   VAL G N   1 
ATOM   7225  C  CA  . VAL G  1 94  ? 28.502  148.867 70.038  1.00 15.85 ? 94   VAL G CA  1 
ATOM   7226  C  C   . VAL G  1 94  ? 27.365  149.853 70.020  1.00 16.74 ? 94   VAL G C   1 
ATOM   7227  O  O   . VAL G  1 94  ? 27.522  151.002 70.447  1.00 15.54 ? 94   VAL G O   1 
ATOM   7228  C  CB  . VAL G  1 94  ? 28.716  148.390 71.483  1.00 16.25 ? 94   VAL G CB  1 
ATOM   7229  C  CG1 . VAL G  1 94  ? 27.398  147.892 72.072  1.00 16.69 ? 94   VAL G CG1 1 
ATOM   7230  C  CG2 . VAL G  1 94  ? 29.782  147.298 71.534  1.00 17.28 ? 94   VAL G CG2 1 
ATOM   7231  N  N   . ALA G  1 95  ? 26.228  149.403 69.507  1.00 17.05 ? 95   ALA G N   1 
ATOM   7232  C  CA  . ALA G  1 95  ? 25.028  150.204 69.528  1.00 18.05 ? 95   ALA G CA  1 
ATOM   7233  C  C   . ALA G  1 95  ? 24.029  149.550 70.469  1.00 19.09 ? 95   ALA G C   1 
ATOM   7234  O  O   . ALA G  1 95  ? 23.549  148.440 70.240  1.00 19.37 ? 95   ALA G O   1 
ATOM   7235  C  CB  . ALA G  1 95  ? 24.449  150.360 68.140  1.00 18.03 ? 95   ALA G CB  1 
ATOM   7236  N  N   . ASP G  1 96  ? 23.746  150.233 71.563  1.00 20.22 ? 96   ASP G N   1 
ATOM   7237  C  CA  . ASP G  1 96  ? 22.743  149.728 72.467  1.00 21.20 ? 96   ASP G CA  1 
ATOM   7238  C  C   . ASP G  1 96  ? 21.444  150.320 71.993  1.00 21.72 ? 96   ASP G C   1 
ATOM   7239  O  O   . ASP G  1 96  ? 21.256  151.537 71.973  1.00 21.06 ? 96   ASP G O   1 
ATOM   7240  C  CB  . ASP G  1 96  ? 23.065  150.091 73.912  1.00 22.60 ? 96   ASP G CB  1 
ATOM   7241  C  CG  . ASP G  1 96  ? 24.134  149.170 74.502  1.00 24.56 ? 96   ASP G CG  1 
ATOM   7242  O  OD1 . ASP G  1 96  ? 24.733  149.538 75.529  1.00 29.38 ? 96   ASP G OD1 1 
ATOM   7243  O  OD2 . ASP G  1 96  ? 24.428  148.047 74.012  1.00 27.14 ? 96   ASP G OD2 1 
ATOM   7244  N  N   . VAL G  1 97  ? 20.542  149.431 71.607  1.00 21.20 ? 97   VAL G N   1 
ATOM   7245  C  CA  . VAL G  1 97  ? 19.272  149.828 71.038  1.00 22.14 ? 97   VAL G CA  1 
ATOM   7246  C  C   . VAL G  1 97  ? 18.147  149.815 72.056  1.00 22.35 ? 97   VAL G C   1 
ATOM   7247  O  O   . VAL G  1 97  ? 17.906  148.810 72.737  1.00 22.57 ? 97   VAL G O   1 
ATOM   7248  C  CB  . VAL G  1 97  ? 18.877  148.866 69.901  1.00 21.45 ? 97   VAL G CB  1 
ATOM   7249  C  CG1 . VAL G  1 97  ? 17.603  149.333 69.228  1.00 23.08 ? 97   VAL G CG1 1 
ATOM   7250  C  CG2 . VAL G  1 97  ? 19.977  148.788 68.903  1.00 22.28 ? 97   VAL G CG2 1 
ATOM   7251  N  N   . SER G  1 98  ? 17.437  150.928 72.123  1.00 23.14 ? 98   SER G N   1 
ATOM   7252  C  CA  . SER G  1 98  ? 16.286  151.059 73.005  1.00 23.98 ? 98   SER G CA  1 
ATOM   7253  C  C   . SER G  1 98  ? 15.346  152.072 72.368  1.00 24.56 ? 98   SER G C   1 
ATOM   7254  O  O   . SER G  1 98  ? 15.504  153.282 72.526  1.00 24.39 ? 98   SER G O   1 
ATOM   7255  C  CB  . SER G  1 98  ? 16.701  151.532 74.399  1.00 24.52 ? 98   SER G CB  1 
ATOM   7256  O  OG  . SER G  1 98  ? 15.560  151.562 75.244  1.00 24.11 ? 98   SER G OG  1 
ATOM   7257  N  N   . ILE G  1 99  ? 14.355  151.549 71.673  1.00 24.73 ? 99   ILE G N   1 
ATOM   7258  C  CA  . ILE G  1 99  ? 13.437  152.325 70.861  1.00 25.06 ? 99   ILE G CA  1 
ATOM   7259  C  C   . ILE G  1 99  ? 12.005  152.040 71.260  1.00 25.21 ? 99   ILE G C   1 
ATOM   7260  O  O   . ILE G  1 99  ? 11.697  150.962 71.786  1.00 25.37 ? 99   ILE G O   1 
ATOM   7261  C  CB  . ILE G  1 99  ? 13.618  151.857 69.386  1.00 24.77 ? 99   ILE G CB  1 
ATOM   7262  C  CG1 . ILE G  1 99  ? 14.875  152.481 68.779  1.00 25.31 ? 99   ILE G CG1 1 
ATOM   7263  C  CG2 . ILE G  1 99  ? 12.378  152.145 68.542  1.00 25.75 ? 99   ILE G CG2 1 
ATOM   7264  C  CD1 . ILE G  1 99  ? 15.268  151.891 67.417  1.00 22.61 ? 99   ILE G CD1 1 
ATOM   7265  N  N   . GLU G  1 100 ? 11.121  152.992 70.981  1.00 25.40 ? 100  GLU G N   1 
ATOM   7266  C  CA  . GLU G  1 100 ? 9.687   152.784 71.177  1.00 25.53 ? 100  GLU G CA  1 
ATOM   7267  C  C   . GLU G  1 100 ? 8.955   153.219 69.912  1.00 25.13 ? 100  GLU G C   1 
ATOM   7268  O  O   . GLU G  1 100 ? 9.237   154.271 69.331  1.00 24.55 ? 100  GLU G O   1 
ATOM   7269  C  CB  . GLU G  1 100 ? 9.164   153.498 72.423  1.00 26.41 ? 100  GLU G CB  1 
ATOM   7270  C  CG  . GLU G  1 100 ? 8.188   152.644 73.228  1.00 28.18 ? 100  GLU G CG  1 
ATOM   7271  C  CD  . GLU G  1 100 ? 8.492   152.673 74.717  1.00 31.59 ? 100  GLU G CD  1 
ATOM   7272  O  OE1 . GLU G  1 100 ? 9.661   152.406 75.094  1.00 33.16 ? 100  GLU G OE1 1 
ATOM   7273  O  OE2 . GLU G  1 100 ? 7.565   152.962 75.506  1.00 31.21 ? 100  GLU G OE2 1 
ATOM   7274  N  N   . ASP G  1 101 ? 8.051   152.368 69.452  1.00 25.08 ? 101  ASP G N   1 
ATOM   7275  C  CA  . ASP G  1 101 ? 7.336   152.641 68.223  1.00 25.03 ? 101  ASP G CA  1 
ATOM   7276  C  C   . ASP G  1 101 ? 5.926   152.102 68.283  1.00 24.81 ? 101  ASP G C   1 
ATOM   7277  O  O   . ASP G  1 101 ? 5.706   150.937 68.637  1.00 25.01 ? 101  ASP G O   1 
ATOM   7278  C  CB  . ASP G  1 101 ? 8.077   152.022 67.041  1.00 25.27 ? 101  ASP G CB  1 
ATOM   7279  C  CG  . ASP G  1 101 ? 7.669   152.635 65.727  1.00 25.84 ? 101  ASP G CG  1 
ATOM   7280  O  OD1 . ASP G  1 101 ? 8.199   153.716 65.394  1.00 27.21 ? 101  ASP G OD1 1 
ATOM   7281  O  OD2 . ASP G  1 101 ? 6.812   152.128 64.976  1.00 25.62 ? 101  ASP G OD2 1 
ATOM   7282  N  N   . SER G  1 102 ? 4.978   152.955 67.911  1.00 24.11 ? 102  SER G N   1 
ATOM   7283  C  CA  . SER G  1 102 ? 3.564   152.619 67.936  1.00 24.01 ? 102  SER G CA  1 
ATOM   7284  C  C   . SER G  1 102 ? 3.011   152.425 66.550  1.00 23.70 ? 102  SER G C   1 
ATOM   7285  O  O   . SER G  1 102 ? 1.794   152.380 66.367  1.00 23.98 ? 102  SER G O   1 
ATOM   7286  C  CB  . SER G  1 102 ? 2.769   153.740 68.603  1.00 23.65 ? 102  SER G CB  1 
ATOM   7287  O  OG  . SER G  1 102 ? 3.346   154.065 69.842  1.00 24.59 ? 102  SER G OG  1 
ATOM   7288  N  N   . VAL G  1 103 ? 3.881   152.344 65.556  1.00 22.60 ? 103  VAL G N   1 
ATOM   7289  C  CA  . VAL G  1 103 ? 3.385   152.092 64.216  1.00 21.94 ? 103  VAL G CA  1 
ATOM   7290  C  C   . VAL G  1 103 ? 3.596   150.610 63.936  1.00 21.68 ? 103  VAL G C   1 
ATOM   7291  O  O   . VAL G  1 103 ? 2.650   149.893 63.636  1.00 21.31 ? 103  VAL G O   1 
ATOM   7292  C  CB  . VAL G  1 103 ? 4.047   152.999 63.173  1.00 21.96 ? 103  VAL G CB  1 
ATOM   7293  C  CG1 . VAL G  1 103 ? 3.521   152.682 61.790  1.00 21.83 ? 103  VAL G CG1 1 
ATOM   7294  C  CG2 . VAL G  1 103 ? 3.796   154.476 63.522  1.00 22.93 ? 103  VAL G CG2 1 
ATOM   7295  N  N   . ILE G  1 104 ? 4.820   150.136 64.090  1.00 21.42 ? 104  ILE G N   1 
ATOM   7296  C  CA  . ILE G  1 104 ? 5.036   148.704 63.910  1.00 21.12 ? 104  ILE G CA  1 
ATOM   7297  C  C   . ILE G  1 104 ? 4.211   147.983 64.971  1.00 21.28 ? 104  ILE G C   1 
ATOM   7298  O  O   . ILE G  1 104 ? 3.856   148.573 65.994  1.00 20.67 ? 104  ILE G O   1 
ATOM   7299  C  CB  . ILE G  1 104 ? 6.512   148.322 64.050  1.00 21.61 ? 104  ILE G CB  1 
ATOM   7300  C  CG1 . ILE G  1 104 ? 7.064   148.725 65.414  1.00 20.78 ? 104  ILE G CG1 1 
ATOM   7301  C  CG2 . ILE G  1 104 ? 7.360   148.958 62.953  1.00 21.80 ? 104  ILE G CG2 1 
ATOM   7302  C  CD1 . ILE G  1 104 ? 8.517   148.262 65.590  1.00 20.02 ? 104  ILE G CD1 1 
ATOM   7303  N  N   . SER G  1 105 ? 3.893   146.715 64.714  1.00 21.14 ? 105  SER G N   1 
ATOM   7304  C  CA  . SER G  1 105 ? 3.146   145.908 65.669  1.00 21.52 ? 105  SER G CA  1 
ATOM   7305  C  C   . SER G  1 105 ? 3.587   144.467 65.547  1.00 22.03 ? 105  SER G C   1 
ATOM   7306  O  O   . SER G  1 105 ? 4.252   144.111 64.589  1.00 21.69 ? 105  SER G O   1 
ATOM   7307  C  CB  . SER G  1 105 ? 1.640   146.022 65.412  1.00 21.47 ? 105  SER G CB  1 
ATOM   7308  O  OG  . SER G  1 105 ? 0.905   145.219 66.320  1.00 21.31 ? 105  SER G OG  1 
ATOM   7309  N  N   . LEU G  1 106 ? 3.219   143.647 66.520  1.00 22.99 ? 106  LEU G N   1 
ATOM   7310  C  CA  . LEU G  1 106 ? 3.528   142.225 66.473  1.00 23.88 ? 106  LEU G CA  1 
ATOM   7311  C  C   . LEU G  1 106 ? 2.243   141.440 66.149  1.00 24.65 ? 106  LEU G C   1 
ATOM   7312  O  O   . LEU G  1 106 ? 2.168   140.218 66.293  1.00 25.77 ? 106  LEU G O   1 
ATOM   7313  C  CB  . LEU G  1 106 ? 4.186   141.783 67.780  1.00 23.40 ? 106  LEU G CB  1 
ATOM   7314  C  CG  . LEU G  1 106 ? 5.487   142.544 68.073  1.00 24.50 ? 106  LEU G CG  1 
ATOM   7315  C  CD1 . LEU G  1 106 ? 6.247   141.973 69.259  1.00 24.59 ? 106  LEU G CD1 1 
ATOM   7316  C  CD2 . LEU G  1 106 ? 6.384   142.517 66.840  1.00 24.19 ? 106  LEU G CD2 1 
ATOM   7317  N  N   . SER G  1 107 ? 1.247   142.165 65.666  1.00 25.39 ? 107  SER G N   1 
ATOM   7318  C  CA  . SER G  1 107 ? -0.028  141.576 65.249  1.00 25.75 ? 107  SER G CA  1 
ATOM   7319  C  C   . SER G  1 107 ? -0.786  142.572 64.374  1.00 25.46 ? 107  SER G C   1 
ATOM   7320  O  O   . SER G  1 107 ? -0.393  143.729 64.284  1.00 25.38 ? 107  SER G O   1 
ATOM   7321  C  CB  . SER G  1 107 ? -0.863  141.156 66.462  1.00 25.89 ? 107  SER G CB  1 
ATOM   7322  O  OG  . SER G  1 107 ? -1.339  142.277 67.178  1.00 27.12 ? 107  SER G OG  1 
ATOM   7323  N  N   . GLY G  1 108 ? -1.851  142.116 63.710  1.00 25.61 ? 108  GLY G N   1 
ATOM   7324  C  CA  . GLY G  1 108 ? -2.683  142.984 62.879  1.00 25.65 ? 108  GLY G CA  1 
ATOM   7325  C  C   . GLY G  1 108 ? -2.059  143.505 61.589  1.00 25.81 ? 108  GLY G C   1 
ATOM   7326  O  O   . GLY G  1 108 ? -1.046  142.986 61.126  1.00 25.65 ? 108  GLY G O   1 
ATOM   7327  N  N   . ASP G  1 109 ? -2.644  144.564 61.032  1.00 26.17 ? 109  ASP G N   1 
ATOM   7328  C  CA  . ASP G  1 109 ? -2.181  145.155 59.773  1.00 26.69 ? 109  ASP G CA  1 
ATOM   7329  C  C   . ASP G  1 109 ? -0.705  145.559 59.738  1.00 26.47 ? 109  ASP G C   1 
ATOM   7330  O  O   . ASP G  1 109 ? -0.091  145.571 58.666  1.00 27.06 ? 109  ASP G O   1 
ATOM   7331  C  CB  . ASP G  1 109 ? -3.014  146.385 59.426  1.00 27.34 ? 109  ASP G CB  1 
ATOM   7332  C  CG  . ASP G  1 109 ? -4.077  146.098 58.398  1.00 29.35 ? 109  ASP G CG  1 
ATOM   7333  O  OD1 . ASP G  1 109 ? -5.257  146.372 58.699  1.00 30.63 ? 109  ASP G OD1 1 
ATOM   7334  O  OD2 . ASP G  1 109 ? -3.832  145.609 57.268  1.00 32.08 ? 109  ASP G OD2 1 
ATOM   7335  N  N   . HIS G  1 110 ? -0.143  145.893 60.893  1.00 25.50 ? 110  HIS G N   1 
ATOM   7336  C  CA  . HIS G  1 110 ? 1.245   146.347 60.943  1.00 25.18 ? 110  HIS G CA  1 
ATOM   7337  C  C   . HIS G  1 110 ? 2.220   145.318 61.494  1.00 24.77 ? 110  HIS G C   1 
ATOM   7338  O  O   . HIS G  1 110 ? 3.289   145.665 62.001  1.00 24.34 ? 110  HIS G O   1 
ATOM   7339  C  CB  . HIS G  1 110 ? 1.338   147.649 61.731  1.00 25.52 ? 110  HIS G CB  1 
ATOM   7340  C  CG  . HIS G  1 110 ? 0.590   148.771 61.094  1.00 26.47 ? 110  HIS G CG  1 
ATOM   7341  N  ND1 . HIS G  1 110 ? 0.306   149.949 61.751  1.00 27.09 ? 110  HIS G ND1 1 
ATOM   7342  C  CD2 . HIS G  1 110 ? 0.068   148.894 59.852  1.00 26.70 ? 110  HIS G CD2 1 
ATOM   7343  C  CE1 . HIS G  1 110 ? -0.360  150.749 60.938  1.00 28.62 ? 110  HIS G CE1 1 
ATOM   7344  N  NE2 . HIS G  1 110 ? -0.518  150.131 59.780  1.00 27.47 ? 110  HIS G NE2 1 
ATOM   7345  N  N   . CYS G  1 111 ? 1.861   144.047 61.360  1.00 24.09 ? 111  CYS G N   1 
ATOM   7346  C  CA  . CYS G  1 111 ? 2.690   142.977 61.878  1.00 23.68 ? 111  CYS G CA  1 
ATOM   7347  C  C   . CYS G  1 111 ? 4.040   142.929 61.162  1.00 22.41 ? 111  CYS G C   1 
ATOM   7348  O  O   . CYS G  1 111 ? 4.098   142.953 59.929  1.00 21.57 ? 111  CYS G O   1 
ATOM   7349  C  CB  . CYS G  1 111 ? 1.955   141.644 61.737  1.00 24.04 ? 111  CYS G CB  1 
ATOM   7350  S  SG  . CYS G  1 111 ? 2.446   140.431 62.962  1.00 29.70 ? 111  CYS G SG  1 
ATOM   7351  N  N   . ILE G  1 112 ? 5.124   142.871 61.934  1.00 20.77 ? 112  ILE G N   1 
ATOM   7352  C  CA  . ILE G  1 112 ? 6.452   142.750 61.343  1.00 20.29 ? 112  ILE G CA  1 
ATOM   7353  C  C   . ILE G  1 112 ? 7.029   141.357 61.547  1.00 20.07 ? 112  ILE G C   1 
ATOM   7354  O  O   . ILE G  1 112 ? 8.174   141.094 61.158  1.00 19.37 ? 112  ILE G O   1 
ATOM   7355  C  CB  . ILE G  1 112 ? 7.428   143.792 61.923  1.00 20.24 ? 112  ILE G CB  1 
ATOM   7356  C  CG1 . ILE G  1 112 ? 7.667   143.528 63.412  1.00 19.98 ? 112  ILE G CG1 1 
ATOM   7357  C  CG2 . ILE G  1 112 ? 6.906   145.204 61.657  1.00 20.26 ? 112  ILE G CG2 1 
ATOM   7358  C  CD1 . ILE G  1 112 ? 8.512   144.601 64.092  1.00 21.20 ? 112  ILE G CD1 1 
ATOM   7359  N  N   . ILE G  1 113 ? 6.260   140.462 62.161  1.00 19.84 ? 113  ILE G N   1 
ATOM   7360  C  CA  . ILE G  1 113 ? 6.748   139.090 62.306  1.00 19.88 ? 113  ILE G CA  1 
ATOM   7361  C  C   . ILE G  1 113 ? 6.951   138.481 60.912  1.00 19.66 ? 113  ILE G C   1 
ATOM   7362  O  O   . ILE G  1 113 ? 6.135   138.676 60.007  1.00 18.08 ? 113  ILE G O   1 
ATOM   7363  C  CB  . ILE G  1 113 ? 5.776   138.221 63.113  1.00 20.42 ? 113  ILE G CB  1 
ATOM   7364  C  CG1 . ILE G  1 113 ? 5.467   138.857 64.467  1.00 21.25 ? 113  ILE G CG1 1 
ATOM   7365  C  CG2 . ILE G  1 113 ? 6.369   136.847 63.350  1.00 19.71 ? 113  ILE G CG2 1 
ATOM   7366  C  CD1 . ILE G  1 113 ? 6.500   138.540 65.496  1.00 23.57 ? 113  ILE G CD1 1 
ATOM   7367  N  N   . GLY G  1 114 ? 8.054   137.769 60.717  1.00 18.37 ? 114  GLY G N   1 
ATOM   7368  C  CA  . GLY G  1 114 ? 8.262   137.134 59.429  1.00 18.32 ? 114  GLY G CA  1 
ATOM   7369  C  C   . GLY G  1 114 ? 8.869   138.092 58.435  1.00 17.93 ? 114  GLY G C   1 
ATOM   7370  O  O   . GLY G  1 114 ? 9.130   137.752 57.286  1.00 18.56 ? 114  GLY G O   1 
ATOM   7371  N  N   . ARG G  1 115 ? 9.114   139.313 58.875  1.00 17.23 ? 115  ARG G N   1 
ATOM   7372  C  CA  . ARG G  1 115 ? 9.776   140.248 57.987  1.00 17.01 ? 115  ARG G CA  1 
ATOM   7373  C  C   . ARG G  1 115 ? 11.265  140.363 58.394  1.00 16.49 ? 115  ARG G C   1 
ATOM   7374  O  O   . ARG G  1 115 ? 11.711  139.623 59.284  1.00 17.53 ? 115  ARG G O   1 
ATOM   7375  C  CB  . ARG G  1 115 ? 9.009   141.563 57.945  1.00 17.32 ? 115  ARG G CB  1 
ATOM   7376  C  CG  . ARG G  1 115 ? 7.563   141.348 57.413  1.00 17.37 ? 115  ARG G CG  1 
ATOM   7377  C  CD  . ARG G  1 115 ? 6.753   142.644 57.229  1.00 18.41 ? 115  ARG G CD  1 
ATOM   7378  N  NE  . ARG G  1 115 ? 5.336   142.341 57.030  1.00 19.73 ? 115  ARG G NE  1 
ATOM   7379  C  CZ  . ARG G  1 115 ? 4.795   142.021 55.865  1.00 19.54 ? 115  ARG G CZ  1 
ATOM   7380  N  NH1 . ARG G  1 115 ? 5.544   141.971 54.771  1.00 18.72 ? 115  ARG G NH1 1 
ATOM   7381  N  NH2 . ARG G  1 115 ? 3.490   141.764 55.790  1.00 21.49 ? 115  ARG G NH2 1 
ATOM   7382  N  N   . THR G  1 116 ? 12.039  141.234 57.736  1.00 16.03 ? 116  THR G N   1 
ATOM   7383  C  CA  . THR G  1 116 ? 13.499  141.337 58.019  1.00 15.23 ? 116  THR G CA  1 
ATOM   7384  C  C   . THR G  1 116 ? 13.955  142.642 58.646  1.00 15.22 ? 116  THR G C   1 
ATOM   7385  O  O   . THR G  1 116 ? 13.721  143.706 58.090  1.00 13.85 ? 116  THR G O   1 
ATOM   7386  C  CB  . THR G  1 116 ? 14.299  141.198 56.748  1.00 15.21 ? 116  THR G CB  1 
ATOM   7387  O  OG1 . THR G  1 116 ? 14.082  139.897 56.191  1.00 16.40 ? 116  THR G OG1 1 
ATOM   7388  C  CG2 . THR G  1 116 ? 15.847  141.219 57.057  1.00 14.76 ? 116  THR G CG2 1 
ATOM   7389  N  N   . LEU G  1 117 ? 14.674  142.553 59.764  1.00 14.88 ? 117  LEU G N   1 
ATOM   7390  C  CA  . LEU G  1 117 ? 15.209  143.750 60.384  1.00 15.58 ? 117  LEU G CA  1 
ATOM   7391  C  C   . LEU G  1 117 ? 16.581  143.983 59.764  1.00 16.17 ? 117  LEU G C   1 
ATOM   7392  O  O   . LEU G  1 117 ? 17.345  143.034 59.558  1.00 17.33 ? 117  LEU G O   1 
ATOM   7393  C  CB  . LEU G  1 117 ? 15.323  143.552 61.889  1.00 15.41 ? 117  LEU G CB  1 
ATOM   7394  C  CG  . LEU G  1 117 ? 15.891  144.749 62.649  1.00 14.68 ? 117  LEU G CG  1 
ATOM   7395  C  CD1 . LEU G  1 117 ? 14.892  145.875 62.657  1.00 18.34 ? 117  LEU G CD1 1 
ATOM   7396  C  CD2 . LEU G  1 117 ? 16.213  144.326 64.053  1.00 16.19 ? 117  LEU G CD2 1 
ATOM   7397  N  N   . VAL G  1 118 ? 16.899  145.228 59.439  1.00 16.14 ? 118  VAL G N   1 
ATOM   7398  C  CA  . VAL G  1 118 ? 18.160  145.513 58.770  1.00 16.06 ? 118  VAL G CA  1 
ATOM   7399  C  C   . VAL G  1 118 ? 18.908  146.705 59.410  1.00 16.24 ? 118  VAL G C   1 
ATOM   7400  O  O   . VAL G  1 118 ? 18.294  147.726 59.710  1.00 17.49 ? 118  VAL G O   1 
ATOM   7401  C  CB  . VAL G  1 118 ? 17.898  145.868 57.298  1.00 15.97 ? 118  VAL G CB  1 
ATOM   7402  C  CG1 . VAL G  1 118 ? 19.206  146.241 56.614  1.00 16.24 ? 118  VAL G CG1 1 
ATOM   7403  C  CG2 . VAL G  1 118 ? 17.199  144.697 56.578  1.00 13.15 ? 118  VAL G CG2 1 
ATOM   7404  N  N   . VAL G  1 119 ? 20.220  146.558 59.626  1.00 15.97 ? 119  VAL G N   1 
ATOM   7405  C  CA  . VAL G  1 119 ? 21.045  147.667 60.125  1.00 15.96 ? 119  VAL G CA  1 
ATOM   7406  C  C   . VAL G  1 119 ? 21.961  148.048 58.964  1.00 17.14 ? 119  VAL G C   1 
ATOM   7407  O  O   . VAL G  1 119 ? 22.540  147.176 58.300  1.00 16.98 ? 119  VAL G O   1 
ATOM   7408  C  CB  . VAL G  1 119 ? 21.792  147.348 61.462  1.00 15.27 ? 119  VAL G CB  1 
ATOM   7409  C  CG1 . VAL G  1 119 ? 22.830  146.216 61.307  1.00 16.13 ? 119  VAL G CG1 1 
ATOM   7410  C  CG2 . VAL G  1 119 ? 22.468  148.634 62.081  1.00 15.07 ? 119  VAL G CG2 1 
ATOM   7411  N  N   . HIS G  1 120 ? 22.063  149.353 58.715  1.00 16.67 ? 120  HIS G N   1 
ATOM   7412  C  CA  . HIS G  1 120 ? 22.711  149.886 57.523  1.00 17.73 ? 120  HIS G CA  1 
ATOM   7413  C  C   . HIS G  1 120 ? 24.076  150.519 57.738  1.00 17.81 ? 120  HIS G C   1 
ATOM   7414  O  O   . HIS G  1 120 ? 24.491  150.798 58.875  1.00 16.96 ? 120  HIS G O   1 
ATOM   7415  C  CB  . HIS G  1 120 ? 21.826  150.966 56.888  1.00 17.69 ? 120  HIS G CB  1 
ATOM   7416  C  CG  . HIS G  1 120 ? 20.601  150.431 56.210  1.00 17.89 ? 120  HIS G CG  1 
ATOM   7417  N  ND1 . HIS G  1 120 ? 20.572  150.130 54.864  1.00 18.59 ? 120  HIS G ND1 1 
ATOM   7418  C  CD2 . HIS G  1 120 ? 19.344  150.210 56.671  1.00 18.17 ? 120  HIS G CD2 1 
ATOM   7419  C  CE1 . HIS G  1 120 ? 19.363  149.711 54.532  1.00 18.15 ? 120  HIS G CE1 1 
ATOM   7420  N  NE2 . HIS G  1 120 ? 18.601  149.741 55.611  1.00 18.64 ? 120  HIS G NE2 1 
ATOM   7421  N  N   . GLU G  1 121 ? 24.705  150.829 56.605  1.00 17.59 ? 121  GLU G N   1 
ATOM   7422  C  CA  . GLU G  1 121 ? 26.064  151.341 56.527  1.00 18.27 ? 121  GLU G CA  1 
ATOM   7423  C  C   . GLU G  1 121 ? 26.159  152.766 57.034  1.00 18.32 ? 121  GLU G C   1 
ATOM   7424  O  O   . GLU G  1 121 ? 27.059  153.113 57.816  1.00 16.96 ? 121  GLU G O   1 
ATOM   7425  C  CB  . GLU G  1 121 ? 26.487  151.307 55.057  1.00 19.01 ? 121  GLU G CB  1 
ATOM   7426  C  CG  . GLU G  1 121 ? 27.879  151.823 54.756  1.00 22.75 ? 121  GLU G CG  1 
ATOM   7427  C  CD  . GLU G  1 121 ? 28.080  152.067 53.263  1.00 26.41 ? 121  GLU G CD  1 
ATOM   7428  O  OE1 . GLU G  1 121 ? 29.218  152.422 52.859  1.00 27.07 ? 121  GLU G OE1 1 
ATOM   7429  O  OE2 . GLU G  1 121 ? 27.094  151.911 52.493  1.00 24.51 ? 121  GLU G OE2 1 
ATOM   7430  N  N   . LYS G  1 122 ? 25.204  153.573 56.590  1.00 18.39 ? 122  LYS G N   1 
ATOM   7431  C  CA  . LYS G  1 122 ? 25.184  154.997 56.929  1.00 19.83 ? 122  LYS G CA  1 
ATOM   7432  C  C   . LYS G  1 122 ? 23.979  155.437 57.744  1.00 19.43 ? 122  LYS G C   1 
ATOM   7433  O  O   . LYS G  1 122 ? 23.062  154.658 58.021  1.00 18.27 ? 122  LYS G O   1 
ATOM   7434  C  CB  . LYS G  1 122 ? 25.200  155.837 55.637  1.00 20.77 ? 122  LYS G CB  1 
ATOM   7435  C  CG  . LYS G  1 122 ? 26.396  155.543 54.728  1.00 24.09 ? 122  LYS G CG  1 
ATOM   7436  C  CD  . LYS G  1 122 ? 26.370  156.408 53.465  1.00 28.19 ? 122  LYS G CD  1 
ATOM   7437  C  CE  . LYS G  1 122 ? 26.993  155.660 52.287  1.00 31.36 ? 122  LYS G CE  1 
ATOM   7438  N  NZ  . LYS G  1 122 ? 26.756  156.325 50.956  1.00 32.85 ? 122  LYS G NZ  1 
ATOM   7439  N  N   . ALA G  1 123 ? 23.985  156.721 58.097  1.00 17.87 ? 123  ALA G N   1 
ATOM   7440  C  CA  . ALA G  1 123 ? 22.845  157.311 58.777  1.00 19.02 ? 123  ALA G CA  1 
ATOM   7441  C  C   . ALA G  1 123 ? 21.683  157.404 57.813  1.00 18.91 ? 123  ALA G C   1 
ATOM   7442  O  O   . ALA G  1 123 ? 21.868  157.596 56.618  1.00 20.20 ? 123  ALA G O   1 
ATOM   7443  C  CB  . ALA G  1 123 ? 23.181  158.734 59.313  1.00 17.37 ? 123  ALA G CB  1 
ATOM   7444  N  N   . ASP G  1 124 ? 20.483  157.237 58.349  1.00 19.70 ? 124  ASP G N   1 
ATOM   7445  C  CA  . ASP G  1 124 ? 19.244  157.415 57.614  1.00 19.72 ? 124  ASP G CA  1 
ATOM   7446  C  C   . ASP G  1 124 ? 18.955  158.914 57.757  1.00 20.26 ? 124  ASP G C   1 
ATOM   7447  O  O   . ASP G  1 124 ? 18.959  159.427 58.873  1.00 19.48 ? 124  ASP G O   1 
ATOM   7448  C  CB  . ASP G  1 124 ? 18.168  156.628 58.350  1.00 19.58 ? 124  ASP G CB  1 
ATOM   7449  C  CG  . ASP G  1 124 ? 16.809  156.703 57.697  1.00 20.14 ? 124  ASP G CG  1 
ATOM   7450  O  OD1 . ASP G  1 124 ? 16.489  157.707 57.017  1.00 20.10 ? 124  ASP G OD1 1 
ATOM   7451  O  OD2 . ASP G  1 124 ? 15.985  155.773 57.842  1.00 21.27 ? 124  ASP G OD2 1 
ATOM   7452  N  N   . ASP G  1 125 ? 18.714  159.605 56.646  1.00 20.42 ? 125  ASP G N   1 
ATOM   7453  C  CA  . ASP G  1 125 ? 18.420  161.023 56.702  1.00 21.73 ? 125  ASP G CA  1 
ATOM   7454  C  C   . ASP G  1 125 ? 16.979  161.358 57.075  1.00 21.84 ? 125  ASP G C   1 
ATOM   7455  O  O   . ASP G  1 125 ? 16.588  162.519 57.021  1.00 21.81 ? 125  ASP G O   1 
ATOM   7456  C  CB  . ASP G  1 125 ? 18.816  161.739 55.412  1.00 22.26 ? 125  ASP G CB  1 
ATOM   7457  C  CG  . ASP G  1 125 ? 18.036  161.264 54.212  1.00 22.64 ? 125  ASP G CG  1 
ATOM   7458  O  OD1 . ASP G  1 125 ? 16.856  160.843 54.336  1.00 25.27 ? 125  ASP G OD1 1 
ATOM   7459  O  OD2 . ASP G  1 125 ? 18.543  161.280 53.075  1.00 24.08 ? 125  ASP G OD2 1 
ATOM   7460  N  N   . LEU G  1 126 ? 16.221  160.344 57.469  1.00 21.06 ? 126  LEU G N   1 
ATOM   7461  C  CA  . LEU G  1 126 ? 14.875  160.517 57.998  1.00 21.13 ? 126  LEU G CA  1 
ATOM   7462  C  C   . LEU G  1 126 ? 13.892  161.002 56.957  1.00 22.00 ? 126  LEU G C   1 
ATOM   7463  O  O   . LEU G  1 126 ? 12.824  161.507 57.295  1.00 22.41 ? 126  LEU G O   1 
ATOM   7464  C  CB  . LEU G  1 126 ? 14.886  161.439 59.218  1.00 21.14 ? 126  LEU G CB  1 
ATOM   7465  C  CG  . LEU G  1 126 ? 15.930  161.012 60.246  1.00 20.39 ? 126  LEU G CG  1 
ATOM   7466  C  CD1 . LEU G  1 126 ? 15.837  161.808 61.543  1.00 21.66 ? 126  LEU G CD1 1 
ATOM   7467  C  CD2 . LEU G  1 126 ? 15.801  159.501 60.502  1.00 19.66 ? 126  LEU G CD2 1 
ATOM   7468  N  N   . GLY G  1 127 ? 14.251  160.845 55.687  1.00 22.39 ? 127  GLY G N   1 
ATOM   7469  C  CA  . GLY G  1 127 ? 13.377  161.251 54.600  1.00 23.56 ? 127  GLY G CA  1 
ATOM   7470  C  C   . GLY G  1 127 ? 13.352  162.748 54.366  1.00 24.83 ? 127  GLY G C   1 
ATOM   7471  O  O   . GLY G  1 127 ? 12.387  163.276 53.803  1.00 24.24 ? 127  GLY G O   1 
ATOM   7472  N  N   . LYS G  1 128 ? 14.415  163.431 54.781  1.00 25.74 ? 128  LYS G N   1 
ATOM   7473  C  CA  . LYS G  1 128 ? 14.481  164.879 54.613  1.00 27.31 ? 128  LYS G CA  1 
ATOM   7474  C  C   . LYS G  1 128 ? 15.767  165.326 53.933  1.00 28.34 ? 128  LYS G C   1 
ATOM   7475  O  O   . LYS G  1 128 ? 16.246  166.425 54.183  1.00 27.70 ? 128  LYS G O   1 
ATOM   7476  C  CB  . LYS G  1 128 ? 14.385  165.565 55.976  1.00 27.34 ? 128  LYS G CB  1 
ATOM   7477  C  CG  . LYS G  1 128 ? 13.473  164.861 56.955  1.00 28.68 ? 128  LYS G CG  1 
ATOM   7478  C  CD  . LYS G  1 128 ? 12.978  165.771 58.067  1.00 31.27 ? 128  LYS G CD  1 
ATOM   7479  C  CE  . LYS G  1 128 ? 12.620  164.957 59.309  1.00 32.38 ? 128  LYS G CE  1 
ATOM   7480  N  NZ  . LYS G  1 128 ? 12.233  163.546 58.970  1.00 31.80 ? 128  LYS G NZ  1 
ATOM   7481  N  N   . GLY G  1 129 ? 16.338  164.484 53.082  1.00 29.93 ? 129  GLY G N   1 
ATOM   7482  C  CA  . GLY G  1 129 ? 17.598  164.826 52.446  1.00 32.41 ? 129  GLY G CA  1 
ATOM   7483  C  C   . GLY G  1 129 ? 17.456  165.448 51.072  1.00 34.30 ? 129  GLY G C   1 
ATOM   7484  O  O   . GLY G  1 129 ? 18.460  165.708 50.391  1.00 34.27 ? 129  GLY G O   1 
ATOM   7485  N  N   . GLY G  1 130 ? 16.209  165.717 50.684  1.00 35.82 ? 130  GLY G N   1 
ATOM   7486  C  CA  . GLY G  1 130 ? 15.908  166.197 49.352  1.00 37.18 ? 130  GLY G CA  1 
ATOM   7487  C  C   . GLY G  1 130 ? 15.784  164.941 48.513  1.00 38.55 ? 130  GLY G C   1 
ATOM   7488  O  O   . GLY G  1 130 ? 14.896  164.125 48.744  1.00 38.56 ? 130  GLY G O   1 
ATOM   7489  N  N   . ASN G  1 131 ? 16.709  164.774 47.573  1.00 39.50 ? 131  ASN G N   1 
ATOM   7490  C  CA  . ASN G  1 131 ? 16.771  163.640 46.638  1.00 39.52 ? 131  ASN G CA  1 
ATOM   7491  C  C   . ASN G  1 131 ? 15.672  162.543 46.682  1.00 39.74 ? 131  ASN G C   1 
ATOM   7492  O  O   . ASN G  1 131 ? 15.022  162.301 47.705  1.00 39.87 ? 131  ASN G O   1 
ATOM   7493  C  CB  . ASN G  1 131 ? 18.187  163.035 46.656  1.00 40.15 ? 131  ASN G CB  1 
ATOM   7494  C  CG  . ASN G  1 131 ? 18.349  161.936 47.696  1.00 41.54 ? 131  ASN G CG  1 
ATOM   7495  O  OD1 . ASN G  1 131 ? 17.450  161.681 48.495  1.00 42.09 ? 131  ASN G OD1 1 
ATOM   7496  N  ND2 . ASN G  1 131 ? 19.502  161.267 47.677  1.00 44.14 ? 131  ASN G ND2 1 
ATOM   7497  N  N   . GLU G  1 132 ? 15.478  161.869 45.555  1.00 38.96 ? 132  GLU G N   1 
ATOM   7498  C  CA  . GLU G  1 132 ? 14.460  160.834 45.470  1.00 38.92 ? 132  GLU G CA  1 
ATOM   7499  C  C   . GLU G  1 132 ? 14.763  159.689 46.427  1.00 37.48 ? 132  GLU G C   1 
ATOM   7500  O  O   . GLU G  1 132 ? 13.885  159.215 47.145  1.00 37.31 ? 132  GLU G O   1 
ATOM   7501  C  CB  . GLU G  1 132 ? 14.371  160.312 44.044  1.00 39.38 ? 132  GLU G CB  1 
ATOM   7502  C  CG  . GLU G  1 132 ? 12.951  160.087 43.568  1.00 43.12 ? 132  GLU G CG  1 
ATOM   7503  C  CD  . GLU G  1 132 ? 12.743  160.642 42.173  1.00 47.91 ? 132  GLU G CD  1 
ATOM   7504  O  OE1 . GLU G  1 132 ? 11.774  161.414 41.961  1.00 48.80 ? 132  GLU G OE1 1 
ATOM   7505  O  OE2 . GLU G  1 132 ? 13.572  160.321 41.293  1.00 49.95 ? 132  GLU G OE2 1 
ATOM   7506  N  N   . GLU G  1 133 ? 16.018  159.262 46.445  1.00 36.03 ? 133  GLU G N   1 
ATOM   7507  C  CA  . GLU G  1 133 ? 16.425  158.169 47.313  1.00 34.86 ? 133  GLU G CA  1 
ATOM   7508  C  C   . GLU G  1 133 ? 15.962  158.411 48.750  1.00 33.51 ? 133  GLU G C   1 
ATOM   7509  O  O   . GLU G  1 133 ? 15.508  157.497 49.435  1.00 33.40 ? 133  GLU G O   1 
ATOM   7510  C  CB  . GLU G  1 133 ? 17.946  158.000 47.264  1.00 35.20 ? 133  GLU G CB  1 
ATOM   7511  C  CG  . GLU G  1 133 ? 18.469  156.742 47.943  1.00 36.26 ? 133  GLU G CG  1 
ATOM   7512  C  CD  . GLU G  1 133 ? 18.115  155.469 47.184  1.00 38.33 ? 133  GLU G CD  1 
ATOM   7513  O  OE1 . GLU G  1 133 ? 18.247  155.449 45.937  1.00 38.01 ? 133  GLU G OE1 1 
ATOM   7514  O  OE2 . GLU G  1 133 ? 17.702  154.485 47.836  1.00 38.50 ? 133  GLU G OE2 1 
ATOM   7515  N  N   . SER G  1 134 ? 16.052  159.650 49.208  1.00 31.63 ? 134  SER G N   1 
ATOM   7516  C  CA  . SER G  1 134 ? 15.690  159.938 50.588  1.00 30.14 ? 134  SER G CA  1 
ATOM   7517  C  C   . SER G  1 134 ? 14.260  159.557 50.924  1.00 29.50 ? 134  SER G C   1 
ATOM   7518  O  O   . SER G  1 134 ? 13.981  159.173 52.056  1.00 28.95 ? 134  SER G O   1 
ATOM   7519  C  CB  . SER G  1 134 ? 15.901  161.419 50.931  1.00 30.33 ? 134  SER G CB  1 
ATOM   7520  O  OG  . SER G  1 134 ? 15.581  161.655 52.292  1.00 29.31 ? 134  SER G OG  1 
ATOM   7521  N  N   . THR G  1 135 ? 13.362  159.668 49.945  1.00 28.39 ? 135  THR G N   1 
ATOM   7522  C  CA  . THR G  1 135 ? 11.946  159.384 50.154  1.00 27.98 ? 135  THR G CA  1 
ATOM   7523  C  C   . THR G  1 135 ? 11.633  157.886 50.211  1.00 27.84 ? 135  THR G C   1 
ATOM   7524  O  O   . THR G  1 135 ? 10.522  157.481 50.576  1.00 27.03 ? 135  THR G O   1 
ATOM   7525  C  CB  . THR G  1 135 ? 11.118  160.039 49.040  1.00 27.88 ? 135  THR G CB  1 
ATOM   7526  O  OG1 . THR G  1 135 ? 11.509  159.495 47.773  1.00 29.38 ? 135  THR G OG1 1 
ATOM   7527  C  CG2 . THR G  1 135 ? 11.468  161.508 48.905  1.00 28.87 ? 135  THR G CG2 1 
ATOM   7528  N  N   . LYS G  1 136 ? 12.609  157.071 49.836  1.00 27.66 ? 136  LYS G N   1 
ATOM   7529  C  CA  . LYS G  1 136 ? 12.425  155.625 49.859  1.00 27.93 ? 136  LYS G CA  1 
ATOM   7530  C  C   . LYS G  1 136 ? 13.252  154.941 50.937  1.00 27.59 ? 136  LYS G C   1 
ATOM   7531  O  O   . LYS G  1 136 ? 12.753  154.059 51.654  1.00 27.62 ? 136  LYS G O   1 
ATOM   7532  C  CB  . LYS G  1 136 ? 12.891  155.004 48.559  1.00 28.53 ? 136  LYS G CB  1 
ATOM   7533  C  CG  . LYS G  1 136 ? 12.552  155.716 47.279  1.00 30.39 ? 136  LYS G CG  1 
ATOM   7534  C  CD  . LYS G  1 136 ? 13.503  155.138 46.236  1.00 33.06 ? 136  LYS G CD  1 
ATOM   7535  C  CE  . LYS G  1 136 ? 12.932  155.057 44.853  1.00 34.52 ? 136  LYS G CE  1 
ATOM   7536  N  NZ  . LYS G  1 136 ? 13.753  154.065 44.089  1.00 38.05 ? 136  LYS G NZ  1 
ATOM   7537  N  N   . THR G  1 137 ? 14.534  155.303 50.996  1.00 26.58 ? 137  THR G N   1 
ATOM   7538  C  CA  . THR G  1 137 ? 15.489  154.624 51.881  1.00 26.66 ? 137  THR G CA  1 
ATOM   7539  C  C   . THR G  1 137 ? 16.193  155.478 52.907  1.00 26.15 ? 137  THR G C   1 
ATOM   7540  O  O   . THR G  1 137 ? 16.770  154.943 53.844  1.00 26.73 ? 137  THR G O   1 
ATOM   7541  C  CB  . THR G  1 137 ? 16.597  153.945 51.062  1.00 27.12 ? 137  THR G CB  1 
ATOM   7542  O  OG1 . THR G  1 137 ? 17.425  154.953 50.462  1.00 25.66 ? 137  THR G OG1 1 
ATOM   7543  C  CG2 . THR G  1 137 ? 16.010  153.159 49.892  1.00 27.19 ? 137  THR G CG2 1 
ATOM   7544  N  N   . GLY G  1 138 ? 16.191  156.793 52.725  1.00 25.60 ? 138  GLY G N   1 
ATOM   7545  C  CA  . GLY G  1 138 ? 16.898  157.653 53.656  1.00 24.61 ? 138  GLY G CA  1 
ATOM   7546  C  C   . GLY G  1 138 ? 18.392  157.691 53.391  1.00 23.89 ? 138  GLY G C   1 
ATOM   7547  O  O   . GLY G  1 138 ? 19.153  158.140 54.240  1.00 24.49 ? 138  GLY G O   1 
ATOM   7548  N  N   . ASN G  1 139 ? 18.810  157.228 52.213  1.00 23.87 ? 139  ASN G N   1 
ATOM   7549  C  CA  . ASN G  1 139 ? 20.225  157.189 51.834  1.00 23.59 ? 139  ASN G CA  1 
ATOM   7550  C  C   . ASN G  1 139 ? 21.106  156.486 52.853  1.00 23.16 ? 139  ASN G C   1 
ATOM   7551  O  O   . ASN G  1 139 ? 22.255  156.892 53.064  1.00 23.09 ? 139  ASN G O   1 
ATOM   7552  C  CB  . ASN G  1 139 ? 20.771  158.611 51.627  1.00 23.84 ? 139  ASN G CB  1 
ATOM   7553  C  CG  . ASN G  1 139 ? 20.316  159.221 50.324  1.00 24.87 ? 139  ASN G CG  1 
ATOM   7554  O  OD1 . ASN G  1 139 ? 20.686  158.751 49.243  1.00 26.53 ? 139  ASN G OD1 1 
ATOM   7555  N  ND2 . ASN G  1 139 ? 19.478  160.253 50.414  1.00 23.29 ? 139  ASN G ND2 1 
ATOM   7556  N  N   . ALA G  1 140 ? 20.575  155.449 53.497  1.00 22.66 ? 140  ALA G N   1 
ATOM   7557  C  CA  . ALA G  1 140 ? 21.317  154.733 54.543  1.00 22.51 ? 140  ALA G CA  1 
ATOM   7558  C  C   . ALA G  1 140 ? 22.393  153.776 54.007  1.00 21.96 ? 140  ALA G C   1 
ATOM   7559  O  O   . ALA G  1 140 ? 23.119  153.126 54.773  1.00 20.80 ? 140  ALA G O   1 
ATOM   7560  C  CB  . ALA G  1 140 ? 20.352  153.999 55.454  1.00 22.57 ? 140  ALA G CB  1 
ATOM   7561  N  N   . GLY G  1 141 ? 22.492  153.684 52.690  1.00 21.89 ? 141  GLY G N   1 
ATOM   7562  C  CA  . GLY G  1 141 ? 23.493  152.833 52.074  1.00 21.68 ? 141  GLY G CA  1 
ATOM   7563  C  C   . GLY G  1 141 ? 23.329  151.337 52.310  1.00 21.62 ? 141  GLY G C   1 
ATOM   7564  O  O   . GLY G  1 141 ? 22.226  150.823 52.509  1.00 21.83 ? 141  GLY G O   1 
ATOM   7565  N  N   . SER G  1 142 ? 24.458  150.642 52.279  1.00 21.31 ? 142  SER G N   1 
ATOM   7566  C  CA  . SER G  1 142 ? 24.516  149.187 52.401  1.00 21.38 ? 142  SER G CA  1 
ATOM   7567  C  C   . SER G  1 142 ? 23.771  148.553 53.545  1.00 20.13 ? 142  SER G C   1 
ATOM   7568  O  O   . SER G  1 142 ? 23.577  149.159 54.591  1.00 19.73 ? 142  SER G O   1 
ATOM   7569  C  CB  . SER G  1 142 ? 25.973  148.734 52.538  1.00 21.69 ? 142  SER G CB  1 
ATOM   7570  O  OG  . SER G  1 142 ? 26.406  148.172 51.319  1.00 27.50 ? 142  SER G OG  1 
ATOM   7571  N  N   . ARG G  1 143 ? 23.434  147.277 53.346  1.00 18.64 ? 143  ARG G N   1 
ATOM   7572  C  CA  . ARG G  1 143 ? 22.815  146.483 54.377  1.00 17.86 ? 143  ARG G CA  1 
ATOM   7573  C  C   . ARG G  1 143 ? 23.923  145.673 55.038  1.00 17.81 ? 143  ARG G C   1 
ATOM   7574  O  O   . ARG G  1 143 ? 24.393  144.678 54.496  1.00 17.90 ? 143  ARG G O   1 
ATOM   7575  C  CB  . ARG G  1 143 ? 21.742  145.565 53.767  1.00 17.71 ? 143  ARG G CB  1 
ATOM   7576  C  CG  . ARG G  1 143 ? 20.728  146.335 52.922  1.00 17.33 ? 143  ARG G CG  1 
ATOM   7577  C  CD  . ARG G  1 143 ? 19.498  145.538 52.402  1.00 16.50 ? 143  ARG G CD  1 
ATOM   7578  N  NE  . ARG G  1 143 ? 18.691  146.420 51.542  1.00 18.74 ? 143  ARG G NE  1 
ATOM   7579  C  CZ  . ARG G  1 143 ? 17.556  146.088 50.958  1.00 19.16 ? 143  ARG G CZ  1 
ATOM   7580  N  NH1 . ARG G  1 143 ? 17.037  144.868 51.128  1.00 16.97 ? 143  ARG G NH1 1 
ATOM   7581  N  NH2 . ARG G  1 143 ? 16.937  146.980 50.194  1.00 19.30 ? 143  ARG G NH2 1 
ATOM   7582  N  N   . LEU G  1 144 ? 24.326  146.096 56.222  1.00 17.17 ? 144  LEU G N   1 
ATOM   7583  C  CA  . LEU G  1 144 ? 25.440  145.463 56.902  1.00 16.32 ? 144  LEU G CA  1 
ATOM   7584  C  C   . LEU G  1 144 ? 25.115  144.135 57.562  1.00 15.84 ? 144  LEU G C   1 
ATOM   7585  O  O   . LEU G  1 144 ? 25.962  143.273 57.611  1.00 14.25 ? 144  LEU G O   1 
ATOM   7586  C  CB  . LEU G  1 144 ? 25.991  146.419 57.956  1.00 16.59 ? 144  LEU G CB  1 
ATOM   7587  C  CG  . LEU G  1 144 ? 26.540  147.722 57.396  1.00 17.08 ? 144  LEU G CG  1 
ATOM   7588  C  CD1 . LEU G  1 144 ? 27.278  148.423 58.510  1.00 17.61 ? 144  LEU G CD1 1 
ATOM   7589  C  CD2 . LEU G  1 144 ? 27.471  147.448 56.244  1.00 19.11 ? 144  LEU G CD2 1 
ATOM   7590  N  N   . ALA G  1 145 ? 23.923  144.022 58.135  1.00 15.70 ? 145  ALA G N   1 
ATOM   7591  C  CA  . ALA G  1 145 ? 23.488  142.788 58.773  1.00 15.79 ? 145  ALA G CA  1 
ATOM   7592  C  C   . ALA G  1 145 ? 21.979  142.778 58.741  1.00 16.27 ? 145  ALA G C   1 
ATOM   7593  O  O   . ALA G  1 145 ? 21.342  143.851 58.623  1.00 16.00 ? 145  ALA G O   1 
ATOM   7594  C  CB  . ALA G  1 145 ? 24.007  142.674 60.227  1.00 15.94 ? 145  ALA G CB  1 
ATOM   7595  N  N   . CYS G  1 146 ? 21.396  141.581 58.812  1.00 16.02 ? 146  CYS G N   1 
ATOM   7596  C  CA  . CYS G  1 146 ? 19.940  141.475 58.820  1.00 16.49 ? 146  CYS G CA  1 
ATOM   7597  C  C   . CYS G  1 146 ? 19.535  140.137 59.392  1.00 15.32 ? 146  CYS G C   1 
ATOM   7598  O  O   . CYS G  1 146 ? 20.366  139.251 59.554  1.00 13.88 ? 146  CYS G O   1 
ATOM   7599  C  CB  . CYS G  1 146 ? 19.364  141.592 57.401  1.00 16.91 ? 146  CYS G CB  1 
ATOM   7600  S  SG  . CYS G  1 146 ? 19.966  140.336 56.213  1.00 20.33 ? 146  CYS G SG  1 
ATOM   7601  N  N   . GLY G  1 147 ? 18.252  139.980 59.692  1.00 15.43 ? 147  GLY G N   1 
ATOM   7602  C  CA  . GLY G  1 147 ? 17.773  138.681 60.168  1.00 16.23 ? 147  GLY G CA  1 
ATOM   7603  C  C   . GLY G  1 147 ? 16.266  138.686 60.050  1.00 16.64 ? 147  GLY G C   1 
ATOM   7604  O  O   . GLY G  1 147 ? 15.657  139.763 59.966  1.00 17.62 ? 147  GLY G O   1 
ATOM   7605  N  N   . VAL G  1 148 ? 15.649  137.518 60.035  1.00 15.57 ? 148  VAL G N   1 
ATOM   7606  C  CA  . VAL G  1 148 ? 14.191  137.484 59.976  1.00 16.26 ? 148  VAL G CA  1 
ATOM   7607  C  C   . VAL G  1 148 ? 13.672  137.632 61.398  1.00 16.81 ? 148  VAL G C   1 
ATOM   7608  O  O   . VAL G  1 148 ? 14.225  137.054 62.328  1.00 17.91 ? 148  VAL G O   1 
ATOM   7609  C  CB  . VAL G  1 148 ? 13.674  136.163 59.372  1.00 16.29 ? 148  VAL G CB  1 
ATOM   7610  C  CG1 . VAL G  1 148 ? 12.102  136.138 59.323  1.00 15.41 ? 148  VAL G CG1 1 
ATOM   7611  C  CG2 . VAL G  1 148 ? 14.299  135.976 57.992  1.00 15.31 ? 148  VAL G CG2 1 
ATOM   7612  N  N   . ILE G  1 149 ? 12.613  138.404 61.562  1.00 17.09 ? 149  ILE G N   1 
ATOM   7613  C  CA  . ILE G  1 149 ? 12.004  138.598 62.876  1.00 17.79 ? 149  ILE G CA  1 
ATOM   7614  C  C   . ILE G  1 149 ? 11.116  137.410 63.242  1.00 17.59 ? 149  ILE G C   1 
ATOM   7615  O  O   . ILE G  1 149 ? 10.106  137.151 62.595  1.00 19.63 ? 149  ILE G O   1 
ATOM   7616  C  CB  . ILE G  1 149 ? 11.169  139.896 62.856  1.00 17.32 ? 149  ILE G CB  1 
ATOM   7617  C  CG1 . ILE G  1 149 ? 12.077  141.086 62.583  1.00 18.68 ? 149  ILE G CG1 1 
ATOM   7618  C  CG2 . ILE G  1 149 ? 10.334  140.061 64.149  1.00 15.74 ? 149  ILE G CG2 1 
ATOM   7619  C  CD1 . ILE G  1 149 ? 11.322  142.385 62.331  1.00 19.84 ? 149  ILE G CD1 1 
ATOM   7620  N  N   . GLY G  1 150 ? 11.473  136.717 64.308  1.00 17.19 ? 150  GLY G N   1 
ATOM   7621  C  CA  . GLY G  1 150 ? 10.757  135.521 64.697  1.00 17.53 ? 150  GLY G CA  1 
ATOM   7622  C  C   . GLY G  1 150 ? 10.021  135.694 65.997  1.00 18.88 ? 150  GLY G C   1 
ATOM   7623  O  O   . GLY G  1 150 ? 10.307  136.611 66.785  1.00 16.91 ? 150  GLY G O   1 
ATOM   7624  N  N   . ILE G  1 151 ? 9.033   134.828 66.193  1.00 18.91 ? 151  ILE G N   1 
ATOM   7625  C  CA  . ILE G  1 151 ? 8.250   134.801 67.415  1.00 19.75 ? 151  ILE G CA  1 
ATOM   7626  C  C   . ILE G  1 151 ? 9.094   134.229 68.555  1.00 19.89 ? 151  ILE G C   1 
ATOM   7627  O  O   . ILE G  1 151 ? 9.793   133.217 68.382  1.00 18.56 ? 151  ILE G O   1 
ATOM   7628  C  CB  . ILE G  1 151 ? 6.983   133.947 67.189  1.00 20.72 ? 151  ILE G CB  1 
ATOM   7629  C  CG1 . ILE G  1 151 ? 6.101   134.609 66.128  1.00 21.25 ? 151  ILE G CG1 1 
ATOM   7630  C  CG2 . ILE G  1 151 ? 6.197   133.809 68.473  1.00 21.05 ? 151  ILE G CG2 1 
ATOM   7631  C  CD1 . ILE G  1 151 ? 4.898   133.751 65.665  1.00 20.93 ? 151  ILE G CD1 1 
ATOM   7632  N  N   . ALA G  1 152 ? 9.051   134.878 69.719  1.00 19.27 ? 152  ALA G N   1 
ATOM   7633  C  CA  . ALA G  1 152 ? 9.851   134.395 70.833  1.00 20.19 ? 152  ALA G CA  1 
ATOM   7634  C  C   . ALA G  1 152 ? 9.011   134.030 72.047  1.00 20.97 ? 152  ALA G C   1 
ATOM   7635  O  O   . ALA G  1 152 ? 7.888   134.486 72.184  1.00 20.99 ? 152  ALA G O   1 
ATOM   7636  C  CB  . ALA G  1 152 ? 10.893  135.420 71.208  1.00 20.27 ? 152  ALA G CB  1 
ATOM   7637  N  N   . GLN G  1 153 ? 9.580   133.199 72.915  1.00 22.17 ? 153  GLN G N   1 
ATOM   7638  C  CA  . GLN G  1 153 ? 8.926   132.738 74.123  1.00 23.70 ? 153  GLN G CA  1 
ATOM   7639  C  C   . GLN G  1 153 ? 8.769   133.905 75.090  1.00 24.31 ? 153  GLN G C   1 
ATOM   7640  O  O   . GLN G  1 153 ? 9.751   134.357 75.681  1.00 24.14 ? 153  GLN G O   1 
ATOM   7641  C  CB  . GLN G  1 153 ? 9.765   131.634 74.765  1.00 24.21 ? 153  GLN G CB  1 
ATOM   7642  C  CG  . GLN G  1 153 ? 9.020   130.741 75.763  1.00 25.25 ? 153  GLN G CG  1 
ATOM   7643  C  CD  . GLN G  1 153 ? 9.960   129.808 76.513  1.00 26.44 ? 153  GLN G CD  1 
ATOM   7644  O  OE1 . GLN G  1 153 ? 11.069  130.217 76.897  1.00 27.11 ? 153  GLN G OE1 1 
ATOM   7645  N  NE2 . GLN G  1 153 ? 9.527   128.563 76.734  1.00 25.41 ? 153  GLN G NE2 1 
ATOM   7646  O  OXT . GLN G  1 153 ? 7.657   134.400 75.291  1.00 24.80 ? 153  GLN G OXT 1 
ATOM   7647  N  N   . ALA H  1 1   ? 52.099  94.733  101.803 1.00 21.61 ? 1    ALA H N   1 
ATOM   7648  C  CA  . ALA H  1 1   ? 51.118  93.626  102.022 1.00 18.97 ? 1    ALA H CA  1 
ATOM   7649  C  C   . ALA H  1 1   ? 50.497  93.236  100.670 1.00 18.56 ? 1    ALA H C   1 
ATOM   7650  O  O   . ALA H  1 1   ? 50.271  94.116  99.827  1.00 19.86 ? 1    ALA H O   1 
ATOM   7651  C  CB  . ALA H  1 1   ? 50.028  94.064  103.007 1.00 19.80 ? 1    ALA H CB  1 
ATOM   7652  N  N   . THR H  1 2   ? 50.279  91.952  100.412 1.00 15.37 ? 2    THR H N   1 
ATOM   7653  C  CA  . THR H  1 2   ? 49.502  91.630  99.220  1.00 14.68 ? 2    THR H CA  1 
ATOM   7654  C  C   . THR H  1 2   ? 48.025  91.533  99.594  1.00 13.11 ? 2    THR H C   1 
ATOM   7655  O  O   . THR H  1 2   ? 47.691  91.170  100.732 1.00 11.59 ? 2    THR H O   1 
ATOM   7656  C  CB  . THR H  1 2   ? 50.088  90.540  98.257  1.00 16.83 ? 2    THR H CB  1 
ATOM   7657  O  OG1 . THR H  1 2   ? 49.058  89.615  97.843  1.00 21.87 ? 2    THR H OG1 1 
ATOM   7658  C  CG2 . THR H  1 2   ? 51.110  89.710  98.901  1.00 17.94 ? 2    THR H CG2 1 
ATOM   7659  N  N   . LYS H  1 3   ? 47.171  92.022  98.698  1.00 9.98  ? 3    LYS H N   1 
ATOM   7660  C  CA  . LYS H  1 3   ? 45.748  92.114  98.969  1.00 10.99 ? 3    LYS H CA  1 
ATOM   7661  C  C   . LYS H  1 3   ? 44.997  91.443  97.843  1.00 10.50 ? 3    LYS H C   1 
ATOM   7662  O  O   . LYS H  1 3   ? 45.462  91.480  96.684  1.00 8.35  ? 3    LYS H O   1 
ATOM   7663  C  CB  . LYS H  1 3   ? 45.344  93.570  99.053  1.00 10.31 ? 3    LYS H CB  1 
ATOM   7664  C  CG  . LYS H  1 3   ? 46.135  94.348  100.132 1.00 16.72 ? 3    LYS H CG  1 
ATOM   7665  C  CD  . LYS H  1 3   ? 45.830  95.863  100.158 1.00 23.04 ? 3    LYS H CD  1 
ATOM   7666  C  CE  . LYS H  1 3   ? 47.031  96.685  100.726 1.00 29.72 ? 3    LYS H CE  1 
ATOM   7667  N  NZ  . LYS H  1 3   ? 46.985  98.203  100.481 1.00 32.91 ? 3    LYS H NZ  1 
ATOM   7668  N  N   . ALA H  1 4   ? 43.863  90.831  98.190  1.00 9.69  ? 4    ALA H N   1 
ATOM   7669  C  CA  . ALA H  1 4   ? 42.965  90.233  97.209  1.00 8.42  ? 4    ALA H CA  1 
ATOM   7670  C  C   . ALA H  1 4   ? 41.533  90.514  97.622  1.00 9.30  ? 4    ALA H C   1 
ATOM   7671  O  O   . ALA H  1 4   ? 41.299  90.942  98.766  1.00 8.46  ? 4    ALA H O   1 
ATOM   7672  C  CB  . ALA H  1 4   ? 43.222  88.753  97.110  1.00 8.33  ? 4    ALA H CB  1 
ATOM   7673  N  N   . VAL H  1 5   ? 40.566  90.290  96.716  1.00 6.87  ? 5    VAL H N   1 
ATOM   7674  C  CA  . VAL H  1 5   ? 39.178  90.612  96.996  1.00 8.39  ? 5    VAL H CA  1 
ATOM   7675  C  C   . VAL H  1 5   ? 38.359  89.642  96.181  1.00 8.05  ? 5    VAL H C   1 
ATOM   7676  O  O   . VAL H  1 5   ? 38.815  89.136  95.150  1.00 8.85  ? 5    VAL H O   1 
ATOM   7677  C  CB  . VAL H  1 5   ? 38.856  92.119  96.639  1.00 8.61  ? 5    VAL H CB  1 
ATOM   7678  C  CG1 . VAL H  1 5   ? 39.002  92.365  95.129  1.00 6.80  ? 5    VAL H CG1 1 
ATOM   7679  C  CG2 . VAL H  1 5   ? 37.471  92.563  97.174  1.00 10.68 ? 5    VAL H CG2 1 
ATOM   7680  N  N   . CYS H  1 6   ? 37.160  89.354  96.649  1.00 8.45  ? 6    CYS H N   1 
ATOM   7681  C  CA  . CYS H  1 6   ? 36.294  88.439  95.958  1.00 9.38  ? 6    CYS H CA  1 
ATOM   7682  C  C   . CYS H  1 6   ? 34.868  88.966  96.148  1.00 9.23  ? 6    CYS H C   1 
ATOM   7683  O  O   . CYS H  1 6   ? 34.441  89.240  97.267  1.00 8.62  ? 6    CYS H O   1 
ATOM   7684  C  CB  . CYS H  1 6   ? 36.420  87.063  96.603  1.00 10.43 ? 6    CYS H CB  1 
ATOM   7685  S  SG  . CYS H  1 6   ? 35.351  85.841  95.826  1.00 12.25 ? 6    CYS H SG  1 
ATOM   7686  N  N   . VAL H  1 7   ? 34.142  89.091  95.054  1.00 8.62  ? 7    VAL H N   1 
ATOM   7687  C  CA  . VAL H  1 7   ? 32.739  89.462  95.098  1.00 9.61  ? 7    VAL H CA  1 
ATOM   7688  C  C   . VAL H  1 7   ? 31.931  88.201  94.888  1.00 9.51  ? 7    VAL H C   1 
ATOM   7689  O  O   . VAL H  1 7   ? 32.011  87.576  93.849  1.00 9.29  ? 7    VAL H O   1 
ATOM   7690  C  CB  . VAL H  1 7   ? 32.417  90.488  93.962  1.00 9.98  ? 7    VAL H CB  1 
ATOM   7691  C  CG1 . VAL H  1 7   ? 30.949  90.855  93.989  1.00 9.88  ? 7    VAL H CG1 1 
ATOM   7692  C  CG2 . VAL H  1 7   ? 33.290  91.715  94.134  1.00 11.47 ? 7    VAL H CG2 1 
ATOM   7693  N  N   . LEU H  1 8   ? 31.155  87.809  95.888  1.00 9.31  ? 8    LEU H N   1 
ATOM   7694  C  CA  . LEU H  1 8   ? 30.370  86.599  95.809  1.00 10.45 ? 8    LEU H CA  1 
ATOM   7695  C  C   . LEU H  1 8   ? 28.975  86.855  95.272  1.00 11.03 ? 8    LEU H C   1 
ATOM   7696  O  O   . LEU H  1 8   ? 28.261  87.713  95.796  1.00 10.53 ? 8    LEU H O   1 
ATOM   7697  C  CB  . LEU H  1 8   ? 30.160  86.057  97.224  1.00 9.53  ? 8    LEU H CB  1 
ATOM   7698  C  CG  . LEU H  1 8   ? 31.396  85.707  98.041  1.00 13.34 ? 8    LEU H CG  1 
ATOM   7699  C  CD1 . LEU H  1 8   ? 30.935  85.411  99.458  1.00 13.40 ? 8    LEU H CD1 1 
ATOM   7700  C  CD2 . LEU H  1 8   ? 32.063  84.481  97.474  1.00 14.03 ? 8    LEU H CD2 1 
ATOM   7701  N  N   . LYS H  1 9   ? 28.582  86.068  94.270  1.00 11.31 ? 9    LYS H N   1 
ATOM   7702  C  CA  . LYS H  1 9   ? 27.220  86.118  93.698  1.00 12.13 ? 9    LYS H CA  1 
ATOM   7703  C  C   . LYS H  1 9   ? 26.767  84.717  93.302  1.00 11.95 ? 9    LYS H C   1 
ATOM   7704  O  O   . LYS H  1 9   ? 27.585  83.826  93.089  1.00 11.17 ? 9    LYS H O   1 
ATOM   7705  C  CB  . LYS H  1 9   ? 27.169  87.082  92.474  1.00 12.66 ? 9    LYS H CB  1 
ATOM   7706  C  CG  . LYS H  1 9   ? 27.553  88.512  92.860  1.00 16.98 ? 9    LYS H CG  1 
ATOM   7707  C  CD  . LYS H  1 9   ? 27.446  89.559  91.761  1.00 25.90 ? 9    LYS H CD  1 
ATOM   7708  C  CE  . LYS H  1 9   ? 27.458  90.945  92.424  1.00 30.00 ? 9    LYS H CE  1 
ATOM   7709  N  NZ  . LYS H  1 9   ? 27.026  92.063  91.523  1.00 33.99 ? 9    LYS H NZ  1 
ATOM   7710  N  N   . GLY H  1 10  ? 25.457  84.513  93.206  1.00 13.27 ? 10   GLY H N   1 
ATOM   7711  C  CA  . GLY H  1 10  ? 24.940  83.228  92.773  1.00 15.18 ? 10   GLY H CA  1 
ATOM   7712  C  C   . GLY H  1 10  ? 23.581  83.369  92.110  1.00 15.99 ? 10   GLY H C   1 
ATOM   7713  O  O   . GLY H  1 10  ? 23.228  84.450  91.666  1.00 16.04 ? 10   GLY H O   1 
ATOM   7714  N  N   . ASP H  1 11  ? 22.828  82.281  92.048  1.00 17.26 ? 11   ASP H N   1 
ATOM   7715  C  CA  . ASP H  1 11  ? 21.517  82.294  91.394  1.00 19.16 ? 11   ASP H CA  1 
ATOM   7716  C  C   . ASP H  1 11  ? 20.425  82.902  92.292  1.00 19.14 ? 11   ASP H C   1 
ATOM   7717  O  O   . ASP H  1 11  ? 19.397  83.389  91.784  1.00 20.07 ? 11   ASP H O   1 
ATOM   7718  C  CB  . ASP H  1 11  ? 21.108  80.874  90.993  1.00 20.16 ? 11   ASP H CB  1 
ATOM   7719  C  CG  . ASP H  1 11  ? 22.002  80.287  89.909  1.00 22.97 ? 11   ASP H CG  1 
ATOM   7720  O  OD1 . ASP H  1 11  ? 22.412  81.037  88.999  1.00 24.71 ? 11   ASP H OD1 1 
ATOM   7721  O  OD2 . ASP H  1 11  ? 22.327  79.074  89.883  1.00 27.79 ? 11   ASP H OD2 1 
ATOM   7722  N  N   . GLY H  1 12  ? 20.651  82.847  93.610  1.00 18.01 ? 12   GLY H N   1 
ATOM   7723  C  CA  . GLY H  1 12  ? 19.740  83.401  94.601  1.00 16.45 ? 12   GLY H CA  1 
ATOM   7724  C  C   . GLY H  1 12  ? 20.130  84.784  95.112  1.00 15.26 ? 12   GLY H C   1 
ATOM   7725  O  O   . GLY H  1 12  ? 20.777  85.555  94.413  1.00 14.77 ? 12   GLY H O   1 
ATOM   7726  N  N   . PRO H  1 13  ? 19.746  85.096  96.344  1.00 14.71 ? 13   PRO H N   1 
ATOM   7727  C  CA  . PRO H  1 13  ? 19.976  86.414  96.934  1.00 14.67 ? 13   PRO H CA  1 
ATOM   7728  C  C   . PRO H  1 13  ? 21.278  86.540  97.728  1.00 14.65 ? 13   PRO H C   1 
ATOM   7729  O  O   . PRO H  1 13  ? 21.529  87.612  98.283  1.00 15.62 ? 13   PRO H O   1 
ATOM   7730  C  CB  . PRO H  1 13  ? 18.806  86.525  97.909  1.00 14.92 ? 13   PRO H CB  1 
ATOM   7731  C  CG  . PRO H  1 13  ? 18.708  85.150  98.456  1.00 15.03 ? 13   PRO H CG  1 
ATOM   7732  C  CD  . PRO H  1 13  ? 19.015  84.222  97.273  1.00 14.58 ? 13   PRO H CD  1 
ATOM   7733  N  N   . VAL H  1 14  ? 22.090  85.496  97.788  1.00 13.57 ? 14   VAL H N   1 
ATOM   7734  C  CA  . VAL H  1 14  ? 23.342  85.573  98.556  1.00 12.74 ? 14   VAL H CA  1 
ATOM   7735  C  C   . VAL H  1 14  ? 24.385  86.401  97.805  1.00 12.97 ? 14   VAL H C   1 
ATOM   7736  O  O   . VAL H  1 14  ? 24.667  86.126  96.631  1.00 13.04 ? 14   VAL H O   1 
ATOM   7737  C  CB  . VAL H  1 14  ? 23.880  84.163  98.851  1.00 12.97 ? 14   VAL H CB  1 
ATOM   7738  C  CG1 . VAL H  1 14  ? 25.213  84.205  99.596  1.00 11.06 ? 14   VAL H CG1 1 
ATOM   7739  C  CG2 . VAL H  1 14  ? 22.860  83.395  99.682  1.00 12.06 ? 14   VAL H CG2 1 
ATOM   7740  N  N   . GLN H  1 15  ? 24.905  87.426  98.475  1.00 11.98 ? 15   GLN H N   1 
ATOM   7741  C  CA  . GLN H  1 15  ? 25.864  88.367  97.871  1.00 12.90 ? 15   GLN H CA  1 
ATOM   7742  C  C   . GLN H  1 15  ? 26.819  88.817  98.927  1.00 11.46 ? 15   GLN H C   1 
ATOM   7743  O  O   . GLN H  1 15  ? 26.416  89.057  100.066 1.00 11.40 ? 15   GLN H O   1 
ATOM   7744  C  CB  . GLN H  1 15  ? 25.183  89.672  97.471  1.00 12.89 ? 15   GLN H CB  1 
ATOM   7745  C  CG  . GLN H  1 15  ? 24.362  89.665  96.260  1.00 20.02 ? 15   GLN H CG  1 
ATOM   7746  C  CD  . GLN H  1 15  ? 24.038  91.079  95.824  1.00 25.27 ? 15   GLN H CD  1 
ATOM   7747  O  OE1 . GLN H  1 15  ? 23.175  91.731  96.417  1.00 29.07 ? 15   GLN H OE1 1 
ATOM   7748  N  NE2 . GLN H  1 15  ? 24.732  91.560  94.800  1.00 27.20 ? 15   GLN H NE2 1 
ATOM   7749  N  N   . GLY H  1 16  ? 28.064  89.045  98.547  1.00 10.68 ? 16   GLY H N   1 
ATOM   7750  C  CA  . GLY H  1 16  ? 29.004  89.555  99.523  1.00 10.10 ? 16   GLY H CA  1 
ATOM   7751  C  C   . GLY H  1 16  ? 30.300  89.994  98.897  1.00 9.59  ? 16   GLY H C   1 
ATOM   7752  O  O   . GLY H  1 16  ? 30.517  89.779  97.694  1.00 8.82  ? 16   GLY H O   1 
ATOM   7753  N  N   . ILE H  1 17  ? 31.146  90.593  99.734  1.00 9.35  ? 17   ILE H N   1 
ATOM   7754  C  CA  . ILE H  1 17  ? 32.485  91.026  99.362  1.00 9.76  ? 17   ILE H CA  1 
ATOM   7755  C  C   . ILE H  1 17  ? 33.408  90.566  100.456 1.00 9.02  ? 17   ILE H C   1 
ATOM   7756  O  O   . ILE H  1 17  ? 33.152  90.817  101.636 1.00 8.95  ? 17   ILE H O   1 
ATOM   7757  C  CB  . ILE H  1 17  ? 32.547  92.541  99.215  1.00 10.21 ? 17   ILE H CB  1 
ATOM   7758  C  CG1 . ILE H  1 17  ? 31.600  93.012  98.092  1.00 12.21 ? 17   ILE H CG1 1 
ATOM   7759  C  CG2 . ILE H  1 17  ? 33.989  93.003  98.915  1.00 12.59 ? 17   ILE H CG2 1 
ATOM   7760  C  CD1 . ILE H  1 17  ? 31.541  94.521  97.986  1.00 14.28 ? 17   ILE H CD1 1 
ATOM   7761  N  N   . ILE H  1 18  ? 34.452  89.854  100.079 1.00 8.06  ? 18   ILE H N   1 
ATOM   7762  C  CA  . ILE H  1 18  ? 35.397  89.322  101.046 1.00 7.84  ? 18   ILE H CA  1 
ATOM   7763  C  C   . ILE H  1 18  ? 36.777  89.815  100.629 1.00 8.42  ? 18   ILE H C   1 
ATOM   7764  O  O   . ILE H  1 18  ? 37.144  89.671  99.459  1.00 7.85  ? 18   ILE H O   1 
ATOM   7765  C  CB  . ILE H  1 18  ? 35.353  87.777  101.027 1.00 7.41  ? 18   ILE H CB  1 
ATOM   7766  C  CG1 . ILE H  1 18  ? 33.985  87.250  101.525 1.00 9.12  ? 18   ILE H CG1 1 
ATOM   7767  C  CG2 . ILE H  1 18  ? 36.542  87.181  101.837 1.00 5.40  ? 18   ILE H CG2 1 
ATOM   7768  C  CD1 . ILE H  1 18  ? 33.699  87.716  102.988 1.00 8.92  ? 18   ILE H CD1 1 
ATOM   7769  N  N   . ASN H  1 19  ? 37.516  90.360  101.602 1.00 6.57  ? 19   ASN H N   1 
ATOM   7770  C  CA  . ASN H  1 19  ? 38.835  90.927  101.423 1.00 8.77  ? 19   ASN H CA  1 
ATOM   7771  C  C   . ASN H  1 19  ? 39.843  89.950  101.972 1.00 7.31  ? 19   ASN H C   1 
ATOM   7772  O  O   . ASN H  1 19  ? 39.526  89.207  102.931 1.00 6.94  ? 19   ASN H O   1 
ATOM   7773  C  CB  . ASN H  1 19  ? 38.907  92.209  102.272 1.00 7.65  ? 19   ASN H CB  1 
ATOM   7774  C  CG  . ASN H  1 19  ? 37.829  93.185  101.913 1.00 12.74 ? 19   ASN H CG  1 
ATOM   7775  O  OD1 . ASN H  1 19  ? 36.884  93.443  102.691 1.00 16.06 ? 19   ASN H OD1 1 
ATOM   7776  N  ND2 . ASN H  1 19  ? 37.915  93.696  100.708 1.00 7.59  ? 19   ASN H ND2 1 
ATOM   7777  N  N   . PHE H  1 20  ? 41.035  89.945  101.382 1.00 6.60  ? 20   PHE H N   1 
ATOM   7778  C  CA  . PHE H  1 20  ? 42.132  89.134  101.873 1.00 6.27  ? 20   PHE H CA  1 
ATOM   7779  C  C   . PHE H  1 20  ? 43.351  90.046  102.002 1.00 6.84  ? 20   PHE H C   1 
ATOM   7780  O  O   . PHE H  1 20  ? 43.623  90.867  101.096 1.00 5.89  ? 20   PHE H O   1 
ATOM   7781  C  CB  . PHE H  1 20  ? 42.522  88.018  100.871 1.00 6.90  ? 20   PHE H CB  1 
ATOM   7782  C  CG  . PHE H  1 20  ? 41.417  87.033  100.568 1.00 6.63  ? 20   PHE H CG  1 
ATOM   7783  C  CD1 . PHE H  1 20  ? 40.377  87.386  99.692  1.00 8.68  ? 20   PHE H CD1 1 
ATOM   7784  C  CD2 . PHE H  1 20  ? 41.409  85.757  101.151 1.00 8.37  ? 20   PHE H CD2 1 
ATOM   7785  C  CE1 . PHE H  1 20  ? 39.358  86.489  99.411  1.00 8.47  ? 20   PHE H CE1 1 
ATOM   7786  C  CE2 . PHE H  1 20  ? 40.363  84.846  100.886 1.00 9.84  ? 20   PHE H CE2 1 
ATOM   7787  C  CZ  . PHE H  1 20  ? 39.346  85.212  100.002 1.00 9.18  ? 20   PHE H CZ  1 
ATOM   7788  N  N   . GLU H  1 21  ? 44.157  89.828  103.049 1.00 6.81  ? 21   GLU H N   1 
ATOM   7789  C  CA  . GLU H  1 21  ? 45.369  90.610  103.210 1.00 6.81  ? 21   GLU H CA  1 
ATOM   7790  C  C   . GLU H  1 21  ? 46.436  89.749  103.837 1.00 6.47  ? 21   GLU H C   1 
ATOM   7791  O  O   . GLU H  1 21  ? 46.191  89.076  104.824 1.00 6.75  ? 21   GLU H O   1 
ATOM   7792  C  CB  . GLU H  1 21  ? 45.152  91.824  104.121 1.00 7.47  ? 21   GLU H CB  1 
ATOM   7793  C  CG  . GLU H  1 21  ? 46.441  92.605  104.287 1.00 12.46 ? 21   GLU H CG  1 
ATOM   7794  C  CD  . GLU H  1 21  ? 46.155  93.897  104.973 1.00 21.81 ? 21   GLU H CD  1 
ATOM   7795  O  OE1 . GLU H  1 21  ? 46.180  93.904  106.223 1.00 23.79 ? 21   GLU H OE1 1 
ATOM   7796  O  OE2 . GLU H  1 21  ? 45.831  94.861  104.251 1.00 26.52 ? 21   GLU H OE2 1 
ATOM   7797  N  N   . GLN H  1 22  ? 47.629  89.761  103.253 1.00 5.76  ? 22   GLN H N   1 
ATOM   7798  C  CA  . GLN H  1 22  ? 48.745  89.000  103.782 1.00 6.61  ? 22   GLN H CA  1 
ATOM   7799  C  C   . GLN H  1 22  ? 49.888  89.949  103.946 1.00 7.56  ? 22   GLN H C   1 
ATOM   7800  O  O   . GLN H  1 22  ? 50.526  90.347  102.956 1.00 7.63  ? 22   GLN H O   1 
ATOM   7801  C  CB  . GLN H  1 22  ? 49.091  87.846  102.853 1.00 6.03  ? 22   GLN H CB  1 
ATOM   7802  C  CG  . GLN H  1 22  ? 50.146  86.887  103.417 1.00 6.60  ? 22   GLN H CG  1 
ATOM   7803  C  CD  . GLN H  1 22  ? 50.388  85.702  102.490 1.00 9.75  ? 22   GLN H CD  1 
ATOM   7804  O  OE1 . GLN H  1 22  ? 50.296  85.843  101.252 1.00 10.34 ? 22   GLN H OE1 1 
ATOM   7805  N  NE2 . GLN H  1 22  ? 50.738  84.553  103.063 1.00 6.58  ? 22   GLN H NE2 1 
ATOM   7806  N  N   . LYS H  1 23  ? 50.158  90.341  105.196 1.00 8.11  ? 23   LYS H N   1 
ATOM   7807  C  CA  . LYS H  1 23  ? 51.187  91.354  105.435 1.00 9.37  ? 23   LYS H CA  1 
ATOM   7808  C  C   . LYS H  1 23  ? 52.598  90.849  105.201 1.00 9.85  ? 23   LYS H C   1 
ATOM   7809  O  O   . LYS H  1 23  ? 53.476  91.618  104.804 1.00 9.55  ? 23   LYS H O   1 
ATOM   7810  C  CB  . LYS H  1 23  ? 51.095  91.900  106.866 1.00 11.40 ? 23   LYS H CB  1 
ATOM   7811  C  CG  . LYS H  1 23  ? 49.899  92.785  107.096 1.00 14.72 ? 23   LYS H CG  1 
ATOM   7812  C  CD  . LYS H  1 23  ? 49.735  93.077  108.584 1.00 22.47 ? 23   LYS H CD  1 
ATOM   7813  C  CE  . LYS H  1 23  ? 49.014  94.401  108.883 1.00 26.86 ? 23   LYS H CE  1 
ATOM   7814  N  NZ  . LYS H  1 23  ? 48.204  94.947  107.750 1.00 32.54 ? 23   LYS H NZ  1 
ATOM   7815  N  N   . GLU H  1 24  ? 52.830  89.580  105.483 1.00 10.32 ? 24   GLU H N   1 
ATOM   7816  C  CA  . GLU H  1 24  ? 54.177  89.039  105.353 1.00 12.47 ? 24   GLU H CA  1 
ATOM   7817  C  C   . GLU H  1 24  ? 54.223  87.795  104.464 1.00 11.13 ? 24   GLU H C   1 
ATOM   7818  O  O   . GLU H  1 24  ? 53.286  87.001  104.448 1.00 9.99  ? 24   GLU H O   1 
ATOM   7819  C  CB  . GLU H  1 24  ? 54.724  88.685  106.740 1.00 12.14 ? 24   GLU H CB  1 
ATOM   7820  C  CG  . GLU H  1 24  ? 56.084  89.304  107.024 1.00 22.43 ? 24   GLU H CG  1 
ATOM   7821  C  CD  . GLU H  1 24  ? 55.995  90.467  107.996 1.00 29.41 ? 24   GLU H CD  1 
ATOM   7822  O  OE1 . GLU H  1 24  ? 55.094  90.448  108.870 1.00 35.75 ? 24   GLU H OE1 1 
ATOM   7823  O  OE2 . GLU H  1 24  ? 56.812  91.395  107.895 1.00 31.89 ? 24   GLU H OE2 1 
ATOM   7824  N  N   . SER H  1 25  ? 55.314  87.635  103.727 1.00 10.36 ? 25   SER H N   1 
ATOM   7825  C  CA  . SER H  1 25  ? 55.470  86.440  102.909 1.00 11.68 ? 25   SER H CA  1 
ATOM   7826  C  C   . SER H  1 25  ? 55.241  85.135  103.705 1.00 10.54 ? 25   SER H C   1 
ATOM   7827  O  O   . SER H  1 25  ? 55.803  84.928  104.783 1.00 9.41  ? 25   SER H O   1 
ATOM   7828  C  CB  . SER H  1 25  ? 56.847  86.440  102.222 1.00 11.62 ? 25   SER H CB  1 
ATOM   7829  O  OG  . SER H  1 25  ? 56.882  85.324  101.347 1.00 14.03 ? 25   SER H OG  1 
ATOM   7830  N  N   . ASN H  1 26  ? 54.376  84.272  103.176 1.00 11.06 ? 26   ASN H N   1 
ATOM   7831  C  CA  . ASN H  1 26  ? 54.016  83.008  103.821 1.00 11.92 ? 26   ASN H CA  1 
ATOM   7832  C  C   . ASN H  1 26  ? 53.312  83.213  105.172 1.00 11.48 ? 26   ASN H C   1 
ATOM   7833  O  O   . ASN H  1 26  ? 53.030  82.248  105.886 1.00 10.68 ? 26   ASN H O   1 
ATOM   7834  C  CB  . ASN H  1 26  ? 55.235  82.064  103.955 1.00 13.29 ? 26   ASN H CB  1 
ATOM   7835  C  CG  . ASN H  1 26  ? 54.827  80.606  104.269 1.00 16.59 ? 26   ASN H CG  1 
ATOM   7836  O  OD1 . ASN H  1 26  ? 53.747  80.142  103.870 1.00 21.20 ? 26   ASN H OD1 1 
ATOM   7837  N  ND2 . ASN H  1 26  ? 55.676  79.895  105.008 1.00 19.05 ? 26   ASN H ND2 1 
ATOM   7838  N  N   . GLY H  1 27  ? 53.001  84.464  105.517 1.00 9.73  ? 27   GLY H N   1 
ATOM   7839  C  CA  . GLY H  1 27  ? 52.354  84.703  106.806 1.00 9.98  ? 27   GLY H CA  1 
ATOM   7840  C  C   . GLY H  1 27  ? 50.841  84.503  106.863 1.00 9.03  ? 27   GLY H C   1 
ATOM   7841  O  O   . GLY H  1 27  ? 50.204  84.082  105.906 1.00 8.56  ? 27   GLY H O   1 
ATOM   7842  N  N   . PRO H  1 28  ? 50.248  84.786  108.016 1.00 9.24  ? 28   PRO H N   1 
ATOM   7843  C  CA  . PRO H  1 28  ? 48.788  84.684  108.170 1.00 9.45  ? 28   PRO H CA  1 
ATOM   7844  C  C   . PRO H  1 28  ? 48.072  85.568  107.131 1.00 8.72  ? 28   PRO H C   1 
ATOM   7845  O  O   . PRO H  1 28  ? 48.513  86.680  106.847 1.00 8.92  ? 28   PRO H O   1 
ATOM   7846  C  CB  . PRO H  1 28  ? 48.532  85.310  109.549 1.00 9.99  ? 28   PRO H CB  1 
ATOM   7847  C  CG  . PRO H  1 28  ? 49.812  85.198  110.267 1.00 10.74 ? 28   PRO H CG  1 
ATOM   7848  C  CD  . PRO H  1 28  ? 50.916  85.233  109.249 1.00 10.22 ? 28   PRO H CD  1 
ATOM   7849  N  N   . VAL H  1 29  ? 46.965  85.077  106.603 1.00 8.11  ? 29   VAL H N   1 
ATOM   7850  C  CA  . VAL H  1 29  ? 46.109  85.833  105.703 1.00 7.69  ? 29   VAL H CA  1 
ATOM   7851  C  C   . VAL H  1 29  ? 44.833  86.169  106.478 1.00 8.11  ? 29   VAL H C   1 
ATOM   7852  O  O   . VAL H  1 29  ? 44.196  85.262  107.083 1.00 8.52  ? 29   VAL H O   1 
ATOM   7853  C  CB  . VAL H  1 29  ? 45.751  85.008  104.469 1.00 8.71  ? 29   VAL H CB  1 
ATOM   7854  C  CG1 . VAL H  1 29  ? 44.784  85.789  103.530 1.00 8.48  ? 29   VAL H CG1 1 
ATOM   7855  C  CG2 . VAL H  1 29  ? 47.047  84.567  103.742 1.00 8.96  ? 29   VAL H CG2 1 
ATOM   7856  N  N   . LYS H  1 30  ? 44.524  87.465  106.527 1.00 7.87  ? 30   LYS H N   1 
ATOM   7857  C  CA  . LYS H  1 30  ? 43.280  87.907  107.137 1.00 9.42  ? 30   LYS H CA  1 
ATOM   7858  C  C   . LYS H  1 30  ? 42.239  87.837  106.052 1.00 8.52  ? 30   LYS H C   1 
ATOM   7859  O  O   . LYS H  1 30  ? 42.514  88.244  104.905 1.00 8.46  ? 30   LYS H O   1 
ATOM   7860  C  CB  . LYS H  1 30  ? 43.407  89.347  107.707 1.00 10.31 ? 30   LYS H CB  1 
ATOM   7861  C  CG  . LYS H  1 30  ? 44.496  89.480  108.770 1.00 17.02 ? 30   LYS H CG  1 
ATOM   7862  C  CD  . LYS H  1 30  ? 44.508  90.861  109.508 1.00 25.76 ? 30   LYS H CD  1 
ATOM   7863  C  CE  . LYS H  1 30  ? 43.986  90.746  110.950 1.00 30.10 ? 30   LYS H CE  1 
ATOM   7864  N  NZ  . LYS H  1 30  ? 44.145  92.010  111.763 1.00 32.21 ? 30   LYS H NZ  1 
ATOM   7865  N  N   . VAL H  1 31  ? 41.061  87.307  106.390 1.00 6.42  ? 31   VAL H N   1 
ATOM   7866  C  CA  . VAL H  1 31  ? 39.937  87.173  105.467 1.00 6.29  ? 31   VAL H CA  1 
ATOM   7867  C  C   . VAL H  1 31  ? 38.746  87.828  106.141 1.00 7.44  ? 31   VAL H C   1 
ATOM   7868  O  O   . VAL H  1 31  ? 38.354  87.385  107.238 1.00 7.17  ? 31   VAL H O   1 
ATOM   7869  C  CB  . VAL H  1 31  ? 39.612  85.708  105.247 1.00 6.35  ? 31   VAL H CB  1 
ATOM   7870  C  CG1 . VAL H  1 31  ? 38.477  85.541  104.204 1.00 7.67  ? 31   VAL H CG1 1 
ATOM   7871  C  CG2 . VAL H  1 31  ? 40.916  84.956  104.801 1.00 6.80  ? 31   VAL H CG2 1 
ATOM   7872  N  N   . TRP H  1 32  ? 38.167  88.872  105.530 1.00 6.19  ? 32   TRP H N   1 
ATOM   7873  C  CA  . TRP H  1 32  ? 37.084  89.535  106.234 1.00 7.87  ? 32   TRP H CA  1 
ATOM   7874  C  C   . TRP H  1 32  ? 36.176  90.239  105.261 1.00 8.05  ? 32   TRP H C   1 
ATOM   7875  O  O   . TRP H  1 32  ? 36.593  90.630  104.141 1.00 7.79  ? 32   TRP H O   1 
ATOM   7876  C  CB  . TRP H  1 32  ? 37.642  90.552  107.241 1.00 8.11  ? 32   TRP H CB  1 
ATOM   7877  C  CG  . TRP H  1 32  ? 38.075  91.810  106.626 1.00 7.76  ? 32   TRP H CG  1 
ATOM   7878  C  CD1 . TRP H  1 32  ? 37.368  92.987  106.582 1.00 10.26 ? 32   TRP H CD1 1 
ATOM   7879  C  CD2 . TRP H  1 32  ? 39.332  92.074  105.984 1.00 7.76  ? 32   TRP H CD2 1 
ATOM   7880  N  NE1 . TRP H  1 32  ? 38.116  93.954  105.949 1.00 11.04 ? 32   TRP H NE1 1 
ATOM   7881  C  CE2 . TRP H  1 32  ? 39.311  93.410  105.549 1.00 7.23  ? 32   TRP H CE2 1 
ATOM   7882  C  CE3 . TRP H  1 32  ? 40.448  91.287  105.675 1.00 8.71  ? 32   TRP H CE3 1 
ATOM   7883  C  CZ2 . TRP H  1 32  ? 40.401  94.014  104.865 1.00 11.60 ? 32   TRP H CZ2 1 
ATOM   7884  C  CZ3 . TRP H  1 32  ? 41.543  91.878  105.004 1.00 9.67  ? 32   TRP H CZ3 1 
ATOM   7885  C  CH2 . TRP H  1 32  ? 41.500  93.243  104.606 1.00 12.08 ? 32   TRP H CH2 1 
ATOM   7886  N  N   . GLY H  1 33  ? 34.930  90.392  105.677 1.00 8.04  ? 33   GLY H N   1 
ATOM   7887  C  CA  . GLY H  1 33  ? 33.982  91.109  104.838 1.00 8.74  ? 33   GLY H CA  1 
ATOM   7888  C  C   . GLY H  1 33  ? 32.592  90.825  105.304 1.00 10.12 ? 33   GLY H C   1 
ATOM   7889  O  O   . GLY H  1 33  ? 32.389  90.480  106.458 1.00 10.39 ? 33   GLY H O   1 
ATOM   7890  N  N   . SER H  1 34  ? 31.632  90.913  104.406 1.00 10.01 ? 34   SER H N   1 
ATOM   7891  C  CA  . SER H  1 34  ? 30.254  90.653  104.833 1.00 11.07 ? 34   SER H CA  1 
ATOM   7892  C  C   . SER H  1 34  ? 29.536  89.910  103.728 1.00 11.03 ? 34   SER H C   1 
ATOM   7893  O  O   . SER H  1 34  ? 29.814  90.111  102.528 1.00 10.16 ? 34   SER H O   1 
ATOM   7894  C  CB  . SER H  1 34  ? 29.516  91.984  105.134 1.00 13.03 ? 34   SER H CB  1 
ATOM   7895  O  OG  . SER H  1 34  ? 28.349  91.706  105.934 1.00 19.08 ? 34   SER H OG  1 
ATOM   7896  N  N   . ILE H  1 35  ? 28.633  89.022  104.111 1.00 9.22  ? 35   ILE H N   1 
ATOM   7897  C  CA  . ILE H  1 35  ? 27.841  88.325  103.122 1.00 9.66  ? 35   ILE H CA  1 
ATOM   7898  C  C   . ILE H  1 35  ? 26.398  88.500  103.586 1.00 10.06 ? 35   ILE H C   1 
ATOM   7899  O  O   . ILE H  1 35  ? 26.104  88.376  104.790 1.00 9.32  ? 35   ILE H O   1 
ATOM   7900  C  CB  . ILE H  1 35  ? 28.224  86.825  103.083 1.00 9.74  ? 35   ILE H CB  1 
ATOM   7901  C  CG1 . ILE H  1 35  ? 29.731  86.638  102.829 1.00 11.55 ? 35   ILE H CG1 1 
ATOM   7902  C  CG2 . ILE H  1 35  ? 27.384  86.075  102.005 1.00 10.60 ? 35   ILE H CG2 1 
ATOM   7903  C  CD1 . ILE H  1 35  ? 30.147  85.164  102.945 1.00 12.46 ? 35   ILE H CD1 1 
ATOM   7904  N  N   . LYS H  1 36  ? 25.488  88.808  102.664 1.00 11.14 ? 36   LYS H N   1 
ATOM   7905  C  CA  . LYS H  1 36  ? 24.082  88.919  103.058 1.00 12.11 ? 36   LYS H CA  1 
ATOM   7906  C  C   . LYS H  1 36  ? 23.195  87.938  102.281 1.00 12.14 ? 36   LYS H C   1 
ATOM   7907  O  O   . LYS H  1 36  ? 23.660  87.262  101.380 1.00 11.38 ? 36   LYS H O   1 
ATOM   7908  C  CB  . LYS H  1 36  ? 23.593  90.368  102.910 1.00 13.04 ? 36   LYS H CB  1 
ATOM   7909  C  CG  . LYS H  1 36  ? 23.464  90.833  101.471 1.00 16.30 ? 36   LYS H CG  1 
ATOM   7910  C  CD  . LYS H  1 36  ? 23.167  92.329  101.369 1.00 21.05 ? 36   LYS H CD  1 
ATOM   7911  C  CE  . LYS H  1 36  ? 22.916  92.773  99.911  1.00 26.43 ? 36   LYS H CE  1 
ATOM   7912  N  NZ  . LYS H  1 36  ? 21.471  92.574  99.475  1.00 29.90 ? 36   LYS H NZ  1 
ATOM   7913  N  N   . GLY H  1 37  ? 21.932  87.824  102.691 1.00 12.74 ? 37   GLY H N   1 
ATOM   7914  C  CA  . GLY H  1 37  ? 20.962  86.989  102.013 1.00 13.25 ? 37   GLY H CA  1 
ATOM   7915  C  C   . GLY H  1 37  ? 20.993  85.552  102.452 1.00 14.04 ? 37   GLY H C   1 
ATOM   7916  O  O   . GLY H  1 37  ? 20.375  84.709  101.811 1.00 14.63 ? 37   GLY H O   1 
ATOM   7917  N  N   . LEU H  1 38  ? 21.685  85.270  103.552 1.00 13.21 ? 38   LEU H N   1 
ATOM   7918  C  CA  . LEU H  1 38  ? 21.836  83.912  104.040 1.00 13.25 ? 38   LEU H CA  1 
ATOM   7919  C  C   . LEU H  1 38  ? 20.789  83.581  105.100 1.00 13.95 ? 38   LEU H C   1 
ATOM   7920  O  O   . LEU H  1 38  ? 20.361  84.454  105.854 1.00 13.80 ? 38   LEU H O   1 
ATOM   7921  C  CB  . LEU H  1 38  ? 23.202  83.786  104.726 1.00 13.10 ? 38   LEU H CB  1 
ATOM   7922  C  CG  . LEU H  1 38  ? 24.428  83.911  103.833 1.00 13.45 ? 38   LEU H CG  1 
ATOM   7923  C  CD1 . LEU H  1 38  ? 25.700  84.115  104.682 1.00 10.03 ? 38   LEU H CD1 1 
ATOM   7924  C  CD2 . LEU H  1 38  ? 24.546  82.672  102.941 1.00 11.01 ? 38   LEU H CD2 1 
ATOM   7925  N  N   . THR H  1 39  ? 20.403  82.317  105.185 1.00 14.90 ? 39   THR H N   1 
ATOM   7926  C  CA  . THR H  1 39  ? 19.588  81.883  106.310 1.00 15.71 ? 39   THR H CA  1 
ATOM   7927  C  C   . THR H  1 39  ? 20.439  81.929  107.580 1.00 16.11 ? 39   THR H C   1 
ATOM   7928  O  O   . THR H  1 39  ? 21.639  81.677  107.550 1.00 16.15 ? 39   THR H O   1 
ATOM   7929  C  CB  . THR H  1 39  ? 19.118  80.443  106.099 1.00 16.21 ? 39   THR H CB  1 
ATOM   7930  O  OG1 . THR H  1 39  ? 20.257  79.602  105.879 1.00 17.73 ? 39   THR H OG1 1 
ATOM   7931  C  CG2 . THR H  1 39  ? 18.310  80.308  104.819 1.00 16.70 ? 39   THR H CG2 1 
ATOM   7932  N  N   . GLU H  1 40  ? 19.808  82.221  108.711 1.00 16.91 ? 40   GLU H N   1 
ATOM   7933  C  CA  . GLU H  1 40  ? 20.496  82.279  110.003 1.00 16.34 ? 40   GLU H CA  1 
ATOM   7934  C  C   . GLU H  1 40  ? 21.238  80.982  110.363 1.00 16.15 ? 40   GLU H C   1 
ATOM   7935  O  O   . GLU H  1 40  ? 20.725  79.876  110.149 1.00 16.47 ? 40   GLU H O   1 
ATOM   7936  C  CB  . GLU H  1 40  ? 19.492  82.634  111.120 1.00 17.54 ? 40   GLU H CB  1 
ATOM   7937  C  CG  . GLU H  1 40  ? 20.152  82.742  112.481 1.00 16.96 ? 40   GLU H CG  1 
ATOM   7938  C  CD  . GLU H  1 40  ? 19.196  83.130  113.591 1.00 22.99 ? 40   GLU H CD  1 
ATOM   7939  O  OE1 . GLU H  1 40  ? 17.986  83.347  113.305 1.00 20.74 ? 40   GLU H OE1 1 
ATOM   7940  O  OE2 . GLU H  1 40  ? 19.675  83.218  114.747 1.00 21.20 ? 40   GLU H OE2 1 
ATOM   7941  N  N   . GLY H  1 41  ? 22.439  81.110  110.925 1.00 15.85 ? 41   GLY H N   1 
ATOM   7942  C  CA  . GLY H  1 41  ? 23.218  79.933  111.282 1.00 15.85 ? 41   GLY H CA  1 
ATOM   7943  C  C   . GLY H  1 41  ? 24.475  79.691  110.448 1.00 16.08 ? 41   GLY H C   1 
ATOM   7944  O  O   . GLY H  1 41  ? 24.913  80.577  109.712 1.00 13.88 ? 41   GLY H O   1 
ATOM   7945  N  N   . LEU H  1 42  ? 25.032  78.478  110.552 1.00 15.57 ? 42   LEU H N   1 
ATOM   7946  C  CA  . LEU H  1 42  ? 26.352  78.185  109.967 1.00 15.86 ? 42   LEU H CA  1 
ATOM   7947  C  C   . LEU H  1 42  ? 26.344  77.842  108.485 1.00 14.45 ? 42   LEU H C   1 
ATOM   7948  O  O   . LEU H  1 42  ? 25.459  77.109  108.010 1.00 14.18 ? 42   LEU H O   1 
ATOM   7949  C  CB  . LEU H  1 42  ? 26.964  77.005  110.730 1.00 16.61 ? 42   LEU H CB  1 
ATOM   7950  C  CG  . LEU H  1 42  ? 27.221  77.185  112.216 1.00 18.43 ? 42   LEU H CG  1 
ATOM   7951  C  CD1 . LEU H  1 42  ? 27.516  75.825  112.848 1.00 20.77 ? 42   LEU H CD1 1 
ATOM   7952  C  CD2 . LEU H  1 42  ? 28.399  78.171  112.402 1.00 17.03 ? 42   LEU H CD2 1 
ATOM   7953  N  N   . HIS H  1 43  ? 27.327  78.375  107.747 1.00 12.07 ? 43   HIS H N   1 
ATOM   7954  C  CA  . HIS H  1 43  ? 27.453  78.111  106.330 1.00 11.59 ? 43   HIS H CA  1 
ATOM   7955  C  C   . HIS H  1 43  ? 28.902  77.815  105.974 1.00 9.94  ? 43   HIS H C   1 
ATOM   7956  O  O   . HIS H  1 43  ? 29.788  78.592  106.306 1.00 9.07  ? 43   HIS H O   1 
ATOM   7957  C  CB  . HIS H  1 43  ? 26.946  79.300  105.503 1.00 10.87 ? 43   HIS H CB  1 
ATOM   7958  C  CG  . HIS H  1 43  ? 25.469  79.546  105.657 1.00 12.61 ? 43   HIS H CG  1 
ATOM   7959  N  ND1 . HIS H  1 43  ? 24.539  79.050  104.769 1.00 9.87  ? 43   HIS H ND1 1 
ATOM   7960  C  CD2 . HIS H  1 43  ? 24.771  80.240  106.585 1.00 12.18 ? 43   HIS H CD2 1 
ATOM   7961  C  CE1 . HIS H  1 43  ? 23.331  79.437  105.142 1.00 12.44 ? 43   HIS H CE1 1 
ATOM   7962  N  NE2 . HIS H  1 43  ? 23.442  80.143  106.252 1.00 12.57 ? 43   HIS H NE2 1 
ATOM   7963  N  N   . GLY H  1 44  ? 29.127  76.681  105.316 1.00 8.54  ? 44   GLY H N   1 
ATOM   7964  C  CA  . GLY H  1 44  ? 30.451  76.270  104.862 1.00 6.86  ? 44   GLY H CA  1 
ATOM   7965  C  C   . GLY H  1 44  ? 31.073  77.356  103.985 1.00 7.54  ? 44   GLY H C   1 
ATOM   7966  O  O   . GLY H  1 44  ? 30.370  78.005  103.220 1.00 7.39  ? 44   GLY H O   1 
ATOM   7967  N  N   . PHE H  1 45  ? 32.393  77.497  104.072 1.00 6.72  ? 45   PHE H N   1 
ATOM   7968  C  CA  . PHE H  1 45  ? 33.104  78.632  103.446 1.00 7.72  ? 45   PHE H CA  1 
ATOM   7969  C  C   . PHE H  1 45  ? 34.459  78.116  103.030 1.00 6.51  ? 45   PHE H C   1 
ATOM   7970  O  O   . PHE H  1 45  ? 35.298  77.830  103.875 1.00 7.19  ? 45   PHE H O   1 
ATOM   7971  C  CB  . PHE H  1 45  ? 33.207  79.703  104.508 1.00 6.38  ? 45   PHE H CB  1 
ATOM   7972  C  CG  . PHE H  1 45  ? 33.781  81.028  104.048 1.00 8.33  ? 45   PHE H CG  1 
ATOM   7973  C  CD1 . PHE H  1 45  ? 33.071  81.847  103.186 1.00 10.98 ? 45   PHE H CD1 1 
ATOM   7974  C  CD2 . PHE H  1 45  ? 34.979  81.490  104.596 1.00 8.60  ? 45   PHE H CD2 1 
ATOM   7975  C  CE1 . PHE H  1 45  ? 33.588  83.120  102.836 1.00 11.79 ? 45   PHE H CE1 1 
ATOM   7976  C  CE2 . PHE H  1 45  ? 35.494  82.742  104.234 1.00 10.34 ? 45   PHE H CE2 1 
ATOM   7977  C  CZ  . PHE H  1 45  ? 34.797  83.535  103.356 1.00 10.40 ? 45   PHE H CZ  1 
ATOM   7978  N  N   . HIS H  1 46  ? 34.662  77.950  101.717 1.00 7.38  ? 46   HIS H N   1 
ATOM   7979  C  CA  . HIS H  1 46  ? 35.850  77.252  101.200 1.00 6.88  ? 46   HIS H CA  1 
ATOM   7980  C  C   . HIS H  1 46  ? 36.434  77.907  99.967  1.00 7.14  ? 46   HIS H C   1 
ATOM   7981  O  O   . HIS H  1 46  ? 35.706  78.523  99.208  1.00 7.26  ? 46   HIS H O   1 
ATOM   7982  C  CB  . HIS H  1 46  ? 35.452  75.819  100.736 1.00 7.49  ? 46   HIS H CB  1 
ATOM   7983  C  CG  . HIS H  1 46  ? 34.629  75.073  101.732 1.00 8.98  ? 46   HIS H CG  1 
ATOM   7984  N  ND1 . HIS H  1 46  ? 33.359  74.626  101.470 1.00 8.60  ? 46   HIS H ND1 1 
ATOM   7985  C  CD2 . HIS H  1 46  ? 34.873  74.763  103.026 1.00 9.87  ? 46   HIS H CD2 1 
ATOM   7986  C  CE1 . HIS H  1 46  ? 32.875  74.014  102.527 1.00 11.51 ? 46   HIS H CE1 1 
ATOM   7987  N  NE2 . HIS H  1 46  ? 33.759  74.116  103.502 1.00 9.87  ? 46   HIS H NE2 1 
ATOM   7988  N  N   . VAL H  1 47  ? 37.729  77.724  99.759  1.00 6.75  ? 47   VAL H N   1 
ATOM   7989  C  CA  . VAL H  1 47  ? 38.342  78.085  98.494  1.00 8.14  ? 47   VAL H CA  1 
ATOM   7990  C  C   . VAL H  1 47  ? 38.334  76.816  97.638  1.00 8.25  ? 47   VAL H C   1 
ATOM   7991  O  O   . VAL H  1 47  ? 38.903  75.787  98.030  1.00 8.52  ? 47   VAL H O   1 
ATOM   7992  C  CB  . VAL H  1 47  ? 39.749  78.494  98.661  1.00 7.13  ? 47   VAL H CB  1 
ATOM   7993  C  CG1 . VAL H  1 47  ? 40.347  78.831  97.259  1.00 8.52  ? 47   VAL H CG1 1 
ATOM   7994  C  CG2 . VAL H  1 47  ? 39.827  79.707  99.618  1.00 7.10  ? 47   VAL H CG2 1 
ATOM   7995  N  N   . HIS H  1 48  ? 37.677  76.905  96.482  1.00 8.13  ? 48   HIS H N   1 
ATOM   7996  C  CA  . HIS H  1 48  ? 37.598  75.784  95.544  1.00 7.68  ? 48   HIS H CA  1 
ATOM   7997  C  C   . HIS H  1 48  ? 38.693  75.973  94.493  1.00 8.57  ? 48   HIS H C   1 
ATOM   7998  O  O   . HIS H  1 48  ? 39.207  77.063  94.340  1.00 7.28  ? 48   HIS H O   1 
ATOM   7999  C  CB  . HIS H  1 48  ? 36.193  75.699  94.937  1.00 6.67  ? 48   HIS H CB  1 
ATOM   8000  C  CG  . HIS H  1 48  ? 35.175  75.110  95.880  1.00 8.02  ? 48   HIS H CG  1 
ATOM   8001  N  ND1 . HIS H  1 48  ? 34.442  73.988  95.575  1.00 5.97  ? 48   HIS H ND1 1 
ATOM   8002  C  CD2 . HIS H  1 48  ? 34.791  75.483  97.129  1.00 9.33  ? 48   HIS H CD2 1 
ATOM   8003  C  CE1 . HIS H  1 48  ? 33.644  73.691  96.599  1.00 10.72 ? 48   HIS H CE1 1 
ATOM   8004  N  NE2 . HIS H  1 48  ? 33.826  74.593  97.538  1.00 7.80  ? 48   HIS H NE2 1 
ATOM   8005  N  N   . GLU H  1 49  ? 39.062  74.877  93.832  1.00 9.39  ? 49   GLU H N   1 
ATOM   8006  C  CA  . GLU H  1 49  ? 40.225  74.802  92.970  1.00 10.76 ? 49   GLU H CA  1 
ATOM   8007  C  C   . GLU H  1 49  ? 40.300  75.778  91.831  1.00 10.68 ? 49   GLU H C   1 
ATOM   8008  O  O   . GLU H  1 49  ? 41.318  76.449  91.633  1.00 11.36 ? 49   GLU H O   1 
ATOM   8009  C  CB  . GLU H  1 49  ? 40.366  73.397  92.369  1.00 11.16 ? 49   GLU H CB  1 
ATOM   8010  C  CG  . GLU H  1 49  ? 41.782  73.166  91.894  1.00 13.22 ? 49   GLU H CG  1 
ATOM   8011  C  CD  . GLU H  1 49  ? 42.060  71.750  91.444  1.00 15.60 ? 49   GLU H CD  1 
ATOM   8012  O  OE1 . GLU H  1 49  ? 41.235  70.837  91.702  1.00 12.42 ? 49   GLU H OE1 1 
ATOM   8013  O  OE2 . GLU H  1 49  ? 43.132  71.586  90.827  1.00 15.20 ? 49   GLU H OE2 1 
ATOM   8014  N  N   . PHE H  1 50  ? 39.243  75.826  91.036  1.00 10.45 ? 50   PHE H N   1 
ATOM   8015  C  CA  . PHE H  1 50  ? 39.308  76.601  89.813  1.00 10.11 ? 50   PHE H CA  1 
ATOM   8016  C  C   . PHE H  1 50  ? 38.582  77.930  89.847  1.00 10.04 ? 50   PHE H C   1 
ATOM   8017  O  O   . PHE H  1 50  ? 37.474  78.008  90.393  1.00 10.59 ? 50   PHE H O   1 
ATOM   8018  C  CB  . PHE H  1 50  ? 38.720  75.720  88.686  1.00 10.78 ? 50   PHE H CB  1 
ATOM   8019  C  CG  . PHE H  1 50  ? 39.385  74.377  88.587  1.00 11.82 ? 50   PHE H CG  1 
ATOM   8020  C  CD1 . PHE H  1 50  ? 40.732  74.291  88.272  1.00 13.17 ? 50   PHE H CD1 1 
ATOM   8021  C  CD2 . PHE H  1 50  ? 38.679  73.217  88.816  1.00 11.94 ? 50   PHE H CD2 1 
ATOM   8022  C  CE1 . PHE H  1 50  ? 41.352  73.052  88.193  1.00 12.46 ? 50   PHE H CE1 1 
ATOM   8023  C  CE2 . PHE H  1 50  ? 39.292  71.976  88.738  1.00 11.26 ? 50   PHE H CE2 1 
ATOM   8024  C  CZ  . PHE H  1 50  ? 40.629  71.898  88.426  1.00 12.39 ? 50   PHE H CZ  1 
ATOM   8025  N  N   . GLY H  1 51  ? 39.181  78.965  89.249  1.00 10.03 ? 51   GLY H N   1 
ATOM   8026  C  CA  . GLY H  1 51  ? 38.515  80.240  89.099  1.00 9.68  ? 51   GLY H CA  1 
ATOM   8027  C  C   . GLY H  1 51  ? 37.701  80.227  87.819  1.00 10.30 ? 51   GLY H C   1 
ATOM   8028  O  O   . GLY H  1 51  ? 37.828  81.102  86.974  1.00 10.86 ? 51   GLY H O   1 
ATOM   8029  N  N   . ASP H  1 52  ? 36.859  79.214  87.680  1.00 10.71 ? 52   ASP H N   1 
ATOM   8030  C  CA  . ASP H  1 52  ? 36.036  79.003  86.489  1.00 11.53 ? 52   ASP H CA  1 
ATOM   8031  C  C   . ASP H  1 52  ? 34.562  79.044  86.855  1.00 11.94 ? 52   ASP H C   1 
ATOM   8032  O  O   . ASP H  1 52  ? 34.048  78.173  87.552  1.00 11.51 ? 52   ASP H O   1 
ATOM   8033  C  CB  . ASP H  1 52  ? 36.362  77.644  85.904  1.00 10.96 ? 52   ASP H CB  1 
ATOM   8034  C  CG  . ASP H  1 52  ? 35.571  77.331  84.652  1.00 12.50 ? 52   ASP H CG  1 
ATOM   8035  O  OD1 . ASP H  1 52  ? 34.515  77.960  84.392  1.00 13.69 ? 52   ASP H OD1 1 
ATOM   8036  O  OD2 . ASP H  1 52  ? 35.936  76.425  83.880  1.00 12.51 ? 52   ASP H OD2 1 
ATOM   8037  N  N   . ASN H  1 53  ? 33.905  80.080  86.361  1.00 13.14 ? 53   ASN H N   1 
ATOM   8038  C  CA  . ASN H  1 53  ? 32.499  80.324  86.617  1.00 14.37 ? 53   ASN H CA  1 
ATOM   8039  C  C   . ASN H  1 53  ? 31.636  80.145  85.364  1.00 12.97 ? 53   ASN H C   1 
ATOM   8040  O  O   . ASN H  1 53  ? 30.560  80.710  85.277  1.00 12.21 ? 53   ASN H O   1 
ATOM   8041  C  CB  . ASN H  1 53  ? 32.327  81.766  87.096  1.00 15.66 ? 53   ASN H CB  1 
ATOM   8042  C  CG  . ASN H  1 53  ? 30.920  82.042  87.641  1.00 19.72 ? 53   ASN H CG  1 
ATOM   8043  O  OD1 . ASN H  1 53  ? 30.229  82.979  87.200  1.00 25.04 ? 53   ASN H OD1 1 
ATOM   8044  N  ND2 . ASN H  1 53  ? 30.491  81.224  88.576  1.00 22.56 ? 53   ASN H ND2 1 
ATOM   8045  N  N   . THR H  1 54  ? 32.121  79.405  84.381  1.00 13.07 ? 54   THR H N   1 
ATOM   8046  C  CA  . THR H  1 54  ? 31.365  79.268  83.129  1.00 14.57 ? 54   THR H CA  1 
ATOM   8047  C  C   . THR H  1 54  ? 30.048  78.525  83.322  1.00 15.20 ? 54   THR H C   1 
ATOM   8048  O  O   . THR H  1 54  ? 29.087  78.793  82.601  1.00 15.95 ? 54   THR H O   1 
ATOM   8049  C  CB  . THR H  1 54  ? 32.189  78.593  82.024  1.00 14.10 ? 54   THR H CB  1 
ATOM   8050  O  OG1 . THR H  1 54  ? 32.762  77.385  82.545  1.00 14.53 ? 54   THR H OG1 1 
ATOM   8051  C  CG2 . THR H  1 54  ? 33.387  79.448  81.631  1.00 14.00 ? 54   THR H CG2 1 
ATOM   8052  N  N   . ALA H  1 55  ? 30.006  77.606  84.288  1.00 15.70 ? 55   ALA H N   1 
ATOM   8053  C  CA  . ALA H  1 55  ? 28.779  76.880  84.599  1.00 15.91 ? 55   ALA H CA  1 
ATOM   8054  C  C   . ALA H  1 55  ? 28.377  77.229  86.007  1.00 15.96 ? 55   ALA H C   1 
ATOM   8055  O  O   . ALA H  1 55  ? 27.966  76.359  86.799  1.00 16.43 ? 55   ALA H O   1 
ATOM   8056  C  CB  . ALA H  1 55  ? 28.961  75.360  84.452  1.00 16.40 ? 55   ALA H CB  1 
ATOM   8057  N  N   . GLY H  1 56  ? 28.522  78.500  86.367  1.00 14.83 ? 56   GLY H N   1 
ATOM   8058  C  CA  . GLY H  1 56  ? 28.177  78.900  87.728  1.00 14.45 ? 56   GLY H CA  1 
ATOM   8059  C  C   . GLY H  1 56  ? 29.198  78.402  88.747  1.00 14.26 ? 56   GLY H C   1 
ATOM   8060  O  O   . GLY H  1 56  ? 30.324  78.103  88.379  1.00 13.69 ? 56   GLY H O   1 
ATOM   8061  N  N   . CYS H  1 57  ? 28.785  78.250  90.012  1.00 14.13 ? 57   CYS H N   1 
ATOM   8062  C  CA  . CYS H  1 57  ? 29.688  77.778  91.051  1.00 14.49 ? 57   CYS H CA  1 
ATOM   8063  C  C   . CYS H  1 57  ? 30.102  76.330  90.837  1.00 13.87 ? 57   CYS H C   1 
ATOM   8064  O  O   . CYS H  1 57  ? 31.108  75.879  91.360  1.00 13.34 ? 57   CYS H O   1 
ATOM   8065  C  CB  . CYS H  1 57  ? 29.068  77.996  92.444  1.00 13.50 ? 57   CYS H CB  1 
ATOM   8066  S  SG  . CYS H  1 57  ? 28.773  79.763  92.729  1.00 20.41 ? 57   CYS H SG  1 
ATOM   8067  N  N   . THR H  1 58  ? 29.326  75.601  90.049  1.00 12.70 ? 58   THR H N   1 
ATOM   8068  C  CA  . THR H  1 58  ? 29.673  74.215  89.763  1.00 13.62 ? 58   THR H CA  1 
ATOM   8069  C  C   . THR H  1 58  ? 31.066  74.024  89.122  1.00 12.90 ? 58   THR H C   1 
ATOM   8070  O  O   . THR H  1 58  ? 31.827  73.133  89.507  1.00 11.90 ? 58   THR H O   1 
ATOM   8071  C  CB  . THR H  1 58  ? 28.585  73.585  88.883  1.00 13.36 ? 58   THR H CB  1 
ATOM   8072  O  OG1 . THR H  1 58  ? 27.348  73.560  89.617  1.00 14.90 ? 58   THR H OG1 1 
ATOM   8073  C  CG2 . THR H  1 58  ? 28.869  72.086  88.672  1.00 16.42 ? 58   THR H CG2 1 
ATOM   8074  N  N   . SER H  1 59  ? 31.409  74.862  88.154  1.00 12.10 ? 59   SER H N   1 
ATOM   8075  C  CA  . SER H  1 59  ? 32.704  74.727  87.486  1.00 12.26 ? 59   SER H CA  1 
ATOM   8076  C  C   . SER H  1 59  ? 33.930  75.113  88.332  1.00 12.13 ? 59   SER H C   1 
ATOM   8077  O  O   . SER H  1 59  ? 35.062  74.970  87.878  1.00 11.21 ? 59   SER H O   1 
ATOM   8078  C  CB  . SER H  1 59  ? 32.705  75.481  86.145  1.00 12.93 ? 59   SER H CB  1 
ATOM   8079  O  OG  . SER H  1 59  ? 31.902  76.637  86.242  1.00 15.19 ? 59   SER H OG  1 
ATOM   8080  N  N   . ALA H  1 60  ? 33.719  75.593  89.559  1.00 10.92 ? 60   ALA H N   1 
ATOM   8081  C  CA  . ALA H  1 60  ? 34.842  75.888  90.437  1.00 12.12 ? 60   ALA H CA  1 
ATOM   8082  C  C   . ALA H  1 60  ? 35.533  74.610  90.895  1.00 12.09 ? 60   ALA H C   1 
ATOM   8083  O  O   . ALA H  1 60  ? 36.630  74.640  91.441  1.00 11.49 ? 60   ALA H O   1 
ATOM   8084  C  CB  . ALA H  1 60  ? 34.379  76.683  91.677  1.00 10.77 ? 60   ALA H CB  1 
ATOM   8085  N  N   . GLY H  1 61  ? 34.892  73.477  90.677  1.00 11.97 ? 61   GLY H N   1 
ATOM   8086  C  CA  . GLY H  1 61  ? 35.510  72.237  91.073  1.00 12.15 ? 61   GLY H CA  1 
ATOM   8087  C  C   . GLY H  1 61  ? 35.442  72.014  92.578  1.00 11.08 ? 61   GLY H C   1 
ATOM   8088  O  O   . GLY H  1 61  ? 34.672  72.634  93.287  1.00 11.46 ? 61   GLY H O   1 
ATOM   8089  N  N   . PRO H  1 62  ? 36.288  71.126  93.048  1.00 11.05 ? 62   PRO H N   1 
ATOM   8090  C  CA  . PRO H  1 62  ? 36.302  70.712  94.449  1.00 10.56 ? 62   PRO H CA  1 
ATOM   8091  C  C   . PRO H  1 62  ? 37.141  71.649  95.298  1.00 10.35 ? 62   PRO H C   1 
ATOM   8092  O  O   . PRO H  1 62  ? 37.661  72.663  94.839  1.00 8.82  ? 62   PRO H O   1 
ATOM   8093  C  CB  . PRO H  1 62  ? 36.988  69.361  94.365  1.00 10.78 ? 62   PRO H CB  1 
ATOM   8094  C  CG  . PRO H  1 62  ? 38.054  69.670  93.355  1.00 11.78 ? 62   PRO H CG  1 
ATOM   8095  C  CD  . PRO H  1 62  ? 37.301  70.410  92.249  1.00 11.07 ? 62   PRO H CD  1 
ATOM   8096  N  N   . HIS H  1 63  ? 37.298  71.294  96.563  1.00 8.83  ? 63   HIS H N   1 
ATOM   8097  C  CA  . HIS H  1 63  ? 38.084  72.177  97.442  1.00 9.93  ? 63   HIS H CA  1 
ATOM   8098  C  C   . HIS H  1 63  ? 39.536  72.229  97.019  1.00 9.95  ? 63   HIS H C   1 
ATOM   8099  O  O   . HIS H  1 63  ? 40.079  71.209  96.592  1.00 9.85  ? 63   HIS H O   1 
ATOM   8100  C  CB  . HIS H  1 63  ? 38.020  71.652  98.865  1.00 8.53  ? 63   HIS H CB  1 
ATOM   8101  C  CG  . HIS H  1 63  ? 36.668  71.788  99.464  1.00 11.46 ? 63   HIS H CG  1 
ATOM   8102  N  ND1 . HIS H  1 63  ? 36.346  71.306  100.719 1.00 9.28  ? 63   HIS H ND1 1 
ATOM   8103  C  CD2 . HIS H  1 63  ? 35.547  72.369  98.969  1.00 11.36 ? 63   HIS H CD2 1 
ATOM   8104  C  CE1 . HIS H  1 63  ? 35.071  71.578  100.957 1.00 11.58 ? 63   HIS H CE1 1 
ATOM   8105  N  NE2 . HIS H  1 63  ? 34.571  72.245  99.924  1.00 12.50 ? 63   HIS H NE2 1 
ATOM   8106  N  N   . PHE H  1 64  ? 40.172  73.398  97.121  1.00 10.15 ? 64   PHE H N   1 
ATOM   8107  C  CA  . PHE H  1 64  ? 41.583  73.512  96.719  1.00 11.24 ? 64   PHE H CA  1 
ATOM   8108  C  C   . PHE H  1 64  ? 42.380  72.592  97.630  1.00 11.46 ? 64   PHE H C   1 
ATOM   8109  O  O   . PHE H  1 64  ? 42.315  72.721  98.851  1.00 10.79 ? 64   PHE H O   1 
ATOM   8110  C  CB  . PHE H  1 64  ? 42.058  74.958  96.840  1.00 11.65 ? 64   PHE H CB  1 
ATOM   8111  C  CG  . PHE H  1 64  ? 43.518  75.188  96.474  1.00 12.49 ? 64   PHE H CG  1 
ATOM   8112  C  CD1 . PHE H  1 64  ? 44.100  74.597  95.360  1.00 11.43 ? 64   PHE H CD1 1 
ATOM   8113  C  CD2 . PHE H  1 64  ? 44.281  76.070  97.233  1.00 13.65 ? 64   PHE H CD2 1 
ATOM   8114  C  CE1 . PHE H  1 64  ? 45.442  74.854  95.036  1.00 11.87 ? 64   PHE H CE1 1 
ATOM   8115  C  CE2 . PHE H  1 64  ? 45.597  76.341  96.910  1.00 15.82 ? 64   PHE H CE2 1 
ATOM   8116  C  CZ  . PHE H  1 64  ? 46.179  75.739  95.812  1.00 13.01 ? 64   PHE H CZ  1 
ATOM   8117  N  N   . ASN H  1 65  ? 43.137  71.669  97.035  1.00 12.33 ? 65   ASN H N   1 
ATOM   8118  C  CA  . ASN H  1 65  ? 43.732  70.574  97.804  1.00 14.07 ? 65   ASN H CA  1 
ATOM   8119  C  C   . ASN H  1 65  ? 45.039  70.080  97.202  1.00 14.15 ? 65   ASN H C   1 
ATOM   8120  O  O   . ASN H  1 65  ? 45.175  68.912  96.816  1.00 13.44 ? 65   ASN H O   1 
ATOM   8121  C  CB  . ASN H  1 65  ? 42.718  69.421  97.887  1.00 13.67 ? 65   ASN H CB  1 
ATOM   8122  C  CG  . ASN H  1 65  ? 43.165  68.285  98.789  1.00 14.85 ? 65   ASN H CG  1 
ATOM   8123  O  OD1 . ASN H  1 65  ? 44.010  68.457  99.677  1.00 11.64 ? 65   ASN H OD1 1 
ATOM   8124  N  ND2 . ASN H  1 65  ? 42.578  67.090  98.565  1.00 13.67 ? 65   ASN H ND2 1 
ATOM   8125  N  N   . PRO H  1 66  ? 46.007  70.980  97.125  1.00 15.22 ? 66   PRO H N   1 
ATOM   8126  C  CA  . PRO H  1 66  ? 47.296  70.658  96.514  1.00 16.08 ? 66   PRO H CA  1 
ATOM   8127  C  C   . PRO H  1 66  ? 48.047  69.562  97.251  1.00 17.04 ? 66   PRO H C   1 
ATOM   8128  O  O   . PRO H  1 66  ? 48.888  68.913  96.615  1.00 17.05 ? 66   PRO H O   1 
ATOM   8129  C  CB  . PRO H  1 66  ? 48.060  71.976  96.608  1.00 16.33 ? 66   PRO H CB  1 
ATOM   8130  C  CG  . PRO H  1 66  ? 47.418  72.659  97.774  1.00 15.83 ? 66   PRO H CG  1 
ATOM   8131  C  CD  . PRO H  1 66  ? 45.947  72.376  97.596  1.00 14.94 ? 66   PRO H CD  1 
ATOM   8132  N  N   . LEU H  1 67  ? 47.764  69.361  98.538  1.00 17.76 ? 67   LEU H N   1 
ATOM   8133  C  CA  . LEU H  1 67  ? 48.457  68.334  99.319  1.00 18.52 ? 67   LEU H CA  1 
ATOM   8134  C  C   . LEU H  1 67  ? 47.729  67.006  99.378  1.00 18.65 ? 67   LEU H C   1 
ATOM   8135  O  O   . LEU H  1 67  ? 48.141  66.113  100.108 1.00 18.94 ? 67   LEU H O   1 
ATOM   8136  C  CB  . LEU H  1 67  ? 48.796  68.828  100.730 1.00 18.84 ? 67   LEU H CB  1 
ATOM   8137  C  CG  . LEU H  1 67  ? 49.727  70.049  100.769 1.00 19.94 ? 67   LEU H CG  1 
ATOM   8138  C  CD1 . LEU H  1 67  ? 50.015  70.431  102.192 1.00 21.39 ? 67   LEU H CD1 1 
ATOM   8139  C  CD2 . LEU H  1 67  ? 51.028  69.725  100.052 1.00 22.05 ? 67   LEU H CD2 1 
ATOM   8140  N  N   . SER H  1 68  ? 46.649  66.876  98.614  1.00 19.01 ? 68   SER H N   1 
ATOM   8141  C  CA  . SER H  1 68  ? 45.913  65.611  98.525  1.00 19.32 ? 68   SER H CA  1 
ATOM   8142  C  C   . SER H  1 68  ? 45.480  65.064  99.882  1.00 19.86 ? 68   SER H C   1 
ATOM   8143  O  O   . SER H  1 68  ? 45.673  63.878  100.199 1.00 19.09 ? 68   SER H O   1 
ATOM   8144  C  CB  . SER H  1 68  ? 46.751  64.569  97.777  1.00 19.84 ? 68   SER H CB  1 
ATOM   8145  O  OG  . SER H  1 68  ? 47.384  65.147  96.651  1.00 21.33 ? 68   SER H OG  1 
ATOM   8146  N  N   . ARG H  1 69  ? 44.865  65.915  100.692 1.00 18.78 ? 69   ARG H N   1 
ATOM   8147  C  CA  . ARG H  1 69  ? 44.457  65.475  102.015 1.00 18.74 ? 69   ARG H CA  1 
ATOM   8148  C  C   . ARG H  1 69  ? 42.944  65.402  102.090 1.00 18.17 ? 69   ARG H C   1 
ATOM   8149  O  O   . ARG H  1 69  ? 42.276  65.744  101.128 1.00 18.56 ? 69   ARG H O   1 
ATOM   8150  C  CB  . ARG H  1 69  ? 45.050  66.389  103.089 1.00 19.00 ? 69   ARG H CB  1 
ATOM   8151  C  CG  . ARG H  1 69  ? 46.570  66.404  103.048 1.00 22.04 ? 69   ARG H CG  1 
ATOM   8152  C  CD  . ARG H  1 69  ? 47.261  66.415  104.403 1.00 29.14 ? 69   ARG H CD  1 
ATOM   8153  N  NE  . ARG H  1 69  ? 47.841  67.711  104.743 1.00 33.35 ? 69   ARG H NE  1 
ATOM   8154  C  CZ  . ARG H  1 69  ? 49.148  67.933  104.896 1.00 35.59 ? 69   ARG H CZ  1 
ATOM   8155  N  NH1 . ARG H  1 69  ? 50.020  66.950  104.733 1.00 35.89 ? 69   ARG H NH1 1 
ATOM   8156  N  NH2 . ARG H  1 69  ? 49.586  69.147  105.205 1.00 38.19 ? 69   ARG H NH2 1 
ATOM   8157  N  N   . LYS H  1 70  ? 42.407  64.890  103.197 1.00 17.44 ? 70   LYS H N   1 
ATOM   8158  C  CA  . LYS H  1 70  ? 40.963  64.847  103.400 1.00 17.06 ? 70   LYS H CA  1 
ATOM   8159  C  C   . LYS H  1 70  ? 40.459  66.155  103.995 1.00 15.59 ? 70   LYS H C   1 
ATOM   8160  O  O   . LYS H  1 70  ? 41.240  66.958  104.516 1.00 15.27 ? 70   LYS H O   1 
ATOM   8161  C  CB  . LYS H  1 70  ? 40.577  63.706  104.350 1.00 17.93 ? 70   LYS H CB  1 
ATOM   8162  C  CG  . LYS H  1 70  ? 41.169  62.366  103.939 1.00 21.00 ? 70   LYS H CG  1 
ATOM   8163  C  CD  . LYS H  1 70  ? 40.635  61.902  102.581 1.00 26.72 ? 70   LYS H CD  1 
ATOM   8164  C  CE  . LYS H  1 70  ? 41.197  60.523  102.216 1.00 31.07 ? 70   LYS H CE  1 
ATOM   8165  N  NZ  . LYS H  1 70  ? 40.213  59.701  101.459 1.00 34.33 ? 70   LYS H NZ  1 
ATOM   8166  N  N   . HIS H  1 71  ? 39.147  66.346  103.926 1.00 13.58 ? 71   HIS H N   1 
ATOM   8167  C  CA  . HIS H  1 71  ? 38.509  67.553  104.400 1.00 12.68 ? 71   HIS H CA  1 
ATOM   8168  C  C   . HIS H  1 71  ? 38.525  67.665  105.906 1.00 12.53 ? 71   HIS H C   1 
ATOM   8169  O  O   . HIS H  1 71  ? 38.273  66.696  106.621 1.00 12.05 ? 71   HIS H O   1 
ATOM   8170  C  CB  . HIS H  1 71  ? 37.070  67.589  103.925 1.00 11.63 ? 71   HIS H CB  1 
ATOM   8171  C  CG  . HIS H  1 71  ? 36.334  68.801  104.367 1.00 12.46 ? 71   HIS H CG  1 
ATOM   8172  N  ND1 . HIS H  1 71  ? 36.408  69.994  103.686 1.00 8.33  ? 71   HIS H ND1 1 
ATOM   8173  C  CD2 . HIS H  1 71  ? 35.525  69.018  105.427 1.00 12.04 ? 71   HIS H CD2 1 
ATOM   8174  C  CE1 . HIS H  1 71  ? 35.659  70.894  104.295 1.00 9.13  ? 71   HIS H CE1 1 
ATOM   8175  N  NE2 . HIS H  1 71  ? 35.137  70.338  105.375 1.00 11.05 ? 71   HIS H NE2 1 
ATOM   8176  N  N   . GLY H  1 72  ? 38.810  68.856  106.403 1.00 11.40 ? 72   GLY H N   1 
ATOM   8177  C  CA  . GLY H  1 72  ? 38.764  69.064  107.836 1.00 12.06 ? 72   GLY H CA  1 
ATOM   8178  C  C   . GLY H  1 72  ? 38.363  70.489  108.136 1.00 11.73 ? 72   GLY H C   1 
ATOM   8179  O  O   . GLY H  1 72  ? 37.924  71.220  107.246 1.00 12.26 ? 72   GLY H O   1 
ATOM   8180  N  N   . GLY H  1 73  ? 38.489  70.875  109.392 1.00 11.58 ? 73   GLY H N   1 
ATOM   8181  C  CA  . GLY H  1 73  ? 38.270  72.258  109.763 1.00 11.87 ? 73   GLY H CA  1 
ATOM   8182  C  C   . GLY H  1 73  ? 39.601  72.999  109.640 1.00 12.11 ? 73   GLY H C   1 
ATOM   8183  O  O   . GLY H  1 73  ? 40.666  72.391  109.554 1.00 11.60 ? 73   GLY H O   1 
ATOM   8184  N  N   . PRO H  1 74  ? 39.554  74.318  109.637 1.00 12.40 ? 74   PRO H N   1 
ATOM   8185  C  CA  . PRO H  1 74  ? 40.782  75.098  109.450 1.00 13.83 ? 74   PRO H CA  1 
ATOM   8186  C  C   . PRO H  1 74  ? 41.802  74.812  110.546 1.00 14.56 ? 74   PRO H C   1 
ATOM   8187  O  O   . PRO H  1 74  ? 43.009  74.878  110.285 1.00 14.71 ? 74   PRO H O   1 
ATOM   8188  C  CB  . PRO H  1 74  ? 40.322  76.561  109.504 1.00 14.20 ? 74   PRO H CB  1 
ATOM   8189  C  CG  . PRO H  1 74  ? 38.854  76.552  109.924 1.00 13.87 ? 74   PRO H CG  1 
ATOM   8190  C  CD  . PRO H  1 74  ? 38.345  75.132  109.799 1.00 12.98 ? 74   PRO H CD  1 
ATOM   8191  N  N   . LYS H  1 75  ? 41.332  74.473  111.753 1.00 15.50 ? 75   LYS H N   1 
ATOM   8192  C  CA  . LYS H  1 75  ? 42.258  74.204  112.841 1.00 17.70 ? 75   LYS H CA  1 
ATOM   8193  C  C   . LYS H  1 75  ? 42.796  72.767  112.817 1.00 18.39 ? 75   LYS H C   1 
ATOM   8194  O  O   . LYS H  1 75  ? 43.672  72.412  113.607 1.00 19.18 ? 75   LYS H O   1 
ATOM   8195  C  CB  . LYS H  1 75  ? 41.623  74.577  114.210 1.00 18.03 ? 75   LYS H CB  1 
ATOM   8196  C  CG  . LYS H  1 75  ? 41.118  76.052  114.278 1.00 20.51 ? 75   LYS H CG  1 
ATOM   8197  C  CD  . LYS H  1 75  ? 40.955  76.598  115.700 1.00 28.26 ? 75   LYS H CD  1 
ATOM   8198  C  CE  . LYS H  1 75  ? 40.309  78.026  115.735 1.00 31.94 ? 75   LYS H CE  1 
ATOM   8199  N  NZ  . LYS H  1 75  ? 40.793  79.027  114.676 1.00 33.47 ? 75   LYS H NZ  1 
ATOM   8200  N  N   . ASP H  1 76  ? 42.294  71.928  111.912 1.00 18.61 ? 76   ASP H N   1 
ATOM   8201  C  CA  . ASP H  1 76  ? 42.775  70.549  111.867 1.00 19.47 ? 76   ASP H CA  1 
ATOM   8202  C  C   . ASP H  1 76  ? 44.076  70.433  111.115 1.00 20.34 ? 76   ASP H C   1 
ATOM   8203  O  O   . ASP H  1 76  ? 44.315  71.154  110.142 1.00 20.42 ? 76   ASP H O   1 
ATOM   8204  C  CB  . ASP H  1 76  ? 41.767  69.606  111.222 1.00 19.20 ? 76   ASP H CB  1 
ATOM   8205  C  CG  . ASP H  1 76  ? 40.503  69.480  112.034 1.00 21.78 ? 76   ASP H CG  1 
ATOM   8206  O  OD1 . ASP H  1 76  ? 40.625  69.354  113.276 1.00 24.65 ? 76   ASP H OD1 1 
ATOM   8207  O  OD2 . ASP H  1 76  ? 39.360  69.510  111.525 1.00 21.17 ? 76   ASP H OD2 1 
ATOM   8208  N  N   . GLU H  1 77  ? 44.914  69.503  111.568 1.00 20.90 ? 77   GLU H N   1 
ATOM   8209  C  CA  . GLU H  1 77  ? 46.165  69.235  110.880 1.00 21.96 ? 77   GLU H CA  1 
ATOM   8210  C  C   . GLU H  1 77  ? 45.843  68.631  109.508 1.00 20.44 ? 77   GLU H C   1 
ATOM   8211  O  O   . GLU H  1 77  ? 46.492  68.943  108.493 1.00 21.32 ? 77   GLU H O   1 
ATOM   8212  C  CB  . GLU H  1 77  ? 46.957  68.252  111.723 1.00 23.45 ? 77   GLU H CB  1 
ATOM   8213  C  CG  . GLU H  1 77  ? 48.455  68.427  111.706 1.00 28.64 ? 77   GLU H CG  1 
ATOM   8214  C  CD  . GLU H  1 77  ? 49.121  67.496  112.706 1.00 34.99 ? 77   GLU H CD  1 
ATOM   8215  O  OE1 . GLU H  1 77  ? 49.612  67.995  113.756 1.00 38.59 ? 77   GLU H OE1 1 
ATOM   8216  O  OE2 . GLU H  1 77  ? 49.131  66.262  112.454 1.00 37.53 ? 77   GLU H OE2 1 
ATOM   8217  N  N   . GLU H  1 78  ? 44.818  67.779  109.475 1.00 18.76 ? 78   GLU H N   1 
ATOM   8218  C  CA  . GLU H  1 78  ? 44.362  67.156  108.243 1.00 17.30 ? 78   GLU H CA  1 
ATOM   8219  C  C   . GLU H  1 78  ? 43.206  67.969  107.644 1.00 16.38 ? 78   GLU H C   1 
ATOM   8220  O  O   . GLU H  1 78  ? 42.068  67.913  108.109 1.00 15.09 ? 78   GLU H O   1 
ATOM   8221  C  CB  . GLU H  1 78  ? 43.931  65.691  108.483 1.00 17.89 ? 78   GLU H CB  1 
ATOM   8222  C  CG  . GLU H  1 78  ? 43.397  64.971  107.237 1.00 18.91 ? 78   GLU H CG  1 
ATOM   8223  C  CD  . GLU H  1 78  ? 44.480  64.361  106.342 1.00 23.24 ? 78   GLU H CD  1 
ATOM   8224  O  OE1 . GLU H  1 78  ? 45.687  64.462  106.677 1.00 24.38 ? 78   GLU H OE1 1 
ATOM   8225  O  OE2 . GLU H  1 78  ? 44.127  63.774  105.283 1.00 21.00 ? 78   GLU H OE2 1 
ATOM   8226  N  N   . ARG H  1 79  ? 43.504  68.740  106.602 1.00 14.77 ? 79   ARG H N   1 
ATOM   8227  C  CA  . ARG H  1 79  ? 42.478  69.536  105.968 1.00 12.44 ? 79   ARG H CA  1 
ATOM   8228  C  C   . ARG H  1 79  ? 42.946  69.844  104.565 1.00 12.05 ? 79   ARG H C   1 
ATOM   8229  O  O   . ARG H  1 79  ? 44.118  69.637  104.213 1.00 11.64 ? 79   ARG H O   1 
ATOM   8230  C  CB  . ARG H  1 79  ? 42.298  70.866  106.702 1.00 11.54 ? 79   ARG H CB  1 
ATOM   8231  C  CG  . ARG H  1 79  ? 43.594  71.648  106.825 1.00 10.98 ? 79   ARG H CG  1 
ATOM   8232  C  CD  . ARG H  1 79  ? 43.437  73.053  107.361 1.00 9.47  ? 79   ARG H CD  1 
ATOM   8233  N  NE  . ARG H  1 79  ? 43.196  74.047  106.290 1.00 6.23  ? 79   ARG H NE  1 
ATOM   8234  C  CZ  . ARG H  1 79  ? 43.288  75.369  106.466 1.00 8.85  ? 79   ARG H CZ  1 
ATOM   8235  N  NH1 . ARG H  1 79  ? 43.546  75.869  107.678 1.00 8.01  ? 79   ARG H NH1 1 
ATOM   8236  N  NH2 . ARG H  1 79  ? 43.093  76.211  105.422 1.00 8.24  ? 79   ARG H NH2 1 
ATOM   8237  N  N   . HIS H  1 80  ? 42.006  70.304  103.761 1.00 11.33 ? 80   HIS H N   1 
ATOM   8238  C  CA  . HIS H  1 80  ? 42.335  70.835  102.452 1.00 10.88 ? 80   HIS H CA  1 
ATOM   8239  C  C   . HIS H  1 80  ? 42.879  72.241  102.649 1.00 10.50 ? 80   HIS H C   1 
ATOM   8240  O  O   . HIS H  1 80  ? 42.451  72.951  103.551 1.00 10.12 ? 80   HIS H O   1 
ATOM   8241  C  CB  . HIS H  1 80  ? 41.053  70.981  101.652 1.00 11.10 ? 80   HIS H CB  1 
ATOM   8242  C  CG  . HIS H  1 80  ? 40.335  69.691  101.401 1.00 13.10 ? 80   HIS H CG  1 
ATOM   8243  N  ND1 . HIS H  1 80  ? 38.959  69.600  101.399 1.00 12.11 ? 80   HIS H ND1 1 
ATOM   8244  C  CD2 . HIS H  1 80  ? 40.798  68.461  101.070 1.00 14.29 ? 80   HIS H CD2 1 
ATOM   8245  C  CE1 . HIS H  1 80  ? 38.610  68.370  101.069 1.00 15.86 ? 80   HIS H CE1 1 
ATOM   8246  N  NE2 . HIS H  1 80  ? 39.705  67.656  100.867 1.00 12.52 ? 80   HIS H NE2 1 
ATOM   8247  N  N   . VAL H  1 81  ? 43.807  72.673  101.795 1.00 8.74  ? 81   VAL H N   1 
ATOM   8248  C  CA  . VAL H  1 81  ? 44.229  74.070  101.874 1.00 8.06  ? 81   VAL H CA  1 
ATOM   8249  C  C   . VAL H  1 81  ? 43.007  75.008  101.840 1.00 7.80  ? 81   VAL H C   1 
ATOM   8250  O  O   . VAL H  1 81  ? 42.936  76.017  102.581 1.00 7.54  ? 81   VAL H O   1 
ATOM   8251  C  CB  . VAL H  1 81  ? 45.176  74.395  100.708 1.00 7.48  ? 81   VAL H CB  1 
ATOM   8252  C  CG1 . VAL H  1 81  ? 45.395  75.884  100.612 1.00 9.52  ? 81   VAL H CG1 1 
ATOM   8253  C  CG2 . VAL H  1 81  ? 46.508  73.625  100.924 1.00 8.68  ? 81   VAL H CG2 1 
ATOM   8254  N  N   . GLY H  1 82  ? 42.023  74.682  101.012 1.00 7.10  ? 82   GLY H N   1 
ATOM   8255  C  CA  . GLY H  1 82  ? 40.844  75.544  100.919 1.00 8.09  ? 82   GLY H CA  1 
ATOM   8256  C  C   . GLY H  1 82  ? 39.837  75.518  102.085 1.00 8.78  ? 82   GLY H C   1 
ATOM   8257  O  O   . GLY H  1 82  ? 38.807  76.211  102.022 1.00 9.30  ? 82   GLY H O   1 
ATOM   8258  N  N   . ASP H  1 83  ? 40.114  74.746  103.137 1.00 7.99  ? 83   ASP H N   1 
ATOM   8259  C  CA  . ASP H  1 83  ? 39.150  74.572  104.227 1.00 9.21  ? 83   ASP H CA  1 
ATOM   8260  C  C   . ASP H  1 83  ? 39.144  75.691  105.259 1.00 8.68  ? 83   ASP H C   1 
ATOM   8261  O  O   . ASP H  1 83  ? 39.914  75.641  106.249 1.00 9.04  ? 83   ASP H O   1 
ATOM   8262  C  CB  . ASP H  1 83  ? 39.411  73.249  104.956 1.00 9.25  ? 83   ASP H CB  1 
ATOM   8263  C  CG  . ASP H  1 83  ? 39.037  72.047  104.103 1.00 9.70  ? 83   ASP H CG  1 
ATOM   8264  O  OD1 . ASP H  1 83  ? 38.330  72.243  103.078 1.00 9.59  ? 83   ASP H OD1 1 
ATOM   8265  O  OD2 . ASP H  1 83  ? 39.401  70.879  104.377 1.00 9.63  ? 83   ASP H OD2 1 
ATOM   8266  N  N   . LEU H  1 84  ? 38.249  76.660  105.062 1.00 7.92  ? 84   LEU H N   1 
ATOM   8267  C  CA  . LEU H  1 84  ? 38.148  77.798  105.966 1.00 8.63  ? 84   LEU H CA  1 
ATOM   8268  C  C   . LEU H  1 84  ? 36.993  77.683  106.954 1.00 9.18  ? 84   LEU H C   1 
ATOM   8269  O  O   . LEU H  1 84  ? 36.671  78.653  107.640 1.00 10.19 ? 84   LEU H O   1 
ATOM   8270  C  CB  . LEU H  1 84  ? 38.009  79.106  105.178 1.00 7.81  ? 84   LEU H CB  1 
ATOM   8271  C  CG  . LEU H  1 84  ? 39.195  79.276  104.248 1.00 9.68  ? 84   LEU H CG  1 
ATOM   8272  C  CD1 . LEU H  1 84  ? 39.057  80.593  103.501 1.00 10.18 ? 84   LEU H CD1 1 
ATOM   8273  C  CD2 . LEU H  1 84  ? 40.466  79.346  105.127 1.00 11.25 ? 84   LEU H CD2 1 
ATOM   8274  N  N   . GLY H  1 85  ? 36.367  76.513  107.011 1.00 8.76  ? 85   GLY H N   1 
ATOM   8275  C  CA  . GLY H  1 85  ? 35.374  76.282  108.028 1.00 8.90  ? 85   GLY H CA  1 
ATOM   8276  C  C   . GLY H  1 85  ? 34.041  76.907  107.730 1.00 8.96  ? 85   GLY H C   1 
ATOM   8277  O  O   . GLY H  1 85  ? 33.531  76.752  106.629 1.00 8.11  ? 85   GLY H O   1 
ATOM   8278  N  N   . ASN H  1 86  ? 33.451  77.542  108.733 1.00 8.60  ? 86   ASN H N   1 
ATOM   8279  C  CA  . ASN H  1 86  ? 32.115  78.131  108.571 1.00 9.34  ? 86   ASN H CA  1 
ATOM   8280  C  C   . ASN H  1 86  ? 32.105  79.616  108.855 1.00 9.10  ? 86   ASN H C   1 
ATOM   8281  O  O   . ASN H  1 86  ? 32.974  80.100  109.544 1.00 7.88  ? 86   ASN H O   1 
ATOM   8282  C  CB  . ASN H  1 86  ? 31.148  77.519  109.594 1.00 9.53  ? 86   ASN H CB  1 
ATOM   8283  C  CG  . ASN H  1 86  ? 30.846  76.069  109.296 1.00 11.04 ? 86   ASN H CG  1 
ATOM   8284  O  OD1 . ASN H  1 86  ? 30.217  75.781  108.294 1.00 9.11  ? 86   ASN H OD1 1 
ATOM   8285  N  ND2 . ASN H  1 86  ? 31.309  75.151  110.161 1.00 9.32  ? 86   ASN H ND2 1 
ATOM   8286  N  N   . VAL H  1 87  ? 31.109  80.302  108.296 1.00 9.74  ? 87   VAL H N   1 
ATOM   8287  C  CA  . VAL H  1 87  ? 30.782  81.665  108.696 1.00 10.19 ? 87   VAL H CA  1 
ATOM   8288  C  C   . VAL H  1 87  ? 29.392  81.582  109.293 1.00 9.91  ? 87   VAL H C   1 
ATOM   8289  O  O   . VAL H  1 87  ? 28.684  80.597  109.068 1.00 11.03 ? 87   VAL H O   1 
ATOM   8290  C  CB  . VAL H  1 87  ? 30.825  82.622  107.526 1.00 9.94  ? 87   VAL H CB  1 
ATOM   8291  C  CG1 . VAL H  1 87  ? 32.241  82.554  106.935 1.00 12.77 ? 87   VAL H CG1 1 
ATOM   8292  C  CG2 . VAL H  1 87  ? 29.806  82.249  106.459 1.00 9.96  ? 87   VAL H CG2 1 
ATOM   8293  N  N   . THR H  1 88  ? 28.995  82.599  110.041 1.00 10.41 ? 88   THR H N   1 
ATOM   8294  C  CA  . THR H  1 88  ? 27.707  82.546  110.763 1.00 10.91 ? 88   THR H CA  1 
ATOM   8295  C  C   . THR H  1 88  ? 26.853  83.717  110.385 1.00 10.68 ? 88   THR H C   1 
ATOM   8296  O  O   . THR H  1 88  ? 27.280  84.882  110.541 1.00 10.56 ? 88   THR H O   1 
ATOM   8297  C  CB  . THR H  1 88  ? 27.933  82.578  112.303 1.00 11.36 ? 88   THR H CB  1 
ATOM   8298  O  OG1 . THR H  1 88  ? 28.854  81.545  112.710 1.00 11.14 ? 88   THR H OG1 1 
ATOM   8299  C  CG2 . THR H  1 88  ? 26.624  82.244  113.040 1.00 9.84  ? 88   THR H CG2 1 
ATOM   8300  N  N   . ALA H  1 89  ? 25.663  83.444  109.866 1.00 10.89 ? 89   ALA H N   1 
ATOM   8301  C  CA  . ALA H  1 89  ? 24.772  84.527  109.512 1.00 10.90 ? 89   ALA H CA  1 
ATOM   8302  C  C   . ALA H  1 89  ? 23.872  84.783  110.705 1.00 11.65 ? 89   ALA H C   1 
ATOM   8303  O  O   . ALA H  1 89  ? 23.454  83.843  111.370 1.00 12.48 ? 89   ALA H O   1 
ATOM   8304  C  CB  . ALA H  1 89  ? 23.937  84.186  108.285 1.00 10.99 ? 89   ALA H CB  1 
ATOM   8305  N  N   . ASP H  1 90  ? 23.557  86.041  110.944 1.00 12.10 ? 90   ASP H N   1 
ATOM   8306  C  CA  . ASP H  1 90  ? 22.735  86.446  112.102 1.00 14.13 ? 90   ASP H CA  1 
ATOM   8307  C  C   . ASP H  1 90  ? 21.248  86.383  111.767 1.00 14.29 ? 90   ASP H C   1 
ATOM   8308  O  O   . ASP H  1 90  ? 20.876  85.865  110.703 1.00 14.60 ? 90   ASP H O   1 
ATOM   8309  C  CB  . ASP H  1 90  ? 23.158  87.852  112.571 1.00 13.53 ? 90   ASP H CB  1 
ATOM   8310  C  CG  . ASP H  1 90  ? 22.776  88.949  111.594 1.00 14.44 ? 90   ASP H CG  1 
ATOM   8311  O  OD1 . ASP H  1 90  ? 22.083  88.687  110.582 1.00 14.41 ? 90   ASP H OD1 1 
ATOM   8312  O  OD2 . ASP H  1 90  ? 23.154  90.125  111.757 1.00 18.32 ? 90   ASP H OD2 1 
ATOM   8313  N  N   . LYS H  1 91  ? 20.382  86.889  112.654 1.00 16.11 ? 91   LYS H N   1 
ATOM   8314  C  CA  . LYS H  1 91  ? 18.949  86.785  112.386 1.00 17.23 ? 91   LYS H CA  1 
ATOM   8315  C  C   . LYS H  1 91  ? 18.564  87.549  111.118 1.00 17.42 ? 91   LYS H C   1 
ATOM   8316  O  O   . LYS H  1 91  ? 17.638  87.157  110.415 1.00 18.94 ? 91   LYS H O   1 
ATOM   8317  C  CB  . LYS H  1 91  ? 18.072  87.200  113.608 1.00 16.94 ? 91   LYS H CB  1 
ATOM   8318  C  CG  . LYS H  1 91  ? 18.216  88.674  113.998 1.00 20.37 ? 91   LYS H CG  1 
ATOM   8319  C  CD  . LYS H  1 91  ? 16.979  89.243  114.732 1.00 25.22 ? 91   LYS H CD  1 
ATOM   8320  C  CE  . LYS H  1 91  ? 16.879  90.778  114.523 1.00 26.76 ? 91   LYS H CE  1 
ATOM   8321  N  NZ  . LYS H  1 91  ? 15.543  91.356  114.888 1.00 28.99 ? 91   LYS H NZ  1 
ATOM   8322  N  N   . ASP H  1 92  ? 19.292  88.614  110.792 1.00 17.91 ? 92   ASP H N   1 
ATOM   8323  C  CA  . ASP H  1 92  ? 18.993  89.395  109.592 1.00 17.65 ? 92   ASP H CA  1 
ATOM   8324  C  C   . ASP H  1 92  ? 19.617  88.797  108.304 1.00 17.53 ? 92   ASP H C   1 
ATOM   8325  O  O   . ASP H  1 92  ? 19.541  89.402  107.244 1.00 17.00 ? 92   ASP H O   1 
ATOM   8326  C  CB  . ASP H  1 92  ? 19.468  90.843  109.770 1.00 18.23 ? 92   ASP H CB  1 
ATOM   8327  C  CG  . ASP H  1 92  ? 18.859  91.521  110.988 1.00 20.91 ? 92   ASP H CG  1 
ATOM   8328  O  OD1 . ASP H  1 92  ? 17.661  91.295  111.253 1.00 20.73 ? 92   ASP H OD1 1 
ATOM   8329  O  OD2 . ASP H  1 92  ? 19.509  92.294  111.738 1.00 23.09 ? 92   ASP H OD2 1 
ATOM   8330  N  N   . GLY H  1 93  ? 20.236  87.624  108.409 1.00 16.36 ? 93   GLY H N   1 
ATOM   8331  C  CA  . GLY H  1 93  ? 20.827  86.950  107.267 1.00 15.61 ? 93   GLY H CA  1 
ATOM   8332  C  C   . GLY H  1 93  ? 22.215  87.464  106.901 1.00 14.73 ? 93   GLY H C   1 
ATOM   8333  O  O   . GLY H  1 93  ? 22.737  87.191  105.809 1.00 15.71 ? 93   GLY H O   1 
ATOM   8334  N  N   . VAL H  1 94  ? 22.834  88.206  107.806 1.00 13.77 ? 94   VAL H N   1 
ATOM   8335  C  CA  . VAL H  1 94  ? 24.134  88.792  107.508 1.00 12.76 ? 94   VAL H CA  1 
ATOM   8336  C  C   . VAL H  1 94  ? 25.250  88.098  108.241 1.00 12.50 ? 94   VAL H C   1 
ATOM   8337  O  O   . VAL H  1 94  ? 25.179  87.943  109.462 1.00 13.22 ? 94   VAL H O   1 
ATOM   8338  C  CB  . VAL H  1 94  ? 24.192  90.273  107.888 1.00 13.19 ? 94   VAL H CB  1 
ATOM   8339  C  CG1 . VAL H  1 94  ? 25.568  90.856  107.522 1.00 14.87 ? 94   VAL H CG1 1 
ATOM   8340  C  CG2 . VAL H  1 94  ? 23.073  91.049  107.182 1.00 13.95 ? 94   VAL H CG2 1 
ATOM   8341  N  N   . ALA H  1 95  ? 26.260  87.644  107.493 1.00 10.31 ? 95   ALA H N   1 
ATOM   8342  C  CA  . ALA H  1 95  ? 27.458  87.091  108.096 1.00 10.76 ? 95   ALA H CA  1 
ATOM   8343  C  C   . ALA H  1 95  ? 28.590  88.103  108.003 1.00 10.67 ? 95   ALA H C   1 
ATOM   8344  O  O   . ALA H  1 95  ? 29.026  88.479  106.918 1.00 11.40 ? 95   ALA H O   1 
ATOM   8345  C  CB  . ALA H  1 95  ? 27.883  85.792  107.415 1.00 11.01 ? 95   ALA H CB  1 
ATOM   8346  N  N   . ASP H  1 96  ? 29.095  88.521  109.140 1.00 10.63 ? 96   ASP H N   1 
ATOM   8347  C  CA  . ASP H  1 96  ? 30.249  89.413  109.159 1.00 12.60 ? 96   ASP H CA  1 
ATOM   8348  C  C   . ASP H  1 96  ? 31.495  88.575  109.320 1.00 11.81 ? 96   ASP H C   1 
ATOM   8349  O  O   . ASP H  1 96  ? 31.867  88.153  110.397 1.00 13.50 ? 96   ASP H O   1 
ATOM   8350  C  CB  . ASP H  1 96  ? 30.089  90.427  110.259 1.00 14.35 ? 96   ASP H CB  1 
ATOM   8351  C  CG  . ASP H  1 96  ? 29.023  91.427  109.909 1.00 18.87 ? 96   ASP H CG  1 
ATOM   8352  O  OD1 . ASP H  1 96  ? 28.124  91.627  110.741 1.00 24.16 ? 96   ASP H OD1 1 
ATOM   8353  O  OD2 . ASP H  1 96  ? 28.970  91.995  108.781 1.00 22.27 ? 96   ASP H OD2 1 
ATOM   8354  N  N   . VAL H  1 97  ? 32.157  88.321  108.229 1.00 8.81  ? 97   VAL H N   1 
ATOM   8355  C  CA  . VAL H  1 97  ? 33.225  87.363  108.264 1.00 8.14  ? 97   VAL H CA  1 
ATOM   8356  C  C   . VAL H  1 97  ? 34.535  87.943  108.749 1.00 7.64  ? 97   VAL H C   1 
ATOM   8357  O  O   . VAL H  1 97  ? 34.936  89.071  108.370 1.00 5.75  ? 97   VAL H O   1 
ATOM   8358  C  CB  . VAL H  1 97  ? 33.457  86.832  106.824 1.00 8.57  ? 97   VAL H CB  1 
ATOM   8359  C  CG1 . VAL H  1 97  ? 34.626  85.832  106.813 1.00 9.70  ? 97   VAL H CG1 1 
ATOM   8360  C  CG2 . VAL H  1 97  ? 32.162  86.210  106.292 1.00 9.28  ? 97   VAL H CG2 1 
ATOM   8361  N  N   . SER H  1 98  ? 35.196  87.199  109.627 1.00 8.18  ? 98   SER H N   1 
ATOM   8362  C  CA  . SER H  1 98  ? 36.544  87.577  110.020 1.00 9.45  ? 98   SER H CA  1 
ATOM   8363  C  C   . SER H  1 98  ? 37.266  86.336  110.469 1.00 10.27 ? 98   SER H C   1 
ATOM   8364  O  O   . SER H  1 98  ? 36.944  85.782  111.541 1.00 10.25 ? 98   SER H O   1 
ATOM   8365  C  CB  . SER H  1 98  ? 36.551  88.626  111.143 1.00 10.06 ? 98   SER H CB  1 
ATOM   8366  O  OG  . SER H  1 98  ? 37.916  89.060  111.338 1.00 11.15 ? 98   SER H OG  1 
ATOM   8367  N  N   . ILE H  1 99  ? 38.247  85.919  109.665 1.00 8.92  ? 99   ILE H N   1 
ATOM   8368  C  CA  . ILE H  1 99  ? 38.981  84.681  109.844 1.00 10.53 ? 99   ILE H CA  1 
ATOM   8369  C  C   . ILE H  1 99  ? 40.466  84.998  109.626 1.00 11.10 ? 99   ILE H C   1 
ATOM   8370  O  O   . ILE H  1 99  ? 40.791  85.868  108.808 1.00 10.76 ? 99   ILE H O   1 
ATOM   8371  C  CB  . ILE H  1 99  ? 38.510  83.660  108.752 1.00 11.23 ? 99   ILE H CB  1 
ATOM   8372  C  CG1 . ILE H  1 99  ? 37.159  83.049  109.140 1.00 12.79 ? 99   ILE H CG1 1 
ATOM   8373  C  CG2 . ILE H  1 99  ? 39.536  82.525  108.604 1.00 14.49 ? 99   ILE H CG2 1 
ATOM   8374  C  CD1 . ILE H  1 99  ? 36.376  82.343  107.954 1.00 11.83 ? 99   ILE H CD1 1 
ATOM   8375  N  N   . GLU H  1 100 ? 41.365  84.311  110.322 1.00 8.95  ? 100  GLU H N   1 
ATOM   8376  C  CA  . GLU H  1 100 ? 42.781  84.466  110.026 1.00 10.42 ? 100  GLU H CA  1 
ATOM   8377  C  C   . GLU H  1 100 ? 43.254  83.061  109.773 1.00 9.97  ? 100  GLU H C   1 
ATOM   8378  O  O   . GLU H  1 100 ? 42.943  82.144  110.579 1.00 8.62  ? 100  GLU H O   1 
ATOM   8379  C  CB  . GLU H  1 100 ? 43.567  85.091  111.212 1.00 11.31 ? 100  GLU H CB  1 
ATOM   8380  C  CG  . GLU H  1 100 ? 45.079  84.985  110.991 1.00 16.80 ? 100  GLU H CG  1 
ATOM   8381  C  CD  . GLU H  1 100 ? 45.951  85.543  112.111 1.00 23.95 ? 100  GLU H CD  1 
ATOM   8382  O  OE1 . GLU H  1 100 ? 46.045  86.777  112.214 1.00 25.55 ? 100  GLU H OE1 1 
ATOM   8383  O  OE2 . GLU H  1 100 ? 46.569  84.737  112.852 1.00 24.18 ? 100  GLU H OE2 1 
ATOM   8384  N  N   . ASP H  1 101 ? 43.995  82.848  108.689 1.00 9.34  ? 101  ASP H N   1 
ATOM   8385  C  CA  . ASP H  1 101 ? 44.447  81.516  108.343 1.00 9.83  ? 101  ASP H CA  1 
ATOM   8386  C  C   . ASP H  1 101 ? 45.855  81.548  107.782 1.00 10.49 ? 101  ASP H C   1 
ATOM   8387  O  O   . ASP H  1 101 ? 46.214  82.446  106.981 1.00 10.54 ? 101  ASP H O   1 
ATOM   8388  C  CB  . ASP H  1 101 ? 43.514  80.900  107.306 1.00 9.02  ? 101  ASP H CB  1 
ATOM   8389  C  CG  . ASP H  1 101 ? 43.758  79.423  107.118 1.00 10.78 ? 101  ASP H CG  1 
ATOM   8390  O  OD1 . ASP H  1 101 ? 43.319  78.648  108.005 1.00 11.92 ? 101  ASP H OD1 1 
ATOM   8391  O  OD2 . ASP H  1 101 ? 44.405  78.946  106.154 1.00 10.41 ? 101  ASP H OD2 1 
ATOM   8392  N  N   . SER H  1 102 ? 46.641  80.550  108.135 1.00 10.20 ? 102  SER H N   1 
ATOM   8393  C  CA  . SER H  1 102 ? 48.036  80.527  107.679 1.00 10.85 ? 102  SER H CA  1 
ATOM   8394  C  C   . SER H  1 102 ? 48.354  79.388  106.749 1.00 10.13 ? 102  SER H C   1 
ATOM   8395  O  O   . SER H  1 102 ? 49.514  79.198  106.343 1.00 10.56 ? 102  SER H O   1 
ATOM   8396  C  CB  . SER H  1 102 ? 48.992  80.460  108.879 1.00 11.25 ? 102  SER H CB  1 
ATOM   8397  O  OG  . SER H  1 102 ? 48.963  81.698  109.579 1.00 14.65 ? 102  SER H OG  1 
ATOM   8398  N  N   . VAL H  1 103 ? 47.336  78.629  106.402 1.00 8.56  ? 103  VAL H N   1 
ATOM   8399  C  CA  . VAL H  1 103 ? 47.518  77.576  105.441 1.00 8.76  ? 103  VAL H CA  1 
ATOM   8400  C  C   . VAL H  1 103 ? 47.282  78.132  104.038 1.00 8.25  ? 103  VAL H C   1 
ATOM   8401  O  O   . VAL H  1 103 ? 48.072  77.880  103.125 1.00 8.35  ? 103  VAL H O   1 
ATOM   8402  C  CB  . VAL H  1 103 ? 46.642  76.394  105.804 1.00 9.96  ? 103  VAL H CB  1 
ATOM   8403  C  CG1 . VAL H  1 103 ? 46.633  75.348  104.703 1.00 10.31 ? 103  VAL H CG1 1 
ATOM   8404  C  CG2 . VAL H  1 103 ? 47.174  75.829  107.130 1.00 9.70  ? 103  VAL H CG2 1 
ATOM   8405  N  N   . ILE H  1 104 ? 46.198  78.862  103.822 1.00 7.99  ? 104  ILE H N   1 
ATOM   8406  C  CA  . ILE H  1 104 ? 46.087  79.546  102.514 1.00 7.10  ? 104  ILE H CA  1 
ATOM   8407  C  C   . ILE H  1 104 ? 47.216  80.584  102.434 1.00 7.87  ? 104  ILE H C   1 
ATOM   8408  O  O   . ILE H  1 104 ? 47.874  80.913  103.434 1.00 7.59  ? 104  ILE H O   1 
ATOM   8409  C  CB  . ILE H  1 104 ? 44.720  80.281  102.367 1.00 7.00  ? 104  ILE H CB  1 
ATOM   8410  C  CG1 . ILE H  1 104 ? 44.499  81.259  103.529 1.00 6.98  ? 104  ILE H CG1 1 
ATOM   8411  C  CG2 . ILE H  1 104 ? 43.540  79.282  102.228 1.00 7.41  ? 104  ILE H CG2 1 
ATOM   8412  C  CD1 . ILE H  1 104 ? 43.257  82.192  103.359 1.00 7.80  ? 104  ILE H CD1 1 
ATOM   8413  N  N   . SER H  1 105 ? 47.445  81.122  101.236 1.00 7.28  ? 105  SER H N   1 
ATOM   8414  C  CA  . SER H  1 105 ? 48.445  82.160  101.052 1.00 8.29  ? 105  SER H CA  1 
ATOM   8415  C  C   . SER H  1 105 ? 48.066  82.954  99.817  1.00 9.37  ? 105  SER H C   1 
ATOM   8416  O  O   . SER H  1 105 ? 47.281  82.493  99.001  1.00 9.83  ? 105  SER H O   1 
ATOM   8417  C  CB  . SER H  1 105 ? 49.852  81.566  100.852 1.00 8.24  ? 105  SER H CB  1 
ATOM   8418  O  OG  . SER H  1 105 ? 50.855  82.580  100.846 1.00 7.62  ? 105  SER H OG  1 
ATOM   8419  N  N   . LEU H  1 106 ? 48.598  84.154  99.711  1.00 9.60  ? 106  LEU H N   1 
ATOM   8420  C  CA  . LEU H  1 106 ? 48.395  84.972  98.516  1.00 11.41 ? 106  LEU H CA  1 
ATOM   8421  C  C   . LEU H  1 106 ? 49.630  84.893  97.614  1.00 13.29 ? 106  LEU H C   1 
ATOM   8422  O  O   . LEU H  1 106 ? 49.786  85.686  96.663  1.00 11.68 ? 106  LEU H O   1 
ATOM   8423  C  CB  . LEU H  1 106 ? 48.074  86.411  98.894  1.00 10.60 ? 106  LEU H CB  1 
ATOM   8424  C  CG  . LEU H  1 106 ? 46.805  86.504  99.728  1.00 10.49 ? 106  LEU H CG  1 
ATOM   8425  C  CD1 . LEU H  1 106 ? 46.480  87.967  100.056 1.00 8.80  ? 106  LEU H CD1 1 
ATOM   8426  C  CD2 . LEU H  1 106 ? 45.631  85.840  99.024  1.00 9.31  ? 106  LEU H CD2 1 
ATOM   8427  N  N   . SER H  1 107 ? 50.508  83.934  97.905  1.00 15.28 ? 107  SER H N   1 
ATOM   8428  C  CA  . SER H  1 107 ? 51.639  83.656  96.999  1.00 17.80 ? 107  SER H CA  1 
ATOM   8429  C  C   . SER H  1 107 ? 52.145  82.220  97.180  1.00 18.83 ? 107  SER H C   1 
ATOM   8430  O  O   . SER H  1 107 ? 51.777  81.527  98.130  1.00 19.19 ? 107  SER H O   1 
ATOM   8431  C  CB  . SER H  1 107 ? 52.784  84.654  97.215  1.00 18.67 ? 107  SER H CB  1 
ATOM   8432  O  OG  . SER H  1 107 ? 53.626  84.240  98.293  1.00 21.43 ? 107  SER H OG  1 
ATOM   8433  N  N   . GLY H  1 108 ? 52.979  81.741  96.266  1.00 19.57 ? 108  GLY H N   1 
ATOM   8434  C  CA  . GLY H  1 108 ? 53.536  80.411  96.468  1.00 19.49 ? 108  GLY H CA  1 
ATOM   8435  C  C   . GLY H  1 108 ? 52.630  79.228  96.155  1.00 19.75 ? 108  GLY H C   1 
ATOM   8436  O  O   . GLY H  1 108 ? 51.630  79.353  95.442  1.00 19.15 ? 108  GLY H O   1 
ATOM   8437  N  N   . ASP H  1 109 ? 53.001  78.071  96.699  1.00 20.45 ? 109  ASP H N   1 
ATOM   8438  C  CA  . ASP H  1 109 ? 52.315  76.800  96.439  1.00 21.25 ? 109  ASP H CA  1 
ATOM   8439  C  C   . ASP H  1 109 ? 50.870  76.793  96.855  1.00 20.19 ? 109  ASP H C   1 
ATOM   8440  O  O   . ASP H  1 109 ? 50.048  76.080  96.261  1.00 20.86 ? 109  ASP H O   1 
ATOM   8441  C  CB  . ASP H  1 109 ? 53.006  75.649  97.185  1.00 22.45 ? 109  ASP H CB  1 
ATOM   8442  C  CG  . ASP H  1 109 ? 54.026  74.932  96.331  1.00 26.53 ? 109  ASP H CG  1 
ATOM   8443  O  OD1 . ASP H  1 109 ? 54.496  73.840  96.756  1.00 30.12 ? 109  ASP H OD1 1 
ATOM   8444  O  OD2 . ASP H  1 109 ? 54.409  75.377  95.216  1.00 29.10 ? 109  ASP H OD2 1 
ATOM   8445  N  N   . HIS H  1 110 ? 50.571  77.526  97.917  1.00 17.40 ? 110  HIS H N   1 
ATOM   8446  C  CA  . HIS H  1 110 ? 49.205  77.562  98.423  1.00 15.74 ? 110  HIS H CA  1 
ATOM   8447  C  C   . HIS H  1 110 ? 48.448  78.809  98.024  1.00 13.41 ? 110  HIS H C   1 
ATOM   8448  O  O   . HIS H  1 110 ? 47.453  79.167  98.674  1.00 13.13 ? 110  HIS H O   1 
ATOM   8449  C  CB  . HIS H  1 110 ? 49.191  77.464  99.945  1.00 14.69 ? 110  HIS H CB  1 
ATOM   8450  C  CG  . HIS H  1 110 ? 49.623  76.129  100.454 1.00 17.81 ? 110  HIS H CG  1 
ATOM   8451  N  ND1 . HIS H  1 110 ? 49.523  75.775  101.780 1.00 16.93 ? 110  HIS H ND1 1 
ATOM   8452  C  CD2 . HIS H  1 110 ? 50.160  75.063  99.812  1.00 18.80 ? 110  HIS H CD2 1 
ATOM   8453  C  CE1 . HIS H  1 110 ? 49.990  74.547  101.940 1.00 19.87 ? 110  HIS H CE1 1 
ATOM   8454  N  NE2 . HIS H  1 110 ? 50.390  74.095  100.760 1.00 21.14 ? 110  HIS H NE2 1 
ATOM   8455  N  N   . CYS H  1 111 ? 48.893  79.453  96.950  1.00 12.40 ? 111  CYS H N   1 
ATOM   8456  C  CA  . CYS H  1 111 ? 48.260  80.684  96.500  1.00 12.04 ? 111  CYS H CA  1 
ATOM   8457  C  C   . CYS H  1 111 ? 46.822  80.465  96.091  1.00 11.71 ? 111  CYS H C   1 
ATOM   8458  O  O   . CYS H  1 111 ? 46.537  79.510  95.362  1.00 12.71 ? 111  CYS H O   1 
ATOM   8459  C  CB  . CYS H  1 111 ? 49.011  81.231  95.301  1.00 12.09 ? 111  CYS H CB  1 
ATOM   8460  S  SG  . CYS H  1 111 ? 48.564  82.936  95.072  1.00 17.03 ? 111  CYS H SG  1 
ATOM   8461  N  N   . ILE H  1 112 ? 45.919  81.334  96.549  1.00 10.49 ? 112  ILE H N   1 
ATOM   8462  C  CA  . ILE H  1 112 ? 44.506  81.220  96.191  1.00 9.55  ? 112  ILE H CA  1 
ATOM   8463  C  C   . ILE H  1 112 ? 43.997  82.298  95.201  1.00 9.49  ? 112  ILE H C   1 
ATOM   8464  O  O   . ILE H  1 112 ? 42.844  82.282  94.819  1.00 9.56  ? 112  ILE H O   1 
ATOM   8465  C  CB  . ILE H  1 112 ? 43.595  81.215  97.456  1.00 8.07  ? 112  ILE H CB  1 
ATOM   8466  C  CG1 . ILE H  1 112 ? 43.726  82.561  98.196  1.00 8.58  ? 112  ILE H CG1 1 
ATOM   8467  C  CG2 . ILE H  1 112 ? 43.914  80.014  98.352  1.00 9.13  ? 112  ILE H CG2 1 
ATOM   8468  C  CD1 . ILE H  1 112 ? 42.790  82.634  99.424  1.00 8.37  ? 112  ILE H CD1 1 
ATOM   8469  N  N   . ILE H  1 113 ? 44.854  83.211  94.774  1.00 8.77  ? 113  ILE H N   1 
ATOM   8470  C  CA  . ILE H  1 113 ? 44.415  84.238  93.819  1.00 9.30  ? 113  ILE H CA  1 
ATOM   8471  C  C   . ILE H  1 113 ? 44.077  83.506  92.513  1.00 8.87  ? 113  ILE H C   1 
ATOM   8472  O  O   . ILE H  1 113 ? 44.824  82.639  92.108  1.00 8.33  ? 113  ILE H O   1 
ATOM   8473  C  CB  . ILE H  1 113 ? 45.624  85.123  93.524  1.00 9.36  ? 113  ILE H CB  1 
ATOM   8474  C  CG1 . ILE H  1 113 ? 46.071  85.885  94.764  1.00 12.34 ? 113  ILE H CG1 1 
ATOM   8475  C  CG2 . ILE H  1 113 ? 45.361  86.073  92.277  1.00 9.50  ? 113  ILE H CG2 1 
ATOM   8476  C  CD1 . ILE H  1 113 ? 45.205  86.942  95.119  1.00 18.53 ? 113  ILE H CD1 1 
ATOM   8477  N  N   . GLY H  1 114 ? 42.972  83.845  91.857  1.00 9.09  ? 114  GLY H N   1 
ATOM   8478  C  CA  . GLY H  1 114 ? 42.588  83.154  90.638  1.00 8.68  ? 114  GLY H CA  1 
ATOM   8479  C  C   . GLY H  1 114 ? 41.791  81.873  90.898  1.00 9.31  ? 114  GLY H C   1 
ATOM   8480  O  O   . GLY H  1 114 ? 41.375  81.194  89.962  1.00 9.01  ? 114  GLY H O   1 
ATOM   8481  N  N   . ARG H  1 115 ? 41.563  81.547  92.164  1.00 8.80  ? 115  ARG H N   1 
ATOM   8482  C  CA  . ARG H  1 115 ? 40.694  80.408  92.504  1.00 9.26  ? 115  ARG H CA  1 
ATOM   8483  C  C   . ARG H  1 115 ? 39.332  80.948  92.942  1.00 9.48  ? 115  ARG H C   1 
ATOM   8484  O  O   . ARG H  1 115 ? 39.082  82.122  92.814  1.00 9.56  ? 115  ARG H O   1 
ATOM   8485  C  CB  . ARG H  1 115 ? 41.361  79.489  93.535  1.00 8.58  ? 115  ARG H CB  1 
ATOM   8486  C  CG  . ARG H  1 115 ? 42.836  79.191  93.138  1.00 9.29  ? 115  ARG H CG  1 
ATOM   8487  C  CD  . ARG H  1 115 ? 43.543  78.010  93.892  1.00 9.78  ? 115  ARG H CD  1 
ATOM   8488  N  NE  . ARG H  1 115 ? 44.907  77.759  93.405  1.00 11.11 ? 115  ARG H NE  1 
ATOM   8489  C  CZ  . ARG H  1 115 ? 45.194  76.866  92.465  1.00 11.61 ? 115  ARG H CZ  1 
ATOM   8490  N  NH1 . ARG H  1 115 ? 44.214  76.153  91.908  1.00 11.94 ? 115  ARG H NH1 1 
ATOM   8491  N  NH2 . ARG H  1 115 ? 46.455  76.681  92.069  1.00 9.99  ? 115  ARG H NH2 1 
ATOM   8492  N  N   . THR H  1 116 ? 38.433  80.097  93.424  1.00 9.10  ? 116  THR H N   1 
ATOM   8493  C  CA  . THR H  1 116 ? 37.074  80.539  93.699  1.00 9.31  ? 116  THR H CA  1 
ATOM   8494  C  C   . THR H  1 116 ? 36.725  80.439  95.166  1.00 8.54  ? 116  THR H C   1 
ATOM   8495  O  O   . THR H  1 116 ? 36.908  79.391  95.785  1.00 11.20 ? 116  THR H O   1 
ATOM   8496  C  CB  . THR H  1 116 ? 36.070  79.683  92.877  1.00 9.23  ? 116  THR H CB  1 
ATOM   8497  O  OG1 . THR H  1 116 ? 36.156  80.057  91.490  1.00 10.24 ? 116  THR H OG1 1 
ATOM   8498  C  CG2 . THR H  1 116 ? 34.602  79.992  93.269  1.00 8.87  ? 116  THR H CG2 1 
ATOM   8499  N  N   . LEU H  1 117 ? 36.151  81.485  95.720  1.00 6.93  ? 117  LEU H N   1 
ATOM   8500  C  CA  . LEU H  1 117 ? 35.649  81.380  97.086  1.00 7.25  ? 117  LEU H CA  1 
ATOM   8501  C  C   . LEU H  1 117 ? 34.170  81.044  97.001  1.00 7.72  ? 117  LEU H C   1 
ATOM   8502  O  O   . LEU H  1 117 ? 33.440  81.656  96.196  1.00 6.27  ? 117  LEU H O   1 
ATOM   8503  C  CB  . LEU H  1 117 ? 35.862  82.694  97.824  1.00 6.49  ? 117  LEU H CB  1 
ATOM   8504  C  CG  . LEU H  1 117 ? 35.358  82.777  99.261  1.00 6.20  ? 117  LEU H CG  1 
ATOM   8505  C  CD1 . LEU H  1 117 ? 36.269  81.946  100.167 1.00 8.41  ? 117  LEU H CD1 1 
ATOM   8506  C  CD2 . LEU H  1 117 ? 35.417  84.284  99.688  1.00 7.12  ? 117  LEU H CD2 1 
ATOM   8507  N  N   . VAL H  1 118 ? 33.730  80.088  97.836  1.00 7.29  ? 118  VAL H N   1 
ATOM   8508  C  CA  . VAL H  1 118 ? 32.339  79.629  97.830  1.00 8.17  ? 118  VAL H CA  1 
ATOM   8509  C  C   . VAL H  1 118 ? 31.710  79.674  99.191  1.00 7.54  ? 118  VAL H C   1 
ATOM   8510  O  O   . VAL H  1 118 ? 32.338  79.277  100.175 1.00 8.18  ? 118  VAL H O   1 
ATOM   8511  C  CB  . VAL H  1 118 ? 32.239  78.168  97.349  1.00 7.84  ? 118  VAL H CB  1 
ATOM   8512  C  CG1 . VAL H  1 118 ? 30.784  77.647  97.459  1.00 10.13 ? 118  VAL H CG1 1 
ATOM   8513  C  CG2 . VAL H  1 118 ? 32.761  78.075  95.925  1.00 5.44  ? 118  VAL H CG2 1 
ATOM   8514  N  N   . VAL H  1 119 ? 30.466  80.133  99.265  1.00 7.38  ? 119  VAL H N   1 
ATOM   8515  C  CA  . VAL H  1 119 ? 29.713  80.017  100.529 1.00 7.49  ? 119  VAL H CA  1 
ATOM   8516  C  C   . VAL H  1 119 ? 28.569  79.055  100.272 1.00 8.87  ? 119  VAL H C   1 
ATOM   8517  O  O   . VAL H  1 119 ? 27.938  79.094  99.221  1.00 8.75  ? 119  VAL H O   1 
ATOM   8518  C  CB  . VAL H  1 119 ? 29.249  81.353  101.077 1.00 8.30  ? 119  VAL H CB  1 
ATOM   8519  C  CG1 . VAL H  1 119 ? 28.394  82.126  100.038 1.00 8.59  ? 119  VAL H CG1 1 
ATOM   8520  C  CG2 . VAL H  1 119 ? 28.513  81.186  102.401 1.00 6.03  ? 119  VAL H CG2 1 
ATOM   8521  N  N   . HIS H  1 120 ? 28.344  78.167  101.240 1.00 9.32  ? 120  HIS H N   1 
ATOM   8522  C  CA  . HIS H  1 120 ? 27.440  77.021  101.064 1.00 9.82  ? 120  HIS H CA  1 
ATOM   8523  C  C   . HIS H  1 120 ? 26.082  77.107  101.768 1.00 10.93 ? 120  HIS H C   1 
ATOM   8524  O  O   . HIS H  1 120 ? 25.844  77.938  102.653 1.00 10.63 ? 120  HIS H O   1 
ATOM   8525  C  CB  . HIS H  1 120 ? 28.127  75.753  101.562 1.00 9.36  ? 120  HIS H CB  1 
ATOM   8526  C  CG  . HIS H  1 120 ? 29.158  75.211  100.632 1.00 11.26 ? 120  HIS H CG  1 
ATOM   8527  N  ND1 . HIS H  1 120 ? 28.856  74.305  99.638  1.00 10.63 ? 120  HIS H ND1 1 
ATOM   8528  C  CD2 . HIS H  1 120 ? 30.494  75.420  100.555 1.00 10.02 ? 120  HIS H CD2 1 
ATOM   8529  C  CE1 . HIS H  1 120 ? 29.950  74.016  98.958  1.00 13.59 ? 120  HIS H CE1 1 
ATOM   8530  N  NE2 . HIS H  1 120 ? 30.957  74.677  99.492  1.00 12.54 ? 120  HIS H NE2 1 
ATOM   8531  N  N   . GLU H  1 121 ? 25.209  76.202  101.345 1.00 11.47 ? 121  GLU H N   1 
ATOM   8532  C  CA  . GLU H  1 121 ? 23.850  76.079  101.852 1.00 12.86 ? 121  GLU H CA  1 
ATOM   8533  C  C   . GLU H  1 121 ? 23.786  75.722  103.325 1.00 13.36 ? 121  GLU H C   1 
ATOM   8534  O  O   . GLU H  1 121 ? 22.966  76.283  104.058 1.00 14.31 ? 121  GLU H O   1 
ATOM   8535  C  CB  . GLU H  1 121 ? 23.136  74.982  101.057 1.00 12.41 ? 121  GLU H CB  1 
ATOM   8536  C  CG  . GLU H  1 121 ? 21.790  74.557  101.644 1.00 15.23 ? 121  GLU H CG  1 
ATOM   8537  C  CD  . GLU H  1 121 ? 21.360  73.170  101.178 1.00 19.66 ? 121  GLU H CD  1 
ATOM   8538  O  OE1 . GLU H  1 121 ? 22.059  72.585  100.308 1.00 14.66 ? 121  GLU H OE1 1 
ATOM   8539  O  OE2 . GLU H  1 121 ? 20.338  72.649  101.725 1.00 21.96 ? 121  GLU H OE2 1 
ATOM   8540  N  N   . LYS H  1 122 ? 24.646  74.797  103.748 1.00 13.22 ? 122  LYS H N   1 
ATOM   8541  C  CA  . LYS H  1 122 ? 24.587  74.240  105.105 1.00 14.73 ? 122  LYS H CA  1 
ATOM   8542  C  C   . LYS H  1 122 ? 25.895  74.393  105.839 1.00 13.48 ? 122  LYS H C   1 
ATOM   8543  O  O   . LYS H  1 122 ? 26.886  74.811  105.268 1.00 13.62 ? 122  LYS H O   1 
ATOM   8544  C  CB  . LYS H  1 122 ? 24.316  72.719  105.046 1.00 15.05 ? 122  LYS H CB  1 
ATOM   8545  C  CG  . LYS H  1 122 ? 22.944  72.304  104.590 1.00 19.59 ? 122  LYS H CG  1 
ATOM   8546  C  CD  . LYS H  1 122 ? 22.927  70.856  104.022 1.00 22.51 ? 122  LYS H CD  1 
ATOM   8547  C  CE  . LYS H  1 122 ? 23.285  69.830  105.065 1.00 26.98 ? 122  LYS H CE  1 
ATOM   8548  N  NZ  . LYS H  1 122 ? 22.641  68.519  104.761 1.00 30.62 ? 122  LYS H NZ  1 
ATOM   8549  N  N   . ALA H  1 123 ? 25.876  73.999  107.113 1.00 12.10 ? 123  ALA H N   1 
ATOM   8550  C  CA  . ALA H  1 123 ? 27.092  73.965  107.916 1.00 11.29 ? 123  ALA H CA  1 
ATOM   8551  C  C   . ALA H  1 123 ? 28.053  72.928  107.364 1.00 10.79 ? 123  ALA H C   1 
ATOM   8552  O  O   . ALA H  1 123 ? 27.642  71.851  106.915 1.00 11.30 ? 123  ALA H O   1 
ATOM   8553  C  CB  . ALA H  1 123 ? 26.762  73.588  109.372 1.00 11.06 ? 123  ALA H CB  1 
ATOM   8554  N  N   . ASP H  1 124 ? 29.328  73.282  107.415 1.00 9.79  ? 124  ASP H N   1 
ATOM   8555  C  CA  . ASP H  1 124 ? 30.444  72.400  107.176 1.00 9.48  ? 124  ASP H CA  1 
ATOM   8556  C  C   . ASP H  1 124 ? 30.688  71.595  108.475 1.00 8.94  ? 124  ASP H C   1 
ATOM   8557  O  O   . ASP H  1 124 ? 30.888  72.179  109.551 1.00 9.06  ? 124  ASP H O   1 
ATOM   8558  C  CB  . ASP H  1 124 ? 31.654  73.262  106.807 1.00 9.59  ? 124  ASP H CB  1 
ATOM   8559  C  CG  . ASP H  1 124 ? 32.887  72.455  106.498 1.00 10.00 ? 124  ASP H CG  1 
ATOM   8560  O  OD1 . ASP H  1 124 ? 33.005  71.265  106.907 1.00 9.25  ? 124  ASP H OD1 1 
ATOM   8561  O  OD2 . ASP H  1 124 ? 33.836  72.951  105.861 1.00 12.50 ? 124  ASP H OD2 1 
ATOM   8562  N  N   . ASP H  1 125 ? 30.639  70.256  108.402 1.00 9.37  ? 125  ASP H N   1 
ATOM   8563  C  CA  . ASP H  1 125 ? 30.731  69.465  109.647 1.00 9.92  ? 125  ASP H CA  1 
ATOM   8564  C  C   . ASP H  1 125 ? 32.166  69.203  110.038 1.00 9.68  ? 125  ASP H C   1 
ATOM   8565  O  O   . ASP H  1 125 ? 32.457  68.429  110.960 1.00 8.14  ? 125  ASP H O   1 
ATOM   8566  C  CB  . ASP H  1 125 ? 29.897  68.159  109.575 1.00 10.08 ? 125  ASP H CB  1 
ATOM   8567  C  CG  . ASP H  1 125 ? 30.421  67.182  108.544 1.00 10.85 ? 125  ASP H CG  1 
ATOM   8568  O  OD1 . ASP H  1 125 ? 31.594  67.313  108.100 1.00 9.67  ? 125  ASP H OD1 1 
ATOM   8569  O  OD2 . ASP H  1 125 ? 29.697  66.261  108.107 1.00 11.01 ? 125  ASP H OD2 1 
ATOM   8570  N  N   . LEU H  1 126 ? 33.056  69.848  109.289 1.00 8.96  ? 126  LEU H N   1 
ATOM   8571  C  CA  . LEU H  1 126 ? 34.488  69.834  109.545 1.00 9.69  ? 126  LEU H CA  1 
ATOM   8572  C  C   . LEU H  1 126 ? 35.092  68.431  109.533 1.00 8.96  ? 126  LEU H C   1 
ATOM   8573  O  O   . LEU H  1 126 ? 36.077  68.189  110.221 1.00 9.32  ? 126  LEU H O   1 
ATOM   8574  C  CB  . LEU H  1 126 ? 34.800  70.526  110.888 1.00 9.70  ? 126  LEU H CB  1 
ATOM   8575  C  CG  . LEU H  1 126 ? 34.136  71.892  111.096 1.00 11.29 ? 126  LEU H CG  1 
ATOM   8576  C  CD1 . LEU H  1 126 ? 34.573  72.499  112.433 1.00 10.70 ? 126  LEU H CD1 1 
ATOM   8577  C  CD2 . LEU H  1 126 ? 34.428  72.851  109.900 1.00 8.93  ? 126  LEU H CD2 1 
ATOM   8578  N  N   . GLY H  1 127 ? 34.509  67.512  108.777 1.00 8.62  ? 127  GLY H N   1 
ATOM   8579  C  CA  . GLY H  1 127 ? 35.077  66.172  108.674 1.00 8.92  ? 127  GLY H CA  1 
ATOM   8580  C  C   . GLY H  1 127 ? 34.635  65.223  109.768 1.00 8.98  ? 127  GLY H C   1 
ATOM   8581  O  O   . GLY H  1 127 ? 35.117  64.094  109.873 1.00 10.49 ? 127  GLY H O   1 
ATOM   8582  N  N   . LYS H  1 128 ? 33.688  65.655  110.594 1.00 7.70  ? 128  LYS H N   1 
ATOM   8583  C  CA  . LYS H  1 128 ? 33.278  64.827  111.722 1.00 8.38  ? 128  LYS H CA  1 
ATOM   8584  C  C   . LYS H  1 128 ? 31.911  64.176  111.561 1.00 8.24  ? 128  LYS H C   1 
ATOM   8585  O  O   . LYS H  1 128 ? 31.325  63.749  112.573 1.00 8.87  ? 128  LYS H O   1 
ATOM   8586  C  CB  . LYS H  1 128 ? 33.282  65.654  113.026 1.00 8.11  ? 128  LYS H CB  1 
ATOM   8587  C  CG  . LYS H  1 128 ? 34.627  66.293  113.381 1.00 14.26 ? 128  LYS H CG  1 
ATOM   8588  C  CD  . LYS H  1 128 ? 34.439  67.261  114.578 1.00 19.27 ? 128  LYS H CD  1 
ATOM   8589  C  CE  . LYS H  1 128 ? 35.112  68.657  114.332 1.00 24.14 ? 128  LYS H CE  1 
ATOM   8590  N  NZ  . LYS H  1 128 ? 34.558  69.812  115.184 1.00 26.02 ? 128  LYS H NZ  1 
ATOM   8591  N  N   . GLY H  1 129 ? 31.429  64.072  110.322 1.00 7.07  ? 129  GLY H N   1 
ATOM   8592  C  CA  . GLY H  1 129 ? 30.078  63.596  110.034 1.00 8.86  ? 129  GLY H CA  1 
ATOM   8593  C  C   . GLY H  1 129 ? 29.880  62.085  109.896 1.00 9.23  ? 129  GLY H C   1 
ATOM   8594  O  O   . GLY H  1 129 ? 28.734  61.585  109.827 1.00 8.65  ? 129  GLY H O   1 
ATOM   8595  N  N   . GLY H  1 130 ? 30.982  61.351  109.862 1.00 8.70  ? 130  GLY H N   1 
ATOM   8596  C  CA  . GLY H  1 130 ? 30.905  59.891  109.931 1.00 7.95  ? 130  GLY H CA  1 
ATOM   8597  C  C   . GLY H  1 130 ? 30.617  59.205  108.615 1.00 9.08  ? 130  GLY H C   1 
ATOM   8598  O  O   . GLY H  1 130 ? 30.239  58.023  108.596 1.00 8.73  ? 130  GLY H O   1 
ATOM   8599  N  N   . ASN H  1 131 ? 30.772  59.937  107.523 1.00 8.62  ? 131  ASN H N   1 
ATOM   8600  C  CA  . ASN H  1 131 ? 30.604  59.355  106.192 1.00 9.16  ? 131  ASN H CA  1 
ATOM   8601  C  C   . ASN H  1 131 ? 31.654  59.839  105.215 1.00 9.78  ? 131  ASN H C   1 
ATOM   8602  O  O   . ASN H  1 131 ? 32.439  60.757  105.523 1.00 9.27  ? 131  ASN H O   1 
ATOM   8603  C  CB  . ASN H  1 131 ? 29.184  59.536  105.630 1.00 8.52  ? 131  ASN H CB  1 
ATOM   8604  C  CG  . ASN H  1 131 ? 28.766  61.001  105.466 1.00 11.62 ? 131  ASN H CG  1 
ATOM   8605  O  OD1 . ASN H  1 131 ? 29.582  61.906  105.448 1.00 12.46 ? 131  ASN H OD1 1 
ATOM   8606  N  ND2 . ASN H  1 131 ? 27.467  61.222  105.358 1.00 13.94 ? 131  ASN H ND2 1 
ATOM   8607  N  N   . GLU H  1 132 ? 31.675  59.244  104.023 1.00 9.98  ? 132  GLU H N   1 
ATOM   8608  C  CA  . GLU H  1 132 ? 32.626  59.695  103.019 1.00 12.35 ? 132  GLU H CA  1 
ATOM   8609  C  C   . GLU H  1 132 ? 32.439  61.158  102.638 1.00 11.85 ? 132  GLU H C   1 
ATOM   8610  O  O   . GLU H  1 132 ? 33.408  61.915  102.480 1.00 12.89 ? 132  GLU H O   1 
ATOM   8611  C  CB  . GLU H  1 132 ? 32.548  58.807  101.767 1.00 12.42 ? 132  GLU H CB  1 
ATOM   8612  C  CG  . GLU H  1 132 ? 33.122  57.437  102.040 1.00 17.92 ? 132  GLU H CG  1 
ATOM   8613  C  CD  . GLU H  1 132 ? 34.586  57.510  102.439 1.00 23.71 ? 132  GLU H CD  1 
ATOM   8614  O  OE1 . GLU H  1 132 ? 35.407  57.908  101.563 1.00 24.85 ? 132  GLU H OE1 1 
ATOM   8615  O  OE2 . GLU H  1 132 ? 34.900  57.196  103.621 1.00 24.90 ? 132  GLU H OE2 1 
ATOM   8616  N  N   . GLU H  1 133 ? 31.193  61.568  102.459 1.00 12.07 ? 133  GLU H N   1 
ATOM   8617  C  CA  . GLU H  1 133 ? 30.915  62.938  102.064 1.00 12.70 ? 133  GLU H CA  1 
ATOM   8618  C  C   . GLU H  1 133 ? 31.547  63.963  103.050 1.00 11.86 ? 133  GLU H C   1 
ATOM   8619  O  O   . GLU H  1 133 ? 32.040  65.038  102.643 1.00 11.24 ? 133  GLU H O   1 
ATOM   8620  C  CB  . GLU H  1 133 ? 29.406  63.161  101.922 1.00 13.11 ? 133  GLU H CB  1 
ATOM   8621  C  CG  . GLU H  1 133 ? 29.067  64.505  101.260 1.00 15.48 ? 133  GLU H CG  1 
ATOM   8622  C  CD  . GLU H  1 133 ? 29.529  64.619  99.819  1.00 20.39 ? 133  GLU H CD  1 
ATOM   8623  O  OE1 . GLU H  1 133 ? 29.353  63.661  99.050  1.00 21.83 ? 133  GLU H OE1 1 
ATOM   8624  O  OE2 . GLU H  1 133 ? 30.061  65.687  99.442  1.00 20.02 ? 133  GLU H OE2 1 
ATOM   8625  N  N   . SER H  1 134 ? 31.557  63.621  104.328 1.00 11.63 ? 134  SER H N   1 
ATOM   8626  C  CA  . SER H  1 134 ? 32.134  64.509  105.336 1.00 11.84 ? 134  SER H CA  1 
ATOM   8627  C  C   . SER H  1 134 ? 33.623  64.712  105.076 1.00 12.45 ? 134  SER H C   1 
ATOM   8628  O  O   . SER H  1 134 ? 34.154  65.812  105.276 1.00 13.07 ? 134  SER H O   1 
ATOM   8629  C  CB  . SER H  1 134 ? 31.898  63.942  106.757 1.00 11.30 ? 134  SER H CB  1 
ATOM   8630  O  OG  . SER H  1 134 ? 32.457  64.787  107.732 1.00 9.56  ? 134  SER H OG  1 
ATOM   8631  N  N   . THR H  1 135 ? 34.296  63.660  104.629 1.00 13.20 ? 135  THR H N   1 
ATOM   8632  C  CA  . THR H  1 135 ? 35.726  63.748  104.341 1.00 14.31 ? 135  THR H CA  1 
ATOM   8633  C  C   . THR H  1 135 ? 36.040  64.415  103.000 1.00 13.92 ? 135  THR H C   1 
ATOM   8634  O  O   . THR H  1 135 ? 37.216  64.512  102.643 1.00 13.74 ? 135  THR H O   1 
ATOM   8635  C  CB  . THR H  1 135 ? 36.404  62.363  104.354 1.00 15.87 ? 135  THR H CB  1 
ATOM   8636  O  OG1 . THR H  1 135 ? 36.155  61.668  103.114 1.00 18.02 ? 135  THR H OG1 1 
ATOM   8637  C  CG2 . THR H  1 135 ? 35.803  61.514  105.384 1.00 17.03 ? 135  THR H CG2 1 
ATOM   8638  N  N   . LYS H  1 136 ? 35.016  64.840  102.261 1.00 13.64 ? 136  LYS H N   1 
ATOM   8639  C  CA  . LYS H  1 136 ? 35.243  65.502  100.969 1.00 14.54 ? 136  LYS H CA  1 
ATOM   8640  C  C   . LYS H  1 136 ? 34.848  66.956  101.015 1.00 13.80 ? 136  LYS H C   1 
ATOM   8641  O  O   . LYS H  1 136 ? 35.625  67.849  100.616 1.00 13.49 ? 136  LYS H O   1 
ATOM   8642  C  CB  . LYS H  1 136 ? 34.445  64.836  99.830  1.00 15.48 ? 136  LYS H CB  1 
ATOM   8643  C  CG  . LYS H  1 136 ? 34.666  63.356  99.693  1.00 19.83 ? 136  LYS H CG  1 
ATOM   8644  C  CD  . LYS H  1 136 ? 34.480  62.841  98.248  1.00 25.54 ? 136  LYS H CD  1 
ATOM   8645  C  CE  . LYS H  1 136 ? 33.218  63.398  97.553  1.00 29.47 ? 136  LYS H CE  1 
ATOM   8646  N  NZ  . LYS H  1 136 ? 32.657  62.426  96.537  1.00 31.31 ? 136  LYS H NZ  1 
ATOM   8647  N  N   . THR H  1 137 ? 33.628  67.196  101.497 1.00 13.39 ? 137  THR H N   1 
ATOM   8648  C  CA  . THR H  1 137 ? 33.044  68.531  101.506 1.00 12.28 ? 137  THR H CA  1 
ATOM   8649  C  C   . THR H  1 137 ? 32.530  68.977  102.852 1.00 11.60 ? 137  THR H C   1 
ATOM   8650  O  O   . THR H  1 137 ? 32.026  70.073  102.938 1.00 11.08 ? 137  THR H O   1 
ATOM   8651  C  CB  . THR H  1 137 ? 31.814  68.610  100.548 1.00 12.41 ? 137  THR H CB  1 
ATOM   8652  O  OG1 . THR H  1 137 ? 30.751  67.773  101.035 1.00 11.46 ? 137  THR H OG1 1 
ATOM   8653  C  CG2 . THR H  1 137 ? 32.121  68.020  99.186  1.00 14.95 ? 137  THR H CG2 1 
ATOM   8654  N  N   . GLY H  1 138 ? 32.594  68.131  103.880 1.00 10.58 ? 138  GLY H N   1 
ATOM   8655  C  CA  . GLY H  1 138 ? 31.975  68.492  105.155 1.00 8.49  ? 138  GLY H CA  1 
ATOM   8656  C  C   . GLY H  1 138 ? 30.443  68.524  105.098 1.00 9.12  ? 138  GLY H C   1 
ATOM   8657  O  O   . GLY H  1 138 ? 29.808  69.079  105.991 1.00 8.25  ? 138  GLY H O   1 
ATOM   8658  N  N   . ASN H  1 139 ? 29.827  67.908  104.076 1.00 9.97  ? 139  ASN H N   1 
ATOM   8659  C  CA  . ASN H  1 139 ? 28.361  67.934  103.971 1.00 11.01 ? 139  ASN H CA  1 
ATOM   8660  C  C   . ASN H  1 139 ? 27.760  69.361  103.967 1.00 11.62 ? 139  ASN H C   1 
ATOM   8661  O  O   . ASN H  1 139 ? 26.655  69.591  104.471 1.00 10.84 ? 139  ASN H O   1 
ATOM   8662  C  CB  . ASN H  1 139 ? 27.762  67.135  105.139 1.00 11.48 ? 139  ASN H CB  1 
ATOM   8663  C  CG  . ASN H  1 139 ? 27.954  65.641  104.980 1.00 13.29 ? 139  ASN H CG  1 
ATOM   8664  O  OD1 . ASN H  1 139 ? 27.427  65.034  104.040 1.00 14.96 ? 139  ASN H OD1 1 
ATOM   8665  N  ND2 . ASN H  1 139 ? 28.727  65.043  105.879 1.00 12.06 ? 139  ASN H ND2 1 
ATOM   8666  N  N   . ALA H  1 140 ? 28.466  70.329  103.384 1.00 11.77 ? 140  ALA H N   1 
ATOM   8667  C  CA  . ALA H  1 140 ? 27.959  71.695  103.462 1.00 12.65 ? 140  ALA H CA  1 
ATOM   8668  C  C   . ALA H  1 140 ? 26.919  71.991  102.406 1.00 12.14 ? 140  ALA H C   1 
ATOM   8669  O  O   . ALA H  1 140 ? 26.338  73.066  102.383 1.00 12.01 ? 140  ALA H O   1 
ATOM   8670  C  CB  . ALA H  1 140 ? 29.097  72.726  103.422 1.00 13.03 ? 140  ALA H CB  1 
ATOM   8671  N  N   . GLY H  1 141 ? 26.653  71.005  101.560 1.00 12.43 ? 141  GLY H N   1 
ATOM   8672  C  CA  . GLY H  1 141 ? 25.603  71.133  100.566 1.00 13.11 ? 141  GLY H CA  1 
ATOM   8673  C  C   . GLY H  1 141 ? 25.871  72.051  99.376  1.00 12.59 ? 141  GLY H C   1 
ATOM   8674  O  O   . GLY H  1 141 ? 27.018  72.191  98.920  1.00 12.25 ? 141  GLY H O   1 
ATOM   8675  N  N   . SER H  1 142 ? 24.790  72.670  98.894  1.00 12.36 ? 142  SER H N   1 
ATOM   8676  C  CA  . SER H  1 142 ? 24.766  73.484  97.678  1.00 13.49 ? 142  SER H CA  1 
ATOM   8677  C  C   . SER H  1 142 ? 25.659  74.717  97.735  1.00 12.53 ? 142  SER H C   1 
ATOM   8678  O  O   . SER H  1 142 ? 25.950  75.239  98.807  1.00 13.73 ? 142  SER H O   1 
ATOM   8679  C  CB  . SER H  1 142 ? 23.348  73.939  97.381  1.00 11.90 ? 142  SER H CB  1 
ATOM   8680  O  OG  . SER H  1 142 ? 22.544  72.830  96.995  1.00 19.61 ? 142  SER H OG  1 
ATOM   8681  N  N   . ARG H  1 143 ? 26.082  75.185  96.565  1.00 12.40 ? 143  ARG H N   1 
ATOM   8682  C  CA  . ARG H  1 143 ? 26.907  76.393  96.497  1.00 11.80 ? 143  ARG H CA  1 
ATOM   8683  C  C   . ARG H  1 143 ? 25.964  77.558  96.285  1.00 11.38 ? 143  ARG H C   1 
ATOM   8684  O  O   . ARG H  1 143 ? 25.301  77.647  95.236  1.00 12.63 ? 143  ARG H O   1 
ATOM   8685  C  CB  . ARG H  1 143 ? 27.873  76.264  95.336  1.00 11.22 ? 143  ARG H CB  1 
ATOM   8686  C  CG  . ARG H  1 143 ? 28.766  75.065  95.509  1.00 12.07 ? 143  ARG H CG  1 
ATOM   8687  C  CD  . ARG H  1 143 ? 29.651  74.718  94.299  1.00 13.50 ? 143  ARG H CD  1 
ATOM   8688  N  NE  . ARG H  1 143 ? 30.314  73.437  94.549  1.00 14.49 ? 143  ARG H NE  1 
ATOM   8689  C  CZ  . ARG H  1 143 ? 31.404  73.005  93.938  1.00 11.20 ? 143  ARG H CZ  1 
ATOM   8690  N  NH1 . ARG H  1 143 ? 31.994  73.758  93.018  1.00 11.00 ? 143  ARG H NH1 1 
ATOM   8691  N  NH2 . ARG H  1 143 ? 31.907  71.811  94.267  1.00 10.42 ? 143  ARG H NH2 1 
ATOM   8692  N  N   . LEU H  1 144 ? 25.839  78.417  97.287  1.00 10.31 ? 144  LEU H N   1 
ATOM   8693  C  CA  . LEU H  1 144 ? 24.895  79.513  97.187  1.00 9.55  ? 144  LEU H CA  1 
ATOM   8694  C  C   . LEU H  1 144 ? 25.444  80.675  96.398  1.00 9.71  ? 144  LEU H C   1 
ATOM   8695  O  O   . LEU H  1 144 ? 24.717  81.298  95.610  1.00 9.20  ? 144  LEU H O   1 
ATOM   8696  C  CB  . LEU H  1 144 ? 24.452  79.985  98.563  1.00 10.32 ? 144  LEU H CB  1 
ATOM   8697  C  CG  . LEU H  1 144 ? 23.794  78.886  99.406  1.00 11.10 ? 144  LEU H CG  1 
ATOM   8698  C  CD1 . LEU H  1 144 ? 23.376  79.511  100.728 1.00 14.76 ? 144  LEU H CD1 1 
ATOM   8699  C  CD2 . LEU H  1 144 ? 22.604  78.305  98.654  1.00 13.45 ? 144  LEU H CD2 1 
ATOM   8700  N  N   . ALA H  1 145 ? 26.723  80.976  96.598  1.00 8.68  ? 145  ALA H N   1 
ATOM   8701  C  CA  . ALA H  1 145 ? 27.323  82.082  95.870  1.00 9.25  ? 145  ALA H CA  1 
ATOM   8702  C  C   . ALA H  1 145 ? 28.829  81.872  95.797  1.00 9.09  ? 145  ALA H C   1 
ATOM   8703  O  O   . ALA H  1 145 ? 29.417  81.189  96.644  1.00 7.75  ? 145  ALA H O   1 
ATOM   8704  C  CB  . ALA H  1 145 ? 27.016  83.401  96.556  1.00 9.84  ? 145  ALA H CB  1 
ATOM   8705  N  N   . CYS H  1 146 ? 29.456  82.479  94.798  1.00 8.46  ? 146  CYS H N   1 
ATOM   8706  C  CA  . CYS H  1 146 ? 30.880  82.317  94.653  1.00 9.14  ? 146  CYS H CA  1 
ATOM   8707  C  C   . CYS H  1 146 ? 31.453  83.458  93.837  1.00 7.88  ? 146  CYS H C   1 
ATOM   8708  O  O   . CYS H  1 146 ? 30.718  84.226  93.196  1.00 8.38  ? 146  CYS H O   1 
ATOM   8709  C  CB  . CYS H  1 146 ? 31.206  81.005  93.943  1.00 9.23  ? 146  CYS H CB  1 
ATOM   8710  S  SG  . CYS H  1 146 ? 30.476  80.922  92.251  1.00 14.50 ? 146  CYS H SG  1 
ATOM   8711  N  N   . GLY H  1 147 ? 32.777  83.553  93.846  1.00 7.58  ? 147  GLY H N   1 
ATOM   8712  C  CA  . GLY H  1 147 ? 33.436  84.527  92.981  1.00 7.96  ? 147  GLY H CA  1 
ATOM   8713  C  C   . GLY H  1 147 ? 34.905  84.174  92.831  1.00 8.11  ? 147  GLY H C   1 
ATOM   8714  O  O   . GLY H  1 147 ? 35.467  83.426  93.629  1.00 7.81  ? 147  GLY H O   1 
ATOM   8715  N  N   . VAL H  1 148 ? 35.554  84.707  91.799  1.00 7.29  ? 148  VAL H N   1 
ATOM   8716  C  CA  . VAL H  1 148 ? 36.949  84.406  91.615  1.00 7.71  ? 148  VAL H CA  1 
ATOM   8717  C  C   . VAL H  1 148 ? 37.730  85.393  92.469  1.00 8.33  ? 148  VAL H C   1 
ATOM   8718  O  O   . VAL H  1 148 ? 37.343  86.575  92.548  1.00 8.83  ? 148  VAL H O   1 
ATOM   8719  C  CB  . VAL H  1 148 ? 37.350  84.602  90.136  1.00 8.49  ? 148  VAL H CB  1 
ATOM   8720  C  CG1 . VAL H  1 148 ? 38.824  84.287  89.943  1.00 8.58  ? 148  VAL H CG1 1 
ATOM   8721  C  CG2 . VAL H  1 148 ? 36.489  83.650  89.260  1.00 9.97  ? 148  VAL H CG2 1 
ATOM   8722  N  N   . ILE H  1 149 ? 38.811  84.918  93.104  1.00 7.77  ? 149  ILE H N   1 
ATOM   8723  C  CA  . ILE H  1 149 ? 39.628  85.761  93.977  1.00 7.08  ? 149  ILE H CA  1 
ATOM   8724  C  C   . ILE H  1 149 ? 40.622  86.536  93.129  1.00 7.16  ? 149  ILE H C   1 
ATOM   8725  O  O   . ILE H  1 149 ? 41.426  85.941  92.398  1.00 8.26  ? 149  ILE H O   1 
ATOM   8726  C  CB  . ILE H  1 149 ? 40.357  84.897  95.008  1.00 7.50  ? 149  ILE H CB  1 
ATOM   8727  C  CG1 . ILE H  1 149 ? 39.297  84.149  95.816  1.00 5.85  ? 149  ILE H CG1 1 
ATOM   8728  C  CG2 . ILE H  1 149 ? 41.230  85.751  95.869  1.00 7.86  ? 149  ILE H CG2 1 
ATOM   8729  C  CD1 . ILE H  1 149 ? 39.800  82.941  96.604  1.00 8.70  ? 149  ILE H CD1 1 
ATOM   8730  N  N   . GLY H  1 150 ? 40.568  87.848  93.244  1.00 6.17  ? 150  GLY H N   1 
ATOM   8731  C  CA  . GLY H  1 150 ? 41.390  88.697  92.370  1.00 7.21  ? 150  GLY H CA  1 
ATOM   8732  C  C   . GLY H  1 150 ? 42.294  89.648  93.115  1.00 8.47  ? 150  GLY H C   1 
ATOM   8733  O  O   . GLY H  1 150 ? 42.080  89.935  94.309  1.00 9.48  ? 150  GLY H O   1 
ATOM   8734  N  N   . ILE H  1 151 ? 43.305  90.158  92.412  1.00 9.10  ? 151  ILE H N   1 
ATOM   8735  C  CA  . ILE H  1 151 ? 44.276  91.058  93.016  1.00 9.18  ? 151  ILE H CA  1 
ATOM   8736  C  C   . ILE H  1 151 ? 43.614  92.395  93.306  1.00 9.64  ? 151  ILE H C   1 
ATOM   8737  O  O   . ILE H  1 151 ? 42.907  92.949  92.466  1.00 9.50  ? 151  ILE H O   1 
ATOM   8738  C  CB  . ILE H  1 151 ? 45.477  91.236  92.097  1.00 10.18 ? 151  ILE H CB  1 
ATOM   8739  C  CG1 . ILE H  1 151 ? 46.238  89.901  92.050  1.00 11.75 ? 151  ILE H CG1 1 
ATOM   8740  C  CG2 . ILE H  1 151 ? 46.405  92.368  92.664  1.00 8.13  ? 151  ILE H CG2 1 
ATOM   8741  C  CD1 . ILE H  1 151 ? 47.123  89.742  90.841  1.00 15.67 ? 151  ILE H CD1 1 
ATOM   8742  N  N   . ALA H  1 152 ? 43.819  92.911  94.513  1.00 9.02  ? 152  ALA H N   1 
ATOM   8743  C  CA  . ALA H  1 152 ? 43.155  94.131  94.907  1.00 11.23 ? 152  ALA H CA  1 
ATOM   8744  C  C   . ALA H  1 152 ? 44.191  95.222  95.121  1.00 12.97 ? 152  ALA H C   1 
ATOM   8745  O  O   . ALA H  1 152 ? 45.347  94.923  95.350  1.00 12.54 ? 152  ALA H O   1 
ATOM   8746  C  CB  . ALA H  1 152 ? 42.327  93.898  96.183  1.00 10.61 ? 152  ALA H CB  1 
ATOM   8747  N  N   . GLN H  1 153 ? 43.770  96.473  95.048  1.00 15.94 ? 153  GLN H N   1 
ATOM   8748  C  CA  . GLN H  1 153 ? 44.718  97.575  95.218  1.00 19.96 ? 153  GLN H CA  1 
ATOM   8749  C  C   . GLN H  1 153 ? 45.150  97.723  96.669  1.00 21.73 ? 153  GLN H C   1 
ATOM   8750  O  O   . GLN H  1 153 ? 44.249  97.764  97.531  1.00 22.42 ? 153  GLN H O   1 
ATOM   8751  C  CB  . GLN H  1 153 ? 44.093  98.885  94.757  1.00 20.21 ? 153  GLN H CB  1 
ATOM   8752  C  CG  . GLN H  1 153 ? 45.083  100.044 94.709  1.00 24.38 ? 153  GLN H CG  1 
ATOM   8753  C  CD  . GLN H  1 153 ? 44.454  101.290 94.128  1.00 26.29 ? 153  GLN H CD  1 
ATOM   8754  O  OE1 . GLN H  1 153 ? 43.266  101.535 94.334  1.00 29.45 ? 153  GLN H OE1 1 
ATOM   8755  N  NE2 . GLN H  1 153 ? 45.230  102.068 93.410  1.00 26.73 ? 153  GLN H NE2 1 
ATOM   8756  O  OXT . GLN H  1 153 ? 46.366  97.831  96.904  1.00 23.77 ? 153  GLN H OXT 1 
ATOM   8757  N  N   . ALA I  1 1   ? -9.370  79.747  42.442  1.00 22.81 ? 1    ALA I N   1 
ATOM   8758  C  CA  . ALA I  1 1   ? -10.374 79.892  41.333  1.00 21.72 ? 1    ALA I CA  1 
ATOM   8759  C  C   . ALA I  1 1   ? -9.629  80.327  40.075  1.00 20.00 ? 1    ALA I C   1 
ATOM   8760  O  O   . ALA I  1 1   ? -9.105  79.498  39.359  1.00 20.63 ? 1    ALA I O   1 
ATOM   8761  C  CB  . ALA I  1 1   ? -11.412 80.912  41.706  1.00 22.49 ? 1    ALA I CB  1 
ATOM   8762  N  N   . THR I  1 2   ? -9.586  81.619  39.793  1.00 18.30 ? 2    THR I N   1 
ATOM   8763  C  CA  . THR I  1 2   ? -8.701  82.047  38.711  1.00 15.73 ? 2    THR I CA  1 
ATOM   8764  C  C   . THR I  1 2   ? -7.290  82.070  39.355  1.00 12.64 ? 2    THR I C   1 
ATOM   8765  O  O   . THR I  1 2   ? -7.129  82.312  40.570  1.00 9.46  ? 2    THR I O   1 
ATOM   8766  C  CB  . THR I  1 2   ? -9.200  83.337  38.056  1.00 18.13 ? 2    THR I CB  1 
ATOM   8767  O  OG1 . THR I  1 2   ? -8.728  83.445  36.713  1.00 23.79 ? 2    THR I OG1 1 
ATOM   8768  C  CG2 . THR I  1 2   ? -8.652  84.542  38.732  1.00 21.37 ? 2    THR I CG2 1 
ATOM   8769  N  N   . LYS I  1 3   ? -6.280  81.732  38.552  1.00 9.17  ? 3    LYS I N   1 
ATOM   8770  C  CA  . LYS I  1 3   ? -4.907  81.571  39.037  1.00 7.26  ? 3    LYS I CA  1 
ATOM   8771  C  C   . LYS I  1 3   ? -3.963  82.161  38.013  1.00 7.22  ? 3    LYS I C   1 
ATOM   8772  O  O   . LYS I  1 3   ? -4.266  82.141  36.798  1.00 5.52  ? 3    LYS I O   1 
ATOM   8773  C  CB  . LYS I  1 3   ? -4.544  80.101  39.180  1.00 8.19  ? 3    LYS I CB  1 
ATOM   8774  C  CG  . LYS I  1 3   ? -5.254  79.383  40.376  1.00 12.36 ? 3    LYS I CG  1 
ATOM   8775  C  CD  . LYS I  1 3   ? -4.899  77.884  40.452  1.00 20.23 ? 3    LYS I CD  1 
ATOM   8776  C  CE  . LYS I  1 3   ? -5.677  77.226  41.643  1.00 22.85 ? 3    LYS I CE  1 
ATOM   8777  N  NZ  . LYS I  1 3   ? -5.268  75.810  41.953  1.00 27.43 ? 3    LYS I NZ  1 
ATOM   8778  N  N   . ALA I  1 4   ? -2.858  82.714  38.509  1.00 5.00  ? 4    ALA I N   1 
ATOM   8779  C  CA  . ALA I  1 4   ? -1.850  83.305  37.628  1.00 5.02  ? 4    ALA I CA  1 
ATOM   8780  C  C   . ALA I  1 4   ? -0.497  83.000  38.250  1.00 5.00  ? 4    ALA I C   1 
ATOM   8781  O  O   . ALA I  1 4   ? -0.447  82.501  39.382  1.00 5.00  ? 4    ALA I O   1 
ATOM   8782  C  CB  . ALA I  1 4   ? -2.038  84.803  37.492  1.00 5.00  ? 4    ALA I CB  1 
ATOM   8783  N  N   . VAL I  1 5   ? 0.597   83.268  37.513  1.00 5.00  ? 5    VAL I N   1 
ATOM   8784  C  CA  . VAL I  1 5   ? 1.912   82.899  38.024  1.00 5.00  ? 5    VAL I CA  1 
ATOM   8785  C  C   . VAL I  1 5   ? 2.896   83.793  37.329  1.00 5.09  ? 5    VAL I C   1 
ATOM   8786  O  O   . VAL I  1 5   ? 2.626   84.239  36.211  1.00 5.00  ? 5    VAL I O   1 
ATOM   8787  C  CB  . VAL I  1 5   ? 2.242   81.384  37.786  1.00 5.00  ? 5    VAL I CB  1 
ATOM   8788  C  CG1 . VAL I  1 5   ? 2.337   81.050  36.226  1.00 5.00  ? 5    VAL I CG1 1 
ATOM   8789  C  CG2 . VAL I  1 5   ? 3.517   80.892  38.548  1.00 5.00  ? 5    VAL I CG2 1 
ATOM   8790  N  N   . CYS I  1 6   ? 4.037   84.004  37.969  1.00 5.00  ? 6    CYS I N   1 
ATOM   8791  C  CA  . CYS I  1 6   ? 5.027   84.899  37.394  1.00 5.00  ? 6    CYS I CA  1 
ATOM   8792  C  C   . CYS I  1 6   ? 6.389   84.379  37.790  1.00 5.00  ? 6    CYS I C   1 
ATOM   8793  O  O   . CYS I  1 6   ? 6.604   84.084  38.969  1.00 5.22  ? 6    CYS I O   1 
ATOM   8794  C  CB  . CYS I  1 6   ? 4.791   86.295  37.964  1.00 5.30  ? 6    CYS I CB  1 
ATOM   8795  S  SG  . CYS I  1 6   ? 6.022   87.486  37.399  1.00 7.08  ? 6    CYS I SG  1 
ATOM   8796  N  N   . VAL I  1 7   ? 7.268   84.190  36.809  1.00 5.00  ? 7    VAL I N   1 
ATOM   8797  C  CA  . VAL I  1 7   ? 8.641   83.809  37.094  1.00 5.00  ? 7    VAL I CA  1 
ATOM   8798  C  C   . VAL I  1 7   ? 9.499   85.071  37.050  1.00 5.00  ? 7    VAL I C   1 
ATOM   8799  O  O   . VAL I  1 7   ? 9.596   85.737  35.992  1.00 5.00  ? 7    VAL I O   1 
ATOM   8800  C  CB  . VAL I  1 7   ? 9.148   82.804  36.036  1.00 5.00  ? 7    VAL I CB  1 
ATOM   8801  C  CG1 . VAL I  1 7   ? 10.588  82.384  36.343  1.00 5.05  ? 7    VAL I CG1 1 
ATOM   8802  C  CG2 . VAL I  1 7   ? 8.243   81.566  35.985  1.00 5.00  ? 7    VAL I CG2 1 
ATOM   8803  N  N   . LEU I  1 8   ? 10.108  85.414  38.188  1.00 5.00  ? 8    LEU I N   1 
ATOM   8804  C  CA  . LEU I  1 8   ? 10.921  86.620  38.262  1.00 5.57  ? 8    LEU I CA  1 
ATOM   8805  C  C   . LEU I  1 8   ? 12.367  86.273  37.950  1.00 6.34  ? 8    LEU I C   1 
ATOM   8806  O  O   . LEU I  1 8   ? 12.932  85.344  38.522  1.00 5.00  ? 8    LEU I O   1 
ATOM   8807  C  CB  . LEU I  1 8   ? 10.843  87.191  39.679  1.00 6.12  ? 8    LEU I CB  1 
ATOM   8808  C  CG  . LEU I  1 8   ? 9.477   87.686  40.242  1.00 9.77  ? 8    LEU I CG  1 
ATOM   8809  C  CD1 . LEU I  1 8   ? 9.535   87.886  41.804  1.00 13.33 ? 8    LEU I CD1 1 
ATOM   8810  C  CD2 . LEU I  1 8   ? 9.099   88.961  39.612  1.00 11.70 ? 8    LEU I CD2 1 
ATOM   8811  N  N   . LYS I  1 9   ? 12.983  87.047  37.058  1.00 5.57  ? 9    LYS I N   1 
ATOM   8812  C  CA  . LYS I  1 9   ? 14.382  86.847  36.726  1.00 7.09  ? 9    LYS I CA  1 
ATOM   8813  C  C   . LYS I  1 9   ? 14.973  88.229  36.418  1.00 7.15  ? 9    LYS I C   1 
ATOM   8814  O  O   . LYS I  1 9   ? 14.236  89.156  36.073  1.00 6.35  ? 9    LYS I O   1 
ATOM   8815  C  CB  . LYS I  1 9   ? 14.516  85.931  35.471  1.00 8.92  ? 9    LYS I CB  1 
ATOM   8816  C  CG  . LYS I  1 9   ? 13.848  84.534  35.560  1.00 13.57 ? 9    LYS I CG  1 
ATOM   8817  C  CD  . LYS I  1 9   ? 14.144  83.628  34.336  1.00 16.86 ? 9    LYS I CD  1 
ATOM   8818  C  CE  . LYS I  1 9   ? 13.698  82.122  34.597  1.00 20.72 ? 9    LYS I CE  1 
ATOM   8819  N  NZ  . LYS I  1 9   ? 14.134  81.558  35.949  1.00 22.70 ? 9    LYS I NZ  1 
ATOM   8820  N  N   . GLY I  1 10  ? 16.298  88.365  36.470  1.00 8.35  ? 10   GLY I N   1 
ATOM   8821  C  CA  . GLY I  1 10  ? 16.899  89.634  36.114  1.00 8.22  ? 10   GLY I CA  1 
ATOM   8822  C  C   . GLY I  1 10  ? 18.326  89.410  35.631  1.00 10.86 ? 10   GLY I C   1 
ATOM   8823  O  O   . GLY I  1 10  ? 18.686  88.298  35.216  1.00 10.57 ? 10   GLY I O   1 
ATOM   8824  N  N   . ASP I  1 11  ? 19.112  90.471  35.689  1.00 12.00 ? 11   ASP I N   1 
ATOM   8825  C  CA  . ASP I  1 11  ? 20.530  90.429  35.290  1.00 14.68 ? 11   ASP I CA  1 
ATOM   8826  C  C   . ASP I  1 11  ? 21.440  89.904  36.383  1.00 14.68 ? 11   ASP I C   1 
ATOM   8827  O  O   . ASP I  1 11  ? 22.593  89.525  36.126  1.00 15.27 ? 11   ASP I O   1 
ATOM   8828  C  CB  . ASP I  1 11  ? 20.980  91.831  34.909  1.00 16.17 ? 11   ASP I CB  1 
ATOM   8829  C  CG  . ASP I  1 11  ? 20.377  92.293  33.601  1.00 20.89 ? 11   ASP I CG  1 
ATOM   8830  O  OD1 . ASP I  1 11  ? 19.979  91.430  32.787  1.00 23.97 ? 11   ASP I OD1 1 
ATOM   8831  O  OD2 . ASP I  1 11  ? 20.278  93.511  33.313  1.00 27.77 ? 11   ASP I OD2 1 
ATOM   8832  N  N   . GLY I  1 12  ? 20.929  89.874  37.608  1.00 13.67 ? 12   GLY I N   1 
ATOM   8833  C  CA  . GLY I  1 12  ? 21.704  89.434  38.750  1.00 13.13 ? 12   GLY I CA  1 
ATOM   8834  C  C   . GLY I  1 12  ? 21.190  88.099  39.248  1.00 11.89 ? 12   GLY I C   1 
ATOM   8835  O  O   . GLY I  1 12  ? 20.605  87.328  38.490  1.00 12.42 ? 12   GLY I O   1 
ATOM   8836  N  N   . PRO I  1 13  ? 21.413  87.800  40.517  1.00 11.52 ? 13   PRO I N   1 
ATOM   8837  C  CA  . PRO I  1 13  ? 21.002  86.508  41.058  1.00 10.78 ? 13   PRO I CA  1 
ATOM   8838  C  C   . PRO I  1 13  ? 19.576  86.502  41.610  1.00 10.28 ? 13   PRO I C   1 
ATOM   8839  O  O   . PRO I  1 13  ? 19.152  85.474  42.134  1.00 11.45 ? 13   PRO I O   1 
ATOM   8840  C  CB  . PRO I  1 13  ? 21.990  86.313  42.211  1.00 11.56 ? 13   PRO I CB  1 
ATOM   8841  C  CG  . PRO I  1 13  ? 22.028  87.718  42.812  1.00 12.99 ? 13   PRO I CG  1 
ATOM   8842  C  CD  . PRO I  1 13  ? 22.166  88.601  41.506  1.00 12.20 ? 13   PRO I CD  1 
ATOM   8843  N  N   . VAL I  1 14  ? 18.834  87.594  41.478  1.00 7.89  ? 14   VAL I N   1 
ATOM   8844  C  CA  . VAL I  1 14  ? 17.522  87.645  42.122  1.00 6.01  ? 14   VAL I CA  1 
ATOM   8845  C  C   . VAL I  1 14  ? 16.553  86.874  41.254  1.00 5.72  ? 14   VAL I C   1 
ATOM   8846  O  O   . VAL I  1 14  ? 16.461  87.138  40.071  1.00 5.13  ? 14   VAL I O   1 
ATOM   8847  C  CB  . VAL I  1 14  ? 17.050  89.086  42.343  1.00 6.17  ? 14   VAL I CB  1 
ATOM   8848  C  CG1 . VAL I  1 14  ? 15.640  89.112  42.911  1.00 7.24  ? 14   VAL I CG1 1 
ATOM   8849  C  CG2 . VAL I  1 14  ? 18.027  89.776  43.322  1.00 6.89  ? 14   VAL I CG2 1 
ATOM   8850  N  N   . GLN I  1 15  ? 15.847  85.912  41.841  1.00 5.00  ? 15   GLN I N   1 
ATOM   8851  C  CA  . GLN I  1 15  ? 14.984  85.053  41.019  1.00 5.15  ? 15   GLN I CA  1 
ATOM   8852  C  C   . GLN I  1 15  ? 13.905  84.497  41.910  1.00 5.09  ? 15   GLN I C   1 
ATOM   8853  O  O   . GLN I  1 15  ? 14.105  84.341  43.128  1.00 5.00  ? 15   GLN I O   1 
ATOM   8854  C  CB  . GLN I  1 15  ? 15.826  83.898  40.442  1.00 5.35  ? 15   GLN I CB  1 
ATOM   8855  C  CG  . GLN I  1 15  ? 15.045  82.903  39.546  1.00 11.47 ? 15   GLN I CG  1 
ATOM   8856  C  CD  . GLN I  1 15  ? 14.355  81.763  40.336  1.00 16.22 ? 15   GLN I CD  1 
ATOM   8857  O  OE1 . GLN I  1 15  ? 14.830  81.360  41.391  1.00 22.45 ? 15   GLN I OE1 1 
ATOM   8858  N  NE2 . GLN I  1 15  ? 13.250  81.248  39.806  1.00 14.73 ? 15   GLN I NE2 1 
ATOM   8859  N  N   . GLY I  1 16  ? 12.757  84.185  41.332  1.00 5.63  ? 16   GLY I N   1 
ATOM   8860  C  CA  . GLY I  1 16  ? 11.765  83.531  42.163  1.00 5.35  ? 16   GLY I CA  1 
ATOM   8861  C  C   . GLY I  1 16  ? 10.478  83.271  41.405  1.00 5.94  ? 16   GLY I C   1 
ATOM   8862  O  O   . GLY I  1 16  ? 10.352  83.611  40.220  1.00 6.48  ? 16   GLY I O   1 
ATOM   8863  N  N   . ILE I  1 17  ? 9.556   82.579  42.060  1.00 5.00  ? 17   ILE I N   1 
ATOM   8864  C  CA  . ILE I  1 17  ? 8.273   82.273  41.411  1.00 5.00  ? 17   ILE I CA  1 
ATOM   8865  C  C   . ILE I  1 17  ? 7.222   82.815  42.345  1.00 5.19  ? 17   ILE I C   1 
ATOM   8866  O  O   . ILE I  1 17  ? 7.280   82.545  43.551  1.00 5.00  ? 17   ILE I O   1 
ATOM   8867  C  CB  . ILE I  1 17  ? 8.096   80.762  41.274  1.00 5.00  ? 17   ILE I CB  1 
ATOM   8868  C  CG1 . ILE I  1 17  ? 9.083   80.221  40.226  1.00 8.63  ? 17   ILE I CG1 1 
ATOM   8869  C  CG2 . ILE I  1 17  ? 6.618   80.432  40.833  1.00 5.00  ? 17   ILE I CG2 1 
ATOM   8870  C  CD1 . ILE I  1 17  ? 9.016   78.754  40.150  1.00 9.57  ? 17   ILE I CD1 1 
ATOM   8871  N  N   . ILE I  1 18  ? 6.253   83.544  41.793  1.00 5.00  ? 18   ILE I N   1 
ATOM   8872  C  CA  . ILE I  1 18  ? 5.176   84.094  42.596  1.00 5.00  ? 18   ILE I CA  1 
ATOM   8873  C  C   . ILE I  1 18  ? 3.861   83.633  41.988  1.00 5.58  ? 18   ILE I C   1 
ATOM   8874  O  O   . ILE I  1 18  ? 3.638   83.798  40.776  1.00 6.10  ? 18   ILE I O   1 
ATOM   8875  C  CB  . ILE I  1 18  ? 5.227   85.646  42.590  1.00 5.00  ? 18   ILE I CB  1 
ATOM   8876  C  CG1 . ILE I  1 18  ? 6.532   86.163  43.229  1.00 7.21  ? 18   ILE I CG1 1 
ATOM   8877  C  CG2 . ILE I  1 18  ? 3.922   86.217  43.231  1.00 5.00  ? 18   ILE I CG2 1 
ATOM   8878  C  CD1 . ILE I  1 18  ? 6.602   85.774  44.777  1.00 8.02  ? 18   ILE I CD1 1 
ATOM   8879  N  N   . ASN I  1 19  ? 2.971   83.118  42.837  1.00 5.00  ? 19   ASN I N   1 
ATOM   8880  C  CA  . ASN I  1 19  ? 1.689   82.604  42.435  1.00 5.05  ? 19   ASN I CA  1 
ATOM   8881  C  C   . ASN I  1 19  ? 0.628   83.583  42.854  1.00 5.00  ? 19   ASN I C   1 
ATOM   8882  O  O   . ASN I  1 19  ? 0.779   84.276  43.846  1.00 5.00  ? 19   ASN I O   1 
ATOM   8883  C  CB  . ASN I  1 19  ? 1.406   81.302  43.198  1.00 5.00  ? 19   ASN I CB  1 
ATOM   8884  C  CG  . ASN I  1 19  ? 2.495   80.275  42.995  1.00 8.03  ? 19   ASN I CG  1 
ATOM   8885  O  OD1 . ASN I  1 19  ? 3.328   80.004  43.900  1.00 12.72 ? 19   ASN I OD1 1 
ATOM   8886  N  ND2 . ASN I  1 19  ? 2.527   79.716  41.823  1.00 5.00  ? 19   ASN I ND2 1 
ATOM   8887  N  N   . PHE I  1 20  ? -0.471  83.587  42.125  1.00 5.00  ? 20   PHE I N   1 
ATOM   8888  C  CA  . PHE I  1 20  ? -1.612  84.423  42.428  1.00 5.17  ? 20   PHE I CA  1 
ATOM   8889  C  C   . PHE I  1 20  ? -2.877  83.559  42.422  1.00 5.11  ? 20   PHE I C   1 
ATOM   8890  O  O   . PHE I  1 20  ? -3.067  82.692  41.555  1.00 5.47  ? 20   PHE I O   1 
ATOM   8891  C  CB  . PHE I  1 20  ? -1.818  85.490  41.341  1.00 5.00  ? 20   PHE I CB  1 
ATOM   8892  C  CG  . PHE I  1 20  ? -0.659  86.440  41.187  1.00 5.00  ? 20   PHE I CG  1 
ATOM   8893  C  CD1 . PHE I  1 20  ? 0.454   86.064  40.448  1.00 5.53  ? 20   PHE I CD1 1 
ATOM   8894  C  CD2 . PHE I  1 20  ? -0.700  87.701  41.759  1.00 7.00  ? 20   PHE I CD2 1 
ATOM   8895  C  CE1 . PHE I  1 20  ? 1.515   86.958  40.260  1.00 5.74  ? 20   PHE I CE1 1 
ATOM   8896  C  CE2 . PHE I  1 20  ? 0.375   88.584  41.605  1.00 7.81  ? 20   PHE I CE2 1 
ATOM   8897  C  CZ  . PHE I  1 20  ? 1.461   88.211  40.852  1.00 6.08  ? 20   PHE I CZ  1 
ATOM   8898  N  N   . GLU I  1 21  ? -3.773  83.793  43.364  1.00 5.45  ? 21   GLU I N   1 
ATOM   8899  C  CA  . GLU I  1 21  ? -5.012  83.018  43.320  1.00 7.04  ? 21   GLU I CA  1 
ATOM   8900  C  C   . GLU I  1 21  ? -6.169  83.920  43.733  1.00 6.54  ? 21   GLU I C   1 
ATOM   8901  O  O   . GLU I  1 21  ? -6.060  84.613  44.728  1.00 5.46  ? 21   GLU I O   1 
ATOM   8902  C  CB  . GLU I  1 21  ? -4.905  81.850  44.300  1.00 8.67  ? 21   GLU I CB  1 
ATOM   8903  C  CG  . GLU I  1 21  ? -6.094  80.910  44.259  1.00 13.50 ? 21   GLU I CG  1 
ATOM   8904  C  CD  . GLU I  1 21  ? -5.860  79.697  45.153  1.00 22.71 ? 21   GLU I CD  1 
ATOM   8905  O  OE1 . GLU I  1 21  ? -5.242  78.725  44.664  1.00 27.77 ? 21   GLU I OE1 1 
ATOM   8906  O  OE2 . GLU I  1 21  ? -6.239  79.741  46.346  1.00 26.60 ? 21   GLU I OE2 1 
ATOM   8907  N  N   . GLN I  1 22  ? -7.270  83.897  42.991  1.00 5.77  ? 22   GLN I N   1 
ATOM   8908  C  CA  . GLN I  1 22  ? -8.426  84.703  43.355  1.00 7.11  ? 22   GLN I CA  1 
ATOM   8909  C  C   . GLN I  1 22  ? -9.643  83.784  43.339  1.00 8.79  ? 22   GLN I C   1 
ATOM   8910  O  O   . GLN I  1 22  ? -10.150 83.453  42.268  1.00 9.20  ? 22   GLN I O   1 
ATOM   8911  C  CB  . GLN I  1 22  ? -8.576  85.869  42.374  1.00 6.12  ? 22   GLN I CB  1 
ATOM   8912  C  CG  . GLN I  1 22  ? -9.636  86.909  42.820  1.00 5.93  ? 22   GLN I CG  1 
ATOM   8913  C  CD  . GLN I  1 22  ? -9.743  88.067  41.831  1.00 5.33  ? 22   GLN I CD  1 
ATOM   8914  O  OE1 . GLN I  1 22  ? -9.461  87.888  40.648  1.00 8.44  ? 22   GLN I OE1 1 
ATOM   8915  N  NE2 . GLN I  1 22  ? -10.146 89.243  42.313  1.00 7.69  ? 22   GLN I NE2 1 
ATOM   8916  N  N   . LYS I  1 23  ? -10.061 83.329  44.522  1.00 10.19 ? 23   LYS I N   1 
ATOM   8917  C  CA  . LYS I  1 23  ? -11.135 82.366  44.642  1.00 11.83 ? 23   LYS I CA  1 
ATOM   8918  C  C   . LYS I  1 23  ? -12.504 82.910  44.235  1.00 11.68 ? 23   LYS I C   1 
ATOM   8919  O  O   . LYS I  1 23  ? -13.322 82.177  43.671  1.00 12.45 ? 23   LYS I O   1 
ATOM   8920  C  CB  . LYS I  1 23  ? -11.185 81.857  46.097  1.00 13.01 ? 23   LYS I CB  1 
ATOM   8921  C  CG  . LYS I  1 23  ? -12.351 80.903  46.369  1.00 18.42 ? 23   LYS I CG  1 
ATOM   8922  C  CD  . LYS I  1 23  ? -12.142 79.513  45.737  1.00 24.73 ? 23   LYS I CD  1 
ATOM   8923  C  CE  . LYS I  1 23  ? -13.268 78.543  46.166  1.00 30.26 ? 23   LYS I CE  1 
ATOM   8924  N  NZ  . LYS I  1 23  ? -12.761 77.161  46.438  1.00 32.29 ? 23   LYS I NZ  1 
ATOM   8925  N  N   . GLU I  1 24  ? -12.761 84.185  44.522  1.00 10.93 ? 24   GLU I N   1 
ATOM   8926  C  CA  . GLU I  1 24  ? -14.064 84.782  44.232  1.00 11.96 ? 24   GLU I CA  1 
ATOM   8927  C  C   . GLU I  1 24  ? -13.903 85.938  43.266  1.00 11.08 ? 24   GLU I C   1 
ATOM   8928  O  O   . GLU I  1 24  ? -12.901 86.634  43.312  1.00 9.11  ? 24   GLU I O   1 
ATOM   8929  C  CB  . GLU I  1 24  ? -14.710 85.362  45.515  1.00 12.79 ? 24   GLU I CB  1 
ATOM   8930  C  CG  . GLU I  1 24  ? -14.747 84.449  46.730  1.00 16.77 ? 24   GLU I CG  1 
ATOM   8931  C  CD  . GLU I  1 24  ? -15.283 85.149  47.978  1.00 23.62 ? 24   GLU I CD  1 
ATOM   8932  O  OE1 . GLU I  1 24  ? -15.942 86.212  47.875  1.00 28.08 ? 24   GLU I OE1 1 
ATOM   8933  O  OE2 . GLU I  1 24  ? -15.030 84.645  49.088  1.00 25.99 ? 24   GLU I OE2 1 
ATOM   8934  N  N   . SER I  1 25  ? -14.913 86.171  42.439  1.00 10.63 ? 25   SER I N   1 
ATOM   8935  C  CA  . SER I  1 25  ? -14.846 87.282  41.503  1.00 11.47 ? 25   SER I CA  1 
ATOM   8936  C  C   . SER I  1 25  ? -14.620 88.547  42.303  1.00 11.58 ? 25   SER I C   1 
ATOM   8937  O  O   . SER I  1 25  ? -15.301 88.788  43.291  1.00 11.06 ? 25   SER I O   1 
ATOM   8938  C  CB  . SER I  1 25  ? -16.174 87.452  40.784  1.00 11.60 ? 25   SER I CB  1 
ATOM   8939  O  OG  . SER I  1 25  ? -16.534 86.275  40.090  1.00 11.77 ? 25   SER I OG  1 
ATOM   8940  N  N   . ASN I  1 26  ? -13.674 89.362  41.895  1.00 12.37 ? 26   ASN I N   1 
ATOM   8941  C  CA  . ASN I  1 26  ? -13.445 90.598  42.637  1.00 13.02 ? 26   ASN I CA  1 
ATOM   8942  C  C   . ASN I  1 26  ? -13.029 90.442  44.089  1.00 12.88 ? 26   ASN I C   1 
ATOM   8943  O  O   . ASN I  1 26  ? -12.933 91.449  44.797  1.00 12.85 ? 26   ASN I O   1 
ATOM   8944  C  CB  . ASN I  1 26  ? -14.704 91.465  42.604  1.00 12.85 ? 26   ASN I CB  1 
ATOM   8945  C  CG  . ASN I  1 26  ? -15.171 91.717  41.213  1.00 15.74 ? 26   ASN I CG  1 
ATOM   8946  O  OD1 . ASN I  1 26  ? -14.411 92.215  40.372  1.00 15.94 ? 26   ASN I OD1 1 
ATOM   8947  N  ND2 . ASN I  1 26  ? -16.394 91.312  40.924  1.00 13.84 ? 26   ASN I ND2 1 
ATOM   8948  N  N   . GLY I  1 27  ? -12.799 89.211  44.541  1.00 12.14 ? 27   GLY I N   1 
ATOM   8949  C  CA  . GLY I  1 27  ? -12.384 88.978  45.922  1.00 11.98 ? 27   GLY I CA  1 
ATOM   8950  C  C   . GLY I  1 27  ? -10.902 89.217  46.147  1.00 10.78 ? 27   GLY I C   1 
ATOM   8951  O  O   . GLY I  1 27  ? -10.172 89.601  45.238  1.00 10.57 ? 27   GLY I O   1 
ATOM   8952  N  N   . PRO I  1 28  ? -10.432 88.969  47.358  1.00 10.26 ? 28   PRO I N   1 
ATOM   8953  C  CA  . PRO I  1 28  ? -9.003  89.124  47.651  1.00 9.51  ? 28   PRO I CA  1 
ATOM   8954  C  C   . PRO I  1 28  ? -8.157  88.196  46.769  1.00 9.02  ? 28   PRO I C   1 
ATOM   8955  O  O   . PRO I  1 28  ? -8.575  87.092  46.407  1.00 8.81  ? 28   PRO I O   1 
ATOM   8956  C  CB  . PRO I  1 28  ? -8.891  88.661  49.099  1.00 9.57  ? 28   PRO I CB  1 
ATOM   8957  C  CG  . PRO I  1 28  ? -10.259 88.796  49.654  1.00 11.55 ? 28   PRO I CG  1 
ATOM   8958  C  CD  . PRO I  1 28  ? -11.214 88.515  48.522  1.00 10.81 ? 28   PRO I CD  1 
ATOM   8959  N  N   . VAL I  1 29  ? -6.964  88.672  46.400  1.00 7.79  ? 29   VAL I N   1 
ATOM   8960  C  CA  . VAL I  1 29  ? -6.022  87.874  45.637  1.00 6.68  ? 29   VAL I CA  1 
ATOM   8961  C  C   . VAL I  1 29  ? -4.921  87.489  46.599  1.00 7.28  ? 29   VAL I C   1 
ATOM   8962  O  O   . VAL I  1 29  ? -4.369  88.351  47.290  1.00 7.14  ? 29   VAL I O   1 
ATOM   8963  C  CB  . VAL I  1 29  ? -5.411  88.688  44.444  1.00 6.76  ? 29   VAL I CB  1 
ATOM   8964  C  CG1 . VAL I  1 29  ? -4.428  87.802  43.632  1.00 5.03  ? 29   VAL I CG1 1 
ATOM   8965  C  CG2 . VAL I  1 29  ? -6.566  89.188  43.494  1.00 6.55  ? 29   VAL I CG2 1 
ATOM   8966  N  N   . LYS I  1 30  ? -4.610  86.191  46.655  1.00 7.23  ? 30   LYS I N   1 
ATOM   8967  C  CA  . LYS I  1 30  ? -3.527  85.676  47.475  1.00 7.71  ? 30   LYS I CA  1 
ATOM   8968  C  C   . LYS I  1 30  ? -2.299  85.671  46.575  1.00 6.69  ? 30   LYS I C   1 
ATOM   8969  O  O   . LYS I  1 30  ? -2.357  85.152  45.455  1.00 6.03  ? 30   LYS I O   1 
ATOM   8970  C  CB  . LYS I  1 30  ? -3.901  84.263  47.920  1.00 9.24  ? 30   LYS I CB  1 
ATOM   8971  C  CG  . LYS I  1 30  ? -2.869  83.448  48.665  1.00 16.78 ? 30   LYS I CG  1 
ATOM   8972  C  CD  . LYS I  1 30  ? -3.589  82.193  49.256  1.00 25.13 ? 30   LYS I CD  1 
ATOM   8973  C  CE  . LYS I  1 30  ? -2.743  80.876  49.218  1.00 29.51 ? 30   LYS I CE  1 
ATOM   8974  N  NZ  . LYS I  1 30  ? -1.669  80.815  50.290  1.00 33.24 ? 30   LYS I NZ  1 
ATOM   8975  N  N   . VAL I  1 31  ? -1.217  86.292  47.042  1.00 6.06  ? 31   VAL I N   1 
ATOM   8976  C  CA  . VAL I  1 31  ? 0.057   86.406  46.285  1.00 5.95  ? 31   VAL I CA  1 
ATOM   8977  C  C   . VAL I  1 31  ? 1.116   85.716  47.102  1.00 6.94  ? 31   VAL I C   1 
ATOM   8978  O  O   . VAL I  1 31  ? 1.436   86.171  48.212  1.00 7.48  ? 31   VAL I O   1 
ATOM   8979  C  CB  . VAL I  1 31  ? 0.464   87.888  46.060  1.00 5.00  ? 31   VAL I CB  1 
ATOM   8980  C  CG1 . VAL I  1 31  ? 1.738   88.010  45.118  1.00 5.28  ? 31   VAL I CG1 1 
ATOM   8981  C  CG2 . VAL I  1 31  ? -0.685  88.611  45.377  1.00 6.04  ? 31   VAL I CG2 1 
ATOM   8982  N  N   . TRP I  1 32  ? 1.689   84.624  46.583  1.00 6.47  ? 32   TRP I N   1 
ATOM   8983  C  CA  . TRP I  1 32  ? 2.663   83.912  47.423  1.00 6.33  ? 32   TRP I CA  1 
ATOM   8984  C  C   . TRP I  1 32  ? 3.703   83.156  46.623  1.00 5.99  ? 32   TRP I C   1 
ATOM   8985  O  O   . TRP I  1 32  ? 3.465   82.745  45.487  1.00 6.23  ? 32   TRP I O   1 
ATOM   8986  C  CB  . TRP I  1 32  ? 1.942   82.949  48.385  1.00 5.93  ? 32   TRP I CB  1 
ATOM   8987  C  CG  . TRP I  1 32  ? 1.517   81.666  47.716  1.00 7.92  ? 32   TRP I CG  1 
ATOM   8988  C  CD1 . TRP I  1 32  ? 2.161   80.475  47.767  1.00 10.72 ? 32   TRP I CD1 1 
ATOM   8989  C  CD2 . TRP I  1 32  ? 0.385   81.489  46.879  1.00 10.23 ? 32   TRP I CD2 1 
ATOM   8990  N  NE1 . TRP I  1 32  ? 1.486   79.559  47.003  1.00 11.43 ? 32   TRP I NE1 1 
ATOM   8991  C  CE2 . TRP I  1 32  ? 0.379   80.154  46.451  1.00 10.84 ? 32   TRP I CE2 1 
ATOM   8992  C  CE3 . TRP I  1 32  ? -0.631  82.355  46.484  1.00 10.18 ? 32   TRP I CE3 1 
ATOM   8993  C  CZ2 . TRP I  1 32  ? -0.586  79.621  45.617  1.00 15.07 ? 32   TRP I CZ2 1 
ATOM   8994  C  CZ3 . TRP I  1 32  ? -1.599  81.828  45.655  1.00 12.81 ? 32   TRP I CZ3 1 
ATOM   8995  C  CH2 . TRP I  1 32  ? -1.575  80.499  45.230  1.00 17.01 ? 32   TRP I CH2 1 
ATOM   8996  N  N   . GLY I  1 33  ? 4.869   83.006  47.228  1.00 5.83  ? 33   GLY I N   1 
ATOM   8997  C  CA  . GLY I  1 33  ? 5.991   82.350  46.586  1.00 6.41  ? 33   GLY I CA  1 
ATOM   8998  C  C   . GLY I  1 33  ? 7.257   82.680  47.335  1.00 7.35  ? 33   GLY I C   1 
ATOM   8999  O  O   . GLY I  1 33  ? 7.221   82.926  48.530  1.00 6.95  ? 33   GLY I O   1 
ATOM   9000  N  N   . SER I  1 34  ? 8.375   82.614  46.635  1.00 7.27  ? 34   SER I N   1 
ATOM   9001  C  CA  . SER I  1 34  ? 9.655   82.818  47.281  1.00 8.88  ? 34   SER I CA  1 
ATOM   9002  C  C   . SER I  1 34  ? 10.530  83.536  46.285  1.00 8.07  ? 34   SER I C   1 
ATOM   9003  O  O   . SER I  1 34  ? 10.405  83.275  45.085  1.00 7.36  ? 34   SER I O   1 
ATOM   9004  C  CB  . SER I  1 34  ? 10.284  81.452  47.588  1.00 9.14  ? 34   SER I CB  1 
ATOM   9005  O  OG  . SER I  1 34  ? 11.506  81.695  48.262  1.00 15.29 ? 34   SER I OG  1 
ATOM   9006  N  N   . ILE I  1 35  ? 11.376  84.458  46.772  1.00 6.60  ? 35   ILE I N   1 
ATOM   9007  C  CA  . ILE I  1 35  ? 12.366  85.144  45.929  1.00 6.77  ? 35   ILE I CA  1 
ATOM   9008  C  C   . ILE I  1 35  ? 13.708  84.987  46.616  1.00 6.99  ? 35   ILE I C   1 
ATOM   9009  O  O   . ILE I  1 35  ? 13.796  85.156  47.853  1.00 7.82  ? 35   ILE I O   1 
ATOM   9010  C  CB  . ILE I  1 35  ? 12.041  86.666  45.775  1.00 5.47  ? 35   ILE I CB  1 
ATOM   9011  C  CG1 . ILE I  1 35  ? 10.571  86.860  45.292  1.00 6.06  ? 35   ILE I CG1 1 
ATOM   9012  C  CG2 . ILE I  1 35  ? 13.046  87.303  44.830  1.00 5.00  ? 35   ILE I CG2 1 
ATOM   9013  C  CD1 . ILE I  1 35  ? 10.078  88.331  45.380  1.00 6.77  ? 35   ILE I CD1 1 
ATOM   9014  N  N   . LYS I  1 36  ? 14.740  84.588  45.872  1.00 7.04  ? 36   LYS I N   1 
ATOM   9015  C  CA  . LYS I  1 36  ? 16.053  84.442  46.494  1.00 7.55  ? 36   LYS I CA  1 
ATOM   9016  C  C   . LYS I  1 36  ? 17.047  85.402  45.845  1.00 7.33  ? 36   LYS I C   1 
ATOM   9017  O  O   . LYS I  1 36  ? 16.724  86.105  44.884  1.00 7.23  ? 36   LYS I O   1 
ATOM   9018  C  CB  . LYS I  1 36  ? 16.533  82.977  46.383  1.00 7.86  ? 36   LYS I CB  1 
ATOM   9019  C  CG  . LYS I  1 36  ? 16.775  82.523  44.944  1.00 11.02 ? 36   LYS I CG  1 
ATOM   9020  C  CD  . LYS I  1 36  ? 17.156  81.048  44.883  1.00 17.79 ? 36   LYS I CD  1 
ATOM   9021  C  CE  . LYS I  1 36  ? 17.478  80.624  43.456  1.00 21.18 ? 36   LYS I CE  1 
ATOM   9022  N  NZ  . LYS I  1 36  ? 17.566  79.099  43.312  1.00 22.77 ? 36   LYS I NZ  1 
ATOM   9023  N  N   . GLY I  1 37  ? 18.245  85.477  46.410  1.00 6.56  ? 37   GLY I N   1 
ATOM   9024  C  CA  . GLY I  1 37  ? 19.272  86.345  45.860  1.00 6.64  ? 37   GLY I CA  1 
ATOM   9025  C  C   . GLY I  1 37  ? 19.228  87.796  46.303  1.00 7.40  ? 37   GLY I C   1 
ATOM   9026  O  O   . GLY I  1 37  ? 19.935  88.641  45.747  1.00 7.48  ? 37   GLY I O   1 
ATOM   9027  N  N   . LEU I  1 38  ? 18.408  88.112  47.300  1.00 6.28  ? 38   LEU I N   1 
ATOM   9028  C  CA  . LEU I  1 38  ? 18.200  89.495  47.678  1.00 6.64  ? 38   LEU I CA  1 
ATOM   9029  C  C   . LEU I  1 38  ? 19.073  89.884  48.855  1.00 7.14  ? 38   LEU I C   1 
ATOM   9030  O  O   . LEU I  1 38  ? 19.480  89.012  49.627  1.00 6.63  ? 38   LEU I O   1 
ATOM   9031  C  CB  . LEU I  1 38  ? 16.751  89.679  48.160  1.00 6.18  ? 38   LEU I CB  1 
ATOM   9032  C  CG  . LEU I  1 38  ? 15.669  89.607  47.068  1.00 7.28  ? 38   LEU I CG  1 
ATOM   9033  C  CD1 . LEU I  1 38  ? 14.240  89.294  47.654  1.00 7.45  ? 38   LEU I CD1 1 
ATOM   9034  C  CD2 . LEU I  1 38  ? 15.689  90.883  46.246  1.00 9.87  ? 38   LEU I CD2 1 
ATOM   9035  N  N   . THR I  1 39  ? 19.304  91.182  49.034  1.00 6.39  ? 39   THR I N   1 
ATOM   9036  C  CA  . THR I  1 39  ? 19.970  91.603  50.267  1.00 8.54  ? 39   THR I CA  1 
ATOM   9037  C  C   . THR I  1 39  ? 18.976  91.505  51.424  1.00 8.99  ? 39   THR I C   1 
ATOM   9038  O  O   . THR I  1 39  ? 17.775  91.680  51.246  1.00 9.66  ? 39   THR I O   1 
ATOM   9039  C  CB  . THR I  1 39  ? 20.482  93.040  50.204  1.00 8.42  ? 39   THR I CB  1 
ATOM   9040  O  OG1 . THR I  1 39  ? 19.428  93.895  49.752  1.00 9.09  ? 39   THR I OG1 1 
ATOM   9041  C  CG2 . THR I  1 39  ? 21.576  93.192  49.192  1.00 8.39  ? 39   THR I CG2 1 
ATOM   9042  N  N   . GLU I  1 40  ? 19.482  91.202  52.612  1.00 9.81  ? 40   GLU I N   1 
ATOM   9043  C  CA  . GLU I  1 40  ? 18.636  91.106  53.789  1.00 9.43  ? 40   GLU I CA  1 
ATOM   9044  C  C   . GLU I  1 40  ? 17.868  92.400  53.979  1.00 9.39  ? 40   GLU I C   1 
ATOM   9045  O  O   . GLU I  1 40  ? 18.442  93.486  53.848  1.00 9.15  ? 40   GLU I O   1 
ATOM   9046  C  CB  . GLU I  1 40  ? 19.502  90.816  55.026  1.00 9.92  ? 40   GLU I CB  1 
ATOM   9047  C  CG  . GLU I  1 40  ? 18.716  90.513  56.294  1.00 11.33 ? 40   GLU I CG  1 
ATOM   9048  C  CD  . GLU I  1 40  ? 19.627  90.241  57.497  1.00 17.93 ? 40   GLU I CD  1 
ATOM   9049  O  OE1 . GLU I  1 40  ? 20.855  90.149  57.294  1.00 14.65 ? 40   GLU I OE1 1 
ATOM   9050  O  OE2 . GLU I  1 40  ? 19.116  90.108  58.633  1.00 16.98 ? 40   GLU I OE2 1 
ATOM   9051  N  N   . GLY I  1 41  ? 16.579  92.299  54.301  1.00 8.83  ? 41   GLY I N   1 
ATOM   9052  C  CA  . GLY I  1 41  ? 15.770  93.483  54.528  1.00 9.68  ? 41   GLY I CA  1 
ATOM   9053  C  C   . GLY I  1 41  ? 14.630  93.682  53.556  1.00 9.63  ? 41   GLY I C   1 
ATOM   9054  O  O   . GLY I  1 41  ? 14.245  92.764  52.831  1.00 9.94  ? 41   GLY I O   1 
ATOM   9055  N  N   . LEU I  1 42  ? 14.074  94.886  53.539  1.00 9.33  ? 42   LEU I N   1 
ATOM   9056  C  CA  . LEU I  1 42  ? 12.887  95.132  52.729  1.00 8.79  ? 42   LEU I CA  1 
ATOM   9057  C  C   . LEU I  1 42  ? 13.192  95.469  51.292  1.00 7.28  ? 42   LEU I C   1 
ATOM   9058  O  O   . LEU I  1 42  ? 14.159  96.160  50.988  1.00 7.35  ? 42   LEU I O   1 
ATOM   9059  C  CB  . LEU I  1 42  ? 12.122  96.335  53.265  1.00 9.43  ? 42   LEU I CB  1 
ATOM   9060  C  CG  . LEU I  1 42  ? 11.626  96.230  54.705  1.00 11.18 ? 42   LEU I CG  1 
ATOM   9061  C  CD1 . LEU I  1 42  ? 11.170  97.658  55.197  1.00 12.69 ? 42   LEU I CD1 1 
ATOM   9062  C  CD2 . LEU I  1 42  ? 10.562  95.240  54.797  1.00 12.64 ? 42   LEU I CD2 1 
ATOM   9063  N  N   . HIS I  1 43  ? 12.282  95.033  50.435  1.00 6.62  ? 43   HIS I N   1 
ATOM   9064  C  CA  . HIS I  1 43  ? 12.367  95.268  49.016  1.00 5.46  ? 43   HIS I CA  1 
ATOM   9065  C  C   . HIS I  1 43  ? 11.005  95.584  48.433  1.00 5.43  ? 43   HIS I C   1 
ATOM   9066  O  O   . HIS I  1 43  ? 10.058  94.831  48.613  1.00 5.71  ? 43   HIS I O   1 
ATOM   9067  C  CB  . HIS I  1 43  ? 12.922  94.017  48.317  1.00 5.00  ? 43   HIS I CB  1 
ATOM   9068  C  CG  . HIS I  1 43  ? 14.354  93.747  48.666  1.00 5.08  ? 43   HIS I CG  1 
ATOM   9069  N  ND1 . HIS I  1 43  ? 15.406  94.322  47.989  1.00 6.85  ? 43   HIS I ND1 1 
ATOM   9070  C  CD2 . HIS I  1 43  ? 14.907  93.006  49.663  1.00 8.72  ? 43   HIS I CD2 1 
ATOM   9071  C  CE1 . HIS I  1 43  ? 16.550  93.946  48.547  1.00 7.69  ? 43   HIS I CE1 1 
ATOM   9072  N  NE2 . HIS I  1 43  ? 16.276  93.138  49.561  1.00 9.01  ? 43   HIS I NE2 1 
ATOM   9073  N  N   . GLY I  1 44  ? 10.919  96.692  47.690  1.00 5.19  ? 44   GLY I N   1 
ATOM   9074  C  CA  . GLY I  1 44  ? 9.642   97.102  47.089  1.00 5.00  ? 44   GLY I CA  1 
ATOM   9075  C  C   . GLY I  1 44  ? 9.150   96.023  46.125  1.00 5.12  ? 44   GLY I C   1 
ATOM   9076  O  O   . GLY I  1 44  ? 9.968   95.361  45.473  1.00 5.00  ? 44   GLY I O   1 
ATOM   9077  N  N   . PHE I  1 45  ? 7.839   95.859  46.036  1.00 5.00  ? 45   PHE I N   1 
ATOM   9078  C  CA  . PHE I  1 45  ? 7.238   94.730  45.299  1.00 5.00  ? 45   PHE I CA  1 
ATOM   9079  C  C   . PHE I  1 45  ? 5.971   95.319  44.653  1.00 5.00  ? 45   PHE I C   1 
ATOM   9080  O  O   . PHE I  1 45  ? 5.027   95.682  45.353  1.00 5.33  ? 45   PHE I O   1 
ATOM   9081  C  CB  . PHE I  1 45  ? 6.886   93.697  46.350  1.00 5.00  ? 45   PHE I CB  1 
ATOM   9082  C  CG  . PHE I  1 45  ? 6.403   92.367  45.821  1.00 5.00  ? 45   PHE I CG  1 
ATOM   9083  C  CD1 . PHE I  1 45  ? 7.213   91.573  44.991  1.00 5.32  ? 45   PHE I CD1 1 
ATOM   9084  C  CD2 . PHE I  1 45  ? 5.178   91.885  46.215  1.00 6.56  ? 45   PHE I CD2 1 
ATOM   9085  C  CE1 . PHE I  1 45  ? 6.770   90.315  44.542  1.00 7.70  ? 45   PHE I CE1 1 
ATOM   9086  C  CE2 . PHE I  1 45  ? 4.737   90.589  45.760  1.00 5.10  ? 45   PHE I CE2 1 
ATOM   9087  C  CZ  . PHE I  1 45  ? 5.551   89.829  44.943  1.00 5.77  ? 45   PHE I CZ  1 
ATOM   9088  N  N   . HIS I  1 46  ? 5.978   95.450  43.331  1.00 5.00  ? 46   HIS I N   1 
ATOM   9089  C  CA  . HIS I  1 46  ? 4.899   96.156  42.640  1.00 5.25  ? 46   HIS I CA  1 
ATOM   9090  C  C   . HIS I  1 46  ? 4.518   95.507  41.330  1.00 5.00  ? 46   HIS I C   1 
ATOM   9091  O  O   . HIS I  1 46  ? 5.360   94.914  40.626  1.00 5.00  ? 46   HIS I O   1 
ATOM   9092  C  CB  . HIS I  1 46  ? 5.379   97.559  42.219  1.00 6.08  ? 46   HIS I CB  1 
ATOM   9093  C  CG  . HIS I  1 46  ? 6.046   98.325  43.308  1.00 5.00  ? 46   HIS I CG  1 
ATOM   9094  N  ND1 . HIS I  1 46  ? 7.286   98.885  43.189  1.00 5.90  ? 46   HIS I ND1 1 
ATOM   9095  C  CD2 . HIS I  1 46  ? 5.646   98.582  44.581  1.00 5.25  ? 46   HIS I CD2 1 
ATOM   9096  C  CE1 . HIS I  1 46  ? 7.622   99.494  44.307  1.00 8.23  ? 46   HIS I CE1 1 
ATOM   9097  N  NE2 . HIS I  1 46  ? 6.648   99.298  45.179  1.00 5.46  ? 46   HIS I NE2 1 
ATOM   9098  N  N   . VAL I  1 47  ? 3.274   95.724  40.973  1.00 5.00  ? 47   VAL I N   1 
ATOM   9099  C  CA  . VAL I  1 47  ? 2.858   95.447  39.628  1.00 5.00  ? 47   VAL I CA  1 
ATOM   9100  C  C   . VAL I  1 47  ? 3.060   96.713  38.774  1.00 5.49  ? 47   VAL I C   1 
ATOM   9101  O  O   . VAL I  1 47  ? 2.481   97.786  39.058  1.00 5.00  ? 47   VAL I O   1 
ATOM   9102  C  CB  . VAL I  1 47  ? 1.431   95.001  39.573  1.00 5.00  ? 47   VAL I CB  1 
ATOM   9103  C  CG1 . VAL I  1 47  ? 1.043   94.730  38.110  1.00 5.00  ? 47   VAL I CG1 1 
ATOM   9104  C  CG2 . VAL I  1 47  ? 1.271   93.723  40.497  1.00 5.53  ? 47   VAL I CG2 1 
ATOM   9105  N  N   . HIS I  1 48  ? 3.855   96.575  37.717  1.00 5.00  ? 48   HIS I N   1 
ATOM   9106  C  CA  . HIS I  1 48  ? 4.091   97.674  36.790  1.00 5.15  ? 48   HIS I CA  1 
ATOM   9107  C  C   . HIS I  1 48  ? 3.175   97.477  35.589  1.00 5.00  ? 48   HIS I C   1 
ATOM   9108  O  O   . HIS I  1 48  ? 2.716   96.369  35.337  1.00 5.00  ? 48   HIS I O   1 
ATOM   9109  C  CB  . HIS I  1 48  ? 5.561   97.725  36.377  1.00 5.00  ? 48   HIS I CB  1 
ATOM   9110  C  CG  . HIS I  1 48  ? 6.447   98.274  37.447  1.00 5.00  ? 48   HIS I CG  1 
ATOM   9111  N  ND1 . HIS I  1 48  ? 7.268   99.356  37.250  1.00 5.00  ? 48   HIS I ND1 1 
ATOM   9112  C  CD2 . HIS I  1 48  ? 6.665   97.857  38.720  1.00 6.69  ? 48   HIS I CD2 1 
ATOM   9113  C  CE1 . HIS I  1 48  ? 7.945   99.602  38.361  1.00 5.61  ? 48   HIS I CE1 1 
ATOM   9114  N  NE2 . HIS I  1 48  ? 7.612   98.690  39.258  1.00 5.39  ? 48   HIS I NE2 1 
ATOM   9115  N  N   . GLU I  1 49  ? 3.008   98.545  34.805  1.00 5.04  ? 49   GLU I N   1 
ATOM   9116  C  CA  . GLU I  1 49  ? 1.944   98.657  33.819  1.00 5.02  ? 49   GLU I CA  1 
ATOM   9117  C  C   . GLU I  1 49  ? 2.029   97.709  32.635  1.00 5.00  ? 49   GLU I C   1 
ATOM   9118  O  O   . GLU I  1 49  ? 1.032   97.082  32.260  1.00 5.00  ? 49   GLU I O   1 
ATOM   9119  C  CB  . GLU I  1 49  ? 1.913   100.096 33.264  1.00 5.46  ? 49   GLU I CB  1 
ATOM   9120  C  CG  . GLU I  1 49  ? 0.686   100.339 32.410  1.00 8.19  ? 49   GLU I CG  1 
ATOM   9121  C  CD  . GLU I  1 49  ? 0.559   101.790 31.987  1.00 10.13 ? 49   GLU I CD  1 
ATOM   9122  O  OE1 . GLU I  1 49  ? 1.402   102.627 32.406  1.00 8.02  ? 49   GLU I OE1 1 
ATOM   9123  O  OE2 . GLU I  1 49  ? -0.395  102.073 31.225  1.00 10.44 ? 49   GLU I OE2 1 
ATOM   9124  N  N   . PHE I  1 50  ? 3.230   97.582  32.053  1.00 5.00  ? 50   PHE I N   1 
ATOM   9125  C  CA  . PHE I  1 50  ? 3.342   96.825  30.809  1.00 5.00  ? 50   PHE I CA  1 
ATOM   9126  C  C   . PHE I  1 50  ? 4.053   95.499  30.981  1.00 5.00  ? 50   PHE I C   1 
ATOM   9127  O  O   . PHE I  1 50  ? 5.076   95.449  31.668  1.00 5.00  ? 50   PHE I O   1 
ATOM   9128  C  CB  . PHE I  1 50  ? 4.139   97.654  29.772  1.00 5.00  ? 50   PHE I CB  1 
ATOM   9129  C  CG  . PHE I  1 50  ? 3.563   99.019  29.568  1.00 6.24  ? 50   PHE I CG  1 
ATOM   9130  C  CD1 . PHE I  1 50  ? 2.275   99.163  29.103  1.00 8.77  ? 50   PHE I CD1 1 
ATOM   9131  C  CD2 . PHE I  1 50  ? 4.283   100.145 29.901  1.00 8.84  ? 50   PHE I CD2 1 
ATOM   9132  C  CE1 . PHE I  1 50  ? 1.716   100.437 28.958  1.00 10.22 ? 50   PHE I CE1 1 
ATOM   9133  C  CE2 . PHE I  1 50  ? 3.726   101.417 29.752  1.00 11.93 ? 50   PHE I CE2 1 
ATOM   9134  C  CZ  . PHE I  1 50  ? 2.453   101.542 29.274  1.00 9.52  ? 50   PHE I CZ  1 
ATOM   9135  N  N   . GLY I  1 51  ? 3.528   94.459  30.322  1.00 5.00  ? 51   GLY I N   1 
ATOM   9136  C  CA  . GLY I  1 51  ? 4.123   93.107  30.316  1.00 5.00  ? 51   GLY I CA  1 
ATOM   9137  C  C   . GLY I  1 51  ? 5.155   93.113  29.176  1.00 5.65  ? 51   GLY I C   1 
ATOM   9138  O  O   . GLY I  1 51  ? 5.162   92.220  28.333  1.00 6.18  ? 51   GLY I O   1 
ATOM   9139  N  N   . ASP I  1 52  ? 6.042   94.109  29.181  1.00 6.06  ? 52   ASP I N   1 
ATOM   9140  C  CA  . ASP I  1 52  ? 7.036   94.293  28.112  1.00 5.90  ? 52   ASP I CA  1 
ATOM   9141  C  C   . ASP I  1 52  ? 8.449   94.134  28.658  1.00 5.71  ? 52   ASP I C   1 
ATOM   9142  O  O   . ASP I  1 52  ? 8.919   94.984  29.396  1.00 7.45  ? 52   ASP I O   1 
ATOM   9143  C  CB  . ASP I  1 52  ? 6.857   95.708  27.531  1.00 5.70  ? 52   ASP I CB  1 
ATOM   9144  C  CG  . ASP I  1 52  ? 7.727   95.971  26.321  1.00 7.51  ? 52   ASP I CG  1 
ATOM   9145  O  OD1 . ASP I  1 52  ? 8.798   95.331  26.183  1.00 5.00  ? 52   ASP I OD1 1 
ATOM   9146  O  OD2 . ASP I  1 52  ? 7.381   96.828  25.460  1.00 6.32  ? 52   ASP I OD2 1 
ATOM   9147  N  N   . ASN I  1 53  ? 9.090   93.020  28.332  1.00 5.97  ? 53   ASN I N   1 
ATOM   9148  C  CA  . ASN I  1 53  ? 10.450  92.731  28.774  1.00 7.42  ? 53   ASN I CA  1 
ATOM   9149  C  C   . ASN I  1 53  ? 11.473  92.941  27.672  1.00 6.81  ? 53   ASN I C   1 
ATOM   9150  O  O   . ASN I  1 53  ? 12.590  92.426  27.767  1.00 7.51  ? 53   ASN I O   1 
ATOM   9151  C  CB  . ASN I  1 53  ? 10.524  91.246  29.270  1.00 8.87  ? 53   ASN I CB  1 
ATOM   9152  C  CG  . ASN I  1 53  ? 11.821  90.930  30.021  1.00 13.50 ? 53   ASN I CG  1 
ATOM   9153  O  OD1 . ASN I  1 53  ? 12.536  89.968  29.682  1.00 21.98 ? 53   ASN I OD1 1 
ATOM   9154  N  ND2 . ASN I  1 53  ? 12.152  91.752  31.007  1.00 15.82 ? 53   ASN I ND2 1 
ATOM   9155  N  N   . THR I  1 54  ? 11.134  93.707  26.637  1.00 6.93  ? 54   THR I N   1 
ATOM   9156  C  CA  . THR I  1 54  ? 12.097  93.925  25.527  1.00 7.76  ? 54   THR I CA  1 
ATOM   9157  C  C   . THR I  1 54  ? 13.386  94.642  25.909  1.00 9.43  ? 54   THR I C   1 
ATOM   9158  O  O   . THR I  1 54  ? 14.430  94.498  25.215  1.00 10.19 ? 54   THR I O   1 
ATOM   9159  C  CB  . THR I  1 54  ? 11.466  94.633  24.340  1.00 6.59  ? 54   THR I CB  1 
ATOM   9160  O  OG1 . THR I  1 54  ? 10.878  95.869  24.731  1.00 6.88  ? 54   THR I OG1 1 
ATOM   9161  C  CG2 . THR I  1 54  ? 10.311  93.810  23.786  1.00 8.30  ? 54   THR I CG2 1 
ATOM   9162  N  N   . ALA I  1 55  ? 13.310  95.482  26.927  1.00 9.35  ? 55   ALA I N   1 
ATOM   9163  C  CA  . ALA I  1 55  ? 14.494  96.168  27.459  1.00 10.91 ? 55   ALA I CA  1 
ATOM   9164  C  C   . ALA I  1 55  ? 14.665  95.792  28.920  1.00 11.18 ? 55   ALA I C   1 
ATOM   9165  O  O   . ALA I  1 55  ? 14.929  96.642  29.769  1.00 12.80 ? 55   ALA I O   1 
ATOM   9166  C  CB  . ALA I  1 55  ? 14.378  97.714  27.311  1.00 10.56 ? 55   ALA I CB  1 
ATOM   9167  N  N   . GLY I  1 56  ? 14.504  94.513  29.232  1.00 9.41  ? 56   GLY I N   1 
ATOM   9168  C  CA  . GLY I  1 56  ? 14.586  94.109  30.625  1.00 9.28  ? 56   GLY I CA  1 
ATOM   9169  C  C   . GLY I  1 56  ? 13.437  94.684  31.466  1.00 9.83  ? 56   GLY I C   1 
ATOM   9170  O  O   . GLY I  1 56  ? 12.359  95.009  30.940  1.00 9.06  ? 56   GLY I O   1 
ATOM   9171  N  N   . CYS I  1 57  ? 13.682  94.897  32.755  1.00 8.36  ? 57   CYS I N   1 
ATOM   9172  C  CA  . CYS I  1 57  ? 12.620  95.419  33.593  1.00 8.86  ? 57   CYS I CA  1 
ATOM   9173  C  C   . CYS I  1 57  ? 12.250  96.869  33.286  1.00 8.16  ? 57   CYS I C   1 
ATOM   9174  O  O   . CYS I  1 57  ? 11.176  97.303  33.647  1.00 6.30  ? 57   CYS I O   1 
ATOM   9175  C  CB  . CYS I  1 57  ? 12.969  95.231  35.057  1.00 9.87  ? 57   CYS I CB  1 
ATOM   9176  S  SG  . CYS I  1 57  ? 13.224  93.479  35.433  1.00 13.25 ? 57   CYS I SG  1 
ATOM   9177  N  N   . THR I  1 58  ? 13.131  97.596  32.604  1.00 6.29  ? 58   THR I N   1 
ATOM   9178  C  CA  . THR I  1 58  ? 12.875  99.015  32.291  1.00 7.83  ? 58   THR I CA  1 
ATOM   9179  C  C   . THR I  1 58  ? 11.642  99.201  31.416  1.00 7.04  ? 58   THR I C   1 
ATOM   9180  O  O   . THR I  1 58  ? 10.870  100.158 31.605  1.00 7.32  ? 58   THR I O   1 
ATOM   9181  C  CB  . THR I  1 58  ? 14.145  99.608  31.628  1.00 9.05  ? 58   THR I CB  1 
ATOM   9182  O  OG1 . THR I  1 58  ? 15.201  99.550  32.590  1.00 12.58 ? 58   THR I OG1 1 
ATOM   9183  C  CG2 . THR I  1 58  ? 14.016  101.112 31.304  1.00 10.73 ? 58   THR I CG2 1 
ATOM   9184  N  N   . SER I  1 59  ? 11.424  98.290  30.472  1.00 6.48  ? 59   SER I N   1 
ATOM   9185  C  CA  . SER I  1 59  ? 10.292  98.421  29.580  1.00 6.10  ? 59   SER I CA  1 
ATOM   9186  C  C   . SER I  1 59  ? 8.944   98.101  30.203  1.00 6.12  ? 59   SER I C   1 
ATOM   9187  O  O   . SER I  1 59  ? 7.922   98.266  29.538  1.00 6.42  ? 59   SER I O   1 
ATOM   9188  C  CB  . SER I  1 59  ? 10.536  97.679  28.245  1.00 7.73  ? 59   SER I CB  1 
ATOM   9189  O  OG  . SER I  1 59  ? 11.082  96.413  28.514  1.00 10.26 ? 59   SER I OG  1 
ATOM   9190  N  N   . ALA I  1 60  ? 8.933   97.677  31.479  1.00 5.00  ? 60   ALA I N   1 
ATOM   9191  C  CA  . ALA I  1 60  ? 7.665   97.449  32.172  1.00 5.44  ? 60   ALA I CA  1 
ATOM   9192  C  C   . ALA I  1 60  ? 6.951   98.746  32.479  1.00 5.22  ? 60   ALA I C   1 
ATOM   9193  O  O   . ALA I  1 60  ? 5.791   98.728  32.899  1.00 5.00  ? 60   ALA I O   1 
ATOM   9194  C  CB  . ALA I  1 60  ? 7.849   96.645  33.480  1.00 5.00  ? 60   ALA I CB  1 
ATOM   9195  N  N   . GLY I  1 61  ? 7.643   99.870  32.328  1.00 6.15  ? 61   GLY I N   1 
ATOM   9196  C  CA  . GLY I  1 61  ? 6.993   101.133 32.618  1.00 5.70  ? 61   GLY I CA  1 
ATOM   9197  C  C   . GLY I  1 61  ? 6.783   101.390 34.123  1.00 6.17  ? 61   GLY I C   1 
ATOM   9198  O  O   . GLY I  1 61  ? 7.419   100.765 34.979  1.00 5.58  ? 61   GLY I O   1 
ATOM   9199  N  N   . PRO I  1 62  ? 5.887   102.314 34.439  1.00 6.20  ? 62   PRO I N   1 
ATOM   9200  C  CA  . PRO I  1 62  ? 5.679   102.741 35.831  1.00 6.65  ? 62   PRO I CA  1 
ATOM   9201  C  C   . PRO I  1 62  ? 4.680   101.814 36.535  1.00 6.53  ? 62   PRO I C   1 
ATOM   9202  O  O   . PRO I  1 62  ? 4.268   100.805 35.954  1.00 6.00  ? 62   PRO I O   1 
ATOM   9203  C  CB  . PRO I  1 62  ? 5.092   104.131 35.672  1.00 8.33  ? 62   PRO I CB  1 
ATOM   9204  C  CG  . PRO I  1 62  ? 4.192   103.979 34.433  1.00 7.79  ? 62   PRO I CG  1 
ATOM   9205  C  CD  . PRO I  1 62  ? 4.989   103.030 33.504  1.00 7.67  ? 62   PRO I CD  1 
ATOM   9206  N  N   . HIS I  1 63  ? 4.302   102.148 37.767  1.00 5.85  ? 63   HIS I N   1 
ATOM   9207  C  CA  . HIS I  1 63  ? 3.363   101.289 38.503  1.00 6.53  ? 63   HIS I CA  1 
ATOM   9208  C  C   . HIS I  1 63  ? 2.015   101.271 37.828  1.00 6.31  ? 63   HIS I C   1 
ATOM   9209  O  O   . HIS I  1 63  ? 1.598   102.272 37.289  1.00 6.53  ? 63   HIS I O   1 
ATOM   9210  C  CB  . HIS I  1 63  ? 3.222   101.829 39.931  1.00 5.15  ? 63   HIS I CB  1 
ATOM   9211  C  CG  . HIS I  1 63  ? 4.469   101.695 40.730  1.00 7.50  ? 63   HIS I CG  1 
ATOM   9212  N  ND1 . HIS I  1 63  ? 4.556   102.103 42.041  1.00 5.52  ? 63   HIS I ND1 1 
ATOM   9213  C  CD2 . HIS I  1 63  ? 5.672   101.150 40.422  1.00 7.52  ? 63   HIS I CD2 1 
ATOM   9214  C  CE1 . HIS I  1 63  ? 5.763   101.817 42.508  1.00 7.35  ? 63   HIS I CE1 1 
ATOM   9215  N  NE2 . HIS I  1 63  ? 6.464   101.252 41.541  1.00 11.31 ? 63   HIS I NE2 1 
ATOM   9216  N  N   . PHE I  1 64  ? 1.343   100.127 37.821  1.00 5.14  ? 64   PHE I N   1 
ATOM   9217  C  CA  . PHE I  1 64  ? 0.040   100.025 37.207  1.00 5.68  ? 64   PHE I CA  1 
ATOM   9218  C  C   . PHE I  1 64  ? -0.876  100.960 38.009  1.00 6.54  ? 64   PHE I C   1 
ATOM   9219  O  O   . PHE I  1 64  ? -1.001  100.790 39.190  1.00 5.48  ? 64   PHE I O   1 
ATOM   9220  C  CB  . PHE I  1 64  ? -0.398  98.588  37.323  1.00 6.67  ? 64   PHE I CB  1 
ATOM   9221  C  CG  . PHE I  1 64  ? -1.746  98.313  36.769  1.00 5.96  ? 64   PHE I CG  1 
ATOM   9222  C  CD1 . PHE I  1 64  ? -2.185  98.928  35.593  1.00 7.32  ? 64   PHE I CD1 1 
ATOM   9223  C  CD2 . PHE I  1 64  ? -2.609  97.465  37.468  1.00 7.18  ? 64   PHE I CD2 1 
ATOM   9224  C  CE1 . PHE I  1 64  ? -3.464  98.661  35.098  1.00 6.89  ? 64   PHE I CE1 1 
ATOM   9225  C  CE2 . PHE I  1 64  ? -3.883  97.202  36.980  1.00 7.35  ? 64   PHE I CE2 1 
ATOM   9226  C  CZ  . PHE I  1 64  ? -4.304  97.797  35.794  1.00 6.44  ? 64   PHE I CZ  1 
ATOM   9227  N  N   . ASN I  1 65  ? -1.497  101.931 37.351  1.00 6.66  ? 65   ASN I N   1 
ATOM   9228  C  CA  . ASN I  1 65  ? -2.186  103.014 38.070  1.00 8.53  ? 65   ASN I CA  1 
ATOM   9229  C  C   . ASN I  1 65  ? -3.393  103.496 37.279  1.00 9.65  ? 65   ASN I C   1 
ATOM   9230  O  O   . ASN I  1 65  ? -3.446  104.675 36.889  1.00 10.79 ? 65   ASN I O   1 
ATOM   9231  C  CB  . ASN I  1 65  ? -1.180  104.158 38.272  1.00 7.99  ? 65   ASN I CB  1 
ATOM   9232  C  CG  . ASN I  1 65  ? -1.747  105.339 39.070  1.00 9.26  ? 65   ASN I CG  1 
ATOM   9233  O  OD1 . ASN I  1 65  ? -2.682  105.182 39.844  1.00 9.16  ? 65   ASN I OD1 1 
ATOM   9234  N  ND2 . ASN I  1 65  ? -1.155  106.523 38.889  1.00 8.62  ? 65   ASN I ND2 1 
ATOM   9235  N  N   . PRO I  1 66  ? -4.355  102.608 37.028  1.00 9.69  ? 66   PRO I N   1 
ATOM   9236  C  CA  . PRO I  1 66  ? -5.500  102.955 36.171  1.00 10.81 ? 66   PRO I CA  1 
ATOM   9237  C  C   . PRO I  1 66  ? -6.360  104.091 36.759  1.00 11.59 ? 66   PRO I C   1 
ATOM   9238  O  O   . PRO I  1 66  ? -7.035  104.802 36.018  1.00 11.41 ? 66   PRO I O   1 
ATOM   9239  C  CB  . PRO I  1 66  ? -6.297  101.654 36.115  1.00 10.61 ? 66   PRO I CB  1 
ATOM   9240  C  CG  . PRO I  1 66  ? -5.925  100.955 37.417  1.00 10.93 ? 66   PRO I CG  1 
ATOM   9241  C  CD  . PRO I  1 66  ? -4.430  101.216 37.491  1.00 10.86 ? 66   PRO I CD  1 
ATOM   9242  N  N   . LEU I  1 67  ? -6.304  104.272 38.062  1.00 11.93 ? 67   LEU I N   1 
ATOM   9243  C  CA  . LEU I  1 67  ? -7.109  105.339 38.691  1.00 13.45 ? 67   LEU I CA  1 
ATOM   9244  C  C   . LEU I  1 67  ? -6.354  106.649 38.887  1.00 13.85 ? 67   LEU I C   1 
ATOM   9245  O  O   . LEU I  1 67  ? -6.853  107.575 39.535  1.00 13.72 ? 67   LEU I O   1 
ATOM   9246  C  CB  . LEU I  1 67  ? -7.680  104.843 40.011  1.00 13.80 ? 67   LEU I CB  1 
ATOM   9247  C  CG  . LEU I  1 67  ? -8.685  103.708 39.855  1.00 16.63 ? 67   LEU I CG  1 
ATOM   9248  C  CD1 . LEU I  1 67  ? -9.143  103.227 41.239  1.00 19.39 ? 67   LEU I CD1 1 
ATOM   9249  C  CD2 . LEU I  1 67  ? -9.862  104.232 39.068  1.00 19.60 ? 67   LEU I CD2 1 
ATOM   9250  N  N   . SER I  1 68  ? -5.150  106.733 38.324  1.00 14.41 ? 68   SER I N   1 
ATOM   9251  C  CA  . SER I  1 68  ? -4.334  107.942 38.406  1.00 14.78 ? 68   SER I CA  1 
ATOM   9252  C  C   . SER I  1 68  ? -4.213  108.513 39.817  1.00 14.62 ? 68   SER I C   1 
ATOM   9253  O  O   . SER I  1 68  ? -4.531  109.695 40.048  1.00 14.48 ? 68   SER I O   1 
ATOM   9254  C  CB  . SER I  1 68  ? -4.867  109.048 37.468  1.00 15.06 ? 68   SER I CB  1 
ATOM   9255  O  OG  . SER I  1 68  ? -5.124  108.549 36.156  1.00 16.57 ? 68   SER I OG  1 
ATOM   9256  N  N   . ARG I  1 69  ? -3.765  107.689 40.762  1.00 13.74 ? 69   ARG I N   1 
ATOM   9257  C  CA  . ARG I  1 69  ? -3.499  108.163 42.104  1.00 13.59 ? 69   ARG I CA  1 
ATOM   9258  C  C   . ARG I  1 69  ? -2.013  108.264 42.352  1.00 13.03 ? 69   ARG I C   1 
ATOM   9259  O  O   . ARG I  1 69  ? -1.196  107.955 41.476  1.00 11.95 ? 69   ARG I O   1 
ATOM   9260  C  CB  . ARG I  1 69  ? -4.104  107.228 43.134  1.00 14.55 ? 69   ARG I CB  1 
ATOM   9261  C  CG  . ARG I  1 69  ? -5.493  106.793 42.750  1.00 17.83 ? 69   ARG I CG  1 
ATOM   9262  C  CD  . ARG I  1 69  ? -6.455  106.807 43.879  1.00 23.20 ? 69   ARG I CD  1 
ATOM   9263  N  NE  . ARG I  1 69  ? -7.838  106.747 43.423  1.00 27.30 ? 69   ARG I NE  1 
ATOM   9264  C  CZ  . ARG I  1 69  ? -8.820  106.186 44.127  1.00 29.81 ? 69   ARG I CZ  1 
ATOM   9265  N  NH1 . ARG I  1 69  ? -8.556  105.634 45.310  1.00 28.02 ? 69   ARG I NH1 1 
ATOM   9266  N  NH2 . ARG I  1 69  ? -10.062 106.174 43.644  1.00 31.54 ? 69   ARG I NH2 1 
ATOM   9267  N  N   . LYS I  1 70  ? -1.670  108.690 43.556  1.00 12.05 ? 70   LYS I N   1 
ATOM   9268  C  CA  . LYS I  1 70  ? -0.276  108.747 43.953  1.00 11.31 ? 70   LYS I CA  1 
ATOM   9269  C  C   . LYS I  1 70  ? 0.083   107.423 44.594  1.00 9.52  ? 70   LYS I C   1 
ATOM   9270  O  O   . LYS I  1 70  ? -0.774  106.658 45.022  1.00 9.20  ? 70   LYS I O   1 
ATOM   9271  C  CB  . LYS I  1 70  ? -0.033  109.879 44.958  1.00 12.92 ? 70   LYS I CB  1 
ATOM   9272  C  CG  . LYS I  1 70  ? -0.237  111.277 44.339  1.00 16.73 ? 70   LYS I CG  1 
ATOM   9273  C  CD  . LYS I  1 70  ? 0.706   112.266 45.005  1.00 25.16 ? 70   LYS I CD  1 
ATOM   9274  C  CE  . LYS I  1 70  ? 0.014   113.578 45.360  1.00 28.95 ? 70   LYS I CE  1 
ATOM   9275  N  NZ  . LYS I  1 70  ? 0.715   114.325 46.479  1.00 30.76 ? 70   LYS I NZ  1 
ATOM   9276  N  N   . HIS I  1 71  ? 1.376   107.174 44.657  1.00 8.84  ? 71   HIS I N   1 
ATOM   9277  C  CA  . HIS I  1 71  ? 1.907   105.970 45.243  1.00 8.22  ? 71   HIS I CA  1 
ATOM   9278  C  C   . HIS I  1 71  ? 1.648   105.872 46.746  1.00 8.54  ? 71   HIS I C   1 
ATOM   9279  O  O   . HIS I  1 71  ? 1.668   106.880 47.474  1.00 8.48  ? 71   HIS I O   1 
ATOM   9280  C  CB  . HIS I  1 71  ? 3.408   105.922 44.951  1.00 8.73  ? 71   HIS I CB  1 
ATOM   9281  C  CG  . HIS I  1 71  ? 4.095   104.730 45.540  1.00 8.59  ? 71   HIS I CG  1 
ATOM   9282  N  ND1 . HIS I  1 71  ? 4.153   103.511 44.897  1.00 6.71  ? 71   HIS I ND1 1 
ATOM   9283  C  CD2 . HIS I  1 71  ? 4.740   104.570 46.720  1.00 6.99  ? 71   HIS I CD2 1 
ATOM   9284  C  CE1 . HIS I  1 71  ? 4.792   102.646 45.666  1.00 6.77  ? 71   HIS I CE1 1 
ATOM   9285  N  NE2 . HIS I  1 71  ? 5.174   103.266 46.773  1.00 6.15  ? 71   HIS I NE2 1 
ATOM   9286  N  N   . GLY I  1 72  ? 1.412   104.660 47.230  1.00 8.08  ? 72   GLY I N   1 
ATOM   9287  C  CA  . GLY I  1 72  ? 1.293   104.463 48.658  1.00 8.05  ? 72   GLY I CA  1 
ATOM   9288  C  C   . GLY I  1 72  ? 1.595   103.027 49.004  1.00 8.82  ? 72   GLY I C   1 
ATOM   9289  O  O   . GLY I  1 72  ? 2.155   102.260 48.179  1.00 7.31  ? 72   GLY I O   1 
ATOM   9290  N  N   . GLY I  1 73  ? 1.242   102.663 50.225  1.00 8.36  ? 73   GLY I N   1 
ATOM   9291  C  CA  . GLY I  1 73  ? 1.376   101.291 50.676  1.00 9.30  ? 73   GLY I CA  1 
ATOM   9292  C  C   . GLY I  1 73  ? 0.072   100.562 50.354  1.00 8.88  ? 73   GLY I C   1 
ATOM   9293  O  O   . GLY I  1 73  ? -0.909  101.194 50.067  1.00 8.72  ? 73   GLY I O   1 
ATOM   9294  N  N   . PRO I  1 74  ? 0.067   99.245  50.399  1.00 9.43  ? 74   PRO I N   1 
ATOM   9295  C  CA  . PRO I  1 74  ? -1.138  98.474  50.073  1.00 10.24 ? 74   PRO I CA  1 
ATOM   9296  C  C   . PRO I  1 74  ? -2.336  98.796  50.976  1.00 11.35 ? 74   PRO I C   1 
ATOM   9297  O  O   . PRO I  1 74  ? -3.485  98.697  50.533  1.00 10.03 ? 74   PRO I O   1 
ATOM   9298  C  CB  . PRO I  1 74  ? -0.734  97.013  50.317  1.00 11.06 ? 74   PRO I CB  1 
ATOM   9299  C  CG  . PRO I  1 74  ? 0.690   97.024  50.775  1.00 10.74 ? 74   PRO I CG  1 
ATOM   9300  C  CD  . PRO I  1 74  ? 1.235   98.411  50.714  1.00 10.12 ? 74   PRO I CD  1 
ATOM   9301  N  N   . LYS I  1 75  ? -2.061  99.152  52.224  1.00 12.59 ? 75   LYS I N   1 
ATOM   9302  C  CA  . LYS I  1 75  ? -3.120  99.511  53.163  1.00 14.62 ? 75   LYS I CA  1 
ATOM   9303  C  C   . LYS I  1 75  ? -3.694  100.905 52.976  1.00 14.77 ? 75   LYS I C   1 
ATOM   9304  O  O   . LYS I  1 75  ? -4.725  101.229 53.570  1.00 15.47 ? 75   LYS I O   1 
ATOM   9305  C  CB  . LYS I  1 75  ? -2.614  99.368  54.593  1.00 15.29 ? 75   LYS I CB  1 
ATOM   9306  C  CG  . LYS I  1 75  ? -2.199  97.955  54.938  1.00 18.48 ? 75   LYS I CG  1 
ATOM   9307  C  CD  . LYS I  1 75  ? -3.377  96.977  54.778  1.00 26.60 ? 75   LYS I CD  1 
ATOM   9308  C  CE  . LYS I  1 75  ? -2.910  95.516  54.548  1.00 31.06 ? 75   LYS I CE  1 
ATOM   9309  N  NZ  . LYS I  1 75  ? -2.031  94.973  55.650  1.00 31.44 ? 75   LYS I NZ  1 
ATOM   9310  N  N   . ASP I  1 76  ? -3.029  101.754 52.202  1.00 14.22 ? 76   ASP I N   1 
ATOM   9311  C  CA  . ASP I  1 76  ? -3.530  103.103 51.971  1.00 15.38 ? 76   ASP I CA  1 
ATOM   9312  C  C   . ASP I  1 76  ? -4.617  103.200 50.924  1.00 15.77 ? 76   ASP I C   1 
ATOM   9313  O  O   . ASP I  1 76  ? -4.619  102.489 49.916  1.00 14.37 ? 76   ASP I O   1 
ATOM   9314  C  CB  . ASP I  1 76  ? -2.427  104.068 51.540  1.00 14.71 ? 76   ASP I CB  1 
ATOM   9315  C  CG  . ASP I  1 76  ? -1.361  104.204 52.570  1.00 18.55 ? 76   ASP I CG  1 
ATOM   9316  O  OD1 . ASP I  1 76  ? -1.686  104.208 53.790  1.00 19.82 ? 76   ASP I OD1 1 
ATOM   9317  O  OD2 . ASP I  1 76  ? -0.164  104.293 52.255  1.00 18.89 ? 76   ASP I OD2 1 
ATOM   9318  N  N   . GLU I  1 77  ? -5.520  104.147 51.143  1.00 15.88 ? 77   GLU I N   1 
ATOM   9319  C  CA  . GLU I  1 77  ? -6.556  104.393 50.158  1.00 16.79 ? 77   GLU I CA  1 
ATOM   9320  C  C   . GLU I  1 77  ? -5.918  105.104 48.964  1.00 15.50 ? 77   GLU I C   1 
ATOM   9321  O  O   . GLU I  1 77  ? -6.256  104.823 47.803  1.00 15.70 ? 77   GLU I O   1 
ATOM   9322  C  CB  . GLU I  1 77  ? -7.700  105.200 50.792  1.00 18.45 ? 77   GLU I CB  1 
ATOM   9323  C  CG  . GLU I  1 77  ? -9.088  104.813 50.298  1.00 23.43 ? 77   GLU I CG  1 
ATOM   9324  C  CD  . GLU I  1 77  ? -9.244  105.065 48.819  1.00 30.31 ? 77   GLU I CD  1 
ATOM   9325  O  OE1 . GLU I  1 77  ? -8.796  106.155 48.382  1.00 32.54 ? 77   GLU I OE1 1 
ATOM   9326  O  OE2 . GLU I  1 77  ? -9.802  104.178 48.104  1.00 33.13 ? 77   GLU I OE2 1 
ATOM   9327  N  N   . GLU I  1 78  ? -4.977  106.012 49.228  1.00 13.19 ? 78   GLU I N   1 
ATOM   9328  C  CA  . GLU I  1 78  ? -4.269  106.676 48.148  1.00 11.56 ? 78   GLU I CA  1 
ATOM   9329  C  C   . GLU I  1 78  ? -3.087  105.756 47.761  1.00 10.71 ? 78   GLU I C   1 
ATOM   9330  O  O   . GLU I  1 78  ? -2.062  105.763 48.426  1.00 9.17  ? 78   GLU I O   1 
ATOM   9331  C  CB  . GLU I  1 78  ? -3.749  108.056 48.567  1.00 12.52 ? 78   GLU I CB  1 
ATOM   9332  C  CG  . GLU I  1 78  ? -3.077  108.858 47.443  1.00 15.09 ? 78   GLU I CG  1 
ATOM   9333  C  CD  . GLU I  1 78  ? -4.057  109.378 46.387  1.00 21.34 ? 78   GLU I CD  1 
ATOM   9334  O  OE1 . GLU I  1 78  ? -5.293  109.208 46.575  1.00 25.97 ? 78   GLU I OE1 1 
ATOM   9335  O  OE2 . GLU I  1 78  ? -3.611  109.964 45.364  1.00 18.39 ? 78   GLU I OE2 1 
ATOM   9336  N  N   . ARG I  1 79  ? -3.266  104.942 46.729  1.00 9.24  ? 79   ARG I N   1 
ATOM   9337  C  CA  . ARG I  1 79  ? -2.185  104.065 46.233  1.00 8.84  ? 79   ARG I CA  1 
ATOM   9338  C  C   . ARG I  1 79  ? -2.447  103.744 44.777  1.00 8.86  ? 79   ARG I C   1 
ATOM   9339  O  O   . ARG I  1 79  ? -3.556  103.973 44.259  1.00 8.67  ? 79   ARG I O   1 
ATOM   9340  C  CB  . ARG I  1 79  ? -2.119  102.735 46.998  1.00 9.77  ? 79   ARG I CB  1 
ATOM   9341  C  CG  . ARG I  1 79  ? -3.418  101.933 46.946  1.00 9.23  ? 79   ARG I CG  1 
ATOM   9342  C  CD  . ARG I  1 79  ? -3.368  100.534 47.502  1.00 10.75 ? 79   ARG I CD  1 
ATOM   9343  N  NE  . ARG I  1 79  ? -2.982  99.542  46.483  1.00 9.22  ? 79   ARG I NE  1 
ATOM   9344  C  CZ  . ARG I  1 79  ? -3.108  98.228  46.647  1.00 7.86  ? 79   ARG I CZ  1 
ATOM   9345  N  NH1 . ARG I  1 79  ? -3.570  97.751  47.794  1.00 5.66  ? 79   ARG I NH1 1 
ATOM   9346  N  NH2 . ARG I  1 79  ? -2.790  97.386  45.652  1.00 5.16  ? 79   ARG I NH2 1 
ATOM   9347  N  N   . HIS I  1 80  ? -1.398  103.284 44.099  1.00 8.45  ? 80   HIS I N   1 
ATOM   9348  C  CA  . HIS I  1 80  ? -1.539  102.750 42.771  1.00 7.82  ? 80   HIS I CA  1 
ATOM   9349  C  C   . HIS I  1 80  ? -2.122  101.350 42.914  1.00 7.26  ? 80   HIS I C   1 
ATOM   9350  O  O   . HIS I  1 80  ? -1.892  100.680 43.891  1.00 6.51  ? 80   HIS I O   1 
ATOM   9351  C  CB  . HIS I  1 80  ? -0.140  102.625 42.153  1.00 6.73  ? 80   HIS I CB  1 
ATOM   9352  C  CG  . HIS I  1 80  ? 0.562   103.941 41.981  1.00 6.92  ? 80   HIS I CG  1 
ATOM   9353  N  ND1 . HIS I  1 80  ? 1.933   104.071 42.050  1.00 6.71  ? 80   HIS I ND1 1 
ATOM   9354  C  CD2 . HIS I  1 80  ? 0.077   105.170 41.694  1.00 7.75  ? 80   HIS I CD2 1 
ATOM   9355  C  CE1 . HIS I  1 80  ? 2.263   105.326 41.793  1.00 9.96  ? 80   HIS I CE1 1 
ATOM   9356  N  NE2 . HIS I  1 80  ? 1.157   106.019 41.591  1.00 8.41  ? 80   HIS I NE2 1 
ATOM   9357  N  N   . VAL I  1 81  ? -2.861  100.893 41.915  1.00 6.93  ? 81   VAL I N   1 
ATOM   9358  C  CA  . VAL I  1 81  ? -3.310  99.516  41.962  1.00 6.54  ? 81   VAL I CA  1 
ATOM   9359  C  C   . VAL I  1 81  ? -2.142  98.544  42.131  1.00 5.37  ? 81   VAL I C   1 
ATOM   9360  O  O   . VAL I  1 81  ? -2.244  97.566  42.851  1.00 6.39  ? 81   VAL I O   1 
ATOM   9361  C  CB  . VAL I  1 81  ? -4.130  99.136  40.709  1.00 6.04  ? 81   VAL I CB  1 
ATOM   9362  C  CG1 . VAL I  1 81  ? -4.335  97.622  40.678  1.00 6.70  ? 81   VAL I CG1 1 
ATOM   9363  C  CG2 . VAL I  1 81  ? -5.526  99.854  40.747  1.00 8.21  ? 81   VAL I CG2 1 
ATOM   9364  N  N   . GLY I  1 82  ? -1.001  98.837  41.527  1.00 5.98  ? 82   GLY I N   1 
ATOM   9365  C  CA  . GLY I  1 82  ? 0.118   97.899  41.598  1.00 5.37  ? 82   GLY I CA  1 
ATOM   9366  C  C   . GLY I  1 82  ? 0.952   97.967  42.854  1.00 5.75  ? 82   GLY I C   1 
ATOM   9367  O  O   . GLY I  1 82  ? 1.947   97.272  42.943  1.00 5.34  ? 82   GLY I O   1 
ATOM   9368  N  N   . ASP I  1 83  ? 0.535   98.783  43.835  1.00 5.00  ? 83   ASP I N   1 
ATOM   9369  C  CA  . ASP I  1 83  ? 1.311   98.965  45.072  1.00 6.73  ? 83   ASP I CA  1 
ATOM   9370  C  C   . ASP I  1 83  ? 1.135   97.842  46.103  1.00 6.21  ? 83   ASP I C   1 
ATOM   9371  O  O   . ASP I  1 83  ? 0.264   97.904  46.962  1.00 6.88  ? 83   ASP I O   1 
ATOM   9372  C  CB  . ASP I  1 83  ? 0.977   100.314 45.725  1.00 5.00  ? 83   ASP I CB  1 
ATOM   9373  C  CG  . ASP I  1 83  ? 1.494   101.466 44.940  1.00 8.34  ? 83   ASP I CG  1 
ATOM   9374  O  OD1 . ASP I  1 83  ? 2.304   101.236 43.986  1.00 6.44  ? 83   ASP I OD1 1 
ATOM   9375  O  OD2 . ASP I  1 83  ? 1.121   102.641 45.147  1.00 7.25  ? 83   ASP I OD2 1 
ATOM   9376  N  N   . LEU I  1 84  ? 1.992   96.832  46.029  1.00 5.69  ? 84   LEU I N   1 
ATOM   9377  C  CA  . LEU I  1 84  ? 1.925   95.712  46.939  1.00 6.99  ? 84   LEU I CA  1 
ATOM   9378  C  C   . LEU I  1 84  ? 2.910   95.822  48.114  1.00 7.55  ? 84   LEU I C   1 
ATOM   9379  O  O   . LEU I  1 84  ? 3.199   94.835  48.800  1.00 8.40  ? 84   LEU I O   1 
ATOM   9380  C  CB  . LEU I  1 84  ? 2.091   94.366  46.203  1.00 6.36  ? 84   LEU I CB  1 
ATOM   9381  C  CG  . LEU I  1 84  ? 1.010   94.096  45.158  1.00 9.09  ? 84   LEU I CG  1 
ATOM   9382  C  CD1 . LEU I  1 84  ? 1.333   92.759  44.443  1.00 7.17  ? 84   LEU I CD1 1 
ATOM   9383  C  CD2 . LEU I  1 84  ? -0.425  94.025  45.753  1.00 13.17 ? 84   LEU I CD2 1 
ATOM   9384  N  N   . GLY I  1 85  ? 3.472   97.006  48.329  1.00 6.87  ? 85   GLY I N   1 
ATOM   9385  C  CA  . GLY I  1 85  ? 4.277   97.191  49.521  1.00 7.90  ? 85   GLY I CA  1 
ATOM   9386  C  C   . GLY I  1 85  ? 5.662   96.602  49.393  1.00 7.16  ? 85   GLY I C   1 
ATOM   9387  O  O   . GLY I  1 85  ? 6.328   96.757  48.353  1.00 7.11  ? 85   GLY I O   1 
ATOM   9388  N  N   . ASN I  1 86  ? 6.134   95.975  50.466  1.00 6.58  ? 86   ASN I N   1 
ATOM   9389  C  CA  . ASN I  1 86  ? 7.461   95.382  50.461  1.00 6.57  ? 86   ASN I CA  1 
ATOM   9390  C  C   . ASN I  1 86  ? 7.436   93.895  50.727  1.00 7.31  ? 86   ASN I C   1 
ATOM   9391  O  O   . ASN I  1 86  ? 6.502   93.388  51.338  1.00 6.04  ? 86   ASN I O   1 
ATOM   9392  C  CB  . ASN I  1 86  ? 8.265   95.965  51.632  1.00 6.07  ? 86   ASN I CB  1 
ATOM   9393  C  CG  . ASN I  1 86  ? 8.668   97.402  51.380  1.00 7.74  ? 86   ASN I CG  1 
ATOM   9394  O  OD1 . ASN I  1 86  ? 9.434   97.647  50.480  1.00 7.33  ? 86   ASN I OD1 1 
ATOM   9395  N  ND2 . ASN I  1 86  ? 8.109   98.354  52.155  1.00 6.16  ? 86   ASN I ND2 1 
ATOM   9396  N  N   . VAL I  1 87  ? 8.493   93.206  50.309  1.00 5.88  ? 87   VAL I N   1 
ATOM   9397  C  CA  . VAL I  1 87  ? 8.669   91.852  50.788  1.00 6.52  ? 87   VAL I CA  1 
ATOM   9398  C  C   . VAL I  1 87  ? 9.936   91.895  51.637  1.00 7.03  ? 87   VAL I C   1 
ATOM   9399  O  O   . VAL I  1 87  ? 10.723  92.865  51.559  1.00 8.48  ? 87   VAL I O   1 
ATOM   9400  C  CB  . VAL I  1 87  ? 8.802   90.855  49.655  1.00 6.09  ? 87   VAL I CB  1 
ATOM   9401  C  CG1 . VAL I  1 87  ? 7.440   90.741  48.953  1.00 7.46  ? 87   VAL I CG1 1 
ATOM   9402  C  CG2 . VAL I  1 87  ? 9.962   91.269  48.718  1.00 7.30  ? 87   VAL I CG2 1 
ATOM   9403  N  N   . THR I  1 88  ? 10.135  90.877  52.465  1.00 6.59  ? 88   THR I N   1 
ATOM   9404  C  CA  . THR I  1 88  ? 11.251  90.907  53.414  1.00 6.76  ? 88   THR I CA  1 
ATOM   9405  C  C   . THR I  1 88  ? 12.212  89.722  53.190  1.00 6.22  ? 88   THR I C   1 
ATOM   9406  O  O   . THR I  1 88  ? 11.794  88.583  53.271  1.00 6.98  ? 88   THR I O   1 
ATOM   9407  C  CB  . THR I  1 88  ? 10.713  90.790  54.873  1.00 9.31  ? 88   THR I CB  1 
ATOM   9408  O  OG1 . THR I  1 88  ? 9.760   91.830  55.156  1.00 10.45 ? 88   THR I OG1 1 
ATOM   9409  C  CG2 . THR I  1 88  ? 11.851  91.038  55.843  1.00 9.31  ? 88   THR I CG2 1 
ATOM   9410  N  N   . ALA I  1 89  ? 13.470  89.972  52.850  1.00 6.05  ? 89   ALA I N   1 
ATOM   9411  C  CA  . ALA I  1 89  ? 14.418  88.876  52.650  1.00 6.06  ? 89   ALA I CA  1 
ATOM   9412  C  C   . ALA I  1 89  ? 15.123  88.627  53.978  1.00 8.50  ? 89   ALA I C   1 
ATOM   9413  O  O   . ALA I  1 89  ? 15.484  89.587  54.675  1.00 6.73  ? 89   ALA I O   1 
ATOM   9414  C  CB  . ALA I  1 89  ? 15.492  89.225  51.581  1.00 6.65  ? 89   ALA I CB  1 
ATOM   9415  N  N   . ASP I  1 90  ? 15.344  87.346  54.274  1.00 8.91  ? 90   ASP I N   1 
ATOM   9416  C  CA  . ASP I  1 90  ? 16.055  86.945  55.486  1.00 11.19 ? 90   ASP I CA  1 
ATOM   9417  C  C   . ASP I  1 90  ? 17.550  87.017  55.330  1.00 11.55 ? 90   ASP I C   1 
ATOM   9418  O  O   . ASP I  1 90  ? 18.052  87.450  54.298  1.00 10.57 ? 90   ASP I O   1 
ATOM   9419  C  CB  . ASP I  1 90  ? 15.595  85.566  55.982  1.00 11.30 ? 90   ASP I CB  1 
ATOM   9420  C  CG  . ASP I  1 90  ? 15.926  84.456  55.043  1.00 11.71 ? 90   ASP I CG  1 
ATOM   9421  O  OD1 . ASP I  1 90  ? 16.823  84.593  54.167  1.00 11.39 ? 90   ASP I OD1 1 
ATOM   9422  O  OD2 . ASP I  1 90  ? 15.302  83.374  55.111  1.00 13.74 ? 90   ASP I OD2 1 
ATOM   9423  N  N   . LYS I  1 91  ? 18.297  86.596  56.353  1.00 12.69 ? 91   LYS I N   1 
ATOM   9424  C  CA  . LYS I  1 91  ? 19.738  86.785  56.270  1.00 13.96 ? 91   LYS I CA  1 
ATOM   9425  C  C   . LYS I  1 91  ? 20.377  85.895  55.202  1.00 13.77 ? 91   LYS I C   1 
ATOM   9426  O  O   . LYS I  1 91  ? 21.521  86.119  54.811  1.00 14.07 ? 91   LYS I O   1 
ATOM   9427  C  CB  . LYS I  1 91  ? 20.385  86.495  57.621  1.00 15.26 ? 91   LYS I CB  1 
ATOM   9428  C  CG  . LYS I  1 91  ? 19.987  85.123  58.085  1.00 18.69 ? 91   LYS I CG  1 
ATOM   9429  C  CD  . LYS I  1 91  ? 21.229  84.331  58.413  1.00 27.36 ? 91   LYS I CD  1 
ATOM   9430  C  CE  . LYS I  1 91  ? 20.955  83.294  59.467  1.00 28.52 ? 91   LYS I CE  1 
ATOM   9431  N  NZ  . LYS I  1 91  ? 22.175  82.466  59.668  1.00 33.98 ? 91   LYS I NZ  1 
ATOM   9432  N  N   . ASP I  1 92  ? 19.641  84.892  54.733  1.00 12.71 ? 92   ASP I N   1 
ATOM   9433  C  CA  . ASP I  1 92  ? 20.111  84.054  53.639  1.00 12.17 ? 92   ASP I CA  1 
ATOM   9434  C  C   . ASP I  1 92  ? 19.698  84.647  52.251  1.00 11.19 ? 92   ASP I C   1 
ATOM   9435  O  O   . ASP I  1 92  ? 20.012  84.075  51.209  1.00 10.00 ? 92   ASP I O   1 
ATOM   9436  C  CB  . ASP I  1 92  ? 19.576  82.628  53.789  1.00 13.29 ? 92   ASP I CB  1 
ATOM   9437  C  CG  . ASP I  1 92  ? 20.164  81.884  54.989  1.00 15.82 ? 92   ASP I CG  1 
ATOM   9438  O  OD1 . ASP I  1 92  ? 21.308  82.177  55.409  1.00 16.37 ? 92   ASP I OD1 1 
ATOM   9439  O  OD2 . ASP I  1 92  ? 19.560  80.937  55.548  1.00 22.78 ? 92   ASP I OD2 1 
ATOM   9440  N  N   . GLY I  1 93  ? 19.028  85.800  52.253  1.00 10.09 ? 93   GLY I N   1 
ATOM   9441  C  CA  . GLY I  1 93  ? 18.637  86.463  51.004  1.00 7.47  ? 93   GLY I CA  1 
ATOM   9442  C  C   . GLY I  1 93  ? 17.333  85.947  50.430  1.00 8.44  ? 93   GLY I C   1 
ATOM   9443  O  O   . GLY I  1 93  ? 16.999  86.220  49.253  1.00 6.60  ? 93   GLY I O   1 
ATOM   9444  N  N   . VAL I  1 94  ? 16.579  85.203  51.248  1.00 6.67  ? 94   VAL I N   1 
ATOM   9445  C  CA  . VAL I  1 94  ? 15.335  84.630  50.789  1.00 8.27  ? 94   VAL I CA  1 
ATOM   9446  C  C   . VAL I  1 94  ? 14.121  85.354  51.353  1.00 8.37  ? 94   VAL I C   1 
ATOM   9447  O  O   . VAL I  1 94  ? 13.964  85.499  52.579  1.00 7.88  ? 94   VAL I O   1 
ATOM   9448  C  CB  . VAL I  1 94  ? 15.207  83.150  51.184  1.00 8.09  ? 94   VAL I CB  1 
ATOM   9449  C  CG1 . VAL I  1 94  ? 13.835  82.577  50.704  1.00 11.22 ? 94   VAL I CG1 1 
ATOM   9450  C  CG2 . VAL I  1 94  ? 16.392  82.367  50.597  1.00 10.60 ? 94   VAL I CG2 1 
ATOM   9451  N  N   . ALA I  1 95  ? 13.250  85.784  50.454  1.00 8.33  ? 95   ALA I N   1 
ATOM   9452  C  CA  . ALA I  1 95  ? 12.002  86.352  50.879  1.00 9.24  ? 95   ALA I CA  1 
ATOM   9453  C  C   . ALA I  1 95  ? 10.879  85.376  50.664  1.00 10.15 ? 95   ALA I C   1 
ATOM   9454  O  O   . ALA I  1 95  ? 10.566  85.037  49.532  1.00 10.00 ? 95   ALA I O   1 
ATOM   9455  C  CB  . ALA I  1 95  ? 11.708  87.629  50.103  1.00 9.48  ? 95   ALA I CB  1 
ATOM   9456  N  N   . ASP I  1 96  ? 10.239  84.953  51.739  1.00 10.26 ? 96   ASP I N   1 
ATOM   9457  C  CA  . ASP I  1 96  ? 9.037   84.149  51.605  1.00 12.68 ? 96   ASP I CA  1 
ATOM   9458  C  C   . ASP I  1 96  ? 7.926   85.129  51.493  1.00 12.25 ? 96   ASP I C   1 
ATOM   9459  O  O   . ASP I  1 96  ? 7.812   86.037  52.330  1.00 15.39 ? 96   ASP I O   1 
ATOM   9460  C  CB  . ASP I  1 96  ? 8.884   83.270  52.825  1.00 13.57 ? 96   ASP I CB  1 
ATOM   9461  C  CG  . ASP I  1 96  ? 9.888   82.211  52.815  1.00 18.34 ? 96   ASP I CG  1 
ATOM   9462  O  OD1 . ASP I  1 96  ? 9.954   81.562  51.749  1.00 23.95 ? 96   ASP I OD1 1 
ATOM   9463  O  OD2 . ASP I  1 96  ? 10.711  82.003  53.736  1.00 25.69 ? 96   ASP I OD2 1 
ATOM   9464  N  N   . VAL I  1 97  ? 7.172   85.040  50.402  1.00 9.58  ? 97   VAL I N   1 
ATOM   9465  C  CA  . VAL I  1 97  ? 6.173   86.031  50.137  1.00 6.87  ? 97   VAL I CA  1 
ATOM   9466  C  C   . VAL I  1 97  ? 4.800   85.453  50.357  1.00 7.58  ? 97   VAL I C   1 
ATOM   9467  O  O   . VAL I  1 97  ? 4.501   84.344  49.888  1.00 6.08  ? 97   VAL I O   1 
ATOM   9468  C  CB  . VAL I  1 97  ? 6.264   86.532  48.658  1.00 6.92  ? 97   VAL I CB  1 
ATOM   9469  C  CG1 . VAL I  1 97  ? 5.145   87.504  48.388  1.00 7.05  ? 97   VAL I CG1 1 
ATOM   9470  C  CG2 . VAL I  1 97  ? 7.626   87.151  48.389  1.00 7.29  ? 97   VAL I CG2 1 
ATOM   9471  N  N   . SER I  1 98  ? 3.990   86.168  51.132  1.00 6.69  ? 98   SER I N   1 
ATOM   9472  C  CA  . SER I  1 98  ? 2.592   85.795  51.262  1.00 8.15  ? 98   SER I CA  1 
ATOM   9473  C  C   . SER I  1 98  ? 1.838   87.072  51.574  1.00 9.05  ? 98   SER I C   1 
ATOM   9474  O  O   . SER I  1 98  ? 1.989   87.652  52.658  1.00 9.32  ? 98   SER I O   1 
ATOM   9475  C  CB  . SER I  1 98  ? 2.363   84.755  52.356  1.00 8.28  ? 98   SER I CB  1 
ATOM   9476  O  OG  . SER I  1 98  ? 0.993   84.330  52.311  1.00 9.50  ? 98   SER I OG  1 
ATOM   9477  N  N   . ILE I  1 99  ? 1.051   87.527  50.608  1.00 8.15  ? 99   ILE I N   1 
ATOM   9478  C  CA  . ILE I  1 99  ? 0.314   88.780  50.729  1.00 9.73  ? 99   ILE I CA  1 
ATOM   9479  C  C   . ILE I  1 99  ? -1.135  88.498  50.320  1.00 9.97  ? 99   ILE I C   1 
ATOM   9480  O  O   . ILE I  1 99  ? -1.389  87.626  49.488  1.00 9.08  ? 99   ILE I O   1 
ATOM   9481  C  CB  . ILE I  1 99  ? 0.948   89.855  49.795  1.00 9.05  ? 99   ILE I CB  1 
ATOM   9482  C  CG1 . ILE I  1 99  ? 2.256   90.441  50.393  1.00 9.64  ? 99   ILE I CG1 1 
ATOM   9483  C  CG2 . ILE I  1 99  ? -0.075  91.004  49.500  1.00 10.76 ? 99   ILE I CG2 1 
ATOM   9484  C  CD1 . ILE I  1 99  ? 3.284   91.072  49.280  1.00 11.43 ? 99   ILE I CD1 1 
ATOM   9485  N  N   . GLU I  1 100 ? -2.085  89.201  50.921  1.00 9.41  ? 100  GLU I N   1 
ATOM   9486  C  CA  . GLU I  1 100 ? -3.443  89.132  50.425  1.00 10.32 ? 100  GLU I CA  1 
ATOM   9487  C  C   . GLU I  1 100 ? -3.827  90.558  50.068  1.00 10.26 ? 100  GLU I C   1 
ATOM   9488  O  O   . GLU I  1 100 ? -3.651  91.491  50.897  1.00 10.25 ? 100  GLU I O   1 
ATOM   9489  C  CB  . GLU I  1 100 ? -4.378  88.546  51.497  1.00 11.69 ? 100  GLU I CB  1 
ATOM   9490  C  CG  . GLU I  1 100 ? -5.758  88.244  50.982  1.00 17.79 ? 100  GLU I CG  1 
ATOM   9491  C  CD  . GLU I  1 100 ? -6.612  87.484  51.999  1.00 22.00 ? 100  GLU I CD  1 
ATOM   9492  O  OE1 . GLU I  1 100 ? -6.377  86.271  52.189  1.00 24.16 ? 100  GLU I OE1 1 
ATOM   9493  O  OE2 . GLU I  1 100 ? -7.493  88.128  52.592  1.00 22.26 ? 100  GLU I OE2 1 
ATOM   9494  N  N   . ASP I  1 101 ? -4.318  90.781  48.854  1.00 8.66  ? 101  ASP I N   1 
ATOM   9495  C  CA  . ASP I  1 101 ? -4.670  92.146  48.455  1.00 9.30  ? 101  ASP I CA  1 
ATOM   9496  C  C   . ASP I  1 101 ? -6.002  92.196  47.726  1.00 9.55  ? 101  ASP I C   1 
ATOM   9497  O  O   . ASP I  1 101 ? -6.278  91.367  46.858  1.00 8.92  ? 101  ASP I O   1 
ATOM   9498  C  CB  . ASP I  1 101 ? -3.575  92.749  47.542  1.00 9.16  ? 101  ASP I CB  1 
ATOM   9499  C  CG  . ASP I  1 101 ? -3.789  94.222  47.269  1.00 9.99  ? 101  ASP I CG  1 
ATOM   9500  O  OD1 . ASP I  1 101 ? -3.455  95.028  48.159  1.00 12.55 ? 101  ASP I OD1 1 
ATOM   9501  O  OD2 . ASP I  1 101 ? -4.267  94.677  46.208  1.00 8.50  ? 101  ASP I OD2 1 
ATOM   9502  N  N   . SER I  1 102 ? -6.822  93.188  48.052  1.00 8.56  ? 102  SER I N   1 
ATOM   9503  C  CA  . SER I  1 102 ? -8.126  93.235  47.409  1.00 9.83  ? 102  SER I CA  1 
ATOM   9504  C  C   . SER I  1 102 ? -8.240  94.326  46.378  1.00 9.21  ? 102  SER I C   1 
ATOM   9505  O  O   . SER I  1 102 ? -9.333  94.567  45.843  1.00 9.36  ? 102  SER I O   1 
ATOM   9506  C  CB  . SER I  1 102 ? -9.246  93.353  48.449  1.00 11.64 ? 102  SER I CB  1 
ATOM   9507  O  OG  . SER I  1 102 ? -9.258  92.188  49.245  1.00 14.60 ? 102  SER I OG  1 
ATOM   9508  N  N   . VAL I  1 103 ? -7.125  95.007  46.084  1.00 8.17  ? 103  VAL I N   1 
ATOM   9509  C  CA  . VAL I  1 103 ? -7.167  96.089  45.078  1.00 8.02  ? 103  VAL I CA  1 
ATOM   9510  C  C   . VAL I  1 103 ? -6.744  95.523  43.707  1.00 8.54  ? 103  VAL I C   1 
ATOM   9511  O  O   . VAL I  1 103 ? -7.388  95.795  42.686  1.00 7.95  ? 103  VAL I O   1 
ATOM   9512  C  CB  . VAL I  1 103 ? -6.344  97.316  45.526  1.00 8.38  ? 103  VAL I CB  1 
ATOM   9513  C  CG1 . VAL I  1 103 ? -6.147  98.310  44.409  1.00 8.38  ? 103  VAL I CG1 1 
ATOM   9514  C  CG2 . VAL I  1 103 ? -7.065  97.995  46.774  1.00 8.68  ? 103  VAL I CG2 1 
ATOM   9515  N  N   . ILE I  1 104 ? -5.657  94.756  43.674  1.00 8.04  ? 104  ILE I N   1 
ATOM   9516  C  CA  . ILE I  1 104 ? -5.349  94.068  42.403  1.00 7.17  ? 104  ILE I CA  1 
ATOM   9517  C  C   . ILE I  1 104 ? -6.454  93.047  42.158  1.00 7.58  ? 104  ILE I C   1 
ATOM   9518  O  O   . ILE I  1 104 ? -7.236  92.726  43.076  1.00 6.52  ? 104  ILE I O   1 
ATOM   9519  C  CB  . ILE I  1 104 ? -3.996  93.349  42.453  1.00 7.52  ? 104  ILE I CB  1 
ATOM   9520  C  CG1 . ILE I  1 104 ? -3.944  92.379  43.648  1.00 7.88  ? 104  ILE I CG1 1 
ATOM   9521  C  CG2 . ILE I  1 104 ? -2.870  94.351  42.521  1.00 6.36  ? 104  ILE I CG2 1 
ATOM   9522  C  CD1 . ILE I  1 104 ? -2.835  91.320  43.542  1.00 7.91  ? 104  ILE I CD1 1 
ATOM   9523  N  N   . SER I  1 105 ? -6.511  92.515  40.932  1.00 6.64  ? 105  SER I N   1 
ATOM   9524  C  CA  . SER I  1 105 ? -7.509  91.511  40.590  1.00 6.64  ? 105  SER I CA  1 
ATOM   9525  C  C   . SER I  1 105 ? -7.027  90.725  39.365  1.00 6.86  ? 105  SER I C   1 
ATOM   9526  O  O   . SER I  1 105 ? -6.134  91.168  38.619  1.00 6.36  ? 105  SER I O   1 
ATOM   9527  C  CB  . SER I  1 105 ? -8.875  92.173  40.273  1.00 8.01  ? 105  SER I CB  1 
ATOM   9528  O  OG  . SER I  1 105 ? -9.880  91.190  40.039  1.00 8.66  ? 105  SER I OG  1 
ATOM   9529  N  N   . LEU I  1 106 ? -7.617  89.560  39.162  1.00 6.00  ? 106  LEU I N   1 
ATOM   9530  C  CA  . LEU I  1 106 ? -7.304  88.739  38.015  1.00 7.93  ? 106  LEU I CA  1 
ATOM   9531  C  C   . LEU I  1 106 ? -8.433  88.885  36.977  1.00 9.04  ? 106  LEU I C   1 
ATOM   9532  O  O   . LEU I  1 106 ? -8.505  88.103  36.039  1.00 10.65 ? 106  LEU I O   1 
ATOM   9533  C  CB  . LEU I  1 106 ? -7.047  87.282  38.420  1.00 7.25  ? 106  LEU I CB  1 
ATOM   9534  C  CG  . LEU I  1 106 ? -5.914  87.109  39.434  1.00 7.46  ? 106  LEU I CG  1 
ATOM   9535  C  CD1 . LEU I  1 106 ? -5.661  85.632  39.770  1.00 10.48 ? 106  LEU I CD1 1 
ATOM   9536  C  CD2 . LEU I  1 106 ? -4.612  87.729  38.926  1.00 9.23  ? 106  LEU I CD2 1 
ATOM   9537  N  N   . SER I  1 107 ? -9.248  89.934  37.134  1.00 9.99  ? 107  SER I N   1 
ATOM   9538  C  CA  . SER I  1 107 ? -10.308 90.349  36.160  1.00 11.75 ? 107  SER I CA  1 
ATOM   9539  C  C   . SER I  1 107 ? -10.651 91.837  36.341  1.00 12.26 ? 107  SER I C   1 
ATOM   9540  O  O   . SER I  1 107 ? -10.201 92.461  37.297  1.00 12.66 ? 107  SER I O   1 
ATOM   9541  C  CB  . SER I  1 107 ? -11.607 89.539  36.350  1.00 12.24 ? 107  SER I CB  1 
ATOM   9542  O  OG  . SER I  1 107 ? -12.281 89.901  37.562  1.00 12.79 ? 107  SER I OG  1 
ATOM   9543  N  N   . GLY I  1 108 ? -11.436 92.426  35.437  1.00 13.03 ? 108  GLY I N   1 
ATOM   9544  C  CA  . GLY I  1 108 ? -11.882 93.813  35.622  1.00 14.31 ? 108  GLY I CA  1 
ATOM   9545  C  C   . GLY I  1 108 ? -10.890 94.920  35.272  1.00 15.10 ? 108  GLY I C   1 
ATOM   9546  O  O   . GLY I  1 108 ? -9.852  94.660  34.674  1.00 14.38 ? 108  GLY I O   1 
ATOM   9547  N  N   . ASP I  1 109 ? -11.188 96.161  35.644  1.00 16.00 ? 109  ASP I N   1 
ATOM   9548  C  CA  . ASP I  1 109 ? -10.281 97.259  35.269  1.00 18.19 ? 109  ASP I CA  1 
ATOM   9549  C  C   . ASP I  1 109 ? -9.010  97.275  36.124  1.00 17.82 ? 109  ASP I C   1 
ATOM   9550  O  O   . ASP I  1 109 ? -8.039  97.996  35.830  1.00 19.10 ? 109  ASP I O   1 
ATOM   9551  C  CB  . ASP I  1 109 ? -10.992 98.637  35.252  1.00 19.53 ? 109  ASP I CB  1 
ATOM   9552  C  CG  . ASP I  1 109 ? -10.265 99.676  34.356  1.00 25.06 ? 109  ASP I CG  1 
ATOM   9553  O  OD1 . ASP I  1 109 ? -10.187 100.874 34.748  1.00 30.70 ? 109  ASP I OD1 1 
ATOM   9554  O  OD2 . ASP I  1 109 ? -9.732  99.399  33.246  1.00 30.90 ? 109  ASP I OD2 1 
ATOM   9555  N  N   . HIS I  1 110 ? -8.991  96.473  37.180  1.00 16.11 ? 110  HIS I N   1 
ATOM   9556  C  CA  . HIS I  1 110 ? -7.769  96.359  37.977  1.00 14.25 ? 110  HIS I CA  1 
ATOM   9557  C  C   . HIS I  1 110 ? -6.969  95.076  37.635  1.00 12.36 ? 110  HIS I C   1 
ATOM   9558  O  O   . HIS I  1 110 ? -6.085  94.673  38.398  1.00 11.31 ? 110  HIS I O   1 
ATOM   9559  C  CB  . HIS I  1 110 ? -8.120  96.390  39.466  1.00 14.64 ? 110  HIS I CB  1 
ATOM   9560  C  CG  . HIS I  1 110 ? -8.653  97.712  39.928  1.00 17.32 ? 110  HIS I CG  1 
ATOM   9561  N  ND1 . HIS I  1 110 ? -8.742  98.057  41.259  1.00 19.41 ? 110  HIS I ND1 1 
ATOM   9562  C  CD2 . HIS I  1 110 ? -9.082  98.789  39.228  1.00 18.85 ? 110  HIS I CD2 1 
ATOM   9563  C  CE1 . HIS I  1 110 ? -9.230  99.281  41.357  1.00 21.63 ? 110  HIS I CE1 1 
ATOM   9564  N  NE2 . HIS I  1 110 ? -9.432  99.750  40.140  1.00 19.84 ? 110  HIS I NE2 1 
ATOM   9565  N  N   . CYS I  1 111 ? -7.288  94.452  36.515  1.00 10.52 ? 111  CYS I N   1 
ATOM   9566  C  CA  . CYS I  1 111 ? -6.692  93.163  36.146  1.00 10.16 ? 111  CYS I CA  1 
ATOM   9567  C  C   . CYS I  1 111 ? -5.188  93.278  35.881  1.00 8.78  ? 111  CYS I C   1 
ATOM   9568  O  O   . CYS I  1 111 ? -4.760  94.201  35.167  1.00 8.00  ? 111  CYS I O   1 
ATOM   9569  C  CB  . CYS I  1 111 ? -7.398  92.608  34.927  1.00 11.28 ? 111  CYS I CB  1 
ATOM   9570  S  SG  . CYS I  1 111 ? -6.883  90.909  34.546  1.00 18.40 ? 111  CYS I SG  1 
ATOM   9571  N  N   . ILE I  1 112 ? -4.407  92.376  36.485  1.00 7.17  ? 112  ILE I N   1 
ATOM   9572  C  CA  . ILE I  1 112 ? -2.947  92.414  36.387  1.00 5.99  ? 112  ILE I CA  1 
ATOM   9573  C  C   . ILE I  1 112 ? -2.358  91.343  35.455  1.00 6.28  ? 112  ILE I C   1 
ATOM   9574  O  O   . ILE I  1 112 ? -1.137  91.310  35.258  1.00 6.09  ? 112  ILE I O   1 
ATOM   9575  C  CB  . ILE I  1 112 ? -2.287  92.329  37.767  1.00 5.58  ? 112  ILE I CB  1 
ATOM   9576  C  CG1 . ILE I  1 112 ? -2.583  90.972  38.429  1.00 6.41  ? 112  ILE I CG1 1 
ATOM   9577  C  CG2 . ILE I  1 112 ? -2.803  93.529  38.633  1.00 6.67  ? 112  ILE I CG2 1 
ATOM   9578  C  CD1 . ILE I  1 112 ? -1.803  90.763  39.717  1.00 6.20  ? 112  ILE I CD1 1 
ATOM   9579  N  N   . ILE I  1 113 ? -3.206  90.527  34.844  1.00 5.77  ? 113  ILE I N   1 
ATOM   9580  C  CA  . ILE I  1 113 ? -2.696  89.507  33.893  1.00 6.64  ? 113  ILE I CA  1 
ATOM   9581  C  C   . ILE I  1 113 ? -2.081  90.226  32.678  1.00 6.45  ? 113  ILE I C   1 
ATOM   9582  O  O   . ILE I  1 113 ? -2.645  91.189  32.142  1.00 5.85  ? 113  ILE I O   1 
ATOM   9583  C  CB  . ILE I  1 113 ? -3.825  88.564  33.426  1.00 8.00  ? 113  ILE I CB  1 
ATOM   9584  C  CG1 . ILE I  1 113 ? -4.456  87.799  34.577  1.00 11.32 ? 113  ILE I CG1 1 
ATOM   9585  C  CG2 . ILE I  1 113 ? -3.340  87.589  32.316  1.00 5.00  ? 113  ILE I CG2 1 
ATOM   9586  C  CD1 . ILE I  1 113 ? -3.516  86.998  35.313  1.00 14.90 ? 113  ILE I CD1 1 
ATOM   9587  N  N   . GLY I  1 114 ? -0.914  89.785  32.244  1.00 5.00  ? 114  GLY I N   1 
ATOM   9588  C  CA  . GLY I  1 114 ? -0.279  90.467  31.108  1.00 5.00  ? 114  GLY I CA  1 
ATOM   9589  C  C   . GLY I  1 114 ? 0.576   91.645  31.512  1.00 5.00  ? 114  GLY I C   1 
ATOM   9590  O  O   . GLY I  1 114 ? 1.217   92.294  30.657  1.00 5.00  ? 114  GLY I O   1 
ATOM   9591  N  N   . ARG I  1 115 ? 0.582   91.938  32.800  1.00 5.00  ? 115  ARG I N   1 
ATOM   9592  C  CA  . ARG I  1 115 ? 1.427   93.022  33.329  1.00 5.00  ? 115  ARG I CA  1 
ATOM   9593  C  C   . ARG I  1 115 ? 2.703   92.477  33.999  1.00 5.00  ? 115  ARG I C   1 
ATOM   9594  O  O   . ARG I  1 115 ? 2.951   91.301  33.957  1.00 7.01  ? 115  ARG I O   1 
ATOM   9595  C  CB  . ARG I  1 115 ? 0.606   93.940  34.245  1.00 5.00  ? 115  ARG I CB  1 
ATOM   9596  C  CG  . ARG I  1 115 ? -0.653  94.432  33.481  1.00 5.66  ? 115  ARG I CG  1 
ATOM   9597  C  CD  . ARG I  1 115 ? -1.378  95.614  34.137  1.00 6.26  ? 115  ARG I CD  1 
ATOM   9598  N  NE  . ARG I  1 115 ? -2.614  95.939  33.428  1.00 6.28  ? 115  ARG I NE  1 
ATOM   9599  C  CZ  . ARG I  1 115 ? -2.732  96.850  32.467  1.00 7.57  ? 115  ARG I CZ  1 
ATOM   9600  N  NH1 . ARG I  1 115 ? -1.669  97.517  31.996  1.00 5.00  ? 115  ARG I NH1 1 
ATOM   9601  N  NH2 . ARG I  1 115 ? -3.939  97.049  31.921  1.00 5.59  ? 115  ARG I NH2 1 
ATOM   9602  N  N   . THR I  1 116 ? 3.534   93.331  34.572  1.00 5.00  ? 116  THR I N   1 
ATOM   9603  C  CA  . THR I  1 116 ? 4.842   92.866  35.056  1.00 5.00  ? 116  THR I CA  1 
ATOM   9604  C  C   . THR I  1 116 ? 4.989   93.007  36.554  1.00 5.86  ? 116  THR I C   1 
ATOM   9605  O  O   . THR I  1 116 ? 4.705   94.072  37.104  1.00 5.28  ? 116  THR I O   1 
ATOM   9606  C  CB  . THR I  1 116 ? 5.963   93.678  34.376  1.00 6.00  ? 116  THR I CB  1 
ATOM   9607  O  OG1 . THR I  1 116 ? 6.028   93.304  32.986  1.00 5.00  ? 116  THR I OG1 1 
ATOM   9608  C  CG2 . THR I  1 116 ? 7.326   93.286  34.970  1.00 5.00  ? 116  THR I CG2 1 
ATOM   9609  N  N   . LEU I  1 117 ? 5.414   91.934  37.220  1.00 5.00  ? 117  LEU I N   1 
ATOM   9610  C  CA  . LEU I  1 117 ? 5.705   92.024  38.662  1.00 5.04  ? 117  LEU I CA  1 
ATOM   9611  C  C   . LEU I  1 117 ? 7.184   92.356  38.788  1.00 5.00  ? 117  LEU I C   1 
ATOM   9612  O  O   . LEU I  1 117 ? 7.982   91.753  38.077  1.00 5.00  ? 117  LEU I O   1 
ATOM   9613  C  CB  . LEU I  1 117 ? 5.418   90.668  39.328  1.00 5.00  ? 117  LEU I CB  1 
ATOM   9614  C  CG  . LEU I  1 117 ? 5.568   90.564  40.857  1.00 7.12  ? 117  LEU I CG  1 
ATOM   9615  C  CD1 . LEU I  1 117 ? 4.536   91.459  41.575  1.00 5.18  ? 117  LEU I CD1 1 
ATOM   9616  C  CD2 . LEU I  1 117 ? 5.334   89.124  41.309  1.00 5.00  ? 117  LEU I CD2 1 
ATOM   9617  N  N   . VAL I  1 118 ? 7.529   93.297  39.670  1.00 5.00  ? 118  VAL I N   1 
ATOM   9618  C  CA  . VAL I  1 118 ? 8.924   93.764  39.836  1.00 5.00  ? 118  VAL I CA  1 
ATOM   9619  C  C   . VAL I  1 118 ? 9.286   93.719  41.297  1.00 5.00  ? 118  VAL I C   1 
ATOM   9620  O  O   . VAL I  1 118 ? 8.499   94.118  42.144  1.00 5.00  ? 118  VAL I O   1 
ATOM   9621  C  CB  . VAL I  1 118 ? 9.099   95.241  39.379  1.00 5.00  ? 118  VAL I CB  1 
ATOM   9622  C  CG1 . VAL I  1 118 ? 10.572  95.715  39.647  1.00 5.87  ? 118  VAL I CG1 1 
ATOM   9623  C  CG2 . VAL I  1 118 ? 8.732   95.321  37.899  1.00 5.00  ? 118  VAL I CG2 1 
ATOM   9624  N  N   . VAL I  1 119 ? 10.467  93.200  41.593  1.00 5.35  ? 119  VAL I N   1 
ATOM   9625  C  CA  . VAL I  1 119 ? 10.989  93.334  42.935  1.00 5.00  ? 119  VAL I CA  1 
ATOM   9626  C  C   . VAL I  1 119 ? 12.184  94.287  42.839  1.00 5.11  ? 119  VAL I C   1 
ATOM   9627  O  O   . VAL I  1 119 ? 12.996  94.223  41.887  1.00 5.00  ? 119  VAL I O   1 
ATOM   9628  C  CB  . VAL I  1 119 ? 11.343  91.980  43.589  1.00 5.91  ? 119  VAL I CB  1 
ATOM   9629  C  CG1 . VAL I  1 119 ? 12.360  91.211  42.719  1.00 5.40  ? 119  VAL I CG1 1 
ATOM   9630  C  CG2 . VAL I  1 119 ? 11.911  92.211  45.010  1.00 5.00  ? 119  VAL I CG2 1 
ATOM   9631  N  N   . HIS I  1 120 ? 12.306  95.167  43.830  1.00 5.00  ? 120  HIS I N   1 
ATOM   9632  C  CA  . HIS I  1 120 ? 13.255  96.282  43.766  1.00 5.49  ? 120  HIS I CA  1 
ATOM   9633  C  C   . HIS I  1 120 ? 14.471  96.164  44.664  1.00 6.54  ? 120  HIS I C   1 
ATOM   9634  O  O   . HIS I  1 120 ? 14.519  95.379  45.609  1.00 5.68  ? 120  HIS I O   1 
ATOM   9635  C  CB  . HIS I  1 120 ? 12.537  97.583  44.150  1.00 5.69  ? 120  HIS I CB  1 
ATOM   9636  C  CG  . HIS I  1 120 ? 11.638  98.101  43.092  1.00 8.12  ? 120  HIS I CG  1 
ATOM   9637  N  ND1 . HIS I  1 120 ? 12.052  99.017  42.145  1.00 7.99  ? 120  HIS I ND1 1 
ATOM   9638  C  CD2 . HIS I  1 120 ? 10.331  97.856  42.839  1.00 8.66  ? 120  HIS I CD2 1 
ATOM   9639  C  CE1 . HIS I  1 120 ? 11.038  99.289  41.337  1.00 6.28  ? 120  HIS I CE1 1 
ATOM   9640  N  NE2 . HIS I  1 120 ? 9.996   98.594  41.734  1.00 8.45  ? 120  HIS I NE2 1 
ATOM   9641  N  N   . GLU I  1 121 ? 15.417  97.058  44.400  1.00 6.81  ? 121  GLU I N   1 
ATOM   9642  C  CA  . GLU I  1 121 ? 16.680  97.139  45.071  1.00 8.25  ? 121  GLU I CA  1 
ATOM   9643  C  C   . GLU I  1 121 ? 16.558  97.517  46.526  1.00 7.69  ? 121  GLU I C   1 
ATOM   9644  O  O   . GLU I  1 121 ? 17.268  96.959  47.364  1.00 7.85  ? 121  GLU I O   1 
ATOM   9645  C  CB  . GLU I  1 121 ? 17.499  98.238  44.373  1.00 8.25  ? 121  GLU I CB  1 
ATOM   9646  C  CG  . GLU I  1 121 ? 18.787  98.687  45.074  1.00 12.09 ? 121  GLU I CG  1 
ATOM   9647  C  CD  . GLU I  1 121 ? 19.283  100.048 44.558  1.00 17.98 ? 121  GLU I CD  1 
ATOM   9648  O  OE1 . GLU I  1 121 ? 18.591  100.723 43.738  1.00 10.81 ? 121  GLU I OE1 1 
ATOM   9649  O  OE2 . GLU I  1 121 ? 20.384  100.459 44.994  1.00 21.24 ? 121  GLU I OE2 1 
ATOM   9650  N  N   . LYS I  1 122 ? 15.645  98.449  46.814  1.00 8.15  ? 122  LYS I N   1 
ATOM   9651  C  CA  . LYS I  1 122 ? 15.510  99.051  48.143  1.00 9.16  ? 122  LYS I CA  1 
ATOM   9652  C  C   . LYS I  1 122 ? 14.105  98.970  48.675  1.00 7.99  ? 122  LYS I C   1 
ATOM   9653  O  O   . LYS I  1 122 ? 13.177  98.586  47.957  1.00 7.37  ? 122  LYS I O   1 
ATOM   9654  C  CB  . LYS I  1 122 ? 15.831  100.567 48.070  1.00 9.99  ? 122  LYS I CB  1 
ATOM   9655  C  CG  . LYS I  1 122 ? 17.166  100.942 47.573  1.00 14.66 ? 122  LYS I CG  1 
ATOM   9656  C  CD  . LYS I  1 122 ? 17.358  102.416 47.865  1.00 19.61 ? 122  LYS I CD  1 
ATOM   9657  C  CE  . LYS I  1 122 ? 18.181  103.094 46.832  1.00 23.99 ? 122  LYS I CE  1 
ATOM   9658  N  NZ  . LYS I  1 122 ? 18.071  104.584 46.982  1.00 27.45 ? 122  LYS I NZ  1 
ATOM   9659  N  N   . ALA I  1 123 ? 13.931  99.417  49.924  1.00 7.98  ? 123  ALA I N   1 
ATOM   9660  C  CA  . ALA I  1 123 ? 12.606  99.425  50.520  1.00 7.76  ? 123  ALA I CA  1 
ATOM   9661  C  C   . ALA I  1 123 ? 11.721  100.458 49.846  1.00 8.12  ? 123  ALA I C   1 
ATOM   9662  O  O   . ALA I  1 123 ? 12.175  101.543 49.467  1.00 8.47  ? 123  ALA I O   1 
ATOM   9663  C  CB  . ALA I  1 123 ? 12.681  99.743  52.041  1.00 7.92  ? 123  ALA I CB  1 
ATOM   9664  N  N   . ASP I  1 124 ? 10.447  100.122 49.741  1.00 6.39  ? 124  ASP I N   1 
ATOM   9665  C  CA  . ASP I  1 124 ? 9.431   101.040 49.287  1.00 7.13  ? 124  ASP I CA  1 
ATOM   9666  C  C   . ASP I  1 124 ? 9.049   101.864 50.525  1.00 6.99  ? 124  ASP I C   1 
ATOM   9667  O  O   . ASP I  1 124 ? 8.636   101.294 51.553  1.00 6.76  ? 124  ASP I O   1 
ATOM   9668  C  CB  . ASP I  1 124 ? 8.241   100.201 48.857  1.00 7.13  ? 124  ASP I CB  1 
ATOM   9669  C  CG  . ASP I  1 124 ? 7.090   101.005 48.311  1.00 9.03  ? 124  ASP I CG  1 
ATOM   9670  O  OD1 . ASP I  1 124 ? 6.955   102.206 48.648  1.00 6.05  ? 124  ASP I OD1 1 
ATOM   9671  O  OD2 . ASP I  1 124 ? 6.281   100.500 47.488  1.00 10.31 ? 124  ASP I OD2 1 
ATOM   9672  N  N   . ASP I  1 125 ? 9.188   103.195 50.449  1.00 6.75  ? 125  ASP I N   1 
ATOM   9673  C  CA  . ASP I  1 125 ? 8.847   104.027 51.602  1.00 7.44  ? 125  ASP I CA  1 
ATOM   9674  C  C   . ASP I  1 125 ? 7.332   104.302 51.754  1.00 7.38  ? 125  ASP I C   1 
ATOM   9675  O  O   . ASP I  1 125 ? 6.885   105.067 52.616  1.00 6.86  ? 125  ASP I O   1 
ATOM   9676  C  CB  . ASP I  1 125 ? 9.688   105.322 51.592  1.00 6.68  ? 125  ASP I CB  1 
ATOM   9677  C  CG  . ASP I  1 125 ? 9.293   106.295 50.532  1.00 7.30  ? 125  ASP I CG  1 
ATOM   9678  O  OD1 . ASP I  1 125 ? 8.173   106.246 49.976  1.00 7.75  ? 125  ASP I OD1 1 
ATOM   9679  O  OD2 . ASP I  1 125 ? 10.078  107.232 50.261  1.00 8.47  ? 125  ASP I OD2 1 
ATOM   9680  N  N   . LEU I  1 126 ? 6.542   103.638 50.918  1.00 6.89  ? 126  LEU I N   1 
ATOM   9681  C  CA  . LEU I  1 126 ? 5.088   103.696 51.007  1.00 7.20  ? 126  LEU I CA  1 
ATOM   9682  C  C   . LEU I  1 126 ? 4.524   105.111 50.869  1.00 6.68  ? 126  LEU I C   1 
ATOM   9683  O  O   . LEU I  1 126 ? 3.450   105.398 51.370  1.00 8.01  ? 126  LEU I O   1 
ATOM   9684  C  CB  . LEU I  1 126 ? 4.563   102.995 52.265  1.00 7.83  ? 126  LEU I CB  1 
ATOM   9685  C  CG  . LEU I  1 126 ? 5.125   101.602 52.605  1.00 9.96  ? 126  LEU I CG  1 
ATOM   9686  C  CD1 . LEU I  1 126 ? 4.446   100.951 53.838  1.00 10.73 ? 126  LEU I CD1 1 
ATOM   9687  C  CD2 . LEU I  1 126 ? 5.034   100.686 51.362  1.00 8.96  ? 126  LEU I CD2 1 
ATOM   9688  N  N   . GLY I  1 127 ? 5.244   105.972 50.167  1.00 6.86  ? 127  GLY I N   1 
ATOM   9689  C  CA  . GLY I  1 127 ? 4.766   107.322 49.944  1.00 6.26  ? 127  GLY I CA  1 
ATOM   9690  C  C   . GLY I  1 127 ? 5.065   108.275 51.078  1.00 6.55  ? 127  GLY I C   1 
ATOM   9691  O  O   . GLY I  1 127 ? 4.597   109.455 51.056  1.00 6.75  ? 127  GLY I O   1 
ATOM   9692  N  N   . LYS I  1 128 ? 5.853   107.826 52.058  1.00 5.25  ? 128  LYS I N   1 
ATOM   9693  C  CA  . LYS I  1 128 ? 6.079   108.698 53.234  1.00 5.90  ? 128  LYS I CA  1 
ATOM   9694  C  C   . LYS I  1 128 ? 7.461   109.341 53.249  1.00 5.80  ? 128  LYS I C   1 
ATOM   9695  O  O   . LYS I  1 128 ? 7.942   109.776 54.300  1.00 6.45  ? 128  LYS I O   1 
ATOM   9696  C  CB  . LYS I  1 128 ? 5.914   107.865 54.499  1.00 6.37  ? 128  LYS I CB  1 
ATOM   9697  C  CG  . LYS I  1 128 ? 4.487   107.386 54.670  1.00 11.70 ? 128  LYS I CG  1 
ATOM   9698  C  CD  . LYS I  1 128 ? 4.383   106.259 55.702  1.00 17.87 ? 128  LYS I CD  1 
ATOM   9699  C  CE  . LYS I  1 128 ? 4.525   106.727 57.130  1.00 20.74 ? 128  LYS I CE  1 
ATOM   9700  N  NZ  . LYS I  1 128 ? 4.671   105.542 58.075  1.00 21.88 ? 128  LYS I NZ  1 
ATOM   9701  N  N   . GLY I  1 129 ? 8.085   109.441 52.089  1.00 5.00  ? 129  GLY I N   1 
ATOM   9702  C  CA  . GLY I  1 129 ? 9.458   109.916 52.043  1.00 5.45  ? 129  GLY I CA  1 
ATOM   9703  C  C   . GLY I  1 129 ? 9.631   111.423 51.928  1.00 5.94  ? 129  GLY I C   1 
ATOM   9704  O  O   . GLY I  1 129 ? 10.754  111.899 51.981  1.00 6.15  ? 129  GLY I O   1 
ATOM   9705  N  N   . GLY I  1 130 ? 8.551   112.163 51.713  1.00 5.00  ? 130  GLY I N   1 
ATOM   9706  C  CA  . GLY I  1 130 ? 8.660   113.618 51.659  1.00 5.41  ? 130  GLY I CA  1 
ATOM   9707  C  C   . GLY I  1 130 ? 9.231   114.255 50.395  1.00 7.25  ? 130  GLY I C   1 
ATOM   9708  O  O   . GLY I  1 130 ? 9.698   115.378 50.435  1.00 5.89  ? 130  GLY I O   1 
ATOM   9709  N  N   . ASN I  1 131 ? 9.238   113.528 49.277  1.00 7.82  ? 131  ASN I N   1 
ATOM   9710  C  CA  . ASN I  1 131 ? 9.673   114.095 47.989  1.00 9.48  ? 131  ASN I CA  1 
ATOM   9711  C  C   . ASN I  1 131 ? 8.756   113.577 46.883  1.00 10.24 ? 131  ASN I C   1 
ATOM   9712  O  O   . ASN I  1 131 ? 7.918   112.724 47.131  1.00 10.26 ? 131  ASN I O   1 
ATOM   9713  C  CB  . ASN I  1 131 ? 11.153  113.793 47.653  1.00 9.22  ? 131  ASN I CB  1 
ATOM   9714  C  CG  . ASN I  1 131 ? 11.473  112.310 47.643  1.00 12.32 ? 131  ASN I CG  1 
ATOM   9715  O  OD1 . ASN I  1 131 ? 10.577  111.454 47.564  1.00 10.99 ? 131  ASN I OD1 1 
ATOM   9716  N  ND2 . ASN I  1 131 ? 12.765  111.989 47.727  1.00 13.37 ? 131  ASN I ND2 1 
ATOM   9717  N  N   . GLU I  1 132 ? 8.892   114.106 45.673  1.00 9.94  ? 132  GLU I N   1 
ATOM   9718  C  CA  . GLU I  1 132 ? 8.003   113.681 44.591  1.00 11.81 ? 132  GLU I CA  1 
ATOM   9719  C  C   . GLU I  1 132 ? 8.265   112.217 44.219  1.00 10.53 ? 132  GLU I C   1 
ATOM   9720  O  O   . GLU I  1 132 ? 7.352   111.452 43.870  1.00 10.67 ? 132  GLU I O   1 
ATOM   9721  C  CB  . GLU I  1 132 ? 8.214   114.588 43.353  1.00 12.18 ? 132  GLU I CB  1 
ATOM   9722  C  CG  . GLU I  1 132 ? 7.378   114.145 42.163  1.00 18.76 ? 132  GLU I CG  1 
ATOM   9723  C  CD  . GLU I  1 132 ? 6.222   115.089 41.872  1.00 28.18 ? 132  GLU I CD  1 
ATOM   9724  O  OE1 . GLU I  1 132 ? 5.448   115.399 42.831  1.00 29.78 ? 132  GLU I OE1 1 
ATOM   9725  O  OE2 . GLU I  1 132 ? 6.116   115.533 40.682  1.00 28.20 ? 132  GLU I OE2 1 
ATOM   9726  N  N   . GLU I  1 133 ? 9.521   111.809 44.323  1.00 9.69  ? 133  GLU I N   1 
ATOM   9727  C  CA  . GLU I  1 133 ? 9.858   110.443 43.954  1.00 9.34  ? 133  GLU I CA  1 
ATOM   9728  C  C   . GLU I  1 133 ? 9.095   109.487 44.853  1.00 8.48  ? 133  GLU I C   1 
ATOM   9729  O  O   . GLU I  1 133 ? 8.625   108.433 44.409  1.00 9.11  ? 133  GLU I O   1 
ATOM   9730  C  CB  . GLU I  1 133 ? 11.367  110.201 44.064  1.00 10.09 ? 133  GLU I CB  1 
ATOM   9731  C  CG  . GLU I  1 133 ? 11.784  108.840 43.485  1.00 11.02 ? 133  GLU I CG  1 
ATOM   9732  C  CD  . GLU I  1 133 ? 11.477  108.724 41.998  1.00 14.79 ? 133  GLU I CD  1 
ATOM   9733  O  OE1 . GLU I  1 133 ? 11.610  109.723 41.241  1.00 17.85 ? 133  GLU I OE1 1 
ATOM   9734  O  OE2 . GLU I  1 133 ? 11.116  107.620 41.571  1.00 17.19 ? 133  GLU I OE2 1 
ATOM   9735  N  N   . SER I  1 134 ? 8.962   109.851 46.119  1.00 7.41  ? 134  SER I N   1 
ATOM   9736  C  CA  . SER I  1 134 ? 8.209   108.981 47.052  1.00 7.54  ? 134  SER I CA  1 
ATOM   9737  C  C   . SER I  1 134 ? 6.755   108.756 46.613  1.00 7.68  ? 134  SER I C   1 
ATOM   9738  O  O   . SER I  1 134 ? 6.209   107.653 46.779  1.00 7.27  ? 134  SER I O   1 
ATOM   9739  C  CB  . SER I  1 134 ? 8.257   109.540 48.470  1.00 6.72  ? 134  SER I CB  1 
ATOM   9740  O  OG  . SER I  1 134 ? 7.492   108.753 49.398  1.00 5.00  ? 134  SER I OG  1 
ATOM   9741  N  N   . THR I  1 135 ? 6.154   109.774 45.994  1.00 9.20  ? 135  THR I N   1 
ATOM   9742  C  CA  . THR I  1 135 ? 4.749   109.739 45.574  1.00 9.35  ? 135  THR I CA  1 
ATOM   9743  C  C   . THR I  1 135 ? 4.636   109.078 44.214  1.00 9.33  ? 135  THR I C   1 
ATOM   9744  O  O   . THR I  1 135 ? 3.510   108.921 43.687  1.00 9.17  ? 135  THR I O   1 
ATOM   9745  C  CB  . THR I  1 135 ? 4.185   111.202 45.443  1.00 10.70 ? 135  THR I CB  1 
ATOM   9746  O  OG1 . THR I  1 135 ? 4.563   111.739 44.168  1.00 15.62 ? 135  THR I OG1 1 
ATOM   9747  C  CG2 . THR I  1 135 ? 4.894   112.078 46.312  1.00 11.20 ? 135  THR I CG2 1 
ATOM   9748  N  N   . LYS I  1 136 ? 5.780   108.681 43.656  1.00 8.30  ? 136  LYS I N   1 
ATOM   9749  C  CA  . LYS I  1 136 ? 5.793   107.986 42.361  1.00 9.74  ? 136  LYS I CA  1 
ATOM   9750  C  C   . LYS I  1 136 ? 6.186   106.525 42.485  1.00 9.98  ? 136  LYS I C   1 
ATOM   9751  O  O   . LYS I  1 136 ? 5.472   105.641 41.985  1.00 9.90  ? 136  LYS I O   1 
ATOM   9752  C  CB  . LYS I  1 136 ? 6.711   108.677 41.345  1.00 10.10 ? 136  LYS I CB  1 
ATOM   9753  C  CG  . LYS I  1 136 ? 6.329   110.125 41.066  1.00 15.00 ? 136  LYS I CG  1 
ATOM   9754  C  CD  . LYS I  1 136 ? 6.892   110.632 39.746  1.00 20.93 ? 136  LYS I CD  1 
ATOM   9755  C  CE  . LYS I  1 136 ? 8.245   111.302 39.910  1.00 26.20 ? 136  LYS I CE  1 
ATOM   9756  N  NZ  . LYS I  1 136 ? 8.878   111.610 38.554  1.00 28.61 ? 136  LYS I NZ  1 
ATOM   9757  N  N   . THR I  1 137 ? 7.303   106.256 43.162  1.00 9.69  ? 137  THR I N   1 
ATOM   9758  C  CA  . THR I  1 137 ? 7.844   104.897 43.180  1.00 10.21 ? 137  THR I CA  1 
ATOM   9759  C  C   . THR I  1 137 ? 8.131   104.398 44.575  1.00 9.62  ? 137  THR I C   1 
ATOM   9760  O  O   . THR I  1 137 ? 8.588   103.276 44.750  1.00 8.95  ? 137  THR I O   1 
ATOM   9761  C  CB  . THR I  1 137 ? 9.209   104.890 42.432  1.00 10.59 ? 137  THR I CB  1 
ATOM   9762  O  OG1 . THR I  1 137 ? 10.124  105.781 43.119  1.00 9.85  ? 137  THR I OG1 1 
ATOM   9763  C  CG2 . THR I  1 137 ? 9.104   105.498 41.059  1.00 11.95 ? 137  THR I CG2 1 
ATOM   9764  N  N   . GLY I  1 138 ? 7.952   105.254 45.571  1.00 8.06  ? 138  GLY I N   1 
ATOM   9765  C  CA  . GLY I  1 138 ? 8.332   104.881 46.922  1.00 7.07  ? 138  GLY I CA  1 
ATOM   9766  C  C   . GLY I  1 138 ? 9.840   104.869 47.175  1.00 7.04  ? 138  GLY I C   1 
ATOM   9767  O  O   . GLY I  1 138 ? 10.274  104.321 48.183  1.00 5.24  ? 138  GLY I O   1 
ATOM   9768  N  N   . ASN I  1 139 ? 10.628  105.493 46.287  1.00 5.76  ? 139  ASN I N   1 
ATOM   9769  C  CA  . ASN I  1 139 ? 12.075  105.475 46.423  1.00 6.31  ? 139  ASN I CA  1 
ATOM   9770  C  C   . ASN I  1 139 ? 12.640  104.043 46.494  1.00 6.29  ? 139  ASN I C   1 
ATOM   9771  O  O   . ASN I  1 139 ? 13.665  103.818 47.131  1.00 5.01  ? 139  ASN I O   1 
ATOM   9772  C  CB  . ASN I  1 139 ? 12.491  106.317 47.656  1.00 6.36  ? 139  ASN I CB  1 
ATOM   9773  C  CG  . ASN I  1 139 ? 12.351  107.834 47.393  1.00 9.78  ? 139  ASN I CG  1 
ATOM   9774  O  OD1 . ASN I  1 139 ? 13.008  108.373 46.503  1.00 10.67 ? 139  ASN I OD1 1 
ATOM   9775  N  ND2 . ASN I  1 139 ? 11.503  108.494 48.133  1.00 7.12  ? 139  ASN I ND2 1 
ATOM   9776  N  N   . ALA I  1 140 ? 11.979  103.088 45.820  1.00 5.70  ? 140  ALA I N   1 
ATOM   9777  C  CA  . ALA I  1 140 ? 12.391  101.692 45.935  1.00 6.66  ? 140  ALA I CA  1 
ATOM   9778  C  C   . ALA I  1 140 ? 13.601  101.348 45.064  1.00 6.46  ? 140  ALA I C   1 
ATOM   9779  O  O   . ALA I  1 140 ? 14.163  100.256 45.151  1.00 6.47  ? 140  ALA I O   1 
ATOM   9780  C  CB  . ALA I  1 140 ? 11.221  100.781 45.633  1.00 6.82  ? 140  ALA I CB  1 
ATOM   9781  N  N   . GLY I  1 141 ? 14.032  102.304 44.251  1.00 6.65  ? 141  GLY I N   1 
ATOM   9782  C  CA  . GLY I  1 141 ? 15.268  102.099 43.503  1.00 7.69  ? 141  GLY I CA  1 
ATOM   9783  C  C   . GLY I  1 141 ? 15.168  101.171 42.301  1.00 6.81  ? 141  GLY I C   1 
ATOM   9784  O  O   . GLY I  1 141 ? 14.118  101.011 41.710  1.00 5.33  ? 141  GLY I O   1 
ATOM   9785  N  N   . SER I  1 142 ? 16.281  100.542 41.964  1.00 7.89  ? 142  SER I N   1 
ATOM   9786  C  CA  . SER I  1 142 ? 16.373  99.822  40.704  1.00 8.01  ? 142  SER I CA  1 
ATOM   9787  C  C   . SER I  1 142 ? 15.545  98.563  40.706  1.00 7.75  ? 142  SER I C   1 
ATOM   9788  O  O   . SER I  1 142 ? 15.132  98.062  41.765  1.00 6.34  ? 142  SER I O   1 
ATOM   9789  C  CB  . SER I  1 142 ? 17.839  99.485  40.414  1.00 9.12  ? 142  SER I CB  1 
ATOM   9790  O  OG  . SER I  1 142 ? 18.195  98.327  41.155  1.00 12.50 ? 142  SER I OG  1 
ATOM   9791  N  N   . ARG I  1 143 ? 15.310  98.031  39.512  1.00 7.70  ? 143  ARG I N   1 
ATOM   9792  C  CA  . ARG I  1 143 ? 14.469  96.845  39.400  1.00 8.14  ? 143  ARG I CA  1 
ATOM   9793  C  C   . ARG I  1 143 ? 15.374  95.625  39.305  1.00 8.37  ? 143  ARG I C   1 
ATOM   9794  O  O   . ARG I  1 143 ? 16.082  95.489  38.337  1.00 9.78  ? 143  ARG I O   1 
ATOM   9795  C  CB  . ARG I  1 143 ? 13.638  96.991  38.147  1.00 8.09  ? 143  ARG I CB  1 
ATOM   9796  C  CG  . ARG I  1 143 ? 12.858  98.287  38.120  1.00 9.58  ? 143  ARG I CG  1 
ATOM   9797  C  CD  . ARG I  1 143 ? 12.085  98.585  36.806  1.00 7.23  ? 143  ARG I CD  1 
ATOM   9798  N  NE  . ARG I  1 143 ? 11.453  99.914  36.924  1.00 6.73  ? 143  ARG I NE  1 
ATOM   9799  C  CZ  . ARG I  1 143 ? 10.478  100.376 36.139  1.00 7.03  ? 143  ARG I CZ  1 
ATOM   9800  N  NH1 . ARG I  1 143 ? 9.996   99.624  35.138  1.00 5.39  ? 143  ARG I NH1 1 
ATOM   9801  N  NH2 . ARG I  1 143 ? 9.951   101.571 36.395  1.00 6.00  ? 143  ARG I NH2 1 
ATOM   9802  N  N   . LEU I  1 144 ? 15.366  94.749  40.305  1.00 7.60  ? 144  LEU I N   1 
ATOM   9803  C  CA  . LEU I  1 144 ? 16.305  93.631  40.327  1.00 6.07  ? 144  LEU I CA  1 
ATOM   9804  C  C   . LEU I  1 144 ? 15.841  92.448  39.516  1.00 5.97  ? 144  LEU I C   1 
ATOM   9805  O  O   . LEU I  1 144 ? 16.675  91.763  38.918  1.00 6.83  ? 144  LEU I O   1 
ATOM   9806  C  CB  . LEU I  1 144 ? 16.565  93.207  41.758  1.00 6.01  ? 144  LEU I CB  1 
ATOM   9807  C  CG  . LEU I  1 144 ? 17.213  94.347  42.602  1.00 9.33  ? 144  LEU I CG  1 
ATOM   9808  C  CD1 . LEU I  1 144 ? 17.621  93.810  43.926  1.00 14.64 ? 144  LEU I CD1 1 
ATOM   9809  C  CD2 . LEU I  1 144 ? 18.455  94.927  41.915  1.00 9.99  ? 144  LEU I CD2 1 
ATOM   9810  N  N   . ALA I  1 145 ? 14.525  92.205  39.484  1.00 5.00  ? 145  ALA I N   1 
ATOM   9811  C  CA  . ALA I  1 145 ? 14.009  91.057  38.767  1.00 5.00  ? 145  ALA I CA  1 
ATOM   9812  C  C   . ALA I  1 145 ? 12.551  91.321  38.440  1.00 5.05  ? 145  ALA I C   1 
ATOM   9813  O  O   . ALA I  1 145 ? 11.894  92.063  39.140  1.00 5.00  ? 145  ALA I O   1 
ATOM   9814  C  CB  . ALA I  1 145 ? 14.146  89.780  39.616  1.00 5.00  ? 145  ALA I CB  1 
ATOM   9815  N  N   . CYS I  1 146 ? 12.056  90.737  37.364  1.00 5.00  ? 146  CYS I N   1 
ATOM   9816  C  CA  . CYS I  1 146 ? 10.675  90.935  37.001  1.00 5.33  ? 146  CYS I CA  1 
ATOM   9817  C  C   . CYS I  1 146 ? 10.242  89.783  36.113  1.00 5.00  ? 146  CYS I C   1 
ATOM   9818  O  O   . CYS I  1 146 ? 11.065  88.961  35.654  1.00 5.00  ? 146  CYS I O   1 
ATOM   9819  C  CB  . CYS I  1 146 ? 10.500  92.231  36.205  1.00 5.85  ? 146  CYS I CB  1 
ATOM   9820  S  SG  . CYS I  1 146 ? 11.532  92.327  34.710  1.00 10.44 ? 146  CYS I SG  1 
ATOM   9821  N  N   . GLY I  1 147 ? 8.938   89.729  35.882  1.00 5.00  ? 147  GLY I N   1 
ATOM   9822  C  CA  . GLY I  1 147 ? 8.409   88.748  34.958  1.00 5.55  ? 147  GLY I CA  1 
ATOM   9823  C  C   . GLY I  1 147 ? 6.998   89.135  34.568  1.00 5.00  ? 147  GLY I C   1 
ATOM   9824  O  O   . GLY I  1 147 ? 6.337   89.918  35.270  1.00 5.00  ? 147  GLY I O   1 
ATOM   9825  N  N   . VAL I  1 148 ? 6.508   88.589  33.470  1.00 5.00  ? 148  VAL I N   1 
ATOM   9826  C  CA  . VAL I  1 148 ? 5.148   88.941  33.070  1.00 5.00  ? 148  VAL I CA  1 
ATOM   9827  C  C   . VAL I  1 148 ? 4.174   88.030  33.804  1.00 5.06  ? 148  VAL I C   1 
ATOM   9828  O  O   . VAL I  1 148 ? 4.448   86.879  33.943  1.00 5.00  ? 148  VAL I O   1 
ATOM   9829  C  CB  . VAL I  1 148 ? 5.001   88.715  31.559  1.00 5.00  ? 148  VAL I CB  1 
ATOM   9830  C  CG1 . VAL I  1 148 ? 3.534   89.090  31.118  1.00 5.09  ? 148  VAL I CG1 1 
ATOM   9831  C  CG2 . VAL I  1 148 ? 6.098   89.522  30.814  1.00 5.00  ? 148  VAL I CG2 1 
ATOM   9832  N  N   . ILE I  1 149 ? 3.031   88.533  34.249  1.00 5.00  ? 149  ILE I N   1 
ATOM   9833  C  CA  . ILE I  1 149 ? 2.091   87.705  34.985  1.00 5.00  ? 149  ILE I CA  1 
ATOM   9834  C  C   . ILE I  1 149 ? 1.233   86.937  34.024  1.00 5.00  ? 149  ILE I C   1 
ATOM   9835  O  O   . ILE I  1 149 ? 0.499   87.532  33.249  1.00 6.21  ? 149  ILE I O   1 
ATOM   9836  C  CB  . ILE I  1 149 ? 1.253   88.597  35.866  1.00 5.00  ? 149  ILE I CB  1 
ATOM   9837  C  CG1 . ILE I  1 149 ? 2.187   89.264  36.915  1.00 5.00  ? 149  ILE I CG1 1 
ATOM   9838  C  CG2 . ILE I  1 149 ? 0.127   87.838  36.529  1.00 5.00  ? 149  ILE I CG2 1 
ATOM   9839  C  CD1 . ILE I  1 149 ? 1.495   90.502  37.571  1.00 6.70  ? 149  ILE I CD1 1 
ATOM   9840  N  N   . GLY I  1 150 ? 1.299   85.616  34.084  1.00 5.00  ? 150  GLY I N   1 
ATOM   9841  C  CA  . GLY I  1 150 ? 0.578   84.798  33.117  1.00 5.00  ? 150  GLY I CA  1 
ATOM   9842  C  C   . GLY I  1 150 ? -0.534  83.963  33.735  1.00 5.41  ? 150  GLY I C   1 
ATOM   9843  O  O   . GLY I  1 150 ? -0.493  83.682  34.932  1.00 5.00  ? 150  GLY I O   1 
ATOM   9844  N  N   . ILE I  1 151 ? -1.481  83.526  32.899  1.00 5.00  ? 151  ILE I N   1 
ATOM   9845  C  CA  . ILE I  1 151 ? -2.577  82.678  33.359  1.00 5.24  ? 151  ILE I CA  1 
ATOM   9846  C  C   . ILE I  1 151 ? -2.051  81.318  33.688  1.00 5.00  ? 151  ILE I C   1 
ATOM   9847  O  O   . ILE I  1 151 ? -1.267  80.741  32.925  1.00 5.00  ? 151  ILE I O   1 
ATOM   9848  C  CB  . ILE I  1 151 ? -3.659  82.543  32.263  1.00 5.00  ? 151  ILE I CB  1 
ATOM   9849  C  CG1 . ILE I  1 151 ? -4.337  83.907  32.090  1.00 7.29  ? 151  ILE I CG1 1 
ATOM   9850  C  CG2 . ILE I  1 151 ? -4.692  81.411  32.633  1.00 6.69  ? 151  ILE I CG2 1 
ATOM   9851  C  CD1 . ILE I  1 151 ? -5.232  83.993  30.814  1.00 8.60  ? 151  ILE I CD1 1 
ATOM   9852  N  N   . ALA I  1 152 ? -2.508  80.771  34.807  1.00 5.00  ? 152  ALA I N   1 
ATOM   9853  C  CA  . ALA I  1 152 ? -2.011  79.471  35.282  1.00 6.79  ? 152  ALA I CA  1 
ATOM   9854  C  C   . ALA I  1 152 ? -3.164  78.484  35.370  1.00 7.65  ? 152  ALA I C   1 
ATOM   9855  O  O   . ALA I  1 152 ? -4.306  78.907  35.489  1.00 8.12  ? 152  ALA I O   1 
ATOM   9856  C  CB  . ALA I  1 152 ? -1.427  79.645  36.692  1.00 6.74  ? 152  ALA I CB  1 
ATOM   9857  N  N   . GLN I  1 153 ? -2.831  77.198  35.349  1.00 9.27  ? 153  GLN I N   1 
ATOM   9858  C  CA  . GLN I  1 153 ? -3.804  76.121  35.407  1.00 12.54 ? 153  GLN I CA  1 
ATOM   9859  C  C   . GLN I  1 153 ? -4.297  75.972  36.839  1.00 14.27 ? 153  GLN I C   1 
ATOM   9860  O  O   . GLN I  1 153 ? -3.499  76.098  37.761  1.00 14.49 ? 153  GLN I O   1 
ATOM   9861  C  CB  . GLN I  1 153 ? -3.163  74.803  34.958  1.00 11.30 ? 153  GLN I CB  1 
ATOM   9862  C  CG  . GLN I  1 153 ? -4.151  73.617  34.900  1.00 16.04 ? 153  GLN I CG  1 
ATOM   9863  C  CD  . GLN I  1 153 ? -3.502  72.351  34.354  1.00 18.40 ? 153  GLN I CD  1 
ATOM   9864  O  OE1 . GLN I  1 153 ? -2.461  71.907  34.856  1.00 22.16 ? 153  GLN I OE1 1 
ATOM   9865  N  NE2 . GLN I  1 153 ? -4.128  71.758  33.365  1.00 20.87 ? 153  GLN I NE2 1 
ATOM   9866  O  OXT . GLN I  1 153 ? -5.490  75.701  37.034  1.00 18.18 ? 153  GLN I OXT 1 
ATOM   9867  N  N   . ALA J  1 1   ? 56.066  99.395  31.007  1.00 20.58 ? 1    ALA J N   1 
ATOM   9868  C  CA  . ALA J  1 1   ? 55.660  98.872  29.686  1.00 19.83 ? 1    ALA J CA  1 
ATOM   9869  C  C   . ALA J  1 1   ? 54.668  97.699  29.764  1.00 18.59 ? 1    ALA J C   1 
ATOM   9870  O  O   . ALA J  1 1   ? 53.917  97.514  28.820  1.00 20.52 ? 1    ALA J O   1 
ATOM   9871  C  CB  . ALA J  1 1   ? 56.899  98.507  28.807  1.00 19.21 ? 1    ALA J CB  1 
ATOM   9872  N  N   . THR J  1 2   ? 54.679  96.894  30.833  1.00 16.01 ? 2    THR J N   1 
ATOM   9873  C  CA  . THR J  1 2   ? 53.680  95.820  30.955  1.00 13.73 ? 2    THR J CA  1 
ATOM   9874  C  C   . THR J  1 2   ? 52.389  96.459  31.460  1.00 10.57 ? 2    THR J C   1 
ATOM   9875  O  O   . THR J  1 2   ? 52.412  97.290  32.374  1.00 7.84  ? 2    THR J O   1 
ATOM   9876  C  CB  . THR J  1 2   ? 54.140  94.639  31.879  1.00 14.81 ? 2    THR J CB  1 
ATOM   9877  O  OG1 . THR J  1 2   ? 55.296  94.016  31.299  1.00 20.64 ? 2    THR J OG1 1 
ATOM   9878  C  CG2 . THR J  1 2   ? 53.161  93.524  31.829  1.00 15.30 ? 2    THR J CG2 1 
ATOM   9879  N  N   . LYS J  1 3   ? 51.279  96.094  30.829  1.00 8.11  ? 3    LYS J N   1 
ATOM   9880  C  CA  . LYS J  1 3   ? 49.979  96.633  31.196  1.00 7.84  ? 3    LYS J CA  1 
ATOM   9881  C  C   . LYS J  1 3   ? 48.992  95.502  31.369  1.00 6.37  ? 3    LYS J C   1 
ATOM   9882  O  O   . LYS J  1 3   ? 49.053  94.499  30.667  1.00 5.00  ? 3    LYS J O   1 
ATOM   9883  C  CB  . LYS J  1 3   ? 49.439  97.569  30.110  1.00 7.94  ? 3    LYS J CB  1 
ATOM   9884  C  CG  . LYS J  1 3   ? 50.367  98.808  29.885  1.00 12.08 ? 3    LYS J CG  1 
ATOM   9885  C  CD  . LYS J  1 3   ? 49.724  99.829  28.921  1.00 18.25 ? 3    LYS J CD  1 
ATOM   9886  C  CE  . LYS J  1 3   ? 48.400  100.388 29.490  1.00 22.94 ? 3    LYS J CE  1 
ATOM   9887  N  NZ  . LYS J  1 3   ? 47.794  101.508 28.674  1.00 25.15 ? 3    LYS J NZ  1 
ATOM   9888  N  N   . ALA J  1 4   ? 48.055  95.703  32.279  1.00 5.25  ? 4    ALA J N   1 
ATOM   9889  C  CA  . ALA J  1 4   ? 47.016  94.718  32.499  1.00 5.00  ? 4    ALA J CA  1 
ATOM   9890  C  C   . ALA J  1 4   ? 45.736  95.468  32.839  1.00 5.00  ? 4    ALA J C   1 
ATOM   9891  O  O   . ALA J  1 4   ? 45.792  96.654  33.137  1.00 5.00  ? 4    ALA J O   1 
ATOM   9892  C  CB  . ALA J  1 4   ? 47.427  93.750  33.647  1.00 5.00  ? 4    ALA J CB  1 
ATOM   9893  N  N   . VAL J  1 5   ? 44.584  94.792  32.786  1.00 5.00  ? 5    VAL J N   1 
ATOM   9894  C  CA  . VAL J  1 5   ? 43.337  95.455  33.054  1.00 5.00  ? 5    VAL J CA  1 
ATOM   9895  C  C   . VAL J  1 5   ? 42.368  94.433  33.669  1.00 5.28  ? 5    VAL J C   1 
ATOM   9896  O  O   . VAL J  1 5   ? 42.498  93.255  33.431  1.00 5.00  ? 5    VAL J O   1 
ATOM   9897  C  CB  . VAL J  1 5   ? 42.750  96.098  31.733  1.00 5.00  ? 5    VAL J CB  1 
ATOM   9898  C  CG1 . VAL J  1 5   ? 42.356  94.996  30.623  1.00 5.00  ? 5    VAL J CG1 1 
ATOM   9899  C  CG2 . VAL J  1 5   ? 41.547  97.027  31.988  1.00 5.00  ? 5    VAL J CG2 1 
ATOM   9900  N  N   . CYS J  1 6   ? 41.367  94.915  34.408  1.00 5.00  ? 6    CYS J N   1 
ATOM   9901  C  CA  . CYS J  1 6   ? 40.415  94.007  35.021  1.00 5.00  ? 6    CYS J CA  1 
ATOM   9902  C  C   . CYS J  1 6   ? 39.077  94.693  35.033  1.00 5.00  ? 6    CYS J C   1 
ATOM   9903  O  O   . CYS J  1 6   ? 38.977  95.863  35.475  1.00 5.00  ? 6    CYS J O   1 
ATOM   9904  C  CB  . CYS J  1 6   ? 40.855  93.814  36.475  1.00 5.42  ? 6    CYS J CB  1 
ATOM   9905  S  SG  . CYS J  1 6   ? 39.779  92.658  37.375  1.00 6.52  ? 6    CYS J SG  1 
ATOM   9906  N  N   . VAL J  1 7   ? 38.069  93.997  34.561  1.00 5.00  ? 7    VAL J N   1 
ATOM   9907  C  CA  . VAL J  1 7   ? 36.694  94.471  34.597  1.00 5.00  ? 7    VAL J CA  1 
ATOM   9908  C  C   . VAL J  1 7   ? 36.038  93.834  35.795  1.00 5.00  ? 7    VAL J C   1 
ATOM   9909  O  O   . VAL J  1 7   ? 35.940  92.606  35.871  1.00 5.00  ? 7    VAL J O   1 
ATOM   9910  C  CB  . VAL J  1 7   ? 35.917  94.091  33.334  1.00 5.00  ? 7    VAL J CB  1 
ATOM   9911  C  CG1 . VAL J  1 7   ? 34.491  94.618  33.461  1.00 6.45  ? 7    VAL J CG1 1 
ATOM   9912  C  CG2 . VAL J  1 7   ? 36.570  94.709  32.100  1.00 5.00  ? 7    VAL J CG2 1 
ATOM   9913  N  N   . LEU J  1 8   ? 35.654  94.661  36.761  1.00 5.00  ? 8    LEU J N   1 
ATOM   9914  C  CA  . LEU J  1 8   ? 35.012  94.155  37.964  1.00 5.69  ? 8    LEU J CA  1 
ATOM   9915  C  C   . LEU J  1 8   ? 33.478  94.129  37.821  1.00 5.47  ? 8    LEU J C   1 
ATOM   9916  O  O   . LEU J  1 8   ? 32.863  95.158  37.519  1.00 5.00  ? 8    LEU J O   1 
ATOM   9917  C  CB  . LEU J  1 8   ? 35.331  95.072  39.147  1.00 5.60  ? 8    LEU J CB  1 
ATOM   9918  C  CG  . LEU J  1 8   ? 36.819  95.144  39.595  1.00 9.86  ? 8    LEU J CG  1 
ATOM   9919  C  CD1 . LEU J  1 8   ? 37.044  96.266  40.683  1.00 14.92 ? 8    LEU J CD1 1 
ATOM   9920  C  CD2 . LEU J  1 8   ? 37.289  93.826  40.131  1.00 11.92 ? 8    LEU J CD2 1 
ATOM   9921  N  N   . LYS J  1 9   ? 32.897  92.960  38.029  1.00 5.00  ? 9    LYS J N   1 
ATOM   9922  C  CA  . LYS J  1 9   ? 31.436  92.803  37.985  1.00 7.42  ? 9    LYS J CA  1 
ATOM   9923  C  C   . LYS J  1 9   ? 31.037  91.852  39.095  1.00 6.42  ? 9    LYS J C   1 
ATOM   9924  O  O   . LYS J  1 9   ? 31.837  91.004  39.530  1.00 5.00  ? 9    LYS J O   1 
ATOM   9925  C  CB  . LYS J  1 9   ? 31.037  92.204  36.612  1.00 8.34  ? 9    LYS J CB  1 
ATOM   9926  C  CG  . LYS J  1 9   ? 31.183  93.250  35.436  1.00 13.84 ? 9    LYS J CG  1 
ATOM   9927  C  CD  . LYS J  1 9   ? 30.723  92.703  34.065  1.00 22.35 ? 9    LYS J CD  1 
ATOM   9928  C  CE  . LYS J  1 9   ? 30.914  93.732  32.896  1.00 22.65 ? 9    LYS J CE  1 
ATOM   9929  N  NZ  . LYS J  1 9   ? 30.226  95.056  33.202  1.00 29.09 ? 9    LYS J NZ  1 
ATOM   9930  N  N   . GLY J  1 10  ? 29.794  91.945  39.555  1.00 7.04  ? 10   GLY J N   1 
ATOM   9931  C  CA  . GLY J  1 10  ? 29.337  91.059  40.611  1.00 7.07  ? 10   GLY J CA  1 
ATOM   9932  C  C   . GLY J  1 10  ? 27.816  90.936  40.579  1.00 8.70  ? 10   GLY J C   1 
ATOM   9933  O  O   . GLY J  1 10  ? 27.193  91.238  39.561  1.00 7.56  ? 10   GLY J O   1 
ATOM   9934  N  N   . ASP J  1 11  ? 27.225  90.526  41.699  1.00 9.88  ? 11   ASP J N   1 
ATOM   9935  C  CA  . ASP J  1 11  ? 25.773  90.275  41.757  1.00 12.25 ? 11   ASP J CA  1 
ATOM   9936  C  C   . ASP J  1 11  ? 24.961  91.543  42.005  1.00 12.62 ? 11   ASP J C   1 
ATOM   9937  O  O   . ASP J  1 11  ? 23.748  91.523  41.904  1.00 13.47 ? 11   ASP J O   1 
ATOM   9938  C  CB  . ASP J  1 11  ? 25.447  89.347  42.903  1.00 12.88 ? 11   ASP J CB  1 
ATOM   9939  C  CG  . ASP J  1 11  ? 25.887  87.921  42.681  1.00 16.78 ? 11   ASP J CG  1 
ATOM   9940  O  OD1 . ASP J  1 11  ? 26.054  87.470  41.523  1.00 17.26 ? 11   ASP J OD1 1 
ATOM   9941  O  OD2 . ASP J  1 11  ? 26.059  87.161  43.669  1.00 21.52 ? 11   ASP J OD2 1 
ATOM   9942  N  N   . GLY J  1 12  ? 25.611  92.651  42.335  1.00 12.21 ? 12   GLY J N   1 
ATOM   9943  C  CA  . GLY J  1 12  ? 24.882  93.863  42.652  1.00 12.00 ? 12   GLY J CA  1 
ATOM   9944  C  C   . GLY J  1 12  ? 25.269  94.978  41.713  1.00 11.45 ? 12   GLY J C   1 
ATOM   9945  O  O   . GLY J  1 12  ? 25.666  94.739  40.575  1.00 12.34 ? 12   GLY J O   1 
ATOM   9946  N  N   . PRO J  1 13  ? 25.208  96.203  42.204  1.00 10.66 ? 13   PRO J N   1 
ATOM   9947  C  CA  . PRO J  1 13  ? 25.490  97.360  41.365  1.00 10.46 ? 13   PRO J CA  1 
ATOM   9948  C  C   . PRO J  1 13  ? 26.963  97.734  41.309  1.00 9.27  ? 13   PRO J C   1 
ATOM   9949  O  O   . PRO J  1 13  ? 27.320  98.661  40.588  1.00 8.41  ? 13   PRO J O   1 
ATOM   9950  C  CB  . PRO J  1 13  ? 24.704  98.460  42.074  1.00 10.52 ? 13   PRO J CB  1 
ATOM   9951  C  CG  . PRO J  1 13  ? 24.923  98.122  43.538  1.00 11.04 ? 13   PRO J CG  1 
ATOM   9952  C  CD  . PRO J  1 13  ? 24.872  96.595  43.586  1.00 11.07 ? 13   PRO J CD  1 
ATOM   9953  N  N   . VAL J  1 14  ? 27.806  97.043  42.059  1.00 8.42  ? 14   VAL J N   1 
ATOM   9954  C  CA  . VAL J  1 14  ? 29.220  97.398  42.035  1.00 8.13  ? 14   VAL J CA  1 
ATOM   9955  C  C   . VAL J  1 14  ? 29.876  96.968  40.729  1.00 8.11  ? 14   VAL J C   1 
ATOM   9956  O  O   . VAL J  1 14  ? 29.816  95.794  40.337  1.00 8.03  ? 14   VAL J O   1 
ATOM   9957  C  CB  . VAL J  1 14  ? 29.957  96.796  43.213  1.00 8.44  ? 14   VAL J CB  1 
ATOM   9958  C  CG1 . VAL J  1 14  ? 31.464  97.154  43.125  1.00 7.95  ? 14   VAL J CG1 1 
ATOM   9959  C  CG2 . VAL J  1 14  ? 29.322  97.350  44.539  1.00 6.35  ? 14   VAL J CG2 1 
ATOM   9960  N  N   . GLN J  1 15  ? 30.499  97.923  40.043  1.00 7.83  ? 15   GLN J N   1 
ATOM   9961  C  CA  . GLN J  1 15  ? 31.188  97.612  38.810  1.00 8.59  ? 15   GLN J CA  1 
ATOM   9962  C  C   . GLN J  1 15  ? 32.300  98.589  38.600  1.00 8.40  ? 15   GLN J C   1 
ATOM   9963  O  O   . GLN J  1 15  ? 32.240  99.717  39.092  1.00 7.87  ? 15   GLN J O   1 
ATOM   9964  C  CB  . GLN J  1 15  ? 30.223  97.615  37.602  1.00 10.00 ? 15   GLN J CB  1 
ATOM   9965  C  CG  . GLN J  1 15  ? 29.475  98.858  37.366  1.00 14.18 ? 15   GLN J CG  1 
ATOM   9966  C  CD  . GLN J  1 15  ? 28.245  98.634  36.436  1.00 25.56 ? 15   GLN J CD  1 
ATOM   9967  O  OE1 . GLN J  1 15  ? 27.898  99.507  35.655  1.00 29.75 ? 15   GLN J OE1 1 
ATOM   9968  N  NE2 . GLN J  1 15  ? 27.602  97.460  36.537  1.00 29.16 ? 15   GLN J NE2 1 
ATOM   9969  N  N   . GLY J  1 16  ? 33.339  98.166  37.890  1.00 6.87  ? 16   GLY J N   1 
ATOM   9970  C  CA  . GLY J  1 16  ? 34.441  99.091  37.695  1.00 7.58  ? 16   GLY J CA  1 
ATOM   9971  C  C   . GLY J  1 16  ? 35.471  98.561  36.750  1.00 5.43  ? 16   GLY J C   1 
ATOM   9972  O  O   . GLY J  1 16  ? 35.352  97.421  36.291  1.00 5.00  ? 16   GLY J O   1 
ATOM   9973  N  N   . ILE J  1 17  ? 36.455  99.396  36.437  1.00 5.15  ? 17   ILE J N   1 
ATOM   9974  C  CA  . ILE J  1 17  ? 37.554  98.964  35.592  1.00 5.36  ? 17   ILE J CA  1 
ATOM   9975  C  C   . ILE J  1 17  ? 38.819  99.393  36.265  1.00 5.70  ? 17   ILE J C   1 
ATOM   9976  O  O   . ILE J  1 17  ? 38.949  100.563 36.676  1.00 5.79  ? 17   ILE J O   1 
ATOM   9977  C  CB  . ILE J  1 17  ? 37.486  99.666  34.239  1.00 7.18  ? 17   ILE J CB  1 
ATOM   9978  C  CG1 . ILE J  1 17  ? 36.278  99.144  33.480  1.00 8.77  ? 17   ILE J CG1 1 
ATOM   9979  C  CG2 . ILE J  1 17  ? 38.801  99.363  33.441  1.00 5.61  ? 17   ILE J CG2 1 
ATOM   9980  C  CD1 . ILE J  1 17  ? 36.067  99.830  32.104  1.00 11.72 ? 17   ILE J CD1 1 
ATOM   9981  N  N   . ILE J  1 18  ? 39.754  98.472  36.386  1.00 5.00  ? 18   ILE J N   1 
ATOM   9982  C  CA  . ILE J  1 18  ? 41.007  98.796  37.056  1.00 5.00  ? 18   ILE J CA  1 
ATOM   9983  C  C   . ILE J  1 18  ? 42.177  98.462  36.130  1.00 5.13  ? 18   ILE J C   1 
ATOM   9984  O  O   . ILE J  1 18  ? 42.226  97.351  35.567  1.00 5.21  ? 18   ILE J O   1 
ATOM   9985  C  CB  . ILE J  1 18  ? 41.151  97.980  38.330  1.00 5.00  ? 18   ILE J CB  1 
ATOM   9986  C  CG1 . ILE J  1 18  ? 40.062  98.377  39.341  1.00 5.00  ? 18   ILE J CG1 1 
ATOM   9987  C  CG2 . ILE J  1 18  ? 42.579  98.175  39.000  1.00 5.00  ? 18   ILE J CG2 1 
ATOM   9988  C  CD1 . ILE J  1 18  ? 40.233  99.804  39.950  1.00 5.95  ? 18   ILE J CD1 1 
ATOM   9989  N  N   . ASN J  1 19  ? 43.102  99.405  36.021  1.00 5.00  ? 19   ASN J N   1 
ATOM   9990  C  CA  . ASN J  1 19  ? 44.273  99.313  35.148  1.00 5.00  ? 19   ASN J CA  1 
ATOM   9991  C  C   . ASN J  1 19  ? 45.499  99.052  35.995  1.00 5.00  ? 19   ASN J C   1 
ATOM   9992  O  O   . ASN J  1 19  ? 45.557  99.464  37.188  1.00 5.00  ? 19   ASN J O   1 
ATOM   9993  C  CB  . ASN J  1 19  ? 44.484  100.639 34.418  1.00 5.83  ? 19   ASN J CB  1 
ATOM   9994  C  CG  . ASN J  1 19  ? 43.242  101.079 33.675  1.00 7.65  ? 19   ASN J CG  1 
ATOM   9995  O  OD1 . ASN J  1 19  ? 42.530  102.039 34.085  1.00 10.41 ? 19   ASN J OD1 1 
ATOM   9996  N  ND2 . ASN J  1 19  ? 42.947  100.387 32.606  1.00 5.00  ? 19   ASN J ND2 1 
ATOM   9997  N  N   . PHE J  1 20  ? 46.423  98.316  35.407  1.00 5.00  ? 20   PHE J N   1 
ATOM   9998  C  CA  . PHE J  1 20  ? 47.714  98.041  36.033  1.00 5.10  ? 20   PHE J CA  1 
ATOM   9999  C  C   . PHE J  1 20  ? 48.837  98.408  35.061  1.00 5.00  ? 20   PHE J C   1 
ATOM   10000 O  O   . PHE J  1 20  ? 48.767  98.081  33.857  1.00 5.00  ? 20   PHE J O   1 
ATOM   10001 C  CB  . PHE J  1 20  ? 47.880  96.538  36.331  1.00 5.00  ? 20   PHE J CB  1 
ATOM   10002 C  CG  . PHE J  1 20  ? 46.839  95.978  37.270  1.00 6.84  ? 20   PHE J CG  1 
ATOM   10003 C  CD1 . PHE J  1 20  ? 45.559  95.672  36.789  1.00 6.70  ? 20   PHE J CD1 1 
ATOM   10004 C  CD2 . PHE J  1 20  ? 47.136  95.759  38.599  1.00 5.00  ? 20   PHE J CD2 1 
ATOM   10005 C  CE1 . PHE J  1 20  ? 44.561  95.121  37.639  1.00 8.24  ? 20   PHE J CE1 1 
ATOM   10006 C  CE2 . PHE J  1 20  ? 46.152  95.223  39.482  1.00 8.73  ? 20   PHE J CE2 1 
ATOM   10007 C  CZ  . PHE J  1 20  ? 44.873  94.908  39.004  1.00 7.77  ? 20   PHE J CZ  1 
ATOM   10008 N  N   . GLU J  1 21  ? 49.889  99.052  35.547  1.00 5.02  ? 21   GLU J N   1 
ATOM   10009 C  CA  . GLU J  1 21  ? 51.006  99.325  34.661  1.00 7.25  ? 21   GLU J CA  1 
ATOM   10010 C  C   . GLU J  1 21  ? 52.294  99.158  35.449  1.00 7.37  ? 21   GLU J C   1 
ATOM   10011 O  O   . GLU J  1 21  ? 52.385  99.610  36.592  1.00 5.00  ? 21   GLU J O   1 
ATOM   10012 C  CB  . GLU J  1 21  ? 50.922  100.762 34.093  1.00 8.16  ? 21   GLU J CB  1 
ATOM   10013 C  CG  . GLU J  1 21  ? 52.113  101.095 33.201  1.00 15.54 ? 21   GLU J CG  1 
ATOM   10014 C  CD  . GLU J  1 21  ? 51.967  102.414 32.442  1.00 24.01 ? 21   GLU J CD  1 
ATOM   10015 O  OE1 . GLU J  1 21  ? 50.839  102.750 31.987  1.00 26.39 ? 21   GLU J OE1 1 
ATOM   10016 O  OE2 . GLU J  1 21  ? 53.003  103.098 32.263  1.00 27.66 ? 21   GLU J OE2 1 
ATOM   10017 N  N   . GLN J  1 22  ? 53.263  98.502  34.833  1.00 7.08  ? 22   GLN J N   1 
ATOM   10018 C  CA  . GLN J  1 22  ? 54.561  98.286  35.457  1.00 8.01  ? 22   GLN J CA  1 
ATOM   10019 C  C   . GLN J  1 22  ? 55.673  98.543  34.419  1.00 7.76  ? 22   GLN J C   1 
ATOM   10020 O  O   . GLN J  1 22  ? 55.874  97.760  33.489  1.00 8.09  ? 22   GLN J O   1 
ATOM   10021 C  CB  . GLN J  1 22  ? 54.642  96.857  35.969  1.00 7.03  ? 22   GLN J CB  1 
ATOM   10022 C  CG  . GLN J  1 22  ? 55.833  96.593  36.865  1.00 8.45  ? 22   GLN J CG  1 
ATOM   10023 C  CD  . GLN J  1 22  ? 55.886  95.138  37.317  1.00 10.01 ? 22   GLN J CD  1 
ATOM   10024 O  OE1 . GLN J  1 22  ? 55.351  94.263  36.632  1.00 9.29  ? 22   GLN J OE1 1 
ATOM   10025 N  NE2 . GLN J  1 22  ? 56.609  94.868  38.415  1.00 8.22  ? 22   GLN J NE2 1 
ATOM   10026 N  N   . LYS J  1 23  ? 56.371  99.653  34.582  1.00 9.85  ? 23   LYS J N   1 
ATOM   10027 C  CA  . LYS J  1 23  ? 57.378  100.049 33.581  1.00 13.16 ? 23   LYS J CA  1 
ATOM   10028 C  C   . LYS J  1 23  ? 58.571  99.103  33.461  1.00 13.47 ? 23   LYS J C   1 
ATOM   10029 O  O   . LYS J  1 23  ? 59.109  98.889  32.360  1.00 14.36 ? 23   LYS J O   1 
ATOM   10030 C  CB  . LYS J  1 23  ? 57.805  101.502 33.830  1.00 14.30 ? 23   LYS J CB  1 
ATOM   10031 C  CG  . LYS J  1 23  ? 56.593  102.461 33.792  1.00 18.13 ? 23   LYS J CG  1 
ATOM   10032 N  N   . GLU J  1 24  ? 58.995  98.551  34.593  1.00 14.79 ? 24   GLU J N   1 
ATOM   10033 C  CA  . GLU J  1 24  ? 60.147  97.647  34.644  1.00 15.87 ? 24   GLU J CA  1 
ATOM   10034 C  C   . GLU J  1 24  ? 59.763  96.514  35.576  1.00 15.63 ? 24   GLU J C   1 
ATOM   10035 O  O   . GLU J  1 24  ? 59.058  96.742  36.546  1.00 14.81 ? 24   GLU J O   1 
ATOM   10036 C  CB  . GLU J  1 24  ? 61.365  98.364  35.226  1.00 16.60 ? 24   GLU J CB  1 
ATOM   10037 C  CG  . GLU J  1 24  ? 61.858  99.536  34.388  1.00 20.82 ? 24   GLU J CG  1 
ATOM   10038 C  CD  . GLU J  1 24  ? 62.575  99.104  33.117  1.00 25.06 ? 24   GLU J CD  1 
ATOM   10039 O  OE1 . GLU J  1 24  ? 62.933  97.904  32.999  1.00 28.85 ? 24   GLU J OE1 1 
ATOM   10040 O  OE2 . GLU J  1 24  ? 62.780  99.965  32.227  1.00 27.73 ? 24   GLU J OE2 1 
ATOM   10041 N  N   . SER J  1 25  ? 60.239  95.307  35.305  1.00 15.22 ? 25   SER J N   1 
ATOM   10042 C  CA  . SER J  1 25  ? 59.819  94.169  36.117  1.00 15.76 ? 25   SER J CA  1 
ATOM   10043 C  C   . SER J  1 25  ? 60.235  94.236  37.573  1.00 16.35 ? 25   SER J C   1 
ATOM   10044 O  O   . SER J  1 25  ? 59.694  93.524  38.408  1.00 16.59 ? 25   SER J O   1 
ATOM   10045 C  CB  . SER J  1 25  ? 60.283  92.862  35.459  1.00 16.16 ? 25   SER J CB  1 
ATOM   10046 O  OG  . SER J  1 25  ? 61.656  92.945  35.149  1.00 14.07 ? 25   SER J OG  1 
ATOM   10047 N  N   . ASN J  1 26  ? 61.198  95.092  37.900  1.00 16.52 ? 26   ASN J N   1 
ATOM   10048 C  CA  . ASN J  1 26  ? 61.613  95.209  39.293  1.00 16.30 ? 26   ASN J CA  1 
ATOM   10049 C  C   . ASN J  1 26  ? 60.934  96.415  39.904  1.00 16.37 ? 26   ASN J C   1 
ATOM   10050 O  O   . ASN J  1 26  ? 61.171  96.763  41.075  1.00 17.69 ? 26   ASN J O   1 
ATOM   10051 C  CB  . ASN J  1 26  ? 63.123  95.396  39.383  1.00 16.83 ? 26   ASN J CB  1 
ATOM   10052 C  CG  . ASN J  1 26  ? 63.604  96.530  38.503  1.00 16.61 ? 26   ASN J CG  1 
ATOM   10053 O  OD1 . ASN J  1 26  ? 63.507  96.458  37.266  1.00 15.12 ? 26   ASN J OD1 1 
ATOM   10054 N  ND2 . ASN J  1 26  ? 64.079  97.605  39.131  1.00 15.55 ? 26   ASN J ND2 1 
ATOM   10055 N  N   . GLY J  1 27  ? 60.074  97.060  39.129  1.00 14.96 ? 27   GLY J N   1 
ATOM   10056 C  CA  . GLY J  1 27  ? 59.462  98.279  39.620  1.00 13.15 ? 27   GLY J CA  1 
ATOM   10057 C  C   . GLY J  1 27  ? 58.066  98.087  40.183  1.00 11.20 ? 27   GLY J C   1 
ATOM   10058 O  O   . GLY J  1 27  ? 57.468  97.015  40.068  1.00 9.94  ? 27   GLY J O   1 
ATOM   10059 N  N   . PRO J  1 28  ? 57.549  99.158  40.769  1.00 10.53 ? 28   PRO J N   1 
ATOM   10060 C  CA  . PRO J  1 28  ? 56.217  99.139  41.361  1.00 9.32  ? 28   PRO J CA  1 
ATOM   10061 C  C   . PRO J  1 28  ? 55.197  99.031  40.238  1.00 8.02  ? 28   PRO J C   1 
ATOM   10062 O  O   . PRO J  1 28  ? 55.452  99.353  39.066  1.00 8.29  ? 28   PRO J O   1 
ATOM   10063 C  CB  . PRO J  1 28  ? 56.079  100.510 42.012  1.00 10.17 ? 28   PRO J CB  1 
ATOM   10064 C  CG  . PRO J  1 28  ? 57.508  101.128 42.005  1.00 12.11 ? 28   PRO J CG  1 
ATOM   10065 C  CD  . PRO J  1 28  ? 58.219  100.471 40.873  1.00 11.58 ? 28   PRO J CD  1 
ATOM   10066 N  N   . VAL J  1 29  ? 54.038  98.562  40.615  1.00 7.18  ? 29   VAL J N   1 
ATOM   10067 C  CA  . VAL J  1 29  ? 52.922  98.458  39.718  1.00 6.25  ? 29   VAL J CA  1 
ATOM   10068 C  C   . VAL J  1 29  ? 51.972  99.567  40.135  1.00 6.69  ? 29   VAL J C   1 
ATOM   10069 O  O   . VAL J  1 29  ? 51.602  99.654  41.314  1.00 7.44  ? 29   VAL J O   1 
ATOM   10070 C  CB  . VAL J  1 29  ? 52.189  97.123  39.964  1.00 6.95  ? 29   VAL J CB  1 
ATOM   10071 C  CG1 . VAL J  1 29  ? 50.954  97.050  39.046  1.00 7.22  ? 29   VAL J CG1 1 
ATOM   10072 C  CG2 . VAL J  1 29  ? 53.106  95.927  39.647  1.00 6.84  ? 29   VAL J CG2 1 
ATOM   10073 N  N   . LYS J  1 30  ? 51.572  100.404 39.190  1.00 6.70  ? 30   LYS J N   1 
ATOM   10074 C  CA  . LYS J  1 30  ? 50.562  101.402 39.482  1.00 7.51  ? 30   LYS J CA  1 
ATOM   10075 C  C   . LYS J  1 30  ? 49.224  100.735 39.185  1.00 6.84  ? 30   LYS J C   1 
ATOM   10076 O  O   . LYS J  1 30  ? 49.077  100.080 38.150  1.00 5.89  ? 30   LYS J O   1 
ATOM   10077 C  CB  . LYS J  1 30  ? 50.737  102.618 38.579  1.00 9.10  ? 30   LYS J CB  1 
ATOM   10078 C  CG  . LYS J  1 30  ? 51.724  103.608 39.150  1.00 16.18 ? 30   LYS J CG  1 
ATOM   10079 C  CD  . LYS J  1 30  ? 52.423  104.409 38.063  1.00 21.71 ? 30   LYS J CD  1 
ATOM   10080 N  N   . VAL J  1 31  ? 48.269  100.945 40.099  1.00 5.53  ? 31   VAL J N   1 
ATOM   10081 C  CA  . VAL J  1 31  ? 46.948  100.374 40.028  1.00 5.22  ? 31   VAL J CA  1 
ATOM   10082 C  C   . VAL J  1 31  ? 45.957  101.513 40.115  1.00 5.70  ? 31   VAL J C   1 
ATOM   10083 O  O   . VAL J  1 31  ? 45.986  102.285 41.085  1.00 6.48  ? 31   VAL J O   1 
ATOM   10084 C  CB  . VAL J  1 31  ? 46.739  99.430  41.230  1.00 5.00  ? 31   VAL J CB  1 
ATOM   10085 C  CG1 . VAL J  1 31  ? 45.362  98.763  41.093  1.00 6.69  ? 31   VAL J CG1 1 
ATOM   10086 C  CG2 . VAL J  1 31  ? 47.844  98.357  41.255  1.00 5.00  ? 31   VAL J CG2 1 
ATOM   10087 N  N   . TRP J  1 32  ? 45.110  101.651 39.099  1.00 5.27  ? 32   TRP J N   1 
ATOM   10088 C  CA  . TRP J  1 32  ? 44.219  102.806 39.070  1.00 5.86  ? 32   TRP J CA  1 
ATOM   10089 C  C   . TRP J  1 32  ? 43.000  102.589 38.228  1.00 5.64  ? 32   TRP J C   1 
ATOM   10090 O  O   . TRP J  1 32  ? 43.036  101.875 37.229  1.00 5.00  ? 32   TRP J O   1 
ATOM   10091 C  CB  . TRP J  1 32  ? 44.954  104.058 38.611  1.00 5.51  ? 32   TRP J CB  1 
ATOM   10092 C  CG  . TRP J  1 32  ? 45.091  104.166 37.163  1.00 8.35  ? 32   TRP J CG  1 
ATOM   10093 C  CD1 . TRP J  1 32  ? 44.302  104.910 36.315  1.00 12.22 ? 32   TRP J CD1 1 
ATOM   10094 C  CD2 . TRP J  1 32  ? 46.056  103.518 36.349  1.00 9.49  ? 32   TRP J CD2 1 
ATOM   10095 N  NE1 . TRP J  1 32  ? 44.746  104.763 35.025  1.00 14.28 ? 32   TRP J NE1 1 
ATOM   10096 C  CE2 . TRP J  1 32  ? 45.819  103.913 35.020  1.00 11.47 ? 32   TRP J CE2 1 
ATOM   10097 C  CE3 . TRP J  1 32  ? 47.118  102.643 36.610  1.00 11.18 ? 32   TRP J CE3 1 
ATOM   10098 C  CZ2 . TRP J  1 32  ? 46.577  103.456 33.966  1.00 15.00 ? 32   TRP J CZ2 1 
ATOM   10099 C  CZ3 . TRP J  1 32  ? 47.864  102.182 35.555  1.00 10.83 ? 32   TRP J CZ3 1 
ATOM   10100 C  CH2 . TRP J  1 32  ? 47.596  102.599 34.250  1.00 13.85 ? 32   TRP J CH2 1 
ATOM   10101 N  N   . GLY J  1 33  ? 41.907  103.233 38.629  1.00 5.59  ? 33   GLY J N   1 
ATOM   10102 C  CA  . GLY J  1 33  ? 40.692  103.118 37.855  1.00 6.12  ? 33   GLY J CA  1 
ATOM   10103 C  C   . GLY J  1 33  ? 39.527  103.593 38.685  1.00 7.64  ? 33   GLY J C   1 
ATOM   10104 O  O   . GLY J  1 33  ? 39.702  104.292 39.681  1.00 7.41  ? 33   GLY J O   1 
ATOM   10105 N  N   . SER J  1 34  ? 38.331  103.249 38.263  1.00 7.16  ? 34   SER J N   1 
ATOM   10106 C  CA  . SER J  1 34  ? 37.142  103.750 38.925  1.00 7.86  ? 34   SER J CA  1 
ATOM   10107 C  C   . SER J  1 34  ? 36.217  102.581 39.233  1.00 8.48  ? 34   SER J C   1 
ATOM   10108 O  O   . SER J  1 34  ? 36.020  101.721 38.369  1.00 9.44  ? 34   SER J O   1 
ATOM   10109 C  CB  . SER J  1 34  ? 36.440  104.721 37.952  1.00 8.78  ? 34   SER J CB  1 
ATOM   10110 O  OG  . SER J  1 34  ? 35.371  105.347 38.594  1.00 13.24 ? 34   SER J OG  1 
ATOM   10111 N  N   . ILE J  1 35  ? 35.654  102.533 40.434  1.00 6.96  ? 35   ILE J N   1 
ATOM   10112 C  CA  . ILE J  1 35  ? 34.680  101.503 40.757  1.00 6.61  ? 35   ILE J CA  1 
ATOM   10113 C  C   . ILE J  1 35  ? 33.467  102.287 41.209  1.00 7.19  ? 35   ILE J C   1 
ATOM   10114 O  O   . ILE J  1 35  ? 33.583  103.177 42.067  1.00 7.14  ? 35   ILE J O   1 
ATOM   10115 C  CB  . ILE J  1 35  ? 35.167  100.601 41.900  1.00 7.12  ? 35   ILE J CB  1 
ATOM   10116 C  CG1 . ILE J  1 35  ? 36.549  100.014 41.550  1.00 7.53  ? 35   ILE J CG1 1 
ATOM   10117 C  CG2 . ILE J  1 35  ? 34.143  99.495  42.240  1.00 5.00  ? 35   ILE J CG2 1 
ATOM   10118 C  CD1 . ILE J  1 35  ? 37.269  99.327  42.727  1.00 9.70  ? 35   ILE J CD1 1 
ATOM   10119 N  N   . LYS J  1 36  ? 32.323  102.002 40.604  1.00 7.10  ? 36   LYS J N   1 
ATOM   10120 C  CA  . LYS J  1 36  ? 31.106  102.682 41.001  1.00 9.96  ? 36   LYS J CA  1 
ATOM   10121 C  C   . LYS J  1 36  ? 30.160  101.777 41.763  1.00 8.40  ? 36   LYS J C   1 
ATOM   10122 O  O   . LYS J  1 36  ? 30.294  100.568 41.750  1.00 8.54  ? 36   LYS J O   1 
ATOM   10123 C  CB  . LYS J  1 36  ? 30.394  103.170 39.734  1.00 11.48 ? 36   LYS J CB  1 
ATOM   10124 C  CG  . LYS J  1 36  ? 31.033  104.412 39.101  1.00 19.09 ? 36   LYS J CG  1 
ATOM   10125 C  CD  . LYS J  1 36  ? 32.213  104.116 38.154  1.00 25.79 ? 36   LYS J CD  1 
ATOM   10126 C  CE  . LYS J  1 36  ? 32.533  105.369 37.318  1.00 29.05 ? 36   LYS J CE  1 
ATOM   10127 N  NZ  . LYS J  1 36  ? 33.306  105.043 36.069  1.00 32.88 ? 36   LYS J NZ  1 
ATOM   10128 N  N   . GLY J  1 37  ? 29.134  102.368 42.380  1.00 8.88  ? 37   GLY J N   1 
ATOM   10129 C  CA  . GLY J  1 37  ? 28.103  101.591 43.046  1.00 8.04  ? 37   GLY J CA  1 
ATOM   10130 C  C   . GLY J  1 37  ? 28.391  101.123 44.457  1.00 8.52  ? 37   GLY J C   1 
ATOM   10131 O  O   . GLY J  1 37  ? 27.616  100.337 45.024  1.00 9.08  ? 37   GLY J O   1 
ATOM   10132 N  N   . LEU J  1 38  ? 29.478  101.615 45.044  1.00 7.51  ? 38   LEU J N   1 
ATOM   10133 C  CA  . LEU J  1 38  ? 29.856  101.230 46.389  1.00 7.75  ? 38   LEU J CA  1 
ATOM   10134 C  C   . LEU J  1 38  ? 29.181  102.107 47.455  1.00 8.46  ? 38   LEU J C   1 
ATOM   10135 O  O   . LEU J  1 38  ? 28.762  103.228 47.174  1.00 9.69  ? 38   LEU J O   1 
ATOM   10136 C  CB  . LEU J  1 38  ? 31.376  101.395 46.555  1.00 7.36  ? 38   LEU J CB  1 
ATOM   10137 C  CG  . LEU J  1 38  ? 32.238  100.413 45.720  1.00 6.72  ? 38   LEU J CG  1 
ATOM   10138 C  CD1 . LEU J  1 38  ? 33.682  100.934 45.576  1.00 7.41  ? 38   LEU J CD1 1 
ATOM   10139 C  CD2 . LEU J  1 38  ? 32.290  99.052  46.409  1.00 5.00  ? 38   LEU J CD2 1 
ATOM   10140 N  N   . THR J  1 39  ? 29.129  101.605 48.681  1.00 8.43  ? 39   THR J N   1 
ATOM   10141 C  CA  . THR J  1 39  ? 28.763  102.458 49.818  1.00 9.66  ? 39   THR J CA  1 
ATOM   10142 C  C   . THR J  1 39  ? 29.963  103.365 50.150  1.00 10.11 ? 39   THR J C   1 
ATOM   10143 O  O   . THR J  1 39  ? 31.146  102.998 49.950  1.00 8.84  ? 39   THR J O   1 
ATOM   10144 C  CB  . THR J  1 39  ? 28.459  101.623 51.052  1.00 9.25  ? 39   THR J CB  1 
ATOM   10145 O  OG1 . THR J  1 39  ? 29.572  100.754 51.328  1.00 10.58 ? 39   THR J OG1 1 
ATOM   10146 C  CG2 . THR J  1 39  ? 27.236  100.683 50.830  1.00 11.15 ? 39   THR J CG2 1 
ATOM   10147 N  N   . GLU J  1 40  ? 29.667  104.528 50.728  1.00 9.59  ? 40   GLU J N   1 
ATOM   10148 C  CA  . GLU J  1 40  ? 30.701  105.485 51.067  1.00 9.40  ? 40   GLU J CA  1 
ATOM   10149 C  C   . GLU J  1 40  ? 31.610  104.860 52.101  1.00 9.37  ? 40   GLU J C   1 
ATOM   10150 O  O   . GLU J  1 40  ? 31.127  104.223 53.037  1.00 10.32 ? 40   GLU J O   1 
ATOM   10151 C  CB  . GLU J  1 40  ? 30.060  106.745 51.682  1.00 10.41 ? 40   GLU J CB  1 
ATOM   10152 C  CG  . GLU J  1 40  ? 31.044  107.881 51.927  1.00 11.83 ? 40   GLU J CG  1 
ATOM   10153 C  CD  . GLU J  1 40  ? 30.401  109.073 52.627  1.00 18.18 ? 40   GLU J CD  1 
ATOM   10154 O  OE1 . GLU J  1 40  ? 29.343  108.899 53.265  1.00 16.75 ? 40   GLU J OE1 1 
ATOM   10155 O  OE2 . GLU J  1 40  ? 30.964  110.184 52.536  1.00 18.95 ? 40   GLU J OE2 1 
ATOM   10156 N  N   . GLY J  1 41  ? 32.920  105.029 51.931  1.00 7.90  ? 41   GLY J N   1 
ATOM   10157 C  CA  . GLY J  1 41  ? 33.867  104.561 52.928  1.00 7.84  ? 41   GLY J CA  1 
ATOM   10158 C  C   . GLY J  1 41  ? 34.877  103.536 52.405  1.00 8.49  ? 41   GLY J C   1 
ATOM   10159 O  O   . GLY J  1 41  ? 35.054  103.377 51.206  1.00 8.50  ? 41   GLY J O   1 
ATOM   10160 N  N   . LEU J  1 42  ? 35.489  102.806 53.331  1.00 8.11  ? 42   LEU J N   1 
ATOM   10161 C  CA  . LEU J  1 42  ? 36.545  101.850 53.009  1.00 8.92  ? 42   LEU J CA  1 
ATOM   10162 C  C   . LEU J  1 42  ? 36.047  100.492 52.528  1.00 7.36  ? 42   LEU J C   1 
ATOM   10163 O  O   . LEU J  1 42  ? 35.074  99.940  53.073  1.00 7.79  ? 42   LEU J O   1 
ATOM   10164 C  CB  . LEU J  1 42  ? 37.403  101.623 54.276  1.00 9.98  ? 42   LEU J CB  1 
ATOM   10165 C  CG  . LEU J  1 42  ? 38.170  102.826 54.805  1.00 12.28 ? 42   LEU J CG  1 
ATOM   10166 C  CD1 . LEU J  1 42  ? 38.907  102.435 56.088  1.00 14.33 ? 42   LEU J CD1 1 
ATOM   10167 C  CD2 . LEU J  1 42  ? 39.169  103.296 53.769  1.00 13.80 ? 42   LEU J CD2 1 
ATOM   10168 N  N   . HIS J  1 43  ? 36.731  99.925  51.526  1.00 5.92  ? 43   HIS J N   1 
ATOM   10169 C  CA  . HIS J  1 43  ? 36.409  98.606  50.992  1.00 5.00  ? 43   HIS J CA  1 
ATOM   10170 C  C   . HIS J  1 43  ? 37.690  97.821  50.713  1.00 5.08  ? 43   HIS J C   1 
ATOM   10171 O  O   . HIS J  1 43  ? 38.591  98.323  50.014  1.00 5.00  ? 43   HIS J O   1 
ATOM   10172 C  CB  . HIS J  1 43  ? 35.633  98.773  49.662  1.00 5.00  ? 43   HIS J CB  1 
ATOM   10173 C  CG  . HIS J  1 43  ? 34.269  99.382  49.866  1.00 6.03  ? 43   HIS J CG  1 
ATOM   10174 N  ND1 . HIS J  1 43  ? 33.170  98.626  50.203  1.00 7.28  ? 43   HIS J ND1 1 
ATOM   10175 C  CD2 . HIS J  1 43  ? 33.859  100.673 49.862  1.00 6.26  ? 43   HIS J CD2 1 
ATOM   10176 C  CE1 . HIS J  1 43  ? 32.121  99.426  50.379  1.00 6.76  ? 43   HIS J CE1 1 
ATOM   10177 N  NE2 . HIS J  1 43  ? 32.516  100.673 50.162  1.00 6.85  ? 43   HIS J NE2 1 
ATOM   10178 N  N   . GLY J  1 44  ? 37.755  96.597  51.234  1.00 5.00  ? 44   GLY J N   1 
ATOM   10179 C  CA  . GLY J  1 44  ? 38.943  95.778  51.052  1.00 5.00  ? 44   GLY J CA  1 
ATOM   10180 C  C   . GLY J  1 44  ? 39.171  95.541  49.556  1.00 5.01  ? 44   GLY J C   1 
ATOM   10181 O  O   . GLY J  1 44  ? 38.211  95.456  48.777  1.00 5.00  ? 44   GLY J O   1 
ATOM   10182 N  N   . PHE J  1 45  ? 40.434  95.406  49.160  1.00 5.00  ? 45   PHE J N   1 
ATOM   10183 C  CA  . PHE J  1 45  ? 40.753  95.383  47.729  1.00 5.00  ? 45   PHE J CA  1 
ATOM   10184 C  C   . PHE J  1 45  ? 41.914  94.437  47.595  1.00 5.00  ? 45   PHE J C   1 
ATOM   10185 O  O   . PHE J  1 45  ? 43.010  94.744  48.049  1.00 5.10  ? 45   PHE J O   1 
ATOM   10186 C  CB  . PHE J  1 45  ? 41.154  96.815  47.352  1.00 5.00  ? 45   PHE J CB  1 
ATOM   10187 C  CG  . PHE J  1 45  ? 41.371  97.066  45.870  1.00 5.20  ? 45   PHE J CG  1 
ATOM   10188 C  CD1 . PHE J  1 45  ? 40.336  96.913  44.951  1.00 5.97  ? 45   PHE J CD1 1 
ATOM   10189 C  CD2 . PHE J  1 45  ? 42.601  97.510  45.428  1.00 5.00  ? 45   PHE J CD2 1 
ATOM   10190 C  CE1 . PHE J  1 45  ? 40.518  97.207  43.597  1.00 6.35  ? 45   PHE J CE1 1 
ATOM   10191 C  CE2 . PHE J  1 45  ? 42.790  97.827  44.070  1.00 7.19  ? 45   PHE J CE2 1 
ATOM   10192 C  CZ  . PHE J  1 45  ? 41.768  97.652  43.168  1.00 6.38  ? 45   PHE J CZ  1 
ATOM   10193 N  N   . HIS J  1 46  ? 41.704  93.270  47.000  1.00 5.00  ? 46   HIS J N   1 
ATOM   10194 C  CA  . HIS J  1 46  ? 42.757  92.271  47.032  1.00 5.00  ? 46   HIS J CA  1 
ATOM   10195 C  C   . HIS J  1 46  ? 42.894  91.479  45.728  1.00 5.00  ? 46   HIS J C   1 
ATOM   10196 O  O   . HIS J  1 46  ? 41.912  91.294  44.998  1.00 5.00  ? 46   HIS J O   1 
ATOM   10197 C  CB  . HIS J  1 46  ? 42.441  91.173  48.081  1.00 5.00  ? 46   HIS J CB  1 
ATOM   10198 C  CG  . HIS J  1 46  ? 42.012  91.697  49.420  1.00 5.00  ? 46   HIS J CG  1 
ATOM   10199 N  ND1 . HIS J  1 46  ? 40.840  91.322  50.034  1.00 5.00  ? 46   HIS J ND1 1 
ATOM   10200 C  CD2 . HIS J  1 46  ? 42.611  92.573  50.267  1.00 5.62  ? 46   HIS J CD2 1 
ATOM   10201 C  CE1 . HIS J  1 46  ? 40.717  91.939  51.191  1.00 5.00  ? 46   HIS J CE1 1 
ATOM   10202 N  NE2 . HIS J  1 46  ? 41.782  92.702  51.366  1.00 5.00  ? 46   HIS J NE2 1 
ATOM   10203 N  N   . VAL J  1 47  ? 44.087  90.919  45.539  1.00 5.00  ? 47   VAL J N   1 
ATOM   10204 C  CA  . VAL J  1 47  ? 44.302  89.949  44.480  1.00 5.00  ? 47   VAL J CA  1 
ATOM   10205 C  C   . VAL J  1 47  ? 44.126  88.547  45.090  1.00 5.00  ? 47   VAL J C   1 
ATOM   10206 O  O   . VAL J  1 47  ? 44.831  88.180  46.043  1.00 5.00  ? 47   VAL J O   1 
ATOM   10207 C  CB  . VAL J  1 47  ? 45.636  90.079  43.801  1.00 5.00  ? 47   VAL J CB  1 
ATOM   10208 C  CG1 . VAL J  1 47  ? 45.704  88.974  42.704  1.00 5.00  ? 47   VAL J CG1 1 
ATOM   10209 C  CG2 . VAL J  1 47  ? 45.806  91.516  43.193  1.00 5.00  ? 47   VAL J CG2 1 
ATOM   10210 N  N   . HIS J  1 48  ? 43.150  87.801  44.566  1.00 5.00  ? 48   HIS J N   1 
ATOM   10211 C  CA  . HIS J  1 48  ? 42.852  86.456  45.064  1.00 5.00  ? 48   HIS J CA  1 
ATOM   10212 C  C   . HIS J  1 48  ? 43.532  85.481  44.124  1.00 5.33  ? 48   HIS J C   1 
ATOM   10213 O  O   . HIS J  1 48  ? 43.876  85.834  43.015  1.00 5.00  ? 48   HIS J O   1 
ATOM   10214 C  CB  . HIS J  1 48  ? 41.335  86.205  45.156  1.00 5.00  ? 48   HIS J CB  1 
ATOM   10215 C  CG  . HIS J  1 48  ? 40.700  86.858  46.347  1.00 5.00  ? 48   HIS J CG  1 
ATOM   10216 N  ND1 . HIS J  1 48  ? 40.037  86.150  47.334  1.00 5.60  ? 48   HIS J ND1 1 
ATOM   10217 C  CD2 . HIS J  1 48  ? 40.580  88.163  46.682  1.00 5.00  ? 48   HIS J CD2 1 
ATOM   10218 C  CE1 . HIS J  1 48  ? 39.592  86.985  48.258  1.00 5.00  ? 48   HIS J CE1 1 
ATOM   10219 N  NE2 . HIS J  1 48  ? 39.901  88.208  47.880  1.00 5.00  ? 48   HIS J NE2 1 
ATOM   10220 N  N   . GLU J  1 49  ? 43.774  84.279  44.620  1.00 5.00  ? 49   GLU J N   1 
ATOM   10221 C  CA  . GLU J  1 49  ? 44.703  83.370  43.977  1.00 5.00  ? 49   GLU J CA  1 
ATOM   10222 C  C   . GLU J  1 49  ? 44.303  82.894  42.571  1.00 5.29  ? 49   GLU J C   1 
ATOM   10223 O  O   . GLU J  1 49  ? 45.161  82.774  41.677  1.00 5.30  ? 49   GLU J O   1 
ATOM   10224 C  CB  . GLU J  1 49  ? 44.828  82.131  44.888  1.00 5.27  ? 49   GLU J CB  1 
ATOM   10225 C  CG  . GLU J  1 49  ? 45.908  81.171  44.412  1.00 7.17  ? 49   GLU J CG  1 
ATOM   10226 C  CD  . GLU J  1 49  ? 46.117  80.016  45.372  1.00 10.90 ? 49   GLU J CD  1 
ATOM   10227 O  OE1 . GLU J  1 49  ? 45.389  79.928  46.396  1.00 9.13  ? 49   GLU J OE1 1 
ATOM   10228 O  OE2 . GLU J  1 49  ? 46.996  79.189  45.058  1.00 11.19 ? 49   GLU J OE2 1 
ATOM   10229 N  N   . PHE J  1 50  ? 43.025  82.570  42.396  1.00 5.00  ? 50   PHE J N   1 
ATOM   10230 C  CA  . PHE J  1 50  ? 42.610  81.910  41.136  1.00 5.00  ? 50   PHE J CA  1 
ATOM   10231 C  C   . PHE J  1 50  ? 41.753  82.808  40.241  1.00 5.25  ? 50   PHE J C   1 
ATOM   10232 O  O   . PHE J  1 50  ? 40.851  83.471  40.738  1.00 5.00  ? 50   PHE J O   1 
ATOM   10233 C  CB  . PHE J  1 50  ? 41.815  80.622  41.430  1.00 5.00  ? 50   PHE J CB  1 
ATOM   10234 C  CG  . PHE J  1 50  ? 42.605  79.629  42.273  1.00 6.63  ? 50   PHE J CG  1 
ATOM   10235 C  CD1 . PHE J  1 50  ? 43.769  79.055  41.756  1.00 7.72  ? 50   PHE J CD1 1 
ATOM   10236 C  CD2 . PHE J  1 50  ? 42.218  79.336  43.565  1.00 10.06 ? 50   PHE J CD2 1 
ATOM   10237 C  CE1 . PHE J  1 50  ? 44.532  78.147  42.536  1.00 11.20 ? 50   PHE J CE1 1 
ATOM   10238 C  CE2 . PHE J  1 50  ? 42.980  78.433  44.340  1.00 10.16 ? 50   PHE J CE2 1 
ATOM   10239 C  CZ  . PHE J  1 50  ? 44.132  77.854  43.804  1.00 11.56 ? 50   PHE J CZ  1 
ATOM   10240 N  N   . GLY J  1 51  ? 42.081  82.816  38.936  1.00 5.00  ? 51   GLY J N   1 
ATOM   10241 C  CA  . GLY J  1 51  ? 41.309  83.536  37.919  1.00 5.00  ? 51   GLY J CA  1 
ATOM   10242 C  C   . GLY J  1 51  ? 40.131  82.642  37.513  1.00 5.00  ? 51   GLY J C   1 
ATOM   10243 O  O   . GLY J  1 51  ? 39.890  82.423  36.337  1.00 6.49  ? 51   GLY J O   1 
ATOM   10244 N  N   . ASP J  1 52  ? 39.395  82.129  38.502  1.00 5.00  ? 52   ASP J N   1 
ATOM   10245 C  CA  . ASP J  1 52  ? 38.307  81.192  38.280  1.00 5.00  ? 52   ASP J CA  1 
ATOM   10246 C  C   . ASP J  1 52  ? 36.994  81.818  38.738  1.00 5.60  ? 52   ASP J C   1 
ATOM   10247 O  O   . ASP J  1 52  ? 36.792  82.053  39.946  1.00 5.49  ? 52   ASP J O   1 
ATOM   10248 C  CB  . ASP J  1 52  ? 38.593  79.954  39.138  1.00 5.00  ? 52   ASP J CB  1 
ATOM   10249 C  CG  . ASP J  1 52  ? 37.565  78.868  38.973  1.00 6.63  ? 52   ASP J CG  1 
ATOM   10250 O  OD1 . ASP J  1 52  ? 36.392  79.144  38.575  1.00 5.81  ? 52   ASP J OD1 1 
ATOM   10251 O  OD2 . ASP J  1 52  ? 37.844  77.675  39.271  1.00 7.06  ? 52   ASP J OD2 1 
ATOM   10252 N  N   . ASN J  1 53  ? 36.112  82.098  37.781  1.00 6.90  ? 53   ASN J N   1 
ATOM   10253 C  CA  . ASN J  1 53  ? 34.849  82.765  38.075  1.00 7.43  ? 53   ASN J CA  1 
ATOM   10254 C  C   . ASN J  1 53  ? 33.694  81.826  37.821  1.00 6.88  ? 53   ASN J C   1 
ATOM   10255 O  O   . ASN J  1 53  ? 32.560  82.277  37.636  1.00 7.64  ? 53   ASN J O   1 
ATOM   10256 C  CB  . ASN J  1 53  ? 34.702  84.008  37.183  1.00 10.07 ? 53   ASN J CB  1 
ATOM   10257 C  CG  . ASN J  1 53  ? 33.593  84.948  37.640  1.00 14.34 ? 53   ASN J CG  1 
ATOM   10258 O  OD1 . ASN J  1 53  ? 32.736  85.388  36.825  1.00 22.34 ? 53   ASN J OD1 1 
ATOM   10259 N  ND2 . ASN J  1 53  ? 33.597  85.275  38.920  1.00 15.31 ? 53   ASN J ND2 1 
ATOM   10260 N  N   . THR J  1 54  ? 33.953  80.520  37.787  1.00 6.54  ? 54   THR J N   1 
ATOM   10261 C  CA  . THR J  1 54  ? 32.893  79.560  37.499  1.00 6.81  ? 54   THR J CA  1 
ATOM   10262 C  C   . THR J  1 54  ? 31.765  79.614  38.525  1.00 9.45  ? 54   THR J C   1 
ATOM   10263 O  O   . THR J  1 54  ? 30.624  79.276  38.195  1.00 10.70 ? 54   THR J O   1 
ATOM   10264 C  CB  . THR J  1 54  ? 33.405  78.107  37.446  1.00 7.24  ? 54   THR J CB  1 
ATOM   10265 O  OG1 . THR J  1 54  ? 34.097  77.801  38.647  1.00 6.06  ? 54   THR J OG1 1 
ATOM   10266 C  CG2 . THR J  1 54  ? 34.438  77.929  36.381  1.00 8.80  ? 54   THR J CG2 1 
ATOM   10267 N  N   . ALA J  1 55  ? 32.083  79.951  39.762  1.00 8.65  ? 55   ALA J N   1 
ATOM   10268 C  CA  . ALA J  1 55  ? 31.022  80.108  40.767  1.00 11.22 ? 55   ALA J CA  1 
ATOM   10269 C  C   . ALA J  1 55  ? 30.992  81.539  41.253  1.00 10.97 ? 55   ALA J C   1 
ATOM   10270 O  O   . ALA J  1 55  ? 30.859  81.804  42.491  1.00 13.19 ? 55   ALA J O   1 
ATOM   10271 C  CB  . ALA J  1 55  ? 31.232  79.159  41.938  1.00 11.83 ? 55   ALA J CB  1 
ATOM   10272 N  N   . GLY J  1 56  ? 31.140  82.476  40.314  1.00 9.08  ? 56   GLY J N   1 
ATOM   10273 C  CA  . GLY J  1 56  ? 31.217  83.874  40.675  1.00 8.60  ? 56   GLY J CA  1 
ATOM   10274 C  C   . GLY J  1 56  ? 32.515  84.162  41.430  1.00 7.72  ? 56   GLY J C   1 
ATOM   10275 O  O   . GLY J  1 56  ? 33.494  83.407  41.301  1.00 9.23  ? 56   GLY J O   1 
ATOM   10276 N  N   . CYS J  1 57  ? 32.520  85.192  42.271  1.00 7.32  ? 57   CYS J N   1 
ATOM   10277 C  CA  . CYS J  1 57  ? 33.751  85.599  42.949  1.00 8.04  ? 57   CYS J CA  1 
ATOM   10278 C  C   . CYS J  1 57  ? 34.189  84.567  43.979  1.00 8.00  ? 57   CYS J C   1 
ATOM   10279 O  O   . CYS J  1 57  ? 35.345  84.534  44.375  1.00 6.35  ? 57   CYS J O   1 
ATOM   10280 C  CB  . CYS J  1 57  ? 33.565  86.964  43.627  1.00 9.09  ? 57   CYS J CB  1 
ATOM   10281 S  SG  . CYS J  1 57  ? 33.116  88.265  42.416  1.00 14.38 ? 57   CYS J SG  1 
ATOM   10282 N  N   . THR J  1 58  ? 33.264  83.713  44.408  1.00 7.48  ? 58   THR J N   1 
ATOM   10283 C  CA  . THR J  1 58  ? 33.613  82.681  45.377  1.00 8.54  ? 58   THR J CA  1 
ATOM   10284 C  C   . THR J  1 58  ? 34.710  81.741  44.900  1.00 8.45  ? 58   THR J C   1 
ATOM   10285 O  O   . THR J  1 58  ? 35.562  81.310  45.670  1.00 7.56  ? 58   THR J O   1 
ATOM   10286 C  CB  . THR J  1 58  ? 32.336  81.884  45.755  1.00 10.25 ? 58   THR J CB  1 
ATOM   10287 O  OG1 . THR J  1 58  ? 31.430  82.812  46.365  1.00 14.09 ? 58   THR J OG1 1 
ATOM   10288 C  CG2 . THR J  1 58  ? 32.642  80.946  46.900  1.00 11.30 ? 58   THR J CG2 1 
ATOM   10289 N  N   . SER J  1 59  ? 34.718  81.415  43.618  1.00 6.18  ? 59   SER J N   1 
ATOM   10290 C  CA  . SER J  1 59  ? 35.724  80.466  43.161  1.00 7.11  ? 59   SER J CA  1 
ATOM   10291 C  C   . SER J  1 59  ? 37.138  81.027  42.951  1.00 6.97  ? 59   SER J C   1 
ATOM   10292 O  O   . SER J  1 59  ? 38.040  80.266  42.598  1.00 6.66  ? 59   SER J O   1 
ATOM   10293 C  CB  . SER J  1 59  ? 35.231  79.731  41.926  1.00 9.05  ? 59   SER J CB  1 
ATOM   10294 O  OG  . SER J  1 59  ? 34.584  80.626  41.065  1.00 10.96 ? 59   SER J OG  1 
ATOM   10295 N  N   . ALA J  1 60  ? 37.342  82.325  43.199  1.00 5.00  ? 60   ALA J N   1 
ATOM   10296 C  CA  . ALA J  1 60  ? 38.671  82.917  43.077  1.00 5.00  ? 60   ALA J CA  1 
ATOM   10297 C  C   . ALA J  1 60  ? 39.574  82.417  44.208  1.00 5.19  ? 60   ALA J C   1 
ATOM   10298 O  O   . ALA J  1 60  ? 40.790  82.687  44.244  1.00 5.13  ? 60   ALA J O   1 
ATOM   10299 C  CB  . ALA J  1 60  ? 38.581  84.493  43.115  1.00 6.22  ? 60   ALA J CB  1 
ATOM   10300 N  N   . GLY J  1 61  ? 38.989  81.735  45.178  1.00 5.00  ? 61   GLY J N   1 
ATOM   10301 C  CA  . GLY J  1 61  ? 39.807  81.258  46.292  1.00 5.82  ? 61   GLY J CA  1 
ATOM   10302 C  C   . GLY J  1 61  ? 40.230  82.368  47.281  1.00 5.00  ? 61   GLY J C   1 
ATOM   10303 O  O   . GLY J  1 61  ? 39.675  83.461  47.321  1.00 6.01  ? 61   GLY J O   1 
ATOM   10304 N  N   . PRO J  1 62  ? 41.259  82.087  48.063  1.00 5.00  ? 62   PRO J N   1 
ATOM   10305 C  CA  . PRO J  1 62  ? 41.733  83.014  49.093  1.00 5.58  ? 62   PRO J CA  1 
ATOM   10306 C  C   . PRO J  1 62  ? 42.710  84.041  48.530  1.00 5.87  ? 62   PRO J C   1 
ATOM   10307 O  O   . PRO J  1 62  ? 42.934  84.114  47.299  1.00 5.00  ? 62   PRO J O   1 
ATOM   10308 C  CB  . PRO J  1 62  ? 42.435  82.065  50.071  1.00 6.11  ? 62   PRO J CB  1 
ATOM   10309 C  CG  . PRO J  1 62  ? 43.089  81.064  49.161  1.00 7.65  ? 62   PRO J CG  1 
ATOM   10310 C  CD  . PRO J  1 62  ? 42.085  80.872  47.979  1.00 5.00  ? 62   PRO J CD  1 
ATOM   10311 N  N   . HIS J  1 63  ? 43.344  84.804  49.398  1.00 5.00  ? 63   HIS J N   1 
ATOM   10312 C  CA  . HIS J  1 63  ? 44.269  85.810  48.864  1.00 5.00  ? 63   HIS J CA  1 
ATOM   10313 C  C   . HIS J  1 63  ? 45.496  85.155  48.250  1.00 5.47  ? 63   HIS J C   1 
ATOM   10314 O  O   . HIS J  1 63  ? 45.982  84.133  48.738  1.00 6.53  ? 63   HIS J O   1 
ATOM   10315 C  CB  . HIS J  1 63  ? 44.697  86.735  50.014  1.00 5.76  ? 63   HIS J CB  1 
ATOM   10316 C  CG  . HIS J  1 63  ? 43.574  87.549  50.547  1.00 6.83  ? 63   HIS J CG  1 
ATOM   10317 N  ND1 . HIS J  1 63  ? 43.690  88.366  51.647  1.00 7.78  ? 63   HIS J ND1 1 
ATOM   10318 C  CD2 . HIS J  1 63  ? 42.320  87.731  50.066  1.00 10.66 ? 63   HIS J CD2 1 
ATOM   10319 C  CE1 . HIS J  1 63  ? 42.533  88.971  51.853  1.00 7.95  ? 63   HIS J CE1 1 
ATOM   10320 N  NE2 . HIS J  1 63  ? 41.691  88.606  50.904  1.00 13.72 ? 63   HIS J NE2 1 
ATOM   10321 N  N   . PHE J  1 64  ? 45.990  85.734  47.163  1.00 5.00  ? 64   PHE J N   1 
ATOM   10322 C  CA  . PHE J  1 64  ? 47.203  85.280  46.510  1.00 5.00  ? 64   PHE J CA  1 
ATOM   10323 C  C   . PHE J  1 64  ? 48.334  85.404  47.521  1.00 5.00  ? 64   PHE J C   1 
ATOM   10324 O  O   . PHE J  1 64  ? 48.645  86.487  47.987  1.00 5.00  ? 64   PHE J O   1 
ATOM   10325 C  CB  . PHE J  1 64  ? 47.471  86.154  45.273  1.00 5.00  ? 64   PHE J CB  1 
ATOM   10326 C  CG  . PHE J  1 64  ? 48.750  85.761  44.503  1.00 5.00  ? 64   PHE J CG  1 
ATOM   10327 C  CD1 . PHE J  1 64  ? 49.072  84.424  44.293  1.00 5.08  ? 64   PHE J CD1 1 
ATOM   10328 C  CD2 . PHE J  1 64  ? 49.597  86.742  44.005  1.00 5.06  ? 64   PHE J CD2 1 
ATOM   10329 C  CE1 . PHE J  1 64  ? 50.236  84.080  43.561  1.00 7.84  ? 64   PHE J CE1 1 
ATOM   10330 C  CE2 . PHE J  1 64  ? 50.748  86.404  43.292  1.00 5.13  ? 64   PHE J CE2 1 
ATOM   10331 C  CZ  . PHE J  1 64  ? 51.065  85.073  43.095  1.00 5.57  ? 64   PHE J CZ  1 
ATOM   10332 N  N   . ASN J  1 65  ? 48.944  84.267  47.833  1.00 6.23  ? 65   ASN J N   1 
ATOM   10333 C  CA  . ASN J  1 65  ? 49.869  84.202  48.963  1.00 7.14  ? 65   ASN J CA  1 
ATOM   10334 C  C   . ASN J  1 65  ? 50.950  83.163  48.692  1.00 8.24  ? 65   ASN J C   1 
ATOM   10335 O  O   . ASN J  1 65  ? 51.066  82.185  49.442  1.00 7.68  ? 65   ASN J O   1 
ATOM   10336 C  CB  . ASN J  1 65  ? 49.070  83.748  50.195  1.00 7.95  ? 65   ASN J CB  1 
ATOM   10337 C  CG  . ASN J  1 65  ? 49.877  83.786  51.495  1.00 7.31  ? 65   ASN J CG  1 
ATOM   10338 O  OD1 . ASN J  1 65  ? 50.830  84.530  51.617  1.00 9.98  ? 65   ASN J OD1 1 
ATOM   10339 N  ND2 . ASN J  1 65  ? 49.429  83.015  52.497  1.00 7.65  ? 65   ASN J ND2 1 
ATOM   10340 N  N   . PRO J  1 66  ? 51.786  83.381  47.678  1.00 8.42  ? 66   PRO J N   1 
ATOM   10341 C  CA  . PRO J  1 66  ? 52.803  82.379  47.330  1.00 10.44 ? 66   PRO J CA  1 
ATOM   10342 C  C   . PRO J  1 66  ? 53.882  82.306  48.419  1.00 11.18 ? 66   PRO J C   1 
ATOM   10343 O  O   . PRO J  1 66  ? 54.663  81.354  48.406  1.00 11.27 ? 66   PRO J O   1 
ATOM   10344 C  CB  . PRO J  1 66  ? 53.392  82.942  46.026  1.00 9.20  ? 66   PRO J CB  1 
ATOM   10345 C  CG  . PRO J  1 66  ? 53.243  84.443  46.236  1.00 9.62  ? 66   PRO J CG  1 
ATOM   10346 C  CD  . PRO J  1 66  ? 51.854  84.550  46.782  1.00 9.94  ? 66   PRO J CD  1 
ATOM   10347 N  N   . LEU J  1 67  ? 53.936  83.269  49.340  1.00 11.93 ? 67   LEU J N   1 
ATOM   10348 C  CA  . LEU J  1 67  ? 54.976  83.217  50.385  1.00 12.70 ? 67   LEU J CA  1 
ATOM   10349 C  C   . LEU J  1 67  ? 54.467  82.625  51.689  1.00 12.92 ? 67   LEU J C   1 
ATOM   10350 O  O   . LEU J  1 67  ? 55.204  82.562  52.659  1.00 13.70 ? 67   LEU J O   1 
ATOM   10351 C  CB  . LEU J  1 67  ? 55.658  84.583  50.588  1.00 13.64 ? 67   LEU J CB  1 
ATOM   10352 C  CG  . LEU J  1 67  ? 56.482  85.006  49.359  1.00 13.80 ? 67   LEU J CG  1 
ATOM   10353 C  CD1 . LEU J  1 67  ? 57.113  86.397  49.461  1.00 17.67 ? 67   LEU J CD1 1 
ATOM   10354 C  CD2 . LEU J  1 67  ? 57.552  83.965  49.081  1.00 20.19 ? 67   LEU J CD2 1 
ATOM   10355 N  N   . SER J  1 68  ? 53.218  82.167  51.696  1.00 12.69 ? 68   SER J N   1 
ATOM   10356 C  CA  . SER J  1 68  ? 52.588  81.526  52.868  1.00 13.75 ? 68   SER J CA  1 
ATOM   10357 C  C   . SER J  1 68  ? 52.555  82.359  54.150  1.00 14.51 ? 68   SER J C   1 
ATOM   10358 O  O   . SER J  1 68  ? 52.807  81.843  55.258  1.00 15.28 ? 68   SER J O   1 
ATOM   10359 C  CB  . SER J  1 68  ? 53.195  80.127  53.119  1.00 14.19 ? 68   SER J CB  1 
ATOM   10360 O  OG  . SER J  1 68  ? 53.385  79.466  51.879  1.00 15.93 ? 68   SER J OG  1 
ATOM   10361 N  N   . ARG J  1 69  ? 52.231  83.642  54.006  1.00 13.83 ? 69   ARG J N   1 
ATOM   10362 C  CA  . ARG J  1 69  ? 52.177  84.570  55.129  1.00 13.87 ? 69   ARG J CA  1 
ATOM   10363 C  C   . ARG J  1 69  ? 50.772  84.819  55.625  1.00 13.35 ? 69   ARG J C   1 
ATOM   10364 O  O   . ARG J  1 69  ? 49.824  84.318  55.029  1.00 13.24 ? 69   ARG J O   1 
ATOM   10365 C  CB  . ARG J  1 69  ? 52.798  85.889  54.735  1.00 14.70 ? 69   ARG J CB  1 
ATOM   10366 C  CG  . ARG J  1 69  ? 54.164  85.738  54.112  1.00 17.92 ? 69   ARG J CG  1 
ATOM   10367 C  CD  . ARG J  1 69  ? 55.256  86.554  54.789  1.00 28.91 ? 69   ARG J CD  1 
ATOM   10368 N  NE  . ARG J  1 69  ? 56.238  87.020  53.812  1.00 34.96 ? 69   ARG J NE  1 
ATOM   10369 C  CZ  . ARG J  1 69  ? 57.463  87.419  54.110  1.00 37.02 ? 69   ARG J CZ  1 
ATOM   10370 N  NH1 . ARG J  1 69  ? 57.873  87.417  55.367  1.00 39.83 ? 69   ARG J NH1 1 
ATOM   10371 N  NH2 . ARG J  1 69  ? 58.286  87.818  53.149  1.00 38.74 ? 69   ARG J NH2 1 
ATOM   10372 N  N   . LYS J  1 70  ? 50.652  85.568  56.730  1.00 11.55 ? 70   LYS J N   1 
ATOM   10373 C  CA  . LYS J  1 70  ? 49.352  85.933  57.257  1.00 11.31 ? 70   LYS J CA  1 
ATOM   10374 C  C   . LYS J  1 70  ? 48.980  87.242  56.597  1.00 9.62  ? 70   LYS J C   1 
ATOM   10375 O  O   . LYS J  1 70  ? 49.835  87.984  56.100  1.00 8.83  ? 70   LYS J O   1 
ATOM   10376 C  CB  . LYS J  1 70  ? 49.392  86.186  58.766  1.00 11.52 ? 70   LYS J CB  1 
ATOM   10377 C  CG  . LYS J  1 70  ? 49.673  84.942  59.622  1.00 14.34 ? 70   LYS J CG  1 
ATOM   10378 C  CD  . LYS J  1 70  ? 48.784  83.766  59.206  1.00 18.63 ? 70   LYS J CD  1 
ATOM   10379 C  CE  . LYS J  1 70  ? 48.970  82.515  60.131  1.00 22.29 ? 70   LYS J CE  1 
ATOM   10380 N  NZ  . LYS J  1 70  ? 48.462  81.254  59.465  1.00 22.64 ? 70   LYS J NZ  1 
ATOM   10381 N  N   . HIS J  1 71  ? 47.704  87.545  56.681  1.00 9.02  ? 71   HIS J N   1 
ATOM   10382 C  CA  . HIS J  1 71  ? 47.160  88.760  56.095  1.00 8.42  ? 71   HIS J CA  1 
ATOM   10383 C  C   . HIS J  1 71  ? 47.637  90.035  56.772  1.00 8.62  ? 71   HIS J C   1 
ATOM   10384 O  O   . HIS J  1 71  ? 47.790  90.021  58.011  1.00 8.61  ? 71   HIS J O   1 
ATOM   10385 C  CB  . HIS J  1 71  ? 45.673  88.714  56.308  1.00 8.71  ? 71   HIS J CB  1 
ATOM   10386 C  CG  . HIS J  1 71  ? 44.963  89.852  55.664  1.00 10.60 ? 71   HIS J CG  1 
ATOM   10387 N  ND1 . HIS J  1 71  ? 44.776  89.939  54.300  1.00 7.47  ? 71   HIS J ND1 1 
ATOM   10388 C  CD2 . HIS J  1 71  ? 44.441  90.974  56.195  1.00 8.05  ? 71   HIS J CD2 1 
ATOM   10389 C  CE1 . HIS J  1 71  ? 44.128  91.056  54.026  1.00 7.97  ? 71   HIS J CE1 1 
ATOM   10390 N  NE2 . HIS J  1 71  ? 43.903  91.692  55.163  1.00 7.98  ? 71   HIS J NE2 1 
ATOM   10391 N  N   . GLY J  1 72  ? 47.815  91.126  56.013  1.00 6.80  ? 72   GLY J N   1 
ATOM   10392 C  CA  . GLY J  1 72  ? 48.175  92.414  56.594  1.00 7.31  ? 72   GLY J CA  1 
ATOM   10393 C  C   . GLY J  1 72  ? 47.779  93.533  55.647  1.00 8.08  ? 72   GLY J C   1 
ATOM   10394 O  O   . GLY J  1 72  ? 47.083  93.311  54.648  1.00 7.05  ? 72   GLY J O   1 
ATOM   10395 N  N   . GLY J  1 73  ? 48.210  94.749  55.948  1.00 7.98  ? 73   GLY J N   1 
ATOM   10396 C  CA  . GLY J  1 73  ? 48.008  95.830  55.011  1.00 8.86  ? 73   GLY J CA  1 
ATOM   10397 C  C   . GLY J  1 73  ? 49.192  95.878  54.055  1.00 8.98  ? 73   GLY J C   1 
ATOM   10398 O  O   . GLY J  1 73  ? 50.205  95.226  54.269  1.00 9.31  ? 73   GLY J O   1 
ATOM   10399 N  N   . PRO J  1 74  ? 49.075  96.636  52.990  1.00 9.90  ? 74   PRO J N   1 
ATOM   10400 C  CA  . PRO J  1 74  ? 50.127  96.674  51.963  1.00 9.34  ? 74   PRO J CA  1 
ATOM   10401 C  C   . PRO J  1 74  ? 51.448  97.212  52.480  1.00 10.31 ? 74   PRO J C   1 
ATOM   10402 O  O   . PRO J  1 74  ? 52.481  96.872  51.928  1.00 8.38  ? 74   PRO J O   1 
ATOM   10403 C  CB  . PRO J  1 74  ? 49.576  97.612  50.885  1.00 10.60 ? 74   PRO J CB  1 
ATOM   10404 C  CG  . PRO J  1 74  ? 48.318  98.226  51.443  1.00 10.31 ? 74   PRO J CG  1 
ATOM   10405 C  CD  . PRO J  1 74  ? 47.888  97.417  52.631  1.00 10.02 ? 74   PRO J CD  1 
ATOM   10406 N  N   . LYS J  1 75  ? 51.422  97.996  53.553  1.00 11.04 ? 75   LYS J N   1 
ATOM   10407 C  CA  . LYS J  1 75  ? 52.679  98.535  54.076  1.00 12.69 ? 75   LYS J CA  1 
ATOM   10408 C  C   . LYS J  1 75  ? 53.384  97.569  55.011  1.00 13.24 ? 75   LYS J C   1 
ATOM   10409 O  O   . LYS J  1 75  ? 54.517  97.838  55.434  1.00 14.40 ? 75   LYS J O   1 
ATOM   10410 C  CB  . LYS J  1 75  ? 52.444  99.852  54.824  1.00 12.83 ? 75   LYS J CB  1 
ATOM   10411 C  CG  . LYS J  1 75  ? 51.770  100.943 54.022  1.00 14.06 ? 75   LYS J CG  1 
ATOM   10412 C  CD  . LYS J  1 75  ? 51.165  101.976 55.001  1.00 17.74 ? 75   LYS J CD  1 
ATOM   10413 C  CE  . LYS J  1 75  ? 52.269  102.675 55.789  1.00 19.82 ? 75   LYS J CE  1 
ATOM   10414 N  NZ  . LYS J  1 75  ? 51.743  103.752 56.676  1.00 23.62 ? 75   LYS J NZ  1 
ATOM   10415 N  N   . ASP J  1 76  ? 52.712  96.493  55.392  1.00 13.39 ? 76   ASP J N   1 
ATOM   10416 C  CA  . ASP J  1 76  ? 53.272  95.537  56.343  1.00 14.36 ? 76   ASP J CA  1 
ATOM   10417 C  C   . ASP J  1 76  ? 54.230  94.526  55.733  1.00 15.14 ? 76   ASP J C   1 
ATOM   10418 O  O   . ASP J  1 76  ? 54.025  94.055  54.607  1.00 15.77 ? 76   ASP J O   1 
ATOM   10419 C  CB  . ASP J  1 76  ? 52.155  94.753  57.034  1.00 14.04 ? 76   ASP J CB  1 
ATOM   10420 C  CG  . ASP J  1 76  ? 51.255  95.623  57.860  1.00 15.80 ? 76   ASP J CG  1 
ATOM   10421 O  OD1 . ASP J  1 76  ? 51.757  96.638  58.447  1.00 16.97 ? 76   ASP J OD1 1 
ATOM   10422 O  OD2 . ASP J  1 76  ? 50.035  95.370  57.998  1.00 12.33 ? 76   ASP J OD2 1 
ATOM   10423 N  N   . GLU J  1 77  ? 55.264  94.162  56.486  1.00 14.87 ? 77   GLU J N   1 
ATOM   10424 C  CA  . GLU J  1 77  ? 56.178  93.107  56.047  1.00 14.95 ? 77   GLU J CA  1 
ATOM   10425 C  C   . GLU J  1 77  ? 55.426  91.812  56.013  1.00 13.52 ? 77   GLU J C   1 
ATOM   10426 O  O   . GLU J  1 77  ? 55.617  90.978  55.123  1.00 13.73 ? 77   GLU J O   1 
ATOM   10427 C  CB  . GLU J  1 77  ? 57.362  92.939  57.039  1.00 15.87 ? 77   GLU J CB  1 
ATOM   10428 C  CG  . GLU J  1 77  ? 58.380  91.885  56.615  1.00 20.22 ? 77   GLU J CG  1 
ATOM   10429 C  CD  . GLU J  1 77  ? 58.008  90.450  57.015  1.00 26.98 ? 77   GLU J CD  1 
ATOM   10430 O  OE1 . GLU J  1 77  ? 57.299  90.255  58.029  1.00 30.06 ? 77   GLU J OE1 1 
ATOM   10431 O  OE2 . GLU J  1 77  ? 58.450  89.506  56.321  1.00 27.54 ? 77   GLU J OE2 1 
ATOM   10432 N  N   . GLU J  1 78  ? 54.589  91.607  57.016  1.00 11.94 ? 78   GLU J N   1 
ATOM   10433 C  CA  . GLU J  1 78  ? 53.804  90.399  57.079  1.00 11.24 ? 78   GLU J CA  1 
ATOM   10434 C  C   . GLU J  1 78  ? 52.479  90.658  56.324  1.00 9.69  ? 78   GLU J C   1 
ATOM   10435 O  O   . GLU J  1 78  ? 51.519  91.205  56.874  1.00 8.96  ? 78   GLU J O   1 
ATOM   10436 C  CB  . GLU J  1 78  ? 53.538  89.972  58.519  1.00 12.07 ? 78   GLU J CB  1 
ATOM   10437 C  CG  . GLU J  1 78  ? 52.865  88.624  58.644  1.00 15.83 ? 78   GLU J CG  1 
ATOM   10438 C  CD  . GLU J  1 78  ? 53.791  87.459  58.279  1.00 22.20 ? 78   GLU J CD  1 
ATOM   10439 O  OE1 . GLU J  1 78  ? 55.028  87.672  58.144  1.00 25.17 ? 78   GLU J OE1 1 
ATOM   10440 O  OE2 . GLU J  1 78  ? 53.281  86.319  58.130  1.00 21.98 ? 78   GLU J OE2 1 
ATOM   10441 N  N   . ARG J  1 79  ? 52.451  90.290  55.043  1.00 8.77  ? 79   ARG J N   1 
ATOM   10442 C  CA  . ARG J  1 79  ? 51.246  90.451  54.227  1.00 7.85  ? 79   ARG J CA  1 
ATOM   10443 C  C   . ARG J  1 79  ? 51.227  89.366  53.162  1.00 6.68  ? 79   ARG J C   1 
ATOM   10444 O  O   . ARG J  1 79  ? 52.250  88.759  52.874  1.00 7.15  ? 79   ARG J O   1 
ATOM   10445 C  CB  . ARG J  1 79  ? 51.200  91.798  53.495  1.00 8.12  ? 79   ARG J CB  1 
ATOM   10446 C  CG  . ARG J  1 79  ? 52.462  92.093  52.637  1.00 8.04  ? 79   ARG J CG  1 
ATOM   10447 C  CD  . ARG J  1 79  ? 52.305  93.309  51.750  1.00 9.04  ? 79   ARG J CD  1 
ATOM   10448 N  NE  . ARG J  1 79  ? 51.619  93.021  50.469  1.00 5.96  ? 79   ARG J NE  1 
ATOM   10449 C  CZ  . ARG J  1 79  ? 51.502  93.903  49.481  1.00 7.18  ? 79   ARG J CZ  1 
ATOM   10450 N  NH1 . ARG J  1 79  ? 52.000  95.133  49.618  1.00 6.72  ? 79   ARG J NH1 1 
ATOM   10451 N  NH2 . ARG J  1 79  ? 50.934  93.540  48.307  1.00 5.00  ? 79   ARG J NH2 1 
ATOM   10452 N  N   . HIS J  1 80  ? 50.048  89.110  52.626  1.00 6.54  ? 80   HIS J N   1 
ATOM   10453 C  CA  . HIS J  1 80  ? 49.924  88.267  51.441  1.00 6.30  ? 80   HIS J CA  1 
ATOM   10454 C  C   . HIS J  1 80  ? 50.364  89.126  50.223  1.00 5.76  ? 80   HIS J C   1 
ATOM   10455 O  O   . HIS J  1 80  ? 50.186  90.344  50.221  1.00 5.59  ? 80   HIS J O   1 
ATOM   10456 C  CB  . HIS J  1 80  ? 48.449  87.909  51.257  1.00 6.51  ? 80   HIS J CB  1 
ATOM   10457 C  CG  . HIS J  1 80  ? 47.841  87.125  52.387  1.00 5.00  ? 80   HIS J CG  1 
ATOM   10458 N  ND1 . HIS J  1 80  ? 46.545  87.335  52.808  1.00 7.47  ? 80   HIS J ND1 1 
ATOM   10459 C  CD2 . HIS J  1 80  ? 48.314  86.081  53.123  1.00 6.72  ? 80   HIS J CD2 1 
ATOM   10460 C  CE1 . HIS J  1 80  ? 46.244  86.452  53.746  1.00 8.23  ? 80   HIS J CE1 1 
ATOM   10461 N  NE2 . HIS J  1 80  ? 47.294  85.665  53.943  1.00 7.49  ? 80   HIS J NE2 1 
ATOM   10462 N  N   . VAL J  1 81  ? 50.868  88.514  49.148  1.00 5.29  ? 81   VAL J N   1 
ATOM   10463 C  CA  . VAL J  1 81  ? 51.208  89.320  47.966  1.00 5.00  ? 81   VAL J CA  1 
ATOM   10464 C  C   . VAL J  1 81  ? 49.947  90.054  47.472  1.00 5.00  ? 81   VAL J C   1 
ATOM   10465 O  O   . VAL J  1 81  ? 50.022  91.199  47.057  1.00 5.00  ? 81   VAL J O   1 
ATOM   10466 C  CB  . VAL J  1 81  ? 51.760  88.446  46.797  1.00 5.70  ? 81   VAL J CB  1 
ATOM   10467 C  CG1 . VAL J  1 81  ? 51.704  89.230  45.476  1.00 5.11  ? 81   VAL J CG1 1 
ATOM   10468 C  CG2 . VAL J  1 81  ? 53.191  87.963  47.118  1.00 6.93  ? 81   VAL J CG2 1 
ATOM   10469 N  N   . GLY J  1 82  ? 48.781  89.432  47.621  1.00 5.00  ? 82   GLY J N   1 
ATOM   10470 C  CA  . GLY J  1 82  ? 47.554  90.073  47.139  1.00 5.23  ? 82   GLY J CA  1 
ATOM   10471 C  C   . GLY J  1 82  ? 46.944  91.163  48.004  1.00 5.31  ? 82   GLY J C   1 
ATOM   10472 O  O   . GLY J  1 82  ? 45.880  91.703  47.669  1.00 5.60  ? 82   GLY J O   1 
ATOM   10473 N  N   . ASP J  1 83  ? 47.598  91.492  49.123  1.00 5.00  ? 83   ASP J N   1 
ATOM   10474 C  CA  . ASP J  1 83  ? 47.036  92.443  50.069  1.00 5.01  ? 83   ASP J CA  1 
ATOM   10475 C  C   . ASP J  1 83  ? 47.249  93.886  49.688  1.00 6.11  ? 83   ASP J C   1 
ATOM   10476 O  O   . ASP J  1 83  ? 48.223  94.503  50.151  1.00 6.56  ? 83   ASP J O   1 
ATOM   10477 C  CB  . ASP J  1 83  ? 47.683  92.223  51.434  1.00 5.19  ? 83   ASP J CB  1 
ATOM   10478 C  CG  . ASP J  1 83  ? 47.172  90.973  52.091  1.00 5.00  ? 83   ASP J CG  1 
ATOM   10479 O  OD1 . ASP J  1 83  ? 46.165  90.403  51.590  1.00 5.00  ? 83   ASP J OD1 1 
ATOM   10480 O  OD2 . ASP J  1 83  ? 47.670  90.524  53.130  1.00 5.60  ? 83   ASP J OD2 1 
ATOM   10481 N  N   . LEU J  1 84  ? 46.345  94.437  48.886  1.00 5.40  ? 84   LEU J N   1 
ATOM   10482 C  CA  . LEU J  1 84  ? 46.412  95.845  48.494  1.00 6.21  ? 84   LEU J CA  1 
ATOM   10483 C  C   . LEU J  1 84  ? 45.667  96.818  49.408  1.00 6.85  ? 84   LEU J C   1 
ATOM   10484 O  O   . LEU J  1 84  ? 45.497  97.992  49.062  1.00 8.06  ? 84   LEU J O   1 
ATOM   10485 C  CB  . LEU J  1 84  ? 45.870  96.004  47.056  1.00 5.59  ? 84   LEU J CB  1 
ATOM   10486 C  CG  . LEU J  1 84  ? 46.708  95.221  46.026  1.00 7.65  ? 84   LEU J CG  1 
ATOM   10487 C  CD1 . LEU J  1 84  ? 46.141  95.378  44.594  1.00 7.84  ? 84   LEU J CD1 1 
ATOM   10488 C  CD2 . LEU J  1 84  ? 48.204  95.529  46.048  1.00 9.61  ? 84   LEU J CD2 1 
ATOM   10489 N  N   . GLY J  1 85  ? 45.191  96.356  50.560  1.00 6.02  ? 85   GLY J N   1 
ATOM   10490 C  CA  . GLY J  1 85  ? 44.569  97.264  51.507  1.00 5.90  ? 85   GLY J CA  1 
ATOM   10491 C  C   . GLY J  1 85  ? 43.128  97.635  51.215  1.00 6.37  ? 85   GLY J C   1 
ATOM   10492 O  O   . GLY J  1 85  ? 42.306  96.783  50.887  1.00 6.93  ? 85   GLY J O   1 
ATOM   10493 N  N   . ASN J  1 86  ? 42.816  98.917  51.358  1.00 5.00  ? 86   ASN J N   1 
ATOM   10494 C  CA  . ASN J  1 86  ? 41.484  99.422  51.121  1.00 5.00  ? 86   ASN J CA  1 
ATOM   10495 C  C   . ASN J  1 86  ? 41.451  100.403 49.979  1.00 5.00  ? 86   ASN J C   1 
ATOM   10496 O  O   . ASN J  1 86  ? 42.444  101.055 49.706  1.00 5.23  ? 86   ASN J O   1 
ATOM   10497 C  CB  . ASN J  1 86  ? 40.994  100.161 52.371  1.00 5.12  ? 86   ASN J CB  1 
ATOM   10498 C  CG  . ASN J  1 86  ? 40.622  99.167  53.468  1.00 6.29  ? 86   ASN J CG  1 
ATOM   10499 O  OD1 . ASN J  1 86  ? 39.798  98.306  53.248  1.00 5.28  ? 86   ASN J OD1 1 
ATOM   10500 N  ND2 . ASN J  1 86  ? 41.302  99.223  54.582  1.00 7.94  ? 86   ASN J ND2 1 
ATOM   10501 N  N   . VAL J  1 87  ? 40.286  100.536 49.365  1.00 5.15  ? 87   VAL J N   1 
ATOM   10502 C  CA  . VAL J  1 87  ? 40.036  101.685 48.497  1.00 5.00  ? 87   VAL J CA  1 
ATOM   10503 C  C   . VAL J  1 87  ? 38.892  102.430 49.162  1.00 5.23  ? 87   VAL J C   1 
ATOM   10504 O  O   . VAL J  1 87  ? 38.161  101.865 49.968  1.00 5.90  ? 87   VAL J O   1 
ATOM   10505 C  CB  . VAL J  1 87  ? 39.665  101.273 47.053  1.00 5.73  ? 87   VAL J CB  1 
ATOM   10506 C  CG1 . VAL J  1 87  ? 40.898  100.584 46.366  1.00 6.07  ? 87   VAL J CG1 1 
ATOM   10507 C  CG2 . VAL J  1 87  ? 38.469  100.350 47.074  1.00 5.00  ? 87   VAL J CG2 1 
ATOM   10508 N  N   . THR J  1 88  ? 38.710  103.689 48.791  1.00 5.76  ? 88   THR J N   1 
ATOM   10509 C  CA  . THR J  1 88  ? 37.751  104.546 49.466  1.00 6.14  ? 88   THR J CA  1 
ATOM   10510 C  C   . THR J  1 88  ? 36.746  105.043 48.470  1.00 6.01  ? 88   THR J C   1 
ATOM   10511 O  O   . THR J  1 88  ? 37.112  105.678 47.477  1.00 6.92  ? 88   THR J O   1 
ATOM   10512 C  CB  . THR J  1 88  ? 38.519  105.784 50.066  1.00 6.71  ? 88   THR J CB  1 
ATOM   10513 O  OG1 . THR J  1 88  ? 39.408  105.351 51.127  1.00 6.30  ? 88   THR J OG1 1 
ATOM   10514 C  CG2 . THR J  1 88  ? 37.554  106.761 50.692  1.00 7.30  ? 88   THR J CG2 1 
ATOM   10515 N  N   . ALA J  1 89  ? 35.481  104.772 48.716  1.00 6.28  ? 89   ALA J N   1 
ATOM   10516 C  CA  . ALA J  1 89  ? 34.451  105.329 47.849  1.00 7.47  ? 89   ALA J CA  1 
ATOM   10517 C  C   . ALA J  1 89  ? 33.955  106.639 48.433  1.00 8.75  ? 89   ALA J C   1 
ATOM   10518 O  O   . ALA J  1 89  ? 33.811  106.788 49.662  1.00 7.85  ? 89   ALA J O   1 
ATOM   10519 C  CB  . ALA J  1 89  ? 33.305  104.390 47.711  1.00 7.56  ? 89   ALA J CB  1 
ATOM   10520 N  N   . ASP J  1 90  ? 33.674  107.575 47.536  1.00 10.02 ? 90   ASP J N   1 
ATOM   10521 C  CA  . ASP J  1 90  ? 33.188  108.876 47.950  1.00 11.22 ? 90   ASP J CA  1 
ATOM   10522 C  C   . ASP J  1 90  ? 31.705  108.859 48.267  1.00 11.93 ? 90   ASP J C   1 
ATOM   10523 O  O   . ASP J  1 90  ? 31.054  107.812 48.231  1.00 10.67 ? 90   ASP J O   1 
ATOM   10524 C  CB  . ASP J  1 90  ? 33.570  109.996 46.964  1.00 12.95 ? 90   ASP J CB  1 
ATOM   10525 C  CG  . ASP J  1 90  ? 32.961  109.828 45.567  1.00 16.32 ? 90   ASP J CG  1 
ATOM   10526 O  OD1 . ASP J  1 90  ? 31.903  109.170 45.397  1.00 20.78 ? 90   ASP J OD1 1 
ATOM   10527 O  OD2 . ASP J  1 90  ? 33.492  110.352 44.557  1.00 18.41 ? 90   ASP J OD2 1 
ATOM   10528 N  N   . LYS J  1 91  ? 31.146  110.026 48.591  1.00 13.26 ? 91   LYS J N   1 
ATOM   10529 C  CA  . LYS J  1 91  ? 29.748  110.011 48.971  1.00 13.94 ? 91   LYS J CA  1 
ATOM   10530 C  C   . LYS J  1 91  ? 28.897  109.517 47.810  1.00 13.61 ? 91   LYS J C   1 
ATOM   10531 O  O   . LYS J  1 91  ? 27.900  108.844 48.037  1.00 15.34 ? 91   LYS J O   1 
ATOM   10532 C  CB  . LYS J  1 91  ? 29.290  111.372 49.534  1.00 13.91 ? 91   LYS J CB  1 
ATOM   10533 C  CG  . LYS J  1 91  ? 29.648  112.562 48.669  1.00 17.73 ? 91   LYS J CG  1 
ATOM   10534 C  CD  . LYS J  1 91  ? 28.446  113.023 47.865  1.00 21.58 ? 91   LYS J CD  1 
ATOM   10535 C  CE  . LYS J  1 91  ? 28.255  114.538 47.964  1.00 20.22 ? 91   LYS J CE  1 
ATOM   10536 N  NZ  . LYS J  1 91  ? 27.095  114.950 47.130  1.00 19.40 ? 91   LYS J NZ  1 
ATOM   10537 N  N   . ASP J  1 92  ? 29.322  109.780 46.574  1.00 13.22 ? 92   ASP J N   1 
ATOM   10538 C  CA  . ASP J  1 92  ? 28.583  109.335 45.376  1.00 12.73 ? 92   ASP J CA  1 
ATOM   10539 C  C   . ASP J  1 92  ? 28.737  107.814 45.108  1.00 12.11 ? 92   ASP J C   1 
ATOM   10540 O  O   . ASP J  1 92  ? 28.141  107.288 44.168  1.00 10.25 ? 92   ASP J O   1 
ATOM   10541 C  CB  . ASP J  1 92  ? 29.031  110.102 44.119  1.00 13.19 ? 92   ASP J CB  1 
ATOM   10542 C  CG  . ASP J  1 92  ? 28.697  111.611 44.171  1.00 17.90 ? 92   ASP J CG  1 
ATOM   10543 O  OD1 . ASP J  1 92  ? 27.634  112.004 44.732  1.00 20.42 ? 92   ASP J OD1 1 
ATOM   10544 O  OD2 . ASP J  1 92  ? 29.434  112.476 43.630  1.00 20.95 ? 92   ASP J OD2 1 
ATOM   10545 N  N   . GLY J  1 93  ? 29.545  107.133 45.920  1.00 10.60 ? 93   GLY J N   1 
ATOM   10546 C  CA  . GLY J  1 93  ? 29.738  105.689 45.788  1.00 10.08 ? 93   GLY J CA  1 
ATOM   10547 C  C   . GLY J  1 93  ? 30.811  105.296 44.790  1.00 9.84  ? 93   GLY J C   1 
ATOM   10548 O  O   . GLY J  1 93  ? 30.911  104.136 44.379  1.00 9.43  ? 93   GLY J O   1 
ATOM   10549 N  N   . VAL J  1 94  ? 31.636  106.257 44.411  1.00 9.30  ? 94   VAL J N   1 
ATOM   10550 C  CA  . VAL J  1 94  ? 32.656  106.030 43.414  1.00 9.78  ? 94   VAL J CA  1 
ATOM   10551 C  C   . VAL J  1 94  ? 33.993  106.001 44.109  1.00 9.14  ? 94   VAL J C   1 
ATOM   10552 O  O   . VAL J  1 94  ? 34.313  106.905 44.891  1.00 9.40  ? 94   VAL J O   1 
ATOM   10553 C  CB  . VAL J  1 94  ? 32.681  107.164 42.358  1.00 10.38 ? 94   VAL J CB  1 
ATOM   10554 C  CG1 . VAL J  1 94  ? 33.946  107.087 41.514  1.00 11.63 ? 94   VAL J CG1 1 
ATOM   10555 C  CG2 . VAL J  1 94  ? 31.448  107.105 41.465  1.00 11.16 ? 94   VAL J CG2 1 
ATOM   10556 N  N   . ALA J  1 95  ? 34.752  104.935 43.869  1.00 8.77  ? 95   ALA J N   1 
ATOM   10557 C  CA  . ALA J  1 95  ? 36.112  104.853 44.364  1.00 8.44  ? 95   ALA J CA  1 
ATOM   10558 C  C   . ALA J  1 95  ? 37.025  105.130 43.202  1.00 8.99  ? 95   ALA J C   1 
ATOM   10559 O  O   . ALA J  1 95  ? 37.057  104.342 42.223  1.00 8.76  ? 95   ALA J O   1 
ATOM   10560 C  CB  . ALA J  1 95  ? 36.423  103.456 44.970  1.00 8.27  ? 95   ALA J CB  1 
ATOM   10561 N  N   . ASP J  1 96  ? 37.756  106.246 43.287  1.00 7.64  ? 96   ASP J N   1 
ATOM   10562 C  CA  . ASP J  1 96  ? 38.782  106.548 42.292  1.00 9.52  ? 96   ASP J CA  1 
ATOM   10563 C  C   . ASP J  1 96  ? 40.101  105.973 42.800  1.00 8.66  ? 96   ASP J C   1 
ATOM   10564 O  O   . ASP J  1 96  ? 40.848  106.600 43.531  1.00 10.35 ? 96   ASP J O   1 
ATOM   10565 C  CB  . ASP J  1 96  ? 38.902  108.044 42.045  1.00 10.79 ? 96   ASP J CB  1 
ATOM   10566 C  CG  . ASP J  1 96  ? 37.756  108.563 41.234  1.00 13.78 ? 96   ASP J CG  1 
ATOM   10567 O  OD1 . ASP J  1 96  ? 37.110  109.516 41.713  1.00 17.61 ? 96   ASP J OD1 1 
ATOM   10568 O  OD2 . ASP J  1 96  ? 37.412  108.037 40.134  1.00 15.16 ? 96   ASP J OD2 1 
ATOM   10569 N  N   . VAL J  1 97  ? 40.365  104.747 42.403  1.00 6.65  ? 97   VAL J N   1 
ATOM   10570 C  CA  . VAL J  1 97  ? 41.486  104.016 42.905  1.00 5.77  ? 97   VAL J CA  1 
ATOM   10571 C  C   . VAL J  1 97  ? 42.792  104.500 42.327  1.00 5.69  ? 97   VAL J C   1 
ATOM   10572 O  O   . VAL J  1 97  ? 42.895  104.774 41.116  1.00 5.66  ? 97   VAL J O   1 
ATOM   10573 C  CB  . VAL J  1 97  ? 41.279  102.529 42.534  1.00 6.93  ? 97   VAL J CB  1 
ATOM   10574 C  CG1 . VAL J  1 97  ? 42.472  101.705 43.044  1.00 6.29  ? 97   VAL J CG1 1 
ATOM   10575 C  CG2 . VAL J  1 97  ? 39.914  102.074 43.087  1.00 5.97  ? 97   VAL J CG2 1 
ATOM   10576 N  N   . SER J  1 98  ? 43.775  104.672 43.194  1.00 6.05  ? 98   SER J N   1 
ATOM   10577 C  CA  . SER J  1 98  ? 45.109  105.004 42.715  1.00 7.12  ? 98   SER J CA  1 
ATOM   10578 C  C   . SER J  1 98  ? 46.077  104.494 43.786  1.00 8.19  ? 98   SER J C   1 
ATOM   10579 O  O   . SER J  1 98  ? 46.169  105.043 44.895  1.00 8.32  ? 98   SER J O   1 
ATOM   10580 C  CB  . SER J  1 98  ? 45.245  106.497 42.412  1.00 8.87  ? 98   SER J CB  1 
ATOM   10581 O  OG  . SER J  1 98  ? 46.545  106.769 41.891  1.00 10.95 ? 98   SER J OG  1 
ATOM   10582 N  N   . ILE J  1 99  ? 46.756  103.397 43.472  1.00 7.31  ? 99   ILE J N   1 
ATOM   10583 C  CA  . ILE J  1 99  ? 47.619  102.759 44.406  1.00 8.92  ? 99   ILE J CA  1 
ATOM   10584 C  C   . ILE J  1 99  ? 48.900  102.474 43.677  1.00 9.06  ? 99   ILE J C   1 
ATOM   10585 O  O   . ILE J  1 99  ? 48.904  102.324 42.466  1.00 9.25  ? 99   ILE J O   1 
ATOM   10586 C  CB  . ILE J  1 99  ? 46.957  101.441 44.851  1.00 9.78  ? 99   ILE J CB  1 
ATOM   10587 C  CG1 . ILE J  1 99  ? 45.894  101.719 45.941  1.00 10.61 ? 99   ILE J CG1 1 
ATOM   10588 C  CG2 . ILE J  1 99  ? 47.982  100.481 45.437  1.00 14.71 ? 99   ILE J CG2 1 
ATOM   10589 C  CD1 . ILE J  1 99  ? 44.987  100.459 46.219  1.00 10.83 ? 99   ILE J CD1 1 
ATOM   10590 N  N   . GLU J  1 100 ? 49.992  102.450 44.410  1.00 8.25  ? 100  GLU J N   1 
ATOM   10591 C  CA  . GLU J  1 100 ? 51.242  101.994 43.836  1.00 9.01  ? 100  GLU J CA  1 
ATOM   10592 C  C   . GLU J  1 100 ? 51.723  100.878 44.749  1.00 9.06  ? 100  GLU J C   1 
ATOM   10593 O  O   . GLU J  1 100 ? 51.714  101.045 45.973  1.00 9.20  ? 100  GLU J O   1 
ATOM   10594 C  CB  . GLU J  1 100 ? 52.261  103.127 43.797  1.00 10.24 ? 100  GLU J CB  1 
ATOM   10595 C  CG  . GLU J  1 100 ? 53.529  102.712 43.078  1.00 15.07 ? 100  GLU J CG  1 
ATOM   10596 C  CD  . GLU J  1 100 ? 54.594  103.799 43.105  1.00 21.49 ? 100  GLU J CD  1 
ATOM   10597 O  OE1 . GLU J  1 100 ? 54.511  104.659 42.228  1.00 24.65 ? 100  GLU J OE1 1 
ATOM   10598 O  OE2 . GLU J  1 100 ? 55.471  103.790 44.014  1.00 22.73 ? 100  GLU J OE2 1 
ATOM   10599 N  N   . ASP J  1 101 ? 52.132  99.749  44.182  1.00 8.60  ? 101  ASP J N   1 
ATOM   10600 C  CA  . ASP J  1 101 ? 52.567  98.638  44.990  1.00 8.41  ? 101  ASP J CA  1 
ATOM   10601 C  C   . ASP J  1 101 ? 53.798  97.926  44.464  1.00 8.46  ? 101  ASP J C   1 
ATOM   10602 O  O   . ASP J  1 101 ? 53.920  97.675  43.277  1.00 8.21  ? 101  ASP J O   1 
ATOM   10603 C  CB  . ASP J  1 101 ? 51.389  97.649  45.223  1.00 8.73  ? 101  ASP J CB  1 
ATOM   10604 C  CG  . ASP J  1 101 ? 51.686  96.642  46.320  1.00 10.72 ? 101  ASP J CG  1 
ATOM   10605 O  OD1 . ASP J  1 101 ? 51.632  97.002  47.530  1.00 12.72 ? 101  ASP J OD1 1 
ATOM   10606 O  OD2 . ASP J  1 101 ? 52.032  95.465  46.088  1.00 8.70  ? 101  ASP J OD2 1 
ATOM   10607 N  N   . SER J  1 102 ? 54.692  97.537  45.373  1.00 8.73  ? 102  SER J N   1 
ATOM   10608 C  CA  . SER J  1 102 ? 55.935  96.917  44.932  1.00 9.52  ? 102  SER J CA  1 
ATOM   10609 C  C   . SER J  1 102 ? 56.021  95.433  45.249  1.00 8.91  ? 102  SER J C   1 
ATOM   10610 O  O   . SER J  1 102 ? 57.078  94.816  45.024  1.00 9.30  ? 102  SER J O   1 
ATOM   10611 C  CB  . SER J  1 102 ? 57.141  97.672  45.528  1.00 10.00 ? 102  SER J CB  1 
ATOM   10612 O  OG  . SER J  1 102 ? 57.298  98.896  44.818  1.00 14.46 ? 102  SER J OG  1 
ATOM   10613 N  N   . VAL J  1 103 ? 54.948  94.857  45.792  1.00 7.00  ? 103  VAL J N   1 
ATOM   10614 C  CA  . VAL J  1 103 ? 54.943  93.431  46.134  1.00 5.89  ? 103  VAL J CA  1 
ATOM   10615 C  C   . VAL J  1 103 ? 54.270  92.639  44.999  1.00 5.23  ? 103  VAL J C   1 
ATOM   10616 O  O   . VAL J  1 103 ? 54.789  91.610  44.550  1.00 5.00  ? 103  VAL J O   1 
ATOM   10617 C  CB  . VAL J  1 103 ? 54.301  93.184  47.526  1.00 6.60  ? 103  VAL J CB  1 
ATOM   10618 C  CG1 . VAL J  1 103 ? 54.152  91.707  47.802  1.00 8.42  ? 103  VAL J CG1 1 
ATOM   10619 C  CG2 . VAL J  1 103 ? 55.217  93.832  48.673  1.00 7.40  ? 103  VAL J CG2 1 
ATOM   10620 N  N   . ILE J  1 104 ? 53.142  93.145  44.505  1.00 5.08  ? 104  ILE J N   1 
ATOM   10621 C  CA  . ILE J  1 104 ? 52.543  92.535  43.321  1.00 5.00  ? 104  ILE J CA  1 
ATOM   10622 C  C   . ILE J  1 104 ? 53.465  92.808  42.130  1.00 5.00  ? 104  ILE J C   1 
ATOM   10623 O  O   . ILE J  1 104 ? 54.300  93.697  42.179  1.00 5.44  ? 104  ILE J O   1 
ATOM   10624 C  CB  . ILE J  1 104 ? 51.109  93.097  43.028  1.00 5.00  ? 104  ILE J CB  1 
ATOM   10625 C  CG1 . ILE J  1 104 ? 51.099  94.615  42.914  1.00 6.00  ? 104  ILE J CG1 1 
ATOM   10626 C  CG2 . ILE J  1 104 ? 50.116  92.565  44.093  1.00 5.22  ? 104  ILE J CG2 1 
ATOM   10627 C  CD1 . ILE J  1 104 ? 49.869  95.169  42.144  1.00 5.69  ? 104  ILE J CD1 1 
ATOM   10628 N  N   . SER J  1 105 ? 53.295  92.051  41.059  1.00 5.00  ? 105  SER J N   1 
ATOM   10629 C  CA  . SER J  1 105 ? 54.059  92.292  39.845  1.00 5.00  ? 105  SER J CA  1 
ATOM   10630 C  C   . SER J  1 105 ? 53.255  91.799  38.637  1.00 5.30  ? 105  SER J C   1 
ATOM   10631 O  O   . SER J  1 105 ? 52.322  91.034  38.800  1.00 5.00  ? 105  SER J O   1 
ATOM   10632 C  CB  . SER J  1 105 ? 55.412  91.540  39.917  1.00 5.00  ? 105  SER J CB  1 
ATOM   10633 O  OG  . SER J  1 105 ? 56.213  91.917  38.804  1.00 5.85  ? 105  SER J OG  1 
ATOM   10634 N  N   . LEU J  1 106 ? 53.613  92.262  37.440  1.00 5.00  ? 106  LEU J N   1 
ATOM   10635 C  CA  . LEU J  1 106 ? 52.972  91.801  36.236  1.00 6.44  ? 106  LEU J CA  1 
ATOM   10636 C  C   . LEU J  1 106 ? 53.858  90.778  35.509  1.00 8.11  ? 106  LEU J C   1 
ATOM   10637 O  O   . LEU J  1 106 ? 53.560  90.370  34.381  1.00 9.45  ? 106  LEU J O   1 
ATOM   10638 C  CB  . LEU J  1 106 ? 52.679  92.973  35.337  1.00 5.40  ? 106  LEU J CB  1 
ATOM   10639 C  CG  . LEU J  1 106 ? 51.697  93.952  35.962  1.00 7.18  ? 106  LEU J CG  1 
ATOM   10640 C  CD1 . LEU J  1 106 ? 51.336  94.988  34.900  1.00 10.82 ? 106  LEU J CD1 1 
ATOM   10641 C  CD2 . LEU J  1 106 ? 50.441  93.273  36.522  1.00 6.53  ? 106  LEU J CD2 1 
ATOM   10642 N  N   . SER J  1 107 ? 54.933  90.352  36.170  1.00 8.75  ? 107  SER J N   1 
ATOM   10643 C  CA  . SER J  1 107 ? 55.791  89.285  35.643  1.00 10.11 ? 107  SER J CA  1 
ATOM   10644 C  C   . SER J  1 107 ? 56.491  88.582  36.814  1.00 9.56  ? 107  SER J C   1 
ATOM   10645 O  O   . SER J  1 107 ? 56.429  89.060  37.927  1.00 9.31  ? 107  SER J O   1 
ATOM   10646 C  CB  . SER J  1 107 ? 56.797  89.846  34.641  1.00 10.17 ? 107  SER J CB  1 
ATOM   10647 O  OG  . SER J  1 107 ? 57.852  90.515  35.297  1.00 12.21 ? 107  SER J OG  1 
ATOM   10648 N  N   . GLY J  1 108 ? 57.142  87.440  36.587  1.00 10.76 ? 108  GLY J N   1 
ATOM   10649 C  CA  . GLY J  1 108 ? 57.848  86.764  37.679  1.00 11.61 ? 108  GLY J CA  1 
ATOM   10650 C  C   . GLY J  1 108 ? 57.009  85.968  38.683  1.00 12.42 ? 108  GLY J C   1 
ATOM   10651 O  O   . GLY J  1 108 ? 55.834  85.642  38.439  1.00 12.39 ? 108  GLY J O   1 
ATOM   10652 N  N   . ASP J  1 109 ? 57.629  85.663  39.820  1.00 12.56 ? 109  ASP J N   1 
ATOM   10653 C  CA  . ASP J  1 109 ? 57.047  84.900  40.941  1.00 13.35 ? 109  ASP J CA  1 
ATOM   10654 C  C   . ASP J  1 109 ? 55.813  85.494  41.611  1.00 12.61 ? 109  ASP J C   1 
ATOM   10655 O  O   . ASP J  1 109 ? 55.040  84.780  42.280  1.00 13.68 ? 109  ASP J O   1 
ATOM   10656 C  CB  . ASP J  1 109 ? 58.085  84.804  42.077  1.00 14.19 ? 109  ASP J CB  1 
ATOM   10657 C  CG  . ASP J  1 109 ? 59.165  83.833  41.786  1.00 19.91 ? 109  ASP J CG  1 
ATOM   10658 O  OD1 . ASP J  1 109 ? 60.010  83.650  42.695  1.00 21.87 ? 109  ASP J OD1 1 
ATOM   10659 O  OD2 . ASP J  1 109 ? 59.242  83.209  40.695  1.00 22.56 ? 109  ASP J OD2 1 
ATOM   10660 N  N   . HIS J  1 110 ? 55.672  86.801  41.530  1.00 10.75 ? 110  HIS J N   1 
ATOM   10661 C  CA  . HIS J  1 110 ? 54.533  87.454  42.176  1.00 9.56  ? 110  HIS J CA  1 
ATOM   10662 C  C   . HIS J  1 110 ? 53.568  87.945  41.131  1.00 8.65  ? 110  HIS J C   1 
ATOM   10663 O  O   . HIS J  1 110 ? 52.777  88.863  41.412  1.00 6.95  ? 110  HIS J O   1 
ATOM   10664 C  CB  . HIS J  1 110 ? 55.019  88.640  43.031  1.00 10.07 ? 110  HIS J CB  1 
ATOM   10665 C  CG  . HIS J  1 110 ? 55.704  88.234  44.299  1.00 13.47 ? 110  HIS J CG  1 
ATOM   10666 N  ND1 . HIS J  1 110 ? 56.029  89.141  45.286  1.00 16.22 ? 110  HIS J ND1 1 
ATOM   10667 C  CD2 . HIS J  1 110 ? 56.140  87.029  44.736  1.00 16.63 ? 110  HIS J CD2 1 
ATOM   10668 C  CE1 . HIS J  1 110 ? 56.621  88.510  46.287  1.00 17.37 ? 110  HIS J CE1 1 
ATOM   10669 N  NE2 . HIS J  1 110 ? 56.705  87.228  45.975  1.00 16.23 ? 110  HIS J NE2 1 
ATOM   10670 N  N   . CYS J  1 111 ? 53.649  87.369  39.920  1.00 8.04  ? 111  CYS J N   1 
ATOM   10671 C  CA  . CYS J  1 111 ? 52.804  87.805  38.805  1.00 7.53  ? 111  CYS J CA  1 
ATOM   10672 C  C   . CYS J  1 111 ? 51.309  87.586  39.116  1.00 5.98  ? 111  CYS J C   1 
ATOM   10673 O  O   . CYS J  1 111 ? 50.938  86.516  39.584  1.00 6.09  ? 111  CYS J O   1 
ATOM   10674 C  CB  . CYS J  1 111 ? 53.166  87.018  37.570  1.00 8.01  ? 111  CYS J CB  1 
ATOM   10675 S  SG  . CYS J  1 111 ? 52.325  87.669  36.161  1.00 15.24 ? 111  CYS J SG  1 
ATOM   10676 N  N   . ILE J  1 112 ? 50.498  88.617  38.917  1.00 5.00  ? 112  ILE J N   1 
ATOM   10677 C  CA  . ILE J  1 112 ? 49.052  88.566  39.212  1.00 5.00  ? 112  ILE J CA  1 
ATOM   10678 C  C   . ILE J  1 112 ? 48.188  88.435  37.960  1.00 5.08  ? 112  ILE J C   1 
ATOM   10679 O  O   . ILE J  1 112 ? 46.961  88.398  38.066  1.00 5.00  ? 112  ILE J O   1 
ATOM   10680 C  CB  . ILE J  1 112 ? 48.585  89.798  40.018  1.00 5.00  ? 112  ILE J CB  1 
ATOM   10681 C  CG1 . ILE J  1 112 ? 48.755  91.127  39.236  1.00 5.19  ? 112  ILE J CG1 1 
ATOM   10682 C  CG2 . ILE J  1 112 ? 49.292  89.819  41.420  1.00 5.00  ? 112  ILE J CG2 1 
ATOM   10683 C  CD1 . ILE J  1 112 ? 48.168  92.378  39.969  1.00 5.83  ? 112  ILE J CD1 1 
ATOM   10684 N  N   . ILE J  1 113 ? 48.819  88.374  36.783  1.00 5.00  ? 113  ILE J N   1 
ATOM   10685 C  CA  . ILE J  1 113 ? 48.036  88.210  35.548  1.00 5.46  ? 113  ILE J CA  1 
ATOM   10686 C  C   . ILE J  1 113 ? 47.316  86.838  35.602  1.00 5.00  ? 113  ILE J C   1 
ATOM   10687 O  O   . ILE J  1 113 ? 47.932  85.814  35.930  1.00 5.00  ? 113  ILE J O   1 
ATOM   10688 C  CB  . ILE J  1 113 ? 48.952  88.224  34.323  1.00 6.52  ? 113  ILE J CB  1 
ATOM   10689 C  CG1 . ILE J  1 113 ? 49.643  89.569  34.148  1.00 9.92  ? 113  ILE J CG1 1 
ATOM   10690 C  CG2 . ILE J  1 113 ? 48.175  87.818  33.027  1.00 6.97  ? 113  ILE J CG2 1 
ATOM   10691 C  CD1 . ILE J  1 113 ? 48.765  90.667  34.064  1.00 13.40 ? 113  ILE J CD1 1 
ATOM   10692 N  N   . GLY J  1 114 ? 46.039  86.805  35.251  1.00 5.00  ? 114  GLY J N   1 
ATOM   10693 C  CA  . GLY J  1 114 ? 45.308  85.551  35.292  1.00 5.00  ? 114  GLY J CA  1 
ATOM   10694 C  C   . GLY J  1 114 ? 44.798  85.211  36.679  1.00 5.00  ? 114  GLY J C   1 
ATOM   10695 O  O   . GLY J  1 114 ? 44.193  84.144  36.855  1.00 5.00  ? 114  GLY J O   1 
ATOM   10696 N  N   . ARG J  1 115 ? 45.040  86.099  37.657  1.00 5.00  ? 115  ARG J N   1 
ATOM   10697 C  CA  . ARG J  1 115 ? 44.414  85.916  38.987  1.00 5.00  ? 115  ARG J CA  1 
ATOM   10698 C  C   . ARG J  1 115 ? 43.185  86.832  39.070  1.00 5.00  ? 115  ARG J C   1 
ATOM   10699 O  O   . ARG J  1 115 ? 42.842  87.495  38.083  1.00 5.00  ? 115  ARG J O   1 
ATOM   10700 C  CB  . ARG J  1 115 ? 45.464  86.133  40.120  1.00 5.00  ? 115  ARG J CB  1 
ATOM   10701 C  CG  . ARG J  1 115 ? 46.662  85.142  39.841  1.00 5.00  ? 115  ARG J CG  1 
ATOM   10702 C  CD  . ARG J  1 115 ? 47.687  85.078  40.951  1.00 7.68  ? 115  ARG J CD  1 
ATOM   10703 N  NE  . ARG J  1 115 ? 48.825  84.216  40.611  1.00 5.81  ? 115  ARG J NE  1 
ATOM   10704 C  CZ  . ARG J  1 115 ? 48.866  82.892  40.815  1.00 9.30  ? 115  ARG J CZ  1 
ATOM   10705 N  NH1 . ARG J  1 115 ? 47.838  82.229  41.333  1.00 5.59  ? 115  ARG J NH1 1 
ATOM   10706 N  NH2 . ARG J  1 115 ? 49.967  82.223  40.510  1.00 7.38  ? 115  ARG J NH2 1 
ATOM   10707 N  N   . THR J  1 116 ? 42.517  86.889  40.223  1.00 5.00  ? 116  THR J N   1 
ATOM   10708 C  CA  . THR J  1 116 ? 41.288  87.678  40.337  1.00 5.00  ? 116  THR J CA  1 
ATOM   10709 C  C   . THR J  1 116 ? 41.415  88.869  41.269  1.00 5.09  ? 116  THR J C   1 
ATOM   10710 O  O   . THR J  1 116 ? 41.920  88.726  42.378  1.00 5.00  ? 116  THR J O   1 
ATOM   10711 C  CB  . THR J  1 116 ? 40.168  86.778  40.896  1.00 5.00  ? 116  THR J CB  1 
ATOM   10712 O  OG1 . THR J  1 116 ? 39.835  85.843  39.874  1.00 5.00  ? 116  THR J OG1 1 
ATOM   10713 C  CG2 . THR J  1 116 ? 38.864  87.569  41.101  1.00 5.00  ? 116  THR J CG2 1 
ATOM   10714 N  N   . LEU J  1 117 ? 40.992  90.041  40.806  1.00 5.00  ? 117  LEU J N   1 
ATOM   10715 C  CA  . LEU J  1 117 ? 40.935  91.225  41.683  1.00 5.00  ? 117  LEU J CA  1 
ATOM   10716 C  C   . LEU J  1 117 ? 39.555  91.248  42.298  1.00 5.00  ? 117  LEU J C   1 
ATOM   10717 O  O   . LEU J  1 117 ? 38.556  91.108  41.563  1.00 5.00  ? 117  LEU J O   1 
ATOM   10718 C  CB  . LEU J  1 117 ? 41.085  92.484  40.810  1.00 5.00  ? 117  LEU J CB  1 
ATOM   10719 C  CG  . LEU J  1 117 ? 41.144  93.819  41.551  1.00 5.00  ? 117  LEU J CG  1 
ATOM   10720 C  CD1 . LEU J  1 117 ? 42.361  93.864  42.523  1.00 5.00  ? 117  LEU J CD1 1 
ATOM   10721 C  CD2 . LEU J  1 117 ? 41.269  95.001  40.563  1.00 5.69  ? 117  LEU J CD2 1 
ATOM   10722 N  N   . VAL J  1 118 ? 39.496  91.499  43.599  1.00 5.00  ? 118  VAL J N   1 
ATOM   10723 C  CA  . VAL J  1 118 ? 38.211  91.547  44.309  1.00 5.00  ? 118  VAL J CA  1 
ATOM   10724 C  C   . VAL J  1 118 ? 38.038  92.818  45.094  1.00 5.00  ? 118  VAL J C   1 
ATOM   10725 O  O   . VAL J  1 118 ? 38.968  93.223  45.778  1.00 5.00  ? 118  VAL J O   1 
ATOM   10726 C  CB  . VAL J  1 118 ? 38.078  90.352  45.304  1.00 5.00  ? 118  VAL J CB  1 
ATOM   10727 C  CG1 . VAL J  1 118 ? 36.716  90.450  46.088  1.00 5.00  ? 118  VAL J CG1 1 
ATOM   10728 C  CG2 . VAL J  1 118 ? 38.124  89.051  44.536  1.00 5.00  ? 118  VAL J CG2 1 
ATOM   10729 N  N   . VAL J  1 119 ? 36.857  93.460  44.964  1.00 5.00  ? 119  VAL J N   1 
ATOM   10730 C  CA  . VAL J  1 119 ? 36.480  94.551  45.875  1.00 5.00  ? 119  VAL J CA  1 
ATOM   10731 C  C   . VAL J  1 119 ? 35.411  94.050  46.854  1.00 5.00  ? 119  VAL J C   1 
ATOM   10732 O  O   . VAL J  1 119 ? 34.433  93.402  46.474  1.00 5.00  ? 119  VAL J O   1 
ATOM   10733 C  CB  . VAL J  1 119 ? 36.076  95.840  45.133  1.00 5.32  ? 119  VAL J CB  1 
ATOM   10734 C  CG1 . VAL J  1 119 ? 34.841  95.595  44.280  1.00 5.51  ? 119  VAL J CG1 1 
ATOM   10735 C  CG2 . VAL J  1 119 ? 35.896  97.031  46.164  1.00 5.62  ? 119  VAL J CG2 1 
ATOM   10736 N  N   . HIS J  1 120 ? 35.603  94.360  48.129  1.00 5.00  ? 120  HIS J N   1 
ATOM   10737 C  CA  . HIS J  1 120 ? 34.800  93.752  49.185  1.00 5.00  ? 120  HIS J CA  1 
ATOM   10738 C  C   . HIS J  1 120 ? 33.758  94.673  49.792  1.00 5.98  ? 120  HIS J C   1 
ATOM   10739 O  O   . HIS J  1 120 ? 33.796  95.892  49.630  1.00 5.15  ? 120  HIS J O   1 
ATOM   10740 C  CB  . HIS J  1 120 ? 35.746  93.383  50.329  1.00 5.00  ? 120  HIS J CB  1 
ATOM   10741 C  CG  . HIS J  1 120 ? 36.447  92.098  50.107  1.00 5.22  ? 120  HIS J CG  1 
ATOM   10742 N  ND1 . HIS J  1 120 ? 35.874  90.886  50.410  1.00 5.00  ? 120  HIS J ND1 1 
ATOM   10743 C  CD2 . HIS J  1 120 ? 37.664  91.821  49.582  1.00 5.00  ? 120  HIS J CD2 1 
ATOM   10744 C  CE1 . HIS J  1 120 ? 36.716  89.911  50.104  1.00 7.19  ? 120  HIS J CE1 1 
ATOM   10745 N  NE2 . HIS J  1 120 ? 37.795  90.455  49.591  1.00 5.00  ? 120  HIS J NE2 1 
ATOM   10746 N  N   . GLU J  1 121 ? 32.872  94.049  50.560  1.00 6.45  ? 121  GLU J N   1 
ATOM   10747 C  CA  . GLU J  1 121 ? 31.739  94.685  51.211  1.00 7.45  ? 121  GLU J CA  1 
ATOM   10748 C  C   . GLU J  1 121 ? 32.148  95.713  52.250  1.00 8.20  ? 121  GLU J C   1 
ATOM   10749 O  O   . GLU J  1 121 ? 31.531  96.792  52.353  1.00 8.59  ? 121  GLU J O   1 
ATOM   10750 C  CB  . GLU J  1 121 ? 30.943  93.581  51.903  1.00 7.97  ? 121  GLU J CB  1 
ATOM   10751 C  CG  . GLU J  1 121 ? 29.716  94.046  52.695  1.00 10.21 ? 121  GLU J CG  1 
ATOM   10752 C  CD  . GLU J  1 121 ? 29.137  92.922  53.545  1.00 17.31 ? 121  GLU J CD  1 
ATOM   10753 O  OE1 . GLU J  1 121 ? 29.802  91.859  53.706  1.00 12.46 ? 121  GLU J OE1 1 
ATOM   10754 O  OE2 . GLU J  1 121 ? 28.030  93.119  54.101  1.00 19.45 ? 121  GLU J OE2 1 
ATOM   10755 N  N   . LYS J  1 122 ? 33.140  95.360  53.057  1.00 7.78  ? 122  LYS J N   1 
ATOM   10756 C  CA  . LYS J  1 122 ? 33.559  96.226  54.173  1.00 9.28  ? 122  LYS J CA  1 
ATOM   10757 C  C   . LYS J  1 122 ? 35.044  96.505  54.175  1.00 8.27  ? 122  LYS J C   1 
ATOM   10758 O  O   . LYS J  1 122 ? 35.800  96.030  53.331  1.00 7.24  ? 122  LYS J O   1 
ATOM   10759 C  CB  . LYS J  1 122 ? 33.272  95.552  55.526  1.00 10.24 ? 122  LYS J CB  1 
ATOM   10760 C  CG  . LYS J  1 122 ? 32.210  94.549  55.499  1.00 16.03 ? 122  LYS J CG  1 
ATOM   10761 C  CD  . LYS J  1 122 ? 31.824  94.176  56.890  1.00 22.39 ? 122  LYS J CD  1 
ATOM   10762 C  CE  . LYS J  1 122 ? 31.959  92.675  57.107  1.00 26.28 ? 122  LYS J CE  1 
ATOM   10763 N  NZ  . LYS J  1 122 ? 32.431  92.421  58.509  1.00 29.21 ? 122  LYS J NZ  1 
ATOM   10764 N  N   . ALA J  1 123 ? 35.456  97.270  55.183  1.00 7.56  ? 123  ALA J N   1 
ATOM   10765 C  CA  . ALA J  1 123 ? 36.849  97.572  55.291  1.00 7.58  ? 123  ALA J CA  1 
ATOM   10766 C  C   . ALA J  1 123 ? 37.667  96.353  55.633  1.00 6.19  ? 123  ALA J C   1 
ATOM   10767 O  O   . ALA J  1 123 ? 37.256  95.499  56.421  1.00 6.29  ? 123  ALA J O   1 
ATOM   10768 C  CB  . ALA J  1 123 ? 37.101  98.672  56.388  1.00 6.58  ? 123  ALA J CB  1 
ATOM   10769 N  N   . ASP J  1 124 ? 38.844  96.323  55.048  1.00 6.50  ? 124  ASP J N   1 
ATOM   10770 C  CA  . ASP J  1 124 ? 39.890  95.394  55.395  1.00 6.31  ? 124  ASP J CA  1 
ATOM   10771 C  C   . ASP J  1 124 ? 40.516  95.949  56.695  1.00 6.73  ? 124  ASP J C   1 
ATOM   10772 O  O   . ASP J  1 124 ? 40.980  97.109  56.750  1.00 5.72  ? 124  ASP J O   1 
ATOM   10773 C  CB  . ASP J  1 124 ? 40.894  95.330  54.246  1.00 7.67  ? 124  ASP J CB  1 
ATOM   10774 C  CG  . ASP J  1 124 ? 42.038  94.349  54.474  1.00 7.30  ? 124  ASP J CG  1 
ATOM   10775 O  OD1 . ASP J  1 124 ? 42.379  93.965  55.637  1.00 5.61  ? 124  ASP J OD1 1 
ATOM   10776 O  OD2 . ASP J  1 124 ? 42.702  93.925  53.485  1.00 9.53  ? 124  ASP J OD2 1 
ATOM   10777 N  N   . ASP J  1 125 ? 40.526  95.135  57.758  1.00 5.14  ? 125  ASP J N   1 
ATOM   10778 C  CA  . ASP J  1 125 ? 41.072  95.630  59.018  1.00 5.14  ? 125  ASP J CA  1 
ATOM   10779 C  C   . ASP J  1 125 ? 42.588  95.459  59.134  1.00 5.16  ? 125  ASP J C   1 
ATOM   10780 O  O   . ASP J  1 125 ? 43.156  95.706  60.189  1.00 5.00  ? 125  ASP J O   1 
ATOM   10781 C  CB  . ASP J  1 125 ? 40.364  94.964  60.222  1.00 5.00  ? 125  ASP J CB  1 
ATOM   10782 C  CG  . ASP J  1 125 ? 40.635  93.475  60.323  1.00 6.15  ? 125  ASP J CG  1 
ATOM   10783 O  OD1 . ASP J  1 125 ? 41.645  92.932  59.780  1.00 5.00  ? 125  ASP J OD1 1 
ATOM   10784 O  OD2 . ASP J  1 125 ? 39.870  92.743  61.007  1.00 5.00  ? 125  ASP J OD2 1 
ATOM   10785 N  N   . LEU J  1 126 ? 43.221  95.031  58.047  1.00 5.24  ? 126  LEU J N   1 
ATOM   10786 C  CA  . LEU J  1 126 ? 44.669  94.935  57.925  1.00 5.70  ? 126  LEU J CA  1 
ATOM   10787 C  C   . LEU J  1 126 ? 45.317  93.990  58.910  1.00 6.27  ? 126  LEU J C   1 
ATOM   10788 O  O   . LEU J  1 126 ? 46.490  94.132  59.207  1.00 7.64  ? 126  LEU J O   1 
ATOM   10789 C  CB  . LEU J  1 126 ? 45.297  96.333  57.966  1.00 5.71  ? 126  LEU J CB  1 
ATOM   10790 C  CG  . LEU J  1 126 ? 44.610  97.346  57.036  1.00 7.18  ? 126  LEU J CG  1 
ATOM   10791 C  CD1 . LEU J  1 126 ? 45.387  98.650  57.120  1.00 9.67  ? 126  LEU J CD1 1 
ATOM   10792 C  CD2 . LEU J  1 126 ? 44.522  96.820  55.593  1.00 6.85  ? 126  LEU J CD2 1 
ATOM   10793 N  N   . GLY J  1 127 ? 44.535  93.012  59.401  1.00 5.27  ? 127  GLY J N   1 
ATOM   10794 C  CA  . GLY J  1 127 ? 45.038  92.029  60.340  1.00 5.53  ? 127  GLY J CA  1 
ATOM   10795 C  C   . GLY J  1 127 ? 44.914  92.456  61.770  1.00 5.27  ? 127  GLY J C   1 
ATOM   10796 O  O   . GLY J  1 127 ? 45.466  91.781  62.680  1.00 5.78  ? 127  GLY J O   1 
ATOM   10797 N  N   . LYS J  1 128 ? 44.196  93.549  62.025  1.00 5.00  ? 128  LYS J N   1 
ATOM   10798 C  CA  . LYS J  1 128 ? 44.155  94.038  63.401  1.00 5.44  ? 128  LYS J CA  1 
ATOM   10799 C  C   . LYS J  1 128 ? 42.827  93.868  64.121  1.00 5.00  ? 128  LYS J C   1 
ATOM   10800 O  O   . LYS J  1 128 ? 42.547  94.602  65.080  1.00 5.00  ? 128  LYS J O   1 
ATOM   10801 C  CB  . LYS J  1 128 ? 44.557  95.509  63.478  1.00 5.30  ? 128  LYS J CB  1 
ATOM   10802 C  CG  . LYS J  1 128 ? 45.929  95.808  62.828  1.00 10.91 ? 128  LYS J CG  1 
ATOM   10803 C  CD  . LYS J  1 128 ? 46.259  97.296  62.880  1.00 16.90 ? 128  LYS J CD  1 
ATOM   10804 C  CE  . LYS J  1 128 ? 47.734  97.492  62.507  1.00 23.85 ? 128  LYS J CE  1 
ATOM   10805 N  N   . GLY J  1 129 ? 42.054  92.896  63.686  1.00 5.00  ? 129  GLY J N   1 
ATOM   10806 C  CA  . GLY J  1 129 ? 40.704  92.704  64.190  1.00 5.00  ? 129  GLY J CA  1 
ATOM   10807 C  C   . GLY J  1 129 ? 40.537  91.719  65.355  1.00 5.00  ? 129  GLY J C   1 
ATOM   10808 O  O   . GLY J  1 129 ? 39.429  91.511  65.825  1.00 5.00  ? 129  GLY J O   1 
ATOM   10809 N  N   . GLY J  1 130 ? 41.628  91.099  65.805  1.00 5.00  ? 130  GLY J N   1 
ATOM   10810 C  CA  . GLY J  1 130 ? 41.520  90.256  66.991  1.00 5.00  ? 130  GLY J CA  1 
ATOM   10811 C  C   . GLY J  1 130 ? 40.847  88.891  66.813  1.00 5.00  ? 130  GLY J C   1 
ATOM   10812 O  O   . GLY J  1 130 ? 40.315  88.296  67.775  1.00 5.17  ? 130  GLY J O   1 
ATOM   10813 N  N   . ASN J  1 131 ? 40.843  88.392  65.588  1.00 5.23  ? 131  ASN J N   1 
ATOM   10814 C  CA  . ASN J  1 131 ? 40.333  87.035  65.377  1.00 6.23  ? 131  ASN J CA  1 
ATOM   10815 C  C   . ASN J  1 131 ? 41.012  86.343  64.233  1.00 6.88  ? 131  ASN J C   1 
ATOM   10816 O  O   . ASN J  1 131 ? 41.855  86.951  63.525  1.00 5.11  ? 131  ASN J O   1 
ATOM   10817 C  CB  . ASN J  1 131 ? 38.799  86.966  65.256  1.00 6.34  ? 131  ASN J CB  1 
ATOM   10818 C  CG  . ASN J  1 131 ? 38.233  87.777  64.111  1.00 9.88  ? 131  ASN J CG  1 
ATOM   10819 O  OD1 . ASN J  1 131 ? 38.912  88.107  63.132  1.00 8.08  ? 131  ASN J OD1 1 
ATOM   10820 N  ND2 . ASN J  1 131 ? 36.940  88.042  64.193  1.00 12.46 ? 131  ASN J ND2 1 
ATOM   10821 N  N   . GLU J  1 132 ? 40.680  85.069  64.062  1.00 6.28  ? 132  GLU J N   1 
ATOM   10822 C  CA  . GLU J  1 132 ? 41.339  84.295  63.001  1.00 9.06  ? 132  GLU J CA  1 
ATOM   10823 C  C   . GLU J  1 132 ? 41.014  84.829  61.602  1.00 8.42  ? 132  GLU J C   1 
ATOM   10824 O  O   . GLU J  1 132 ? 41.878  84.902  60.713  1.00 6.41  ? 132  GLU J O   1 
ATOM   10825 C  CB  . GLU J  1 132 ? 41.058  82.794  63.169  1.00 9.41  ? 132  GLU J CB  1 
ATOM   10826 C  CG  . GLU J  1 132 ? 41.922  81.915  62.263  1.00 15.86 ? 132  GLU J CG  1 
ATOM   10827 C  CD  . GLU J  1 132 ? 41.758  80.421  62.536  1.00 20.91 ? 132  GLU J CD  1 
ATOM   10828 O  OE1 . GLU J  1 132 ? 41.332  80.042  63.655  1.00 25.29 ? 132  GLU J OE1 1 
ATOM   10829 O  OE2 . GLU J  1 132 ? 42.066  79.634  61.618  1.00 24.71 ? 132  GLU J OE2 1 
ATOM   10830 N  N   . GLU J  1 133 ? 39.779  85.256  61.416  1.00 8.27  ? 133  GLU J N   1 
ATOM   10831 C  CA  . GLU J  1 133 ? 39.362  85.812  60.131  1.00 9.28  ? 133  GLU J CA  1 
ATOM   10832 C  C   . GLU J  1 133 ? 40.207  87.051  59.739  1.00 8.79  ? 133  GLU J C   1 
ATOM   10833 O  O   . GLU J  1 133 ? 40.575  87.233  58.556  1.00 8.09  ? 133  GLU J O   1 
ATOM   10834 C  CB  . GLU J  1 133 ? 37.883  86.181  60.196  1.00 10.79 ? 133  GLU J CB  1 
ATOM   10835 C  CG  . GLU J  1 133 ? 37.307  86.558  58.844  1.00 12.24 ? 133  GLU J CG  1 
ATOM   10836 C  CD  . GLU J  1 133 ? 37.308  85.402  57.861  1.00 17.81 ? 133  GLU J CD  1 
ATOM   10837 O  OE1 . GLU J  1 133 ? 36.941  84.269  58.237  1.00 19.13 ? 133  GLU J OE1 1 
ATOM   10838 O  OE2 . GLU J  1 133 ? 37.703  85.625  56.708  1.00 20.03 ? 133  GLU J OE2 1 
ATOM   10839 N  N   . SER J  1 134 ? 40.534  87.880  60.731  1.00 6.43  ? 134  SER J N   1 
ATOM   10840 C  CA  . SER J  1 134 ? 41.388  89.045  60.480  1.00 5.54  ? 134  SER J CA  1 
ATOM   10841 C  C   . SER J  1 134 ? 42.715  88.651  59.853  1.00 6.39  ? 134  SER J C   1 
ATOM   10842 O  O   . SER J  1 134 ? 43.217  89.345  58.952  1.00 5.00  ? 134  SER J O   1 
ATOM   10843 C  CB  . SER J  1 134 ? 41.661  89.827  61.791  1.00 5.49  ? 134  SER J CB  1 
ATOM   10844 O  OG  . SER J  1 134 ? 42.388  91.012  61.502  1.00 5.00  ? 134  SER J OG  1 
ATOM   10845 N  N   . THR J  1 135 ? 43.297  87.560  60.339  1.00 7.11  ? 135  THR J N   1 
ATOM   10846 C  CA  . THR J  1 135 ? 44.583  87.082  59.824  1.00 9.67  ? 135  THR J CA  1 
ATOM   10847 C  C   . THR J  1 135 ? 44.449  86.357  58.497  1.00 9.93  ? 135  THR J C   1 
ATOM   10848 O  O   . THR J  1 135 ? 45.459  85.909  57.919  1.00 9.42  ? 135  THR J O   1 
ATOM   10849 C  CB  . THR J  1 135 ? 45.268  86.154  60.846  1.00 11.16 ? 135  THR J CB  1 
ATOM   10850 O  OG1 . THR J  1 135 ? 44.647  84.860  60.758  1.00 14.83 ? 135  THR J OG1 1 
ATOM   10851 C  CG2 . THR J  1 135 ? 44.977  86.605  62.176  1.00 11.56 ? 135  THR J CG2 1 
ATOM   10852 N  N   . LYS J  1 136 ? 43.222  86.258  57.985  1.00 10.33 ? 136  LYS J N   1 
ATOM   10853 C  CA  . LYS J  1 136 ? 42.994  85.624  56.695  1.00 11.58 ? 136  LYS J CA  1 
ATOM   10854 C  C   . LYS J  1 136 ? 42.506  86.546  55.601  1.00 10.97 ? 136  LYS J C   1 
ATOM   10855 O  O   . LYS J  1 136 ? 43.080  86.568  54.505  1.00 10.81 ? 136  LYS J O   1 
ATOM   10856 C  CB  . LYS J  1 136 ? 41.998  84.468  56.819  1.00 11.64 ? 136  LYS J CB  1 
ATOM   10857 C  CG  . LYS J  1 136 ? 42.558  83.316  57.602  1.00 16.39 ? 136  LYS J CG  1 
ATOM   10858 C  CD  . LYS J  1 136 ? 41.713  82.068  57.399  1.00 21.39 ? 136  LYS J CD  1 
ATOM   10859 N  N   . THR J  1 137 ? 41.455  87.303  55.905  1.00 10.32 ? 137  THR J N   1 
ATOM   10860 C  CA  . THR J  1 137 ? 40.812  88.136  54.916  1.00 10.55 ? 137  THR J CA  1 
ATOM   10861 C  C   . THR J  1 137 ? 40.709  89.571  55.382  1.00 9.81  ? 137  THR J C   1 
ATOM   10862 O  O   . THR J  1 137 ? 40.160  90.393  54.669  1.00 10.11 ? 137  THR J O   1 
ATOM   10863 C  CB  . THR J  1 137 ? 39.377  87.623  54.715  1.00 11.34 ? 137  THR J CB  1 
ATOM   10864 O  OG1 . THR J  1 137 ? 38.677  87.706  55.967  1.00 10.50 ? 137  THR J OG1 1 
ATOM   10865 C  CG2 . THR J  1 137 ? 39.342  86.131  54.416  1.00 13.09 ? 137  THR J CG2 1 
ATOM   10866 N  N   . GLY J  1 138 ? 41.185  89.888  56.598  1.00 8.02  ? 138  GLY J N   1 
ATOM   10867 C  CA  . GLY J  1 138 ? 40.997  91.224  57.135  1.00 5.57  ? 138  GLY J CA  1 
ATOM   10868 C  C   . GLY J  1 138 ? 39.523  91.559  57.452  1.00 5.73  ? 138  GLY J C   1 
ATOM   10869 O  O   . GLY J  1 138 ? 39.168  92.721  57.626  1.00 5.00  ? 138  GLY J O   1 
ATOM   10870 N  N   . ASN J  1 139 ? 38.662  90.546  57.519  1.00 5.15  ? 139  ASN J N   1 
ATOM   10871 C  CA  . ASN J  1 139 ? 37.237  90.752  57.829  1.00 6.63  ? 139  ASN J CA  1 
ATOM   10872 C  C   . ASN J  1 139 ? 36.567  91.692  56.835  1.00 6.10  ? 139  ASN J C   1 
ATOM   10873 O  O   . ASN J  1 139 ? 35.647  92.420  57.166  1.00 6.55  ? 139  ASN J O   1 
ATOM   10874 C  CB  . ASN J  1 139 ? 37.065  91.282  59.280  1.00 7.64  ? 139  ASN J CB  1 
ATOM   10875 C  CG  . ASN J  1 139 ? 37.192  90.193  60.305  1.00 9.62  ? 139  ASN J CG  1 
ATOM   10876 O  OD1 . ASN J  1 139 ? 36.394  89.256  60.309  1.00 10.01 ? 139  ASN J OD1 1 
ATOM   10877 N  ND2 . ASN J  1 139 ? 38.186  90.311  61.196  1.00 7.48  ? 139  ASN J ND2 1 
ATOM   10878 N  N   . ALA J  1 140 ? 37.021  91.683  55.581  1.00 5.00  ? 140  ALA J N   1 
ATOM   10879 C  CA  . ALA J  1 140 ? 36.445  92.599  54.609  1.00 5.92  ? 140  ALA J CA  1 
ATOM   10880 C  C   . ALA J  1 140 ? 35.081  92.156  54.123  1.00 6.61  ? 140  ALA J C   1 
ATOM   10881 O  O   . ALA J  1 140 ? 34.447  92.832  53.302  1.00 6.85  ? 140  ALA J O   1 
ATOM   10882 C  CB  . ALA J  1 140 ? 37.409  92.746  53.391  1.00 5.00  ? 140  ALA J CB  1 
ATOM   10883 N  N   . GLY J  1 141 ? 34.641  90.990  54.593  1.00 7.28  ? 141  GLY J N   1 
ATOM   10884 C  CA  . GLY J  1 141 ? 33.308  90.513  54.243  1.00 7.88  ? 141  GLY J CA  1 
ATOM   10885 C  C   . GLY J  1 141 ? 33.134  90.045  52.803  1.00 7.62  ? 141  GLY J C   1 
ATOM   10886 O  O   . GLY J  1 141 ? 34.112  89.619  52.117  1.00 7.10  ? 141  GLY J O   1 
ATOM   10887 N  N   . SER J  1 142 ? 31.910  90.174  52.300  1.00 6.43  ? 142  SER J N   1 
ATOM   10888 C  CA  . SER J  1 142 ? 31.590  89.576  51.006  1.00 6.18  ? 142  SER J CA  1 
ATOM   10889 C  C   . SER J  1 142 ? 32.334  90.196  49.815  1.00 6.63  ? 142  SER J C   1 
ATOM   10890 O  O   . SER J  1 142 ? 32.887  91.298  49.886  1.00 5.42  ? 142  SER J O   1 
ATOM   10891 C  CB  . SER J  1 142 ? 30.077  89.517  50.769  1.00 7.90  ? 142  SER J CB  1 
ATOM   10892 O  OG  . SER J  1 142 ? 29.592  90.779  50.389  1.00 8.18  ? 142  SER J OG  1 
ATOM   10893 N  N   . ARG J  1 143 ? 32.352  89.452  48.719  1.00 5.98  ? 143  ARG J N   1 
ATOM   10894 C  CA  . ARG J  1 143 ? 33.047  89.879  47.521  1.00 6.08  ? 143  ARG J CA  1 
ATOM   10895 C  C   . ARG J  1 143 ? 32.004  90.512  46.638  1.00 6.44  ? 143  ARG J C   1 
ATOM   10896 O  O   . ARG J  1 143 ? 31.145  89.805  46.079  1.00 7.27  ? 143  ARG J O   1 
ATOM   10897 C  CB  . ARG J  1 143 ? 33.593  88.633  46.843  1.00 6.24  ? 143  ARG J CB  1 
ATOM   10898 C  CG  . ARG J  1 143 ? 34.564  87.913  47.752  1.00 5.19  ? 143  ARG J CG  1 
ATOM   10899 C  CD  . ARG J  1 143 ? 35.137  86.615  47.191  1.00 5.53  ? 143  ARG J CD  1 
ATOM   10900 N  NE  . ARG J  1 143 ? 35.886  85.940  48.264  1.00 5.87  ? 143  ARG J NE  1 
ATOM   10901 C  CZ  . ARG J  1 143 ? 36.741  84.921  48.069  1.00 8.18  ? 143  ARG J CZ  1 
ATOM   10902 N  NH1 . ARG J  1 143 ? 36.988  84.452  46.835  1.00 7.61  ? 143  ARG J NH1 1 
ATOM   10903 N  NH2 . ARG J  1 143 ? 37.388  84.408  49.110  1.00 6.46  ? 143  ARG J NH2 1 
ATOM   10904 N  N   . LEU J  1 144 ? 32.015  91.835  46.564  1.00 5.10  ? 144  LEU J N   1 
ATOM   10905 C  CA  . LEU J  1 144 ? 30.984  92.552  45.837  1.00 5.00  ? 144  LEU J CA  1 
ATOM   10906 C  C   . LEU J  1 144 ? 31.165  92.528  44.329  1.00 5.00  ? 144  LEU J C   1 
ATOM   10907 O  O   . LEU J  1 144 ? 30.201  92.535  43.591  1.00 5.00  ? 144  LEU J O   1 
ATOM   10908 C  CB  . LEU J  1 144 ? 30.933  93.999  46.279  1.00 5.88  ? 144  LEU J CB  1 
ATOM   10909 C  CG  . LEU J  1 144 ? 30.590  94.236  47.760  1.00 7.79  ? 144  LEU J CG  1 
ATOM   10910 C  CD1 . LEU J  1 144 ? 30.537  95.772  47.958  1.00 9.83  ? 144  LEU J CD1 1 
ATOM   10911 C  CD2 . LEU J  1 144 ? 29.272  93.594  48.177  1.00 5.70  ? 144  LEU J CD2 1 
ATOM   10912 N  N   . ALA J  1 145 ? 32.412  92.551  43.868  1.00 5.00  ? 145  ALA J N   1 
ATOM   10913 C  CA  . ALA J  1 145 ? 32.630  92.452  42.444  1.00 5.00  ? 145  ALA J CA  1 
ATOM   10914 C  C   . ALA J  1 145 ? 34.055  91.925  42.259  1.00 5.49  ? 145  ALA J C   1 
ATOM   10915 O  O   . ALA J  1 145 ? 34.934  92.141  43.112  1.00 5.00  ? 145  ALA J O   1 
ATOM   10916 C  CB  . ALA J  1 145 ? 32.505  93.829  41.759  1.00 5.00  ? 145  ALA J CB  1 
ATOM   10917 N  N   . CYS J  1 146 ? 34.286  91.292  41.118  1.00 5.00  ? 146  CYS J N   1 
ATOM   10918 C  CA  . CYS J  1 146 ? 35.630  90.777  40.832  1.00 5.00  ? 146  CYS J CA  1 
ATOM   10919 C  C   . CYS J  1 146 ? 35.813  90.598  39.340  1.00 5.00  ? 146  CYS J C   1 
ATOM   10920 O  O   . CYS J  1 146 ? 34.836  90.657  38.556  1.00 5.00  ? 146  CYS J O   1 
ATOM   10921 C  CB  . CYS J  1 146 ? 35.832  89.410  41.464  1.00 6.21  ? 146  CYS J CB  1 
ATOM   10922 S  SG  . CYS J  1 146 ? 34.653  88.158  40.881  1.00 9.01  ? 146  CYS J SG  1 
ATOM   10923 N  N   . GLY J  1 147 ? 37.058  90.345  38.941  1.00 5.00  ? 147  GLY J N   1 
ATOM   10924 C  CA  . GLY J  1 147 ? 37.303  90.022  37.545  1.00 5.00  ? 147  GLY J CA  1 
ATOM   10925 C  C   . GLY J  1 147 ? 38.667  89.366  37.384  1.00 5.00  ? 147  GLY J C   1 
ATOM   10926 O  O   . GLY J  1 147 ? 39.517  89.467  38.259  1.00 5.00  ? 147  GLY J O   1 
ATOM   10927 N  N   . VAL J  1 148 ? 38.907  88.729  36.239  1.00 5.00  ? 148  VAL J N   1 
ATOM   10928 C  CA  . VAL J  1 148 ? 40.249  88.168  36.029  1.00 5.00  ? 148  VAL J CA  1 
ATOM   10929 C  C   . VAL J  1 148 ? 41.158  89.257  35.508  1.00 5.00  ? 148  VAL J C   1 
ATOM   10930 O  O   . VAL J  1 148 ? 40.741  90.049  34.685  1.00 5.00  ? 148  VAL J O   1 
ATOM   10931 C  CB  . VAL J  1 148 ? 40.185  86.994  35.013  1.00 5.00  ? 148  VAL J CB  1 
ATOM   10932 C  CG1 . VAL J  1 148 ? 41.583  86.391  34.780  1.00 5.57  ? 148  VAL J CG1 1 
ATOM   10933 C  CG2 . VAL J  1 148 ? 39.180  85.953  35.526  1.00 6.27  ? 148  VAL J CG2 1 
ATOM   10934 N  N   . ILE J  1 149 ? 42.390  89.309  36.000  1.00 5.00  ? 149  ILE J N   1 
ATOM   10935 C  CA  . ILE J  1 149 ? 43.349  90.321  35.538  1.00 5.22  ? 149  ILE J CA  1 
ATOM   10936 C  C   . ILE J  1 149 ? 43.925  89.864  34.209  1.00 5.00  ? 149  ILE J C   1 
ATOM   10937 O  O   . ILE J  1 149 ? 44.592  88.810  34.142  1.00 5.12  ? 149  ILE J O   1 
ATOM   10938 C  CB  . ILE J  1 149 ? 44.466  90.472  36.590  1.00 5.02  ? 149  ILE J CB  1 
ATOM   10939 C  CG1 . ILE J  1 149 ? 43.809  90.997  37.891  1.00 5.00  ? 149  ILE J CG1 1 
ATOM   10940 C  CG2 . ILE J  1 149 ? 45.476  91.552  36.163  1.00 6.84  ? 149  ILE J CG2 1 
ATOM   10941 C  CD1 . ILE J  1 149 ? 44.712  90.801  39.187  1.00 5.00  ? 149  ILE J CD1 1 
ATOM   10942 N  N   . GLY J  1 150 ? 43.690  90.662  33.163  1.00 5.00  ? 150  GLY J N   1 
ATOM   10943 C  CA  . GLY J  1 150 ? 44.104  90.237  31.823  1.00 5.00  ? 150  GLY J CA  1 
ATOM   10944 C  C   . GLY J  1 150 ? 45.211  91.139  31.254  1.00 5.00  ? 150  GLY J C   1 
ATOM   10945 O  O   . GLY J  1 150 ? 45.388  92.279  31.664  1.00 5.00  ? 150  GLY J O   1 
ATOM   10946 N  N   . ILE J  1 151 ? 45.923  90.612  30.283  1.00 5.00  ? 151  ILE J N   1 
ATOM   10947 C  CA  . ILE J  1 151 ? 46.943  91.369  29.579  1.00 5.00  ? 151  ILE J CA  1 
ATOM   10948 C  C   . ILE J  1 151 ? 46.299  92.480  28.745  1.00 5.00  ? 151  ILE J C   1 
ATOM   10949 O  O   . ILE J  1 151 ? 45.338  92.241  28.029  1.00 5.40  ? 151  ILE J O   1 
ATOM   10950 C  CB  . ILE J  1 151 ? 47.729  90.422  28.688  1.00 5.00  ? 151  ILE J CB  1 
ATOM   10951 C  CG1 . ILE J  1 151 ? 48.540  89.517  29.594  1.00 7.35  ? 151  ILE J CG1 1 
ATOM   10952 C  CG2 . ILE J  1 151 ? 48.680  91.221  27.743  1.00 8.30  ? 151  ILE J CG2 1 
ATOM   10953 C  CD1 . ILE J  1 151 ? 49.114  88.292  28.881  1.00 8.54  ? 151  ILE J CD1 1 
ATOM   10954 N  N   . ALA J  1 152 ? 46.834  93.701  28.835  1.00 5.00  ? 152  ALA J N   1 
ATOM   10955 C  CA  . ALA J  1 152 ? 46.221  94.815  28.097  1.00 5.18  ? 152  ALA J CA  1 
ATOM   10956 C  C   . ALA J  1 152 ? 47.203  95.359  27.084  1.00 6.94  ? 152  ALA J C   1 
ATOM   10957 O  O   . ALA J  1 152 ? 48.425  95.110  27.201  1.00 5.51  ? 152  ALA J O   1 
ATOM   10958 C  CB  . ALA J  1 152 ? 45.793  95.933  29.065  1.00 5.75  ? 152  ALA J CB  1 
ATOM   10959 N  N   . GLN J  1 153 ? 46.673  96.051  26.084  1.00 7.87  ? 153  GLN J N   1 
ATOM   10960 C  CA  . GLN J  1 153 ? 47.517  96.637  25.059  1.00 11.90 ? 153  GLN J CA  1 
ATOM   10961 C  C   . GLN J  1 153 ? 48.224  97.836  25.687  1.00 13.33 ? 153  GLN J C   1 
ATOM   10962 O  O   . GLN J  1 153 ? 47.626  98.632  26.419  1.00 15.11 ? 153  GLN J O   1 
ATOM   10963 C  CB  . GLN J  1 153 ? 46.697  97.099  23.846  1.00 11.03 ? 153  GLN J CB  1 
ATOM   10964 C  CG  . GLN J  1 153 ? 47.582  97.585  22.660  1.00 15.00 ? 153  GLN J CG  1 
ATOM   10965 C  CD  . GLN J  1 153 ? 46.756  97.997  21.470  1.00 17.43 ? 153  GLN J CD  1 
ATOM   10966 O  OE1 . GLN J  1 153 ? 45.777  98.724  21.620  1.00 21.05 ? 153  GLN J OE1 1 
ATOM   10967 N  NE2 . GLN J  1 153 ? 47.122  97.515  20.292  1.00 17.24 ? 153  GLN J NE2 1 
ATOM   10968 O  OXT . GLN J  1 153 ? 49.397  98.016  25.413  1.00 15.46 ? 153  GLN J OXT 1 
ATOM   10969 N  N   . ALA K  1 1   ? -13.488 74.019  83.032  1.00 22.03 ? 1    ALA K N   1 
ATOM   10970 C  CA  . ALA K  1 1   ? -13.952 75.245  82.325  1.00 22.17 ? 1    ALA K CA  1 
ATOM   10971 C  C   . ALA K  1 1   ? -12.833 76.270  82.307  1.00 21.42 ? 1    ALA K C   1 
ATOM   10972 O  O   . ALA K  1 1   ? -11.930 76.156  81.479  1.00 22.69 ? 1    ALA K O   1 
ATOM   10973 C  CB  . ALA K  1 1   ? -15.182 75.814  82.989  1.00 23.66 ? 1    ALA K CB  1 
ATOM   10974 N  N   . THR K  1 2   ? -12.861 77.266  83.188  1.00 18.80 ? 2    THR K N   1 
ATOM   10975 C  CA  . THR K  1 2   ? -11.731 78.182  83.177  1.00 16.94 ? 2    THR K CA  1 
ATOM   10976 C  C   . THR K  1 2   ? -10.599 77.570  83.967  1.00 13.57 ? 2    THR K C   1 
ATOM   10977 O  O   . THR K  1 2   ? -10.817 76.792  84.910  1.00 11.69 ? 2    THR K O   1 
ATOM   10978 C  CB  . THR K  1 2   ? -12.079 79.708  83.438  1.00 17.84 ? 2    THR K CB  1 
ATOM   10979 O  OG1 . THR K  1 2   ? -11.113 80.323  84.295  1.00 21.68 ? 2    THR K OG1 1 
ATOM   10980 C  CG2 . THR K  1 2   ? -13.329 79.865  84.191  1.00 20.34 ? 2    THR K CG2 1 
ATOM   10981 N  N   . LYS K  1 3   ? -9.395  77.830  83.471  1.00 11.25 ? 3    LYS K N   1 
ATOM   10982 C  CA  . LYS K  1 3   ? -8.205  77.223  83.987  1.00 10.16 ? 3    LYS K CA  1 
ATOM   10983 C  C   . LYS K  1 3   ? -7.191  78.334  84.233  1.00 8.87  ? 3    LYS K C   1 
ATOM   10984 O  O   . LYS K  1 3   ? -7.193  79.381  83.555  1.00 7.72  ? 3    LYS K O   1 
ATOM   10985 C  CB  . LYS K  1 3   ? -7.614  76.249  82.965  1.00 10.15 ? 3    LYS K CB  1 
ATOM   10986 C  CG  . LYS K  1 3   ? -8.636  75.197  82.455  1.00 15.50 ? 3    LYS K CG  1 
ATOM   10987 C  CD  . LYS K  1 3   ? -7.979  74.092  81.630  1.00 18.92 ? 3    LYS K CD  1 
ATOM   10988 C  CE  . LYS K  1 3   ? -9.054  73.100  81.127  1.00 24.39 ? 3    LYS K CE  1 
ATOM   10989 N  NZ  . LYS K  1 3   ? -8.532  71.716  80.947  1.00 25.94 ? 3    LYS K NZ  1 
ATOM   10990 N  N   . ALA K  1 4   ? -6.355  78.093  85.225  1.00 6.57  ? 4    ALA K N   1 
ATOM   10991 C  CA  . ALA K  1 4   ? -5.319  79.033  85.536  1.00 6.57  ? 4    ALA K CA  1 
ATOM   10992 C  C   . ALA K  1 4   ? -4.083  78.231  85.953  1.00 5.87  ? 4    ALA K C   1 
ATOM   10993 O  O   . ALA K  1 4   ? -4.181  77.027  86.255  1.00 6.10  ? 4    ALA K O   1 
ATOM   10994 C  CB  . ALA K  1 4   ? -5.794  79.972  86.622  1.00 5.98  ? 4    ALA K CB  1 
ATOM   10995 N  N   . VAL K  1 5   ? -2.919  78.883  85.980  1.00 5.00  ? 5    VAL K N   1 
ATOM   10996 C  CA  . VAL K  1 5   ? -1.716  78.170  86.319  1.00 5.42  ? 5    VAL K CA  1 
ATOM   10997 C  C   . VAL K  1 5   ? -0.795  79.147  87.040  1.00 5.27  ? 5    VAL K C   1 
ATOM   10998 O  O   . VAL K  1 5   ? -0.876  80.361  86.806  1.00 6.20  ? 5    VAL K O   1 
ATOM   10999 C  CB  . VAL K  1 5   ? -1.063  77.548  85.029  1.00 5.00  ? 5    VAL K CB  1 
ATOM   11000 C  CG1 . VAL K  1 5   ? -0.555  78.676  84.069  1.00 5.04  ? 5    VAL K CG1 1 
ATOM   11001 C  CG2 . VAL K  1 5   ? 0.060   76.586  85.401  1.00 7.61  ? 5    VAL K CG2 1 
ATOM   11002 N  N   . CYS K  1 6   ? 0.075   78.625  87.887  1.00 5.00  ? 6    CYS K N   1 
ATOM   11003 C  CA  . CYS K  1 6   ? 1.016   79.441  88.634  1.00 5.57  ? 6    CYS K CA  1 
ATOM   11004 C  C   . CYS K  1 6   ? 2.371   78.729  88.702  1.00 5.61  ? 6    CYS K C   1 
ATOM   11005 O  O   . CYS K  1 6   ? 2.427   77.567  89.139  1.00 6.62  ? 6    CYS K O   1 
ATOM   11006 C  CB  . CYS K  1 6   ? 0.462   79.625  90.056  1.00 5.00  ? 6    CYS K CB  1 
ATOM   11007 S  SG  . CYS K  1 6   ? 1.501   80.773  90.964  1.00 7.01  ? 6    CYS K SG  1 
ATOM   11008 N  N   . VAL K  1 7   ? 3.441   79.404  88.287  1.00 5.00  ? 7    VAL K N   1 
ATOM   11009 C  CA  . VAL K  1 7   ? 4.781   78.857  88.421  1.00 5.00  ? 7    VAL K CA  1 
ATOM   11010 C  C   . VAL K  1 7   ? 5.361   79.473  89.691  1.00 5.01  ? 7    VAL K C   1 
ATOM   11011 O  O   . VAL K  1 7   ? 5.480   80.692  89.788  1.00 5.00  ? 7    VAL K O   1 
ATOM   11012 C  CB  . VAL K  1 7   ? 5.660   79.190  87.219  1.00 5.37  ? 7    VAL K CB  1 
ATOM   11013 C  CG1 . VAL K  1 7   ? 7.079   78.645  87.459  1.00 7.93  ? 7    VAL K CG1 1 
ATOM   11014 C  CG2 . VAL K  1 7   ? 5.086   78.518  85.982  1.00 6.93  ? 7    VAL K CG2 1 
ATOM   11015 N  N   . LEU K  1 8   ? 5.705   78.629  90.662  1.00 5.00  ? 8    LEU K N   1 
ATOM   11016 C  CA  . LEU K  1 8   ? 6.259   79.152  91.919  1.00 5.73  ? 8    LEU K CA  1 
ATOM   11017 C  C   . LEU K  1 8   ? 7.776   79.131  91.877  1.00 6.85  ? 8    LEU K C   1 
ATOM   11018 O  O   . LEU K  1 8   ? 8.364   78.081  91.617  1.00 6.29  ? 8    LEU K O   1 
ATOM   11019 C  CB  . LEU K  1 8   ? 5.803   78.298  93.106  1.00 5.22  ? 8    LEU K CB  1 
ATOM   11020 C  CG  . LEU K  1 8   ? 4.285   78.229  93.354  1.00 9.02  ? 8    LEU K CG  1 
ATOM   11021 C  CD1 . LEU K  1 8   ? 3.958   77.081  94.383  1.00 15.16 ? 8    LEU K CD1 1 
ATOM   11022 C  CD2 . LEU K  1 8   ? 3.796   79.535  93.907  1.00 12.74 ? 8    LEU K CD2 1 
ATOM   11023 N  N   . LYS K  1 9   ? 8.401   80.268  92.161  1.00 7.45  ? 9    LYS K N   1 
ATOM   11024 C  CA  . LYS K  1 9   ? 9.864   80.366  92.252  1.00 9.00  ? 9    LYS K CA  1 
ATOM   11025 C  C   . LYS K  1 9   ? 10.205  81.256  93.428  1.00 8.01  ? 9    LYS K C   1 
ATOM   11026 O  O   . LYS K  1 9   ? 9.407   82.118  93.823  1.00 6.10  ? 9    LYS K O   1 
ATOM   11027 C  CB  . LYS K  1 9   ? 10.430  80.994  90.961  1.00 10.30 ? 9    LYS K CB  1 
ATOM   11028 C  CG  . LYS K  1 9   ? 10.036  80.165  89.747  1.00 17.01 ? 9    LYS K CG  1 
ATOM   11029 C  CD  . LYS K  1 9   ? 10.665  78.765  89.885  1.00 23.98 ? 9    LYS K CD  1 
ATOM   11030 C  CE  . LYS K  1 9   ? 10.271  77.802  88.751  1.00 27.35 ? 9    LYS K CE  1 
ATOM   11031 N  NZ  . LYS K  1 9   ? 11.340  76.767  88.512  1.00 32.15 ? 9    LYS K NZ  1 
ATOM   11032 N  N   . GLY K  1 10  ? 11.388  81.076  94.009  1.00 7.65  ? 10   GLY K N   1 
ATOM   11033 C  CA  . GLY K  1 10  ? 11.752  81.951  95.102  1.00 8.42  ? 10   GLY K CA  1 
ATOM   11034 C  C   . GLY K  1 10  ? 13.256  82.098  95.264  1.00 11.25 ? 10   GLY K C   1 
ATOM   11035 O  O   . GLY K  1 10  ? 14.013  81.838  94.335  1.00 10.49 ? 10   GLY K O   1 
ATOM   11036 N  N   . ASP K  1 11  ? 13.643  82.549  96.448  1.00 12.34 ? 11   ASP K N   1 
ATOM   11037 C  CA  . ASP K  1 11  ? 15.045  82.770  96.823  1.00 14.71 ? 11   ASP K CA  1 
ATOM   11038 C  C   . ASP K  1 11  ? 15.866  81.498  97.016  1.00 15.23 ? 11   ASP K C   1 
ATOM   11039 O  O   . ASP K  1 11  ? 17.092  81.530  96.873  1.00 17.21 ? 11   ASP K O   1 
ATOM   11040 C  CB  . ASP K  1 11  ? 15.086  83.575  98.104  1.00 15.00 ? 11   ASP K CB  1 
ATOM   11041 C  CG  . ASP K  1 11  ? 14.985  85.052  97.844  1.00 17.87 ? 11   ASP K CG  1 
ATOM   11042 O  OD1 . ASP K  1 11  ? 15.046  85.451  96.655  1.00 20.26 ? 11   ASP K OD1 1 
ATOM   11043 O  OD2 . ASP K  1 11  ? 14.832  85.886  98.754  1.00 22.93 ? 11   ASP K OD2 1 
ATOM   11044 N  N   . GLY K  1 12  ? 15.215  80.397  97.366  1.00 14.50 ? 12   GLY K N   1 
ATOM   11045 C  CA  . GLY K  1 12  ? 15.898  79.123  97.615  1.00 14.13 ? 12   GLY K CA  1 
ATOM   11046 C  C   . GLY K  1 12  ? 15.543  78.038  96.620  1.00 13.66 ? 12   GLY K C   1 
ATOM   11047 O  O   . GLY K  1 12  ? 15.279  78.314  95.457  1.00 14.82 ? 12   GLY K O   1 
ATOM   11048 N  N   . PRO K  1 13  ? 15.557  76.784  97.062  1.00 12.54 ? 13   PRO K N   1 
ATOM   11049 C  CA  . PRO K  1 13  ? 15.321  75.645  96.170  1.00 11.73 ? 13   PRO K CA  1 
ATOM   11050 C  C   . PRO K  1 13  ? 13.849  75.322  95.948  1.00 10.79 ? 13   PRO K C   1 
ATOM   11051 O  O   . PRO K  1 13  ? 13.541  74.358  95.231  1.00 8.94  ? 13   PRO K O   1 
ATOM   11052 C  CB  . PRO K  1 13  ? 15.954  74.485  96.941  1.00 12.36 ? 13   PRO K CB  1 
ATOM   11053 C  CG  . PRO K  1 13  ? 15.723  74.867  98.394  1.00 12.40 ? 13   PRO K CG  1 
ATOM   11054 C  CD  . PRO K  1 13  ? 15.849  76.362  98.443  1.00 12.45 ? 13   PRO K CD  1 
ATOM   11055 N  N   . VAL K  1 14  ? 12.935  76.090  96.551  1.00 9.25  ? 14   VAL K N   1 
ATOM   11056 C  CA  . VAL K  1 14  ? 11.528  75.752  96.380  1.00 8.10  ? 14   VAL K CA  1 
ATOM   11057 C  C   . VAL K  1 14  ? 11.018  76.166  95.015  1.00 8.29  ? 14   VAL K C   1 
ATOM   11058 O  O   . VAL K  1 14  ? 11.190  77.311  94.585  1.00 7.29  ? 14   VAL K O   1 
ATOM   11059 C  CB  . VAL K  1 14  ? 10.643  76.363  97.520  1.00 8.47  ? 14   VAL K CB  1 
ATOM   11060 C  CG1 . VAL K  1 14  ? 9.150   76.056  97.282  1.00 7.43  ? 14   VAL K CG1 1 
ATOM   11061 C  CG2 . VAL K  1 14  ? 11.099  75.799  98.870  1.00 6.70  ? 14   VAL K CG2 1 
ATOM   11062 N  N   . GLN K  1 15  ? 10.356  75.256  94.327  1.00 8.01  ? 15   GLN K N   1 
ATOM   11063 C  CA  . GLN K  1 15  ? 9.797   75.598  93.031  1.00 9.07  ? 15   GLN K CA  1 
ATOM   11064 C  C   . GLN K  1 15  ? 8.688   74.631  92.707  1.00 8.91  ? 15   GLN K C   1 
ATOM   11065 O  O   . GLN K  1 15  ? 8.707   73.487  93.154  1.00 9.72  ? 15   GLN K O   1 
ATOM   11066 C  CB  . GLN K  1 15  ? 10.877  75.571  91.933  1.00 9.60  ? 15   GLN K CB  1 
ATOM   11067 C  CG  . GLN K  1 15  ? 11.508  74.215  91.678  1.00 13.31 ? 15   GLN K CG  1 
ATOM   11068 N  N   . GLY K  1 16  ? 7.706   75.079  91.940  1.00 7.44  ? 16   GLY K N   1 
ATOM   11069 C  CA  . GLY K  1 16  ? 6.605   74.210  91.624  1.00 7.50  ? 16   GLY K CA  1 
ATOM   11070 C  C   . GLY K  1 16  ? 5.677   74.813  90.596  1.00 6.49  ? 16   GLY K C   1 
ATOM   11071 O  O   . GLY K  1 16  ? 5.875   75.925  90.170  1.00 5.55  ? 16   GLY K O   1 
ATOM   11072 N  N   . ILE K  1 17  ? 4.680   74.037  90.200  1.00 6.54  ? 17   ILE K N   1 
ATOM   11073 C  CA  . ILE K  1 17  ? 3.657   74.488  89.270  1.00 6.67  ? 17   ILE K CA  1 
ATOM   11074 C  C   . ILE K  1 17  ? 2.335   74.071  89.869  1.00 6.39  ? 17   ILE K C   1 
ATOM   11075 O  O   . ILE K  1 17  ? 2.151   72.880  90.228  1.00 7.05  ? 17   ILE K O   1 
ATOM   11076 C  CB  . ILE K  1 17  ? 3.869   73.753  87.916  1.00 7.03  ? 17   ILE K CB  1 
ATOM   11077 C  CG1 . ILE K  1 17  ? 5.204   74.196  87.285  1.00 8.10  ? 17   ILE K CG1 1 
ATOM   11078 C  CG2 . ILE K  1 17  ? 2.712   74.006  86.982  1.00 8.43  ? 17   ILE K CG2 1 
ATOM   11079 C  CD1 . ILE K  1 17  ? 5.602   73.357  86.067  1.00 13.67 ? 17   ILE K CD1 1 
ATOM   11080 N  N   . ILE K  1 18  ? 1.409   75.015  89.963  1.00 5.00  ? 18   ILE K N   1 
ATOM   11081 C  CA  . ILE K  1 18  ? 0.083   74.736  90.504  1.00 5.29  ? 18   ILE K CA  1 
ATOM   11082 C  C   . ILE K  1 18  ? -0.958  75.097  89.471  1.00 6.16  ? 18   ILE K C   1 
ATOM   11083 O  O   . ILE K  1 18  ? -0.945  76.232  88.923  1.00 5.00  ? 18   ILE K O   1 
ATOM   11084 C  CB  . ILE K  1 18  ? -0.148  75.569  91.811  1.00 5.60  ? 18   ILE K CB  1 
ATOM   11085 C  CG1 . ILE K  1 18  ? 0.844   75.154  92.913  1.00 5.22  ? 18   ILE K CG1 1 
ATOM   11086 C  CG2 . ILE K  1 18  ? -1.620  75.465  92.314  1.00 6.17  ? 18   ILE K CG2 1 
ATOM   11087 C  CD1 . ILE K  1 18  ? 0.572   73.658  93.397  1.00 5.00  ? 18   ILE K CD1 1 
ATOM   11088 N  N   . ASN K  1 19  ? -1.911  74.174  89.297  1.00 5.30  ? 19   ASN K N   1 
ATOM   11089 C  CA  . ASN K  1 19  ? -2.991  74.328  88.357  1.00 6.10  ? 19   ASN K CA  1 
ATOM   11090 C  C   . ASN K  1 19  ? -4.274  74.684  89.090  1.00 6.04  ? 19   ASN K C   1 
ATOM   11091 O  O   . ASN K  1 19  ? -4.473  74.248  90.231  1.00 5.43  ? 19   ASN K O   1 
ATOM   11092 C  CB  . ASN K  1 19  ? -3.195  72.996  87.639  1.00 5.33  ? 19   ASN K CB  1 
ATOM   11093 C  CG  . ASN K  1 19  ? -1.915  72.478  87.025  1.00 9.50  ? 19   ASN K CG  1 
ATOM   11094 O  OD1 . ASN K  1 19  ? -1.311  71.495  87.514  1.00 13.05 ? 19   ASN K OD1 1 
ATOM   11095 N  ND2 . ASN K  1 19  ? -1.468  73.144  85.973  1.00 5.00  ? 19   ASN K ND2 1 
ATOM   11096 N  N   . PHE K  1 20  ? -5.131  75.482  88.446  1.00 5.57  ? 20   PHE K N   1 
ATOM   11097 C  CA  . PHE K  1 20  ? -6.455  75.750  88.969  1.00 5.65  ? 20   PHE K CA  1 
ATOM   11098 C  C   . PHE K  1 20  ? -7.503  75.429  87.881  1.00 5.74  ? 20   PHE K C   1 
ATOM   11099 O  O   . PHE K  1 20  ? -7.292  75.714  86.705  1.00 5.58  ? 20   PHE K O   1 
ATOM   11100 C  CB  . PHE K  1 20  ? -6.626  77.214  89.317  1.00 5.00  ? 20   PHE K CB  1 
ATOM   11101 C  CG  . PHE K  1 20  ? -5.597  77.751  90.288  1.00 5.21  ? 20   PHE K CG  1 
ATOM   11102 C  CD1 . PHE K  1 20  ? -4.334  78.063  89.854  1.00 5.00  ? 20   PHE K CD1 1 
ATOM   11103 C  CD2 . PHE K  1 20  ? -5.942  77.964  91.605  1.00 8.05  ? 20   PHE K CD2 1 
ATOM   11104 C  CE1 . PHE K  1 20  ? -3.381  78.604  90.743  1.00 8.42  ? 20   PHE K CE1 1 
ATOM   11105 C  CE2 . PHE K  1 20  ? -5.009  78.482  92.538  1.00 8.51  ? 20   PHE K CE2 1 
ATOM   11106 C  CZ  . PHE K  1 20  ? -3.743  78.819  92.095  1.00 6.55  ? 20   PHE K CZ  1 
ATOM   11107 N  N   . GLU K  1 21  ? -8.628  74.861  88.276  1.00 5.38  ? 21   GLU K N   1 
ATOM   11108 C  CA  . GLU K  1 21  ? -9.664  74.579  87.300  1.00 7.40  ? 21   GLU K CA  1 
ATOM   11109 C  C   . GLU K  1 21  ? -11.001 74.877  87.976  1.00 7.42  ? 21   GLU K C   1 
ATOM   11110 O  O   . GLU K  1 21  ? -11.237 74.508  89.137  1.00 8.16  ? 21   GLU K O   1 
ATOM   11111 C  CB  . GLU K  1 21  ? -9.557  73.131  86.811  1.00 6.76  ? 21   GLU K CB  1 
ATOM   11112 C  CG  . GLU K  1 21  ? -10.638 72.724  85.817  1.00 14.61 ? 21   GLU K CG  1 
ATOM   11113 C  CD  . GLU K  1 21  ? -10.393 71.331  85.234  1.00 21.03 ? 21   GLU K CD  1 
ATOM   11114 O  OE1 . GLU K  1 21  ? -10.701 70.327  85.920  1.00 24.59 ? 21   GLU K OE1 1 
ATOM   11115 O  OE2 . GLU K  1 21  ? -9.879  71.243  84.106  1.00 24.63 ? 21   GLU K OE2 1 
ATOM   11116 N  N   . GLN K  1 22  ? -11.871 75.607  87.287  1.00 7.99  ? 22   GLN K N   1 
ATOM   11117 C  CA  . GLN K  1 22  ? -13.192 75.879  87.844  1.00 8.65  ? 22   GLN K CA  1 
ATOM   11118 C  C   . GLN K  1 22  ? -14.215 75.609  86.753  1.00 10.95 ? 22   GLN K C   1 
ATOM   11119 O  O   . GLN K  1 22  ? -14.301 76.355  85.812  1.00 11.38 ? 22   GLN K O   1 
ATOM   11120 C  CB  . GLN K  1 22  ? -13.302 77.328  88.288  1.00 7.87  ? 22   GLN K CB  1 
ATOM   11121 C  CG  . GLN K  1 22  ? -14.598 77.688  89.014  1.00 5.97  ? 22   GLN K CG  1 
ATOM   11122 C  CD  . GLN K  1 22  ? -14.625 79.140  89.486  1.00 7.57  ? 22   GLN K CD  1 
ATOM   11123 O  OE1 . GLN K  1 22  ? -14.086 80.021  88.824  1.00 10.97 ? 22   GLN K OE1 1 
ATOM   11124 N  NE2 . GLN K  1 22  ? -15.285 79.390  90.595  1.00 7.43  ? 22   GLN K NE2 1 
ATOM   11125 N  N   . LYS K  1 23  ? -14.961 74.535  86.896  1.00 13.70 ? 23   LYS K N   1 
ATOM   11126 C  CA  . LYS K  1 23  ? -15.940 74.147  85.887  1.00 17.12 ? 23   LYS K CA  1 
ATOM   11127 C  C   . LYS K  1 23  ? -17.128 75.104  85.763  1.00 18.53 ? 23   LYS K C   1 
ATOM   11128 O  O   . LYS K  1 23  ? -17.604 75.387  84.658  1.00 19.78 ? 23   LYS K O   1 
ATOM   11129 C  CB  . LYS K  1 23  ? -16.459 72.755  86.206  1.00 17.63 ? 23   LYS K CB  1 
ATOM   11130 C  CG  . LYS K  1 23  ? -15.532 71.635  85.761  1.00 20.78 ? 23   LYS K CG  1 
ATOM   11131 C  CD  . LYS K  1 23  ? -15.902 70.332  86.444  1.00 27.05 ? 23   LYS K CD  1 
ATOM   11132 C  CE  . LYS K  1 23  ? -14.801 69.290  86.243  1.00 29.95 ? 23   LYS K CE  1 
ATOM   11133 N  NZ  . LYS K  1 23  ? -13.586 69.928  85.659  1.00 32.13 ? 23   LYS K NZ  1 
ATOM   11134 N  N   . GLU K  1 24  ? -17.618 75.585  86.896  1.00 19.80 ? 24   GLU K N   1 
ATOM   11135 C  CA  . GLU K  1 24  ? -18.787 76.447  86.909  1.00 21.69 ? 24   GLU K CA  1 
ATOM   11136 C  C   . GLU K  1 24  ? -18.419 77.765  87.522  1.00 21.62 ? 24   GLU K C   1 
ATOM   11137 O  O   . GLU K  1 24  ? -17.594 77.811  88.443  1.00 20.41 ? 24   GLU K O   1 
ATOM   11138 C  CB  . GLU K  1 24  ? -19.891 75.841  87.782  1.00 22.10 ? 24   GLU K CB  1 
ATOM   11139 C  CG  . GLU K  1 24  ? -21.004 75.125  87.035  1.00 27.43 ? 24   GLU K CG  1 
ATOM   11140 C  CD  . GLU K  1 24  ? -20.776 73.635  86.963  1.00 31.40 ? 24   GLU K CD  1 
ATOM   11141 O  OE1 . GLU K  1 24  ? -19.750 73.162  87.512  1.00 34.48 ? 24   GLU K OE1 1 
ATOM   11142 O  OE2 . GLU K  1 24  ? -21.619 72.942  86.361  1.00 33.75 ? 24   GLU K OE2 1 
ATOM   11143 N  N   . SER K  1 25  ? -19.045 78.833  87.037  1.00 21.29 ? 25   SER K N   1 
ATOM   11144 C  CA  . SER K  1 25  ? -18.826 80.134  87.634  1.00 22.10 ? 25   SER K CA  1 
ATOM   11145 C  C   . SER K  1 25  ? -19.235 80.036  89.097  1.00 21.76 ? 25   SER K C   1 
ATOM   11146 O  O   . SER K  1 25  ? -20.245 79.405  89.456  1.00 21.49 ? 25   SER K O   1 
ATOM   11147 C  CB  . SER K  1 25  ? -19.594 81.250  86.905  1.00 22.44 ? 25   SER K CB  1 
ATOM   11148 O  OG  . SER K  1 25  ? -20.703 81.684  87.678  1.00 25.89 ? 25   SER K OG  1 
ATOM   11149 N  N   . ASN K  1 26  ? -18.412 80.617  89.956  1.00 21.22 ? 26   ASN K N   1 
ATOM   11150 C  CA  . ASN K  1 26  ? -18.663 80.562  91.382  1.00 21.08 ? 26   ASN K CA  1 
ATOM   11151 C  C   . ASN K  1 26  ? -18.714 79.130  91.928  1.00 19.94 ? 26   ASN K C   1 
ATOM   11152 O  O   . ASN K  1 26  ? -19.065 78.966  93.074  1.00 20.06 ? 26   ASN K O   1 
ATOM   11153 C  CB  . ASN K  1 26  ? -19.971 81.285  91.741  1.00 22.37 ? 26   ASN K CB  1 
ATOM   11154 C  CG  . ASN K  1 26  ? -20.061 82.683  91.144  1.00 25.48 ? 26   ASN K CG  1 
ATOM   11155 O  OD1 . ASN K  1 26  ? -19.254 83.559  91.457  1.00 32.32 ? 26   ASN K OD1 1 
ATOM   11156 N  ND2 . ASN K  1 26  ? -21.060 82.903  90.283  1.00 31.15 ? 26   ASN K ND2 1 
ATOM   11157 N  N   . GLY K  1 27  ? -18.431 78.102  91.108  1.00 18.34 ? 27   GLY K N   1 
ATOM   11158 C  CA  . GLY K  1 27  ? -18.351 76.719  91.609  1.00 16.42 ? 27   GLY K CA  1 
ATOM   11159 C  C   . GLY K  1 27  ? -17.004 76.477  92.313  1.00 14.58 ? 27   GLY K C   1 
ATOM   11160 O  O   . GLY K  1 27  ? -16.186 77.390  92.376  1.00 14.14 ? 27   GLY K O   1 
ATOM   11161 N  N   . PRO K  1 28  ? -16.765 75.285  92.868  1.00 13.24 ? 28   PRO K N   1 
ATOM   11162 C  CA  . PRO K  1 28  ? -15.485 75.013  93.520  1.00 11.92 ? 28   PRO K CA  1 
ATOM   11163 C  C   . PRO K  1 28  ? -14.332 75.083  92.535  1.00 10.08 ? 28   PRO K C   1 
ATOM   11164 O  O   . PRO K  1 28  ? -14.475 74.824  91.321  1.00 9.16  ? 28   PRO K O   1 
ATOM   11165 C  CB  . PRO K  1 28  ? -15.624 73.561  94.028  1.00 11.81 ? 28   PRO K CB  1 
ATOM   11166 C  CG  . PRO K  1 28  ? -17.065 73.295  94.047  1.00 13.77 ? 28   PRO K CG  1 
ATOM   11167 C  CD  . PRO K  1 28  ? -17.684 74.136  92.964  1.00 13.90 ? 28   PRO K CD  1 
ATOM   11168 N  N   . VAL K  1 29  ? -13.183 75.450  93.076  1.00 7.55  ? 29   VAL K N   1 
ATOM   11169 C  CA  . VAL K  1 29  ? -11.979 75.521  92.301  1.00 6.82  ? 29   VAL K CA  1 
ATOM   11170 C  C   . VAL K  1 29  ? -11.085 74.393  92.781  1.00 7.23  ? 29   VAL K C   1 
ATOM   11171 O  O   . VAL K  1 29  ? -10.764 74.289  93.986  1.00 7.44  ? 29   VAL K O   1 
ATOM   11172 C  CB  . VAL K  1 29  ? -11.254 76.867  92.511  1.00 6.11  ? 29   VAL K CB  1 
ATOM   11173 C  CG1 . VAL K  1 29  ? -9.973  76.897  91.653  1.00 6.52  ? 29   VAL K CG1 1 
ATOM   11174 C  CG2 . VAL K  1 29  ? -12.195 78.061  92.173  1.00 8.11  ? 29   VAL K CG2 1 
ATOM   11175 N  N   . LYS K  1 30  ? -10.691 73.537  91.847  1.00 7.36  ? 30   LYS K N   1 
ATOM   11176 C  CA  . LYS K  1 30  ? -9.709  72.513  92.135  1.00 8.39  ? 30   LYS K CA  1 
ATOM   11177 C  C   . LYS K  1 30  ? -8.334  73.120  91.983  1.00 7.80  ? 30   LYS K C   1 
ATOM   11178 O  O   . LYS K  1 30  ? -8.074  73.806  91.005  1.00 6.44  ? 30   LYS K O   1 
ATOM   11179 C  CB  . LYS K  1 30  ? -9.843  71.353  91.160  1.00 9.75  ? 30   LYS K CB  1 
ATOM   11180 C  CG  . LYS K  1 30  ? -11.209 70.656  91.293  1.00 15.40 ? 30   LYS K CG  1 
ATOM   11181 C  CD  . LYS K  1 30  ? -11.324 69.360  90.486  1.00 22.77 ? 30   LYS K CD  1 
ATOM   11182 C  CE  . LYS K  1 30  ? -12.570 68.551  90.951  1.00 24.83 ? 30   LYS K CE  1 
ATOM   11183 N  NZ  . LYS K  1 30  ? -12.986 67.494  89.994  1.00 29.27 ? 30   LYS K NZ  1 
ATOM   11184 N  N   . VAL K  1 31  ? -7.445  72.810  92.920  1.00 6.51  ? 31   VAL K N   1 
ATOM   11185 C  CA  . VAL K  1 31  ? -6.079  73.318  92.884  1.00 6.85  ? 31   VAL K CA  1 
ATOM   11186 C  C   . VAL K  1 31  ? -5.107  72.199  93.128  1.00 6.87  ? 31   VAL K C   1 
ATOM   11187 O  O   . VAL K  1 31  ? -5.222  71.484  94.134  1.00 6.48  ? 31   VAL K O   1 
ATOM   11188 C  CB  . VAL K  1 31  ? -5.836  74.601  93.778  1.00 8.42  ? 31   VAL K CB  1 
ATOM   11189 C  CG1 . VAL K  1 31  ? -6.998  75.207  94.453  1.00 9.12  ? 31   VAL K CG1 1 
ATOM   11190 C  CG2 . VAL K  1 31  ? -4.441  74.929  94.229  1.00 5.03  ? 31   VAL K CG2 1 
ATOM   11191 N  N   . TRP K  1 32  ? -4.197  71.997  92.181  1.00 5.82  ? 32   TRP K N   1 
ATOM   11192 C  CA  . TRP K  1 32  ? -3.354  70.821  92.282  1.00 6.55  ? 32   TRP K CA  1 
ATOM   11193 C  C   . TRP K  1 32  ? -2.067  71.035  91.529  1.00 6.66  ? 32   TRP K C   1 
ATOM   11194 O  O   . TRP K  1 32  ? -2.013  71.823  90.598  1.00 6.94  ? 32   TRP K O   1 
ATOM   11195 C  CB  . TRP K  1 32  ? -4.066  69.564  91.726  1.00 7.40  ? 32   TRP K CB  1 
ATOM   11196 C  CG  . TRP K  1 32  ? -4.082  69.451  90.243  1.00 9.52  ? 32   TRP K CG  1 
ATOM   11197 C  CD1 . TRP K  1 32  ? -3.239  68.694  89.440  1.00 10.96 ? 32   TRP K CD1 1 
ATOM   11198 C  CD2 . TRP K  1 32  ? -4.955  70.133  89.363  1.00 10.57 ? 32   TRP K CD2 1 
ATOM   11199 N  NE1 . TRP K  1 32  ? -3.559  68.881  88.118  1.00 12.13 ? 32   TRP K NE1 1 
ATOM   11200 C  CE2 . TRP K  1 32  ? -4.607  69.763  88.045  1.00 11.67 ? 32   TRP K CE2 1 
ATOM   11201 C  CE3 . TRP K  1 32  ? -5.996  71.048  89.550  1.00 12.15 ? 32   TRP K CE3 1 
ATOM   11202 C  CZ2 . TRP K  1 32  ? -5.264  70.259  86.944  1.00 15.85 ? 32   TRP K CZ2 1 
ATOM   11203 C  CZ3 . TRP K  1 32  ? -6.639  71.544  88.452  1.00 13.08 ? 32   TRP K CZ3 1 
ATOM   11204 C  CH2 . TRP K  1 32  ? -6.272  71.160  87.165  1.00 16.32 ? 32   TRP K CH2 1 
ATOM   11205 N  N   . GLY K  1 33  ? -1.044  70.297  91.922  1.00 7.45  ? 33   GLY K N   1 
ATOM   11206 C  CA  . GLY K  1 33  ? 0.239   70.380  91.251  1.00 8.92  ? 33   GLY K CA  1 
ATOM   11207 C  C   . GLY K  1 33  ? 1.300   69.943  92.229  1.00 9.61  ? 33   GLY K C   1 
ATOM   11208 O  O   . GLY K  1 33  ? 1.008   69.582  93.359  1.00 12.18 ? 33   GLY K O   1 
ATOM   11209 N  N   . SER K  1 34  ? 2.544   70.037  91.832  1.00 9.25  ? 34   SER K N   1 
ATOM   11210 C  CA  . SER K  1 34  ? 3.593   69.580  92.686  1.00 10.35 ? 34   SER K CA  1 
ATOM   11211 C  C   . SER K  1 34  ? 4.547   70.724  93.011  1.00 10.44 ? 34   SER K C   1 
ATOM   11212 O  O   . SER K  1 34  ? 4.896   71.544  92.133  1.00 10.79 ? 34   SER K O   1 
ATOM   11213 C  CB  . SER K  1 34  ? 4.287   68.397  91.990  1.00 12.24 ? 34   SER K CB  1 
ATOM   11214 O  OG  . SER K  1 34  ? 5.665   68.296  92.286  1.00 15.30 ? 34   SER K OG  1 
ATOM   11215 N  N   . ILE K  1 35  ? 4.945   70.806  94.276  1.00 7.89  ? 35   ILE K N   1 
ATOM   11216 C  CA  . ILE K  1 35  ? 5.931   71.778  94.687  1.00 6.17  ? 35   ILE K CA  1 
ATOM   11217 C  C   . ILE K  1 35  ? 7.110   71.015  95.238  1.00 6.29  ? 35   ILE K C   1 
ATOM   11218 O  O   . ILE K  1 35  ? 6.914   70.173  96.100  1.00 7.70  ? 35   ILE K O   1 
ATOM   11219 C  CB  . ILE K  1 35  ? 5.381   72.680  95.802  1.00 6.68  ? 35   ILE K CB  1 
ATOM   11220 C  CG1 . ILE K  1 35  ? 4.115   73.379  95.332  1.00 6.87  ? 35   ILE K CG1 1 
ATOM   11221 C  CG2 . ILE K  1 35  ? 6.448   73.729  96.218  1.00 5.27  ? 35   ILE K CG2 1 
ATOM   11222 C  CD1 . ILE K  1 35  ? 3.376   74.144  96.433  1.00 8.22  ? 35   ILE K CD1 1 
ATOM   11223 N  N   . LYS K  1 36  ? 8.326   71.303  94.807  1.00 6.00  ? 36   LYS K N   1 
ATOM   11224 C  CA  . LYS K  1 36  ? 9.447   70.543  95.345  1.00 7.25  ? 36   LYS K CA  1 
ATOM   11225 C  C   . LYS K  1 36  ? 10.451  71.417  96.100  1.00 7.13  ? 36   LYS K C   1 
ATOM   11226 O  O   . LYS K  1 36  ? 10.344  72.643  96.088  1.00 7.11  ? 36   LYS K O   1 
ATOM   11227 C  CB  . LYS K  1 36  ? 10.118  69.725  94.234  1.00 8.31  ? 36   LYS K CB  1 
ATOM   11228 C  CG  . LYS K  1 36  ? 10.884  70.542  93.253  1.00 13.13 ? 36   LYS K CG  1 
ATOM   11229 C  CD  . LYS K  1 36  ? 11.379  69.682  92.086  1.00 21.13 ? 36   LYS K CD  1 
ATOM   11230 C  CE  . LYS K  1 36  ? 12.182  70.581  91.117  1.00 23.89 ? 36   LYS K CE  1 
ATOM   11231 N  NZ  . LYS K  1 36  ? 12.541  69.848  89.853  1.00 24.89 ? 36   LYS K NZ  1 
ATOM   11232 N  N   . GLY K  1 37  ? 11.404  70.779  96.792  1.00 5.81  ? 37   GLY K N   1 
ATOM   11233 C  CA  . GLY K  1 37  ? 12.413  71.520  97.527  1.00 6.11  ? 37   GLY K CA  1 
ATOM   11234 C  C   . GLY K  1 37  ? 12.027  72.002  98.919  1.00 5.24  ? 37   GLY K C   1 
ATOM   11235 O  O   . GLY K  1 37  ? 12.782  72.757  99.551  1.00 5.68  ? 37   GLY K O   1 
ATOM   11236 N  N   . LEU K  1 38  ? 10.866  71.544  99.419  1.00 5.78  ? 38   LEU K N   1 
ATOM   11237 C  CA  . LEU K  1 38  ? 10.357  71.953  100.744 1.00 5.27  ? 38   LEU K CA  1 
ATOM   11238 C  C   . LEU K  1 38  ? 10.896  71.033  101.834 1.00 6.20  ? 38   LEU K C   1 
ATOM   11239 O  O   . LEU K  1 38  ? 11.292  69.896  101.544 1.00 5.72  ? 38   LEU K O   1 
ATOM   11240 C  CB  . LEU K  1 38  ? 8.822   71.787  100.749 1.00 5.66  ? 38   LEU K CB  1 
ATOM   11241 C  CG  . LEU K  1 38  ? 8.026   72.729  99.844  1.00 5.59  ? 38   LEU K CG  1 
ATOM   11242 C  CD1 . LEU K  1 38  ? 6.547   72.287  99.673  1.00 7.18  ? 38   LEU K CD1 1 
ATOM   11243 C  CD2 . LEU K  1 38  ? 8.038   74.115  100.456 1.00 5.81  ? 38   LEU K CD2 1 
ATOM   11244 N  N   . THR K  1 39  ? 10.925  71.512  103.079 1.00 6.17  ? 39   THR K N   1 
ATOM   11245 C  CA  . THR K  1 39  ? 11.177  70.640  104.227 1.00 6.79  ? 39   THR K CA  1 
ATOM   11246 C  C   . THR K  1 39  ? 9.943   69.772  104.441 1.00 7.04  ? 39   THR K C   1 
ATOM   11247 O  O   . THR K  1 39  ? 8.806   70.197  104.162 1.00 6.43  ? 39   THR K O   1 
ATOM   11248 C  CB  . THR K  1 39  ? 11.377  71.431  105.526 1.00 7.68  ? 39   THR K CB  1 
ATOM   11249 O  OG1 . THR K  1 39  ? 10.294  72.376  105.687 1.00 5.20  ? 39   THR K OG1 1 
ATOM   11250 C  CG2 . THR K  1 39  ? 12.664  72.216  105.486 1.00 7.58  ? 39   THR K CG2 1 
ATOM   11251 N  N   . GLU K  1 40  ? 10.150  68.556  104.940 1.00 5.00  ? 40   GLU K N   1 
ATOM   11252 C  CA  . GLU K  1 40  ? 9.025   67.671  105.207 1.00 6.94  ? 40   GLU K CA  1 
ATOM   11253 C  C   . GLU K  1 40  ? 8.066   68.326  106.208 1.00 6.13  ? 40   GLU K C   1 
ATOM   11254 O  O   . GLU K  1 40  ? 8.516   68.978  107.141 1.00 6.05  ? 40   GLU K O   1 
ATOM   11255 C  CB  . GLU K  1 40  ? 9.551   66.335  105.786 1.00 6.66  ? 40   GLU K CB  1 
ATOM   11256 C  CG  . GLU K  1 40  ? 8.476   65.365  106.189 1.00 7.84  ? 40   GLU K CG  1 
ATOM   11257 C  CD  . GLU K  1 40  ? 9.068   64.014  106.608 1.00 13.30 ? 40   GLU K CD  1 
ATOM   11258 O  OE1 . GLU K  1 40  ? 10.315  63.903  106.699 1.00 14.97 ? 40   GLU K OE1 1 
ATOM   11259 O  OE2 . GLU K  1 40  ? 8.282   63.076  106.825 1.00 13.87 ? 40   GLU K OE2 1 
ATOM   11260 N  N   . GLY K  1 41  ? 6.760   68.191  105.980 1.00 5.65  ? 41   GLY K N   1 
ATOM   11261 C  CA  . GLY K  1 41  ? 5.770   68.682  106.907 1.00 6.22  ? 41   GLY K CA  1 
ATOM   11262 C  C   . GLY K  1 41  ? 4.894   69.797  106.344 1.00 6.65  ? 41   GLY K C   1 
ATOM   11263 O  O   . GLY K  1 41  ? 4.828   69.995  105.138 1.00 6.48  ? 41   GLY K O   1 
ATOM   11264 N  N   . LEU K  1 42  ? 4.245   70.536  107.240 1.00 6.90  ? 42   LEU K N   1 
ATOM   11265 C  CA  . LEU K  1 42  ? 3.264   71.553  106.800 1.00 7.87  ? 42   LEU K CA  1 
ATOM   11266 C  C   . LEU K  1 42  ? 3.849   72.879  106.364 1.00 7.47  ? 42   LEU K C   1 
ATOM   11267 O  O   . LEU K  1 42  ? 4.759   73.408  106.999 1.00 6.17  ? 42   LEU K O   1 
ATOM   11268 C  CB  . LEU K  1 42  ? 2.308   71.854  107.954 1.00 9.40  ? 42   LEU K CB  1 
ATOM   11269 C  CG  . LEU K  1 42  ? 1.459   70.695  108.442 1.00 12.23 ? 42   LEU K CG  1 
ATOM   11270 C  CD1 . LEU K  1 42  ? 0.875   71.058  109.816 1.00 14.39 ? 42   LEU K CD1 1 
ATOM   11271 C  CD2 . LEU K  1 42  ? 0.365   70.371  107.468 1.00 14.01 ? 42   LEU K CD2 1 
ATOM   11272 N  N   . HIS K  1 43  ? 3.249   73.466  105.322 1.00 5.10  ? 43   HIS K N   1 
ATOM   11273 C  CA  . HIS K  1 43  ? 3.641   74.771  104.836 1.00 5.00  ? 43   HIS K CA  1 
ATOM   11274 C  C   . HIS K  1 43  ? 2.409   75.606  104.480 1.00 5.00  ? 43   HIS K C   1 
ATOM   11275 O  O   . HIS K  1 43  ? 1.550   75.158  103.710 1.00 5.00  ? 43   HIS K O   1 
ATOM   11276 C  CB  . HIS K  1 43  ? 4.476   74.565  103.568 1.00 5.00  ? 43   HIS K CB  1 
ATOM   11277 C  CG  . HIS K  1 43  ? 5.815   73.960  103.845 1.00 6.61  ? 43   HIS K CG  1 
ATOM   11278 N  ND1 . HIS K  1 43  ? 6.903   74.711  104.236 1.00 5.19  ? 43   HIS K ND1 1 
ATOM   11279 C  CD2 . HIS K  1 43  ? 6.227   72.667  103.843 1.00 6.93  ? 43   HIS K CD2 1 
ATOM   11280 C  CE1 . HIS K  1 43  ? 7.941   73.909  104.436 1.00 5.22  ? 43   HIS K CE1 1 
ATOM   11281 N  NE2 . HIS K  1 43  ? 7.554   72.660  104.225 1.00 6.26  ? 43   HIS K NE2 1 
ATOM   11282 N  N   . GLY K  1 44  ? 2.347   76.831  104.994 1.00 5.00  ? 44   GLY K N   1 
ATOM   11283 C  CA  . GLY K  1 44  ? 1.230   77.702  104.667 1.00 5.00  ? 44   GLY K CA  1 
ATOM   11284 C  C   . GLY K  1 44  ? 1.149   77.946  103.145 1.00 5.00  ? 44   GLY K C   1 
ATOM   11285 O  O   . GLY K  1 44  ? 2.175   78.005  102.445 1.00 5.00  ? 44   GLY K O   1 
ATOM   11286 N  N   . PHE K  1 45  ? -0.071  78.134  102.653 1.00 5.00  ? 45   PHE K N   1 
ATOM   11287 C  CA  . PHE K  1 45  ? -0.296  78.187  101.207 1.00 5.00  ? 45   PHE K CA  1 
ATOM   11288 C  C   . PHE K  1 45  ? -1.455  79.158  101.003 1.00 5.00  ? 45   PHE K C   1 
ATOM   11289 O  O   . PHE K  1 45  ? -2.600  78.884  101.399 1.00 5.00  ? 45   PHE K O   1 
ATOM   11290 C  CB  . PHE K  1 45  ? -0.660  76.755  100.796 1.00 5.17  ? 45   PHE K CB  1 
ATOM   11291 C  CG  . PHE K  1 45  ? -0.832  76.527  99.310  1.00 5.00  ? 45   PHE K CG  1 
ATOM   11292 C  CD1 . PHE K  1 45  ? 0.289   76.540  98.467  1.00 6.76  ? 45   PHE K CD1 1 
ATOM   11293 C  CD2 . PHE K  1 45  ? -2.072  76.187  98.795  1.00 5.13  ? 45   PHE K CD2 1 
ATOM   11294 C  CE1 . PHE K  1 45  ? 0.172   76.244  97.132  1.00 7.30  ? 45   PHE K CE1 1 
ATOM   11295 C  CE2 . PHE K  1 45  ? -2.224  75.891  97.428  1.00 5.00  ? 45   PHE K CE2 1 
ATOM   11296 C  CZ  . PHE K  1 45  ? -1.088  75.925  96.602  1.00 5.00  ? 45   PHE K CZ  1 
ATOM   11297 N  N   . HIS K  1 46  ? -1.163  80.329  100.427 1.00 5.00  ? 46   HIS K N   1 
ATOM   11298 C  CA  . HIS K  1 46  ? -2.180  81.379  100.412 1.00 5.00  ? 46   HIS K CA  1 
ATOM   11299 C  C   . HIS K  1 46  ? -2.174  82.135  99.098  1.00 5.00  ? 46   HIS K C   1 
ATOM   11300 O  O   . HIS K  1 46  ? -1.138  82.199  98.423  1.00 5.00  ? 46   HIS K O   1 
ATOM   11301 C  CB  . HIS K  1 46  ? -1.843  82.466  101.467 1.00 5.00  ? 46   HIS K CB  1 
ATOM   11302 C  CG  . HIS K  1 46  ? -1.564  81.906  102.833 1.00 5.00  ? 46   HIS K CG  1 
ATOM   11303 N  ND1 . HIS K  1 46  ? -0.435  82.207  103.537 1.00 5.00  ? 46   HIS K ND1 1 
ATOM   11304 C  CD2 . HIS K  1 46  ? -2.240  80.999  103.585 1.00 5.29  ? 46   HIS K CD2 1 
ATOM   11305 C  CE1 . HIS K  1 46  ? -0.440  81.578  104.695 1.00 7.78  ? 46   HIS K CE1 1 
ATOM   11306 N  NE2 . HIS K  1 46  ? -1.514  80.812  104.737 1.00 5.00  ? 46   HIS K NE2 1 
ATOM   11307 N  N   . VAL K  1 47  ? -3.297  82.756  98.825  1.00 5.00  ? 47   VAL K N   1 
ATOM   11308 C  CA  . VAL K  1 47  ? -3.351  83.716  97.728  1.00 5.00  ? 47   VAL K CA  1 
ATOM   11309 C  C   . VAL K  1 47  ? -3.181  85.096  98.378  1.00 5.00  ? 47   VAL K C   1 
ATOM   11310 O  O   . VAL K  1 47  ? -4.000  85.522  99.209  1.00 5.00  ? 47   VAL K O   1 
ATOM   11311 C  CB  . VAL K  1 47  ? -4.663  83.703  96.959  1.00 5.00  ? 47   VAL K CB  1 
ATOM   11312 C  CG1 . VAL K  1 47  ? -4.627  84.788  95.796  1.00 5.26  ? 47   VAL K CG1 1 
ATOM   11313 C  CG2 . VAL K  1 47  ? -4.896  82.313  96.355  1.00 5.00  ? 47   VAL K CG2 1 
ATOM   11314 N  N   . HIS K  1 48  ? -2.120  85.782  97.961  1.00 5.00  ? 48   HIS K N   1 
ATOM   11315 C  CA  . HIS K  1 48  ? -1.835  87.129  98.448  1.00 5.00  ? 48   HIS K CA  1 
ATOM   11316 C  C   . HIS K  1 48  ? -2.421  88.135  97.467  1.00 5.00  ? 48   HIS K C   1 
ATOM   11317 O  O   . HIS K  1 48  ? -2.705  87.792  96.330  1.00 5.00  ? 48   HIS K O   1 
ATOM   11318 C  CB  . HIS K  1 48  ? -0.316  87.331  98.620  1.00 5.00  ? 48   HIS K CB  1 
ATOM   11319 C  CG  . HIS K  1 48  ? 0.197   86.649  99.851  1.00 5.00  ? 48   HIS K CG  1 
ATOM   11320 N  ND1 . HIS K  1 48  ? 0.826   87.321  100.883 1.00 5.00  ? 48   HIS K ND1 1 
ATOM   11321 C  CD2 . HIS K  1 48  ? 0.155   85.339  100.216 1.00 5.17  ? 48   HIS K CD2 1 
ATOM   11322 C  CE1 . HIS K  1 48  ? 1.146   86.445  101.837 1.00 5.00  ? 48   HIS K CE1 1 
ATOM   11323 N  NE2 . HIS K  1 48  ? 0.747   85.253  101.451 1.00 5.00  ? 48   HIS K NE2 1 
ATOM   11324 N  N   . GLU K  1 49  ? -2.524  89.369  97.903  1.00 5.00  ? 49   GLU K N   1 
ATOM   11325 C  CA  . GLU K  1 49  ? -3.418  90.262  97.197  1.00 5.00  ? 49   GLU K CA  1 
ATOM   11326 C  C   . GLU K  1 49  ? -2.921  90.752  95.857  1.00 5.00  ? 49   GLU K C   1 
ATOM   11327 O  O   . GLU K  1 49  ? -3.734  90.907  94.926  1.00 5.00  ? 49   GLU K O   1 
ATOM   11328 C  CB  . GLU K  1 49  ? -3.692  91.472  98.084  1.00 5.00  ? 49   GLU K CB  1 
ATOM   11329 C  CG  . GLU K  1 49  ? -4.727  92.444  97.498  1.00 7.78  ? 49   GLU K CG  1 
ATOM   11330 C  CD  . GLU K  1 49  ? -5.069  93.581  98.457  1.00 9.16  ? 49   GLU K CD  1 
ATOM   11331 O  OE1 . GLU K  1 49  ? -4.521  93.632  99.578  1.00 8.37  ? 49   GLU K OE1 1 
ATOM   11332 O  OE2 . GLU K  1 49  ? -5.817  94.481  98.036  1.00 9.63  ? 49   GLU K OE2 1 
ATOM   11333 N  N   . PHE K  1 50  ? -1.624  91.049  95.774  1.00 5.00  ? 50   PHE K N   1 
ATOM   11334 C  CA  . PHE K  1 50  ? -1.089  91.693  94.551  1.00 5.00  ? 50   PHE K CA  1 
ATOM   11335 C  C   . PHE K  1 50  ? -0.232  90.780  93.724  1.00 5.00  ? 50   PHE K C   1 
ATOM   11336 O  O   . PHE K  1 50  ? 0.539   90.045  94.317  1.00 5.00  ? 50   PHE K O   1 
ATOM   11337 C  CB  . PHE K  1 50  ? -0.245  92.931  94.940  1.00 5.00  ? 50   PHE K CB  1 
ATOM   11338 C  CG  . PHE K  1 50  ? -0.999  93.859  95.848  1.00 5.00  ? 50   PHE K CG  1 
ATOM   11339 C  CD1 . PHE K  1 50  ? -2.189  94.420  95.412  1.00 7.58  ? 50   PHE K CD1 1 
ATOM   11340 C  CD2 . PHE K  1 50  ? -0.568  94.077  97.145  1.00 6.82  ? 50   PHE K CD2 1 
ATOM   11341 C  CE1 . PHE K  1 50  ? -2.962  95.234  96.256  1.00 10.60 ? 50   PHE K CE1 1 
ATOM   11342 C  CE2 . PHE K  1 50  ? -1.321  94.909  97.996  1.00 8.39  ? 50   PHE K CE2 1 
ATOM   11343 C  CZ  . PHE K  1 50  ? -2.518  95.453  97.540  1.00 7.27  ? 50   PHE K CZ  1 
ATOM   11344 N  N   . GLY K  1 51  ? -0.414  90.818  92.392  1.00 5.00  ? 51   GLY K N   1 
ATOM   11345 C  CA  . GLY K  1 51  ? 0.408   90.030  91.460  1.00 5.13  ? 51   GLY K CA  1 
ATOM   11346 C  C   . GLY K  1 51  ? 1.651   90.868  91.153  1.00 5.00  ? 51   GLY K C   1 
ATOM   11347 O  O   . GLY K  1 51  ? 1.966   91.122  89.994  1.00 5.96  ? 51   GLY K O   1 
ATOM   11348 N  N   . ASP K  1 52  ? 2.319   91.354  92.204  1.00 5.59  ? 52   ASP K N   1 
ATOM   11349 C  CA  . ASP K  1 52  ? 3.466   92.244  92.043  1.00 5.00  ? 52   ASP K CA  1 
ATOM   11350 C  C   . ASP K  1 52  ? 4.730   91.544  92.554  1.00 5.83  ? 52   ASP K C   1 
ATOM   11351 O  O   . ASP K  1 52  ? 4.835   91.310  93.770  1.00 6.16  ? 52   ASP K O   1 
ATOM   11352 C  CB  . ASP K  1 52  ? 3.177   93.508  92.875  1.00 5.00  ? 52   ASP K CB  1 
ATOM   11353 C  CG  . ASP K  1 52  ? 4.273   94.562  92.746  1.00 8.60  ? 52   ASP K CG  1 
ATOM   11354 O  OD1 . ASP K  1 52  ? 5.440   94.180  92.524  1.00 6.53  ? 52   ASP K OD1 1 
ATOM   11355 O  OD2 . ASP K  1 52  ? 4.043   95.786  92.869  1.00 11.39 ? 52   ASP K OD2 1 
ATOM   11356 N  N   . ASN K  1 53  ? 5.650   91.193  91.641  1.00 5.77  ? 53   ASN K N   1 
ATOM   11357 C  CA  . ASN K  1 53  ? 6.857   90.471  92.003  1.00 7.77  ? 53   ASN K CA  1 
ATOM   11358 C  C   . ASN K  1 53  ? 8.053   91.401  91.900  1.00 6.66  ? 53   ASN K C   1 
ATOM   11359 O  O   . ASN K  1 53  ? 9.175   90.913  91.789  1.00 7.99  ? 53   ASN K O   1 
ATOM   11360 C  CB  . ASN K  1 53  ? 7.064   89.252  91.040  1.00 9.58  ? 53   ASN K CB  1 
ATOM   11361 C  CG  . ASN K  1 53  ? 8.056   88.199  91.597  1.00 14.54 ? 53   ASN K CG  1 
ATOM   11362 O  OD1 . ASN K  1 53  ? 8.994   87.764  90.891  1.00 21.85 ? 53   ASN K OD1 1 
ATOM   11363 N  ND2 . ASN K  1 53  ? 7.822   87.748  92.821  1.00 15.92 ? 53   ASN K ND2 1 
ATOM   11364 N  N   . THR K  1 54  ? 7.839   92.717  91.865  1.00 6.20  ? 54   THR K N   1 
ATOM   11365 C  CA  . THR K  1 54  ? 8.974   93.627  91.735  1.00 6.80  ? 54   THR K CA  1 
ATOM   11366 C  C   . THR K  1 54  ? 10.000  93.513  92.856  1.00 8.13  ? 54   THR K C   1 
ATOM   11367 O  O   . THR K  1 54  ? 11.169  93.840  92.652  1.00 9.24  ? 54   THR K O   1 
ATOM   11368 C  CB  . THR K  1 54  ? 8.576   95.085  91.628  1.00 7.27  ? 54   THR K CB  1 
ATOM   11369 O  OG1 . THR K  1 54  ? 7.808   95.460  92.770  1.00 6.08  ? 54   THR K OG1 1 
ATOM   11370 C  CG2 . THR K  1 54  ? 7.650   95.297  90.437  1.00 8.38  ? 54   THR K CG2 1 
ATOM   11371 N  N   . ALA K  1 55  ? 9.571   93.135  94.032  1.00 6.38  ? 55   ALA K N   1 
ATOM   11372 C  CA  . ALA K  1 55  ? 10.534  92.835  95.107  1.00 8.72  ? 55   ALA K CA  1 
ATOM   11373 C  C   . ALA K  1 55  ? 10.412  91.391  95.546  1.00 9.57  ? 55   ALA K C   1 
ATOM   11374 O  O   . ALA K  1 55  ? 10.285  91.111  96.746  1.00 12.62 ? 55   ALA K O   1 
ATOM   11375 C  CB  . ALA K  1 55  ? 10.324  93.793  96.307  1.00 9.43  ? 55   ALA K CB  1 
ATOM   11376 N  N   . GLY K  1 56  ? 10.416  90.464  94.595  1.00 8.84  ? 56   GLY K N   1 
ATOM   11377 C  CA  . GLY K  1 56  ? 10.214  89.061  94.943  1.00 8.44  ? 56   GLY K CA  1 
ATOM   11378 C  C   . GLY K  1 56  ? 8.865   88.879  95.635  1.00 8.87  ? 56   GLY K C   1 
ATOM   11379 O  O   . GLY K  1 56  ? 7.908   89.631  95.364  1.00 10.29 ? 56   GLY K O   1 
ATOM   11380 N  N   . CYS K  1 57  ? 8.769   87.932  96.560  1.00 7.31  ? 57   CYS K N   1 
ATOM   11381 C  CA  . CYS K  1 57  ? 7.473   87.625  97.132  1.00 7.06  ? 57   CYS K CA  1 
ATOM   11382 C  C   . CYS K  1 57  ? 6.934   88.707  98.085  1.00 6.78  ? 57   CYS K C   1 
ATOM   11383 O  O   . CYS K  1 57  ? 5.736   88.737  98.374  1.00 5.24  ? 57   CYS K O   1 
ATOM   11384 C  CB  . CYS K  1 57  ? 7.542   86.270  97.849  1.00 8.07  ? 57   CYS K CB  1 
ATOM   11385 S  SG  . CYS K  1 57  ? 7.970   84.960  96.647  1.00 12.97 ? 57   CYS K SG  1 
ATOM   11386 N  N   . THR K  1 58  ? 7.828   89.564  98.574  1.00 5.00  ? 58   THR K N   1 
ATOM   11387 C  CA  . THR K  1 58  ? 7.436   90.616  99.525  1.00 5.54  ? 58   THR K CA  1 
ATOM   11388 C  C   . THR K  1 58  ? 6.399   91.594  98.960  1.00 5.83  ? 58   THR K C   1 
ATOM   11389 O  O   . THR K  1 58  ? 5.473   92.046  99.669  1.00 5.00  ? 58   THR K O   1 
ATOM   11390 C  CB  . THR K  1 58  ? 8.676   91.384  99.880  1.00 5.92  ? 58   THR K CB  1 
ATOM   11391 O  OG1 . THR K  1 58  ? 9.577   90.456  100.500 1.00 8.42  ? 58   THR K OG1 1 
ATOM   11392 C  CG2 . THR K  1 58  ? 8.335   92.459  101.005 1.00 9.26  ? 58   THR K CG2 1 
ATOM   11393 N  N   . SER K  1 59  ? 6.553   91.926  97.689  1.00 5.00  ? 59   SER K N   1 
ATOM   11394 C  CA  . SER K  1 59  ? 5.642   92.910  97.111  1.00 5.00  ? 59   SER K CA  1 
ATOM   11395 C  C   . SER K  1 59  ? 4.248   92.344  96.787  1.00 5.00  ? 59   SER K C   1 
ATOM   11396 O  O   . SER K  1 59  ? 3.392   93.085  96.336  1.00 5.00  ? 59   SER K O   1 
ATOM   11397 C  CB  . SER K  1 59  ? 6.298   93.579  95.867  1.00 5.50  ? 59   SER K CB  1 
ATOM   11398 O  OG  . SER K  1 59  ? 6.929   92.614  95.094  1.00 7.78  ? 59   SER K OG  1 
ATOM   11399 N  N   . ALA K  1 60  ? 4.019   91.067  97.065  1.00 5.00  ? 60   ALA K N   1 
ATOM   11400 C  CA  . ALA K  1 60  ? 2.684   90.500  96.837  1.00 5.11  ? 60   ALA K CA  1 
ATOM   11401 C  C   . ALA K  1 60  ? 1.683   90.995  97.911  1.00 5.00  ? 60   ALA K C   1 
ATOM   11402 O  O   . ALA K  1 60  ? 0.471   90.768  97.795  1.00 6.02  ? 60   ALA K O   1 
ATOM   11403 C  CB  . ALA K  1 60  ? 2.736   88.961  96.837  1.00 5.42  ? 60   ALA K CB  1 
ATOM   11404 N  N   . GLY K  1 61  ? 2.205   91.638  98.954  1.00 5.00  ? 61   GLY K N   1 
ATOM   11405 C  CA  . GLY K  1 61  ? 1.348   92.222  99.957  1.00 5.00  ? 61   GLY K CA  1 
ATOM   11406 C  C   . GLY K  1 61  ? 0.725   91.151  100.852 1.00 5.00  ? 61   GLY K C   1 
ATOM   11407 O  O   . GLY K  1 61  ? 1.193   90.039  100.909 1.00 5.00  ? 61   GLY K O   1 
ATOM   11408 N  N   . PRO K  1 62  ? -0.354  91.490  101.539 1.00 5.00  ? 62   PRO K N   1 
ATOM   11409 C  CA  . PRO K  1 62  ? -0.912  90.586  102.544 1.00 5.23  ? 62   PRO K CA  1 
ATOM   11410 C  C   . PRO K  1 62  ? -1.898  89.591  101.887 1.00 5.29  ? 62   PRO K C   1 
ATOM   11411 O  O   . PRO K  1 62  ? -2.054  89.577  100.662 1.00 5.00  ? 62   PRO K O   1 
ATOM   11412 C  CB  . PRO K  1 62  ? -1.655  91.547  103.463 1.00 5.10  ? 62   PRO K CB  1 
ATOM   11413 C  CG  . PRO K  1 62  ? -2.254  92.552  102.518 1.00 7.09  ? 62   PRO K CG  1 
ATOM   11414 C  CD  . PRO K  1 62  ? -1.124  92.755  101.416 1.00 6.01  ? 62   PRO K CD  1 
ATOM   11415 N  N   . HIS K  1 63  ? -2.585  88.794  102.693 1.00 5.00  ? 63   HIS K N   1 
ATOM   11416 C  CA  . HIS K  1 63  ? -3.550  87.867  102.128 1.00 5.00  ? 63   HIS K CA  1 
ATOM   11417 C  C   . HIS K  1 63  ? -4.710  88.568  101.405 1.00 5.00  ? 63   HIS K C   1 
ATOM   11418 O  O   . HIS K  1 63  ? -5.182  89.625  101.852 1.00 5.16  ? 63   HIS K O   1 
ATOM   11419 C  CB  . HIS K  1 63  ? -4.083  86.936  103.231 1.00 5.00  ? 63   HIS K CB  1 
ATOM   11420 C  CG  . HIS K  1 63  ? -3.021  86.060  103.812 1.00 6.05  ? 63   HIS K CG  1 
ATOM   11421 N  ND1 . HIS K  1 63  ? -3.243  85.242  104.894 1.00 5.00  ? 63   HIS K ND1 1 
ATOM   11422 C  CD2 . HIS K  1 63  ? -1.724  85.871  103.440 1.00 8.22  ? 63   HIS K CD2 1 
ATOM   11423 C  CE1 . HIS K  1 63  ? -2.119  84.599  105.184 1.00 6.91  ? 63   HIS K CE1 1 
ATOM   11424 N  NE2 . HIS K  1 63  ? -1.188  84.950  104.308 1.00 11.22 ? 63   HIS K NE2 1 
ATOM   11425 N  N   . PHE K  1 64  ? -5.145  87.979  100.294 1.00 5.00  ? 64   PHE K N   1 
ATOM   11426 C  CA  . PHE K  1 64  ? -6.284  88.505  99.525  1.00 5.00  ? 64   PHE K CA  1 
ATOM   11427 C  C   . PHE K  1 64  ? -7.512  88.434  100.464 1.00 5.17  ? 64   PHE K C   1 
ATOM   11428 O  O   . PHE K  1 64  ? -7.872  87.352  100.925 1.00 5.00  ? 64   PHE K O   1 
ATOM   11429 C  CB  . PHE K  1 64  ? -6.478  87.654  98.266  1.00 5.00  ? 64   PHE K CB  1 
ATOM   11430 C  CG  . PHE K  1 64  ? -7.660  88.096  97.376  1.00 5.00  ? 64   PHE K CG  1 
ATOM   11431 C  CD1 . PHE K  1 64  ? -7.962  89.434  97.220  1.00 5.00  ? 64   PHE K CD1 1 
ATOM   11432 C  CD2 . PHE K  1 64  ? -8.470  87.142  96.776  1.00 5.00  ? 64   PHE K CD2 1 
ATOM   11433 C  CE1 . PHE K  1 64  ? -9.020  89.851  96.416  1.00 6.44  ? 64   PHE K CE1 1 
ATOM   11434 C  CE2 . PHE K  1 64  ? -9.559  87.512  95.990  1.00 7.85  ? 64   PHE K CE2 1 
ATOM   11435 C  CZ  . PHE K  1 64  ? -9.829  88.899  95.781  1.00 6.02  ? 64   PHE K CZ  1 
ATOM   11436 N  N   . ASN K  1 65  ? -8.134  89.591  100.725 1.00 5.00  ? 65   ASN K N   1 
ATOM   11437 C  CA  . ASN K  1 65  ? -9.135  89.669  101.792 1.00 5.77  ? 65   ASN K CA  1 
ATOM   11438 C  C   . ASN K  1 65  ? -10.223 90.725  101.480 1.00 6.39  ? 65   ASN K C   1 
ATOM   11439 O  O   . ASN K  1 65  ? -10.354 91.727  102.189 1.00 7.52  ? 65   ASN K O   1 
ATOM   11440 C  CB  . ASN K  1 65  ? -8.357  89.990  103.091 1.00 5.05  ? 65   ASN K CB  1 
ATOM   11441 C  CG  . ASN K  1 65  ? -9.237  90.049  104.313 1.00 8.23  ? 65   ASN K CG  1 
ATOM   11442 O  OD1 . ASN K  1 65  ? -10.299 89.405  104.372 1.00 6.81  ? 65   ASN K OD1 1 
ATOM   11443 N  ND2 . ASN K  1 65  ? -8.815  90.851  105.289 1.00 6.98  ? 65   ASN K ND2 1 
ATOM   11444 N  N   . PRO K  1 66  ? -10.986 90.502  100.411 1.00 6.48  ? 66   PRO K N   1 
ATOM   11445 C  CA  . PRO K  1 66  ? -11.962 91.495  99.955  1.00 7.76  ? 66   PRO K CA  1 
ATOM   11446 C  C   . PRO K  1 66  ? -13.110 91.582  100.936 1.00 8.60  ? 66   PRO K C   1 
ATOM   11447 O  O   . PRO K  1 66  ? -13.819 92.581  100.870 1.00 8.56  ? 66   PRO K O   1 
ATOM   11448 C  CB  . PRO K  1 66  ? -12.505 90.924  98.642  1.00 7.51  ? 66   PRO K CB  1 
ATOM   11449 C  CG  . PRO K  1 66  ? -12.126 89.453  98.625  1.00 7.31  ? 66   PRO K CG  1 
ATOM   11450 C  CD  . PRO K  1 66  ? -10.963 89.293  99.561  1.00 6.59  ? 66   PRO K CD  1 
ATOM   11451 N  N   . LEU K  1 67  ? -13.308 90.579  101.782 1.00 8.20  ? 67   LEU K N   1 
ATOM   11452 C  CA  . LEU K  1 67  ? -14.401 90.668  102.787 1.00 9.43  ? 67   LEU K CA  1 
ATOM   11453 C  C   . LEU K  1 67  ? -13.929 91.266  104.130 1.00 8.98  ? 67   LEU K C   1 
ATOM   11454 O  O   . LEU K  1 67  ? -14.721 91.376  105.064 1.00 9.13  ? 67   LEU K O   1 
ATOM   11455 C  CB  . LEU K  1 67  ? -15.088 89.316  102.991 1.00 8.86  ? 67   LEU K CB  1 
ATOM   11456 C  CG  . LEU K  1 67  ? -15.718 88.624  101.774 1.00 11.61 ? 67   LEU K CG  1 
ATOM   11457 C  CD1 . LEU K  1 67  ? -16.471 87.379  102.195 1.00 12.41 ? 67   LEU K CD1 1 
ATOM   11458 C  CD2 . LEU K  1 67  ? -16.647 89.534  100.958 1.00 15.01 ? 67   LEU K CD2 1 
ATOM   11459 N  N   . SER K  1 68  ? -12.661 91.693  104.214 1.00 8.76  ? 68   SER K N   1 
ATOM   11460 C  CA  . SER K  1 68  ? -12.088 92.287  105.442 1.00 9.01  ? 68   SER K CA  1 
ATOM   11461 C  C   . SER K  1 68  ? -12.347 91.427  106.692 1.00 9.18  ? 68   SER K C   1 
ATOM   11462 O  O   . SER K  1 68  ? -12.902 91.890  107.674 1.00 8.55  ? 68   SER K O   1 
ATOM   11463 C  CB  . SER K  1 68  ? -12.600 93.716  105.718 1.00 10.01 ? 68   SER K CB  1 
ATOM   11464 O  OG  . SER K  1 68  ? -12.349 94.560  104.593 1.00 13.42 ? 68   SER K OG  1 
ATOM   11465 N  N   . ARG K  1 69  ? -11.970 90.161  106.620 1.00 9.30  ? 69   ARG K N   1 
ATOM   11466 C  CA  . ARG K  1 69  ? -12.125 89.250  107.750 1.00 8.56  ? 69   ARG K CA  1 
ATOM   11467 C  C   . ARG K  1 69  ? -10.765 88.946  108.351 1.00 8.48  ? 69   ARG K C   1 
ATOM   11468 O  O   . ARG K  1 69  ? -9.764  89.394  107.829 1.00 7.81  ? 69   ARG K O   1 
ATOM   11469 C  CB  . ARG K  1 69  ? -12.847 87.980  107.291 1.00 8.54  ? 69   ARG K CB  1 
ATOM   11470 C  CG  . ARG K  1 69  ? -14.295 88.247  106.891 1.00 8.98  ? 69   ARG K CG  1 
ATOM   11471 C  CD  . ARG K  1 69  ? -15.130 86.981  106.629 1.00 7.73  ? 69   ARG K CD  1 
ATOM   11472 N  NE  . ARG K  1 69  ? -16.491 87.298  106.220 1.00 9.03  ? 69   ARG K NE  1 
ATOM   11473 C  CZ  . ARG K  1 69  ? -17.436 86.380  105.971 1.00 9.81  ? 69   ARG K CZ  1 
ATOM   11474 N  NH1 . ARG K  1 69  ? -17.162 85.086  106.052 1.00 8.61  ? 69   ARG K NH1 1 
ATOM   11475 N  NH2 . ARG K  1 69  ? -18.645 86.748  105.607 1.00 6.68  ? 69   ARG K NH2 1 
ATOM   11476 N  N   . LYS K  1 70  ? -10.716 88.216  109.472 1.00 7.60  ? 70   LYS K N   1 
ATOM   11477 C  CA  . LYS K  1 70  ? -9.429  87.851  110.043 1.00 8.34  ? 70   LYS K CA  1 
ATOM   11478 C  C   . LYS K  1 70  ? -8.951  86.559  109.400 1.00 7.29  ? 70   LYS K C   1 
ATOM   11479 O  O   . LYS K  1 70  ? -9.729  85.835  108.759 1.00 6.32  ? 70   LYS K O   1 
ATOM   11480 C  CB  . LYS K  1 70  ? -9.545  87.677  111.563 1.00 10.52 ? 70   LYS K CB  1 
ATOM   11481 C  CG  . LYS K  1 70  ? -9.814  89.028  112.252 1.00 13.78 ? 70   LYS K CG  1 
ATOM   11482 C  CD  . LYS K  1 70  ? -9.480  88.992  113.732 1.00 23.40 ? 70   LYS K CD  1 
ATOM   11483 C  CE  . LYS K  1 70  ? -10.020 87.742  114.484 1.00 26.94 ? 70   LYS K CE  1 
ATOM   11484 N  NZ  . LYS K  1 70  ? -9.891  87.948  115.979 1.00 30.05 ? 70   LYS K NZ  1 
ATOM   11485 N  N   . HIS K  1 71  ? -7.668  86.273  109.571 1.00 5.98  ? 71   HIS K N   1 
ATOM   11486 C  CA  . HIS K  1 71  ? -7.087  85.032  109.078 1.00 5.39  ? 71   HIS K CA  1 
ATOM   11487 C  C   . HIS K  1 71  ? -7.685  83.782  109.732 1.00 5.76  ? 71   HIS K C   1 
ATOM   11488 O  O   . HIS K  1 71  ? -7.966  83.756  110.956 1.00 5.00  ? 71   HIS K O   1 
ATOM   11489 C  CB  . HIS K  1 71  ? -5.595  85.040  109.360 1.00 5.83  ? 71   HIS K CB  1 
ATOM   11490 C  CG  . HIS K  1 71  ? -4.886  83.836  108.830 1.00 6.29  ? 71   HIS K CG  1 
ATOM   11491 N  ND1 . HIS K  1 71  ? -4.572  83.689  107.497 1.00 5.25  ? 71   HIS K ND1 1 
ATOM   11492 C  CD2 . HIS K  1 71  ? -4.513  82.684  109.438 1.00 5.00  ? 71   HIS K CD2 1 
ATOM   11493 C  CE1 . HIS K  1 71  ? -3.983  82.519  107.314 1.00 5.35  ? 71   HIS K CE1 1 
ATOM   11494 N  NE2 . HIS K  1 71  ? -3.945  81.883  108.476 1.00 5.00  ? 71   HIS K NE2 1 
ATOM   11495 N  N   . GLY K  1 72  ? -7.873  82.740  108.935 1.00 5.00  ? 72   GLY K N   1 
ATOM   11496 C  CA  . GLY K  1 72  ? -8.358  81.472  109.463 1.00 5.69  ? 72   GLY K CA  1 
ATOM   11497 C  C   . GLY K  1 72  ? -7.925  80.331  108.548 1.00 6.38  ? 72   GLY K C   1 
ATOM   11498 O  O   . GLY K  1 72  ? -7.084  80.563  107.653 1.00 5.75  ? 72   GLY K O   1 
ATOM   11499 N  N   . GLY K  1 73  ? -8.455  79.117  108.768 1.00 5.18  ? 73   GLY K N   1 
ATOM   11500 C  CA  . GLY K  1 73  ? -8.211  78.022  107.841 1.00 5.79  ? 73   GLY K CA  1 
ATOM   11501 C  C   . GLY K  1 73  ? -9.309  78.014  106.764 1.00 6.02  ? 73   GLY K C   1 
ATOM   11502 O  O   . GLY K  1 73  ? -10.352 78.671  106.936 1.00 5.01  ? 73   GLY K O   1 
ATOM   11503 N  N   . PRO K  1 74  ? -9.106  77.285  105.676 1.00 5.00  ? 74   PRO K N   1 
ATOM   11504 C  CA  . PRO K  1 74  ? -10.081 77.279  104.584 1.00 5.71  ? 74   PRO K CA  1 
ATOM   11505 C  C   . PRO K  1 74  ? -11.451 76.793  105.062 1.00 6.85  ? 74   PRO K C   1 
ATOM   11506 O  O   . PRO K  1 74  ? -12.440 77.227  104.459 1.00 5.89  ? 74   PRO K O   1 
ATOM   11507 C  CB  . PRO K  1 74  ? -9.468  76.324  103.515 1.00 6.68  ? 74   PRO K CB  1 
ATOM   11508 C  CG  . PRO K  1 74  ? -8.258  75.631  104.215 1.00 5.89  ? 74   PRO K CG  1 
ATOM   11509 C  CD  . PRO K  1 74  ? -7.906  76.482  105.391 1.00 5.54  ? 74   PRO K CD  1 
ATOM   11510 N  N   . LYS K  1 75  ? -11.510 75.938  106.099 1.00 5.79  ? 75   LYS K N   1 
ATOM   11511 C  CA  . LYS K  1 75  ? -12.795 75.460  106.569 1.00 7.54  ? 75   LYS K CA  1 
ATOM   11512 C  C   . LYS K  1 75  ? -13.536 76.438  107.471 1.00 7.15  ? 75   LYS K C   1 
ATOM   11513 O  O   . LYS K  1 75  ? -14.699 76.197  107.820 1.00 8.02  ? 75   LYS K O   1 
ATOM   11514 C  CB  . LYS K  1 75  ? -12.629 74.135  107.354 1.00 6.46  ? 75   LYS K CB  1 
ATOM   11515 C  CG  . LYS K  1 75  ? -11.884 73.054  106.550 1.00 9.36  ? 75   LYS K CG  1 
ATOM   11516 C  CD  . LYS K  1 75  ? -11.500 71.825  107.449 1.00 9.92  ? 75   LYS K CD  1 
ATOM   11517 C  CE  . LYS K  1 75  ? -12.757 71.026  107.844 1.00 17.13 ? 75   LYS K CE  1 
ATOM   11518 N  NZ  . LYS K  1 75  ? -12.436 69.962  108.823 1.00 19.11 ? 75   LYS K NZ  1 
ATOM   11519 N  N   . ASP K  1 76  ? -12.877 77.509  107.872 1.00 6.54  ? 76   ASP K N   1 
ATOM   11520 C  CA  . ASP K  1 76  ? -13.507 78.485  108.754 1.00 7.56  ? 76   ASP K CA  1 
ATOM   11521 C  C   . ASP K  1 76  ? -14.349 79.504  108.003 1.00 7.45  ? 76   ASP K C   1 
ATOM   11522 O  O   . ASP K  1 76  ? -13.957 79.976  106.931 1.00 6.92  ? 76   ASP K O   1 
ATOM   11523 C  CB  . ASP K  1 76  ? -12.462 79.280  109.540 1.00 7.63  ? 76   ASP K CB  1 
ATOM   11524 C  CG  . ASP K  1 76  ? -11.688 78.425  110.528 1.00 11.39 ? 76   ASP K CG  1 
ATOM   11525 O  OD1 . ASP K  1 76  ? -12.329 77.587  111.235 1.00 10.03 ? 76   ASP K OD1 1 
ATOM   11526 O  OD2 . ASP K  1 76  ? -10.443 78.542  110.696 1.00 11.11 ? 76   ASP K OD2 1 
ATOM   11527 N  N   . GLU K  1 77  ? -15.463 79.887  108.607 1.00 7.11  ? 77   GLU K N   1 
ATOM   11528 C  CA  . GLU K  1 77  ? -16.245 80.969  108.013 1.00 8.61  ? 77   GLU K CA  1 
ATOM   11529 C  C   . GLU K  1 77  ? -15.398 82.254  108.092 1.00 7.75  ? 77   GLU K C   1 
ATOM   11530 O  O   . GLU K  1 77  ? -15.324 83.024  107.114 1.00 8.20  ? 77   GLU K O   1 
ATOM   11531 C  CB  . GLU K  1 77  ? -17.598 81.142  108.718 1.00 9.01  ? 77   GLU K CB  1 
ATOM   11532 C  CG  . GLU K  1 77  ? -18.417 82.209  108.026 1.00 11.95 ? 77   GLU K CG  1 
ATOM   11533 C  CD  . GLU K  1 77  ? -18.810 81.807  106.615 1.00 13.92 ? 77   GLU K CD  1 
ATOM   11534 O  OE1 . GLU K  1 77  ? -18.822 82.683  105.738 1.00 14.61 ? 77   GLU K OE1 1 
ATOM   11535 O  OE2 . GLU K  1 77  ? -19.096 80.610  106.402 1.00 13.14 ? 77   GLU K OE2 1 
ATOM   11536 N  N   . GLU K  1 78  ? -14.750 82.470  109.238 1.00 6.99  ? 78   GLU K N   1 
ATOM   11537 C  CA  . GLU K  1 78  ? -13.941 83.659  109.433 1.00 7.88  ? 78   GLU K CA  1 
ATOM   11538 C  C   . GLU K  1 78  ? -12.560 83.366  108.828 1.00 7.03  ? 78   GLU K C   1 
ATOM   11539 O  O   . GLU K  1 78  ? -11.705 82.748  109.460 1.00 7.18  ? 78   GLU K O   1 
ATOM   11540 C  CB  . GLU K  1 78  ? -13.809 84.044  110.915 1.00 8.66  ? 78   GLU K CB  1 
ATOM   11541 C  CG  . GLU K  1 78  ? -13.040 85.364  111.209 1.00 9.93  ? 78   GLU K CG  1 
ATOM   11542 C  CD  . GLU K  1 78  ? -13.742 86.633  110.746 1.00 12.00 ? 78   GLU K CD  1 
ATOM   11543 O  OE1 . GLU K  1 78  ? -14.890 86.563  110.278 1.00 15.79 ? 78   GLU K OE1 1 
ATOM   11544 O  OE2 . GLU K  1 78  ? -13.144 87.726  110.823 1.00 5.89  ? 78   GLU K OE2 1 
ATOM   11545 N  N   . ARG K  1 79  ? -12.367 83.774  107.590 1.00 6.33  ? 79   ARG K N   1 
ATOM   11546 C  CA  . ARG K  1 79  ? -11.082 83.557  106.944 1.00 5.00  ? 79   ARG K CA  1 
ATOM   11547 C  C   . ARG K  1 79  ? -10.927 84.610  105.883 1.00 5.00  ? 79   ARG K C   1 
ATOM   11548 O  O   . ARG K  1 79  ? -11.904 85.235  105.485 1.00 5.41  ? 79   ARG K O   1 
ATOM   11549 C  CB  . ARG K  1 79  ? -11.038 82.212  106.221 1.00 5.00  ? 79   ARG K CB  1 
ATOM   11550 C  CG  . ARG K  1 79  ? -12.158 81.997  105.145 1.00 5.00  ? 79   ARG K CG  1 
ATOM   11551 C  CD  . ARG K  1 79  ? -11.982 80.731  104.302 1.00 5.49  ? 79   ARG K CD  1 
ATOM   11552 N  NE  . ARG K  1 79  ? -11.166 80.904  103.092 1.00 5.00  ? 79   ARG K NE  1 
ATOM   11553 C  CZ  . ARG K  1 79  ? -11.140 80.037  102.087 1.00 5.35  ? 79   ARG K CZ  1 
ATOM   11554 N  NH1 . ARG K  1 79  ? -11.776 78.879  102.205 1.00 5.00  ? 79   ARG K NH1 1 
ATOM   11555 N  NH2 . ARG K  1 79  ? -10.453 80.327  100.962 1.00 5.10  ? 79   ARG K NH2 1 
ATOM   11556 N  N   . HIS K  1 80  ? -9.710  84.767  105.387 1.00 5.20  ? 80   HIS K N   1 
ATOM   11557 C  CA  . HIS K  1 80  ? -9.469  85.617  104.194 1.00 5.00  ? 80   HIS K CA  1 
ATOM   11558 C  C   . HIS K  1 80  ? -9.817  84.760  102.998 1.00 5.00  ? 80   HIS K C   1 
ATOM   11559 O  O   . HIS K  1 80  ? -9.664  83.548  103.044 1.00 5.63  ? 80   HIS K O   1 
ATOM   11560 C  CB  . HIS K  1 80  ? -7.953  85.944  104.105 1.00 5.00  ? 80   HIS K CB  1 
ATOM   11561 C  CG  . HIS K  1 80  ? -7.426  86.687  105.297 1.00 5.00  ? 80   HIS K CG  1 
ATOM   11562 N  ND1 . HIS K  1 80  ? -6.153  86.484  105.829 1.00 5.23  ? 80   HIS K ND1 1 
ATOM   11563 C  CD2 . HIS K  1 80  ? -8.000  87.668  106.042 1.00 5.00  ? 80   HIS K CD2 1 
ATOM   11564 C  CE1 . HIS K  1 80  ? -5.969  87.344  106.820 1.00 7.62  ? 80   HIS K CE1 1 
ATOM   11565 N  NE2 . HIS K  1 80  ? -7.077  88.059  106.977 1.00 5.35  ? 80   HIS K NE2 1 
ATOM   11566 N  N   . VAL K  1 81  ? -10.253 85.379  101.896 1.00 5.00  ? 81   VAL K N   1 
ATOM   11567 C  CA  . VAL K  1 81  ? -10.495 84.627  100.679 1.00 5.00  ? 81   VAL K CA  1 
ATOM   11568 C  C   . VAL K  1 81  ? -9.245  83.858  100.284 1.00 5.04  ? 81   VAL K C   1 
ATOM   11569 O  O   . VAL K  1 81  ? -9.337  82.709  99.844  1.00 5.00  ? 81   VAL K O   1 
ATOM   11570 C  CB  . VAL K  1 81  ? -10.949 85.575  99.489  1.00 5.00  ? 81   VAL K CB  1 
ATOM   11571 C  CG1 . VAL K  1 81  ? -10.840 84.820  98.140  1.00 5.20  ? 81   VAL K CG1 1 
ATOM   11572 C  CG2 . VAL K  1 81  ? -12.416 86.041  99.754  1.00 5.00  ? 81   VAL K CG2 1 
ATOM   11573 N  N   . GLY K  1 82  ? -8.062  84.468  100.467 1.00 5.00  ? 82   GLY K N   1 
ATOM   11574 C  CA  . GLY K  1 82  ? -6.843  83.754  100.051 1.00 5.00  ? 82   GLY K CA  1 
ATOM   11575 C  C   . GLY K  1 82  ? -6.342  82.654  101.003 1.00 5.00  ? 82   GLY K C   1 
ATOM   11576 O  O   . GLY K  1 82  ? -5.282  82.095  100.784 1.00 5.00  ? 82   GLY K O   1 
ATOM   11577 N  N   . ASP K  1 83  ? -7.107  82.318  102.040 1.00 5.00  ? 83   ASP K N   1 
ATOM   11578 C  CA  . ASP K  1 83  ? -6.615  81.340  103.032 1.00 5.05  ? 83   ASP K CA  1 
ATOM   11579 C  C   . ASP K  1 83  ? -6.828  79.896  102.631 1.00 5.45  ? 83   ASP K C   1 
ATOM   11580 O  O   . ASP K  1 83  ? -7.860  79.324  102.952 1.00 5.27  ? 83   ASP K O   1 
ATOM   11581 C  CB  . ASP K  1 83  ? -7.279  81.575  104.399 1.00 5.00  ? 83   ASP K CB  1 
ATOM   11582 C  CG  . ASP K  1 83  ? -6.794  82.832  105.088 1.00 5.00  ? 83   ASP K CG  1 
ATOM   11583 O  OD1 . ASP K  1 83  ? -5.740  83.443  104.696 1.00 5.00  ? 83   ASP K OD1 1 
ATOM   11584 O  OD2 . ASP K  1 83  ? -7.399  83.280  106.090 1.00 5.00  ? 83   ASP K OD2 1 
ATOM   11585 N  N   . LEU K  1 84  ? -5.852  79.315  101.934 1.00 5.00  ? 84   LEU K N   1 
ATOM   11586 C  CA  . LEU K  1 84  ? -5.965  77.931  101.509 1.00 5.00  ? 84   LEU K CA  1 
ATOM   11587 C  C   . LEU K  1 84  ? -5.297  76.923  102.480 1.00 5.75  ? 84   LEU K C   1 
ATOM   11588 O  O   . LEU K  1 84  ? -5.158  75.752  102.131 1.00 6.47  ? 84   LEU K O   1 
ATOM   11589 C  CB  . LEU K  1 84  ? -5.422  77.795  100.099 1.00 5.00  ? 84   LEU K CB  1 
ATOM   11590 C  CG  . LEU K  1 84  ? -6.213  78.616  99.060  1.00 5.00  ? 84   LEU K CG  1 
ATOM   11591 C  CD1 . LEU K  1 84  ? -5.530  78.417  97.708  1.00 6.63  ? 84   LEU K CD1 1 
ATOM   11592 C  CD2 . LEU K  1 84  ? -7.659  78.149  98.987  1.00 5.71  ? 84   LEU K CD2 1 
ATOM   11593 N  N   . GLY K  1 85  ? -4.909  77.371  103.679 1.00 5.00  ? 85   GLY K N   1 
ATOM   11594 C  CA  . GLY K  1 85  ? -4.447  76.449  104.714 1.00 5.00  ? 85   GLY K CA  1 
ATOM   11595 C  C   . GLY K  1 85  ? -3.020  76.025  104.514 1.00 5.00  ? 85   GLY K C   1 
ATOM   11596 O  O   . GLY K  1 85  ? -2.134  76.850  104.200 1.00 5.00  ? 85   GLY K O   1 
ATOM   11597 N  N   . ASN K  1 86  ? -2.783  74.733  104.718 1.00 5.00  ? 86   ASN K N   1 
ATOM   11598 C  CA  . ASN K  1 86  ? -1.452  74.196  104.544 1.00 5.00  ? 86   ASN K CA  1 
ATOM   11599 C  C   . ASN K  1 86  ? -1.381  73.206  103.414 1.00 5.00  ? 86   ASN K C   1 
ATOM   11600 O  O   . ASN K  1 86  ? -2.385  72.568  103.065 1.00 5.00  ? 86   ASN K O   1 
ATOM   11601 C  CB  . ASN K  1 86  ? -1.043  73.431  105.809 1.00 5.00  ? 86   ASN K CB  1 
ATOM   11602 C  CG  . ASN K  1 86  ? -0.783  74.383  106.956 1.00 5.79  ? 86   ASN K CG  1 
ATOM   11603 O  OD1 . ASN K  1 86  ? 0.103   75.199  106.873 1.00 5.00  ? 86   ASN K OD1 1 
ATOM   11604 N  ND2 . ASN K  1 86  ? -1.597  74.295  108.006 1.00 5.88  ? 86   ASN K ND2 1 
ATOM   11605 N  N   . VAL K  1 87  ? -0.182  73.064  102.878 1.00 5.00  ? 87   VAL K N   1 
ATOM   11606 C  CA  . VAL K  1 87  ? 0.139   71.926  102.027 1.00 5.00  ? 87   VAL K CA  1 
ATOM   11607 C  C   . VAL K  1 87  ? 1.231   71.119  102.735 1.00 5.51  ? 87   VAL K C   1 
ATOM   11608 O  O   . VAL K  1 87  ? 2.005   71.664  103.524 1.00 6.07  ? 87   VAL K O   1 
ATOM   11609 C  CB  . VAL K  1 87  ? 0.558   72.311  100.625 1.00 5.79  ? 87   VAL K CB  1 
ATOM   11610 C  CG1 . VAL K  1 87  ? -0.638  73.005  99.902  1.00 5.00  ? 87   VAL K CG1 1 
ATOM   11611 C  CG2 . VAL K  1 87  ? 1.808   73.192  100.636 1.00 5.88  ? 87   VAL K CG2 1 
ATOM   11612 N  N   . THR K  1 88  ? 1.279   69.814  102.469 1.00 5.00  ? 88   THR K N   1 
ATOM   11613 C  CA  . THR K  1 88  ? 2.198   68.950  103.170 1.00 5.00  ? 88   THR K CA  1 
ATOM   11614 C  C   . THR K  1 88  ? 3.265   68.394  102.258 1.00 5.00  ? 88   THR K C   1 
ATOM   11615 O  O   . THR K  1 88  ? 2.942   67.803  101.226 1.00 5.00  ? 88   THR K O   1 
ATOM   11616 C  CB  . THR K  1 88  ? 1.397   67.783  103.763 1.00 5.00  ? 88   THR K CB  1 
ATOM   11617 O  OG1 . THR K  1 88  ? 0.543   68.272  104.809 1.00 6.10  ? 88   THR K OG1 1 
ATOM   11618 C  CG2 . THR K  1 88  ? 2.345   66.834  104.466 1.00 7.03  ? 88   THR K CG2 1 
ATOM   11619 N  N   . ALA K  1 89  ? 4.521   68.626  102.601 1.00 5.00  ? 89   ALA K N   1 
ATOM   11620 C  CA  . ALA K  1 89  ? 5.600   68.023  101.848 1.00 5.63  ? 89   ALA K CA  1 
ATOM   11621 C  C   . ALA K  1 89  ? 6.028   66.671  102.457 1.00 6.58  ? 89   ALA K C   1 
ATOM   11622 O  O   . ALA K  1 89  ? 6.091   66.485  103.685 1.00 5.60  ? 89   ALA K O   1 
ATOM   11623 C  CB  . ALA K  1 89  ? 6.811   68.957  101.730 1.00 5.01  ? 89   ALA K CB  1 
ATOM   11624 N  N   . ASP K  1 90  ? 6.352   65.743  101.572 1.00 7.49  ? 90   ASP K N   1 
ATOM   11625 C  CA  . ASP K  1 90  ? 6.787   64.416  102.010 1.00 8.99  ? 90   ASP K CA  1 
ATOM   11626 C  C   . ASP K  1 90  ? 8.277   64.391  102.330 1.00 9.63  ? 90   ASP K C   1 
ATOM   11627 O  O   . ASP K  1 90  ? 8.937   65.416  102.318 1.00 9.26  ? 90   ASP K O   1 
ATOM   11628 C  CB  . ASP K  1 90  ? 6.379   63.319  101.000 1.00 9.83  ? 90   ASP K CB  1 
ATOM   11629 C  CG  . ASP K  1 90  ? 7.128   63.401  99.669  1.00 10.47 ? 90   ASP K CG  1 
ATOM   11630 O  OD1 . ASP K  1 90  ? 8.219   64.003  99.617  1.00 11.41 ? 90   ASP K OD1 1 
ATOM   11631 O  OD2 . ASP K  1 90  ? 6.684   62.880  98.614  1.00 10.00 ? 90   ASP K OD2 1 
ATOM   11632 N  N   . LYS K  1 91  ? 8.828   63.209  102.616 1.00 10.45 ? 91   LYS K N   1 
ATOM   11633 C  CA  . LYS K  1 91  ? 10.220  63.135  103.006 1.00 11.11 ? 91   LYS K CA  1 
ATOM   11634 C  C   . LYS K  1 91  ? 11.176  63.465  101.905 1.00 11.07 ? 91   LYS K C   1 
ATOM   11635 O  O   . LYS K  1 91  ? 12.383  63.582  102.151 1.00 12.97 ? 91   LYS K O   1 
ATOM   11636 C  CB  . LYS K  1 91  ? 10.551  61.725  103.500 1.00 11.07 ? 91   LYS K CB  1 
ATOM   11637 C  CG  . LYS K  1 91  ? 10.309  60.638  102.409 1.00 14.11 ? 91   LYS K CG  1 
ATOM   11638 C  CD  . LYS K  1 91  ? 11.474  60.484  101.386 1.00 19.17 ? 91   LYS K CD  1 
ATOM   11639 C  CE  . LYS K  1 91  ? 11.638  58.981  100.891 1.00 22.01 ? 91   LYS K CE  1 
ATOM   11640 N  NZ  . LYS K  1 91  ? 12.715  58.757  99.841  1.00 19.70 ? 91   LYS K NZ  1 
ATOM   11641 N  N   . ASP K  1 92  ? 10.683  63.506  100.676 1.00 9.82  ? 92   ASP K N   1 
ATOM   11642 C  CA  . ASP K  1 92  ? 11.546  63.855  99.570  1.00 9.43  ? 92   ASP K CA  1 
ATOM   11643 C  C   . ASP K  1 92  ? 11.417  65.344  99.274  1.00 8.97  ? 92   ASP K C   1 
ATOM   11644 O  O   . ASP K  1 92  ? 11.956  65.812  98.276  1.00 8.68  ? 92   ASP K O   1 
ATOM   11645 C  CB  . ASP K  1 92  ? 11.193  63.064  98.312  1.00 9.22  ? 92   ASP K CB  1 
ATOM   11646 C  CG  . ASP K  1 92  ? 11.336  61.576  98.492  1.00 13.48 ? 92   ASP K CG  1 
ATOM   11647 O  OD1 . ASP K  1 92  ? 12.332  61.125  99.130  1.00 13.92 ? 92   ASP K OD1 1 
ATOM   11648 O  OD2 . ASP K  1 92  ? 10.492  60.780  98.014  1.00 15.65 ? 92   ASP K OD2 1 
ATOM   11649 N  N   . GLY K  1 93  ? 10.694  66.063  100.137 1.00 8.06  ? 93   GLY K N   1 
ATOM   11650 C  CA  . GLY K  1 93  ? 10.490  67.490  99.970  1.00 7.33  ? 93   GLY K CA  1 
ATOM   11651 C  C   . GLY K  1 93  ? 9.405   67.862  98.969  1.00 6.95  ? 93   GLY K C   1 
ATOM   11652 O  O   . GLY K  1 93  ? 9.322   69.026  98.535  1.00 5.95  ? 93   GLY K O   1 
ATOM   11653 N  N   . VAL K  1 94  ? 8.564   66.893  98.599  1.00 6.51  ? 94   VAL K N   1 
ATOM   11654 C  CA  . VAL K  1 94  ? 7.557   67.116  97.570  1.00 7.96  ? 94   VAL K CA  1 
ATOM   11655 C  C   . VAL K  1 94  ? 6.165   67.275  98.128  1.00 7.39  ? 94   VAL K C   1 
ATOM   11656 O  O   . VAL K  1 94  ? 5.732   66.457  98.944  1.00 8.23  ? 94   VAL K O   1 
ATOM   11657 C  CB  . VAL K  1 94  ? 7.572   65.959  96.525  1.00 7.72  ? 94   VAL K CB  1 
ATOM   11658 C  CG1 . VAL K  1 94  ? 6.493   66.184  95.472  1.00 8.74  ? 94   VAL K CG1 1 
ATOM   11659 C  CG2 . VAL K  1 94  ? 8.956   65.848  95.904  1.00 8.87  ? 94   VAL K CG2 1 
ATOM   11660 N  N   . ALA K  1 95  ? 5.488   68.372  97.763  1.00 6.67  ? 95   ALA K N   1 
ATOM   11661 C  CA  . ALA K  1 95  ? 4.101   68.556  98.183  1.00 6.40  ? 95   ALA K CA  1 
ATOM   11662 C  C   . ALA K  1 95  ? 3.266   68.299  96.951  1.00 6.42  ? 95   ALA K C   1 
ATOM   11663 O  O   . ALA K  1 95  ? 3.367   69.066  95.964  1.00 5.04  ? 95   ALA K O   1 
ATOM   11664 C  CB  . ALA K  1 95  ? 3.825   69.976  98.712  1.00 7.18  ? 95   ALA K CB  1 
ATOM   11665 N  N   . ASP K  1 96  ? 2.506   67.202  96.975  1.00 6.15  ? 96   ASP K N   1 
ATOM   11666 C  CA  . ASP K  1 96  ? 1.592   66.897  95.878  1.00 6.01  ? 96   ASP K CA  1 
ATOM   11667 C  C   . ASP K  1 96  ? 0.256   67.520  96.252  1.00 5.80  ? 96   ASP K C   1 
ATOM   11668 O  O   . ASP K  1 96  ? -0.620  66.884  96.838  1.00 6.27  ? 96   ASP K O   1 
ATOM   11669 C  CB  . ASP K  1 96  ? 1.497   65.385  95.627  1.00 6.59  ? 96   ASP K CB  1 
ATOM   11670 C  CG  . ASP K  1 96  ? 2.781   64.833  95.024  1.00 10.71 ? 96   ASP K CG  1 
ATOM   11671 O  OD1 . ASP K  1 96  ? 3.357   63.852  95.571  1.00 16.07 ? 96   ASP K OD1 1 
ATOM   11672 O  OD2 . ASP K  1 96  ? 3.295   65.362  94.010  1.00 10.48 ? 96   ASP K OD2 1 
ATOM   11673 N  N   . VAL K  1 97  ? 0.107   68.783  95.887  1.00 5.07  ? 97   VAL K N   1 
ATOM   11674 C  CA  . VAL K  1 97  ? -1.023  69.567  96.309  1.00 5.00  ? 97   VAL K CA  1 
ATOM   11675 C  C   . VAL K  1 97  ? -2.309  69.095  95.674  1.00 7.00  ? 97   VAL K C   1 
ATOM   11676 O  O   . VAL K  1 97  ? -2.346  68.787  94.472  1.00 6.18  ? 97   VAL K O   1 
ATOM   11677 C  CB  . VAL K  1 97  ? -0.774  71.066  95.960  1.00 5.00  ? 97   VAL K CB  1 
ATOM   11678 C  CG1 . VAL K  1 97  ? -1.945  71.923  96.406  1.00 5.00  ? 97   VAL K CG1 1 
ATOM   11679 C  CG2 . VAL K  1 97  ? 0.531   71.514  96.629  1.00 5.00  ? 97   VAL K CG2 1 
ATOM   11680 N  N   . SER K  1 98  ? -3.363  69.068  96.482  1.00 7.57  ? 98   SER K N   1 
ATOM   11681 C  CA  . SER K  1 98  ? -4.660  68.652  96.017  1.00 9.92  ? 98   SER K CA  1 
ATOM   11682 C  C   . SER K  1 98  ? -5.701  69.234  96.918  1.00 9.56  ? 98   SER K C   1 
ATOM   11683 O  O   . SER K  1 98  ? -6.032  68.668  97.981  1.00 11.21 ? 98   SER K O   1 
ATOM   11684 C  CB  . SER K  1 98  ? -4.789  67.117  96.061  1.00 11.81 ? 98   SER K CB  1 
ATOM   11685 O  OG  . SER K  1 98  ? -6.016  66.744  95.456  1.00 14.37 ? 98   SER K OG  1 
ATOM   11686 N  N   . ILE K  1 99  ? -6.253  70.356  96.500  1.00 8.34  ? 99   ILE K N   1 
ATOM   11687 C  CA  . ILE K  1 99  ? -7.168  71.083  97.328  1.00 8.51  ? 99   ILE K CA  1 
ATOM   11688 C  C   . ILE K  1 99  ? -8.377  71.419  96.501  1.00 9.32  ? 99   ILE K C   1 
ATOM   11689 O  O   . ILE K  1 99  ? -8.289  71.550  95.271  1.00 8.41  ? 99   ILE K O   1 
ATOM   11690 C  CB  . ILE K  1 99  ? -6.435  72.357  97.784  1.00 9.64  ? 99   ILE K CB  1 
ATOM   11691 C  CG1 . ILE K  1 99  ? -5.534  72.060  99.002  1.00 10.14 ? 99   ILE K CG1 1 
ATOM   11692 C  CG2 . ILE K  1 99  ? -7.395  73.520  98.070  1.00 11.42 ? 99   ILE K CG2 1 
ATOM   11693 C  CD1 . ILE K  1 99  ? -4.630  73.318  99.351  1.00 12.06 ? 99   ILE K CD1 1 
ATOM   11694 N  N   . GLU K  1 100 ? -9.526  71.537  97.157  1.00 9.30  ? 100  GLU K N   1 
ATOM   11695 C  CA  . GLU K  1 100 ? -10.692 72.054  96.460  1.00 10.26 ? 100  GLU K CA  1 
ATOM   11696 C  C   . GLU K  1 100 ? -11.237 73.164  97.349  1.00 9.73  ? 100  GLU K C   1 
ATOM   11697 O  O   . GLU K  1 100 ? -11.342 72.990  98.569  1.00 9.93  ? 100  GLU K O   1 
ATOM   11698 C  CB  . GLU K  1 100 ? -11.747 70.952  96.247  1.00 11.54 ? 100  GLU K CB  1 
ATOM   11699 C  CG  . GLU K  1 100 ? -13.057 71.500  95.705  1.00 16.41 ? 100  GLU K CG  1 
ATOM   11700 C  CD  . GLU K  1 100 ? -14.153 70.442  95.541  1.00 21.88 ? 100  GLU K CD  1 
ATOM   11701 O  OE1 . GLU K  1 100 ? -13.967 69.585  94.667  1.00 23.71 ? 100  GLU K OE1 1 
ATOM   11702 O  OE2 . GLU K  1 100 ? -15.188 70.483  96.271  1.00 20.65 ? 100  GLU K OE2 1 
ATOM   11703 N  N   . ASP K  1 101 ? -11.606 74.304  96.774  1.00 8.18  ? 101  ASP K N   1 
ATOM   11704 C  CA  . ASP K  1 101 ? -12.065 75.403  97.608  1.00 7.82  ? 101  ASP K CA  1 
ATOM   11705 C  C   . ASP K  1 101 ? -13.155 76.152  96.907  1.00 8.70  ? 101  ASP K C   1 
ATOM   11706 O  O   . ASP K  1 101 ? -13.080 76.375  95.697  1.00 9.93  ? 101  ASP K O   1 
ATOM   11707 C  CB  . ASP K  1 101 ? -10.914 76.386  97.858  1.00 7.50  ? 101  ASP K CB  1 
ATOM   11708 C  CG  . ASP K  1 101 ? -11.232 77.386  98.958  1.00 9.29  ? 101  ASP K CG  1 
ATOM   11709 O  OD1 . ASP K  1 101 ? -11.229 76.968  100.166 1.00 10.76 ? 101  ASP K OD1 1 
ATOM   11710 O  OD2 . ASP K  1 101 ? -11.514 78.580  98.732  1.00 6.42  ? 101  ASP K OD2 1 
ATOM   11711 N  N   . SER K  1 102 ? -14.131 76.596  97.675  1.00 8.29  ? 102  SER K N   1 
ATOM   11712 C  CA  . SER K  1 102 ? -15.287 77.239  97.081  1.00 9.93  ? 102  SER K CA  1 
ATOM   11713 C  C   . SER K  1 102 ? -15.346 78.741  97.373  1.00 8.31  ? 102  SER K C   1 
ATOM   11714 O  O   . SER K  1 102 ? -16.231 79.451  96.880  1.00 8.15  ? 102  SER K O   1 
ATOM   11715 C  CB  . SER K  1 102 ? -16.551 76.511  97.553  1.00 11.06 ? 102  SER K CB  1 
ATOM   11716 O  OG  . SER K  1 102 ? -16.705 75.321  96.760  1.00 16.81 ? 102  SER K OG  1 
ATOM   11717 N  N   . VAL K  1 103 ? -14.359 79.232  98.109  1.00 6.50  ? 103  VAL K N   1 
ATOM   11718 C  CA  . VAL K  1 103 ? -14.310 80.637  98.482  1.00 5.23  ? 103  VAL K CA  1 
ATOM   11719 C  C   . VAL K  1 103 ? -13.499 81.443  97.461  1.00 5.26  ? 103  VAL K C   1 
ATOM   11720 O  O   . VAL K  1 103 ? -13.933 82.543  97.027  1.00 5.00  ? 103  VAL K O   1 
ATOM   11721 C  CB  . VAL K  1 103 ? -13.756 80.787  99.888  1.00 5.61  ? 103  VAL K CB  1 
ATOM   11722 C  CG1 . VAL K  1 103 ? -13.610 82.259  100.243 1.00 5.47  ? 103  VAL K CG1 1 
ATOM   11723 C  CG2 . VAL K  1 103 ? -14.732 80.116  100.883 1.00 7.34  ? 103  VAL K CG2 1 
ATOM   11724 N  N   . ILE K  1 104 ? -12.340 80.925  97.069  1.00 5.00  ? 104  ILE K N   1 
ATOM   11725 C  CA  . ILE K  1 104 ? -11.664 81.549  95.912  1.00 5.00  ? 104  ILE K CA  1 
ATOM   11726 C  C   . ILE K  1 104 ? -12.510 81.302  94.658  1.00 5.39  ? 104  ILE K C   1 
ATOM   11727 O  O   . ILE K  1 104 ? -13.411 80.474  94.640  1.00 5.30  ? 104  ILE K O   1 
ATOM   11728 C  CB  . ILE K  1 104 ? -10.269 80.956  95.664  1.00 5.00  ? 104  ILE K CB  1 
ATOM   11729 C  CG1 . ILE K  1 104 ? -10.352 79.434  95.532  1.00 5.00  ? 104  ILE K CG1 1 
ATOM   11730 C  CG2 . ILE K  1 104 ? -9.306  81.303  96.810  1.00 5.00  ? 104  ILE K CG2 1 
ATOM   11731 C  CD1 . ILE K  1 104 ? -9.066  78.796  94.996  1.00 7.66  ? 104  ILE K CD1 1 
ATOM   11732 N  N   . SER K  1 105 ? -12.165 81.995  93.579  1.00 5.00  ? 105  SER K N   1 
ATOM   11733 C  CA  . SER K  1 105 ? -12.863 81.810  92.303  1.00 5.34  ? 105  SER K CA  1 
ATOM   11734 C  C   . SER K  1 105 ? -11.921 82.229  91.188  1.00 5.56  ? 105  SER K C   1 
ATOM   11735 O  O   . SER K  1 105 ? -10.920 82.913  91.441  1.00 5.00  ? 105  SER K O   1 
ATOM   11736 C  CB  . SER K  1 105 ? -14.108 82.691  92.251  1.00 7.24  ? 105  SER K CB  1 
ATOM   11737 O  OG  . SER K  1 105 ? -14.950 82.303  91.161  1.00 8.47  ? 105  SER K OG  1 
ATOM   11738 N  N   . LEU K  1 106 ? -12.220 81.796  89.965  1.00 6.44  ? 106  LEU K N   1 
ATOM   11739 C  CA  . LEU K  1 106 ? -11.466 82.253  88.787  1.00 8.45  ? 106  LEU K CA  1 
ATOM   11740 C  C   . LEU K  1 106 ? -12.257 83.300  87.989  1.00 10.35 ? 106  LEU K C   1 
ATOM   11741 O  O   . LEU K  1 106 ? -11.880 83.638  86.858  1.00 11.39 ? 106  LEU K O   1 
ATOM   11742 C  CB  . LEU K  1 106 ? -11.017 81.087  87.891  1.00 7.86  ? 106  LEU K CB  1 
ATOM   11743 C  CG  . LEU K  1 106 ? -10.209 80.026  88.639  1.00 7.12  ? 106  LEU K CG  1 
ATOM   11744 C  CD1 . LEU K  1 106 ? -9.765  78.931  87.670  1.00 11.40 ? 106  LEU K CD1 1 
ATOM   11745 C  CD2 . LEU K  1 106 ? -8.983  80.653  89.375  1.00 7.65  ? 106  LEU K CD2 1 
ATOM   11746 N  N   . SER K  1 107 ? -13.314 83.844  88.575  1.00 10.69 ? 107  SER K N   1 
ATOM   11747 C  CA  . SER K  1 107 ? -14.031 84.962  87.948  1.00 13.59 ? 107  SER K CA  1 
ATOM   11748 C  C   . SER K  1 107 ? -14.814 85.693  89.040  1.00 13.60 ? 107  SER K C   1 
ATOM   11749 O  O   . SER K  1 107 ? -14.865 85.224  90.173  1.00 13.76 ? 107  SER K O   1 
ATOM   11750 C  CB  . SER K  1 107 ? -14.969 84.456  86.868  1.00 13.46 ? 107  SER K CB  1 
ATOM   11751 O  OG  . SER K  1 107 ? -16.077 83.892  87.520  1.00 17.46 ? 107  SER K OG  1 
ATOM   11752 N  N   . GLY K  1 108 ? -15.366 86.866  88.744  1.00 14.31 ? 108  GLY K N   1 
ATOM   11753 C  CA  . GLY K  1 108 ? -16.148 87.590  89.747  1.00 15.33 ? 108  GLY K CA  1 
ATOM   11754 C  C   . GLY K  1 108 ? -15.368 88.257  90.870  1.00 16.78 ? 108  GLY K C   1 
ATOM   11755 O  O   . GLY K  1 108 ? -14.160 88.419  90.788  1.00 16.06 ? 108  GLY K O   1 
ATOM   11756 N  N   . ASP K  1 109 ? -16.059 88.589  91.960  1.00 17.19 ? 109  ASP K N   1 
ATOM   11757 C  CA  . ASP K  1 109 ? -15.451 89.342  93.050  1.00 18.01 ? 109  ASP K CA  1 
ATOM   11758 C  C   . ASP K  1 109 ? -14.309 88.677  93.823  1.00 17.02 ? 109  ASP K C   1 
ATOM   11759 O  O   . ASP K  1 109 ? -13.437 89.363  94.363  1.00 18.88 ? 109  ASP K O   1 
ATOM   11760 C  CB  . ASP K  1 109 ? -16.514 89.769  94.048  1.00 18.49 ? 109  ASP K CB  1 
ATOM   11761 C  CG  . ASP K  1 109 ? -17.355 90.914  93.528  1.00 22.56 ? 109  ASP K CG  1 
ATOM   11762 O  OD1 . ASP K  1 109 ? -18.236 91.403  94.283  1.00 25.01 ? 109  ASP K OD1 1 
ATOM   11763 O  OD2 . ASP K  1 109 ? -17.195 91.389  92.374  1.00 25.73 ? 109  ASP K OD2 1 
ATOM   11764 N  N   . HIS K  1 110 ? -14.323 87.356  93.915  1.00 14.25 ? 110  HIS K N   1 
ATOM   11765 C  CA  . HIS K  1 110 ? -13.252 86.688  94.649  1.00 11.47 ? 110  HIS K CA  1 
ATOM   11766 C  C   . HIS K  1 110 ? -12.248 86.077  93.690  1.00 9.50  ? 110  HIS K C   1 
ATOM   11767 O  O   . HIS K  1 110 ? -11.596 85.080  94.026  1.00 7.27  ? 110  HIS K O   1 
ATOM   11768 C  CB  . HIS K  1 110 ? -13.807 85.584  95.523  1.00 12.02 ? 110  HIS K CB  1 
ATOM   11769 C  CG  . HIS K  1 110 ? -14.645 86.077  96.658  1.00 14.76 ? 110  HIS K CG  1 
ATOM   11770 N  ND1 . HIS K  1 110 ? -15.168 85.232  97.614  1.00 14.63 ? 110  HIS K ND1 1 
ATOM   11771 C  CD2 . HIS K  1 110 ? -15.063 87.324  96.980  1.00 15.52 ? 110  HIS K CD2 1 
ATOM   11772 C  CE1 . HIS K  1 110 ? -15.870 85.942  98.480  1.00 17.83 ? 110  HIS K CE1 1 
ATOM   11773 N  NE2 . HIS K  1 110 ? -15.805 87.215  98.126  1.00 16.57 ? 110  HIS K NE2 1 
ATOM   11774 N  N   . CYS K  1 111 ? -12.151 86.683  92.505  1.00 7.87  ? 111  CYS K N   1 
ATOM   11775 C  CA  . CYS K  1 111 ? -11.314 86.183  91.434  1.00 8.56  ? 111  CYS K CA  1 
ATOM   11776 C  C   . CYS K  1 111 ? -9.855  86.295  91.894  1.00 7.78  ? 111  CYS K C   1 
ATOM   11777 O  O   . CYS K  1 111 ? -9.495  87.321  92.472  1.00 8.17  ? 111  CYS K O   1 
ATOM   11778 C  CB  . CYS K  1 111 ? -11.572 86.999  90.152  1.00 8.70  ? 111  CYS K CB  1 
ATOM   11779 S  SG  . CYS K  1 111 ? -10.652 86.251  88.816  1.00 15.65 ? 111  CYS K SG  1 
ATOM   11780 N  N   . ILE K  1 112 ? -9.040  85.244  91.681  1.00 5.84  ? 112  ILE K N   1 
ATOM   11781 C  CA  . ILE K  1 112 ? -7.607  85.287  92.080  1.00 5.94  ? 112  ILE K CA  1 
ATOM   11782 C  C   . ILE K  1 112 ? -6.625  85.387  90.902  1.00 5.44  ? 112  ILE K C   1 
ATOM   11783 O  O   . ILE K  1 112 ? -5.425  85.384  91.102  1.00 5.26  ? 112  ILE K O   1 
ATOM   11784 C  CB  . ILE K  1 112 ? -7.265  84.096  92.924  1.00 5.36  ? 112  ILE K CB  1 
ATOM   11785 C  CG1 . ILE K  1 112 ? -7.478  82.802  92.109  1.00 5.00  ? 112  ILE K CG1 1 
ATOM   11786 C  CG2 . ILE K  1 112 ? -8.129  84.165  94.247  1.00 5.11  ? 112  ILE K CG2 1 
ATOM   11787 C  CD1 . ILE K  1 112 ? -7.089  81.501  92.937  1.00 5.00  ? 112  ILE K CD1 1 
ATOM   11788 N  N   . ILE K  1 113 ? -7.166  85.453  89.680  1.00 5.00  ? 113  ILE K N   1 
ATOM   11789 C  CA  . ILE K  1 113 ? -6.327  85.654  88.512  1.00 5.27  ? 113  ILE K CA  1 
ATOM   11790 C  C   . ILE K  1 113 ? -5.596  87.003  88.659  1.00 5.00  ? 113  ILE K C   1 
ATOM   11791 O  O   . ILE K  1 113 ? -6.212  87.993  89.014  1.00 5.00  ? 113  ILE K O   1 
ATOM   11792 C  CB  . ILE K  1 113 ? -7.159  85.621  87.192  1.00 6.16  ? 113  ILE K CB  1 
ATOM   11793 C  CG1 . ILE K  1 113 ? -7.883  84.291  87.013  1.00 8.12  ? 113  ILE K CG1 1 
ATOM   11794 C  CG2 . ILE K  1 113 ? -6.192  85.857  85.975  1.00 5.97  ? 113  ILE K CG2 1 
ATOM   11795 C  CD1 . ILE K  1 113 ? -6.975  83.157  86.903  1.00 14.81 ? 113  ILE K CD1 1 
ATOM   11796 N  N   . GLY K  1 114 ? -4.279  86.998  88.428  1.00 5.00  ? 114  GLY K N   1 
ATOM   11797 C  CA  . GLY K  1 114 ? -3.465  88.201  88.516  1.00 5.00  ? 114  GLY K CA  1 
ATOM   11798 C  C   . GLY K  1 114 ? -3.075  88.509  89.949  1.00 5.00  ? 114  GLY K C   1 
ATOM   11799 O  O   . GLY K  1 114 ? -2.501  89.554  90.205  1.00 5.00  ? 114  GLY K O   1 
ATOM   11800 N  N   . ARG K  1 115 ? -3.417  87.605  90.885  1.00 5.00  ? 115  ARG K N   1 
ATOM   11801 C  CA  . ARG K  1 115 ? -2.919  87.730  92.256  1.00 5.00  ? 115  ARG K CA  1 
ATOM   11802 C  C   . ARG K  1 115 ? -1.736  86.740  92.426  1.00 5.48  ? 115  ARG K C   1 
ATOM   11803 O  O   . ARG K  1 115 ? -1.328  86.107  91.461  1.00 5.00  ? 115  ARG K O   1 
ATOM   11804 C  CB  . ARG K  1 115 ? -4.067  87.531  93.233  1.00 5.00  ? 115  ARG K CB  1 
ATOM   11805 C  CG  . ARG K  1 115 ? -5.188  88.526  92.957  1.00 5.00  ? 115  ARG K CG  1 
ATOM   11806 C  CD  . ARG K  1 115 ? -6.239  88.612  94.054  1.00 5.00  ? 115  ARG K CD  1 
ATOM   11807 N  NE  . ARG K  1 115 ? -7.329  89.481  93.624  1.00 5.52  ? 115  ARG K NE  1 
ATOM   11808 C  CZ  . ARG K  1 115 ? -7.375  90.806  93.799  1.00 5.44  ? 115  ARG K CZ  1 
ATOM   11809 N  NH1 . ARG K  1 115 ? -6.378  91.480  94.383  1.00 5.00  ? 115  ARG K NH1 1 
ATOM   11810 N  NH2 . ARG K  1 115 ? -8.453  91.470  93.383  1.00 5.67  ? 115  ARG K NH2 1 
ATOM   11811 N  N   . THR K  1 116 ? -1.170  86.645  93.634  1.00 5.00  ? 116  THR K N   1 
ATOM   11812 C  CA  . THR K  1 116 ? 0.034   85.833  93.828  1.00 5.00  ? 116  THR K CA  1 
ATOM   11813 C  C   . THR K  1 116 ? -0.221  84.673  94.726  1.00 5.27  ? 116  THR K C   1 
ATOM   11814 O  O   . THR K  1 116 ? -0.732  84.874  95.845  1.00 5.00  ? 116  THR K O   1 
ATOM   11815 C  CB  . THR K  1 116 ? 1.102   86.694  94.481  1.00 5.00  ? 116  THR K CB  1 
ATOM   11816 O  OG1 . THR K  1 116 ? 1.561   87.651  93.507  1.00 5.00  ? 116  THR K OG1 1 
ATOM   11817 C  CG2 . THR K  1 116 ? 2.411   85.887  94.775  1.00 5.18  ? 116  THR K CG2 1 
ATOM   11818 N  N   . LEU K  1 117 ? 0.194   83.489  94.295  1.00 5.00  ? 117  LEU K N   1 
ATOM   11819 C  CA  . LEU K  1 117 ? 0.090   82.313  95.178  1.00 5.00  ? 117  LEU K CA  1 
ATOM   11820 C  C   . LEU K  1 117 ? 1.437   82.232  95.899  1.00 5.00  ? 117  LEU K C   1 
ATOM   11821 O  O   . LEU K  1 117 ? 2.476   82.359  95.262  1.00 5.00  ? 117  LEU K O   1 
ATOM   11822 C  CB  . LEU K  1 117 ? -0.098  81.060  94.332  1.00 5.00  ? 117  LEU K CB  1 
ATOM   11823 C  CG  . LEU K  1 117 ? -0.184  79.719  95.100  1.00 5.00  ? 117  LEU K CG  1 
ATOM   11824 C  CD1 . LEU K  1 117 ? -1.461  79.708  95.936  1.00 5.02  ? 117  LEU K CD1 1 
ATOM   11825 C  CD2 . LEU K  1 117 ? -0.261  78.529  94.077  1.00 5.00  ? 117  LEU K CD2 1 
ATOM   11826 N  N   . VAL K  1 118 ? 1.413   81.988  97.212  1.00 5.00  ? 118  VAL K N   1 
ATOM   11827 C  CA  . VAL K  1 118 ? 2.648   81.926  98.012  1.00 5.00  ? 118  VAL K CA  1 
ATOM   11828 C  C   . VAL K  1 118 ? 2.715   80.632  98.797  1.00 5.00  ? 118  VAL K C   1 
ATOM   11829 O  O   . VAL K  1 118 ? 1.704   80.251  99.370  1.00 5.00  ? 118  VAL K O   1 
ATOM   11830 C  CB  . VAL K  1 118 ? 2.715   83.110  99.000  1.00 5.00  ? 118  VAL K CB  1 
ATOM   11831 C  CG1 . VAL K  1 118 ? 4.045   83.083  99.854  1.00 5.39  ? 118  VAL K CG1 1 
ATOM   11832 C  CG2 . VAL K  1 118 ? 2.671   84.455  98.216  1.00 5.00  ? 118  VAL K CG2 1 
ATOM   11833 N  N   . VAL K  1 119 ? 3.898   79.978  98.827  1.00 5.00  ? 119  VAL K N   1 
ATOM   11834 C  CA  . VAL K  1 119 ? 4.097   78.843  99.730  1.00 5.00  ? 119  VAL K CA  1 
ATOM   11835 C  C   . VAL K  1 119 ? 5.128   79.297  100.776 1.00 5.00  ? 119  VAL K C   1 
ATOM   11836 O  O   . VAL K  1 119 ? 6.126   79.921  100.440 1.00 5.00  ? 119  VAL K O   1 
ATOM   11837 C  CB  . VAL K  1 119 ? 4.480   77.535  99.019  1.00 5.00  ? 119  VAL K CB  1 
ATOM   11838 C  CG1 . VAL K  1 119 ? 5.772   77.708  98.207  1.00 5.00  ? 119  VAL K CG1 1 
ATOM   11839 C  CG2 . VAL K  1 119 ? 4.651   76.383  100.060 1.00 5.02  ? 119  VAL K CG2 1 
ATOM   11840 N  N   . HIS K  1 120 ? 4.852   78.962  102.048 1.00 5.00  ? 120  HIS K N   1 
ATOM   11841 C  CA  . HIS K  1 120 ? 5.590   79.549  103.164 1.00 5.00  ? 120  HIS K CA  1 
ATOM   11842 C  C   . HIS K  1 120 ? 6.522   78.594  103.865 1.00 5.00  ? 120  HIS K C   1 
ATOM   11843 O  O   . HIS K  1 120 ? 6.450   77.378  103.689 1.00 5.00  ? 120  HIS K O   1 
ATOM   11844 C  CB  . HIS K  1 120 ? 4.578   80.003  104.226 1.00 5.00  ? 120  HIS K CB  1 
ATOM   11845 C  CG  . HIS K  1 120 ? 3.927   81.299  103.919 1.00 5.00  ? 120  HIS K CG  1 
ATOM   11846 N  ND1 . HIS K  1 120 ? 4.505   82.514  104.256 1.00 5.00  ? 120  HIS K ND1 1 
ATOM   11847 C  CD2 . HIS K  1 120 ? 2.746   81.591  103.317 1.00 5.00  ? 120  HIS K CD2 1 
ATOM   11848 C  CE1 . HIS K  1 120 ? 3.696   83.496  103.884 1.00 9.08  ? 120  HIS K CE1 1 
ATOM   11849 N  NE2 . HIS K  1 120 ? 2.622   82.961  103.343 1.00 5.00  ? 120  HIS K NE2 1 
ATOM   11850 N  N   . GLU K  1 121 ? 7.349   79.193  104.712 1.00 5.00  ? 121  GLU K N   1 
ATOM   11851 C  CA  . GLU K  1 121 ? 8.375   78.498  105.496 1.00 5.00  ? 121  GLU K CA  1 
ATOM   11852 C  C   . GLU K  1 121 ? 7.863   77.449  106.461 1.00 5.00  ? 121  GLU K C   1 
ATOM   11853 O  O   . GLU K  1 121 ? 8.444   76.361  106.585 1.00 5.99  ? 121  GLU K O   1 
ATOM   11854 C  CB  . GLU K  1 121 ? 9.068   79.575  106.331 1.00 5.00  ? 121  GLU K CB  1 
ATOM   11855 C  CG  . GLU K  1 121 ? 10.168  79.076  107.242 1.00 8.62  ? 121  GLU K CG  1 
ATOM   11856 C  CD  . GLU K  1 121 ? 10.690  80.200  108.131 1.00 13.74 ? 121  GLU K CD  1 
ATOM   11857 O  OE1 . GLU K  1 121 ? 10.105  81.336  108.138 1.00 10.48 ? 121  GLU K OE1 1 
ATOM   11858 O  OE2 . GLU K  1 121 ? 11.679  79.928  108.860 1.00 15.01 ? 121  GLU K OE2 1 
ATOM   11859 N  N   . LYS K  1 122 ? 6.782   77.789  107.133 1.00 5.31  ? 122  LYS K N   1 
ATOM   11860 C  CA  . LYS K  1 122 ? 6.277   77.069  108.276 1.00 7.29  ? 122  LYS K CA  1 
ATOM   11861 C  C   . LYS K  1 122 ? 4.796   76.796  108.170 1.00 6.60  ? 122  LYS K C   1 
ATOM   11862 O  O   . LYS K  1 122 ? 4.112   77.290  107.256 1.00 6.28  ? 122  LYS K O   1 
ATOM   11863 C  CB  . LYS K  1 122 ? 6.499   77.977  109.520 1.00 9.89  ? 122  LYS K CB  1 
ATOM   11864 C  CG  . LYS K  1 122 ? 7.959   78.167  109.895 1.00 14.53 ? 122  LYS K CG  1 
ATOM   11865 C  CD  . LYS K  1 122 ? 8.066   78.868  111.231 1.00 18.70 ? 122  LYS K CD  1 
ATOM   11866 C  CE  . LYS K  1 122 ? 7.912   80.363  111.143 1.00 22.06 ? 122  LYS K CE  1 
ATOM   11867 N  NZ  . LYS K  1 122 ? 8.409   81.019  112.444 1.00 26.53 ? 122  LYS K NZ  1 
ATOM   11868 N  N   . ALA K  1 123 ? 4.285   76.002  109.105 1.00 5.50  ? 123  ALA K N   1 
ATOM   11869 C  CA  . ALA K  1 123 ? 2.854   75.750  109.112 1.00 5.29  ? 123  ALA K CA  1 
ATOM   11870 C  C   . ALA K  1 123 ? 2.027   76.992  109.362 1.00 5.24  ? 123  ALA K C   1 
ATOM   11871 O  O   . ALA K  1 123 ? 2.395   77.892  110.146 1.00 5.00  ? 123  ALA K O   1 
ATOM   11872 C  CB  . ALA K  1 123 ? 2.501   74.690  110.198 1.00 7.22  ? 123  ALA K CB  1 
ATOM   11873 N  N   . ASP K  1 124 ? 0.866   77.010  108.733 1.00 5.00  ? 124  ASP K N   1 
ATOM   11874 C  CA  . ASP K  1 124 ? -0.118  78.058  108.987 1.00 5.00  ? 124  ASP K CA  1 
ATOM   11875 C  C   . ASP K  1 124 ? -0.875  77.533  110.201 1.00 5.00  ? 124  ASP K C   1 
ATOM   11876 O  O   . ASP K  1 124 ? -1.322  76.379  110.187 1.00 5.00  ? 124  ASP K O   1 
ATOM   11877 C  CB  . ASP K  1 124 ? -1.006  78.155  107.727 1.00 5.00  ? 124  ASP K CB  1 
ATOM   11878 C  CG  . ASP K  1 124 ? -2.098  79.161  107.835 1.00 6.26  ? 124  ASP K CG  1 
ATOM   11879 O  OD1 . ASP K  1 124 ? -2.507  79.559  108.974 1.00 5.04  ? 124  ASP K OD1 1 
ATOM   11880 O  OD2 . ASP K  1 124 ? -2.611  79.642  106.804 1.00 5.82  ? 124  ASP K OD2 1 
ATOM   11881 N  N   . ASP K  1 125 ? -0.940  78.335  111.271 1.00 5.00  ? 125  ASP K N   1 
ATOM   11882 C  CA  . ASP K  1 125 ? -1.665  77.908  112.467 1.00 5.00  ? 125  ASP K CA  1 
ATOM   11883 C  C   . ASP K  1 125 ? -3.184  78.100  112.415 1.00 5.00  ? 125  ASP K C   1 
ATOM   11884 O  O   . ASP K  1 125 ? -3.911  77.849  113.390 1.00 5.00  ? 125  ASP K O   1 
ATOM   11885 C  CB  . ASP K  1 125 ? -1.062  78.521  113.766 1.00 5.00  ? 125  ASP K CB  1 
ATOM   11886 C  CG  . ASP K  1 125 ? -1.239  80.036  113.879 1.00 5.00  ? 125  ASP K CG  1 
ATOM   11887 O  OD1 . ASP K  1 125 ? -2.123  80.646  113.219 1.00 5.00  ? 125  ASP K OD1 1 
ATOM   11888 O  OD2 . ASP K  1 125 ? -0.548  80.703  114.682 1.00 5.00  ? 125  ASP K OD2 1 
ATOM   11889 N  N   . LEU K  1 126 ? -3.647  78.578  111.264 1.00 5.00  ? 126  LEU K N   1 
ATOM   11890 C  CA  . LEU K  1 126 ? -5.065  78.680  110.993 1.00 5.01  ? 126  LEU K CA  1 
ATOM   11891 C  C   . LEU K  1 126 ? -5.784  79.658  111.935 1.00 5.45  ? 126  LEU K C   1 
ATOM   11892 O  O   . LEU K  1 126 ? -6.985  79.522  112.131 1.00 5.06  ? 126  LEU K O   1 
ATOM   11893 C  CB  . LEU K  1 126 ? -5.724  77.272  110.933 1.00 5.05  ? 126  LEU K CB  1 
ATOM   11894 C  CG  . LEU K  1 126 ? -4.941  76.199  110.160 1.00 6.82  ? 126  LEU K CG  1 
ATOM   11895 C  CD1 . LEU K  1 126 ? -5.774  74.894  110.128 1.00 8.60  ? 126  LEU K CD1 1 
ATOM   11896 C  CD2 . LEU K  1 126 ? -4.611  76.629  108.703 1.00 5.94  ? 126  LEU K CD2 1 
ATOM   11897 N  N   . GLY K  1 127 ? -5.032  80.629  112.488 1.00 5.00  ? 127  GLY K N   1 
ATOM   11898 C  CA  . GLY K  1 127 ? -5.590  81.694  113.306 1.00 5.00  ? 127  GLY K CA  1 
ATOM   11899 C  C   . GLY K  1 127 ? -5.686  81.274  114.765 1.00 5.00  ? 127  GLY K C   1 
ATOM   11900 O  O   . GLY K  1 127 ? -6.240  82.009  115.575 1.00 5.00  ? 127  GLY K O   1 
ATOM   11901 N  N   . LYS K  1 128 ? -5.114  80.121  115.089 1.00 5.00  ? 128  LYS K N   1 
ATOM   11902 C  CA  . LYS K  1 128 ? -5.180  79.591  116.468 1.00 5.00  ? 128  LYS K CA  1 
ATOM   11903 C  C   . LYS K  1 128 ? -3.915  79.741  117.295 1.00 5.00  ? 128  LYS K C   1 
ATOM   11904 O  O   . LYS K  1 128 ? -3.771  79.075  118.335 1.00 5.00  ? 128  LYS K O   1 
ATOM   11905 C  CB  . LYS K  1 128 ? -5.627  78.117  116.468 1.00 5.32  ? 128  LYS K CB  1 
ATOM   11906 C  CG  . LYS K  1 128 ? -6.998  77.927  115.806 1.00 7.28  ? 128  LYS K CG  1 
ATOM   11907 C  CD  . LYS K  1 128 ? -7.491  76.490  116.036 1.00 11.10 ? 128  LYS K CD  1 
ATOM   11908 C  CE  . LYS K  1 128 ? -8.969  76.362  115.622 1.00 16.94 ? 128  LYS K CE  1 
ATOM   11909 N  NZ  . LYS K  1 128 ? -9.030  75.776  114.248 1.00 19.86 ? 128  LYS K NZ  1 
ATOM   11910 N  N   . GLY K  1 129 ? -3.004  80.604  116.872 1.00 5.00  ? 129  GLY K N   1 
ATOM   11911 C  CA  . GLY K  1 129 ? -1.732  80.737  117.589 1.00 5.00  ? 129  GLY K CA  1 
ATOM   11912 C  C   . GLY K  1 129 ? -1.664  81.703  118.771 1.00 5.00  ? 129  GLY K C   1 
ATOM   11913 O  O   . GLY K  1 129 ? -0.604  81.807  119.397 1.00 5.00  ? 129  GLY K O   1 
ATOM   11914 N  N   . GLY K  1 130 ? -2.746  82.405  119.080 1.00 5.00  ? 130  GLY K N   1 
ATOM   11915 C  CA  . GLY K  1 130 ? -2.734  83.202  120.305 1.00 5.00  ? 130  GLY K CA  1 
ATOM   11916 C  C   . GLY K  1 130 ? -1.962  84.527  120.233 1.00 5.00  ? 130  GLY K C   1 
ATOM   11917 O  O   . GLY K  1 130 ? -1.572  85.106  121.271 1.00 5.00  ? 130  GLY K O   1 
ATOM   11918 N  N   . ASN K  1 131 ? -1.737  85.011  119.014 1.00 5.00  ? 131  ASN K N   1 
ATOM   11919 C  CA  . ASN K  1 131 ? -1.132  86.358  118.860 1.00 5.38  ? 131  ASN K CA  1 
ATOM   11920 C  C   . ASN K  1 131 ? -1.645  87.129  117.657 1.00 6.20  ? 131  ASN K C   1 
ATOM   11921 O  O   . ASN K  1 131 ? -2.414  86.591  116.880 1.00 5.99  ? 131  ASN K O   1 
ATOM   11922 C  CB  . ASN K  1 131 ? 0.393   86.280  118.883 1.00 5.31  ? 131  ASN K CB  1 
ATOM   11923 C  CG  . ASN K  1 131 ? 0.987   85.473  117.719 1.00 8.24  ? 131  ASN K CG  1 
ATOM   11924 O  OD1 . ASN K  1 131 ? 0.323   85.141  116.731 1.00 7.22  ? 131  ASN K OD1 1 
ATOM   11925 N  ND2 . ASN K  1 131 ? 2.266   85.146  117.853 1.00 10.91 ? 131  ASN K ND2 1 
ATOM   11926 N  N   . GLU K  1 132 ? -1.264  88.407  117.541 1.00 5.37  ? 132  GLU K N   1 
ATOM   11927 C  CA  . GLU K  1 132 ? -1.743  89.218  116.443 1.00 8.43  ? 132  GLU K CA  1 
ATOM   11928 C  C   . GLU K  1 132 ? -1.352  88.604  115.096 1.00 7.35  ? 132  GLU K C   1 
ATOM   11929 O  O   . GLU K  1 132 ? -2.156  88.573  114.145 1.00 8.05  ? 132  GLU K O   1 
ATOM   11930 C  CB  . GLU K  1 132 ? -1.189  90.639  116.527 1.00 8.27  ? 132  GLU K CB  1 
ATOM   11931 C  CG  . GLU K  1 132 ? -1.940  91.560  115.593 1.00 14.34 ? 132  GLU K CG  1 
ATOM   11932 C  CD  . GLU K  1 132 ? -1.559  93.026  115.742 1.00 22.88 ? 132  GLU K CD  1 
ATOM   11933 O  OE1 . GLU K  1 132 ? -0.549  93.346  116.425 1.00 26.03 ? 132  GLU K OE1 1 
ATOM   11934 O  OE2 . GLU K  1 132 ? -2.277  93.852  115.143 1.00 25.70 ? 132  GLU K OE2 1 
ATOM   11935 N  N   . GLU K  1 133 ? -0.119  88.122  115.012 1.00 6.73  ? 133  GLU K N   1 
ATOM   11936 C  CA  . GLU K  1 133 ? 0.369   87.572  113.755 1.00 8.33  ? 133  GLU K CA  1 
ATOM   11937 C  C   . GLU K  1 133 ? -0.493  86.392  113.326 1.00 6.53  ? 133  GLU K C   1 
ATOM   11938 O  O   . GLU K  1 133 ? -0.766  86.214  112.136 1.00 7.35  ? 133  GLU K O   1 
ATOM   11939 C  CB  . GLU K  1 133 ? 1.836   87.148  113.919 1.00 9.30  ? 133  GLU K CB  1 
ATOM   11940 C  CG  . GLU K  1 133 ? 2.545   86.840  112.621 1.00 11.50 ? 133  GLU K CG  1 
ATOM   11941 C  CD  . GLU K  1 133 ? 2.707   88.065  111.730 1.00 16.16 ? 133  GLU K CD  1 
ATOM   11942 O  OE1 . GLU K  1 133 ? 3.154   89.125  112.200 1.00 17.37 ? 133  GLU K OE1 1 
ATOM   11943 O  OE2 . GLU K  1 133 ? 2.402   87.951  110.540 1.00 19.82 ? 133  GLU K OE2 1 
ATOM   11944 N  N   . SER K  1 134 ? -0.954  85.588  114.294 1.00 5.49  ? 134  SER K N   1 
ATOM   11945 C  CA  . SER K  1 134 ? -1.825  84.447  113.953 1.00 5.25  ? 134  SER K CA  1 
ATOM   11946 C  C   . SER K  1 134 ? -3.089  84.907  113.209 1.00 5.51  ? 134  SER K C   1 
ATOM   11947 O  O   . SER K  1 134 ? -3.554  84.241  112.278 1.00 5.00  ? 134  SER K O   1 
ATOM   11948 C  CB  . SER K  1 134 ? -2.233  83.618  115.198 1.00 5.15  ? 134  SER K CB  1 
ATOM   11949 O  OG  . SER K  1 134 ? -3.090  82.558  114.800 1.00 5.00  ? 134  SER K OG  1 
ATOM   11950 N  N   . THR K  1 135 ? -3.630  86.044  113.626 1.00 5.45  ? 135  THR K N   1 
ATOM   11951 C  CA  . THR K  1 135 ? -4.873  86.572  113.024 1.00 6.80  ? 135  THR K CA  1 
ATOM   11952 C  C   . THR K  1 135 ? -4.627  87.286  111.704 1.00 6.98  ? 135  THR K C   1 
ATOM   11953 O  O   . THR K  1 135 ? -5.576  87.794  111.074 1.00 5.32  ? 135  THR K O   1 
ATOM   11954 C  CB  . THR K  1 135 ? -5.546  87.614  113.983 1.00 7.36  ? 135  THR K CB  1 
ATOM   11955 O  OG1 . THR K  1 135 ? -4.755  88.819  113.999 1.00 11.59 ? 135  THR K OG1 1 
ATOM   11956 C  CG2 . THR K  1 135 ? -5.514  87.123  115.368 1.00 9.91  ? 135  THR K CG2 1 
ATOM   11957 N  N   . LYS K  1 136 ? -3.362  87.387  111.315 1.00 6.86  ? 136  LYS K N   1 
ATOM   11958 C  CA  . LYS K  1 136 ? -3.007  87.996  110.023 1.00 8.24  ? 136  LYS K CA  1 
ATOM   11959 C  C   . LYS K  1 136 ? -2.443  87.036  108.991 1.00 8.05  ? 136  LYS K C   1 
ATOM   11960 O  O   . LYS K  1 136 ? -2.903  87.024  107.848 1.00 7.70  ? 136  LYS K O   1 
ATOM   11961 C  CB  . LYS K  1 136 ? -1.995  89.112  110.243 1.00 8.08  ? 136  LYS K CB  1 
ATOM   11962 C  CG  . LYS K  1 136 ? -2.554  90.271  110.970 1.00 14.75 ? 136  LYS K CG  1 
ATOM   11963 C  CD  . LYS K  1 136 ? -1.749  91.529  110.700 1.00 22.11 ? 136  LYS K CD  1 
ATOM   11964 C  CE  . LYS K  1 136 ? -0.671  91.731  111.716 1.00 25.21 ? 136  LYS K CE  1 
ATOM   11965 N  N   . THR K  1 137 ? -1.466  86.216  109.373 1.00 6.67  ? 137  THR K N   1 
ATOM   11966 C  CA  . THR K  1 137 ? -0.777  85.355  108.408 1.00 7.57  ? 137  THR K CA  1 
ATOM   11967 C  C   . THR K  1 137 ? -0.733  83.910  108.871 1.00 8.05  ? 137  THR K C   1 
ATOM   11968 O  O   . THR K  1 137 ? -0.104  83.106  108.209 1.00 8.81  ? 137  THR K O   1 
ATOM   11969 C  CB  . THR K  1 137 ? 0.722   85.738  108.296 1.00 8.27  ? 137  THR K CB  1 
ATOM   11970 O  OG1 . THR K  1 137 ? 1.313   85.613  109.619 1.00 6.44  ? 137  THR K OG1 1 
ATOM   11971 C  CG2 . THR K  1 137 ? 0.911   87.215  107.915 1.00 10.06 ? 137  THR K CG2 1 
ATOM   11972 N  N   . GLY K  1 138 ? -1.328  83.583  110.028 1.00 5.00  ? 138  GLY K N   1 
ATOM   11973 C  CA  . GLY K  1 138 ? -1.228  82.243  110.593 1.00 5.60  ? 138  GLY K CA  1 
ATOM   11974 C  C   . GLY K  1 138 ? 0.178   81.878  111.076 1.00 5.00  ? 138  GLY K C   1 
ATOM   11975 O  O   . GLY K  1 138 ? 0.477   80.714  111.290 1.00 5.19  ? 138  GLY K O   1 
ATOM   11976 N  N   . ASN K  1 139 ? 1.053   82.860  111.233 1.00 5.00  ? 139  ASN K N   1 
ATOM   11977 C  CA  . ASN K  1 139 ? 2.444   82.586  111.652 1.00 5.18  ? 139  ASN K CA  1 
ATOM   11978 C  C   . ASN K  1 139 ? 3.193   81.670  110.708 1.00 5.08  ? 139  ASN K C   1 
ATOM   11979 O  O   . ASN K  1 139 ? 4.026   80.899  111.108 1.00 5.00  ? 139  ASN K O   1 
ATOM   11980 C  CB  . ASN K  1 139 ? 2.481   82.017  113.072 1.00 5.78  ? 139  ASN K CB  1 
ATOM   11981 C  CG  . ASN K  1 139 ? 2.297   83.095  114.105 1.00 11.80 ? 139  ASN K CG  1 
ATOM   11982 O  OD1 . ASN K  1 139 ? 3.141   83.968  114.245 1.00 11.49 ? 139  ASN K OD1 1 
ATOM   11983 N  ND2 . ASN K  1 139 ? 1.185   83.050  114.822 1.00 10.67 ? 139  ASN K ND2 1 
ATOM   11984 N  N   . ALA K  1 140 ? 2.885   81.773  109.419 1.00 5.00  ? 140  ALA K N   1 
ATOM   11985 C  CA  . ALA K  1 140 ? 3.471   80.851  108.495 1.00 5.67  ? 140  ALA K CA  1 
ATOM   11986 C  C   . ALA K  1 140 ? 4.886   81.203  108.088 1.00 5.13  ? 140  ALA K C   1 
ATOM   11987 O  O   . ALA K  1 140 ? 5.537   80.465  107.362 1.00 5.00  ? 140  ALA K O   1 
ATOM   11988 C  CB  . ALA K  1 140 ? 2.535   80.652  107.276 1.00 5.00  ? 140  ALA K CB  1 
ATOM   11989 N  N   . GLY K  1 141 ? 5.379   82.338  108.583 1.00 5.60  ? 141  GLY K N   1 
ATOM   11990 C  CA  . GLY K  1 141 ? 6.763   82.684  108.340 1.00 5.90  ? 141  GLY K CA  1 
ATOM   11991 C  C   . GLY K  1 141 ? 7.084   83.165  106.933 1.00 5.46  ? 141  GLY K C   1 
ATOM   11992 O  O   . GLY K  1 141 ? 6.206   83.660  106.201 1.00 5.00  ? 141  GLY K O   1 
ATOM   11993 N  N   . SER K  1 142 ? 8.334   82.971  106.524 1.00 5.24  ? 142  SER K N   1 
ATOM   11994 C  CA  . SER K  1 142 ? 8.774   83.595  105.286 1.00 5.62  ? 142  SER K CA  1 
ATOM   11995 C  C   . SER K  1 142 ? 8.128   83.027  104.034 1.00 5.58  ? 142  SER K C   1 
ATOM   11996 O  O   . SER K  1 142 ? 7.536   81.951  104.051 1.00 5.07  ? 142  SER K O   1 
ATOM   11997 C  CB  . SER K  1 142 ? 10.286  83.556  105.140 1.00 6.46  ? 142  SER K CB  1 
ATOM   11998 O  OG  . SER K  1 142 ? 10.728  82.241  104.859 1.00 9.26  ? 142  SER K OG  1 
ATOM   11999 N  N   . ARG K  1 143 ? 8.262   83.769  102.941 1.00 5.30  ? 143  ARG K N   1 
ATOM   12000 C  CA  . ARG K  1 143 ? 7.665   83.366  101.684 1.00 5.00  ? 143  ARG K CA  1 
ATOM   12001 C  C   . ARG K  1 143 ? 8.709   82.636  100.863 1.00 5.35  ? 143  ARG K C   1 
ATOM   12002 O  O   . ARG K  1 143 ? 9.664   83.263  100.337 1.00 5.40  ? 143  ARG K O   1 
ATOM   12003 C  CB  . ARG K  1 143 ? 7.207   84.636  100.976 1.00 5.00  ? 143  ARG K CB  1 
ATOM   12004 C  CG  . ARG K  1 143 ? 6.148   85.384  101.839 1.00 5.00  ? 143  ARG K CG  1 
ATOM   12005 C  CD  . ARG K  1 143 ? 5.690   86.754  101.209 1.00 5.00  ? 143  ARG K CD  1 
ATOM   12006 N  NE  . ARG K  1 143 ? 4.842   87.425  102.204 1.00 6.03  ? 143  ARG K NE  1 
ATOM   12007 C  CZ  . ARG K  1 143 ? 4.026   88.442  101.924 1.00 6.93  ? 143  ARG K CZ  1 
ATOM   12008 N  NH1 . ARG K  1 143 ? 3.958   88.902  100.672 1.00 6.47  ? 143  ARG K NH1 1 
ATOM   12009 N  NH2 . ARG K  1 143 ? 3.280   88.973  102.903 1.00 5.00  ? 143  ARG K NH2 1 
ATOM   12010 N  N   . LEU K  1 144 ? 8.584   81.318  100.786 1.00 5.00  ? 144  LEU K N   1 
ATOM   12011 C  CA  . LEU K  1 144 ? 9.647   80.567  100.139 1.00 5.00  ? 144  LEU K CA  1 
ATOM   12012 C  C   . LEU K  1 144 ? 9.610   80.668  98.619  1.00 5.00  ? 144  LEU K C   1 
ATOM   12013 O  O   . LEU K  1 144 ? 10.650  80.654  97.974  1.00 5.00  ? 144  LEU K O   1 
ATOM   12014 C  CB  . LEU K  1 144 ? 9.580   79.099  100.516 1.00 5.07  ? 144  LEU K CB  1 
ATOM   12015 C  CG  . LEU K  1 144 ? 9.831   78.862  102.011 1.00 8.04  ? 144  LEU K CG  1 
ATOM   12016 C  CD1 . LEU K  1 144 ? 9.860   77.347  102.222 1.00 12.70 ? 144  LEU K CD1 1 
ATOM   12017 C  CD2 . LEU K  1 144 ? 11.157  79.503  102.519 1.00 10.29 ? 144  LEU K CD2 1 
ATOM   12018 N  N   . ALA K  1 145 ? 8.415   80.670  98.043  1.00 5.00  ? 145  ALA K N   1 
ATOM   12019 C  CA  . ALA K  1 145 ? 8.299   80.780  96.576  1.00 5.00  ? 145  ALA K CA  1 
ATOM   12020 C  C   . ALA K  1 145 ? 6.940   81.358  96.256  1.00 5.00  ? 145  ALA K C   1 
ATOM   12021 O  O   . ALA K  1 145 ? 5.992   81.210  97.037  1.00 5.00  ? 145  ALA K O   1 
ATOM   12022 C  CB  . ALA K  1 145 ? 8.409   79.411  95.873  1.00 5.00  ? 145  ALA K CB  1 
ATOM   12023 N  N   . CYS K  1 146 ? 6.837   81.980  95.096  1.00 5.00  ? 146  CYS K N   1 
ATOM   12024 C  CA  . CYS K  1 146 ? 5.558   82.553  94.729  1.00 5.00  ? 146  CYS K CA  1 
ATOM   12025 C  C   . CYS K  1 146 ? 5.498   82.739  93.228  1.00 5.00  ? 146  CYS K C   1 
ATOM   12026 O  O   . CYS K  1 146 ? 6.498   82.608  92.537  1.00 5.00  ? 146  CYS K O   1 
ATOM   12027 C  CB  . CYS K  1 146 ? 5.322   83.934  95.376  1.00 5.01  ? 146  CYS K CB  1 
ATOM   12028 S  SG  . CYS K  1 146 ? 6.593   85.170  94.964  1.00 9.10  ? 146  CYS K SG  1 
ATOM   12029 N  N   . GLY K  1 147 ? 4.312   83.042  92.742  1.00 5.00  ? 147  GLY K N   1 
ATOM   12030 C  CA  . GLY K  1 147 ? 4.129   83.328  91.315  1.00 5.47  ? 147  GLY K CA  1 
ATOM   12031 C  C   . GLY K  1 147 ? 2.795   84.031  91.097  1.00 5.42  ? 147  GLY K C   1 
ATOM   12032 O  O   . GLY K  1 147 ? 1.918   83.961  91.927  1.00 5.00  ? 147  GLY K O   1 
ATOM   12033 N  N   . VAL K  1 148 ? 2.636   84.692  89.944  1.00 5.00  ? 148  VAL K N   1 
ATOM   12034 C  CA  . VAL K  1 148 ? 1.384   85.339  89.647  1.00 5.00  ? 148  VAL K CA  1 
ATOM   12035 C  C   . VAL K  1 148 ? 0.484   84.294  89.027  1.00 5.28  ? 148  VAL K C   1 
ATOM   12036 O  O   . VAL K  1 148 ? 0.951   83.485  88.213  1.00 5.77  ? 148  VAL K O   1 
ATOM   12037 C  CB  . VAL K  1 148 ? 1.617   86.507  88.658  1.00 5.00  ? 148  VAL K CB  1 
ATOM   12038 C  CG1 . VAL K  1 148 ? 0.290   87.165  88.317  1.00 5.00  ? 148  VAL K CG1 1 
ATOM   12039 C  CG2 . VAL K  1 148 ? 2.597   87.527  89.300  1.00 5.00  ? 148  VAL K CG2 1 
ATOM   12040 N  N   . ILE K  1 149 ? -0.782  84.298  89.410  1.00 5.00  ? 149  ILE K N   1 
ATOM   12041 C  CA  . ILE K  1 149 ? -1.758  83.334  88.881  1.00 5.09  ? 149  ILE K CA  1 
ATOM   12042 C  C   . ILE K  1 149 ? -2.215  83.795  87.519  1.00 5.00  ? 149  ILE K C   1 
ATOM   12043 O  O   . ILE K  1 149 ? -2.777  84.887  87.380  1.00 5.23  ? 149  ILE K O   1 
ATOM   12044 C  CB  . ILE K  1 149 ? -2.948  83.233  89.857  1.00 5.55  ? 149  ILE K CB  1 
ATOM   12045 C  CG1 . ILE K  1 149 ? -2.412  82.594  91.159  1.00 5.00  ? 149  ILE K CG1 1 
ATOM   12046 C  CG2 . ILE K  1 149 ? -3.984  82.240  89.334  1.00 5.00  ? 149  ILE K CG2 1 
ATOM   12047 C  CD1 . ILE K  1 149 ? -3.378  82.787  92.347  1.00 6.00  ? 149  ILE K CD1 1 
ATOM   12048 N  N   . GLY K  1 150 ? -1.980  82.961  86.512  1.00 5.00  ? 150  GLY K N   1 
ATOM   12049 C  CA  . GLY K  1 150 ? -2.220  83.394  85.128  1.00 5.00  ? 150  GLY K CA  1 
ATOM   12050 C  C   . GLY K  1 150 ? -3.265  82.538  84.407  1.00 5.00  ? 150  GLY K C   1 
ATOM   12051 O  O   . GLY K  1 150 ? -3.534  81.401  84.812  1.00 5.00  ? 150  GLY K O   1 
ATOM   12052 N  N   . ILE K  1 151 ? -3.871  83.099  83.366  1.00 5.00  ? 151  ILE K N   1 
ATOM   12053 C  CA  . ILE K  1 151 ? -4.864  82.353  82.589  1.00 5.12  ? 151  ILE K CA  1 
ATOM   12054 C  C   . ILE K  1 151 ? -4.182  81.244  81.806  1.00 5.52  ? 151  ILE K C   1 
ATOM   12055 O  O   . ILE K  1 151 ? -3.186  81.512  81.114  1.00 5.00  ? 151  ILE K O   1 
ATOM   12056 C  CB  . ILE K  1 151 ? -5.572  83.320  81.638  1.00 5.54  ? 151  ILE K CB  1 
ATOM   12057 C  CG1 . ILE K  1 151 ? -6.366  84.315  82.495  1.00 7.84  ? 151  ILE K CG1 1 
ATOM   12058 C  CG2 . ILE K  1 151 ? -6.527  82.533  80.663  1.00 6.96  ? 151  ILE K CG2 1 
ATOM   12059 C  CD1 . ILE K  1 151 ? -6.923  85.502  81.699  1.00 10.82 ? 151  ILE K CD1 1 
ATOM   12060 N  N   . ALA K  1 152 ? -4.742  80.015  81.868  1.00 5.48  ? 152  ALA K N   1 
ATOM   12061 C  CA  . ALA K  1 152 ? -4.129  78.848  81.250  1.00 7.08  ? 152  ALA K CA  1 
ATOM   12062 C  C   . ALA K  1 152 ? -4.994  78.408  80.063  1.00 8.67  ? 152  ALA K C   1 
ATOM   12063 O  O   . ALA K  1 152 ? -6.171  78.755  80.005  1.00 5.99  ? 152  ALA K O   1 
ATOM   12064 C  CB  . ALA K  1 152 ? -4.029  77.727  82.239  1.00 7.94  ? 152  ALA K CB  1 
ATOM   12065 N  N   . GLN K  1 153 ? -4.376  77.706  79.118  1.00 10.01 ? 153  GLN K N   1 
ATOM   12066 C  CA  . GLN K  1 153 ? -5.115  77.174  77.966  1.00 13.39 ? 153  GLN K CA  1 
ATOM   12067 C  C   . GLN K  1 153 ? -5.928  75.984  78.448  1.00 15.05 ? 153  GLN K C   1 
ATOM   12068 O  O   . GLN K  1 153 ? -5.377  75.064  79.094  1.00 15.08 ? 153  GLN K O   1 
ATOM   12069 C  CB  . GLN K  1 153 ? -4.157  76.749  76.869  1.00 12.59 ? 153  GLN K CB  1 
ATOM   12070 C  CG  . GLN K  1 153 ? -4.825  76.032  75.667  1.00 15.44 ? 153  GLN K CG  1 
ATOM   12071 C  CD  . GLN K  1 153 ? -3.824  75.744  74.574  1.00 18.29 ? 153  GLN K CD  1 
ATOM   12072 O  OE1 . GLN K  1 153 ? -2.885  74.976  74.783  1.00 20.24 ? 153  GLN K OE1 1 
ATOM   12073 N  NE2 . GLN K  1 153 ? -4.006  76.367  73.409  1.00 17.77 ? 153  GLN K NE2 1 
ATOM   12074 O  OXT . GLN K  1 153 ? -7.126  76.000  78.152  1.00 18.42 ? 153  GLN K OXT 1 
ATOM   12075 N  N   . THR L  1 2   ? 60.853  135.925 49.523  1.00 22.42 ? 2    THR L N   1 
ATOM   12076 C  CA  . THR L  1 2   ? 59.851  135.968 50.589  1.00 20.74 ? 2    THR L CA  1 
ATOM   12077 C  C   . THR L  1 2   ? 58.664  136.942 50.429  1.00 18.11 ? 2    THR L C   1 
ATOM   12078 O  O   . THR L  1 2   ? 58.792  138.121 50.098  1.00 16.32 ? 2    THR L O   1 
ATOM   12079 C  CB  . THR L  1 2   ? 60.528  136.237 51.957  1.00 22.12 ? 2    THR L CB  1 
ATOM   12080 O  OG1 . THR L  1 2   ? 61.847  135.683 51.953  1.00 25.04 ? 2    THR L OG1 1 
ATOM   12081 C  CG2 . THR L  1 2   ? 59.823  135.447 53.077  1.00 24.56 ? 2    THR L CG2 1 
ATOM   12082 N  N   . LYS L  1 3   ? 57.496  136.418 50.734  1.00 14.75 ? 3    LYS L N   1 
ATOM   12083 C  CA  . LYS L  1 3   ? 56.275  137.180 50.717  1.00 13.13 ? 3    LYS L CA  1 
ATOM   12084 C  C   . LYS L  1 3   ? 55.523  136.851 52.010  1.00 12.33 ? 3    LYS L C   1 
ATOM   12085 O  O   . LYS L  1 3   ? 55.631  135.738 52.539  1.00 13.48 ? 3    LYS L O   1 
ATOM   12086 C  CB  . LYS L  1 3   ? 55.417  136.811 49.515  1.00 13.25 ? 3    LYS L CB  1 
ATOM   12087 C  CG  . LYS L  1 3   ? 55.905  137.444 48.157  1.00 14.06 ? 3    LYS L CG  1 
ATOM   12088 N  N   . ALA L  1 4   ? 54.731  137.791 52.488  1.00 10.30 ? 4    ALA L N   1 
ATOM   12089 C  CA  . ALA L  1 4   ? 53.964  137.582 53.715  1.00 10.21 ? 4    ALA L CA  1 
ATOM   12090 C  C   . ALA L  1 4   ? 52.643  138.358 53.650  1.00 10.65 ? 4    ALA L C   1 
ATOM   12091 O  O   . ALA L  1 4   ? 52.477  139.244 52.809  1.00 11.38 ? 4    ALA L O   1 
ATOM   12092 C  CB  . ALA L  1 4   ? 54.800  138.004 54.959  1.00 9.00  ? 4    ALA L CB  1 
ATOM   12093 N  N   . VAL L  1 5   ? 51.714  138.039 54.544  1.00 10.20 ? 5    VAL L N   1 
ATOM   12094 C  CA  . VAL L  1 5   ? 50.409  138.673 54.532  1.00 10.15 ? 5    VAL L CA  1 
ATOM   12095 C  C   . VAL L  1 5   ? 49.807  138.697 55.928  1.00 10.07 ? 5    VAL L C   1 
ATOM   12096 O  O   . VAL L  1 5   ? 50.161  137.872 56.778  1.00 10.52 ? 5    VAL L O   1 
ATOM   12097 C  CB  . VAL L  1 5   ? 49.468  137.938 53.516  1.00 10.58 ? 5    VAL L CB  1 
ATOM   12098 C  CG1 . VAL L  1 5   ? 49.143  136.493 53.963  1.00 9.10  ? 5    VAL L CG1 1 
ATOM   12099 C  CG2 . VAL L  1 5   ? 48.211  138.742 53.250  1.00 11.56 ? 5    VAL L CG2 1 
ATOM   12100 N  N   . CYS L  1 6   ? 48.902  139.637 56.165  1.00 9.71  ? 6    CYS L N   1 
ATOM   12101 C  CA  . CYS L  1 6   ? 48.299  139.783 57.478  1.00 10.77 ? 6    CYS L CA  1 
ATOM   12102 C  C   . CYS L  1 6   ? 46.853  140.228 57.310  1.00 10.53 ? 6    CYS L C   1 
ATOM   12103 O  O   . CYS L  1 6   ? 46.577  141.220 56.598  1.00 12.74 ? 6    CYS L O   1 
ATOM   12104 C  CB  . CYS L  1 6   ? 49.093  140.824 58.283  1.00 10.34 ? 6    CYS L CB  1 
ATOM   12105 S  SG  . CYS L  1 6   ? 48.460  141.006 59.972  1.00 12.15 ? 6    CYS L SG  1 
ATOM   12106 N  N   . VAL L  1 7   ? 45.940  139.495 57.940  1.00 10.24 ? 7    VAL L N   1 
ATOM   12107 C  CA  . VAL L  1 7   ? 44.545  139.889 58.003  1.00 9.84  ? 7    VAL L CA  1 
ATOM   12108 C  C   . VAL L  1 7   ? 44.265  140.530 59.373  1.00 9.90  ? 7    VAL L C   1 
ATOM   12109 O  O   . VAL L  1 7   ? 44.391  139.872 60.403  1.00 7.37  ? 7    VAL L O   1 
ATOM   12110 C  CB  . VAL L  1 7   ? 43.623  138.696 57.779  1.00 10.15 ? 7    VAL L CB  1 
ATOM   12111 C  CG1 . VAL L  1 7   ? 42.144  139.115 57.914  1.00 9.60  ? 7    VAL L CG1 1 
ATOM   12112 C  CG2 . VAL L  1 7   ? 43.923  138.098 56.424  1.00 10.41 ? 7    VAL L CG2 1 
ATOM   12113 N  N   . LEU L  1 8   ? 43.913  141.822 59.365  1.00 10.53 ? 8    LEU L N   1 
ATOM   12114 C  CA  . LEU L  1 8   ? 43.673  142.607 60.584  1.00 12.26 ? 8    LEU L CA  1 
ATOM   12115 C  C   . LEU L  1 8   ? 42.180  142.554 60.944  1.00 11.79 ? 8    LEU L C   1 
ATOM   12116 O  O   . LEU L  1 8   ? 41.327  142.831 60.101  1.00 12.26 ? 8    LEU L O   1 
ATOM   12117 C  CB  . LEU L  1 8   ? 44.065  144.087 60.335  1.00 11.97 ? 8    LEU L CB  1 
ATOM   12118 C  CG  . LEU L  1 8   ? 45.550  144.496 60.131  1.00 16.42 ? 8    LEU L CG  1 
ATOM   12119 C  CD1 . LEU L  1 8   ? 46.186  143.818 58.939  1.00 17.89 ? 8    LEU L CD1 1 
ATOM   12120 C  CD2 . LEU L  1 8   ? 45.683  146.024 59.913  1.00 20.38 ? 8    LEU L CD2 1 
ATOM   12121 N  N   . LYS L  1 9   ? 41.860  142.131 62.154  1.00 11.67 ? 9    LYS L N   1 
ATOM   12122 C  CA  . LYS L  1 9   ? 40.485  142.137 62.631  1.00 12.86 ? 9    LYS L CA  1 
ATOM   12123 C  C   . LYS L  1 9   ? 40.508  142.511 64.092  1.00 12.26 ? 9    LYS L C   1 
ATOM   12124 O  O   . LYS L  1 9   ? 41.555  142.414 64.752  1.00 10.83 ? 9    LYS L O   1 
ATOM   12125 C  CB  . LYS L  1 9   ? 39.810  140.746 62.506  1.00 13.12 ? 9    LYS L CB  1 
ATOM   12126 C  CG  . LYS L  1 9   ? 39.855  140.132 61.133  1.00 18.09 ? 9    LYS L CG  1 
ATOM   12127 C  CD  . LYS L  1 9   ? 39.118  138.764 61.107  1.00 22.33 ? 9    LYS L CD  1 
ATOM   12128 C  CE  . LYS L  1 9   ? 38.455  138.544 59.731  1.00 24.04 ? 9    LYS L CE  1 
ATOM   12129 N  N   . GLY L  1 10  ? 39.361  142.943 64.594  1.00 12.11 ? 10   GLY L N   1 
ATOM   12130 C  CA  . GLY L  1 10  ? 39.255  143.296 65.997  1.00 13.04 ? 10   GLY L CA  1 
ATOM   12131 C  C   . GLY L  1 10  ? 37.865  143.017 66.501  1.00 14.39 ? 10   GLY L C   1 
ATOM   12132 O  O   . GLY L  1 10  ? 37.128  142.227 65.903  1.00 13.27 ? 10   GLY L O   1 
ATOM   12133 N  N   . ASP L  1 11  ? 37.496  143.660 67.603  1.00 14.46 ? 11   ASP L N   1 
ATOM   12134 C  CA  . ASP L  1 11  ? 36.156  143.428 68.165  1.00 16.27 ? 11   ASP L CA  1 
ATOM   12135 C  C   . ASP L  1 11  ? 35.196  144.478 67.640  1.00 14.59 ? 11   ASP L C   1 
ATOM   12136 O  O   . ASP L  1 11  ? 34.030  144.446 67.990  1.00 14.99 ? 11   ASP L O   1 
ATOM   12137 C  CB  . ASP L  1 11  ? 36.150  143.579 69.680  1.00 17.10 ? 11   ASP L CB  1 
ATOM   12138 C  CG  . ASP L  1 11  ? 36.883  142.465 70.398  1.00 22.05 ? 11   ASP L CG  1 
ATOM   12139 O  OD1 . ASP L  1 11  ? 36.769  141.275 70.008  1.00 24.04 ? 11   ASP L OD1 1 
ATOM   12140 O  OD2 . ASP L  1 11  ? 37.588  142.720 71.398  1.00 26.83 ? 11   ASP L OD2 1 
ATOM   12141 N  N   . GLY L  1 12  ? 35.714  145.435 66.868  1.00 13.79 ? 12   GLY L N   1 
ATOM   12142 C  CA  . GLY L  1 12  ? 34.931  146.537 66.308  1.00 12.25 ? 12   GLY L CA  1 
ATOM   12143 C  C   . GLY L  1 12  ? 34.846  146.449 64.787  1.00 12.17 ? 12   GLY L C   1 
ATOM   12144 O  O   . GLY L  1 12  ? 34.903  145.356 64.235  1.00 11.67 ? 12   GLY L O   1 
ATOM   12145 N  N   . PRO L  1 13  ? 34.672  147.579 64.105  1.00 11.93 ? 13   PRO L N   1 
ATOM   12146 C  CA  . PRO L  1 13  ? 34.533  147.594 62.643  1.00 11.37 ? 13   PRO L CA  1 
ATOM   12147 C  C   . PRO L  1 13  ? 35.826  147.588 61.846  1.00 12.04 ? 13   PRO L C   1 
ATOM   12148 O  O   . PRO L  1 13  ? 35.771  147.544 60.617  1.00 10.22 ? 13   PRO L O   1 
ATOM   12149 C  CB  . PRO L  1 13  ? 33.823  148.936 62.409  1.00 11.52 ? 13   PRO L CB  1 
ATOM   12150 C  CG  . PRO L  1 13  ? 34.534  149.828 63.414  1.00 12.30 ? 13   PRO L CG  1 
ATOM   12151 C  CD  . PRO L  1 13  ? 34.498  148.939 64.675  1.00 12.48 ? 13   PRO L CD  1 
ATOM   12152 N  N   . VAL L  1 14  ? 36.988  147.653 62.500  1.00 11.66 ? 14   VAL L N   1 
ATOM   12153 C  CA  . VAL L  1 14  ? 38.204  147.803 61.714  1.00 12.81 ? 14   VAL L CA  1 
ATOM   12154 C  C   . VAL L  1 14  ? 38.667  146.499 61.090  1.00 14.10 ? 14   VAL L C   1 
ATOM   12155 O  O   . VAL L  1 14  ? 38.812  145.481 61.787  1.00 13.85 ? 14   VAL L O   1 
ATOM   12156 C  CB  . VAL L  1 14  ? 39.338  148.446 62.559  1.00 13.02 ? 14   VAL L CB  1 
ATOM   12157 C  CG1 . VAL L  1 14  ? 40.655  148.507 61.762  1.00 12.77 ? 14   VAL L CG1 1 
ATOM   12158 C  CG2 . VAL L  1 14  ? 38.896  149.862 63.021  1.00 12.95 ? 14   VAL L CG2 1 
ATOM   12159 N  N   . GLN L  1 15  ? 38.878  146.506 59.774  1.00 14.33 ? 15   GLN L N   1 
ATOM   12160 C  CA  . GLN L  1 15  ? 39.378  145.297 59.122  1.00 15.17 ? 15   GLN L CA  1 
ATOM   12161 C  C   . GLN L  1 15  ? 40.287  145.657 57.965  1.00 14.76 ? 15   GLN L C   1 
ATOM   12162 O  O   . GLN L  1 15  ? 40.098  146.682 57.306  1.00 14.92 ? 15   GLN L O   1 
ATOM   12163 C  CB  . GLN L  1 15  ? 38.204  144.400 58.659  1.00 16.19 ? 15   GLN L CB  1 
ATOM   12164 C  CG  . GLN L  1 15  ? 37.117  145.219 58.058  1.00 17.51 ? 15   GLN L CG  1 
ATOM   12165 N  N   . GLY L  1 16  ? 41.267  144.801 57.703  1.00 14.79 ? 16   GLY L N   1 
ATOM   12166 C  CA  . GLY L  1 16  ? 42.157  145.049 56.593  1.00 13.80 ? 16   GLY L CA  1 
ATOM   12167 C  C   . GLY L  1 16  ? 42.994  143.863 56.214  1.00 12.85 ? 16   GLY L C   1 
ATOM   12168 O  O   . GLY L  1 16  ? 42.961  142.794 56.860  1.00 11.63 ? 16   GLY L O   1 
ATOM   12169 N  N   . ILE L  1 17  ? 43.708  144.036 55.112  1.00 11.78 ? 17   ILE L N   1 
ATOM   12170 C  CA  . ILE L  1 17  ? 44.620  143.040 54.637  1.00 12.28 ? 17   ILE L CA  1 
ATOM   12171 C  C   . ILE L  1 17  ? 45.875  143.794 54.257  1.00 12.20 ? 17   ILE L C   1 
ATOM   12172 O  O   . ILE L  1 17  ? 45.804  144.798 53.517  1.00 13.15 ? 17   ILE L O   1 
ATOM   12173 C  CB  . ILE L  1 17  ? 44.035  142.335 53.386  1.00 13.13 ? 17   ILE L CB  1 
ATOM   12174 C  CG1 . ILE L  1 17  ? 42.810  141.483 53.768  1.00 13.78 ? 17   ILE L CG1 1 
ATOM   12175 C  CG2 . ILE L  1 17  ? 45.129  141.500 52.715  1.00 12.20 ? 17   ILE L CG2 1 
ATOM   12176 C  CD1 . ILE L  1 17  ? 42.099  140.824 52.580  1.00 18.17 ? 17   ILE L CD1 1 
ATOM   12177 N  N   . ILE L  1 18  ? 47.031  143.323 54.728  1.00 11.42 ? 18   ILE L N   1 
ATOM   12178 C  CA  . ILE L  1 18  ? 48.294  143.995 54.431  1.00 11.80 ? 18   ILE L CA  1 
ATOM   12179 C  C   . ILE L  1 18  ? 49.251  142.974 53.914  1.00 11.59 ? 18   ILE L C   1 
ATOM   12180 O  O   . ILE L  1 18  ? 49.421  141.933 54.536  1.00 10.87 ? 18   ILE L O   1 
ATOM   12181 C  CB  . ILE L  1 18  ? 48.912  144.643 55.700  1.00 11.54 ? 18   ILE L CB  1 
ATOM   12182 C  CG1 . ILE L  1 18  ? 47.996  145.710 56.251  1.00 10.83 ? 18   ILE L CG1 1 
ATOM   12183 C  CG2 . ILE L  1 18  ? 50.325  145.286 55.404  1.00 12.55 ? 18   ILE L CG2 1 
ATOM   12184 C  CD1 . ILE L  1 18  ? 47.918  146.975 55.359  1.00 9.39  ? 18   ILE L CD1 1 
ATOM   12185 N  N   . ASN L  1 19  ? 49.885  143.298 52.788  1.00 12.08 ? 19   ASN L N   1 
ATOM   12186 C  CA  . ASN L  1 19  ? 50.827  142.405 52.126  1.00 12.34 ? 19   ASN L CA  1 
ATOM   12187 C  C   . ASN L  1 19  ? 52.233  142.883 52.316  1.00 11.85 ? 19   ASN L C   1 
ATOM   12188 O  O   . ASN L  1 19  ? 52.463  144.094 52.393  1.00 11.95 ? 19   ASN L O   1 
ATOM   12189 C  CB  . ASN L  1 19  ? 50.530  142.394 50.620  1.00 12.76 ? 19   ASN L CB  1 
ATOM   12190 C  CG  . ASN L  1 19  ? 49.077  142.122 50.343  1.00 14.24 ? 19   ASN L CG  1 
ATOM   12191 O  OD1 . ASN L  1 19  ? 48.267  143.040 50.210  1.00 18.52 ? 19   ASN L OD1 1 
ATOM   12192 N  ND2 . ASN L  1 19  ? 48.730  140.870 50.318  1.00 9.47  ? 19   ASN L ND2 1 
ATOM   12193 N  N   . PHE L  1 20  ? 53.167  141.943 52.427  1.00 11.70 ? 20   PHE L N   1 
ATOM   12194 C  CA  . PHE L  1 20  ? 54.590  142.272 52.510  1.00 12.34 ? 20   PHE L CA  1 
ATOM   12195 C  C   . PHE L  1 20  ? 55.357  141.559 51.389  1.00 12.61 ? 20   PHE L C   1 
ATOM   12196 O  O   . PHE L  1 20  ? 55.013  140.437 51.033  1.00 12.48 ? 20   PHE L O   1 
ATOM   12197 C  CB  . PHE L  1 20  ? 55.202  141.806 53.844  1.00 11.85 ? 20   PHE L CB  1 
ATOM   12198 C  CG  . PHE L  1 20  ? 54.497  142.330 55.052  1.00 11.83 ? 20   PHE L CG  1 
ATOM   12199 C  CD1 . PHE L  1 20  ? 53.290  141.786 55.446  1.00 11.62 ? 20   PHE L CD1 1 
ATOM   12200 C  CD2 . PHE L  1 20  ? 55.038  143.362 55.779  1.00 12.45 ? 20   PHE L CD2 1 
ATOM   12201 C  CE1 . PHE L  1 20  ? 52.645  142.256 56.577  1.00 13.49 ? 20   PHE L CE1 1 
ATOM   12202 C  CE2 . PHE L  1 20  ? 54.390  143.841 56.896  1.00 14.00 ? 20   PHE L CE2 1 
ATOM   12203 C  CZ  . PHE L  1 20  ? 53.197  143.280 57.294  1.00 12.86 ? 20   PHE L CZ  1 
ATOM   12204 N  N   . GLU L  1 21  ? 56.415  142.195 50.886  1.00 12.94 ? 21   GLU L N   1 
ATOM   12205 C  CA  . GLU L  1 21  ? 57.269  141.607 49.849  1.00 15.00 ? 21   GLU L CA  1 
ATOM   12206 C  C   . GLU L  1 21  ? 58.699  142.058 50.018  1.00 14.93 ? 21   GLU L C   1 
ATOM   12207 O  O   . GLU L  1 21  ? 58.969  143.242 50.190  1.00 14.88 ? 21   GLU L O   1 
ATOM   12208 C  CB  . GLU L  1 21  ? 56.781  141.931 48.423  1.00 15.73 ? 21   GLU L CB  1 
ATOM   12209 C  CG  . GLU L  1 21  ? 57.334  140.944 47.393  1.00 19.26 ? 21   GLU L CG  1 
ATOM   12210 C  CD  . GLU L  1 21  ? 56.876  141.219 45.968  1.00 26.32 ? 21   GLU L CD  1 
ATOM   12211 O  OE1 . GLU L  1 21  ? 56.415  142.340 45.671  1.00 31.27 ? 21   GLU L OE1 1 
ATOM   12212 O  OE2 . GLU L  1 21  ? 56.996  140.314 45.129  1.00 29.09 ? 21   GLU L OE2 1 
ATOM   12213 N  N   . GLN L  1 22  ? 59.615  141.101 49.988  1.00 15.63 ? 22   GLN L N   1 
ATOM   12214 C  CA  . GLN L  1 22  ? 61.032  141.397 50.106  1.00 17.02 ? 22   GLN L CA  1 
ATOM   12215 C  C   . GLN L  1 22  ? 61.795  140.621 49.024  1.00 18.22 ? 22   GLN L C   1 
ATOM   12216 O  O   . GLN L  1 22  ? 61.870  139.402 49.054  1.00 18.15 ? 22   GLN L O   1 
ATOM   12217 C  CB  . GLN L  1 22  ? 61.536  141.035 51.502  1.00 16.96 ? 22   GLN L CB  1 
ATOM   12218 C  CG  . GLN L  1 22  ? 62.941  141.514 51.786  1.00 16.30 ? 22   GLN L CG  1 
ATOM   12219 C  CD  . GLN L  1 22  ? 63.426  141.139 53.176  1.00 15.85 ? 22   GLN L CD  1 
ATOM   12220 O  OE1 . GLN L  1 22  ? 63.037  140.104 53.725  1.00 17.26 ? 22   GLN L OE1 1 
ATOM   12221 N  NE2 . GLN L  1 22  ? 64.286  141.968 53.737  1.00 13.71 ? 22   GLN L NE2 1 
ATOM   12222 N  N   . LYS L  1 23  ? 62.336  141.345 48.058  1.00 19.78 ? 23   LYS L N   1 
ATOM   12223 C  CA  . LYS L  1 23  ? 63.038  140.725 46.935  1.00 21.98 ? 23   LYS L CA  1 
ATOM   12224 C  C   . LYS L  1 23  ? 64.403  140.127 47.279  1.00 22.28 ? 23   LYS L C   1 
ATOM   12225 O  O   . LYS L  1 23  ? 64.773  139.054 46.771  1.00 21.85 ? 23   LYS L O   1 
ATOM   12226 C  CB  . LYS L  1 23  ? 63.149  141.730 45.792  1.00 22.11 ? 23   LYS L CB  1 
ATOM   12227 C  CG  . LYS L  1 23  ? 61.781  142.168 45.269  1.00 26.04 ? 23   LYS L CG  1 
ATOM   12228 C  CD  . LYS L  1 23  ? 61.875  142.870 43.919  1.00 31.78 ? 23   LYS L CD  1 
ATOM   12229 C  CE  . LYS L  1 23  ? 60.637  143.723 43.614  1.00 33.60 ? 23   LYS L CE  1 
ATOM   12230 N  NZ  . LYS L  1 23  ? 60.778  145.142 44.086  1.00 35.38 ? 23   LYS L NZ  1 
ATOM   12231 N  N   . GLU L  1 24  ? 65.147  140.810 48.137  1.00 23.15 ? 24   GLU L N   1 
ATOM   12232 C  CA  . GLU L  1 24  ? 66.476  140.346 48.524  1.00 25.29 ? 24   GLU L CA  1 
ATOM   12233 C  C   . GLU L  1 24  ? 66.614  140.239 50.027  1.00 25.25 ? 24   GLU L C   1 
ATOM   12234 O  O   . GLU L  1 24  ? 65.984  140.978 50.777  1.00 24.83 ? 24   GLU L O   1 
ATOM   12235 C  CB  . GLU L  1 24  ? 67.582  141.316 48.073  1.00 25.59 ? 24   GLU L CB  1 
ATOM   12236 C  CG  . GLU L  1 24  ? 67.294  142.237 46.905  1.00 30.18 ? 24   GLU L CG  1 
ATOM   12237 C  CD  . GLU L  1 24  ? 68.547  143.011 46.494  1.00 35.36 ? 24   GLU L CD  1 
ATOM   12238 O  OE1 . GLU L  1 24  ? 69.496  143.083 47.315  1.00 36.70 ? 24   GLU L OE1 1 
ATOM   12239 O  OE2 . GLU L  1 24  ? 68.602  143.543 45.356  1.00 38.85 ? 24   GLU L OE2 1 
ATOM   12240 N  N   . SER L  1 25  ? 67.488  139.337 50.452  1.00 25.88 ? 25   SER L N   1 
ATOM   12241 C  CA  . SER L  1 25  ? 67.790  139.171 51.859  1.00 26.24 ? 25   SER L CA  1 
ATOM   12242 C  C   . SER L  1 25  ? 68.242  140.510 52.436  1.00 26.02 ? 25   SER L C   1 
ATOM   12243 O  O   . SER L  1 25  ? 69.130  141.164 51.891  1.00 25.87 ? 25   SER L O   1 
ATOM   12244 C  CB  . SER L  1 25  ? 68.891  138.122 52.015  1.00 26.74 ? 25   SER L CB  1 
ATOM   12245 O  OG  . SER L  1 25  ? 69.421  138.128 53.328  1.00 28.94 ? 25   SER L OG  1 
ATOM   12246 N  N   . ASN L  1 26  ? 67.612  140.926 53.526  1.00 25.79 ? 26   ASN L N   1 
ATOM   12247 C  CA  . ASN L  1 26  ? 67.990  142.168 54.201  1.00 25.52 ? 26   ASN L CA  1 
ATOM   12248 C  C   . ASN L  1 26  ? 67.721  143.406 53.352  1.00 23.90 ? 26   ASN L C   1 
ATOM   12249 O  O   . ASN L  1 26  ? 68.183  144.494 53.659  1.00 24.31 ? 26   ASN L O   1 
ATOM   12250 C  CB  . ASN L  1 26  ? 69.474  142.107 54.595  1.00 26.84 ? 26   ASN L CB  1 
ATOM   12251 C  CG  . ASN L  1 26  ? 69.807  142.997 55.776  1.00 29.25 ? 26   ASN L CG  1 
ATOM   12252 O  OD1 . ASN L  1 26  ? 69.053  143.916 56.122  1.00 33.51 ? 26   ASN L OD1 1 
ATOM   12253 N  ND2 . ASN L  1 26  ? 70.948  142.726 56.411  1.00 32.32 ? 26   ASN L ND2 1 
ATOM   12254 N  N   . GLY L  1 27  ? 66.982  143.234 52.268  1.00 22.31 ? 27   GLY L N   1 
ATOM   12255 C  CA  . GLY L  1 27  ? 66.631  144.347 51.413  1.00 20.02 ? 27   GLY L CA  1 
ATOM   12256 C  C   . GLY L  1 27  ? 65.310  144.946 51.852  1.00 18.79 ? 27   GLY L C   1 
ATOM   12257 O  O   . GLY L  1 27  ? 64.693  144.464 52.792  1.00 18.20 ? 27   GLY L O   1 
ATOM   12258 N  N   . PRO L  1 28  ? 64.857  145.971 51.142  1.00 17.36 ? 28   PRO L N   1 
ATOM   12259 C  CA  . PRO L  1 28  ? 63.627  146.687 51.492  1.00 16.10 ? 28   PRO L CA  1 
ATOM   12260 C  C   . PRO L  1 28  ? 62.389  145.819 51.425  1.00 15.07 ? 28   PRO L C   1 
ATOM   12261 O  O   . PRO L  1 28  ? 62.260  144.927 50.564  1.00 13.45 ? 28   PRO L O   1 
ATOM   12262 C  CB  . PRO L  1 28  ? 63.519  147.771 50.419  1.00 16.69 ? 28   PRO L CB  1 
ATOM   12263 C  CG  . PRO L  1 28  ? 64.858  147.842 49.770  1.00 17.28 ? 28   PRO L CG  1 
ATOM   12264 C  CD  . PRO L  1 28  ? 65.506  146.508 49.935  1.00 17.88 ? 28   PRO L CD  1 
ATOM   12265 N  N   . VAL L  1 29  ? 61.459  146.089 52.336  1.00 13.35 ? 29   VAL L N   1 
ATOM   12266 C  CA  . VAL L  1 29  ? 60.213  145.350 52.365  1.00 13.32 ? 29   VAL L CA  1 
ATOM   12267 C  C   . VAL L  1 29  ? 59.117  146.296 51.936  1.00 13.10 ? 29   VAL L C   1 
ATOM   12268 O  O   . VAL L  1 29  ? 58.940  147.375 52.511  1.00 12.85 ? 29   VAL L O   1 
ATOM   12269 C  CB  . VAL L  1 29  ? 59.892  144.807 53.772  1.00 12.41 ? 29   VAL L CB  1 
ATOM   12270 C  CG1 . VAL L  1 29  ? 58.581  144.044 53.761  1.00 13.74 ? 29   VAL L CG1 1 
ATOM   12271 C  CG2 . VAL L  1 29  ? 61.030  143.901 54.262  1.00 12.50 ? 29   VAL L CG2 1 
ATOM   12272 N  N   . LYS L  1 30  ? 58.399  145.905 50.903  1.00 13.19 ? 30   LYS L N   1 
ATOM   12273 C  CA  . LYS L  1 30  ? 57.278  146.691 50.456  1.00 13.71 ? 30   LYS L CA  1 
ATOM   12274 C  C   . LYS L  1 30  ? 56.110  146.222 51.296  1.00 13.62 ? 30   LYS L C   1 
ATOM   12275 O  O   . LYS L  1 30  ? 55.921  145.015 51.509  1.00 12.56 ? 30   LYS L O   1 
ATOM   12276 C  CB  . LYS L  1 30  ? 57.015  146.471 48.958  1.00 14.50 ? 30   LYS L CB  1 
ATOM   12277 C  CG  . LYS L  1 30  ? 57.963  147.303 48.089  1.00 18.76 ? 30   LYS L CG  1 
ATOM   12278 C  CD  . LYS L  1 30  ? 57.994  146.901 46.590  1.00 27.22 ? 30   LYS L CD  1 
ATOM   12279 C  CE  . LYS L  1 30  ? 57.010  147.714 45.735  1.00 30.75 ? 30   LYS L CE  1 
ATOM   12280 N  NZ  . LYS L  1 30  ? 57.160  147.486 44.241  1.00 33.57 ? 30   LYS L NZ  1 
ATOM   12281 N  N   . VAL L  1 31  ? 55.348  147.177 51.796  1.00 13.15 ? 31   VAL L N   1 
ATOM   12282 C  CA  . VAL L  1 31  ? 54.169  146.833 52.569  1.00 14.22 ? 31   VAL L CA  1 
ATOM   12283 C  C   . VAL L  1 31  ? 52.997  147.601 52.026  1.00 14.13 ? 31   VAL L C   1 
ATOM   12284 O  O   . VAL L  1 31  ? 53.043  148.814 51.878  1.00 13.95 ? 31   VAL L O   1 
ATOM   12285 C  CB  . VAL L  1 31  ? 54.370  146.838 54.144  1.00 15.51 ? 31   VAL L CB  1 
ATOM   12286 C  CG1 . VAL L  1 31  ? 55.777  147.171 54.595  1.00 14.23 ? 31   VAL L CG1 1 
ATOM   12287 C  CG2 . VAL L  1 31  ? 53.219  147.472 54.938  1.00 16.91 ? 31   VAL L CG2 1 
ATOM   12288 N  N   . TRP L  1 32  ? 51.965  146.876 51.633  1.00 13.56 ? 32   TRP L N   1 
ATOM   12289 C  CA  . TRP L  1 32  ? 50.851  147.556 51.011  1.00 14.60 ? 32   TRP L CA  1 
ATOM   12290 C  C   . TRP L  1 32  ? 49.542  146.818 51.208  1.00 13.95 ? 32   TRP L C   1 
ATOM   12291 O  O   . TRP L  1 32  ? 49.512  145.603 51.403  1.00 13.84 ? 32   TRP L O   1 
ATOM   12292 C  CB  . TRP L  1 32  ? 51.132  147.716 49.520  1.00 15.53 ? 32   TRP L CB  1 
ATOM   12293 C  CG  . TRP L  1 32  ? 50.858  146.492 48.770  1.00 17.62 ? 32   TRP L CG  1 
ATOM   12294 C  CD1 . TRP L  1 32  ? 49.683  146.158 48.144  1.00 19.68 ? 32   TRP L CD1 1 
ATOM   12295 C  CD2 . TRP L  1 32  ? 51.748  145.393 48.556  1.00 19.99 ? 32   TRP L CD2 1 
ATOM   12296 N  NE1 . TRP L  1 32  ? 49.800  144.931 47.546  1.00 20.12 ? 32   TRP L NE1 1 
ATOM   12297 C  CE2 . TRP L  1 32  ? 51.058  144.440 47.780  1.00 20.17 ? 32   TRP L CE2 1 
ATOM   12298 C  CE3 . TRP L  1 32  ? 53.069  145.123 48.927  1.00 21.72 ? 32   TRP L CE3 1 
ATOM   12299 C  CZ2 . TRP L  1 32  ? 51.636  143.241 47.377  1.00 21.99 ? 32   TRP L CZ2 1 
ATOM   12300 C  CZ3 . TRP L  1 32  ? 53.636  143.925 48.539  1.00 21.51 ? 32   TRP L CZ3 1 
ATOM   12301 C  CH2 . TRP L  1 32  ? 52.927  143.005 47.767  1.00 23.08 ? 32   TRP L CH2 1 
ATOM   12302 N  N   . GLY L  1 33  ? 48.446  147.557 51.142  1.00 12.99 ? 33   GLY L N   1 
ATOM   12303 C  CA  . GLY L  1 33  ? 47.153  146.952 51.358  1.00 13.16 ? 33   GLY L CA  1 
ATOM   12304 C  C   . GLY L  1 33  ? 46.137  147.996 51.748  1.00 13.77 ? 33   GLY L C   1 
ATOM   12305 O  O   . GLY L  1 33  ? 46.314  149.198 51.467  1.00 12.83 ? 33   GLY L O   1 
ATOM   12306 N  N   . SER L  1 34  ? 45.080  147.561 52.420  1.00 13.92 ? 34   SER L N   1 
ATOM   12307 C  CA  . SER L  1 34  ? 44.029  148.496 52.787  1.00 14.93 ? 34   SER L CA  1 
ATOM   12308 C  C   . SER L  1 34  ? 43.429  148.143 54.128  1.00 13.95 ? 34   SER L C   1 
ATOM   12309 O  O   . SER L  1 34  ? 43.278  146.977 54.435  1.00 13.92 ? 34   SER L O   1 
ATOM   12310 C  CB  . SER L  1 34  ? 42.914  148.432 51.721  1.00 15.74 ? 34   SER L CB  1 
ATOM   12311 O  OG  . SER L  1 34  ? 42.079  149.580 51.832  1.00 20.79 ? 34   SER L OG  1 
ATOM   12312 N  N   . ILE L  1 35  ? 43.015  149.155 54.881  1.00 13.81 ? 35   ILE L N   1 
ATOM   12313 C  CA  . ILE L  1 35  ? 42.332  148.943 56.152  1.00 13.69 ? 35   ILE L CA  1 
ATOM   12314 C  C   . ILE L  1 35  ? 41.085  149.820 56.124  1.00 14.12 ? 35   ILE L C   1 
ATOM   12315 O  O   . ILE L  1 35  ? 41.161  151.010 55.774  1.00 13.47 ? 35   ILE L O   1 
ATOM   12316 C  CB  . ILE L  1 35  ? 43.217  149.372 57.328  1.00 14.06 ? 35   ILE L CB  1 
ATOM   12317 C  CG1 . ILE L  1 35  ? 44.554  148.634 57.322  1.00 12.38 ? 35   ILE L CG1 1 
ATOM   12318 C  CG2 . ILE L  1 35  ? 42.521  149.098 58.647  1.00 14.02 ? 35   ILE L CG2 1 
ATOM   12319 C  CD1 . ILE L  1 35  ? 45.535  149.206 58.406  1.00 14.67 ? 35   ILE L CD1 1 
ATOM   12320 N  N   . LYS L  1 36  ? 39.945  149.246 56.496  1.00 13.85 ? 36   LYS L N   1 
ATOM   12321 C  CA  . LYS L  1 36  ? 38.697  149.993 56.497  1.00 14.37 ? 36   LYS L CA  1 
ATOM   12322 C  C   . LYS L  1 36  ? 38.095  150.017 57.893  1.00 14.27 ? 36   LYS L C   1 
ATOM   12323 O  O   . LYS L  1 36  ? 38.543  149.286 58.775  1.00 13.66 ? 36   LYS L O   1 
ATOM   12324 C  CB  . LYS L  1 36  ? 37.703  149.388 55.496  1.00 15.33 ? 36   LYS L CB  1 
ATOM   12325 C  CG  . LYS L  1 36  ? 36.903  148.190 56.009  1.00 17.07 ? 36   LYS L CG  1 
ATOM   12326 C  CD  . LYS L  1 36  ? 36.065  147.544 54.883  1.00 23.48 ? 36   LYS L CD  1 
ATOM   12327 C  CE  . LYS L  1 36  ? 34.724  148.256 54.677  1.00 25.74 ? 36   LYS L CE  1 
ATOM   12328 N  NZ  . LYS L  1 36  ? 33.839  147.598 53.635  1.00 28.90 ? 36   LYS L NZ  1 
ATOM   12329 N  N   . GLY L  1 37  ? 37.074  150.858 58.081  1.00 13.70 ? 37   GLY L N   1 
ATOM   12330 C  CA  . GLY L  1 37  ? 36.363  150.949 59.343  1.00 13.13 ? 37   GLY L CA  1 
ATOM   12331 C  C   . GLY L  1 37  ? 37.029  151.873 60.355  1.00 13.36 ? 37   GLY L C   1 
ATOM   12332 O  O   . GLY L  1 37  ? 36.689  151.815 61.543  1.00 13.34 ? 37   GLY L O   1 
ATOM   12333 N  N   . LEU L  1 38  ? 37.950  152.722 59.885  1.00 13.40 ? 38   LEU L N   1 
ATOM   12334 C  CA  . LEU L  1 38  ? 38.727  153.634 60.740  1.00 13.96 ? 38   LEU L CA  1 
ATOM   12335 C  C   . LEU L  1 38  ? 38.163  155.050 60.733  1.00 14.54 ? 38   LEU L C   1 
ATOM   12336 O  O   . LEU L  1 38  ? 37.544  155.454 59.755  1.00 15.27 ? 38   LEU L O   1 
ATOM   12337 C  CB  . LEU L  1 38  ? 40.167  153.750 60.217  1.00 14.31 ? 38   LEU L CB  1 
ATOM   12338 C  CG  . LEU L  1 38  ? 41.150  152.575 60.324  1.00 16.29 ? 38   LEU L CG  1 
ATOM   12339 C  CD1 . LEU L  1 38  ? 42.324  152.789 59.371  1.00 16.66 ? 38   LEU L CD1 1 
ATOM   12340 C  CD2 . LEU L  1 38  ? 41.646  152.447 61.767  1.00 14.76 ? 38   LEU L CD2 1 
ATOM   12341 N  N   . THR L  1 39  ? 38.369  155.784 61.823  1.00 14.20 ? 39   THR L N   1 
ATOM   12342 C  CA  . THR L  1 39  ? 38.000  157.199 61.865  1.00 14.75 ? 39   THR L CA  1 
ATOM   12343 C  C   . THR L  1 39  ? 38.957  157.977 60.990  1.00 14.80 ? 39   THR L C   1 
ATOM   12344 O  O   . THR L  1 39  ? 40.124  157.620 60.874  1.00 14.58 ? 39   THR L O   1 
ATOM   12345 C  CB  . THR L  1 39  ? 38.042  157.762 63.275  1.00 14.33 ? 39   THR L CB  1 
ATOM   12346 O  OG1 . THR L  1 39  ? 39.342  157.557 63.862  1.00 15.91 ? 39   THR L OG1 1 
ATOM   12347 C  CG2 . THR L  1 39  ? 37.090  157.029 64.184  1.00 15.75 ? 39   THR L CG2 1 
ATOM   12348 N  N   . GLU L  1 40  ? 38.467  159.053 60.377  1.00 14.10 ? 40   GLU L N   1 
ATOM   12349 C  CA  . GLU L  1 40  ? 39.310  159.835 59.484  1.00 14.23 ? 40   GLU L CA  1 
ATOM   12350 C  C   . GLU L  1 40  ? 40.538  160.319 60.232  1.00 14.37 ? 40   GLU L C   1 
ATOM   12351 O  O   . GLU L  1 40  ? 40.452  160.707 61.402  1.00 14.99 ? 40   GLU L O   1 
ATOM   12352 C  CB  . GLU L  1 40  ? 38.516  161.014 58.901  1.00 14.77 ? 40   GLU L CB  1 
ATOM   12353 C  CG  . GLU L  1 40  ? 39.329  161.962 58.033  1.00 15.64 ? 40   GLU L CG  1 
ATOM   12354 C  CD  . GLU L  1 40  ? 38.433  162.979 57.320  1.00 18.20 ? 40   GLU L CD  1 
ATOM   12355 O  OE1 . GLU L  1 40  ? 37.245  163.116 57.715  1.00 16.74 ? 40   GLU L OE1 1 
ATOM   12356 O  OE2 . GLU L  1 40  ? 38.917  163.628 56.368  1.00 18.52 ? 40   GLU L OE2 1 
ATOM   12357 N  N   . GLY L  1 41  ? 41.694  160.296 59.583  1.00 13.92 ? 41   GLY L N   1 
ATOM   12358 C  CA  . GLY L  1 41  ? 42.887  160.771 60.264  1.00 13.94 ? 41   GLY L CA  1 
ATOM   12359 C  C   . GLY L  1 41  ? 43.967  159.702 60.439  1.00 13.95 ? 41   GLY L C   1 
ATOM   12360 O  O   . GLY L  1 41  ? 43.905  158.647 59.800  1.00 13.74 ? 41   GLY L O   1 
ATOM   12361 N  N   . LEU L  1 42  ? 44.941  159.993 61.299  1.00 13.30 ? 42   LEU L N   1 
ATOM   12362 C  CA  . LEU L  1 42  ? 46.124  159.141 61.482  1.00 14.16 ? 42   LEU L CA  1 
ATOM   12363 C  C   . LEU L  1 42  ? 45.917  158.056 62.516  1.00 13.78 ? 42   LEU L C   1 
ATOM   12364 O  O   . LEU L  1 42  ? 45.287  158.288 63.554  1.00 13.63 ? 42   LEU L O   1 
ATOM   12365 C  CB  . LEU L  1 42  ? 47.309  159.995 61.932  1.00 14.79 ? 42   LEU L CB  1 
ATOM   12366 C  CG  . LEU L  1 42  ? 47.773  161.079 60.957  1.00 16.85 ? 42   LEU L CG  1 
ATOM   12367 C  CD1 . LEU L  1 42  ? 48.641  162.125 61.652  1.00 16.07 ? 42   LEU L CD1 1 
ATOM   12368 C  CD2 . LEU L  1 42  ? 48.523  160.475 59.818  1.00 18.22 ? 42   LEU L CD2 1 
ATOM   12369 N  N   . HIS L  1 43  ? 46.521  156.898 62.255  1.00 12.36 ? 43   HIS L N   1 
ATOM   12370 C  CA  . HIS L  1 43  ? 46.422  155.766 63.151  1.00 11.84 ? 43   HIS L CA  1 
ATOM   12371 C  C   . HIS L  1 43  ? 47.751  155.070 63.234  1.00 10.64 ? 43   HIS L C   1 
ATOM   12372 O  O   . HIS L  1 43  ? 48.322  154.702 62.212  1.00 10.55 ? 43   HIS L O   1 
ATOM   12373 C  CB  . HIS L  1 43  ? 45.375  154.785 62.612  1.00 10.91 ? 43   HIS L CB  1 
ATOM   12374 C  CG  . HIS L  1 43  ? 43.990  155.328 62.695  1.00 10.58 ? 43   HIS L CG  1 
ATOM   12375 N  ND1 . HIS L  1 43  ? 43.249  155.288 63.852  1.00 12.38 ? 43   HIS L ND1 1 
ATOM   12376 C  CD2 . HIS L  1 43  ? 43.231  155.970 61.782  1.00 12.57 ? 43   HIS L CD2 1 
ATOM   12377 C  CE1 . HIS L  1 43  ? 42.074  155.854 63.638  1.00 13.30 ? 43   HIS L CE1 1 
ATOM   12378 N  NE2 . HIS L  1 43  ? 42.034  156.265 62.385  1.00 13.71 ? 43   HIS L NE2 1 
ATOM   12379 N  N   . GLY L  1 44  ? 48.248  154.902 64.450  1.00 10.60 ? 44   GLY L N   1 
ATOM   12380 C  CA  . GLY L  1 44  ? 49.530  154.226 64.640  1.00 10.73 ? 44   GLY L CA  1 
ATOM   12381 C  C   . GLY L  1 44  ? 49.513  152.838 64.011  1.00 11.39 ? 44   GLY L C   1 
ATOM   12382 O  O   . GLY L  1 44  ? 48.483  152.163 64.036  1.00 9.93  ? 44   GLY L O   1 
ATOM   12383 N  N   . PHE L  1 45  ? 50.665  152.392 63.512  1.00 10.49 ? 45   PHE L N   1 
ATOM   12384 C  CA  . PHE L  1 45  ? 50.749  151.141 62.723  1.00 10.05 ? 45   PHE L CA  1 
ATOM   12385 C  C   . PHE L  1 45  ? 52.065  150.482 63.098  1.00 9.37  ? 45   PHE L C   1 
ATOM   12386 O  O   . PHE L  1 45  ? 53.122  151.004 62.754  1.00 9.62  ? 45   PHE L O   1 
ATOM   12387 C  CB  . PHE L  1 45  ? 50.817  151.578 61.272  1.00 10.47 ? 45   PHE L CB  1 
ATOM   12388 C  CG  . PHE L  1 45  ? 50.628  150.482 60.252  1.00 10.75 ? 45   PHE L CG  1 
ATOM   12389 C  CD1 . PHE L  1 45  ? 49.607  149.558 60.359  1.00 11.85 ? 45   PHE L CD1 1 
ATOM   12390 C  CD2 . PHE L  1 45  ? 51.466  150.417 59.163  1.00 8.80  ? 45   PHE L CD2 1 
ATOM   12391 C  CE1 . PHE L  1 45  ? 49.452  148.556 59.380  1.00 14.89 ? 45   PHE L CE1 1 
ATOM   12392 C  CE2 . PHE L  1 45  ? 51.304  149.430 58.180  1.00 10.29 ? 45   PHE L CE2 1 
ATOM   12393 C  CZ  . PHE L  1 45  ? 50.292  148.510 58.298  1.00 13.27 ? 45   PHE L CZ  1 
ATOM   12394 N  N   . HIS L  1 46  ? 52.026  149.368 63.825  1.00 9.15  ? 46   HIS L N   1 
ATOM   12395 C  CA  . HIS L  1 46  ? 53.266  148.764 64.317  1.00 8.29  ? 46   HIS L CA  1 
ATOM   12396 C  C   . HIS L  1 46  ? 53.288  147.255 64.230  1.00 8.19  ? 46   HIS L C   1 
ATOM   12397 O  O   . HIS L  1 46  ? 52.226  146.581 64.305  1.00 7.99  ? 46   HIS L O   1 
ATOM   12398 C  CB  . HIS L  1 46  ? 53.473  149.066 65.800  1.00 7.95  ? 46   HIS L CB  1 
ATOM   12399 C  CG  . HIS L  1 46  ? 53.185  150.487 66.180  1.00 7.82  ? 46   HIS L CG  1 
ATOM   12400 N  ND1 . HIS L  1 46  ? 52.265  150.833 67.142  1.00 10.00 ? 46   HIS L ND1 1 
ATOM   12401 C  CD2 . HIS L  1 46  ? 53.688  151.644 65.712  1.00 10.28 ? 46   HIS L CD2 1 
ATOM   12402 C  CE1 . HIS L  1 46  ? 52.232  152.141 67.271  1.00 10.86 ? 46   HIS L CE1 1 
ATOM   12403 N  NE2 . HIS L  1 46  ? 53.088  152.656 66.413  1.00 9.97  ? 46   HIS L NE2 1 
ATOM   12404 N  N   . VAL L  1 47  ? 54.504  146.714 64.172  1.00 7.48  ? 47   VAL L N   1 
ATOM   12405 C  CA  . VAL L  1 47  ? 54.675  145.280 64.388  1.00 8.16  ? 47   VAL L CA  1 
ATOM   12406 C  C   . VAL L  1 47  ? 54.980  145.086 65.885  1.00 8.61  ? 47   VAL L C   1 
ATOM   12407 O  O   . VAL L  1 47  ? 55.943  145.667 66.419  1.00 8.55  ? 47   VAL L O   1 
ATOM   12408 C  CB  . VAL L  1 47  ? 55.820  144.704 63.607  1.00 7.63  ? 47   VAL L CB  1 
ATOM   12409 C  CG1 . VAL L  1 47  ? 55.923  143.227 63.939  1.00 7.74  ? 47   VAL L CG1 1 
ATOM   12410 C  CG2 . VAL L  1 47  ? 55.591  144.928 62.070  1.00 8.48  ? 47   VAL L CG2 1 
ATOM   12411 N  N   . HIS L  1 48  ? 54.117  144.330 66.558  1.00 8.84  ? 48   HIS L N   1 
ATOM   12412 C  CA  . HIS L  1 48  ? 54.282  143.988 67.961  1.00 9.02  ? 48   HIS L CA  1 
ATOM   12413 C  C   . HIS L  1 48  ? 54.954  142.632 68.074  1.00 9.47  ? 48   HIS L C   1 
ATOM   12414 O  O   . HIS L  1 48  ? 54.919  141.838 67.134  1.00 10.76 ? 48   HIS L O   1 
ATOM   12415 C  CB  . HIS L  1 48  ? 52.957  144.013 68.719  1.00 7.18  ? 48   HIS L CB  1 
ATOM   12416 C  CG  . HIS L  1 48  ? 52.429  145.406 68.953  1.00 8.36  ? 48   HIS L CG  1 
ATOM   12417 N  ND1 . HIS L  1 48  ? 52.142  145.903 70.203  1.00 8.42  ? 48   HIS L ND1 1 
ATOM   12418 C  CD2 . HIS L  1 48  ? 52.131  146.391 68.080  1.00 9.35  ? 48   HIS L CD2 1 
ATOM   12419 C  CE1 . HIS L  1 48  ? 51.723  147.161 70.094  1.00 7.37  ? 48   HIS L CE1 1 
ATOM   12420 N  NE2 . HIS L  1 48  ? 51.675  147.460 68.810  1.00 9.20  ? 48   HIS L NE2 1 
ATOM   12421 N  N   . GLU L  1 49  ? 55.523  142.369 69.249  1.00 9.19  ? 49   GLU L N   1 
ATOM   12422 C  CA  . GLU L  1 49  ? 56.465  141.269 69.406  1.00 8.72  ? 49   GLU L CA  1 
ATOM   12423 C  C   . GLU L  1 49  ? 55.912  139.869 69.197  1.00 9.06  ? 49   GLU L C   1 
ATOM   12424 O  O   . GLU L  1 49  ? 56.529  139.087 68.503  1.00 8.35  ? 49   GLU L O   1 
ATOM   12425 C  CB  . GLU L  1 49  ? 57.141  141.347 70.778  1.00 9.45  ? 49   GLU L CB  1 
ATOM   12426 C  CG  . GLU L  1 49  ? 58.204  140.288 70.967  1.00 8.82  ? 49   GLU L CG  1 
ATOM   12427 C  CD  . GLU L  1 49  ? 58.968  140.453 72.264  1.00 13.67 ? 49   GLU L CD  1 
ATOM   12428 O  OE1 . GLU L  1 49  ? 58.617  141.349 73.066  1.00 10.95 ? 49   GLU L OE1 1 
ATOM   12429 O  OE2 . GLU L  1 49  ? 59.920  139.677 72.478  1.00 13.08 ? 49   GLU L OE2 1 
ATOM   12430 N  N   . PHE L  1 50  ? 54.760  139.574 69.791  1.00 7.87  ? 50   PHE L N   1 
ATOM   12431 C  CA  . PHE L  1 50  ? 54.231  138.195 69.775  1.00 7.95  ? 50   PHE L CA  1 
ATOM   12432 C  C   . PHE L  1 50  ? 53.078  138.034 68.810  1.00 8.45  ? 50   PHE L C   1 
ATOM   12433 O  O   . PHE L  1 50  ? 52.221  138.938 68.700  1.00 8.32  ? 50   PHE L O   1 
ATOM   12434 C  CB  . PHE L  1 50  ? 53.799  137.781 71.180  1.00 7.12  ? 50   PHE L CB  1 
ATOM   12435 C  CG  . PHE L  1 50  ? 54.871  138.041 72.242  1.00 9.72  ? 50   PHE L CG  1 
ATOM   12436 C  CD1 . PHE L  1 50  ? 56.096  137.429 72.154  1.00 10.66 ? 50   PHE L CD1 1 
ATOM   12437 C  CD2 . PHE L  1 50  ? 54.643  138.953 73.286  1.00 11.74 ? 50   PHE L CD2 1 
ATOM   12438 C  CE1 . PHE L  1 50  ? 57.123  137.689 73.115  1.00 14.55 ? 50   PHE L CE1 1 
ATOM   12439 C  CE2 . PHE L  1 50  ? 55.648  139.228 74.235  1.00 12.00 ? 50   PHE L CE2 1 
ATOM   12440 C  CZ  . PHE L  1 50  ? 56.882  138.597 74.156  1.00 11.09 ? 50   PHE L CZ  1 
ATOM   12441 N  N   . GLY L  1 51  ? 53.051  136.880 68.131  1.00 7.72  ? 51   GLY L N   1 
ATOM   12442 C  CA  . GLY L  1 51  ? 51.960  136.531 67.217  1.00 8.48  ? 51   GLY L CA  1 
ATOM   12443 C  C   . GLY L  1 51  ? 50.946  135.734 68.028  1.00 8.76  ? 51   GLY L C   1 
ATOM   12444 O  O   . GLY L  1 51  ? 50.569  134.593 67.704  1.00 8.52  ? 51   GLY L O   1 
ATOM   12445 N  N   . ASP L  1 52  ? 50.599  136.321 69.178  1.00 9.08  ? 52   ASP L N   1 
ATOM   12446 C  CA  . ASP L  1 52  ? 49.713  135.709 70.174  1.00 9.72  ? 52   ASP L CA  1 
ATOM   12447 C  C   . ASP L  1 52  ? 48.392  136.502 70.272  1.00 10.00 ? 52   ASP L C   1 
ATOM   12448 O  O   . ASP L  1 52  ? 48.343  137.654 70.770  1.00 10.79 ? 52   ASP L O   1 
ATOM   12449 C  CB  . ASP L  1 52  ? 50.463  135.665 71.528  1.00 9.27  ? 52   ASP L CB  1 
ATOM   12450 C  CG  . ASP L  1 52  ? 49.679  134.969 72.621  1.00 10.46 ? 52   ASP L CG  1 
ATOM   12451 O  OD1 . ASP L  1 52  ? 48.434  134.877 72.512  1.00 10.08 ? 52   ASP L OD1 1 
ATOM   12452 O  OD2 . ASP L  1 52  ? 50.237  134.447 73.629  1.00 11.48 ? 52   ASP L OD2 1 
ATOM   12453 N  N   . ASN L  1 53  ? 47.341  135.895 69.760  1.00 10.45 ? 53   ASN L N   1 
ATOM   12454 C  CA  . ASN L  1 53  ? 46.011  136.518 69.731  1.00 11.76 ? 53   ASN L CA  1 
ATOM   12455 C  C   . ASN L  1 53  ? 45.063  135.906 70.761  1.00 10.05 ? 53   ASN L C   1 
ATOM   12456 O  O   . ASN L  1 53  ? 43.858  136.084 70.660  1.00 10.35 ? 53   ASN L O   1 
ATOM   12457 C  CB  . ASN L  1 53  ? 45.394  136.376 68.320  1.00 12.40 ? 53   ASN L CB  1 
ATOM   12458 C  CG  . ASN L  1 53  ? 44.156  137.280 68.119  1.00 19.98 ? 53   ASN L CG  1 
ATOM   12459 O  OD1 . ASN L  1 53  ? 43.116  136.847 67.591  1.00 26.04 ? 53   ASN L OD1 1 
ATOM   12460 N  ND2 . ASN L  1 53  ? 44.269  138.528 68.530  1.00 22.20 ? 53   ASN L ND2 1 
ATOM   12461 N  N   . THR L  1 54  ? 45.596  135.140 71.709  1.00 9.91  ? 54   THR L N   1 
ATOM   12462 C  CA  . THR L  1 54  ? 44.762  134.456 72.681  1.00 10.49 ? 54   THR L CA  1 
ATOM   12463 C  C   . THR L  1 54  ? 43.933  135.395 73.561  1.00 11.93 ? 54   THR L C   1 
ATOM   12464 O  O   . THR L  1 54  ? 42.852  135.025 73.975  1.00 13.53 ? 54   THR L O   1 
ATOM   12465 C  CB  . THR L  1 54  ? 45.565  133.500 73.585  1.00 10.04 ? 54   THR L CB  1 
ATOM   12466 O  OG1 . THR L  1 54  ? 46.559  134.257 74.326  1.00 9.75  ? 54   THR L OG1 1 
ATOM   12467 C  CG2 . THR L  1 54  ? 46.306  132.429 72.742  1.00 9.98  ? 54   THR L CG2 1 
ATOM   12468 N  N   . ALA L  1 55  ? 44.426  136.581 73.874  1.00 12.27 ? 55   ALA L N   1 
ATOM   12469 C  CA  . ALA L  1 55  ? 43.590  137.541 74.605  1.00 13.88 ? 55   ALA L CA  1 
ATOM   12470 C  C   . ALA L  1 55  ? 43.317  138.739 73.707  1.00 14.62 ? 55   ALA L C   1 
ATOM   12471 O  O   . ALA L  1 55  ? 43.411  139.900 74.123  1.00 16.10 ? 55   ALA L O   1 
ATOM   12472 C  CB  . ALA L  1 55  ? 44.270  137.982 75.933  1.00 14.00 ? 55   ALA L CB  1 
ATOM   12473 N  N   . GLY L  1 56  ? 43.026  138.481 72.446  1.00 14.43 ? 56   GLY L N   1 
ATOM   12474 C  CA  . GLY L  1 56  ? 42.855  139.576 71.508  1.00 14.69 ? 56   GLY L CA  1 
ATOM   12475 C  C   . GLY L  1 56  ? 44.182  140.298 71.206  1.00 14.83 ? 56   GLY L C   1 
ATOM   12476 O  O   . GLY L  1 56  ? 45.273  139.715 71.306  1.00 15.24 ? 56   GLY L O   1 
ATOM   12477 N  N   . CYS L  1 57  ? 44.099  141.577 70.873  1.00 13.02 ? 57   CYS L N   1 
ATOM   12478 C  CA  . CYS L  1 57  ? 45.294  142.301 70.456  1.00 14.29 ? 57   CYS L CA  1 
ATOM   12479 C  C   . CYS L  1 57  ? 46.253  142.564 71.609  1.00 13.18 ? 57   CYS L C   1 
ATOM   12480 O  O   . CYS L  1 57  ? 47.420  142.823 71.404  1.00 11.76 ? 57   CYS L O   1 
ATOM   12481 C  CB  . CYS L  1 57  ? 44.905  143.600 69.769  1.00 14.21 ? 57   CYS L CB  1 
ATOM   12482 S  SG  . CYS L  1 57  ? 44.125  143.257 68.177  1.00 20.27 ? 57   CYS L SG  1 
ATOM   12483 N  N   . THR L  1 58  ? 45.735  142.468 72.826  1.00 12.95 ? 58   THR L N   1 
ATOM   12484 C  CA  . THR L  1 58  ? 46.550  142.722 74.002  1.00 13.31 ? 58   THR L CA  1 
ATOM   12485 C  C   . THR L  1 58  ? 47.693  141.720 74.153  1.00 12.42 ? 58   THR L C   1 
ATOM   12486 O  O   . THR L  1 58  ? 48.776  142.058 74.613  1.00 10.38 ? 58   THR L O   1 
ATOM   12487 C  CB  . THR L  1 58  ? 45.654  142.599 75.213  1.00 13.02 ? 58   THR L CB  1 
ATOM   12488 O  OG1 . THR L  1 58  ? 44.638  143.600 75.115  1.00 17.56 ? 58   THR L OG1 1 
ATOM   12489 C  CG2 . THR L  1 58  ? 46.426  142.943 76.523  1.00 15.73 ? 58   THR L CG2 1 
ATOM   12490 N  N   . SER L  1 59  ? 47.445  140.470 73.778  1.00 9.97  ? 59   SER L N   1 
ATOM   12491 C  CA  . SER L  1 59  ? 48.471  139.463 73.960  1.00 9.81  ? 59   SER L CA  1 
ATOM   12492 C  C   . SER L  1 59  ? 49.618  139.549 72.946  1.00 8.64  ? 59   SER L C   1 
ATOM   12493 O  O   . SER L  1 59  ? 50.571  138.779 73.062  1.00 8.75  ? 59   SER L O   1 
ATOM   12494 C  CB  . SER L  1 59  ? 47.858  138.058 74.041  1.00 9.93  ? 59   SER L CB  1 
ATOM   12495 O  OG  . SER L  1 59  ? 46.891  137.909 73.036  1.00 12.33 ? 59   SER L OG  1 
ATOM   12496 N  N   . ALA L  1 60  ? 49.539  140.498 71.997  1.00 7.76  ? 60   ALA L N   1 
ATOM   12497 C  CA  . ALA L  1 60  ? 50.647  140.715 71.050  1.00 8.83  ? 60   ALA L CA  1 
ATOM   12498 C  C   . ALA L  1 60  ? 51.882  141.354 71.730  1.00 8.95  ? 60   ALA L C   1 
ATOM   12499 O  O   . ALA L  1 60  ? 52.975  141.437 71.145  1.00 8.08  ? 60   ALA L O   1 
ATOM   12500 C  CB  . ALA L  1 60  ? 50.193  141.569 69.912  1.00 9.70  ? 60   ALA L CB  1 
ATOM   12501 N  N   . GLY L  1 61  ? 51.690  141.858 72.940  1.00 9.34  ? 61   GLY L N   1 
ATOM   12502 C  CA  . GLY L  1 61  ? 52.819  142.433 73.652  1.00 9.30  ? 61   GLY L CA  1 
ATOM   12503 C  C   . GLY L  1 61  ? 53.204  143.812 73.131  1.00 8.13  ? 61   GLY L C   1 
ATOM   12504 O  O   . GLY L  1 61  ? 52.437  144.480 72.464  1.00 7.18  ? 61   GLY L O   1 
ATOM   12505 N  N   . PRO L  1 62  ? 54.415  144.240 73.470  1.00 8.50  ? 62   PRO L N   1 
ATOM   12506 C  CA  . PRO L  1 62  ? 54.884  145.568 73.111  1.00 8.73  ? 62   PRO L CA  1 
ATOM   12507 C  C   . PRO L  1 62  ? 55.440  145.610 71.695  1.00 8.91  ? 62   PRO L C   1 
ATOM   12508 O  O   . PRO L  1 62  ? 55.378  144.603 70.982  1.00 7.84  ? 62   PRO L O   1 
ATOM   12509 C  CB  . PRO L  1 62  ? 55.980  145.824 74.162  1.00 9.11  ? 62   PRO L CB  1 
ATOM   12510 C  CG  . PRO L  1 62  ? 56.654  144.427 74.282  1.00 9.14  ? 62   PRO L CG  1 
ATOM   12511 C  CD  . PRO L  1 62  ? 55.457  143.453 74.169  1.00 7.93  ? 62   PRO L CD  1 
ATOM   12512 N  N   . HIS L  1 63  ? 55.963  146.757 71.276  1.00 8.91  ? 63   HIS L N   1 
ATOM   12513 C  CA  . HIS L  1 63  ? 56.511  146.824 69.922  1.00 9.02  ? 63   HIS L CA  1 
ATOM   12514 C  C   . HIS L  1 63  ? 57.705  145.892 69.772  1.00 9.14  ? 63   HIS L C   1 
ATOM   12515 O  O   . HIS L  1 63  ? 58.476  145.699 70.711  1.00 9.68  ? 63   HIS L O   1 
ATOM   12516 C  CB  . HIS L  1 63  ? 56.925  148.261 69.568  1.00 8.79  ? 63   HIS L CB  1 
ATOM   12517 C  CG  . HIS L  1 63  ? 55.787  149.229 69.568  1.00 9.40  ? 63   HIS L CG  1 
ATOM   12518 N  ND1 . HIS L  1 63  ? 55.938  150.569 69.287  1.00 9.22  ? 63   HIS L ND1 1 
ATOM   12519 C  CD2 . HIS L  1 63  ? 54.460  149.032 69.762  1.00 12.99 ? 63   HIS L CD2 1 
ATOM   12520 C  CE1 . HIS L  1 63  ? 54.760  151.154 69.330  1.00 10.37 ? 63   HIS L CE1 1 
ATOM   12521 N  NE2 . HIS L  1 63  ? 53.857  150.252 69.661  1.00 17.18 ? 63   HIS L NE2 1 
ATOM   12522 N  N   . PHE L  1 64  ? 57.833  145.301 68.590  1.00 8.49  ? 64   PHE L N   1 
ATOM   12523 C  CA  . PHE L  1 64  ? 58.973  144.436 68.264  1.00 8.74  ? 64   PHE L CA  1 
ATOM   12524 C  C   . PHE L  1 64  ? 60.245  145.296 68.323  1.00 8.98  ? 64   PHE L C   1 
ATOM   12525 O  O   . PHE L  1 64  ? 60.393  146.258 67.556  1.00 8.79  ? 64   PHE L O   1 
ATOM   12526 C  CB  . PHE L  1 64  ? 58.771  143.848 66.877  1.00 8.67  ? 64   PHE L CB  1 
ATOM   12527 C  CG  . PHE L  1 64  ? 59.888  142.927 66.443  1.00 9.46  ? 64   PHE L CG  1 
ATOM   12528 C  CD1 . PHE L  1 64  ? 60.416  142.002 67.329  1.00 12.28 ? 64   PHE L CD1 1 
ATOM   12529 C  CD2 . PHE L  1 64  ? 60.400  142.999 65.153  1.00 11.78 ? 64   PHE L CD2 1 
ATOM   12530 C  CE1 . PHE L  1 64  ? 61.441  141.122 66.927  1.00 12.60 ? 64   PHE L CE1 1 
ATOM   12531 C  CE2 . PHE L  1 64  ? 61.427  142.140 64.739  1.00 11.62 ? 64   PHE L CE2 1 
ATOM   12532 C  CZ  . PHE L  1 64  ? 61.952  141.206 65.644  1.00 12.82 ? 64   PHE L CZ  1 
ATOM   12533 N  N   . ASN L  1 65  ? 61.143  144.950 69.244  1.00 8.28  ? 65   ASN L N   1 
ATOM   12534 C  CA  . ASN L  1 65  ? 62.292  145.828 69.536  1.00 10.04 ? 65   ASN L CA  1 
ATOM   12535 C  C   . ASN L  1 65  ? 63.527  145.040 69.941  1.00 10.08 ? 65   ASN L C   1 
ATOM   12536 O  O   . ASN L  1 65  ? 64.036  145.210 71.065  1.00 10.77 ? 65   ASN L O   1 
ATOM   12537 C  CB  . ASN L  1 65  ? 61.896  146.751 70.685  1.00 8.93  ? 65   ASN L CB  1 
ATOM   12538 C  CG  . ASN L  1 65  ? 62.939  147.867 70.981  1.00 11.05 ? 65   ASN L CG  1 
ATOM   12539 O  OD1 . ASN L  1 65  ? 63.715  148.280 70.116  1.00 13.11 ? 65   ASN L OD1 1 
ATOM   12540 N  ND2 . ASN L  1 65  ? 62.909  148.372 72.199  1.00 10.30 ? 65   ASN L ND2 1 
ATOM   12541 N  N   . PRO L  1 66  ? 64.030  144.222 69.028  1.00 11.57 ? 66   PRO L N   1 
ATOM   12542 C  CA  . PRO L  1 66  ? 65.167  143.339 69.317  1.00 11.91 ? 66   PRO L CA  1 
ATOM   12543 C  C   . PRO L  1 66  ? 66.454  144.130 69.568  1.00 12.56 ? 66   PRO L C   1 
ATOM   12544 O  O   . PRO L  1 66  ? 67.401  143.574 70.138  1.00 12.85 ? 66   PRO L O   1 
ATOM   12545 C  CB  . PRO L  1 66  ? 65.281  142.502 68.036  1.00 11.93 ? 66   PRO L CB  1 
ATOM   12546 C  CG  . PRO L  1 66  ? 64.765  143.462 66.960  1.00 11.62 ? 66   PRO L CG  1 
ATOM   12547 C  CD  . PRO L  1 66  ? 63.576  144.105 67.625  1.00 11.71 ? 66   PRO L CD  1 
ATOM   12548 N  N   . LEU L  1 67  ? 66.507  145.396 69.157  1.00 13.47 ? 67   LEU L N   1 
ATOM   12549 C  CA  . LEU L  1 67  ? 67.712  146.210 69.443  1.00 14.66 ? 67   LEU L CA  1 
ATOM   12550 C  C   . LEU L  1 67  ? 67.606  147.113 70.671  1.00 15.10 ? 67   LEU L C   1 
ATOM   12551 O  O   . LEU L  1 67  ? 68.492  147.950 70.935  1.00 14.75 ? 67   LEU L O   1 
ATOM   12552 C  CB  . LEU L  1 67  ? 68.137  147.026 68.224  1.00 15.52 ? 67   LEU L CB  1 
ATOM   12553 C  CG  . LEU L  1 67  ? 68.372  146.132 67.018  1.00 17.78 ? 67   LEU L CG  1 
ATOM   12554 C  CD1 . LEU L  1 67  ? 68.758  146.991 65.857  1.00 19.70 ? 67   LEU L CD1 1 
ATOM   12555 C  CD2 . LEU L  1 67  ? 69.451  145.157 67.353  1.00 22.00 ? 67   LEU L CD2 1 
ATOM   12556 N  N   . SER L  1 68  ? 66.536  146.928 71.435  1.00 14.42 ? 68   SER L N   1 
ATOM   12557 C  CA  . SER L  1 68  ? 66.328  147.661 72.671  1.00 14.26 ? 68   SER L CA  1 
ATOM   12558 C  C   . SER L  1 68  ? 66.488  149.161 72.500  1.00 13.56 ? 68   SER L C   1 
ATOM   12559 O  O   . SER L  1 68  ? 67.192  149.799 73.284  1.00 13.55 ? 68   SER L O   1 
ATOM   12560 C  CB  . SER L  1 68  ? 67.284  147.170 73.776  1.00 15.03 ? 68   SER L CB  1 
ATOM   12561 O  OG  . SER L  1 68  ? 66.992  145.827 74.149  1.00 16.03 ? 68   SER L OG  1 
ATOM   12562 N  N   . ARG L  1 69  ? 65.840  149.729 71.493  1.00 13.22 ? 69   ARG L N   1 
ATOM   12563 C  CA  . ARG L  1 69  ? 65.861  151.166 71.280  1.00 12.20 ? 69   ARG L CA  1 
ATOM   12564 C  C   . ARG L  1 69  ? 64.582  151.815 71.770  1.00 12.08 ? 69   ARG L C   1 
ATOM   12565 O  O   . ARG L  1 69  ? 63.662  151.127 72.190  1.00 10.32 ? 69   ARG L O   1 
ATOM   12566 C  CB  . ARG L  1 69  ? 66.055  151.475 69.796  1.00 13.02 ? 69   ARG L CB  1 
ATOM   12567 C  CG  . ARG L  1 69  ? 67.330  150.825 69.248  1.00 17.65 ? 69   ARG L CG  1 
ATOM   12568 C  CD  . ARG L  1 69  ? 68.095  151.645 68.257  1.00 24.68 ? 69   ARG L CD  1 
ATOM   12569 N  NE  . ARG L  1 69  ? 68.920  150.802 67.391  1.00 30.43 ? 69   ARG L NE  1 
ATOM   12570 C  CZ  . ARG L  1 69  ? 70.203  151.008 67.154  1.00 33.00 ? 69   ARG L CZ  1 
ATOM   12571 N  NH1 . ARG L  1 69  ? 70.835  152.029 67.735  1.00 37.75 ? 69   ARG L NH1 1 
ATOM   12572 N  NH2 . ARG L  1 69  ? 70.868  150.190 66.347  1.00 34.58 ? 69   ARG L NH2 1 
ATOM   12573 N  N   . LYS L  1 70  ? 64.549  153.150 71.755  1.00 10.68 ? 70   LYS L N   1 
ATOM   12574 C  CA  . LYS L  1 70  ? 63.321  153.856 72.107  1.00 10.32 ? 70   LYS L CA  1 
ATOM   12575 C  C   . LYS L  1 70  ? 62.420  153.958 70.908  1.00 9.81  ? 70   LYS L C   1 
ATOM   12576 O  O   . LYS L  1 70  ? 62.873  153.796 69.756  1.00 10.15 ? 70   LYS L O   1 
ATOM   12577 C  CB  . LYS L  1 70  ? 63.623  155.234 72.661  1.00 11.25 ? 70   LYS L CB  1 
ATOM   12578 C  CG  . LYS L  1 70  ? 64.308  155.206 74.001  1.00 11.78 ? 70   LYS L CG  1 
ATOM   12579 C  CD  . LYS L  1 70  ? 64.577  156.643 74.505  1.00 21.17 ? 70   LYS L CD  1 
ATOM   12580 C  CE  . LYS L  1 70  ? 65.719  157.330 73.745  1.00 28.32 ? 70   LYS L CE  1 
ATOM   12581 N  NZ  . LYS L  1 70  ? 65.291  158.112 72.516  1.00 34.69 ? 70   LYS L NZ  1 
ATOM   12582 N  N   . HIS L  1 71  ? 61.136  154.213 71.163  1.00 9.22  ? 71   HIS L N   1 
ATOM   12583 C  CA  . HIS L  1 71  ? 60.157  154.348 70.105  1.00 9.24  ? 71   HIS L CA  1 
ATOM   12584 C  C   . HIS L  1 71  ? 60.450  155.536 69.179  1.00 9.64  ? 71   HIS L C   1 
ATOM   12585 O  O   . HIS L  1 71  ? 60.906  156.615 69.633  1.00 9.79  ? 71   HIS L O   1 
ATOM   12586 C  CB  . HIS L  1 71  ? 58.745  154.449 70.719  1.00 9.44  ? 71   HIS L CB  1 
ATOM   12587 C  CG  . HIS L  1 71  ? 57.660  154.596 69.692  1.00 11.19 ? 71   HIS L CG  1 
ATOM   12588 N  ND1 . HIS L  1 71  ? 57.204  153.539 68.937  1.00 10.29 ? 71   HIS L ND1 1 
ATOM   12589 C  CD2 . HIS L  1 71  ? 56.985  155.687 69.256  1.00 9.66  ? 71   HIS L CD2 1 
ATOM   12590 C  CE1 . HIS L  1 71  ? 56.290  153.966 68.080  1.00 9.40  ? 71   HIS L CE1 1 
ATOM   12591 N  NE2 . HIS L  1 71  ? 56.139  155.269 68.256  1.00 11.89 ? 71   HIS L NE2 1 
ATOM   12592 N  N   . GLY L  1 72  ? 60.227  155.346 67.880  1.00 9.85  ? 72   GLY L N   1 
ATOM   12593 C  CA  . GLY L  1 72  ? 60.462  156.397 66.907  1.00 9.39  ? 72   GLY L CA  1 
ATOM   12594 C  C   . GLY L  1 72  ? 59.529  156.283 65.708  1.00 10.15 ? 72   GLY L C   1 
ATOM   12595 O  O   . GLY L  1 72  ? 58.672  155.408 65.651  1.00 9.13  ? 72   GLY L O   1 
ATOM   12596 N  N   . GLY L  1 73  ? 59.659  157.201 64.766  1.00 9.54  ? 73   GLY L N   1 
ATOM   12597 C  CA  . GLY L  1 73  ? 58.938  157.068 63.510  1.00 10.67 ? 73   GLY L CA  1 
ATOM   12598 C  C   . GLY L  1 73  ? 59.800  156.229 62.577  1.00 11.22 ? 73   GLY L C   1 
ATOM   12599 O  O   . GLY L  1 73  ? 60.980  155.991 62.860  1.00 12.34 ? 73   GLY L O   1 
ATOM   12600 N  N   . PRO L  1 74  ? 59.224  155.760 61.480  1.00 12.83 ? 74   PRO L N   1 
ATOM   12601 C  CA  . PRO L  1 74  ? 59.947  154.903 60.537  1.00 13.25 ? 74   PRO L CA  1 
ATOM   12602 C  C   . PRO L  1 74  ? 61.235  155.543 60.012  1.00 14.06 ? 74   PRO L C   1 
ATOM   12603 O  O   . PRO L  1 74  ? 62.188  154.836 59.732  1.00 13.70 ? 74   PRO L O   1 
ATOM   12604 C  CB  . PRO L  1 74  ? 58.946  154.696 59.376  1.00 13.49 ? 74   PRO L CB  1 
ATOM   12605 C  CG  . PRO L  1 74  ? 57.732  155.501 59.683  1.00 14.96 ? 74   PRO L CG  1 
ATOM   12606 C  CD  . PRO L  1 74  ? 57.827  156.008 61.086  1.00 12.25 ? 74   PRO L CD  1 
ATOM   12607 N  N   . LYS L  1 75  ? 61.276  156.860 59.901  1.00 15.15 ? 75   LYS L N   1 
ATOM   12608 C  CA  . LYS L  1 75  ? 62.473  157.499 59.349  1.00 17.00 ? 75   LYS L CA  1 
ATOM   12609 C  C   . LYS L  1 75  ? 63.578  157.726 60.383  1.00 16.82 ? 75   LYS L C   1 
ATOM   12610 O  O   . LYS L  1 75  ? 64.711  158.081 60.021  1.00 16.39 ? 75   LYS L O   1 
ATOM   12611 C  CB  . LYS L  1 75  ? 62.113  158.835 58.690  1.00 17.72 ? 75   LYS L CB  1 
ATOM   12612 C  CG  . LYS L  1 75  ? 61.167  158.711 57.500  1.00 20.68 ? 75   LYS L CG  1 
ATOM   12613 C  CD  . LYS L  1 75  ? 61.215  159.984 56.624  1.00 26.24 ? 75   LYS L CD  1 
ATOM   12614 C  CE  . LYS L  1 75  ? 60.099  160.973 56.941  1.00 29.00 ? 75   LYS L CE  1 
ATOM   12615 N  NZ  . LYS L  1 75  ? 60.321  162.263 56.208  1.00 32.23 ? 75   LYS L NZ  1 
ATOM   12616 N  N   . ASP L  1 76  ? 63.266  157.542 61.659  1.00 16.43 ? 76   ASP L N   1 
ATOM   12617 C  CA  . ASP L  1 76  ? 64.265  157.776 62.713  1.00 17.70 ? 76   ASP L CA  1 
ATOM   12618 C  C   . ASP L  1 76  ? 65.283  156.657 62.878  1.00 18.08 ? 76   ASP L C   1 
ATOM   12619 O  O   . ASP L  1 76  ? 64.933  155.500 62.829  1.00 17.81 ? 76   ASP L O   1 
ATOM   12620 C  CB  . ASP L  1 76  ? 63.590  158.033 64.063  1.00 16.84 ? 76   ASP L CB  1 
ATOM   12621 C  CG  . ASP L  1 76  ? 62.694  159.243 64.032  1.00 17.64 ? 76   ASP L CG  1 
ATOM   12622 O  OD1 . ASP L  1 76  ? 63.148  160.281 63.505  1.00 19.56 ? 76   ASP L OD1 1 
ATOM   12623 O  OD2 . ASP L  1 76  ? 61.524  159.266 64.465  1.00 16.55 ? 76   ASP L OD2 1 
ATOM   12624 N  N   . GLU L  1 77  ? 66.543  157.021 63.102  1.00 18.65 ? 77   GLU L N   1 
ATOM   12625 C  CA  . GLU L  1 77  ? 67.573  156.030 63.384  1.00 19.02 ? 77   GLU L CA  1 
ATOM   12626 C  C   . GLU L  1 77  ? 67.219  155.358 64.713  1.00 17.68 ? 77   GLU L C   1 
ATOM   12627 O  O   . GLU L  1 77  ? 67.330  154.135 64.864  1.00 18.37 ? 77   GLU L O   1 
ATOM   12628 C  CB  . GLU L  1 77  ? 68.943  156.714 63.474  1.00 20.06 ? 77   GLU L CB  1 
ATOM   12629 C  CG  . GLU L  1 77  ? 70.104  155.759 63.710  1.00 24.67 ? 77   GLU L CG  1 
ATOM   12630 C  CD  . GLU L  1 77  ? 70.153  154.618 62.707  1.00 31.53 ? 77   GLU L CD  1 
ATOM   12631 O  OE1 . GLU L  1 77  ? 69.765  153.495 63.090  1.00 34.57 ? 77   GLU L OE1 1 
ATOM   12632 O  OE2 . GLU L  1 77  ? 70.589  154.829 61.546  1.00 35.16 ? 77   GLU L OE2 1 
ATOM   12633 N  N   . GLU L  1 78  ? 66.755  156.165 65.663  1.00 15.72 ? 78   GLU L N   1 
ATOM   12634 C  CA  . GLU L  1 78  ? 66.310  155.647 66.937  1.00 14.56 ? 78   GLU L CA  1 
ATOM   12635 C  C   . GLU L  1 78  ? 64.819  155.269 66.819  1.00 12.44 ? 78   GLU L C   1 
ATOM   12636 O  O   . GLU L  1 78  ? 63.940  156.137 66.876  1.00 10.55 ? 78   GLU L O   1 
ATOM   12637 C  CB  . GLU L  1 78  ? 66.499  156.669 68.059  1.00 15.23 ? 78   GLU L CB  1 
ATOM   12638 C  CG  . GLU L  1 78  ? 66.104  156.131 69.424  1.00 17.81 ? 78   GLU L CG  1 
ATOM   12639 C  CD  . GLU L  1 78  ? 67.182  155.255 70.044  1.00 21.69 ? 78   GLU L CD  1 
ATOM   12640 O  OE1 . GLU L  1 78  ? 68.303  155.215 69.475  1.00 26.33 ? 78   GLU L OE1 1 
ATOM   12641 O  OE2 . GLU L  1 78  ? 66.928  154.616 71.104  1.00 19.32 ? 78   GLU L OE2 1 
ATOM   12642 N  N   . ARG L  1 79  ? 64.567  153.974 66.598  1.00 11.10 ? 79   ARG L N   1 
ATOM   12643 C  CA  . ARG L  1 79  ? 63.205  153.429 66.537  1.00 10.36 ? 79   ARG L CA  1 
ATOM   12644 C  C   . ARG L  1 79  ? 63.222  151.949 66.884  1.00 10.06 ? 79   ARG L C   1 
ATOM   12645 O  O   . ARG L  1 79  ? 64.282  151.300 66.906  1.00 10.75 ? 79   ARG L O   1 
ATOM   12646 C  CB  . ARG L  1 79  ? 62.597  153.561 65.130  1.00 10.82 ? 79   ARG L CB  1 
ATOM   12647 C  CG  . ARG L  1 79  ? 63.486  152.945 64.007  1.00 11.59 ? 79   ARG L CG  1 
ATOM   12648 C  CD  . ARG L  1 79  ? 62.781  152.916 62.632  1.00 10.45 ? 79   ARG L CD  1 
ATOM   12649 N  NE  . ARG L  1 79  ? 61.997  151.687 62.458  1.00 12.15 ? 79   ARG L NE  1 
ATOM   12650 C  CZ  . ARG L  1 79  ? 61.533  151.243 61.283  1.00 13.64 ? 79   ARG L CZ  1 
ATOM   12651 N  NH1 . ARG L  1 79  ? 61.719  151.947 60.174  1.00 13.31 ? 79   ARG L NH1 1 
ATOM   12652 N  NH2 . ARG L  1 79  ? 60.866  150.096 61.210  1.00 12.94 ? 79   ARG L NH2 1 
ATOM   12653 N  N   . HIS L  1 80  ? 62.036  151.409 67.140  1.00 9.75  ? 80   HIS L N   1 
ATOM   12654 C  CA  . HIS L  1 80  ? 61.871  149.985 67.337  1.00 9.42  ? 80   HIS L CA  1 
ATOM   12655 C  C   . HIS L  1 80  ? 61.828  149.443 65.910  1.00 8.92  ? 80   HIS L C   1 
ATOM   12656 O  O   . HIS L  1 80  ? 61.402  150.166 65.003  1.00 7.64  ? 80   HIS L O   1 
ATOM   12657 C  CB  . HIS L  1 80  ? 60.488  149.717 68.010  1.00 8.73  ? 80   HIS L CB  1 
ATOM   12658 C  CG  . HIS L  1 80  ? 60.365  150.307 69.386  1.00 8.73  ? 80   HIS L CG  1 
ATOM   12659 N  ND1 . HIS L  1 80  ? 59.188  150.835 69.881  1.00 7.90  ? 80   HIS L ND1 1 
ATOM   12660 C  CD2 . HIS L  1 80  ? 61.277  150.420 70.381  1.00 9.67  ? 80   HIS L CD2 1 
ATOM   12661 C  CE1 . HIS L  1 80  ? 59.382  151.240 71.126  1.00 6.71  ? 80   HIS L CE1 1 
ATOM   12662 N  NE2 . HIS L  1 80  ? 60.638  150.987 71.455  1.00 9.34  ? 80   HIS L NE2 1 
ATOM   12663 N  N   . VAL L  1 81  ? 62.287  148.206 65.713  1.00 8.27  ? 81   VAL L N   1 
ATOM   12664 C  CA  . VAL L  1 81  ? 62.106  147.514 64.413  1.00 8.80  ? 81   VAL L CA  1 
ATOM   12665 C  C   . VAL L  1 81  ? 60.667  147.580 63.937  1.00 9.24  ? 81   VAL L C   1 
ATOM   12666 O  O   . VAL L  1 81  ? 60.401  147.877 62.769  1.00 9.15  ? 81   VAL L O   1 
ATOM   12667 C  CB  . VAL L  1 81  ? 62.561  146.034 64.491  1.00 8.43  ? 81   VAL L CB  1 
ATOM   12668 C  CG1 . VAL L  1 81  ? 62.230  145.267 63.184  1.00 8.45  ? 81   VAL L CG1 1 
ATOM   12669 C  CG2 . VAL L  1 81  ? 64.065  145.992 64.759  1.00 9.48  ? 81   VAL L CG2 1 
ATOM   12670 N  N   . GLY L  1 82  ? 59.709  147.367 64.838  1.00 8.83  ? 82   GLY L N   1 
ATOM   12671 C  CA  . GLY L  1 82  ? 58.316  147.358 64.416  1.00 9.66  ? 82   GLY L CA  1 
ATOM   12672 C  C   . GLY L  1 82  ? 57.660  148.719 64.207  1.00 10.65 ? 82   GLY L C   1 
ATOM   12673 O  O   . GLY L  1 82  ? 56.450  148.767 63.997  1.00 10.60 ? 82   GLY L O   1 
ATOM   12674 N  N   . ASP L  1 83  ? 58.415  149.822 64.302  1.00 9.74  ? 83   ASP L N   1 
ATOM   12675 C  CA  . ASP L  1 83  ? 57.796  151.154 64.172  1.00 9.89  ? 83   ASP L CA  1 
ATOM   12676 C  C   . ASP L  1 83  ? 57.550  151.572 62.729  1.00 10.63 ? 83   ASP L C   1 
ATOM   12677 O  O   . ASP L  1 83  ? 58.444  152.134 62.079  1.00 11.05 ? 83   ASP L O   1 
ATOM   12678 C  CB  . ASP L  1 83  ? 58.625  152.253 64.864  1.00 10.33 ? 83   ASP L CB  1 
ATOM   12679 C  CG  . ASP L  1 83  ? 58.692  152.089 66.365  1.00 10.57 ? 83   ASP L CG  1 
ATOM   12680 O  OD1 . ASP L  1 83  ? 57.827  151.374 66.966  1.00 8.95  ? 83   ASP L OD1 1 
ATOM   12681 O  OD2 . ASP L  1 83  ? 59.586  152.640 67.032  1.00 9.89  ? 83   ASP L OD2 1 
ATOM   12682 N  N   . LEU L  1 84  ? 56.322  151.376 62.258  1.00 9.98  ? 84   LEU L N   1 
ATOM   12683 C  CA  . LEU L  1 84  ? 55.970  151.722 60.875  1.00 11.02 ? 84   LEU L CA  1 
ATOM   12684 C  C   . LEU L  1 84  ? 55.126  152.997 60.784  1.00 11.08 ? 84   LEU L C   1 
ATOM   12685 O  O   . LEU L  1 84  ? 54.522  153.308 59.757  1.00 12.62 ? 84   LEU L O   1 
ATOM   12686 C  CB  . LEU L  1 84  ? 55.285  150.534 60.189  1.00 10.16 ? 84   LEU L CB  1 
ATOM   12687 C  CG  . LEU L  1 84  ? 56.122  149.249 60.140  1.00 11.50 ? 84   LEU L CG  1 
ATOM   12688 C  CD1 . LEU L  1 84  ? 55.262  148.156 59.533  1.00 9.94  ? 84   LEU L CD1 1 
ATOM   12689 C  CD2 . LEU L  1 84  ? 57.420  149.440 59.328  1.00 11.41 ? 84   LEU L CD2 1 
ATOM   12690 N  N   . GLY L  1 85  ? 55.108  153.756 61.869  1.00 11.56 ? 85   GLY L N   1 
ATOM   12691 C  CA  . GLY L  1 85  ? 54.499  155.071 61.861  1.00 11.78 ? 85   GLY L CA  1 
ATOM   12692 C  C   . GLY L  1 85  ? 52.996  155.106 61.917  1.00 11.53 ? 85   GLY L C   1 
ATOM   12693 O  O   . GLY L  1 85  ? 52.375  154.494 62.791  1.00 11.04 ? 85   GLY L O   1 
ATOM   12694 N  N   . ASN L  1 86  ? 52.412  155.877 60.999  1.00 11.89 ? 86   ASN L N   1 
ATOM   12695 C  CA  . ASN L  1 86  ? 50.973  156.059 60.905  1.00 11.47 ? 86   ASN L CA  1 
ATOM   12696 C  C   . ASN L  1 86  ? 50.411  155.704 59.510  1.00 12.32 ? 86   ASN L C   1 
ATOM   12697 O  O   . ASN L  1 86  ? 51.052  155.938 58.480  1.00 12.55 ? 86   ASN L O   1 
ATOM   12698 C  CB  . ASN L  1 86  ? 50.599  157.538 61.150  1.00 12.45 ? 86   ASN L CB  1 
ATOM   12699 C  CG  . ASN L  1 86  ? 50.740  157.944 62.599  1.00 10.99 ? 86   ASN L CG  1 
ATOM   12700 O  OD1 . ASN L  1 86  ? 50.085  157.395 63.457  1.00 10.67 ? 86   ASN L OD1 1 
ATOM   12701 N  ND2 . ASN L  1 86  ? 51.616  158.911 62.874  1.00 11.15 ? 86   ASN L ND2 1 
ATOM   12702 N  N   . VAL L  1 87  ? 49.199  155.188 59.484  1.00 12.19 ? 87   VAL L N   1 
ATOM   12703 C  CA  . VAL L  1 87  ? 48.503  155.093 58.209  1.00 12.61 ? 87   VAL L CA  1 
ATOM   12704 C  C   . VAL L  1 87  ? 47.437  156.160 58.281  1.00 13.56 ? 87   VAL L C   1 
ATOM   12705 O  O   . VAL L  1 87  ? 47.074  156.610 59.374  1.00 14.46 ? 87   VAL L O   1 
ATOM   12706 C  CB  . VAL L  1 87  ? 47.911  153.723 57.910  1.00 12.60 ? 87   VAL L CB  1 
ATOM   12707 C  CG1 . VAL L  1 87  ? 49.015  152.665 57.923  1.00 13.05 ? 87   VAL L CG1 1 
ATOM   12708 C  CG2 . VAL L  1 87  ? 46.791  153.379 58.871  1.00 11.98 ? 87   VAL L CG2 1 
ATOM   12709 N  N   . THR L  1 88  ? 46.934  156.571 57.130  1.00 13.11 ? 88   THR L N   1 
ATOM   12710 C  CA  . THR L  1 88  ? 45.982  157.674 57.093  1.00 14.20 ? 88   THR L CA  1 
ATOM   12711 C  C   . THR L  1 88  ? 44.652  157.235 56.493  1.00 13.92 ? 88   THR L C   1 
ATOM   12712 O  O   . THR L  1 88  ? 44.600  156.785 55.370  1.00 13.82 ? 88   THR L O   1 
ATOM   12713 C  CB  . THR L  1 88  ? 46.619  158.827 56.292  1.00 14.12 ? 88   THR L CB  1 
ATOM   12714 O  OG1 . THR L  1 88  ? 47.744  159.318 57.030  1.00 16.20 ? 88   THR L OG1 1 
ATOM   12715 C  CG2 . THR L  1 88  ? 45.683  160.051 56.190  1.00 15.06 ? 88   THR L CG2 1 
ATOM   12716 N  N   . ALA L  1 89  ? 43.584  157.332 57.273  1.00 14.59 ? 89   ALA L N   1 
ATOM   12717 C  CA  . ALA L  1 89  ? 42.270  156.968 56.782  1.00 14.63 ? 89   ALA L CA  1 
ATOM   12718 C  C   . ALA L  1 89  ? 41.609  158.195 56.184  1.00 15.59 ? 89   ALA L C   1 
ATOM   12719 O  O   . ALA L  1 89  ? 41.697  159.301 56.738  1.00 14.19 ? 89   ALA L O   1 
ATOM   12720 C  CB  . ALA L  1 89  ? 41.426  156.413 57.892  1.00 14.99 ? 89   ALA L CB  1 
ATOM   12721 N  N   . ASP L  1 90  ? 40.972  157.995 55.040  1.00 16.13 ? 90   ASP L N   1 
ATOM   12722 C  CA  . ASP L  1 90  ? 40.275  159.091 54.379  1.00 17.63 ? 90   ASP L CA  1 
ATOM   12723 C  C   . ASP L  1 90  ? 38.909  159.293 55.004  1.00 17.97 ? 90   ASP L C   1 
ATOM   12724 O  O   . ASP L  1 90  ? 38.598  158.686 56.026  1.00 17.09 ? 90   ASP L O   1 
ATOM   12725 C  CB  . ASP L  1 90  ? 40.145  158.844 52.880  1.00 17.83 ? 90   ASP L CB  1 
ATOM   12726 C  CG  . ASP L  1 90  ? 39.319  157.618 52.553  1.00 18.76 ? 90   ASP L CG  1 
ATOM   12727 O  OD1 . ASP L  1 90  ? 38.550  157.136 53.418  1.00 20.73 ? 90   ASP L OD1 1 
ATOM   12728 O  OD2 . ASP L  1 90  ? 39.361  157.078 51.425  1.00 20.48 ? 90   ASP L OD2 1 
ATOM   12729 N  N   . LYS L  1 91  ? 38.098  160.156 54.384  1.00 18.43 ? 91   LYS L N   1 
ATOM   12730 C  CA  . LYS L  1 91  ? 36.788  160.490 54.914  1.00 19.24 ? 91   LYS L CA  1 
ATOM   12731 C  C   . LYS L  1 91  ? 35.829  159.308 54.943  1.00 19.25 ? 91   LYS L C   1 
ATOM   12732 O  O   . LYS L  1 91  ? 34.862  159.312 55.695  1.00 19.80 ? 91   LYS L O   1 
ATOM   12733 C  CB  . LYS L  1 91  ? 36.174  161.642 54.111  1.00 20.30 ? 91   LYS L CB  1 
ATOM   12734 C  CG  . LYS L  1 91  ? 36.407  161.536 52.610  1.00 21.96 ? 91   LYS L CG  1 
ATOM   12735 C  CD  . LYS L  1 91  ? 35.310  160.756 51.917  1.00 25.73 ? 91   LYS L CD  1 
ATOM   12736 N  N   . ASP L  1 92  ? 36.080  158.302 54.121  1.00 18.98 ? 92   ASP L N   1 
ATOM   12737 C  CA  . ASP L  1 92  ? 35.228  157.128 54.127  1.00 19.14 ? 92   ASP L CA  1 
ATOM   12738 C  C   . ASP L  1 92  ? 35.731  156.071 55.105  1.00 18.32 ? 92   ASP L C   1 
ATOM   12739 O  O   . ASP L  1 92  ? 35.194  154.960 55.177  1.00 18.37 ? 92   ASP L O   1 
ATOM   12740 C  CB  . ASP L  1 92  ? 35.116  156.564 52.723  1.00 19.49 ? 92   ASP L CB  1 
ATOM   12741 C  CG  . ASP L  1 92  ? 34.490  157.559 51.767  1.00 21.29 ? 92   ASP L CG  1 
ATOM   12742 O  OD1 . ASP L  1 92  ? 33.696  158.396 52.252  1.00 21.33 ? 92   ASP L OD1 1 
ATOM   12743 O  OD2 . ASP L  1 92  ? 34.739  157.597 50.540  1.00 22.33 ? 92   ASP L OD2 1 
ATOM   12744 N  N   . GLY L  1 93  ? 36.765  156.422 55.860  1.00 17.91 ? 93   GLY L N   1 
ATOM   12745 C  CA  . GLY L  1 93  ? 37.333  155.502 56.841  1.00 16.38 ? 93   GLY L CA  1 
ATOM   12746 C  C   . GLY L  1 93  ? 38.277  154.469 56.257  1.00 16.18 ? 93   GLY L C   1 
ATOM   12747 O  O   . GLY L  1 93  ? 38.571  153.446 56.895  1.00 14.53 ? 93   GLY L O   1 
ATOM   12748 N  N   . VAL L  1 94  ? 38.784  154.747 55.062  1.00 15.41 ? 94   VAL L N   1 
ATOM   12749 C  CA  . VAL L  1 94  ? 39.662  153.820 54.375  1.00 15.76 ? 94   VAL L CA  1 
ATOM   12750 C  C   . VAL L  1 94  ? 41.108  154.315 54.352  1.00 16.12 ? 94   VAL L C   1 
ATOM   12751 O  O   . VAL L  1 94  ? 41.395  155.467 53.975  1.00 15.87 ? 94   VAL L O   1 
ATOM   12752 C  CB  . VAL L  1 94  ? 39.185  153.579 52.940  1.00 15.80 ? 94   VAL L CB  1 
ATOM   12753 C  CG1 . VAL L  1 94  ? 40.068  152.579 52.240  1.00 16.66 ? 94   VAL L CG1 1 
ATOM   12754 C  CG2 . VAL L  1 94  ? 37.735  153.109 52.934  1.00 15.85 ? 94   VAL L CG2 1 
ATOM   12755 N  N   . ALA L  1 95  ? 42.021  153.448 54.776  1.00 15.69 ? 95   ALA L N   1 
ATOM   12756 C  CA  . ALA L  1 95  ? 43.430  153.787 54.742  1.00 16.73 ? 95   ALA L CA  1 
ATOM   12757 C  C   . ALA L  1 95  ? 44.136  152.914 53.736  1.00 17.49 ? 95   ALA L C   1 
ATOM   12758 O  O   . ALA L  1 95  ? 44.215  151.688 53.895  1.00 17.61 ? 95   ALA L O   1 
ATOM   12759 C  CB  . ALA L  1 95  ? 44.075  153.622 56.127  1.00 17.66 ? 95   ALA L CB  1 
ATOM   12760 N  N   . ASP L  1 96  ? 44.639  153.536 52.686  1.00 17.09 ? 96   ASP L N   1 
ATOM   12761 C  CA  . ASP L  1 96  ? 45.385  152.795 51.695  1.00 18.53 ? 96   ASP L CA  1 
ATOM   12762 C  C   . ASP L  1 96  ? 46.836  152.831 52.131  1.00 18.44 ? 96   ASP L C   1 
ATOM   12763 O  O   . ASP L  1 96  ? 47.357  153.879 52.479  1.00 18.50 ? 96   ASP L O   1 
ATOM   12764 C  CB  . ASP L  1 96  ? 45.200  153.427 50.322  1.00 19.42 ? 96   ASP L CB  1 
ATOM   12765 C  CG  . ASP L  1 96  ? 43.855  153.081 49.708  1.00 22.56 ? 96   ASP L CG  1 
ATOM   12766 O  OD1 . ASP L  1 96  ? 43.136  154.022 49.282  1.00 27.21 ? 96   ASP L OD1 1 
ATOM   12767 O  OD2 . ASP L  1 96  ? 43.429  151.896 49.610  1.00 26.54 ? 96   ASP L OD2 1 
ATOM   12768 N  N   . VAL L  1 97  ? 47.487  151.683 52.148  1.00 17.48 ? 97   VAL L N   1 
ATOM   12769 C  CA  . VAL L  1 97  ? 48.850  151.654 52.616  1.00 17.88 ? 97   VAL L CA  1 
ATOM   12770 C  C   . VAL L  1 97  ? 49.792  151.244 51.518  1.00 18.18 ? 97   VAL L C   1 
ATOM   12771 O  O   . VAL L  1 97  ? 49.569  150.246 50.859  1.00 15.68 ? 97   VAL L O   1 
ATOM   12772 C  CB  . VAL L  1 97  ? 49.038  150.620 53.714  1.00 17.78 ? 97   VAL L CB  1 
ATOM   12773 C  CG1 . VAL L  1 97  ? 50.431  150.718 54.260  1.00 18.57 ? 97   VAL L CG1 1 
ATOM   12774 C  CG2 . VAL L  1 97  ? 47.985  150.768 54.811  1.00 17.09 ? 97   VAL L CG2 1 
ATOM   12775 N  N   . SER L  1 98  ? 50.854  152.016 51.333  1.00 18.33 ? 98   SER L N   1 
ATOM   12776 C  CA  . SER L  1 98  ? 51.871  151.648 50.366  1.00 19.99 ? 98   SER L CA  1 
ATOM   12777 C  C   . SER L  1 98  ? 53.174  152.207 50.883  1.00 20.60 ? 98   SER L C   1 
ATOM   12778 O  O   . SER L  1 98  ? 53.563  153.319 50.531  1.00 22.17 ? 98   SER L O   1 
ATOM   12779 C  CB  . SER L  1 98  ? 51.555  152.214 48.987  1.00 20.64 ? 98   SER L CB  1 
ATOM   12780 O  OG  . SER L  1 98  ? 52.230  151.469 48.001  1.00 21.62 ? 98   SER L OG  1 
ATOM   12781 N  N   . ILE L  1 99  ? 53.841  151.401 51.697  1.00 20.19 ? 99   ILE L N   1 
ATOM   12782 C  CA  . ILE L  1 99  ? 55.017  151.766 52.472  1.00 20.42 ? 99   ILE L CA  1 
ATOM   12783 C  C   . ILE L  1 99  ? 56.200  150.978 51.950  1.00 19.34 ? 99   ILE L C   1 
ATOM   12784 O  O   . ILE L  1 99  ? 56.029  149.893 51.401  1.00 18.41 ? 99   ILE L O   1 
ATOM   12785 C  CB  . ILE L  1 99  ? 54.787  151.246 53.928  1.00 20.16 ? 99   ILE L CB  1 
ATOM   12786 C  CG1 . ILE L  1 99  ? 53.887  152.163 54.746  1.00 22.60 ? 99   ILE L CG1 1 
ATOM   12787 C  CG2 . ILE L  1 99  ? 56.099  151.090 54.660  1.00 22.50 ? 99   ILE L CG2 1 
ATOM   12788 C  CD1 . ILE L  1 99  ? 53.644  151.645 56.144  1.00 21.32 ? 99   ILE L CD1 1 
ATOM   12789 N  N   . GLU L  1 100 ? 57.398  151.495 52.153  1.00 17.85 ? 100  GLU L N   1 
ATOM   12790 C  CA  . GLU L  1 100 ? 58.595  150.691 51.944  1.00 17.40 ? 100  GLU L CA  1 
ATOM   12791 C  C   . GLU L  1 100 ? 59.415  150.876 53.208  1.00 16.20 ? 100  GLU L C   1 
ATOM   12792 O  O   . GLU L  1 100 ? 59.571  151.988 53.685  1.00 15.56 ? 100  GLU L O   1 
ATOM   12793 C  CB  . GLU L  1 100 ? 59.384  151.143 50.716  1.00 18.62 ? 100  GLU L CB  1 
ATOM   12794 C  CG  . GLU L  1 100 ? 60.361  150.094 50.222  1.00 22.56 ? 100  GLU L CG  1 
ATOM   12795 C  CD  . GLU L  1 100 ? 60.706  150.218 48.737  1.00 27.99 ? 100  GLU L CD  1 
ATOM   12796 O  OE1 . GLU L  1 100 ? 59.828  150.595 47.921  1.00 30.42 ? 100  GLU L OE1 1 
ATOM   12797 O  OE2 . GLU L  1 100 ? 61.864  149.904 48.381  1.00 28.89 ? 100  GLU L OE2 1 
ATOM   12798 N  N   . ASP L  1 101 ? 59.935  149.797 53.766  1.00 15.01 ? 101  ASP L N   1 
ATOM   12799 C  CA  . ASP L  1 101 ? 60.720  149.912 54.970  1.00 15.14 ? 101  ASP L CA  1 
ATOM   12800 C  C   . ASP L  1 101 ? 61.897  148.961 54.931  1.00 15.08 ? 101  ASP L C   1 
ATOM   12801 O  O   . ASP L  1 101 ? 61.746  147.818 54.494  1.00 15.71 ? 101  ASP L O   1 
ATOM   12802 C  CB  . ASP L  1 101 ? 59.851  149.645 56.216  1.00 14.86 ? 101  ASP L CB  1 
ATOM   12803 C  CG  . ASP L  1 101 ? 60.565  150.007 57.490  1.00 15.30 ? 101  ASP L CG  1 
ATOM   12804 O  OD1 . ASP L  1 101 ? 60.604  151.225 57.831  1.00 17.66 ? 101  ASP L OD1 1 
ATOM   12805 O  OD2 . ASP L  1 101 ? 61.163  149.173 58.208  1.00 14.47 ? 101  ASP L OD2 1 
ATOM   12806 N  N   . SER L  1 102 ? 63.059  149.416 55.392  1.00 15.38 ? 102  SER L N   1 
ATOM   12807 C  CA  . SER L  1 102 ? 64.272  148.582 55.363  1.00 15.71 ? 102  SER L CA  1 
ATOM   12808 C  C   . SER L  1 102 ? 64.770  148.150 56.734  1.00 15.03 ? 102  SER L C   1 
ATOM   12809 O  O   . SER L  1 102 ? 65.852  147.573 56.847  1.00 14.84 ? 102  SER L O   1 
ATOM   12810 C  CB  . SER L  1 102 ? 65.410  149.276 54.599  1.00 16.89 ? 102  SER L CB  1 
ATOM   12811 O  OG  . SER L  1 102 ? 65.226  149.106 53.203  1.00 19.23 ? 102  SER L OG  1 
ATOM   12812 N  N   . VAL L  1 103 ? 63.999  148.426 57.787  1.00 13.18 ? 103  VAL L N   1 
ATOM   12813 C  CA  . VAL L  1 103 ? 64.414  147.976 59.105  1.00 12.53 ? 103  VAL L CA  1 
ATOM   12814 C  C   . VAL L  1 103 ? 63.747  146.644 59.418  1.00 11.67 ? 103  VAL L C   1 
ATOM   12815 O  O   . VAL L  1 103 ? 64.391  145.721 59.928  1.00 11.84 ? 103  VAL L O   1 
ATOM   12816 C  CB  . VAL L  1 103 ? 64.097  149.050 60.167  1.00 12.48 ? 103  VAL L CB  1 
ATOM   12817 C  CG1 . VAL L  1 103 ? 64.379  148.527 61.559  1.00 13.84 ? 103  VAL L CG1 1 
ATOM   12818 C  CG2 . VAL L  1 103 ? 64.940  150.265 59.854  1.00 13.68 ? 103  VAL L CG2 1 
ATOM   12819 N  N   . ILE L  1 104 ? 62.465  146.532 59.099  1.00 11.32 ? 104  ILE L N   1 
ATOM   12820 C  CA  . ILE L  1 104 ? 61.826  145.229 59.201  1.00 11.04 ? 104  ILE L CA  1 
ATOM   12821 C  C   . ILE L  1 104 ? 62.440  144.348 58.120  1.00 11.64 ? 104  ILE L C   1 
ATOM   12822 O  O   . ILE L  1 104 ? 63.088  144.829 57.173  1.00 9.69  ? 104  ILE L O   1 
ATOM   12823 C  CB  . ILE L  1 104 ? 60.310  145.294 58.968  1.00 11.02 ? 104  ILE L CB  1 
ATOM   12824 C  CG1 . ILE L  1 104 ? 60.016  145.877 57.582  1.00 10.40 ? 104  ILE L CG1 1 
ATOM   12825 C  CG2 . ILE L  1 104 ? 59.618  146.102 60.097  1.00 10.19 ? 104  ILE L CG2 1 
ATOM   12826 C  CD1 . ILE L  1 104 ? 58.526  145.845 57.193  1.00 10.40 ? 104  ILE L CD1 1 
ATOM   12827 N  N   . SER L  1 105 ? 62.233  143.050 58.279  1.00 12.17 ? 105  SER L N   1 
ATOM   12828 C  CA  . SER L  1 105 ? 62.694  142.085 57.302  1.00 12.66 ? 105  SER L CA  1 
ATOM   12829 C  C   . SER L  1 105 ? 61.759  140.859 57.320  1.00 13.73 ? 105  SER L C   1 
ATOM   12830 O  O   . SER L  1 105 ? 60.972  140.706 58.258  1.00 13.44 ? 105  SER L O   1 
ATOM   12831 C  CB  . SER L  1 105 ? 64.114  141.651 57.638  1.00 12.73 ? 105  SER L CB  1 
ATOM   12832 O  OG  . SER L  1 105 ? 64.644  140.889 56.575  1.00 11.67 ? 105  SER L OG  1 
ATOM   12833 N  N   . LEU L  1 106 ? 61.828  140.023 56.276  1.00 14.14 ? 106  LEU L N   1 
ATOM   12834 C  CA  . LEU L  1 106 ? 61.095  138.773 56.261  1.00 15.24 ? 106  LEU L CA  1 
ATOM   12835 C  C   . LEU L  1 106 ? 62.052  137.580 56.401  1.00 16.56 ? 106  LEU L C   1 
ATOM   12836 O  O   . LEU L  1 106 ? 61.666  136.446 56.204  1.00 17.30 ? 106  LEU L O   1 
ATOM   12837 C  CB  . LEU L  1 106 ? 60.218  138.630 55.008  1.00 14.86 ? 106  LEU L CB  1 
ATOM   12838 C  CG  . LEU L  1 106 ? 59.174  139.733 54.745  1.00 14.75 ? 106  LEU L CG  1 
ATOM   12839 C  CD1 . LEU L  1 106 ? 58.362  139.355 53.509  1.00 15.49 ? 106  LEU L CD1 1 
ATOM   12840 C  CD2 . LEU L  1 106 ? 58.239  139.974 55.922  1.00 12.86 ? 106  LEU L CD2 1 
ATOM   12841 N  N   . SER L  1 107 ? 63.290  137.860 56.772  1.00 18.06 ? 107  SER L N   1 
ATOM   12842 C  CA  . SER L  1 107 ? 64.299  136.850 57.070  1.00 19.74 ? 107  SER L CA  1 
ATOM   12843 C  C   . SER L  1 107 ? 65.242  137.478 58.088  1.00 19.70 ? 107  SER L C   1 
ATOM   12844 O  O   . SER L  1 107 ? 65.298  138.709 58.215  1.00 19.74 ? 107  SER L O   1 
ATOM   12845 C  CB  . SER L  1 107 ? 65.132  136.521 55.818  1.00 19.77 ? 107  SER L CB  1 
ATOM   12846 O  OG  . SER L  1 107 ? 64.343  135.849 54.850  1.00 24.84 ? 107  SER L OG  1 
ATOM   12847 N  N   . GLY L  1 108 ? 66.001  136.658 58.808  1.00 20.17 ? 108  GLY L N   1 
ATOM   12848 C  CA  . GLY L  1 108 ? 67.023  137.201 59.700  1.00 20.48 ? 108  GLY L CA  1 
ATOM   12849 C  C   . GLY L  1 108 ? 66.548  137.674 61.065  1.00 20.93 ? 108  GLY L C   1 
ATOM   12850 O  O   . GLY L  1 108 ? 65.450  137.337 61.502  1.00 20.76 ? 108  GLY L O   1 
ATOM   12851 N  N   . ASP L  1 109 ? 67.373  138.476 61.733  1.00 21.14 ? 109  ASP L N   1 
ATOM   12852 C  CA  . ASP L  1 109 ? 67.083  138.898 63.102  1.00 21.85 ? 109  ASP L CA  1 
ATOM   12853 C  C   . ASP L  1 109 ? 65.972  139.935 63.215  1.00 20.36 ? 109  ASP L C   1 
ATOM   12854 O  O   . ASP L  1 109 ? 65.399  140.119 64.272  1.00 21.70 ? 109  ASP L O   1 
ATOM   12855 C  CB  . ASP L  1 109 ? 68.349  139.430 63.788  1.00 23.05 ? 109  ASP L CB  1 
ATOM   12856 C  CG  . ASP L  1 109 ? 69.304  138.320 64.202  1.00 26.30 ? 109  ASP L CG  1 
ATOM   12857 O  OD1 . ASP L  1 109 ? 69.495  137.370 63.417  1.00 29.36 ? 109  ASP L OD1 1 
ATOM   12858 O  OD2 . ASP L  1 109 ? 69.909  138.322 65.300  1.00 30.77 ? 109  ASP L OD2 1 
ATOM   12859 N  N   . HIS L  1 110 ? 65.703  140.649 62.137  1.00 18.74 ? 110  HIS L N   1 
ATOM   12860 C  CA  . HIS L  1 110 ? 64.621  141.614 62.160  1.00 17.03 ? 110  HIS L CA  1 
ATOM   12861 C  C   . HIS L  1 110 ? 63.353  141.026 61.551  1.00 15.34 ? 110  HIS L C   1 
ATOM   12862 O  O   . HIS L  1 110 ? 62.432  141.766 61.224  1.00 14.13 ? 110  HIS L O   1 
ATOM   12863 C  CB  . HIS L  1 110 ? 65.022  142.862 61.400  1.00 17.08 ? 110  HIS L CB  1 
ATOM   12864 C  CG  . HIS L  1 110 ? 66.050  143.680 62.114  1.00 19.11 ? 110  HIS L CG  1 
ATOM   12865 N  ND1 . HIS L  1 110 ? 66.357  144.974 61.754  1.00 19.15 ? 110  HIS L ND1 1 
ATOM   12866 C  CD2 . HIS L  1 110 ? 66.857  143.373 63.158  1.00 20.08 ? 110  HIS L CD2 1 
ATOM   12867 C  CE1 . HIS L  1 110 ? 67.309  145.432 62.551  1.00 20.84 ? 110  HIS L CE1 1 
ATOM   12868 N  NE2 . HIS L  1 110 ? 67.629  144.480 63.413  1.00 19.90 ? 110  HIS L NE2 1 
ATOM   12869 N  N   . CYS L  1 111 ? 63.351  139.704 61.351  1.00 14.54 ? 111  CYS L N   1 
ATOM   12870 C  CA  . CYS L  1 111 ? 62.184  138.981 60.796  1.00 13.81 ? 111  CYS L CA  1 
ATOM   12871 C  C   . CYS L  1 111 ? 60.887  139.200 61.579  1.00 12.74 ? 111  CYS L C   1 
ATOM   12872 O  O   . CYS L  1 111 ? 60.857  139.032 62.808  1.00 12.43 ? 111  CYS L O   1 
ATOM   12873 C  CB  . CYS L  1 111 ? 62.463  137.488 60.772  1.00 14.16 ? 111  CYS L CB  1 
ATOM   12874 S  SG  . CYS L  1 111 ? 61.371  136.661 59.608  1.00 20.22 ? 111  CYS L SG  1 
ATOM   12875 N  N   . ILE L  1 112 ? 59.818  139.554 60.862  1.00 10.66 ? 112  ILE L N   1 
ATOM   12876 C  CA  . ILE L  1 112 ? 58.504  139.869 61.478  1.00 10.31 ? 112  ILE L CA  1 
ATOM   12877 C  C   . ILE L  1 112 ? 57.429  138.791 61.249  1.00 9.93  ? 112  ILE L C   1 
ATOM   12878 O  O   . ILE L  1 112 ? 56.283  138.930 61.639  1.00 9.27  ? 112  ILE L O   1 
ATOM   12879 C  CB  . ILE L  1 112 ? 57.999  141.219 60.986  1.00 9.86  ? 112  ILE L CB  1 
ATOM   12880 C  CG1 . ILE L  1 112 ? 57.749  141.223 59.468  1.00 11.49 ? 112  ILE L CG1 1 
ATOM   12881 C  CG2 . ILE L  1 112 ? 58.977  142.356 61.487  1.00 8.39  ? 112  ILE L CG2 1 
ATOM   12882 C  CD1 . ILE L  1 112 ? 57.013  142.492 59.013  1.00 11.51 ? 112  ILE L CD1 1 
ATOM   12883 N  N   . ILE L  1 113 ? 57.816  137.729 60.565  1.00 9.59  ? 113  ILE L N   1 
ATOM   12884 C  CA  . ILE L  1 113 ? 56.867  136.651 60.286  1.00 10.12 ? 113  ILE L CA  1 
ATOM   12885 C  C   . ILE L  1 113 ? 56.511  135.986 61.612  1.00 8.85  ? 113  ILE L C   1 
ATOM   12886 O  O   . ILE L  1 113 ? 57.389  135.762 62.464  1.00 8.41  ? 113  ILE L O   1 
ATOM   12887 C  CB  . ILE L  1 113 ? 57.493  135.609 59.338  1.00 9.96  ? 113  ILE L CB  1 
ATOM   12888 C  CG1 . ILE L  1 113 ? 57.793  136.224 57.978  1.00 13.78 ? 113  ILE L CG1 1 
ATOM   12889 C  CG2 . ILE L  1 113 ? 56.582  134.383 59.213  1.00 10.43 ? 113  ILE L CG2 1 
ATOM   12890 C  CD1 . ILE L  1 113 ? 56.619  136.441 57.170  1.00 18.89 ? 113  ILE L CD1 1 
ATOM   12891 N  N   . GLY L  1 114 ? 55.230  135.737 61.823  1.00 8.65  ? 114  GLY L N   1 
ATOM   12892 C  CA  . GLY L  1 114 ? 54.791  135.137 63.065  1.00 8.71  ? 114  GLY L CA  1 
ATOM   12893 C  C   . GLY L  1 114 ? 54.645  136.149 64.211  1.00 7.99  ? 114  GLY L C   1 
ATOM   12894 O  O   . GLY L  1 114 ? 54.396  135.757 65.364  1.00 9.24  ? 114  GLY L O   1 
ATOM   12895 N  N   . ARG L  1 115 ? 54.860  137.428 63.920  1.00 7.74  ? 115  ARG L N   1 
ATOM   12896 C  CA  . ARG L  1 115 ? 54.621  138.476 64.923  1.00 8.58  ? 115  ARG L CA  1 
ATOM   12897 C  C   . ARG L  1 115 ? 53.256  139.114 64.588  1.00 9.76  ? 115  ARG L C   1 
ATOM   12898 O  O   . ARG L  1 115 ? 52.572  138.620 63.664  1.00 10.23 ? 115  ARG L O   1 
ATOM   12899 C  CB  . ARG L  1 115 ? 55.783  139.467 64.926  1.00 8.11  ? 115  ARG L CB  1 
ATOM   12900 C  CG  . ARG L  1 115 ? 57.090  138.696 65.213  1.00 8.64  ? 115  ARG L CG  1 
ATOM   12901 C  CD  . ARG L  1 115 ? 58.316  139.586 65.535  1.00 8.78  ? 115  ARG L CD  1 
ATOM   12902 N  NE  . ARG L  1 115 ? 59.532  138.768 65.674  1.00 8.52  ? 115  ARG L NE  1 
ATOM   12903 C  CZ  . ARG L  1 115 ? 59.937  138.212 66.814  1.00 11.24 ? 115  ARG L CZ  1 
ATOM   12904 N  NH1 . ARG L  1 115 ? 59.229  138.379 67.933  1.00 9.99  ? 115  ARG L NH1 1 
ATOM   12905 N  NH2 . ARG L  1 115 ? 61.073  137.524 66.849  1.00 11.21 ? 115  ARG L NH2 1 
ATOM   12906 N  N   . THR L  1 116 ? 52.871  140.196 65.266  1.00 9.28  ? 116  THR L N   1 
ATOM   12907 C  CA  . THR L  1 116 ? 51.548  140.748 65.067  1.00 9.97  ? 116  THR L CA  1 
ATOM   12908 C  C   . THR L  1 116 ? 51.580  142.177 64.545  1.00 10.66 ? 116  THR L C   1 
ATOM   12909 O  O   . THR L  1 116 ? 52.295  143.060 65.096  1.00 10.31 ? 116  THR L O   1 
ATOM   12910 C  CB  . THR L  1 116 ? 50.755  140.751 66.419  1.00 11.40 ? 116  THR L CB  1 
ATOM   12911 O  OG1 . THR L  1 116 ? 50.430  139.406 66.815  1.00 11.52 ? 116  THR L OG1 1 
ATOM   12912 C  CG2 . THR L  1 116 ? 49.430  141.392 66.243  1.00 7.73  ? 116  THR L CG2 1 
ATOM   12913 N  N   . LEU L  1 117 ? 50.807  142.419 63.492  1.00 9.22  ? 117  LEU L N   1 
ATOM   12914 C  CA  . LEU L  1 117 ? 50.653  143.773 62.984  1.00 9.50  ? 117  LEU L CA  1 
ATOM   12915 C  C   . LEU L  1 117 ? 49.453  144.407 63.661  1.00 9.64  ? 117  LEU L C   1 
ATOM   12916 O  O   . LEU L  1 117 ? 48.394  143.756 63.783  1.00 8.47  ? 117  LEU L O   1 
ATOM   12917 C  CB  . LEU L  1 117 ? 50.444  143.750 61.460  1.00 9.81  ? 117  LEU L CB  1 
ATOM   12918 C  CG  . LEU L  1 117 ? 50.348  145.104 60.766  1.00 10.31 ? 117  LEU L CG  1 
ATOM   12919 C  CD1 . LEU L  1 117 ? 51.682  145.807 60.823  1.00 10.23 ? 117  LEU L CD1 1 
ATOM   12920 C  CD2 . LEU L  1 117 ? 50.020  144.844 59.267  1.00 8.05  ? 117  LEU L CD2 1 
ATOM   12921 N  N   . VAL L  1 118 ? 49.598  145.651 64.132  1.00 8.64  ? 118  VAL L N   1 
ATOM   12922 C  CA  . VAL L  1 118 ? 48.508  146.287 64.892  1.00 9.45  ? 118  VAL L CA  1 
ATOM   12923 C  C   . VAL L  1 118 ? 48.211  147.672 64.349  1.00 9.04  ? 118  VAL L C   1 
ATOM   12924 O  O   . VAL L  1 118 ? 49.143  148.444 63.990  1.00 9.18  ? 118  VAL L O   1 
ATOM   12925 C  CB  . VAL L  1 118 ? 48.871  146.480 66.398  1.00 10.64 ? 118  VAL L CB  1 
ATOM   12926 C  CG1 . VAL L  1 118 ? 47.722  147.129 67.176  1.00 10.64 ? 118  VAL L CG1 1 
ATOM   12927 C  CG2 . VAL L  1 118 ? 49.250  145.145 67.037  1.00 7.47  ? 118  VAL L CG2 1 
ATOM   12928 N  N   . VAL L  1 119 ? 46.929  147.994 64.255  1.00 8.69  ? 119  VAL L N   1 
ATOM   12929 C  CA  . VAL L  1 119 ? 46.555  149.373 63.894  1.00 9.13  ? 119  VAL L CA  1 
ATOM   12930 C  C   . VAL L  1 119 ? 45.835  149.952 65.101  1.00 9.55  ? 119  VAL L C   1 
ATOM   12931 O  O   . VAL L  1 119 ? 45.016  149.274 65.732  1.00 8.29  ? 119  VAL L O   1 
ATOM   12932 C  CB  . VAL L  1 119 ? 45.711  149.485 62.611  1.00 8.89  ? 119  VAL L CB  1 
ATOM   12933 C  CG1 . VAL L  1 119 ? 44.395  148.700 62.722  1.00 10.22 ? 119  VAL L CG1 1 
ATOM   12934 C  CG2 . VAL L  1 119 ? 45.456  150.955 62.284  1.00 8.72  ? 119  VAL L CG2 1 
ATOM   12935 N  N   . HIS L  1 120 ? 46.186  151.193 65.444  1.00 10.24 ? 120  HIS L N   1 
ATOM   12936 C  CA  . HIS L  1 120 ? 45.759  151.808 66.679  1.00 10.36 ? 120  HIS L CA  1 
ATOM   12937 C  C   . HIS L  1 120 ? 44.669  152.863 66.561  1.00 11.46 ? 120  HIS L C   1 
ATOM   12938 O  O   . HIS L  1 120 ? 44.417  153.373 65.477  1.00 11.45 ? 120  HIS L O   1 
ATOM   12939 C  CB  . HIS L  1 120 ? 46.978  152.501 67.319  1.00 9.87  ? 120  HIS L CB  1 
ATOM   12940 C  CG  . HIS L  1 120 ? 47.926  151.544 67.969  1.00 11.37 ? 120  HIS L CG  1 
ATOM   12941 N  ND1 . HIS L  1 120 ? 47.785  151.139 69.279  1.00 12.40 ? 120  HIS L ND1 1 
ATOM   12942 C  CD2 . HIS L  1 120 ? 49.015  150.897 67.487  1.00 12.03 ? 120  HIS L CD2 1 
ATOM   12943 C  CE1 . HIS L  1 120 ? 48.790  150.337 69.593  1.00 13.68 ? 120  HIS L CE1 1 
ATOM   12944 N  NE2 . HIS L  1 120 ? 49.516  150.134 68.506  1.00 9.82  ? 120  HIS L NE2 1 
ATOM   12945 N  N   . GLU L  1 121 ? 44.117  153.215 67.727  1.00 11.23 ? 121  GLU L N   1 
ATOM   12946 C  CA  . GLU L  1 121 ? 43.035  154.181 67.900  1.00 13.12 ? 121  GLU L CA  1 
ATOM   12947 C  C   . GLU L  1 121 ? 43.407  155.595 67.489  1.00 13.76 ? 121  GLU L C   1 
ATOM   12948 O  O   . GLU L  1 121 ? 42.631  156.284 66.818  1.00 12.35 ? 121  GLU L O   1 
ATOM   12949 C  CB  . GLU L  1 121 ? 42.638  154.178 69.377  1.00 14.16 ? 121  GLU L CB  1 
ATOM   12950 C  CG  . GLU L  1 121 ? 41.590  155.193 69.849  1.00 16.92 ? 121  GLU L CG  1 
ATOM   12951 C  CD  . GLU L  1 121 ? 41.682  155.442 71.358  1.00 21.43 ? 121  GLU L CD  1 
ATOM   12952 O  OE1 . GLU L  1 121 ? 42.548  154.830 72.043  1.00 20.14 ? 121  GLU L OE1 1 
ATOM   12953 O  OE2 . GLU L  1 121 ? 40.901  156.283 71.883  1.00 23.10 ? 121  GLU L OE2 1 
ATOM   12954 N  N   . LYS L  1 122 ? 44.602  156.007 67.898  1.00 13.92 ? 122  LYS L N   1 
ATOM   12955 C  CA  . LYS L  1 122 ? 45.063  157.386 67.754  1.00 15.28 ? 122  LYS L CA  1 
ATOM   12956 C  C   . LYS L  1 122 ? 46.355  157.460 66.959  1.00 14.18 ? 122  LYS L C   1 
ATOM   12957 O  O   . LYS L  1 122 ? 46.988  156.442 66.687  1.00 13.20 ? 122  LYS L O   1 
ATOM   12958 C  CB  . LYS L  1 122 ? 45.375  157.943 69.147  1.00 15.70 ? 122  LYS L CB  1 
ATOM   12959 C  CG  . LYS L  1 122 ? 44.253  157.889 70.144  1.00 21.07 ? 122  LYS L CG  1 
ATOM   12960 C  CD  . LYS L  1 122 ? 44.631  158.720 71.380  1.00 26.45 ? 122  LYS L CD  1 
ATOM   12961 C  CE  . LYS L  1 122 ? 43.645  158.491 72.539  1.00 31.95 ? 122  LYS L CE  1 
ATOM   12962 N  NZ  . LYS L  1 122 ? 44.170  159.022 73.848  1.00 32.75 ? 122  LYS L NZ  1 
ATOM   12963 N  N   . ALA L  1 123 ? 46.778  158.680 66.637  1.00 12.81 ? 123  ALA L N   1 
ATOM   12964 C  CA  . ALA L  1 123 ? 48.011  158.867 65.893  1.00 12.14 ? 123  ALA L CA  1 
ATOM   12965 C  C   . ALA L  1 123 ? 49.219  158.527 66.776  1.00 11.38 ? 123  ALA L C   1 
ATOM   12966 O  O   . ALA L  1 123 ? 49.198  158.729 68.009  1.00 12.00 ? 123  ALA L O   1 
ATOM   12967 C  CB  . ALA L  1 123 ? 48.132  160.326 65.406  1.00 12.28 ? 123  ALA L CB  1 
ATOM   12968 N  N   . ASP L  1 124 ? 50.238  157.993 66.126  1.00 9.71  ? 124  ASP L N   1 
ATOM   12969 C  CA  . ASP L  1 124 ? 51.526  157.706 66.746  1.00 10.19 ? 124  ASP L CA  1 
ATOM   12970 C  C   . ASP L  1 124 ? 52.290  159.046 66.753  1.00 9.81  ? 124  ASP L C   1 
ATOM   12971 O  O   . ASP L  1 124 ? 52.423  159.663 65.704  1.00 9.60  ? 124  ASP L O   1 
ATOM   12972 C  CB  . ASP L  1 124 ? 52.244  156.689 65.856  1.00 9.89  ? 124  ASP L CB  1 
ATOM   12973 C  CG  . ASP L  1 124 ? 53.567  156.204 66.424  1.00 12.34 ? 124  ASP L CG  1 
ATOM   12974 O  OD1 . ASP L  1 124 ? 54.256  156.964 67.178  1.00 8.20  ? 124  ASP L OD1 1 
ATOM   12975 O  OD2 . ASP L  1 124 ? 54.015  155.062 66.116  1.00 12.92 ? 124  ASP L OD2 1 
ATOM   12976 N  N   . ASP L  1 125 ? 52.738  159.503 67.934  1.00 9.58  ? 125  ASP L N   1 
ATOM   12977 C  CA  . ASP L  1 125 ? 53.489  160.772 68.042  1.00 10.39 ? 125  ASP L CA  1 
ATOM   12978 C  C   . ASP L  1 125 ? 54.991  160.655 67.681  1.00 10.31 ? 125  ASP L C   1 
ATOM   12979 O  O   . ASP L  1 125 ? 55.785  161.606 67.850  1.00 10.51 ? 125  ASP L O   1 
ATOM   12980 C  CB  . ASP L  1 125 ? 53.246  161.454 69.407  1.00 10.77 ? 125  ASP L CB  1 
ATOM   12981 C  CG  . ASP L  1 125 ? 53.952  160.761 70.581  1.00 9.54  ? 125  ASP L CG  1 
ATOM   12982 O  OD1 . ASP L  1 125 ? 54.880  159.925 70.371  1.00 10.09 ? 125  ASP L OD1 1 
ATOM   12983 O  OD2 . ASP L  1 125 ? 53.616  160.995 71.770  1.00 10.47 ? 125  ASP L OD2 1 
ATOM   12984 N  N   . LEU L  1 126 ? 55.358  159.499 67.135  1.00 8.71  ? 126  LEU L N   1 
ATOM   12985 C  CA  . LEU L  1 126 ? 56.684  159.248 66.570  1.00 9.98  ? 126  LEU L CA  1 
ATOM   12986 C  C   . LEU L  1 126 ? 57.793  159.328 67.626  1.00 8.58  ? 126  LEU L C   1 
ATOM   12987 O  O   . LEU L  1 126 ? 58.972  159.488 67.314  1.00 8.94  ? 126  LEU L O   1 
ATOM   12988 C  CB  . LEU L  1 126 ? 56.969  160.187 65.392  1.00 11.33 ? 126  LEU L CB  1 
ATOM   12989 C  CG  . LEU L  1 126 ? 55.854  160.227 64.325  1.00 12.87 ? 126  LEU L CG  1 
ATOM   12990 C  CD1 . LEU L  1 126 ? 56.364  161.030 63.135  1.00 17.45 ? 126  LEU L CD1 1 
ATOM   12991 C  CD2 . LEU L  1 126 ? 55.450  158.831 63.878  1.00 13.64 ? 126  LEU L CD2 1 
ATOM   12992 N  N   . GLY L  1 127 ? 57.399  159.216 68.887  1.00 8.50  ? 127  GLY L N   1 
ATOM   12993 C  CA  . GLY L  1 127 ? 58.367  159.162 69.966  1.00 8.49  ? 127  GLY L CA  1 
ATOM   12994 C  C   . GLY L  1 127 ? 58.820  160.527 70.431  1.00 8.90  ? 127  GLY L C   1 
ATOM   12995 O  O   . GLY L  1 127 ? 59.725  160.653 71.267  1.00 7.96  ? 127  GLY L O   1 
ATOM   12996 N  N   . LYS L  1 128 ? 58.103  161.548 69.985  1.00 8.49  ? 128  LYS L N   1 
ATOM   12997 C  CA  . LYS L  1 128 ? 58.538  162.913 70.267  1.00 9.44  ? 128  LYS L CA  1 
ATOM   12998 C  C   . LYS L  1 128 ? 57.544  163.716 71.089  1.00 8.38  ? 128  LYS L C   1 
ATOM   12999 O  O   . LYS L  1 128 ? 57.574  164.945 71.039  1.00 8.69  ? 128  LYS L O   1 
ATOM   13000 C  CB  . LYS L  1 128 ? 58.811  163.647 68.942  1.00 11.00 ? 128  LYS L CB  1 
ATOM   13001 C  CG  . LYS L  1 128 ? 59.779  162.958 67.984  1.00 12.77 ? 128  LYS L CG  1 
ATOM   13002 C  CD  . LYS L  1 128 ? 61.123  162.736 68.594  1.00 18.27 ? 128  LYS L CD  1 
ATOM   13003 C  CE  . LYS L  1 128 ? 62.217  162.610 67.494  1.00 25.51 ? 128  LYS L CE  1 
ATOM   13004 N  NZ  . LYS L  1 128 ? 61.690  162.289 66.129  1.00 26.27 ? 128  LYS L NZ  1 
ATOM   13005 N  N   . GLY L  1 129 ? 56.683  163.041 71.861  1.00 8.23  ? 129  GLY L N   1 
ATOM   13006 C  CA  . GLY L  1 129 ? 55.685  163.764 72.663  1.00 8.96  ? 129  GLY L CA  1 
ATOM   13007 C  C   . GLY L  1 129 ? 56.210  164.304 73.973  1.00 9.68  ? 129  GLY L C   1 
ATOM   13008 O  O   . GLY L  1 129 ? 55.501  164.988 74.715  1.00 9.26  ? 129  GLY L O   1 
ATOM   13009 N  N   . GLY L  1 130 ? 57.456  163.971 74.315  1.00 9.33  ? 130  GLY L N   1 
ATOM   13010 C  CA  . GLY L  1 130 ? 58.016  164.577 75.510  1.00 9.35  ? 130  GLY L CA  1 
ATOM   13011 C  C   . GLY L  1 130 ? 57.511  163.996 76.821  1.00 10.09 ? 130  GLY L C   1 
ATOM   13012 O  O   . GLY L  1 130 ? 57.417  164.703 77.835  1.00 9.53  ? 130  GLY L O   1 
ATOM   13013 N  N   . ASN L  1 131 ? 57.185  162.707 76.784  1.00 9.21  ? 131  ASN L N   1 
ATOM   13014 C  CA  . ASN L  1 131 ? 56.845  161.951 77.990  1.00 9.94  ? 131  ASN L CA  1 
ATOM   13015 C  C   . ASN L  1 131 ? 57.312  160.514 77.868  1.00 9.20  ? 131  ASN L C   1 
ATOM   13016 O  O   . ASN L  1 131 ? 57.674  160.048 76.773  1.00 9.47  ? 131  ASN L O   1 
ATOM   13017 C  CB  . ASN L  1 131 ? 55.366  162.050 78.339  1.00 9.06  ? 131  ASN L CB  1 
ATOM   13018 C  CG  . ASN L  1 131 ? 54.475  161.709 77.162  1.00 11.19 ? 131  ASN L CG  1 
ATOM   13019 O  OD1 . ASN L  1 131 ? 54.613  160.656 76.556  1.00 10.79 ? 131  ASN L OD1 1 
ATOM   13020 N  ND2 . ASN L  1 131 ? 53.545  162.605 76.847  1.00 16.25 ? 131  ASN L ND2 1 
ATOM   13021 N  N   . GLU L  1 132 ? 57.330  159.793 78.980  1.00 9.00  ? 132  GLU L N   1 
ATOM   13022 C  CA  . GLU L  1 132 ? 57.836  158.439 78.930  1.00 10.13 ? 132  GLU L CA  1 
ATOM   13023 C  C   . GLU L  1 132 ? 57.009  157.568 77.978  1.00 10.14 ? 132  GLU L C   1 
ATOM   13024 O  O   . GLU L  1 132 ? 57.564  156.776 77.194  1.00 10.17 ? 132  GLU L O   1 
ATOM   13025 C  CB  . GLU L  1 132 ? 57.904  157.847 80.349  1.00 10.24 ? 132  GLU L CB  1 
ATOM   13026 C  CG  . GLU L  1 132 ? 58.258  156.383 80.386  1.00 12.99 ? 132  GLU L CG  1 
ATOM   13027 C  CD  . GLU L  1 132 ? 58.184  155.791 81.800  1.00 15.95 ? 132  GLU L CD  1 
ATOM   13028 O  OE1 . GLU L  1 132 ? 57.563  156.393 82.710  1.00 18.69 ? 132  GLU L OE1 1 
ATOM   13029 O  OE2 . GLU L  1 132 ? 58.779  154.725 81.996  1.00 19.41 ? 132  GLU L OE2 1 
ATOM   13030 N  N   . GLU L  1 133 ? 55.689  157.748 77.999  1.00 9.50  ? 133  GLU L N   1 
ATOM   13031 C  CA  . GLU L  1 133 ? 54.834  156.897 77.187  1.00 11.18 ? 133  GLU L CA  1 
ATOM   13032 C  C   . GLU L  1 133 ? 55.178  157.067 75.715  1.00 9.54  ? 133  GLU L C   1 
ATOM   13033 O  O   . GLU L  1 133 ? 55.193  156.104 74.933  1.00 9.33  ? 133  GLU L O   1 
ATOM   13034 C  CB  . GLU L  1 133 ? 53.359  157.241 77.442  1.00 11.29 ? 133  GLU L CB  1 
ATOM   13035 C  CG  . GLU L  1 133 ? 52.404  156.277 76.753  1.00 15.54 ? 133  GLU L CG  1 
ATOM   13036 C  CD  . GLU L  1 133 ? 52.539  154.870 77.284  1.00 18.73 ? 133  GLU L CD  1 
ATOM   13037 O  OE1 . GLU L  1 133 ? 52.730  154.707 78.520  1.00 22.48 ? 133  GLU L OE1 1 
ATOM   13038 O  OE2 . GLU L  1 133 ? 52.465  153.933 76.462  1.00 20.90 ? 133  GLU L OE2 1 
ATOM   13039 N  N   . SER L  1 134 ? 55.487  158.294 75.337  1.00 9.28  ? 134  SER L N   1 
ATOM   13040 C  CA  . SER L  1 134 ? 55.811  158.557 73.934  1.00 9.06  ? 134  SER L CA  1 
ATOM   13041 C  C   . SER L  1 134 ? 56.960  157.682 73.467  1.00 9.03  ? 134  SER L C   1 
ATOM   13042 O  O   . SER L  1 134 ? 56.930  157.152 72.342  1.00 9.60  ? 134  SER L O   1 
ATOM   13043 C  CB  . SER L  1 134 ? 56.199  160.019 73.705  1.00 9.26  ? 134  SER L CB  1 
ATOM   13044 O  OG  . SER L  1 134 ? 56.602  160.174 72.349  1.00 8.05  ? 134  SER L OG  1 
ATOM   13045 N  N   . THR L  1 135 ? 57.949  157.514 74.343  1.00 7.81  ? 135  THR L N   1 
ATOM   13046 C  CA  . THR L  1 135 ? 59.165  156.766 74.021  1.00 9.21  ? 135  THR L CA  1 
ATOM   13047 C  C   . THR L  1 135 ? 58.949  155.284 74.052  1.00 8.64  ? 135  THR L C   1 
ATOM   13048 O  O   . THR L  1 135 ? 59.867  154.530 73.736  1.00 9.17  ? 135  THR L O   1 
ATOM   13049 C  CB  . THR L  1 135 ? 60.348  157.138 74.985  1.00 9.74  ? 135  THR L CB  1 
ATOM   13050 O  OG1 . THR L  1 135 ? 60.087  156.673 76.334  1.00 7.39  ? 135  THR L OG1 1 
ATOM   13051 C  CG2 . THR L  1 135 ? 60.512  158.673 75.082  1.00 7.51  ? 135  THR L CG2 1 
ATOM   13052 N  N   . LYS L  1 136 ? 57.749  154.854 74.440  1.00 9.60  ? 136  LYS L N   1 
ATOM   13053 C  CA  . LYS L  1 136 ? 57.437  153.419 74.456  1.00 10.12 ? 136  LYS L CA  1 
ATOM   13054 C  C   . LYS L  1 136 ? 56.480  153.034 73.351  1.00 10.85 ? 136  LYS L C   1 
ATOM   13055 O  O   . LYS L  1 136 ? 56.709  152.060 72.627  1.00 10.80 ? 136  LYS L O   1 
ATOM   13056 C  CB  . LYS L  1 136 ? 56.779  152.991 75.783  1.00 11.05 ? 136  LYS L CB  1 
ATOM   13057 C  CG  . LYS L  1 136 ? 57.612  153.403 77.003  1.00 14.74 ? 136  LYS L CG  1 
ATOM   13058 C  CD  . LYS L  1 136 ? 57.478  152.507 78.232  1.00 21.15 ? 136  LYS L CD  1 
ATOM   13059 C  CE  . LYS L  1 136 ? 56.063  152.180 78.630  1.00 23.95 ? 136  LYS L CE  1 
ATOM   13060 N  NZ  . LYS L  1 136 ? 55.979  151.720 80.066  1.00 24.86 ? 136  LYS L NZ  1 
ATOM   13061 N  N   . THR L  1 137 ? 55.390  153.772 73.236  1.00 9.85  ? 137  THR L N   1 
ATOM   13062 C  CA  . THR L  1 137 ? 54.335  153.354 72.323  1.00 11.53 ? 137  THR L CA  1 
ATOM   13063 C  C   . THR L  1 137 ? 53.946  154.464 71.368  1.00 11.71 ? 137  THR L C   1 
ATOM   13064 O  O   . THR L  1 137 ? 53.075  154.270 70.514  1.00 11.37 ? 137  THR L O   1 
ATOM   13065 C  CB  . THR L  1 137 ? 53.054  153.032 73.115  1.00 12.24 ? 137  THR L CB  1 
ATOM   13066 O  OG1 . THR L  1 137 ? 52.658  154.224 73.805  1.00 11.51 ? 137  THR L OG1 1 
ATOM   13067 C  CG2 . THR L  1 137 ? 53.289  152.044 74.266  1.00 13.53 ? 137  THR L CG2 1 
ATOM   13068 N  N   . GLY L  1 138 ? 54.494  155.658 71.531  1.00 9.89  ? 138  GLY L N   1 
ATOM   13069 C  CA  . GLY L  1 138 ? 54.059  156.736 70.648  1.00 9.72  ? 138  GLY L CA  1 
ATOM   13070 C  C   . GLY L  1 138 ? 52.691  157.319 71.035  1.00 8.87  ? 138  GLY L C   1 
ATOM   13071 O  O   . GLY L  1 138 ? 52.126  158.105 70.274  1.00 9.14  ? 138  GLY L O   1 
ATOM   13072 N  N   . ASN L  1 139 ? 52.158  156.923 72.193  1.00 8.85  ? 139  ASN L N   1 
ATOM   13073 C  CA  . ASN L  1 139 ? 50.841  157.387 72.664  1.00 10.55 ? 139  ASN L CA  1 
ATOM   13074 C  C   . ASN L  1 139 ? 49.741  157.107 71.659  1.00 11.42 ? 139  ASN L C   1 
ATOM   13075 O  O   . ASN L  1 139 ? 48.790  157.874 71.516  1.00 11.74 ? 139  ASN L O   1 
ATOM   13076 C  CB  . ASN L  1 139 ? 50.878  158.892 72.981  1.00 11.05 ? 139  ASN L CB  1 
ATOM   13077 C  CG  . ASN L  1 139 ? 51.628  159.184 74.244  1.00 13.60 ? 139  ASN L CG  1 
ATOM   13078 O  OD1 . ASN L  1 139 ? 51.235  158.740 75.332  1.00 16.24 ? 139  ASN L OD1 1 
ATOM   13079 N  ND2 . ASN L  1 139 ? 52.747  159.895 74.122  1.00 12.05 ? 139  ASN L ND2 1 
ATOM   13080 N  N   . ALA L  1 140 ? 49.839  155.963 70.991  1.00 11.42 ? 140  ALA L N   1 
ATOM   13081 C  CA  . ALA L  1 140 ? 48.864  155.665 69.947  1.00 11.90 ? 140  ALA L CA  1 
ATOM   13082 C  C   . ALA L  1 140 ? 47.544  155.114 70.484  1.00 12.81 ? 140  ALA L C   1 
ATOM   13083 O  O   . ALA L  1 140 ? 46.608  154.872 69.721  1.00 12.64 ? 140  ALA L O   1 
ATOM   13084 C  CB  . ALA L  1 140 ? 49.481  154.713 68.929  1.00 12.23 ? 140  ALA L CB  1 
ATOM   13085 N  N   . GLY L  1 141 ? 47.486  154.887 71.788  1.00 13.74 ? 141  GLY L N   1 
ATOM   13086 C  CA  . GLY L  1 141 ? 46.271  154.390 72.408  1.00 12.76 ? 141  GLY L CA  1 
ATOM   13087 C  C   . GLY L  1 141 ? 45.941  152.921 72.093  1.00 13.01 ? 141  GLY L C   1 
ATOM   13088 O  O   . GLY L  1 141 ? 46.810  152.071 71.826  1.00 11.73 ? 141  GLY L O   1 
ATOM   13089 N  N   . SER L  1 142 ? 44.653  152.635 72.135  1.00 12.68 ? 142  SER L N   1 
ATOM   13090 C  CA  . SER L  1 142 ? 44.182  151.257 72.042  1.00 12.62 ? 142  SER L CA  1 
ATOM   13091 C  C   . SER L  1 142 ? 44.423  150.579 70.698  1.00 12.06 ? 142  SER L C   1 
ATOM   13092 O  O   . SER L  1 142 ? 44.678  151.203 69.668  1.00 12.03 ? 142  SER L O   1 
ATOM   13093 C  CB  . SER L  1 142 ? 42.680  151.186 72.441  1.00 13.61 ? 142  SER L CB  1 
ATOM   13094 O  OG  . SER L  1 142 ? 41.854  151.598 71.352  1.00 15.56 ? 142  SER L OG  1 
ATOM   13095 N  N   . ARG L  1 143 ? 44.309  149.263 70.717  1.00 10.93 ? 143  ARG L N   1 
ATOM   13096 C  CA  . ARG L  1 143 ? 44.545  148.448 69.535  1.00 9.75  ? 143  ARG L CA  1 
ATOM   13097 C  C   . ARG L  1 143 ? 43.215  148.069 68.937  1.00 10.20 ? 143  ARG L C   1 
ATOM   13098 O  O   . ARG L  1 143 ? 42.447  147.327 69.546  1.00 10.77 ? 143  ARG L O   1 
ATOM   13099 C  CB  . ARG L  1 143 ? 45.290  147.204 69.959  1.00 9.39  ? 143  ARG L CB  1 
ATOM   13100 C  CG  . ARG L  1 143 ? 46.537  147.566 70.781  1.00 8.28  ? 143  ARG L CG  1 
ATOM   13101 C  CD  . ARG L  1 143 ? 47.330  146.339 71.333  1.00 11.59 ? 143  ARG L CD  1 
ATOM   13102 N  NE  . ARG L  1 143 ? 48.487  146.794 72.103  1.00 10.67 ? 143  ARG L NE  1 
ATOM   13103 C  CZ  . ARG L  1 143 ? 49.487  146.026 72.537  1.00 11.14 ? 143  ARG L CZ  1 
ATOM   13104 N  NH1 . ARG L  1 143 ? 49.492  144.713 72.285  1.00 9.78  ? 143  ARG L NH1 1 
ATOM   13105 N  NH2 . ARG L  1 143 ? 50.512  146.581 73.233  1.00 8.12  ? 143  ARG L NH2 1 
ATOM   13106 N  N   . LEU L  1 144 ? 42.951  148.577 67.754  1.00 9.55  ? 144  LEU L N   1 
ATOM   13107 C  CA  . LEU L  1 144 ? 41.635  148.393 67.122  1.00 10.01 ? 144  LEU L CA  1 
ATOM   13108 C  C   . LEU L  1 144 ? 41.479  147.097 66.379  1.00 9.30  ? 144  LEU L C   1 
ATOM   13109 O  O   . LEU L  1 144 ? 40.377  146.544 66.326  1.00 9.99  ? 144  LEU L O   1 
ATOM   13110 C  CB  . LEU L  1 144 ? 41.372  149.527 66.146  1.00 10.34 ? 144  LEU L CB  1 
ATOM   13111 C  CG  . LEU L  1 144 ? 41.439  150.956 66.715  1.00 12.72 ? 144  LEU L CG  1 
ATOM   13112 C  CD1 . LEU L  1 144 ? 41.108  151.952 65.603  1.00 11.42 ? 144  LEU L CD1 1 
ATOM   13113 C  CD2 . LEU L  1 144 ? 40.467  151.137 67.877  1.00 13.97 ? 144  LEU L CD2 1 
ATOM   13114 N  N   . ALA L  1 145 ? 42.561  146.660 65.744  1.00 8.70  ? 145  ALA L N   1 
ATOM   13115 C  CA  . ALA L  1 145 ? 42.559  145.431 64.962  1.00 8.93  ? 145  ALA L CA  1 
ATOM   13116 C  C   . ALA L  1 145 ? 43.993  144.931 64.847  1.00 8.54  ? 145  ALA L C   1 
ATOM   13117 O  O   . ALA L  1 145 ? 44.958  145.717 64.935  1.00 10.11 ? 145  ALA L O   1 
ATOM   13118 C  CB  . ALA L  1 145 ? 41.940  145.632 63.549  1.00 10.25 ? 145  ALA L CB  1 
ATOM   13119 N  N   . CYS L  1 146 ? 44.144  143.626 64.685  1.00 7.66  ? 146  CYS L N   1 
ATOM   13120 C  CA  . CYS L  1 146 ? 45.481  143.078 64.551  1.00 9.18  ? 146  CYS L CA  1 
ATOM   13121 C  C   . CYS L  1 146 ? 45.424  141.751 63.838  1.00 9.23  ? 146  CYS L C   1 
ATOM   13122 O  O   . CYS L  1 146 ? 44.343  141.198 63.606  1.00 7.62  ? 146  CYS L O   1 
ATOM   13123 C  CB  . CYS L  1 146 ? 46.124  142.900 65.938  1.00 9.67  ? 146  CYS L CB  1 
ATOM   13124 S  SG  . CYS L  1 146 ? 45.188  141.791 67.036  1.00 13.96 ? 146  CYS L SG  1 
ATOM   13125 N  N   . GLY L  1 147 ? 46.596  141.233 63.494  1.00 8.23  ? 147  GLY L N   1 
ATOM   13126 C  CA  . GLY L  1 147 ? 46.630  139.891 62.936  1.00 9.82  ? 147  GLY L CA  1 
ATOM   13127 C  C   . GLY L  1 147 ? 48.044  139.362 62.948  1.00 9.99  ? 147  GLY L C   1 
ATOM   13128 O  O   . GLY L  1 147 ? 48.984  140.139 63.017  1.00 10.21 ? 147  GLY L O   1 
ATOM   13129 N  N   . VAL L  1 148 ? 48.190  138.044 62.840  1.00 9.43  ? 148  VAL L N   1 
ATOM   13130 C  CA  . VAL L  1 148 ? 49.505  137.452 62.806  1.00 9.15  ? 148  VAL L CA  1 
ATOM   13131 C  C   . VAL L  1 148 ? 50.028  137.498 61.384  1.00 9.50  ? 148  VAL L C   1 
ATOM   13132 O  O   . VAL L  1 148 ? 49.300  137.256 60.417  1.00 10.68 ? 148  VAL L O   1 
ATOM   13133 C  CB  . VAL L  1 148 ? 49.493  135.986 63.326  1.00 8.92  ? 148  VAL L CB  1 
ATOM   13134 C  CG1 . VAL L  1 148 ? 50.888  135.446 63.330  1.00 8.73  ? 148  VAL L CG1 1 
ATOM   13135 C  CG2 . VAL L  1 148 ? 48.906  135.932 64.733  1.00 8.83  ? 148  VAL L CG2 1 
ATOM   13136 N  N   . ILE L  1 149 ? 51.287  137.873 61.247  1.00 9.05  ? 149  ILE L N   1 
ATOM   13137 C  CA  . ILE L  1 149 ? 51.917  137.993 59.932  1.00 9.25  ? 149  ILE L CA  1 
ATOM   13138 C  C   . ILE L  1 149 ? 52.312  136.585 59.472  1.00 8.67  ? 149  ILE L C   1 
ATOM   13139 O  O   . ILE L  1 149 ? 53.100  135.915 60.137  1.00 8.03  ? 149  ILE L O   1 
ATOM   13140 C  CB  . ILE L  1 149 ? 53.137  138.908 60.080  1.00 9.42  ? 149  ILE L CB  1 
ATOM   13141 C  CG1 . ILE L  1 149 ? 52.666  140.325 60.490  1.00 9.26  ? 149  ILE L CG1 1 
ATOM   13142 C  CG2 . ILE L  1 149 ? 53.956  138.937 58.799  1.00 8.08  ? 149  ILE L CG2 1 
ATOM   13143 C  CD1 . ILE L  1 149 ? 53.853  141.321 60.825  1.00 8.74  ? 149  ILE L CD1 1 
ATOM   13144 N  N   . GLY L  1 150 ? 51.789  136.164 58.314  1.00 9.20  ? 150  GLY L N   1 
ATOM   13145 C  CA  . GLY L  1 150 ? 51.959  134.791 57.883  1.00 10.02 ? 150  GLY L CA  1 
ATOM   13146 C  C   . GLY L  1 150 ? 52.679  134.723 56.550  1.00 10.35 ? 150  GLY L C   1 
ATOM   13147 O  O   . GLY L  1 150 ? 52.704  135.707 55.785  1.00 10.21 ? 150  GLY L O   1 
ATOM   13148 N  N   . ILE L  1 151 ? 53.309  133.587 56.305  1.00 10.33 ? 151  ILE L N   1 
ATOM   13149 C  CA  . ILE L  1 151 ? 53.976  133.362 55.020  1.00 11.09 ? 151  ILE L CA  1 
ATOM   13150 C  C   . ILE L  1 151 ? 52.956  133.275 53.916  1.00 12.18 ? 151  ILE L C   1 
ATOM   13151 O  O   . ILE L  1 151 ? 51.933  132.591 54.033  1.00 12.58 ? 151  ILE L O   1 
ATOM   13152 C  CB  . ILE L  1 151 ? 54.803  132.073 55.072  1.00 11.99 ? 151  ILE L CB  1 
ATOM   13153 C  CG1 . ILE L  1 151 ? 55.922  132.264 56.097  1.00 9.99  ? 151  ILE L CG1 1 
ATOM   13154 C  CG2 . ILE L  1 151 ? 55.340  131.724 53.675  1.00 8.84  ? 151  ILE L CG2 1 
ATOM   13155 C  CD1 . ILE L  1 151 ? 56.673  130.962 56.481  1.00 14.59 ? 151  ILE L CD1 1 
ATOM   13156 N  N   . ALA L  1 152 ? 53.230  133.967 52.818  1.00 13.34 ? 152  ALA L N   1 
ATOM   13157 C  CA  . ALA L  1 152 ? 52.310  133.985 51.710  1.00 14.16 ? 152  ALA L CA  1 
ATOM   13158 C  C   . ALA L  1 152 ? 52.947  133.366 50.474  1.00 16.07 ? 152  ALA L C   1 
ATOM   13159 O  O   . ALA L  1 152 ? 54.175  133.300 50.346  1.00 16.14 ? 152  ALA L O   1 
ATOM   13160 C  CB  . ALA L  1 152 ? 51.861  135.407 51.415  1.00 15.05 ? 152  ALA L CB  1 
ATOM   13161 N  N   . GLN L  1 153 ? 52.105  132.931 49.555  1.00 16.87 ? 153  GLN L N   1 
ATOM   13162 C  CA  . GLN L  1 153 ? 52.616  132.314 48.332  1.00 19.68 ? 153  GLN L CA  1 
ATOM   13163 C  C   . GLN L  1 153 ? 53.175  133.354 47.378  1.00 20.81 ? 153  GLN L C   1 
ATOM   13164 O  O   . GLN L  1 153 ? 52.498  134.370 47.202  1.00 21.96 ? 153  GLN L O   1 
ATOM   13165 C  CB  . GLN L  1 153 ? 51.504  131.543 47.640  1.00 18.84 ? 153  GLN L CB  1 
ATOM   13166 C  CG  . GLN L  1 153 ? 51.990  130.756 46.411  1.00 22.00 ? 153  GLN L CG  1 
ATOM   13167 C  CD  . GLN L  1 153 ? 50.925  129.819 45.882  1.00 24.07 ? 153  GLN L CD  1 
ATOM   13168 O  OE1 . GLN L  1 153 ? 49.760  130.203 45.786  1.00 26.17 ? 153  GLN L OE1 1 
ATOM   13169 N  NE2 . GLN L  1 153 ? 51.312  128.585 45.549  1.00 24.63 ? 153  GLN L NE2 1 
ATOM   13170 O  OXT . GLN L  1 153 ? 54.256  133.175 46.777  1.00 21.79 ? 153  GLN L OXT 1 
ATOM   13171 C  C   . THR M  1 2   ? 9.148   131.962 102.600 1.00 14.11 ? 2    THR M C   1 
ATOM   13172 O  O   . THR M  1 2   ? 8.873   133.142 102.285 1.00 12.65 ? 2    THR M O   1 
ATOM   13173 N  N   . LYS M  1 3   ? 8.261   130.971 102.506 1.00 12.35 ? 3    LYS M N   1 
ATOM   13174 C  CA  . LYS M  1 3   ? 6.898   131.217 102.052 1.00 12.65 ? 3    LYS M CA  1 
ATOM   13175 C  C   . LYS M  1 3   ? 5.967   130.564 103.062 1.00 11.76 ? 3    LYS M C   1 
ATOM   13176 O  O   . LYS M  1 3   ? 6.301   129.538 103.666 1.00 10.40 ? 3    LYS M O   1 
ATOM   13177 C  CB  . LYS M  1 3   ? 6.646   130.617 100.656 1.00 13.75 ? 3    LYS M CB  1 
ATOM   13178 C  CG  . LYS M  1 3   ? 7.302   131.392 99.492  1.00 17.79 ? 3    LYS M CG  1 
ATOM   13179 C  CD  . LYS M  1 3   ? 7.384   130.566 98.192  1.00 21.41 ? 3    LYS M CD  1 
ATOM   13180 C  CE  . LYS M  1 3   ? 7.785   131.451 96.985  1.00 25.84 ? 3    LYS M CE  1 
ATOM   13181 N  NZ  . LYS M  1 3   ? 8.015   130.676 95.698  1.00 28.37 ? 3    LYS M NZ  1 
ATOM   13182 N  N   . ALA M  1 4   ? 4.804   131.169 103.254 1.00 9.66  ? 4    ALA M N   1 
ATOM   13183 C  CA  . ALA M  1 4   ? 3.802   130.582 104.122 1.00 8.96  ? 4    ALA M CA  1 
ATOM   13184 C  C   . ALA M  1 4   ? 2.472   130.811 103.448 1.00 8.55  ? 4    ALA M C   1 
ATOM   13185 O  O   . ALA M  1 4   ? 2.379   131.587 102.513 1.00 8.52  ? 4    ALA M O   1 
ATOM   13186 C  CB  . ALA M  1 4   ? 3.811   131.229 105.485 1.00 9.09  ? 4    ALA M CB  1 
ATOM   13187 N  N   . VAL M  1 5   ? 1.432   130.159 103.939 1.00 8.92  ? 5    VAL M N   1 
ATOM   13188 C  CA  . VAL M  1 5   ? 0.147   130.288 103.310 1.00 9.05  ? 5    VAL M CA  1 
ATOM   13189 C  C   . VAL M  1 5   ? -0.904  130.070 104.368 1.00 9.22  ? 5    VAL M C   1 
ATOM   13190 O  O   . VAL M  1 5   ? -0.640  129.418 105.386 1.00 8.71  ? 5    VAL M O   1 
ATOM   13191 C  CB  . VAL M  1 5   ? 0.006   129.262 102.142 1.00 9.81  ? 5    VAL M CB  1 
ATOM   13192 C  CG1 . VAL M  1 5   ? -0.038  127.802 102.714 1.00 7.87  ? 5    VAL M CG1 1 
ATOM   13193 C  CG2 . VAL M  1 5   ? -1.223  129.594 101.303 1.00 10.57 ? 5    VAL M CG2 1 
ATOM   13194 N  N   . CYS M  1 6   ? -2.092  130.657 104.182 1.00 8.15  ? 6    CYS M N   1 
ATOM   13195 C  CA  . CYS M  1 6   ? -3.123  130.499 105.176 1.00 8.96  ? 6    CYS M CA  1 
ATOM   13196 C  C   . CYS M  1 6   ? -4.450  130.424 104.437 1.00 9.40  ? 6    CYS M C   1 
ATOM   13197 O  O   . CYS M  1 6   ? -4.719  131.270 103.606 1.00 9.75  ? 6    CYS M O   1 
ATOM   13198 C  CB  . CYS M  1 6   ? -3.153  131.728 106.109 1.00 9.44  ? 6    CYS M CB  1 
ATOM   13199 S  SG  . CYS M  1 6   ? -4.437  131.603 107.345 1.00 11.82 ? 6    CYS M SG  1 
ATOM   13200 N  N   . VAL M  1 7   ? -5.244  129.417 104.755 1.00 7.82  ? 7    VAL M N   1 
ATOM   13201 C  CA  . VAL M  1 7   ? -6.579  129.292 104.227 1.00 8.52  ? 7    VAL M CA  1 
ATOM   13202 C  C   . VAL M  1 7   ? -7.561  129.733 105.288 1.00 9.00  ? 7    VAL M C   1 
ATOM   13203 O  O   . VAL M  1 7   ? -7.599  129.148 106.367 1.00 8.81  ? 7    VAL M O   1 
ATOM   13204 C  CB  . VAL M  1 7   ? -6.889  127.832 103.867 1.00 7.95  ? 7    VAL M CB  1 
ATOM   13205 C  CG1 . VAL M  1 7   ? -8.372  127.746 103.412 1.00 8.24  ? 7    VAL M CG1 1 
ATOM   13206 C  CG2 . VAL M  1 7   ? -5.980  127.429 102.810 1.00 7.88  ? 7    VAL M CG2 1 
ATOM   13207 N  N   . LEU M  1 8   ? -8.286  130.821 105.009 1.00 8.46  ? 8    LEU M N   1 
ATOM   13208 C  CA  . LEU M  1 8   ? -9.254  131.377 105.941 1.00 9.64  ? 8    LEU M CA  1 
ATOM   13209 C  C   . LEU M  1 8   ? -10.629 130.795 105.709 1.00 10.38 ? 8    LEU M C   1 
ATOM   13210 O  O   . LEU M  1 8   ? -11.097 130.760 104.571 1.00 10.65 ? 8    LEU M O   1 
ATOM   13211 C  CB  . LEU M  1 8   ? -9.323  132.912 105.763 1.00 10.10 ? 8    LEU M CB  1 
ATOM   13212 C  CG  . LEU M  1 8   ? -8.060  133.754 106.079 1.00 12.79 ? 8    LEU M CG  1 
ATOM   13213 C  CD1 . LEU M  1 8   ? -6.881  133.415 105.179 1.00 16.31 ? 8    LEU M CD1 1 
ATOM   13214 C  CD2 . LEU M  1 8   ? -8.362  135.253 105.846 1.00 19.38 ? 8    LEU M CD2 1 
ATOM   13215 N  N   . LYS M  1 9   ? -11.240 130.327 106.792 1.00 9.52  ? 9    LYS M N   1 
ATOM   13216 C  CA  . LYS M  1 9   ? -12.605 129.810 106.793 1.00 11.96 ? 9    LYS M CA  1 
ATOM   13217 C  C   . LYS M  1 9   ? -13.286 130.171 108.101 1.00 10.63 ? 9    LYS M C   1 
ATOM   13218 O  O   . LYS M  1 9   ? -12.619 130.376 109.116 1.00 10.26 ? 9    LYS M O   1 
ATOM   13219 C  CB  . LYS M  1 9   ? -12.625 128.275 106.608 1.00 12.30 ? 9    LYS M CB  1 
ATOM   13220 C  CG  . LYS M  1 9   ? -12.192 127.818 105.212 1.00 19.10 ? 9    LYS M CG  1 
ATOM   13221 C  CD  . LYS M  1 9   ? -11.716 126.330 105.188 1.00 25.07 ? 9    LYS M CD  1 
ATOM   13222 C  CE  . LYS M  1 9   ? -11.692 125.740 103.750 1.00 28.32 ? 9    LYS M CE  1 
ATOM   13223 N  NZ  . LYS M  1 9   ? -11.850 126.791 102.676 1.00 32.06 ? 9    LYS M NZ  1 
ATOM   13224 N  N   . GLY M  1 10  ? -14.622 130.235 108.076 1.00 11.40 ? 10   GLY M N   1 
ATOM   13225 C  CA  . GLY M  1 10  ? -15.411 130.559 109.254 1.00 12.70 ? 10   GLY M CA  1 
ATOM   13226 C  C   . GLY M  1 10  ? -16.777 129.838 109.191 1.00 13.94 ? 10   GLY M C   1 
ATOM   13227 O  O   . GLY M  1 10  ? -16.944 128.863 108.466 1.00 14.26 ? 10   GLY M O   1 
ATOM   13228 N  N   . ASP M  1 11  ? -17.732 130.304 109.977 1.00 15.28 ? 11   ASP M N   1 
ATOM   13229 C  CA  . ASP M  1 11  ? -19.062 129.696 110.015 1.00 16.55 ? 11   ASP M CA  1 
ATOM   13230 C  C   . ASP M  1 11  ? -19.981 130.345 108.997 1.00 16.15 ? 11   ASP M C   1 
ATOM   13231 O  O   . ASP M  1 11  ? -21.080 129.861 108.754 1.00 16.39 ? 11   ASP M O   1 
ATOM   13232 C  CB  . ASP M  1 11  ? -19.687 129.885 111.403 1.00 17.76 ? 11   ASP M CB  1 
ATOM   13233 C  CG  . ASP M  1 11  ? -18.939 129.142 112.489 1.00 20.79 ? 11   ASP M CG  1 
ATOM   13234 O  OD1 . ASP M  1 11  ? -18.442 128.036 112.199 1.00 26.11 ? 11   ASP M OD1 1 
ATOM   13235 O  OD2 . ASP M  1 11  ? -18.806 129.587 113.658 1.00 24.83 ? 11   ASP M OD2 1 
ATOM   13236 N  N   . GLY M  1 12  ? -19.533 131.443 108.409 1.00 14.75 ? 12   GLY M N   1 
ATOM   13237 C  CA  . GLY M  1 12  ? -20.340 132.169 107.454 1.00 13.90 ? 12   GLY M CA  1 
ATOM   13238 C  C   . GLY M  1 12  ? -19.736 132.021 106.078 1.00 13.33 ? 12   GLY M C   1 
ATOM   13239 O  O   . GLY M  1 12  ? -19.077 131.020 105.770 1.00 13.37 ? 12   GLY M O   1 
ATOM   13240 N  N   . PRO M  1 13  ? -19.968 133.030 105.255 1.00 12.18 ? 13   PRO M N   1 
ATOM   13241 C  CA  . PRO M  1 13  ? -19.518 133.032 103.860 1.00 11.85 ? 13   PRO M CA  1 
ATOM   13242 C  C   . PRO M  1 13  ? -18.082 133.515 103.635 1.00 11.60 ? 13   PRO M C   1 
ATOM   13243 O  O   . PRO M  1 13  ? -17.602 133.495 102.503 1.00 11.95 ? 13   PRO M O   1 
ATOM   13244 C  CB  . PRO M  1 13  ? -20.411 134.064 103.219 1.00 12.16 ? 13   PRO M CB  1 
ATOM   13245 C  CG  . PRO M  1 13  ? -20.818 135.013 104.369 1.00 13.12 ? 13   PRO M CG  1 
ATOM   13246 C  CD  . PRO M  1 13  ? -20.677 134.255 105.648 1.00 11.69 ? 13   PRO M CD  1 
ATOM   13247 N  N   . VAL M  1 14  ? -17.408 133.947 104.681 1.00 10.32 ? 14   VAL M N   1 
ATOM   13248 C  CA  . VAL M  1 14  ? -16.111 134.548 104.487 1.00 9.37  ? 14   VAL M CA  1 
ATOM   13249 C  C   . VAL M  1 14  ? -15.033 133.470 104.329 1.00 9.94  ? 14   VAL M C   1 
ATOM   13250 O  O   . VAL M  1 14  ? -14.866 132.603 105.187 1.00 10.35 ? 14   VAL M O   1 
ATOM   13251 C  CB  . VAL M  1 14  ? -15.748 135.510 105.635 1.00 9.51  ? 14   VAL M CB  1 
ATOM   13252 C  CG1 . VAL M  1 14  ? -14.366 136.093 105.383 1.00 7.25  ? 14   VAL M CG1 1 
ATOM   13253 C  CG2 . VAL M  1 14  ? -16.791 136.665 105.754 1.00 8.75  ? 14   VAL M CG2 1 
ATOM   13254 N  N   . GLN M  1 15  ? -14.302 133.523 103.225 1.00 10.33 ? 15   GLN M N   1 
ATOM   13255 C  CA  . GLN M  1 15  ? -13.242 132.560 103.002 1.00 10.87 ? 15   GLN M CA  1 
ATOM   13256 C  C   . GLN M  1 15  ? -12.213 133.112 102.031 1.00 10.26 ? 15   GLN M C   1 
ATOM   13257 O  O   . GLN M  1 15  ? -12.523 133.958 101.173 1.00 10.15 ? 15   GLN M O   1 
ATOM   13258 C  CB  . GLN M  1 15  ? -13.795 131.221 102.476 1.00 12.41 ? 15   GLN M CB  1 
ATOM   13259 C  CG  . GLN M  1 15  ? -14.752 131.298 101.346 1.00 12.87 ? 15   GLN M CG  1 
ATOM   13260 C  CD  . GLN M  1 15  ? -15.363 129.904 101.074 1.00 19.89 ? 15   GLN M CD  1 
ATOM   13261 N  N   . GLY M  1 16  ? -10.984 132.646 102.154 1.00 9.32  ? 16   GLY M N   1 
ATOM   13262 C  CA  . GLY M  1 16  ? -9.985  133.130 101.218 1.00 9.94  ? 16   GLY M CA  1 
ATOM   13263 C  C   . GLY M  1 16  ? -8.665  132.442 101.452 1.00 9.01  ? 16   GLY M C   1 
ATOM   13264 O  O   . GLY M  1 16  ? -8.549  131.574 102.298 1.00 7.74  ? 16   GLY M O   1 
ATOM   13265 N  N   . ILE M  1 17  ? -7.665  132.886 100.718 1.00 8.72  ? 17   ILE M N   1 
ATOM   13266 C  CA  . ILE M  1 17  ? -6.326  132.330 100.792 1.00 9.15  ? 17   ILE M CA  1 
ATOM   13267 C  C   . ILE M  1 17  ? -5.376  133.514 100.814 1.00 8.39  ? 17   ILE M C   1 
ATOM   13268 O  O   . ILE M  1 17  ? -5.484  134.443 99.976  1.00 7.98  ? 17   ILE M O   1 
ATOM   13269 C  CB  . ILE M  1 17  ? -6.063  131.502 99.533  1.00 8.63  ? 17   ILE M CB  1 
ATOM   13270 C  CG1 . ILE M  1 17  ? -6.993  130.293 99.475  1.00 10.66 ? 17   ILE M CG1 1 
ATOM   13271 C  CG2 . ILE M  1 17  ? -4.563  131.153 99.418  1.00 10.73 ? 17   ILE M CG2 1 
ATOM   13272 C  CD1 . ILE M  1 17  ? -6.841  129.483 98.196  1.00 12.14 ? 17   ILE M CD1 1 
ATOM   13273 N  N   . ILE M  1 18  ? -4.460  133.483 101.761 1.00 7.50  ? 18   ILE M N   1 
ATOM   13274 C  CA  . ILE M  1 18  ? -3.466  134.534 101.923 1.00 8.10  ? 18   ILE M CA  1 
ATOM   13275 C  C   . ILE M  1 18  ? -2.096  133.897 101.899 1.00 8.54  ? 18   ILE M C   1 
ATOM   13276 O  O   . ILE M  1 18  ? -1.824  132.905 102.602 1.00 8.24  ? 18   ILE M O   1 
ATOM   13277 C  CB  . ILE M  1 18  ? -3.663  135.304 103.266 1.00 7.83  ? 18   ILE M CB  1 
ATOM   13278 C  CG1 . ILE M  1 18  ? -5.013  136.034 103.275 1.00 7.00  ? 18   ILE M CG1 1 
ATOM   13279 C  CG2 . ILE M  1 18  ? -2.498  136.278 103.491 1.00 8.14  ? 18   ILE M CG2 1 
ATOM   13280 C  CD1 . ILE M  1 18  ? -5.098  137.162 102.210 1.00 8.99  ? 18   ILE M CD1 1 
ATOM   13281 N  N   . ASN M  1 19  ? -1.254  134.500 101.080 1.00 8.92  ? 19   ASN M N   1 
ATOM   13282 C  CA  . ASN M  1 19  ? 0.116   134.067 100.868 1.00 9.96  ? 19   ASN M CA  1 
ATOM   13283 C  C   . ASN M  1 19  ? 1.039   135.028 101.581 1.00 10.44 ? 19   ASN M C   1 
ATOM   13284 O  O   . ASN M  1 19  ? 0.741   136.229 101.681 1.00 9.62  ? 19   ASN M O   1 
ATOM   13285 C  CB  . ASN M  1 19  ? 0.417   134.174 99.381  1.00 10.70 ? 19   ASN M CB  1 
ATOM   13286 C  CG  . ASN M  1 19  ? -0.556  133.386 98.530  1.00 11.47 ? 19   ASN M CG  1 
ATOM   13287 O  OD1 . ASN M  1 19  ? -1.388  133.950 97.802  1.00 13.07 ? 19   ASN M OD1 1 
ATOM   13288 N  ND2 . ASN M  1 19  ? -0.474  132.073 98.631  1.00 6.34  ? 19   ASN M ND2 1 
ATOM   13289 N  N   . PHE M  1 20  ? 2.132   134.492 102.126 1.00 10.34 ? 20   PHE M N   1 
ATOM   13290 C  CA  . PHE M  1 20  ? 3.188   135.277 102.725 1.00 10.24 ? 20   PHE M CA  1 
ATOM   13291 C  C   . PHE M  1 20  ? 4.524   134.919 102.042 1.00 11.17 ? 20   PHE M C   1 
ATOM   13292 O  O   . PHE M  1 20  ? 4.781   133.744 101.715 1.00 9.05  ? 20   PHE M O   1 
ATOM   13293 C  CB  . PHE M  1 20  ? 3.358   134.980 104.214 1.00 10.37 ? 20   PHE M CB  1 
ATOM   13294 C  CG  . PHE M  1 20  ? 2.118   135.185 105.027 1.00 9.43  ? 20   PHE M CG  1 
ATOM   13295 C  CD1 . PHE M  1 20  ? 1.094   134.257 104.969 1.00 11.29 ? 20   PHE M CD1 1 
ATOM   13296 C  CD2 . PHE M  1 20  ? 1.995   136.278 105.876 1.00 10.02 ? 20   PHE M CD2 1 
ATOM   13297 C  CE1 . PHE M  1 20  ? -0.039  134.410 105.743 1.00 11.17 ? 20   PHE M CE1 1 
ATOM   13298 C  CE2 . PHE M  1 20  ? 0.870   136.441 106.649 1.00 11.06 ? 20   PHE M CE2 1 
ATOM   13299 C  CZ  . PHE M  1 20  ? -0.165  135.491 106.562 1.00 9.19  ? 20   PHE M CZ  1 
ATOM   13300 N  N   . GLU M  1 21  ? 5.351   135.927 101.802 1.00 10.95 ? 21   GLU M N   1 
ATOM   13301 C  CA  . GLU M  1 21  ? 6.663   135.694 101.203 1.00 13.35 ? 21   GLU M CA  1 
ATOM   13302 C  C   . GLU M  1 21  ? 7.658   136.631 101.846 1.00 13.03 ? 21   GLU M C   1 
ATOM   13303 O  O   . GLU M  1 21  ? 7.399   137.821 101.947 1.00 12.12 ? 21   GLU M O   1 
ATOM   13304 C  CB  . GLU M  1 21  ? 6.657   135.937 99.688  1.00 13.67 ? 21   GLU M CB  1 
ATOM   13305 C  CG  . GLU M  1 21  ? 7.989   135.565 99.034  1.00 20.18 ? 21   GLU M CG  1 
ATOM   13306 C  CD  . GLU M  1 21  ? 7.927   135.474 97.507  1.00 27.03 ? 21   GLU M CD  1 
ATOM   13307 O  OE1 . GLU M  1 21  ? 6.917   135.897 96.903  1.00 32.81 ? 21   GLU M OE1 1 
ATOM   13308 O  OE2 . GLU M  1 21  ? 8.908   134.989 96.906  1.00 32.20 ? 21   GLU M OE2 1 
ATOM   13309 N  N   . GLN M  1 22  ? 8.818   136.094 102.253 1.00 13.02 ? 22   GLN M N   1 
ATOM   13310 C  CA  . GLN M  1 22  ? 9.867   136.901 102.855 1.00 14.58 ? 22   GLN M CA  1 
ATOM   13311 C  C   . GLN M  1 22  ? 11.186  136.489 102.193 1.00 17.13 ? 22   GLN M C   1 
ATOM   13312 O  O   . GLN M  1 22  ? 11.647  135.370 102.389 1.00 16.25 ? 22   GLN M O   1 
ATOM   13313 C  CB  . GLN M  1 22  ? 9.929   136.663 104.366 1.00 14.33 ? 22   GLN M CB  1 
ATOM   13314 C  CG  . GLN M  1 22  ? 10.901  137.601 105.114 1.00 12.16 ? 22   GLN M CG  1 
ATOM   13315 C  CD  . GLN M  1 22  ? 10.937  137.363 106.619 1.00 11.19 ? 22   GLN M CD  1 
ATOM   13316 O  OE1 . GLN M  1 22  ? 10.772  136.235 107.071 1.00 14.51 ? 22   GLN M OE1 1 
ATOM   13317 N  NE2 . GLN M  1 22  ? 11.197  138.410 107.387 1.00 11.55 ? 22   GLN M NE2 1 
ATOM   13318 N  N   . LYS M  1 23  ? 11.768  137.374 101.390 1.00 20.46 ? 23   LYS M N   1 
ATOM   13319 C  CA  . LYS M  1 23  ? 13.003  137.023 100.676 1.00 24.66 ? 23   LYS M CA  1 
ATOM   13320 C  C   . LYS M  1 23  ? 14.192  136.991 101.614 1.00 26.02 ? 23   LYS M C   1 
ATOM   13321 O  O   . LYS M  1 23  ? 15.038  136.096 101.562 1.00 27.32 ? 23   LYS M O   1 
ATOM   13322 C  CB  . LYS M  1 23  ? 13.284  138.034 99.557  1.00 25.07 ? 23   LYS M CB  1 
ATOM   13323 C  CG  . LYS M  1 23  ? 12.101  138.259 98.629  1.00 28.93 ? 23   LYS M CG  1 
ATOM   13324 C  CD  . LYS M  1 23  ? 12.474  139.133 97.437  1.00 32.72 ? 23   LYS M CD  1 
ATOM   13325 C  CE  . LYS M  1 23  ? 11.329  139.223 96.426  1.00 34.85 ? 23   LYS M CE  1 
ATOM   13326 N  NZ  . LYS M  1 23  ? 10.445  140.406 96.638  1.00 37.45 ? 23   LYS M NZ  1 
ATOM   13327 N  N   . GLU M  1 24  ? 14.239  137.966 102.497 1.00 28.05 ? 24   GLU M N   1 
ATOM   13328 C  C   . GLU M  1 24  ? 15.077  137.898 104.817 1.00 30.83 ? 24   GLU M C   1 
ATOM   13329 O  O   . GLU M  1 24  ? 14.050  138.344 105.346 1.00 30.48 ? 24   GLU M O   1 
ATOM   13330 N  N   . SER M  1 25  ? 16.018  137.228 105.466 1.00 31.49 ? 25   SER M N   1 
ATOM   13331 C  CA  . SER M  1 25  ? 15.961  136.915 106.892 1.00 32.48 ? 25   SER M CA  1 
ATOM   13332 C  C   . SER M  1 25  ? 15.424  137.991 107.857 1.00 32.48 ? 25   SER M C   1 
ATOM   13333 O  O   . SER M  1 25  ? 14.860  137.660 108.894 1.00 33.44 ? 25   SER M O   1 
ATOM   13334 N  N   . ASN M  1 26  ? 15.616  139.271 107.573 1.00 32.19 ? 26   ASN M N   1 
ATOM   13335 C  CA  . ASN M  1 26  ? 15.070  140.288 108.484 1.00 31.24 ? 26   ASN M CA  1 
ATOM   13336 C  C   . ASN M  1 26  ? 14.303  141.180 107.581 1.00 29.58 ? 26   ASN M C   1 
ATOM   13337 O  O   . ASN M  1 26  ? 14.381  142.412 107.664 1.00 30.34 ? 26   ASN M O   1 
ATOM   13338 N  N   . GLY M  1 27  ? 13.603  140.564 106.658 1.00 26.11 ? 27   GLY M N   1 
ATOM   13339 C  CA  . GLY M  1 27  ? 13.078  141.371 105.593 1.00 22.23 ? 27   GLY M CA  1 
ATOM   13340 C  C   . GLY M  1 27  ? 11.606  141.586 105.710 1.00 18.86 ? 27   GLY M C   1 
ATOM   13341 O  O   . GLY M  1 27  ? 10.946  140.997 106.580 1.00 17.82 ? 27   GLY M O   1 
ATOM   13342 N  N   . PRO M  1 28  ? 11.106  142.443 104.828 1.00 16.55 ? 28   PRO M N   1 
ATOM   13343 C  CA  . PRO M  1 28  ? 9.672   142.703 104.755 1.00 15.01 ? 28   PRO M CA  1 
ATOM   13344 C  C   . PRO M  1 28  ? 8.988   141.438 104.270 1.00 13.15 ? 28   PRO M C   1 
ATOM   13345 O  O   . PRO M  1 28  ? 9.544   140.665 103.481 1.00 11.91 ? 28   PRO M O   1 
ATOM   13346 C  CB  . PRO M  1 28  ? 9.556   143.783 103.675 1.00 13.87 ? 28   PRO M CB  1 
ATOM   13347 C  CG  . PRO M  1 28  ? 10.926  144.304 103.460 1.00 17.52 ? 28   PRO M CG  1 
ATOM   13348 C  CD  . PRO M  1 28  ? 11.872  143.219 103.831 1.00 16.54 ? 28   PRO M CD  1 
ATOM   13349 N  N   . VAL M  1 29  ? 7.774   141.235 104.754 1.00 11.50 ? 29   VAL M N   1 
ATOM   13350 C  CA  . VAL M  1 29  ? 6.984   140.095 104.368 1.00 11.02 ? 29   VAL M CA  1 
ATOM   13351 C  C   . VAL M  1 29  ? 5.896   140.641 103.459 1.00 11.67 ? 29   VAL M C   1 
ATOM   13352 O  O   . VAL M  1 29  ? 5.211   141.584 103.842 1.00 10.63 ? 29   VAL M O   1 
ATOM   13353 C  CB  . VAL M  1 29  ? 6.385   139.466 105.631 1.00 10.86 ? 29   VAL M CB  1 
ATOM   13354 C  CG1 . VAL M  1 29  ? 5.554   138.260 105.293 1.00 11.22 ? 29   VAL M CG1 1 
ATOM   13355 C  CG2 . VAL M  1 29  ? 7.530   139.077 106.619 1.00 10.36 ? 29   VAL M CG2 1 
ATOM   13356 N  N   . LYS M  1 30  ? 5.792   140.102 102.242 1.00 11.37 ? 30   LYS M N   1 
ATOM   13357 C  CA  . LYS M  1 30  ? 4.704   140.451 101.340 1.00 12.13 ? 30   LYS M CA  1 
ATOM   13358 C  C   . LYS M  1 30  ? 3.531   139.562 101.715 1.00 11.48 ? 30   LYS M C   1 
ATOM   13359 O  O   . LYS M  1 30  ? 3.697   138.361 101.937 1.00 11.29 ? 30   LYS M O   1 
ATOM   13360 C  CB  . LYS M  1 30  ? 5.038   140.188 99.872  1.00 12.38 ? 30   LYS M CB  1 
ATOM   13361 C  CG  . LYS M  1 30  ? 6.098   141.109 99.259  1.00 18.05 ? 30   LYS M CG  1 
ATOM   13362 C  CD  . LYS M  1 30  ? 6.058   141.080 97.715  1.00 22.37 ? 30   LYS M CD  1 
ATOM   13363 N  N   . VAL M  1 31  ? 2.351   140.153 101.832 1.00 11.37 ? 31   VAL M N   1 
ATOM   13364 C  CA  . VAL M  1 31  ? 1.167   139.348 102.107 1.00 10.58 ? 31   VAL M CA  1 
ATOM   13365 C  C   . VAL M  1 31  ? 0.091   139.726 101.120 1.00 11.38 ? 31   VAL M C   1 
ATOM   13366 O  O   . VAL M  1 31  ? -0.209  140.921 100.902 1.00 9.67  ? 31   VAL M O   1 
ATOM   13367 C  CB  . VAL M  1 31  ? 0.794   139.312 103.658 1.00 13.72 ? 31   VAL M CB  1 
ATOM   13368 C  CG1 . VAL M  1 31  ? 1.682   140.195 104.519 1.00 11.48 ? 31   VAL M CG1 1 
ATOM   13369 C  CG2 . VAL M  1 31  ? -0.663  139.271 104.005 1.00 7.47  ? 31   VAL M CG2 1 
ATOM   13370 N  N   . TRP M  1 32  ? -0.430  138.711 100.440 1.00 9.68  ? 32   TRP M N   1 
ATOM   13371 C  CA  . TRP M  1 32  ? -1.363  138.980 99.374  1.00 10.06 ? 32   TRP M CA  1 
ATOM   13372 C  C   . TRP M  1 32  ? -2.257  137.807 99.145  1.00 9.72  ? 32   TRP M C   1 
ATOM   13373 O  O   . TRP M  1 32  ? -1.893  136.667 99.446  1.00 9.36  ? 32   TRP M O   1 
ATOM   13374 C  CB  . TRP M  1 32  ? -0.637  139.357 98.100  1.00 11.12 ? 32   TRP M CB  1 
ATOM   13375 C  CG  . TRP M  1 32  ? -0.085  138.215 97.367  1.00 13.45 ? 32   TRP M CG  1 
ATOM   13376 C  CD1 . TRP M  1 32  ? -0.633  137.586 96.271  1.00 15.67 ? 32   TRP M CD1 1 
ATOM   13377 C  CD2 . TRP M  1 32  ? 1.127   137.533 97.653  1.00 16.50 ? 32   TRP M CD2 1 
ATOM   13378 N  NE1 . TRP M  1 32  ? 0.189   136.566 95.864  1.00 17.20 ? 32   TRP M NE1 1 
ATOM   13379 C  CE2 . TRP M  1 32  ? 1.271   136.506 96.699  1.00 14.30 ? 32   TRP M CE2 1 
ATOM   13380 C  CE3 . TRP M  1 32  ? 2.114   137.679 98.627  1.00 17.51 ? 32   TRP M CE3 1 
ATOM   13381 C  CZ2 . TRP M  1 32  ? 2.350   135.649 96.683  1.00 18.61 ? 32   TRP M CZ2 1 
ATOM   13382 C  CZ3 . TRP M  1 32  ? 3.196   136.814 98.614  1.00 20.90 ? 32   TRP M CZ3 1 
ATOM   13383 C  CH2 . TRP M  1 32  ? 3.305   135.807 97.639  1.00 19.81 ? 32   TRP M CH2 1 
ATOM   13384 N  N   . GLY M  1 33  ? -3.447  138.073 98.618  1.00 8.31  ? 33   GLY M N   1 
ATOM   13385 C  CA  . GLY M  1 33  ? -4.380  136.987 98.389  1.00 8.87  ? 33   GLY M CA  1 
ATOM   13386 C  C   . GLY M  1 33  ? -5.755  137.598 98.240  1.00 10.72 ? 33   GLY M C   1 
ATOM   13387 O  O   . GLY M  1 33  ? -5.884  138.800 98.030  1.00 10.98 ? 33   GLY M O   1 
ATOM   13388 N  N   . SER M  1 34  ? -6.760  136.755 98.295  1.00 10.91 ? 34   SER M N   1 
ATOM   13389 C  CA  . SER M  1 34  ? -8.115  137.185 98.033  1.00 13.15 ? 34   SER M CA  1 
ATOM   13390 C  C   . SER M  1 34  ? -9.004  136.588 99.097  1.00 11.79 ? 34   SER M C   1 
ATOM   13391 O  O   . SER M  1 34  ? -8.919  135.360 99.349  1.00 12.53 ? 34   SER M O   1 
ATOM   13392 C  CB  . SER M  1 34  ? -8.572  136.573 96.713  1.00 13.68 ? 34   SER M CB  1 
ATOM   13393 O  OG  . SER M  1 34  ? -9.849  137.085 96.403  1.00 18.16 ? 34   SER M OG  1 
ATOM   13394 N  N   . ILE M  1 35  ? -9.848  137.415 99.691  1.00 9.61  ? 35   ILE M N   1 
ATOM   13395 C  CA  . ILE M  1 35  ? -10.841 136.974 100.658 1.00 9.13  ? 35   ILE M CA  1 
ATOM   13396 C  C   . ILE M  1 35  ? -12.193 137.375 100.095 1.00 10.49 ? 35   ILE M C   1 
ATOM   13397 O  O   . ILE M  1 35  ? -12.391 138.529 99.743  1.00 10.09 ? 35   ILE M O   1 
ATOM   13398 C  CB  . ILE M  1 35  ? -10.672 137.670 102.004 1.00 10.00 ? 35   ILE M CB  1 
ATOM   13399 C  CG1 . ILE M  1 35  ? -9.222  137.511 102.506 1.00 11.53 ? 35   ILE M CG1 1 
ATOM   13400 C  CG2 . ILE M  1 35  ? -11.666 137.072 103.020 1.00 8.86  ? 35   ILE M CG2 1 
ATOM   13401 C  CD1 . ILE M  1 35  ? -8.910  138.263 103.896 1.00 13.37 ? 35   ILE M CD1 1 
ATOM   13402 N  N   . LYS M  1 36  ? -13.132 136.440 100.047 1.00 10.00 ? 36   LYS M N   1 
ATOM   13403 C  CA  . LYS M  1 36  ? -14.456 136.745 99.534  1.00 11.57 ? 36   LYS M CA  1 
ATOM   13404 C  C   . LYS M  1 36  ? -15.541 136.618 100.610 1.00 11.65 ? 36   LYS M C   1 
ATOM   13405 O  O   . LYS M  1 36  ? -15.302 136.115 101.721 1.00 11.23 ? 36   LYS M O   1 
ATOM   13406 C  CB  . LYS M  1 36  ? -14.764 135.856 98.324  1.00 12.10 ? 36   LYS M CB  1 
ATOM   13407 C  CG  . LYS M  1 36  ? -15.036 134.424 98.658  1.00 15.10 ? 36   LYS M CG  1 
ATOM   13408 C  CD  . LYS M  1 36  ? -15.331 133.574 97.363  1.00 18.69 ? 36   LYS M CD  1 
ATOM   13409 N  N   . GLY M  1 37  ? -16.728 137.126 100.285 1.00 11.59 ? 37   GLY M N   1 
ATOM   13410 C  CA  . GLY M  1 37  ? -17.861 137.045 101.184 1.00 10.97 ? 37   GLY M CA  1 
ATOM   13411 C  C   . GLY M  1 37  ? -17.944 138.126 102.252 1.00 11.43 ? 37   GLY M C   1 
ATOM   13412 O  O   . GLY M  1 37  ? -18.737 138.018 103.191 1.00 11.07 ? 37   GLY M O   1 
ATOM   13413 N  N   . LEU M  1 38  ? -17.134 139.166 102.126 1.00 10.43 ? 38   LEU M N   1 
ATOM   13414 C  CA  . LEU M  1 38  ? -17.123 140.228 103.124 1.00 9.98  ? 38   LEU M CA  1 
ATOM   13415 C  C   . LEU M  1 38  ? -18.068 141.388 102.785 1.00 11.01 ? 38   LEU M C   1 
ATOM   13416 O  O   . LEU M  1 38  ? -18.441 141.585 101.619 1.00 11.37 ? 38   LEU M O   1 
ATOM   13417 C  CB  . LEU M  1 38  ? -15.714 140.781 103.229 1.00 10.52 ? 38   LEU M CB  1 
ATOM   13418 C  CG  . LEU M  1 38  ? -14.664 139.874 103.873 1.00 9.26  ? 38   LEU M CG  1 
ATOM   13419 C  CD1 . LEU M  1 38  ? -13.262 140.277 103.357 1.00 9.76  ? 38   LEU M CD1 1 
ATOM   13420 C  CD2 . LEU M  1 38  ? -14.763 139.954 105.395 1.00 10.87 ? 38   LEU M CD2 1 
ATOM   13421 N  N   . THR M  1 39  ? -18.432 142.159 103.799 1.00 11.57 ? 39   THR M N   1 
ATOM   13422 C  CA  . THR M  1 39  ? -19.159 143.401 103.539 1.00 12.00 ? 39   THR M CA  1 
ATOM   13423 C  C   . THR M  1 39  ? -18.214 144.427 102.934 1.00 12.59 ? 39   THR M C   1 
ATOM   13424 O  O   . THR M  1 39  ? -17.026 144.506 103.303 1.00 11.55 ? 39   THR M O   1 
ATOM   13425 C  CB  . THR M  1 39  ? -19.788 143.983 104.810 1.00 11.94 ? 39   THR M CB  1 
ATOM   13426 O  OG1 . THR M  1 39  ? -18.781 144.185 105.815 1.00 9.81  ? 39   THR M OG1 1 
ATOM   13427 C  CG2 . THR M  1 39  ? -20.757 142.990 105.449 1.00 14.93 ? 39   THR M CG2 1 
ATOM   13428 N  N   . GLU M  1 40  ? -18.745 145.240 102.025 1.00 11.66 ? 40   GLU M N   1 
ATOM   13429 C  CA  . GLU M  1 40  ? -17.927 146.297 101.438 1.00 12.45 ? 40   GLU M CA  1 
ATOM   13430 C  C   . GLU M  1 40  ? -17.283 147.151 102.537 1.00 12.92 ? 40   GLU M C   1 
ATOM   13431 O  O   . GLU M  1 40  ? -17.938 147.507 103.520 1.00 14.28 ? 40   GLU M O   1 
ATOM   13432 C  CB  . GLU M  1 40  ? -18.803 147.198 100.553 1.00 13.04 ? 40   GLU M CB  1 
ATOM   13433 C  CG  . GLU M  1 40  ? -18.007 148.245 99.792  1.00 13.68 ? 40   GLU M CG  1 
ATOM   13434 C  CD  . GLU M  1 40  ? -18.855 149.040 98.806  1.00 18.46 ? 40   GLU M CD  1 
ATOM   13435 O  OE1 . GLU M  1 40  ? -20.071 148.809 98.742  1.00 15.05 ? 40   GLU M OE1 1 
ATOM   13436 O  OE2 . GLU M  1 40  ? -18.287 149.889 98.089  1.00 20.30 ? 40   GLU M OE2 1 
ATOM   13437 N  N   . GLY M  1 41  ? -16.014 147.496 102.384 1.00 11.29 ? 41   GLY M N   1 
ATOM   13438 C  CA  . GLY M  1 41  ? -15.389 148.405 103.322 1.00 10.62 ? 41   GLY M CA  1 
ATOM   13439 C  C   . GLY M  1 41  ? -14.229 147.763 104.084 1.00 10.67 ? 41   GLY M C   1 
ATOM   13440 O  O   . GLY M  1 41  ? -13.704 146.715 103.695 1.00 8.66  ? 41   GLY M O   1 
ATOM   13441 N  N   . LEU M  1 42  ? -13.841 148.410 105.183 1.00 10.20 ? 42   LEU M N   1 
ATOM   13442 C  CA  . LEU M  1 42  ? -12.652 147.989 105.940 1.00 9.93  ? 42   LEU M CA  1 
ATOM   13443 C  C   . LEU M  1 42  ? -12.911 146.871 106.903 1.00 9.26  ? 42   LEU M C   1 
ATOM   13444 O  O   . LEU M  1 42  ? -13.973 146.814 107.527 1.00 10.10 ? 42   LEU M O   1 
ATOM   13445 C  CB  . LEU M  1 42  ? -12.105 149.184 106.742 1.00 9.28  ? 42   LEU M CB  1 
ATOM   13446 C  CG  . LEU M  1 42  ? -11.612 150.402 105.982 1.00 11.39 ? 42   LEU M CG  1 
ATOM   13447 C  CD1 . LEU M  1 42  ? -11.477 151.568 107.000 1.00 14.13 ? 42   LEU M CD1 1 
ATOM   13448 C  CD2 . LEU M  1 42  ? -10.261 150.148 105.433 1.00 12.61 ? 42   LEU M CD2 1 
ATOM   13449 N  N   . HIS M  1 43  ? -11.929 145.983 107.036 1.00 7.56  ? 43   HIS M N   1 
ATOM   13450 C  CA  . HIS M  1 43  ? -12.016 144.872 107.965 1.00 7.87  ? 43   HIS M CA  1 
ATOM   13451 C  C   . HIS M  1 43  ? -10.681 144.646 108.663 1.00 6.75  ? 43   HIS M C   1 
ATOM   13452 O  O   . HIS M  1 43  ? -9.624  144.517 108.007 1.00 8.11  ? 43   HIS M O   1 
ATOM   13453 C  CB  . HIS M  1 43  ? -12.400 143.604 107.189 1.00 7.29  ? 43   HIS M CB  1 
ATOM   13454 C  CG  . HIS M  1 43  ? -13.797 143.639 106.667 1.00 8.52  ? 43   HIS M CG  1 
ATOM   13455 N  ND1 . HIS M  1 43  ? -14.870 143.236 107.422 1.00 11.80 ? 43   HIS M ND1 1 
ATOM   13456 C  CD2 . HIS M  1 43  ? -14.305 144.062 105.485 1.00 10.27 ? 43   HIS M CD2 1 
ATOM   13457 C  CE1 . HIS M  1 43  ? -15.986 143.404 106.731 1.00 9.57  ? 43   HIS M CE1 1 
ATOM   13458 N  NE2 . HIS M  1 43  ? -15.672 143.910 105.551 1.00 11.69 ? 43   HIS M NE2 1 
ATOM   13459 N  N   . GLY M  1 44  ? -10.705 144.548 109.986 1.00 7.04  ? 44   GLY M N   1 
ATOM   13460 C  CA  . GLY M  1 44  ? -9.466  144.329 110.753 1.00 5.40  ? 44   GLY M CA  1 
ATOM   13461 C  C   . GLY M  1 44  ? -8.754  143.030 110.317 1.00 7.55  ? 44   GLY M C   1 
ATOM   13462 O  O   . GLY M  1 44  ? -9.427  142.046 109.997 1.00 8.38  ? 44   GLY M O   1 
ATOM   13463 N  N   . PHE M  1 45  ? -7.422  143.007 110.337 1.00 6.18  ? 45   PHE M N   1 
ATOM   13464 C  CA  . PHE M  1 45  ? -6.695  141.880 109.719 1.00 7.17  ? 45   PHE M CA  1 
ATOM   13465 C  C   . PHE M  1 45  ? -5.484  141.699 110.594 1.00 6.69  ? 45   PHE M C   1 
ATOM   13466 O  O   . PHE M  1 45  ? -4.570  142.536 110.579 1.00 6.81  ? 45   PHE M O   1 
ATOM   13467 C  CB  . PHE M  1 45  ? -6.344  142.303 108.269 1.00 7.03  ? 45   PHE M CB  1 
ATOM   13468 C  CG  . PHE M  1 45  ? -5.673  141.249 107.411 1.00 6.19  ? 45   PHE M CG  1 
ATOM   13469 C  CD1 . PHE M  1 45  ? -6.356  140.117 107.020 1.00 8.04  ? 45   PHE M CD1 1 
ATOM   13470 C  CD2 . PHE M  1 45  ? -4.398  141.458 106.906 1.00 7.89  ? 45   PHE M CD2 1 
ATOM   13471 C  CE1 . PHE M  1 45  ? -5.761  139.176 106.157 1.00 7.95  ? 45   PHE M CE1 1 
ATOM   13472 C  CE2 . PHE M  1 45  ? -3.811  140.527 106.038 1.00 6.73  ? 45   PHE M CE2 1 
ATOM   13473 C  CZ  . PHE M  1 45  ? -4.498  139.379 105.689 1.00 7.52  ? 45   PHE M CZ  1 
ATOM   13474 N  N   . HIS M  1 46  ? -5.455  140.596 111.340 1.00 7.77  ? 46   HIS M N   1 
ATOM   13475 C  CA  . HIS M  1 46  ? -4.422  140.442 112.369 1.00 7.11  ? 46   HIS M CA  1 
ATOM   13476 C  C   . HIS M  1 46  ? -3.895  139.029 112.503 1.00 6.94  ? 46   HIS M C   1 
ATOM   13477 O  O   . HIS M  1 46  ? -4.622  138.053 112.261 1.00 7.17  ? 46   HIS M O   1 
ATOM   13478 C  CB  . HIS M  1 46  ? -5.032  140.710 113.739 1.00 8.76  ? 46   HIS M CB  1 
ATOM   13479 C  CG  . HIS M  1 46  ? -5.801  141.978 113.822 1.00 8.92  ? 46   HIS M CG  1 
ATOM   13480 N  ND1 . HIS M  1 46  ? -7.056  142.046 114.372 1.00 9.31  ? 46   HIS M ND1 1 
ATOM   13481 C  CD2 . HIS M  1 46  ? -5.494  143.236 113.431 1.00 10.19 ? 46   HIS M CD2 1 
ATOM   13482 C  CE1 . HIS M  1 46  ? -7.491  143.281 114.333 1.00 8.70  ? 46   HIS M CE1 1 
ATOM   13483 N  NE2 . HIS M  1 46  ? -6.567  144.023 113.761 1.00 7.31  ? 46   HIS M NE2 1 
ATOM   13484 N  N   . VAL M  1 47  ? -2.659  138.941 112.979 1.00 7.94  ? 47   VAL M N   1 
ATOM   13485 C  CA  . VAL M  1 47  ? -2.128  137.641 113.378 1.00 8.39  ? 47   VAL M CA  1 
ATOM   13486 C  C   . VAL M  1 47  ? -2.391  137.485 114.865 1.00 9.21  ? 47   VAL M C   1 
ATOM   13487 O  O   . VAL M  1 47  ? -1.952  138.321 115.692 1.00 8.81  ? 47   VAL M O   1 
ATOM   13488 C  CB  . VAL M  1 47  ? -0.628  137.543 113.095 1.00 8.56  ? 47   VAL M CB  1 
ATOM   13489 C  CG1 . VAL M  1 47  ? -0.098  136.178 113.526 1.00 9.42  ? 47   VAL M CG1 1 
ATOM   13490 C  CG2 . VAL M  1 47  ? -0.370  137.678 111.618 1.00 9.48  ? 47   VAL M CG2 1 
ATOM   13491 N  N   . HIS M  1 48  ? -3.127  136.434 115.219 1.00 8.91  ? 48   HIS M N   1 
ATOM   13492 C  CA  . HIS M  1 48  ? -3.454  136.160 116.616 1.00 8.85  ? 48   HIS M CA  1 
ATOM   13493 C  C   . HIS M  1 48  ? -2.484  135.146 117.175 1.00 9.05  ? 48   HIS M C   1 
ATOM   13494 O  O   . HIS M  1 48  ? -1.863  134.399 116.414 1.00 9.83  ? 48   HIS M O   1 
ATOM   13495 C  CB  . HIS M  1 48  ? -4.897  135.685 116.731 1.00 9.77  ? 48   HIS M CB  1 
ATOM   13496 C  CG  . HIS M  1 48  ? -5.893  136.794 116.621 1.00 9.16  ? 48   HIS M CG  1 
ATOM   13497 N  ND1 . HIS M  1 48  ? -6.844  137.049 117.591 1.00 8.31  ? 48   HIS M ND1 1 
ATOM   13498 C  CD2 . HIS M  1 48  ? -6.084  137.722 115.652 1.00 9.77  ? 48   HIS M CD2 1 
ATOM   13499 C  CE1 . HIS M  1 48  ? -7.576  138.094 117.218 1.00 9.06  ? 48   HIS M CE1 1 
ATOM   13500 N  NE2 . HIS M  1 48  ? -7.135  138.507 116.049 1.00 9.75  ? 48   HIS M NE2 1 
ATOM   13501 N  N   . GLU M  1 49  ? -2.367  135.081 118.501 1.00 9.18  ? 49   GLU M N   1 
ATOM   13502 C  CA  . GLU M  1 49  ? -1.258  134.364 119.110 1.00 9.62  ? 49   GLU M CA  1 
ATOM   13503 C  C   . GLU M  1 49  ? -1.146  132.856 118.824 1.00 9.62  ? 49   GLU M C   1 
ATOM   13504 O  O   . GLU M  1 49  ? -0.051  132.353 118.493 1.00 8.70  ? 49   GLU M O   1 
ATOM   13505 C  CB  . GLU M  1 49  ? -1.240  134.614 120.616 1.00 9.23  ? 49   GLU M CB  1 
ATOM   13506 C  CG  . GLU M  1 49  ? -0.037  133.981 121.301 1.00 10.92 ? 49   GLU M CG  1 
ATOM   13507 C  CD  . GLU M  1 49  ? 0.011   134.321 122.785 1.00 15.49 ? 49   GLU M CD  1 
ATOM   13508 O  OE1 . GLU M  1 49  ? -0.875  135.073 123.255 1.00 16.11 ? 49   GLU M OE1 1 
ATOM   13509 O  OE2 . GLU M  1 49  ? 0.934   133.842 123.488 1.00 15.30 ? 49   GLU M OE2 1 
ATOM   13510 N  N   . PHE M  1 50  ? -2.261  132.149 118.997 1.00 10.30 ? 50   PHE M N   1 
ATOM   13511 C  CA  . PHE M  1 50  ? -2.292  130.678 118.922 1.00 10.58 ? 50   PHE M CA  1 
ATOM   13512 C  C   . PHE M  1 50  ? -2.826  130.115 117.618 1.00 10.78 ? 50   PHE M C   1 
ATOM   13513 O  O   . PHE M  1 50  ? -3.766  130.670 117.021 1.00 11.87 ? 50   PHE M O   1 
ATOM   13514 C  CB  . PHE M  1 50  ? -3.108  130.108 120.102 1.00 10.57 ? 50   PHE M CB  1 
ATOM   13515 C  CG  . PHE M  1 50  ? -2.670  130.648 121.432 1.00 11.89 ? 50   PHE M CG  1 
ATOM   13516 C  CD1 . PHE M  1 50  ? -1.384  130.396 121.908 1.00 13.47 ? 50   PHE M CD1 1 
ATOM   13517 C  CD2 . PHE M  1 50  ? -3.508  131.467 122.175 1.00 13.11 ? 50   PHE M CD2 1 
ATOM   13518 C  CE1 . PHE M  1 50  ? -0.954  130.938 123.118 1.00 12.98 ? 50   PHE M CE1 1 
ATOM   13519 C  CE2 . PHE M  1 50  ? -3.079  131.996 123.401 1.00 13.43 ? 50   PHE M CE2 1 
ATOM   13520 C  CZ  . PHE M  1 50  ? -1.800  131.727 123.858 1.00 13.01 ? 50   PHE M CZ  1 
ATOM   13521 N  N   . GLY M  1 51  ? -2.213  129.023 117.162 1.00 11.06 ? 51   GLY M N   1 
ATOM   13522 C  CA  . GLY M  1 51  ? -2.670  128.350 115.967 1.00 11.62 ? 51   GLY M CA  1 
ATOM   13523 C  C   . GLY M  1 51  ? -3.672  127.293 116.390 1.00 12.39 ? 51   GLY M C   1 
ATOM   13524 O  O   . GLY M  1 51  ? -3.592  126.147 115.970 1.00 13.36 ? 51   GLY M O   1 
ATOM   13525 N  N   . ASP M  1 52  ? -4.621  127.693 117.235 1.00 12.24 ? 52   ASP M N   1 
ATOM   13526 C  CA  . ASP M  1 52  ? -5.606  126.779 117.792 1.00 12.31 ? 52   ASP M CA  1 
ATOM   13527 C  C   . ASP M  1 52  ? -6.987  127.182 117.321 1.00 12.64 ? 52   ASP M C   1 
ATOM   13528 O  O   . ASP M  1 52  ? -7.501  128.257 117.684 1.00 12.26 ? 52   ASP M O   1 
ATOM   13529 C  CB  . ASP M  1 52  ? -5.505  126.855 119.323 1.00 12.58 ? 52   ASP M CB  1 
ATOM   13530 C  CG  . ASP M  1 52  ? -6.479  125.934 120.048 1.00 13.32 ? 52   ASP M CG  1 
ATOM   13531 O  OD1 . ASP M  1 52  ? -7.461  125.427 119.459 1.00 12.19 ? 52   ASP M OD1 1 
ATOM   13532 O  OD2 . ASP M  1 52  ? -6.314  125.669 121.254 1.00 13.47 ? 52   ASP M OD2 1 
ATOM   13533 N  N   . ASN M  1 53  ? -7.575  126.335 116.496 1.00 12.10 ? 53   ASN M N   1 
ATOM   13534 C  CA  . ASN M  1 53  ? -8.906  126.572 115.989 1.00 13.76 ? 53   ASN M CA  1 
ATOM   13535 C  C   . ASN M  1 53  ? -9.882  125.547 116.563 1.00 12.62 ? 53   ASN M C   1 
ATOM   13536 O  O   . ASN M  1 53  ? -10.915 125.295 115.957 1.00 12.16 ? 53   ASN M O   1 
ATOM   13537 C  CB  . ASN M  1 53  ? -8.885  126.443 114.451 1.00 14.99 ? 53   ASN M CB  1 
ATOM   13538 C  CG  . ASN M  1 53  ? -10.215 126.796 113.805 1.00 19.77 ? 53   ASN M CG  1 
ATOM   13539 O  OD1 . ASN M  1 53  ? -10.801 125.972 113.063 1.00 27.27 ? 53   ASN M OD1 1 
ATOM   13540 N  ND2 . ASN M  1 53  ? -10.707 128.016 114.064 1.00 24.53 ? 53   ASN M ND2 1 
ATOM   13541 N  N   . THR M  1 54  ? -9.554  124.935 117.704 1.00 11.86 ? 54   THR M N   1 
ATOM   13542 C  CA  . THR M  1 54  ? -10.420 123.899 118.247 1.00 11.91 ? 54   THR M CA  1 
ATOM   13543 C  C   . THR M  1 54  ? -11.835 124.317 118.578 1.00 12.72 ? 54   THR M C   1 
ATOM   13544 O  O   . THR M  1 54  ? -12.759 123.509 118.433 1.00 13.34 ? 54   THR M O   1 
ATOM   13545 C  CB  . THR M  1 54  ? -9.806  123.168 119.465 1.00 12.44 ? 54   THR M CB  1 
ATOM   13546 O  OG1 . THR M  1 54  ? -9.465  124.114 120.495 1.00 10.41 ? 54   THR M OG1 1 
ATOM   13547 C  CG2 . THR M  1 54  ? -8.503  122.505 119.082 1.00 12.76 ? 54   THR M CG2 1 
ATOM   13548 N  N   . ALA M  1 55  ? -12.008 125.522 119.093 1.00 13.30 ? 55   ALA M N   1 
ATOM   13549 C  CA  . ALA M  1 55  ? -13.357 126.015 119.374 1.00 14.47 ? 55   ALA M CA  1 
ATOM   13550 C  C   . ALA M  1 55  ? -13.716 127.125 118.383 1.00 14.67 ? 55   ALA M C   1 
ATOM   13551 O  O   . ALA M  1 55  ? -14.452 128.035 118.728 1.00 16.11 ? 55   ALA M O   1 
ATOM   13552 C  CB  . ALA M  1 55  ? -13.472 126.544 120.812 1.00 14.58 ? 55   ALA M CB  1 
ATOM   13553 N  N   . GLY M  1 56  ? -13.202 127.037 117.164 1.00 13.93 ? 56   GLY M N   1 
ATOM   13554 C  CA  . GLY M  1 56  ? -13.430 128.074 116.164 1.00 14.37 ? 56   GLY M CA  1 
ATOM   13555 C  C   . GLY M  1 56  ? -12.389 129.183 116.294 1.00 14.08 ? 56   GLY M C   1 
ATOM   13556 O  O   . GLY M  1 56  ? -11.354 129.006 116.956 1.00 13.19 ? 56   GLY M O   1 
ATOM   13557 N  N   . CYS M  1 57  ? -12.646 130.348 115.691 1.00 13.77 ? 57   CYS M N   1 
ATOM   13558 C  CA  . CYS M  1 57  ? -11.648 131.413 115.738 1.00 14.11 ? 57   CYS M CA  1 
ATOM   13559 C  C   . CYS M  1 57  ? -11.319 131.931 117.158 1.00 14.58 ? 57   CYS M C   1 
ATOM   13560 O  O   . CYS M  1 57  ? -10.261 132.529 117.389 1.00 13.25 ? 57   CYS M O   1 
ATOM   13561 C  CB  . CYS M  1 57  ? -12.078 132.570 114.823 1.00 14.19 ? 57   CYS M CB  1 
ATOM   13562 S  SG  . CYS M  1 57  ? -12.089 132.016 113.085 1.00 18.90 ? 57   CYS M SG  1 
ATOM   13563 N  N   . THR M  1 58  ? -12.223 131.684 118.097 1.00 14.89 ? 58   THR M N   1 
ATOM   13564 C  CA  . THR M  1 58  ? -12.066 132.169 119.472 1.00 16.51 ? 58   THR M CA  1 
ATOM   13565 C  C   . THR M  1 58  ? -10.821 131.593 120.102 1.00 15.18 ? 58   THR M C   1 
ATOM   13566 O  O   . THR M  1 58  ? -10.156 132.239 120.923 1.00 14.77 ? 58   THR M O   1 
ATOM   13567 C  CB  . THR M  1 58  ? -13.264 131.700 120.313 1.00 17.60 ? 58   THR M CB  1 
ATOM   13568 O  OG1 . THR M  1 58  ? -14.459 132.303 119.791 1.00 23.50 ? 58   THR M OG1 1 
ATOM   13569 C  CG2 . THR M  1 58  ? -13.157 132.266 121.704 1.00 19.49 ? 58   THR M CG2 1 
ATOM   13570 N  N   . SER M  1 59  ? -10.525 130.349 119.732 1.00 13.59 ? 59   SER M N   1 
ATOM   13571 C  CA  . SER M  1 59  ? -9.366  129.651 120.289 1.00 13.33 ? 59   SER M CA  1 
ATOM   13572 C  C   . SER M  1 59  ? -8.031  130.267 119.928 1.00 11.73 ? 59   SER M C   1 
ATOM   13573 O  O   . SER M  1 59  ? -7.033  129.946 120.538 1.00 11.16 ? 59   SER M O   1 
ATOM   13574 C  CB  . SER M  1 59  ? -9.350  128.178 119.823 1.00 13.21 ? 59   SER M CB  1 
ATOM   13575 O  OG  . SER M  1 59  ? -10.459 127.531 120.352 1.00 16.53 ? 59   SER M OG  1 
ATOM   13576 N  N   . ALA M  1 60  ? -7.993  131.150 118.945 1.00 11.80 ? 60   ALA M N   1 
ATOM   13577 C  CA  . ALA M  1 60  ? -6.717  131.722 118.521 1.00 12.25 ? 60   ALA M CA  1 
ATOM   13578 C  C   . ALA M  1 60  ? -6.171  132.698 119.564 1.00 12.61 ? 60   ALA M C   1 
ATOM   13579 O  O   . ALA M  1 60  ? -5.000  133.125 119.498 1.00 10.90 ? 60   ALA M O   1 
ATOM   13580 C  CB  . ALA M  1 60  ? -6.893  132.438 117.185 1.00 13.11 ? 60   ALA M CB  1 
ATOM   13581 N  N   . GLY M  1 61  ? -7.030  133.044 120.528 1.00 11.97 ? 61   GLY M N   1 
ATOM   13582 C  CA  . GLY M  1 61  ? -6.647  133.987 121.560 1.00 11.66 ? 61   GLY M CA  1 
ATOM   13583 C  C   . GLY M  1 61  ? -6.488  135.403 121.048 1.00 11.77 ? 61   GLY M C   1 
ATOM   13584 O  O   . GLY M  1 61  ? -7.069  135.782 120.032 1.00 11.33 ? 61   GLY M O   1 
ATOM   13585 N  N   . PRO M  1 62  ? -5.698  136.186 121.772 1.00 11.62 ? 62   PRO M N   1 
ATOM   13586 C  CA  . PRO M  1 62  ? -5.499  137.618 121.475 1.00 12.70 ? 62   PRO M CA  1 
ATOM   13587 C  C   . PRO M  1 62  ? -4.464  137.871 120.364 1.00 12.40 ? 62   PRO M C   1 
ATOM   13588 O  O   . PRO M  1 62  ? -3.980  136.912 119.751 1.00 12.24 ? 62   PRO M O   1 
ATOM   13589 C  CB  . PRO M  1 62  ? -5.012  138.170 122.815 1.00 12.58 ? 62   PRO M CB  1 
ATOM   13590 C  CG  . PRO M  1 62  ? -4.256  136.983 123.439 1.00 11.79 ? 62   PRO M CG  1 
ATOM   13591 C  CD  . PRO M  1 62  ? -4.948  135.746 122.959 1.00 11.99 ? 62   PRO M CD  1 
ATOM   13592 N  N   . HIS M  1 63  ? -4.161  139.139 120.083 1.00 12.61 ? 63   HIS M N   1 
ATOM   13593 C  CA  . HIS M  1 63  ? -3.175  139.453 119.032 1.00 12.10 ? 63   HIS M CA  1 
ATOM   13594 C  C   . HIS M  1 63  ? -1.819  138.982 119.420 1.00 12.45 ? 63   HIS M C   1 
ATOM   13595 O  O   . HIS M  1 63  ? -1.470  139.010 120.600 1.00 12.91 ? 63   HIS M O   1 
ATOM   13596 C  CB  . HIS M  1 63  ? -3.122  140.973 118.705 1.00 12.40 ? 63   HIS M CB  1 
ATOM   13597 C  CG  . HIS M  1 63  ? -4.385  141.468 118.080 1.00 13.09 ? 63   HIS M CG  1 
ATOM   13598 N  ND1 . HIS M  1 63  ? -4.604  142.784 117.739 1.00 13.51 ? 63   HIS M ND1 1 
ATOM   13599 C  CD2 . HIS M  1 63  ? -5.517  140.803 117.769 1.00 12.57 ? 63   HIS M CD2 1 
ATOM   13600 C  CE1 . HIS M  1 63  ? -5.825  142.909 117.251 1.00 15.59 ? 63   HIS M CE1 1 
ATOM   13601 N  NE2 . HIS M  1 63  ? -6.393  141.717 117.244 1.00 18.66 ? 63   HIS M NE2 1 
ATOM   13602 N  N   . PHE M  1 64  ? -1.047  138.539 118.430 1.00 11.49 ? 64   PHE M N   1 
ATOM   13603 C  CA  . PHE M  1 64  ? 0.311   138.128 118.676 1.00 12.08 ? 64   PHE M CA  1 
ATOM   13604 C  C   . PHE M  1 64  ? 1.034   139.347 119.177 1.00 12.45 ? 64   PHE M C   1 
ATOM   13605 O  O   . PHE M  1 64  ? 1.159   140.331 118.449 1.00 12.57 ? 64   PHE M O   1 
ATOM   13606 C  CB  . PHE M  1 64  ? 0.935   137.618 117.387 1.00 12.31 ? 64   PHE M CB  1 
ATOM   13607 C  CG  . PHE M  1 64  ? 2.338   137.094 117.555 1.00 12.57 ? 64   PHE M CG  1 
ATOM   13608 C  CD1 . PHE M  1 64  ? 2.720   136.416 118.722 1.00 10.02 ? 64   PHE M CD1 1 
ATOM   13609 C  CD2 . PHE M  1 64  ? 3.276   137.297 116.562 1.00 9.28  ? 64   PHE M CD2 1 
ATOM   13610 C  CE1 . PHE M  1 64  ? 3.989   135.928 118.859 1.00 11.84 ? 64   PHE M CE1 1 
ATOM   13611 C  CE2 . PHE M  1 64  ? 4.559   136.823 116.694 1.00 12.34 ? 64   PHE M CE2 1 
ATOM   13612 C  CZ  . PHE M  1 64  ? 4.922   136.124 117.840 1.00 13.67 ? 64   PHE M CZ  1 
ATOM   13613 N  N   . ASN M  1 65  ? 1.545   139.262 120.404 1.00 13.42 ? 65   ASN M N   1 
ATOM   13614 C  CA  . ASN M  1 65  ? 2.108   140.433 121.092 1.00 14.13 ? 65   ASN M CA  1 
ATOM   13615 C  C   . ASN M  1 65  ? 3.257   140.075 122.060 1.00 15.40 ? 65   ASN M C   1 
ATOM   13616 O  O   . ASN M  1 65  ? 3.139   140.228 123.288 1.00 16.80 ? 65   ASN M O   1 
ATOM   13617 C  CB  . ASN M  1 65  ? 0.983   141.073 121.878 1.00 13.87 ? 65   ASN M CB  1 
ATOM   13618 C  CG  . ASN M  1 65  ? 1.389   142.376 122.539 1.00 14.87 ? 65   ASN M CG  1 
ATOM   13619 O  OD1 . ASN M  1 65  ? 2.303   143.069 122.083 1.00 10.24 ? 65   ASN M OD1 1 
ATOM   13620 N  ND2 . ASN M  1 65  ? 0.680   142.732 123.617 1.00 16.62 ? 65   ASN M ND2 1 
ATOM   13621 N  N   . PRO M  1 66  ? 4.370   139.607 121.515 1.00 15.37 ? 66   PRO M N   1 
ATOM   13622 C  CA  . PRO M  1 66  ? 5.507   139.181 122.338 1.00 15.43 ? 66   PRO M CA  1 
ATOM   13623 C  C   . PRO M  1 66  ? 6.199   140.352 123.040 1.00 16.51 ? 66   PRO M C   1 
ATOM   13624 O  O   . PRO M  1 66  ? 6.857   140.108 124.057 1.00 16.06 ? 66   PRO M O   1 
ATOM   13625 C  CB  . PRO M  1 66  ? 6.460   138.571 121.315 1.00 15.08 ? 66   PRO M CB  1 
ATOM   13626 C  CG  . PRO M  1 66  ? 6.105   139.287 120.038 1.00 15.93 ? 66   PRO M CG  1 
ATOM   13627 C  CD  . PRO M  1 66  ? 4.607   139.406 120.072 1.00 14.94 ? 66   PRO M CD  1 
ATOM   13628 N  N   . LEU M  1 67  ? 6.085   141.567 122.503 1.00 15.94 ? 67   LEU M N   1 
ATOM   13629 C  CA  . LEU M  1 67  ? 6.725   142.736 123.126 1.00 16.55 ? 67   LEU M CA  1 
ATOM   13630 C  C   . LEU M  1 67  ? 5.806   143.429 124.116 1.00 16.39 ? 67   LEU M C   1 
ATOM   13631 O  O   . LEU M  1 67  ? 6.173   144.455 124.697 1.00 16.36 ? 67   LEU M O   1 
ATOM   13632 C  CB  . LEU M  1 67  ? 7.237   143.732 122.092 1.00 17.01 ? 67   LEU M CB  1 
ATOM   13633 C  CG  . LEU M  1 67  ? 8.222   143.134 121.092 1.00 17.77 ? 67   LEU M CG  1 
ATOM   13634 C  CD1 . LEU M  1 67  ? 8.840   144.216 120.217 1.00 18.94 ? 67   LEU M CD1 1 
ATOM   13635 C  CD2 . LEU M  1 67  ? 9.272   142.389 121.837 1.00 20.44 ? 67   LEU M CD2 1 
ATOM   13636 N  N   . SER M  1 68  ? 4.611   142.869 124.303 1.00 16.06 ? 68   SER M N   1 
ATOM   13637 C  CA  . SER M  1 68  ? 3.704   143.346 125.343 1.00 17.01 ? 68   SER M CA  1 
ATOM   13638 C  C   . SER M  1 68  ? 3.376   144.838 125.155 1.00 16.52 ? 68   SER M C   1 
ATOM   13639 O  O   . SER M  1 68  ? 3.479   145.662 126.089 1.00 16.93 ? 68   SER M O   1 
ATOM   13640 C  CB  . SER M  1 68  ? 4.311   143.052 126.737 1.00 17.17 ? 68   SER M CB  1 
ATOM   13641 O  OG  . SER M  1 68  ? 4.805   141.706 126.815 1.00 19.53 ? 68   SER M OG  1 
ATOM   13642 N  N   . ARG M  1 69  ? 3.000   145.190 123.930 1.00 15.79 ? 69   ARG M N   1 
ATOM   13643 C  CA  . ARG M  1 69  ? 2.610   146.558 123.618 1.00 16.21 ? 69   ARG M CA  1 
ATOM   13644 C  C   . ARG M  1 69  ? 1.114   146.678 123.469 1.00 15.84 ? 69   ARG M C   1 
ATOM   13645 O  O   . ARG M  1 69  ? 0.381   145.685 123.506 1.00 15.86 ? 69   ARG M O   1 
ATOM   13646 C  CB  . ARG M  1 69  ? 3.251   147.017 122.324 1.00 16.45 ? 69   ARG M CB  1 
ATOM   13647 C  CG  . ARG M  1 69  ? 4.657   146.545 122.192 1.00 19.97 ? 69   ARG M CG  1 
ATOM   13648 C  CD  . ARG M  1 69  ? 5.691   147.589 122.426 1.00 25.23 ? 69   ARG M CD  1 
ATOM   13649 N  NE  . ARG M  1 69  ? 6.341   147.891 121.158 1.00 30.17 ? 69   ARG M NE  1 
ATOM   13650 C  CZ  . ARG M  1 69  ? 7.652   147.948 120.993 1.00 30.92 ? 69   ARG M CZ  1 
ATOM   13651 N  NH1 . ARG M  1 69  ? 8.458   147.742 122.025 1.00 30.70 ? 69   ARG M NH1 1 
ATOM   13652 N  NH2 . ARG M  1 69  ? 8.156   148.223 119.793 1.00 31.55 ? 69   ARG M NH2 1 
ATOM   13653 N  N   . LYS M  1 70  ? 0.672   147.911 123.291 1.00 15.21 ? 70   LYS M N   1 
ATOM   13654 C  CA  . LYS M  1 70  ? -0.720  148.189 123.024 1.00 15.33 ? 70   LYS M CA  1 
ATOM   13655 C  C   . LYS M  1 70  ? -0.997  148.025 121.534 1.00 13.71 ? 70   LYS M C   1 
ATOM   13656 O  O   . LYS M  1 70  ? -0.108  148.117 120.705 1.00 13.00 ? 70   LYS M O   1 
ATOM   13657 C  CB  . LYS M  1 70  ? -1.087  149.614 123.436 1.00 15.02 ? 70   LYS M CB  1 
ATOM   13658 C  CG  . LYS M  1 70  ? -0.830  149.912 124.918 1.00 19.50 ? 70   LYS M CG  1 
ATOM   13659 N  N   . HIS M  1 71  ? -2.265  147.848 121.214 1.00 13.35 ? 71   HIS M N   1 
ATOM   13660 C  CA  . HIS M  1 71  ? -2.690  147.717 119.825 1.00 12.07 ? 71   HIS M CA  1 
ATOM   13661 C  C   . HIS M  1 71  ? -2.457  149.000 119.019 1.00 12.69 ? 71   HIS M C   1 
ATOM   13662 O  O   . HIS M  1 71  ? -2.702  150.105 119.510 1.00 12.47 ? 71   HIS M O   1 
ATOM   13663 C  CB  . HIS M  1 71  ? -4.167  147.358 119.802 1.00 11.73 ? 71   HIS M CB  1 
ATOM   13664 C  CG  . HIS M  1 71  ? -4.706  147.160 118.420 1.00 13.03 ? 71   HIS M CG  1 
ATOM   13665 N  ND1 . HIS M  1 71  ? -4.507  145.994 117.708 1.00 10.91 ? 71   HIS M ND1 1 
ATOM   13666 C  CD2 . HIS M  1 71  ? -5.410  147.988 117.611 1.00 13.36 ? 71   HIS M CD2 1 
ATOM   13667 C  CE1 . HIS M  1 71  ? -5.088  146.108 116.522 1.00 9.15  ? 71   HIS M CE1 1 
ATOM   13668 N  NE2 . HIS M  1 71  ? -5.638  147.311 116.435 1.00 8.86  ? 71   HIS M NE2 1 
ATOM   13669 N  N   . GLY M  1 72  ? -1.946  148.876 117.799 1.00 10.76 ? 72   GLY M N   1 
ATOM   13670 C  CA  . GLY M  1 72  ? -1.846  150.037 116.935 1.00 10.86 ? 72   GLY M CA  1 
ATOM   13671 C  C   . GLY M  1 72  ? -2.110  149.660 115.481 1.00 10.39 ? 72   GLY M C   1 
ATOM   13672 O  O   . GLY M  1 72  ? -2.618  148.562 115.188 1.00 9.83  ? 72   GLY M O   1 
ATOM   13673 N  N   . GLY M  1 73  ? -1.755  150.561 114.574 1.00 10.08 ? 73   GLY M N   1 
ATOM   13674 C  CA  . GLY M  1 73  ? -1.807  150.285 113.139 1.00 10.12 ? 73   GLY M CA  1 
ATOM   13675 C  C   . GLY M  1 73  ? -0.412  149.828 112.729 1.00 10.62 ? 73   GLY M C   1 
ATOM   13676 O  O   . GLY M  1 73  ? 0.547   149.975 113.477 1.00 10.70 ? 73   GLY M O   1 
ATOM   13677 N  N   . PRO M  1 74  ? -0.266  149.281 111.537 1.00 11.32 ? 74   PRO M N   1 
ATOM   13678 C  CA  . PRO M  1 74  ? 1.031   148.692 111.134 1.00 11.48 ? 74   PRO M CA  1 
ATOM   13679 C  C   . PRO M  1 74  ? 2.152   149.725 111.083 1.00 11.88 ? 74   PRO M C   1 
ATOM   13680 O  O   . PRO M  1 74  ? 3.341   149.386 111.237 1.00 11.29 ? 74   PRO M O   1 
ATOM   13681 C  CB  . PRO M  1 74  ? 0.770   148.114 109.734 1.00 12.60 ? 74   PRO M CB  1 
ATOM   13682 C  CG  . PRO M  1 74  ? -0.634  148.577 109.340 1.00 12.57 ? 74   PRO M CG  1 
ATOM   13683 C  CD  . PRO M  1 74  ? -1.300  149.212 110.497 1.00 12.03 ? 74   PRO M CD  1 
ATOM   13684 N  N   . LYS M  1 75  ? 1.797   150.988 110.854 1.00 12.91 ? 75   LYS M N   1 
ATOM   13685 C  CA  . LYS M  1 75  ? 2.842   152.020 110.791 1.00 14.74 ? 75   LYS M CA  1 
ATOM   13686 C  C   . LYS M  1 75  ? 3.292   152.543 112.149 1.00 15.83 ? 75   LYS M C   1 
ATOM   13687 O  O   . LYS M  1 75  ? 4.270   153.296 112.235 1.00 15.14 ? 75   LYS M O   1 
ATOM   13688 C  CB  . LYS M  1 75  ? 2.410   153.190 109.916 1.00 15.44 ? 75   LYS M CB  1 
ATOM   13689 C  CG  . LYS M  1 75  ? 1.965   152.784 108.510 1.00 18.04 ? 75   LYS M CG  1 
ATOM   13690 N  N   . ASP M  1 76  ? 2.586   152.162 113.206 1.00 15.58 ? 76   ASP M N   1 
ATOM   13691 C  CA  . ASP M  1 76  ? 2.938   152.628 114.535 1.00 16.06 ? 76   ASP M CA  1 
ATOM   13692 C  C   . ASP M  1 76  ? 4.101   151.891 115.154 1.00 16.73 ? 76   ASP M C   1 
ATOM   13693 O  O   . ASP M  1 76  ? 4.233   150.671 114.990 1.00 16.16 ? 76   ASP M O   1 
ATOM   13694 C  CB  . ASP M  1 76  ? 1.742   152.479 115.467 1.00 16.18 ? 76   ASP M CB  1 
ATOM   13695 C  CG  . ASP M  1 76  ? 0.604   153.392 115.080 1.00 16.73 ? 76   ASP M CG  1 
ATOM   13696 O  OD1 . ASP M  1 76  ? 0.870   154.575 114.732 1.00 15.67 ? 76   ASP M OD1 1 
ATOM   13697 O  OD2 . ASP M  1 76  ? -0.584  153.013 115.085 1.00 16.96 ? 76   ASP M OD2 1 
ATOM   13698 N  N   . GLU M  1 77  ? 4.925   152.625 115.900 1.00 16.36 ? 77   GLU M N   1 
ATOM   13699 C  CA  . GLU M  1 77  ? 5.985   152.002 116.645 1.00 17.77 ? 77   GLU M CA  1 
ATOM   13700 C  C   . GLU M  1 77  ? 5.282   151.246 117.762 1.00 16.58 ? 77   GLU M C   1 
ATOM   13701 O  O   . GLU M  1 77  ? 5.664   150.121 118.114 1.00 17.30 ? 77   GLU M O   1 
ATOM   13702 C  CB  . GLU M  1 77  ? 6.926   153.065 117.215 1.00 19.10 ? 77   GLU M CB  1 
ATOM   13703 C  CG  . GLU M  1 77  ? 8.391   152.766 116.959 1.00 23.73 ? 77   GLU M CG  1 
ATOM   13704 C  CD  . GLU M  1 77  ? 9.257   153.994 117.172 1.00 29.26 ? 77   GLU M CD  1 
ATOM   13705 O  OE1 . GLU M  1 77  ? 9.788   154.544 116.171 1.00 30.87 ? 77   GLU M OE1 1 
ATOM   13706 O  OE2 . GLU M  1 77  ? 9.383   154.422 118.344 1.00 31.60 ? 77   GLU M OE2 1 
ATOM   13707 N  N   . GLU M  1 78  ? 4.218   151.845 118.294 1.00 14.90 ? 78   GLU M N   1 
ATOM   13708 C  CA  . GLU M  1 78  ? 3.458   151.150 119.328 1.00 13.88 ? 78   GLU M CA  1 
ATOM   13709 C  C   . GLU M  1 78  ? 2.343   150.274 118.709 1.00 12.57 ? 78   GLU M C   1 
ATOM   13710 O  O   . GLU M  1 78  ? 1.258   150.762 118.366 1.00 11.43 ? 78   GLU M O   1 
ATOM   13711 C  CB  . GLU M  1 78  ? 2.901   152.154 120.350 1.00 14.31 ? 78   GLU M CB  1 
ATOM   13712 C  CG  . GLU M  1 78  ? 2.218   151.492 121.531 1.00 17.51 ? 78   GLU M CG  1 
ATOM   13713 C  CD  . GLU M  1 78  ? 3.216   150.962 122.541 1.00 21.68 ? 78   GLU M CD  1 
ATOM   13714 O  OE1 . GLU M  1 78  ? 4.388   151.403 122.491 1.00 24.23 ? 78   GLU M OE1 1 
ATOM   13715 O  OE2 . GLU M  1 78  ? 2.832   150.100 123.369 1.00 21.79 ? 78   GLU M OE2 1 
ATOM   13716 N  N   . ARG M  1 79  ? 2.639   148.986 118.546 1.00 11.59 ? 79   ARG M N   1 
ATOM   13717 C  CA  . ARG M  1 79  ? 1.694   148.054 117.977 1.00 11.35 ? 79   ARG M CA  1 
ATOM   13718 C  C   . ARG M  1 79  ? 2.038   146.635 118.427 1.00 11.58 ? 79   ARG M C   1 
ATOM   13719 O  O   . ARG M  1 79  ? 3.109   146.370 118.987 1.00 11.61 ? 79   ARG M O   1 
ATOM   13720 C  CB  . ARG M  1 79  ? 1.760   148.109 116.450 1.00 11.38 ? 79   ARG M CB  1 
ATOM   13721 C  CG  . ARG M  1 79  ? 3.116   147.704 115.875 1.00 10.68 ? 79   ARG M CG  1 
ATOM   13722 C  CD  . ARG M  1 79  ? 3.143   147.535 114.378 1.00 11.76 ? 79   ARG M CD  1 
ATOM   13723 N  NE  . ARG M  1 79  ? 2.878   146.140 113.969 1.00 8.96  ? 79   ARG M NE  1 
ATOM   13724 C  CZ  . ARG M  1 79  ? 3.048   145.712 112.729 1.00 8.82  ? 79   ARG M CZ  1 
ATOM   13725 N  NH1 . ARG M  1 79  ? 3.484   146.559 111.809 1.00 6.32  ? 79   ARG M NH1 1 
ATOM   13726 N  NH2 . ARG M  1 79  ? 2.826   144.423 112.409 1.00 8.60  ? 79   ARG M NH2 1 
ATOM   13727 N  N   . HIS M  1 80  ? 1.088   145.741 118.245 1.00 11.21 ? 80   HIS M N   1 
ATOM   13728 C  CA  . HIS M  1 80  ? 1.339   144.345 118.476 1.00 11.02 ? 80   HIS M CA  1 
ATOM   13729 C  C   . HIS M  1 80  ? 2.041   143.840 117.225 1.00 10.72 ? 80   HIS M C   1 
ATOM   13730 O  O   . HIS M  1 80  ? 1.828   144.384 116.142 1.00 10.07 ? 80   HIS M O   1 
ATOM   13731 C  CB  . HIS M  1 80  ? 0.019   143.622 118.574 1.00 11.19 ? 80   HIS M CB  1 
ATOM   13732 C  CG  . HIS M  1 80  ? -0.828  144.031 119.737 1.00 11.01 ? 80   HIS M CG  1 
ATOM   13733 N  ND1 . HIS M  1 80  ? -2.204  144.056 119.673 1.00 8.35  ? 80   HIS M ND1 1 
ATOM   13734 C  CD2 . HIS M  1 80  ? -0.500  144.377 121.005 1.00 10.25 ? 80   HIS M CD2 1 
ATOM   13735 C  CE1 . HIS M  1 80  ? -2.691  144.383 120.856 1.00 12.05 ? 80   HIS M CE1 1 
ATOM   13736 N  NE2 . HIS M  1 80  ? -1.677  144.589 121.679 1.00 14.41 ? 80   HIS M NE2 1 
ATOM   13737 N  N   . VAL M  1 81  ? 2.872   142.798 117.346 1.00 10.28 ? 81   VAL M N   1 
ATOM   13738 C  CA  . VAL M  1 81  ? 3.480   142.237 116.147 1.00 9.24  ? 81   VAL M CA  1 
ATOM   13739 C  C   . VAL M  1 81  ? 2.383   141.839 115.151 1.00 9.50  ? 81   VAL M C   1 
ATOM   13740 O  O   . VAL M  1 81  ? 2.512   142.052 113.968 1.00 9.19  ? 81   VAL M O   1 
ATOM   13741 C  CB  . VAL M  1 81  ? 4.436   141.051 116.483 1.00 9.56  ? 81   VAL M CB  1 
ATOM   13742 C  CG1 . VAL M  1 81  ? 4.800   140.267 115.233 1.00 8.18  ? 81   VAL M CG1 1 
ATOM   13743 C  CG2 . VAL M  1 81  ? 5.708   141.614 117.212 1.00 8.17  ? 81   VAL M CG2 1 
ATOM   13744 N  N   . GLY M  1 82  ? 1.260   141.325 115.640 1.00 9.44  ? 82   GLY M N   1 
ATOM   13745 C  CA  . GLY M  1 82  ? 0.205   140.875 114.733 1.00 10.30 ? 82   GLY M CA  1 
ATOM   13746 C  C   . GLY M  1 82  ? -0.660  141.974 114.092 1.00 10.30 ? 82   GLY M C   1 
ATOM   13747 O  O   . GLY M  1 82  ? -1.571  141.664 113.317 1.00 9.11  ? 82   GLY M O   1 
ATOM   13748 N  N   . ASP M  1 83  ? -0.360  143.253 114.353 1.00 9.75  ? 83   ASP M N   1 
ATOM   13749 C  CA  . ASP M  1 83  ? -1.199  144.345 113.854 1.00 9.34  ? 83   ASP M CA  1 
ATOM   13750 C  C   . ASP M  1 83  ? -0.986  144.734 112.372 1.00 9.67  ? 83   ASP M C   1 
ATOM   13751 O  O   . ASP M  1 83  ? -0.206  145.634 112.069 1.00 9.89  ? 83   ASP M O   1 
ATOM   13752 C  CB  . ASP M  1 83  ? -1.046  145.590 114.766 1.00 9.02  ? 83   ASP M CB  1 
ATOM   13753 C  CG  . ASP M  1 83  ? -1.635  145.388 116.163 1.00 11.31 ? 83   ASP M CG  1 
ATOM   13754 O  OD1 . ASP M  1 83  ? -2.390  144.411 116.404 1.00 8.99  ? 83   ASP M OD1 1 
ATOM   13755 O  OD2 . ASP M  1 83  ? -1.394  146.202 117.088 1.00 9.70  ? 83   ASP M OD2 1 
ATOM   13756 N  N   . LEU M  1 84  ? -1.687  144.067 111.444 1.00 8.05  ? 84   LEU M N   1 
ATOM   13757 C  CA  . LEU M  1 84  ? -1.538  144.339 110.012 1.00 8.21  ? 84   LEU M CA  1 
ATOM   13758 C  C   . LEU M  1 84  ? -2.562  145.360 109.477 1.00 9.13  ? 84   LEU M C   1 
ATOM   13759 O  O   . LEU M  1 84  ? -2.596  145.673 108.277 1.00 11.48 ? 84   LEU M O   1 
ATOM   13760 C  CB  . LEU M  1 84  ? -1.622  143.018 109.210 1.00 7.09  ? 84   LEU M CB  1 
ATOM   13761 C  CG  . LEU M  1 84  ? -0.483  142.071 109.576 1.00 8.50  ? 84   LEU M CG  1 
ATOM   13762 C  CD1 . LEU M  1 84  ? -0.602  140.811 108.682 1.00 11.43 ? 84   LEU M CD1 1 
ATOM   13763 C  CD2 . LEU M  1 84  ? 0.848   142.774 109.339 1.00 11.38 ? 84   LEU M CD2 1 
ATOM   13764 N  N   . GLY M  1 85  ? -3.371  145.907 110.361 1.00 8.98  ? 85   GLY M N   1 
ATOM   13765 C  CA  . GLY M  1 85  ? -4.252  146.988 109.951 1.00 8.76  ? 85   GLY M CA  1 
ATOM   13766 C  C   . GLY M  1 85  ? -5.557  146.478 109.384 1.00 8.62  ? 85   GLY M C   1 
ATOM   13767 O  O   . GLY M  1 85  ? -6.172  145.565 109.937 1.00 9.12  ? 85   GLY M O   1 
ATOM   13768 N  N   . ASN M  1 86  ? -6.010  147.114 108.319 1.00 7.22  ? 86   ASN M N   1 
ATOM   13769 C  CA  . ASN M  1 86  ? -7.254  146.752 107.683 1.00 8.10  ? 86   ASN M CA  1 
ATOM   13770 C  C   . ASN M  1 86  ? -7.046  146.238 106.276 1.00 8.26  ? 86   ASN M C   1 
ATOM   13771 O  O   . ASN M  1 86  ? -6.075  146.591 105.632 1.00 9.68  ? 86   ASN M O   1 
ATOM   13772 C  CB  . ASN M  1 86  ? -8.145  147.989 107.561 1.00 7.60  ? 86   ASN M CB  1 
ATOM   13773 C  CG  . ASN M  1 86  ? -8.730  148.378 108.873 1.00 9.54  ? 86   ASN M CG  1 
ATOM   13774 O  OD1 . ASN M  1 86  ? -9.477  147.609 109.460 1.00 6.37  ? 86   ASN M OD1 1 
ATOM   13775 N  ND2 . ASN M  1 86  ? -8.364  149.564 109.368 1.00 10.43 ? 86   ASN M ND2 1 
ATOM   13776 N  N   . VAL M  1 87  ? -7.967  145.416 105.824 1.00 8.74  ? 87   VAL M N   1 
ATOM   13777 C  CA  . VAL M  1 87  ? -8.053  145.074 104.417 1.00 7.73  ? 87   VAL M CA  1 
ATOM   13778 C  C   . VAL M  1 87  ? -9.372  145.647 103.929 1.00 8.37  ? 87   VAL M C   1 
ATOM   13779 O  O   . VAL M  1 87  ? -10.250 145.971 104.716 1.00 9.15  ? 87   VAL M O   1 
ATOM   13780 C  CB  . VAL M  1 87  ? -7.900  143.569 104.119 1.00 8.34  ? 87   VAL M CB  1 
ATOM   13781 C  CG1 . VAL M  1 87  ? -6.533  143.124 104.600 1.00 7.05  ? 87   VAL M CG1 1 
ATOM   13782 C  CG2 . VAL M  1 87  ? -9.020  142.760 104.807 1.00 7.07  ? 87   VAL M CG2 1 
ATOM   13783 N  N   . THR M  1 88  ? -9.518  145.810 102.628 1.00 6.69  ? 88   THR M N   1 
ATOM   13784 C  CA  . THR M  1 88  ? -10.698 146.495 102.112 1.00 7.57  ? 88   THR M CA  1 
ATOM   13785 C  C   . THR M  1 88  ? -11.440 145.591 101.174 1.00 7.58  ? 88   THR M C   1 
ATOM   13786 O  O   . THR M  1 88  ? -10.846 145.075 100.274 1.00 7.87  ? 88   THR M O   1 
ATOM   13787 C  CB  . THR M  1 88  ? -10.275 147.745 101.323 1.00 8.29  ? 88   THR M CB  1 
ATOM   13788 O  OG1 . THR M  1 88  ? -9.821  148.744 102.241 1.00 8.27  ? 88   THR M OG1 1 
ATOM   13789 C  CG2 . THR M  1 88  ? -11.522 148.397 100.608 1.00 8.65  ? 88   THR M CG2 1 
ATOM   13790 N  N   . ALA M  1 89  ? -12.720 145.372 101.413 1.00 6.31  ? 89   ALA M N   1 
ATOM   13791 C  CA  . ALA M  1 89  ? -13.531 144.602 100.472 1.00 7.71  ? 89   ALA M CA  1 
ATOM   13792 C  C   . ALA M  1 89  ? -14.291 145.538 99.495  1.00 8.91  ? 89   ALA M C   1 
ATOM   13793 O  O   . ALA M  1 89  ? -14.794 146.603 99.886  1.00 8.95  ? 89   ALA M O   1 
ATOM   13794 C  CB  . ALA M  1 89  ? -14.513 143.741 101.253 1.00 7.49  ? 89   ALA M CB  1 
ATOM   13795 N  N   . ASP M  1 90  ? -14.367 145.126 98.227  1.00 9.24  ? 90   ASP M N   1 
ATOM   13796 C  CA  . ASP M  1 90  ? -15.083 145.878 97.217  1.00 10.54 ? 90   ASP M CA  1 
ATOM   13797 C  C   . ASP M  1 90  ? -16.572 145.611 97.262  1.00 10.77 ? 90   ASP M C   1 
ATOM   13798 O  O   . ASP M  1 90  ? -17.041 144.937 98.149  1.00 9.60  ? 90   ASP M O   1 
ATOM   13799 C  CB  . ASP M  1 90  ? -14.463 145.659 95.825  1.00 10.93 ? 90   ASP M CB  1 
ATOM   13800 C  CG  . ASP M  1 90  ? -14.587 144.244 95.340  1.00 11.66 ? 90   ASP M CG  1 
ATOM   13801 O  OD1 . ASP M  1 90  ? -15.513 143.552 95.800  1.00 9.89  ? 90   ASP M OD1 1 
ATOM   13802 O  OD2 . ASP M  1 90  ? -13.805 143.763 94.479  1.00 12.49 ? 90   ASP M OD2 1 
ATOM   13803 N  N   . LYS M  1 91  ? -17.341 146.214 96.344  1.00 11.95 ? 91   LYS M N   1 
ATOM   13804 C  CA  . LYS M  1 91  ? -18.797 146.086 96.395  1.00 13.19 ? 91   LYS M CA  1 
ATOM   13805 C  C   . LYS M  1 91  ? -19.247 144.664 96.102  1.00 13.36 ? 91   LYS M C   1 
ATOM   13806 O  O   . LYS M  1 91  ? -20.405 144.309 96.350  1.00 13.60 ? 91   LYS M O   1 
ATOM   13807 C  CB  . LYS M  1 91  ? -19.491 147.091 95.453  1.00 13.41 ? 91   LYS M CB  1 
ATOM   13808 C  CG  . LYS M  1 91  ? -19.258 146.878 93.944  1.00 18.30 ? 91   LYS M CG  1 
ATOM   13809 C  CD  . LYS M  1 91  ? -17.858 146.293 93.617  1.00 26.06 ? 91   LYS M CD  1 
ATOM   13810 C  CE  . LYS M  1 91  ? -17.580 146.191 92.098  1.00 30.75 ? 91   LYS M CE  1 
ATOM   13811 N  NZ  . LYS M  1 91  ? -16.325 145.404 91.802  1.00 30.69 ? 91   LYS M NZ  1 
ATOM   13812 N  N   . ASP M  1 92  ? -18.334 143.846 95.589  1.00 12.84 ? 92   ASP M N   1 
ATOM   13813 C  CA  . ASP M  1 92  ? -18.666 142.449 95.340  1.00 13.40 ? 92   ASP M CA  1 
ATOM   13814 C  C   . ASP M  1 92  ? -18.269 141.588 96.521  1.00 12.53 ? 92   ASP M C   1 
ATOM   13815 O  O   . ASP M  1 92  ? -18.419 140.359 96.486  1.00 11.89 ? 92   ASP M O   1 
ATOM   13816 C  CB  . ASP M  1 92  ? -17.988 141.930 94.074  1.00 13.53 ? 92   ASP M CB  1 
ATOM   13817 C  CG  . ASP M  1 92  ? -18.465 142.635 92.847  1.00 17.72 ? 92   ASP M CG  1 
ATOM   13818 O  OD1 . ASP M  1 92  ? -19.682 142.954 92.778  1.00 18.28 ? 92   ASP M OD1 1 
ATOM   13819 O  OD2 . ASP M  1 92  ? -17.691 142.930 91.912  1.00 20.32 ? 92   ASP M OD2 1 
ATOM   13820 N  N   . GLY M  1 93  ? -17.757 142.225 97.565  1.00 11.54 ? 93   GLY M N   1 
ATOM   13821 C  CA  . GLY M  1 93  ? -17.418 141.492 98.777  1.00 10.76 ? 93   GLY M CA  1 
ATOM   13822 C  C   . GLY M  1 93  ? -16.034 140.890 98.788  1.00 9.35  ? 93   GLY M C   1 
ATOM   13823 O  O   . GLY M  1 93  ? -15.696 140.105 99.682  1.00 9.67  ? 93   GLY M O   1 
ATOM   13824 N  N   . VAL M  1 94  ? -15.230 141.247 97.792  1.00 9.09  ? 94   VAL M N   1 
ATOM   13825 C  CA  . VAL M  1 94  ? -13.882 140.716 97.658  1.00 8.90  ? 94   VAL M CA  1 
ATOM   13826 C  C   . VAL M  1 94  ? -12.811 141.676 98.161  1.00 9.09  ? 94   VAL M C   1 
ATOM   13827 O  O   . VAL M  1 94  ? -12.739 142.836 97.736  1.00 8.28  ? 94   VAL M O   1 
ATOM   13828 C  CB  . VAL M  1 94  ? -13.588 140.388 96.201  1.00 9.41  ? 94   VAL M CB  1 
ATOM   13829 C  CG1 . VAL M  1 94  ? -12.190 139.795 96.045  1.00 8.88  ? 94   VAL M CG1 1 
ATOM   13830 C  CG2 . VAL M  1 94  ? -14.681 139.412 95.673  1.00 10.89 ? 94   VAL M CG2 1 
ATOM   13831 N  N   . ALA M  1 95  ? -12.009 141.193 99.100  1.00 9.22  ? 95   ALA M N   1 
ATOM   13832 C  CA  . ALA M  1 95  ? -10.828 141.908 99.516  1.00 9.42  ? 95   ALA M CA  1 
ATOM   13833 C  C   . ALA M  1 95  ? -9.606  141.287 98.790  1.00 8.88  ? 95   ALA M C   1 
ATOM   13834 O  O   . ALA M  1 95  ? -9.207  140.154 99.093  1.00 9.80  ? 95   ALA M O   1 
ATOM   13835 C  CB  . ALA M  1 95  ? -10.660 141.823 101.016 1.00 9.08  ? 95   ALA M CB  1 
ATOM   13836 N  N   . ASP M  1 96  ? -9.040  142.037 97.843  1.00 7.86  ? 96   ASP M N   1 
ATOM   13837 C  CA  . ASP M  1 96  ? -7.770  141.676 97.203  1.00 9.54  ? 96   ASP M CA  1 
ATOM   13838 C  C   . ASP M  1 96  ? -6.594  142.235 98.028  1.00 8.55  ? 96   ASP M C   1 
ATOM   13839 O  O   . ASP M  1 96  ? -6.106  143.330 97.813  1.00 10.33 ? 96   ASP M O   1 
ATOM   13840 C  CB  . ASP M  1 96  ? -7.749  142.187 95.771  1.00 10.04 ? 96   ASP M CB  1 
ATOM   13841 C  CG  . ASP M  1 96  ? -8.628  141.366 94.869  1.00 13.48 ? 96   ASP M CG  1 
ATOM   13842 O  OD1 . ASP M  1 96  ? -9.432  141.967 94.126  1.00 15.08 ? 96   ASP M OD1 1 
ATOM   13843 O  OD2 . ASP M  1 96  ? -8.590  140.112 94.848  1.00 13.94 ? 96   ASP M OD2 1 
ATOM   13844 N  N   . VAL M  1 97  ? -6.164  141.473 99.012  1.00 7.97  ? 97   VAL M N   1 
ATOM   13845 C  CA  . VAL M  1 97  ? -5.189  141.952 99.958  1.00 7.19  ? 97   VAL M CA  1 
ATOM   13846 C  C   . VAL M  1 97  ? -3.829  142.151 99.348  1.00 7.78  ? 97   VAL M C   1 
ATOM   13847 O  O   . VAL M  1 97  ? -3.338  141.300 98.608  1.00 8.67  ? 97   VAL M O   1 
ATOM   13848 C  CB  . VAL M  1 97  ? -5.069  140.882 101.065 1.00 7.32  ? 97   VAL M CB  1 
ATOM   13849 C  CG1 . VAL M  1 97  ? -3.951  141.235 102.114 1.00 6.18  ? 97   VAL M CG1 1 
ATOM   13850 C  CG2 . VAL M  1 97  ? -6.452  140.692 101.722 1.00 9.11  ? 97   VAL M CG2 1 
ATOM   13851 N  N   . SER M  1 98  ? -3.178  143.245 99.690  1.00 9.09  ? 98   SER M N   1 
ATOM   13852 C  CA  . SER M  1 98  ? -1.818  143.441 99.222  1.00 10.65 ? 98   SER M CA  1 
ATOM   13853 C  C   . SER M  1 98  ? -1.157  144.376 100.189 1.00 10.55 ? 98   SER M C   1 
ATOM   13854 O  O   . SER M  1 98  ? -1.421  145.580 100.197 1.00 11.31 ? 98   SER M O   1 
ATOM   13855 C  CB  . SER M  1 98  ? -1.794  143.991 97.799  1.00 11.27 ? 98   SER M CB  1 
ATOM   13856 O  OG  . SER M  1 98  ? -0.444  144.077 97.337  1.00 13.83 ? 98   SER M OG  1 
ATOM   13857 N  N   . ILE M  1 99  ? -0.324  143.794 101.048 1.00 10.62 ? 99   ILE M N   1 
ATOM   13858 C  CA  . ILE M  1 99  ? 0.264   144.515 102.149 1.00 11.98 ? 99   ILE M CA  1 
ATOM   13859 C  C   . ILE M  1 99  ? 1.733   144.137 102.207 1.00 12.01 ? 99   ILE M C   1 
ATOM   13860 O  O   . ILE M  1 99  ? 2.112   143.024 101.837 1.00 11.73 ? 99   ILE M O   1 
ATOM   13861 C  CB  . ILE M  1 99  ? -0.453  144.025 103.451 1.00 13.16 ? 99   ILE M CB  1 
ATOM   13862 C  CG1 . ILE M  1 99  ? -1.779  144.770 103.658 1.00 15.13 ? 99   ILE M CG1 1 
ATOM   13863 C  CG2 . ILE M  1 99  ? 0.389   144.168 104.690 1.00 16.00 ? 99   ILE M CG2 1 
ATOM   13864 C  CD1 . ILE M  1 99  ? -2.592  144.099 104.802 1.00 17.29 ? 99   ILE M CD1 1 
ATOM   13865 N  N   . GLU M  1 100 ? 2.572   145.046 102.674 1.00 12.53 ? 100  GLU M N   1 
ATOM   13866 C  CA  . GLU M  1 100 ? 3.954   144.638 102.915 1.00 12.66 ? 100  GLU M CA  1 
ATOM   13867 C  C   . GLU M  1 100 ? 4.252   145.044 104.338 1.00 12.15 ? 100  GLU M C   1 
ATOM   13868 O  O   . GLU M  1 100 ? 3.956   146.165 104.728 1.00 12.25 ? 100  GLU M O   1 
ATOM   13869 C  CB  . GLU M  1 100 ? 4.911   145.334 101.942 1.00 13.37 ? 100  GLU M CB  1 
ATOM   13870 C  CG  . GLU M  1 100 ? 6.350   145.076 102.337 1.00 17.17 ? 100  GLU M CG  1 
ATOM   13871 C  CD  . GLU M  1 100 ? 7.344   145.779 101.439 1.00 22.98 ? 100  GLU M CD  1 
ATOM   13872 O  OE1 . GLU M  1 100 ? 7.534   145.298 100.296 1.00 22.34 ? 100  GLU M OE1 1 
ATOM   13873 O  OE2 . GLU M  1 100 ? 7.929   146.793 101.888 1.00 24.91 ? 100  GLU M OE2 1 
ATOM   13874 N  N   . ASP M  1 101 ? 4.827   144.157 105.132 1.00 11.56 ? 101  ASP M N   1 
ATOM   13875 C  CA  . ASP M  1 101 ? 5.042   144.496 106.532 1.00 12.13 ? 101  ASP M CA  1 
ATOM   13876 C  C   . ASP M  1 101 ? 6.413   143.999 107.001 1.00 12.30 ? 101  ASP M C   1 
ATOM   13877 O  O   . ASP M  1 101 ? 6.817   142.892 106.649 1.00 11.67 ? 101  ASP M O   1 
ATOM   13878 C  CB  . ASP M  1 101 ? 3.924   143.914 107.413 1.00 11.43 ? 101  ASP M CB  1 
ATOM   13879 C  CG  . ASP M  1 101 ? 3.970   144.452 108.827 1.00 12.91 ? 101  ASP M CG  1 
ATOM   13880 O  OD1 . ASP M  1 101 ? 3.455   145.589 109.037 1.00 12.46 ? 101  ASP M OD1 1 
ATOM   13881 O  OD2 . ASP M  1 101 ? 4.515   143.828 109.781 1.00 10.55 ? 101  ASP M OD2 1 
ATOM   13882 N  N   . SER M  1 102 ? 7.105   144.828 107.794 1.00 12.83 ? 102  SER M N   1 
ATOM   13883 C  CA  . SER M  1 102 ? 8.444   144.509 108.302 1.00 13.68 ? 102  SER M CA  1 
ATOM   13884 C  C   . SER M  1 102 ? 8.525   144.147 109.785 1.00 13.04 ? 102  SER M C   1 
ATOM   13885 O  O   . SER M  1 102 ? 9.621   143.911 110.305 1.00 14.44 ? 102  SER M O   1 
ATOM   13886 C  CB  . SER M  1 102 ? 9.383   145.681 108.010 1.00 14.69 ? 102  SER M CB  1 
ATOM   13887 O  OG  . SER M  1 102 ? 9.723   145.680 106.627 1.00 16.46 ? 102  SER M OG  1 
ATOM   13888 N  N   . VAL M  1 103 ? 7.386   144.049 110.456 1.00 10.96 ? 103  VAL M N   1 
ATOM   13889 C  CA  . VAL M  1 103 ? 7.368   143.669 111.863 1.00 10.86 ? 103  VAL M CA  1 
ATOM   13890 C  C   . VAL M  1 103 ? 7.094   142.179 112.022 1.00 10.77 ? 103  VAL M C   1 
ATOM   13891 O  O   . VAL M  1 103 ? 7.782   141.499 112.771 1.00 10.60 ? 103  VAL M O   1 
ATOM   13892 C  CB  . VAL M  1 103 ? 6.364   144.494 112.684 1.00 11.59 ? 103  VAL M CB  1 
ATOM   13893 C  CG1 . VAL M  1 103 ? 6.322   143.995 114.110 1.00 10.20 ? 103  VAL M CG1 1 
ATOM   13894 C  CG2 . VAL M  1 103 ? 6.736   145.990 112.645 1.00 12.39 ? 103  VAL M CG2 1 
ATOM   13895 N  N   . ILE M  1 104 ? 6.082   141.660 111.331 1.00 9.94  ? 104  ILE M N   1 
ATOM   13896 C  CA  . ILE M  1 104 ? 5.928   140.212 111.337 1.00 10.39 ? 104  ILE M CA  1 
ATOM   13897 C  C   . ILE M  1 104 ? 7.132   139.658 110.621 1.00 11.18 ? 104  ILE M C   1 
ATOM   13898 O  O   . ILE M  1 104 ? 7.781   140.364 109.872 1.00 10.57 ? 104  ILE M O   1 
ATOM   13899 C  CB  . ILE M  1 104 ? 4.679   139.787 110.515 1.00 10.66 ? 104  ILE M CB  1 
ATOM   13900 C  CG1 . ILE M  1 104 ? 4.713   140.372 109.100 1.00 10.31 ? 104  ILE M CG1 1 
ATOM   13901 C  CG2 . ILE M  1 104 ? 3.407   140.231 111.196 1.00 9.91  ? 104  ILE M CG2 1 
ATOM   13902 C  CD1 . ILE M  1 104 ? 3.625   139.743 108.186 1.00 10.17 ? 104  ILE M CD1 1 
ATOM   13903 N  N   . SER M  1 105 ? 7.403   138.374 110.815 1.00 11.25 ? 105  SER M N   1 
ATOM   13904 C  CA  . SER M  1 105 ? 8.461   137.698 110.085 1.00 11.79 ? 105  SER M CA  1 
ATOM   13905 C  C   . SER M  1 105 ? 8.110   136.222 109.925 1.00 13.00 ? 105  SER M C   1 
ATOM   13906 O  O   . SER M  1 105 ? 7.194   135.718 110.590 1.00 11.43 ? 105  SER M O   1 
ATOM   13907 C  CB  . SER M  1 105 ? 9.793   137.853 110.842 1.00 12.47 ? 105  SER M CB  1 
ATOM   13908 O  OG  . SER M  1 105 ? 10.827  137.244 110.123 1.00 9.98  ? 105  SER M OG  1 
ATOM   13909 N  N   . LEU M  1 106 ? 8.846   135.530 109.058 1.00 14.48 ? 106  LEU M N   1 
ATOM   13910 C  CA  . LEU M  1 106 ? 8.652   134.096 108.896 1.00 17.11 ? 106  LEU M CA  1 
ATOM   13911 C  C   . LEU M  1 106 ? 9.743   133.280 109.614 1.00 19.02 ? 106  LEU M C   1 
ATOM   13912 O  O   . LEU M  1 106 ? 9.888   132.087 109.345 1.00 18.65 ? 106  LEU M O   1 
ATOM   13913 C  CB  . LEU M  1 106 ? 8.529   133.716 107.416 1.00 16.28 ? 106  LEU M CB  1 
ATOM   13914 C  CG  . LEU M  1 106 ? 7.411   134.432 106.652 1.00 17.47 ? 106  LEU M CG  1 
ATOM   13915 C  CD1 . LEU M  1 106 ? 7.365   134.068 105.146 1.00 17.09 ? 106  LEU M CD1 1 
ATOM   13916 C  CD2 . LEU M  1 106 ? 6.064   134.200 107.331 1.00 14.85 ? 106  LEU M CD2 1 
ATOM   13917 N  N   . SER M  1 107 ? 10.482  133.936 110.520 1.00 20.69 ? 107  SER M N   1 
ATOM   13918 C  CA  . SER M  1 107 ? 11.526  133.322 111.351 1.00 22.47 ? 107  SER M CA  1 
ATOM   13919 C  C   . SER M  1 107 ? 11.771  134.232 112.562 1.00 22.53 ? 107  SER M C   1 
ATOM   13920 O  O   . SER M  1 107 ? 11.356  135.383 112.559 1.00 24.01 ? 107  SER M O   1 
ATOM   13921 C  CB  . SER M  1 107 ? 12.837  133.243 110.574 1.00 22.38 ? 107  SER M CB  1 
ATOM   13922 O  OG  . SER M  1 107 ? 13.388  134.559 110.507 1.00 26.36 ? 107  SER M OG  1 
ATOM   13923 N  N   . GLY M  1 108 ? 12.452  133.741 113.595 1.00 22.35 ? 108  GLY M N   1 
ATOM   13924 C  CA  . GLY M  1 108 ? 12.791  134.591 114.725 1.00 21.73 ? 108  GLY M CA  1 
ATOM   13925 C  C   . GLY M  1 108 ? 11.719  134.878 115.773 1.00 21.49 ? 108  GLY M C   1 
ATOM   13926 O  O   . GLY M  1 108 ? 10.664  134.230 115.800 1.00 21.65 ? 108  GLY M O   1 
ATOM   13927 N  N   . ASP M  1 109 ? 11.993  135.870 116.624 1.00 20.32 ? 109  ASP M N   1 
ATOM   13928 C  CA  . ASP M  1 109 ? 11.144  136.210 117.756 1.00 20.41 ? 109  ASP M CA  1 
ATOM   13929 C  C   . ASP M  1 109 ? 9.759   136.622 117.297 1.00 19.47 ? 109  ASP M C   1 
ATOM   13930 O  O   . ASP M  1 109 ? 8.766   136.348 117.969 1.00 20.26 ? 109  ASP M O   1 
ATOM   13931 C  CB  . ASP M  1 109 ? 11.782  137.335 118.599 1.00 21.07 ? 109  ASP M CB  1 
ATOM   13932 C  CG  . ASP M  1 109 ? 13.090  136.886 119.314 1.00 25.55 ? 109  ASP M CG  1 
ATOM   13933 O  OD1 . ASP M  1 109 ? 13.334  137.326 120.466 1.00 28.88 ? 109  ASP M OD1 1 
ATOM   13934 O  OD2 . ASP M  1 109 ? 13.932  136.101 118.807 1.00 28.77 ? 109  ASP M OD2 1 
ATOM   13935 N  N   . HIS M  1 110 ? 9.701   137.274 116.143 1.00 17.21 ? 110  HIS M N   1 
ATOM   13936 C  CA  . HIS M  1 110 ? 8.435   137.758 115.616 1.00 15.21 ? 110  HIS M CA  1 
ATOM   13937 C  C   . HIS M  1 110 ? 7.801   136.785 114.621 1.00 14.06 ? 110  HIS M C   1 
ATOM   13938 O  O   . HIS M  1 110 ? 6.973   137.196 113.824 1.00 12.71 ? 110  HIS M O   1 
ATOM   13939 C  CB  . HIS M  1 110 ? 8.633   139.101 114.910 1.00 15.24 ? 110  HIS M CB  1 
ATOM   13940 C  CG  . HIS M  1 110 ? 8.977   140.235 115.821 1.00 17.08 ? 110  HIS M CG  1 
ATOM   13941 N  ND1 . HIS M  1 110 ? 8.938   141.553 115.409 1.00 17.95 ? 110  HIS M ND1 1 
ATOM   13942 C  CD2 . HIS M  1 110 ? 9.413   140.254 117.106 1.00 17.59 ? 110  HIS M CD2 1 
ATOM   13943 C  CE1 . HIS M  1 110 ? 9.312   142.336 116.408 1.00 18.80 ? 110  HIS M CE1 1 
ATOM   13944 N  NE2 . HIS M  1 110 ? 9.597   141.576 117.451 1.00 20.09 ? 110  HIS M NE2 1 
ATOM   13945 N  N   . CYS M  1 111 ? 8.165   135.507 114.684 1.00 12.99 ? 111  CYS M N   1 
ATOM   13946 C  CA  . CYS M  1 111 ? 7.704   134.517 113.710 1.00 12.42 ? 111  CYS M CA  1 
ATOM   13947 C  C   . CYS M  1 111 ? 6.215   134.223 113.850 1.00 11.84 ? 111  CYS M C   1 
ATOM   13948 O  O   . CYS M  1 111 ? 5.715   134.073 114.977 1.00 11.10 ? 111  CYS M O   1 
ATOM   13949 C  CB  . CYS M  1 111 ? 8.523   133.222 113.861 1.00 13.50 ? 111  CYS M CB  1 
ATOM   13950 S  SG  . CYS M  1 111 ? 8.149   132.012 112.572 1.00 17.10 ? 111  CYS M SG  1 
ATOM   13951 N  N   . ILE M  1 112 ? 5.497   134.179 112.713 1.00 11.31 ? 112  ILE M N   1 
ATOM   13952 C  CA  . ILE M  1 112 ? 4.066   133.946 112.719 1.00 10.18 ? 112  ILE M CA  1 
ATOM   13953 C  C   . ILE M  1 112 ? 3.633   132.556 112.221 1.00 11.05 ? 112  ILE M C   1 
ATOM   13954 O  O   . ILE M  1 112 ? 2.433   132.267 112.215 1.00 11.86 ? 112  ILE M O   1 
ATOM   13955 C  CB  . ILE M  1 112 ? 3.299   135.048 111.936 1.00 10.72 ? 112  ILE M CB  1 
ATOM   13956 C  CG1 . ILE M  1 112 ? 3.719   135.087 110.457 1.00 9.75  ? 112  ILE M CG1 1 
ATOM   13957 C  CG2 . ILE M  1 112 ? 3.501   136.436 112.594 1.00 6.59  ? 112  ILE M CG2 1 
ATOM   13958 C  CD1 . ILE M  1 112 ? 2.798   135.983 109.577 1.00 9.74  ? 112  ILE M CD1 1 
ATOM   13959 N  N   . ILE M  1 113 ? 4.576   131.683 111.872 1.00 11.64 ? 113  ILE M N   1 
ATOM   13960 C  CA  . ILE M  1 113 ? 4.230   130.334 111.427 1.00 11.56 ? 113  ILE M CA  1 
ATOM   13961 C  C   . ILE M  1 113 ? 3.543   129.593 112.558 1.00 11.30 ? 113  ILE M C   1 
ATOM   13962 O  O   . ILE M  1 113 ? 4.025   129.577 113.699 1.00 10.96 ? 113  ILE M O   1 
ATOM   13963 C  CB  . ILE M  1 113 ? 5.485   129.552 111.053 1.00 12.89 ? 113  ILE M CB  1 
ATOM   13964 C  CG1 . ILE M  1 113 ? 6.301   130.285 109.989 1.00 13.22 ? 113  ILE M CG1 1 
ATOM   13965 C  CG2 . ILE M  1 113 ? 5.112   128.123 110.558 1.00 12.19 ? 113  ILE M CG2 1 
ATOM   13966 C  CD1 . ILE M  1 113 ? 5.585   130.426 108.704 1.00 14.90 ? 113  ILE M CD1 1 
ATOM   13967 N  N   . GLY M  1 114 ? 2.435   128.935 112.270 1.00 11.01 ? 114  GLY M N   1 
ATOM   13968 C  CA  . GLY M  1 114 ? 1.773   128.179 113.324 1.00 9.68  ? 114  GLY M CA  1 
ATOM   13969 C  C   . GLY M  1 114 ? 0.892   129.049 114.205 1.00 9.49  ? 114  GLY M C   1 
ATOM   13970 O  O   . GLY M  1 114 ? 0.319   128.579 115.198 1.00 8.66  ? 114  GLY M O   1 
ATOM   13971 N  N   . ARG M  1 115 ? 0.765   130.314 113.829 1.00 9.17  ? 115  ARG M N   1 
ATOM   13972 C  CA  . ARG M  1 115 ? -0.157  131.205 114.530 1.00 10.14 ? 115  ARG M CA  1 
ATOM   13973 C  C   . ARG M  1 115 ? -1.398  131.362 113.644 1.00 10.16 ? 115  ARG M C   1 
ATOM   13974 O  O   . ARG M  1 115 ? -1.509  130.651 112.625 1.00 11.72 ? 115  ARG M O   1 
ATOM   13975 C  CB  . ARG M  1 115 ? 0.529   132.521 114.915 1.00 9.23  ? 115  ARG M CB  1 
ATOM   13976 C  CG  . ARG M  1 115 ? 1.790   132.239 115.744 1.00 10.89 ? 115  ARG M CG  1 
ATOM   13977 C  CD  . ARG M  1 115 ? 2.459   133.458 116.383 1.00 12.28 ? 115  ARG M CD  1 
ATOM   13978 N  NE  . ARG M  1 115 ? 3.641   133.054 117.159 1.00 11.28 ? 115  ARG M NE  1 
ATOM   13979 C  CZ  . ARG M  1 115 ? 3.618   132.652 118.428 1.00 10.10 ? 115  ARG M CZ  1 
ATOM   13980 N  NH1 . ARG M  1 115 ? 2.477   132.563 119.104 1.00 10.37 ? 115  ARG M NH1 1 
ATOM   13981 N  NH2 . ARG M  1 115 ? 4.750   132.364 119.038 1.00 9.57  ? 115  ARG M NH2 1 
ATOM   13982 N  N   . THR M  1 116 ? -2.338  132.231 114.007 1.00 9.97  ? 116  THR M N   1 
ATOM   13983 C  CA  . THR M  1 116 ? -3.595  132.323 113.261 1.00 9.34  ? 116  THR M CA  1 
ATOM   13984 C  C   . THR M  1 116 ? -3.799  133.680 112.631 1.00 10.24 ? 116  THR M C   1 
ATOM   13985 O  O   . THR M  1 116 ? -3.613  134.714 113.286 1.00 10.83 ? 116  THR M O   1 
ATOM   13986 C  CB  . THR M  1 116 ? -4.797  132.035 114.209 1.00 9.91  ? 116  THR M CB  1 
ATOM   13987 O  OG1 . THR M  1 116 ? -4.761  130.663 114.620 1.00 7.97  ? 116  THR M OG1 1 
ATOM   13988 C  CG2 . THR M  1 116 ? -6.150  132.136 113.470 1.00 8.94  ? 116  THR M CG2 1 
ATOM   13989 N  N   . LEU M  1 117 ? -4.153  133.690 111.357 1.00 9.16  ? 117  LEU M N   1 
ATOM   13990 C  CA  . LEU M  1 117 ? -4.520  134.933 110.699 1.00 9.32  ? 117  LEU M CA  1 
ATOM   13991 C  C   . LEU M  1 117 ? -6.054  135.066 110.803 1.00 8.92  ? 117  LEU M C   1 
ATOM   13992 O  O   . LEU M  1 117 ? -6.760  134.106 110.524 1.00 8.81  ? 117  LEU M O   1 
ATOM   13993 C  CB  . LEU M  1 117 ? -4.073  134.868 109.228 1.00 8.50  ? 117  LEU M CB  1 
ATOM   13994 C  CG  . LEU M  1 117 ? -4.358  136.140 108.414 1.00 10.78 ? 117  LEU M CG  1 
ATOM   13995 C  CD1 . LEU M  1 117 ? -3.560  137.347 108.923 1.00 9.09  ? 117  LEU M CD1 1 
ATOM   13996 C  CD2 . LEU M  1 117 ? -4.025  135.880 106.908 1.00 9.92  ? 117  LEU M CD2 1 
ATOM   13997 N  N   . VAL M  1 118 ? -6.556  136.233 111.228 1.00 7.95  ? 118  VAL M N   1 
ATOM   13998 C  CA  . VAL M  1 118 ? -7.992  136.466 111.405 1.00 6.48  ? 118  VAL M CA  1 
ATOM   13999 C  C   . VAL M  1 118 ? -8.453  137.687 110.614 1.00 6.22  ? 118  VAL M C   1 
ATOM   14000 O  O   . VAL M  1 118 ? -7.782  138.698 110.615 1.00 6.48  ? 118  VAL M O   1 
ATOM   14001 C  CB  . VAL M  1 118 ? -8.318  136.731 112.888 1.00 7.73  ? 118  VAL M CB  1 
ATOM   14002 C  CG1 . VAL M  1 118 ? -9.834  137.033 113.076 1.00 9.04  ? 118  VAL M CG1 1 
ATOM   14003 C  CG2 . VAL M  1 118 ? -7.842  135.523 113.765 1.00 6.04  ? 118  VAL M CG2 1 
ATOM   14004 N  N   . VAL M  1 119 ? -9.562  137.577 109.906 1.00 6.89  ? 119  VAL M N   1 
ATOM   14005 C  CA  . VAL M  1 119 ? -10.185 138.754 109.322 1.00 7.00  ? 119  VAL M CA  1 
ATOM   14006 C  C   . VAL M  1 119 ? -11.471 139.009 110.130 1.00 7.45  ? 119  VAL M C   1 
ATOM   14007 O  O   . VAL M  1 119 ? -12.253 138.084 110.430 1.00 7.61  ? 119  VAL M O   1 
ATOM   14008 C  CB  . VAL M  1 119 ? -10.407 138.612 107.808 1.00 8.55  ? 119  VAL M CB  1 
ATOM   14009 C  CG1 . VAL M  1 119 ? -11.267 137.367 107.459 1.00 7.89  ? 119  VAL M CG1 1 
ATOM   14010 C  CG2 . VAL M  1 119 ? -10.987 139.923 107.222 1.00 7.79  ? 119  VAL M CG2 1 
ATOM   14011 N  N   . HIS M  1 120 ? -11.707 140.283 110.452 1.00 7.81  ? 120  HIS M N   1 
ATOM   14012 C  CA  . HIS M  1 120 ? -12.755 140.659 111.374 1.00 7.57  ? 120  HIS M CA  1 
ATOM   14013 C  C   . HIS M  1 120 ? -13.997 141.285 110.768 1.00 8.84  ? 120  HIS M C   1 
ATOM   14014 O  O   . HIS M  1 120 ? -13.991 141.754 109.620 1.00 7.63  ? 120  HIS M O   1 
ATOM   14015 C  CB  . HIS M  1 120 ? -12.168 141.693 112.320 1.00 8.20  ? 120  HIS M CB  1 
ATOM   14016 C  CG  . HIS M  1 120 ? -11.299 141.104 113.377 1.00 9.09  ? 120  HIS M CG  1 
ATOM   14017 N  ND1 . HIS M  1 120 ? -11.807 140.600 114.558 1.00 11.56 ? 120  HIS M ND1 1 
ATOM   14018 C  CD2 . HIS M  1 120 ? -9.952  140.975 113.455 1.00 10.80 ? 120  HIS M CD2 1 
ATOM   14019 C  CE1 . HIS M  1 120 ? -10.806 140.183 115.315 1.00 12.03 ? 120  HIS M CE1 1 
ATOM   14020 N  NE2 . HIS M  1 120 ? -9.679  140.386 114.661 1.00 11.99 ? 120  HIS M NE2 1 
ATOM   14021 N  N   . GLU M  1 121 ? -15.025 141.361 111.617 1.00 9.56  ? 121  GLU M N   1 
ATOM   14022 C  CA  . GLU M  1 121 ? -16.316 141.924 111.287 1.00 11.22 ? 121  GLU M CA  1 
ATOM   14023 C  C   . GLU M  1 121 ? -16.283 143.420 110.938 1.00 11.42 ? 121  GLU M C   1 
ATOM   14024 O  O   . GLU M  1 121 ? -16.931 143.854 109.985 1.00 11.19 ? 121  GLU M O   1 
ATOM   14025 C  CB  . GLU M  1 121 ? -17.217 141.693 112.506 1.00 13.15 ? 121  GLU M CB  1 
ATOM   14026 C  CG  . GLU M  1 121 ? -18.526 142.427 112.478 1.00 16.95 ? 121  GLU M CG  1 
ATOM   14027 C  CD  . GLU M  1 121 ? -19.269 142.318 113.805 1.00 23.69 ? 121  GLU M CD  1 
ATOM   14028 O  OE1 . GLU M  1 121 ? -18.610 142.328 114.899 1.00 18.77 ? 121  GLU M OE1 1 
ATOM   14029 O  OE2 . GLU M  1 121 ? -20.526 142.230 113.734 1.00 26.89 ? 121  GLU M OE2 1 
ATOM   14030 N  N   . LYS M  1 122 ? -15.535 144.193 111.721 1.00 11.28 ? 122  LYS M N   1 
ATOM   14031 C  CA  . LYS M  1 122 ? -15.520 145.648 111.609 1.00 11.82 ? 122  LYS M CA  1 
ATOM   14032 C  C   . LYS M  1 122 ? -14.139 146.190 111.319 1.00 11.41 ? 122  LYS M C   1 
ATOM   14033 O  O   . LYS M  1 122 ? -13.122 145.469 111.307 1.00 11.67 ? 122  LYS M O   1 
ATOM   14034 C  CB  . LYS M  1 122 ? -15.942 146.283 112.935 1.00 12.34 ? 122  LYS M CB  1 
ATOM   14035 C  CG  . LYS M  1 122 ? -17.184 145.718 113.583 1.00 17.47 ? 122  LYS M CG  1 
ATOM   14036 C  CD  . LYS M  1 122 ? -17.460 146.491 114.888 1.00 17.82 ? 122  LYS M CD  1 
ATOM   14037 C  CE  . LYS M  1 122 ? -18.897 146.268 115.373 1.00 25.02 ? 122  LYS M CE  1 
ATOM   14038 N  NZ  . LYS M  1 122 ? -19.139 146.920 116.711 1.00 26.62 ? 122  LYS M NZ  1 
ATOM   14039 N  N   . ALA M  1 123 ? -14.102 147.488 111.050 1.00 9.91  ? 123  ALA M N   1 
ATOM   14040 C  CA  . ALA M  1 123 ? -12.821 148.102 110.801 1.00 10.25 ? 123  ALA M CA  1 
ATOM   14041 C  C   . ALA M  1 123 ? -12.006 148.164 112.099 1.00 10.34 ? 123  ALA M C   1 
ATOM   14042 O  O   . ALA M  1 123 ? -12.546 148.301 113.212 1.00 10.15 ? 123  ALA M O   1 
ATOM   14043 C  CB  . ALA M  1 123 ? -13.037 149.487 110.243 1.00 10.70 ? 123  ALA M CB  1 
ATOM   14044 N  N   . ASP M  1 124 ? -10.698 148.017 111.950 1.00 9.54  ? 124  ASP M N   1 
ATOM   14045 C  CA  . ASP M  1 124 ? -9.778  148.219 113.055 1.00 9.08  ? 124  ASP M CA  1 
ATOM   14046 C  C   . ASP M  1 124 ? -9.536  149.733 113.147 1.00 8.25  ? 124  ASP M C   1 
ATOM   14047 O  O   . ASP M  1 124 ? -9.143  150.366 112.146 1.00 6.54  ? 124  ASP M O   1 
ATOM   14048 C  CB  . ASP M  1 124 ? -8.490  147.475 112.670 1.00 9.41  ? 124  ASP M CB  1 
ATOM   14049 C  CG  . ASP M  1 124 ? -7.385  147.536 113.704 1.00 12.18 ? 124  ASP M CG  1 
ATOM   14050 O  OD1 . ASP M  1 124 ? -7.311  148.416 114.605 1.00 9.63  ? 124  ASP M OD1 1 
ATOM   14051 O  OD2 . ASP M  1 124 ? -6.460  146.686 113.619 1.00 12.19 ? 124  ASP M OD2 1 
ATOM   14052 N  N   . ASP M  1 125 ? -9.771  150.303 114.340 1.00 7.29  ? 125  ASP M N   1 
ATOM   14053 C  CA  . ASP M  1 125 ? -9.524  151.733 114.559 1.00 7.77  ? 125  ASP M CA  1 
ATOM   14054 C  C   . ASP M  1 125 ? -8.056  152.108 114.744 1.00 8.07  ? 125  ASP M C   1 
ATOM   14055 O  O   . ASP M  1 125 ? -7.720  153.270 114.991 1.00 7.56  ? 125  ASP M O   1 
ATOM   14056 C  CB  . ASP M  1 125 ? -10.401 152.317 115.699 1.00 8.03  ? 125  ASP M CB  1 
ATOM   14057 C  CG  . ASP M  1 125 ? -10.074 151.755 117.093 1.00 7.74  ? 125  ASP M CG  1 
ATOM   14058 O  OD1 . ASP M  1 125 ? -8.943  151.280 117.375 1.00 9.34  ? 125  ASP M OD1 1 
ATOM   14059 O  OD2 . ASP M  1 125 ? -10.911 151.823 118.040 1.00 9.03  ? 125  ASP M OD2 1 
ATOM   14060 N  N   . LEU M  1 126 ? -7.173  151.130 114.590 1.00 7.83  ? 126  LEU M N   1 
ATOM   14061 C  CA  . LEU M  1 126 ? -5.740  151.327 114.696 1.00 7.30  ? 126  LEU M CA  1 
ATOM   14062 C  C   . LEU M  1 126 ? -5.256  151.855 116.049 1.00 7.80  ? 126  LEU M C   1 
ATOM   14063 O  O   . LEU M  1 126 ? -4.236  152.492 116.124 1.00 8.57  ? 126  LEU M O   1 
ATOM   14064 C  CB  . LEU M  1 126 ? -5.210  152.174 113.515 1.00 7.88  ? 126  LEU M CB  1 
ATOM   14065 C  CG  . LEU M  1 126 ? -5.741  151.758 112.117 1.00 8.45  ? 126  LEU M CG  1 
ATOM   14066 C  CD1 . LEU M  1 126 ? -5.058  152.579 111.007 1.00 7.62  ? 126  LEU M CD1 1 
ATOM   14067 C  CD2 . LEU M  1 126 ? -5.522  150.263 111.848 1.00 8.51  ? 126  LEU M CD2 1 
ATOM   14068 N  N   . GLY M  1 127 ? -6.007  151.585 117.105 1.00 7.71  ? 127  GLY M N   1 
ATOM   14069 C  CA  . GLY M  1 127 ? -5.622  152.006 118.439 1.00 6.32  ? 127  GLY M CA  1 
ATOM   14070 C  C   . GLY M  1 127 ? -6.037  153.431 118.744 1.00 6.27  ? 127  GLY M C   1 
ATOM   14071 O  O   . GLY M  1 127 ? -5.660  153.969 119.799 1.00 5.77  ? 127  GLY M O   1 
ATOM   14072 N  N   . LYS M  1 128 ? -6.839  154.031 117.867 1.00 5.23  ? 128  LYS M N   1 
ATOM   14073 C  CA  . LYS M  1 128 ? -7.179  155.455 117.981 1.00 6.40  ? 128  LYS M CA  1 
ATOM   14074 C  C   . LYS M  1 128 ? -8.581  155.699 118.507 1.00 5.68  ? 128  LYS M C   1 
ATOM   14075 O  O   . LYS M  1 128 ? -9.100  156.817 118.393 1.00 6.21  ? 128  LYS M O   1 
ATOM   14076 C  CB  . LYS M  1 128 ? -7.022  156.146 116.628 1.00 7.45  ? 128  LYS M CB  1 
ATOM   14077 C  CG  . LYS M  1 128 ? -5.576  156.083 116.100 1.00 8.75  ? 128  LYS M CG  1 
ATOM   14078 C  CD  . LYS M  1 128 ? -5.467  156.592 114.661 1.00 10.88 ? 128  LYS M CD  1 
ATOM   14079 C  CE  . LYS M  1 128 ? -5.589  158.130 114.534 1.00 13.40 ? 128  LYS M CE  1 
ATOM   14080 N  NZ  . LYS M  1 128 ? -5.542  158.584 113.086 1.00 12.62 ? 128  LYS M NZ  1 
ATOM   14081 N  N   . GLY M  1 129 ? -9.175  154.654 119.066 1.00 5.53  ? 129  GLY M N   1 
ATOM   14082 C  CA  . GLY M  1 129 ? -10.561 154.737 119.521 1.00 5.34  ? 129  GLY M CA  1 
ATOM   14083 C  C   . GLY M  1 129 ? -10.842 155.295 120.907 1.00 5.00  ? 129  GLY M C   1 
ATOM   14084 O  O   . GLY M  1 129 ? -12.004 155.534 121.238 1.00 5.40  ? 129  GLY M O   1 
ATOM   14085 N  N   . GLY M  1 130 ? -9.814  155.438 121.736 1.00 5.00  ? 130  GLY M N   1 
ATOM   14086 C  CA  . GLY M  1 130 ? -9.956  156.122 123.025 1.00 5.00  ? 130  GLY M CA  1 
ATOM   14087 C  C   . GLY M  1 130 ? -10.622 155.329 124.134 1.00 5.59  ? 130  GLY M C   1 
ATOM   14088 O  O   . GLY M  1 130 ? -10.773 155.805 125.250 1.00 5.70  ? 130  GLY M O   1 
ATOM   14089 N  N   . ASN M  1 131 ? -11.071 154.130 123.811 1.00 6.33  ? 131  ASN M N   1 
ATOM   14090 C  CA  . ASN M  1 131 ? -11.641 153.273 124.822 1.00 8.26  ? 131  ASN M CA  1 
ATOM   14091 C  C   . ASN M  1 131 ? -10.689 152.130 125.148 1.00 8.79  ? 131  ASN M C   1 
ATOM   14092 O  O   . ASN M  1 131 ? -9.692  151.892 124.440 1.00 9.70  ? 131  ASN M O   1 
ATOM   14093 C  CB  . ASN M  1 131 ? -13.059 152.806 124.455 1.00 7.63  ? 131  ASN M CB  1 
ATOM   14094 C  CG  . ASN M  1 131 ? -13.109 151.843 123.263 1.00 10.24 ? 131  ASN M CG  1 
ATOM   14095 O  OD1 . ASN M  1 131 ? -12.186 151.736 122.453 1.00 9.89  ? 131  ASN M OD1 1 
ATOM   14096 N  ND2 . ASN M  1 131 ? -14.250 151.179 123.129 1.00 9.33  ? 131  ASN M ND2 1 
ATOM   14097 N  N   . GLU M  1 132 ? -10.985 151.369 126.181 1.00 9.39  ? 132  GLU M N   1 
ATOM   14098 C  CA  . GLU M  1 132 ? -10.088 150.257 126.508 1.00 10.77 ? 132  GLU M CA  1 
ATOM   14099 C  C   . GLU M  1 132 ? -9.896  149.230 125.379 1.00 10.29 ? 132  GLU M C   1 
ATOM   14100 O  O   . GLU M  1 132 ? -8.795  148.739 125.145 1.00 9.15  ? 132  GLU M O   1 
ATOM   14101 C  CB  . GLU M  1 132 ? -10.609 149.510 127.732 1.00 11.86 ? 132  GLU M CB  1 
ATOM   14102 C  CG  . GLU M  1 132 ? -9.646  148.455 128.232 1.00 17.72 ? 132  GLU M CG  1 
ATOM   14103 C  CD  . GLU M  1 132 ? -9.457  148.513 129.737 1.00 26.82 ? 132  GLU M CD  1 
ATOM   14104 O  OE1 . GLU M  1 132 ? -10.357 149.061 130.450 1.00 29.12 ? 132  GLU M OE1 1 
ATOM   14105 O  OE2 . GLU M  1 132 ? -8.393  148.016 130.201 1.00 29.98 ? 132  GLU M OE2 1 
ATOM   14106 N  N   . GLU M  1 133 ? -10.988 148.903 124.704 1.00 10.08 ? 133  GLU M N   1 
ATOM   14107 C  CA  . GLU M  1 133 ? -10.988 147.881 123.662 1.00 10.17 ? 133  GLU M CA  1 
ATOM   14108 C  C   . GLU M  1 133 ? -10.103 148.305 122.491 1.00 10.23 ? 133  GLU M C   1 
ATOM   14109 O  O   . GLU M  1 133 ? -9.500  147.472 121.803 1.00 9.42  ? 133  GLU M O   1 
ATOM   14110 C  CB  . GLU M  1 133 ? -12.412 147.653 123.184 1.00 11.50 ? 133  GLU M CB  1 
ATOM   14111 C  CG  . GLU M  1 133 ? -12.569 146.426 122.278 1.00 12.47 ? 133  GLU M CG  1 
ATOM   14112 C  CD  . GLU M  1 133 ? -12.263 145.132 123.008 1.00 16.00 ? 133  GLU M CD  1 
ATOM   14113 O  OE1 . GLU M  1 133 ? -12.873 144.879 124.064 1.00 17.29 ? 133  GLU M OE1 1 
ATOM   14114 O  OE2 . GLU M  1 133 ? -11.401 144.370 122.546 1.00 20.29 ? 133  GLU M OE2 1 
ATOM   14115 N  N   . SER M  1 134 ? -10.023 149.600 122.235 1.00 9.23  ? 134  SER M N   1 
ATOM   14116 C  CA  . SER M  1 134 ? -9.178  150.054 121.133 1.00 9.40  ? 134  SER M CA  1 
ATOM   14117 C  C   . SER M  1 134 ? -7.708  149.649 121.309 1.00 9.60  ? 134  SER M C   1 
ATOM   14118 O  O   . SER M  1 134 ? -7.008  149.290 120.340 1.00 9.49  ? 134  SER M O   1 
ATOM   14119 C  CB  . SER M  1 134 ? -9.281  151.569 120.980 1.00 8.53  ? 134  SER M CB  1 
ATOM   14120 O  OG  . SER M  1 134 ? -8.481  151.959 119.901 1.00 7.40  ? 134  SER M OG  1 
ATOM   14121 N  N   . THR M  1 135 ? -7.255  149.671 122.554 1.00 10.10 ? 135  THR M N   1 
ATOM   14122 C  CA  . THR M  1 135 ? -5.856  149.413 122.876 1.00 10.51 ? 135  THR M CA  1 
ATOM   14123 C  C   . THR M  1 135 ? -5.559  147.925 122.853 1.00 10.77 ? 135  THR M C   1 
ATOM   14124 O  O   . THR M  1 135 ? -4.402  147.528 123.017 1.00 10.38 ? 135  THR M O   1 
ATOM   14125 C  CB  . THR M  1 135 ? -5.531  149.970 124.290 1.00 12.29 ? 135  THR M CB  1 
ATOM   14126 O  OG1 . THR M  1 135 ? -6.286  149.230 125.272 1.00 14.92 ? 135  THR M OG1 1 
ATOM   14127 C  CG2 . THR M  1 135 ? -6.067  151.360 124.423 1.00 11.92 ? 135  THR M CG2 1 
ATOM   14128 N  N   . LYS M  1 136 ? -6.606  147.117 122.647 1.00 10.85 ? 136  LYS M N   1 
ATOM   14129 C  CA  . LYS M  1 136 ? -6.488  145.658 122.638 1.00 11.94 ? 136  LYS M CA  1 
ATOM   14130 C  C   . LYS M  1 136 ? -6.734  145.061 121.250 1.00 11.79 ? 136  LYS M C   1 
ATOM   14131 O  O   . LYS M  1 136 ? -5.896  144.289 120.729 1.00 11.58 ? 136  LYS M O   1 
ATOM   14132 C  CB  . LYS M  1 136 ? -7.480  145.040 123.640 1.00 12.36 ? 136  LYS M CB  1 
ATOM   14133 C  CG  . LYS M  1 136 ? -7.287  145.456 125.086 1.00 14.49 ? 136  LYS M CG  1 
ATOM   14134 C  CD  . LYS M  1 136 ? -8.232  144.693 126.016 1.00 19.21 ? 136  LYS M CD  1 
ATOM   14135 C  CE  . LYS M  1 136 ? -9.388  145.548 126.504 1.00 23.66 ? 136  LYS M CE  1 
ATOM   14136 N  N   . THR M  1 137 ? -7.871  145.414 120.640 1.00 11.65 ? 137  THR M N   1 
ATOM   14137 C  CA  . THR M  1 137 ? -8.267  144.792 119.376 1.00 11.60 ? 137  THR M CA  1 
ATOM   14138 C  C   . THR M  1 137 ? -8.611  145.781 118.293 1.00 11.65 ? 137  THR M C   1 
ATOM   14139 O  O   . THR M  1 137 ? -9.029  145.371 117.209 1.00 11.14 ? 137  THR M O   1 
ATOM   14140 C  CB  . THR M  1 137 ? -9.544  144.002 119.600 1.00 11.83 ? 137  THR M CB  1 
ATOM   14141 O  OG1 . THR M  1 137 ? -10.571 144.904 120.068 1.00 11.84 ? 137  THR M OG1 1 
ATOM   14142 C  CG2 . THR M  1 137 ? -9.361  143.011 120.735 1.00 14.40 ? 137  THR M CG2 1 
ATOM   14143 N  N   . GLY M  1 138 ? -8.546  147.073 118.599 1.00 10.16 ? 138  GLY M N   1 
ATOM   14144 C  CA  . GLY M  1 138 ? -8.920  148.073 117.631 1.00 9.90  ? 138  GLY M CA  1 
ATOM   14145 C  C   . GLY M  1 138 ? -10.426 148.141 117.398 1.00 9.08  ? 138  GLY M C   1 
ATOM   14146 O  O   . GLY M  1 138 ? -10.906 148.732 116.425 1.00 8.07  ? 138  GLY M O   1 
ATOM   14147 N  N   . ASN M  1 139 ? -11.181 147.568 118.322 1.00 9.00  ? 139  ASN M N   1 
ATOM   14148 C  CA  . ASN M  1 139 ? -12.621 147.502 118.169 1.00 9.63  ? 139  ASN M CA  1 
ATOM   14149 C  C   . ASN M  1 139 ? -13.022 146.814 116.872 1.00 9.51  ? 139  ASN M C   1 
ATOM   14150 O  O   . ASN M  1 139 ? -14.066 147.138 116.295 1.00 8.92  ? 139  ASN M O   1 
ATOM   14151 C  CB  . ASN M  1 139 ? -13.225 148.916 118.207 1.00 9.08  ? 139  ASN M CB  1 
ATOM   14152 C  CG  . ASN M  1 139 ? -13.192 149.506 119.594 1.00 11.04 ? 139  ASN M CG  1 
ATOM   14153 O  OD1 . ASN M  1 139 ? -13.924 149.076 120.456 1.00 11.41 ? 139  ASN M OD1 1 
ATOM   14154 N  ND2 . ASN M  1 139 ? -12.340 150.489 119.810 1.00 8.87  ? 139  ASN M ND2 1 
ATOM   14155 N  N   . ALA M  1 140 ? -12.206 145.869 116.409 1.00 10.02 ? 140  ALA M N   1 
ATOM   14156 C  CA  . ALA M  1 140 ? -12.498 145.201 115.150 1.00 10.68 ? 140  ALA M CA  1 
ATOM   14157 C  C   . ALA M  1 140 ? -13.658 144.195 115.199 1.00 11.60 ? 140  ALA M C   1 
ATOM   14158 O  O   . ALA M  1 140 ? -14.080 143.666 114.152 1.00 11.46 ? 140  ALA M O   1 
ATOM   14159 C  CB  . ALA M  1 140 ? -11.253 144.536 114.590 1.00 11.60 ? 140  ALA M CB  1 
ATOM   14160 N  N   . GLY M  1 141 ? -14.168 143.904 116.394 1.00 10.19 ? 141  GLY M N   1 
ATOM   14161 C  CA  . GLY M  1 141 ? -15.323 143.037 116.468 1.00 11.66 ? 141  GLY M CA  1 
ATOM   14162 C  C   . GLY M  1 141 ? -15.094 141.546 116.244 1.00 10.58 ? 141  GLY M C   1 
ATOM   14163 O  O   . GLY M  1 141 ? -14.007 141.027 116.485 1.00 10.69 ? 141  GLY M O   1 
ATOM   14164 N  N   . SER M  1 142 ? -16.141 140.864 115.780 1.00 10.83 ? 142  SER M N   1 
ATOM   14165 C  CA  . SER M  1 142 ? -16.125 139.397 115.703 1.00 11.16 ? 142  SER M CA  1 
ATOM   14166 C  C   . SER M  1 142 ? -15.119 138.919 114.697 1.00 10.84 ? 142  SER M C   1 
ATOM   14167 O  O   . SER M  1 142 ? -14.734 139.649 113.783 1.00 9.03  ? 142  SER M O   1 
ATOM   14168 C  CB  . SER M  1 142 ? -17.499 138.854 115.274 1.00 11.48 ? 142  SER M CB  1 
ATOM   14169 O  OG  . SER M  1 142 ? -18.452 139.156 116.281 1.00 19.49 ? 142  SER M OG  1 
ATOM   14170 N  N   . ARG M  1 143 ? -14.713 137.665 114.857 1.00 9.87  ? 143  ARG M N   1 
ATOM   14171 C  CA  . ARG M  1 143 ? -13.766 137.065 113.925 1.00 10.91 ? 143  ARG M CA  1 
ATOM   14172 C  C   . ARG M  1 143 ? -14.580 136.305 112.898 1.00 10.78 ? 143  ARG M C   1 
ATOM   14173 O  O   . ARG M  1 143 ? -15.212 135.311 113.255 1.00 11.33 ? 143  ARG M O   1 
ATOM   14174 C  CB  . ARG M  1 143 ? -12.897 136.080 114.701 1.00 10.48 ? 143  ARG M CB  1 
ATOM   14175 C  CG  . ARG M  1 143 ? -12.383 136.716 115.981 1.00 10.17 ? 143  ARG M CG  1 
ATOM   14176 C  CD  . ARG M  1 143 ? -11.517 135.806 116.853 1.00 10.02 ? 143  ARG M CD  1 
ATOM   14177 N  NE  . ARG M  1 143 ? -11.027 136.601 117.970 1.00 10.58 ? 143  ARG M NE  1 
ATOM   14178 C  CZ  . ARG M  1 143 ? -10.064 136.209 118.807 1.00 12.60 ? 143  ARG M CZ  1 
ATOM   14179 N  NH1 . ARG M  1 143 ? -9.493  135.024 118.665 1.00 11.06 ? 143  ARG M NH1 1 
ATOM   14180 N  NH2 . ARG M  1 143 ? -9.646  137.030 119.767 1.00 10.24 ? 143  ARG M NH2 1 
ATOM   14181 N  N   . LEU M  1 144 ? -14.563 136.763 111.638 1.00 9.46  ? 144  LEU M N   1 
ATOM   14182 C  CA  . LEU M  1 144 ? -15.410 136.154 110.611 1.00 9.51  ? 144  LEU M CA  1 
ATOM   14183 C  C   . LEU M  1 144 ? -14.796 134.906 109.988 1.00 8.93  ? 144  LEU M C   1 
ATOM   14184 O  O   . LEU M  1 144 ? -15.520 134.018 109.545 1.00 9.66  ? 144  LEU M O   1 
ATOM   14185 C  CB  . LEU M  1 144 ? -15.672 137.141 109.495 1.00 9.12  ? 144  LEU M CB  1 
ATOM   14186 C  CG  . LEU M  1 144 ? -16.379 138.417 109.966 1.00 8.51  ? 144  LEU M CG  1 
ATOM   14187 C  CD1 . LEU M  1 144 ? -16.577 139.334 108.765 1.00 13.86 ? 144  LEU M CD1 1 
ATOM   14188 C  CD2 . LEU M  1 144 ? -17.680 138.051 110.628 1.00 9.63  ? 144  LEU M CD2 1 
ATOM   14189 N  N   . ALA M  1 145 ? -13.479 134.901 109.848 1.00 7.72  ? 145  ALA M N   1 
ATOM   14190 C  CA  . ALA M  1 145 ? -12.795 133.744 109.276 1.00 9.00  ? 145  ALA M CA  1 
ATOM   14191 C  C   . ALA M  1 145 ? -11.370 133.751 109.765 1.00 8.88  ? 145  ALA M C   1 
ATOM   14192 O  O   . ALA M  1 145 ? -10.813 134.811 110.068 1.00 7.90  ? 145  ALA M O   1 
ATOM   14193 C  CB  . ALA M  1 145 ? -12.818 133.795 107.775 1.00 9.06  ? 145  ALA M CB  1 
ATOM   14194 N  N   . CYS M  1 146 ? -10.771 132.572 109.859 1.00 8.70  ? 146  CYS M N   1 
ATOM   14195 C  CA  . CYS M  1 146 ? -9.392  132.507 110.296 1.00 9.53  ? 146  CYS M CA  1 
ATOM   14196 C  C   . CYS M  1 146 ? -8.749  131.231 109.751 1.00 8.97  ? 146  CYS M C   1 
ATOM   14197 O  O   . CYS M  1 146 ? -9.438  130.320 109.250 1.00 7.89  ? 146  CYS M O   1 
ATOM   14198 C  CB  . CYS M  1 146 ? -9.305  132.484 111.830 1.00 11.35 ? 146  CYS M CB  1 
ATOM   14199 S  SG  . CYS M  1 146 ? -10.194 131.098 112.634 1.00 15.69 ? 146  CYS M SG  1 
ATOM   14200 N  N   . GLY M  1 147 ? -7.442  131.140 109.913 1.00 9.06  ? 147  GLY M N   1 
ATOM   14201 C  CA  . GLY M  1 147 ? -6.769  129.918 109.520 1.00 8.87  ? 147  GLY M CA  1 
ATOM   14202 C  C   . GLY M  1 147 ? -5.396  129.854 110.158 1.00 9.22  ? 147  GLY M C   1 
ATOM   14203 O  O   . GLY M  1 147 ? -4.856  130.860 110.589 1.00 8.75  ? 147  GLY M O   1 
ATOM   14204 N  N   . VAL M  1 148 ? -4.796  128.655 110.199 1.00 7.92  ? 148  VAL M N   1 
ATOM   14205 C  CA  . VAL M  1 148 ? -3.483  128.579 110.789 1.00 8.74  ? 148  VAL M CA  1 
ATOM   14206 C  C   . VAL M  1 148 ? -2.467  128.878 109.699 1.00 9.03  ? 148  VAL M C   1 
ATOM   14207 O  O   . VAL M  1 148 ? -2.623  128.398 108.573 1.00 9.89  ? 148  VAL M O   1 
ATOM   14208 C  CB  . VAL M  1 148 ? -3.231  127.184 111.385 1.00 9.39  ? 148  VAL M CB  1 
ATOM   14209 C  CG1 . VAL M  1 148 ? -1.833  127.130 111.989 1.00 8.67  ? 148  VAL M CG1 1 
ATOM   14210 C  CG2 . VAL M  1 148 ? -4.304  126.897 112.439 1.00 9.22  ? 148  VAL M CG2 1 
ATOM   14211 N  N   . ILE M  1 149 ? -1.434  129.655 110.006 1.00 8.68  ? 149  ILE M N   1 
ATOM   14212 C  CA  . ILE M  1 149 ? -0.426  130.002 109.003 1.00 8.06  ? 149  ILE M CA  1 
ATOM   14213 C  C   . ILE M  1 149 ? 0.573   128.833 108.866 1.00 8.38  ? 149  ILE M C   1 
ATOM   14214 O  O   . ILE M  1 149 ? 1.275   128.476 109.821 1.00 8.50  ? 149  ILE M O   1 
ATOM   14215 C  CB  . ILE M  1 149 ? 0.317   131.330 109.441 1.00 9.60  ? 149  ILE M CB  1 
ATOM   14216 C  CG1 . ILE M  1 149 ? -0.680  132.498 109.525 1.00 9.83  ? 149  ILE M CG1 1 
ATOM   14217 C  CG2 . ILE M  1 149 ? 1.456   131.704 108.475 1.00 8.65  ? 149  ILE M CG2 1 
ATOM   14218 C  CD1 . ILE M  1 149 ? -0.184  133.725 110.371 1.00 8.50  ? 149  ILE M CD1 1 
ATOM   14219 N  N   . GLY M  1 150 ? 0.675   128.258 107.678 1.00 7.67  ? 150  GLY M N   1 
ATOM   14220 C  CA  . GLY M  1 150 ? 1.543   127.093 107.529 1.00 8.90  ? 150  GLY M CA  1 
ATOM   14221 C  C   . GLY M  1 150 ? 2.696   127.326 106.579 1.00 9.39  ? 150  GLY M C   1 
ATOM   14222 O  O   . GLY M  1 150 ? 2.685   128.267 105.761 1.00 10.27 ? 150  GLY M O   1 
ATOM   14223 N  N   . ILE M  1 151 ? 3.693   126.441 106.640 1.00 9.98  ? 151  ILE M N   1 
ATOM   14224 C  CA  . ILE M  1 151 ? 4.838   126.548 105.745 1.00 10.53 ? 151  ILE M CA  1 
ATOM   14225 C  C   . ILE M  1 151 ? 4.440   126.155 104.339 1.00 10.82 ? 151  ILE M C   1 
ATOM   14226 O  O   . ILE M  1 151 ? 3.782   125.116 104.136 1.00 10.94 ? 151  ILE M O   1 
ATOM   14227 C  CB  . ILE M  1 151 ? 5.953   125.599 106.252 1.00 11.11 ? 151  ILE M CB  1 
ATOM   14228 C  CG1 . ILE M  1 151 ? 6.483   126.113 107.609 1.00 11.45 ? 151  ILE M CG1 1 
ATOM   14229 C  CG2 . ILE M  1 151 ? 7.064   125.474 105.201 1.00 13.23 ? 151  ILE M CG2 1 
ATOM   14230 C  CD1 . ILE M  1 151 ? 7.407   125.094 108.370 1.00 13.38 ? 151  ILE M CD1 1 
ATOM   14231 N  N   . ALA M  1 152 ? 4.867   126.935 103.346 1.00 10.59 ? 152  ALA M N   1 
ATOM   14232 C  CA  . ALA M  1 152 ? 4.492   126.646 101.966 1.00 12.40 ? 152  ALA M CA  1 
ATOM   14233 C  C   . ALA M  1 152 ? 5.717   126.255 101.149 1.00 13.96 ? 152  ALA M C   1 
ATOM   14234 O  O   . ALA M  1 152 ? 6.828   126.518 101.570 1.00 14.29 ? 152  ALA M O   1 
ATOM   14235 C  CB  . ALA M  1 152 ? 3.793   127.870 101.329 1.00 12.51 ? 152  ALA M CB  1 
ATOM   14236 N  N   . GLN M  1 153 ? 5.501   125.670 99.974  1.00 14.79 ? 153  GLN M N   1 
ATOM   14237 C  CA  . GLN M  1 153 ? 6.603   125.176 99.138  1.00 18.23 ? 153  GLN M CA  1 
ATOM   14238 C  C   . GLN M  1 153 ? 7.383   126.277 98.402  1.00 19.33 ? 153  GLN M C   1 
ATOM   14239 O  O   . GLN M  1 153 ? 6.782   127.202 97.864  1.00 20.84 ? 153  GLN M O   1 
ATOM   14240 C  CB  . GLN M  1 153 ? 6.073   124.137 98.150  1.00 17.54 ? 153  GLN M CB  1 
ATOM   14241 C  CG  . GLN M  1 153 ? 7.103   123.690 97.117  1.00 21.48 ? 153  GLN M CG  1 
ATOM   14242 C  CD  . GLN M  1 153 ? 6.598   122.537 96.267  1.00 23.85 ? 153  GLN M CD  1 
ATOM   14243 O  OE1 . GLN M  1 153 ? 5.588   122.669 95.561  1.00 27.05 ? 153  GLN M OE1 1 
ATOM   14244 N  NE2 . GLN M  1 153 ? 7.299   121.407 96.325  1.00 25.15 ? 153  GLN M NE2 1 
ATOM   14245 O  OXT . GLN M  1 153 ? 8.630   126.284 98.325  1.00 20.13 ? 153  GLN M OXT 1 
ATOM   14246 N  N   . ALA N  1 1   ? -1.940  132.524 46.676  1.00 28.79 ? 1    ALA N N   1 
ATOM   14247 C  CA  . ALA N  1 1   ? -1.861  133.716 47.566  1.00 28.60 ? 1    ALA N CA  1 
ATOM   14248 C  C   . ALA N  1 1   ? -0.551  133.713 48.385  1.00 27.97 ? 1    ALA N C   1 
ATOM   14249 O  O   . ALA N  1 1   ? 0.534   133.803 47.802  1.00 28.93 ? 1    ALA N O   1 
ATOM   14250 C  CB  . ALA N  1 1   ? -3.107  133.804 48.466  1.00 28.67 ? 1    ALA N CB  1 
ATOM   14251 N  N   . THR N  1 2   ? -0.650  133.571 49.710  1.00 26.48 ? 2    THR N N   1 
ATOM   14252 C  CA  . THR N  1 2   ? 0.512   133.624 50.621  1.00 24.26 ? 2    THR N CA  1 
ATOM   14253 C  C   . THR N  1 2   ? 1.736   132.770 50.247  1.00 21.95 ? 2    THR N C   1 
ATOM   14254 O  O   . THR N  1 2   ? 1.607   131.619 49.821  1.00 21.06 ? 2    THR N O   1 
ATOM   14255 C  CB  . THR N  1 2   ? 0.082   133.281 52.070  1.00 24.51 ? 2    THR N CB  1 
ATOM   14256 O  OG1 . THR N  1 2   ? -1.101  134.002 52.414  1.00 26.31 ? 2    THR N OG1 1 
ATOM   14257 C  CG2 . THR N  1 2   ? 1.070   133.832 53.061  1.00 26.40 ? 2    THR N CG2 1 
ATOM   14258 N  N   . LYS N  1 3   ? 2.923   133.352 50.403  1.00 19.13 ? 3    LYS N N   1 
ATOM   14259 C  CA  . LYS N  1 3   ? 4.181   132.635 50.165  1.00 17.49 ? 3    LYS N CA  1 
ATOM   14260 C  C   . LYS N  1 3   ? 5.163   132.943 51.275  1.00 16.32 ? 3    LYS N C   1 
ATOM   14261 O  O   . LYS N  1 3   ? 5.185   134.067 51.795  1.00 14.64 ? 3    LYS N O   1 
ATOM   14262 C  CB  . LYS N  1 3   ? 4.807   133.038 48.837  1.00 18.16 ? 3    LYS N CB  1 
ATOM   14263 C  CG  . LYS N  1 3   ? 4.123   132.431 47.607  1.00 19.59 ? 3    LYS N CG  1 
ATOM   14264 C  CD  . LYS N  1 3   ? 4.577   133.131 46.318  1.00 23.28 ? 3    LYS N CD  1 
ATOM   14265 C  CE  . LYS N  1 3   ? 4.010   132.448 45.075  1.00 24.35 ? 3    LYS N CE  1 
ATOM   14266 N  NZ  . LYS N  1 3   ? 4.083   133.295 43.843  1.00 26.70 ? 3    LYS N NZ  1 
ATOM   14267 N  N   . ALA N  1 4   ? 5.945   131.931 51.650  1.00 14.34 ? 4    ALA N N   1 
ATOM   14268 C  CA  . ALA N  1 4   ? 6.956   132.072 52.695  1.00 13.65 ? 4    ALA N CA  1 
ATOM   14269 C  C   . ALA N  1 4   ? 8.199   131.347 52.225  1.00 13.06 ? 4    ALA N C   1 
ATOM   14270 O  O   . ALA N  1 4   ? 8.144   130.538 51.292  1.00 12.41 ? 4    ALA N O   1 
ATOM   14271 C  CB  . ALA N  1 4   ? 6.468   131.465 53.999  1.00 13.70 ? 4    ALA N CB  1 
ATOM   14272 N  N   . VAL N  1 5   ? 9.312   131.605 52.899  1.00 12.21 ? 5    VAL N N   1 
ATOM   14273 C  CA  . VAL N  1 5   ? 10.578  130.987 52.535  1.00 11.57 ? 5    VAL N CA  1 
ATOM   14274 C  C   . VAL N  1 5   ? 11.399  130.816 53.799  1.00 11.45 ? 5    VAL N C   1 
ATOM   14275 O  O   . VAL N  1 5   ? 11.242  131.577 54.772  1.00 11.41 ? 5    VAL N O   1 
ATOM   14276 C  CB  . VAL N  1 5   ? 11.321  131.844 51.476  1.00 11.91 ? 5    VAL N CB  1 
ATOM   14277 C  CG1 . VAL N  1 5   ? 11.811  133.206 52.080  1.00 11.77 ? 5    VAL N CG1 1 
ATOM   14278 C  CG2 . VAL N  1 5   ? 12.486  131.066 50.816  1.00 12.83 ? 5    VAL N CG2 1 
ATOM   14279 N  N   . CYS N  1 6   ? 12.264  129.825 53.798  1.00 11.64 ? 6    CYS N N   1 
ATOM   14280 C  CA  . CYS N  1 6   ? 13.121  129.590 54.944  1.00 11.84 ? 6    CYS N CA  1 
ATOM   14281 C  C   . CYS N  1 6   ? 14.511  129.209 54.451  1.00 11.18 ? 6    CYS N C   1 
ATOM   14282 O  O   . CYS N  1 6   ? 14.649  128.296 53.623  1.00 12.53 ? 6    CYS N O   1 
ATOM   14283 C  CB  . CYS N  1 6   ? 12.513  128.459 55.781  1.00 11.49 ? 6    CYS N CB  1 
ATOM   14284 S  SG  . CYS N  1 6   ? 13.477  128.084 57.265  1.00 13.55 ? 6    CYS N SG  1 
ATOM   14285 N  N   . VAL N  1 7   ? 15.536  129.898 54.945  1.00 10.79 ? 7    VAL N N   1 
ATOM   14286 C  CA  . VAL N  1 7   ? 16.909  129.505 54.677  1.00 10.76 ? 7    VAL N CA  1 
ATOM   14287 C  C   . VAL N  1 7   ? 17.373  128.681 55.882  1.00 12.14 ? 7    VAL N C   1 
ATOM   14288 O  O   . VAL N  1 7   ? 17.425  129.206 56.998  1.00 11.40 ? 7    VAL N O   1 
ATOM   14289 C  CB  . VAL N  1 7   ? 17.814  130.750 54.487  1.00 11.16 ? 7    VAL N CB  1 
ATOM   14290 C  CG1 . VAL N  1 7   ? 19.284  130.345 54.266  1.00 10.07 ? 7    VAL N CG1 1 
ATOM   14291 C  CG2 . VAL N  1 7   ? 17.310  131.525 53.284  1.00 11.75 ? 7    VAL N CG2 1 
ATOM   14292 N  N   . LEU N  1 8   ? 17.702  127.406 55.662  1.00 10.86 ? 8    LEU N N   1 
ATOM   14293 C  CA  . LEU N  1 8   ? 18.210  126.526 56.721  1.00 11.72 ? 8    LEU N CA  1 
ATOM   14294 C  C   . LEU N  1 8   ? 19.730  126.536 56.787  1.00 11.26 ? 8    LEU N C   1 
ATOM   14295 O  O   . LEU N  1 8   ? 20.398  126.316 55.755  1.00 10.55 ? 8    LEU N O   1 
ATOM   14296 C  CB  . LEU N  1 8   ? 17.759  125.086 56.466  1.00 12.11 ? 8    LEU N CB  1 
ATOM   14297 C  CG  . LEU N  1 8   ? 16.241  125.074 56.670  1.00 17.49 ? 8    LEU N CG  1 
ATOM   14298 C  CD1 . LEU N  1 8   ? 15.563  125.145 55.330  1.00 19.24 ? 8    LEU N CD1 1 
ATOM   14299 C  CD2 . LEU N  1 8   ? 15.788  123.899 57.428  1.00 21.60 ? 8    LEU N CD2 1 
ATOM   14300 N  N   . LYS N  1 9   ? 20.258  126.797 57.985  1.00 10.48 ? 9    LYS N N   1 
ATOM   14301 C  CA  . LYS N  1 9   ? 21.689  126.768 58.230  1.00 12.42 ? 9    LYS N CA  1 
ATOM   14302 C  C   . LYS N  1 9   ? 21.901  126.173 59.607  1.00 11.58 ? 9    LYS N C   1 
ATOM   14303 O  O   . LYS N  1 9   ? 21.014  126.219 60.447  1.00 11.13 ? 9    LYS N O   1 
ATOM   14304 C  CB  . LYS N  1 9   ? 22.272  128.186 58.150  1.00 12.97 ? 9    LYS N CB  1 
ATOM   14305 C  CG  . LYS N  1 9   ? 22.272  128.780 56.702  1.00 18.65 ? 9    LYS N CG  1 
ATOM   14306 C  CD  . LYS N  1 9   ? 22.450  130.317 56.780  1.00 25.06 ? 9    LYS N CD  1 
ATOM   14307 C  CE  . LYS N  1 9   ? 23.204  130.954 55.601  1.00 25.60 ? 9    LYS N CE  1 
ATOM   14308 N  NZ  . LYS N  1 9   ? 22.924  130.381 54.275  1.00 29.30 ? 9    LYS N NZ  1 
ATOM   14309 N  N   . GLY N  1 10  ? 23.090  125.645 59.839  1.00 11.85 ? 10   GLY N N   1 
ATOM   14310 C  CA  . GLY N  1 10  ? 23.406  125.103 61.144  1.00 12.39 ? 10   GLY N CA  1 
ATOM   14311 C  C   . GLY N  1 10  ? 24.913  125.103 61.387  1.00 13.18 ? 10   GLY N C   1 
ATOM   14312 O  O   . GLY N  1 10  ? 25.693  125.815 60.734  1.00 13.32 ? 10   GLY N O   1 
ATOM   14313 N  N   . ASP N  1 11  ? 25.344  124.268 62.321  1.00 13.74 ? 11   ASP N N   1 
ATOM   14314 C  CA  . ASP N  1 11  ? 26.753  124.240 62.683  1.00 15.24 ? 11   ASP N CA  1 
ATOM   14315 C  C   . ASP N  1 11  ? 27.597  123.425 61.721  1.00 15.91 ? 11   ASP N C   1 
ATOM   14316 O  O   . ASP N  1 11  ? 28.822  123.534 61.728  1.00 15.44 ? 11   ASP N O   1 
ATOM   14317 C  CB  . ASP N  1 11  ? 26.908  123.689 64.097  1.00 16.04 ? 11   ASP N CB  1 
ATOM   14318 C  CG  . ASP N  1 11  ? 26.417  124.658 65.149  1.00 18.01 ? 11   ASP N CG  1 
ATOM   14319 O  OD1 . ASP N  1 11  ? 26.408  125.875 64.859  1.00 19.01 ? 11   ASP N OD1 1 
ATOM   14320 O  OD2 . ASP N  1 11  ? 26.021  124.297 66.279  1.00 20.51 ? 11   ASP N OD2 1 
ATOM   14321 N  N   . GLY N  1 12  ? 26.950  122.594 60.904  1.00 15.32 ? 12   GLY N N   1 
ATOM   14322 C  CA  . GLY N  1 12  ? 27.667  121.683 60.014  1.00 14.71 ? 12   GLY N CA  1 
ATOM   14323 C  C   . GLY N  1 12  ? 27.434  122.027 58.566  1.00 15.18 ? 12   GLY N C   1 
ATOM   14324 O  O   . GLY N  1 12  ? 27.143  123.189 58.242  1.00 15.91 ? 12   GLY N O   1 
ATOM   14325 N  N   . PRO N  1 13  ? 27.531  121.042 57.683  1.00 14.27 ? 13   PRO N N   1 
ATOM   14326 C  CA  . PRO N  1 13  ? 27.418  121.303 56.255  1.00 14.28 ? 13   PRO N CA  1 
ATOM   14327 C  C   . PRO N  1 13  ? 25.987  121.264 55.741  1.00 13.66 ? 13   PRO N C   1 
ATOM   14328 O  O   . PRO N  1 13  ? 25.789  121.439 54.547  1.00 13.33 ? 13   PRO N O   1 
ATOM   14329 C  CB  . PRO N  1 13  ? 28.215  120.157 55.661  1.00 14.96 ? 13   PRO N CB  1 
ATOM   14330 C  CG  . PRO N  1 13  ? 27.841  119.027 56.540  1.00 13.24 ? 13   PRO N CG  1 
ATOM   14331 C  CD  . PRO N  1 13  ? 27.720  119.603 57.946  1.00 14.98 ? 13   PRO N CD  1 
ATOM   14332 N  N   . VAL N  1 14  ? 25.010  121.043 56.611  1.00 12.81 ? 14   VAL N N   1 
ATOM   14333 C  CA  . VAL N  1 14  ? 23.642  121.015 56.140  1.00 11.44 ? 14   VAL N CA  1 
ATOM   14334 C  C   . VAL N  1 14  ? 23.111  122.416 55.929  1.00 12.44 ? 14   VAL N C   1 
ATOM   14335 O  O   . VAL N  1 14  ? 23.184  123.269 56.811  1.00 11.82 ? 14   VAL N O   1 
ATOM   14336 C  CB  . VAL N  1 14  ? 22.700  120.262 57.128  1.00 12.03 ? 14   VAL N CB  1 
ATOM   14337 C  CG1 . VAL N  1 14  ? 21.256  120.254 56.613  1.00 11.43 ? 14   VAL N CG1 1 
ATOM   14338 C  CG2 . VAL N  1 14  ? 23.176  118.833 57.278  1.00 9.25  ? 14   VAL N CG2 1 
ATOM   14339 N  N   . GLN N  1 15  ? 22.559  122.648 54.753  1.00 12.63 ? 15   GLN N N   1 
ATOM   14340 C  CA  . GLN N  1 15  ? 21.998  123.948 54.442  1.00 13.67 ? 15   GLN N CA  1 
ATOM   14341 C  C   . GLN N  1 15  ? 21.050  123.773 53.295  1.00 13.09 ? 15   GLN N C   1 
ATOM   14342 O  O   . GLN N  1 15  ? 21.203  122.841 52.472  1.00 13.48 ? 15   GLN N O   1 
ATOM   14343 C  CB  . GLN N  1 15  ? 23.087  124.974 54.086  1.00 14.60 ? 15   GLN N CB  1 
ATOM   14344 C  CG  . GLN N  1 15  ? 24.023  124.569 52.998  1.00 18.63 ? 15   GLN N CG  1 
ATOM   14345 C  CD  . GLN N  1 15  ? 24.996  125.698 52.637  1.00 26.90 ? 15   GLN N CD  1 
ATOM   14346 O  OE1 . GLN N  1 15  ? 25.386  125.824 51.485  1.00 30.27 ? 15   GLN N OE1 1 
ATOM   14347 N  NE2 . GLN N  1 15  ? 25.364  126.526 53.620  1.00 29.63 ? 15   GLN N NE2 1 
ATOM   14348 N  N   . GLY N  1 16  ? 20.058  124.651 53.236  1.00 12.36 ? 16   GLY N N   1 
ATOM   14349 C  CA  . GLY N  1 16  ? 19.068  124.564 52.187  1.00 12.36 ? 16   GLY N CA  1 
ATOM   14350 C  C   . GLY N  1 16  ? 18.094  125.716 52.190  1.00 12.35 ? 16   GLY N C   1 
ATOM   14351 O  O   . GLY N  1 16  ? 18.196  126.632 53.007  1.00 11.00 ? 16   GLY N O   1 
ATOM   14352 N  N   . ILE N  1 17  ? 17.143  125.651 51.259  1.00 12.52 ? 17   ILE N N   1 
ATOM   14353 C  CA  . ILE N  1 17  ? 16.123  126.667 51.090  1.00 12.56 ? 17   ILE N CA  1 
ATOM   14354 C  C   . ILE N  1 17  ? 14.810  125.958 50.893  1.00 12.53 ? 17   ILE N C   1 
ATOM   14355 O  O   . ILE N  1 17  ? 14.705  125.061 50.011  1.00 12.72 ? 17   ILE N O   1 
ATOM   14356 C  CB  . ILE N  1 17  ? 16.407  127.518 49.830  1.00 14.43 ? 17   ILE N CB  1 
ATOM   14357 C  CG1 . ILE N  1 17  ? 17.690  128.332 49.997  1.00 15.45 ? 17   ILE N CG1 1 
ATOM   14358 C  CG2 . ILE N  1 17  ? 15.203  128.451 49.545  1.00 14.46 ? 17   ILE N CG2 1 
ATOM   14359 C  CD1 . ILE N  1 17  ? 18.000  129.258 48.772  1.00 19.03 ? 17   ILE N CD1 1 
ATOM   14360 N  N   . ILE N  1 18  ? 13.821  126.309 51.701  1.00 10.96 ? 18   ILE N N   1 
ATOM   14361 C  CA  . ILE N  1 18  ? 12.514  125.676 51.602  1.00 11.01 ? 18   ILE N CA  1 
ATOM   14362 C  C   . ILE N  1 18  ? 11.454  126.740 51.373  1.00 12.01 ? 18   ILE N C   1 
ATOM   14363 O  O   . ILE N  1 18  ? 11.408  127.763 52.106  1.00 12.10 ? 18   ILE N O   1 
ATOM   14364 C  CB  . ILE N  1 18  ? 12.191  124.863 52.868  1.00 10.01 ? 18   ILE N CB  1 
ATOM   14365 C  CG1 . ILE N  1 18  ? 13.177  123.674 53.037  1.00 10.20 ? 18   ILE N CG1 1 
ATOM   14366 C  CG2 . ILE N  1 18  ? 10.676  124.525 52.922  1.00 10.81 ? 18   ILE N CG2 1 
ATOM   14367 C  CD1 . ILE N  1 18  ? 13.075  122.584 51.918  1.00 10.14 ? 18   ILE N CD1 1 
ATOM   14368 N  N   . ASN N  1 19  ? 10.624  126.498 50.361  1.00 11.16 ? 19   ASN N N   1 
ATOM   14369 C  CA  . ASN N  1 19  ? 9.563   127.411 49.981  1.00 13.05 ? 19   ASN N CA  1 
ATOM   14370 C  C   . ASN N  1 19  ? 8.244   126.883 50.479  1.00 12.85 ? 19   ASN N C   1 
ATOM   14371 O  O   . ASN N  1 19  ? 8.080   125.672 50.607  1.00 11.92 ? 19   ASN N O   1 
ATOM   14372 C  CB  . ASN N  1 19  ? 9.484   127.519 48.454  1.00 13.03 ? 19   ASN N CB  1 
ATOM   14373 C  CG  . ASN N  1 19  ? 10.809  127.903 47.825  1.00 14.86 ? 19   ASN N CG  1 
ATOM   14374 O  OD1 . ASN N  1 19  ? 11.494  127.078 47.205  1.00 18.81 ? 19   ASN N OD1 1 
ATOM   14375 N  ND2 . ASN N  1 19  ? 11.182  129.141 47.985  1.00 9.65  ? 19   ASN N ND2 1 
ATOM   14376 N  N   . PHE N  1 20  ? 7.308   127.794 50.758  1.00 13.25 ? 20   PHE N N   1 
ATOM   14377 C  CA  . PHE N  1 20  ? 5.970   127.443 51.213  1.00 13.70 ? 20   PHE N CA  1 
ATOM   14378 C  C   . PHE N  1 20  ? 5.008   128.278 50.414  1.00 14.34 ? 20   PHE N C   1 
ATOM   14379 O  O   . PHE N  1 20  ? 5.245   129.482 50.213  1.00 13.69 ? 20   PHE N O   1 
ATOM   14380 C  CB  . PHE N  1 20  ? 5.692   127.811 52.690  1.00 13.56 ? 20   PHE N CB  1 
ATOM   14381 C  CG  . PHE N  1 20  ? 6.609   127.165 53.708  1.00 12.83 ? 20   PHE N CG  1 
ATOM   14382 C  CD1 . PHE N  1 20  ? 7.894   127.642 53.903  1.00 12.77 ? 20   PHE N CD1 1 
ATOM   14383 C  CD2 . PHE N  1 20  ? 6.147   126.152 54.527  1.00 12.70 ? 20   PHE N CD2 1 
ATOM   14384 C  CE1 . PHE N  1 20  ? 8.721   127.081 54.882  1.00 12.69 ? 20   PHE N CE1 1 
ATOM   14385 C  CE2 . PHE N  1 20  ? 6.964   125.568 55.469  1.00 14.24 ? 20   PHE N CE2 1 
ATOM   14386 C  CZ  . PHE N  1 20  ? 8.251   126.034 55.660  1.00 14.98 ? 20   PHE N CZ  1 
ATOM   14387 N  N   . GLU N  1 21  ? 3.898   127.666 49.998  1.00 14.95 ? 21   GLU N N   1 
ATOM   14388 C  CA  . GLU N  1 21  ? 2.851   128.399 49.290  1.00 17.53 ? 21   GLU N CA  1 
ATOM   14389 C  C   . GLU N  1 21  ? 1.443   127.922 49.652  1.00 17.76 ? 21   GLU N C   1 
ATOM   14390 O  O   . GLU N  1 21  ? 1.167   126.728 49.698  1.00 16.24 ? 21   GLU N O   1 
ATOM   14391 C  CB  . GLU N  1 21  ? 3.014   128.310 47.777  1.00 17.48 ? 21   GLU N CB  1 
ATOM   14392 C  CG  . GLU N  1 21  ? 1.724   128.669 47.058  1.00 22.52 ? 21   GLU N CG  1 
ATOM   14393 C  CD  . GLU N  1 21  ? 1.941   128.967 45.594  1.00 26.77 ? 21   GLU N CD  1 
ATOM   14394 O  OE1 . GLU N  1 21  ? 3.066   129.385 45.252  1.00 28.62 ? 21   GLU N OE1 1 
ATOM   14395 O  OE2 . GLU N  1 21  ? 0.991   128.779 44.793  1.00 30.61 ? 21   GLU N OE2 1 
ATOM   14396 N  N   . GLN N  1 22  ? 0.546   128.878 49.872  1.00 18.08 ? 22   GLN N N   1 
ATOM   14397 C  CA  . GLN N  1 22  ? -0.824  128.560 50.228  1.00 19.40 ? 22   GLN N CA  1 
ATOM   14398 C  C   . GLN N  1 22  ? -1.750  129.421 49.391  1.00 20.71 ? 22   GLN N C   1 
ATOM   14399 O  O   . GLN N  1 22  ? -1.752  130.639 49.537  1.00 20.35 ? 22   GLN N O   1 
ATOM   14400 C  CB  . GLN N  1 22  ? -1.057  128.856 51.699  1.00 19.53 ? 22   GLN N CB  1 
ATOM   14401 C  CG  . GLN N  1 22  ? -2.340  128.285 52.262  1.00 19.33 ? 22   GLN N CG  1 
ATOM   14402 C  CD  . GLN N  1 22  ? -2.519  128.633 53.717  1.00 19.02 ? 22   GLN N CD  1 
ATOM   14403 O  OE1 . GLN N  1 22  ? -1.921  129.593 54.204  1.00 21.63 ? 22   GLN N OE1 1 
ATOM   14404 N  NE2 . GLN N  1 22  ? -3.333  127.855 54.419  1.00 19.40 ? 22   GLN N NE2 1 
ATOM   14405 N  N   . LYS N  1 23  ? -2.527  128.788 48.517  1.00 22.43 ? 23   LYS N N   1 
ATOM   14406 C  CA  . LYS N  1 23  ? -3.428  129.547 47.650  1.00 24.54 ? 23   LYS N CA  1 
ATOM   14407 C  C   . LYS N  1 23  ? -4.688  130.001 48.367  1.00 25.13 ? 23   LYS N C   1 
ATOM   14408 O  O   . LYS N  1 23  ? -5.308  130.977 47.957  1.00 25.10 ? 23   LYS N O   1 
ATOM   14409 C  CB  . LYS N  1 23  ? -3.801  128.747 46.394  1.00 24.95 ? 23   LYS N CB  1 
ATOM   14410 C  CG  . LYS N  1 23  ? -2.607  128.397 45.516  1.00 27.05 ? 23   LYS N CG  1 
ATOM   14411 C  CD  . LYS N  1 23  ? -3.039  127.912 44.148  1.00 29.88 ? 23   LYS N CD  1 
ATOM   14412 C  CE  . LYS N  1 23  ? -3.842  126.620 44.235  1.00 30.76 ? 23   LYS N CE  1 
ATOM   14413 N  NZ  . LYS N  1 23  ? -4.747  126.436 43.053  1.00 32.83 ? 23   LYS N NZ  1 
ATOM   14414 N  N   . GLU N  1 24  ? -5.050  129.324 49.451  1.00 25.83 ? 24   GLU N N   1 
ATOM   14415 C  CA  . GLU N  1 24  ? -6.307  129.645 50.120  1.00 27.44 ? 24   GLU N CA  1 
ATOM   14416 C  C   . GLU N  1 24  ? -6.288  129.483 51.638  1.00 27.30 ? 24   GLU N C   1 
ATOM   14417 O  O   . GLU N  1 24  ? -5.628  128.593 52.169  1.00 26.76 ? 24   GLU N O   1 
ATOM   14418 C  CB  . GLU N  1 24  ? -7.436  128.797 49.510  1.00 27.39 ? 24   GLU N CB  1 
ATOM   14419 C  CG  . GLU N  1 24  ? -8.030  129.407 48.251  1.00 31.87 ? 24   GLU N CG  1 
ATOM   14420 C  CD  . GLU N  1 24  ? -8.237  128.414 47.111  1.00 37.16 ? 24   GLU N CD  1 
ATOM   14421 O  OE1 . GLU N  1 24  ? -8.425  127.196 47.365  1.00 38.11 ? 24   GLU N OE1 1 
ATOM   14422 O  OE2 . GLU N  1 24  ? -8.221  128.868 45.939  1.00 39.31 ? 24   GLU N OE2 1 
ATOM   14423 N  N   . SER N  1 25  ? -7.041  130.337 52.329  1.00 27.24 ? 25   SER N N   1 
ATOM   14424 C  CA  . SER N  1 25  ? -7.136  130.246 53.784  1.00 27.37 ? 25   SER N CA  1 
ATOM   14425 C  C   . SER N  1 25  ? -7.633  128.862 54.211  1.00 27.03 ? 25   SER N C   1 
ATOM   14426 O  O   . SER N  1 25  ? -8.521  128.284 53.565  1.00 26.31 ? 25   SER N O   1 
ATOM   14427 C  CB  . SER N  1 25  ? -8.033  131.360 54.346  1.00 27.41 ? 25   SER N CB  1 
ATOM   14428 O  OG  . SER N  1 25  ? -9.220  131.525 53.581  1.00 28.60 ? 25   SER N OG  1 
ATOM   14429 N  N   . ASN N  1 26  ? -7.029  128.327 55.275  1.00 26.67 ? 26   ASN N N   1 
ATOM   14430 C  CA  . ASN N  1 26  ? -7.358  126.995 55.791  1.00 26.74 ? 26   ASN N CA  1 
ATOM   14431 C  C   . ASN N  1 26  ? -7.073  125.882 54.771  1.00 25.72 ? 26   ASN N C   1 
ATOM   14432 O  O   . ASN N  1 26  ? -7.505  124.732 54.950  1.00 26.29 ? 26   ASN N O   1 
ATOM   14433 C  CB  . ASN N  1 26  ? -8.838  126.899 56.199  1.00 26.97 ? 26   ASN N CB  1 
ATOM   14434 C  CG  . ASN N  1 26  ? -9.271  127.987 57.182  1.00 29.17 ? 26   ASN N CG  1 
ATOM   14435 O  OD1 . ASN N  1 26  ? -8.447  128.579 57.885  1.00 31.54 ? 26   ASN N OD1 1 
ATOM   14436 N  ND2 . ASN N  1 26  ? -10.583 128.244 57.240  1.00 29.21 ? 26   ASN N ND2 1 
ATOM   14437 N  N   . GLY N  1 27  ? -6.393  126.226 53.683  1.00 24.06 ? 27   GLY N N   1 
ATOM   14438 C  CA  . GLY N  1 27  ? -6.128  125.258 52.632  1.00 22.66 ? 27   GLY N CA  1 
ATOM   14439 C  C   . GLY N  1 27  ? -4.727  124.672 52.711  1.00 21.28 ? 27   GLY N C   1 
ATOM   14440 O  O   . GLY N  1 27  ? -3.938  125.060 53.560  1.00 20.90 ? 27   GLY N O   1 
ATOM   14441 N  N   . PRO N  1 28  ? -4.412  123.769 51.786  1.00 20.74 ? 28   PRO N N   1 
ATOM   14442 C  CA  . PRO N  1 28  ? -3.125  123.066 51.778  1.00 19.47 ? 28   PRO N CA  1 
ATOM   14443 C  C   . PRO N  1 28  ? -1.955  123.977 51.473  1.00 18.58 ? 28   PRO N C   1 
ATOM   14444 O  O   . PRO N  1 28  ? -2.031  124.874 50.620  1.00 18.07 ? 28   PRO N O   1 
ATOM   14445 C  CB  . PRO N  1 28  ? -3.250  122.087 50.614  1.00 20.16 ? 28   PRO N CB  1 
ATOM   14446 C  CG  . PRO N  1 28  ? -4.678  122.112 50.189  1.00 20.69 ? 28   PRO N CG  1 
ATOM   14447 C  CD  . PRO N  1 28  ? -5.267  123.395 50.650  1.00 20.51 ? 28   PRO N CD  1 
ATOM   14448 N  N   . VAL N  1 29  ? -0.861  123.723 52.166  1.00 16.60 ? 29   VAL N N   1 
ATOM   14449 C  CA  . VAL N  1 29  ? 0.363   124.453 51.931  1.00 15.85 ? 29   VAL N CA  1 
ATOM   14450 C  C   . VAL N  1 29  ? 1.304   123.499 51.210  1.00 15.51 ? 29   VAL N C   1 
ATOM   14451 O  O   . VAL N  1 29  ? 1.519   122.381 51.671  1.00 15.22 ? 29   VAL N O   1 
ATOM   14452 C  CB  . VAL N  1 29  ? 1.009   124.885 53.255  1.00 15.66 ? 29   VAL N CB  1 
ATOM   14453 C  CG1 . VAL N  1 29  ? 2.287   125.650 53.006  1.00 15.11 ? 29   VAL N CG1 1 
ATOM   14454 C  CG2 . VAL N  1 29  ? 0.016   125.771 54.068  1.00 15.58 ? 29   VAL N CG2 1 
ATOM   14455 N  N   . LYS N  1 30  ? 1.840   123.952 50.080  1.00 14.58 ? 30   LYS N N   1 
ATOM   14456 C  CA  . LYS N  1 30  ? 2.874   123.237 49.361  1.00 14.81 ? 30   LYS N CA  1 
ATOM   14457 C  C   . LYS N  1 30  ? 4.197   123.604 50.002  1.00 13.70 ? 30   LYS N C   1 
ATOM   14458 O  O   . LYS N  1 30  ? 4.475   124.798 50.180  1.00 14.03 ? 30   LYS N O   1 
ATOM   14459 C  CB  . LYS N  1 30  ? 2.934   123.739 47.917  1.00 16.19 ? 30   LYS N CB  1 
ATOM   14460 C  CG  . LYS N  1 30  ? 3.783   122.843 47.013  1.00 21.29 ? 30   LYS N CG  1 
ATOM   14461 C  CD  . LYS N  1 30  ? 3.988   123.448 45.615  1.00 28.81 ? 30   LYS N CD  1 
ATOM   14462 C  CE  . LYS N  1 30  ? 4.848   122.531 44.716  1.00 31.93 ? 30   LYS N CE  1 
ATOM   14463 N  NZ  . LYS N  1 30  ? 5.448   123.280 43.558  1.00 34.23 ? 30   LYS N NZ  1 
ATOM   14464 N  N   . VAL N  1 31  ? 5.014   122.615 50.334  1.00 11.79 ? 31   VAL N N   1 
ATOM   14465 C  CA  . VAL N  1 31  ? 6.327   122.852 50.959  1.00 11.59 ? 31   VAL N CA  1 
ATOM   14466 C  C   . VAL N  1 31  ? 7.363   122.235 50.032  1.00 11.90 ? 31   VAL N C   1 
ATOM   14467 O  O   . VAL N  1 31  ? 7.302   121.017 49.797  1.00 11.91 ? 31   VAL N O   1 
ATOM   14468 C  CB  . VAL N  1 31  ? 6.386   122.151 52.349  1.00 11.31 ? 31   VAL N CB  1 
ATOM   14469 C  CG1 . VAL N  1 31  ? 7.673   122.466 53.066  1.00 10.99 ? 31   VAL N CG1 1 
ATOM   14470 C  CG2 . VAL N  1 31  ? 5.199   122.608 53.226  1.00 10.07 ? 31   VAL N CG2 1 
ATOM   14471 N  N   . TRP N  1 32  ? 8.312   123.015 49.507  1.00 10.96 ? 32   TRP N N   1 
ATOM   14472 C  CA  . TRP N  1 32  ? 9.289   122.406 48.580  1.00 11.64 ? 32   TRP N CA  1 
ATOM   14473 C  C   . TRP N  1 32  ? 10.610  123.125 48.507  1.00 11.40 ? 32   TRP N C   1 
ATOM   14474 O  O   . TRP N  1 32  ? 10.706  124.325 48.769  1.00 12.19 ? 32   TRP N O   1 
ATOM   14475 C  CB  . TRP N  1 32  ? 8.733   122.273 47.157  1.00 11.25 ? 32   TRP N CB  1 
ATOM   14476 C  CG  . TRP N  1 32  ? 8.836   123.532 46.356  1.00 13.49 ? 32   TRP N CG  1 
ATOM   14477 C  CD1 . TRP N  1 32  ? 9.789   123.849 45.423  1.00 13.44 ? 32   TRP N CD1 1 
ATOM   14478 C  CD2 . TRP N  1 32  ? 7.980   124.652 46.444  1.00 14.88 ? 32   TRP N CD2 1 
ATOM   14479 N  NE1 . TRP N  1 32  ? 9.549   125.092 44.900  1.00 17.85 ? 32   TRP N NE1 1 
ATOM   14480 C  CE2 . TRP N  1 32  ? 8.437   125.611 45.510  1.00 17.72 ? 32   TRP N CE2 1 
ATOM   14481 C  CE3 . TRP N  1 32  ? 6.848   124.943 47.199  1.00 16.33 ? 32   TRP N CE3 1 
ATOM   14482 C  CZ2 . TRP N  1 32  ? 7.810   126.837 45.327  1.00 19.03 ? 32   TRP N CZ2 1 
ATOM   14483 C  CZ3 . TRP N  1 32  ? 6.226   126.165 47.020  1.00 16.94 ? 32   TRP N CZ3 1 
ATOM   14484 C  CH2 . TRP N  1 32  ? 6.705   127.094 46.092  1.00 20.48 ? 32   TRP N CH2 1 
ATOM   14485 N  N   . GLY N  1 33  ? 11.638  122.389 48.132  1.00 11.44 ? 33   GLY N N   1 
ATOM   14486 C  CA  . GLY N  1 33  ? 12.945  122.969 47.985  1.00 11.96 ? 33   GLY N CA  1 
ATOM   14487 C  C   . GLY N  1 33  ? 13.989  121.902 48.097  1.00 12.82 ? 33   GLY N C   1 
ATOM   14488 O  O   . GLY N  1 33  ? 13.720  120.733 47.892  1.00 12.34 ? 33   GLY N O   1 
ATOM   14489 N  N   . SER N  1 34  ? 15.189  122.324 48.455  1.00 13.09 ? 34   SER N N   1 
ATOM   14490 C  CA  . SER N  1 34  ? 16.314  121.421 48.448  1.00 14.06 ? 34   SER N CA  1 
ATOM   14491 C  C   . SER N  1 34  ? 17.171  121.644 49.683  1.00 13.66 ? 34   SER N C   1 
ATOM   14492 O  O   . SER N  1 34  ? 17.405  122.806 50.094  1.00 14.02 ? 34   SER N O   1 
ATOM   14493 C  CB  . SER N  1 34  ? 17.112  121.738 47.172  1.00 14.83 ? 34   SER N CB  1 
ATOM   14494 O  OG  . SER N  1 34  ? 18.300  120.996 47.088  1.00 19.54 ? 34   SER N OG  1 
ATOM   14495 N  N   . ILE N  1 35  ? 17.636  120.555 50.281  1.00 12.80 ? 35   ILE N N   1 
ATOM   14496 C  CA  . ILE N  1 35  ? 18.530  120.621 51.420  1.00 12.24 ? 35   ILE N CA  1 
ATOM   14497 C  C   . ILE N  1 35  ? 19.733  119.758 51.090  1.00 12.56 ? 35   ILE N C   1 
ATOM   14498 O  O   . ILE N  1 35  ? 19.561  118.611 50.647  1.00 13.11 ? 35   ILE N O   1 
ATOM   14499 C  CB  . ILE N  1 35  ? 17.844  120.081 52.703  1.00 11.52 ? 35   ILE N CB  1 
ATOM   14500 C  CG1 . ILE N  1 35  ? 16.555  120.850 52.964  1.00 12.23 ? 35   ILE N CG1 1 
ATOM   14501 C  CG2 . ILE N  1 35  ? 18.751  120.302 53.903  1.00 12.68 ? 35   ILE N CG2 1 
ATOM   14502 C  CD1 . ILE N  1 35  ? 15.714  120.298 54.195  1.00 14.86 ? 35   ILE N CD1 1 
ATOM   14503 N  N   . LYS N  1 36  ? 20.952  120.267 51.292  1.00 12.47 ? 36   LYS N N   1 
ATOM   14504 C  CA  . LYS N  1 36  ? 22.114  119.452 50.933  1.00 13.28 ? 36   LYS N CA  1 
ATOM   14505 C  C   . LYS N  1 36  ? 22.975  119.205 52.144  1.00 13.31 ? 36   LYS N C   1 
ATOM   14506 O  O   . LYS N  1 36  ? 22.728  119.765 53.207  1.00 12.60 ? 36   LYS N O   1 
ATOM   14507 C  CB  . LYS N  1 36  ? 22.956  120.149 49.857  1.00 14.51 ? 36   LYS N CB  1 
ATOM   14508 C  CG  . LYS N  1 36  ? 23.642  121.383 50.388  1.00 15.94 ? 36   LYS N CG  1 
ATOM   14509 C  CD  . LYS N  1 36  ? 24.521  122.004 49.287  1.00 22.64 ? 36   LYS N CD  1 
ATOM   14510 C  CE  . LYS N  1 36  ? 25.221  123.252 49.767  1.00 24.85 ? 36   LYS N CE  1 
ATOM   14511 N  NZ  . LYS N  1 36  ? 26.460  123.443 48.949  1.00 29.08 ? 36   LYS N NZ  1 
ATOM   14512 N  N   . GLY N  1 37  ? 23.973  118.334 52.001  1.00 12.98 ? 37   GLY N N   1 
ATOM   14513 C  CA  . GLY N  1 37  ? 24.891  118.079 53.104  1.00 12.92 ? 37   GLY N CA  1 
ATOM   14514 C  C   . GLY N  1 37  ? 24.437  117.053 54.120  1.00 13.29 ? 37   GLY N C   1 
ATOM   14515 O  O   . GLY N  1 37  ? 25.067  116.885 55.181  1.00 14.12 ? 37   GLY N O   1 
ATOM   14516 N  N   . LEU N  1 38  ? 23.347  116.363 53.802  1.00 11.64 ? 38   LEU N N   1 
ATOM   14517 C  CA  . LEU N  1 38  ? 22.749  115.383 54.693  1.00 12.08 ? 38   LEU N CA  1 
ATOM   14518 C  C   . LEU N  1 38  ? 23.248  113.980 54.433  1.00 13.18 ? 38   LEU N C   1 
ATOM   14519 O  O   . LEU N  1 38  ? 23.702  113.676 53.322  1.00 13.48 ? 38   LEU N O   1 
ATOM   14520 C  CB  . LEU N  1 38  ? 21.240  115.358 54.432  1.00 12.19 ? 38   LEU N CB  1 
ATOM   14521 C  CG  . LEU N  1 38  ? 20.438  116.595 54.872  1.00 12.29 ? 38   LEU N CG  1 
ATOM   14522 C  CD1 . LEU N  1 38  ? 19.060  116.594 54.199  1.00 11.18 ? 38   LEU N CD1 1 
ATOM   14523 C  CD2 . LEU N  1 38  ? 20.222  116.566 56.388  1.00 9.59  ? 38   LEU N CD2 1 
ATOM   14524 N  N   . THR N  1 39  ? 23.172  113.121 55.441  1.00 13.14 ? 39   THR N N   1 
ATOM   14525 C  CA  . THR N  1 39  ? 23.473  111.714 55.192  1.00 14.36 ? 39   THR N CA  1 
ATOM   14526 C  C   . THR N  1 39  ? 22.290  111.118 54.428  1.00 14.10 ? 39   THR N C   1 
ATOM   14527 O  O   . THR N  1 39  ? 21.131  111.536 54.592  1.00 13.50 ? 39   THR N O   1 
ATOM   14528 C  CB  . THR N  1 39  ? 23.634  110.932 56.502  1.00 14.30 ? 39   THR N CB  1 
ATOM   14529 O  OG1 . THR N  1 39  ? 22.522  111.217 57.366  1.00 15.55 ? 39   THR N OG1 1 
ATOM   14530 C  CG2 . THR N  1 39  ? 24.844  111.400 57.289  1.00 15.76 ? 39   THR N CG2 1 
ATOM   14531 N  N   . GLU N  1 40  ? 22.588  110.153 53.573  1.00 14.42 ? 40   GLU N N   1 
ATOM   14532 C  CA  . GLU N  1 40  ? 21.572  109.468 52.813  1.00 14.66 ? 40   GLU N CA  1 
ATOM   14533 C  C   . GLU N  1 40  ? 20.494  108.903 53.726  1.00 14.58 ? 40   GLU N C   1 
ATOM   14534 O  O   . GLU N  1 40  ? 20.782  108.298 54.756  1.00 16.07 ? 40   GLU N O   1 
ATOM   14535 C  CB  . GLU N  1 40  ? 22.216  108.317 52.019  1.00 15.48 ? 40   GLU N CB  1 
ATOM   14536 C  CG  . GLU N  1 40  ? 21.255  107.644 51.056  1.00 16.61 ? 40   GLU N CG  1 
ATOM   14537 C  CD  . GLU N  1 40  ? 21.836  106.408 50.422  1.00 22.74 ? 40   GLU N CD  1 
ATOM   14538 O  OE1 . GLU N  1 40  ? 22.915  105.933 50.883  1.00 21.46 ? 40   GLU N OE1 1 
ATOM   14539 O  OE2 . GLU N  1 40  ? 21.206  105.915 49.458  1.00 23.20 ? 40   GLU N OE2 1 
ATOM   14540 N  N   . GLY N  1 41  ? 19.236  109.067 53.368  1.00 13.58 ? 41   GLY N N   1 
ATOM   14541 C  CA  . GLY N  1 41  ? 18.213  108.466 54.192  1.00 12.50 ? 41   GLY N CA  1 
ATOM   14542 C  C   . GLY N  1 41  ? 17.208  109.461 54.765  1.00 12.24 ? 41   GLY N C   1 
ATOM   14543 O  O   . GLY N  1 41  ? 17.129  110.613 54.326  1.00 10.31 ? 41   GLY N O   1 
ATOM   14544 N  N   . LEU N  1 42  ? 16.391  108.993 55.706  1.00 12.10 ? 42   LEU N N   1 
ATOM   14545 C  CA  . LEU N  1 42  ? 15.314  109.835 56.256  1.00 12.50 ? 42   LEU N CA  1 
ATOM   14546 C  C   . LEU N  1 42  ? 15.816  110.790 57.323  1.00 12.72 ? 42   LEU N C   1 
ATOM   14547 O  O   . LEU N  1 42  ? 16.706  110.445 58.100  1.00 12.82 ? 42   LEU N O   1 
ATOM   14548 C  CB  . LEU N  1 42  ? 14.229  108.973 56.886  1.00 12.59 ? 42   LEU N CB  1 
ATOM   14549 C  CG  . LEU N  1 42  ? 13.428  108.008 56.015  1.00 14.14 ? 42   LEU N CG  1 
ATOM   14550 C  CD1 . LEU N  1 42  ? 12.700  107.026 56.951  1.00 15.13 ? 42   LEU N CD1 1 
ATOM   14551 C  CD2 . LEU N  1 42  ? 12.424  108.736 55.138  1.00 11.94 ? 42   LEU N CD2 1 
ATOM   14552 N  N   . HIS N  1 43  ? 15.228  111.988 57.357  1.00 12.56 ? 43   HIS N N   1 
ATOM   14553 C  CA  . HIS N  1 43  ? 15.538  113.023 58.355  1.00 11.37 ? 43   HIS N CA  1 
ATOM   14554 C  C   . HIS N  1 43  ? 14.258  113.697 58.799  1.00 11.39 ? 43   HIS N C   1 
ATOM   14555 O  O   . HIS N  1 43  ? 13.484  114.130 57.974  1.00 10.58 ? 43   HIS N O   1 
ATOM   14556 C  CB  . HIS N  1 43  ? 16.462  114.082 57.730  1.00 11.31 ? 43   HIS N CB  1 
ATOM   14557 C  CG  . HIS N  1 43  ? 17.824  113.549 57.421  1.00 11.63 ? 43   HIS N CG  1 
ATOM   14558 N  ND1 . HIS N  1 43  ? 18.833  113.541 58.355  1.00 11.09 ? 43   HIS N ND1 1 
ATOM   14559 C  CD2 . HIS N  1 43  ? 18.315  112.920 56.322  1.00 12.85 ? 43   HIS N CD2 1 
ATOM   14560 C  CE1 . HIS N  1 43  ? 19.903  112.960 57.832  1.00 15.53 ? 43   HIS N CE1 1 
ATOM   14561 N  NE2 . HIS N  1 43  ? 19.602  112.542 56.614  1.00 14.21 ? 43   HIS N NE2 1 
ATOM   14562 N  N   . GLY N  1 44  ? 14.048  113.811 60.104  1.00 10.07 ? 44   GLY N N   1 
ATOM   14563 C  CA  . GLY N  1 44  ? 12.843  114.445 60.623  1.00 10.06 ? 44   GLY N CA  1 
ATOM   14564 C  C   . GLY N  1 44  ? 12.825  115.897 60.163  1.00 11.68 ? 44   GLY N C   1 
ATOM   14565 O  O   . GLY N  1 44  ? 13.880  116.531 60.001  1.00 10.80 ? 44   GLY N O   1 
ATOM   14566 N  N   . PHE N  1 45  ? 11.622  116.424 59.979  1.00 10.93 ? 45   PHE N N   1 
ATOM   14567 C  CA  . PHE N  1 45  ? 11.437  117.736 59.384  1.00 10.68 ? 45   PHE N CA  1 
ATOM   14568 C  C   . PHE N  1 45  ? 10.220  118.357 60.053  1.00 11.33 ? 45   PHE N C   1 
ATOM   14569 O  O   . PHE N  1 45  ? 9.102   117.911 59.842  1.00 11.00 ? 45   PHE N O   1 
ATOM   14570 C  CB  . PHE N  1 45  ? 11.201  117.475 57.906  1.00 10.69 ? 45   PHE N CB  1 
ATOM   14571 C  CG  . PHE N  1 45  ? 11.157  118.692 57.016  1.00 10.91 ? 45   PHE N CG  1 
ATOM   14572 C  CD1 . PHE N  1 45  ? 12.274  119.484 56.833  1.00 10.50 ? 45   PHE N CD1 1 
ATOM   14573 C  CD2 . PHE N  1 45  ? 10.008  118.961 56.278  1.00 9.55  ? 45   PHE N CD2 1 
ATOM   14574 C  CE1 . PHE N  1 45  ? 12.227  120.586 55.983  1.00 11.51 ? 45   PHE N CE1 1 
ATOM   14575 C  CE2 . PHE N  1 45  ? 9.957   120.037 55.398  1.00 10.88 ? 45   PHE N CE2 1 
ATOM   14576 C  CZ  . PHE N  1 45  ? 11.079  120.839 55.225  1.00 11.33 ? 45   PHE N CZ  1 
ATOM   14577 N  N   . HIS N  1 46  ? 10.433  119.399 60.852  1.00 11.22 ? 46   HIS N N   1 
ATOM   14578 C  CA  . HIS N  1 46  ? 9.365   119.910 61.674  1.00 12.30 ? 46   HIS N CA  1 
ATOM   14579 C  C   . HIS N  1 46  ? 9.357   121.428 61.777  1.00 11.73 ? 46   HIS N C   1 
ATOM   14580 O  O   . HIS N  1 46  ? 10.407  122.074 61.665  1.00 13.34 ? 46   HIS N O   1 
ATOM   14581 C  CB  . HIS N  1 46  ? 9.564   119.437 63.125  1.00 12.45 ? 46   HIS N CB  1 
ATOM   14582 C  CG  . HIS N  1 46  ? 9.832   117.974 63.276  1.00 11.69 ? 46   HIS N CG  1 
ATOM   14583 N  ND1 . HIS N  1 46  ? 10.892  117.499 64.006  1.00 10.37 ? 46   HIS N ND1 1 
ATOM   14584 C  CD2 . HIS N  1 46  ? 9.211   116.882 62.766  1.00 11.10 ? 46   HIS N CD2 1 
ATOM   14585 C  CE1 . HIS N  1 46  ? 10.894  116.182 63.984  1.00 12.31 ? 46   HIS N CE1 1 
ATOM   14586 N  NE2 . HIS N  1 46  ? 9.883   115.780 63.234  1.00 11.10 ? 46   HIS N NE2 1 
ATOM   14587 N  N   . VAL N  1 47  ? 8.186   121.983 62.066  1.00 12.13 ? 47   VAL N N   1 
ATOM   14588 C  CA  . VAL N  1 47  ? 8.117   123.387 62.406  1.00 11.30 ? 47   VAL N CA  1 
ATOM   14589 C  C   . VAL N  1 47  ? 8.187   123.415 63.941  1.00 11.95 ? 47   VAL N C   1 
ATOM   14590 O  O   . VAL N  1 47  ? 7.358   122.761 64.641  1.00 11.15 ? 47   VAL N O   1 
ATOM   14591 C  CB  . VAL N  1 47  ? 6.822   124.044 61.976  1.00 12.09 ? 47   VAL N CB  1 
ATOM   14592 C  CG1 . VAL N  1 47  ? 6.775   125.500 62.482  1.00 10.94 ? 47   VAL N CG1 1 
ATOM   14593 C  CG2 . VAL N  1 47  ? 6.621   123.968 60.445  1.00 12.09 ? 47   VAL N CG2 1 
ATOM   14594 N  N   . HIS N  1 48  ? 9.179   124.140 64.468  1.00 11.38 ? 48   HIS N N   1 
ATOM   14595 C  CA  . HIS N  1 48  ? 9.317   124.296 65.925  1.00 12.09 ? 48   HIS N CA  1 
ATOM   14596 C  C   . HIS N  1 48  ? 8.700   125.612 66.346  1.00 11.91 ? 48   HIS N C   1 
ATOM   14597 O  O   . HIS N  1 48  ? 8.564   126.516 65.534  1.00 12.28 ? 48   HIS N O   1 
ATOM   14598 C  CB  . HIS N  1 48  ? 10.790  124.201 66.348  1.00 11.79 ? 48   HIS N CB  1 
ATOM   14599 C  CG  . HIS N  1 48  ? 11.314  122.798 66.342  1.00 11.01 ? 48   HIS N CG  1 
ATOM   14600 N  ND1 . HIS N  1 48  ? 11.911  122.221 67.442  1.00 10.76 ? 48   HIS N ND1 1 
ATOM   14601 C  CD2 . HIS N  1 48  ? 11.318  121.852 65.369  1.00 10.52 ? 48   HIS N CD2 1 
ATOM   14602 C  CE1 . HIS N  1 48  ? 12.279  120.989 67.142  1.00 11.03 ? 48   HIS N CE1 1 
ATOM   14603 N  NE2 . HIS N  1 48  ? 11.913  120.739 65.901  1.00 10.15 ? 48   HIS N NE2 1 
ATOM   14604 N  N   . GLU N  1 49  ? 8.376   125.736 67.630  1.00 11.82 ? 49   GLU N N   1 
ATOM   14605 C  CA  . GLU N  1 49  ? 7.557   126.850 68.092  1.00 12.11 ? 49   GLU N CA  1 
ATOM   14606 C  C   . GLU N  1 49  ? 8.122   128.245 67.922  1.00 12.34 ? 49   GLU N C   1 
ATOM   14607 O  O   . GLU N  1 49  ? 7.398   129.137 67.504  1.00 12.28 ? 49   GLU N O   1 
ATOM   14608 C  CB  . GLU N  1 49  ? 7.174   126.615 69.545  1.00 11.83 ? 49   GLU N CB  1 
ATOM   14609 C  CG  . GLU N  1 49  ? 6.215   127.639 70.138  1.00 13.58 ? 49   GLU N CG  1 
ATOM   14610 C  CD  . GLU N  1 49  ? 5.799   127.252 71.539  1.00 14.22 ? 49   GLU N CD  1 
ATOM   14611 O  OE1 . GLU N  1 49  ? 6.325   126.226 72.043  1.00 12.08 ? 49   GLU N OE1 1 
ATOM   14612 O  OE2 . GLU N  1 49  ? 4.979   127.985 72.150  1.00 12.32 ? 49   GLU N OE2 1 
ATOM   14613 N  N   . PHE N  1 50  ? 9.397   128.449 68.245  1.00 11.56 ? 50   PHE N N   1 
ATOM   14614 C  CA  . PHE N  1 50  ? 9.919   129.822 68.237  1.00 12.24 ? 50   PHE N CA  1 
ATOM   14615 C  C   . PHE N  1 50  ? 10.852  130.150 67.097  1.00 11.62 ? 50   PHE N C   1 
ATOM   14616 O  O   . PHE N  1 50  ? 11.732  129.363 66.780  1.00 12.57 ? 50   PHE N O   1 
ATOM   14617 C  CB  . PHE N  1 50  ? 10.632  130.123 69.559  1.00 11.88 ? 50   PHE N CB  1 
ATOM   14618 C  CG  . PHE N  1 50  ? 9.786   129.813 70.773  1.00 14.01 ? 50   PHE N CG  1 
ATOM   14619 C  CD1 . PHE N  1 50  ? 8.613   130.509 71.003  1.00 16.37 ? 50   PHE N CD1 1 
ATOM   14620 C  CD2 . PHE N  1 50  ? 10.145  128.797 71.651  1.00 14.67 ? 50   PHE N CD2 1 
ATOM   14621 C  CE1 . PHE N  1 50  ? 7.790   130.221 72.128  1.00 17.53 ? 50   PHE N CE1 1 
ATOM   14622 C  CE2 . PHE N  1 50  ? 9.342   128.491 72.761  1.00 17.91 ? 50   PHE N CE2 1 
ATOM   14623 C  CZ  . PHE N  1 50  ? 8.158   129.209 73.003  1.00 15.79 ? 50   PHE N CZ  1 
ATOM   14624 N  N   . GLY N  1 51  ? 10.678  131.336 66.521  1.00 11.44 ? 51   GLY N N   1 
ATOM   14625 C  CA  . GLY N  1 51  ? 11.599  131.838 65.515  1.00 12.00 ? 51   GLY N CA  1 
ATOM   14626 C  C   . GLY N  1 51  ? 12.784  132.484 66.211  1.00 12.01 ? 51   GLY N C   1 
ATOM   14627 O  O   . GLY N  1 51  ? 13.155  133.603 65.905  1.00 12.69 ? 51   GLY N O   1 
ATOM   14628 N  N   . ASP N  1 52  ? 13.394  131.757 67.141  1.00 13.18 ? 52   ASP N N   1 
ATOM   14629 C  CA  . ASP N  1 52  ? 14.467  132.298 67.980  1.00 13.53 ? 52   ASP N CA  1 
ATOM   14630 C  C   . ASP N  1 52  ? 15.778  131.582 67.710  1.00 13.85 ? 52   ASP N C   1 
ATOM   14631 O  O   . ASP N  1 52  ? 15.938  130.419 68.084  1.00 14.85 ? 52   ASP N O   1 
ATOM   14632 C  CB  . ASP N  1 52  ? 14.082  132.105 69.447  1.00 13.17 ? 52   ASP N CB  1 
ATOM   14633 C  CG  . ASP N  1 52  ? 15.052  132.749 70.395  1.00 15.05 ? 52   ASP N CG  1 
ATOM   14634 O  OD1 . ASP N  1 52  ? 16.222  132.943 70.019  1.00 12.30 ? 52   ASP N OD1 1 
ATOM   14635 O  OD2 . ASP N  1 52  ? 14.728  133.124 71.552  1.00 15.79 ? 52   ASP N OD2 1 
ATOM   14636 N  N   . ASN N  1 53  ? 16.720  132.255 67.060  1.00 13.40 ? 53   ASN N N   1 
ATOM   14637 C  CA  . ASN N  1 53  ? 17.989  131.616 66.733  1.00 13.22 ? 53   ASN N CA  1 
ATOM   14638 C  C   . ASN N  1 53  ? 19.150  132.088 67.624  1.00 12.71 ? 53   ASN N C   1 
ATOM   14639 O  O   . ASN N  1 53  ? 20.317  131.938 67.251  1.00 11.93 ? 53   ASN N O   1 
ATOM   14640 C  CB  . ASN N  1 53  ? 18.326  131.876 65.244  1.00 13.56 ? 53   ASN N CB  1 
ATOM   14641 C  CG  . ASN N  1 53  ? 19.384  130.926 64.698  1.00 18.40 ? 53   ASN N CG  1 
ATOM   14642 O  OD1 . ASN N  1 53  ? 20.355  131.355 64.043  1.00 24.43 ? 53   ASN N OD1 1 
ATOM   14643 N  ND2 . ASN N  1 53  ? 19.198  129.629 64.933  1.00 19.42 ? 53   ASN N ND2 1 
ATOM   14644 N  N   . THR N  1 54  ? 18.842  132.649 68.791  1.00 12.65 ? 54   THR N N   1 
ATOM   14645 C  CA  . THR N  1 54  ? 19.884  133.240 69.639  1.00 13.50 ? 54   THR N CA  1 
ATOM   14646 C  C   . THR N  1 54  ? 20.848  132.228 70.184  1.00 14.23 ? 54   THR N C   1 
ATOM   14647 O  O   . THR N  1 54  ? 21.989  132.563 70.505  1.00 15.57 ? 54   THR N O   1 
ATOM   14648 C  CB  . THR N  1 54  ? 19.283  134.053 70.807  1.00 13.70 ? 54   THR N CB  1 
ATOM   14649 O  OG1 . THR N  1 54  ? 18.383  133.226 71.545  1.00 11.81 ? 54   THR N OG1 1 
ATOM   14650 C  CG2 . THR N  1 54  ? 18.412  135.158 70.292  1.00 12.75 ? 54   THR N CG2 1 
ATOM   14651 N  N   . ALA N  1 55  ? 20.416  130.986 70.299  1.00 14.51 ? 55   ALA N N   1 
ATOM   14652 C  CA  . ALA N  1 55  ? 21.318  129.929 70.715  1.00 15.94 ? 55   ALA N CA  1 
ATOM   14653 C  C   . ALA N  1 55  ? 21.294  128.859 69.641  1.00 16.71 ? 55   ALA N C   1 
ATOM   14654 O  O   . ALA N  1 55  ? 21.232  127.669 69.926  1.00 18.01 ? 55   ALA N O   1 
ATOM   14655 C  CB  . ALA N  1 55  ? 20.893  129.348 72.075  1.00 16.13 ? 55   ALA N CB  1 
ATOM   14656 N  N   . GLY N  1 56  ? 21.287  129.288 68.392  1.00 16.56 ? 56   GLY N N   1 
ATOM   14657 C  CA  . GLY N  1 56  ? 21.241  128.336 67.307  1.00 17.29 ? 56   GLY N CA  1 
ATOM   14658 C  C   . GLY N  1 56  ? 19.894  127.632 67.281  1.00 16.81 ? 56   GLY N C   1 
ATOM   14659 O  O   . GLY N  1 56  ? 18.870  128.178 67.747  1.00 17.35 ? 56   GLY N O   1 
ATOM   14660 N  N   . CYS N  1 57  ? 19.888  126.394 66.800  1.00 16.21 ? 57   CYS N N   1 
ATOM   14661 C  CA  . CYS N  1 57  ? 18.618  125.690 66.650  1.00 15.96 ? 57   CYS N CA  1 
ATOM   14662 C  C   . CYS N  1 57  ? 18.006  125.328 67.993  1.00 15.71 ? 57   CYS N C   1 
ATOM   14663 O  O   . CYS N  1 57  ? 16.814  125.083 68.091  1.00 14.68 ? 57   CYS N O   1 
ATOM   14664 C  CB  . CYS N  1 57  ? 18.776  124.466 65.750  1.00 16.52 ? 57   CYS N CB  1 
ATOM   14665 S  SG  . CYS N  1 57  ? 19.343  124.949 64.088  1.00 19.76 ? 57   CYS N SG  1 
ATOM   14666 N  N   . THR N  1 58  ? 18.833  125.283 69.033  1.00 14.66 ? 58   THR N N   1 
ATOM   14667 C  CA  . THR N  1 58  ? 18.312  124.934 70.342  1.00 15.16 ? 58   THR N CA  1 
ATOM   14668 C  C   . THR N  1 58  ? 17.203  125.879 70.803  1.00 14.48 ? 58   THR N C   1 
ATOM   14669 O  O   . THR N  1 58  ? 16.163  125.446 71.360  1.00 14.00 ? 58   THR N O   1 
ATOM   14670 C  CB  . THR N  1 58  ? 19.438  124.881 71.370  1.00 15.82 ? 58   THR N CB  1 
ATOM   14671 O  OG1 . THR N  1 58  ? 20.324  123.809 71.021  1.00 17.28 ? 58   THR N OG1 1 
ATOM   14672 C  CG2 . THR N  1 58  ? 18.879  124.473 72.735  1.00 16.26 ? 58   THR N CG2 1 
ATOM   14673 N  N   . SER N  1 59  ? 17.369  127.159 70.551  1.00 12.95 ? 59   SER N N   1 
ATOM   14674 C  CA  . SER N  1 59  ? 16.386  128.089 71.087  1.00 14.01 ? 59   SER N CA  1 
ATOM   14675 C  C   . SER N  1 59  ? 15.067  128.170 70.331  1.00 14.05 ? 59   SER N C   1 
ATOM   14676 O  O   . SER N  1 59  ? 14.203  128.972 70.678  1.00 13.21 ? 59   SER N O   1 
ATOM   14677 C  CB  . SER N  1 59  ? 16.990  129.476 71.266  1.00 14.18 ? 59   SER N CB  1 
ATOM   14678 O  OG  . SER N  1 59  ? 17.570  129.902 70.061  1.00 15.55 ? 59   SER N OG  1 
ATOM   14679 N  N   . ALA N  1 60  ? 14.900  127.332 69.310  1.00 13.17 ? 60   ALA N N   1 
ATOM   14680 C  CA  . ALA N  1 60  ? 13.651  127.328 68.571  1.00 13.81 ? 60   ALA N CA  1 
ATOM   14681 C  C   . ALA N  1 60  ? 12.554  126.645 69.383  1.00 13.66 ? 60   ALA N C   1 
ATOM   14682 O  O   . ALA N  1 60  ? 11.386  126.711 69.023  1.00 14.40 ? 60   ALA N O   1 
ATOM   14683 C  CB  . ALA N  1 60  ? 13.829  126.601 67.191  1.00 12.28 ? 60   ALA N CB  1 
ATOM   14684 N  N   . GLY N  1 61  ? 12.955  125.938 70.438  1.00 13.52 ? 61   GLY N N   1 
ATOM   14685 C  CA  . GLY N  1 61  ? 12.021  125.255 71.319  1.00 12.66 ? 61   GLY N CA  1 
ATOM   14686 C  C   . GLY N  1 61  ? 11.522  123.921 70.754  1.00 12.22 ? 61   GLY N C   1 
ATOM   14687 O  O   . GLY N  1 61  ? 12.125  123.310 69.869  1.00 11.12 ? 61   GLY N O   1 
ATOM   14688 N  N   . PRO N  1 62  ? 10.419  123.443 71.312  1.00 12.21 ? 62   PRO N N   1 
ATOM   14689 C  CA  . PRO N  1 62  ? 9.824   122.178 70.882  1.00 12.15 ? 62   PRO N CA  1 
ATOM   14690 C  C   . PRO N  1 62  ? 8.956   122.362 69.642  1.00 11.50 ? 62   PRO N C   1 
ATOM   14691 O  O   . PRO N  1 62  ? 8.817   123.469 69.105  1.00 10.66 ? 62   PRO N O   1 
ATOM   14692 C  CB  . PRO N  1 62  ? 8.879   121.798 72.035  1.00 12.53 ? 62   PRO N CB  1 
ATOM   14693 C  CG  . PRO N  1 62  ? 8.634   123.042 72.779  1.00 13.69 ? 62   PRO N CG  1 
ATOM   14694 C  CD  . PRO N  1 62  ? 9.681   124.075 72.414  1.00 11.54 ? 62   PRO N CD  1 
ATOM   14695 N  N   . HIS N  1 63  ? 8.288   121.284 69.258  1.00 11.09 ? 63   HIS N N   1 
ATOM   14696 C  CA  . HIS N  1 63  ? 7.468   121.341 68.063  1.00 11.38 ? 63   HIS N CA  1 
ATOM   14697 C  C   . HIS N  1 63  ? 6.313   122.276 68.251  1.00 12.00 ? 63   HIS N C   1 
ATOM   14698 O  O   . HIS N  1 63  ? 5.761   122.397 69.354  1.00 12.40 ? 63   HIS N O   1 
ATOM   14699 C  CB  . HIS N  1 63  ? 6.942   119.954 67.697  1.00 11.50 ? 63   HIS N CB  1 
ATOM   14700 C  CG  . HIS N  1 63  ? 8.026   119.008 67.306  1.00 11.85 ? 63   HIS N CG  1 
ATOM   14701 N  ND1 . HIS N  1 63  ? 7.792   117.697 66.968  1.00 11.56 ? 63   HIS N ND1 1 
ATOM   14702 C  CD2 . HIS N  1 63  ? 9.367   119.186 67.229  1.00 12.59 ? 63   HIS N CD2 1 
ATOM   14703 C  CE1 . HIS N  1 63  ? 8.943   117.103 66.705  1.00 12.99 ? 63   HIS N CE1 1 
ATOM   14704 N  NE2 . HIS N  1 63  ? 9.909   117.982 66.866  1.00 15.34 ? 63   HIS N NE2 1 
ATOM   14705 N  N   . PHE N  1 64  ? 5.942   122.952 67.183  1.00 12.08 ? 64   PHE N N   1 
ATOM   14706 C  CA  . PHE N  1 64  ? 4.784   123.815 67.239  1.00 13.03 ? 64   PHE N CA  1 
ATOM   14707 C  C   . PHE N  1 64  ? 3.567   122.919 67.589  1.00 12.54 ? 64   PHE N C   1 
ATOM   14708 O  O   . PHE N  1 64  ? 3.217   122.029 66.823  1.00 11.03 ? 64   PHE N O   1 
ATOM   14709 C  CB  . PHE N  1 64  ? 4.669   124.531 65.893  1.00 13.29 ? 64   PHE N CB  1 
ATOM   14710 C  CG  . PHE N  1 64  ? 3.569   125.559 65.835  1.00 15.89 ? 64   PHE N CG  1 
ATOM   14711 C  CD1 . PHE N  1 64  ? 3.347   126.411 66.899  1.00 15.56 ? 64   PHE N CD1 1 
ATOM   14712 C  CD2 . PHE N  1 64  ? 2.776   125.672 64.700  1.00 15.62 ? 64   PHE N CD2 1 
ATOM   14713 C  CE1 . PHE N  1 64  ? 2.328   127.365 66.847  1.00 18.67 ? 64   PHE N CE1 1 
ATOM   14714 C  CE2 . PHE N  1 64  ? 1.754   126.609 64.621  1.00 19.44 ? 64   PHE N CE2 1 
ATOM   14715 C  CZ  . PHE N  1 64  ? 1.515   127.466 65.702  1.00 17.01 ? 64   PHE N CZ  1 
ATOM   14716 N  N   . ASN N  1 65  ? 2.930   123.140 68.749  1.00 13.28 ? 65   ASN N N   1 
ATOM   14717 C  CA  . ASN N  1 65  ? 1.902   122.225 69.240  1.00 14.38 ? 65   ASN N CA  1 
ATOM   14718 C  C   . ASN N  1 65  ? 0.792   122.900 70.053  1.00 15.64 ? 65   ASN N C   1 
ATOM   14719 O  O   . ASN N  1 65  ? 0.648   122.669 71.253  1.00 15.51 ? 65   ASN N O   1 
ATOM   14720 C  CB  . ASN N  1 65  ? 2.573   121.175 70.116  1.00 14.56 ? 65   ASN N CB  1 
ATOM   14721 C  CG  . ASN N  1 65  ? 1.617   120.102 70.614  1.00 15.08 ? 65   ASN N CG  1 
ATOM   14722 O  OD1 . ASN N  1 65  ? 0.581   119.810 69.999  1.00 18.13 ? 65   ASN N OD1 1 
ATOM   14723 N  ND2 . ASN N  1 65  ? 1.993   119.468 71.715  1.00 13.78 ? 65   ASN N ND2 1 
ATOM   14724 N  N   . PRO N  1 66  ? 0.019   123.731 69.377  1.00 16.59 ? 66   PRO N N   1 
ATOM   14725 C  CA  . PRO N  1 66  ? -1.026  124.535 70.019  1.00 17.31 ? 66   PRO N CA  1 
ATOM   14726 C  C   . PRO N  1 66  ? -2.184  123.739 70.622  1.00 18.32 ? 66   PRO N C   1 
ATOM   14727 O  O   . PRO N  1 66  ? -2.832  124.250 71.529  1.00 18.99 ? 66   PRO N O   1 
ATOM   14728 C  CB  . PRO N  1 66  ? -1.542  125.438 68.892  1.00 17.42 ? 66   PRO N CB  1 
ATOM   14729 C  CG  . PRO N  1 66  ? -0.878  124.991 67.614  1.00 16.98 ? 66   PRO N CG  1 
ATOM   14730 C  CD  . PRO N  1 66  ? 0.136   123.965 67.929  1.00 16.29 ? 66   PRO N CD  1 
ATOM   14731 N  N   . LEU N  1 67  ? -2.435  122.528 70.139  1.00 19.29 ? 67   LEU N N   1 
ATOM   14732 C  CA  . LEU N  1 67  ? -3.512  121.706 70.659  1.00 19.98 ? 67   LEU N CA  1 
ATOM   14733 C  C   . LEU N  1 67  ? -3.026  120.641 71.651  1.00 20.15 ? 67   LEU N C   1 
ATOM   14734 O  O   . LEU N  1 67  ? -3.780  119.721 72.008  1.00 19.23 ? 67   LEU N O   1 
ATOM   14735 C  CB  . LEU N  1 67  ? -4.280  121.082 69.502  1.00 20.87 ? 67   LEU N CB  1 
ATOM   14736 C  CG  . LEU N  1 67  ? -4.401  121.972 68.252  1.00 22.14 ? 67   LEU N CG  1 
ATOM   14737 C  CD1 . LEU N  1 67  ? -5.357  121.345 67.246  1.00 23.75 ? 67   LEU N CD1 1 
ATOM   14738 C  CD2 . LEU N  1 67  ? -4.844  123.389 68.602  1.00 22.18 ? 67   LEU N CD2 1 
ATOM   14739 N  N   . SER N  1 68  ? -1.764  120.774 72.082  1.00 19.92 ? 68   SER N N   1 
ATOM   14740 C  CA  . SER N  1 68  ? -1.177  119.916 73.110  1.00 19.75 ? 68   SER N CA  1 
ATOM   14741 C  C   . SER N  1 68  ? -1.409  118.424 72.855  1.00 19.35 ? 68   SER N C   1 
ATOM   14742 O  O   . SER N  1 68  ? -1.952  117.703 73.710  1.00 18.41 ? 68   SER N O   1 
ATOM   14743 C  CB  . SER N  1 68  ? -1.756  120.286 74.481  1.00 20.81 ? 68   SER N CB  1 
ATOM   14744 O  OG  . SER N  1 68  ? -1.713  121.693 74.720  1.00 22.47 ? 68   SER N OG  1 
ATOM   14745 N  N   . ARG N  1 69  ? -1.018  117.969 71.674  1.00 18.34 ? 69   ARG N N   1 
ATOM   14746 C  CA  . ARG N  1 69  ? -1.155  116.577 71.312  1.00 17.90 ? 69   ARG N CA  1 
ATOM   14747 C  C   . ARG N  1 69  ? 0.194   115.901 71.416  1.00 17.09 ? 69   ARG N C   1 
ATOM   14748 O  O   . ARG N  1 69  ? 1.222   116.545 71.646  1.00 16.35 ? 69   ARG N O   1 
ATOM   14749 C  CB  . ARG N  1 69  ? -1.623  116.487 69.869  1.00 18.06 ? 69   ARG N CB  1 
ATOM   14750 C  CG  . ARG N  1 69  ? -2.818  117.363 69.578  1.00 22.17 ? 69   ARG N CG  1 
ATOM   14751 C  CD  . ARG N  1 69  ? -4.155  116.652 69.636  1.00 28.23 ? 69   ARG N CD  1 
ATOM   14752 N  NE  . ARG N  1 69  ? -4.818  116.853 68.348  1.00 33.95 ? 69   ARG N NE  1 
ATOM   14753 C  CZ  . ARG N  1 69  ? -6.127  116.824 68.126  1.00 34.72 ? 69   ARG N CZ  1 
ATOM   14754 N  NH1 . ARG N  1 69  ? -6.985  116.590 69.115  1.00 36.93 ? 69   ARG N NH1 1 
ATOM   14755 N  NH2 . ARG N  1 69  ? -6.581  117.030 66.891  1.00 35.29 ? 69   ARG N NH2 1 
ATOM   14756 N  N   . LYS N  1 70  ? 0.211   114.594 71.239  1.00 16.57 ? 70   LYS N N   1 
ATOM   14757 C  CA  . LYS N  1 70  ? 1.489   113.923 71.227  1.00 16.55 ? 70   LYS N CA  1 
ATOM   14758 C  C   . LYS N  1 70  ? 2.012   114.006 69.812  1.00 15.47 ? 70   LYS N C   1 
ATOM   14759 O  O   . LYS N  1 70  ? 1.272   114.295 68.862  1.00 15.52 ? 70   LYS N O   1 
ATOM   14760 C  CB  . LYS N  1 70  ? 1.376   112.474 71.655  1.00 17.19 ? 70   LYS N CB  1 
ATOM   14761 C  CG  . LYS N  1 70  ? 0.847   112.327 73.077  1.00 20.24 ? 70   LYS N CG  1 
ATOM   14762 C  CD  . LYS N  1 70  ? 0.703   110.863 73.478  1.00 25.75 ? 70   LYS N CD  1 
ATOM   14763 C  CE  . LYS N  1 70  ? -0.055  110.046 72.450  1.00 28.24 ? 70   LYS N CE  1 
ATOM   14764 N  NZ  . LYS N  1 70  ? -0.763  108.895 73.127  1.00 30.43 ? 70   LYS N NZ  1 
ATOM   14765 N  N   . HIS N  1 71  ? 3.290   113.723 69.676  1.00 14.51 ? 71   HIS N N   1 
ATOM   14766 C  CA  . HIS N  1 71  ? 3.926   113.769 68.368  1.00 13.36 ? 71   HIS N CA  1 
ATOM   14767 C  C   . HIS N  1 71  ? 3.386   112.658 67.460  1.00 13.96 ? 71   HIS N C   1 
ATOM   14768 O  O   . HIS N  1 71  ? 3.060   111.555 67.936  1.00 14.40 ? 71   HIS N O   1 
ATOM   14769 C  CB  . HIS N  1 71  ? 5.407   113.554 68.588  1.00 13.53 ? 71   HIS N CB  1 
ATOM   14770 C  CG  . HIS N  1 71  ? 6.201   113.566 67.331  1.00 11.74 ? 71   HIS N CG  1 
ATOM   14771 N  ND1 . HIS N  1 71  ? 6.528   114.735 66.682  1.00 11.84 ? 71   HIS N ND1 1 
ATOM   14772 C  CD2 . HIS N  1 71  ? 6.693   112.558 66.574  1.00 13.07 ? 71   HIS N CD2 1 
ATOM   14773 C  CE1 . HIS N  1 71  ? 7.221   114.451 65.593  1.00 12.65 ? 71   HIS N CE1 1 
ATOM   14774 N  NE2 . HIS N  1 71  ? 7.338   113.139 65.503  1.00 12.48 ? 71   HIS N NE2 1 
ATOM   14775 N  N   . GLY N  1 72  ? 3.285   112.920 66.155  1.00 13.16 ? 72   GLY N N   1 
ATOM   14776 C  CA  . GLY N  1 72  ? 2.844   111.888 65.231  1.00 12.56 ? 72   GLY N CA  1 
ATOM   14777 C  C   . GLY N  1 72  ? 3.462   112.156 63.855  1.00 13.40 ? 72   GLY N C   1 
ATOM   14778 O  O   . GLY N  1 72  ? 4.304   113.041 63.704  1.00 13.35 ? 72   GLY N O   1 
ATOM   14779 N  N   . GLY N  1 73  ? 3.055   111.395 62.856  1.00 13.95 ? 73   GLY N N   1 
ATOM   14780 C  CA  . GLY N  1 73  ? 3.432   111.704 61.485  1.00 14.51 ? 73   GLY N CA  1 
ATOM   14781 C  C   . GLY N  1 73  ? 2.377   112.658 60.919  1.00 14.91 ? 73   GLY N C   1 
ATOM   14782 O  O   . GLY N  1 73  ? 1.336   112.871 61.542  1.00 14.80 ? 73   GLY N O   1 
ATOM   14783 N  N   . PRO N  1 74  ? 2.631   113.250 59.754  1.00 14.62 ? 74   PRO N N   1 
ATOM   14784 C  CA  . PRO N  1 74  ? 1.713   114.251 59.218  1.00 15.51 ? 74   PRO N CA  1 
ATOM   14785 C  C   . PRO N  1 74  ? 0.364   113.670 58.863  1.00 16.12 ? 74   PRO N C   1 
ATOM   14786 O  O   . PRO N  1 74  ? -0.583  114.437 58.763  1.00 15.87 ? 74   PRO N O   1 
ATOM   14787 C  CB  . PRO N  1 74  ? 2.375   114.725 57.920  1.00 15.83 ? 74   PRO N CB  1 
ATOM   14788 C  CG  . PRO N  1 74  ? 3.519   113.756 57.633  1.00 14.44 ? 74   PRO N CG  1 
ATOM   14789 C  CD  . PRO N  1 74  ? 3.802   113.011 58.889  1.00 14.86 ? 74   PRO N CD  1 
ATOM   14790 N  N   . LYS N  1 75  ? 0.286   112.359 58.651  1.00 17.60 ? 75   LYS N N   1 
ATOM   14791 C  CA  . LYS N  1 75  ? -0.998  111.749 58.238  1.00 19.07 ? 75   LYS N CA  1 
ATOM   14792 C  C   . LYS N  1 75  ? -1.862  111.379 59.423  1.00 19.69 ? 75   LYS N C   1 
ATOM   14793 O  O   . LYS N  1 75  ? -3.010  110.947 59.247  1.00 20.21 ? 75   LYS N O   1 
ATOM   14794 C  CB  . LYS N  1 75  ? -0.775  110.489 57.389  1.00 19.84 ? 75   LYS N CB  1 
ATOM   14795 C  CG  . LYS N  1 75  ? -0.137  110.696 56.012  1.00 23.04 ? 75   LYS N CG  1 
ATOM   14796 C  CD  . LYS N  1 75  ? -0.904  111.695 55.157  1.00 28.79 ? 75   LYS N CD  1 
ATOM   14797 C  CE  . LYS N  1 75  ? -0.099  112.983 54.934  1.00 32.76 ? 75   LYS N CE  1 
ATOM   14798 N  NZ  . LYS N  1 75  ? 0.927   112.836 53.844  1.00 35.63 ? 75   LYS N NZ  1 
ATOM   14799 N  N   . ASP N  1 76  ? -1.334  111.545 60.631  1.00 20.06 ? 76   ASP N N   1 
ATOM   14800 C  CA  . ASP N  1 76  ? -2.077  111.176 61.840  1.00 20.93 ? 76   ASP N CA  1 
ATOM   14801 C  C   . ASP N  1 76  ? -2.944  112.284 62.380  1.00 20.90 ? 76   ASP N C   1 
ATOM   14802 O  O   . ASP N  1 76  ? -2.568  113.448 62.329  1.00 20.86 ? 76   ASP N O   1 
ATOM   14803 C  CB  . ASP N  1 76  ? -1.126  110.758 62.955  1.00 21.22 ? 76   ASP N CB  1 
ATOM   14804 C  CG  . ASP N  1 76  ? -0.285  109.568 62.582  1.00 23.37 ? 76   ASP N CG  1 
ATOM   14805 O  OD1 . ASP N  1 76  ? -0.860  108.496 62.211  1.00 23.88 ? 76   ASP N OD1 1 
ATOM   14806 O  OD2 . ASP N  1 76  ? 0.964   109.619 62.627  1.00 24.52 ? 76   ASP N OD2 1 
ATOM   14807 N  N   . GLU N  1 77  ? -4.119  111.915 62.898  1.00 20.69 ? 77   GLU N N   1 
ATOM   14808 C  CA  . GLU N  1 77  ? -4.992  112.874 63.544  1.00 20.70 ? 77   GLU N CA  1 
ATOM   14809 C  C   . GLU N  1 77  ? -4.319  113.358 64.828  1.00 19.55 ? 77   GLU N C   1 
ATOM   14810 O  O   . GLU N  1 77  ? -4.408  114.536 65.191  1.00 19.71 ? 77   GLU N O   1 
ATOM   14811 C  CB  . GLU N  1 77  ? -6.352  112.235 63.861  1.00 21.45 ? 77   GLU N CB  1 
ATOM   14812 C  CG  . GLU N  1 77  ? -7.437  113.235 64.212  1.00 25.08 ? 77   GLU N CG  1 
ATOM   14813 C  CD  . GLU N  1 77  ? -8.827  112.614 64.222  1.00 30.45 ? 77   GLU N CD  1 
ATOM   14814 O  OE1 . GLU N  1 77  ? -9.320  112.193 63.141  1.00 32.56 ? 77   GLU N OE1 1 
ATOM   14815 O  OE2 . GLU N  1 77  ? -9.434  112.540 65.318  1.00 33.25 ? 77   GLU N OE2 1 
ATOM   14816 N  N   . GLU N  1 78  ? -3.637  112.448 65.519  1.00 18.20 ? 78   GLU N N   1 
ATOM   14817 C  CA  . GLU N  1 78  ? -2.922  112.833 66.737  1.00 16.88 ? 78   GLU N CA  1 
ATOM   14818 C  C   . GLU N  1 78  ? -1.497  113.254 66.356  1.00 15.41 ? 78   GLU N C   1 
ATOM   14819 O  O   . GLU N  1 78  ? -0.596  112.409 66.212  1.00 14.18 ? 78   GLU N O   1 
ATOM   14820 C  CB  . GLU N  1 78  ? -2.864  111.703 67.755  1.00 16.87 ? 78   GLU N CB  1 
ATOM   14821 C  CG  . GLU N  1 78  ? -2.097  112.061 69.025  1.00 18.57 ? 78   GLU N CG  1 
ATOM   14822 C  CD  . GLU N  1 78  ? -2.896  112.883 70.023  1.00 21.58 ? 78   GLU N CD  1 
ATOM   14823 O  OE1 . GLU N  1 78  ? -4.111  113.097 69.818  1.00 20.05 ? 78   GLU N OE1 1 
ATOM   14824 O  OE2 . GLU N  1 78  ? -2.305  113.311 71.033  1.00 22.67 ? 78   GLU N OE2 1 
ATOM   14825 N  N   . ARG N  1 79  ? -1.312  114.556 66.181  1.00 14.66 ? 79   ARG N N   1 
ATOM   14826 C  CA  . ARG N  1 79  ? 0.006   115.086 65.823  1.00 14.68 ? 79   ARG N CA  1 
ATOM   14827 C  C   . ARG N  1 79  ? 0.144   116.546 66.219  1.00 14.65 ? 79   ARG N C   1 
ATOM   14828 O  O   . ARG N  1 79  ? -0.865  117.224 66.482  1.00 14.74 ? 79   ARG N O   1 
ATOM   14829 C  CB  . ARG N  1 79  ? 0.240   114.931 64.320  1.00 15.42 ? 79   ARG N CB  1 
ATOM   14830 C  CG  . ARG N  1 79  ? -0.584  115.885 63.417  1.00 16.67 ? 79   ARG N CG  1 
ATOM   14831 C  CD  . ARG N  1 79  ? 0.278   116.965 62.680  1.00 21.44 ? 79   ARG N CD  1 
ATOM   14832 N  NE  . ARG N  1 79  ? -0.012  116.864 61.280  1.00 20.70 ? 79   ARG N NE  1 
ATOM   14833 C  CZ  . ARG N  1 79  ? 0.376   117.667 60.312  1.00 17.33 ? 79   ARG N CZ  1 
ATOM   14834 N  NH1 . ARG N  1 79  ? 1.106   118.738 60.519  1.00 12.70 ? 79   ARG N NH1 1 
ATOM   14835 N  NH2 . ARG N  1 79  ? 0.003   117.348 59.083  1.00 17.36 ? 79   ARG N NH2 1 
ATOM   14836 N  N   . HIS N  1 80  ? 1.393   117.012 66.320  1.00 13.55 ? 80   HIS N N   1 
ATOM   14837 C  CA  . HIS N  1 80  ? 1.664   118.418 66.521  1.00 13.97 ? 80   HIS N CA  1 
ATOM   14838 C  C   . HIS N  1 80  ? 1.405   119.114 65.187  1.00 13.27 ? 80   HIS N C   1 
ATOM   14839 O  O   . HIS N  1 80  ? 1.614   118.527 64.130  1.00 13.52 ? 80   HIS N O   1 
ATOM   14840 C  CB  . HIS N  1 80  ? 3.148   118.619 66.896  1.00 13.05 ? 80   HIS N CB  1 
ATOM   14841 C  CG  . HIS N  1 80  ? 3.520   117.961 68.180  1.00 14.74 ? 80   HIS N CG  1 
ATOM   14842 N  ND1 . HIS N  1 80  ? 4.751   117.390 68.403  1.00 16.93 ? 80   HIS N ND1 1 
ATOM   14843 C  CD2 . HIS N  1 80  ? 2.802   117.769 69.310  1.00 14.63 ? 80   HIS N CD2 1 
ATOM   14844 C  CE1 . HIS N  1 80  ? 4.785   116.893 69.627  1.00 17.54 ? 80   HIS N CE1 1 
ATOM   14845 N  NE2 . HIS N  1 80  ? 3.611   117.101 70.194  1.00 18.81 ? 80   HIS N NE2 1 
ATOM   14846 N  N   . VAL N  1 81  ? 0.944   120.354 65.223  1.00 13.18 ? 81   VAL N N   1 
ATOM   14847 C  CA  . VAL N  1 81  ? 0.813   121.085 63.971  1.00 12.39 ? 81   VAL N CA  1 
ATOM   14848 C  C   . VAL N  1 81  ? 2.146   121.081 63.171  1.00 12.32 ? 81   VAL N C   1 
ATOM   14849 O  O   . VAL N  1 81  ? 2.160   120.986 61.940  1.00 12.02 ? 81   VAL N O   1 
ATOM   14850 C  CB  . VAL N  1 81  ? 0.344   122.526 64.251  1.00 12.82 ? 81   VAL N CB  1 
ATOM   14851 C  CG1 . VAL N  1 81  ? 0.424   123.390 63.013  1.00 13.82 ? 81   VAL N CG1 1 
ATOM   14852 C  CG2 . VAL N  1 81  ? -1.120  122.516 64.786  1.00 12.82 ? 81   VAL N CG2 1 
ATOM   14853 N  N   . GLY N  1 82  ? 3.269   121.155 63.872  1.00 11.54 ? 82   GLY N N   1 
ATOM   14854 C  CA  . GLY N  1 82  ? 4.570   121.201 63.203  1.00 11.59 ? 82   GLY N CA  1 
ATOM   14855 C  C   . GLY N  1 82  ? 5.124   119.897 62.675  1.00 11.63 ? 82   GLY N C   1 
ATOM   14856 O  O   . GLY N  1 82  ? 6.238   119.890 62.169  1.00 10.56 ? 82   GLY N O   1 
ATOM   14857 N  N   . ASP N  1 83  ? 4.375   118.811 62.817  1.00 10.83 ? 83   ASP N N   1 
ATOM   14858 C  CA  . ASP N  1 83  ? 4.843   117.486 62.400  1.00 11.95 ? 83   ASP N CA  1 
ATOM   14859 C  C   . ASP N  1 83  ? 4.712   117.212 60.910  1.00 11.97 ? 83   ASP N C   1 
ATOM   14860 O  O   . ASP N  1 83  ? 3.681   116.688 60.447  1.00 13.07 ? 83   ASP N O   1 
ATOM   14861 C  CB  . ASP N  1 83  ? 4.115   116.396 63.180  1.00 11.93 ? 83   ASP N CB  1 
ATOM   14862 C  CG  . ASP N  1 83  ? 4.507   116.374 64.626  1.00 13.42 ? 83   ASP N CG  1 
ATOM   14863 O  OD1 . ASP N  1 83  ? 5.509   117.026 64.978  1.00 11.70 ? 83   ASP N OD1 1 
ATOM   14864 O  OD2 . ASP N  1 83  ? 3.868   115.759 65.491  1.00 10.18 ? 83   ASP N OD2 1 
ATOM   14865 N  N   . LEU N  1 84  ? 5.756   117.532 60.166  1.00 10.92 ? 84   LEU N N   1 
ATOM   14866 C  CA  . LEU N  1 84  ? 5.745   117.329 58.716  1.00 11.96 ? 84   LEU N CA  1 
ATOM   14867 C  C   . LEU N  1 84  ? 6.406   116.022 58.336  1.00 11.71 ? 84   LEU N C   1 
ATOM   14868 O  O   . LEU N  1 84  ? 6.625   115.735 57.150  1.00 13.72 ? 84   LEU N O   1 
ATOM   14869 C  CB  . LEU N  1 84  ? 6.455   118.497 58.025  1.00 11.90 ? 84   LEU N CB  1 
ATOM   14870 C  CG  . LEU N  1 84  ? 5.713   119.835 58.162  1.00 11.78 ? 84   LEU N CG  1 
ATOM   14871 C  CD1 . LEU N  1 84  ? 6.503   120.920 57.415  1.00 15.49 ? 84   LEU N CD1 1 
ATOM   14872 C  CD2 . LEU N  1 84  ? 4.250   119.750 57.677  1.00 13.69 ? 84   LEU N CD2 1 
ATOM   14873 N  N   . GLY N  1 85  ? 6.735   115.223 59.335  1.00 11.40 ? 85   GLY N N   1 
ATOM   14874 C  CA  . GLY N  1 85  ? 7.306   113.915 59.086  1.00 11.41 ? 85   GLY N CA  1 
ATOM   14875 C  C   . GLY N  1 85  ? 8.779   113.898 58.691  1.00 11.09 ? 85   GLY N C   1 
ATOM   14876 O  O   . GLY N  1 85  ? 9.600   114.530 59.345  1.00 11.25 ? 85   GLY N O   1 
ATOM   14877 N  N   . ASN N  1 86  ? 9.100   113.113 57.675  1.00 10.76 ? 86   ASN N N   1 
ATOM   14878 C  CA  . ASN N  1 86  ? 10.472  113.005 57.203  1.00 10.03 ? 86   ASN N CA  1 
ATOM   14879 C  C   . ASN N  1 86  ? 10.696  113.534 55.788  1.00 11.52 ? 86   ASN N C   1 
ATOM   14880 O  O   . ASN N  1 86  ? 9.772   113.553 54.969  1.00 10.79 ? 86   ASN N O   1 
ATOM   14881 C  CB  . ASN N  1 86  ? 10.885  111.558 57.170  1.00 11.05 ? 86   ASN N CB  1 
ATOM   14882 C  CG  . ASN N  1 86  ? 11.111  110.989 58.560  1.00 12.40 ? 86   ASN N CG  1 
ATOM   14883 O  OD1 . ASN N  1 86  ? 11.969  111.461 59.302  1.00 11.60 ? 86   ASN N OD1 1 
ATOM   14884 N  ND2 . ASN N  1 86  ? 10.336  109.963 58.905  1.00 13.65 ? 86   ASN N ND2 1 
ATOM   14885 N  N   . VAL N  1 87  ? 11.947  113.888 55.509  1.00 9.66  ? 87   VAL N N   1 
ATOM   14886 C  CA  . VAL N  1 87  ? 12.350  114.190 54.140  1.00 11.27 ? 87   VAL N CA  1 
ATOM   14887 C  C   . VAL N  1 87  ? 13.435  113.180 53.870  1.00 11.62 ? 87   VAL N C   1 
ATOM   14888 O  O   . VAL N  1 87  ? 14.012  112.623 54.814  1.00 13.05 ? 87   VAL N O   1 
ATOM   14889 C  CB  . VAL N  1 87  ? 12.872  115.627 53.939  1.00 10.43 ? 87   VAL N CB  1 
ATOM   14890 C  CG1 . VAL N  1 87  ? 11.720  116.638 54.140  1.00 10.79 ? 87   VAL N CG1 1 
ATOM   14891 C  CG2 . VAL N  1 87  ? 14.067  115.859 54.854  1.00 9.68  ? 87   VAL N CG2 1 
ATOM   14892 N  N   . THR N  1 88  ? 13.692  112.890 52.596  1.00 10.95 ? 88   THR N N   1 
ATOM   14893 C  CA  . THR N  1 88  ? 14.609  111.817 52.248  1.00 10.79 ? 88   THR N CA  1 
ATOM   14894 C  C   . THR N  1 88  ? 15.818  112.358 51.509  1.00 11.15 ? 88   THR N C   1 
ATOM   14895 O  O   . THR N  1 88  ? 15.636  112.996 50.492  1.00 10.57 ? 88   THR N O   1 
ATOM   14896 C  CB  . THR N  1 88  ? 13.877  110.859 51.293  1.00 12.03 ? 88   THR N CB  1 
ATOM   14897 O  OG1 . THR N  1 88  ? 12.819  110.187 51.984  1.00 12.37 ? 88   THR N OG1 1 
ATOM   14898 C  CG2 . THR N  1 88  ? 14.791  109.731 50.844  1.00 13.49 ? 88   THR N CG2 1 
ATOM   14899 N  N   . ALA N  1 89  ? 17.041  112.116 51.986  1.00 11.18 ? 89   ALA N N   1 
ATOM   14900 C  CA  . ALA N  1 89  ? 18.213  112.587 51.224  1.00 11.95 ? 89   ALA N CA  1 
ATOM   14901 C  C   . ALA N  1 89  ? 18.678  111.460 50.346  1.00 12.31 ? 89   ALA N C   1 
ATOM   14902 O  O   . ALA N  1 89  ? 18.716  110.312 50.797  1.00 11.88 ? 89   ALA N O   1 
ATOM   14903 C  CB  . ALA N  1 89  ? 19.347  112.984 52.133  1.00 11.89 ? 89   ALA N CB  1 
ATOM   14904 N  N   . ASP N  1 90  ? 19.064  111.812 49.126  1.00 14.21 ? 90   ASP N N   1 
ATOM   14905 C  CA  . ASP N  1 90  ? 19.560  110.826 48.161  1.00 15.07 ? 90   ASP N CA  1 
ATOM   14906 C  C   . ASP N  1 90  ? 21.008  110.438 48.477  1.00 15.51 ? 90   ASP N C   1 
ATOM   14907 O  O   . ASP N  1 90  ? 21.606  111.004 49.382  1.00 15.17 ? 90   ASP N O   1 
ATOM   14908 C  CB  . ASP N  1 90  ? 19.269  111.263 46.702  1.00 16.17 ? 90   ASP N CB  1 
ATOM   14909 C  CG  . ASP N  1 90  ? 19.940  112.587 46.282  1.00 20.35 ? 90   ASP N CG  1 
ATOM   14910 O  OD1 . ASP N  1 90  ? 20.951  113.017 46.904  1.00 23.84 ? 90   ASP N OD1 1 
ATOM   14911 O  OD2 . ASP N  1 90  ? 19.519  113.280 45.298  1.00 21.99 ? 90   ASP N OD2 1 
ATOM   14912 N  N   . LYS N  1 91  ? 21.591  109.465 47.775  1.00 15.77 ? 91   LYS N N   1 
ATOM   14913 C  CA  . LYS N  1 91  ? 22.975  109.082 48.105  1.00 16.94 ? 91   LYS N CA  1 
ATOM   14914 C  C   . LYS N  1 91  ? 23.968  110.246 48.173  1.00 17.00 ? 91   LYS N C   1 
ATOM   14915 O  O   . LYS N  1 91  ? 24.896  110.232 48.991  1.00 18.61 ? 91   LYS N O   1 
ATOM   14916 C  CB  . LYS N  1 91  ? 23.501  107.992 47.155  1.00 17.20 ? 91   LYS N CB  1 
ATOM   14917 C  CG  . LYS N  1 91  ? 22.706  107.880 45.878  1.00 21.24 ? 91   LYS N CG  1 
ATOM   14918 C  CD  . LYS N  1 91  ? 23.255  108.739 44.740  1.00 26.27 ? 91   LYS N CD  1 
ATOM   14919 C  CE  . LYS N  1 91  ? 23.281  107.913 43.430  1.00 26.70 ? 91   LYS N CE  1 
ATOM   14920 N  NZ  . LYS N  1 91  ? 23.659  108.684 42.188  1.00 28.98 ? 91   LYS N NZ  1 
ATOM   14921 N  N   . ASP N  1 92  ? 23.778  111.254 47.337  1.00 15.97 ? 92   ASP N N   1 
ATOM   14922 C  CA  . ASP N  1 92  ? 24.677  112.394 47.342  1.00 15.70 ? 92   ASP N CA  1 
ATOM   14923 C  C   . ASP N  1 92  ? 24.390  113.432 48.429  1.00 14.99 ? 92   ASP N C   1 
ATOM   14924 O  O   . ASP N  1 92  ? 24.980  114.516 48.415  1.00 14.78 ? 92   ASP N O   1 
ATOM   14925 C  CB  . ASP N  1 92  ? 24.596  113.093 46.021  1.00 16.50 ? 92   ASP N CB  1 
ATOM   14926 C  CG  . ASP N  1 92  ? 23.221  113.541 45.726  0.50 19.09 ? 92   ASP N CG  1 
ATOM   14927 O  OD1 . ASP N  1 92  ? 22.354  113.366 46.615  0.50 23.46 ? 92   ASP N OD1 1 
ATOM   14928 O  OD2 . ASP N  1 92  ? 22.908  114.119 44.668  0.50 21.92 ? 92   ASP N OD2 1 
ATOM   14929 N  N   . GLY N  1 93  ? 23.468  113.114 49.327  1.00 14.29 ? 93   GLY N N   1 
ATOM   14930 C  CA  . GLY N  1 93  ? 23.171  113.978 50.458  1.00 13.50 ? 93   GLY N CA  1 
ATOM   14931 C  C   . GLY N  1 93  ? 22.165  115.075 50.174  1.00 13.17 ? 93   GLY N C   1 
ATOM   14932 O  O   . GLY N  1 93  ? 21.953  115.961 51.008  1.00 12.97 ? 93   GLY N O   1 
ATOM   14933 N  N   . VAL N  1 94  ? 21.533  115.033 49.015  1.00 12.20 ? 94   VAL N N   1 
ATOM   14934 C  CA  . VAL N  1 94  ? 20.531  116.036 48.681  1.00 13.13 ? 94   VAL N CA  1 
ATOM   14935 C  C   . VAL N  1 94  ? 19.104  115.563 48.913  1.00 13.22 ? 94   VAL N C   1 
ATOM   14936 O  O   . VAL N  1 94  ? 18.715  114.502 48.406  1.00 13.66 ? 94   VAL N O   1 
ATOM   14937 C  CB  . VAL N  1 94  ? 20.597  116.471 47.214  1.00 13.47 ? 94   VAL N CB  1 
ATOM   14938 C  CG1 . VAL N  1 94  ? 19.428  117.397 46.940  1.00 14.64 ? 94   VAL N CG1 1 
ATOM   14939 C  CG2 . VAL N  1 94  ? 21.923  117.144 46.917  1.00 15.00 ? 94   VAL N CG2 1 
ATOM   14940 N  N   . ALA N  1 95  ? 18.337  116.326 49.698  1.00 11.98 ? 95   ALA N N   1 
ATOM   14941 C  CA  . ALA N  1 95  ? 16.930  116.021 49.887  1.00 12.78 ? 95   ALA N CA  1 
ATOM   14942 C  C   . ALA N  1 95  ? 16.164  117.010 49.054  1.00 12.74 ? 95   ALA N C   1 
ATOM   14943 O  O   . ALA N  1 95  ? 16.161  118.223 49.316  1.00 13.88 ? 95   ALA N O   1 
ATOM   14944 C  CB  . ALA N  1 95  ? 16.497  116.139 51.392  1.00 12.55 ? 95   ALA N CB  1 
ATOM   14945 N  N   . ASP N  1 96  ? 15.479  116.503 48.051  1.00 12.68 ? 96   ASP N N   1 
ATOM   14946 C  CA  . ASP N  1 96  ? 14.653  117.368 47.252  1.00 13.77 ? 96   ASP N CA  1 
ATOM   14947 C  C   . ASP N  1 96  ? 13.298  117.232 47.886  1.00 13.24 ? 96   ASP N C   1 
ATOM   14948 O  O   . ASP N  1 96  ? 12.657  116.189 47.780  1.00 16.38 ? 96   ASP N O   1 
ATOM   14949 C  CB  . ASP N  1 96  ? 14.687  116.901 45.818  1.00 15.07 ? 96   ASP N CB  1 
ATOM   14950 C  CG  . ASP N  1 96  ? 15.981  117.305 45.152  1.00 17.83 ? 96   ASP N CG  1 
ATOM   14951 O  OD1 . ASP N  1 96  ? 16.662  116.425 44.578  1.00 20.40 ? 96   ASP N OD1 1 
ATOM   14952 O  OD2 . ASP N  1 96  ? 16.408  118.489 45.230  1.00 19.91 ? 96   ASP N OD2 1 
ATOM   14953 N  N   . VAL N  1 97  ? 12.904  118.258 48.622  1.00 11.97 ? 97   VAL N N   1 
ATOM   14954 C  CA  . VAL N  1 97  ? 11.699  118.203 49.414  1.00 10.83 ? 97   VAL N CA  1 
ATOM   14955 C  C   . VAL N  1 97  ? 10.464  118.563 48.609  1.00 11.33 ? 97   VAL N C   1 
ATOM   14956 O  O   . VAL N  1 97  ? 10.510  119.534 47.846  1.00 11.06 ? 97   VAL N O   1 
ATOM   14957 C  CB  . VAL N  1 97  ? 11.856  119.201 50.615  1.00 10.71 ? 97   VAL N CB  1 
ATOM   14958 C  CG1 . VAL N  1 97  ? 10.626  119.229 51.435  1.00 12.57 ? 97   VAL N CG1 1 
ATOM   14959 C  CG2 . VAL N  1 97  ? 13.081  118.804 51.456  1.00 10.81 ? 97   VAL N CG2 1 
ATOM   14960 N  N   . SER N  1 98  ? 9.377   117.797 48.781  1.00 11.11 ? 98   SER N N   1 
ATOM   14961 C  CA  . SER N  1 98  ? 8.079   118.147 48.211  1.00 12.41 ? 98   SER N CA  1 
ATOM   14962 C  C   . SER N  1 98  ? 6.971   117.468 49.012  1.00 12.80 ? 98   SER N C   1 
ATOM   14963 O  O   . SER N  1 98  ? 6.782   116.240 48.975  1.00 11.61 ? 98   SER N O   1 
ATOM   14964 C  CB  . SER N  1 98  ? 7.984   117.782 46.719  1.00 13.76 ? 98   SER N CB  1 
ATOM   14965 O  OG  . SER N  1 98  ? 6.715   118.130 46.172  1.00 14.94 ? 98   SER N OG  1 
ATOM   14966 N  N   . ILE N  1 99  ? 6.225   118.285 49.738  1.00 12.60 ? 99   ILE N N   1 
ATOM   14967 C  CA  . ILE N  1 99  ? 5.249   117.814 50.690  1.00 14.46 ? 99   ILE N CA  1 
ATOM   14968 C  C   . ILE N  1 99  ? 4.046   118.725 50.539  1.00 14.92 ? 99   ILE N C   1 
ATOM   14969 O  O   . ILE N  1 99  ? 4.185   119.899 50.166  1.00 15.00 ? 99   ILE N O   1 
ATOM   14970 C  CB  . ILE N  1 99  ? 5.901   117.994 52.100  1.00 15.18 ? 99   ILE N CB  1 
ATOM   14971 C  CG1 . ILE N  1 99  ? 6.794   116.796 52.468  1.00 16.85 ? 99   ILE N CG1 1 
ATOM   14972 C  CG2 . ILE N  1 99  ? 4.898   118.335 53.218  1.00 17.17 ? 99   ILE N CG2 1 
ATOM   14973 C  CD1 . ILE N  1 99  ? 7.684   117.088 53.721  1.00 17.47 ? 99   ILE N CD1 1 
ATOM   14974 N  N   . GLU N  1 100 ? 2.856   118.207 50.790  1.00 14.60 ? 100  GLU N N   1 
ATOM   14975 C  CA  . GLU N  1 100 ? 1.699   119.085 50.844  1.00 15.08 ? 100  GLU N CA  1 
ATOM   14976 C  C   . GLU N  1 100 ? 1.040   118.808 52.187  1.00 15.13 ? 100  GLU N C   1 
ATOM   14977 O  O   . GLU N  1 100 ? 0.868   117.646 52.571  1.00 14.42 ? 100  GLU N O   1 
ATOM   14978 C  CB  . GLU N  1 100 ? 0.737   118.824 49.680  1.00 16.08 ? 100  GLU N CB  1 
ATOM   14979 C  CG  . GLU N  1 100 ? -0.396  119.833 49.605  1.00 18.40 ? 100  GLU N CG  1 
ATOM   14980 C  CD  . GLU N  1 100 ? -1.362  119.526 48.468  1.00 22.86 ? 100  GLU N CD  1 
ATOM   14981 O  OE1 . GLU N  1 100 ? -1.052  119.934 47.323  1.00 22.86 ? 100  GLU N OE1 1 
ATOM   14982 O  OE2 . GLU N  1 100 ? -2.409  118.859 48.721  1.00 22.53 ? 100  GLU N OE2 1 
ATOM   14983 N  N   . ASP N  1 101 ? 0.683   119.859 52.927  1.00 14.89 ? 101  ASP N N   1 
ATOM   14984 C  CA  . ASP N  1 101 ? 0.138   119.654 54.259  1.00 15.73 ? 101  ASP N CA  1 
ATOM   14985 C  C   . ASP N  1 101 ? -0.954  120.667 54.489  1.00 16.28 ? 101  ASP N C   1 
ATOM   14986 O  O   . ASP N  1 101 ? -0.791  121.826 54.114  1.00 16.09 ? 101  ASP N O   1 
ATOM   14987 C  CB  . ASP N  1 101 ? 1.230   119.865 55.338  1.00 15.96 ? 101  ASP N CB  1 
ATOM   14988 C  CG  . ASP N  1 101 ? 0.781   119.389 56.699  1.00 17.95 ? 101  ASP N CG  1 
ATOM   14989 O  OD1 . ASP N  1 101 ? 0.822   118.150 56.931  1.00 19.99 ? 101  ASP N OD1 1 
ATOM   14990 O  OD2 . ASP N  1 101 ? 0.332   120.166 57.576  1.00 16.19 ? 101  ASP N OD2 1 
ATOM   14991 N  N   . SER N  1 102 ? -2.047  120.241 55.121  1.00 16.81 ? 102  SER N N   1 
ATOM   14992 C  CA  . SER N  1 102 ? -3.150  121.150 55.401  1.00 17.12 ? 102  SER N CA  1 
ATOM   14993 C  C   . SER N  1 102 ? -3.332  121.436 56.875  1.00 17.22 ? 102  SER N C   1 
ATOM   14994 O  O   . SER N  1 102 ? -4.298  122.128 57.256  1.00 16.88 ? 102  SER N O   1 
ATOM   14995 C  CB  . SER N  1 102 ? -4.479  120.585 54.872  1.00 18.00 ? 102  SER N CB  1 
ATOM   14996 O  OG  . SER N  1 102 ? -4.414  120.296 53.495  1.00 20.55 ? 102  SER N OG  1 
ATOM   14997 N  N   . VAL N  1 103 ? -2.461  120.897 57.718  1.00 16.29 ? 103  VAL N N   1 
ATOM   14998 C  CA  . VAL N  1 103 ? -2.551  121.199 59.146  1.00 16.48 ? 103  VAL N CA  1 
ATOM   14999 C  C   . VAL N  1 103 ? -1.795  122.507 59.433  1.00 16.36 ? 103  VAL N C   1 
ATOM   15000 O  O   . VAL N  1 103 ? -2.290  123.370 60.173  1.00 16.56 ? 103  VAL N O   1 
ATOM   15001 C  CB  . VAL N  1 103 ? -2.112  119.994 60.040  1.00 16.75 ? 103  VAL N CB  1 
ATOM   15002 C  CG1 . VAL N  1 103 ? -2.068  120.379 61.507  1.00 16.36 ? 103  VAL N CG1 1 
ATOM   15003 C  CG2 . VAL N  1 103 ? -3.079  118.804 59.863  1.00 17.77 ? 103  VAL N CG2 1 
ATOM   15004 N  N   . ILE N  1 104 ? -0.617  122.685 58.833  1.00 15.77 ? 104  ILE N N   1 
ATOM   15005 C  CA  . ILE N  1 104 ? 0.085   123.967 58.955  1.00 15.09 ? 104  ILE N CA  1 
ATOM   15006 C  C   . ILE N  1 104 ? -0.629  124.972 58.080  1.00 15.35 ? 104  ILE N C   1 
ATOM   15007 O  O   . ILE N  1 104 ? -1.361  124.595 57.169  1.00 15.19 ? 104  ILE N O   1 
ATOM   15008 C  CB  . ILE N  1 104 ? 1.544   123.888 58.450  1.00 14.62 ? 104  ILE N CB  1 
ATOM   15009 C  CG1 . ILE N  1 104 ? 1.585   123.385 56.992  1.00 15.43 ? 104  ILE N CG1 1 
ATOM   15010 C  CG2 . ILE N  1 104 ? 2.372   123.050 59.367  1.00 15.84 ? 104  ILE N CG2 1 
ATOM   15011 C  CD1 . ILE N  1 104 ? 2.966   123.501 56.337  1.00 13.06 ? 104  ILE N CD1 1 
ATOM   15012 N  N   . SER N  1 105 ? -0.431  126.256 58.354  1.00 14.57 ? 105  SER N N   1 
ATOM   15013 C  CA  . SER N  1 105 ? -1.006  127.307 57.527  1.00 14.71 ? 105  SER N CA  1 
ATOM   15014 C  C   . SER N  1 105 ? -0.065  128.516 57.486  1.00 15.28 ? 105  SER N C   1 
ATOM   15015 O  O   . SER N  1 105 ? 0.814   128.633 58.343  1.00 15.44 ? 105  SER N O   1 
ATOM   15016 C  CB  . SER N  1 105 ? -2.370  127.748 58.091  1.00 14.70 ? 105  SER N CB  1 
ATOM   15017 O  OG  . SER N  1 105 ? -3.032  128.550 57.147  1.00 13.06 ? 105  SER N OG  1 
ATOM   15018 N  N   . LEU N  1 106 ? -0.233  129.388 56.486  1.00 15.78 ? 106  LEU N N   1 
ATOM   15019 C  CA  . LEU N  1 106 ? 0.543   130.642 56.399  1.00 17.01 ? 106  LEU N CA  1 
ATOM   15020 C  C   . LEU N  1 106 ? -0.292  131.831 56.871  1.00 18.61 ? 106  LEU N C   1 
ATOM   15021 O  O   . LEU N  1 106 ? 0.051   133.000 56.625  1.00 18.64 ? 106  LEU N O   1 
ATOM   15022 C  CB  . LEU N  1 106 ? 1.040   130.872 54.984  1.00 16.88 ? 106  LEU N CB  1 
ATOM   15023 C  CG  . LEU N  1 106 ? 1.844   129.681 54.451  1.00 16.02 ? 106  LEU N CG  1 
ATOM   15024 C  CD1 . LEU N  1 106 ? 2.402   130.002 53.076  1.00 15.15 ? 106  LEU N CD1 1 
ATOM   15025 C  CD2 . LEU N  1 106 ? 2.969   129.339 55.444  1.00 13.93 ? 106  LEU N CD2 1 
ATOM   15026 N  N   . SER N  1 107 ? -1.394  131.518 57.545  1.00 19.41 ? 107  SER N N   1 
ATOM   15027 C  CA  . SER N  1 107 ? -2.222  132.521 58.210  1.00 21.30 ? 107  SER N CA  1 
ATOM   15028 C  C   . SER N  1 107 ? -3.173  131.832 59.182  1.00 21.82 ? 107  SER N C   1 
ATOM   15029 O  O   . SER N  1 107 ? -3.470  130.650 59.024  1.00 22.23 ? 107  SER N O   1 
ATOM   15030 C  CB  . SER N  1 107 ? -3.029  133.321 57.193  1.00 21.07 ? 107  SER N CB  1 
ATOM   15031 O  OG  . SER N  1 107 ? -3.913  132.465 56.517  1.00 21.85 ? 107  SER N OG  1 
ATOM   15032 N  N   . GLY N  1 108 ? -3.647  132.573 60.183  1.00 22.82 ? 108  GLY N N   1 
ATOM   15033 C  CA  . GLY N  1 108 ? -4.609  132.050 61.145  1.00 23.35 ? 108  GLY N CA  1 
ATOM   15034 C  C   . GLY N  1 108 ? -3.977  131.531 62.427  1.00 24.10 ? 108  GLY N C   1 
ATOM   15035 O  O   . GLY N  1 108 ? -2.832  131.856 62.745  1.00 23.99 ? 108  GLY N O   1 
ATOM   15036 N  N   . ASP N  1 109 ? -4.708  130.693 63.157  1.00 24.66 ? 109  ASP N N   1 
ATOM   15037 C  CA  . ASP N  1 109 ? -4.207  130.180 64.432  1.00 25.39 ? 109  ASP N CA  1 
ATOM   15038 C  C   . ASP N  1 109 ? -3.086  129.137 64.308  1.00 24.80 ? 109  ASP N C   1 
ATOM   15039 O  O   . ASP N  1 109 ? -2.288  129.005 65.231  1.00 25.52 ? 109  ASP N O   1 
ATOM   15040 C  CB  . ASP N  1 109 ? -5.360  129.666 65.294  1.00 25.46 ? 109  ASP N CB  1 
ATOM   15041 C  CG  . ASP N  1 109 ? -6.446  130.713 65.477  1.00 28.12 ? 109  ASP N CG  1 
ATOM   15042 O  OD1 . ASP N  1 109 ? -6.086  131.906 65.667  1.00 29.24 ? 109  ASP N OD1 1 
ATOM   15043 O  OD2 . ASP N  1 109 ? -7.678  130.447 65.433  1.00 29.51 ? 109  ASP N OD2 1 
ATOM   15044 N  N   . HIS N  1 110 ? -3.030  128.411 63.183  1.00 24.42 ? 110  HIS N N   1 
ATOM   15045 C  CA  . HIS N  1 110 ? -1.976  127.404 62.928  1.00 23.87 ? 110  HIS N CA  1 
ATOM   15046 C  C   . HIS N  1 110 ? -0.858  127.996 62.069  1.00 22.63 ? 110  HIS N C   1 
ATOM   15047 O  O   . HIS N  1 110 ? -0.100  127.261 61.403  1.00 21.93 ? 110  HIS N O   1 
ATOM   15048 C  CB  . HIS N  1 110 ? -2.519  126.164 62.187  1.00 24.87 ? 110  HIS N CB  1 
ATOM   15049 C  CG  . HIS N  1 110 ? -3.452  125.313 62.996  1.00 27.19 ? 110  HIS N CG  1 
ATOM   15050 N  ND1 . HIS N  1 110 ? -3.978  124.132 62.517  1.00 29.64 ? 110  HIS N ND1 1 
ATOM   15051 C  CD2 . HIS N  1 110 ? -3.960  125.474 64.244  1.00 28.56 ? 110  HIS N CD2 1 
ATOM   15052 C  CE1 . HIS N  1 110 ? -4.779  123.606 63.429  1.00 30.70 ? 110  HIS N CE1 1 
ATOM   15053 N  NE2 . HIS N  1 110 ? -4.780  124.396 64.489  1.00 29.54 ? 110  HIS N NE2 1 
ATOM   15054 N  N   . CYS N  1 111 ? -0.771  129.320 62.069  1.00 21.06 ? 111  CYS N N   1 
ATOM   15055 C  CA  . CYS N  1 111 ? 0.180   130.021 61.236  1.00 20.50 ? 111  CYS N CA  1 
ATOM   15056 C  C   . CYS N  1 111 ? 1.625   129.722 61.659  1.00 18.54 ? 111  CYS N C   1 
ATOM   15057 O  O   . CYS N  1 111 ? 1.959   129.816 62.828  1.00 17.85 ? 111  CYS N O   1 
ATOM   15058 C  CB  . CYS N  1 111 ? -0.103  131.524 61.282  1.00 20.45 ? 111  CYS N CB  1 
ATOM   15059 S  SG  . CYS N  1 111 ? 0.843   132.465 60.075  1.00 28.06 ? 111  CYS N SG  1 
ATOM   15060 N  N   . ILE N  1 112 ? 2.470   129.355 60.705  1.00 16.66 ? 112  ILE N N   1 
ATOM   15061 C  CA  . ILE N  1 112 ? 3.859   129.069 61.030  1.00 14.78 ? 112  ILE N CA  1 
ATOM   15062 C  C   . ILE N  1 112 ? 4.840   130.191 60.666  1.00 15.17 ? 112  ILE N C   1 
ATOM   15063 O  O   . ILE N  1 112 ? 6.050   130.007 60.787  1.00 14.88 ? 112  ILE N O   1 
ATOM   15064 C  CB  . ILE N  1 112 ? 4.277   127.756 60.354  1.00 14.90 ? 112  ILE N CB  1 
ATOM   15065 C  CG1 . ILE N  1 112 ? 4.400   127.958 58.839  1.00 13.13 ? 112  ILE N CG1 1 
ATOM   15066 C  CG2 . ILE N  1 112 ? 3.287   126.629 60.758  1.00 10.48 ? 112  ILE N CG2 1 
ATOM   15067 C  CD1 . ILE N  1 112 ? 4.837   126.689 58.050  1.00 12.73 ? 112  ILE N CD1 1 
ATOM   15068 N  N   . ILE N  1 113 ? 4.341   131.348 60.228  1.00 14.63 ? 113  ILE N N   1 
ATOM   15069 C  CA  . ILE N  1 113 ? 5.238   132.427 59.845  1.00 14.99 ? 113  ILE N CA  1 
ATOM   15070 C  C   . ILE N  1 113 ? 5.881   132.941 61.120  1.00 13.44 ? 113  ILE N C   1 
ATOM   15071 O  O   . ILE N  1 113 ? 5.211   133.067 62.131  1.00 11.87 ? 113  ILE N O   1 
ATOM   15072 C  CB  . ILE N  1 113 ? 4.475   133.583 59.181  1.00 15.53 ? 113  ILE N CB  1 
ATOM   15073 C  CG1 . ILE N  1 113 ? 3.829   133.147 57.868  1.00 18.13 ? 113  ILE N CG1 1 
ATOM   15074 C  CG2 . ILE N  1 113 ? 5.400   134.777 58.958  1.00 15.83 ? 113  ILE N CG2 1 
ATOM   15075 C  CD1 . ILE N  1 113 ? 4.813   132.805 56.794  1.00 19.20 ? 113  ILE N CD1 1 
ATOM   15076 N  N   . GLY N  1 114 ? 7.186   133.222 61.097  1.00 12.34 ? 114  GLY N N   1 
ATOM   15077 C  CA  . GLY N  1 114 ? 7.829   133.690 62.293  1.00 11.22 ? 114  GLY N CA  1 
ATOM   15078 C  C   . GLY N  1 114 ? 8.252   132.528 63.141  1.00 11.65 ? 114  GLY N C   1 
ATOM   15079 O  O   . GLY N  1 114 ? 8.826   132.720 64.204  1.00 11.09 ? 114  GLY N O   1 
ATOM   15080 N  N   . ARG N  1 115 ? 8.003   131.307 62.675  1.00 11.02 ? 115  ARG N N   1 
ATOM   15081 C  CA  . ARG N  1 115 ? 8.414   130.158 63.468  1.00 11.41 ? 115  ARG N CA  1 
ATOM   15082 C  C   . ARG N  1 115 ? 9.651   129.531 62.807  1.00 10.83 ? 115  ARG N C   1 
ATOM   15083 O  O   . ARG N  1 115 ? 10.152  130.086 61.843  1.00 12.06 ? 115  ARG N O   1 
ATOM   15084 C  CB  . ARG N  1 115 ? 7.256   129.186 63.681  1.00 11.52 ? 115  ARG N CB  1 
ATOM   15085 C  CG  . ARG N  1 115 ? 6.061   129.887 64.430  1.00 12.05 ? 115  ARG N CG  1 
ATOM   15086 C  CD  . ARG N  1 115 ? 4.952   128.948 64.879  1.00 14.40 ? 115  ARG N CD  1 
ATOM   15087 N  NE  . ARG N  1 115 ? 3.773   129.666 65.419  1.00 14.64 ? 115  ARG N NE  1 
ATOM   15088 C  CZ  . ARG N  1 115 ? 3.674   130.120 66.671  1.00 14.98 ? 115  ARG N CZ  1 
ATOM   15089 N  NH1 . ARG N  1 115 ? 4.659   129.930 67.536  1.00 13.47 ? 115  ARG N NH1 1 
ATOM   15090 N  NH2 . ARG N  1 115 ? 2.562   130.741 67.075  1.00 16.39 ? 115  ARG N NH2 1 
ATOM   15091 N  N   . THR N  1 116 ? 10.144  128.417 63.331  1.00 10.99 ? 116  THR N N   1 
ATOM   15092 C  CA  . THR N  1 116 ? 11.393  127.845 62.836  1.00 10.98 ? 116  THR N CA  1 
ATOM   15093 C  C   . THR N  1 116 ? 11.226  126.480 62.182  1.00 11.96 ? 116  THR N C   1 
ATOM   15094 O  O   . THR N  1 116 ? 10.646  125.585 62.781  1.00 12.31 ? 116  THR N O   1 
ATOM   15095 C  CB  . THR N  1 116 ? 12.362  127.690 64.017  1.00 10.81 ? 116  THR N CB  1 
ATOM   15096 O  OG1 . THR N  1 116 ? 12.810  128.982 64.409  1.00 11.83 ? 116  THR N OG1 1 
ATOM   15097 C  CG2 . THR N  1 116 ? 13.685  127.008 63.563  1.00 10.11 ? 116  THR N CG2 1 
ATOM   15098 N  N   . LEU N  1 117 ? 11.742  126.332 60.959  1.00 11.28 ? 117  LEU N N   1 
ATOM   15099 C  CA  . LEU N  1 117 ? 11.762  125.020 60.300  1.00 10.41 ? 117  LEU N CA  1 
ATOM   15100 C  C   . LEU N  1 117 ? 13.055  124.317 60.689  1.00 10.53 ? 117  LEU N C   1 
ATOM   15101 O  O   . LEU N  1 117 ? 14.134  124.911 60.631  1.00 10.25 ? 117  LEU N O   1 
ATOM   15102 C  CB  . LEU N  1 117 ? 11.643  125.190 58.779  1.00 9.86  ? 117  LEU N CB  1 
ATOM   15103 C  CG  . LEU N  1 117 ? 11.571  123.891 57.940  1.00 9.10  ? 117  LEU N CG  1 
ATOM   15104 C  CD1 . LEU N  1 117 ? 10.278  123.120 58.191  1.00 12.44 ? 117  LEU N CD1 1 
ATOM   15105 C  CD2 . LEU N  1 117 ? 11.702  124.249 56.454  1.00 10.09 ? 117  LEU N CD2 1 
ATOM   15106 N  N   . VAL N  1 118 ? 12.965  123.046 61.116  1.00 9.63  ? 118  VAL N N   1 
ATOM   15107 C  CA  . VAL N  1 118 ? 14.143  122.315 61.522  1.00 9.27  ? 118  VAL N CA  1 
ATOM   15108 C  C   . VAL N  1 118 ? 14.304  121.005 60.745  1.00 9.34  ? 118  VAL N C   1 
ATOM   15109 O  O   . VAL N  1 118 ? 13.317  120.284 60.553  1.00 9.61  ? 118  VAL N O   1 
ATOM   15110 C  CB  . VAL N  1 118 ? 14.115  121.975 63.041  1.00 9.52  ? 118  VAL N CB  1 
ATOM   15111 C  CG1 . VAL N  1 118 ? 15.343  121.196 63.423  1.00 10.82 ? 118  VAL N CG1 1 
ATOM   15112 C  CG2 . VAL N  1 118 ? 14.091  123.245 63.858  1.00 8.66  ? 118  VAL N CG2 1 
ATOM   15113 N  N   . VAL N  1 119 ? 15.532  120.720 60.280  1.00 8.60  ? 119  VAL N N   1 
ATOM   15114 C  CA  . VAL N  1 119 ? 15.820  119.384 59.725  1.00 8.55  ? 119  VAL N CA  1 
ATOM   15115 C  C   . VAL N  1 119 ? 16.751  118.648 60.682  1.00 9.10  ? 119  VAL N C   1 
ATOM   15116 O  O   . VAL N  1 119 ? 17.755  119.227 61.187  1.00 8.98  ? 119  VAL N O   1 
ATOM   15117 C  CB  . VAL N  1 119 ? 16.384  119.398 58.254  1.00 8.32  ? 119  VAL N CB  1 
ATOM   15118 C  CG1 . VAL N  1 119 ? 17.743  120.130 58.166  1.00 8.29  ? 119  VAL N CG1 1 
ATOM   15119 C  CG2 . VAL N  1 119 ? 16.569  117.948 57.731  1.00 8.54  ? 119  VAL N CG2 1 
ATOM   15120 N  N   . HIS N  1 120 ? 16.416  117.393 60.958  1.00 8.93  ? 120  HIS N N   1 
ATOM   15121 C  CA  . HIS N  1 120 ? 17.107  116.615 62.003  1.00 9.78  ? 120  HIS N CA  1 
ATOM   15122 C  C   . HIS N  1 120 ? 18.152  115.602 61.575  1.00 10.68 ? 120  HIS N C   1 
ATOM   15123 O  O   . HIS N  1 120 ? 18.226  115.170 60.441  1.00 11.10 ? 120  HIS N O   1 
ATOM   15124 C  CB  . HIS N  1 120 ? 16.070  115.865 62.852  1.00 9.09  ? 120  HIS N CB  1 
ATOM   15125 C  CG  . HIS N  1 120 ? 15.266  116.763 63.744  1.00 9.21  ? 120  HIS N CG  1 
ATOM   15126 N  ND1 . HIS N  1 120 ? 15.673  117.079 65.022  1.00 9.71  ? 120  HIS N ND1 1 
ATOM   15127 C  CD2 . HIS N  1 120 ? 14.097  117.422 63.546  1.00 9.66  ? 120  HIS N CD2 1 
ATOM   15128 C  CE1 . HIS N  1 120 ? 14.779  117.886 65.585  1.00 7.77  ? 120  HIS N CE1 1 
ATOM   15129 N  NE2 . HIS N  1 120 ? 13.831  118.125 64.699  1.00 8.12  ? 120  HIS N NE2 1 
ATOM   15130 N  N   . GLU N  1 121 ? 18.890  115.155 62.574  1.00 12.30 ? 121  GLU N N   1 
ATOM   15131 C  CA  . GLU N  1 121 ? 19.955  114.183 62.428  1.00 13.83 ? 121  GLU N CA  1 
ATOM   15132 C  C   . GLU N  1 121 ? 19.466  112.825 61.938  1.00 14.25 ? 121  GLU N C   1 
ATOM   15133 O  O   . GLU N  1 121 ? 20.085  112.212 61.068  1.00 14.81 ? 121  GLU N O   1 
ATOM   15134 C  CB  . GLU N  1 121 ? 20.569  113.985 63.821  1.00 14.56 ? 121  GLU N CB  1 
ATOM   15135 C  CG  . GLU N  1 121 ? 21.670  112.944 63.950  1.00 17.46 ? 121  GLU N CG  1 
ATOM   15136 C  CD  . GLU N  1 121 ? 21.827  112.448 65.394  1.00 23.16 ? 121  GLU N CD  1 
ATOM   15137 O  OE1 . GLU N  1 121 ? 21.231  113.036 66.341  1.00 21.59 ? 121  GLU N OE1 1 
ATOM   15138 O  OE2 . GLU N  1 121 ? 22.539  111.438 65.598  1.00 25.07 ? 121  GLU N OE2 1 
ATOM   15139 N  N   . LYS N  1 122 ? 18.373  112.371 62.545  1.00 14.22 ? 122  LYS N N   1 
ATOM   15140 C  CA  . LYS N  1 122 ? 17.840  111.014 62.375  1.00 14.29 ? 122  LYS N CA  1 
ATOM   15141 C  C   . LYS N  1 122 ? 16.399  111.014 61.813  1.00 13.26 ? 122  LYS N C   1 
ATOM   15142 O  O   . LYS N  1 122 ? 15.734  112.049 61.745  1.00 12.22 ? 122  LYS N O   1 
ATOM   15143 C  CB  . LYS N  1 122 ? 17.779  110.339 63.767  1.00 14.92 ? 122  LYS N CB  1 
ATOM   15144 C  CG  . LYS N  1 122 ? 19.123  109.951 64.432  1.00 18.78 ? 122  LYS N CG  1 
ATOM   15145 C  CD  . LYS N  1 122 ? 18.914  109.393 65.865  1.00 21.04 ? 122  LYS N CD  1 
ATOM   15146 C  CE  . LYS N  1 122 ? 20.244  108.988 66.512  1.00 26.66 ? 122  LYS N CE  1 
ATOM   15147 N  NZ  . LYS N  1 122 ? 20.130  108.426 67.907  1.00 26.69 ? 122  LYS N NZ  1 
ATOM   15148 N  N   . ALA N  1 123 ? 15.921  109.827 61.442  1.00 12.58 ? 123  ALA N N   1 
ATOM   15149 C  CA  . ALA N  1 123 ? 14.554  109.682 60.993  1.00 12.97 ? 123  ALA N CA  1 
ATOM   15150 C  C   . ALA N  1 123 ? 13.619  110.006 62.158  1.00 12.82 ? 123  ALA N C   1 
ATOM   15151 O  O   . ALA N  1 123 ? 13.908  109.672 63.300  1.00 13.00 ? 123  ALA N O   1 
ATOM   15152 C  CB  . ALA N  1 123 ? 14.317  108.238 60.575  1.00 13.45 ? 123  ALA N CB  1 
ATOM   15153 N  N   . ASP N  1 124 ? 12.517  110.666 61.862  1.00 12.31 ? 124  ASP N N   1 
ATOM   15154 C  CA  . ASP N  1 124 ? 11.440  110.837 62.812  1.00 12.48 ? 124  ASP N CA  1 
ATOM   15155 C  C   . ASP N  1 124 ? 10.708  109.466 62.886  1.00 12.49 ? 124  ASP N C   1 
ATOM   15156 O  O   . ASP N  1 124 ? 10.352  108.932 61.830  1.00 12.40 ? 124  ASP N O   1 
ATOM   15157 C  CB  . ASP N  1 124 ? 10.510  111.882 62.221  1.00 12.36 ? 124  ASP N CB  1 
ATOM   15158 C  CG  . ASP N  1 124 ? 9.378   112.283 63.148  1.00 14.08 ? 124  ASP N CG  1 
ATOM   15159 O  OD1 . ASP N  1 124 ? 8.945   111.483 64.031  1.00 12.26 ? 124  ASP N OD1 1 
ATOM   15160 O  OD2 . ASP N  1 124 ? 8.828   113.385 63.030  1.00 13.25 ? 124  ASP N OD2 1 
ATOM   15161 N  N   . ASP N  1 125 ? 10.463  108.895 64.084  1.00 12.27 ? 125  ASP N N   1 
ATOM   15162 C  CA  . ASP N  1 125 ? 9.743   107.599 64.141  1.00 12.10 ? 125  ASP N CA  1 
ATOM   15163 C  C   . ASP N  1 125 ? 8.222   107.736 64.088  1.00 11.39 ? 125  ASP N C   1 
ATOM   15164 O  O   . ASP N  1 125 ? 7.463   106.753 64.190  1.00 11.16 ? 125  ASP N O   1 
ATOM   15165 C  CB  . ASP N  1 125 ? 10.145  106.707 65.334  1.00 11.57 ? 125  ASP N CB  1 
ATOM   15166 C  CG  . ASP N  1 125 ? 9.775   107.290 66.666  1.00 11.94 ? 125  ASP N CG  1 
ATOM   15167 O  OD1 . ASP N  1 125 ? 8.913   108.193 66.777  1.00 9.52  ? 125  ASP N OD1 1 
ATOM   15168 O  OD2 . ASP N  1 125 ? 10.335  106.873 67.693  1.00 15.66 ? 125  ASP N OD2 1 
ATOM   15169 N  N   . LEU N  1 126 ? 7.795   108.978 63.899  1.00 9.10  ? 126  LEU N N   1 
ATOM   15170 C  CA  . LEU N  1 126 ? 6.405   109.323 63.712  1.00 9.54  ? 126  LEU N CA  1 
ATOM   15171 C  C   . LEU N  1 126 ? 5.545   108.932 64.925  1.00 8.52  ? 126  LEU N C   1 
ATOM   15172 O  O   . LEU N  1 126 ? 4.335   108.734 64.807  1.00 8.08  ? 126  LEU N O   1 
ATOM   15173 C  CB  . LEU N  1 126 ? 5.867   108.753 62.398  1.00 10.41 ? 126  LEU N CB  1 
ATOM   15174 C  CG  . LEU N  1 126 ? 6.793   108.983 61.198  1.00 13.56 ? 126  LEU N CG  1 
ATOM   15175 C  CD1 . LEU N  1 126 ? 6.218   108.226 60.002  1.00 15.57 ? 126  LEU N CD1 1 
ATOM   15176 C  CD2 . LEU N  1 126 ? 6.997   110.479 60.903  1.00 14.32 ? 126  LEU N CD2 1 
ATOM   15177 N  N   . GLY N  1 127 ? 6.184   108.892 66.094  1.00 7.78  ? 127  GLY N N   1 
ATOM   15178 C  CA  . GLY N  1 127 ? 5.472   108.631 67.345  1.00 6.44  ? 127  GLY N CA  1 
ATOM   15179 C  C   . GLY N  1 127 ? 5.231   107.156 67.578  1.00 7.36  ? 127  GLY N C   1 
ATOM   15180 O  O   . GLY N  1 127 ? 4.501   106.766 68.500  1.00 5.00  ? 127  GLY N O   1 
ATOM   15181 N  N   . LYS N  1 128 ? 5.853   106.321 66.764  1.00 7.22  ? 128  LYS N N   1 
ATOM   15182 C  CA  . LYS N  1 128 ? 5.592   104.894 66.891  1.00 9.45  ? 128  LYS N CA  1 
ATOM   15183 C  C   . LYS N  1 128 ? 6.724   104.171 67.602  1.00 8.69  ? 128  LYS N C   1 
ATOM   15184 O  O   . LYS N  1 128 ? 6.820   102.964 67.511  1.00 10.30 ? 128  LYS N O   1 
ATOM   15185 C  CB  . LYS N  1 128 ? 5.323   104.299 65.493  1.00 9.01  ? 128  LYS N CB  1 
ATOM   15186 C  CG  . LYS N  1 128 ? 4.163   105.032 64.764  1.00 15.16 ? 128  LYS N CG  1 
ATOM   15187 C  CD  . LYS N  1 128 ? 3.959   104.580 63.315  1.00 19.89 ? 128  LYS N CD  1 
ATOM   15188 C  CE  . LYS N  1 128 ? 2.593   103.925 63.103  1.00 25.63 ? 128  LYS N CE  1 
ATOM   15189 N  NZ  . LYS N  1 128 ? 1.499   104.872 62.644  1.00 29.99 ? 128  LYS N NZ  1 
ATOM   15190 N  N   . GLY N  1 129 ? 7.553   104.909 68.324  1.00 7.82  ? 129  GLY N N   1 
ATOM   15191 C  CA  . GLY N  1 129 ? 8.694   104.340 69.009  1.00 7.44  ? 129  GLY N CA  1 
ATOM   15192 C  C   . GLY N  1 129 ? 8.467   103.689 70.373  1.00 7.03  ? 129  GLY N C   1 
ATOM   15193 O  O   . GLY N  1 129 ? 9.397   103.109 70.938  1.00 7.27  ? 129  GLY N O   1 
ATOM   15194 N  N   . GLY N  1 130 ? 7.258   103.783 70.926  1.00 5.97  ? 130  GLY N N   1 
ATOM   15195 C  CA  . GLY N  1 130 ? 7.004   103.156 72.225  1.00 5.31  ? 130  GLY N CA  1 
ATOM   15196 C  C   . GLY N  1 130 ? 7.696   103.771 73.442  1.00 6.43  ? 130  GLY N C   1 
ATOM   15197 O  O   . GLY N  1 130 ? 7.490   103.288 74.553  1.00 6.74  ? 130  GLY N O   1 
ATOM   15198 N  N   . ASN N  1 131 ? 8.558   104.779 73.259  1.00 6.34  ? 131  ASN N N   1 
ATOM   15199 C  CA  . ASN N  1 131 ? 9.167   105.441 74.431  1.00 7.10  ? 131  ASN N CA  1 
ATOM   15200 C  C   . ASN N  1 131 ? 8.662   106.873 74.599  1.00 7.29  ? 131  ASN N C   1 
ATOM   15201 O  O   . ASN N  1 131 ? 7.968   107.392 73.733  1.00 7.83  ? 131  ASN N O   1 
ATOM   15202 C  CB  . ASN N  1 131 ? 10.717  105.351 74.456  1.00 6.69  ? 131  ASN N CB  1 
ATOM   15203 C  CG  . ASN N  1 131 ? 11.379  106.046 73.285  1.00 8.61  ? 131  ASN N CG  1 
ATOM   15204 O  OD1 . ASN N  1 131 ? 10.734  106.748 72.524  1.00 12.57 ? 131  ASN N OD1 1 
ATOM   15205 N  ND2 . ASN N  1 131 ? 12.691  105.871 73.156  1.00 6.42  ? 131  ASN N ND2 1 
ATOM   15206 N  N   . GLU N  1 132 ? 9.013   107.542 75.681  1.00 8.79  ? 132  GLU N N   1 
ATOM   15207 C  CA  . GLU N  1 132 ? 8.474   108.879 75.877  1.00 10.60 ? 132  GLU N CA  1 
ATOM   15208 C  C   . GLU N  1 132 ? 9.030   109.862 74.836  1.00 11.02 ? 132  GLU N C   1 
ATOM   15209 O  O   . GLU N  1 132 ? 8.323   110.755 74.380  1.00 10.23 ? 132  GLU N O   1 
ATOM   15210 C  CB  . GLU N  1 132 ? 8.717   109.363 77.310  1.00 12.63 ? 132  GLU N CB  1 
ATOM   15211 C  CG  . GLU N  1 132 ? 8.323   110.812 77.539  1.00 17.07 ? 132  GLU N CG  1 
ATOM   15212 C  CD  . GLU N  1 132 ? 7.062   110.985 78.367  1.00 24.26 ? 132  GLU N CD  1 
ATOM   15213 O  OE1 . GLU N  1 132 ? 6.225   110.035 78.453  1.00 26.50 ? 132  GLU N OE1 1 
ATOM   15214 O  OE2 . GLU N  1 132 ? 6.918   112.091 78.959  1.00 27.35 ? 132  GLU N OE2 1 
ATOM   15215 N  N   . GLU N  1 133 ? 10.287  109.669 74.448  1.00 11.28 ? 133  GLU N N   1 
ATOM   15216 C  CA  . GLU N  1 133 ? 10.896  110.524 73.451  1.00 12.74 ? 133  GLU N CA  1 
ATOM   15217 C  C   . GLU N  1 133 ? 10.060  110.458 72.184  1.00 11.94 ? 133  GLU N C   1 
ATOM   15218 O  O   . GLU N  1 133 ? 9.805   111.479 71.537  1.00 12.85 ? 133  GLU N O   1 
ATOM   15219 C  CB  . GLU N  1 133 ? 12.320  110.054 73.142  1.00 13.55 ? 133  GLU N CB  1 
ATOM   15220 C  CG  . GLU N  1 133 ? 13.126  111.099 72.406  1.00 18.29 ? 133  GLU N CG  1 
ATOM   15221 C  CD  . GLU N  1 133 ? 13.141  112.397 73.185  1.00 23.44 ? 133  GLU N CD  1 
ATOM   15222 O  OE1 . GLU N  1 133 ? 13.639  112.396 74.335  1.00 25.96 ? 133  GLU N OE1 1 
ATOM   15223 O  OE2 . GLU N  1 133 ? 12.615  113.408 72.666  1.00 26.22 ? 133  GLU N OE2 1 
ATOM   15224 N  N   . SER N  1 134 ? 9.640   109.258 71.814  1.00 11.59 ? 134  SER N N   1 
ATOM   15225 C  CA  . SER N  1 134 ? 8.890   109.105 70.565  1.00 10.52 ? 134  SER N CA  1 
ATOM   15226 C  C   . SER N  1 134 ? 7.662   110.012 70.535  1.00 11.24 ? 134  SER N C   1 
ATOM   15227 O  O   . SER N  1 134 ? 7.362   110.632 69.512  1.00 10.10 ? 134  SER N O   1 
ATOM   15228 C  CB  . SER N  1 134 ? 8.468   107.656 70.342  1.00 10.19 ? 134  SER N CB  1 
ATOM   15229 O  OG  . SER N  1 134 ? 7.743   107.577 69.141  1.00 7.17  ? 134  SER N OG  1 
ATOM   15230 N  N   . THR N  1 135 ? 6.980   110.123 71.666  1.00 11.17 ? 135  THR N N   1 
ATOM   15231 C  CA  . THR N  1 135 ? 5.786   110.948 71.759  1.00 12.46 ? 135  THR N CA  1 
ATOM   15232 C  C   . THR N  1 135 ? 6.017   112.444 71.805  1.00 12.70 ? 135  THR N C   1 
ATOM   15233 O  O   . THR N  1 135 ? 5.041   113.198 71.800  1.00 12.47 ? 135  THR N O   1 
ATOM   15234 C  CB  . THR N  1 135 ? 5.001   110.577 73.041  1.00 12.37 ? 135  THR N CB  1 
ATOM   15235 O  OG1 . THR N  1 135 ? 5.639   111.186 74.183  1.00 16.40 ? 135  THR N OG1 1 
ATOM   15236 C  CG2 . THR N  1 135 ? 5.114   109.096 73.306  1.00 11.60 ? 135  THR N CG2 1 
ATOM   15237 N  N   . LYS N  1 136 ? 7.284   112.870 71.872  1.00 12.89 ? 136  LYS N N   1 
ATOM   15238 C  CA  . LYS N  1 136 ? 7.613   114.291 71.946  1.00 14.21 ? 136  LYS N CA  1 
ATOM   15239 C  C   . LYS N  1 136 ? 8.313   114.789 70.690  1.00 13.33 ? 136  LYS N C   1 
ATOM   15240 O  O   . LYS N  1 136 ? 7.876   115.760 70.095  1.00 12.78 ? 136  LYS N O   1 
ATOM   15241 C  CB  . LYS N  1 136 ? 8.465   114.600 73.187  1.00 14.57 ? 136  LYS N CB  1 
ATOM   15242 C  CG  . LYS N  1 136 ? 7.691   114.499 74.484  1.00 18.61 ? 136  LYS N CG  1 
ATOM   15243 C  CD  . LYS N  1 136 ? 8.581   114.804 75.699  1.00 24.83 ? 136  LYS N CD  1 
ATOM   15244 C  CE  . LYS N  1 136 ? 9.756   113.832 75.767  1.00 27.02 ? 136  LYS N CE  1 
ATOM   15245 N  NZ  . LYS N  1 136 ? 10.585  114.000 77.002  1.00 29.09 ? 136  LYS N NZ  1 
ATOM   15246 N  N   . THR N  1 137 ? 9.356   114.086 70.267  1.00 13.83 ? 137  THR N N   1 
ATOM   15247 C  CA  . THR N  1 137 ? 10.158  114.514 69.097  1.00 14.60 ? 137  THR N CA  1 
ATOM   15248 C  C   . THR N  1 137 ? 10.284  113.488 67.987  1.00 14.45 ? 137  THR N C   1 
ATOM   15249 O  O   . THR N  1 137 ? 10.888  113.765 66.953  1.00 14.94 ? 137  THR N O   1 
ATOM   15250 C  CB  . THR N  1 137 ? 11.580  114.826 69.552  1.00 14.61 ? 137  THR N CB  1 
ATOM   15251 O  OG1 . THR N  1 137 ? 12.141  113.642 70.133  1.00 14.24 ? 137  THR N OG1 1 
ATOM   15252 C  CG2 . THR N  1 137 ? 11.565  115.804 70.662  1.00 15.98 ? 137  THR N CG2 1 
ATOM   15253 N  N   . GLY N  1 138 ? 9.766   112.284 68.189  1.00 13.82 ? 138  GLY N N   1 
ATOM   15254 C  CA  . GLY N  1 138 ? 9.895   111.257 67.161  1.00 14.01 ? 138  GLY N CA  1 
ATOM   15255 C  C   . GLY N  1 138 ? 11.271  110.613 67.183  1.00 13.20 ? 138  GLY N C   1 
ATOM   15256 O  O   . GLY N  1 138 ? 11.603  109.856 66.289  1.00 14.13 ? 138  GLY N O   1 
ATOM   15257 N  N   . ASN N  1 139 ? 12.042  110.889 68.238  1.00 13.63 ? 139  ASN N N   1 
ATOM   15258 C  CA  . ASN N  1 139 ? 13.402  110.410 68.360  1.00 13.87 ? 139  ASN N CA  1 
ATOM   15259 C  C   . ASN N  1 139 ? 14.252  110.852 67.160  1.00 13.14 ? 139  ASN N C   1 
ATOM   15260 O  O   . ASN N  1 139 ? 15.175  110.146 66.786  1.00 12.63 ? 139  ASN N O   1 
ATOM   15261 C  CB  . ASN N  1 139 ? 13.441  108.893 68.411  1.00 13.25 ? 139  ASN N CB  1 
ATOM   15262 C  CG  . ASN N  1 139 ? 12.997  108.349 69.742  1.00 15.60 ? 139  ASN N CG  1 
ATOM   15263 O  OD1 . ASN N  1 139 ? 13.584  108.666 70.748  1.00 18.51 ? 139  ASN N OD1 1 
ATOM   15264 N  ND2 . ASN N  1 139 ? 11.945  107.543 69.743  1.00 15.57 ? 139  ASN N ND2 1 
ATOM   15265 N  N   . ALA N  1 140 ? 13.976  112.023 66.599  1.00 13.21 ? 140  ALA N N   1 
ATOM   15266 C  CA  . ALA N  1 140 ? 14.702  112.480 65.401  1.00 13.45 ? 140  ALA N CA  1 
ATOM   15267 C  C   . ALA N  1 140 ? 16.103  113.018 65.683  1.00 13.92 ? 140  ALA N C   1 
ATOM   15268 O  O   . ALA N  1 140 ? 16.835  113.436 64.778  1.00 14.20 ? 140  ALA N O   1 
ATOM   15269 C  CB  . ALA N  1 140 ? 13.876  113.498 64.631  1.00 12.81 ? 140  ALA N CB  1 
ATOM   15270 N  N   . GLY N  1 141 ? 16.478  113.051 66.949  1.00 13.72 ? 141  GLY N N   1 
ATOM   15271 C  CA  . GLY N  1 141 ? 17.830  113.435 67.262  1.00 13.80 ? 141  GLY N CA  1 
ATOM   15272 C  C   . GLY N  1 141 ? 18.164  114.908 67.082  1.00 13.42 ? 141  GLY N C   1 
ATOM   15273 O  O   . GLY N  1 141 ? 17.301  115.774 67.208  1.00 12.04 ? 141  GLY N O   1 
ATOM   15274 N  N   . SER N  1 142 ? 19.435  115.186 66.796  1.00 13.54 ? 142  SER N N   1 
ATOM   15275 C  CA  . SER N  1 142 ? 19.897  116.564 66.807  1.00 13.20 ? 142  SER N CA  1 
ATOM   15276 C  C   . SER N  1 142 ? 19.321  117.440 65.690  1.00 12.55 ? 142  SER N C   1 
ATOM   15277 O  O   . SER N  1 142 ? 18.786  116.942 64.694  1.00 12.13 ? 142  SER N O   1 
ATOM   15278 C  CB  . SER N  1 142 ? 21.436  116.655 66.873  1.00 14.11 ? 142  SER N CB  1 
ATOM   15279 O  OG  . SER N  1 142 ? 21.999  116.382 65.615  1.00 17.09 ? 142  SER N OG  1 
ATOM   15280 N  N   . ARG N  1 143 ? 19.423  118.755 65.883  1.00 11.71 ? 143  ARG N N   1 
ATOM   15281 C  CA  . ARG N  1 143 ? 18.932  119.702 64.884  1.00 11.38 ? 143  ARG N CA  1 
ATOM   15282 C  C   . ARG N  1 143 ? 20.118  120.134 64.060  1.00 11.49 ? 143  ARG N C   1 
ATOM   15283 O  O   . ARG N  1 143 ? 20.956  120.920 64.513  1.00 11.52 ? 143  ARG N O   1 
ATOM   15284 C  CB  . ARG N  1 143 ? 18.310  120.921 65.546  1.00 11.08 ? 143  ARG N CB  1 
ATOM   15285 C  CG  . ARG N  1 143 ? 17.280  120.539 66.604  1.00 11.95 ? 143  ARG N CG  1 
ATOM   15286 C  CD  . ARG N  1 143 ? 16.757  121.702 67.502  1.00 13.00 ? 143  ARG N CD  1 
ATOM   15287 N  NE  . ARG N  1 143 ? 15.802  121.157 68.479  1.00 13.97 ? 143  ARG N NE  1 
ATOM   15288 C  CZ  . ARG N  1 143 ? 14.922  121.862 69.193  1.00 13.84 ? 143  ARG N CZ  1 
ATOM   15289 N  NH1 . ARG N  1 143 ? 14.873  123.167 69.100  1.00 13.22 ? 143  ARG N NH1 1 
ATOM   15290 N  NH2 . ARG N  1 143 ? 14.098  121.240 70.026  1.00 13.07 ? 143  ARG N NH2 1 
ATOM   15291 N  N   . LEU N  1 144 ? 20.164  119.632 62.840  1.00 11.35 ? 144  LEU N N   1 
ATOM   15292 C  CA  . LEU N  1 144 ? 21.297  119.874 61.979  1.00 10.81 ? 144  LEU N CA  1 
ATOM   15293 C  C   . LEU N  1 144 ? 21.279  121.249 61.333  1.00 11.32 ? 144  LEU N C   1 
ATOM   15294 O  O   . LEU N  1 144 ? 22.338  121.816 61.095  1.00 10.46 ? 144  LEU N O   1 
ATOM   15295 C  CB  . LEU N  1 144 ? 21.339  118.814 60.889  1.00 11.98 ? 144  LEU N CB  1 
ATOM   15296 C  CG  . LEU N  1 144 ? 21.408  117.382 61.403  1.00 10.88 ? 144  LEU N CG  1 
ATOM   15297 C  CD1 . LEU N  1 144 ? 21.485  116.527 60.185  1.00 13.36 ? 144  LEU N CD1 1 
ATOM   15298 C  CD2 . LEU N  1 144 ? 22.647  117.203 62.279  1.00 14.98 ? 144  LEU N CD2 1 
ATOM   15299 N  N   . ALA N  1 145 ? 20.090  121.750 60.997  1.00 10.49 ? 145  ALA N N   1 
ATOM   15300 C  CA  . ALA N  1 145 ? 19.977  123.071 60.410  1.00 10.89 ? 145  ALA N CA  1 
ATOM   15301 C  C   . ALA N  1 145 ? 18.579  123.603 60.629  1.00 11.06 ? 145  ALA N C   1 
ATOM   15302 O  O   . ALA N  1 145 ? 17.610  122.841 60.777  1.00 11.52 ? 145  ALA N O   1 
ATOM   15303 C  CB  . ALA N  1 145 ? 20.334  123.080 58.874  1.00 9.98  ? 145  ALA N CB  1 
ATOM   15304 N  N   . CYS N  1 146 ? 18.467  124.924 60.642  1.00 10.38 ? 146  CYS N N   1 
ATOM   15305 C  CA  . CYS N  1 146 ? 17.181  125.531 60.889  1.00 10.86 ? 146  CYS N CA  1 
ATOM   15306 C  C   . CYS N  1 146 ? 17.154  126.965 60.352  1.00 10.52 ? 146  CYS N C   1 
ATOM   15307 O  O   . CYS N  1 146 ? 18.196  127.555 60.024  1.00 9.18  ? 146  CYS N O   1 
ATOM   15308 C  CB  . CYS N  1 146 ? 16.843  125.550 62.387  1.00 11.50 ? 146  CYS N CB  1 
ATOM   15309 S  SG  . CYS N  1 146 ? 18.031  126.500 63.369  1.00 16.60 ? 146  CYS N SG  1 
ATOM   15310 N  N   . GLY N  1 147 ? 15.949  127.516 60.244  1.00 11.03 ? 147  GLY N N   1 
ATOM   15311 C  CA  . GLY N  1 147 ? 15.838  128.919 59.888  1.00 11.30 ? 147  GLY N CA  1 
ATOM   15312 C  C   . GLY N  1 147 ? 14.455  129.444 60.253  1.00 11.41 ? 147  GLY N C   1 
ATOM   15313 O  O   . GLY N  1 147 ? 13.530  128.663 60.500  1.00 10.30 ? 147  GLY N O   1 
ATOM   15314 N  N   . VAL N  1 148 ? 14.313  130.759 60.319  1.00 11.19 ? 148  VAL N N   1 
ATOM   15315 C  CA  . VAL N  1 148 ? 12.999  131.323 60.567  1.00 11.59 ? 148  VAL N CA  1 
ATOM   15316 C  C   . VAL N  1 148 ? 12.189  131.371 59.272  1.00 11.58 ? 148  VAL N C   1 
ATOM   15317 O  O   . VAL N  1 148 ? 12.712  131.731 58.208  1.00 11.96 ? 148  VAL N O   1 
ATOM   15318 C  CB  . VAL N  1 148 ? 13.120  132.736 61.118  1.00 11.87 ? 148  VAL N CB  1 
ATOM   15319 C  CG1 . VAL N  1 148 ? 11.741  133.252 61.581  1.00 11.45 ? 148  VAL N CG1 1 
ATOM   15320 C  CG2 . VAL N  1 148 ? 14.084  132.742 62.283  1.00 10.76 ? 148  VAL N CG2 1 
ATOM   15321 N  N   . ILE N  1 149 ? 10.902  131.036 59.369  1.00 11.26 ? 149  ILE N N   1 
ATOM   15322 C  CA  . ILE N  1 149 ? 10.018  131.043 58.209  1.00 11.68 ? 149  ILE N CA  1 
ATOM   15323 C  C   . ILE N  1 149 ? 9.577   132.466 57.959  1.00 11.35 ? 149  ILE N C   1 
ATOM   15324 O  O   . ILE N  1 149 ? 8.942   133.050 58.812  1.00 12.56 ? 149  ILE N O   1 
ATOM   15325 C  CB  . ILE N  1 149 ? 8.809   130.100 58.464  1.00 12.49 ? 149  ILE N CB  1 
ATOM   15326 C  CG1 . ILE N  1 149 ? 9.315   128.661 58.591  1.00 13.59 ? 149  ILE N CG1 1 
ATOM   15327 C  CG2 . ILE N  1 149 ? 7.808   130.228 57.352  1.00 11.63 ? 149  ILE N CG2 1 
ATOM   15328 C  CD1 . ILE N  1 149 ? 8.319   127.674 59.204  1.00 12.40 ? 149  ILE N CD1 1 
ATOM   15329 N  N   . GLY N  1 150 ? 9.942   133.031 56.811  1.00 10.51 ? 150  GLY N N   1 
ATOM   15330 C  CA  . GLY N  1 150 ? 9.737   134.456 56.559  1.00 11.62 ? 150  GLY N CA  1 
ATOM   15331 C  C   . GLY N  1 150 ? 8.753   134.699 55.426  1.00 11.15 ? 150  GLY N C   1 
ATOM   15332 O  O   . GLY N  1 150 ? 8.586   133.845 54.554  1.00 11.22 ? 150  GLY N O   1 
ATOM   15333 N  N   . ILE N  1 151 ? 8.122   135.865 55.410  1.00 11.66 ? 151  ILE N N   1 
ATOM   15334 C  CA  . ILE N  1 151 ? 7.152   136.181 54.382  1.00 12.32 ? 151  ILE N CA  1 
ATOM   15335 C  C   . ILE N  1 151 ? 7.909   136.390 53.093  1.00 12.69 ? 151  ILE N C   1 
ATOM   15336 O  O   . ILE N  1 151 ? 8.937   137.078 53.079  1.00 11.63 ? 151  ILE N O   1 
ATOM   15337 C  CB  . ILE N  1 151 ? 6.350   137.468 54.752  1.00 12.48 ? 151  ILE N CB  1 
ATOM   15338 C  CG1 . ILE N  1 151 ? 5.568   137.250 56.049  1.00 12.89 ? 151  ILE N CG1 1 
ATOM   15339 C  CG2 . ILE N  1 151 ? 5.395   137.818 53.640  1.00 12.95 ? 151  ILE N CG2 1 
ATOM   15340 C  CD1 . ILE N  1 151 ? 4.934   138.528 56.641  1.00 13.85 ? 151  ILE N CD1 1 
ATOM   15341 N  N   . ALA N  1 152 ? 7.422   135.778 52.014  1.00 12.71 ? 152  ALA N N   1 
ATOM   15342 C  CA  . ALA N  1 152 ? 8.080   135.904 50.720  1.00 14.67 ? 152  ALA N CA  1 
ATOM   15343 C  C   . ALA N  1 152 ? 7.222   136.671 49.734  1.00 16.23 ? 152  ALA N C   1 
ATOM   15344 O  O   . ALA N  1 152 ? 6.006   136.748 49.888  1.00 17.40 ? 152  ALA N O   1 
ATOM   15345 C  CB  . ALA N  1 152 ? 8.410   134.504 50.140  1.00 14.61 ? 152  ALA N CB  1 
ATOM   15346 N  N   . GLN N  1 153 ? 7.850   137.210 48.700  1.00 17.02 ? 153  GLN N N   1 
ATOM   15347 C  CA  . GLN N  1 153 ? 7.123   137.996 47.713  1.00 19.34 ? 153  GLN N CA  1 
ATOM   15348 C  C   . GLN N  1 153 ? 6.049   137.178 46.979  1.00 19.89 ? 153  GLN N C   1 
ATOM   15349 O  O   . GLN N  1 153 ? 6.290   136.041 46.616  1.00 18.87 ? 153  GLN N O   1 
ATOM   15350 C  CB  . GLN N  1 153 ? 8.107   138.596 46.719  1.00 19.25 ? 153  GLN N CB  1 
ATOM   15351 C  CG  . GLN N  1 153 ? 7.496   139.619 45.799  1.00 22.82 ? 153  GLN N CG  1 
ATOM   15352 C  CD  . GLN N  1 153 ? 8.544   140.489 45.139  1.00 25.68 ? 153  GLN N CD  1 
ATOM   15353 O  OE1 . GLN N  1 153 ? 9.489   139.975 44.530  1.00 27.43 ? 153  GLN N OE1 1 
ATOM   15354 N  NE2 . GLN N  1 153 ? 8.399   141.804 45.273  1.00 26.50 ? 153  GLN N NE2 1 
ATOM   15355 O  OXT . GLN N  1 153 ? 4.915   137.615 46.719  1.00 21.30 ? 153  GLN N OXT 1 
ATOM   15356 N  N   . ALA O  1 1   ? 28.020  121.718 96.512  1.00 34.93 ? 1    ALA O N   1 
ATOM   15357 C  CA  . ALA O  1 1   ? 29.198  122.234 95.740  1.00 34.57 ? 1    ALA O CA  1 
ATOM   15358 C  C   . ALA O  1 1   ? 29.735  121.213 94.732  1.00 34.04 ? 1    ALA O C   1 
ATOM   15359 O  O   . ALA O  1 1   ? 29.484  120.012 94.859  1.00 34.33 ? 1    ALA O O   1 
ATOM   15360 C  CB  . ALA O  1 1   ? 30.301  122.672 96.688  1.00 34.63 ? 1    ALA O CB  1 
ATOM   15361 N  N   . THR O  1 2   ? 30.467  121.697 93.730  1.00 33.09 ? 2    THR O N   1 
ATOM   15362 C  CA  . THR O  1 2   ? 31.029  120.806 92.714  1.00 32.38 ? 2    THR O CA  1 
ATOM   15363 C  C   . THR O  1 2   ? 32.529  120.496 92.892  1.00 30.80 ? 2    THR O C   1 
ATOM   15364 O  O   . THR O  1 2   ? 32.942  119.370 92.656  1.00 30.22 ? 2    THR O O   1 
ATOM   15365 C  CB  . THR O  1 2   ? 30.684  121.280 91.271  1.00 32.77 ? 2    THR O CB  1 
ATOM   15366 O  OG1 . THR O  1 2   ? 31.130  120.304 90.326  1.00 34.27 ? 2    THR O OG1 1 
ATOM   15367 C  CG2 . THR O  1 2   ? 31.468  122.534 90.885  1.00 34.08 ? 2    THR O CG2 1 
ATOM   15368 N  N   . LYS O  1 3   ? 33.336  121.488 93.280  1.00 29.29 ? 3    LYS O N   1 
ATOM   15369 C  CA  . LYS O  1 3   ? 34.752  121.247 93.584  1.00 27.58 ? 3    LYS O CA  1 
ATOM   15370 C  C   . LYS O  1 3   ? 35.110  121.783 94.966  1.00 26.19 ? 3    LYS O C   1 
ATOM   15371 O  O   . LYS O  1 3   ? 34.543  122.783 95.431  1.00 24.83 ? 3    LYS O O   1 
ATOM   15372 C  CB  . LYS O  1 3   ? 35.697  121.892 92.558  1.00 28.25 ? 3    LYS O CB  1 
ATOM   15373 C  CG  . LYS O  1 3   ? 35.719  121.267 91.160  1.00 30.49 ? 3    LYS O CG  1 
ATOM   15374 C  CD  . LYS O  1 3   ? 36.737  121.982 90.262  1.00 34.31 ? 3    LYS O CD  1 
ATOM   15375 C  CE  . LYS O  1 3   ? 36.227  122.133 88.823  1.00 35.28 ? 3    LYS O CE  1 
ATOM   15376 N  NZ  . LYS O  1 3   ? 35.868  120.818 88.199  1.00 37.63 ? 3    LYS O NZ  1 
ATOM   15377 N  N   . ALA O  1 4   ? 36.066  121.120 95.608  1.00 23.96 ? 4    ALA O N   1 
ATOM   15378 C  CA  . ALA O  1 4   ? 36.586  121.554 96.896  1.00 22.47 ? 4    ALA O CA  1 
ATOM   15379 C  C   . ALA O  1 4   ? 38.088  121.361 96.908  1.00 21.37 ? 4    ALA O C   1 
ATOM   15380 O  O   . ALA O  1 4   ? 38.661  120.667 96.045  1.00 19.24 ? 4    ALA O O   1 
ATOM   15381 C  CB  . ALA O  1 4   ? 35.963  120.762 98.037  1.00 23.26 ? 4    ALA O CB  1 
ATOM   15382 N  N   . VAL O  1 5   ? 38.734  121.971 97.896  1.00 20.16 ? 5    VAL O N   1 
ATOM   15383 C  CA  . VAL O  1 5   ? 40.160  121.789 98.058  1.00 19.98 ? 5    VAL O CA  1 
ATOM   15384 C  C   . VAL O  1 5   ? 40.506  121.804 99.532  1.00 19.87 ? 5    VAL O C   1 
ATOM   15385 O  O   . VAL O  1 5   ? 39.756  122.335 100.360 1.00 19.98 ? 5    VAL O O   1 
ATOM   15386 C  CB  . VAL O  1 5   ? 40.938  122.891 97.334  1.00 20.25 ? 5    VAL O CB  1 
ATOM   15387 C  CG1 . VAL O  1 5   ? 40.614  124.261 97.943  1.00 20.34 ? 5    VAL O CG1 1 
ATOM   15388 C  CG2 . VAL O  1 5   ? 42.433  122.606 97.394  1.00 21.60 ? 5    VAL O CG2 1 
ATOM   15389 N  N   . CYS O  1 6   ? 41.652  121.234 99.868  1.00 18.76 ? 6    CYS O N   1 
ATOM   15390 C  CA  . CYS O  1 6   ? 42.087  121.236 101.251 1.00 17.76 ? 6    CYS O CA  1 
ATOM   15391 C  C   . CYS O  1 6   ? 43.608  121.298 101.342 1.00 17.88 ? 6    CYS O C   1 
ATOM   15392 O  O   . CYS O  1 6   ? 44.313  120.513 100.702 1.00 17.73 ? 6    CYS O O   1 
ATOM   15393 C  CB  . CYS O  1 6   ? 41.576  119.987 101.954 1.00 18.55 ? 6    CYS O CB  1 
ATOM   15394 S  SG  . CYS O  1 6   ? 42.141  119.836 103.662 1.00 18.37 ? 6    CYS O SG  1 
ATOM   15395 N  N   . VAL O  1 7   ? 44.099  122.258 102.123 1.00 16.50 ? 7    VAL O N   1 
ATOM   15396 C  CA  . VAL O  1 7   ? 45.512  122.388 102.392 1.00 16.21 ? 7    VAL O CA  1 
ATOM   15397 C  C   . VAL O  1 7   ? 45.824  121.750 103.722 1.00 15.72 ? 7    VAL O C   1 
ATOM   15398 O  O   . VAL O  1 7   ? 45.362  122.206 104.753 1.00 16.17 ? 7    VAL O O   1 
ATOM   15399 C  CB  . VAL O  1 7   ? 45.945  123.866 102.410 1.00 15.64 ? 7    VAL O CB  1 
ATOM   15400 C  CG1 . VAL O  1 7   ? 47.459  124.008 102.743 1.00 17.23 ? 7    VAL O CG1 1 
ATOM   15401 C  CG2 . VAL O  1 7   ? 45.683  124.451 101.037 1.00 15.79 ? 7    VAL O CG2 1 
ATOM   15402 N  N   . LEU O  1 8   ? 46.633  120.692 103.683 1.00 16.39 ? 8    LEU O N   1 
ATOM   15403 C  CA  . LEU O  1 8   ? 47.009  119.929 104.865 1.00 16.89 ? 8    LEU O CA  1 
ATOM   15404 C  C   . LEU O  1 8   ? 48.291  120.477 105.457 1.00 17.32 ? 8    LEU O C   1 
ATOM   15405 O  O   . LEU O  1 8   ? 49.287  120.623 104.746 1.00 17.63 ? 8    LEU O O   1 
ATOM   15406 C  CB  . LEU O  1 8   ? 47.296  118.468 104.438 1.00 16.85 ? 8    LEU O CB  1 
ATOM   15407 C  CG  . LEU O  1 8   ? 46.312  117.304 104.580 1.00 22.82 ? 8    LEU O CG  1 
ATOM   15408 C  CD1 . LEU O  1 8   ? 44.896  117.635 104.855 1.00 20.73 ? 8    LEU O CD1 1 
ATOM   15409 C  CD2 . LEU O  1 8   ? 46.478  116.250 103.442 1.00 22.72 ? 8    LEU O CD2 1 
ATOM   15410 N  N   . LYS O  1 9   ? 48.276  120.789 106.743 1.00 17.03 ? 9    LYS O N   1 
ATOM   15411 C  CA  . LYS O  1 9   ? 49.473  121.300 107.419 1.00 18.20 ? 9    LYS O CA  1 
ATOM   15412 C  C   . LYS O  1 9   ? 49.466  120.797 108.855 1.00 17.57 ? 9    LYS O C   1 
ATOM   15413 O  O   . LYS O  1 9   ? 48.415  120.469 109.383 1.00 17.14 ? 9    LYS O O   1 
ATOM   15414 C  CB  . LYS O  1 9   ? 49.501  122.846 107.381 1.00 19.16 ? 9    LYS O CB  1 
ATOM   15415 C  CG  . LYS O  1 9   ? 49.928  123.353 105.989 1.00 23.12 ? 9    LYS O CG  1 
ATOM   15416 C  CD  . LYS O  1 9   ? 49.698  124.847 105.735 1.00 30.61 ? 9    LYS O CD  1 
ATOM   15417 C  CE  . LYS O  1 9   ? 50.496  125.286 104.493 1.00 33.43 ? 9    LYS O CE  1 
ATOM   15418 N  NZ  . LYS O  1 9   ? 51.035  124.066 103.723 1.00 36.34 ? 9    LYS O NZ  1 
ATOM   15419 N  N   . GLY O  1 10  ? 50.627  120.766 109.498 1.00 17.57 ? 10   GLY O N   1 
ATOM   15420 C  CA  . GLY O  1 10  ? 50.718  120.252 110.852 1.00 19.57 ? 10   GLY O CA  1 
ATOM   15421 C  C   . GLY O  1 10  ? 51.955  120.815 111.532 1.00 21.38 ? 10   GLY O C   1 
ATOM   15422 O  O   . GLY O  1 10  ? 52.537  121.803 111.046 1.00 21.81 ? 10   GLY O O   1 
ATOM   15423 N  N   . ASP O  1 11  ? 52.346  120.231 112.657 1.00 22.80 ? 11   ASP O N   1 
ATOM   15424 C  CA  . ASP O  1 11  ? 53.544  120.721 113.368 1.00 24.19 ? 11   ASP O CA  1 
ATOM   15425 C  C   . ASP O  1 11  ? 54.856  120.300 112.669 1.00 24.29 ? 11   ASP O C   1 
ATOM   15426 O  O   . ASP O  1 11  ? 55.889  120.965 112.808 1.00 24.49 ? 11   ASP O O   1 
ATOM   15427 C  CB  . ASP O  1 11  ? 53.571  120.239 114.830 1.00 25.12 ? 11   ASP O CB  1 
ATOM   15428 C  CG  . ASP O  1 11  ? 52.313  120.636 115.643 1.00 27.65 ? 11   ASP O CG  1 
ATOM   15429 O  OD1 . ASP O  1 11  ? 51.857  121.793 115.566 1.00 29.87 ? 11   ASP O OD1 1 
ATOM   15430 O  OD2 . ASP O  1 11  ? 51.725  119.843 116.416 1.00 32.30 ? 11   ASP O OD2 1 
ATOM   15431 N  N   . GLY O  1 12  ? 54.810  119.210 111.899 1.00 23.99 ? 12   GLY O N   1 
ATOM   15432 C  CA  . GLY O  1 12  ? 56.033  118.660 111.325 1.00 23.89 ? 12   GLY O CA  1 
ATOM   15433 C  C   . GLY O  1 12  ? 56.224  118.903 109.844 1.00 23.23 ? 12   GLY O C   1 
ATOM   15434 O  O   . GLY O  1 12  ? 55.779  119.913 109.306 1.00 22.93 ? 12   GLY O O   1 
ATOM   15435 N  N   . PRO O  1 13  ? 56.875  117.953 109.186 1.00 22.66 ? 13   PRO O N   1 
ATOM   15436 C  CA  . PRO O  1 13  ? 57.174  118.055 107.753 1.00 21.98 ? 13   PRO O CA  1 
ATOM   15437 C  C   . PRO O  1 13  ? 56.036  117.661 106.845 1.00 20.57 ? 13   PRO O C   1 
ATOM   15438 O  O   . PRO O  1 13  ? 56.193  117.784 105.644 1.00 20.01 ? 13   PRO O O   1 
ATOM   15439 C  CB  . PRO O  1 13  ? 58.293  117.020 107.538 1.00 22.67 ? 13   PRO O CB  1 
ATOM   15440 C  CG  . PRO O  1 13  ? 58.363  116.182 108.777 1.00 23.00 ? 13   PRO O CG  1 
ATOM   15441 C  CD  . PRO O  1 13  ? 57.430  116.735 109.801 1.00 22.91 ? 13   PRO O CD  1 
ATOM   15442 N  N   . VAL O  1 14  ? 54.927  117.185 107.379 1.00 19.52 ? 14   VAL O N   1 
ATOM   15443 C  CA  . VAL O  1 14  ? 53.856  116.713 106.514 1.00 18.55 ? 14   VAL O CA  1 
ATOM   15444 C  C   . VAL O  1 14  ? 53.005  117.832 105.946 1.00 19.43 ? 14   VAL O C   1 
ATOM   15445 O  O   . VAL O  1 14  ? 52.449  118.660 106.693 1.00 20.30 ? 14   VAL O O   1 
ATOM   15446 C  CB  . VAL O  1 14  ? 52.987  115.664 107.215 1.00 18.58 ? 14   VAL O CB  1 
ATOM   15447 C  CG1 . VAL O  1 14  ? 51.808  115.271 106.338 1.00 16.53 ? 14   VAL O CG1 1 
ATOM   15448 C  CG2 . VAL O  1 14  ? 53.821  114.425 107.540 1.00 17.25 ? 14   VAL O CG2 1 
ATOM   15449 N  N   . GLN O  1 15  ? 52.928  117.890 104.624 1.00 19.61 ? 15   GLN O N   1 
ATOM   15450 C  CA  . GLN O  1 15  ? 52.059  118.877 103.988 1.00 20.41 ? 15   GLN O CA  1 
ATOM   15451 C  C   . GLN O  1 15  ? 51.586  118.427 102.607 1.00 20.18 ? 15   GLN O C   1 
ATOM   15452 O  O   . GLN O  1 15  ? 52.234  117.616 101.941 1.00 18.89 ? 15   GLN O O   1 
ATOM   15453 C  CB  . GLN O  1 15  ? 52.695  120.273 103.973 1.00 21.93 ? 15   GLN O CB  1 
ATOM   15454 C  CG  . GLN O  1 15  ? 54.081  120.322 103.457 1.00 25.38 ? 15   GLN O CG  1 
ATOM   15455 C  CD  . GLN O  1 15  ? 54.583  121.735 103.267 1.00 29.01 ? 15   GLN O CD  1 
ATOM   15456 O  OE1 . GLN O  1 15  ? 55.718  121.925 102.881 1.00 32.69 ? 15   GLN O OE1 1 
ATOM   15457 N  NE2 . GLN O  1 15  ? 53.736  122.728 103.541 1.00 34.19 ? 15   GLN O NE2 1 
ATOM   15458 N  N   . GLY O  1 16  ? 50.439  118.943 102.191 1.00 20.04 ? 16   GLY O N   1 
ATOM   15459 C  CA  . GLY O  1 16  ? 49.868  118.556 100.915 1.00 19.49 ? 16   GLY O CA  1 
ATOM   15460 C  C   . GLY O  1 16  ? 48.642  119.353 100.532 1.00 20.31 ? 16   GLY O C   1 
ATOM   15461 O  O   . GLY O  1 16  ? 48.154  120.206 101.270 1.00 19.07 ? 16   GLY O O   1 
ATOM   15462 N  N   . ILE O  1 17  ? 48.159  119.081 99.337  1.00 20.34 ? 17   ILE O N   1 
ATOM   15463 C  CA  . ILE O  1 17  ? 46.972  119.722 98.847  1.00 20.17 ? 17   ILE O CA  1 
ATOM   15464 C  C   . ILE O  1 17  ? 46.129  118.598 98.291  1.00 20.34 ? 17   ILE O C   1 
ATOM   15465 O  O   . ILE O  1 17  ? 46.620  117.728 97.535  1.00 20.08 ? 17   ILE O O   1 
ATOM   15466 C  CB  . ILE O  1 17  ? 47.342  120.702 97.766  1.00 20.43 ? 17   ILE O CB  1 
ATOM   15467 C  CG1 . ILE O  1 17  ? 48.159  121.844 98.364  1.00 22.30 ? 17   ILE O CG1 1 
ATOM   15468 C  CG2 . ILE O  1 17  ? 46.089  121.208 97.044  1.00 22.08 ? 17   ILE O CG2 1 
ATOM   15469 C  CD1 . ILE O  1 17  ? 48.788  122.758 97.296  1.00 26.08 ? 17   ILE O CD1 1 
ATOM   15470 N  N   . ILE O  1 18  ? 44.871  118.579 98.695  1.00 19.96 ? 18   ILE O N   1 
ATOM   15471 C  CA  . ILE O  1 18  ? 43.968  117.552 98.258  1.00 19.82 ? 18   ILE O CA  1 
ATOM   15472 C  C   . ILE O  1 18  ? 42.789  118.224 97.608  1.00 20.60 ? 18   ILE O C   1 
ATOM   15473 O  O   . ILE O  1 18  ? 42.221  119.186 98.148  1.00 19.07 ? 18   ILE O O   1 
ATOM   15474 C  CB  . ILE O  1 18  ? 43.505  116.722 99.442  1.00 19.78 ? 18   ILE O CB  1 
ATOM   15475 C  CG1 . ILE O  1 18  ? 44.717  116.041 100.063 1.00 20.47 ? 18   ILE O CG1 1 
ATOM   15476 C  CG2 . ILE O  1 18  ? 42.494  115.666 98.986  1.00 19.35 ? 18   ILE O CG2 1 
ATOM   15477 C  CD1 . ILE O  1 18  ? 45.300  114.933 99.131  1.00 20.28 ? 18   ILE O CD1 1 
ATOM   15478 N  N   . ASN O  1 19  ? 42.441  117.716 96.434  1.00 21.40 ? 19   ASN O N   1 
ATOM   15479 C  CA  . ASN O  1 19  ? 41.351  118.277 95.666  1.00 22.52 ? 19   ASN O CA  1 
ATOM   15480 C  C   . ASN O  1 19  ? 40.165  117.323 95.607  1.00 22.39 ? 19   ASN O C   1 
ATOM   15481 O  O   . ASN O  1 19  ? 40.341  116.110 95.674  1.00 22.61 ? 19   ASN O O   1 
ATOM   15482 C  CB  . ASN O  1 19  ? 41.855  118.723 94.288  1.00 23.14 ? 19   ASN O CB  1 
ATOM   15483 C  CG  . ASN O  1 19  ? 42.374  120.173 94.301  1.00 25.70 ? 19   ASN O CG  1 
ATOM   15484 O  OD1 . ASN O  1 19  ? 43.541  120.436 94.041  1.00 28.71 ? 19   ASN O OD1 1 
ATOM   15485 N  ND2 . ASN O  1 19  ? 41.490  121.110 94.608  1.00 29.31 ? 19   ASN O ND2 1 
ATOM   15486 N  N   . PHE O  1 20  ? 38.958  117.885 95.529  1.00 22.81 ? 20   PHE O N   1 
ATOM   15487 C  CA  . PHE O  1 20  ? 37.706  117.126 95.452  1.00 23.41 ? 20   PHE O CA  1 
ATOM   15488 C  C   . PHE O  1 20  ? 36.881  117.637 94.273  1.00 24.47 ? 20   PHE O C   1 
ATOM   15489 O  O   . PHE O  1 20  ? 36.857  118.835 94.012  1.00 23.43 ? 20   PHE O O   1 
ATOM   15490 C  CB  . PHE O  1 20  ? 36.865  117.305 96.725  1.00 23.28 ? 20   PHE O CB  1 
ATOM   15491 C  CG  . PHE O  1 20  ? 37.562  116.881 98.009  1.00 23.05 ? 20   PHE O CG  1 
ATOM   15492 C  CD1 . PHE O  1 20  ? 38.416  117.748 98.676  1.00 25.23 ? 20   PHE O CD1 1 
ATOM   15493 C  CD2 . PHE O  1 20  ? 37.302  115.651 98.573  1.00 22.97 ? 20   PHE O CD2 1 
ATOM   15494 C  CE1 . PHE O  1 20  ? 39.031  117.367 99.859  1.00 23.03 ? 20   PHE O CE1 1 
ATOM   15495 C  CE2 . PHE O  1 20  ? 37.912  115.257 99.747  1.00 23.82 ? 20   PHE O CE2 1 
ATOM   15496 C  CZ  . PHE O  1 20  ? 38.790  116.136 100.399 1.00 21.87 ? 20   PHE O CZ  1 
ATOM   15497 N  N   . GLU O  1 21  ? 36.198  116.713 93.594  1.00 25.65 ? 21   GLU O N   1 
ATOM   15498 C  CA  . GLU O  1 21  ? 35.314  117.029 92.481  1.00 27.84 ? 21   GLU O CA  1 
ATOM   15499 C  C   . GLU O  1 21  ? 34.125  116.082 92.485  1.00 28.26 ? 21   GLU O C   1 
ATOM   15500 O  O   . GLU O  1 21  ? 34.300  114.880 92.615  1.00 28.39 ? 21   GLU O O   1 
ATOM   15501 C  CB  . GLU O  1 21  ? 36.041  116.829 91.170  1.00 27.97 ? 21   GLU O CB  1 
ATOM   15502 C  CG  . GLU O  1 21  ? 36.787  118.033 90.676  1.00 31.26 ? 21   GLU O CG  1 
ATOM   15503 C  CD  . GLU O  1 21  ? 37.054  117.937 89.195  1.00 36.12 ? 21   GLU O CD  1 
ATOM   15504 O  OE1 . GLU O  1 21  ? 36.156  118.293 88.397  1.00 37.63 ? 21   GLU O OE1 1 
ATOM   15505 O  OE2 . GLU O  1 21  ? 38.155  117.469 88.834  1.00 40.07 ? 21   GLU O OE2 1 
ATOM   15506 N  N   . GLN O  1 22  ? 32.920  116.623 92.317  1.00 29.52 ? 22   GLN O N   1 
ATOM   15507 C  CA  . GLN O  1 22  ? 31.712  115.802 92.252  1.00 30.49 ? 22   GLN O CA  1 
ATOM   15508 C  C   . GLN O  1 22  ? 30.869  116.301 91.074  1.00 31.84 ? 22   GLN O C   1 
ATOM   15509 O  O   . GLN O  1 22  ? 30.149  117.302 91.181  1.00 31.35 ? 22   GLN O O   1 
ATOM   15510 C  CB  . GLN O  1 22  ? 30.926  115.865 93.562  1.00 30.11 ? 22   GLN O CB  1 
ATOM   15511 C  CG  . GLN O  1 22  ? 29.718  114.942 93.617  1.00 30.27 ? 22   GLN O CG  1 
ATOM   15512 C  CD  . GLN O  1 22  ? 29.016  114.987 94.964  1.00 30.29 ? 22   GLN O CD  1 
ATOM   15513 O  OE1 . GLN O  1 22  ? 28.794  116.063 95.518  1.00 30.51 ? 22   GLN O OE1 1 
ATOM   15514 N  NE2 . GLN O  1 22  ? 28.679  113.826 95.495  1.00 29.54 ? 22   GLN O NE2 1 
ATOM   15515 N  N   . LYS O  1 23  ? 30.983  115.601 89.948  1.00 33.29 ? 23   LYS O N   1 
ATOM   15516 C  CA  . LYS O  1 23  ? 30.315  116.014 88.720  1.00 35.35 ? 23   LYS O CA  1 
ATOM   15517 C  C   . LYS O  1 23  ? 28.802  115.904 88.825  1.00 35.87 ? 23   LYS O C   1 
ATOM   15518 O  O   . LYS O  1 23  ? 28.078  116.596 88.114  1.00 36.06 ? 23   LYS O O   1 
ATOM   15519 C  CB  . LYS O  1 23  ? 30.856  115.227 87.517  1.00 35.76 ? 23   LYS O CB  1 
ATOM   15520 C  CG  . LYS O  1 23  ? 32.154  115.811 86.941  1.00 38.13 ? 23   LYS O CG  1 
ATOM   15521 C  CD  . LYS O  1 23  ? 32.951  114.780 86.131  1.00 41.74 ? 23   LYS O CD  1 
ATOM   15522 C  CE  . LYS O  1 23  ? 34.108  115.440 85.365  1.00 43.94 ? 23   LYS O CE  1 
ATOM   15523 N  NZ  . LYS O  1 23  ? 35.010  116.265 86.242  1.00 45.88 ? 23   LYS O NZ  1 
ATOM   15524 N  N   . GLU O  1 24  ? 28.328  115.054 89.731  1.00 36.62 ? 24   GLU O N   1 
ATOM   15525 C  CA  . GLU O  1 24  ? 26.892  114.872 89.904  1.00 37.72 ? 24   GLU O CA  1 
ATOM   15526 C  C   . GLU O  1 24  ? 26.440  114.974 91.354  1.00 37.59 ? 24   GLU O C   1 
ATOM   15527 O  O   . GLU O  1 24  ? 26.987  114.315 92.232  1.00 37.58 ? 24   GLU O O   1 
ATOM   15528 C  CB  . GLU O  1 24  ? 26.454  113.535 89.318  1.00 37.97 ? 24   GLU O CB  1 
ATOM   15529 C  CG  . GLU O  1 24  ? 26.454  113.503 87.803  1.00 40.34 ? 24   GLU O CG  1 
ATOM   15530 C  CD  . GLU O  1 24  ? 25.626  112.356 87.282  1.00 43.10 ? 24   GLU O CD  1 
ATOM   15531 O  OE1 . GLU O  1 24  ? 24.702  111.938 88.009  1.00 44.83 ? 24   GLU O OE1 1 
ATOM   15532 O  OE2 . GLU O  1 24  ? 25.898  111.869 86.163  1.00 44.90 ? 24   GLU O OE2 1 
ATOM   15533 N  N   . SER O  1 25  ? 25.400  115.771 91.575  1.00 37.65 ? 25   SER O N   1 
ATOM   15534 C  CA  . SER O  1 25  ? 24.873  116.051 92.911  1.00 37.79 ? 25   SER O CA  1 
ATOM   15535 C  C   . SER O  1 25  ? 24.609  114.837 93.801  1.00 37.72 ? 25   SER O C   1 
ATOM   15536 O  O   . SER O  1 25  ? 23.664  114.834 94.591  1.00 37.91 ? 25   SER O O   1 
ATOM   15537 C  CB  . SER O  1 25  ? 23.604  116.907 92.806  1.00 37.93 ? 25   SER O CB  1 
ATOM   15538 O  OG  . SER O  1 25  ? 22.703  116.375 91.851  1.00 38.21 ? 25   SER O OG  1 
ATOM   15539 N  N   . ASN O  1 26  ? 25.454  113.818 93.696  1.00 37.22 ? 26   ASN O N   1 
ATOM   15540 C  CA  . ASN O  1 26  ? 25.259  112.612 94.483  1.00 36.94 ? 26   ASN O CA  1 
ATOM   15541 C  C   . ASN O  1 26  ? 26.171  111.485 94.018  1.00 36.12 ? 26   ASN O C   1 
ATOM   15542 O  O   . ASN O  1 26  ? 26.216  110.411 94.624  1.00 36.01 ? 26   ASN O O   1 
ATOM   15543 C  CB  . ASN O  1 26  ? 23.814  112.157 94.325  1.00 37.44 ? 26   ASN O CB  1 
ATOM   15544 C  CG  . ASN O  1 26  ? 23.406  112.056 92.868  1.00 38.49 ? 26   ASN O CG  1 
ATOM   15545 O  OD1 . ASN O  1 26  ? 24.031  112.673 92.000  1.00 39.49 ? 26   ASN O OD1 1 
ATOM   15546 N  ND2 . ASN O  1 26  ? 22.368  111.277 92.590  1.00 39.56 ? 26   ASN O ND2 1 
ATOM   15547 N  N   . GLY O  1 27  ? 26.890  111.733 92.930  1.00 35.10 ? 27   GLY O N   1 
ATOM   15548 C  CA  . GLY O  1 27  ? 27.733  110.715 92.337  1.00 33.62 ? 27   GLY O CA  1 
ATOM   15549 C  C   . GLY O  1 27  ? 29.089  110.634 92.991  1.00 32.34 ? 27   GLY O C   1 
ATOM   15550 O  O   . GLY O  1 27  ? 29.332  111.267 94.020  1.00 32.69 ? 27   GLY O O   1 
ATOM   15551 N  N   . PRO O  1 28  ? 29.976  109.851 92.390  1.00 31.19 ? 28   PRO O N   1 
ATOM   15552 C  CA  . PRO O  1 28  ? 31.329  109.696 92.914  1.00 30.19 ? 28   PRO O CA  1 
ATOM   15553 C  C   . PRO O  1 28  ? 32.020  111.056 93.049  1.00 29.05 ? 28   PRO O C   1 
ATOM   15554 O  O   . PRO O  1 28  ? 31.717  112.023 92.324  1.00 28.71 ? 28   PRO O O   1 
ATOM   15555 C  CB  . PRO O  1 28  ? 32.027  108.842 91.855  1.00 30.50 ? 28   PRO O CB  1 
ATOM   15556 C  CG  . PRO O  1 28  ? 30.930  108.160 91.106  1.00 31.10 ? 28   PRO O CG  1 
ATOM   15557 C  CD  . PRO O  1 28  ? 29.747  109.061 91.168  1.00 31.07 ? 28   PRO O CD  1 
ATOM   15558 N  N   . VAL O  1 29  ? 32.934  111.115 94.006  1.00 27.53 ? 29   VAL O N   1 
ATOM   15559 C  CA  . VAL O  1 29  ? 33.753  112.299 94.270  1.00 26.52 ? 29   VAL O CA  1 
ATOM   15560 C  C   . VAL O  1 29  ? 35.200  111.893 94.038  1.00 25.96 ? 29   VAL O C   1 
ATOM   15561 O  O   . VAL O  1 29  ? 35.687  110.952 94.672  1.00 24.95 ? 29   VAL O O   1 
ATOM   15562 C  CB  . VAL O  1 29  ? 33.622  112.759 95.732  1.00 26.32 ? 29   VAL O CB  1 
ATOM   15563 C  CG1 . VAL O  1 29  ? 34.617  113.886 96.039  1.00 26.75 ? 29   VAL O CG1 1 
ATOM   15564 C  CG2 . VAL O  1 29  ? 32.198  113.180 96.055  1.00 25.31 ? 29   VAL O CG2 1 
ATOM   15565 N  N   . LYS O  1 30  ? 35.869  112.567 93.105  1.00 25.30 ? 30   LYS O N   1 
ATOM   15566 C  CA  . LYS O  1 30  ? 37.260  112.242 92.816  1.00 25.34 ? 30   LYS O CA  1 
ATOM   15567 C  C   . LYS O  1 30  ? 38.126  113.017 93.784  1.00 24.78 ? 30   LYS O C   1 
ATOM   15568 O  O   . LYS O  1 30  ? 37.991  114.232 93.936  1.00 24.41 ? 30   LYS O O   1 
ATOM   15569 C  CB  . LYS O  1 30  ? 37.657  112.601 91.384  1.00 25.79 ? 30   LYS O CB  1 
ATOM   15570 C  CG  . LYS O  1 30  ? 36.842  111.945 90.286  1.00 27.58 ? 30   LYS O CG  1 
ATOM   15571 C  CD  . LYS O  1 30  ? 37.027  112.740 88.981  1.00 32.23 ? 30   LYS O CD  1 
ATOM   15572 C  CE  . LYS O  1 30  ? 35.971  112.405 87.929  1.00 34.82 ? 30   LYS O CE  1 
ATOM   15573 N  NZ  . LYS O  1 30  ? 35.959  113.416 86.808  1.00 35.38 ? 30   LYS O NZ  1 
ATOM   15574 N  N   . VAL O  1 31  ? 39.016  112.301 94.449  1.00 23.81 ? 31   VAL O N   1 
ATOM   15575 C  CA  . VAL O  1 31  ? 39.890  112.920 95.424  1.00 23.66 ? 31   VAL O CA  1 
ATOM   15576 C  C   . VAL O  1 31  ? 41.291  112.697 94.903  1.00 23.90 ? 31   VAL O C   1 
ATOM   15577 O  O   . VAL O  1 31  ? 41.686  111.556 94.616  1.00 23.39 ? 31   VAL O O   1 
ATOM   15578 C  CB  . VAL O  1 31  ? 39.741  112.233 96.791  1.00 23.65 ? 31   VAL O CB  1 
ATOM   15579 C  CG1 . VAL O  1 31  ? 40.679  112.864 97.802  1.00 22.27 ? 31   VAL O CG1 1 
ATOM   15580 C  CG2 . VAL O  1 31  ? 38.282  112.301 97.253  1.00 23.30 ? 31   VAL O CG2 1 
ATOM   15581 N  N   . TRP O  1 32  ? 42.034  113.769 94.709  1.00 23.44 ? 32   TRP O N   1 
ATOM   15582 C  CA  . TRP O  1 32  ? 43.385  113.582 94.231  1.00 23.69 ? 32   TRP O CA  1 
ATOM   15583 C  C   . TRP O  1 32  ? 44.268  114.715 94.660  1.00 23.18 ? 32   TRP O C   1 
ATOM   15584 O  O   . TRP O  1 32  ? 43.813  115.836 94.912  1.00 22.01 ? 32   TRP O O   1 
ATOM   15585 C  CB  . TRP O  1 32  ? 43.411  113.508 92.724  1.00 23.99 ? 32   TRP O CB  1 
ATOM   15586 C  CG  . TRP O  1 32  ? 43.244  114.829 92.082  1.00 25.23 ? 32   TRP O CG  1 
ATOM   15587 C  CD1 . TRP O  1 32  ? 44.221  115.600 91.525  1.00 25.65 ? 32   TRP O CD1 1 
ATOM   15588 C  CD2 . TRP O  1 32  ? 42.020  115.528 91.887  1.00 27.07 ? 32   TRP O CD2 1 
ATOM   15589 N  NE1 . TRP O  1 32  ? 43.676  116.745 90.990  1.00 28.48 ? 32   TRP O NE1 1 
ATOM   15590 C  CE2 . TRP O  1 32  ? 42.322  116.724 91.202  1.00 28.15 ? 32   TRP O CE2 1 
ATOM   15591 C  CE3 . TRP O  1 32  ? 40.689  115.267 92.224  1.00 27.78 ? 32   TRP O CE3 1 
ATOM   15592 C  CZ2 . TRP O  1 32  ? 41.348  117.648 90.850  1.00 29.86 ? 32   TRP O CZ2 1 
ATOM   15593 C  CZ3 . TRP O  1 32  ? 39.723  116.178 91.874  1.00 28.24 ? 32   TRP O CZ3 1 
ATOM   15594 C  CH2 . TRP O  1 32  ? 40.053  117.359 91.196  1.00 30.07 ? 32   TRP O CH2 1 
ATOM   15595 N  N   . GLY O  1 33  ? 45.550  114.413 94.732  1.00 23.01 ? 33   GLY O N   1 
ATOM   15596 C  CA  . GLY O  1 33  ? 46.504  115.408 95.152  1.00 22.54 ? 33   GLY O CA  1 
ATOM   15597 C  C   . GLY O  1 33  ? 47.765  114.723 95.585  1.00 22.15 ? 33   GLY O C   1 
ATOM   15598 O  O   . GLY O  1 33  ? 48.004  113.571 95.227  1.00 22.08 ? 33   GLY O O   1 
ATOM   15599 N  N   . SER O  1 34  ? 48.564  115.430 96.372  1.00 21.69 ? 34   SER O N   1 
ATOM   15600 C  CA  . SER O  1 34  ? 49.846  114.906 96.798  1.00 21.99 ? 34   SER O CA  1 
ATOM   15601 C  C   . SER O  1 34  ? 50.087  115.311 98.248  1.00 21.12 ? 34   SER O C   1 
ATOM   15602 O  O   . SER O  1 34  ? 49.693  116.398 98.666  1.00 20.30 ? 34   SER O O   1 
ATOM   15603 C  CB  . SER O  1 34  ? 50.959  115.446 95.881  1.00 22.55 ? 34   SER O CB  1 
ATOM   15604 O  OG  . SER O  1 34  ? 52.229  114.829 96.131  1.00 24.80 ? 34   SER O OG  1 
ATOM   15605 N  N   . ILE O  1 35  ? 50.658  114.402 99.027  1.00 20.09 ? 35   ILE O N   1 
ATOM   15606 C  CA  . ILE O  1 35  ? 51.054  114.699 100.404 1.00 19.39 ? 35   ILE O CA  1 
ATOM   15607 C  C   . ILE O  1 35  ? 52.518  114.348 100.527 1.00 19.27 ? 35   ILE O C   1 
ATOM   15608 O  O   . ILE O  1 35  ? 52.940  113.300 100.046 1.00 19.21 ? 35   ILE O O   1 
ATOM   15609 C  CB  . ILE O  1 35  ? 50.245  113.894 101.440 1.00 19.39 ? 35   ILE O CB  1 
ATOM   15610 C  CG1 . ILE O  1 35  ? 48.748  114.104 101.236 1.00 20.33 ? 35   ILE O CG1 1 
ATOM   15611 C  CG2 . ILE O  1 35  ? 50.600  114.348 102.862 1.00 17.32 ? 35   ILE O CG2 1 
ATOM   15612 C  CD1 . ILE O  1 35  ? 47.924  113.331 102.281 1.00 24.99 ? 35   ILE O CD1 1 
ATOM   15613 N  N   . LYS O  1 36  ? 53.320  115.232 101.118 1.00 19.02 ? 36   LYS O N   1 
ATOM   15614 C  CA  . LYS O  1 36  ? 54.736  114.889 101.279 1.00 18.66 ? 36   LYS O CA  1 
ATOM   15615 C  C   . LYS O  1 36  ? 55.134  114.897 102.745 1.00 17.30 ? 36   LYS O C   1 
ATOM   15616 O  O   . LYS O  1 36  ? 54.320  115.251 103.598 1.00 17.32 ? 36   LYS O O   1 
ATOM   15617 C  CB  . LYS O  1 36  ? 55.652  115.813 100.461 1.00 19.14 ? 36   LYS O CB  1 
ATOM   15618 C  CG  . LYS O  1 36  ? 55.609  117.277 100.824 1.00 22.15 ? 36   LYS O CG  1 
ATOM   15619 C  CD  . LYS O  1 36  ? 56.592  118.056 99.975  1.00 27.19 ? 36   LYS O CD  1 
ATOM   15620 C  CE  . LYS O  1 36  ? 56.258  119.546 99.964  1.00 31.10 ? 36   LYS O CE  1 
ATOM   15621 N  NZ  . LYS O  1 36  ? 56.925  120.263 98.825  1.00 34.02 ? 36   LYS O NZ  1 
ATOM   15622 N  N   . GLY O  1 37  ? 56.361  114.458 103.032 1.00 16.08 ? 37   GLY O N   1 
ATOM   15623 C  CA  . GLY O  1 37  ? 56.902  114.486 104.379 1.00 15.00 ? 37   GLY O CA  1 
ATOM   15624 C  C   . GLY O  1 37  ? 56.569  113.277 105.244 1.00 14.83 ? 37   GLY O C   1 
ATOM   15625 O  O   . GLY O  1 37  ? 56.846  113.280 106.432 1.00 14.07 ? 37   GLY O O   1 
ATOM   15626 N  N   . LEU O  1 38  ? 56.064  112.219 104.621 1.00 15.87 ? 38   LEU O N   1 
ATOM   15627 C  CA  . LEU O  1 38  ? 55.607  111.013 105.337 1.00 15.55 ? 38   LEU O CA  1 
ATOM   15628 C  C   . LEU O  1 38  ? 56.578  109.835 105.359 1.00 15.81 ? 38   LEU O C   1 
ATOM   15629 O  O   . LEU O  1 38  ? 57.408  109.661 104.459 1.00 15.05 ? 38   LEU O O   1 
ATOM   15630 C  CB  . LEU O  1 38  ? 54.326  110.498 104.664 1.00 16.26 ? 38   LEU O CB  1 
ATOM   15631 C  CG  . LEU O  1 38  ? 53.064  111.349 104.653 1.00 16.20 ? 38   LEU O CG  1 
ATOM   15632 C  CD1 . LEU O  1 38  ? 52.037  110.844 103.589 1.00 19.44 ? 38   LEU O CD1 1 
ATOM   15633 C  CD2 . LEU O  1 38  ? 52.454  111.297 106.051 1.00 17.51 ? 38   LEU O CD2 1 
ATOM   15634 N  N   . THR O  1 39  ? 56.488  109.014 106.390 1.00 15.75 ? 39   THR O N   1 
ATOM   15635 C  CA  . THR O  1 39  ? 57.250  107.768 106.359 1.00 16.41 ? 39   THR O CA  1 
ATOM   15636 C  C   . THR O  1 39  ? 56.704  106.863 105.247 1.00 17.35 ? 39   THR O C   1 
ATOM   15637 O  O   . THR O  1 39  ? 55.492  106.793 105.006 1.00 17.21 ? 39   THR O O   1 
ATOM   15638 C  CB  . THR O  1 39  ? 57.158  107.018 107.683 1.00 16.02 ? 39   THR O CB  1 
ATOM   15639 O  OG1 . THR O  1 39  ? 55.789  106.971 108.114 1.00 17.71 ? 39   THR O OG1 1 
ATOM   15640 C  CG2 . THR O  1 39  ? 57.897  107.735 108.787 1.00 15.54 ? 39   THR O CG2 1 
ATOM   15641 N  N   . GLU O  1 40  ? 57.594  106.142 104.588 1.00 16.80 ? 40   GLU O N   1 
ATOM   15642 C  CA  . GLU O  1 40  ? 57.154  105.265 103.511 1.00 18.34 ? 40   GLU O CA  1 
ATOM   15643 C  C   . GLU O  1 40  ? 56.094  104.276 104.025 1.00 18.28 ? 40   GLU O C   1 
ATOM   15644 O  O   . GLU O  1 40  ? 56.237  103.715 105.124 1.00 19.31 ? 40   GLU O O   1 
ATOM   15645 C  CB  . GLU O  1 40  ? 58.364  104.500 102.982 1.00 18.54 ? 40   GLU O CB  1 
ATOM   15646 C  CG  . GLU O  1 40  ? 58.041  103.642 101.793 1.00 20.00 ? 40   GLU O CG  1 
ATOM   15647 C  CD  . GLU O  1 40  ? 59.184  102.717 101.427 1.00 23.40 ? 40   GLU O CD  1 
ATOM   15648 O  OE1 . GLU O  1 40  ? 60.312  102.869 101.976 1.00 22.40 ? 40   GLU O OE1 1 
ATOM   15649 O  OE2 . GLU O  1 40  ? 58.929  101.835 100.591 1.00 25.89 ? 40   GLU O OE2 1 
ATOM   15650 N  N   . GLY O  1 41  ? 55.037  104.047 103.249 1.00 17.66 ? 41   GLY O N   1 
ATOM   15651 C  CA  . GLY O  1 41  ? 54.011  103.110 103.689 1.00 18.16 ? 41   GLY O CA  1 
ATOM   15652 C  C   . GLY O  1 41  ? 52.627  103.714 103.886 1.00 18.25 ? 41   GLY O C   1 
ATOM   15653 O  O   . GLY O  1 41  ? 52.328  104.801 103.381 1.00 17.95 ? 41   GLY O O   1 
ATOM   15654 N  N   . LEU O  1 42  ? 51.779  103.010 104.633 1.00 18.04 ? 42   LEU O N   1 
ATOM   15655 C  CA  . LEU O  1 42  ? 50.369  103.408 104.749 1.00 18.60 ? 42   LEU O CA  1 
ATOM   15656 C  C   . LEU O  1 42  ? 50.080  104.396 105.867 1.00 17.63 ? 42   LEU O C   1 
ATOM   15657 O  O   . LEU O  1 42  ? 50.631  104.311 106.991 1.00 16.80 ? 42   LEU O O   1 
ATOM   15658 C  CB  . LEU O  1 42  ? 49.472  102.166 104.938 1.00 18.97 ? 42   LEU O CB  1 
ATOM   15659 C  CG  . LEU O  1 42  ? 48.978  101.307 103.759 1.00 22.63 ? 42   LEU O CG  1 
ATOM   15660 C  CD1 . LEU O  1 42  ? 49.870  101.419 102.539 1.00 24.71 ? 42   LEU O CD1 1 
ATOM   15661 C  CD2 . LEU O  1 42  ? 48.769  99.847  104.179 1.00 23.15 ? 42   LEU O CD2 1 
ATOM   15662 N  N   . HIS O  1 43  ? 49.182  105.329 105.547 1.00 16.38 ? 43   HIS O N   1 
ATOM   15663 C  CA  . HIS O  1 43  ? 48.737  106.341 106.489 1.00 15.77 ? 43   HIS O CA  1 
ATOM   15664 C  C   . HIS O  1 43  ? 47.236  106.537 106.384 1.00 15.71 ? 43   HIS O C   1 
ATOM   15665 O  O   . HIS O  1 43  ? 46.709  106.759 105.274 1.00 15.26 ? 43   HIS O O   1 
ATOM   15666 C  CB  . HIS O  1 43  ? 49.460  107.673 106.199 1.00 15.71 ? 43   HIS O CB  1 
ATOM   15667 C  CG  . HIS O  1 43  ? 50.937  107.608 106.443 1.00 16.41 ? 43   HIS O CG  1 
ATOM   15668 N  ND1 . HIS O  1 43  ? 51.498  107.883 107.675 1.00 14.53 ? 43   HIS O ND1 1 
ATOM   15669 C  CD2 . HIS O  1 43  ? 51.959  107.209 105.643 1.00 15.24 ? 43   HIS O CD2 1 
ATOM   15670 C  CE1 . HIS O  1 43  ? 52.807  107.705 107.606 1.00 16.68 ? 43   HIS O CE1 1 
ATOM   15671 N  NE2 . HIS O  1 43  ? 53.111  107.291 106.386 1.00 17.11 ? 43   HIS O NE2 1 
ATOM   15672 N  N   . GLY O  1 44  ? 46.553  106.466 107.528 1.00 15.45 ? 44   GLY O N   1 
ATOM   15673 C  CA  . GLY O  1 44  ? 45.111  106.683 107.586 1.00 16.76 ? 44   GLY O CA  1 
ATOM   15674 C  C   . GLY O  1 44  ? 44.763  108.060 107.051 1.00 16.94 ? 44   GLY O C   1 
ATOM   15675 O  O   . GLY O  1 44  ? 45.549  108.982 107.175 1.00 17.33 ? 44   GLY O O   1 
ATOM   15676 N  N   . PHE O  1 45  ? 43.575  108.195 106.465 1.00 17.01 ? 45   PHE O N   1 
ATOM   15677 C  CA  . PHE O  1 45  ? 43.214  109.383 105.717 1.00 16.26 ? 45   PHE O CA  1 
ATOM   15678 C  C   . PHE O  1 45  ? 41.723  109.458 105.871 1.00 16.62 ? 45   PHE O C   1 
ATOM   15679 O  O   . PHE O  1 45  ? 40.989  108.614 105.306 1.00 16.22 ? 45   PHE O O   1 
ATOM   15680 C  CB  . PHE O  1 45  ? 43.570  109.126 104.265 1.00 16.49 ? 45   PHE O CB  1 
ATOM   15681 C  CG  . PHE O  1 45  ? 43.355  110.283 103.345 1.00 15.37 ? 45   PHE O CG  1 
ATOM   15682 C  CD1 . PHE O  1 45  ? 44.044  111.478 103.521 1.00 19.59 ? 45   PHE O CD1 1 
ATOM   15683 C  CD2 . PHE O  1 45  ? 42.517  110.147 102.259 1.00 18.24 ? 45   PHE O CD2 1 
ATOM   15684 C  CE1 . PHE O  1 45  ? 43.871  112.525 102.625 1.00 17.51 ? 45   PHE O CE1 1 
ATOM   15685 C  CE2 . PHE O  1 45  ? 42.333  111.182 101.365 1.00 16.85 ? 45   PHE O CE2 1 
ATOM   15686 C  CZ  . PHE O  1 45  ? 43.014  112.366 101.542 1.00 17.88 ? 45   PHE O CZ  1 
ATOM   15687 N  N   . HIS O  1 46  ? 41.269  110.463 106.625 1.00 16.64 ? 46   HIS O N   1 
ATOM   15688 C  CA  . HIS O  1 46  ? 39.874  110.528 107.058 1.00 16.78 ? 46   HIS O CA  1 
ATOM   15689 C  C   . HIS O  1 46  ? 39.316  111.932 107.043 1.00 16.73 ? 46   HIS O C   1 
ATOM   15690 O  O   . HIS O  1 46  ? 40.050  112.907 107.211 1.00 15.50 ? 46   HIS O O   1 
ATOM   15691 C  CB  . HIS O  1 46  ? 39.782  110.067 108.518 1.00 17.64 ? 46   HIS O CB  1 
ATOM   15692 C  CG  . HIS O  1 46  ? 40.449  108.746 108.771 1.00 18.59 ? 46   HIS O CG  1 
ATOM   15693 N  ND1 . HIS O  1 46  ? 41.270  108.510 109.853 1.00 17.89 ? 46   HIS O ND1 1 
ATOM   15694 C  CD2 . HIS O  1 46  ? 40.416  107.591 108.066 1.00 18.27 ? 46   HIS O CD2 1 
ATOM   15695 C  CE1 . HIS O  1 46  ? 41.722  107.271 109.801 1.00 18.94 ? 46   HIS O CE1 1 
ATOM   15696 N  NE2 . HIS O  1 46  ? 41.213  106.687 108.730 1.00 18.53 ? 46   HIS O NE2 1 
ATOM   15697 N  N   . VAL O  1 47  ? 38.006  112.021 106.890 1.00 16.31 ? 47   VAL O N   1 
ATOM   15698 C  CA  . VAL O  1 47  ? 37.340  113.297 107.061 1.00 15.95 ? 47   VAL O CA  1 
ATOM   15699 C  C   . VAL O  1 47  ? 36.826  113.278 108.493 1.00 16.57 ? 47   VAL O C   1 
ATOM   15700 O  O   . VAL O  1 47  ? 36.047  112.409 108.854 1.00 16.96 ? 47   VAL O O   1 
ATOM   15701 C  CB  . VAL O  1 47  ? 36.158  113.473 106.103 1.00 16.61 ? 47   VAL O CB  1 
ATOM   15702 C  CG1 . VAL O  1 47  ? 35.330  114.711 106.489 1.00 15.93 ? 47   VAL O CG1 1 
ATOM   15703 C  CG2 . VAL O  1 47  ? 36.645  113.592 104.671 1.00 16.54 ? 47   VAL O CG2 1 
ATOM   15704 N  N   . HIS O  1 48  ? 37.298  114.194 109.322 1.00 16.53 ? 48   HIS O N   1 
ATOM   15705 C  CA  . HIS O  1 48  ? 36.833  114.298 110.696 1.00 16.86 ? 48   HIS O CA  1 
ATOM   15706 C  C   . HIS O  1 48  ? 35.678  115.294 110.768 1.00 17.47 ? 48   HIS O C   1 
ATOM   15707 O  O   . HIS O  1 48  ? 35.478  116.091 109.845 1.00 17.03 ? 48   HIS O O   1 
ATOM   15708 C  CB  . HIS O  1 48  ? 37.963  114.737 111.600 1.00 17.08 ? 48   HIS O CB  1 
ATOM   15709 C  CG  . HIS O  1 48  ? 38.940  113.653 111.909 1.00 17.97 ? 48   HIS O CG  1 
ATOM   15710 N  ND1 . HIS O  1 48  ? 39.284  113.318 113.200 1.00 16.72 ? 48   HIS O ND1 1 
ATOM   15711 C  CD2 . HIS O  1 48  ? 39.645  112.824 111.100 1.00 17.31 ? 48   HIS O CD2 1 
ATOM   15712 C  CE1 . HIS O  1 48  ? 40.159  112.321 113.173 1.00 17.94 ? 48   HIS O CE1 1 
ATOM   15713 N  NE2 . HIS O  1 48  ? 40.396  112.012 111.913 1.00 14.91 ? 48   HIS O NE2 1 
ATOM   15714 N  N   . GLU O  1 49  ? 34.963  115.290 111.880 1.00 17.06 ? 49   GLU O N   1 
ATOM   15715 C  CA  . GLU O  1 49  ? 33.683  115.982 111.953 1.00 17.84 ? 49   GLU O CA  1 
ATOM   15716 C  C   . GLU O  1 49  ? 33.704  117.496 111.924 1.00 17.38 ? 49   GLU O C   1 
ATOM   15717 O  O   . GLU O  1 49  ? 32.935  118.126 111.186 1.00 18.28 ? 49   GLU O O   1 
ATOM   15718 C  CB  . GLU O  1 49  ? 32.916  115.513 113.186 1.00 17.50 ? 49   GLU O CB  1 
ATOM   15719 C  CG  . GLU O  1 49  ? 31.589  116.229 113.406 1.00 19.42 ? 49   GLU O CG  1 
ATOM   15720 C  CD  . GLU O  1 49  ? 30.778  115.574 114.506 1.00 20.19 ? 49   GLU O CD  1 
ATOM   15721 O  OE1 . GLU O  1 49  ? 31.310  114.643 115.145 1.00 20.65 ? 49   GLU O OE1 1 
ATOM   15722 O  OE2 . GLU O  1 49  ? 29.618  115.981 114.729 1.00 20.56 ? 49   GLU O OE2 1 
ATOM   15723 N  N   . PHE O  1 50  ? 34.558  118.090 112.738 1.00 17.33 ? 50   PHE O N   1 
ATOM   15724 C  CA  . PHE O  1 50  ? 34.574  119.530 112.839 1.00 18.13 ? 50   PHE O CA  1 
ATOM   15725 C  C   . PHE O  1 50  ? 35.661  120.156 111.982 1.00 17.98 ? 50   PHE O C   1 
ATOM   15726 O  O   . PHE O  1 50  ? 36.764  119.593 111.840 1.00 18.72 ? 50   PHE O O   1 
ATOM   15727 C  CB  . PHE O  1 50  ? 34.753  119.927 114.300 1.00 17.88 ? 50   PHE O CB  1 
ATOM   15728 C  CG  . PHE O  1 50  ? 33.737  119.318 115.200 1.00 20.23 ? 50   PHE O CG  1 
ATOM   15729 C  CD1 . PHE O  1 50  ? 32.417  119.723 115.136 1.00 20.87 ? 50   PHE O CD1 1 
ATOM   15730 C  CD2 . PHE O  1 50  ? 34.086  118.319 116.086 1.00 20.67 ? 50   PHE O CD2 1 
ATOM   15731 C  CE1 . PHE O  1 50  ? 31.458  119.136 115.958 1.00 24.72 ? 50   PHE O CE1 1 
ATOM   15732 C  CE2 . PHE O  1 50  ? 33.124  117.739 116.916 1.00 21.95 ? 50   PHE O CE2 1 
ATOM   15733 C  CZ  . PHE O  1 50  ? 31.818  118.153 116.846 1.00 21.21 ? 50   PHE O CZ  1 
ATOM   15734 N  N   . GLY O  1 51  ? 35.343  121.314 111.413 1.00 17.50 ? 51   GLY O N   1 
ATOM   15735 C  CA  . GLY O  1 51  ? 36.304  122.080 110.653 1.00 17.02 ? 51   GLY O CA  1 
ATOM   15736 C  C   . GLY O  1 51  ? 36.918  123.081 111.615 1.00 17.54 ? 51   GLY O C   1 
ATOM   15737 O  O   . GLY O  1 51  ? 37.022  124.286 111.327 1.00 17.09 ? 51   GLY O O   1 
ATOM   15738 N  N   . ASP O  1 52  ? 37.299  122.573 112.785 1.00 17.42 ? 52   ASP O N   1 
ATOM   15739 C  CA  . ASP O  1 52  ? 37.821  123.393 113.876 1.00 17.66 ? 52   ASP O CA  1 
ATOM   15740 C  C   . ASP O  1 52  ? 39.298  123.100 114.115 1.00 18.79 ? 52   ASP O C   1 
ATOM   15741 O  O   . ASP O  1 52  ? 39.660  121.981 114.472 1.00 18.84 ? 52   ASP O O   1 
ATOM   15742 C  CB  . ASP O  1 52  ? 37.012  123.086 115.138 1.00 18.09 ? 52   ASP O CB  1 
ATOM   15743 C  CG  . ASP O  1 52  ? 37.401  123.932 116.325 1.00 17.62 ? 52   ASP O CG  1 
ATOM   15744 O  OD1 . ASP O  1 52  ? 38.519  124.498 116.338 1.00 19.73 ? 52   ASP O OD1 1 
ATOM   15745 O  OD2 . ASP O  1 52  ? 36.634  124.087 117.310 1.00 17.74 ? 52   ASP O OD2 1 
ATOM   15746 N  N   . ASN O  1 53  ? 40.136  124.120 113.962 1.00 19.29 ? 53   ASN O N   1 
ATOM   15747 C  CA  . ASN O  1 53  ? 41.586  123.989 114.110 1.00 20.69 ? 53   ASN O CA  1 
ATOM   15748 C  C   . ASN O  1 53  ? 42.183  124.867 115.172 1.00 19.84 ? 53   ASN O C   1 
ATOM   15749 O  O   . ASN O  1 53  ? 43.392  125.170 115.144 1.00 18.64 ? 53   ASN O O   1 
ATOM   15750 C  CB  . ASN O  1 53  ? 42.265  124.351 112.787 1.00 22.85 ? 53   ASN O CB  1 
ATOM   15751 C  CG  . ASN O  1 53  ? 42.836  123.145 112.094 1.00 28.18 ? 53   ASN O CG  1 
ATOM   15752 O  OD1 . ASN O  1 53  ? 42.285  122.641 111.081 1.00 30.86 ? 53   ASN O OD1 1 
ATOM   15753 N  ND2 . ASN O  1 53  ? 43.949  122.650 112.631 1.00 31.42 ? 53   ASN O ND2 1 
ATOM   15754 N  N   . THR O  1 54  ? 41.351  125.292 116.117 1.00 18.77 ? 54   THR O N   1 
ATOM   15755 C  CA  . THR O  1 54  ? 41.818  126.196 117.150 1.00 18.79 ? 54   THR O CA  1 
ATOM   15756 C  C   . THR O  1 54  ? 42.928  125.620 118.026 1.00 20.07 ? 54   THR O C   1 
ATOM   15757 O  O   . THR O  1 54  ? 43.760  126.356 118.556 1.00 20.25 ? 54   THR O O   1 
ATOM   15758 C  CB  . THR O  1 54  ? 40.636  126.655 118.033 1.00 19.15 ? 54   THR O CB  1 
ATOM   15759 O  OG1 . THR O  1 54  ? 39.875  125.513 118.450 1.00 18.77 ? 54   THR O OG1 1 
ATOM   15760 C  CG2 . THR O  1 54  ? 39.634  127.476 117.194 1.00 16.77 ? 54   THR O CG2 1 
ATOM   15761 N  N   . ALA O  1 55  ? 42.950  124.306 118.184 1.00 20.07 ? 55   ALA O N   1 
ATOM   15762 C  CA  . ALA O  1 55  ? 43.981  123.691 119.003 1.00 20.83 ? 55   ALA O CA  1 
ATOM   15763 C  C   . ALA O  1 55  ? 44.779  122.773 118.133 1.00 21.10 ? 55   ALA O C   1 
ATOM   15764 O  O   . ALA O  1 55  ? 45.293  121.762 118.612 1.00 22.74 ? 55   ALA O O   1 
ATOM   15765 C  CB  . ALA O  1 55  ? 43.360  122.882 120.123 1.00 20.88 ? 55   ALA O CB  1 
ATOM   15766 N  N   . GLY O  1 56  ? 44.850  123.094 116.852 1.00 20.99 ? 56   GLY O N   1 
ATOM   15767 C  CA  . GLY O  1 56  ? 45.460  122.206 115.892 1.00 20.41 ? 56   GLY O CA  1 
ATOM   15768 C  C   . GLY O  1 56  ? 44.532  121.084 115.433 1.00 20.79 ? 56   GLY O C   1 
ATOM   15769 O  O   . GLY O  1 56  ? 43.299  121.179 115.500 1.00 19.70 ? 56   GLY O O   1 
ATOM   15770 N  N   . CYS O  1 57  ? 45.127  119.971 115.010 1.00 20.00 ? 57   CYS O N   1 
ATOM   15771 C  CA  . CYS O  1 57  ? 44.337  118.881 114.452 1.00 21.18 ? 57   CYS O CA  1 
ATOM   15772 C  C   . CYS O  1 57  ? 43.388  118.180 115.437 1.00 20.62 ? 57   CYS O C   1 
ATOM   15773 O  O   . CYS O  1 57  ? 42.403  117.592 115.022 1.00 19.55 ? 57   CYS O O   1 
ATOM   15774 C  CB  . CYS O  1 57  ? 45.256  117.846 113.789 1.00 21.57 ? 57   CYS O CB  1 
ATOM   15775 S  SG  . CYS O  1 57  ? 46.068  118.533 112.335 1.00 26.07 ? 57   CYS O SG  1 
ATOM   15776 N  N   . THR O  1 58  ? 43.652  118.275 116.732 1.00 20.22 ? 58   THR O N   1 
ATOM   15777 C  CA  . THR O  1 58  ? 42.775  117.600 117.682 1.00 21.60 ? 58   THR O CA  1 
ATOM   15778 C  C   . THR O  1 58  ? 41.372  118.187 117.799 1.00 20.76 ? 58   THR O C   1 
ATOM   15779 O  O   . THR O  1 58  ? 40.449  117.510 118.267 1.00 19.54 ? 58   THR O O   1 
ATOM   15780 C  CB  . THR O  1 58  ? 43.399  117.552 119.090 1.00 22.52 ? 58   THR O CB  1 
ATOM   15781 O  OG1 . THR O  1 58  ? 42.357  117.801 120.054 1.00 27.12 ? 58   THR O OG1 1 
ATOM   15782 C  CG2 . THR O  1 58  ? 44.285  118.731 119.305 1.00 23.36 ? 58   THR O CG2 1 
ATOM   15783 N  N   . SER O  1 59  ? 41.220  119.444 117.386 1.00 19.69 ? 59   SER O N   1 
ATOM   15784 C  CA  . SER O  1 59  ? 39.961  120.162 117.486 1.00 20.26 ? 59   SER O CA  1 
ATOM   15785 C  C   . SER O  1 59  ? 38.964  119.647 116.465 1.00 20.31 ? 59   SER O C   1 
ATOM   15786 O  O   . SER O  1 59  ? 37.771  119.993 116.530 1.00 19.91 ? 59   SER O O   1 
ATOM   15787 C  CB  . SER O  1 59  ? 40.207  121.669 117.190 1.00 20.60 ? 59   SER O CB  1 
ATOM   15788 O  OG  . SER O  1 59  ? 41.025  122.266 118.174 1.00 21.43 ? 59   SER O OG  1 
ATOM   15789 N  N   . ALA O  1 60  ? 39.451  118.849 115.513 1.00 20.21 ? 60   ALA O N   1 
ATOM   15790 C  CA  . ALA O  1 60  ? 38.596  118.368 114.429 1.00 21.27 ? 60   ALA O CA  1 
ATOM   15791 C  C   . ALA O  1 60  ? 37.590  117.320 114.833 1.00 21.29 ? 60   ALA O C   1 
ATOM   15792 O  O   . ALA O  1 60  ? 36.741  116.940 114.033 1.00 21.98 ? 60   ALA O O   1 
ATOM   15793 C  CB  . ALA O  1 60  ? 39.417  117.865 113.262 1.00 20.79 ? 60   ALA O CB  1 
ATOM   15794 N  N   . GLY O  1 61  ? 37.688  116.837 116.060 1.00 21.01 ? 61   GLY O N   1 
ATOM   15795 C  CA  . GLY O  1 61  ? 36.764  115.824 116.520 1.00 21.20 ? 61   GLY O CA  1 
ATOM   15796 C  C   . GLY O  1 61  ? 37.117  114.444 115.977 1.00 20.74 ? 61   GLY O C   1 
ATOM   15797 O  O   . GLY O  1 61  ? 38.202  114.245 115.426 1.00 21.34 ? 61   GLY O O   1 
ATOM   15798 N  N   . PRO O  1 62  ? 36.181  113.509 116.103 1.00 20.23 ? 62   PRO O N   1 
ATOM   15799 C  CA  . PRO O  1 62  ? 36.363  112.126 115.655 1.00 20.22 ? 62   PRO O CA  1 
ATOM   15800 C  C   . PRO O  1 62  ? 35.940  112.041 114.201 1.00 20.22 ? 62   PRO O C   1 
ATOM   15801 O  O   . PRO O  1 62  ? 35.694  113.090 113.579 1.00 19.10 ? 62   PRO O O   1 
ATOM   15802 C  CB  . PRO O  1 62  ? 35.388  111.331 116.536 1.00 20.76 ? 62   PRO O CB  1 
ATOM   15803 C  CG  . PRO O  1 62  ? 34.591  112.382 117.329 1.00 20.62 ? 62   PRO O CG  1 
ATOM   15804 C  CD  . PRO O  1 62  ? 34.854  113.726 116.690 1.00 20.35 ? 62   PRO O CD  1 
ATOM   15805 N  N   . HIS O  1 63  ? 35.839  110.833 113.658 1.00 19.91 ? 63   HIS O N   1 
ATOM   15806 C  CA  . HIS O  1 63  ? 35.499  110.721 112.244 1.00 20.42 ? 63   HIS O CA  1 
ATOM   15807 C  C   . HIS O  1 63  ? 34.067  111.256 111.956 1.00 20.59 ? 63   HIS O C   1 
ATOM   15808 O  O   . HIS O  1 63  ? 33.165  111.125 112.798 1.00 20.02 ? 63   HIS O O   1 
ATOM   15809 C  CB  . HIS O  1 63  ? 35.708  109.260 111.768 1.00 20.80 ? 63   HIS O CB  1 
ATOM   15810 C  CG  . HIS O  1 63  ? 37.134  108.791 111.854 1.00 21.37 ? 63   HIS O CG  1 
ATOM   15811 N  ND1 . HIS O  1 63  ? 37.528  107.511 111.518 1.00 23.35 ? 63   HIS O ND1 1 
ATOM   15812 C  CD2 . HIS O  1 63  ? 38.265  109.442 112.237 1.00 23.90 ? 63   HIS O CD2 1 
ATOM   15813 C  CE1 . HIS O  1 63  ? 38.832  107.389 111.701 1.00 21.97 ? 63   HIS O CE1 1 
ATOM   15814 N  NE2 . HIS O  1 63  ? 39.303  108.548 112.135 1.00 22.65 ? 63   HIS O NE2 1 
ATOM   15815 N  N   . PHE O  1 64  ? 33.880  111.889 110.792 1.00 19.98 ? 64   PHE O N   1 
ATOM   15816 C  CA  . PHE O  1 64  ? 32.555  112.322 110.344 1.00 20.25 ? 64   PHE O CA  1 
ATOM   15817 C  C   . PHE O  1 64  ? 31.695  111.078 110.258 1.00 21.12 ? 64   PHE O C   1 
ATOM   15818 O  O   . PHE O  1 64  ? 31.980  110.188 109.446 1.00 20.69 ? 64   PHE O O   1 
ATOM   15819 C  CB  . PHE O  1 64  ? 32.635  112.927 108.950 1.00 19.66 ? 64   PHE O CB  1 
ATOM   15820 C  CG  . PHE O  1 64  ? 31.336  113.454 108.447 1.00 18.23 ? 64   PHE O CG  1 
ATOM   15821 C  CD1 . PHE O  1 64  ? 30.423  114.013 109.318 1.00 15.39 ? 64   PHE O CD1 1 
ATOM   15822 C  CD2 . PHE O  1 64  ? 31.048  113.428 107.094 1.00 18.50 ? 64   PHE O CD2 1 
ATOM   15823 C  CE1 . PHE O  1 64  ? 29.226  114.542 108.845 1.00 19.29 ? 64   PHE O CE1 1 
ATOM   15824 C  CE2 . PHE O  1 64  ? 29.865  113.942 106.602 1.00 19.98 ? 64   PHE O CE2 1 
ATOM   15825 C  CZ  . PHE O  1 64  ? 28.942  114.513 107.481 1.00 19.81 ? 64   PHE O CZ  1 
ATOM   15826 N  N   . ASN O  1 65  ? 30.641  111.029 111.072 1.00 21.99 ? 65   ASN O N   1 
ATOM   15827 C  CA  . ASN O  1 65  ? 29.821  109.831 111.191 1.00 23.36 ? 65   ASN O CA  1 
ATOM   15828 C  C   . ASN O  1 65  ? 28.406  110.198 111.607 1.00 24.73 ? 65   ASN O C   1 
ATOM   15829 O  O   . ASN O  1 65  ? 28.033  110.048 112.777 1.00 25.11 ? 65   ASN O O   1 
ATOM   15830 C  CB  . ASN O  1 65  ? 30.455  108.925 112.246 1.00 22.89 ? 65   ASN O CB  1 
ATOM   15831 C  CG  . ASN O  1 65  ? 29.795  107.572 112.336 1.00 23.51 ? 65   ASN O CG  1 
ATOM   15832 O  OD1 . ASN O  1 65  ? 29.379  106.996 111.327 1.00 23.08 ? 65   ASN O OD1 1 
ATOM   15833 N  ND2 . ASN O  1 65  ? 29.722  107.038 113.554 1.00 20.53 ? 65   ASN O ND2 1 
ATOM   15834 N  N   . PRO O  1 66  ? 27.626  110.686 110.643 1.00 25.64 ? 66   PRO O N   1 
ATOM   15835 C  CA  . PRO O  1 66  ? 26.258  111.138 110.886 1.00 26.19 ? 66   PRO O CA  1 
ATOM   15836 C  C   . PRO O  1 66  ? 25.290  109.976 111.066 1.00 26.80 ? 66   PRO O C   1 
ATOM   15837 O  O   . PRO O  1 66  ? 24.175  110.200 111.544 1.00 26.69 ? 66   PRO O O   1 
ATOM   15838 C  CB  . PRO O  1 66  ? 25.930  111.893 109.596 1.00 26.85 ? 66   PRO O CB  1 
ATOM   15839 C  CG  . PRO O  1 66  ? 26.699  111.143 108.565 1.00 26.60 ? 66   PRO O CG  1 
ATOM   15840 C  CD  . PRO O  1 66  ? 28.010  110.850 109.228 1.00 25.70 ? 66   PRO O CD  1 
ATOM   15841 N  N   . LEU O  1 67  ? 25.707  108.771 110.686 1.00 27.06 ? 67   LEU O N   1 
ATOM   15842 C  CA  . LEU O  1 67  ? 24.874  107.574 110.832 1.00 28.05 ? 67   LEU O CA  1 
ATOM   15843 C  C   . LEU O  1 67  ? 25.146  106.803 112.135 1.00 28.51 ? 67   LEU O C   1 
ATOM   15844 O  O   . LEU O  1 67  ? 24.508  105.778 112.402 1.00 28.54 ? 67   LEU O O   1 
ATOM   15845 C  CB  . LEU O  1 67  ? 25.031  106.653 109.616 1.00 27.92 ? 67   LEU O CB  1 
ATOM   15846 C  CG  . LEU O  1 67  ? 24.884  107.284 108.223 1.00 27.84 ? 67   LEU O CG  1 
ATOM   15847 C  CD1 . LEU O  1 67  ? 24.977  106.205 107.146 1.00 27.44 ? 67   LEU O CD1 1 
ATOM   15848 C  CD2 . LEU O  1 67  ? 23.594  108.092 108.070 1.00 28.44 ? 67   LEU O CD2 1 
ATOM   15849 N  N   . SER O  1 68  ? 26.084  107.310 112.935 1.00 29.32 ? 68   SER O N   1 
ATOM   15850 C  CA  . SER O  1 68  ? 26.451  106.745 114.245 1.00 29.89 ? 68   SER O CA  1 
ATOM   15851 C  C   . SER O  1 68  ? 27.139  105.381 114.168 1.00 30.47 ? 68   SER O C   1 
ATOM   15852 O  O   . SER O  1 68  ? 27.341  104.716 115.205 1.00 31.40 ? 68   SER O O   1 
ATOM   15853 C  CB  . SER O  1 68  ? 25.234  106.678 115.182 1.00 29.91 ? 68   SER O CB  1 
ATOM   15854 O  OG  . SER O  1 68  ? 24.955  107.942 115.771 1.00 29.46 ? 68   SER O OG  1 
ATOM   15855 N  N   . ARG O  1 69  ? 27.512  104.982 112.945 1.00 30.21 ? 69   ARG O N   1 
ATOM   15856 C  CA  . ARG O  1 69  ? 28.080  103.653 112.657 1.00 29.75 ? 69   ARG O CA  1 
ATOM   15857 C  C   . ARG O  1 69  ? 29.501  103.369 113.172 1.00 29.09 ? 69   ARG O C   1 
ATOM   15858 O  O   . ARG O  1 69  ? 30.130  104.212 113.817 1.00 29.03 ? 69   ARG O O   1 
ATOM   15859 C  CB  . ARG O  1 69  ? 28.037  103.370 111.145 1.00 29.89 ? 69   ARG O CB  1 
ATOM   15860 C  CG  . ARG O  1 69  ? 26.637  103.239 110.539 1.00 31.95 ? 69   ARG O CG  1 
ATOM   15861 C  CD  . ARG O  1 69  ? 26.570  102.280 109.341 1.00 34.10 ? 69   ARG O CD  1 
ATOM   15862 N  NE  . ARG O  1 69  ? 25.473  102.575 108.423 1.00 34.09 ? 69   ARG O NE  1 
ATOM   15863 C  CZ  . ARG O  1 69  ? 24.194  102.411 108.715 1.00 36.26 ? 69   ARG O CZ  1 
ATOM   15864 N  NH1 . ARG O  1 69  ? 23.835  101.941 109.903 1.00 37.71 ? 69   ARG O NH1 1 
ATOM   15865 N  NH2 . ARG O  1 69  ? 23.266  102.709 107.816 1.00 36.15 ? 69   ARG O NH2 1 
ATOM   15866 N  N   . LYS O  1 70  ? 29.997  102.166 112.870 1.00 28.12 ? 70   LYS O N   1 
ATOM   15867 C  CA  . LYS O  1 70  ? 31.350  101.753 113.256 1.00 27.49 ? 70   LYS O CA  1 
ATOM   15868 C  C   . LYS O  1 70  ? 32.393  102.031 112.163 1.00 26.40 ? 70   LYS O C   1 
ATOM   15869 O  O   . LYS O  1 70  ? 32.078  102.093 110.970 1.00 25.64 ? 70   LYS O O   1 
ATOM   15870 C  CB  . LYS O  1 70  ? 31.390  100.263 113.627 1.00 28.16 ? 70   LYS O CB  1 
ATOM   15871 C  CG  . LYS O  1 70  ? 30.792  99.949  115.010 1.00 30.11 ? 70   LYS O CG  1 
ATOM   15872 C  CD  . LYS O  1 70  ? 31.241  101.023 116.024 1.00 33.51 ? 70   LYS O CD  1 
ATOM   15873 C  CE  . LYS O  1 70  ? 30.386  101.039 117.292 1.00 34.40 ? 70   LYS O CE  1 
ATOM   15874 N  NZ  . LYS O  1 70  ? 30.435  99.785  118.090 1.00 35.73 ? 70   LYS O NZ  1 
ATOM   15875 N  N   . HIS O  1 71  ? 33.648  102.156 112.576 1.00 25.35 ? 71   HIS O N   1 
ATOM   15876 C  CA  . HIS O  1 71  ? 34.710  102.466 111.638 1.00 24.89 ? 71   HIS O CA  1 
ATOM   15877 C  C   . HIS O  1 71  ? 35.016  101.317 110.700 1.00 25.26 ? 71   HIS O C   1 
ATOM   15878 O  O   . HIS O  1 71  ? 35.010  100.149 111.106 1.00 25.09 ? 71   HIS O O   1 
ATOM   15879 C  CB  . HIS O  1 71  ? 35.983  102.840 112.382 1.00 24.95 ? 71   HIS O CB  1 
ATOM   15880 C  CG  . HIS O  1 71  ? 37.124  103.180 111.475 1.00 24.11 ? 71   HIS O CG  1 
ATOM   15881 N  ND1 . HIS O  1 71  ? 37.240  104.402 110.855 1.00 20.52 ? 71   HIS O ND1 1 
ATOM   15882 C  CD2 . HIS O  1 71  ? 38.188  102.448 111.069 1.00 23.25 ? 71   HIS O CD2 1 
ATOM   15883 C  CE1 . HIS O  1 71  ? 38.330  104.412 110.108 1.00 21.44 ? 71   HIS O CE1 1 
ATOM   15884 N  NE2 . HIS O  1 71  ? 38.925  103.240 110.222 1.00 20.40 ? 71   HIS O NE2 1 
ATOM   15885 N  N   . GLY O  1 72  ? 35.303  101.646 109.448 1.00 24.73 ? 72   GLY O N   1 
ATOM   15886 C  CA  . GLY O  1 72  ? 35.662  100.635 108.472 1.00 24.59 ? 72   GLY O CA  1 
ATOM   15887 C  C   . GLY O  1 72  ? 36.498  101.254 107.382 1.00 24.87 ? 72   GLY O C   1 
ATOM   15888 O  O   . GLY O  1 72  ? 36.945  102.401 107.507 1.00 24.69 ? 72   GLY O O   1 
ATOM   15889 N  N   . GLY O  1 73  ? 36.718  100.512 106.310 1.00 24.89 ? 73   GLY O N   1 
ATOM   15890 C  CA  . GLY O  1 73  ? 37.450  101.052 105.181 1.00 26.16 ? 73   GLY O CA  1 
ATOM   15891 C  C   . GLY O  1 73  ? 36.458  101.590 104.171 1.00 26.34 ? 73   GLY O C   1 
ATOM   15892 O  O   . GLY O  1 73  ? 35.261  101.341 104.276 1.00 26.16 ? 73   GLY O O   1 
ATOM   15893 N  N   . PRO O  1 74  ? 36.962  102.259 103.150 1.00 26.96 ? 74   PRO O N   1 
ATOM   15894 C  CA  . PRO O  1 74  ? 36.097  102.884 102.138 1.00 27.85 ? 74   PRO O CA  1 
ATOM   15895 C  C   . PRO O  1 74  ? 35.118  101.880 101.496 1.00 28.95 ? 74   PRO O C   1 
ATOM   15896 O  O   . PRO O  1 74  ? 33.907  102.152 101.434 1.00 28.32 ? 74   PRO O O   1 
ATOM   15897 C  CB  . PRO O  1 74  ? 37.089  103.399 101.080 1.00 27.82 ? 74   PRO O CB  1 
ATOM   15898 C  CG  . PRO O  1 74  ? 38.458  103.298 101.693 1.00 27.57 ? 74   PRO O CG  1 
ATOM   15899 C  CD  . PRO O  1 74  ? 38.395  102.400 102.860 1.00 26.62 ? 74   PRO O CD  1 
ATOM   15900 N  N   . LYS O  1 75  ? 35.638  100.735 101.048 1.00 29.96 ? 75   LYS O N   1 
ATOM   15901 C  CA  . LYS O  1 75  ? 34.846  99.718  100.329 1.00 31.26 ? 75   LYS O CA  1 
ATOM   15902 C  C   . LYS O  1 75  ? 33.833  98.945  101.163 1.00 31.56 ? 75   LYS O C   1 
ATOM   15903 O  O   . LYS O  1 75  ? 33.086  98.108  100.622 1.00 31.36 ? 75   LYS O O   1 
ATOM   15904 C  CB  . LYS O  1 75  ? 35.766  98.713  99.624  1.00 31.84 ? 75   LYS O CB  1 
ATOM   15905 C  CG  . LYS O  1 75  ? 36.412  99.247  98.360  1.00 34.75 ? 75   LYS O CG  1 
ATOM   15906 C  CD  . LYS O  1 75  ? 37.730  98.548  98.073  1.00 38.02 ? 75   LYS O CD  1 
ATOM   15907 C  CE  . LYS O  1 75  ? 38.713  99.506  97.391  1.00 39.62 ? 75   LYS O CE  1 
ATOM   15908 N  NZ  . LYS O  1 75  ? 39.259  100.566 98.308  1.00 40.97 ? 75   LYS O NZ  1 
ATOM   15909 N  N   . ASP O  1 76  ? 33.809  99.204  102.467 1.00 31.61 ? 76   ASP O N   1 
ATOM   15910 C  CA  . ASP O  1 76  ? 32.896  98.504  103.359 1.00 32.25 ? 76   ASP O CA  1 
ATOM   15911 C  C   . ASP O  1 76  ? 31.469  98.948  103.079 1.00 31.94 ? 76   ASP O C   1 
ATOM   15912 O  O   . ASP O  1 76  ? 31.227  99.775  102.202 1.00 33.38 ? 76   ASP O O   1 
ATOM   15913 C  CB  . ASP O  1 76  ? 33.224  98.827  104.822 1.00 32.33 ? 76   ASP O CB  1 
ATOM   15914 C  CG  . ASP O  1 76  ? 34.315  97.934  105.409 1.00 34.03 ? 76   ASP O CG  1 
ATOM   15915 O  OD1 . ASP O  1 76  ? 35.507  98.151  105.104 1.00 35.26 ? 76   ASP O OD1 1 
ATOM   15916 O  OD2 . ASP O  1 76  ? 34.072  97.005  106.212 1.00 34.69 ? 76   ASP O OD2 1 
ATOM   15917 N  N   . GLU O  1 77  ? 30.521  98.379  103.810 1.00 30.75 ? 77   GLU O N   1 
ATOM   15918 C  CA  . GLU O  1 77  ? 29.167  98.902  103.823 1.00 29.25 ? 77   GLU O CA  1 
ATOM   15919 C  C   . GLU O  1 77  ? 29.094  99.551  105.202 1.00 28.06 ? 77   GLU O C   1 
ATOM   15920 O  O   . GLU O  1 77  ? 28.460  100.580 105.384 1.00 27.76 ? 77   GLU O O   1 
ATOM   15921 C  CB  . GLU O  1 77  ? 28.119  97.795  103.660 1.00 29.64 ? 77   GLU O CB  1 
ATOM   15922 C  CG  . GLU O  1 77  ? 26.687  98.297  103.601 1.00 30.87 ? 77   GLU O CG  1 
ATOM   15923 C  CD  . GLU O  1 77  ? 25.709  97.241  103.111 1.00 32.88 ? 77   GLU O CD  1 
ATOM   15924 O  OE1 . GLU O  1 77  ? 26.152  96.250  102.485 1.00 33.17 ? 77   GLU O OE1 1 
ATOM   15925 O  OE2 . GLU O  1 77  ? 24.489  97.394  103.346 1.00 35.99 ? 77   GLU O OE2 1 
ATOM   15926 N  N   . GLU O  1 78  ? 29.792  98.948  106.164 1.00 26.54 ? 78   GLU O N   1 
ATOM   15927 C  CA  . GLU O  1 78  ? 29.886  99.471  107.523 1.00 25.26 ? 78   GLU O CA  1 
ATOM   15928 C  C   . GLU O  1 78  ? 31.129  100.367 107.666 1.00 24.48 ? 78   GLU O C   1 
ATOM   15929 O  O   . GLU O  1 78  ? 32.094  100.017 108.342 1.00 24.28 ? 78   GLU O O   1 
ATOM   15930 C  CB  . GLU O  1 78  ? 29.945  98.328  108.544 1.00 25.86 ? 78   GLU O CB  1 
ATOM   15931 C  CG  . GLU O  1 78  ? 29.846  98.766  110.002 1.00 26.08 ? 78   GLU O CG  1 
ATOM   15932 C  CD  . GLU O  1 78  ? 28.444  99.202  110.411 1.00 28.29 ? 78   GLU O CD  1 
ATOM   15933 O  OE1 . GLU O  1 78  ? 27.453  98.842  109.724 1.00 28.95 ? 78   GLU O OE1 1 
ATOM   15934 O  OE2 . GLU O  1 78  ? 28.321  99.898  111.443 1.00 28.03 ? 78   GLU O OE2 1 
ATOM   15935 N  N   . ARG O  1 79  ? 31.102  101.517 107.009 1.00 23.38 ? 79   ARG O N   1 
ATOM   15936 C  CA  . ARG O  1 79  ? 32.191  102.500 107.130 1.00 22.04 ? 79   ARG O CA  1 
ATOM   15937 C  C   . ARG O  1 79  ? 31.605  103.792 107.686 1.00 22.10 ? 79   ARG O C   1 
ATOM   15938 O  O   . ARG O  1 79  ? 30.381  103.971 107.679 1.00 21.11 ? 79   ARG O O   1 
ATOM   15939 C  CB  . ARG O  1 79  ? 32.812  102.795 105.756 1.00 22.33 ? 79   ARG O CB  1 
ATOM   15940 C  CG  . ARG O  1 79  ? 31.896  103.587 104.791 1.00 20.59 ? 79   ARG O CG  1 
ATOM   15941 C  CD  . ARG O  1 79  ? 32.496  104.936 104.294 1.00 24.26 ? 79   ARG O CD  1 
ATOM   15942 N  NE  . ARG O  1 79  ? 33.148  104.808 102.995 1.00 23.12 ? 79   ARG O NE  1 
ATOM   15943 C  CZ  . ARG O  1 79  ? 33.691  105.798 102.301 1.00 24.37 ? 79   ARG O CZ  1 
ATOM   15944 N  NH1 . ARG O  1 79  ? 33.680  107.051 102.742 1.00 15.31 ? 79   ARG O NH1 1 
ATOM   15945 N  NH2 . ARG O  1 79  ? 34.265  105.519 101.137 1.00 28.68 ? 79   ARG O NH2 1 
ATOM   15946 N  N   . HIS O  1 80  ? 32.468  104.693 108.163 1.00 21.76 ? 80   HIS O N   1 
ATOM   15947 C  CA  . HIS O  1 80  ? 32.034  106.038 108.570 1.00 21.77 ? 80   HIS O CA  1 
ATOM   15948 C  C   . HIS O  1 80  ? 31.992  106.826 107.285 1.00 21.31 ? 80   HIS O C   1 
ATOM   15949 O  O   . HIS O  1 80  ? 32.734  106.516 106.367 1.00 21.50 ? 80   HIS O O   1 
ATOM   15950 C  CB  . HIS O  1 80  ? 33.066  106.719 109.455 1.00 22.05 ? 80   HIS O CB  1 
ATOM   15951 C  CG  . HIS O  1 80  ? 33.086  106.231 110.865 1.00 23.47 ? 80   HIS O CG  1 
ATOM   15952 N  ND1 . HIS O  1 80  ? 34.231  106.235 111.635 1.00 24.56 ? 80   HIS O ND1 1 
ATOM   15953 C  CD2 . HIS O  1 80  ? 32.103  105.738 111.654 1.00 24.74 ? 80   HIS O CD2 1 
ATOM   15954 C  CE1 . HIS O  1 80  ? 33.954  105.758 112.836 1.00 25.03 ? 80   HIS O CE1 1 
ATOM   15955 N  NE2 . HIS O  1 80  ? 32.669  105.451 112.875 1.00 26.52 ? 80   HIS O NE2 1 
ATOM   15956 N  N   . VAL O  1 81  ? 31.163  107.857 107.197 1.00 20.63 ? 81   VAL O N   1 
ATOM   15957 C  CA  . VAL O  1 81  ? 31.141  108.607 105.957 1.00 20.38 ? 81   VAL O CA  1 
ATOM   15958 C  C   . VAL O  1 81  ? 32.561  109.091 105.638 1.00 20.60 ? 81   VAL O C   1 
ATOM   15959 O  O   . VAL O  1 81  ? 32.995  109.071 104.486 1.00 20.83 ? 81   VAL O O   1 
ATOM   15960 C  CB  . VAL O  1 81  ? 30.152  109.780 106.008 1.00 20.27 ? 81   VAL O CB  1 
ATOM   15961 C  CG1 . VAL O  1 81  ? 30.370  110.709 104.826 1.00 21.06 ? 81   VAL O CG1 1 
ATOM   15962 C  CG2 . VAL O  1 81  ? 28.705  109.261 106.017 1.00 20.86 ? 81   VAL O CG2 1 
ATOM   15963 N  N   . GLY O  1 82  ? 33.305  109.458 106.671 1.00 19.98 ? 82   GLY O N   1 
ATOM   15964 C  CA  . GLY O  1 82  ? 34.627  110.039 106.461 1.00 19.87 ? 82   GLY O CA  1 
ATOM   15965 C  C   . GLY O  1 82  ? 35.758  109.036 106.365 1.00 19.95 ? 82   GLY O C   1 
ATOM   15966 O  O   . GLY O  1 82  ? 36.919  109.410 106.325 1.00 18.99 ? 82   GLY O O   1 
ATOM   15967 N  N   . ASP O  1 83  ? 35.429  107.751 106.320 1.00 20.07 ? 83   ASP O N   1 
ATOM   15968 C  CA  . ASP O  1 83  ? 36.469  106.719 106.276 1.00 20.20 ? 83   ASP O CA  1 
ATOM   15969 C  C   . ASP O  1 83  ? 37.053  106.551 104.887 1.00 20.54 ? 83   ASP O C   1 
ATOM   15970 O  O   . ASP O  1 83  ? 36.591  105.716 104.109 1.00 20.48 ? 83   ASP O O   1 
ATOM   15971 C  CB  . ASP O  1 83  ? 35.915  105.382 106.779 1.00 20.58 ? 83   ASP O CB  1 
ATOM   15972 C  CG  . ASP O  1 83  ? 35.680  105.390 108.267 1.00 20.86 ? 83   ASP O CG  1 
ATOM   15973 O  OD1 . ASP O  1 83  ? 36.196  106.331 108.913 1.00 21.01 ? 83   ASP O OD1 1 
ATOM   15974 O  OD2 . ASP O  1 83  ? 35.006  104.515 108.875 1.00 20.43 ? 83   ASP O OD2 1 
ATOM   15975 N  N   . LEU O  1 84  ? 38.086  107.327 104.581 1.00 20.93 ? 84   LEU O N   1 
ATOM   15976 C  CA  . LEU O  1 84  ? 38.706  107.248 103.267 1.00 21.46 ? 84   LEU O CA  1 
ATOM   15977 C  C   . LEU O  1 84  ? 39.902  106.308 103.176 1.00 21.85 ? 84   LEU O C   1 
ATOM   15978 O  O   . LEU O  1 84  ? 40.678  106.413 102.224 1.00 22.41 ? 84   LEU O O   1 
ATOM   15979 C  CB  . LEU O  1 84  ? 39.108  108.629 102.764 1.00 20.66 ? 84   LEU O CB  1 
ATOM   15980 C  CG  . LEU O  1 84  ? 37.922  109.587 102.641 1.00 22.08 ? 84   LEU O CG  1 
ATOM   15981 C  CD1 . LEU O  1 84  ? 38.358  110.896 101.965 1.00 22.07 ? 84   LEU O CD1 1 
ATOM   15982 C  CD2 . LEU O  1 84  ? 36.789  108.922 101.869 1.00 19.17 ? 84   LEU O CD2 1 
ATOM   15983 N  N   . GLY O  1 85  ? 40.090  105.434 104.164 1.00 21.51 ? 85   GLY O N   1 
ATOM   15984 C  CA  . GLY O  1 85  ? 41.129  104.418 104.070 1.00 21.40 ? 85   GLY O CA  1 
ATOM   15985 C  C   . GLY O  1 85  ? 42.557  104.867 104.353 1.00 21.47 ? 85   GLY O C   1 
ATOM   15986 O  O   . GLY O  1 85  ? 42.821  105.555 105.343 1.00 21.43 ? 85   GLY O O   1 
ATOM   15987 N  N   . ASN O  1 86  ? 43.481  104.436 103.498 1.00 20.49 ? 86   ASN O N   1 
ATOM   15988 C  CA  . ASN O  1 86  ? 44.880  104.788 103.627 1.00 19.65 ? 86   ASN O CA  1 
ATOM   15989 C  C   . ASN O  1 86  ? 45.383  105.399 102.349 1.00 19.78 ? 86   ASN O C   1 
ATOM   15990 O  O   . ASN O  1 86  ? 44.925  105.065 101.241 1.00 18.09 ? 86   ASN O O   1 
ATOM   15991 C  CB  . ASN O  1 86  ? 45.715  103.548 103.835 1.00 20.13 ? 86   ASN O CB  1 
ATOM   15992 C  CG  . ASN O  1 86  ? 45.516  102.951 105.171 1.00 20.89 ? 86   ASN O CG  1 
ATOM   15993 O  OD1 . ASN O  1 86  ? 45.794  103.587 106.195 1.00 19.79 ? 86   ASN O OD1 1 
ATOM   15994 N  ND2 . ASN O  1 86  ? 45.033  101.708 105.192 1.00 19.21 ? 86   ASN O ND2 1 
ATOM   15995 N  N   . VAL O  1 87  ? 46.317  106.319 102.499 1.00 18.49 ? 87   VAL O N   1 
ATOM   15996 C  CA  . VAL O  1 87  ? 47.041  106.780 101.354 1.00 18.87 ? 87   VAL O CA  1 
ATOM   15997 C  C   . VAL O  1 87  ? 48.401  106.109 101.532 1.00 18.57 ? 87   VAL O C   1 
ATOM   15998 O  O   . VAL O  1 87  ? 48.753  105.678 102.629 1.00 18.24 ? 87   VAL O O   1 
ATOM   15999 C  CB  . VAL O  1 87  ? 47.138  108.303 101.338 1.00 18.21 ? 87   VAL O CB  1 
ATOM   16000 C  CG1 . VAL O  1 87  ? 45.754  108.904 101.227 1.00 20.53 ? 87   VAL O CG1 1 
ATOM   16001 C  CG2 . VAL O  1 87  ? 47.822  108.769 102.597 1.00 17.90 ? 87   VAL O CG2 1 
ATOM   16002 N  N   . THR O  1 88  ? 49.146  105.970 100.446 1.00 19.22 ? 88   THR O N   1 
ATOM   16003 C  CA  . THR O  1 88  ? 50.406  105.253 100.506 1.00 19.63 ? 88   THR O CA  1 
ATOM   16004 C  C   . THR O  1 88  ? 51.576  106.124 100.105 1.00 19.48 ? 88   THR O C   1 
ATOM   16005 O  O   . THR O  1 88  ? 51.627  106.627 98.969  1.00 18.56 ? 88   THR O O   1 
ATOM   16006 C  CB  . THR O  1 88  ? 50.319  104.045 99.554  1.00 20.90 ? 88   THR O CB  1 
ATOM   16007 O  OG1 . THR O  1 88  ? 49.346  103.127 100.058 1.00 21.14 ? 88   THR O OG1 1 
ATOM   16008 C  CG2 . THR O  1 88  ? 51.616  103.220 99.558  1.00 21.07 ? 88   THR O CG2 1 
ATOM   16009 N  N   . ALA O  1 89  ? 52.513  106.319 101.027 1.00 18.66 ? 89   ALA O N   1 
ATOM   16010 C  CA  . ALA O  1 89  ? 53.698  107.105 100.714 1.00 19.04 ? 89   ALA O CA  1 
ATOM   16011 C  C   . ALA O  1 89  ? 54.843  106.265 100.189 1.00 19.12 ? 89   ALA O C   1 
ATOM   16012 O  O   . ALA O  1 89  ? 55.112  105.141 100.677 1.00 19.31 ? 89   ALA O O   1 
ATOM   16013 C  CB  . ALA O  1 89  ? 54.151  107.959 101.938 1.00 18.51 ? 89   ALA O CB  1 
ATOM   16014 N  N   . ASP O  1 90  ? 55.519  106.811 99.177  1.00 19.93 ? 90   ASP O N   1 
ATOM   16015 C  CA  . ASP O  1 90  ? 56.653  106.132 98.566  1.00 20.63 ? 90   ASP O CA  1 
ATOM   16016 C  C   . ASP O  1 90  ? 57.917  106.365 99.390  1.00 20.81 ? 90   ASP O C   1 
ATOM   16017 O  O   . ASP O  1 90  ? 57.864  107.041 100.423 1.00 20.89 ? 90   ASP O O   1 
ATOM   16018 C  CB  . ASP O  1 90  ? 56.817  106.509 97.085  1.00 20.69 ? 90   ASP O CB  1 
ATOM   16019 C  CG  . ASP O  1 90  ? 57.264  107.934 96.877  1.00 21.64 ? 90   ASP O CG  1 
ATOM   16020 O  OD1 . ASP O  1 90  ? 57.846  108.543 97.809  1.00 22.32 ? 90   ASP O OD1 1 
ATOM   16021 O  OD2 . ASP O  1 90  ? 57.089  108.521 95.787  1.00 23.73 ? 90   ASP O OD2 1 
ATOM   16022 N  N   . LYS O  1 91  ? 59.041  105.810 98.941  1.00 20.59 ? 91   LYS O N   1 
ATOM   16023 C  CA  . LYS O  1 91  ? 60.296  105.911 99.681  1.00 21.09 ? 91   LYS O CA  1 
ATOM   16024 C  C   . LYS O  1 91  ? 60.749  107.343 99.951  1.00 20.93 ? 91   LYS O C   1 
ATOM   16025 O  O   . LYS O  1 91  ? 61.372  107.609 100.969 1.00 21.37 ? 91   LYS O O   1 
ATOM   16026 C  CB  . LYS O  1 91  ? 61.424  105.111 98.988  1.00 21.59 ? 91   LYS O CB  1 
ATOM   16027 C  CG  . LYS O  1 91  ? 61.712  105.542 97.560  1.00 23.75 ? 91   LYS O CG  1 
ATOM   16028 C  CD  . LYS O  1 91  ? 63.156  105.200 97.146  1.00 29.14 ? 91   LYS O CD  1 
ATOM   16029 C  CE  . LYS O  1 91  ? 63.841  106.415 96.461  1.00 31.06 ? 91   LYS O CE  1 
ATOM   16030 N  NZ  . LYS O  1 91  ? 64.083  106.240 94.988  1.00 32.98 ? 91   LYS O NZ  1 
ATOM   16031 N  N   . ASP O  1 92  ? 60.441  108.273 99.050  1.00 20.62 ? 92   ASP O N   1 
ATOM   16032 C  CA  . ASP O  1 92  ? 60.813  109.673 99.252  1.00 19.93 ? 92   ASP O CA  1 
ATOM   16033 C  C   . ASP O  1 92  ? 59.832  110.419 100.171 1.00 19.58 ? 92   ASP O C   1 
ATOM   16034 O  O   . ASP O  1 92  ? 59.971  111.639 100.395 1.00 19.16 ? 92   ASP O O   1 
ATOM   16035 C  CB  . ASP O  1 92  ? 60.894  110.395 97.910  1.00 20.40 ? 92   ASP O CB  1 
ATOM   16036 C  CG  . ASP O  1 92  ? 62.065  109.942 97.071  1.00 21.41 ? 92   ASP O CG  1 
ATOM   16037 O  OD1 . ASP O  1 92  ? 62.913  109.188 97.570  1.00 19.01 ? 92   ASP O OD1 1 
ATOM   16038 O  OD2 . ASP O  1 92  ? 62.232  110.320 95.896  1.00 26.83 ? 92   ASP O OD2 1 
ATOM   16039 N  N   . GLY O  1 93  ? 58.825  109.700 100.667 1.00 18.82 ? 93   GLY O N   1 
ATOM   16040 C  CA  . GLY O  1 93  ? 57.859  110.275 101.585 1.00 18.37 ? 93   GLY O CA  1 
ATOM   16041 C  C   . GLY O  1 93  ? 56.683  110.966 100.918 1.00 18.42 ? 93   GLY O C   1 
ATOM   16042 O  O   . GLY O  1 93  ? 55.901  111.680 101.565 1.00 17.99 ? 93   GLY O O   1 
ATOM   16043 N  N   . VAL O  1 94  ? 56.536  110.747 99.625  1.00 18.26 ? 94   VAL O N   1 
ATOM   16044 C  CA  . VAL O  1 94  ? 55.438  111.360 98.900  1.00 19.33 ? 94   VAL O CA  1 
ATOM   16045 C  C   . VAL O  1 94  ? 54.339  110.353 98.672  1.00 19.56 ? 94   VAL O C   1 
ATOM   16046 O  O   . VAL O  1 94  ? 54.590  109.226 98.229  1.00 19.42 ? 94   VAL O O   1 
ATOM   16047 C  CB  . VAL O  1 94  ? 55.898  111.893 97.545  1.00 19.87 ? 94   VAL O CB  1 
ATOM   16048 C  CG1 . VAL O  1 94  ? 54.712  112.487 96.779  1.00 19.69 ? 94   VAL O CG1 1 
ATOM   16049 C  CG2 . VAL O  1 94  ? 57.015  112.921 97.747  1.00 19.69 ? 94   VAL O CG2 1 
ATOM   16050 N  N   . ALA O  1 95  ? 53.123  110.775 98.982  1.00 19.39 ? 95   ALA O N   1 
ATOM   16051 C  CA  . ALA O  1 95  ? 51.950  109.988 98.769  1.00 20.33 ? 95   ALA O CA  1 
ATOM   16052 C  C   . ALA O  1 95  ? 51.111  110.644 97.676  1.00 21.63 ? 95   ALA O C   1 
ATOM   16053 O  O   . ALA O  1 95  ? 50.548  111.729 97.862  1.00 20.96 ? 95   ALA O O   1 
ATOM   16054 C  CB  . ALA O  1 95  ? 51.167  109.868 100.044 1.00 19.89 ? 95   ALA O CB  1 
ATOM   16055 N  N   . ASP O  1 96  ? 51.048  109.997 96.521  1.00 22.72 ? 96   ASP O N   1 
ATOM   16056 C  CA  . ASP O  1 96  ? 50.196  110.517 95.466  1.00 24.67 ? 96   ASP O CA  1 
ATOM   16057 C  C   . ASP O  1 96  ? 48.798  109.931 95.671  1.00 24.43 ? 96   ASP O C   1 
ATOM   16058 O  O   . ASP O  1 96  ? 48.614  108.726 95.691  1.00 24.25 ? 96   ASP O O   1 
ATOM   16059 C  CB  . ASP O  1 96  ? 50.816  110.274 94.082  1.00 25.41 ? 96   ASP O CB  1 
ATOM   16060 C  CG  . ASP O  1 96  ? 52.015  111.216 93.818  1.00 29.07 ? 96   ASP O CG  1 
ATOM   16061 O  OD1 . ASP O  1 96  ? 53.084  110.742 93.355  1.00 33.26 ? 96   ASP O OD1 1 
ATOM   16062 O  OD2 . ASP O  1 96  ? 51.987  112.450 94.074  1.00 31.61 ? 96   ASP O OD2 1 
ATOM   16063 N  N   . VAL O  1 97  ? 47.825  110.810 95.861  1.00 24.20 ? 97   VAL O N   1 
ATOM   16064 C  CA  . VAL O  1 97  ? 46.474  110.421 96.218  1.00 23.62 ? 97   VAL O CA  1 
ATOM   16065 C  C   . VAL O  1 97  ? 45.562  110.445 95.008  1.00 24.61 ? 97   VAL O C   1 
ATOM   16066 O  O   . VAL O  1 97  ? 45.560  111.401 94.230  1.00 24.20 ? 97   VAL O O   1 
ATOM   16067 C  CB  . VAL O  1 97  ? 45.929  111.356 97.324  1.00 23.82 ? 97   VAL O CB  1 
ATOM   16068 C  CG1 . VAL O  1 97  ? 44.449  111.068 97.638  1.00 23.53 ? 97   VAL O CG1 1 
ATOM   16069 C  CG2 . VAL O  1 97  ? 46.756  111.214 98.566  1.00 23.20 ? 97   VAL O CG2 1 
ATOM   16070 N  N   . SER O  1 98  ? 44.804  109.367 94.846  1.00 25.65 ? 98   SER O N   1 
ATOM   16071 C  CA  . SER O  1 98  ? 43.863  109.259 93.751  1.00 26.91 ? 98   SER O CA  1 
ATOM   16072 C  C   . SER O  1 98  ? 42.795  108.265 94.172  1.00 27.31 ? 98   SER O C   1 
ATOM   16073 O  O   . SER O  1 98  ? 42.978  107.041 94.102  1.00 27.12 ? 98   SER O O   1 
ATOM   16074 C  CB  . SER O  1 98  ? 44.567  108.807 92.475  1.00 27.34 ? 98   SER O CB  1 
ATOM   16075 O  OG  . SER O  1 98  ? 43.634  108.676 91.428  1.00 28.27 ? 98   SER O OG  1 
ATOM   16076 N  N   . ILE O  1 99  ? 41.689  108.813 94.649  1.00 27.73 ? 99   ILE O N   1 
ATOM   16077 C  CA  . ILE O  1 99  ? 40.598  108.012 95.137  1.00 28.61 ? 99   ILE O CA  1 
ATOM   16078 C  C   . ILE O  1 99  ? 39.355  108.446 94.411  1.00 29.10 ? 99   ILE O C   1 
ATOM   16079 O  O   . ILE O  1 99  ? 39.306  109.521 93.814  1.00 28.90 ? 99   ILE O O   1 
ATOM   16080 C  CB  . ILE O  1 99  ? 40.399  108.252 96.643  1.00 28.60 ? 99   ILE O CB  1 
ATOM   16081 C  CG1 . ILE O  1 99  ? 41.567  107.675 97.440  1.00 28.90 ? 99   ILE O CG1 1 
ATOM   16082 C  CG2 . ILE O  1 99  ? 39.103  107.628 97.128  1.00 28.98 ? 99   ILE O CG2 1 
ATOM   16083 C  CD1 . ILE O  1 99  ? 41.454  107.931 98.920  1.00 29.03 ? 99   ILE O CD1 1 
ATOM   16084 N  N   . GLU O  1 100 ? 38.356  107.577 94.441  1.00 29.32 ? 100  GLU O N   1 
ATOM   16085 C  CA  . GLU O  1 100 ? 37.041  107.932 93.973  1.00 29.15 ? 100  GLU O CA  1 
ATOM   16086 C  C   . GLU O  1 100 ? 36.128  107.393 95.061  1.00 28.85 ? 100  GLU O C   1 
ATOM   16087 O  O   . GLU O  1 100 ? 36.359  106.290 95.576  1.00 29.10 ? 100  GLU O O   1 
ATOM   16088 C  CB  . GLU O  1 100 ? 36.757  107.280 92.630  1.00 29.69 ? 100  GLU O CB  1 
ATOM   16089 C  CG  . GLU O  1 100 ? 35.303  107.333 92.248  1.00 31.19 ? 100  GLU O CG  1 
ATOM   16090 C  CD  . GLU O  1 100 ? 35.129  107.269 90.750  1.00 33.73 ? 100  GLU O CD  1 
ATOM   16091 O  OE1 . GLU O  1 100 ? 35.707  108.155 90.067  1.00 34.74 ? 100  GLU O OE1 1 
ATOM   16092 O  OE2 . GLU O  1 100 ? 34.434  106.347 90.274  1.00 31.24 ? 100  GLU O OE2 1 
ATOM   16093 N  N   . ASP O  1 101 ? 35.098  108.148 95.423  1.00 27.82 ? 101  ASP O N   1 
ATOM   16094 C  CA  . ASP O  1 101 ? 34.245  107.726 96.527  1.00 27.42 ? 101  ASP O CA  1 
ATOM   16095 C  C   . ASP O  1 101 ? 32.806  108.222 96.431  1.00 27.41 ? 101  ASP O C   1 
ATOM   16096 O  O   . ASP O  1 101 ? 32.556  109.416 96.234  1.00 27.32 ? 101  ASP O O   1 
ATOM   16097 C  CB  . ASP O  1 101 ? 34.863  108.181 97.850  1.00 27.38 ? 101  ASP O CB  1 
ATOM   16098 C  CG  . ASP O  1 101 ? 34.363  107.384 99.011  1.00 27.22 ? 101  ASP O CG  1 
ATOM   16099 O  OD1 . ASP O  1 101 ? 34.815  106.220 99.159  1.00 26.99 ? 101  ASP O OD1 1 
ATOM   16100 O  OD2 . ASP O  1 101 ? 33.511  107.826 99.808  1.00 24.96 ? 101  ASP O OD2 1 
ATOM   16101 N  N   . SER O  1 102 ? 31.862  107.295 96.597  1.00 27.24 ? 102  SER O N   1 
ATOM   16102 C  CA  . SER O  1 102 ? 30.443  107.635 96.504  1.00 26.98 ? 102  SER O CA  1 
ATOM   16103 C  C   . SER O  1 102 ? 29.710  107.741 97.843  1.00 26.13 ? 102  SER O C   1 
ATOM   16104 O  O   . SER O  1 102 ? 28.485  107.897 97.872  1.00 26.65 ? 102  SER O O   1 
ATOM   16105 C  CB  . SER O  1 102 ? 29.719  106.674 95.559  1.00 27.20 ? 102  SER O CB  1 
ATOM   16106 O  OG  . SER O  1 102 ? 29.632  107.265 94.273  1.00 29.21 ? 102  SER O OG  1 
ATOM   16107 N  N   . VAL O  1 103 ? 30.447  107.663 98.946  1.00 24.50 ? 103  VAL O N   1 
ATOM   16108 C  CA  . VAL O  1 103 ? 29.834  107.869 100.251 1.00 23.37 ? 103  VAL O CA  1 
ATOM   16109 C  C   . VAL O  1 103 ? 29.988  109.329 100.714 1.00 23.48 ? 103  VAL O C   1 
ATOM   16110 O  O   . VAL O  1 103 ? 29.051  109.921 101.229 1.00 23.06 ? 103  VAL O O   1 
ATOM   16111 C  CB  . VAL O  1 103 ? 30.384  106.907 101.278 1.00 23.20 ? 103  VAL O CB  1 
ATOM   16112 C  CG1 . VAL O  1 103 ? 29.676  107.110 102.605 1.00 21.56 ? 103  VAL O CG1 1 
ATOM   16113 C  CG2 . VAL O  1 103 ? 30.176  105.480 100.774 1.00 24.44 ? 103  VAL O CG2 1 
ATOM   16114 N  N   . ILE O  1 104 ? 31.177  109.903 100.556 1.00 23.61 ? 104  ILE O N   1 
ATOM   16115 C  CA  . ILE O  1 104 ? 31.339  111.315 100.849 1.00 23.87 ? 104  ILE O CA  1 
ATOM   16116 C  C   . ILE O  1 104 ? 30.655  112.045 99.715  1.00 24.69 ? 104  ILE O C   1 
ATOM   16117 O  O   . ILE O  1 104 ? 30.513  111.500 98.616  1.00 24.65 ? 104  ILE O O   1 
ATOM   16118 C  CB  . ILE O  1 104 ? 32.817  111.722 100.848 1.00 23.56 ? 104  ILE O CB  1 
ATOM   16119 C  CG1 . ILE O  1 104 ? 33.423  111.426 99.470  1.00 22.34 ? 104  ILE O CG1 1 
ATOM   16120 C  CG2 . ILE O  1 104 ? 33.567  111.051 102.002 1.00 23.48 ? 104  ILE O CG2 1 
ATOM   16121 C  CD1 . ILE O  1 104 ? 34.806  111.955 99.257  1.00 18.52 ? 104  ILE O CD1 1 
ATOM   16122 N  N   . SER O  1 105 ? 30.239  113.275 99.984  1.00 25.22 ? 105  SER O N   1 
ATOM   16123 C  CA  . SER O  1 105 ? 29.616  114.121 98.976  1.00 26.15 ? 105  SER O CA  1 
ATOM   16124 C  C   . SER O  1 105 ? 29.953  115.549 99.334  1.00 27.16 ? 105  SER O C   1 
ATOM   16125 O  O   . SER O  1 105 ? 30.386  115.827 100.451 1.00 27.16 ? 105  SER O O   1 
ATOM   16126 C  CB  . SER O  1 105 ? 28.102  113.928 98.945  1.00 25.86 ? 105  SER O CB  1 
ATOM   16127 O  OG  . SER O  1 105 ? 27.523  114.669 97.877  1.00 24.58 ? 105  SER O OG  1 
ATOM   16128 N  N   . LEU O  1 106 ? 29.770  116.451 98.381  1.00 28.46 ? 106  LEU O N   1 
ATOM   16129 C  CA  . LEU O  1 106 ? 30.033  117.860 98.606  1.00 29.49 ? 106  LEU O CA  1 
ATOM   16130 C  C   . LEU O  1 106 ? 28.696  118.590 98.656  1.00 30.66 ? 106  LEU O C   1 
ATOM   16131 O  O   . LEU O  1 106 ? 28.623  119.829 98.632  1.00 30.52 ? 106  LEU O O   1 
ATOM   16132 C  CB  . LEU O  1 106 ? 30.887  118.412 97.470  1.00 29.24 ? 106  LEU O CB  1 
ATOM   16133 C  CG  . LEU O  1 106 ? 32.097  117.571 97.069  1.00 29.39 ? 106  LEU O CG  1 
ATOM   16134 C  CD1 . LEU O  1 106 ? 32.876  118.278 95.954  1.00 29.24 ? 106  LEU O CD1 1 
ATOM   16135 C  CD2 . LEU O  1 106 ? 32.992  117.303 98.276  1.00 27.86 ? 106  LEU O CD2 1 
ATOM   16136 N  N   . SER O  1 107 ? 27.633  117.805 98.713  1.00 31.99 ? 107  SER O N   1 
ATOM   16137 C  CA  . SER O  1 107 ? 26.287  118.336 98.783  1.00 33.52 ? 107  SER O CA  1 
ATOM   16138 C  C   . SER O  1 107 ? 25.482  117.308 99.547  1.00 34.10 ? 107  SER O C   1 
ATOM   16139 O  O   . SER O  1 107 ? 25.780  116.117 99.476  1.00 34.60 ? 107  SER O O   1 
ATOM   16140 C  CB  . SER O  1 107 ? 25.705  118.504 97.377  1.00 33.63 ? 107  SER O CB  1 
ATOM   16141 O  OG  . SER O  1 107 ? 25.437  117.231 96.791  1.00 34.52 ? 107  SER O OG  1 
ATOM   16142 N  N   . GLY O  1 108 ? 24.484  117.768 100.298 1.00 34.60 ? 108  GLY O N   1 
ATOM   16143 C  CA  . GLY O  1 108 ? 23.596  116.865 101.010 1.00 34.62 ? 108  GLY O CA  1 
ATOM   16144 C  C   . GLY O  1 108 ? 23.954  116.477 102.436 1.00 34.64 ? 108  GLY O C   1 
ATOM   16145 O  O   . GLY O  1 108 ? 24.753  117.130 103.113 1.00 34.81 ? 108  GLY O O   1 
ATOM   16146 N  N   . ASP O  1 109 ? 23.330  115.391 102.881 1.00 34.28 ? 109  ASP O N   1 
ATOM   16147 C  CA  . ASP O  1 109 ? 23.503  114.833 104.213 1.00 33.96 ? 109  ASP O CA  1 
ATOM   16148 C  C   . ASP O  1 109 ? 24.945  114.502 104.494 1.00 33.26 ? 109  ASP O C   1 
ATOM   16149 O  O   . ASP O  1 109 ? 25.424  114.599 105.628 1.00 33.30 ? 109  ASP O O   1 
ATOM   16150 C  CB  . ASP O  1 109 ? 22.744  113.515 104.289 1.00 34.34 ? 109  ASP O CB  1 
ATOM   16151 C  CG  . ASP O  1 109 ? 22.010  113.345 105.589 1.00 36.18 ? 109  ASP O CG  1 
ATOM   16152 O  OD1 . ASP O  1 109 ? 21.097  114.172 105.843 1.00 38.06 ? 109  ASP O OD1 1 
ATOM   16153 O  OD2 . ASP O  1 109 ? 22.265  112.417 106.401 1.00 36.22 ? 109  ASP O OD2 1 
ATOM   16154 N  N   . HIS O  1 110 ? 25.621  114.058 103.448 1.00 32.00 ? 110  HIS O N   1 
ATOM   16155 C  CA  . HIS O  1 110 ? 26.986  113.601 103.573 1.00 30.74 ? 110  HIS O CA  1 
ATOM   16156 C  C   . HIS O  1 110 ? 27.994  114.633 103.093 1.00 29.66 ? 110  HIS O C   1 
ATOM   16157 O  O   . HIS O  1 110 ? 29.066  114.286 102.589 1.00 29.57 ? 110  HIS O O   1 
ATOM   16158 C  CB  . HIS O  1 110 ? 27.131  112.283 102.826 1.00 30.84 ? 110  HIS O CB  1 
ATOM   16159 C  CG  . HIS O  1 110 ? 26.346  111.168 103.444 1.00 31.80 ? 110  HIS O CG  1 
ATOM   16160 N  ND1 . HIS O  1 110 ? 26.225  109.923 102.864 1.00 31.15 ? 110  HIS O ND1 1 
ATOM   16161 C  CD2 . HIS O  1 110 ? 25.650  111.112 104.605 1.00 32.29 ? 110  HIS O CD2 1 
ATOM   16162 C  CE1 . HIS O  1 110 ? 25.491  109.150 103.643 1.00 32.10 ? 110  HIS O CE1 1 
ATOM   16163 N  NE2 . HIS O  1 110 ? 25.131  109.847 104.706 1.00 31.72 ? 110  HIS O NE2 1 
ATOM   16164 N  N   . CYS O  1 111 ? 27.654  115.905 103.268 1.00 28.28 ? 111  CYS O N   1 
ATOM   16165 C  CA  . CYS O  1 111 ? 28.556  116.958 102.850 1.00 26.50 ? 111  CYS O CA  1 
ATOM   16166 C  C   . CYS O  1 111 ? 29.824  117.010 103.701 1.00 25.26 ? 111  CYS O C   1 
ATOM   16167 O  O   . CYS O  1 111 ? 29.756  116.997 104.931 1.00 25.36 ? 111  CYS O O   1 
ATOM   16168 C  CB  . CYS O  1 111 ? 27.870  118.306 102.869 1.00 26.95 ? 111  CYS O CB  1 
ATOM   16169 S  SG  . CYS O  1 111 ? 28.829  119.425 101.870 1.00 28.62 ? 111  CYS O SG  1 
ATOM   16170 N  N   . ILE O  1 112 ? 30.982  117.040 103.041 1.00 23.04 ? 112  ILE O N   1 
ATOM   16171 C  CA  . ILE O  1 112 ? 32.261  117.124 103.750 1.00 21.34 ? 112  ILE O CA  1 
ATOM   16172 C  C   . ILE O  1 112 ? 32.863  118.538 103.714 1.00 20.78 ? 112  ILE O C   1 
ATOM   16173 O  O   . ILE O  1 112 ? 33.893  118.793 104.325 1.00 20.22 ? 112  ILE O O   1 
ATOM   16174 C  CB  . ILE O  1 112 ? 33.286  116.081 103.244 1.00 21.84 ? 112  ILE O CB  1 
ATOM   16175 C  CG1 . ILE O  1 112 ? 33.730  116.390 101.814 1.00 21.10 ? 112  ILE O CG1 1 
ATOM   16176 C  CG2 . ILE O  1 112 ? 32.721  114.663 103.350 1.00 21.06 ? 112  ILE O CG2 1 
ATOM   16177 C  CD1 . ILE O  1 112 ? 34.760  115.402 101.316 1.00 18.20 ? 112  ILE O CD1 1 
ATOM   16178 N  N   . ILE O  1 113 ? 32.204  119.469 103.026 1.00 19.84 ? 113  ILE O N   1 
ATOM   16179 C  CA  . ILE O  1 113 ? 32.695  120.840 102.989 1.00 19.16 ? 113  ILE O CA  1 
ATOM   16180 C  C   . ILE O  1 113 ? 32.619  121.426 104.394 1.00 18.39 ? 113  ILE O C   1 
ATOM   16181 O  O   . ILE O  1 113 ? 31.603  121.268 105.087 1.00 17.98 ? 113  ILE O O   1 
ATOM   16182 C  CB  . ILE O  1 113 ? 31.817  121.694 102.060 1.00 19.90 ? 113  ILE O CB  1 
ATOM   16183 C  CG1 . ILE O  1 113 ? 31.896  121.183 100.632 1.00 20.56 ? 113  ILE O CG1 1 
ATOM   16184 C  CG2 . ILE O  1 113 ? 32.277  123.155 102.086 1.00 20.02 ? 113  ILE O CG2 1 
ATOM   16185 C  CD1 . ILE O  1 113 ? 33.267  121.308 100.059 1.00 23.53 ? 113  ILE O CD1 1 
ATOM   16186 N  N   . GLY O  1 114 ? 33.672  122.114 104.825 1.00 17.18 ? 114  GLY O N   1 
ATOM   16187 C  CA  . GLY O  1 114 ? 33.640  122.735 106.132 1.00 16.81 ? 114  GLY O CA  1 
ATOM   16188 C  C   . GLY O  1 114 ? 34.099  121.813 107.232 1.00 16.83 ? 114  GLY O C   1 
ATOM   16189 O  O   . GLY O  1 114 ? 34.059  122.149 108.413 1.00 16.47 ? 114  GLY O O   1 
ATOM   16190 N  N   . ARG O  1 115 ? 34.532  120.623 106.844 1.00 16.72 ? 115  ARG O N   1 
ATOM   16191 C  CA  . ARG O  1 115 ? 35.000  119.688 107.834 1.00 15.96 ? 115  ARG O CA  1 
ATOM   16192 C  C   . ARG O  1 115 ? 36.519  119.576 107.663 1.00 17.04 ? 115  ARG O C   1 
ATOM   16193 O  O   . ARG O  1 115 ? 37.113  120.274 106.830 1.00 17.36 ? 115  ARG O O   1 
ATOM   16194 C  CB  . ARG O  1 115 ? 34.258  118.350 107.692 1.00 16.19 ? 115  ARG O CB  1 
ATOM   16195 C  CG  . ARG O  1 115 ? 32.718  118.510 107.897 1.00 16.95 ? 115  ARG O CG  1 
ATOM   16196 C  CD  . ARG O  1 115 ? 31.933  117.176 108.092 1.00 18.79 ? 115  ARG O CD  1 
ATOM   16197 N  NE  . ARG O  1 115 ? 30.486  117.405 108.053 1.00 18.52 ? 115  ARG O NE  1 
ATOM   16198 C  CZ  . ARG O  1 115 ? 29.724  117.669 109.115 1.00 19.96 ? 115  ARG O CZ  1 
ATOM   16199 N  NH1 . ARG O  1 115 ? 30.249  117.725 110.332 1.00 21.38 ? 115  ARG O NH1 1 
ATOM   16200 N  NH2 . ARG O  1 115 ? 28.416  117.847 108.960 1.00 20.24 ? 115  ARG O NH2 1 
ATOM   16201 N  N   . THR O  1 116 ? 37.148  118.712 108.445 1.00 16.76 ? 116  THR O N   1 
ATOM   16202 C  CA  . THR O  1 116 ? 38.594  118.600 108.410 1.00 17.21 ? 116  THR O CA  1 
ATOM   16203 C  C   . THR O  1 116 ? 39.093  117.281 107.827 1.00 17.53 ? 116  THR O C   1 
ATOM   16204 O  O   . THR O  1 116 ? 38.685  116.196 108.261 1.00 17.84 ? 116  THR O O   1 
ATOM   16205 C  CB  . THR O  1 116 ? 39.136  118.715 109.830 1.00 17.30 ? 116  THR O CB  1 
ATOM   16206 O  OG1 . THR O  1 116 ? 38.967  120.056 110.290 1.00 18.90 ? 116  THR O OG1 1 
ATOM   16207 C  CG2 . THR O  1 116 ? 40.640  118.525 109.828 1.00 18.35 ? 116  THR O CG2 1 
ATOM   16208 N  N   . LEU O  1 117 ? 39.985  117.376 106.858 1.00 16.67 ? 117  LEU O N   1 
ATOM   16209 C  CA  . LEU O  1 117 ? 40.643  116.187 106.345 1.00 16.27 ? 117  LEU O CA  1 
ATOM   16210 C  C   . LEU O  1 117 ? 41.909  115.998 107.163 1.00 15.95 ? 117  LEU O C   1 
ATOM   16211 O  O   . LEU O  1 117 ? 42.669  116.972 107.371 1.00 15.35 ? 117  LEU O O   1 
ATOM   16212 C  CB  . LEU O  1 117 ? 40.990  116.388 104.876 1.00 16.49 ? 117  LEU O CB  1 
ATOM   16213 C  CG  . LEU O  1 117 ? 41.607  115.206 104.119 1.00 17.62 ? 117  LEU O CG  1 
ATOM   16214 C  CD1 . LEU O  1 117 ? 40.622  114.047 103.920 1.00 19.86 ? 117  LEU O CD1 1 
ATOM   16215 C  CD2 . LEU O  1 117 ? 42.063  115.693 102.739 1.00 20.18 ? 117  LEU O CD2 1 
ATOM   16216 N  N   . VAL O  1 118 ? 42.158  114.764 107.621 1.00 15.99 ? 118  VAL O N   1 
ATOM   16217 C  CA  . VAL O  1 118 ? 43.345  114.463 108.448 1.00 15.50 ? 118  VAL O CA  1 
ATOM   16218 C  C   . VAL O  1 118 ? 44.191  113.325 107.827 1.00 15.34 ? 118  VAL O C   1 
ATOM   16219 O  O   . VAL O  1 118 ? 43.635  112.325 107.344 1.00 16.78 ? 118  VAL O O   1 
ATOM   16220 C  CB  . VAL O  1 118 ? 42.897  114.053 109.895 1.00 15.48 ? 118  VAL O CB  1 
ATOM   16221 C  CG1 . VAL O  1 118 ? 44.075  113.693 110.810 1.00 16.67 ? 118  VAL O CG1 1 
ATOM   16222 C  CG2 . VAL O  1 118 ? 42.005  115.120 110.508 1.00 16.17 ? 118  VAL O CG2 1 
ATOM   16223 N  N   . VAL O  1 119 ? 45.515  113.475 107.790 1.00 15.04 ? 119  VAL O N   1 
ATOM   16224 C  CA  . VAL O  1 119 ? 46.386  112.350 107.389 1.00 15.02 ? 119  VAL O CA  1 
ATOM   16225 C  C   . VAL O  1 119 ? 47.076  111.912 108.677 1.00 15.33 ? 119  VAL O C   1 
ATOM   16226 O  O   . VAL O  1 119 ? 47.536  112.749 109.462 1.00 15.36 ? 119  VAL O O   1 
ATOM   16227 C  CB  . VAL O  1 119 ? 47.383  112.696 106.252 1.00 15.93 ? 119  VAL O CB  1 
ATOM   16228 C  CG1 . VAL O  1 119 ? 48.311  113.855 106.642 1.00 17.27 ? 119  VAL O CG1 1 
ATOM   16229 C  CG2 . VAL O  1 119 ? 48.220  111.448 105.846 1.00 15.36 ? 119  VAL O CG2 1 
ATOM   16230 N  N   . HIS O  1 120 ? 47.153  110.600 108.899 1.00 15.85 ? 120  HIS O N   1 
ATOM   16231 C  CA  . HIS O  1 120 ? 47.594  110.045 110.184 1.00 16.24 ? 120  HIS O CA  1 
ATOM   16232 C  C   . HIS O  1 120 ? 49.012  109.457 110.224 1.00 17.02 ? 120  HIS O C   1 
ATOM   16233 O  O   . HIS O  1 120 ? 49.646  109.231 109.193 1.00 16.09 ? 120  HIS O O   1 
ATOM   16234 C  CB  . HIS O  1 120 ? 46.602  108.950 110.641 1.00 15.26 ? 120  HIS O CB  1 
ATOM   16235 C  CG  . HIS O  1 120 ? 45.341  109.486 111.250 1.00 16.82 ? 120  HIS O CG  1 
ATOM   16236 N  ND1 . HIS O  1 120 ? 45.227  109.769 112.594 1.00 17.10 ? 120  HIS O ND1 1 
ATOM   16237 C  CD2 . HIS O  1 120 ? 44.126  109.761 110.706 1.00 15.21 ? 120  HIS O CD2 1 
ATOM   16238 C  CE1 . HIS O  1 120 ? 44.004  110.202 112.851 1.00 18.83 ? 120  HIS O CE1 1 
ATOM   16239 N  NE2 . HIS O  1 120 ? 43.322  110.215 111.722 1.00 18.84 ? 120  HIS O NE2 1 
ATOM   16240 N  N   . GLU O  1 121 ? 49.484  109.274 111.450 1.00 17.12 ? 121  GLU O N   1 
ATOM   16241 C  CA  . GLU O  1 121 ? 50.792  108.736 111.757 1.00 19.06 ? 121  GLU O CA  1 
ATOM   16242 C  C   . GLU O  1 121 ? 50.954  107.296 111.236 1.00 19.07 ? 121  GLU O C   1 
ATOM   16243 O  O   . GLU O  1 121 ? 51.973  106.956 110.634 1.00 18.67 ? 121  GLU O O   1 
ATOM   16244 C  CB  . GLU O  1 121 ? 50.957  108.808 113.289 1.00 19.88 ? 121  GLU O CB  1 
ATOM   16245 C  CG  . GLU O  1 121 ? 52.097  108.013 113.919 1.00 24.64 ? 121  GLU O CG  1 
ATOM   16246 C  CD  . GLU O  1 121 ? 51.980  107.870 115.451 1.00 29.46 ? 121  GLU O CD  1 
ATOM   16247 O  OE1 . GLU O  1 121 ? 53.040  107.859 116.131 1.00 32.60 ? 121  GLU O OE1 1 
ATOM   16248 O  OE2 . GLU O  1 121 ? 50.846  107.761 115.991 1.00 26.36 ? 121  GLU O OE2 1 
ATOM   16249 N  N   . LYS O  1 122 ? 49.931  106.461 111.445 1.00 19.68 ? 122  LYS O N   1 
ATOM   16250 C  CA  . LYS O  1 122 ? 50.037  105.044 111.110 1.00 20.49 ? 122  LYS O CA  1 
ATOM   16251 C  C   . LYS O  1 122 ? 48.962  104.609 110.160 1.00 20.63 ? 122  LYS O C   1 
ATOM   16252 O  O   . LYS O  1 122 ? 48.049  105.377 109.840 1.00 20.60 ? 122  LYS O O   1 
ATOM   16253 C  CB  . LYS O  1 122 ? 49.858  104.170 112.351 1.00 20.69 ? 122  LYS O CB  1 
ATOM   16254 C  CG  . LYS O  1 122 ? 50.576  104.637 113.574 1.00 22.60 ? 122  LYS O CG  1 
ATOM   16255 C  CD  . LYS O  1 122 ? 50.193  103.820 114.787 1.00 26.05 ? 122  LYS O CD  1 
ATOM   16256 C  CE  . LYS O  1 122 ? 50.770  104.462 116.041 1.00 30.82 ? 122  LYS O CE  1 
ATOM   16257 N  NZ  . LYS O  1 122 ? 50.494  103.689 117.297 1.00 33.90 ? 122  LYS O NZ  1 
ATOM   16258 N  N   . ALA O  1 123 ? 49.038  103.332 109.789 1.00 19.88 ? 123  ALA O N   1 
ATOM   16259 C  CA  . ALA O  1 123 ? 48.031  102.755 108.925 1.00 20.21 ? 123  ALA O CA  1 
ATOM   16260 C  C   . ALA O  1 123 ? 46.678  102.637 109.648 1.00 20.14 ? 123  ALA O C   1 
ATOM   16261 O  O   . ALA O  1 123 ? 46.617  102.464 110.882 1.00 20.84 ? 123  ALA O O   1 
ATOM   16262 C  CB  . ALA O  1 123 ? 48.507  101.381 108.397 1.00 20.64 ? 123  ALA O CB  1 
ATOM   16263 N  N   . ASP O  1 124 ? 45.604  102.791 108.872 1.00 18.79 ? 124  ASP O N   1 
ATOM   16264 C  CA  . ASP O  1 124 ? 44.243  102.581 109.330 1.00 18.26 ? 124  ASP O CA  1 
ATOM   16265 C  C   . ASP O  1 124 ? 44.025  101.067 109.195 1.00 17.93 ? 124  ASP O C   1 
ATOM   16266 O  O   . ASP O  1 124 ? 44.241  100.545 108.121 1.00 18.20 ? 124  ASP O O   1 
ATOM   16267 C  CB  . ASP O  1 124 ? 43.307  103.298 108.355 1.00 17.60 ? 124  ASP O CB  1 
ATOM   16268 C  CG  . ASP O  1 124 ? 41.839  103.224 108.747 1.00 18.61 ? 124  ASP O CG  1 
ATOM   16269 O  OD1 . ASP O  1 124 ? 41.355  102.171 109.247 1.00 19.46 ? 124  ASP O OD1 1 
ATOM   16270 O  OD2 . ASP O  1 124 ? 41.063  104.196 108.554 1.00 17.62 ? 124  ASP O OD2 1 
ATOM   16271 N  N   . ASP O  1 125 ? 43.618  100.368 110.250 1.00 17.40 ? 125  ASP O N   1 
ATOM   16272 C  CA  . ASP O  1 125 ? 43.383  98.916  110.114 1.00 17.80 ? 125  ASP O CA  1 
ATOM   16273 C  C   . ASP O  1 125 ? 42.015  98.555  109.520 1.00 17.77 ? 125  ASP O C   1 
ATOM   16274 O  O   . ASP O  1 125 ? 41.607  97.387  109.498 1.00 18.17 ? 125  ASP O O   1 
ATOM   16275 C  CB  . ASP O  1 125 ? 43.652  98.150  111.414 1.00 17.52 ? 125  ASP O CB  1 
ATOM   16276 C  CG  . ASP O  1 125 ? 42.757  98.570  112.549 1.00 17.99 ? 125  ASP O CG  1 
ATOM   16277 O  OD1 . ASP O  1 125 ? 41.611  99.042  112.305 1.00 15.74 ? 125  ASP O OD1 1 
ATOM   16278 O  OD2 . ASP O  1 125 ? 43.135  98.453  113.746 1.00 15.51 ? 125  ASP O OD2 1 
ATOM   16279 N  N   . LEU O  1 126 ? 41.311  99.568  109.063 1.00 18.17 ? 126  LEU O N   1 
ATOM   16280 C  CA  . LEU O  1 126 ? 40.031  99.393  108.396 1.00 19.03 ? 126  LEU O CA  1 
ATOM   16281 C  C   . LEU O  1 126 ? 38.953  98.802  109.330 1.00 19.55 ? 126  LEU O C   1 
ATOM   16282 O  O   . LEU O  1 126 ? 37.937  98.272  108.870 1.00 18.74 ? 126  LEU O O   1 
ATOM   16283 C  CB  . LEU O  1 126 ? 40.221  98.576  107.101 1.00 18.83 ? 126  LEU O CB  1 
ATOM   16284 C  CG  . LEU O  1 126 ? 41.397  99.090  106.229 1.00 19.59 ? 126  LEU O CG  1 
ATOM   16285 C  CD1 . LEU O  1 126 ? 41.511  98.292  104.918 1.00 21.61 ? 126  LEU O CD1 1 
ATOM   16286 C  CD2 . LEU O  1 126 ? 41.327  100.637 105.922 1.00 16.77 ? 126  LEU O CD2 1 
ATOM   16287 N  N   . GLY O  1 127 ? 39.187  98.913  110.639 1.00 19.92 ? 127  GLY O N   1 
ATOM   16288 C  CA  . GLY O  1 127 ? 38.200  98.498  111.623 1.00 21.49 ? 127  GLY O CA  1 
ATOM   16289 C  C   . GLY O  1 127 ? 38.195  97.019  111.956 1.00 21.53 ? 127  GLY O C   1 
ATOM   16290 O  O   . GLY O  1 127 ? 37.223  96.490  112.503 1.00 21.84 ? 127  GLY O O   1 
ATOM   16291 N  N   . LYS O  1 128 ? 39.279  96.331  111.645 1.00 22.14 ? 128  LYS O N   1 
ATOM   16292 C  CA  . LYS O  1 128 ? 39.319  94.910  111.957 1.00 22.76 ? 128  LYS O CA  1 
ATOM   16293 C  C   . LYS O  1 128 ? 40.568  94.509  112.684 1.00 22.97 ? 128  LYS O C   1 
ATOM   16294 O  O   . LYS O  1 128 ? 41.046  93.383  112.527 1.00 22.33 ? 128  LYS O O   1 
ATOM   16295 C  CB  . LYS O  1 128 ? 39.138  94.051  110.716 1.00 22.99 ? 128  LYS O CB  1 
ATOM   16296 C  CG  . LYS O  1 128 ? 39.449  94.733  109.436 1.00 25.10 ? 128  LYS O CG  1 
ATOM   16297 C  CD  . LYS O  1 128 ? 40.803  94.316  108.895 1.00 29.90 ? 128  LYS O CD  1 
ATOM   16298 C  CE  . LYS O  1 128 ? 41.967  94.988  109.607 1.00 30.15 ? 128  LYS O CE  1 
ATOM   16299 N  NZ  . LYS O  1 128 ? 43.238  94.744  108.884 1.00 27.95 ? 128  LYS O NZ  1 
ATOM   16300 N  N   . GLY O  1 129 ? 41.084  95.426  113.499 1.00 22.78 ? 129  GLY O N   1 
ATOM   16301 C  CA  . GLY O  1 129 ? 42.254  95.156  114.310 1.00 23.50 ? 129  GLY O CA  1 
ATOM   16302 C  C   . GLY O  1 129 ? 41.931  94.374  115.575 1.00 24.25 ? 129  GLY O C   1 
ATOM   16303 O  O   . GLY O  1 129 ? 42.833  94.052  116.346 1.00 24.53 ? 129  GLY O O   1 
ATOM   16304 N  N   . GLY O  1 130 ? 40.650  94.089  115.798 1.00 24.55 ? 130  GLY O N   1 
ATOM   16305 C  CA  . GLY O  1 130 ? 40.220  93.297  116.942 1.00 25.23 ? 130  GLY O CA  1 
ATOM   16306 C  C   . GLY O  1 130 ? 40.031  93.993  118.289 1.00 25.85 ? 130  GLY O C   1 
ATOM   16307 O  O   . GLY O  1 130 ? 39.755  93.334  119.284 1.00 25.27 ? 130  GLY O O   1 
ATOM   16308 N  N   . ASN O  1 131 ? 40.164  95.312  118.337 1.00 26.21 ? 131  ASN O N   1 
ATOM   16309 C  CA  . ASN O  1 131 ? 40.030  96.032  119.602 1.00 26.99 ? 131  ASN O CA  1 
ATOM   16310 C  C   . ASN O  1 131 ? 39.052  97.181  119.485 1.00 27.30 ? 131  ASN O C   1 
ATOM   16311 O  O   . ASN O  1 131 ? 38.626  97.528  118.386 1.00 27.57 ? 131  ASN O O   1 
ATOM   16312 C  CB  . ASN O  1 131 ? 41.385  96.543  120.086 1.00 27.19 ? 131  ASN O CB  1 
ATOM   16313 C  CG  . ASN O  1 131 ? 41.989  97.593  119.155 1.00 28.80 ? 131  ASN O CG  1 
ATOM   16314 O  OD1 . ASN O  1 131 ? 41.356  98.074  118.210 1.00 27.02 ? 131  ASN O OD1 1 
ATOM   16315 N  ND2 . ASN O  1 131 ? 43.222  97.969  119.444 1.00 34.46 ? 131  ASN O ND2 1 
ATOM   16316 N  N   . GLU O  1 132 ? 38.700  97.796  120.608 1.00 27.45 ? 132  GLU O N   1 
ATOM   16317 C  CA  . GLU O  1 132 ? 37.707  98.851  120.551 1.00 27.59 ? 132  GLU O CA  1 
ATOM   16318 C  C   . GLU O  1 132 ? 38.218  100.040 119.723 1.00 26.35 ? 132  GLU O C   1 
ATOM   16319 O  O   . GLU O  1 132 ? 37.519  100.570 118.859 1.00 25.50 ? 132  GLU O O   1 
ATOM   16320 C  CB  . GLU O  1 132 ? 37.264  99.264  121.962 1.00 28.64 ? 132  GLU O CB  1 
ATOM   16321 C  CG  . GLU O  1 132 ? 38.080  100.378 122.603 1.00 32.60 ? 132  GLU O CG  1 
ATOM   16322 C  CD  . GLU O  1 132 ? 37.693  100.636 124.047 1.00 38.57 ? 132  GLU O CD  1 
ATOM   16323 O  OE1 . GLU O  1 132 ? 36.473  100.645 124.365 1.00 40.90 ? 132  GLU O OE1 1 
ATOM   16324 O  OE2 . GLU O  1 132 ? 38.618  100.832 124.867 1.00 41.47 ? 132  GLU O OE2 1 
ATOM   16325 N  N   . GLU O  1 133 ? 39.463  100.422 119.948 1.00 25.44 ? 133  GLU O N   1 
ATOM   16326 C  CA  . GLU O  1 133 ? 40.005  101.570 119.233 1.00 25.07 ? 133  GLU O CA  1 
ATOM   16327 C  C   . GLU O  1 133 ? 39.839  101.383 117.724 1.00 24.41 ? 133  GLU O C   1 
ATOM   16328 O  O   . GLU O  1 133 ? 39.629  102.344 116.979 1.00 23.40 ? 133  GLU O O   1 
ATOM   16329 C  CB  . GLU O  1 133 ? 41.469  101.763 119.603 1.00 25.05 ? 133  GLU O CB  1 
ATOM   16330 C  CG  . GLU O  1 133 ? 42.091  103.031 119.052 1.00 26.19 ? 133  GLU O CG  1 
ATOM   16331 C  CD  . GLU O  1 133 ? 41.447  104.285 119.634 1.00 27.48 ? 133  GLU O CD  1 
ATOM   16332 O  OE1 . GLU O  1 133 ? 41.260  104.352 120.877 1.00 27.68 ? 133  GLU O OE1 1 
ATOM   16333 O  OE2 . GLU O  1 133 ? 41.120  105.182 118.837 1.00 26.45 ? 133  GLU O OE2 1 
ATOM   16334 N  N   . SER O  1 134 ? 39.923  100.136 117.279 1.00 23.67 ? 134  SER O N   1 
ATOM   16335 C  CA  . SER O  1 134 ? 39.799  99.854  115.860 1.00 23.26 ? 134  SER O CA  1 
ATOM   16336 C  C   . SER O  1 134 ? 38.442  100.262 115.307 1.00 22.87 ? 134  SER O C   1 
ATOM   16337 O  O   . SER O  1 134 ? 38.345  100.773 114.193 1.00 22.89 ? 134  SER O O   1 
ATOM   16338 C  CB  . SER O  1 134 ? 40.035  98.370  115.590 1.00 22.96 ? 134  SER O CB  1 
ATOM   16339 O  OG  . SER O  1 134 ? 39.775  98.079  114.229 1.00 23.43 ? 134  SER O OG  1 
ATOM   16340 N  N   . THR O  1 135 ? 37.398  100.047 116.092 1.00 22.48 ? 135  THR O N   1 
ATOM   16341 C  CA  . THR O  1 135 ? 36.026  100.327 115.661 1.00 23.19 ? 135  THR O CA  1 
ATOM   16342 C  C   . THR O  1 135 ? 35.715  101.813 115.500 1.00 22.73 ? 135  THR O C   1 
ATOM   16343 O  O   . THR O  1 135 ? 34.612  102.204 115.080 1.00 22.06 ? 135  THR O O   1 
ATOM   16344 C  CB  . THR O  1 135 ? 35.060  99.725  116.677 1.00 23.40 ? 135  THR O CB  1 
ATOM   16345 O  OG1 . THR O  1 135 ? 35.293  100.343 117.950 1.00 25.10 ? 135  THR O OG1 1 
ATOM   16346 C  CG2 . THR O  1 135 ? 35.408  98.279  116.917 1.00 24.17 ? 135  THR O CG2 1 
ATOM   16347 N  N   . LYS O  1 136 ? 36.676  102.654 115.838 1.00 23.00 ? 136  LYS O N   1 
ATOM   16348 C  CA  . LYS O  1 136 ? 36.411  104.091 115.712 1.00 23.77 ? 136  LYS O CA  1 
ATOM   16349 C  C   . LYS O  1 136 ? 37.386  104.883 114.843 1.00 22.88 ? 136  LYS O C   1 
ATOM   16350 O  O   . LYS O  1 136 ? 36.967  105.801 114.080 1.00 22.16 ? 136  LYS O O   1 
ATOM   16351 C  CB  . LYS O  1 136 ? 36.301  104.739 117.096 1.00 24.76 ? 136  LYS O CB  1 
ATOM   16352 C  CG  . LYS O  1 136 ? 37.075  104.046 118.193 1.00 26.99 ? 136  LYS O CG  1 
ATOM   16353 C  CD  . LYS O  1 136 ? 37.185  104.975 119.384 1.00 31.15 ? 136  LYS O CD  1 
ATOM   16354 C  CE  . LYS O  1 136 ? 37.010  104.240 120.699 1.00 32.76 ? 136  LYS O CE  1 
ATOM   16355 N  NZ  . LYS O  1 136 ? 37.296  105.156 121.848 1.00 35.43 ? 136  LYS O NZ  1 
ATOM   16356 N  N   . THR O  1 137 ? 38.671  104.539 114.981 1.00 21.72 ? 137  THR O N   1 
ATOM   16357 C  CA  . THR O  1 137 ? 39.760  105.226 114.289 1.00 21.24 ? 137  THR O CA  1 
ATOM   16358 C  C   . THR O  1 137 ? 40.624  104.337 113.423 1.00 19.88 ? 137  THR O C   1 
ATOM   16359 O  O   . THR O  1 137 ? 41.539  104.835 112.748 1.00 19.31 ? 137  THR O O   1 
ATOM   16360 C  CB  . THR O  1 137 ? 40.738  105.933 115.295 1.00 21.56 ? 137  THR O CB  1 
ATOM   16361 O  OG1 . THR O  1 137 ? 41.426  104.946 116.092 1.00 21.46 ? 137  THR O OG1 1 
ATOM   16362 C  CG2 . THR O  1 137 ? 39.987  106.807 116.297 1.00 23.11 ? 137  THR O CG2 1 
ATOM   16363 N  N   . GLY O  1 138 ? 40.412  103.026 113.475 1.00 18.94 ? 138  GLY O N   1 
ATOM   16364 C  CA  . GLY O  1 138 ? 41.279  102.163 112.705 1.00 17.41 ? 138  GLY O CA  1 
ATOM   16365 C  C   . GLY O  1 138 ? 42.687  102.090 113.276 1.00 17.40 ? 138  GLY O C   1 
ATOM   16366 O  O   . GLY O  1 138 ? 43.591  101.500 112.669 1.00 17.22 ? 138  GLY O O   1 
ATOM   16367 N  N   . ASN O  1 139 ? 42.875  102.621 114.478 1.00 16.68 ? 139  ASN O N   1 
ATOM   16368 C  CA  . ASN O  1 139 ? 44.185  102.570 115.123 1.00 17.11 ? 139  ASN O CA  1 
ATOM   16369 C  C   . ASN O  1 139 ? 45.253  103.322 114.339 1.00 17.49 ? 139  ASN O C   1 
ATOM   16370 O  O   . ASN O  1 139 ? 46.432  102.951 114.356 1.00 18.57 ? 139  ASN O O   1 
ATOM   16371 C  CB  . ASN O  1 139 ? 44.629  101.123 115.302 1.00 17.29 ? 139  ASN O CB  1 
ATOM   16372 C  CG  . ASN O  1 139 ? 44.026  100.481 116.535 1.00 18.87 ? 139  ASN O CG  1 
ATOM   16373 O  OD1 . ASN O  1 139 ? 44.228  100.961 117.658 1.00 18.17 ? 139  ASN O OD1 1 
ATOM   16374 N  ND2 . ASN O  1 139 ? 43.294  99.379  116.337 1.00 18.89 ? 139  ASN O ND2 1 
ATOM   16375 N  N   . ALA O  1 140 ? 44.831  104.374 113.648 1.00 17.18 ? 140  ALA O N   1 
ATOM   16376 C  CA  . ALA O  1 140 ? 45.741  105.141 112.793 1.00 17.96 ? 140  ALA O CA  1 
ATOM   16377 C  C   . ALA O  1 140 ? 46.689  106.086 113.532 1.00 18.13 ? 140  ALA O C   1 
ATOM   16378 O  O   . ALA O  1 140 ? 47.563  106.723 112.927 1.00 18.41 ? 140  ALA O O   1 
ATOM   16379 C  CB  . ALA O  1 140 ? 44.968  105.863 111.720 1.00 17.71 ? 140  ALA O CB  1 
ATOM   16380 N  N   . GLY O  1 141 ? 46.562  106.153 114.848 1.00 18.56 ? 141  GLY O N   1 
ATOM   16381 C  CA  . GLY O  1 141 ? 47.479  106.975 115.623 1.00 18.43 ? 141  GLY O CA  1 
ATOM   16382 C  C   . GLY O  1 141 ? 47.284  108.482 115.465 1.00 18.90 ? 141  GLY O C   1 
ATOM   16383 O  O   . GLY O  1 141 ? 46.197  108.975 115.137 1.00 18.58 ? 141  GLY O O   1 
ATOM   16384 N  N   . SER O  1 142 ? 48.368  109.217 115.696 1.00 18.55 ? 142  SER O N   1 
ATOM   16385 C  CA  . SER O  1 142 ? 48.319  110.682 115.744 1.00 18.98 ? 142  SER O CA  1 
ATOM   16386 C  C   . SER O  1 142 ? 47.980  111.348 114.402 1.00 19.05 ? 142  SER O C   1 
ATOM   16387 O  O   . SER O  1 142 ? 48.003  110.708 113.344 1.00 19.05 ? 142  SER O O   1 
ATOM   16388 C  CB  . SER O  1 142 ? 49.636  111.220 116.295 1.00 19.20 ? 142  SER O CB  1 
ATOM   16389 O  OG  . SER O  1 142 ? 50.585  111.333 115.250 1.00 21.14 ? 142  SER O OG  1 
ATOM   16390 N  N   . ARG O  1 143 ? 47.598  112.620 114.482 1.00 19.37 ? 143  ARG O N   1 
ATOM   16391 C  CA  . ARG O  1 143 ? 47.240  113.404 113.312 1.00 19.13 ? 143  ARG O CA  1 
ATOM   16392 C  C   . ARG O  1 143 ? 48.473  114.223 112.960 1.00 19.33 ? 143  ARG O C   1 
ATOM   16393 O  O   . ARG O  1 143 ? 48.886  115.092 113.717 1.00 19.87 ? 143  ARG O O   1 
ATOM   16394 C  CB  . ARG O  1 143 ? 46.035  114.309 113.631 1.00 19.54 ? 143  ARG O CB  1 
ATOM   16395 C  CG  . ARG O  1 143 ? 44.846  113.519 114.229 1.00 18.56 ? 143  ARG O CG  1 
ATOM   16396 C  CD  . ARG O  1 143 ? 43.689  114.369 114.833 1.00 19.20 ? 143  ARG O CD  1 
ATOM   16397 N  NE  . ARG O  1 143 ? 42.762  113.458 115.530 1.00 17.94 ? 143  ARG O NE  1 
ATOM   16398 C  CZ  . ARG O  1 143 ? 41.495  113.741 115.803 1.00 20.54 ? 143  ARG O CZ  1 
ATOM   16399 N  NH1 . ARG O  1 143 ? 40.994  114.941 115.496 1.00 20.26 ? 143  ARG O NH1 1 
ATOM   16400 N  NH2 . ARG O  1 143 ? 40.732  112.833 116.419 1.00 20.17 ? 143  ARG O NH2 1 
ATOM   16401 N  N   . LEU O  1 144 ? 49.076  113.905 111.817 1.00 17.67 ? 144  LEU O N   1 
ATOM   16402 C  CA  . LEU O  1 144 ? 50.294  114.566 111.404 1.00 17.45 ? 144  LEU O CA  1 
ATOM   16403 C  C   . LEU O  1 144 ? 49.991  115.894 110.720 1.00 16.50 ? 144  LEU O C   1 
ATOM   16404 O  O   . LEU O  1 144 ? 50.791  116.823 110.753 1.00 15.75 ? 144  LEU O O   1 
ATOM   16405 C  CB  . LEU O  1 144 ? 51.041  113.670 110.422 1.00 16.92 ? 144  LEU O CB  1 
ATOM   16406 C  CG  . LEU O  1 144 ? 51.494  112.357 111.079 1.00 19.04 ? 144  LEU O CG  1 
ATOM   16407 C  CD1 . LEU O  1 144 ? 52.460  111.624 110.158 1.00 19.92 ? 144  LEU O CD1 1 
ATOM   16408 C  CD2 . LEU O  1 144 ? 52.158  112.607 112.439 1.00 19.57 ? 144  LEU O CD2 1 
ATOM   16409 N  N   . ALA O  1 145 ? 48.867  115.941 110.024 1.00 15.70 ? 145  ALA O N   1 
ATOM   16410 C  CA  . ALA O  1 145 ? 48.510  117.167 109.332 1.00 15.39 ? 145  ALA O CA  1 
ATOM   16411 C  C   . ALA O  1 145 ? 47.041  117.166 108.995 1.00 16.05 ? 145  ALA O C   1 
ATOM   16412 O  O   . ALA O  1 145 ? 46.401  116.109 108.803 1.00 15.06 ? 145  ALA O O   1 
ATOM   16413 C  CB  . ALA O  1 145 ? 49.365  117.317 108.066 1.00 15.92 ? 145  ALA O CB  1 
ATOM   16414 N  N   . CYS O  1 146 ? 46.501  118.370 108.882 1.00 16.18 ? 146  CYS O N   1 
ATOM   16415 C  CA  . CYS O  1 146 ? 45.086  118.490 108.645 1.00 16.85 ? 146  CYS O CA  1 
ATOM   16416 C  C   . CYS O  1 146 ? 44.776  119.824 108.025 1.00 15.76 ? 146  CYS O C   1 
ATOM   16417 O  O   . CYS O  1 146 ? 45.598  120.733 108.022 1.00 16.30 ? 146  CYS O O   1 
ATOM   16418 C  CB  . CYS O  1 146 ? 44.310  118.351 109.969 1.00 17.45 ? 146  CYS O CB  1 
ATOM   16419 S  SG  . CYS O  1 146 ? 44.662  119.627 111.212 1.00 20.11 ? 146  CYS O SG  1 
ATOM   16420 N  N   . GLY O  1 147 ? 43.558  119.939 107.519 1.00 16.40 ? 147  GLY O N   1 
ATOM   16421 C  CA  . GLY O  1 147 ? 43.069  121.206 107.004 1.00 15.04 ? 147  GLY O CA  1 
ATOM   16422 C  C   . GLY O  1 147 ? 41.562  121.163 106.864 1.00 15.83 ? 147  GLY O C   1 
ATOM   16423 O  O   . GLY O  1 147 ? 40.971  120.088 106.774 1.00 15.93 ? 147  GLY O O   1 
ATOM   16424 N  N   . VAL O  1 148 ? 40.927  122.332 106.772 1.00 15.71 ? 148  VAL O N   1 
ATOM   16425 C  CA  . VAL O  1 148 ? 39.484  122.381 106.612 1.00 15.36 ? 148  VAL O CA  1 
ATOM   16426 C  C   . VAL O  1 148 ? 39.215  122.277 105.140 1.00 16.67 ? 148  VAL O C   1 
ATOM   16427 O  O   . VAL O  1 148 ? 39.906  122.916 104.337 1.00 16.80 ? 148  VAL O O   1 
ATOM   16428 C  CB  . VAL O  1 148 ? 38.909  123.754 107.156 1.00 16.39 ? 148  VAL O CB  1 
ATOM   16429 C  CG1 . VAL O  1 148 ? 37.379  123.839 106.951 1.00 15.46 ? 148  VAL O CG1 1 
ATOM   16430 C  CG2 . VAL O  1 148 ? 39.320  123.958 108.617 1.00 16.28 ? 148  VAL O CG2 1 
ATOM   16431 N  N   . ILE O  1 149 ? 38.212  121.491 104.758 1.00 16.70 ? 149  ILE O N   1 
ATOM   16432 C  CA  . ILE O  1 149 ? 37.861  121.389 103.347 1.00 17.03 ? 149  ILE O CA  1 
ATOM   16433 C  C   . ILE O  1 149 ? 37.076  122.619 102.893 1.00 17.99 ? 149  ILE O C   1 
ATOM   16434 O  O   . ILE O  1 149 ? 36.054  122.972 103.473 1.00 18.37 ? 149  ILE O O   1 
ATOM   16435 C  CB  . ILE O  1 149 ? 37.087  120.073 103.065 1.00 16.98 ? 149  ILE O CB  1 
ATOM   16436 C  CG1 . ILE O  1 149 ? 37.981  118.868 103.394 1.00 14.53 ? 149  ILE O CG1 1 
ATOM   16437 C  CG2 . ILE O  1 149 ? 36.673  120.007 101.617 1.00 18.01 ? 149  ILE O CG2 1 
ATOM   16438 C  CD1 . ILE O  1 149 ? 37.157  117.535 103.700 1.00 13.38 ? 149  ILE O CD1 1 
ATOM   16439 N  N   . GLY O  1 150 ? 37.554  123.285 101.848 1.00 18.61 ? 150  GLY O N   1 
ATOM   16440 C  CA  . GLY O  1 150 ? 36.870  124.488 101.398 1.00 19.42 ? 150  GLY O CA  1 
ATOM   16441 C  C   . GLY O  1 150 ? 36.331  124.378 99.993  1.00 20.33 ? 150  GLY O C   1 
ATOM   16442 O  O   . GLY O  1 150 ? 36.834  123.585 99.196  1.00 20.35 ? 150  GLY O O   1 
ATOM   16443 N  N   . ILE O  1 151 ? 35.311  125.180 99.692  1.00 20.69 ? 151  ILE O N   1 
ATOM   16444 C  CA  . ILE O  1 151 ? 34.714  125.216 98.368  1.00 21.05 ? 151  ILE O CA  1 
ATOM   16445 C  C   . ILE O  1 151 ? 35.733  125.818 97.393  1.00 21.65 ? 151  ILE O C   1 
ATOM   16446 O  O   . ILE O  1 151 ? 36.391  126.808 97.713  1.00 21.37 ? 151  ILE O O   1 
ATOM   16447 C  CB  . ILE O  1 151 ? 33.458  126.098 98.418  1.00 21.77 ? 151  ILE O CB  1 
ATOM   16448 C  CG1 . ILE O  1 151 ? 32.394  125.498 99.355  1.00 21.64 ? 151  ILE O CG1 1 
ATOM   16449 C  CG2 . ILE O  1 151 ? 32.910  126.359 97.007  1.00 21.35 ? 151  ILE O CG2 1 
ATOM   16450 C  CD1 . ILE O  1 151 ? 31.174  126.452 99.560  1.00 21.90 ? 151  ILE O CD1 1 
ATOM   16451 N  N   . ALA O  1 152 ? 35.881  125.223 96.212  1.00 22.32 ? 152  ALA O N   1 
ATOM   16452 C  CA  . ALA O  1 152 ? 36.885  125.707 95.273  1.00 23.56 ? 152  ALA O CA  1 
ATOM   16453 C  C   . ALA O  1 152 ? 36.293  126.135 93.948  1.00 25.12 ? 152  ALA O C   1 
ATOM   16454 O  O   . ALA O  1 152 ? 35.148  125.831 93.645  1.00 24.21 ? 152  ALA O O   1 
ATOM   16455 C  CB  . ALA O  1 152 ? 37.932  124.637 95.022  1.00 24.10 ? 152  ALA O CB  1 
ATOM   16456 N  N   . GLN O  1 153 ? 37.108  126.847 93.176  1.00 27.28 ? 153  GLN O N   1 
ATOM   16457 C  CA  . GLN O  1 153 ? 36.791  127.199 91.810  1.00 30.19 ? 153  GLN O CA  1 
ATOM   16458 C  C   . GLN O  1 153 ? 37.467  126.122 90.966  1.00 32.00 ? 153  GLN O C   1 
ATOM   16459 O  O   . GLN O  1 153 ? 37.414  126.136 89.735  1.00 33.82 ? 153  GLN O O   1 
ATOM   16460 C  CB  . GLN O  1 153 ? 37.369  128.560 91.458  1.00 29.96 ? 153  GLN O CB  1 
ATOM   16461 C  CG  . GLN O  1 153 ? 36.742  129.193 90.232  1.00 32.06 ? 153  GLN O CG  1 
ATOM   16462 C  CD  . GLN O  1 153 ? 37.594  130.300 89.657  1.00 32.22 ? 153  GLN O CD  1 
ATOM   16463 O  OE1 . GLN O  1 153 ? 38.816  130.185 89.611  1.00 32.22 ? 153  GLN O OE1 1 
ATOM   16464 N  NE2 . GLN O  1 153 ? 36.952  131.379 89.218  1.00 33.41 ? 153  GLN O NE2 1 
ATOM   16465 N  N   . ALA P  1 1   ? 56.821  147.557 20.681  1.00 56.81 ? 1    ALA P N   1 
ATOM   16466 C  CA  . ALA P  1 1   ? 55.395  147.159 20.851  1.00 56.87 ? 1    ALA P CA  1 
ATOM   16467 C  C   . ALA P  1 1   ? 55.249  145.650 21.030  1.00 56.89 ? 1    ALA P C   1 
ATOM   16468 O  O   . ALA P  1 1   ? 55.915  144.868 20.353  1.00 56.96 ? 1    ALA P O   1 
ATOM   16469 C  CB  . ALA P  1 1   ? 54.569  147.633 19.666  1.00 56.84 ? 1    ALA P CB  1 
ATOM   16470 N  N   . THR P  1 2   ? 54.376  145.248 21.948  1.00 56.90 ? 2    THR P N   1 
ATOM   16471 C  CA  . THR P  1 2   ? 54.114  143.834 22.199  1.00 56.83 ? 2    THR P CA  1 
ATOM   16472 C  C   . THR P  1 2   ? 52.696  143.481 21.752  1.00 56.77 ? 2    THR P C   1 
ATOM   16473 O  O   . THR P  1 2   ? 51.800  144.327 21.774  1.00 56.68 ? 2    THR P O   1 
ATOM   16474 C  CB  . THR P  1 2   ? 54.348  143.485 23.692  1.00 56.89 ? 2    THR P CB  1 
ATOM   16475 O  OG1 . THR P  1 2   ? 53.450  142.443 24.096  1.00 56.94 ? 2    THR P OG1 1 
ATOM   16476 C  CG2 . THR P  1 2   ? 53.958  144.658 24.590  1.00 56.86 ? 2    THR P CG2 1 
ATOM   16477 N  N   . LYS P  1 3   ? 52.499  142.240 21.318  1.00 56.69 ? 3    LYS P N   1 
ATOM   16478 C  CA  . LYS P  1 3   ? 51.187  141.804 20.854  1.00 56.66 ? 3    LYS P CA  1 
ATOM   16479 C  C   . LYS P  1 3   ? 50.795  140.466 21.465  1.00 56.48 ? 3    LYS P C   1 
ATOM   16480 O  O   . LYS P  1 3   ? 51.648  139.633 21.762  1.00 56.35 ? 3    LYS P O   1 
ATOM   16481 C  CB  . LYS P  1 3   ? 51.149  141.703 19.326  1.00 56.72 ? 3    LYS P CB  1 
ATOM   16482 C  CG  . LYS P  1 3   ? 51.381  143.011 18.580  1.00 57.15 ? 3    LYS P CG  1 
ATOM   16483 C  CD  . LYS P  1 3   ? 51.156  142.821 17.087  1.00 58.03 ? 3    LYS P CD  1 
ATOM   16484 C  CE  . LYS P  1 3   ? 51.736  143.970 16.272  1.00 59.00 ? 3    LYS P CE  1 
ATOM   16485 N  NZ  . LYS P  1 3   ? 51.068  145.273 16.563  1.00 59.62 ? 3    LYS P NZ  1 
ATOM   16486 N  N   . ALA P  1 4   ? 49.494  140.268 21.638  1.00 56.47 ? 4    ALA P N   1 
ATOM   16487 C  CA  . ALA P  1 4   ? 48.973  139.043 22.224  1.00 56.56 ? 4    ALA P CA  1 
ATOM   16488 C  C   . ALA P  1 4   ? 47.618  138.697 21.630  1.00 56.68 ? 4    ALA P C   1 
ATOM   16489 O  O   . ALA P  1 4   ? 46.914  139.565 21.115  1.00 56.60 ? 4    ALA P O   1 
ATOM   16490 C  CB  . ALA P  1 4   ? 48.863  139.186 23.735  1.00 56.50 ? 4    ALA P CB  1 
ATOM   16491 N  N   . VAL P  1 5   ? 47.253  137.423 21.709  1.00 56.93 ? 5    VAL P N   1 
ATOM   16492 C  CA  . VAL P  1 5   ? 45.973  136.972 21.180  1.00 57.21 ? 5    VAL P CA  1 
ATOM   16493 C  C   . VAL P  1 5   ? 45.393  135.859 22.049  1.00 57.32 ? 5    VAL P C   1 
ATOM   16494 O  O   . VAL P  1 5   ? 46.121  135.161 22.756  1.00 57.40 ? 5    VAL P O   1 
ATOM   16495 C  CB  . VAL P  1 5   ? 46.105  136.486 19.720  1.00 57.11 ? 5    VAL P CB  1 
ATOM   16496 C  CG1 . VAL P  1 5   ? 46.905  135.183 19.659  1.00 57.13 ? 5    VAL P CG1 1 
ATOM   16497 C  CG2 . VAL P  1 5   ? 44.731  136.317 19.079  1.00 57.27 ? 5    VAL P CG2 1 
ATOM   16498 N  N   . CYS P  1 6   ? 44.076  135.705 21.997  1.00 57.64 ? 6    CYS P N   1 
ATOM   16499 C  CA  . CYS P  1 6   ? 43.398  134.689 22.781  1.00 58.04 ? 6    CYS P CA  1 
ATOM   16500 C  C   . CYS P  1 6   ? 42.264  134.077 21.973  1.00 58.29 ? 6    CYS P C   1 
ATOM   16501 O  O   . CYS P  1 6   ? 41.509  134.791 21.311  1.00 58.21 ? 6    CYS P O   1 
ATOM   16502 C  CB  . CYS P  1 6   ? 42.853  135.295 24.075  1.00 58.02 ? 6    CYS P CB  1 
ATOM   16503 S  SG  . CYS P  1 6   ? 42.023  134.102 25.146  1.00 58.36 ? 6    CYS P SG  1 
ATOM   16504 N  N   . VAL P  1 7   ? 42.161  132.751 22.019  1.00 58.83 ? 7    VAL P N   1 
ATOM   16505 C  CA  . VAL P  1 7   ? 41.099  132.032 21.317  1.00 59.20 ? 7    VAL P CA  1 
ATOM   16506 C  C   . VAL P  1 7   ? 40.103  131.464 22.327  1.00 59.63 ? 7    VAL P C   1 
ATOM   16507 O  O   . VAL P  1 7   ? 40.431  130.574 23.115  1.00 59.51 ? 7    VAL P O   1 
ATOM   16508 C  CB  . VAL P  1 7   ? 41.655  130.908 20.410  1.00 59.17 ? 7    VAL P CB  1 
ATOM   16509 C  CG1 . VAL P  1 7   ? 40.519  130.163 19.725  1.00 58.77 ? 7    VAL P CG1 1 
ATOM   16510 C  CG2 . VAL P  1 7   ? 42.620  131.483 19.383  1.00 58.84 ? 7    VAL P CG2 1 
ATOM   16511 N  N   . LEU P  1 8   ? 38.885  131.995 22.294  1.00 60.14 ? 8    LEU P N   1 
ATOM   16512 C  CA  . LEU P  1 8   ? 37.847  131.614 23.245  1.00 60.77 ? 8    LEU P CA  1 
ATOM   16513 C  C   . LEU P  1 8   ? 37.072  130.378 22.813  1.00 60.98 ? 8    LEU P C   1 
ATOM   16514 O  O   . LEU P  1 8   ? 36.516  130.333 21.718  1.00 61.04 ? 8    LEU P O   1 
ATOM   16515 C  CB  . LEU P  1 8   ? 36.880  132.780 23.462  1.00 60.82 ? 8    LEU P CB  1 
ATOM   16516 C  CG  . LEU P  1 8   ? 37.244  133.873 24.471  1.00 61.42 ? 8    LEU P CG  1 
ATOM   16517 C  CD1 . LEU P  1 8   ? 38.742  134.121 24.544  1.00 62.03 ? 8    LEU P CD1 1 
ATOM   16518 C  CD2 . LEU P  1 8   ? 36.504  135.154 24.125  1.00 61.98 ? 8    LEU P CD2 1 
ATOM   16519 N  N   . LYS P  1 9   ? 37.037  129.378 23.687  1.00 61.37 ? 9    LYS P N   1 
ATOM   16520 C  CA  . LYS P  1 9   ? 36.302  128.148 23.424  1.00 61.76 ? 9    LYS P CA  1 
ATOM   16521 C  C   . LYS P  1 9   ? 35.611  127.663 24.692  1.00 62.02 ? 9    LYS P C   1 
ATOM   16522 O  O   . LYS P  1 9   ? 36.123  127.847 25.800  1.00 62.22 ? 9    LYS P O   1 
ATOM   16523 C  CB  . LYS P  1 9   ? 37.230  127.065 22.870  1.00 61.83 ? 9    LYS P CB  1 
ATOM   16524 C  CG  . LYS P  1 9   ? 37.398  127.111 21.357  1.00 62.14 ? 9    LYS P CG  1 
ATOM   16525 C  CD  . LYS P  1 9   ? 38.295  125.985 20.858  1.00 62.90 ? 9    LYS P CD  1 
ATOM   16526 C  CE  . LYS P  1 9   ? 38.088  125.707 19.366  1.00 63.19 ? 9    LYS P CE  1 
ATOM   16527 N  NZ  . LYS P  1 9   ? 38.394  126.883 18.499  1.00 63.46 ? 9    LYS P NZ  1 
ATOM   16528 N  N   . GLY P  1 10  ? 34.444  127.048 24.528  1.00 62.21 ? 10   GLY P N   1 
ATOM   16529 C  CA  . GLY P  1 10  ? 33.684  126.553 25.661  1.00 62.42 ? 10   GLY P CA  1 
ATOM   16530 C  C   . GLY P  1 10  ? 32.891  125.303 25.343  1.00 62.57 ? 10   GLY P C   1 
ATOM   16531 O  O   . GLY P  1 10  ? 33.077  124.685 24.295  1.00 62.51 ? 10   GLY P O   1 
ATOM   16532 N  N   . ASP P  1 11  ? 31.998  124.931 26.254  1.00 62.77 ? 11   ASP P N   1 
ATOM   16533 C  CA  . ASP P  1 11  ? 31.178  123.741 26.073  1.00 62.99 ? 11   ASP P CA  1 
ATOM   16534 C  C   . ASP P  1 11  ? 29.975  124.022 25.177  1.00 63.10 ? 11   ASP P C   1 
ATOM   16535 O  O   . ASP P  1 11  ? 29.276  123.098 24.758  1.00 63.12 ? 11   ASP P O   1 
ATOM   16536 C  CB  . ASP P  1 11  ? 30.711  123.196 27.427  1.00 62.99 ? 11   ASP P CB  1 
ATOM   16537 C  CG  . ASP P  1 11  ? 31.864  122.727 28.294  1.00 63.16 ? 11   ASP P CG  1 
ATOM   16538 O  OD1 . ASP P  1 11  ? 32.904  122.323 27.732  1.00 63.38 ? 11   ASP P OD1 1 
ATOM   16539 O  OD2 . ASP P  1 11  ? 31.823  122.725 29.544  1.00 63.09 ? 11   ASP P OD2 1 
ATOM   16540 N  N   . GLY P  1 12  ? 29.744  125.298 24.879  1.00 63.20 ? 12   GLY P N   1 
ATOM   16541 C  CA  . GLY P  1 12  ? 28.608  125.692 24.062  1.00 63.30 ? 12   GLY P CA  1 
ATOM   16542 C  C   . GLY P  1 12  ? 28.954  126.262 22.698  1.00 63.32 ? 12   GLY P C   1 
ATOM   16543 O  O   . GLY P  1 12  ? 30.025  125.995 22.148  1.00 63.33 ? 12   GLY P O   1 
ATOM   16544 N  N   . PRO P  1 13  ? 28.036  127.053 22.150  1.00 63.31 ? 13   PRO P N   1 
ATOM   16545 C  CA  . PRO P  1 13  ? 28.212  127.662 20.829  1.00 63.32 ? 13   PRO P CA  1 
ATOM   16546 C  C   . PRO P  1 13  ? 29.114  128.895 20.862  1.00 63.35 ? 13   PRO P C   1 
ATOM   16547 O  O   . PRO P  1 13  ? 29.507  129.390 19.801  1.00 63.31 ? 13   PRO P O   1 
ATOM   16548 C  CB  . PRO P  1 13  ? 26.783  128.078 20.446  1.00 63.34 ? 13   PRO P CB  1 
ATOM   16549 C  CG  . PRO P  1 13  ? 25.892  127.500 21.522  1.00 63.32 ? 13   PRO P CG  1 
ATOM   16550 C  CD  . PRO P  1 13  ? 26.742  127.410 22.753  1.00 63.32 ? 13   PRO P CD  1 
ATOM   16551 N  N   . VAL P  1 14  ? 29.439  129.376 22.061  1.00 63.29 ? 14   VAL P N   1 
ATOM   16552 C  CA  . VAL P  1 14  ? 30.259  130.577 22.211  1.00 63.25 ? 14   VAL P CA  1 
ATOM   16553 C  C   . VAL P  1 14  ? 31.723  130.363 21.845  1.00 63.24 ? 14   VAL P C   1 
ATOM   16554 O  O   . VAL P  1 14  ? 32.391  129.472 22.373  1.00 63.23 ? 14   VAL P O   1 
ATOM   16555 C  CB  . VAL P  1 14  ? 30.183  131.156 23.641  1.00 63.25 ? 14   VAL P CB  1 
ATOM   16556 C  CG1 . VAL P  1 14  ? 30.884  132.505 23.702  1.00 63.17 ? 14   VAL P CG1 1 
ATOM   16557 C  CG2 . VAL P  1 14  ? 28.739  131.283 24.085  1.00 63.20 ? 14   VAL P CG2 1 
ATOM   16558 N  N   . GLN P  1 15  ? 32.207  131.194 20.930  1.00 63.26 ? 15   GLN P N   1 
ATOM   16559 C  CA  . GLN P  1 15  ? 33.599  131.168 20.513  1.00 63.26 ? 15   GLN P CA  1 
ATOM   16560 C  C   . GLN P  1 15  ? 33.954  132.506 19.886  1.00 63.18 ? 15   GLN P C   1 
ATOM   16561 O  O   . GLN P  1 15  ? 33.104  133.178 19.299  1.00 63.17 ? 15   GLN P O   1 
ATOM   16562 C  CB  . GLN P  1 15  ? 33.878  130.011 19.546  1.00 63.33 ? 15   GLN P CB  1 
ATOM   16563 C  CG  . GLN P  1 15  ? 33.140  130.079 18.221  1.00 63.57 ? 15   GLN P CG  1 
ATOM   16564 C  CD  . GLN P  1 15  ? 33.211  128.765 17.462  1.00 63.93 ? 15   GLN P CD  1 
ATOM   16565 O  OE1 . GLN P  1 15  ? 32.677  128.648 16.360  1.00 63.78 ? 15   GLN P OE1 1 
ATOM   16566 N  NE2 . GLN P  1 15  ? 33.868  127.774 18.054  1.00 64.12 ? 15   GLN P NE2 1 
ATOM   16567 N  N   . GLY P  1 16  ? 35.211  132.899 20.032  1.00 63.04 ? 16   GLY P N   1 
ATOM   16568 C  CA  . GLY P  1 16  ? 35.665  134.156 19.484  1.00 62.97 ? 16   GLY P CA  1 
ATOM   16569 C  C   . GLY P  1 16  ? 37.170  134.277 19.515  1.00 62.89 ? 16   GLY P C   1 
ATOM   16570 O  O   . GLY P  1 16  ? 37.875  133.377 19.974  1.00 62.97 ? 16   GLY P O   1 
ATOM   16571 N  N   . ILE P  1 17  ? 37.662  135.400 19.008  1.00 62.74 ? 17   ILE P N   1 
ATOM   16572 C  CA  . ILE P  1 17  ? 39.088  135.679 18.993  1.00 62.35 ? 17   ILE P CA  1 
ATOM   16573 C  C   . ILE P  1 17  ? 39.323  137.090 19.512  1.00 62.08 ? 17   ILE P C   1 
ATOM   16574 O  O   . ILE P  1 17  ? 38.678  138.039 19.063  1.00 61.98 ? 17   ILE P O   1 
ATOM   16575 C  CB  . ILE P  1 17  ? 39.646  135.540 17.572  1.00 62.24 ? 17   ILE P CB  1 
ATOM   16576 C  CG1 . ILE P  1 17  ? 39.461  134.106 17.062  1.00 62.33 ? 17   ILE P CG1 1 
ATOM   16577 C  CG2 . ILE P  1 17  ? 41.108  135.949 17.543  1.00 62.01 ? 17   ILE P CG2 1 
ATOM   16578 C  CD1 . ILE P  1 17  ? 39.632  133.952 15.561  1.00 62.01 ? 17   ILE P CD1 1 
ATOM   16579 N  N   . ILE P  1 18  ? 40.243  137.226 20.460  1.00 61.81 ? 18   ILE P N   1 
ATOM   16580 C  CA  . ILE P  1 18  ? 40.537  138.528 21.037  1.00 61.62 ? 18   ILE P CA  1 
ATOM   16581 C  C   . ILE P  1 18  ? 42.010  138.889 20.902  1.00 61.60 ? 18   ILE P C   1 
ATOM   16582 O  O   . ILE P  1 18  ? 42.884  138.145 21.344  1.00 61.50 ? 18   ILE P O   1 
ATOM   16583 C  CB  . ILE P  1 18  ? 40.104  138.570 22.510  1.00 61.59 ? 18   ILE P CB  1 
ATOM   16584 C  CG1 . ILE P  1 18  ? 38.591  138.369 22.622  1.00 61.39 ? 18   ILE P CG1 1 
ATOM   16585 C  CG2 . ILE P  1 18  ? 40.529  139.878 23.153  1.00 61.47 ? 18   ILE P CG2 1 
ATOM   16586 C  CD1 . ILE P  1 18  ? 37.778  139.453 21.958  1.00 61.63 ? 18   ILE P CD1 1 
ATOM   16587 N  N   . ASN P  1 19  ? 42.270  140.036 20.284  1.00 61.63 ? 19   ASN P N   1 
ATOM   16588 C  CA  . ASN P  1 19  ? 43.628  140.524 20.098  1.00 61.62 ? 19   ASN P CA  1 
ATOM   16589 C  C   . ASN P  1 19  ? 44.001  141.550 21.161  1.00 61.86 ? 19   ASN P C   1 
ATOM   16590 O  O   . ASN P  1 19  ? 43.153  142.307 21.634  1.00 61.84 ? 19   ASN P O   1 
ATOM   16591 C  CB  . ASN P  1 19  ? 43.782  141.155 18.715  1.00 61.51 ? 19   ASN P CB  1 
ATOM   16592 C  CG  . ASN P  1 19  ? 43.361  140.226 17.596  1.00 60.95 ? 19   ASN P CG  1 
ATOM   16593 O  OD1 . ASN P  1 19  ? 42.231  140.293 17.108  1.00 60.58 ? 19   ASN P OD1 1 
ATOM   16594 N  ND2 . ASN P  1 19  ? 44.273  139.359 17.174  1.00 59.47 ? 19   ASN P ND2 1 
ATOM   16595 N  N   . PHE P  1 20  ? 45.275  141.560 21.537  1.00 62.10 ? 20   PHE P N   1 
ATOM   16596 C  CA  . PHE P  1 20  ? 45.796  142.525 22.497  1.00 62.37 ? 20   PHE P CA  1 
ATOM   16597 C  C   . PHE P  1 20  ? 47.021  143.197 21.898  1.00 62.55 ? 20   PHE P C   1 
ATOM   16598 O  O   . PHE P  1 20  ? 47.891  142.527 21.336  1.00 62.54 ? 20   PHE P O   1 
ATOM   16599 C  CB  . PHE P  1 20  ? 46.216  141.847 23.801  1.00 62.21 ? 20   PHE P CB  1 
ATOM   16600 C  CG  . PHE P  1 20  ? 45.103  141.145 24.518  1.00 62.31 ? 20   PHE P CG  1 
ATOM   16601 C  CD1 . PHE P  1 20  ? 44.685  139.887 24.110  1.00 62.47 ? 20   PHE P CD1 1 
ATOM   16602 C  CD2 . PHE P  1 20  ? 44.496  141.728 25.624  1.00 61.96 ? 20   PHE P CD2 1 
ATOM   16603 C  CE1 . PHE P  1 20  ? 43.669  139.232 24.777  1.00 62.57 ? 20   PHE P CE1 1 
ATOM   16604 C  CE2 . PHE P  1 20  ? 43.477  141.079 26.296  1.00 61.67 ? 20   PHE P CE2 1 
ATOM   16605 C  CZ  . PHE P  1 20  ? 43.063  139.828 25.873  1.00 62.55 ? 20   PHE P CZ  1 
ATOM   16606 N  N   . GLU P  1 21  ? 47.097  144.517 22.016  1.00 62.72 ? 21   GLU P N   1 
ATOM   16607 C  CA  . GLU P  1 21  ? 48.258  145.240 21.521  1.00 62.99 ? 21   GLU P CA  1 
ATOM   16608 C  C   . GLU P  1 21  ? 48.657  146.336 22.500  1.00 63.08 ? 21   GLU P C   1 
ATOM   16609 O  O   . GLU P  1 21  ? 47.806  147.053 23.028  1.00 63.12 ? 21   GLU P O   1 
ATOM   16610 C  CB  . GLU P  1 21  ? 47.991  145.831 20.135  1.00 63.03 ? 21   GLU P CB  1 
ATOM   16611 C  CG  . GLU P  1 21  ? 49.254  146.232 19.390  1.00 63.65 ? 21   GLU P CG  1 
ATOM   16612 C  CD  . GLU P  1 21  ? 48.966  147.013 18.120  1.00 64.69 ? 21   GLU P CD  1 
ATOM   16613 O  OE1 . GLU P  1 21  ? 47.842  146.897 17.588  1.00 65.09 ? 21   GLU P OE1 1 
ATOM   16614 O  OE2 . GLU P  1 21  ? 49.866  147.744 17.652  1.00 64.92 ? 21   GLU P OE2 1 
ATOM   16615 N  N   . GLN P  1 22  ? 49.956  146.447 22.749  1.00 63.21 ? 22   GLN P N   1 
ATOM   16616 C  CA  . GLN P  1 22  ? 50.485  147.462 23.643  1.00 63.39 ? 22   GLN P CA  1 
ATOM   16617 C  C   . GLN P  1 22  ? 51.670  148.125 22.961  1.00 63.59 ? 22   GLN P C   1 
ATOM   16618 O  O   . GLN P  1 22  ? 52.642  147.460 22.605  1.00 63.55 ? 22   GLN P O   1 
ATOM   16619 C  CB  . GLN P  1 22  ? 50.904  146.843 24.975  1.00 63.38 ? 22   GLN P CB  1 
ATOM   16620 C  CG  . GLN P  1 22  ? 51.033  147.843 26.108  1.00 63.05 ? 22   GLN P CG  1 
ATOM   16621 C  CD  . GLN P  1 22  ? 51.502  147.204 27.400  1.00 62.84 ? 22   GLN P CD  1 
ATOM   16622 O  OE1 . GLN P  1 22  ? 52.189  146.185 27.380  1.00 62.32 ? 22   GLN P OE1 1 
ATOM   16623 N  NE2 . GLN P  1 22  ? 51.134  147.803 28.528  1.00 62.74 ? 22   GLN P NE2 1 
ATOM   16624 N  N   . LYS P  1 23  ? 51.583  149.436 22.772  1.00 63.89 ? 23   LYS P N   1 
ATOM   16625 C  CA  . LYS P  1 23  ? 52.629  150.172 22.074  1.00 64.24 ? 23   LYS P CA  1 
ATOM   16626 C  C   . LYS P  1 23  ? 53.827  150.483 22.966  1.00 64.42 ? 23   LYS P C   1 
ATOM   16627 O  O   . LYS P  1 23  ? 54.974  150.399 22.525  1.00 64.44 ? 23   LYS P O   1 
ATOM   16628 C  CB  . LYS P  1 23  ? 52.059  151.454 21.453  1.00 64.27 ? 23   LYS P CB  1 
ATOM   16629 C  CG  . LYS P  1 23  ? 50.791  151.212 20.639  1.00 64.49 ? 23   LYS P CG  1 
ATOM   16630 C  CD  . LYS P  1 23  ? 50.525  152.308 19.616  1.00 64.72 ? 23   LYS P CD  1 
ATOM   16631 C  CE  . LYS P  1 23  ? 49.422  151.879 18.653  1.00 64.89 ? 23   LYS P CE  1 
ATOM   16632 N  NZ  . LYS P  1 23  ? 49.210  152.852 17.547  1.00 64.98 ? 23   LYS P NZ  1 
ATOM   16633 N  N   . GLU P  1 24  ? 53.560  150.829 24.221  1.00 64.66 ? 24   GLU P N   1 
ATOM   16634 C  CA  . GLU P  1 24  ? 54.624  151.183 25.153  1.00 64.91 ? 24   GLU P CA  1 
ATOM   16635 C  C   . GLU P  1 24  ? 54.476  150.500 26.508  1.00 65.07 ? 24   GLU P C   1 
ATOM   16636 O  O   . GLU P  1 24  ? 53.389  150.050 26.872  1.00 65.07 ? 24   GLU P O   1 
ATOM   16637 C  CB  . GLU P  1 24  ? 54.668  152.702 25.349  1.00 64.94 ? 24   GLU P CB  1 
ATOM   16638 C  CG  . GLU P  1 24  ? 55.223  153.476 24.163  1.00 65.04 ? 24   GLU P CG  1 
ATOM   16639 C  CD  . GLU P  1 24  ? 56.720  153.299 24.002  1.00 65.17 ? 24   GLU P CD  1 
ATOM   16640 O  OE1 . GLU P  1 24  ? 57.152  152.191 23.622  1.00 65.30 ? 24   GLU P OE1 1 
ATOM   16641 O  OE2 . GLU P  1 24  ? 57.468  154.268 24.255  1.00 65.16 ? 24   GLU P OE2 1 
ATOM   16642 N  N   . SER P  1 25  ? 55.580  150.424 27.247  1.00 65.30 ? 25   SER P N   1 
ATOM   16643 C  CA  . SER P  1 25  ? 55.569  149.853 28.588  1.00 65.51 ? 25   SER P CA  1 
ATOM   16644 C  C   . SER P  1 25  ? 54.673  150.741 29.444  1.00 65.63 ? 25   SER P C   1 
ATOM   16645 O  O   . SER P  1 25  ? 54.731  151.968 29.346  1.00 65.66 ? 25   SER P O   1 
ATOM   16646 C  CB  . SER P  1 25  ? 56.987  149.802 29.163  1.00 65.53 ? 25   SER P CB  1 
ATOM   16647 O  OG  . SER P  1 25  ? 57.129  148.749 30.102  1.00 65.50 ? 25   SER P OG  1 
ATOM   16648 N  N   . ASN P  1 26  ? 53.836  150.119 30.268  1.00 65.75 ? 26   ASN P N   1 
ATOM   16649 C  CA  . ASN P  1 26  ? 52.882  150.855 31.091  1.00 65.88 ? 26   ASN P CA  1 
ATOM   16650 C  C   . ASN P  1 26  ? 51.858  151.632 30.269  1.00 65.92 ? 26   ASN P C   1 
ATOM   16651 O  O   . ASN P  1 26  ? 50.998  152.319 30.822  1.00 65.98 ? 26   ASN P O   1 
ATOM   16652 C  CB  . ASN P  1 26  ? 53.594  151.789 32.069  1.00 65.89 ? 26   ASN P CB  1 
ATOM   16653 C  CG  . ASN P  1 26  ? 53.459  151.333 33.502  1.00 65.99 ? 26   ASN P CG  1 
ATOM   16654 O  OD1 . ASN P  1 26  ? 52.868  152.025 34.332  1.00 65.94 ? 26   ASN P OD1 1 
ATOM   16655 N  ND2 . ASN P  1 26  ? 53.994  150.154 33.800  1.00 65.85 ? 26   ASN P ND2 1 
ATOM   16656 N  N   . GLY P  1 27  ? 51.958  151.521 28.947  1.00 65.90 ? 27   GLY P N   1 
ATOM   16657 C  CA  . GLY P  1 27  ? 51.027  152.186 28.057  1.00 65.91 ? 27   GLY P CA  1 
ATOM   16658 C  C   . GLY P  1 27  ? 49.697  151.460 28.054  1.00 65.93 ? 27   GLY P C   1 
ATOM   16659 O  O   . GLY P  1 27  ? 49.570  150.382 28.637  1.00 65.91 ? 27   GLY P O   1 
ATOM   16660 N  N   . PRO P  1 28  ? 48.699  152.054 27.409  1.00 65.96 ? 28   PRO P N   1 
ATOM   16661 C  CA  . PRO P  1 28  ? 47.365  151.450 27.318  1.00 65.94 ? 28   PRO P CA  1 
ATOM   16662 C  C   . PRO P  1 28  ? 47.374  150.180 26.467  1.00 65.90 ? 28   PRO P C   1 
ATOM   16663 O  O   . PRO P  1 28  ? 48.203  150.053 25.565  1.00 65.88 ? 28   PRO P O   1 
ATOM   16664 C  CB  . PRO P  1 28  ? 46.537  152.538 26.625  1.00 65.97 ? 28   PRO P CB  1 
ATOM   16665 C  CG  . PRO P  1 28  ? 47.339  153.796 26.786  1.00 66.06 ? 28   PRO P CG  1 
ATOM   16666 C  CD  . PRO P  1 28  ? 48.769  153.360 26.732  1.00 65.96 ? 28   PRO P CD  1 
ATOM   16667 N  N   . VAL P  1 29  ? 46.470  149.250 26.760  1.00 65.85 ? 29   VAL P N   1 
ATOM   16668 C  CA  . VAL P  1 29  ? 46.373  148.016 25.988  1.00 65.75 ? 29   VAL P CA  1 
ATOM   16669 C  C   . VAL P  1 29  ? 45.079  147.982 25.195  1.00 65.67 ? 29   VAL P C   1 
ATOM   16670 O  O   . VAL P  1 29  ? 43.986  148.051 25.757  1.00 65.68 ? 29   VAL P O   1 
ATOM   16671 C  CB  . VAL P  1 29  ? 46.421  146.763 26.885  1.00 65.79 ? 29   VAL P CB  1 
ATOM   16672 C  CG1 . VAL P  1 29  ? 46.258  145.497 26.045  1.00 65.59 ? 29   VAL P CG1 1 
ATOM   16673 C  CG2 . VAL P  1 29  ? 47.714  146.724 27.687  1.00 65.83 ? 29   VAL P CG2 1 
ATOM   16674 N  N   . LYS P  1 30  ? 45.204  147.890 23.881  1.00 65.68 ? 30   LYS P N   1 
ATOM   16675 C  CA  . LYS P  1 30  ? 44.032  147.782 23.035  1.00 65.69 ? 30   LYS P CA  1 
ATOM   16676 C  C   . LYS P  1 30  ? 43.557  146.340 23.063  1.00 65.63 ? 30   LYS P C   1 
ATOM   16677 O  O   . LYS P  1 30  ? 44.327  145.417 22.792  1.00 65.47 ? 30   LYS P O   1 
ATOM   16678 C  CB  . LYS P  1 30  ? 44.354  148.196 21.598  1.00 65.81 ? 30   LYS P CB  1 
ATOM   16679 C  CG  . LYS P  1 30  ? 44.620  149.682 21.419  1.00 66.09 ? 30   LYS P CG  1 
ATOM   16680 C  CD  . LYS P  1 30  ? 44.562  150.075 19.948  1.00 66.64 ? 30   LYS P CD  1 
ATOM   16681 C  CE  . LYS P  1 30  ? 44.597  151.587 19.773  1.00 66.81 ? 30   LYS P CE  1 
ATOM   16682 N  NZ  . LYS P  1 30  ? 44.215  151.992 18.390  1.00 67.08 ? 30   LYS P NZ  1 
ATOM   16683 N  N   . VAL P  1 31  ? 42.293  146.147 23.419  1.00 65.49 ? 31   VAL P N   1 
ATOM   16684 C  CA  . VAL P  1 31  ? 41.702  144.815 23.430  1.00 65.29 ? 31   VAL P CA  1 
ATOM   16685 C  C   . VAL P  1 31  ? 40.573  144.782 22.405  1.00 65.16 ? 31   VAL P C   1 
ATOM   16686 O  O   . VAL P  1 31  ? 39.543  145.441 22.582  1.00 65.08 ? 31   VAL P O   1 
ATOM   16687 C  CB  . VAL P  1 31  ? 41.173  144.444 24.825  1.00 65.18 ? 31   VAL P CB  1 
ATOM   16688 C  CG1 . VAL P  1 31  ? 40.580  143.046 24.817  1.00 64.98 ? 31   VAL P CG1 1 
ATOM   16689 C  CG2 . VAL P  1 31  ? 42.289  144.545 25.849  1.00 65.09 ? 31   VAL P CG2 1 
ATOM   16690 N  N   . TRP P  1 32  ? 40.774  144.032 21.324  1.00 64.96 ? 32   TRP P N   1 
ATOM   16691 C  CA  . TRP P  1 32  ? 39.765  143.978 20.271  1.00 64.81 ? 32   TRP P CA  1 
ATOM   16692 C  C   . TRP P  1 32  ? 39.638  142.622 19.578  1.00 64.77 ? 32   TRP P C   1 
ATOM   16693 O  O   . TRP P  1 32  ? 40.602  141.861 19.466  1.00 64.41 ? 32   TRP P O   1 
ATOM   16694 C  CB  . TRP P  1 32  ? 39.999  145.081 19.231  1.00 64.82 ? 32   TRP P CB  1 
ATOM   16695 C  CG  . TRP P  1 32  ? 40.994  144.720 18.168  1.00 64.77 ? 32   TRP P CG  1 
ATOM   16696 C  CD1 . TRP P  1 32  ? 40.723  144.339 16.881  1.00 64.79 ? 32   TRP P CD1 1 
ATOM   16697 C  CD2 . TRP P  1 32  ? 42.419  144.710 18.294  1.00 64.77 ? 32   TRP P CD2 1 
ATOM   16698 N  NE1 . TRP P  1 32  ? 41.893  144.090 16.204  1.00 64.52 ? 32   TRP P NE1 1 
ATOM   16699 C  CE2 . TRP P  1 32  ? 42.950  144.310 17.048  1.00 64.58 ? 32   TRP P CE2 1 
ATOM   16700 C  CE3 . TRP P  1 32  ? 43.307  144.996 19.338  1.00 64.80 ? 32   TRP P CE3 1 
ATOM   16701 C  CZ2 . TRP P  1 32  ? 44.319  144.192 16.821  1.00 64.36 ? 32   TRP P CZ2 1 
ATOM   16702 C  CZ3 . TRP P  1 32  ? 44.664  144.879 19.111  1.00 64.59 ? 32   TRP P CZ3 1 
ATOM   16703 C  CH2 . TRP P  1 32  ? 45.158  144.480 17.861  1.00 64.65 ? 32   TRP P CH2 1 
ATOM   16704 N  N   . GLY P  1 33  ? 38.426  142.352 19.102  1.00 64.70 ? 33   GLY P N   1 
ATOM   16705 C  CA  . GLY P  1 33  ? 38.107  141.113 18.427  1.00 64.74 ? 33   GLY P CA  1 
ATOM   16706 C  C   . GLY P  1 33  ? 36.605  140.919 18.331  1.00 64.77 ? 33   GLY P C   1 
ATOM   16707 O  O   . GLY P  1 33  ? 35.840  141.885 18.366  1.00 64.73 ? 33   GLY P O   1 
ATOM   16708 N  N   . SER P  1 34  ? 36.184  139.663 18.222  1.00 64.83 ? 34   SER P N   1 
ATOM   16709 C  CA  . SER P  1 34  ? 34.770  139.328 18.092  1.00 64.81 ? 34   SER P CA  1 
ATOM   16710 C  C   . SER P  1 34  ? 34.441  138.001 18.777  1.00 64.77 ? 34   SER P C   1 
ATOM   16711 O  O   . SER P  1 34  ? 35.242  137.065 18.758  1.00 64.66 ? 34   SER P O   1 
ATOM   16712 C  CB  . SER P  1 34  ? 34.384  139.265 16.608  1.00 64.80 ? 34   SER P CB  1 
ATOM   16713 O  OG  . SER P  1 34  ? 33.048  138.825 16.430  1.00 64.84 ? 34   SER P OG  1 
ATOM   16714 N  N   . ILE P  1 35  ? 33.267  137.934 19.398  1.00 64.70 ? 35   ILE P N   1 
ATOM   16715 C  CA  . ILE P  1 35  ? 32.796  136.705 20.028  1.00 64.79 ? 35   ILE P CA  1 
ATOM   16716 C  C   . ILE P  1 35  ? 31.387  136.407 19.530  1.00 64.83 ? 35   ILE P C   1 
ATOM   16717 O  O   . ILE P  1 35  ? 30.537  137.296 19.509  1.00 64.94 ? 35   ILE P O   1 
ATOM   16718 C  CB  . ILE P  1 35  ? 32.782  136.831 21.569  1.00 64.85 ? 35   ILE P CB  1 
ATOM   16719 C  CG1 . ILE P  1 35  ? 34.102  137.407 22.091  1.00 64.81 ? 35   ILE P CG1 1 
ATOM   16720 C  CG2 . ILE P  1 35  ? 32.490  135.480 22.210  1.00 64.77 ? 35   ILE P CG2 1 
ATOM   16721 C  CD1 . ILE P  1 35  ? 34.055  137.817 23.557  1.00 65.34 ? 35   ILE P CD1 1 
ATOM   16722 N  N   . LYS P  1 36  ? 31.138  135.166 19.123  1.00 64.85 ? 36   LYS P N   1 
ATOM   16723 C  CA  . LYS P  1 36  ? 29.808  134.786 18.649  1.00 64.85 ? 36   LYS P CA  1 
ATOM   16724 C  C   . LYS P  1 36  ? 29.192  133.695 19.523  1.00 64.72 ? 36   LYS P C   1 
ATOM   16725 O  O   . LYS P  1 36  ? 29.865  133.123 20.379  1.00 64.67 ? 36   LYS P O   1 
ATOM   16726 C  CB  . LYS P  1 36  ? 29.846  134.351 17.179  1.00 64.89 ? 36   LYS P CB  1 
ATOM   16727 C  CG  . LYS P  1 36  ? 30.814  133.222 16.877  1.00 65.32 ? 36   LYS P CG  1 
ATOM   16728 C  CD  . LYS P  1 36  ? 30.717  132.797 15.415  1.00 66.37 ? 36   LYS P CD  1 
ATOM   16729 C  CE  . LYS P  1 36  ? 31.811  131.795 15.045  1.00 66.91 ? 36   LYS P CE  1 
ATOM   16730 N  NZ  . LYS P  1 36  ? 31.937  131.589 13.565  1.00 67.14 ? 36   LYS P NZ  1 
ATOM   16731 N  N   . GLY P  1 37  ? 27.905  133.429 19.313  1.00 64.60 ? 37   GLY P N   1 
ATOM   16732 C  CA  . GLY P  1 37  ? 27.190  132.408 20.063  1.00 64.41 ? 37   GLY P CA  1 
ATOM   16733 C  C   . GLY P  1 37  ? 26.629  132.873 21.396  1.00 64.23 ? 37   GLY P C   1 
ATOM   16734 O  O   . GLY P  1 37  ? 26.170  132.064 22.203  1.00 64.15 ? 37   GLY P O   1 
ATOM   16735 N  N   . LEU P  1 38  ? 26.654  134.181 21.622  1.00 64.11 ? 38   LEU P N   1 
ATOM   16736 C  CA  . LEU P  1 38  ? 26.178  134.758 22.873  1.00 64.01 ? 38   LEU P CA  1 
ATOM   16737 C  C   . LEU P  1 38  ? 24.730  135.224 22.795  1.00 63.89 ? 38   LEU P C   1 
ATOM   16738 O  O   . LEU P  1 38  ? 24.212  135.485 21.712  1.00 63.92 ? 38   LEU P O   1 
ATOM   16739 C  CB  . LEU P  1 38  ? 27.054  135.948 23.250  1.00 64.07 ? 38   LEU P CB  1 
ATOM   16740 C  CG  . LEU P  1 38  ? 28.521  135.648 23.528  1.00 64.11 ? 38   LEU P CG  1 
ATOM   16741 C  CD1 . LEU P  1 38  ? 29.344  136.918 23.433  1.00 64.33 ? 38   LEU P CD1 1 
ATOM   16742 C  CD2 . LEU P  1 38  ? 28.659  135.015 24.897  1.00 64.23 ? 38   LEU P CD2 1 
ATOM   16743 N  N   . THR P  1 39  ? 24.077  135.326 23.948  1.00 63.75 ? 39   THR P N   1 
ATOM   16744 C  CA  . THR P  1 39  ? 22.723  135.860 23.993  1.00 63.60 ? 39   THR P CA  1 
ATOM   16745 C  C   . THR P  1 39  ? 22.829  137.375 23.904  1.00 63.46 ? 39   THR P C   1 
ATOM   16746 O  O   . THR P  1 39  ? 23.787  137.967 24.406  1.00 63.30 ? 39   THR P O   1 
ATOM   16747 C  CB  . THR P  1 39  ? 21.995  135.453 25.289  1.00 63.62 ? 39   THR P CB  1 
ATOM   16748 O  OG1 . THR P  1 39  ? 22.768  135.856 26.426  1.00 63.68 ? 39   THR P OG1 1 
ATOM   16749 C  CG2 . THR P  1 39  ? 21.930  133.938 25.417  1.00 63.64 ? 39   THR P CG2 1 
ATOM   16750 N  N   . GLU P  1 40  ? 21.858  138.002 23.253  1.00 63.29 ? 40   GLU P N   1 
ATOM   16751 C  CA  . GLU P  1 40  ? 21.879  139.448 23.108  1.00 63.20 ? 40   GLU P CA  1 
ATOM   16752 C  C   . GLU P  1 40  ? 22.005  140.109 24.477  1.00 63.15 ? 40   GLU P C   1 
ATOM   16753 O  O   . GLU P  1 40  ? 21.317  139.727 25.423  1.00 63.18 ? 40   GLU P O   1 
ATOM   16754 C  CB  . GLU P  1 40  ? 20.620  139.941 22.393  1.00 63.16 ? 40   GLU P CB  1 
ATOM   16755 C  CG  . GLU P  1 40  ? 20.672  141.413 22.017  1.00 63.05 ? 40   GLU P CG  1 
ATOM   16756 C  CD  . GLU P  1 40  ? 19.400  141.896 21.353  1.00 62.90 ? 40   GLU P CD  1 
ATOM   16757 O  OE1 . GLU P  1 40  ? 18.621  141.052 20.861  1.00 62.83 ? 40   GLU P OE1 1 
ATOM   16758 O  OE2 . GLU P  1 40  ? 19.182  143.125 21.324  1.00 62.81 ? 40   GLU P OE2 1 
ATOM   16759 N  N   . GLY P  1 41  ? 22.902  141.083 24.586  1.00 63.07 ? 41   GLY P N   1 
ATOM   16760 C  CA  . GLY P  1 41  ? 23.069  141.805 25.833  1.00 62.92 ? 41   GLY P CA  1 
ATOM   16761 C  C   . GLY P  1 41  ? 24.484  141.867 26.371  1.00 62.85 ? 41   GLY P C   1 
ATOM   16762 O  O   . GLY P  1 41  ? 25.449  141.529 25.684  1.00 62.74 ? 41   GLY P O   1 
ATOM   16763 N  N   . LEU P  1 42  ? 24.591  142.307 27.621  1.00 62.77 ? 42   LEU P N   1 
ATOM   16764 C  CA  . LEU P  1 42  ? 25.874  142.463 28.295  1.00 62.72 ? 42   LEU P CA  1 
ATOM   16765 C  C   . LEU P  1 42  ? 26.419  141.143 28.830  1.00 62.69 ? 42   LEU P C   1 
ATOM   16766 O  O   . LEU P  1 42  ? 25.668  140.306 29.333  1.00 62.74 ? 42   LEU P O   1 
ATOM   16767 C  CB  . LEU P  1 42  ? 25.740  143.466 29.445  1.00 62.72 ? 42   LEU P CB  1 
ATOM   16768 C  CG  . LEU P  1 42  ? 26.115  144.929 29.194  1.00 62.70 ? 42   LEU P CG  1 
ATOM   16769 C  CD1 . LEU P  1 42  ? 26.074  145.274 27.717  1.00 62.93 ? 42   LEU P CD1 1 
ATOM   16770 C  CD2 . LEU P  1 42  ? 25.212  145.860 29.995  1.00 62.85 ? 42   LEU P CD2 1 
ATOM   16771 N  N   . HIS P  1 43  ? 27.733  140.968 28.723  1.00 62.52 ? 43   HIS P N   1 
ATOM   16772 C  CA  . HIS P  1 43  ? 28.390  139.759 29.212  1.00 62.45 ? 43   HIS P CA  1 
ATOM   16773 C  C   . HIS P  1 43  ? 29.703  140.064 29.928  1.00 62.23 ? 43   HIS P C   1 
ATOM   16774 O  O   . HIS P  1 43  ? 30.551  140.791 29.413  1.00 62.20 ? 43   HIS P O   1 
ATOM   16775 C  CB  . HIS P  1 43  ? 28.626  138.773 28.066  1.00 62.49 ? 43   HIS P CB  1 
ATOM   16776 C  CG  . HIS P  1 43  ? 27.367  138.179 27.519  1.00 62.71 ? 43   HIS P CG  1 
ATOM   16777 N  ND1 . HIS P  1 43  ? 26.770  137.065 28.068  1.00 62.90 ? 43   HIS P ND1 1 
ATOM   16778 C  CD2 . HIS P  1 43  ? 26.583  138.551 26.479  1.00 62.86 ? 43   HIS P CD2 1 
ATOM   16779 C  CE1 . HIS P  1 43  ? 25.677  136.773 27.387  1.00 63.01 ? 43   HIS P CE1 1 
ATOM   16780 N  NE2 . HIS P  1 43  ? 25.540  137.659 26.417  1.00 62.98 ? 43   HIS P NE2 1 
ATOM   16781 N  N   . GLY P  1 44  ? 29.862  139.507 31.123  1.00 62.08 ? 44   GLY P N   1 
ATOM   16782 C  CA  . GLY P  1 44  ? 31.075  139.704 31.890  1.00 61.97 ? 44   GLY P CA  1 
ATOM   16783 C  C   . GLY P  1 44  ? 32.305  139.398 31.061  1.00 61.89 ? 44   GLY P C   1 
ATOM   16784 O  O   . GLY P  1 44  ? 32.341  138.411 30.327  1.00 61.79 ? 44   GLY P O   1 
ATOM   16785 N  N   . PHE P  1 45  ? 33.321  140.242 31.186  1.00 61.89 ? 45   PHE P N   1 
ATOM   16786 C  CA  . PHE P  1 45  ? 34.543  140.094 30.404  1.00 61.86 ? 45   PHE P CA  1 
ATOM   16787 C  C   . PHE P  1 45  ? 35.777  140.325 31.284  1.00 61.68 ? 45   PHE P C   1 
ATOM   16788 O  O   . PHE P  1 45  ? 36.152  141.471 31.540  1.00 61.62 ? 45   PHE P O   1 
ATOM   16789 C  CB  . PHE P  1 45  ? 34.512  141.101 29.254  1.00 62.02 ? 45   PHE P CB  1 
ATOM   16790 C  CG  . PHE P  1 45  ? 35.464  140.792 28.143  1.00 62.49 ? 45   PHE P CG  1 
ATOM   16791 C  CD1 . PHE P  1 45  ? 35.348  139.617 27.415  1.00 63.09 ? 45   PHE P CD1 1 
ATOM   16792 C  CD2 . PHE P  1 45  ? 36.469  141.687 27.812  1.00 63.07 ? 45   PHE P CD2 1 
ATOM   16793 C  CE1 . PHE P  1 45  ? 36.227  139.335 26.381  1.00 63.75 ? 45   PHE P CE1 1 
ATOM   16794 C  CE2 . PHE P  1 45  ? 37.352  141.413 26.780  1.00 63.80 ? 45   PHE P CE2 1 
ATOM   16795 C  CZ  . PHE P  1 45  ? 37.231  140.235 26.062  1.00 63.84 ? 45   PHE P CZ  1 
ATOM   16796 N  N   . HIS P  1 46  ? 36.410  139.244 31.744  1.00 61.39 ? 46   HIS P N   1 
ATOM   16797 C  CA  . HIS P  1 46  ? 37.553  139.379 32.651  1.00 60.95 ? 46   HIS P CA  1 
ATOM   16798 C  C   . HIS P  1 46  ? 38.769  138.517 32.342  1.00 60.47 ? 46   HIS P C   1 
ATOM   16799 O  O   . HIS P  1 46  ? 38.678  137.480 31.689  1.00 60.37 ? 46   HIS P O   1 
ATOM   16800 C  CB  . HIS P  1 46  ? 37.146  139.056 34.092  1.00 61.15 ? 46   HIS P CB  1 
ATOM   16801 C  CG  . HIS P  1 46  ? 35.749  139.457 34.442  1.00 61.81 ? 46   HIS P CG  1 
ATOM   16802 N  ND1 . HIS P  1 46  ? 34.766  138.535 34.730  1.00 62.39 ? 46   HIS P ND1 1 
ATOM   16803 C  CD2 . HIS P  1 46  ? 35.174  140.675 34.569  1.00 62.77 ? 46   HIS P CD2 1 
ATOM   16804 C  CE1 . HIS P  1 46  ? 33.642  139.169 35.012  1.00 63.02 ? 46   HIS P CE1 1 
ATOM   16805 N  NE2 . HIS P  1 46  ? 33.861  140.468 34.920  1.00 62.96 ? 46   HIS P NE2 1 
ATOM   16806 N  N   . VAL P  1 47  ? 39.909  138.954 32.863  1.00 59.97 ? 47   VAL P N   1 
ATOM   16807 C  CA  . VAL P  1 47  ? 41.131  138.178 32.792  1.00 59.34 ? 47   VAL P CA  1 
ATOM   16808 C  C   . VAL P  1 47  ? 41.229  137.411 34.100  1.00 58.98 ? 47   VAL P C   1 
ATOM   16809 O  O   . VAL P  1 47  ? 41.343  138.013 35.169  1.00 58.73 ? 47   VAL P O   1 
ATOM   16810 C  CB  . VAL P  1 47  ? 42.370  139.076 32.643  1.00 59.41 ? 47   VAL P CB  1 
ATOM   16811 C  CG1 . VAL P  1 47  ? 43.645  138.287 32.927  1.00 59.03 ? 47   VAL P CG1 1 
ATOM   16812 C  CG2 . VAL P  1 47  ? 42.415  139.698 31.252  1.00 59.27 ? 47   VAL P CG2 1 
ATOM   16813 N  N   . HIS P  1 48  ? 41.150  136.086 34.027  1.00 58.50 ? 48   HIS P N   1 
ATOM   16814 C  CA  . HIS P  1 48  ? 41.261  135.267 35.232  1.00 58.23 ? 48   HIS P CA  1 
ATOM   16815 C  C   . HIS P  1 48  ? 42.719  134.930 35.532  1.00 57.81 ? 48   HIS P C   1 
ATOM   16816 O  O   . HIS P  1 48  ? 43.579  135.032 34.660  1.00 57.66 ? 48   HIS P O   1 
ATOM   16817 C  CB  . HIS P  1 48  ? 40.377  134.021 35.146  1.00 58.27 ? 48   HIS P CB  1 
ATOM   16818 C  CG  . HIS P  1 48  ? 38.919  134.315 35.322  1.00 58.51 ? 48   HIS P CG  1 
ATOM   16819 N  ND1 . HIS P  1 48  ? 38.153  133.730 36.308  1.00 58.08 ? 48   HIS P ND1 1 
ATOM   16820 C  CD2 . HIS P  1 48  ? 38.091  135.151 34.649  1.00 58.11 ? 48   HIS P CD2 1 
ATOM   16821 C  CE1 . HIS P  1 48  ? 36.914  134.182 36.226  1.00 57.98 ? 48   HIS P CE1 1 
ATOM   16822 N  NE2 . HIS P  1 48  ? 36.851  135.048 35.231  1.00 57.78 ? 48   HIS P NE2 1 
ATOM   16823 N  N   . GLU P  1 49  ? 42.987  134.520 36.766  1.00 57.51 ? 49   GLU P N   1 
ATOM   16824 C  CA  . GLU P  1 49  ? 44.360  134.346 37.233  1.00 57.26 ? 49   GLU P CA  1 
ATOM   16825 C  C   . GLU P  1 49  ? 45.257  133.301 36.552  1.00 57.26 ? 49   GLU P C   1 
ATOM   16826 O  O   . GLU P  1 49  ? 46.404  133.603 36.214  1.00 57.34 ? 49   GLU P O   1 
ATOM   16827 C  CB  . GLU P  1 49  ? 44.396  134.145 38.748  1.00 57.04 ? 49   GLU P CB  1 
ATOM   16828 C  CG  . GLU P  1 49  ? 45.808  134.200 39.296  1.00 56.82 ? 49   GLU P CG  1 
ATOM   16829 C  CD  . GLU P  1 49  ? 45.866  134.053 40.799  1.00 56.78 ? 49   GLU P CD  1 
ATOM   16830 O  OE1 . GLU P  1 49  ? 44.799  133.867 41.422  1.00 57.39 ? 49   GLU P OE1 1 
ATOM   16831 O  OE2 . GLU P  1 49  ? 46.981  134.124 41.352  1.00 56.11 ? 49   GLU P OE2 1 
ATOM   16832 N  N   . PHE P  1 50  ? 44.766  132.082 36.359  1.00 57.20 ? 50   PHE P N   1 
ATOM   16833 C  CA  . PHE P  1 50  ? 45.618  131.031 35.794  1.00 57.17 ? 50   PHE P CA  1 
ATOM   16834 C  C   . PHE P  1 50  ? 45.287  130.641 34.360  1.00 57.03 ? 50   PHE P C   1 
ATOM   16835 O  O   . PHE P  1 50  ? 44.117  130.521 34.003  1.00 56.86 ? 50   PHE P O   1 
ATOM   16836 C  CB  . PHE P  1 50  ? 45.579  129.788 36.683  1.00 57.26 ? 50   PHE P CB  1 
ATOM   16837 C  CG  . PHE P  1 50  ? 45.735  130.093 38.138  1.00 57.49 ? 50   PHE P CG  1 
ATOM   16838 C  CD1 . PHE P  1 50  ? 46.917  130.626 38.619  1.00 58.04 ? 50   PHE P CD1 1 
ATOM   16839 C  CD2 . PHE P  1 50  ? 44.694  129.867 39.019  1.00 58.14 ? 50   PHE P CD2 1 
ATOM   16840 C  CE1 . PHE P  1 50  ? 47.067  130.917 39.955  1.00 58.26 ? 50   PHE P CE1 1 
ATOM   16841 C  CE2 . PHE P  1 50  ? 44.833  130.157 40.363  1.00 58.58 ? 50   PHE P CE2 1 
ATOM   16842 C  CZ  . PHE P  1 50  ? 46.023  130.684 40.832  1.00 58.76 ? 50   PHE P CZ  1 
ATOM   16843 N  N   . GLY P  1 51  ? 46.330  130.426 33.558  1.00 56.99 ? 51   GLY P N   1 
ATOM   16844 C  CA  . GLY P  1 51  ? 46.177  129.991 32.176  1.00 57.11 ? 51   GLY P CA  1 
ATOM   16845 C  C   . GLY P  1 51  ? 46.051  128.480 32.157  1.00 57.19 ? 51   GLY P C   1 
ATOM   16846 O  O   . GLY P  1 51  ? 46.669  127.785 31.343  1.00 57.05 ? 51   GLY P O   1 
ATOM   16847 N  N   . ASP P  1 52  ? 45.238  127.984 33.086  1.00 57.27 ? 52   ASP P N   1 
ATOM   16848 C  CA  . ASP P  1 52  ? 44.999  126.561 33.283  1.00 57.32 ? 52   ASP P CA  1 
ATOM   16849 C  C   . ASP P  1 52  ? 43.588  126.167 32.831  1.00 57.48 ? 52   ASP P C   1 
ATOM   16850 O  O   . ASP P  1 52  ? 42.587  126.567 33.443  1.00 57.48 ? 52   ASP P O   1 
ATOM   16851 C  CB  . ASP P  1 52  ? 45.201  126.216 34.763  1.00 57.39 ? 52   ASP P CB  1 
ATOM   16852 C  CG  . ASP P  1 52  ? 45.091  124.731 35.044  1.00 57.33 ? 52   ASP P CG  1 
ATOM   16853 O  OD1 . ASP P  1 52  ? 44.432  124.022 34.257  1.00 57.42 ? 52   ASP P OD1 1 
ATOM   16854 O  OD2 . ASP P  1 52  ? 45.628  124.185 36.032  1.00 57.68 ? 52   ASP P OD2 1 
ATOM   16855 N  N   . ASN P  1 53  ? 43.525  125.380 31.757  1.00 57.47 ? 53   ASN P N   1 
ATOM   16856 C  CA  . ASN P  1 53  ? 42.265  124.911 31.188  1.00 57.43 ? 53   ASN P CA  1 
ATOM   16857 C  C   . ASN P  1 53  ? 42.132  123.395 31.341  1.00 57.35 ? 53   ASN P C   1 
ATOM   16858 O  O   . ASN P  1 53  ? 41.347  122.752 30.642  1.00 57.32 ? 53   ASN P O   1 
ATOM   16859 C  CB  . ASN P  1 53  ? 42.183  125.307 29.707  1.00 57.46 ? 53   ASN P CB  1 
ATOM   16860 C  CG  . ASN P  1 53  ? 40.767  125.246 29.154  1.00 57.73 ? 53   ASN P CG  1 
ATOM   16861 O  OD1 . ASN P  1 53  ? 39.831  125.786 29.748  1.00 57.46 ? 53   ASN P OD1 1 
ATOM   16862 N  ND2 . ASN P  1 53  ? 40.607  124.596 28.004  1.00 57.89 ? 53   ASN P ND2 1 
ATOM   16863 N  N   . THR P  1 54  ? 42.907  122.829 32.263  1.00 57.30 ? 54   THR P N   1 
ATOM   16864 C  CA  . THR P  1 54  ? 42.900  121.385 32.487  1.00 57.35 ? 54   THR P CA  1 
ATOM   16865 C  C   . THR P  1 54  ? 41.498  120.834 32.738  1.00 57.28 ? 54   THR P C   1 
ATOM   16866 O  O   . THR P  1 54  ? 41.156  119.754 32.262  1.00 57.32 ? 54   THR P O   1 
ATOM   16867 C  CB  . THR P  1 54  ? 43.855  120.987 33.643  1.00 57.40 ? 54   THR P CB  1 
ATOM   16868 O  OG1 . THR P  1 54  ? 43.730  121.919 34.724  1.00 57.35 ? 54   THR P OG1 1 
ATOM   16869 C  CG2 . THR P  1 54  ? 45.310  121.138 33.216  1.00 57.43 ? 54   THR P CG2 1 
ATOM   16870 N  N   . ALA P  1 55  ? 40.691  121.575 33.486  1.00 57.20 ? 55   ALA P N   1 
ATOM   16871 C  CA  . ALA P  1 55  ? 39.330  121.148 33.773  1.00 57.17 ? 55   ALA P CA  1 
ATOM   16872 C  C   . ALA P  1 55  ? 38.350  122.127 33.148  1.00 57.15 ? 55   ALA P C   1 
ATOM   16873 O  O   . ALA P  1 55  ? 37.278  122.380 33.697  1.00 57.25 ? 55   ALA P O   1 
ATOM   16874 C  CB  . ALA P  1 55  ? 39.105  121.049 35.280  1.00 57.14 ? 55   ALA P CB  1 
ATOM   16875 N  N   . GLY P  1 56  ? 38.723  122.674 31.995  1.00 57.06 ? 56   GLY P N   1 
ATOM   16876 C  CA  . GLY P  1 56  ? 37.902  123.665 31.327  1.00 57.02 ? 56   GLY P CA  1 
ATOM   16877 C  C   . GLY P  1 56  ? 38.125  125.037 31.940  1.00 57.01 ? 56   GLY P C   1 
ATOM   16878 O  O   . GLY P  1 56  ? 39.153  125.283 32.571  1.00 56.93 ? 56   GLY P O   1 
ATOM   16879 N  N   . CYS P  1 57  ? 37.155  125.927 31.765  1.00 57.02 ? 57   CYS P N   1 
ATOM   16880 C  CA  . CYS P  1 57  ? 37.249  127.293 32.279  1.00 57.01 ? 57   CYS P CA  1 
ATOM   16881 C  C   . CYS P  1 57  ? 37.329  127.387 33.804  1.00 57.20 ? 57   CYS P C   1 
ATOM   16882 O  O   . CYS P  1 57  ? 37.871  128.352 34.345  1.00 57.16 ? 57   CYS P O   1 
ATOM   16883 C  CB  . CYS P  1 57  ? 36.065  128.121 31.779  1.00 56.96 ? 57   CYS P CB  1 
ATOM   16884 S  SG  . CYS P  1 57  ? 36.044  128.355 29.991  1.00 56.34 ? 57   CYS P SG  1 
ATOM   16885 N  N   . THR P  1 58  ? 36.786  126.388 34.492  1.00 57.40 ? 58   THR P N   1 
ATOM   16886 C  CA  . THR P  1 58  ? 36.777  126.379 35.953  1.00 57.62 ? 58   THR P CA  1 
ATOM   16887 C  C   . THR P  1 58  ? 38.181  126.494 36.546  1.00 57.80 ? 58   THR P C   1 
ATOM   16888 O  O   . THR P  1 58  ? 38.403  127.235 37.509  1.00 57.66 ? 58   THR P O   1 
ATOM   16889 C  CB  . THR P  1 58  ? 36.090  125.099 36.486  1.00 57.58 ? 58   THR P CB  1 
ATOM   16890 O  OG1 . THR P  1 58  ? 34.764  124.998 35.950  1.00 57.48 ? 58   THR P OG1 1 
ATOM   16891 C  CG2 . THR P  1 58  ? 35.857  125.199 37.994  1.00 57.79 ? 58   THR P CG2 1 
ATOM   16892 N  N   . SER P  1 59  ? 39.126  125.763 35.960  1.00 58.00 ? 59   SER P N   1 
ATOM   16893 C  CA  . SER P  1 59  ? 40.499  125.725 36.461  1.00 58.21 ? 59   SER P CA  1 
ATOM   16894 C  C   . SER P  1 59  ? 41.282  127.023 36.246  1.00 58.41 ? 59   SER P C   1 
ATOM   16895 O  O   . SER P  1 59  ? 42.438  127.132 36.665  1.00 58.31 ? 59   SER P O   1 
ATOM   16896 C  CB  . SER P  1 59  ? 41.253  124.524 35.878  1.00 58.22 ? 59   SER P CB  1 
ATOM   16897 O  OG  . SER P  1 59  ? 40.964  124.354 34.498  1.00 58.25 ? 59   SER P OG  1 
ATOM   16898 N  N   . ALA P  1 60  ? 40.649  128.003 35.602  1.00 58.67 ? 60   ALA P N   1 
ATOM   16899 C  CA  . ALA P  1 60  ? 41.265  129.309 35.385  1.00 59.03 ? 60   ALA P CA  1 
ATOM   16900 C  C   . ALA P  1 60  ? 41.370  130.093 36.697  1.00 59.34 ? 60   ALA P C   1 
ATOM   16901 O  O   . ALA P  1 60  ? 42.050  131.117 36.774  1.00 59.42 ? 60   ALA P O   1 
ATOM   16902 C  CB  . ALA P  1 60  ? 40.480  130.104 34.353  1.00 58.91 ? 60   ALA P CB  1 
ATOM   16903 N  N   . GLY P  1 61  ? 40.699  129.603 37.732  1.00 59.65 ? 61   GLY P N   1 
ATOM   16904 C  CA  . GLY P  1 61  ? 40.715  130.275 39.015  1.00 60.18 ? 61   GLY P CA  1 
ATOM   16905 C  C   . GLY P  1 61  ? 39.885  131.544 38.977  1.00 60.64 ? 61   GLY P C   1 
ATOM   16906 O  O   . GLY P  1 61  ? 39.035  131.718 38.102  1.00 60.47 ? 61   GLY P O   1 
ATOM   16907 N  N   . PRO P  1 62  ? 40.137  132.440 39.924  1.00 61.00 ? 62   PRO P N   1 
ATOM   16908 C  CA  . PRO P  1 62  ? 39.385  133.692 40.026  1.00 61.36 ? 62   PRO P CA  1 
ATOM   16909 C  C   . PRO P  1 62  ? 39.980  134.806 39.169  1.00 61.73 ? 62   PRO P C   1 
ATOM   16910 O  O   . PRO P  1 62  ? 40.924  134.566 38.410  1.00 61.64 ? 62   PRO P O   1 
ATOM   16911 C  CB  . PRO P  1 62  ? 39.517  134.029 41.507  1.00 61.46 ? 62   PRO P CB  1 
ATOM   16912 C  CG  . PRO P  1 62  ? 40.914  133.552 41.847  1.00 61.33 ? 62   PRO P CG  1 
ATOM   16913 C  CD  . PRO P  1 62  ? 41.173  132.336 40.968  1.00 61.06 ? 62   PRO P CD  1 
ATOM   16914 N  N   . HIS P  1 63  ? 39.419  136.006 39.288  1.00 61.97 ? 63   HIS P N   1 
ATOM   16915 C  CA  . HIS P  1 63  ? 39.901  137.164 38.544  1.00 62.35 ? 63   HIS P CA  1 
ATOM   16916 C  C   . HIS P  1 63  ? 41.340  137.498 38.933  1.00 62.51 ? 63   HIS P C   1 
ATOM   16917 O  O   . HIS P  1 63  ? 41.711  137.405 40.109  1.00 62.35 ? 63   HIS P O   1 
ATOM   16918 C  CB  . HIS P  1 63  ? 39.001  138.374 38.812  1.00 62.44 ? 63   HIS P CB  1 
ATOM   16919 C  CG  . HIS P  1 63  ? 37.595  138.199 38.330  1.00 62.88 ? 63   HIS P CG  1 
ATOM   16920 N  ND1 . HIS P  1 63  ? 36.626  139.164 38.495  1.00 63.62 ? 63   HIS P ND1 1 
ATOM   16921 C  CD2 . HIS P  1 63  ? 36.997  137.175 37.676  1.00 63.60 ? 63   HIS P CD2 1 
ATOM   16922 C  CE1 . HIS P  1 63  ? 35.490  138.740 37.969  1.00 63.45 ? 63   HIS P CE1 1 
ATOM   16923 N  NE2 . HIS P  1 63  ? 35.688  137.535 37.467  1.00 63.37 ? 63   HIS P NE2 1 
ATOM   16924 N  N   . PHE P  1 64  ? 42.150  137.869 37.941  1.00 62.61 ? 64   PHE P N   1 
ATOM   16925 C  CA  . PHE P  1 64  ? 43.532  138.272 38.188  1.00 62.66 ? 64   PHE P CA  1 
ATOM   16926 C  C   . PHE P  1 64  ? 43.519  139.472 39.132  1.00 62.81 ? 64   PHE P C   1 
ATOM   16927 O  O   . PHE P  1 64  ? 43.014  140.541 38.783  1.00 62.67 ? 64   PHE P O   1 
ATOM   16928 C  CB  . PHE P  1 64  ? 44.233  138.618 36.872  1.00 62.87 ? 64   PHE P CB  1 
ATOM   16929 C  CG  . PHE P  1 64  ? 45.684  138.969 37.033  1.00 62.87 ? 64   PHE P CG  1 
ATOM   16930 C  CD1 . PHE P  1 64  ? 46.481  138.283 37.935  1.00 62.82 ? 64   PHE P CD1 1 
ATOM   16931 C  CD2 . PHE P  1 64  ? 46.250  139.983 36.282  1.00 62.96 ? 64   PHE P CD2 1 
ATOM   16932 C  CE1 . PHE P  1 64  ? 47.812  138.607 38.088  1.00 62.62 ? 64   PHE P CE1 1 
ATOM   16933 C  CE2 . PHE P  1 64  ? 47.581  140.310 36.430  1.00 62.85 ? 64   PHE P CE2 1 
ATOM   16934 C  CZ  . PHE P  1 64  ? 48.364  139.621 37.333  1.00 62.72 ? 64   PHE P CZ  1 
ATOM   16935 N  N   . ASN P  1 65  ? 44.072  139.289 40.329  1.00 62.83 ? 65   ASN P N   1 
ATOM   16936 C  CA  . ASN P  1 65  ? 44.013  140.311 41.378  1.00 63.02 ? 65   ASN P CA  1 
ATOM   16937 C  C   . ASN P  1 65  ? 45.294  140.362 42.210  1.00 63.05 ? 65   ASN P C   1 
ATOM   16938 O  O   . ASN P  1 65  ? 45.283  140.037 43.397  1.00 63.19 ? 65   ASN P O   1 
ATOM   16939 C  CB  . ASN P  1 65  ? 42.794  140.022 42.268  1.00 62.89 ? 65   ASN P CB  1 
ATOM   16940 C  CG  . ASN P  1 65  ? 42.593  141.045 43.383  1.00 63.09 ? 65   ASN P CG  1 
ATOM   16941 O  OD1 . ASN P  1 65  ? 43.017  142.197 43.288  1.00 63.41 ? 65   ASN P OD1 1 
ATOM   16942 N  ND2 . ASN P  1 65  ? 41.921  140.617 44.445  1.00 62.02 ? 65   ASN P ND2 1 
ATOM   16943 N  N   . PRO P  1 66  ? 46.400  140.764 41.585  1.00 63.20 ? 66   PRO P N   1 
ATOM   16944 C  CA  . PRO P  1 66  ? 47.694  140.842 42.271  1.00 63.35 ? 66   PRO P CA  1 
ATOM   16945 C  C   . PRO P  1 66  ? 47.727  141.896 43.380  1.00 63.54 ? 66   PRO P C   1 
ATOM   16946 O  O   . PRO P  1 66  ? 48.583  141.812 44.260  1.00 63.58 ? 66   PRO P O   1 
ATOM   16947 C  CB  . PRO P  1 66  ? 48.653  141.233 41.144  1.00 63.27 ? 66   PRO P CB  1 
ATOM   16948 C  CG  . PRO P  1 66  ? 47.783  141.934 40.171  1.00 63.17 ? 66   PRO P CG  1 
ATOM   16949 C  CD  . PRO P  1 66  ? 46.517  141.133 40.162  1.00 63.18 ? 66   PRO P CD  1 
ATOM   16950 N  N   . LEU P  1 67  ? 46.815  142.865 43.337  1.00 63.83 ? 67   LEU P N   1 
ATOM   16951 C  CA  . LEU P  1 67  ? 46.765  143.926 44.347  1.00 64.09 ? 67   LEU P CA  1 
ATOM   16952 C  C   . LEU P  1 67  ? 45.774  143.613 45.455  1.00 64.16 ? 67   LEU P C   1 
ATOM   16953 O  O   . LEU P  1 67  ? 45.572  144.417 46.370  1.00 64.08 ? 67   LEU P O   1 
ATOM   16954 C  CB  . LEU P  1 67  ? 46.420  145.271 43.706  1.00 64.22 ? 67   LEU P CB  1 
ATOM   16955 C  CG  . LEU P  1 67  ? 47.464  145.793 42.716  1.00 64.68 ? 67   LEU P CG  1 
ATOM   16956 C  CD1 . LEU P  1 67  ? 46.986  147.072 42.032  1.00 65.17 ? 67   LEU P CD1 1 
ATOM   16957 C  CD2 . LEU P  1 67  ? 48.804  146.009 43.415  1.00 64.94 ? 67   LEU P CD2 1 
ATOM   16958 N  N   . SER P  1 68  ? 45.156  142.441 45.358  1.00 64.26 ? 68   SER P N   1 
ATOM   16959 C  CA  . SER P  1 68  ? 44.211  141.976 46.368  1.00 64.54 ? 68   SER P CA  1 
ATOM   16960 C  C   . SER P  1 68  ? 43.116  142.995 46.680  1.00 64.60 ? 68   SER P C   1 
ATOM   16961 O  O   . SER P  1 68  ? 42.939  143.396 47.831  1.00 64.61 ? 68   SER P O   1 
ATOM   16962 C  CB  . SER P  1 68  ? 44.950  141.574 47.649  1.00 64.52 ? 68   SER P CB  1 
ATOM   16963 O  OG  . SER P  1 68  ? 45.845  140.502 47.396  1.00 64.56 ? 68   SER P OG  1 
ATOM   16964 N  N   . ARG P  1 69  ? 42.383  143.408 45.651  1.00 64.69 ? 69   ARG P N   1 
ATOM   16965 C  CA  . ARG P  1 69  ? 41.291  144.358 45.830  1.00 64.75 ? 69   ARG P CA  1 
ATOM   16966 C  C   . ARG P  1 69  ? 39.938  143.704 45.582  1.00 64.61 ? 69   ARG P C   1 
ATOM   16967 O  O   . ARG P  1 69  ? 39.860  142.525 45.238  1.00 64.46 ? 69   ARG P O   1 
ATOM   16968 C  CB  . ARG P  1 69  ? 41.476  145.569 44.915  1.00 64.79 ? 69   ARG P CB  1 
ATOM   16969 C  CG  . ARG P  1 69  ? 42.725  146.366 45.232  1.00 65.60 ? 69   ARG P CG  1 
ATOM   16970 C  CD  . ARG P  1 69  ? 42.787  147.727 44.574  1.00 66.77 ? 69   ARG P CD  1 
ATOM   16971 N  NE  . ARG P  1 69  ? 43.992  148.451 44.966  1.00 67.67 ? 69   ARG P NE  1 
ATOM   16972 C  CZ  . ARG P  1 69  ? 44.406  149.570 44.392  1.00 68.19 ? 69   ARG P CZ  1 
ATOM   16973 N  NH1 . ARG P  1 69  ? 43.710  150.102 43.395  1.00 68.56 ? 69   ARG P NH1 1 
ATOM   16974 N  NH2 . ARG P  1 69  ? 45.516  150.160 44.813  1.00 68.27 ? 69   ARG P NH2 1 
ATOM   16975 N  N   . LYS P  1 70  ? 38.872  144.471 45.775  1.00 64.56 ? 70   LYS P N   1 
ATOM   16976 C  CA  . LYS P  1 70  ? 37.530  143.961 45.547  1.00 64.55 ? 70   LYS P CA  1 
ATOM   16977 C  C   . LYS P  1 70  ? 37.162  144.121 44.072  1.00 64.53 ? 70   LYS P C   1 
ATOM   16978 O  O   . LYS P  1 70  ? 37.744  144.942 43.360  1.00 64.41 ? 70   LYS P O   1 
ATOM   16979 C  CB  . LYS P  1 70  ? 36.516  144.690 46.434  1.00 64.52 ? 70   LYS P CB  1 
ATOM   16980 C  CG  . LYS P  1 70  ? 36.856  144.719 47.927  1.00 64.78 ? 70   LYS P CG  1 
ATOM   16981 C  CD  . LYS P  1 70  ? 36.638  143.369 48.599  1.00 64.67 ? 70   LYS P CD  1 
ATOM   16982 C  CE  . LYS P  1 70  ? 36.588  143.506 50.119  1.00 65.00 ? 70   LYS P CE  1 
ATOM   16983 N  NZ  . LYS P  1 70  ? 35.355  144.195 50.597  1.00 64.37 ? 70   LYS P NZ  1 
ATOM   16984 N  N   . HIS P  1 71  ? 36.202  143.328 43.615  1.00 64.53 ? 71   HIS P N   1 
ATOM   16985 C  CA  . HIS P  1 71  ? 35.755  143.399 42.232  1.00 64.63 ? 71   HIS P CA  1 
ATOM   16986 C  C   . HIS P  1 71  ? 35.104  144.738 41.928  1.00 64.80 ? 71   HIS P C   1 
ATOM   16987 O  O   . HIS P  1 71  ? 34.426  145.315 42.775  1.00 64.77 ? 71   HIS P O   1 
ATOM   16988 C  CB  . HIS P  1 71  ? 34.760  142.284 41.935  1.00 64.59 ? 71   HIS P CB  1 
ATOM   16989 C  CG  . HIS P  1 71  ? 34.197  142.341 40.552  1.00 64.69 ? 71   HIS P CG  1 
ATOM   16990 N  ND1 . HIS P  1 71  ? 34.869  141.846 39.457  1.00 64.85 ? 71   HIS P ND1 1 
ATOM   16991 C  CD2 . HIS P  1 71  ? 33.034  142.850 40.083  1.00 64.72 ? 71   HIS P CD2 1 
ATOM   16992 C  CE1 . HIS P  1 71  ? 34.141  142.039 38.372  1.00 64.61 ? 71   HIS P CE1 1 
ATOM   16993 N  NE2 . HIS P  1 71  ? 33.023  142.647 38.724  1.00 64.89 ? 71   HIS P NE2 1 
ATOM   16994 N  N   . GLY P  1 72  ? 35.305  145.228 40.712  1.00 64.99 ? 72   GLY P N   1 
ATOM   16995 C  CA  . GLY P  1 72  ? 34.699  146.481 40.308  1.00 65.35 ? 72   GLY P CA  1 
ATOM   16996 C  C   . GLY P  1 72  ? 34.630  146.639 38.804  1.00 65.53 ? 72   GLY P C   1 
ATOM   16997 O  O   . GLY P  1 72  ? 34.890  145.696 38.056  1.00 65.43 ? 72   GLY P O   1 
ATOM   16998 N  N   . GLY P  1 73  ? 34.259  147.838 38.363  1.00 65.76 ? 73   GLY P N   1 
ATOM   16999 C  CA  . GLY P  1 73  ? 34.211  148.157 36.949  1.00 65.97 ? 73   GLY P CA  1 
ATOM   17000 C  C   . GLY P  1 73  ? 35.589  148.595 36.488  1.00 66.13 ? 73   GLY P C   1 
ATOM   17001 O  O   . GLY P  1 73  ? 36.446  148.917 37.312  1.00 66.06 ? 73   GLY P O   1 
ATOM   17002 N  N   . PRO P  1 74  ? 35.809  148.609 35.176  1.00 66.28 ? 74   PRO P N   1 
ATOM   17003 C  CA  . PRO P  1 74  ? 37.112  148.988 34.614  1.00 66.37 ? 74   PRO P CA  1 
ATOM   17004 C  C   . PRO P  1 74  ? 37.544  150.392 35.028  1.00 66.55 ? 74   PRO P C   1 
ATOM   17005 O  O   . PRO P  1 74  ? 38.740  150.673 35.110  1.00 66.54 ? 74   PRO P O   1 
ATOM   17006 C  CB  . PRO P  1 74  ? 36.861  148.957 33.101  1.00 66.36 ? 74   PRO P CB  1 
ATOM   17007 C  CG  . PRO P  1 74  ? 35.686  148.070 32.920  1.00 66.30 ? 74   PRO P CG  1 
ATOM   17008 C  CD  . PRO P  1 74  ? 34.826  148.265 34.134  1.00 66.29 ? 74   PRO P CD  1 
ATOM   17009 N  N   . LYS P  1 75  ? 36.564  151.249 35.298  1.00 66.74 ? 75   LYS P N   1 
ATOM   17010 C  CA  . LYS P  1 75  ? 36.796  152.651 35.621  1.00 66.90 ? 75   LYS P CA  1 
ATOM   17011 C  C   . LYS P  1 75  ? 36.911  152.931 37.123  1.00 67.24 ? 75   LYS P C   1 
ATOM   17012 O  O   . LYS P  1 75  ? 37.149  154.070 37.529  1.00 67.24 ? 75   LYS P O   1 
ATOM   17013 C  CB  . LYS P  1 75  ? 35.676  153.496 34.997  1.00 66.77 ? 75   LYS P CB  1 
ATOM   17014 C  CG  . LYS P  1 75  ? 35.773  153.596 33.470  1.00 66.17 ? 75   LYS P CG  1 
ATOM   17015 C  CD  . LYS P  1 75  ? 34.430  153.415 32.760  1.00 64.99 ? 75   LYS P CD  1 
ATOM   17016 N  N   . ASP P  1 76  ? 36.745  151.894 37.940  1.00 67.61 ? 76   ASP P N   1 
ATOM   17017 C  CA  . ASP P  1 76  ? 36.827  152.034 39.394  1.00 68.03 ? 76   ASP P CA  1 
ATOM   17018 C  C   . ASP P  1 76  ? 38.251  151.823 39.912  1.00 68.18 ? 76   ASP P C   1 
ATOM   17019 O  O   . ASP P  1 76  ? 38.997  150.999 39.380  1.00 68.20 ? 76   ASP P O   1 
ATOM   17020 C  CB  . ASP P  1 76  ? 35.884  151.045 40.086  1.00 68.14 ? 76   ASP P CB  1 
ATOM   17021 C  CG  . ASP P  1 76  ? 34.436  151.216 39.662  1.00 68.59 ? 76   ASP P CG  1 
ATOM   17022 O  OD1 . ASP P  1 76  ? 34.040  152.346 39.296  1.00 68.98 ? 76   ASP P OD1 1 
ATOM   17023 O  OD2 . ASP P  1 76  ? 33.619  150.270 39.669  1.00 68.97 ? 76   ASP P OD2 1 
ATOM   17024 N  N   . GLU P  1 77  ? 38.628  152.570 40.947  1.00 68.35 ? 77   GLU P N   1 
ATOM   17025 C  CA  . GLU P  1 77  ? 39.943  152.400 41.550  1.00 68.54 ? 77   GLU P CA  1 
ATOM   17026 C  C   . GLU P  1 77  ? 39.954  151.046 42.233  1.00 68.52 ? 77   GLU P C   1 
ATOM   17027 O  O   . GLU P  1 77  ? 40.925  150.295 42.146  1.00 68.53 ? 77   GLU P O   1 
ATOM   17028 C  CB  . GLU P  1 77  ? 40.237  153.498 42.570  1.00 68.65 ? 77   GLU P CB  1 
ATOM   17029 C  CG  . GLU P  1 77  ? 41.638  153.401 43.150  1.00 69.26 ? 77   GLU P CG  1 
ATOM   17030 C  CD  . GLU P  1 77  ? 41.858  154.326 44.329  1.00 70.06 ? 77   GLU P CD  1 
ATOM   17031 O  OE1 . GLU P  1 77  ? 41.044  155.254 44.528  1.00 70.68 ? 77   GLU P OE1 1 
ATOM   17032 O  OE2 . GLU P  1 77  ? 42.852  154.121 45.059  1.00 70.50 ? 77   GLU P OE2 1 
ATOM   17033 N  N   . GLU P  1 78  ? 38.853  150.746 42.911  1.00 68.55 ? 78   GLU P N   1 
ATOM   17034 C  CA  . GLU P  1 78  ? 38.679  149.466 43.575  1.00 68.54 ? 78   GLU P CA  1 
ATOM   17035 C  C   . GLU P  1 78  ? 38.170  148.454 42.556  1.00 68.31 ? 78   GLU P C   1 
ATOM   17036 O  O   . GLU P  1 78  ? 36.965  148.279 42.377  1.00 68.37 ? 78   GLU P O   1 
ATOM   17037 C  CB  . GLU P  1 78  ? 37.701  149.593 44.745  1.00 68.73 ? 78   GLU P CB  1 
ATOM   17038 C  CG  . GLU P  1 78  ? 37.656  148.378 45.657  1.00 69.41 ? 78   GLU P CG  1 
ATOM   17039 C  CD  . GLU P  1 78  ? 38.996  148.079 46.300  1.00 70.37 ? 78   GLU P CD  1 
ATOM   17040 O  OE1 . GLU P  1 78  ? 39.916  148.918 46.191  1.00 70.77 ? 78   GLU P OE1 1 
ATOM   17041 O  OE2 . GLU P  1 78  ? 39.129  147.003 46.919  1.00 71.00 ? 78   GLU P OE2 1 
ATOM   17042 N  N   . ARG P  1 79  ? 39.104  147.803 41.878  1.00 67.86 ? 79   ARG P N   1 
ATOM   17043 C  CA  . ARG P  1 79  ? 38.765  146.820 40.866  1.00 67.57 ? 79   ARG P CA  1 
ATOM   17044 C  C   . ARG P  1 79  ? 39.901  145.828 40.734  1.00 67.23 ? 79   ARG P C   1 
ATOM   17045 O  O   . ARG P  1 79  ? 41.038  146.114 41.106  1.00 67.18 ? 79   ARG P O   1 
ATOM   17046 C  CB  . ARG P  1 79  ? 38.555  147.502 39.516  1.00 67.53 ? 79   ARG P CB  1 
ATOM   17047 C  CG  . ARG P  1 79  ? 39.794  148.224 39.007  1.00 67.53 ? 79   ARG P CG  1 
ATOM   17048 C  CD  . ARG P  1 79  ? 39.798  148.508 37.510  1.00 67.97 ? 79   ARG P CD  1 
ATOM   17049 N  NE  . ARG P  1 79  ? 40.329  147.388 36.735  1.00 68.20 ? 79   ARG P NE  1 
ATOM   17050 C  CZ  . ARG P  1 79  ? 40.694  147.463 35.458  1.00 68.40 ? 79   ARG P CZ  1 
ATOM   17051 N  NH1 . ARG P  1 79  ? 40.583  148.607 34.796  1.00 68.57 ? 79   ARG P NH1 1 
ATOM   17052 N  NH2 . ARG P  1 79  ? 41.170  146.391 34.839  1.00 67.86 ? 79   ARG P NH2 1 
ATOM   17053 N  N   . HIS P  1 80  ? 39.591  144.653 40.206  1.00 66.91 ? 80   HIS P N   1 
ATOM   17054 C  CA  . HIS P  1 80  ? 40.620  143.664 39.947  1.00 66.65 ? 80   HIS P CA  1 
ATOM   17055 C  C   . HIS P  1 80  ? 41.324  144.073 38.658  1.00 66.37 ? 80   HIS P C   1 
ATOM   17056 O  O   . HIS P  1 80  ? 40.716  144.701 37.789  1.00 66.29 ? 80   HIS P O   1 
ATOM   17057 C  CB  . HIS P  1 80  ? 40.001  142.274 39.792  1.00 66.71 ? 80   HIS P CB  1 
ATOM   17058 C  CG  . HIS P  1 80  ? 39.253  141.804 41.002  1.00 67.01 ? 80   HIS P CG  1 
ATOM   17059 N  ND1 . HIS P  1 80  ? 38.129  141.010 40.921  1.00 67.33 ? 80   HIS P ND1 1 
ATOM   17060 C  CD2 . HIS P  1 80  ? 39.473  142.010 42.323  1.00 67.10 ? 80   HIS P CD2 1 
ATOM   17061 C  CE1 . HIS P  1 80  ? 37.689  140.746 42.138  1.00 67.26 ? 80   HIS P CE1 1 
ATOM   17062 N  NE2 . HIS P  1 80  ? 38.485  141.343 43.007  1.00 67.34 ? 80   HIS P NE2 1 
ATOM   17063 N  N   . VAL P  1 81  ? 42.604  143.736 38.533  1.00 66.05 ? 81   VAL P N   1 
ATOM   17064 C  CA  . VAL P  1 81  ? 43.335  144.056 37.310  1.00 65.72 ? 81   VAL P CA  1 
ATOM   17065 C  C   . VAL P  1 81  ? 42.604  143.488 36.096  1.00 65.33 ? 81   VAL P C   1 
ATOM   17066 O  O   . VAL P  1 81  ? 42.539  144.127 35.047  1.00 65.36 ? 81   VAL P O   1 
ATOM   17067 C  CB  . VAL P  1 81  ? 44.781  143.520 37.335  1.00 65.68 ? 81   VAL P CB  1 
ATOM   17068 C  CG1 . VAL P  1 81  ? 45.381  143.540 35.932  1.00 65.85 ? 81   VAL P CG1 1 
ATOM   17069 C  CG2 . VAL P  1 81  ? 45.635  144.332 38.287  1.00 65.85 ? 81   VAL P CG2 1 
ATOM   17070 N  N   . GLY P  1 82  ? 42.032  142.298 36.258  1.00 65.02 ? 82   GLY P N   1 
ATOM   17071 C  CA  . GLY P  1 82  ? 41.341  141.615 35.175  1.00 64.57 ? 82   GLY P CA  1 
ATOM   17072 C  C   . GLY P  1 82  ? 39.884  141.993 34.965  1.00 64.22 ? 82   GLY P C   1 
ATOM   17073 O  O   . GLY P  1 82  ? 39.177  141.336 34.204  1.00 63.96 ? 82   GLY P O   1 
ATOM   17074 N  N   . ASP P  1 83  ? 39.431  143.042 35.646  1.00 63.85 ? 83   ASP P N   1 
ATOM   17075 C  CA  . ASP P  1 83  ? 38.062  143.517 35.484  1.00 63.63 ? 83   ASP P CA  1 
ATOM   17076 C  C   . ASP P  1 83  ? 37.974  144.405 34.257  1.00 63.44 ? 83   ASP P C   1 
ATOM   17077 O  O   . ASP P  1 83  ? 38.264  145.597 34.322  1.00 63.38 ? 83   ASP P O   1 
ATOM   17078 C  CB  . ASP P  1 83  ? 37.605  144.303 36.716  1.00 63.61 ? 83   ASP P CB  1 
ATOM   17079 C  CG  . ASP P  1 83  ? 37.395  143.419 37.921  1.00 63.46 ? 83   ASP P CG  1 
ATOM   17080 O  OD1 . ASP P  1 83  ? 37.233  142.195 37.731  1.00 63.29 ? 83   ASP P OD1 1 
ATOM   17081 O  OD2 . ASP P  1 83  ? 37.379  143.853 39.094  1.00 63.07 ? 83   ASP P OD2 1 
ATOM   17082 N  N   . LEU P  1 84  ? 37.578  143.825 33.133  1.00 63.37 ? 84   LEU P N   1 
ATOM   17083 C  CA  . LEU P  1 84  ? 37.462  144.592 31.902  1.00 63.26 ? 84   LEU P CA  1 
ATOM   17084 C  C   . LEU P  1 84  ? 36.017  144.966 31.626  1.00 63.35 ? 84   LEU P C   1 
ATOM   17085 O  O   . LEU P  1 84  ? 35.682  145.442 30.540  1.00 63.38 ? 84   LEU P O   1 
ATOM   17086 C  CB  . LEU P  1 84  ? 38.049  143.810 30.733  1.00 63.22 ? 84   LEU P CB  1 
ATOM   17087 C  CG  . LEU P  1 84  ? 39.525  143.473 30.918  1.00 62.83 ? 84   LEU P CG  1 
ATOM   17088 C  CD1 . LEU P  1 84  ? 40.006  142.575 29.789  1.00 63.15 ? 84   LEU P CD1 1 
ATOM   17089 C  CD2 . LEU P  1 84  ? 40.354  144.745 30.999  1.00 62.45 ? 84   LEU P CD2 1 
ATOM   17090 N  N   . GLY P  1 85  ? 35.163  144.742 32.619  1.00 63.45 ? 85   GLY P N   1 
ATOM   17091 C  CA  . GLY P  1 85  ? 33.757  145.081 32.515  1.00 63.53 ? 85   GLY P CA  1 
ATOM   17092 C  C   . GLY P  1 85  ? 32.919  144.148 31.663  1.00 63.60 ? 85   GLY P C   1 
ATOM   17093 O  O   . GLY P  1 85  ? 33.000  142.924 31.782  1.00 63.65 ? 85   GLY P O   1 
ATOM   17094 N  N   . ASN P  1 86  ? 32.106  144.743 30.798  1.00 63.67 ? 86   ASN P N   1 
ATOM   17095 C  CA  . ASN P  1 86  ? 31.193  143.996 29.946  1.00 63.74 ? 86   ASN P CA  1 
ATOM   17096 C  C   . ASN P  1 86  ? 31.457  144.198 28.462  1.00 63.71 ? 86   ASN P C   1 
ATOM   17097 O  O   . ASN P  1 86  ? 32.012  145.214 28.044  1.00 63.70 ? 86   ASN P O   1 
ATOM   17098 C  CB  . ASN P  1 86  ? 29.743  144.423 30.219  1.00 63.78 ? 86   ASN P CB  1 
ATOM   17099 C  CG  . ASN P  1 86  ? 29.191  143.864 31.518  1.00 63.94 ? 86   ASN P CG  1 
ATOM   17100 O  OD1 . ASN P  1 86  ? 29.091  142.648 31.692  1.00 64.17 ? 86   ASN P OD1 1 
ATOM   17101 N  ND2 . ASN P  1 86  ? 28.808  144.754 32.430  1.00 63.44 ? 86   ASN P ND2 1 
ATOM   17102 N  N   . VAL P  1 87  ? 31.048  143.210 27.675  1.00 63.74 ? 87   VAL P N   1 
ATOM   17103 C  CA  . VAL P  1 87  ? 31.077  143.308 26.225  1.00 63.64 ? 87   VAL P CA  1 
ATOM   17104 C  C   . VAL P  1 87  ? 29.624  143.211 25.783  1.00 63.66 ? 87   VAL P C   1 
ATOM   17105 O  O   . VAL P  1 87  ? 28.768  142.769 26.552  1.00 63.60 ? 87   VAL P O   1 
ATOM   17106 C  CB  . VAL P  1 87  ? 31.921  142.200 25.571  1.00 63.59 ? 87   VAL P CB  1 
ATOM   17107 C  CG1 . VAL P  1 87  ? 33.399  142.495 25.742  1.00 63.64 ? 87   VAL P CG1 1 
ATOM   17108 C  CG2 . VAL P  1 87  ? 31.566  140.837 26.143  1.00 63.46 ? 87   VAL P CG2 1 
ATOM   17109 N  N   . THR P  1 88  ? 29.336  143.617 24.554  1.00 63.65 ? 88   THR P N   1 
ATOM   17110 C  CA  . THR P  1 88  ? 27.952  143.660 24.103  1.00 63.67 ? 88   THR P CA  1 
ATOM   17111 C  C   . THR P  1 88  ? 27.664  142.828 22.858  1.00 63.62 ? 88   THR P C   1 
ATOM   17112 O  O   . THR P  1 88  ? 28.205  143.090 21.786  1.00 63.65 ? 88   THR P O   1 
ATOM   17113 C  CB  . THR P  1 88  ? 27.543  145.120 23.866  1.00 63.69 ? 88   THR P CB  1 
ATOM   17114 O  OG1 . THR P  1 88  ? 27.877  145.896 25.024  1.00 63.52 ? 88   THR P OG1 1 
ATOM   17115 C  CG2 . THR P  1 88  ? 26.029  145.242 23.766  1.00 63.83 ? 88   THR P CG2 1 
ATOM   17116 N  N   . ALA P  1 89  ? 26.795  141.834 23.011  1.00 63.58 ? 89   ALA P N   1 
ATOM   17117 C  CA  . ALA P  1 89  ? 26.391  140.983 21.899  1.00 63.61 ? 89   ALA P CA  1 
ATOM   17118 C  C   . ALA P  1 89  ? 25.116  141.536 21.281  1.00 63.64 ? 89   ALA P C   1 
ATOM   17119 O  O   . ALA P  1 89  ? 24.177  141.875 21.999  1.00 63.57 ? 89   ALA P O   1 
ATOM   17120 C  CB  . ALA P  1 89  ? 26.171  139.561 22.375  1.00 63.60 ? 89   ALA P CB  1 
ATOM   17121 N  N   . ASP P  1 90  ? 25.077  141.625 19.954  1.00 63.71 ? 90   ASP P N   1 
ATOM   17122 C  CA  . ASP P  1 90  ? 23.904  142.167 19.267  1.00 63.76 ? 90   ASP P CA  1 
ATOM   17123 C  C   . ASP P  1 90  ? 22.768  141.151 19.143  1.00 63.65 ? 90   ASP P C   1 
ATOM   17124 O  O   . ASP P  1 90  ? 22.804  140.086 19.761  1.00 63.66 ? 90   ASP P O   1 
ATOM   17125 C  CB  . ASP P  1 90  ? 24.278  142.736 17.892  1.00 63.88 ? 90   ASP P CB  1 
ATOM   17126 C  CG  . ASP P  1 90  ? 25.016  141.736 17.021  1.00 64.21 ? 90   ASP P CG  1 
ATOM   17127 O  OD1 . ASP P  1 90  ? 24.825  140.516 17.207  1.00 64.57 ? 90   ASP P OD1 1 
ATOM   17128 O  OD2 . ASP P  1 90  ? 25.809  142.083 16.119  1.00 64.54 ? 90   ASP P OD2 1 
ATOM   17129 N  N   . LYS P  1 91  ? 21.761  141.488 18.343  1.00 63.52 ? 91   LYS P N   1 
ATOM   17130 C  CA  . LYS P  1 91  ? 20.614  140.608 18.152  1.00 63.38 ? 91   LYS P CA  1 
ATOM   17131 C  C   . LYS P  1 91  ? 21.013  139.273 17.524  1.00 63.29 ? 91   LYS P C   1 
ATOM   17132 O  O   . LYS P  1 91  ? 20.321  138.269 17.688  1.00 63.27 ? 91   LYS P O   1 
ATOM   17133 C  CB  . LYS P  1 91  ? 19.532  141.301 17.319  1.00 63.35 ? 91   LYS P CB  1 
ATOM   17134 C  CG  . LYS P  1 91  ? 20.055  142.103 16.135  1.00 63.41 ? 91   LYS P CG  1 
ATOM   17135 C  CD  . LYS P  1 91  ? 18.905  142.715 15.337  1.00 63.42 ? 91   LYS P CD  1 
ATOM   17136 C  CE  . LYS P  1 91  ? 19.409  143.581 14.189  1.00 63.40 ? 91   LYS P CE  1 
ATOM   17137 N  NZ  . LYS P  1 91  ? 18.289  144.136 13.369  1.00 63.71 ? 91   LYS P NZ  1 
ATOM   17138 N  N   . ASP P  1 92  ? 22.140  139.269 16.819  1.00 63.19 ? 92   ASP P N   1 
ATOM   17139 C  CA  . ASP P  1 92  ? 22.639  138.060 16.170  1.00 63.12 ? 92   ASP P CA  1 
ATOM   17140 C  C   . ASP P  1 92  ? 23.553  137.254 17.085  1.00 63.05 ? 92   ASP P C   1 
ATOM   17141 O  O   . ASP P  1 92  ? 24.064  136.202 16.698  1.00 63.07 ? 92   ASP P O   1 
ATOM   17142 C  CB  . ASP P  1 92  ? 23.370  138.413 14.876  1.00 63.09 ? 92   ASP P CB  1 
ATOM   17143 C  CG  . ASP P  1 92  ? 22.424  138.839 13.777  1.00 63.25 ? 92   ASP P CG  1 
ATOM   17144 O  OD1 . ASP P  1 92  ? 21.366  138.193 13.628  1.00 63.38 ? 92   ASP P OD1 1 
ATOM   17145 O  OD2 . ASP P  1 92  ? 22.651  139.803 13.016  1.00 63.29 ? 92   ASP P OD2 1 
ATOM   17146 N  N   . GLY P  1 93  ? 23.761  137.754 18.298  1.00 62.97 ? 93   GLY P N   1 
ATOM   17147 C  CA  . GLY P  1 93  ? 24.603  137.076 19.263  1.00 62.80 ? 93   GLY P CA  1 
ATOM   17148 C  C   . GLY P  1 93  ? 26.078  137.359 19.068  1.00 62.78 ? 93   GLY P C   1 
ATOM   17149 O  O   . GLY P  1 93  ? 26.934  136.669 19.625  1.00 62.68 ? 93   GLY P O   1 
ATOM   17150 N  N   . VAL P  1 94  ? 26.381  138.381 18.274  1.00 62.73 ? 94   VAL P N   1 
ATOM   17151 C  CA  . VAL P  1 94  ? 27.768  138.741 18.008  1.00 62.70 ? 94   VAL P CA  1 
ATOM   17152 C  C   . VAL P  1 94  ? 28.180  139.987 18.785  1.00 62.58 ? 94   VAL P C   1 
ATOM   17153 O  O   . VAL P  1 94  ? 27.521  141.024 18.731  1.00 62.54 ? 94   VAL P O   1 
ATOM   17154 C  CB  . VAL P  1 94  ? 28.035  138.939 16.495  1.00 62.73 ? 94   VAL P CB  1 
ATOM   17155 C  CG1 . VAL P  1 94  ? 29.477  139.368 16.252  1.00 62.77 ? 94   VAL P CG1 1 
ATOM   17156 C  CG2 . VAL P  1 94  ? 27.724  137.661 15.724  1.00 62.78 ? 94   VAL P CG2 1 
ATOM   17157 N  N   . ALA P  1 95  ? 29.272  139.868 19.525  1.00 62.50 ? 95   ALA P N   1 
ATOM   17158 C  CA  . ALA P  1 95  ? 29.787  140.990 20.282  1.00 62.47 ? 95   ALA P CA  1 
ATOM   17159 C  C   . ALA P  1 95  ? 31.045  141.525 19.624  1.00 62.45 ? 95   ALA P C   1 
ATOM   17160 O  O   . ALA P  1 95  ? 32.065  140.840 19.569  1.00 62.46 ? 95   ALA P O   1 
ATOM   17161 C  CB  . ALA P  1 95  ? 30.076  140.576 21.715  1.00 62.48 ? 95   ALA P CB  1 
ATOM   17162 N  N   . ASP P  1 96  ? 30.968  142.739 19.097  1.00 62.43 ? 96   ASP P N   1 
ATOM   17163 C  CA  . ASP P  1 96  ? 32.150  143.372 18.541  1.00 62.44 ? 96   ASP P CA  1 
ATOM   17164 C  C   . ASP P  1 96  ? 32.864  144.082 19.681  1.00 62.36 ? 96   ASP P C   1 
ATOM   17165 O  O   . ASP P  1 96  ? 32.370  145.071 20.223  1.00 62.33 ? 96   ASP P O   1 
ATOM   17166 C  CB  . ASP P  1 96  ? 31.784  144.321 17.402  1.00 62.48 ? 96   ASP P CB  1 
ATOM   17167 C  CG  . ASP P  1 96  ? 31.444  143.576 16.129  1.00 62.88 ? 96   ASP P CG  1 
ATOM   17168 O  OD1 . ASP P  1 96  ? 32.053  142.505 15.904  1.00 63.52 ? 96   ASP P OD1 1 
ATOM   17169 O  OD2 . ASP P  1 96  ? 30.587  143.968 15.305  1.00 62.56 ? 96   ASP P OD2 1 
ATOM   17170 N  N   . VAL P  1 97  ? 34.019  143.545 20.056  1.00 62.26 ? 97   VAL P N   1 
ATOM   17171 C  CA  . VAL P  1 97  ? 34.779  144.045 21.195  1.00 62.14 ? 97   VAL P CA  1 
ATOM   17172 C  C   . VAL P  1 97  ? 35.827  145.079 20.812  1.00 62.19 ? 97   VAL P C   1 
ATOM   17173 O  O   . VAL P  1 97  ? 36.650  144.853 19.928  1.00 62.24 ? 97   VAL P O   1 
ATOM   17174 C  CB  . VAL P  1 97  ? 35.483  142.887 21.943  1.00 62.00 ? 97   VAL P CB  1 
ATOM   17175 C  CG1 . VAL P  1 97  ? 36.285  143.414 23.123  1.00 62.06 ? 97   VAL P CG1 1 
ATOM   17176 C  CG2 . VAL P  1 97  ? 34.471  141.851 22.399  1.00 61.69 ? 97   VAL P CG2 1 
ATOM   17177 N  N   . SER P  1 98  ? 35.785  146.220 21.487  1.00 62.29 ? 98   SER P N   1 
ATOM   17178 C  CA  . SER P  1 98  ? 36.768  147.269 21.288  1.00 62.33 ? 98   SER P CA  1 
ATOM   17179 C  C   . SER P  1 98  ? 36.955  147.952 22.628  1.00 62.44 ? 98   SER P C   1 
ATOM   17180 O  O   . SER P  1 98  ? 36.132  148.769 23.041  1.00 62.43 ? 98   SER P O   1 
ATOM   17181 C  CB  . SER P  1 98  ? 36.303  148.266 20.232  1.00 62.27 ? 98   SER P CB  1 
ATOM   17182 O  OG  . SER P  1 98  ? 37.387  149.059 19.782  1.00 62.18 ? 98   SER P OG  1 
ATOM   17183 N  N   . ILE P  1 99  ? 38.030  147.593 23.319  1.00 62.53 ? 99   ILE P N   1 
ATOM   17184 C  CA  . ILE P  1 99  ? 38.289  148.134 24.646  1.00 62.68 ? 99   ILE P CA  1 
ATOM   17185 C  C   . ILE P  1 99  ? 39.703  148.671 24.774  1.00 62.62 ? 99   ILE P C   1 
ATOM   17186 O  O   . ILE P  1 99  ? 40.619  148.225 24.085  1.00 62.51 ? 99   ILE P O   1 
ATOM   17187 C  CB  . ILE P  1 99  ? 38.044  147.048 25.719  1.00 62.67 ? 99   ILE P CB  1 
ATOM   17188 C  CG1 . ILE P  1 99  ? 36.560  146.680 25.778  1.00 62.94 ? 99   ILE P CG1 1 
ATOM   17189 C  CG2 . ILE P  1 99  ? 38.531  147.515 27.091  1.00 62.97 ? 99   ILE P CG2 1 
ATOM   17190 C  CD1 . ILE P  1 99  ? 36.253  145.541 26.724  1.00 63.61 ? 99   ILE P CD1 1 
ATOM   17191 N  N   . GLU P  1 100 ? 39.867  149.653 25.650  1.00 62.63 ? 100  GLU P N   1 
ATOM   17192 C  CA  . GLU P  1 100 ? 41.183  150.174 25.955  1.00 62.67 ? 100  GLU P CA  1 
ATOM   17193 C  C   . GLU P  1 100 ? 41.293  150.249 27.470  1.00 62.53 ? 100  GLU P C   1 
ATOM   17194 O  O   . GLU P  1 100 ? 40.429  150.813 28.142  1.00 62.55 ? 100  GLU P O   1 
ATOM   17195 C  CB  . GLU P  1 100 ? 41.408  151.537 25.305  1.00 62.80 ? 100  GLU P CB  1 
ATOM   17196 C  CG  . GLU P  1 100 ? 42.857  151.784 24.918  1.00 63.28 ? 100  GLU P CG  1 
ATOM   17197 C  CD  . GLU P  1 100 ? 43.043  153.057 24.113  1.00 64.18 ? 100  GLU P CD  1 
ATOM   17198 O  OE1 . GLU P  1 100 ? 42.463  153.156 23.010  1.00 64.57 ? 100  GLU P OE1 1 
ATOM   17199 O  OE2 . GLU P  1 100 ? 43.771  153.958 24.583  1.00 64.41 ? 100  GLU P OE2 1 
ATOM   17200 N  N   . ASP P  1 101 ? 42.350  149.652 28.005  1.00 62.40 ? 101  ASP P N   1 
ATOM   17201 C  CA  . ASP P  1 101 ? 42.545  149.602 29.446  1.00 62.32 ? 101  ASP P CA  1 
ATOM   17202 C  C   . ASP P  1 101 ? 44.012  149.819 29.801  1.00 62.05 ? 101  ASP P C   1 
ATOM   17203 O  O   . ASP P  1 101 ? 44.904  149.319 29.115  1.00 62.11 ? 101  ASP P O   1 
ATOM   17204 C  CB  . ASP P  1 101 ? 42.062  148.256 29.988  1.00 62.48 ? 101  ASP P CB  1 
ATOM   17205 C  CG  . ASP P  1 101 ? 41.997  148.224 31.497  1.00 62.62 ? 101  ASP P CG  1 
ATOM   17206 O  OD1 . ASP P  1 101 ? 40.960  148.643 32.056  1.00 63.35 ? 101  ASP P OD1 1 
ATOM   17207 O  OD2 . ASP P  1 101 ? 42.934  147.795 32.202  1.00 62.63 ? 101  ASP P OD2 1 
ATOM   17208 N  N   . SER P  1 102 ? 44.259  150.559 30.876  1.00 61.56 ? 102  SER P N   1 
ATOM   17209 C  CA  . SER P  1 102 ? 45.624  150.862 31.283  1.00 61.09 ? 102  SER P CA  1 
ATOM   17210 C  C   . SER P  1 102 ? 46.032  150.144 32.570  1.00 60.72 ? 102  SER P C   1 
ATOM   17211 O  O   . SER P  1 102 ? 47.151  150.317 33.056  1.00 60.62 ? 102  SER P O   1 
ATOM   17212 C  CB  . SER P  1 102 ? 45.813  152.376 31.419  1.00 61.21 ? 102  SER P CB  1 
ATOM   17213 O  OG  . SER P  1 102 ? 45.538  153.032 30.192  1.00 61.19 ? 102  SER P OG  1 
ATOM   17214 N  N   . VAL P  1 103 ? 45.125  149.339 33.117  1.00 60.31 ? 103  VAL P N   1 
ATOM   17215 C  CA  . VAL P  1 103 ? 45.411  148.580 34.332  1.00 59.97 ? 103  VAL P CA  1 
ATOM   17216 C  C   . VAL P  1 103 ? 46.078  147.263 33.956  1.00 59.59 ? 103  VAL P C   1 
ATOM   17217 O  O   . VAL P  1 103 ? 47.051  146.840 34.580  1.00 59.49 ? 103  VAL P O   1 
ATOM   17218 C  CB  . VAL P  1 103 ? 44.141  148.323 35.165  1.00 60.01 ? 103  VAL P CB  1 
ATOM   17219 C  CG1 . VAL P  1 103 ? 44.449  147.424 36.351  1.00 60.12 ? 103  VAL P CG1 1 
ATOM   17220 C  CG2 . VAL P  1 103 ? 43.550  149.640 35.639  1.00 60.20 ? 103  VAL P CG2 1 
ATOM   17221 N  N   . ILE P  1 104 ? 45.548  146.613 32.930  1.00 59.15 ? 104  ILE P N   1 
ATOM   17222 C  CA  . ILE P  1 104 ? 46.170  145.403 32.433  1.00 58.81 ? 104  ILE P CA  1 
ATOM   17223 C  C   . ILE P  1 104 ? 47.416  145.823 31.666  1.00 58.68 ? 104  ILE P C   1 
ATOM   17224 O  O   . ILE P  1 104 ? 47.593  147.004 31.356  1.00 58.58 ? 104  ILE P O   1 
ATOM   17225 C  CB  . ILE P  1 104 ? 45.217  144.618 31.522  1.00 58.79 ? 104  ILE P CB  1 
ATOM   17226 C  CG1 . ILE P  1 104 ? 44.806  145.467 30.318  1.00 58.74 ? 104  ILE P CG1 1 
ATOM   17227 C  CG2 . ILE P  1 104 ? 44.001  144.153 32.300  1.00 58.59 ? 104  ILE P CG2 1 
ATOM   17228 C  CD1 . ILE P  1 104 ? 44.200  144.661 29.192  1.00 58.76 ? 104  ILE P CD1 1 
ATOM   17229 N  N   . SER P  1 105 ? 48.282  144.857 31.375  1.00 58.47 ? 105  SER P N   1 
ATOM   17230 C  CA  . SER P  1 105 ? 49.519  145.130 30.653  1.00 58.37 ? 105  SER P CA  1 
ATOM   17231 C  C   . SER P  1 105 ? 50.063  143.858 30.017  1.00 58.19 ? 105  SER P C   1 
ATOM   17232 O  O   . SER P  1 105 ? 49.799  142.753 30.491  1.00 58.15 ? 105  SER P O   1 
ATOM   17233 C  CB  . SER P  1 105 ? 50.566  145.743 31.586  1.00 58.47 ? 105  SER P CB  1 
ATOM   17234 O  OG  . SER P  1 105 ? 51.717  146.146 30.864  1.00 58.68 ? 105  SER P OG  1 
ATOM   17235 N  N   . LEU P  1 106 ? 50.821  144.020 28.938  1.00 57.97 ? 106  LEU P N   1 
ATOM   17236 C  CA  . LEU P  1 106 ? 51.391  142.878 28.232  1.00 57.68 ? 106  LEU P CA  1 
ATOM   17237 C  C   . LEU P  1 106 ? 52.826  142.621 28.680  1.00 57.51 ? 106  LEU P C   1 
ATOM   17238 O  O   . LEU P  1 106 ? 53.520  141.763 28.139  1.00 57.33 ? 106  LEU P O   1 
ATOM   17239 C  CB  . LEU P  1 106 ? 51.307  143.081 26.715  1.00 57.65 ? 106  LEU P CB  1 
ATOM   17240 C  CG  . LEU P  1 106 ? 49.885  143.223 26.158  1.00 57.58 ? 106  LEU P CG  1 
ATOM   17241 C  CD1 . LEU P  1 106 ? 49.876  143.220 24.633  1.00 57.48 ? 106  LEU P CD1 1 
ATOM   17242 C  CD2 . LEU P  1 106 ? 48.982  142.122 26.697  1.00 57.52 ? 106  LEU P CD2 1 
ATOM   17243 N  N   . SER P  1 107 ? 53.259  143.376 29.682  1.00 57.41 ? 107  SER P N   1 
ATOM   17244 C  CA  . SER P  1 107 ? 54.584  143.207 30.261  1.00 57.34 ? 107  SER P CA  1 
ATOM   17245 C  C   . SER P  1 107 ? 54.569  143.792 31.669  1.00 57.28 ? 107  SER P C   1 
ATOM   17246 O  O   . SER P  1 107 ? 53.717  144.619 31.992  1.00 57.33 ? 107  SER P O   1 
ATOM   17247 C  CB  . SER P  1 107 ? 55.658  143.883 29.401  1.00 57.34 ? 107  SER P CB  1 
ATOM   17248 O  OG  . SER P  1 107 ? 55.841  145.241 29.764  1.00 57.27 ? 107  SER P OG  1 
ATOM   17249 N  N   . GLY P  1 108 ? 55.492  143.342 32.514  1.00 57.10 ? 108  GLY P N   1 
ATOM   17250 C  CA  . GLY P  1 108 ? 55.598  143.863 33.864  1.00 56.78 ? 108  GLY P CA  1 
ATOM   17251 C  C   . GLY P  1 108 ? 54.757  143.175 34.924  1.00 56.54 ? 108  GLY P C   1 
ATOM   17252 O  O   . GLY P  1 108 ? 54.330  142.027 34.765  1.00 56.52 ? 108  GLY P O   1 
ATOM   17253 N  N   . ASP P  1 109 ? 54.518  143.907 36.009  1.00 56.16 ? 109  ASP P N   1 
ATOM   17254 C  CA  . ASP P  1 109 ? 53.788  143.412 37.171  1.00 55.86 ? 109  ASP P CA  1 
ATOM   17255 C  C   . ASP P  1 109 ? 52.341  143.001 36.886  1.00 55.59 ? 109  ASP P C   1 
ATOM   17256 O  O   . ASP P  1 109 ? 51.849  142.031 37.461  1.00 55.65 ? 109  ASP P O   1 
ATOM   17257 C  CB  . ASP P  1 109 ? 53.817  144.464 38.288  1.00 55.95 ? 109  ASP P CB  1 
ATOM   17258 C  CG  . ASP P  1 109 ? 55.202  145.062 38.498  1.00 55.94 ? 109  ASP P CG  1 
ATOM   17259 O  OD1 . ASP P  1 109 ? 55.434  145.659 39.569  1.00 56.25 ? 109  ASP P OD1 1 
ATOM   17260 O  OD2 . ASP P  1 109 ? 56.121  144.994 37.654  1.00 55.90 ? 109  ASP P OD2 1 
ATOM   17261 N  N   . HIS P  1 110 ? 51.657  143.740 36.016  1.00 55.16 ? 110  HIS P N   1 
ATOM   17262 C  CA  . HIS P  1 110 ? 50.267  143.427 35.681  1.00 54.81 ? 110  HIS P CA  1 
ATOM   17263 C  C   . HIS P  1 110 ? 50.151  142.642 34.371  1.00 54.41 ? 110  HIS P C   1 
ATOM   17264 O  O   . HIS P  1 110 ? 49.100  142.642 33.721  1.00 54.29 ? 110  HIS P O   1 
ATOM   17265 C  CB  . HIS P  1 110 ? 49.429  144.703 35.601  1.00 55.03 ? 110  HIS P CB  1 
ATOM   17266 C  CG  . HIS P  1 110 ? 49.243  145.387 36.918  1.00 55.51 ? 110  HIS P CG  1 
ATOM   17267 N  ND1 . HIS P  1 110 ? 48.641  146.621 37.036  1.00 56.08 ? 110  HIS P ND1 1 
ATOM   17268 C  CD2 . HIS P  1 110 ? 49.577  145.008 38.175  1.00 56.10 ? 110  HIS P CD2 1 
ATOM   17269 C  CE1 . HIS P  1 110 ? 48.614  146.974 38.309  1.00 56.32 ? 110  HIS P CE1 1 
ATOM   17270 N  NE2 . HIS P  1 110 ? 49.176  146.013 39.020  1.00 56.34 ? 110  HIS P NE2 1 
ATOM   17271 N  N   . CYS P  1 111 ? 51.238  141.976 33.997  1.00 53.73 ? 111  CYS P N   1 
ATOM   17272 C  CA  . CYS P  1 111 ? 51.284  141.195 32.774  1.00 53.23 ? 111  CYS P CA  1 
ATOM   17273 C  C   . CYS P  1 111 ? 50.140  140.187 32.731  1.00 52.91 ? 111  CYS P C   1 
ATOM   17274 O  O   . CYS P  1 111 ? 49.888  139.487 33.712  1.00 52.87 ? 111  CYS P O   1 
ATOM   17275 C  CB  . CYS P  1 111 ? 52.622  140.461 32.690  1.00 53.30 ? 111  CYS P CB  1 
ATOM   17276 S  SG  . CYS P  1 111 ? 53.141  140.015 31.025  1.00 52.94 ? 111  CYS P SG  1 
ATOM   17277 N  N   . ILE P  1 112 ? 49.443  140.114 31.601  1.00 52.39 ? 112  ILE P N   1 
ATOM   17278 C  CA  . ILE P  1 112 ? 48.348  139.159 31.466  1.00 52.08 ? 112  ILE P CA  1 
ATOM   17279 C  C   . ILE P  1 112 ? 48.691  137.993 30.529  1.00 51.85 ? 112  ILE P C   1 
ATOM   17280 O  O   . ILE P  1 112 ? 47.840  137.156 30.230  1.00 51.76 ? 112  ILE P O   1 
ATOM   17281 C  CB  . ILE P  1 112 ? 47.047  139.855 31.017  1.00 52.05 ? 112  ILE P CB  1 
ATOM   17282 C  CG1 . ILE P  1 112 ? 47.272  140.626 29.713  1.00 52.17 ? 112  ILE P CG1 1 
ATOM   17283 C  CG2 . ILE P  1 112 ? 46.507  140.757 32.136  1.00 52.08 ? 112  ILE P CG2 1 
ATOM   17284 C  CD1 . ILE P  1 112 ? 45.993  140.915 28.942  1.00 52.49 ? 112  ILE P CD1 1 
ATOM   17285 N  N   . ILE P  1 113 ? 49.939  137.942 30.075  1.00 51.75 ? 113  ILE P N   1 
ATOM   17286 C  CA  . ILE P  1 113 ? 50.384  136.868 29.191  1.00 51.50 ? 113  ILE P CA  1 
ATOM   17287 C  C   . ILE P  1 113 ? 50.452  135.543 29.940  1.00 51.75 ? 113  ILE P C   1 
ATOM   17288 O  O   . ILE P  1 113 ? 51.065  135.454 31.007  1.00 51.69 ? 113  ILE P O   1 
ATOM   17289 C  CB  . ILE P  1 113 ? 51.760  137.191 28.603  1.00 51.47 ? 113  ILE P CB  1 
ATOM   17290 C  CG1 . ILE P  1 113 ? 51.711  138.506 27.827  1.00 51.01 ? 113  ILE P CG1 1 
ATOM   17291 C  CG2 . ILE P  1 113 ? 52.222  136.059 27.695  1.00 51.29 ? 113  ILE P CG2 1 
ATOM   17292 C  CD1 . ILE P  1 113 ? 50.954  138.412 26.531  1.00 49.95 ? 113  ILE P CD1 1 
ATOM   17293 N  N   . GLY P  1 114 ? 49.826  134.513 29.380  1.00 51.89 ? 114  GLY P N   1 
ATOM   17294 C  CA  . GLY P  1 114 ? 49.806  133.208 30.015  1.00 52.18 ? 114  GLY P CA  1 
ATOM   17295 C  C   . GLY P  1 114 ? 48.612  133.061 30.944  1.00 52.47 ? 114  GLY P C   1 
ATOM   17296 O  O   . GLY P  1 114 ? 48.389  132.000 31.521  1.00 52.28 ? 114  GLY P O   1 
ATOM   17297 N  N   . ARG P  1 115 ? 47.844  134.135 31.094  1.00 52.72 ? 115  ARG P N   1 
ATOM   17298 C  CA  . ARG P  1 115 ? 46.647  134.104 31.928  1.00 53.02 ? 115  ARG P CA  1 
ATOM   17299 C  C   . ARG P  1 115 ? 45.419  133.768 31.083  1.00 53.29 ? 115  ARG P C   1 
ATOM   17300 O  O   . ARG P  1 115 ? 45.542  133.512 29.883  1.00 53.30 ? 115  ARG P O   1 
ATOM   17301 C  CB  . ARG P  1 115 ? 46.485  135.416 32.712  1.00 53.06 ? 115  ARG P CB  1 
ATOM   17302 C  CG  . ARG P  1 115 ? 47.726  135.746 33.556  1.00 52.94 ? 115  ARG P CG  1 
ATOM   17303 C  CD  . ARG P  1 115 ? 47.531  136.753 34.689  1.00 52.63 ? 115  ARG P CD  1 
ATOM   17304 N  NE  . ARG P  1 115 ? 48.798  137.023 35.377  1.00 52.52 ? 115  ARG P NE  1 
ATOM   17305 C  CZ  . ARG P  1 115 ? 49.286  136.305 36.391  1.00 51.69 ? 115  ARG P CZ  1 
ATOM   17306 N  NH1 . ARG P  1 115 ? 48.616  135.261 36.861  1.00 51.33 ? 115  ARG P NH1 1 
ATOM   17307 N  NH2 . ARG P  1 115 ? 50.450  136.633 36.938  1.00 50.95 ? 115  ARG P NH2 1 
ATOM   17308 N  N   . THR P  1 116 ? 44.239  133.765 31.698  1.00 53.56 ? 116  THR P N   1 
ATOM   17309 C  CA  . THR P  1 116 ? 43.035  133.329 30.990  1.00 53.68 ? 116  THR P CA  1 
ATOM   17310 C  C   . THR P  1 116 ? 41.963  134.401 30.798  1.00 53.99 ? 116  THR P C   1 
ATOM   17311 O  O   . THR P  1 116 ? 41.543  135.061 31.753  1.00 53.82 ? 116  THR P O   1 
ATOM   17312 C  CB  . THR P  1 116 ? 42.415  132.103 31.705  1.00 53.80 ? 116  THR P CB  1 
ATOM   17313 O  OG1 . THR P  1 116 ? 43.364  131.026 31.746  1.00 52.82 ? 116  THR P OG1 1 
ATOM   17314 C  CG2 . THR P  1 116 ? 41.260  131.534 30.893  1.00 53.89 ? 116  THR P CG2 1 
ATOM   17315 N  N   . LEU P  1 117 ? 41.514  134.552 29.554  1.00 54.12 ? 117  LEU P N   1 
ATOM   17316 C  CA  . LEU P  1 117 ? 40.447  135.484 29.227  1.00 54.27 ? 117  LEU P CA  1 
ATOM   17317 C  C   . LEU P  1 117 ? 39.111  134.744 29.240  1.00 54.70 ? 117  LEU P C   1 
ATOM   17318 O  O   . LEU P  1 117 ? 38.960  133.706 28.590  1.00 54.54 ? 117  LEU P O   1 
ATOM   17319 C  CB  . LEU P  1 117 ? 40.685  136.110 27.849  1.00 54.34 ? 117  LEU P CB  1 
ATOM   17320 C  CG  . LEU P  1 117 ? 39.658  137.148 27.400  1.00 53.96 ? 117  LEU P CG  1 
ATOM   17321 C  CD1 . LEU P  1 117 ? 39.705  138.380 28.296  1.00 54.94 ? 117  LEU P CD1 1 
ATOM   17322 C  CD2 . LEU P  1 117 ? 39.886  137.534 25.947  1.00 54.12 ? 117  LEU P CD2 1 
ATOM   17323 N  N   . VAL P  1 118 ? 38.133  135.283 29.966  1.00 55.04 ? 118  VAL P N   1 
ATOM   17324 C  CA  . VAL P  1 118 ? 36.833  134.628 30.073  1.00 55.31 ? 118  VAL P CA  1 
ATOM   17325 C  C   . VAL P  1 118 ? 35.645  135.519 29.714  1.00 55.56 ? 118  VAL P C   1 
ATOM   17326 O  O   . VAL P  1 118 ? 35.601  136.694 30.083  1.00 55.81 ? 118  VAL P O   1 
ATOM   17327 C  CB  . VAL P  1 118 ? 36.615  134.091 31.504  1.00 55.33 ? 118  VAL P CB  1 
ATOM   17328 C  CG1 . VAL P  1 118 ? 35.233  133.472 31.649  1.00 55.23 ? 118  VAL P CG1 1 
ATOM   17329 C  CG2 . VAL P  1 118 ? 37.697  133.092 31.867  1.00 55.38 ? 118  VAL P CG2 1 
ATOM   17330 N  N   . VAL P  1 119 ? 34.682  134.955 28.990  1.00 55.58 ? 119  VAL P N   1 
ATOM   17331 C  CA  . VAL P  1 119 ? 33.428  135.655 28.732  1.00 55.59 ? 119  VAL P CA  1 
ATOM   17332 C  C   . VAL P  1 119 ? 32.338  134.940 29.537  1.00 55.66 ? 119  VAL P C   1 
ATOM   17333 O  O   . VAL P  1 119 ? 32.294  133.709 29.569  1.00 55.64 ? 119  VAL P O   1 
ATOM   17334 C  CB  . VAL P  1 119 ? 33.078  135.728 27.233  1.00 55.47 ? 119  VAL P CB  1 
ATOM   17335 C  CG1 . VAL P  1 119 ? 32.765  134.349 26.679  1.00 55.32 ? 119  VAL P CG1 1 
ATOM   17336 C  CG2 . VAL P  1 119 ? 31.912  136.685 27.010  1.00 55.43 ? 119  VAL P CG2 1 
ATOM   17337 N  N   . HIS P  1 120 ? 31.472  135.709 30.193  1.00 55.78 ? 120  HIS P N   1 
ATOM   17338 C  CA  . HIS P  1 120 ? 30.473  135.139 31.101  1.00 55.85 ? 120  HIS P CA  1 
ATOM   17339 C  C   . HIS P  1 120 ? 29.014  135.062 30.633  1.00 56.02 ? 120  HIS P C   1 
ATOM   17340 O  O   . HIS P  1 120 ? 28.593  135.745 29.696  1.00 56.01 ? 120  HIS P O   1 
ATOM   17341 C  CB  . HIS P  1 120 ? 30.513  135.878 32.437  1.00 55.84 ? 120  HIS P CB  1 
ATOM   17342 C  CG  . HIS P  1 120 ? 31.669  135.494 33.303  1.00 55.79 ? 120  HIS P CG  1 
ATOM   17343 N  ND1 . HIS P  1 120 ? 31.611  134.447 34.196  1.00 55.58 ? 120  HIS P ND1 1 
ATOM   17344 C  CD2 . HIS P  1 120 ? 32.912  136.017 33.414  1.00 55.79 ? 120  HIS P CD2 1 
ATOM   17345 C  CE1 . HIS P  1 120 ? 32.767  134.344 34.825  1.00 55.76 ? 120  HIS P CE1 1 
ATOM   17346 N  NE2 . HIS P  1 120 ? 33.575  135.283 34.367  1.00 55.99 ? 120  HIS P NE2 1 
ATOM   17347 N  N   . GLU P  1 121 ? 28.257  134.225 31.339  1.00 56.18 ? 121  GLU P N   1 
ATOM   17348 C  CA  . GLU P  1 121 ? 26.836  133.998 31.094  1.00 56.35 ? 121  GLU P CA  1 
ATOM   17349 C  C   . GLU P  1 121 ? 26.006  135.267 31.252  1.00 56.54 ? 121  GLU P C   1 
ATOM   17350 O  O   . GLU P  1 121 ? 25.174  135.589 30.401  1.00 56.40 ? 121  GLU P O   1 
ATOM   17351 C  CB  . GLU P  1 121 ? 26.311  132.925 32.061  1.00 56.30 ? 121  GLU P CB  1 
ATOM   17352 C  CG  . GLU P  1 121 ? 24.799  132.726 32.057  1.00 56.06 ? 121  GLU P CG  1 
ATOM   17353 C  CD  . GLU P  1 121 ? 24.296  131.982 33.286  1.00 55.80 ? 121  GLU P CD  1 
ATOM   17354 O  OE1 . GLU P  1 121 ? 23.098  131.627 33.322  1.00 55.42 ? 121  GLU P OE1 1 
ATOM   17355 O  OE2 . GLU P  1 121 ? 25.095  131.755 34.220  1.00 55.60 ? 121  GLU P OE2 1 
ATOM   17356 N  N   . LYS P  1 122 ? 26.242  135.983 32.347  1.00 56.86 ? 122  LYS P N   1 
ATOM   17357 C  CA  . LYS P  1 122 ? 25.468  137.179 32.668  1.00 57.20 ? 122  LYS P CA  1 
ATOM   17358 C  C   . LYS P  1 122 ? 26.291  138.467 32.627  1.00 57.38 ? 122  LYS P C   1 
ATOM   17359 O  O   . LYS P  1 122 ? 27.506  138.446 32.409  1.00 57.23 ? 122  LYS P O   1 
ATOM   17360 C  CB  . LYS P  1 122 ? 24.825  137.035 34.059  1.00 57.20 ? 122  LYS P CB  1 
ATOM   17361 C  CG  . LYS P  1 122 ? 23.928  135.810 34.226  1.00 57.06 ? 122  LYS P CG  1 
ATOM   17362 C  CD  . LYS P  1 122 ? 23.516  135.584 35.679  1.00 56.46 ? 122  LYS P CD  1 
ATOM   17363 C  CE  . LYS P  1 122 ? 24.415  134.568 36.367  1.00 56.35 ? 122  LYS P CE  1 
ATOM   17364 N  N   . ALA P  1 123 ? 25.605  139.586 32.843  1.00 57.65 ? 123  ALA P N   1 
ATOM   17365 C  CA  . ALA P  1 123 ? 26.247  140.889 32.890  1.00 57.86 ? 123  ALA P CA  1 
ATOM   17366 C  C   . ALA P  1 123 ? 27.021  141.026 34.191  1.00 58.05 ? 123  ALA P C   1 
ATOM   17367 O  O   . ALA P  1 123 ? 26.647  140.452 35.213  1.00 58.13 ? 123  ALA P O   1 
ATOM   17368 C  CB  . ALA P  1 123 ? 25.210  141.994 32.782  1.00 57.88 ? 123  ALA P CB  1 
ATOM   17369 N  N   . ASP P  1 124 ? 28.115  141.774 34.136  1.00 58.29 ? 124  ASP P N   1 
ATOM   17370 C  CA  . ASP P  1 124 ? 28.924  142.065 35.306  1.00 58.40 ? 124  ASP P CA  1 
ATOM   17371 C  C   . ASP P  1 124 ? 28.245  143.259 35.969  1.00 58.70 ? 124  ASP P C   1 
ATOM   17372 O  O   . ASP P  1 124 ? 28.109  144.317 35.355  1.00 58.61 ? 124  ASP P O   1 
ATOM   17373 C  CB  . ASP P  1 124 ? 30.340  142.422 34.853  1.00 58.33 ? 124  ASP P CB  1 
ATOM   17374 C  CG  . ASP P  1 124 ? 31.303  142.624 36.001  1.00 58.17 ? 124  ASP P CG  1 
ATOM   17375 O  OD1 . ASP P  1 124 ? 30.855  142.883 37.137  1.00 57.80 ? 124  ASP P OD1 1 
ATOM   17376 O  OD2 . ASP P  1 124 ? 32.541  142.553 35.849  1.00 57.70 ? 124  ASP P OD2 1 
ATOM   17377 N  N   . ASP P  1 125 ? 27.791  143.089 37.209  1.00 59.01 ? 125  ASP P N   1 
ATOM   17378 C  CA  . ASP P  1 125 ? 27.088  144.170 37.900  1.00 59.45 ? 125  ASP P CA  1 
ATOM   17379 C  C   . ASP P  1 125 ? 28.046  145.233 38.441  1.00 59.68 ? 125  ASP P C   1 
ATOM   17380 O  O   . ASP P  1 125 ? 27.633  146.173 39.128  1.00 59.65 ? 125  ASP P O   1 
ATOM   17381 C  CB  . ASP P  1 125 ? 26.161  143.631 38.999  1.00 59.47 ? 125  ASP P CB  1 
ATOM   17382 C  CG  . ASP P  1 125 ? 26.915  143.028 40.170  1.00 59.63 ? 125  ASP P CG  1 
ATOM   17383 O  OD1 . ASP P  1 125 ? 28.127  143.294 40.320  1.00 59.43 ? 125  ASP P OD1 1 
ATOM   17384 O  OD2 . ASP P  1 125 ? 26.367  142.275 41.002  1.00 59.99 ? 125  ASP P OD2 1 
ATOM   17385 N  N   . LEU P  1 126 ? 29.326  145.057 38.124  1.00 59.85 ? 126  LEU P N   1 
ATOM   17386 C  CA  . LEU P  1 126 ? 30.381  146.003 38.476  1.00 60.20 ? 126  LEU P CA  1 
ATOM   17387 C  C   . LEU P  1 126 ? 30.533  146.275 39.976  1.00 60.42 ? 126  LEU P C   1 
ATOM   17388 O  O   . LEU P  1 126 ? 31.052  147.318 40.368  1.00 60.52 ? 126  LEU P O   1 
ATOM   17389 C  CB  . LEU P  1 126 ? 30.203  147.316 37.701  1.00 60.16 ? 126  LEU P CB  1 
ATOM   17390 C  CG  . LEU P  1 126 ? 29.927  147.196 36.196  1.00 60.31 ? 126  LEU P CG  1 
ATOM   17391 C  CD1 . LEU P  1 126 ? 29.757  148.568 35.556  1.00 60.33 ? 126  LEU P CD1 1 
ATOM   17392 C  CD2 . LEU P  1 126 ? 31.017  146.397 35.480  1.00 60.52 ? 126  LEU P CD2 1 
ATOM   17393 N  N   . GLY P  1 127 ? 30.095  145.334 40.808  1.00 60.74 ? 127  GLY P N   1 
ATOM   17394 C  CA  . GLY P  1 127 ? 30.213  145.478 42.250  1.00 61.23 ? 127  GLY P CA  1 
ATOM   17395 C  C   . GLY P  1 127 ? 29.066  146.209 42.930  1.00 61.49 ? 127  GLY P C   1 
ATOM   17396 O  O   . GLY P  1 127 ? 29.138  146.522 44.120  1.00 61.57 ? 127  GLY P O   1 
ATOM   17397 N  N   . LYS P  1 128 ? 27.999  146.472 42.183  1.00 61.80 ? 128  LYS P N   1 
ATOM   17398 C  CA  . LYS P  1 128 ? 26.843  147.180 42.727  1.00 62.10 ? 128  LYS P CA  1 
ATOM   17399 C  C   . LYS P  1 128 ? 25.682  146.228 43.023  1.00 62.24 ? 128  LYS P C   1 
ATOM   17400 O  O   . LYS P  1 128 ? 24.539  146.660 43.182  1.00 62.19 ? 128  LYS P O   1 
ATOM   17401 C  CB  . LYS P  1 128 ? 26.379  148.265 41.750  1.00 62.19 ? 128  LYS P CB  1 
ATOM   17402 C  CG  . LYS P  1 128 ? 27.458  149.265 41.347  1.00 62.37 ? 128  LYS P CG  1 
ATOM   17403 C  CD  . LYS P  1 128 ? 27.069  150.021 40.076  1.00 62.62 ? 128  LYS P CD  1 
ATOM   17404 C  CE  . LYS P  1 128 ? 25.758  150.781 40.238  1.00 62.49 ? 128  LYS P CE  1 
ATOM   17405 N  NZ  . LYS P  1 128 ? 25.364  151.484 38.986  1.00 62.18 ? 128  LYS P NZ  1 
ATOM   17406 N  N   . GLY P  1 129 ? 25.982  144.935 43.106  1.00 62.35 ? 129  GLY P N   1 
ATOM   17407 C  CA  . GLY P  1 129 ? 24.960  143.922 43.316  1.00 62.53 ? 129  GLY P CA  1 
ATOM   17408 C  C   . GLY P  1 129 ? 24.337  143.840 44.697  1.00 62.60 ? 129  GLY P C   1 
ATOM   17409 O  O   . GLY P  1 129 ? 23.231  143.323 44.843  1.00 62.56 ? 129  GLY P O   1 
ATOM   17410 N  N   . GLY P  1 130 ? 25.043  144.324 45.713  1.00 62.70 ? 130  GLY P N   1 
ATOM   17411 C  CA  . GLY P  1 130 ? 24.529  144.293 47.071  1.00 63.00 ? 130  GLY P CA  1 
ATOM   17412 C  C   . GLY P  1 130 ? 24.696  142.966 47.794  1.00 63.15 ? 130  GLY P C   1 
ATOM   17413 O  O   . GLY P  1 130 ? 24.198  142.792 48.905  1.00 63.09 ? 130  GLY P O   1 
ATOM   17414 N  N   . ASN P  1 131 ? 25.386  142.023 47.163  1.00 63.33 ? 131  ASN P N   1 
ATOM   17415 C  CA  . ASN P  1 131 ? 25.647  140.729 47.782  1.00 63.55 ? 131  ASN P CA  1 
ATOM   17416 C  C   . ASN P  1 131 ? 27.146  140.444 47.816  1.00 63.70 ? 131  ASN P C   1 
ATOM   17417 O  O   . ASN P  1 131 ? 27.929  141.165 47.201  1.00 63.65 ? 131  ASN P O   1 
ATOM   17418 C  CB  . ASN P  1 131 ? 24.899  139.610 47.054  1.00 63.56 ? 131  ASN P CB  1 
ATOM   17419 C  CG  . ASN P  1 131 ? 25.360  139.439 45.623  1.00 63.49 ? 131  ASN P CG  1 
ATOM   17420 O  OD1 . ASN P  1 131 ? 26.047  140.299 45.076  1.00 63.32 ? 131  ASN P OD1 1 
ATOM   17421 N  ND2 . ASN P  1 131 ? 24.980  138.326 45.006  1.00 63.62 ? 131  ASN P ND2 1 
ATOM   17422 N  N   . GLU P  1 132 ? 27.537  139.396 48.536  1.00 63.93 ? 132  GLU P N   1 
ATOM   17423 C  C   . GLU P  1 132 ? 29.572  138.739 47.324  1.00 64.31 ? 132  GLU P C   1 
ATOM   17424 O  O   . GLU P  1 132 ? 30.708  139.128 47.051  1.00 64.23 ? 132  GLU P O   1 
ATOM   17425 N  N   . GLU P  1 133 ? 28.815  138.047 46.482  1.00 64.46 ? 133  GLU P N   1 
ATOM   17426 C  CA  . GLU P  1 133 ? 29.277  137.649 45.161  1.00 64.66 ? 133  GLU P CA  1 
ATOM   17427 C  C   . GLU P  1 133 ? 29.634  138.835 44.265  1.00 64.67 ? 133  GLU P C   1 
ATOM   17428 O  O   . GLU P  1 133 ? 30.584  138.765 43.482  1.00 64.67 ? 133  GLU P O   1 
ATOM   17429 C  CB  . GLU P  1 133 ? 28.212  136.787 44.482  1.00 64.76 ? 133  GLU P CB  1 
ATOM   17430 C  CG  . GLU P  1 133 ? 28.698  136.078 43.231  1.00 65.09 ? 133  GLU P CG  1 
ATOM   17431 C  CD  . GLU P  1 133 ? 29.788  135.072 43.530  1.00 65.49 ? 133  GLU P CD  1 
ATOM   17432 O  OE1 . GLU P  1 133 ? 29.667  134.347 44.541  1.00 65.75 ? 133  GLU P OE1 1 
ATOM   17433 O  OE2 . GLU P  1 133 ? 30.763  135.008 42.756  1.00 65.75 ? 133  GLU P OE2 1 
ATOM   17434 N  N   . SER P  1 134 ? 28.871  139.918 44.382  1.00 64.65 ? 134  SER P N   1 
ATOM   17435 C  CA  . SER P  1 134 ? 29.087  141.110 43.562  1.00 64.59 ? 134  SER P CA  1 
ATOM   17436 C  C   . SER P  1 134 ? 30.508  141.652 43.690  1.00 64.50 ? 134  SER P C   1 
ATOM   17437 O  O   . SER P  1 134 ? 31.125  142.042 42.697  1.00 64.57 ? 134  SER P O   1 
ATOM   17438 C  CB  . SER P  1 134 ? 28.078  142.201 43.925  1.00 64.63 ? 134  SER P CB  1 
ATOM   17439 O  OG  . SER P  1 134 ? 28.153  143.287 43.020  1.00 64.62 ? 134  SER P OG  1 
ATOM   17440 N  N   . THR P  1 135 ? 31.022  141.675 44.917  1.00 64.34 ? 135  THR P N   1 
ATOM   17441 C  CA  . THR P  1 135 ? 32.374  142.162 45.167  1.00 64.14 ? 135  THR P CA  1 
ATOM   17442 C  C   . THR P  1 135 ? 33.437  141.125 44.789  1.00 64.02 ? 135  THR P C   1 
ATOM   17443 O  O   . THR P  1 135 ? 34.632  141.370 44.950  1.00 63.96 ? 135  THR P O   1 
ATOM   17444 C  CB  . THR P  1 135 ? 32.539  142.613 46.646  1.00 64.20 ? 135  THR P CB  1 
ATOM   17445 O  OG1 . THR P  1 135 ? 31.871  141.690 47.517  1.00 64.00 ? 135  THR P OG1 1 
ATOM   17446 C  CG2 . THR P  1 135 ? 31.799  143.921 46.901  1.00 64.21 ? 135  THR P CG2 1 
ATOM   17447 N  N   . LYS P  1 136 ? 33.002  139.976 44.277  1.00 63.94 ? 136  LYS P N   1 
ATOM   17448 C  CA  . LYS P  1 136 ? 33.929  138.917 43.868  1.00 63.87 ? 136  LYS P CA  1 
ATOM   17449 C  C   . LYS P  1 136 ? 33.980  138.720 42.352  1.00 63.71 ? 136  LYS P C   1 
ATOM   17450 O  O   . LYS P  1 136 ? 35.060  138.683 41.758  1.00 63.53 ? 136  LYS P O   1 
ATOM   17451 C  CB  . LYS P  1 136 ? 33.567  137.581 44.529  1.00 63.94 ? 136  LYS P CB  1 
ATOM   17452 C  CG  . LYS P  1 136 ? 33.880  137.479 46.013  1.00 64.06 ? 136  LYS P CG  1 
ATOM   17453 C  CD  . LYS P  1 136 ? 33.480  136.111 46.550  1.00 64.41 ? 136  LYS P CD  1 
ATOM   17454 C  CE  . LYS P  1 136 ? 33.320  136.131 48.061  1.00 64.69 ? 136  LYS P CE  1 
ATOM   17455 N  NZ  . LYS P  1 136 ? 32.559  134.950 48.559  1.00 65.07 ? 136  LYS P NZ  1 
ATOM   17456 N  N   . THR P  1 137 ? 32.809  138.576 41.735  1.00 63.53 ? 137  THR P N   1 
ATOM   17457 C  CA  . THR P  1 137 ? 32.727  138.309 40.301  1.00 63.44 ? 137  THR P CA  1 
ATOM   17458 C  C   . THR P  1 137 ? 31.706  139.188 39.587  1.00 63.20 ? 137  THR P C   1 
ATOM   17459 O  O   . THR P  1 137 ? 31.530  139.077 38.372  1.00 63.26 ? 137  THR P O   1 
ATOM   17460 C  CB  . THR P  1 137 ? 32.371  136.827 40.048  1.00 63.46 ? 137  THR P CB  1 
ATOM   17461 O  OG1 . THR P  1 137 ? 31.100  136.533 40.646  1.00 63.63 ? 137  THR P OG1 1 
ATOM   17462 C  CG2 . THR P  1 137 ? 33.341  135.899 40.775  1.00 63.50 ? 137  THR P CG2 1 
ATOM   17463 N  N   . GLY P  1 138 ? 31.031  140.052 40.336  1.00 62.83 ? 138  GLY P N   1 
ATOM   17464 C  CA  . GLY P  1 138 ? 30.017  140.913 39.756  1.00 62.45 ? 138  GLY P CA  1 
ATOM   17465 C  C   . GLY P  1 138 ? 28.795  140.122 39.329  1.00 62.16 ? 138  GLY P C   1 
ATOM   17466 O  O   . GLY P  1 138 ? 28.032  140.556 38.466  1.00 62.13 ? 138  GLY P O   1 
ATOM   17467 N  N   . ASN P  1 139 ? 28.620  138.953 39.940  1.00 61.93 ? 139  ASN P N   1 
ATOM   17468 C  CA  . ASN P  1 139 ? 27.492  138.072 39.647  1.00 61.69 ? 139  ASN P CA  1 
ATOM   17469 C  C   . ASN P  1 139 ? 27.375  137.741 38.172  1.00 61.48 ? 139  ASN P C   1 
ATOM   17470 O  O   . ASN P  1 139 ? 26.271  137.579 37.648  1.00 61.44 ? 139  ASN P O   1 
ATOM   17471 C  CB  . ASN P  1 139 ? 26.187  138.683 40.149  1.00 61.72 ? 139  ASN P CB  1 
ATOM   17472 C  CG  . ASN P  1 139 ? 26.068  138.632 41.652  1.00 61.89 ? 139  ASN P CG  1 
ATOM   17473 O  OD1 . ASN P  1 139 ? 25.927  137.559 42.236  1.00 62.08 ? 139  ASN P OD1 1 
ATOM   17474 N  ND2 . ASN P  1 139 ? 26.127  139.794 42.291  1.00 62.15 ? 139  ASN P ND2 1 
ATOM   17475 N  N   . ALA P  1 140 ? 28.525  137.631 37.513  1.00 61.18 ? 140  ALA P N   1 
ATOM   17476 C  CA  . ALA P  1 140 ? 28.578  137.365 36.083  1.00 60.91 ? 140  ALA P CA  1 
ATOM   17477 C  C   . ALA P  1 140 ? 28.165  135.939 35.733  1.00 60.70 ? 140  ALA P C   1 
ATOM   17478 O  O   . ALA P  1 140 ? 27.959  135.613 34.561  1.00 60.75 ? 140  ALA P O   1 
ATOM   17479 C  CB  . ALA P  1 140 ? 29.965  137.669 35.545  1.00 61.05 ? 140  ALA P CB  1 
ATOM   17480 N  N   . GLY P  1 141 ? 28.051  135.089 36.748  1.00 60.33 ? 141  GLY P N   1 
ATOM   17481 C  CA  . GLY P  1 141 ? 27.640  133.713 36.541  1.00 59.87 ? 141  GLY P CA  1 
ATOM   17482 C  C   . GLY P  1 141 ? 28.672  132.825 35.868  1.00 59.50 ? 141  GLY P C   1 
ATOM   17483 O  O   . GLY P  1 141 ? 29.876  133.062 35.970  1.00 59.46 ? 141  GLY P O   1 
ATOM   17484 N  N   . SER P  1 142 ? 28.184  131.805 35.166  1.00 59.10 ? 142  SER P N   1 
ATOM   17485 C  CA  . SER P  1 142 ? 29.040  130.815 34.514  1.00 58.64 ? 142  SER P CA  1 
ATOM   17486 C  C   . SER P  1 142 ? 30.014  131.392 33.488  1.00 58.31 ? 142  SER P C   1 
ATOM   17487 O  O   . SER P  1 142 ? 29.857  132.518 33.014  1.00 58.21 ? 142  SER P O   1 
ATOM   17488 C  CB  . SER P  1 142 ? 28.194  129.709 33.871  1.00 58.67 ? 142  SER P CB  1 
ATOM   17489 O  OG  . SER P  1 142 ? 27.424  130.202 32.788  1.00 58.54 ? 142  SER P OG  1 
ATOM   17490 N  N   . ARG P  1 143 ? 31.029  130.596 33.169  1.00 57.90 ? 143  ARG P N   1 
ATOM   17491 C  CA  . ARG P  1 143 ? 32.030  130.950 32.179  1.00 57.45 ? 143  ARG P CA  1 
ATOM   17492 C  C   . ARG P  1 143 ? 31.668  130.200 30.904  1.00 57.21 ? 143  ARG P C   1 
ATOM   17493 O  O   . ARG P  1 143 ? 31.798  128.979 30.840  1.00 57.20 ? 143  ARG P O   1 
ATOM   17494 C  CB  . ARG P  1 143 ? 33.414  130.537 32.675  1.00 57.50 ? 143  ARG P CB  1 
ATOM   17495 C  CG  . ARG P  1 143 ? 33.736  131.071 34.063  1.00 57.17 ? 143  ARG P CG  1 
ATOM   17496 C  CD  . ARG P  1 143 ? 34.839  130.325 34.798  1.00 57.01 ? 143  ARG P CD  1 
ATOM   17497 N  NE  . ARG P  1 143 ? 35.007  130.839 36.157  1.00 56.49 ? 143  ARG P NE  1 
ATOM   17498 C  CZ  . ARG P  1 143 ? 36.158  130.851 36.815  1.00 55.96 ? 143  ARG P CZ  1 
ATOM   17499 N  NH1 . ARG P  1 143 ? 37.257  130.370 36.247  1.00 54.90 ? 143  ARG P NH1 1 
ATOM   17500 N  NH2 . ARG P  1 143 ? 36.212  131.343 38.047  1.00 55.51 ? 143  ARG P NH2 1 
ATOM   17501 N  N   . LEU P  1 144 ? 31.191  130.934 29.902  1.00 56.83 ? 144  LEU P N   1 
ATOM   17502 C  CA  . LEU P  1 144 ? 30.746  130.334 28.644  1.00 56.42 ? 144  LEU P CA  1 
ATOM   17503 C  C   . LEU P  1 144 ? 31.912  129.915 27.758  1.00 56.01 ? 144  LEU P C   1 
ATOM   17504 O  O   . LEU P  1 144 ? 31.859  128.882 27.090  1.00 55.96 ? 144  LEU P O   1 
ATOM   17505 C  CB  . LEU P  1 144 ? 29.837  131.301 27.882  1.00 56.47 ? 144  LEU P CB  1 
ATOM   17506 C  CG  . LEU P  1 144 ? 28.616  131.832 28.636  1.00 56.60 ? 144  LEU P CG  1 
ATOM   17507 C  CD1 . LEU P  1 144 ? 27.845  132.809 27.764  1.00 56.98 ? 144  LEU P CD1 1 
ATOM   17508 C  CD2 . LEU P  1 144 ? 27.715  130.694 29.097  1.00 56.56 ? 144  LEU P CD2 1 
ATOM   17509 N  N   . ALA P  1 145 ? 32.959  130.730 27.755  1.00 55.54 ? 145  ALA P N   1 
ATOM   17510 C  CA  . ALA P  1 145 ? 34.137  130.447 26.951  1.00 55.12 ? 145  ALA P CA  1 
ATOM   17511 C  C   . ALA P  1 145 ? 35.384  131.085 27.543  1.00 54.80 ? 145  ALA P C   1 
ATOM   17512 O  O   . ALA P  1 145 ? 35.314  132.059 28.300  1.00 54.69 ? 145  ALA P O   1 
ATOM   17513 C  CB  . ALA P  1 145 ? 33.932  130.907 25.506  1.00 55.09 ? 145  ALA P CB  1 
ATOM   17514 N  N   . CYS P  1 146 ? 36.527  130.518 27.188  1.00 54.41 ? 146  CYS P N   1 
ATOM   17515 C  CA  . CYS P  1 146 ? 37.800  131.013 27.660  1.00 54.17 ? 146  CYS P CA  1 
ATOM   17516 C  C   . CYS P  1 146 ? 38.919  130.476 26.796  1.00 53.63 ? 146  CYS P C   1 
ATOM   17517 O  O   . CYS P  1 146 ? 38.752  129.501 26.069  1.00 53.56 ? 146  CYS P O   1 
ATOM   17518 C  CB  . CYS P  1 146 ? 38.033  130.584 29.109  1.00 54.32 ? 146  CYS P CB  1 
ATOM   17519 S  SG  . CYS P  1 146 ? 37.935  128.795 29.372  1.00 55.23 ? 146  CYS P SG  1 
ATOM   17520 N  N   . GLY P  1 147 ? 40.063  131.134 26.889  1.00 53.32 ? 147  GLY P N   1 
ATOM   17521 C  CA  . GLY P  1 147 ? 41.261  130.719 26.194  1.00 53.11 ? 147  GLY P CA  1 
ATOM   17522 C  C   . GLY P  1 147 ? 42.438  131.327 26.929  1.00 53.12 ? 147  GLY P C   1 
ATOM   17523 O  O   . GLY P  1 147 ? 42.270  132.252 27.735  1.00 52.91 ? 147  GLY P O   1 
ATOM   17524 N  N   . VAL P  1 148 ? 43.629  130.798 26.675  1.00 53.04 ? 148  VAL P N   1 
ATOM   17525 C  CA  . VAL P  1 148 ? 44.837  131.333 27.287  1.00 53.19 ? 148  VAL P CA  1 
ATOM   17526 C  C   . VAL P  1 148 ? 45.332  132.503 26.438  1.00 53.34 ? 148  VAL P C   1 
ATOM   17527 O  O   . VAL P  1 148 ? 45.275  132.452 25.207  1.00 53.12 ? 148  VAL P O   1 
ATOM   17528 C  CB  . VAL P  1 148 ? 45.942  130.263 27.377  1.00 53.31 ? 148  VAL P CB  1 
ATOM   17529 C  CG1 . VAL P  1 148 ? 47.179  130.826 28.060  1.00 53.54 ? 148  VAL P CG1 1 
ATOM   17530 C  CG2 . VAL P  1 148 ? 45.430  129.033 28.111  1.00 53.41 ? 148  VAL P CG2 1 
ATOM   17531 N  N   . ILE P  1 149 ? 45.791  133.570 27.087  1.00 53.25 ? 149  ILE P N   1 
ATOM   17532 C  CA  . ILE P  1 149 ? 46.318  134.714 26.349  1.00 52.88 ? 149  ILE P CA  1 
ATOM   17533 C  C   . ILE P  1 149 ? 47.755  134.410 25.941  1.00 52.57 ? 149  ILE P C   1 
ATOM   17534 O  O   . ILE P  1 149 ? 48.621  134.213 26.798  1.00 52.78 ? 149  ILE P O   1 
ATOM   17535 C  CB  . ILE P  1 149 ? 46.249  135.988 27.200  1.00 52.91 ? 149  ILE P CB  1 
ATOM   17536 C  CG1 . ILE P  1 149 ? 44.793  136.345 27.505  1.00 52.96 ? 149  ILE P CG1 1 
ATOM   17537 C  CG2 . ILE P  1 149 ? 46.939  137.140 26.489  1.00 52.73 ? 149  ILE P CG2 1 
ATOM   17538 C  CD1 . ILE P  1 149 ? 44.641  137.255 28.700  1.00 53.95 ? 149  ILE P CD1 1 
ATOM   17539 N  N   . GLY P  1 150 ? 48.000  134.358 24.634  1.00 52.14 ? 150  GLY P N   1 
ATOM   17540 C  CA  . GLY P  1 150 ? 49.313  134.003 24.120  1.00 51.63 ? 150  GLY P CA  1 
ATOM   17541 C  C   . GLY P  1 150 ? 50.027  135.090 23.341  1.00 51.10 ? 150  GLY P C   1 
ATOM   17542 O  O   . GLY P  1 150 ? 49.411  136.045 22.872  1.00 50.82 ? 150  GLY P O   1 
ATOM   17543 N  N   . ILE P  1 151 ? 51.341  134.934 23.206  1.00 50.64 ? 151  ILE P N   1 
ATOM   17544 C  CA  . ILE P  1 151 ? 52.160  135.898 22.485  1.00 50.41 ? 151  ILE P CA  1 
ATOM   17545 C  C   . ILE P  1 151 ? 51.894  135.795 20.990  1.00 50.23 ? 151  ILE P C   1 
ATOM   17546 O  O   . ILE P  1 151 ? 51.948  134.705 20.414  1.00 50.18 ? 151  ILE P O   1 
ATOM   17547 C  CB  . ILE P  1 151 ? 53.654  135.666 22.779  1.00 50.43 ? 151  ILE P CB  1 
ATOM   17548 C  CG1 . ILE P  1 151 ? 53.979  136.040 24.229  1.00 50.33 ? 151  ILE P CG1 1 
ATOM   17549 C  CG2 . ILE P  1 151 ? 54.517  136.469 21.816  1.00 50.78 ? 151  ILE P CG2 1 
ATOM   17550 C  CD1 . ILE P  1 151 ? 55.403  135.734 24.638  1.00 50.43 ? 151  ILE P CD1 1 
ATOM   17551 N  N   . ALA P  1 152 ? 51.598  136.930 20.367  1.00 49.97 ? 152  ALA P N   1 
ATOM   17552 C  CA  . ALA P  1 152 ? 51.327  136.952 18.937  1.00 49.96 ? 152  ALA P CA  1 
ATOM   17553 C  C   . ALA P  1 152 ? 52.451  137.639 18.163  1.00 50.14 ? 152  ALA P C   1 
ATOM   17554 O  O   . ALA P  1 152 ? 53.268  138.363 18.738  1.00 50.06 ? 152  ALA P O   1 
ATOM   17555 C  CB  . ALA P  1 152 ? 49.985  137.605 18.655  1.00 49.88 ? 152  ALA P CB  1 
ATOM   17556 N  N   . GLN P  1 153 ? 52.490  137.401 16.856  1.00 50.27 ? 153  GLN P N   1 
ATOM   17557 C  CA  . GLN P  1 153 ? 53.515  137.977 15.994  1.00 50.74 ? 153  GLN P CA  1 
ATOM   17558 C  C   . GLN P  1 153 ? 53.271  139.459 15.695  1.00 50.80 ? 153  GLN P C   1 
ATOM   17559 O  O   . GLN P  1 153 ? 52.173  139.858 15.298  1.00 50.77 ? 153  GLN P O   1 
ATOM   17560 C  CB  . GLN P  1 153 ? 53.586  137.196 14.685  1.00 50.80 ? 153  GLN P CB  1 
ATOM   17561 C  CG  . GLN P  1 153 ? 54.636  137.687 13.715  1.00 51.60 ? 153  GLN P CG  1 
ATOM   17562 C  CD  . GLN P  1 153 ? 54.842  136.681 12.587  1.00 52.98 ? 153  GLN P CD  1 
ATOM   17563 O  OE1 . GLN P  1 153 ? 53.898  136.051 12.135  1.00 54.32 ? 153  GLN P OE1 1 
ATOM   17564 N  NE2 . GLN P  1 153 ? 56.004  136.372 12.014  1.00 53.25 ? 153  GLN P NE2 1 
ATOM   17565 O  OXT . GLN P  1 153 ? 54.167  140.298 15.828  1.00 50.97 ? 153  GLN P OXT 1 
ATOM   17566 N  N   . ALA Q  1 1   ? 22.127  126.600 118.594 1.00 32.53 ? 1    ALA Q N   1 
ATOM   17567 C  CA  . ALA Q  1 1   ? 22.196  125.708 117.393 1.00 32.13 ? 1    ALA Q CA  1 
ATOM   17568 C  C   . ALA Q  1 1   ? 23.423  126.000 116.526 1.00 31.40 ? 1    ALA Q C   1 
ATOM   17569 O  O   . ALA Q  1 1   ? 24.406  126.545 117.021 1.00 32.44 ? 1    ALA Q O   1 
ATOM   17570 C  CB  . ALA Q  1 1   ? 20.901  125.781 116.578 1.00 32.75 ? 1    ALA Q CB  1 
ATOM   17571 N  N   . THR Q  1 2   ? 23.361  125.673 115.236 1.00 29.49 ? 2    THR Q N   1 
ATOM   17572 C  CA  . THR Q  1 2   ? 24.542  125.750 114.349 1.00 26.82 ? 2    THR Q CA  1 
ATOM   17573 C  C   . THR Q  1 2   ? 25.706  126.699 114.714 1.00 24.67 ? 2    THR Q C   1 
ATOM   17574 O  O   . THR Q  1 2   ? 25.512  127.893 114.991 1.00 23.12 ? 2    THR Q O   1 
ATOM   17575 C  CB  . THR Q  1 2   ? 24.128  125.868 112.866 1.00 26.98 ? 2    THR Q CB  1 
ATOM   17576 O  OG1 . THR Q  1 2   ? 24.607  124.720 112.150 1.00 27.72 ? 2    THR Q OG1 1 
ATOM   17577 C  CG2 . THR Q  1 2   ? 24.870  126.970 112.206 1.00 28.66 ? 2    THR Q CG2 1 
ATOM   17578 N  N   . LYS Q  1 3   ? 26.913  126.131 114.696 1.00 22.43 ? 3    LYS Q N   1 
ATOM   17579 C  CA  . LYS Q  1 3   ? 28.138  126.826 115.071 1.00 20.94 ? 3    LYS Q CA  1 
ATOM   17580 C  C   . LYS Q  1 3   ? 29.226  126.647 114.041 1.00 19.16 ? 3    LYS Q C   1 
ATOM   17581 O  O   . LYS Q  1 3   ? 29.294  125.637 113.353 1.00 17.65 ? 3    LYS Q O   1 
ATOM   17582 C  CB  . LYS Q  1 3   ? 28.678  126.309 116.402 1.00 21.62 ? 3    LYS Q CB  1 
ATOM   17583 C  CG  . LYS Q  1 3   ? 27.885  126.782 117.628 1.00 24.58 ? 3    LYS Q CG  1 
ATOM   17584 C  CD  . LYS Q  1 3   ? 28.454  126.157 118.906 1.00 27.41 ? 3    LYS Q CD  1 
ATOM   17585 C  CE  . LYS Q  1 3   ? 28.558  127.193 120.015 1.00 29.87 ? 3    LYS Q CE  1 
ATOM   17586 N  NZ  . LYS Q  1 3   ? 29.345  128.380 119.537 1.00 28.24 ? 3    LYS Q NZ  1 
ATOM   17587 N  N   . ALA Q  1 4   ? 30.087  127.650 113.940 1.00 17.68 ? 4    ALA Q N   1 
ATOM   17588 C  CA  . ALA Q  1 4   ? 31.202  127.543 113.028 1.00 16.10 ? 4    ALA Q CA  1 
ATOM   17589 C  C   . ALA Q  1 4   ? 32.360  128.323 113.609 1.00 15.27 ? 4    ALA Q C   1 
ATOM   17590 O  O   . ALA Q  1 4   ? 32.187  129.124 114.532 1.00 15.45 ? 4    ALA Q O   1 
ATOM   17591 C  CB  . ALA Q  1 4   ? 30.822  128.053 111.671 1.00 15.83 ? 4    ALA Q CB  1 
ATOM   17592 N  N   . VAL Q  1 5   ? 33.551  128.085 113.085 1.00 14.05 ? 5    VAL Q N   1 
ATOM   17593 C  CA  . VAL Q  1 5   ? 34.712  128.729 113.646 1.00 13.32 ? 5    VAL Q CA  1 
ATOM   17594 C  C   . VAL Q  1 5   ? 35.740  128.938 112.583 1.00 12.60 ? 5    VAL Q C   1 
ATOM   17595 O  O   . VAL Q  1 5   ? 35.752  128.223 111.589 1.00 13.50 ? 5    VAL Q O   1 
ATOM   17596 C  CB  . VAL Q  1 5   ? 35.329  127.904 114.779 1.00 13.73 ? 5    VAL Q CB  1 
ATOM   17597 C  CG1 . VAL Q  1 5   ? 35.886  126.547 114.244 1.00 11.78 ? 5    VAL Q CG1 1 
ATOM   17598 C  CG2 . VAL Q  1 5   ? 36.408  128.702 115.476 1.00 15.46 ? 5    VAL Q CG2 1 
ATOM   17599 N  N   . CYS Q  1 6   ? 36.580  129.951 112.774 1.00 12.56 ? 6    CYS Q N   1 
ATOM   17600 C  CA  . CYS Q  1 6   ? 37.621  130.276 111.792 1.00 12.87 ? 6    CYS Q CA  1 
ATOM   17601 C  C   . CYS Q  1 6   ? 38.899  130.702 112.478 1.00 11.87 ? 6    CYS Q C   1 
ATOM   17602 O  O   . CYS Q  1 6   ? 38.891  131.592 113.337 1.00 12.21 ? 6    CYS Q O   1 
ATOM   17603 C  CB  . CYS Q  1 6   ? 37.150  131.377 110.850 1.00 12.02 ? 6    CYS Q CB  1 
ATOM   17604 S  SG  . CYS Q  1 6   ? 38.329  131.824 109.569 1.00 14.58 ? 6    CYS Q SG  1 
ATOM   17605 N  N   . VAL Q  1 7   ? 39.996  130.058 112.102 1.00 11.38 ? 7    VAL Q N   1 
ATOM   17606 C  CA  . VAL Q  1 7   ? 41.313  130.444 112.583 1.00 10.86 ? 7    VAL Q CA  1 
ATOM   17607 C  C   . VAL Q  1 7   ? 41.991  131.273 111.503 1.00 10.55 ? 7    VAL Q C   1 
ATOM   17608 O  O   . VAL Q  1 7   ? 42.268  130.777 110.423 1.00 9.61  ? 7    VAL Q O   1 
ATOM   17609 C  CB  . VAL Q  1 7   ? 42.173  129.203 112.811 1.00 12.15 ? 7    VAL Q CB  1 
ATOM   17610 C  CG1 . VAL Q  1 7   ? 43.578  129.593 113.351 1.00 13.26 ? 7    VAL Q CG1 1 
ATOM   17611 C  CG2 . VAL Q  1 7   ? 41.453  128.283 113.769 1.00 11.54 ? 7    VAL Q CG2 1 
ATOM   17612 N  N   . LEU Q  1 8   ? 42.258  132.545 111.790 1.00 9.83  ? 8    LEU Q N   1 
ATOM   17613 C  CA  . LEU Q  1 8   ? 42.842  133.400 110.769 1.00 10.49 ? 8    LEU Q CA  1 
ATOM   17614 C  C   . LEU Q  1 8   ? 44.345  133.422 110.901 1.00 10.17 ? 8    LEU Q C   1 
ATOM   17615 O  O   . LEU Q  1 8   ? 44.842  133.641 111.990 1.00 10.59 ? 8    LEU Q O   1 
ATOM   17616 C  CB  . LEU Q  1 8   ? 42.380  134.844 111.005 1.00 10.31 ? 8    LEU Q CB  1 
ATOM   17617 C  CG  . LEU Q  1 8   ? 40.893  135.179 110.902 1.00 14.60 ? 8    LEU Q CG  1 
ATOM   17618 C  CD1 . LEU Q  1 8   ? 40.452  135.021 109.523 1.00 17.99 ? 8    LEU Q CD1 1 
ATOM   17619 C  CD2 . LEU Q  1 8   ? 40.024  134.369 111.819 1.00 18.84 ? 8    LEU Q CD2 1 
ATOM   17620 N  N   . LYS Q  1 9   ? 45.067  133.223 109.802 1.00 10.34 ? 9    LYS Q N   1 
ATOM   17621 C  CA  . LYS Q  1 9   ? 46.527  133.247 109.831 1.00 11.59 ? 9    LYS Q CA  1 
ATOM   17622 C  C   . LYS Q  1 9   ? 46.976  133.849 108.515 1.00 11.71 ? 9    LYS Q C   1 
ATOM   17623 O  O   . LYS Q  1 9   ? 46.254  133.766 107.528 1.00 11.62 ? 9    LYS Q O   1 
ATOM   17624 C  CB  . LYS Q  1 9   ? 47.082  131.805 109.917 1.00 13.25 ? 9    LYS Q CB  1 
ATOM   17625 C  CG  . LYS Q  1 9   ? 46.771  131.139 111.273 1.00 15.85 ? 9    LYS Q CG  1 
ATOM   17626 C  CD  . LYS Q  1 9   ? 47.456  129.796 111.478 1.00 24.10 ? 9    LYS Q CD  1 
ATOM   17627 C  CE  . LYS Q  1 9   ? 47.321  129.359 112.947 1.00 27.81 ? 9    LYS Q CE  1 
ATOM   17628 N  NZ  . LYS Q  1 9   ? 47.839  130.440 113.847 1.00 31.55 ? 9    LYS Q NZ  1 
ATOM   17629 N  N   . GLY Q  1 10  ? 48.185  134.376 108.453 1.00 12.45 ? 10   GLY Q N   1 
ATOM   17630 C  CA  . GLY Q  1 10  ? 48.637  134.956 107.205 1.00 14.47 ? 10   GLY Q CA  1 
ATOM   17631 C  C   . GLY Q  1 10  ? 50.143  134.903 107.139 1.00 15.45 ? 10   GLY Q C   1 
ATOM   17632 O  O   . GLY Q  1 10  ? 50.766  134.118 107.844 1.00 14.44 ? 10   GLY Q O   1 
ATOM   17633 N  N   . ASP Q  1 11  ? 50.726  135.736 106.290 1.00 16.09 ? 11   ASP Q N   1 
ATOM   17634 C  CA  . ASP Q  1 11  ? 52.183  135.764 106.170 1.00 17.39 ? 11   ASP Q CA  1 
ATOM   17635 C  C   . ASP Q  1 11  ? 52.863  136.599 107.239 1.00 17.54 ? 11   ASP Q C   1 
ATOM   17636 O  O   . ASP Q  1 11  ? 54.066  136.436 107.490 1.00 17.72 ? 11   ASP Q O   1 
ATOM   17637 C  CB  . ASP Q  1 11  ? 52.574  136.320 104.818 1.00 17.80 ? 11   ASP Q CB  1 
ATOM   17638 C  CG  . ASP Q  1 11  ? 52.310  135.349 103.711 1.00 20.99 ? 11   ASP Q CG  1 
ATOM   17639 O  OD1 . ASP Q  1 11  ? 52.294  134.124 103.986 1.00 22.93 ? 11   ASP Q OD1 1 
ATOM   17640 O  OD2 . ASP Q  1 11  ? 52.083  135.724 102.540 1.00 27.09 ? 11   ASP Q OD2 1 
ATOM   17641 N  N   . GLY Q  1 12  ? 52.120  137.538 107.832 1.00 17.37 ? 12   GLY Q N   1 
ATOM   17642 C  CA  . GLY Q  1 12  ? 52.701  138.415 108.832 1.00 16.61 ? 12   GLY Q CA  1 
ATOM   17643 C  C   . GLY Q  1 12  ? 52.252  138.028 110.217 1.00 16.69 ? 12   GLY Q C   1 
ATOM   17644 O  O   . GLY Q  1 12  ? 51.888  136.884 110.469 1.00 17.34 ? 12   GLY Q O   1 
ATOM   17645 N  N   . PRO Q  1 13  ? 52.239  139.004 111.112 1.00 16.56 ? 13   PRO Q N   1 
ATOM   17646 C  CA  . PRO Q  1 13  ? 51.901  138.796 112.519 1.00 15.90 ? 13   PRO Q CA  1 
ATOM   17647 C  C   . PRO Q  1 13  ? 50.402  138.749 112.848 1.00 15.18 ? 13   PRO Q C   1 
ATOM   17648 O  O   . PRO Q  1 13  ? 50.052  138.537 114.014 1.00 15.02 ? 13   PRO Q O   1 
ATOM   17649 C  CB  . PRO Q  1 13  ? 52.502  140.037 113.176 1.00 16.16 ? 13   PRO Q CB  1 
ATOM   17650 C  CG  . PRO Q  1 13  ? 52.314  141.079 112.144 1.00 16.65 ? 13   PRO Q CG  1 
ATOM   17651 C  CD  . PRO Q  1 13  ? 52.566  140.408 110.820 1.00 16.67 ? 13   PRO Q CD  1 
ATOM   17652 N  N   . VAL Q  1 14  ? 49.539  138.909 111.855 1.00 13.43 ? 14   VAL Q N   1 
ATOM   17653 C  CA  . VAL Q  1 14  ? 48.104  138.961 112.126 1.00 12.79 ? 14   VAL Q CA  1 
ATOM   17654 C  C   . VAL Q  1 14  ? 47.532  137.571 112.274 1.00 12.71 ? 14   VAL Q C   1 
ATOM   17655 O  O   . VAL Q  1 14  ? 47.689  136.719 111.396 1.00 11.45 ? 14   VAL Q O   1 
ATOM   17656 C  CB  . VAL Q  1 14  ? 47.325  139.708 111.015 1.00 11.86 ? 14   VAL Q CB  1 
ATOM   17657 C  CG1 . VAL Q  1 14  ? 45.840  139.751 111.372 1.00 12.73 ? 14   VAL Q CG1 1 
ATOM   17658 C  CG2 . VAL Q  1 14  ? 47.833  141.160 110.909 1.00 11.34 ? 14   VAL Q CG2 1 
ATOM   17659 N  N   . GLN Q  1 15  ? 46.877  137.334 113.393 1.00 12.22 ? 15   GLN Q N   1 
ATOM   17660 C  CA  . GLN Q  1 15  ? 46.269  136.044 113.611 1.00 13.42 ? 15   GLN Q CA  1 
ATOM   17661 C  C   . GLN Q  1 15  ? 45.151  136.183 114.588 1.00 13.36 ? 15   GLN Q C   1 
ATOM   17662 O  O   . GLN Q  1 15  ? 45.148  137.096 115.422 1.00 13.85 ? 15   GLN Q O   1 
ATOM   17663 C  CB  . GLN Q  1 15  ? 47.294  135.026 114.147 1.00 13.37 ? 15   GLN Q CB  1 
ATOM   17664 C  CG  . GLN Q  1 15  ? 47.866  135.332 115.513 1.00 17.92 ? 15   GLN Q CG  1 
ATOM   17665 C  CD  . GLN Q  1 15  ? 48.949  134.328 115.915 1.00 24.50 ? 15   GLN Q CD  1 
ATOM   17666 O  OE1 . GLN Q  1 15  ? 48.680  133.125 116.042 1.00 28.97 ? 15   GLN Q OE1 1 
ATOM   17667 N  NE2 . GLN Q  1 15  ? 50.178  134.812 116.091 1.00 26.24 ? 15   GLN Q NE2 1 
ATOM   17668 N  N   . GLY Q  1 16  ? 44.188  135.284 114.496 1.00 13.06 ? 16   GLY Q N   1 
ATOM   17669 C  CA  . GLY Q  1 16  ? 43.073  135.332 115.420 1.00 13.01 ? 16   GLY Q CA  1 
ATOM   17670 C  C   . GLY Q  1 16  ? 42.115  134.151 115.277 1.00 13.20 ? 16   GLY Q C   1 
ATOM   17671 O  O   . GLY Q  1 16  ? 42.347  133.248 114.491 1.00 12.24 ? 16   GLY Q O   1 
ATOM   17672 N  N   . ILE Q  1 17  ? 41.034  134.191 116.058 1.00 12.89 ? 17   ILE Q N   1 
ATOM   17673 C  CA  . ILE Q  1 17  ? 39.999  133.177 116.054 1.00 12.71 ? 17   ILE Q CA  1 
ATOM   17674 C  C   . ILE Q  1 17  ? 38.642  133.853 116.056 1.00 12.25 ? 17   ILE Q C   1 
ATOM   17675 O  O   . ILE Q  1 17  ? 38.382  134.694 116.914 1.00 12.15 ? 17   ILE Q O   1 
ATOM   17676 C  CB  . ILE Q  1 17  ? 40.094  132.311 117.320 1.00 13.66 ? 17   ILE Q CB  1 
ATOM   17677 C  CG1 . ILE Q  1 17  ? 41.449  131.614 117.365 1.00 15.47 ? 17   ILE Q CG1 1 
ATOM   17678 C  CG2 . ILE Q  1 17  ? 38.916  131.332 117.372 1.00 14.08 ? 17   ILE Q CG2 1 
ATOM   17679 C  CD1 . ILE Q  1 17  ? 41.445  130.294 118.121 1.00 19.97 ? 17   ILE Q CD1 1 
ATOM   17680 N  N   . ILE Q  1 18  ? 37.786  133.482 115.108 1.00 11.75 ? 18   ILE Q N   1 
ATOM   17681 C  CA  . ILE Q  1 18  ? 36.465  134.084 114.998 1.00 12.30 ? 18   ILE Q CA  1 
ATOM   17682 C  C   . ILE Q  1 18  ? 35.416  132.973 115.071 1.00 12.11 ? 18   ILE Q C   1 
ATOM   17683 O  O   . ILE Q  1 18  ? 35.510  131.959 114.377 1.00 11.69 ? 18   ILE Q O   1 
ATOM   17684 C  CB  . ILE Q  1 18  ? 36.313  134.886 113.684 1.00 12.66 ? 18   ILE Q CB  1 
ATOM   17685 C  CG1 . ILE Q  1 18  ? 37.272  136.104 113.642 1.00 12.17 ? 18   ILE Q CG1 1 
ATOM   17686 C  CG2 . ILE Q  1 18  ? 34.847  135.355 113.505 1.00 12.12 ? 18   ILE Q CG2 1 
ATOM   17687 C  CD1 . ILE Q  1 18  ? 36.978  137.180 114.727 1.00 11.55 ? 18   ILE Q CD1 1 
ATOM   17688 N  N   . ASN Q  1 19  ? 34.432  133.160 115.943 1.00 13.15 ? 19   ASN Q N   1 
ATOM   17689 C  CA  . ASN Q  1 19  ? 33.325  132.228 116.090 1.00 13.89 ? 19   ASN Q CA  1 
ATOM   17690 C  C   . ASN Q  1 19  ? 32.078  132.730 115.405 1.00 14.46 ? 19   ASN Q C   1 
ATOM   17691 O  O   . ASN Q  1 19  ? 31.874  133.946 115.299 1.00 14.22 ? 19   ASN Q O   1 
ATOM   17692 C  CB  . ASN Q  1 19  ? 33.009  132.088 117.574 1.00 14.62 ? 19   ASN Q CB  1 
ATOM   17693 C  CG  . ASN Q  1 19  ? 34.246  131.827 118.392 1.00 16.02 ? 19   ASN Q CG  1 
ATOM   17694 O  OD1 . ASN Q  1 19  ? 34.746  132.713 119.084 1.00 21.06 ? 19   ASN Q OD1 1 
ATOM   17695 N  ND2 . ASN Q  1 19  ? 34.764  130.623 118.299 1.00 10.73 ? 19   ASN Q ND2 1 
ATOM   17696 N  N   . PHE Q  1 20  ? 31.220  131.796 114.995 1.00 14.79 ? 20   PHE Q N   1 
ATOM   17697 C  CA  . PHE Q  1 20  ? 29.949  132.099 114.346 1.00 14.30 ? 20   PHE Q CA  1 
ATOM   17698 C  C   . PHE Q  1 20  ? 28.906  131.239 115.011 1.00 15.14 ? 20   PHE Q C   1 
ATOM   17699 O  O   . PHE Q  1 20  ? 29.127  130.044 115.216 1.00 13.57 ? 20   PHE Q O   1 
ATOM   17700 C  CB  . PHE Q  1 20  ? 29.947  131.736 112.862 1.00 14.34 ? 20   PHE Q CB  1 
ATOM   17701 C  CG  . PHE Q  1 20  ? 31.002  132.431 112.073 1.00 14.26 ? 20   PHE Q CG  1 
ATOM   17702 C  CD1 . PHE Q  1 20  ? 32.317  131.990 112.130 1.00 17.92 ? 20   PHE Q CD1 1 
ATOM   17703 C  CD2 . PHE Q  1 20  ? 30.690  133.508 111.246 1.00 14.46 ? 20   PHE Q CD2 1 
ATOM   17704 C  CE1 . PHE Q  1 20  ? 33.317  132.632 111.411 1.00 15.64 ? 20   PHE Q CE1 1 
ATOM   17705 C  CE2 . PHE Q  1 20  ? 31.696  134.130 110.504 1.00 14.44 ? 20   PHE Q CE2 1 
ATOM   17706 C  CZ  . PHE Q  1 20  ? 33.003  133.704 110.604 1.00 15.29 ? 20   PHE Q CZ  1 
ATOM   17707 N  N   . GLU Q  1 21  ? 27.778  131.857 115.332 1.00 15.52 ? 21   GLU Q N   1 
ATOM   17708 C  CA  . GLU Q  1 21  ? 26.680  131.137 115.960 1.00 18.08 ? 21   GLU Q CA  1 
ATOM   17709 C  C   . GLU Q  1 21  ? 25.369  131.601 115.345 1.00 18.57 ? 21   GLU Q C   1 
ATOM   17710 O  O   . GLU Q  1 21  ? 25.117  132.804 115.232 1.00 18.16 ? 21   GLU Q O   1 
ATOM   17711 C  CB  . GLU Q  1 21  ? 26.698  131.380 117.465 1.00 18.13 ? 21   GLU Q CB  1 
ATOM   17712 C  CG  . GLU Q  1 21  ? 25.712  130.514 118.240 1.00 23.38 ? 21   GLU Q CG  1 
ATOM   17713 C  CD  . GLU Q  1 21  ? 25.827  130.717 119.737 1.00 28.47 ? 21   GLU Q CD  1 
ATOM   17714 O  OE1 . GLU Q  1 21  ? 26.092  131.870 120.170 1.00 32.26 ? 21   GLU Q OE1 1 
ATOM   17715 O  OE2 . GLU Q  1 21  ? 25.648  129.728 120.477 1.00 30.36 ? 21   GLU Q OE2 1 
ATOM   17716 N  N   . GLN Q  1 22  ? 24.566  130.643 114.895 1.00 19.52 ? 22   GLN Q N   1 
ATOM   17717 C  CA  . GLN Q  1 22  ? 23.251  130.934 114.359 1.00 20.67 ? 22   GLN Q CA  1 
ATOM   17718 C  C   . GLN Q  1 22  ? 22.336  130.153 115.298 1.00 22.72 ? 22   GLN Q C   1 
ATOM   17719 O  O   . GLN Q  1 22  ? 22.124  128.963 115.087 1.00 22.12 ? 22   GLN Q O   1 
ATOM   17720 C  CB  . GLN Q  1 22  ? 23.125  130.437 112.914 1.00 19.81 ? 22   GLN Q CB  1 
ATOM   17721 C  CG  . GLN Q  1 22  ? 22.043  131.136 112.085 1.00 18.80 ? 22   GLN Q CG  1 
ATOM   17722 C  CD  . GLN Q  1 22  ? 22.138  130.849 110.575 1.00 17.55 ? 22   GLN Q CD  1 
ATOM   17723 O  OE1 . GLN Q  1 22  ? 22.782  129.881 110.149 1.00 17.15 ? 22   GLN Q OE1 1 
ATOM   17724 N  NE2 . GLN Q  1 22  ? 21.460  131.682 109.768 1.00 15.44 ? 22   GLN Q NE2 1 
ATOM   17725 N  N   . LYS Q  1 23  ? 21.853  130.836 116.345 1.00 25.29 ? 23   LYS Q N   1 
ATOM   17726 C  CA  . LYS Q  1 23  ? 21.021  130.245 117.407 1.00 29.05 ? 23   LYS Q CA  1 
ATOM   17727 C  C   . LYS Q  1 23  ? 19.798  129.517 116.904 1.00 30.04 ? 23   LYS Q C   1 
ATOM   17728 O  O   . LYS Q  1 23  ? 19.306  128.595 117.550 1.00 30.40 ? 23   LYS Q O   1 
ATOM   17729 C  CB  . LYS Q  1 23  ? 20.540  131.322 118.393 1.00 29.84 ? 23   LYS Q CB  1 
ATOM   17730 C  CG  . LYS Q  1 23  ? 21.393  131.520 119.658 1.00 33.21 ? 23   LYS Q CG  1 
ATOM   17731 C  CD  . LYS Q  1 23  ? 20.931  132.766 120.448 1.00 37.78 ? 23   LYS Q CD  1 
ATOM   17732 C  CE  . LYS Q  1 23  ? 21.935  133.163 121.537 1.00 39.82 ? 23   LYS Q CE  1 
ATOM   17733 N  NZ  . LYS Q  1 23  ? 23.225  133.690 120.980 1.00 41.28 ? 23   LYS Q NZ  1 
ATOM   17734 N  N   . GLU Q  1 24  ? 19.260  129.958 115.779 1.00 31.69 ? 24   GLU Q N   1 
ATOM   17735 C  CA  . GLU Q  1 24  ? 18.095  129.270 115.258 1.00 33.99 ? 24   GLU Q CA  1 
ATOM   17736 C  C   . GLU Q  1 24  ? 18.397  128.632 113.914 1.00 34.38 ? 24   GLU Q C   1 
ATOM   17737 O  O   . GLU Q  1 24  ? 19.325  127.815 113.798 1.00 35.55 ? 24   GLU Q O   1 
ATOM   17738 C  CB  . GLU Q  1 24  ? 16.848  130.177 115.222 1.00 34.02 ? 24   GLU Q CB  1 
ATOM   17739 C  CG  . GLU Q  1 24  ? 15.749  129.783 116.213 1.00 37.10 ? 24   GLU Q CG  1 
ATOM   17740 C  CD  . GLU Q  1 24  ? 16.235  129.659 117.653 1.00 39.82 ? 24   GLU Q CD  1 
ATOM   17741 O  OE1 . GLU Q  1 24  ? 17.011  130.540 118.092 1.00 42.07 ? 24   GLU Q OE1 1 
ATOM   17742 O  OE2 . GLU Q  1 24  ? 15.844  128.686 118.342 1.00 38.27 ? 24   GLU Q OE2 1 
ATOM   17743 N  N   . SER Q  1 25  ? 17.627  129.010 112.904 1.00 34.59 ? 25   SER Q N   1 
ATOM   17744 C  CA  . SER Q  1 25  ? 17.742  128.410 111.592 1.00 34.93 ? 25   SER Q CA  1 
ATOM   17745 C  C   . SER Q  1 25  ? 18.259  129.430 110.620 1.00 34.83 ? 25   SER Q C   1 
ATOM   17746 O  O   . SER Q  1 25  ? 19.381  129.331 110.126 1.00 35.55 ? 25   SER Q O   1 
ATOM   17747 C  CB  . SER Q  1 25  ? 16.380  127.899 111.138 1.00 35.25 ? 25   SER Q CB  1 
ATOM   17748 O  OG  . SER Q  1 25  ? 15.369  128.846 111.447 1.00 37.32 ? 25   SER Q OG  1 
ATOM   17749 N  N   . ASN Q  1 26  ? 17.448  130.428 110.328 1.00 34.70 ? 26   ASN Q N   1 
ATOM   17750 C  CA  . ASN Q  1 26  ? 17.928  131.461 109.432 1.00 33.84 ? 26   ASN Q CA  1 
ATOM   17751 C  C   . ASN Q  1 26  ? 17.784  132.835 110.031 1.00 32.39 ? 26   ASN Q C   1 
ATOM   17752 O  O   . ASN Q  1 26  ? 17.489  133.811 109.352 1.00 32.84 ? 26   ASN Q O   1 
ATOM   17753 C  CB  . ASN Q  1 26  ? 17.278  131.330 108.066 1.00 34.76 ? 26   ASN Q CB  1 
ATOM   17754 C  CG  . ASN Q  1 26  ? 17.818  130.137 107.314 1.00 35.54 ? 26   ASN Q CG  1 
ATOM   17755 O  OD1 . ASN Q  1 26  ? 18.794  130.252 106.567 1.00 37.21 ? 26   ASN Q OD1 1 
ATOM   17756 N  ND2 . ASN Q  1 26  ? 17.228  128.973 107.552 1.00 36.83 ? 26   ASN Q ND2 1 
ATOM   17757 N  N   . GLY Q  1 27  ? 18.009  132.883 111.333 1.00 30.52 ? 27   GLY Q N   1 
ATOM   17758 C  CA  . GLY Q  1 27  ? 17.981  134.121 112.056 1.00 28.10 ? 27   GLY Q CA  1 
ATOM   17759 C  C   . GLY Q  1 27  ? 19.332  134.745 111.859 1.00 26.31 ? 27   GLY Q C   1 
ATOM   17760 O  O   . GLY Q  1 27  ? 20.091  134.366 110.955 1.00 26.39 ? 27   GLY Q O   1 
ATOM   17761 N  N   . PRO Q  1 28  ? 19.654  135.688 112.728 1.00 24.69 ? 28   PRO Q N   1 
ATOM   17762 C  CA  . PRO Q  1 28  ? 20.929  136.398 112.639 1.00 23.04 ? 28   PRO Q CA  1 
ATOM   17763 C  C   . PRO Q  1 28  ? 22.062  135.427 112.912 1.00 21.72 ? 28   PRO Q C   1 
ATOM   17764 O  O   . PRO Q  1 28  ? 21.814  134.333 113.398 1.00 20.26 ? 28   PRO Q O   1 
ATOM   17765 C  CB  . PRO Q  1 28  ? 20.851  137.397 113.795 1.00 23.10 ? 28   PRO Q CB  1 
ATOM   17766 C  CG  . PRO Q  1 28  ? 19.389  137.450 114.180 1.00 24.65 ? 28   PRO Q CG  1 
ATOM   17767 C  CD  . PRO Q  1 28  ? 18.842  136.108 113.881 1.00 24.38 ? 28   PRO Q CD  1 
ATOM   17768 N  N   . VAL Q  1 29  ? 23.285  135.821 112.570 1.00 20.13 ? 29   VAL Q N   1 
ATOM   17769 C  CA  . VAL Q  1 29  ? 24.462  135.056 112.915 1.00 18.84 ? 29   VAL Q CA  1 
ATOM   17770 C  C   . VAL Q  1 29  ? 25.292  135.959 113.794 1.00 18.36 ? 29   VAL Q C   1 
ATOM   17771 O  O   . VAL Q  1 29  ? 25.597  137.092 113.414 1.00 18.79 ? 29   VAL Q O   1 
ATOM   17772 C  CB  . VAL Q  1 29  ? 25.315  134.688 111.692 1.00 19.16 ? 29   VAL Q CB  1 
ATOM   17773 C  CG1 . VAL Q  1 29  ? 26.593  133.920 112.136 1.00 18.72 ? 29   VAL Q CG1 1 
ATOM   17774 C  CG2 . VAL Q  1 29  ? 24.507  133.877 110.685 1.00 18.77 ? 29   VAL Q CG2 1 
ATOM   17775 N  N   . LYS Q  1 30  ? 25.638  135.481 114.971 1.00 17.29 ? 30   LYS Q N   1 
ATOM   17776 C  CA  . LYS Q  1 30  ? 26.514  136.220 115.850 1.00 17.54 ? 30   LYS Q CA  1 
ATOM   17777 C  C   . LYS Q  1 30  ? 27.932  135.873 115.436 1.00 16.76 ? 30   LYS Q C   1 
ATOM   17778 O  O   . LYS Q  1 30  ? 28.269  134.707 115.309 1.00 15.82 ? 30   LYS Q O   1 
ATOM   17779 C  CB  . LYS Q  1 30  ? 26.317  135.789 117.299 1.00 18.11 ? 30   LYS Q CB  1 
ATOM   17780 C  CG  . LYS Q  1 30  ? 25.480  136.725 118.141 1.00 22.55 ? 30   LYS Q CG  1 
ATOM   17781 C  CD  . LYS Q  1 30  ? 25.475  136.287 119.607 1.00 29.20 ? 30   LYS Q CD  1 
ATOM   17782 C  CE  . LYS Q  1 30  ? 25.423  137.481 120.564 1.00 32.46 ? 30   LYS Q CE  1 
ATOM   17783 N  NZ  . LYS Q  1 30  ? 25.454  137.042 122.007 1.00 36.27 ? 30   LYS Q NZ  1 
ATOM   17784 N  N   . VAL Q  1 31  ? 28.758  136.884 115.205 1.00 16.41 ? 31   VAL Q N   1 
ATOM   17785 C  CA  . VAL Q  1 31  ? 30.161  136.640 114.874 1.00 15.11 ? 31   VAL Q CA  1 
ATOM   17786 C  C   . VAL Q  1 31  ? 31.055  137.349 115.895 1.00 15.40 ? 31   VAL Q C   1 
ATOM   17787 O  O   . VAL Q  1 31  ? 30.869  138.528 116.145 1.00 15.58 ? 31   VAL Q O   1 
ATOM   17788 C  CB  . VAL Q  1 31  ? 30.487  136.891 113.358 1.00 15.76 ? 31   VAL Q CB  1 
ATOM   17789 C  CG1 . VAL Q  1 31  ? 29.556  137.745 112.709 1.00 16.25 ? 31   VAL Q CG1 1 
ATOM   17790 C  CG2 . VAL Q  1 31  ? 32.018  137.188 113.064 1.00 12.13 ? 31   VAL Q CG2 1 
ATOM   17791 N  N   . TRP Q  1 32  ? 31.998  136.631 116.521 1.00 14.54 ? 32   TRP Q N   1 
ATOM   17792 C  CA  . TRP Q  1 32  ? 32.794  137.228 117.596 1.00 14.15 ? 32   TRP Q CA  1 
ATOM   17793 C  C   . TRP Q  1 32  ? 34.106  136.523 117.886 1.00 14.25 ? 32   TRP Q C   1 
ATOM   17794 O  O   . TRP Q  1 32  ? 34.284  135.337 117.591 1.00 14.24 ? 32   TRP Q O   1 
ATOM   17795 C  CB  . TRP Q  1 32  ? 31.959  137.329 118.904 1.00 14.41 ? 32   TRP Q CB  1 
ATOM   17796 C  CG  . TRP Q  1 32  ? 31.964  136.075 119.697 1.00 16.33 ? 32   TRP Q CG  1 
ATOM   17797 C  CD1 . TRP Q  1 32  ? 32.720  135.802 120.796 1.00 17.77 ? 32   TRP Q CD1 1 
ATOM   17798 C  CD2 . TRP Q  1 32  ? 31.187  134.908 119.446 1.00 16.43 ? 32   TRP Q CD2 1 
ATOM   17799 N  NE1 . TRP Q  1 32  ? 32.458  134.532 121.248 1.00 18.70 ? 32   TRP Q NE1 1 
ATOM   17800 C  CE2 . TRP Q  1 32  ? 31.515  133.963 120.432 1.00 17.63 ? 32   TRP Q CE2 1 
ATOM   17801 C  CE3 . TRP Q  1 32  ? 30.239  134.563 118.479 1.00 15.93 ? 32   TRP Q CE3 1 
ATOM   17802 C  CZ2 . TRP Q  1 32  ? 30.944  132.703 120.470 1.00 16.88 ? 32   TRP Q CZ2 1 
ATOM   17803 C  CZ3 . TRP Q  1 32  ? 29.677  133.324 118.520 1.00 16.19 ? 32   TRP Q CZ3 1 
ATOM   17804 C  CH2 . TRP Q  1 32  ? 30.018  132.408 119.512 1.00 16.38 ? 32   TRP Q CH2 1 
ATOM   17805 N  N   . GLY Q  1 33  ? 35.045  137.264 118.451 1.00 14.52 ? 33   GLY Q N   1 
ATOM   17806 C  CA  . GLY Q  1 33  ? 36.357  136.705 118.735 1.00 15.64 ? 33   GLY Q CA  1 
ATOM   17807 C  C   . GLY Q  1 33  ? 37.373  137.820 118.797 1.00 16.49 ? 33   GLY Q C   1 
ATOM   17808 O  O   . GLY Q  1 33  ? 37.034  138.983 119.032 1.00 15.91 ? 33   GLY Q O   1 
ATOM   17809 N  N   . SER Q  1 34  ? 38.628  137.486 118.559 1.00 16.36 ? 34   SER Q N   1 
ATOM   17810 C  CA  . SER Q  1 34  ? 39.659  138.501 118.612 1.00 17.20 ? 34   SER Q CA  1 
ATOM   17811 C  C   . SER Q  1 34  ? 40.772  138.263 117.592 1.00 16.82 ? 34   SER Q C   1 
ATOM   17812 O  O   . SER Q  1 34  ? 41.104  137.117 117.278 1.00 16.42 ? 34   SER Q O   1 
ATOM   17813 C  CB  . SER Q  1 34  ? 40.181  138.587 120.053 1.00 17.71 ? 34   SER Q CB  1 
ATOM   17814 O  OG  . SER Q  1 34  ? 41.559  138.316 120.135 1.00 22.95 ? 34   SER Q OG  1 
ATOM   17815 N  N   . ILE Q  1 35  ? 41.331  139.345 117.061 1.00 15.39 ? 35   ILE Q N   1 
ATOM   17816 C  CA  . ILE Q  1 35  ? 42.403  139.242 116.084 1.00 14.20 ? 35   ILE Q CA  1 
ATOM   17817 C  C   . ILE Q  1 35  ? 43.499  140.148 116.593 1.00 14.50 ? 35   ILE Q C   1 
ATOM   17818 O  O   . ILE Q  1 35  ? 43.235  141.315 116.973 1.00 13.23 ? 35   ILE Q O   1 
ATOM   17819 C  CB  . ILE Q  1 35  ? 41.952  139.767 114.722 1.00 14.35 ? 35   ILE Q CB  1 
ATOM   17820 C  CG1 . ILE Q  1 35  ? 40.641  139.122 114.292 1.00 13.34 ? 35   ILE Q CG1 1 
ATOM   17821 C  CG2 . ILE Q  1 35  ? 43.049  139.555 113.661 1.00 12.19 ? 35   ILE Q CG2 1 
ATOM   17822 C  CD1 . ILE Q  1 35  ? 39.993  139.861 113.069 1.00 13.14 ? 35   ILE Q CD1 1 
ATOM   17823 N  N   . LYS Q  1 36  ? 44.727  139.637 116.602 1.00 13.43 ? 36   LYS Q N   1 
ATOM   17824 C  CA  . LYS Q  1 36  ? 45.823  140.413 117.122 1.00 13.83 ? 36   LYS Q CA  1 
ATOM   17825 C  C   . LYS Q  1 36  ? 46.849  140.712 116.064 1.00 13.44 ? 36   LYS Q C   1 
ATOM   17826 O  O   . LYS Q  1 36  ? 46.814  140.129 114.980 1.00 12.59 ? 36   LYS Q O   1 
ATOM   17827 C  CB  . LYS Q  1 36  ? 46.471  139.694 118.310 1.00 14.69 ? 36   LYS Q CB  1 
ATOM   17828 C  CG  . LYS Q  1 36  ? 47.196  138.441 117.921 1.00 17.43 ? 36   LYS Q CG  1 
ATOM   17829 C  CD  . LYS Q  1 36  ? 48.105  137.922 119.053 1.00 23.41 ? 36   LYS Q CD  1 
ATOM   17830 C  CE  . LYS Q  1 36  ? 48.854  136.669 118.596 1.00 24.54 ? 36   LYS Q CE  1 
ATOM   17831 N  NZ  . LYS Q  1 36  ? 49.581  136.002 119.727 1.00 28.82 ? 36   LYS Q NZ  1 
ATOM   17832 N  N   . GLY Q  1 37  ? 47.743  141.653 116.378 1.00 12.30 ? 37   GLY Q N   1 
ATOM   17833 C  CA  . GLY Q  1 37  ? 48.806  142.025 115.467 1.00 12.57 ? 37   GLY Q CA  1 
ATOM   17834 C  C   . GLY Q  1 37  ? 48.435  143.073 114.425 1.00 12.06 ? 37   GLY Q C   1 
ATOM   17835 O  O   . GLY Q  1 37  ? 49.187  143.294 113.476 1.00 11.97 ? 37   GLY Q O   1 
ATOM   17836 N  N   . LEU Q  1 38  ? 47.283  143.719 114.578 1.00 12.14 ? 38   LEU Q N   1 
ATOM   17837 C  CA  . LEU Q  1 38  ? 46.843  144.698 113.578 1.00 12.21 ? 38   LEU Q CA  1 
ATOM   17838 C  C   . LEU Q  1 38  ? 47.372  146.107 113.838 1.00 12.69 ? 38   LEU Q C   1 
ATOM   17839 O  O   . LEU Q  1 38  ? 47.722  146.427 114.967 1.00 12.14 ? 38   LEU Q O   1 
ATOM   17840 C  CB  . LEU Q  1 38  ? 45.310  144.751 113.552 1.00 12.07 ? 38   LEU Q CB  1 
ATOM   17841 C  CG  . LEU Q  1 38  ? 44.639  143.462 113.017 1.00 12.73 ? 38   LEU Q CG  1 
ATOM   17842 C  CD1 . LEU Q  1 38  ? 43.203  143.382 113.497 1.00 11.55 ? 38   LEU Q CD1 1 
ATOM   17843 C  CD2 . LEU Q  1 38  ? 44.687  143.424 111.511 1.00 13.33 ? 38   LEU Q CD2 1 
ATOM   17844 N  N   . THR Q  1 39  ? 47.436  146.937 112.793 1.00 12.77 ? 39   THR Q N   1 
ATOM   17845 C  CA  . THR Q  1 39  ? 47.795  148.343 112.958 1.00 13.01 ? 39   THR Q CA  1 
ATOM   17846 C  C   . THR Q  1 39  ? 46.530  148.953 113.506 1.00 13.39 ? 39   THR Q C   1 
ATOM   17847 O  O   . THR Q  1 39  ? 45.414  148.540 113.134 1.00 13.37 ? 39   THR Q O   1 
ATOM   17848 C  CB  . THR Q  1 39  ? 48.137  149.026 111.625 1.00 13.80 ? 39   THR Q CB  1 
ATOM   17849 O  OG1 . THR Q  1 39  ? 47.015  148.948 110.727 1.00 12.42 ? 39   THR Q OG1 1 
ATOM   17850 C  CG2 . THR Q  1 39  ? 49.267  148.322 110.890 1.00 13.93 ? 39   THR Q CG2 1 
ATOM   17851 N  N   . GLU Q  1 40  ? 46.691  149.932 114.387 1.00 13.48 ? 40   GLU Q N   1 
ATOM   17852 C  CA  . GLU Q  1 40  ? 45.570  150.602 115.037 1.00 13.88 ? 40   GLU Q CA  1 
ATOM   17853 C  C   . GLU Q  1 40  ? 44.614  151.166 114.010 1.00 13.66 ? 40   GLU Q C   1 
ATOM   17854 O  O   . GLU Q  1 40  ? 45.049  151.777 113.016 1.00 14.22 ? 40   GLU Q O   1 
ATOM   17855 C  CB  . GLU Q  1 40  ? 46.073  151.744 115.938 1.00 14.14 ? 40   GLU Q CB  1 
ATOM   17856 C  CG  . GLU Q  1 40  ? 44.977  152.354 116.810 1.00 16.01 ? 40   GLU Q CG  1 
ATOM   17857 C  CD  . GLU Q  1 40  ? 45.470  153.513 117.674 1.00 20.25 ? 40   GLU Q CD  1 
ATOM   17858 O  OE1 . GLU Q  1 40  ? 46.686  153.617 117.934 1.00 21.05 ? 40   GLU Q OE1 1 
ATOM   17859 O  OE2 . GLU Q  1 40  ? 44.631  154.332 118.092 1.00 22.95 ? 40   GLU Q OE2 1 
ATOM   17860 N  N   . GLY Q  1 41  ? 43.314  150.981 114.246 1.00 13.18 ? 41   GLY Q N   1 
ATOM   17861 C  CA  . GLY Q  1 41  ? 42.293  151.483 113.325 1.00 12.40 ? 41   GLY Q CA  1 
ATOM   17862 C  C   . GLY Q  1 41  ? 41.322  150.454 112.739 1.00 11.51 ? 41   GLY Q C   1 
ATOM   17863 O  O   . GLY Q  1 41  ? 41.215  149.296 113.201 1.00 10.96 ? 41   GLY Q O   1 
ATOM   17864 N  N   . LEU Q  1 42  ? 40.582  150.886 111.713 1.00 11.71 ? 42   LEU Q N   1 
ATOM   17865 C  CA  . LEU Q  1 42  ? 39.596  150.015 111.043 1.00 10.87 ? 42   LEU Q CA  1 
ATOM   17866 C  C   . LEU Q  1 42  ? 40.256  149.123 110.012 1.00 11.25 ? 42   LEU Q C   1 
ATOM   17867 O  O   . LEU Q  1 42  ? 41.186  149.547 109.329 1.00 10.28 ? 42   LEU Q O   1 
ATOM   17868 C  CB  . LEU Q  1 42  ? 38.606  150.911 110.278 1.00 11.84 ? 42   LEU Q CB  1 
ATOM   17869 C  CG  . LEU Q  1 42  ? 37.764  151.859 111.127 1.00 11.03 ? 42   LEU Q CG  1 
ATOM   17870 C  CD1 . LEU Q  1 42  ? 36.999  152.836 110.216 1.00 16.35 ? 42   LEU Q CD1 1 
ATOM   17871 C  CD2 . LEU Q  1 42  ? 36.798  151.053 111.944 1.00 12.97 ? 42   LEU Q CD2 1 
ATOM   17872 N  N   . HIS Q  1 43  ? 39.758  147.884 109.904 1.00 10.37 ? 43   HIS Q N   1 
ATOM   17873 C  CA  . HIS Q  1 43  ? 40.232  146.894 108.948 1.00 9.19  ? 43   HIS Q CA  1 
ATOM   17874 C  C   . HIS Q  1 43  ? 39.048  146.189 108.331 1.00 9.27  ? 43   HIS Q C   1 
ATOM   17875 O  O   . HIS Q  1 43  ? 38.173  145.695 109.033 1.00 7.58  ? 43   HIS Q O   1 
ATOM   17876 C  CB  . HIS Q  1 43  ? 41.102  145.850 109.646 1.00 10.13 ? 43   HIS Q CB  1 
ATOM   17877 C  CG  . HIS Q  1 43  ? 42.362  146.431 110.204 1.00 10.11 ? 43   HIS Q CG  1 
ATOM   17878 N  ND1 . HIS Q  1 43  ? 43.524  146.523 109.466 1.00 12.61 ? 43   HIS Q ND1 1 
ATOM   17879 C  CD2 . HIS Q  1 43  ? 42.614  147.044 111.386 1.00 11.55 ? 43   HIS Q CD2 1 
ATOM   17880 C  CE1 . HIS Q  1 43  ? 44.455  147.117 110.192 1.00 12.67 ? 43   HIS Q CE1 1 
ATOM   17881 N  NE2 . HIS Q  1 43  ? 43.925  147.453 111.356 1.00 13.37 ? 43   HIS Q NE2 1 
ATOM   17882 N  N   . GLY Q  1 44  ? 39.025  146.128 107.012 1.00 9.54  ? 44   GLY Q N   1 
ATOM   17883 C  CA  . GLY Q  1 44  ? 37.938  145.444 106.351 1.00 8.70  ? 44   GLY Q CA  1 
ATOM   17884 C  C   . GLY Q  1 44  ? 37.850  144.005 106.795 1.00 9.51  ? 44   GLY Q C   1 
ATOM   17885 O  O   . GLY Q  1 44  ? 38.892  143.371 107.071 1.00 9.25  ? 44   GLY Q O   1 
ATOM   17886 N  N   . PHE Q  1 45  ? 36.622  143.471 106.802 1.00 8.36  ? 45   PHE Q N   1 
ATOM   17887 C  CA  . PHE Q  1 45  ? 36.388  142.135 107.374 1.00 7.70  ? 45   PHE Q CA  1 
ATOM   17888 C  C   . PHE Q  1 45  ? 35.327  141.445 106.514 1.00 8.32  ? 45   PHE Q C   1 
ATOM   17889 O  O   . PHE Q  1 45  ? 34.156  141.830 106.574 1.00 7.34  ? 45   PHE Q O   1 
ATOM   17890 C  CB  . PHE Q  1 45  ? 35.879  142.380 108.810 1.00 7.05  ? 45   PHE Q CB  1 
ATOM   17891 C  CG  . PHE Q  1 45  ? 35.748  141.134 109.664 1.00 8.14  ? 45   PHE Q CG  1 
ATOM   17892 C  CD1 . PHE Q  1 45  ? 36.850  140.357 109.935 1.00 9.51  ? 45   PHE Q CD1 1 
ATOM   17893 C  CD2 . PHE Q  1 45  ? 34.538  140.809 110.232 1.00 9.50  ? 45   PHE Q CD2 1 
ATOM   17894 C  CE1 . PHE Q  1 45  ? 36.739  139.244 110.746 1.00 12.56 ? 45   PHE Q CE1 1 
ATOM   17895 C  CE2 . PHE Q  1 45  ? 34.416  139.722 111.046 1.00 11.64 ? 45   PHE Q CE2 1 
ATOM   17896 C  CZ  . PHE Q  1 45  ? 35.519  138.936 111.298 1.00 10.24 ? 45   PHE Q CZ  1 
ATOM   17897 N  N   . HIS Q  1 46  ? 35.709  140.430 105.723 1.00 8.72  ? 46   HIS Q N   1 
ATOM   17898 C  CA  . HIS Q  1 46  ? 34.768  139.883 104.757 1.00 10.59 ? 46   HIS Q CA  1 
ATOM   17899 C  C   . HIS Q  1 46  ? 34.844  138.383 104.573 1.00 10.32 ? 46   HIS Q C   1 
ATOM   17900 O  O   . HIS Q  1 46  ? 35.896  137.781 104.753 1.00 11.15 ? 46   HIS Q O   1 
ATOM   17901 C  CB  . HIS Q  1 46  ? 35.043  140.408 103.339 1.00 10.65 ? 46   HIS Q CB  1 
ATOM   17902 C  CG  . HIS Q  1 46  ? 35.367  141.868 103.259 1.00 10.92 ? 46   HIS Q CG  1 
ATOM   17903 N  ND1 . HIS Q  1 46  ? 36.517  142.337 102.681 1.00 9.55  ? 46   HIS Q ND1 1 
ATOM   17904 C  CD2 . HIS Q  1 46  ? 34.668  142.959 103.633 1.00 10.76 ? 46   HIS Q CD2 1 
ATOM   17905 C  CE1 . HIS Q  1 46  ? 36.525  143.651 102.700 1.00 12.22 ? 46   HIS Q CE1 1 
ATOM   17906 N  NE2 . HIS Q  1 46  ? 35.423  144.056 103.304 1.00 9.58  ? 46   HIS Q NE2 1 
ATOM   17907 N  N   . VAL Q  1 47  ? 33.740  137.804 104.122 1.00 10.98 ? 47   VAL Q N   1 
ATOM   17908 C  CA  . VAL Q  1 47  ? 33.763  136.414 103.678 1.00 11.00 ? 47   VAL Q CA  1 
ATOM   17909 C  C   . VAL Q  1 47  ? 33.998  136.427 102.174 1.00 11.65 ? 47   VAL Q C   1 
ATOM   17910 O  O   . VAL Q  1 47  ? 33.236  137.061 101.416 1.00 11.54 ? 47   VAL Q O   1 
ATOM   17911 C  CB  . VAL Q  1 47  ? 32.430  135.747 103.892 1.00 12.56 ? 47   VAL Q CB  1 
ATOM   17912 C  CG1 . VAL Q  1 47  ? 32.462  134.313 103.340 1.00 11.04 ? 47   VAL Q CG1 1 
ATOM   17913 C  CG2 . VAL Q  1 47  ? 32.045  135.780 105.380 1.00 11.43 ? 47   VAL Q CG2 1 
ATOM   17914 N  N   . HIS Q  1 48  ? 35.034  135.715 101.752 1.00 12.21 ? 48   HIS Q N   1 
ATOM   17915 C  CA  . HIS Q  1 48  ? 35.427  135.601 100.356 1.00 11.86 ? 48   HIS Q CA  1 
ATOM   17916 C  C   . HIS Q  1 48  ? 34.911  134.278 99.823  1.00 13.13 ? 48   HIS Q C   1 
ATOM   17917 O  O   . HIS Q  1 48  ? 34.562  133.376 100.592 1.00 12.58 ? 48   HIS Q O   1 
ATOM   17918 C  CB  . HIS Q  1 48  ? 36.947  135.740 100.178 1.00 11.99 ? 48   HIS Q CB  1 
ATOM   17919 C  CG  . HIS Q  1 48  ? 37.418  137.146 100.344 1.00 9.72  ? 48   HIS Q CG  1 
ATOM   17920 N  ND1 . HIS Q  1 48  ? 38.096  137.843 99.365  1.00 11.46 ? 48   HIS Q ND1 1 
ATOM   17921 C  CD2 . HIS Q  1 48  ? 37.246  138.010 101.372 1.00 9.71  ? 48   HIS Q CD2 1 
ATOM   17922 C  CE1 . HIS Q  1 48  ? 38.353  139.068 99.806  1.00 9.69  ? 48   HIS Q CE1 1 
ATOM   17923 N  NE2 . HIS Q  1 48  ? 37.822  139.194 101.006 1.00 10.40 ? 48   HIS Q NE2 1 
ATOM   17924 N  N   . GLU Q  1 49  ? 34.843  134.185 98.506  1.00 13.31 ? 49   GLU Q N   1 
ATOM   17925 C  CA  . GLU Q  1 49  ? 34.093  133.086 97.880  1.00 15.08 ? 49   GLU Q CA  1 
ATOM   17926 C  C   . GLU Q  1 49  ? 34.619  131.679 98.088  1.00 15.08 ? 49   GLU Q C   1 
ATOM   17927 O  O   . GLU Q  1 49  ? 33.848  130.752 98.309  1.00 15.64 ? 49   GLU Q O   1 
ATOM   17928 C  CB  . GLU Q  1 49  ? 33.936  133.355 96.381  1.00 15.13 ? 49   GLU Q CB  1 
ATOM   17929 C  CG  . GLU Q  1 49  ? 32.978  132.403 95.672  1.00 16.91 ? 49   GLU Q CG  1 
ATOM   17930 C  CD  . GLU Q  1 49  ? 32.825  132.739 94.198  1.00 19.40 ? 49   GLU Q CD  1 
ATOM   17931 O  OE1 . GLU Q  1 49  ? 33.444  133.736 93.763  1.00 18.42 ? 49   GLU Q OE1 1 
ATOM   17932 O  OE2 . GLU Q  1 49  ? 32.119  131.986 93.478  1.00 15.76 ? 49   GLU Q OE2 1 
ATOM   17933 N  N   . PHE Q  1 50  ? 35.925  131.498 97.983  1.00 15.50 ? 50   PHE Q N   1 
ATOM   17934 C  CA  . PHE Q  1 50  ? 36.461  130.135 97.991  1.00 15.41 ? 50   PHE Q CA  1 
ATOM   17935 C  C   . PHE Q  1 50  ? 37.229  129.845 99.268  1.00 15.37 ? 50   PHE Q C   1 
ATOM   17936 O  O   . PHE Q  1 50  ? 37.958  130.718 99.767  1.00 14.90 ? 50   PHE Q O   1 
ATOM   17937 C  CB  . PHE Q  1 50  ? 37.389  129.933 96.802  1.00 15.58 ? 50   PHE Q CB  1 
ATOM   17938 C  CG  . PHE Q  1 50  ? 36.782  130.314 95.510  1.00 17.44 ? 50   PHE Q CG  1 
ATOM   17939 C  CD1 . PHE Q  1 50  ? 35.622  129.709 95.077  1.00 19.62 ? 50   PHE Q CD1 1 
ATOM   17940 C  CD2 . PHE Q  1 50  ? 37.353  131.300 94.737  1.00 19.40 ? 50   PHE Q CD2 1 
ATOM   17941 C  CE1 . PHE Q  1 50  ? 35.049  130.073 93.883  1.00 20.01 ? 50   PHE Q CE1 1 
ATOM   17942 C  CE2 . PHE Q  1 50  ? 36.779  131.681 93.551  1.00 20.55 ? 50   PHE Q CE2 1 
ATOM   17943 C  CZ  . PHE Q  1 50  ? 35.623  131.061 93.126  1.00 20.36 ? 50   PHE Q CZ  1 
ATOM   17944 N  N   . GLY Q  1 51  ? 37.034  128.637 99.798  1.00 14.84 ? 51   GLY Q N   1 
ATOM   17945 C  CA  . GLY Q  1 51  ? 37.763  128.140 100.956 1.00 15.82 ? 51   GLY Q CA  1 
ATOM   17946 C  C   . GLY Q  1 51  ? 39.066  127.507 100.504 1.00 16.95 ? 51   GLY Q C   1 
ATOM   17947 O  O   . GLY Q  1 51  ? 39.417  126.382 100.892 1.00 17.16 ? 51   GLY Q O   1 
ATOM   17948 N  N   . ASP Q  1 52  ? 39.809  128.257 99.694  1.00 16.77 ? 52   ASP Q N   1 
ATOM   17949 C  CA  . ASP Q  1 52  ? 40.997  127.742 99.004  1.00 16.11 ? 52   ASP Q CA  1 
ATOM   17950 C  C   . ASP Q  1 52  ? 42.242  128.521 99.441  1.00 15.90 ? 52   ASP Q C   1 
ATOM   17951 O  O   . ASP Q  1 52  ? 42.427  129.679 99.051  1.00 14.94 ? 52   ASP Q O   1 
ATOM   17952 C  CB  . ASP Q  1 52  ? 40.771  127.896 97.491  1.00 16.34 ? 52   ASP Q CB  1 
ATOM   17953 C  CG  . ASP Q  1 52  ? 41.926  127.366 96.643  1.00 16.94 ? 52   ASP Q CG  1 
ATOM   17954 O  OD1 . ASP Q  1 52  ? 43.042  127.195 97.186  1.00 13.89 ? 52   ASP Q OD1 1 
ATOM   17955 O  OD2 . ASP Q  1 52  ? 41.790  127.088 95.418  1.00 15.86 ? 52   ASP Q OD2 1 
ATOM   17956 N  N   . ASN Q  1 53  ? 43.085  127.886 100.241 1.00 15.78 ? 53   ASN Q N   1 
ATOM   17957 C  CA  . ASN Q  1 53  ? 44.313  128.513 100.738 1.00 16.84 ? 53   ASN Q CA  1 
ATOM   17958 C  C   . ASN Q  1 53  ? 45.564  128.036 100.001 1.00 16.33 ? 53   ASN Q C   1 
ATOM   17959 O  O   . ASN Q  1 53  ? 46.659  128.165 100.530 1.00 15.80 ? 53   ASN Q O   1 
ATOM   17960 C  CB  . ASN Q  1 53  ? 44.478  128.203 102.244 1.00 17.47 ? 53   ASN Q CB  1 
ATOM   17961 C  CG  . ASN Q  1 53  ? 45.368  129.223 102.977 1.00 20.30 ? 53   ASN Q CG  1 
ATOM   17962 O  OD1 . ASN Q  1 53  ? 46.212  128.862 103.819 1.00 22.90 ? 53   ASN Q OD1 1 
ATOM   17963 N  ND2 . ASN Q  1 53  ? 45.177  130.489 102.667 1.00 21.96 ? 53   ASN Q ND2 1 
ATOM   17964 N  N   . THR Q  1 54  ? 45.409  127.464 98.806  1.00 15.60 ? 54   THR Q N   1 
ATOM   17965 C  CA  . THR Q  1 54  ? 46.550  126.870 98.118  1.00 16.15 ? 54   THR Q CA  1 
ATOM   17966 C  C   . THR Q  1 54  ? 47.583  127.918 97.762  1.00 17.13 ? 54   THR Q C   1 
ATOM   17967 O  O   . THR Q  1 54  ? 48.773  127.627 97.669  1.00 16.62 ? 54   THR Q O   1 
ATOM   17968 C  CB  . THR Q  1 54  ? 46.114  126.096 96.854  1.00 16.69 ? 54   THR Q CB  1 
ATOM   17969 O  OG1 . THR Q  1 54  ? 45.455  126.992 95.950  1.00 15.31 ? 54   THR Q OG1 1 
ATOM   17970 C  CG2 . THR Q  1 54  ? 45.034  125.057 97.199  1.00 14.47 ? 54   THR Q CG2 1 
ATOM   17971 N  N   . ALA Q  1 55  ? 47.108  129.140 97.545  1.00 17.01 ? 55   ALA Q N   1 
ATOM   17972 C  CA  . ALA Q  1 55  ? 47.972  130.275 97.226  1.00 17.83 ? 55   ALA Q CA  1 
ATOM   17973 C  C   . ALA Q  1 55  ? 47.829  131.318 98.321  1.00 18.29 ? 55   ALA Q C   1 
ATOM   17974 O  O   . ALA Q  1 55  ? 47.828  132.529 98.061  1.00 18.30 ? 55   ALA Q O   1 
ATOM   17975 C  CB  . ALA Q  1 55  ? 47.570  130.874 95.885  1.00 18.26 ? 55   ALA Q CB  1 
ATOM   17976 N  N   . GLY Q  1 56  ? 47.666  130.862 99.554  1.00 17.52 ? 56   GLY Q N   1 
ATOM   17977 C  CA  . GLY Q  1 56  ? 47.508  131.812 100.633 1.00 17.69 ? 56   GLY Q CA  1 
ATOM   17978 C  C   . GLY Q  1 56  ? 46.153  132.495 100.521 1.00 17.78 ? 56   GLY Q C   1 
ATOM   17979 O  O   . GLY Q  1 56  ? 45.201  131.943 99.939  1.00 17.13 ? 56   GLY Q O   1 
ATOM   17980 N  N   . CYS Q  1 57  ? 46.062  133.717 101.030 1.00 16.79 ? 57   CYS Q N   1 
ATOM   17981 C  CA  . CYS Q  1 57  ? 44.780  134.400 100.998 1.00 17.40 ? 57   CYS Q CA  1 
ATOM   17982 C  C   . CYS Q  1 57  ? 44.313  134.780 99.591  1.00 16.17 ? 57   CYS Q C   1 
ATOM   17983 O  O   . CYS Q  1 57  ? 43.137  135.024 99.370  1.00 15.22 ? 57   CYS Q O   1 
ATOM   17984 C  CB  . CYS Q  1 57  ? 44.788  135.613 101.957 1.00 17.02 ? 57   CYS Q CB  1 
ATOM   17985 S  SG  . CYS Q  1 57  ? 44.988  135.090 103.671 1.00 22.51 ? 57   CYS Q SG  1 
ATOM   17986 N  N   . THR Q  1 58  ? 45.234  134.803 98.638  1.00 15.53 ? 58   THR Q N   1 
ATOM   17987 C  CA  . THR Q  1 58  ? 44.902  135.205 97.278  1.00 16.01 ? 58   THR Q CA  1 
ATOM   17988 C  C   . THR Q  1 58  ? 43.912  134.252 96.636  1.00 16.13 ? 58   THR Q C   1 
ATOM   17989 O  O   . THR Q  1 58  ? 42.977  134.667 95.930  1.00 15.10 ? 58   THR Q O   1 
ATOM   17990 C  CB  . THR Q  1 58  ? 46.192  135.242 96.471  1.00 17.24 ? 58   THR Q CB  1 
ATOM   17991 O  OG1 . THR Q  1 58  ? 47.058  136.230 97.045  1.00 18.10 ? 58   THR Q OG1 1 
ATOM   17992 C  CG2 . THR Q  1 58  ? 45.953  135.732 95.022  1.00 17.72 ? 58   THR Q CG2 1 
ATOM   17993 N  N   . SER Q  1 59  ? 44.100  132.956 96.884  1.00 14.82 ? 59   SER Q N   1 
ATOM   17994 C  CA  . SER Q  1 59  ? 43.225  131.989 96.240  1.00 14.92 ? 59   SER Q CA  1 
ATOM   17995 C  C   . SER Q  1 59  ? 41.781  132.000 96.750  1.00 14.06 ? 59   SER Q C   1 
ATOM   17996 O  O   . SER Q  1 59  ? 40.933  131.316 96.187  1.00 13.28 ? 59   SER Q O   1 
ATOM   17997 C  CB  . SER Q  1 59  ? 43.843  130.562 96.263  1.00 15.47 ? 59   SER Q CB  1 
ATOM   17998 O  OG  . SER Q  1 59  ? 44.611  130.340 97.436  1.00 16.67 ? 59   SER Q OG  1 
ATOM   17999 N  N   . ALA Q  1 60  ? 41.477  132.766 97.802  1.00 13.67 ? 60   ALA Q N   1 
ATOM   18000 C  CA  . ALA Q  1 60  ? 40.077  132.821 98.277  1.00 14.25 ? 60   ALA Q CA  1 
ATOM   18001 C  C   . ALA Q  1 60  ? 39.169  133.522 97.285  1.00 13.95 ? 60   ALA Q C   1 
ATOM   18002 O  O   . ALA Q  1 60  ? 37.931  133.464 97.400  1.00 14.37 ? 60   ALA Q O   1 
ATOM   18003 C  CB  . ALA Q  1 60  ? 39.968  133.497 99.662  1.00 13.50 ? 60   ALA Q CB  1 
ATOM   18004 N  N   . GLY Q  1 61  ? 39.764  134.197 96.305  1.00 13.81 ? 61   GLY Q N   1 
ATOM   18005 C  CA  . GLY Q  1 61  ? 38.942  134.845 95.287  1.00 13.50 ? 61   GLY Q CA  1 
ATOM   18006 C  C   . GLY Q  1 61  ? 38.283  136.115 95.814  1.00 12.62 ? 61   GLY Q C   1 
ATOM   18007 O  O   . GLY Q  1 61  ? 38.743  136.706 96.791  1.00 13.45 ? 61   GLY Q O   1 
ATOM   18008 N  N   . PRO Q  1 62  ? 37.233  136.580 95.150  1.00 13.08 ? 62   PRO Q N   1 
ATOM   18009 C  CA  . PRO Q  1 62  ? 36.593  137.842 95.549  1.00 13.10 ? 62   PRO Q CA  1 
ATOM   18010 C  C   . PRO Q  1 62  ? 35.573  137.631 96.641  1.00 13.10 ? 62   PRO Q C   1 
ATOM   18011 O  O   . PRO Q  1 62  ? 35.438  136.550 97.187  1.00 12.64 ? 62   PRO Q O   1 
ATOM   18012 C  CB  . PRO Q  1 62  ? 35.839  138.295 94.276  1.00 13.71 ? 62   PRO Q CB  1 
ATOM   18013 C  CG  . PRO Q  1 62  ? 35.635  137.009 93.455  1.00 13.73 ? 62   PRO Q CG  1 
ATOM   18014 C  CD  . PRO Q  1 62  ? 36.563  135.939 94.000  1.00 12.43 ? 62   PRO Q CD  1 
ATOM   18015 N  N   . HIS Q  1 63  ? 34.835  138.683 96.954  1.00 13.10 ? 63   HIS Q N   1 
ATOM   18016 C  CA  . HIS Q  1 63  ? 33.835  138.578 97.991  1.00 13.78 ? 63   HIS Q CA  1 
ATOM   18017 C  C   . HIS Q  1 63  ? 32.752  137.604 97.603  1.00 14.52 ? 63   HIS Q C   1 
ATOM   18018 O  O   . HIS Q  1 63  ? 32.376  137.505 96.437  1.00 14.12 ? 63   HIS Q O   1 
ATOM   18019 C  CB  . HIS Q  1 63  ? 33.216  139.963 98.309  1.00 13.68 ? 63   HIS Q CB  1 
ATOM   18020 C  CG  . HIS Q  1 63  ? 34.193  140.919 98.928  1.00 14.05 ? 63   HIS Q CG  1 
ATOM   18021 N  ND1 . HIS Q  1 63  ? 33.852  142.196 99.320  1.00 13.91 ? 63   HIS Q ND1 1 
ATOM   18022 C  CD2 . HIS Q  1 63  ? 35.512  140.773 99.226  1.00 14.73 ? 63   HIS Q CD2 1 
ATOM   18023 C  CE1 . HIS Q  1 63  ? 34.920  142.799 99.818  1.00 14.06 ? 63   HIS Q CE1 1 
ATOM   18024 N  NE2 . HIS Q  1 63  ? 35.944  141.965 99.749  1.00 17.01 ? 63   HIS Q NE2 1 
ATOM   18025 N  N   . PHE Q  1 64  ? 32.245  136.893 98.598  1.00 14.73 ? 64   PHE Q N   1 
ATOM   18026 C  CA  . PHE Q  1 64  ? 31.129  136.010 98.383  1.00 15.69 ? 64   PHE Q CA  1 
ATOM   18027 C  C   . PHE Q  1 64  ? 29.939  136.886 97.947  1.00 15.99 ? 64   PHE Q C   1 
ATOM   18028 O  O   . PHE Q  1 64  ? 29.483  137.729 98.719  1.00 14.72 ? 64   PHE Q O   1 
ATOM   18029 C  CB  . PHE Q  1 64  ? 30.810  135.269 99.661  1.00 15.72 ? 64   PHE Q CB  1 
ATOM   18030 C  CG  . PHE Q  1 64  ? 29.727  134.267 99.505  1.00 16.83 ? 64   PHE Q CG  1 
ATOM   18031 C  CD1 . PHE Q  1 64  ? 29.593  133.562 98.314  1.00 17.19 ? 64   PHE Q CD1 1 
ATOM   18032 C  CD2 . PHE Q  1 64  ? 28.838  134.015 100.535 1.00 17.24 ? 64   PHE Q CD2 1 
ATOM   18033 C  CE1 . PHE Q  1 64  ? 28.589  132.626 98.152  1.00 18.30 ? 64   PHE Q CE1 1 
ATOM   18034 C  CE2 . PHE Q  1 64  ? 27.822  133.078 100.377 1.00 17.70 ? 64   PHE Q CE2 1 
ATOM   18035 C  CZ  . PHE Q  1 64  ? 27.698  132.382 99.182  1.00 17.53 ? 64   PHE Q CZ  1 
ATOM   18036 N  N   . ASN Q  1 65  ? 29.462  136.672 96.715  1.00 15.88 ? 65   ASN Q N   1 
ATOM   18037 C  CA  . ASN Q  1 65  ? 28.479  137.546 96.073  1.00 16.99 ? 65   ASN Q CA  1 
ATOM   18038 C  C   . ASN Q  1 65  ? 27.519  136.751 95.170  1.00 18.20 ? 65   ASN Q C   1 
ATOM   18039 O  O   . ASN Q  1 65  ? 27.504  136.957 93.957  1.00 18.92 ? 65   ASN Q O   1 
ATOM   18040 C  CB  . ASN Q  1 65  ? 29.244  138.549 95.210  1.00 16.58 ? 65   ASN Q CB  1 
ATOM   18041 C  CG  . ASN Q  1 65  ? 28.368  139.675 94.660  1.00 16.14 ? 65   ASN Q CG  1 
ATOM   18042 O  OD1 . ASN Q  1 65  ? 27.312  139.984 95.201  1.00 16.99 ? 65   ASN Q OD1 1 
ATOM   18043 N  ND2 . ASN Q  1 65  ? 28.836  140.312 93.591  1.00 15.38 ? 65   ASN Q ND2 1 
ATOM   18044 N  N   . PRO Q  1 66  ? 26.737  135.851 95.757  1.00 18.38 ? 66   PRO Q N   1 
ATOM   18045 C  CA  . PRO Q  1 66  ? 25.798  135.003 95.005  1.00 19.51 ? 66   PRO Q CA  1 
ATOM   18046 C  C   . PRO Q  1 66  ? 24.624  135.751 94.360  1.00 19.84 ? 66   PRO Q C   1 
ATOM   18047 O  O   . PRO Q  1 66  ? 23.947  135.150 93.524  1.00 20.82 ? 66   PRO Q O   1 
ATOM   18048 C  CB  . PRO Q  1 66  ? 25.270  134.045 96.078  1.00 19.28 ? 66   PRO Q CB  1 
ATOM   18049 C  CG  . PRO Q  1 66  ? 25.387  134.855 97.331  1.00 19.32 ? 66   PRO Q CG  1 
ATOM   18050 C  CD  . PRO Q  1 66  ? 26.729  135.530 97.195  1.00 18.84 ? 66   PRO Q CD  1 
ATOM   18051 N  N   . LEU Q  1 67  ? 24.387  137.006 94.734  1.00 20.22 ? 67   LEU Q N   1 
ATOM   18052 C  CA  . LEU Q  1 67  ? 23.304  137.794 94.130  1.00 20.44 ? 67   LEU Q CA  1 
ATOM   18053 C  C   . LEU Q  1 67  ? 23.842  138.805 93.125  1.00 20.27 ? 67   LEU Q C   1 
ATOM   18054 O  O   . LEU Q  1 67  ? 23.086  139.590 92.550  1.00 20.68 ? 67   LEU Q O   1 
ATOM   18055 C  CB  . LEU Q  1 67  ? 22.444  138.473 95.204  1.00 20.73 ? 67   LEU Q CB  1 
ATOM   18056 C  CG  . LEU Q  1 67  ? 21.984  137.474 96.276  1.00 21.65 ? 67   LEU Q CG  1 
ATOM   18057 C  CD1 . LEU Q  1 67  ? 20.969  138.074 97.225  1.00 22.63 ? 67   LEU Q CD1 1 
ATOM   18058 C  CD2 . LEU Q  1 67  ? 21.402  136.236 95.614  1.00 22.49 ? 67   LEU Q CD2 1 
ATOM   18059 N  N   . SER Q  1 68  ? 25.155  138.785 92.918  1.00 19.96 ? 68   SER Q N   1 
ATOM   18060 C  CA  . SER Q  1 68  ? 25.794  139.653 91.933  1.00 19.37 ? 68   SER Q CA  1 
ATOM   18061 C  C   . SER Q  1 68  ? 25.490  141.117 92.188  1.00 19.17 ? 68   SER Q C   1 
ATOM   18062 O  O   . SER Q  1 68  ? 25.108  141.835 91.264  1.00 19.42 ? 68   SER Q O   1 
ATOM   18063 C  CB  . SER Q  1 68  ? 25.330  139.299 90.515  1.00 19.70 ? 68   SER Q CB  1 
ATOM   18064 O  OG  . SER Q  1 68  ? 25.780  138.023 90.109  1.00 18.73 ? 68   SER Q OG  1 
ATOM   18065 N  N   . ARG Q  1 69  ? 25.614  141.546 93.438  1.00 18.62 ? 69   ARG Q N   1 
ATOM   18066 C  CA  . ARG Q  1 69  ? 25.406  142.938 93.816  1.00 18.39 ? 69   ARG Q CA  1 
ATOM   18067 C  C   . ARG Q  1 69  ? 26.738  143.666 93.906  1.00 17.54 ? 69   ARG Q C   1 
ATOM   18068 O  O   . ARG Q  1 69  ? 27.801  143.040 93.795  1.00 17.36 ? 69   ARG Q O   1 
ATOM   18069 C  CB  . ARG Q  1 69  ? 24.711  143.023 95.172  1.00 19.27 ? 69   ARG Q CB  1 
ATOM   18070 C  CG  . ARG Q  1 69  ? 23.417  142.195 95.298  1.00 22.27 ? 69   ARG Q CG  1 
ATOM   18071 C  CD  . ARG Q  1 69  ? 22.113  143.003 95.290  1.00 28.36 ? 69   ARG Q CD  1 
ATOM   18072 N  NE  . ARG Q  1 69  ? 21.279  142.601 96.425  1.00 32.85 ? 69   ARG Q NE  1 
ATOM   18073 C  CZ  . ARG Q  1 69  ? 20.052  142.105 96.353  1.00 34.33 ? 69   ARG Q CZ  1 
ATOM   18074 N  NH1 . ARG Q  1 69  ? 19.446  141.953 95.183  1.00 36.25 ? 69   ARG Q NH1 1 
ATOM   18075 N  NH2 . ARG Q  1 69  ? 19.417  141.770 97.469  1.00 35.92 ? 69   ARG Q NH2 1 
ATOM   18076 N  N   . LYS Q  1 70  ? 26.681  144.985 94.108  1.00 16.73 ? 70   LYS Q N   1 
ATOM   18077 C  CA  . LYS Q  1 70  ? 27.890  145.785 94.279  1.00 16.00 ? 70   LYS Q CA  1 
ATOM   18078 C  C   . LYS Q  1 70  ? 28.309  145.752 95.751  1.00 14.79 ? 70   LYS Q C   1 
ATOM   18079 O  O   . LYS Q  1 70  ? 27.492  145.448 96.630  1.00 14.42 ? 70   LYS Q O   1 
ATOM   18080 C  CB  . LYS Q  1 70  ? 27.666  147.221 93.806  1.00 17.10 ? 70   LYS Q CB  1 
ATOM   18081 C  CG  . LYS Q  1 70  ? 27.220  147.303 92.346  1.00 20.61 ? 70   LYS Q CG  1 
ATOM   18082 C  CD  . LYS Q  1 70  ? 27.158  148.736 91.845  1.00 26.94 ? 70   LYS Q CD  1 
ATOM   18083 C  CE  . LYS Q  1 70  ? 26.070  149.565 92.547  1.00 30.65 ? 70   LYS Q CE  1 
ATOM   18084 N  NZ  . LYS Q  1 70  ? 26.457  151.015 92.698  1.00 32.62 ? 70   LYS Q NZ  1 
ATOM   18085 N  N   . HIS Q  1 71  ? 29.577  146.056 96.019  1.00 12.74 ? 71   HIS Q N   1 
ATOM   18086 C  CA  . HIS Q  1 71  ? 30.081  146.072 97.388  1.00 12.20 ? 71   HIS Q CA  1 
ATOM   18087 C  C   . HIS Q  1 71  ? 29.414  147.173 98.231  1.00 11.89 ? 71   HIS Q C   1 
ATOM   18088 O  O   . HIS Q  1 71  ? 29.160  148.306 97.745  1.00 12.36 ? 71   HIS Q O   1 
ATOM   18089 C  CB  . HIS Q  1 71  ? 31.604  146.266 97.371  1.00 10.42 ? 71   HIS Q CB  1 
ATOM   18090 C  CG  . HIS Q  1 71  ? 32.229  146.281 98.725  1.00 10.16 ? 71   HIS Q CG  1 
ATOM   18091 N  ND1 . HIS Q  1 71  ? 32.487  145.133 99.442  1.00 8.58  ? 71   HIS Q ND1 1 
ATOM   18092 C  CD2 . HIS Q  1 71  ? 32.648  147.316 99.497  1.00 7.58  ? 71   HIS Q CD2 1 
ATOM   18093 C  CE1 . HIS Q  1 71  ? 33.039  145.459 100.598 1.00 11.11 ? 71   HIS Q CE1 1 
ATOM   18094 N  NE2 . HIS Q  1 71  ? 33.136  146.775 100.662 1.00 8.25  ? 71   HIS Q NE2 1 
ATOM   18095 N  N   . GLY Q  1 72  ? 29.164  146.844 99.499  1.00 11.65 ? 72   GLY Q N   1 
ATOM   18096 C  CA  . GLY Q  1 72  ? 28.603  147.788 100.458 1.00 12.62 ? 72   GLY Q CA  1 
ATOM   18097 C  C   . GLY Q  1 72  ? 28.996  147.481 101.900 1.00 13.29 ? 72   GLY Q C   1 
ATOM   18098 O  O   . GLY Q  1 72  ? 29.835  146.615 102.152 1.00 11.57 ? 72   GLY Q O   1 
ATOM   18099 N  N   . GLY Q  1 73  ? 28.397  148.213 102.845 1.00 13.35 ? 73   GLY Q N   1 
ATOM   18100 C  CA  . GLY Q  1 73  ? 28.609  147.952 104.255 1.00 12.66 ? 73   GLY Q CA  1 
ATOM   18101 C  C   . GLY Q  1 73  ? 27.508  146.989 104.681 1.00 12.63 ? 73   GLY Q C   1 
ATOM   18102 O  O   . GLY Q  1 73  ? 26.571  146.768 103.942 1.00 13.01 ? 73   GLY Q O   1 
ATOM   18103 N  N   . PRO Q  1 74  ? 27.640  146.380 105.848 1.00 11.79 ? 74   PRO Q N   1 
ATOM   18104 C  CA  . PRO Q  1 74  ? 26.674  145.368 106.296 1.00 12.38 ? 74   PRO Q CA  1 
ATOM   18105 C  C   . PRO Q  1 74  ? 25.247  145.906 106.367 1.00 14.07 ? 74   PRO Q C   1 
ATOM   18106 O  O   . PRO Q  1 74  ? 24.312  145.146 106.140 1.00 13.68 ? 74   PRO Q O   1 
ATOM   18107 C  CB  . PRO Q  1 74  ? 27.145  145.002 107.709 1.00 12.38 ? 74   PRO Q CB  1 
ATOM   18108 C  CG  . PRO Q  1 74  ? 28.318  145.849 108.034 1.00 12.16 ? 74   PRO Q CG  1 
ATOM   18109 C  CD  . PRO Q  1 74  ? 28.737  146.605 106.799 1.00 11.81 ? 74   PRO Q CD  1 
ATOM   18110 N  N   . LYS Q  1 75  ? 25.087  147.185 106.677 1.00 15.39 ? 75   LYS Q N   1 
ATOM   18111 C  CA  . LYS Q  1 75  ? 23.739  147.734 106.874 1.00 18.08 ? 75   LYS Q CA  1 
ATOM   18112 C  C   . LYS Q  1 75  ? 23.124  148.145 105.579 1.00 18.47 ? 75   LYS Q C   1 
ATOM   18113 O  O   . LYS Q  1 75  ? 21.979  148.574 105.555 1.00 18.39 ? 75   LYS Q O   1 
ATOM   18114 C  CB  . LYS Q  1 75  ? 23.780  148.926 107.821 1.00 19.17 ? 75   LYS Q CB  1 
ATOM   18115 C  CG  . LYS Q  1 75  ? 24.353  148.581 109.181 1.00 22.53 ? 75   LYS Q CG  1 
ATOM   18116 C  CD  . LYS Q  1 75  ? 23.396  147.694 109.950 1.00 29.92 ? 75   LYS Q CD  1 
ATOM   18117 C  CE  . LYS Q  1 75  ? 24.136  146.809 110.958 1.00 34.67 ? 75   LYS Q CE  1 
ATOM   18118 N  NZ  . LYS Q  1 75  ? 25.370  147.472 111.507 1.00 36.84 ? 75   LYS Q NZ  1 
ATOM   18119 N  N   . ASP Q  1 76  ? 23.878  148.038 104.492 1.00 18.58 ? 76   ASP Q N   1 
ATOM   18120 C  CA  . ASP Q  1 76  ? 23.331  148.396 103.193 1.00 20.54 ? 76   ASP Q CA  1 
ATOM   18121 C  C   . ASP Q  1 76  ? 22.534  147.260 102.593 1.00 21.04 ? 76   ASP Q C   1 
ATOM   18122 O  O   . ASP Q  1 76  ? 22.870  146.090 102.775 1.00 21.28 ? 76   ASP Q O   1 
ATOM   18123 C  CB  . ASP Q  1 76  ? 24.437  148.777 102.212 1.00 20.71 ? 76   ASP Q CB  1 
ATOM   18124 C  CG  . ASP Q  1 76  ? 25.139  150.020 102.617 1.00 21.55 ? 76   ASP Q CG  1 
ATOM   18125 O  OD1 . ASP Q  1 76  ? 24.428  150.924 103.122 1.00 23.09 ? 76   ASP Q OD1 1 
ATOM   18126 O  OD2 . ASP Q  1 76  ? 26.378  150.186 102.478 1.00 21.41 ? 76   ASP Q OD2 1 
ATOM   18127 N  N   . GLU Q  1 77  ? 21.496  147.628 101.843 1.00 21.95 ? 77   GLU Q N   1 
ATOM   18128 C  CA  . GLU Q  1 77  ? 20.736  146.643 101.111 1.00 22.44 ? 77   GLU Q CA  1 
ATOM   18129 C  C   . GLU Q  1 77  ? 21.546  146.282 99.875  1.00 21.45 ? 77   GLU Q C   1 
ATOM   18130 O  O   . GLU Q  1 77  ? 21.563  145.135 99.468  1.00 22.47 ? 77   GLU Q O   1 
ATOM   18131 C  CB  . GLU Q  1 77  ? 19.344  147.153 100.764 1.00 23.86 ? 77   GLU Q CB  1 
ATOM   18132 C  CG  . GLU Q  1 77  ? 18.498  146.150 100.000 1.00 27.37 ? 77   GLU Q CG  1 
ATOM   18133 C  CD  . GLU Q  1 77  ? 18.228  146.595 98.569  1.00 31.72 ? 77   GLU Q CD  1 
ATOM   18134 O  OE1 . GLU Q  1 77  ? 17.083  147.071 98.289  1.00 32.80 ? 77   GLU Q OE1 1 
ATOM   18135 O  OE2 . GLU Q  1 77  ? 19.159  146.472 97.730  1.00 31.46 ? 77   GLU Q OE2 1 
ATOM   18136 N  N   . GLU Q  1 78  ? 22.265  147.241 99.303  1.00 19.76 ? 78   GLU Q N   1 
ATOM   18137 C  CA  . GLU Q  1 78  ? 23.171  146.892 98.219  1.00 18.25 ? 78   GLU Q CA  1 
ATOM   18138 C  C   . GLU Q  1 78  ? 24.511  146.459 98.827  1.00 16.89 ? 78   GLU Q C   1 
ATOM   18139 O  O   . GLU Q  1 78  ? 25.341  147.294 99.207  1.00 16.01 ? 78   GLU Q O   1 
ATOM   18140 C  CB  . GLU Q  1 78  ? 23.350  148.056 97.232  1.00 18.44 ? 78   GLU Q CB  1 
ATOM   18141 C  CG  . GLU Q  1 78  ? 24.161  147.726 95.978  1.00 20.34 ? 78   GLU Q CG  1 
ATOM   18142 C  CD  . GLU Q  1 78  ? 23.460  146.764 95.021  1.00 23.72 ? 78   GLU Q CD  1 
ATOM   18143 O  OE1 . GLU Q  1 78  ? 22.262  146.464 95.247  1.00 26.12 ? 78   GLU Q OE1 1 
ATOM   18144 O  OE2 . GLU Q  1 78  ? 24.101  146.310 94.037  1.00 21.86 ? 78   GLU Q OE2 1 
ATOM   18145 N  N   . ARG Q  1 79  ? 24.714  145.152 98.935  1.00 16.60 ? 79   ARG Q N   1 
ATOM   18146 C  CA  . ARG Q  1 79  ? 25.957  144.618 99.499  1.00 15.95 ? 79   ARG Q CA  1 
ATOM   18147 C  C   . ARG Q  1 79  ? 26.208  143.200 98.996  1.00 15.78 ? 79   ARG Q C   1 
ATOM   18148 O  O   . ARG Q  1 79  ? 25.290  142.536 98.504  1.00 16.43 ? 79   ARG Q O   1 
ATOM   18149 C  CB  . ARG Q  1 79  ? 25.889  144.642 101.040 1.00 16.52 ? 79   ARG Q CB  1 
ATOM   18150 C  CG  . ARG Q  1 79  ? 24.997  143.572 101.669 1.00 14.77 ? 79   ARG Q CG  1 
ATOM   18151 C  CD  . ARG Q  1 79  ? 25.772  142.501 102.488 1.00 22.11 ? 79   ARG Q CD  1 
ATOM   18152 N  NE  . ARG Q  1 79  ? 25.364  142.699 103.855 1.00 20.96 ? 79   ARG Q NE  1 
ATOM   18153 C  CZ  . ARG Q  1 79  ? 25.615  141.947 104.887 1.00 14.41 ? 79   ARG Q CZ  1 
ATOM   18154 N  NH1 . ARG Q  1 79  ? 26.355  140.816 104.823 1.00 11.34 ? 79   ARG Q NH1 1 
ATOM   18155 N  NH2 . ARG Q  1 79  ? 25.064  142.356 106.027 1.00 14.22 ? 79   ARG Q NH2 1 
ATOM   18156 N  N   . HIS Q  1 80  ? 27.456  142.757 99.077  1.00 15.26 ? 80   HIS Q N   1 
ATOM   18157 C  CA  . HIS Q  1 80  ? 27.809  141.361 98.821  1.00 13.55 ? 80   HIS Q CA  1 
ATOM   18158 C  C   . HIS Q  1 80  ? 27.379  140.594 100.040 1.00 12.84 ? 80   HIS Q C   1 
ATOM   18159 O  O   . HIS Q  1 80  ? 27.403  141.137 101.136 1.00 11.85 ? 80   HIS Q O   1 
ATOM   18160 C  CB  . HIS Q  1 80  ? 29.321  141.237 98.709  1.00 13.25 ? 80   HIS Q CB  1 
ATOM   18161 C  CG  . HIS Q  1 80  ? 29.874  141.938 97.517  1.00 12.81 ? 80   HIS Q CG  1 
ATOM   18162 N  ND1 . HIS Q  1 80  ? 31.120  142.515 97.501  1.00 9.10  ? 80   HIS Q ND1 1 
ATOM   18163 C  CD2 . HIS Q  1 80  ? 29.323  142.186 96.303  1.00 12.35 ? 80   HIS Q CD2 1 
ATOM   18164 C  CE1 . HIS Q  1 80  ? 31.343  143.033 96.304  1.00 14.71 ? 80   HIS Q CE1 1 
ATOM   18165 N  NE2 . HIS Q  1 80  ? 30.261  142.859 95.561  1.00 13.60 ? 80   HIS Q NE2 1 
ATOM   18166 N  N   . VAL Q  1 81  ? 26.973  139.339 99.880  1.00 11.86 ? 81   VAL Q N   1 
ATOM   18167 C  CA  . VAL Q  1 81  ? 26.648  138.564 101.063 1.00 12.06 ? 81   VAL Q CA  1 
ATOM   18168 C  C   . VAL Q  1 81  ? 27.854  138.598 102.053 1.00 12.48 ? 81   VAL Q C   1 
ATOM   18169 O  O   . VAL Q  1 81  ? 27.662  138.726 103.261 1.00 12.12 ? 81   VAL Q O   1 
ATOM   18170 C  CB  . VAL Q  1 81  ? 26.224  137.107 100.707 1.00 12.41 ? 81   VAL Q CB  1 
ATOM   18171 C  CG1 . VAL Q  1 81  ? 26.237  136.141 101.939 1.00 11.03 ? 81   VAL Q CG1 1 
ATOM   18172 C  CG2 . VAL Q  1 81  ? 24.815  137.080 100.063 1.00 11.77 ? 81   VAL Q CG2 1 
ATOM   18173 N  N   . GLY Q  1 82  ? 29.082  138.524 101.537 1.00 10.94 ? 82   GLY Q N   1 
ATOM   18174 C  CA  . GLY Q  1 82  ? 30.250  138.514 102.405 1.00 12.03 ? 82   GLY Q CA  1 
ATOM   18175 C  C   . GLY Q  1 82  ? 30.632  139.829 103.077 1.00 11.91 ? 82   GLY Q C   1 
ATOM   18176 O  O   . GLY Q  1 82  ? 31.635  139.895 103.795 1.00 11.32 ? 82   GLY Q O   1 
ATOM   18177 N  N   . ASP Q  1 83  ? 29.855  140.887 102.871 1.00 12.47 ? 83   ASP Q N   1 
ATOM   18178 C  CA  . ASP Q  1 83  ? 30.283  142.210 103.360 1.00 12.32 ? 83   ASP Q CA  1 
ATOM   18179 C  C   . ASP Q  1 83  ? 29.958  142.446 104.830 1.00 12.60 ? 83   ASP Q C   1 
ATOM   18180 O  O   . ASP Q  1 83  ? 28.855  142.892 105.157 1.00 13.97 ? 83   ASP Q O   1 
ATOM   18181 C  CB  . ASP Q  1 83  ? 29.666  143.336 102.497 1.00 13.10 ? 83   ASP Q CB  1 
ATOM   18182 C  CG  . ASP Q  1 83  ? 30.222  143.371 101.082 1.00 13.06 ? 83   ASP Q CG  1 
ATOM   18183 O  OD1 . ASP Q  1 83  ? 31.272  142.735 100.823 1.00 9.16  ? 83   ASP Q OD1 1 
ATOM   18184 O  OD2 . ASP Q  1 83  ? 29.688  144.033 100.160 1.00 13.09 ? 83   ASP Q OD2 1 
ATOM   18185 N  N   . LEU Q  1 84  ? 30.912  142.163 105.714 1.00 12.69 ? 84   LEU Q N   1 
ATOM   18186 C  CA  . LEU Q  1 84  ? 30.698  142.365 107.138 1.00 12.99 ? 84   LEU Q CA  1 
ATOM   18187 C  C   . LEU Q  1 84  ? 31.283  143.681 107.650 1.00 12.55 ? 84   LEU Q C   1 
ATOM   18188 O  O   . LEU Q  1 84  ? 31.318  143.906 108.881 1.00 12.97 ? 84   LEU Q O   1 
ATOM   18189 C  CB  . LEU Q  1 84  ? 31.268  141.195 107.949 1.00 12.04 ? 84   LEU Q CB  1 
ATOM   18190 C  CG  . LEU Q  1 84  ? 30.548  139.888 107.646 1.00 13.40 ? 84   LEU Q CG  1 
ATOM   18191 C  CD1 . LEU Q  1 84  ? 31.208  138.718 108.439 1.00 11.09 ? 84   LEU Q CD1 1 
ATOM   18192 C  CD2 . LEU Q  1 84  ? 29.071  140.004 107.957 1.00 16.31 ? 84   LEU Q CD2 1 
ATOM   18193 N  N   . GLY Q  1 85  ? 31.764  144.537 106.740 1.00 11.93 ? 85   GLY Q N   1 
ATOM   18194 C  CA  . GLY Q  1 85  ? 32.208  145.864 107.178 1.00 11.09 ? 85   GLY Q CA  1 
ATOM   18195 C  C   . GLY Q  1 85  ? 33.600  145.913 107.769 1.00 11.20 ? 85   GLY Q C   1 
ATOM   18196 O  O   . GLY Q  1 85  ? 34.495  145.269 107.267 1.00 11.61 ? 85   GLY Q O   1 
ATOM   18197 N  N   . ASN Q  1 86  ? 33.796  146.678 108.839 1.00 9.69  ? 86   ASN Q N   1 
ATOM   18198 C  CA  . ASN Q  1 86  ? 35.120  146.789 109.420 1.00 9.58  ? 86   ASN Q CA  1 
ATOM   18199 C  C   . ASN Q  1 86  ? 35.166  146.242 110.836 1.00 9.25  ? 86   ASN Q C   1 
ATOM   18200 O  O   . ASN Q  1 86  ? 34.161  146.220 111.494 1.00 8.92  ? 86   ASN Q O   1 
ATOM   18201 C  CB  . ASN Q  1 86  ? 35.474  148.269 109.534 1.00 9.72  ? 86   ASN Q CB  1 
ATOM   18202 C  CG  . ASN Q  1 86  ? 35.804  148.865 108.207 1.00 11.47 ? 86   ASN Q CG  1 
ATOM   18203 O  OD1 . ASN Q  1 86  ? 36.717  148.425 107.568 1.00 8.78  ? 86   ASN Q OD1 1 
ATOM   18204 N  ND2 . ASN Q  1 86  ? 35.072  149.897 107.810 1.00 11.32 ? 86   ASN Q ND2 1 
ATOM   18205 N  N   . VAL Q  1 87  ? 36.335  145.845 111.300 1.00 9.22  ? 87   VAL Q N   1 
ATOM   18206 C  CA  . VAL Q  1 87  ? 36.471  145.575 112.716 1.00 10.79 ? 87   VAL Q CA  1 
ATOM   18207 C  C   . VAL Q  1 87  ? 37.445  146.628 113.154 1.00 11.18 ? 87   VAL Q C   1 
ATOM   18208 O  O   . VAL Q  1 87  ? 38.116  147.233 112.322 1.00 12.57 ? 87   VAL Q O   1 
ATOM   18209 C  CB  . VAL Q  1 87  ? 37.013  144.193 112.974 1.00 10.67 ? 87   VAL Q CB  1 
ATOM   18210 C  CG1 . VAL Q  1 87  ? 35.933  143.182 112.571 1.00 11.32 ? 87   VAL Q CG1 1 
ATOM   18211 C  CG2 . VAL Q  1 87  ? 38.313  143.988 112.196 1.00 10.61 ? 87   VAL Q CG2 1 
ATOM   18212 N  N   . THR Q  1 88  ? 37.531  146.859 114.452 1.00 10.80 ? 88   THR Q N   1 
ATOM   18213 C  CA  . THR Q  1 88  ? 38.351  147.927 114.951 1.00 10.28 ? 88   THR Q CA  1 
ATOM   18214 C  C   . THR Q  1 88  ? 39.494  147.409 115.817 1.00 9.84  ? 88   THR Q C   1 
ATOM   18215 O  O   . THR Q  1 88  ? 39.220  146.738 116.794 1.00 9.16  ? 88   THR Q O   1 
ATOM   18216 C  CB  . THR Q  1 88  ? 37.457  148.794 115.849 1.00 10.08 ? 88   THR Q CB  1 
ATOM   18217 O  OG1 . THR Q  1 88  ? 36.496  149.526 115.057 1.00 9.41  ? 88   THR Q OG1 1 
ATOM   18218 C  CG2 . THR Q  1 88  ? 38.288  149.832 116.521 1.00 11.57 ? 88   THR Q CG2 1 
ATOM   18219 N  N   . ALA Q  1 89  ? 40.751  147.742 115.505 1.00 10.38 ? 89   ALA Q N   1 
ATOM   18220 C  CA  . ALA Q  1 89  ? 41.882  147.316 116.382 1.00 11.99 ? 89   ALA Q CA  1 
ATOM   18221 C  C   . ALA Q  1 89  ? 42.384  148.466 117.273 1.00 13.00 ? 89   ALA Q C   1 
ATOM   18222 O  O   . ALA Q  1 89  ? 42.436  149.616 116.801 1.00 13.52 ? 89   ALA Q O   1 
ATOM   18223 C  CB  . ALA Q  1 89  ? 43.014  146.833 115.561 1.00 11.92 ? 89   ALA Q CB  1 
ATOM   18224 N  N   . ASP Q  1 90  ? 42.773  148.168 118.514 1.00 15.13 ? 90   ASP Q N   1 
ATOM   18225 C  CA  . ASP Q  1 90  ? 43.293  149.212 119.445 1.00 15.56 ? 90   ASP Q CA  1 
ATOM   18226 C  C   . ASP Q  1 90  ? 44.771  149.580 119.209 1.00 15.98 ? 90   ASP Q C   1 
ATOM   18227 O  O   . ASP Q  1 90  ? 45.412  149.006 118.349 1.00 14.29 ? 90   ASP Q O   1 
ATOM   18228 C  CB  . ASP Q  1 90  ? 43.210  148.874 120.946 1.00 17.65 ? 90   ASP Q CB  1 
ATOM   18229 C  CG  . ASP Q  1 90  ? 42.245  147.755 121.297 1.00 19.89 ? 90   ASP Q CG  1 
ATOM   18230 O  OD1 . ASP Q  1 90  ? 42.715  146.629 121.696 1.00 18.50 ? 90   ASP Q OD1 1 
ATOM   18231 O  OD2 . ASP Q  1 90  ? 41.008  147.965 121.306 1.00 22.28 ? 90   ASP Q OD2 1 
ATOM   18232 N  N   . LYS Q  1 91  ? 45.323  150.509 120.017 1.00 14.86 ? 91   LYS Q N   1 
ATOM   18233 C  CA  . LYS Q  1 91  ? 46.758  150.876 119.886 1.00 16.44 ? 91   LYS Q CA  1 
ATOM   18234 C  C   . LYS Q  1 91  ? 47.602  149.635 120.106 1.00 16.70 ? 91   LYS Q C   1 
ATOM   18235 O  O   . LYS Q  1 91  ? 48.722  149.500 119.586 1.00 16.98 ? 91   LYS Q O   1 
ATOM   18236 C  CB  . LYS Q  1 91  ? 47.214  151.977 120.871 1.00 16.81 ? 91   LYS Q CB  1 
ATOM   18237 C  CG  . LYS Q  1 91  ? 48.737  151.891 121.172 1.00 17.19 ? 91   LYS Q CG  1 
ATOM   18238 C  CD  . LYS Q  1 91  ? 49.419  153.248 121.386 1.00 21.53 ? 91   LYS Q CD  1 
ATOM   18239 C  CE  . LYS Q  1 91  ? 48.806  154.035 122.532 1.00 21.75 ? 91   LYS Q CE  1 
ATOM   18240 N  NZ  . LYS Q  1 91  ? 49.571  155.295 122.887 1.00 22.96 ? 91   LYS Q NZ  1 
ATOM   18241 N  N   . ASP Q  1 92  ? 47.020  148.772 120.936 1.00 16.32 ? 92   ASP Q N   1 
ATOM   18242 C  CA  . ASP Q  1 92  ? 47.384  147.386 121.214 1.00 17.40 ? 92   ASP Q CA  1 
ATOM   18243 C  C   . ASP Q  1 92  ? 47.679  146.458 120.019 1.00 16.37 ? 92   ASP Q C   1 
ATOM   18244 O  O   . ASP Q  1 92  ? 48.289  145.385 120.168 1.00 14.90 ? 92   ASP Q O   1 
ATOM   18245 C  CB  . ASP Q  1 92  ? 46.080  146.809 121.739 1.00 18.29 ? 92   ASP Q CB  1 
ATOM   18246 C  CG  . ASP Q  1 92  ? 46.235  146.154 123.006 1.00 20.24 ? 92   ASP Q CG  1 
ATOM   18247 O  OD1 . ASP Q  1 92  ? 47.366  145.726 123.267 1.00 26.13 ? 92   ASP Q OD1 1 
ATOM   18248 O  OD2 . ASP Q  1 92  ? 45.293  146.022 123.815 1.00 25.57 ? 92   ASP Q OD2 1 
ATOM   18249 N  N   . GLY Q  1 93  ? 47.135  146.801 118.861 1.00 15.97 ? 93   GLY Q N   1 
ATOM   18250 C  CA  . GLY Q  1 93  ? 47.216  145.889 117.724 1.00 15.29 ? 93   GLY Q CA  1 
ATOM   18251 C  C   . GLY Q  1 93  ? 46.120  144.823 117.796 1.00 15.44 ? 93   GLY Q C   1 
ATOM   18252 O  O   . GLY Q  1 93  ? 46.005  143.928 116.920 1.00 14.98 ? 93   GLY Q O   1 
ATOM   18253 N  N   . VAL Q  1 94  ? 45.276  144.934 118.817 1.00 13.82 ? 94   VAL Q N   1 
ATOM   18254 C  CA  . VAL Q  1 94  ? 44.207  143.966 119.015 1.00 13.84 ? 94   VAL Q CA  1 
ATOM   18255 C  C   . VAL Q  1 94  ? 42.813  144.458 118.706 1.00 13.97 ? 94   VAL Q C   1 
ATOM   18256 O  O   . VAL Q  1 94  ? 42.402  145.542 119.145 1.00 13.48 ? 94   VAL Q O   1 
ATOM   18257 C  CB  . VAL Q  1 94  ? 44.229  143.395 120.449 1.00 14.62 ? 94   VAL Q CB  1 
ATOM   18258 C  CG1 . VAL Q  1 94  ? 43.030  142.473 120.679 1.00 15.08 ? 94   VAL Q CG1 1 
ATOM   18259 C  CG2 . VAL Q  1 94  ? 45.505  142.627 120.657 1.00 15.27 ? 94   VAL Q CG2 1 
ATOM   18260 N  N   . ALA Q  1 95  ? 42.096  143.648 117.926 1.00 13.84 ? 95   ALA Q N   1 
ATOM   18261 C  CA  . ALA Q  1 95  ? 40.725  143.929 117.552 1.00 14.56 ? 95   ALA Q CA  1 
ATOM   18262 C  C   . ALA Q  1 95  ? 39.792  142.950 118.223 1.00 14.62 ? 95   ALA Q C   1 
ATOM   18263 O  O   . ALA Q  1 95  ? 39.830  141.768 117.944 1.00 14.33 ? 95   ALA Q O   1 
ATOM   18264 C  CB  . ALA Q  1 95  ? 40.534  143.862 116.049 1.00 12.76 ? 95   ALA Q CB  1 
ATOM   18265 N  N   . ASP Q  1 96  ? 38.935  143.450 119.112 1.00 15.95 ? 96   ASP Q N   1 
ATOM   18266 C  CA  . ASP Q  1 96  ? 37.931  142.572 119.710 1.00 16.30 ? 96   ASP Q CA  1 
ATOM   18267 C  C   . ASP Q  1 96  ? 36.743  142.676 118.816 1.00 16.35 ? 96   ASP Q C   1 
ATOM   18268 O  O   . ASP Q  1 96  ? 36.228  143.788 118.583 1.00 18.43 ? 96   ASP Q O   1 
ATOM   18269 C  CB  . ASP Q  1 96  ? 37.561  142.989 121.133 1.00 17.98 ? 96   ASP Q CB  1 
ATOM   18270 C  CG  . ASP Q  1 96  ? 38.490  142.411 122.150 1.00 18.44 ? 96   ASP Q CG  1 
ATOM   18271 O  OD1 . ASP Q  1 96  ? 39.050  143.204 122.915 1.00 24.61 ? 96   ASP Q OD1 1 
ATOM   18272 O  OD2 . ASP Q  1 96  ? 38.761  141.180 122.226 1.00 23.91 ? 96   ASP Q OD2 1 
ATOM   18273 N  N   . VAL Q  1 97  ? 36.313  141.546 118.285 1.00 15.49 ? 97   VAL Q N   1 
ATOM   18274 C  CA  . VAL Q  1 97  ? 35.262  141.525 117.289 1.00 14.73 ? 97   VAL Q CA  1 
ATOM   18275 C  C   . VAL Q  1 97  ? 33.919  141.098 117.847 1.00 15.21 ? 97   VAL Q C   1 
ATOM   18276 O  O   . VAL Q  1 97  ? 33.842  140.134 118.597 1.00 14.78 ? 97   VAL Q O   1 
ATOM   18277 C  CB  . VAL Q  1 97  ? 35.633  140.559 116.129 1.00 14.90 ? 97   VAL Q CB  1 
ATOM   18278 C  CG1 . VAL Q  1 97  ? 34.532  140.522 115.107 1.00 14.35 ? 97   VAL Q CG1 1 
ATOM   18279 C  CG2 . VAL Q  1 97  ? 36.973  140.964 115.487 1.00 12.84 ? 97   VAL Q CG2 1 
ATOM   18280 N  N   . SER Q  1 98  ? 32.864  141.827 117.500 1.00 15.26 ? 98   SER Q N   1 
ATOM   18281 C  CA  . SER Q  1 98  ? 31.514  141.455 117.914 1.00 15.08 ? 98   SER Q CA  1 
ATOM   18282 C  C   . SER Q  1 98  ? 30.507  142.110 116.984 1.00 15.82 ? 98   SER Q C   1 
ATOM   18283 O  O   . SER Q  1 98  ? 30.298  143.342 117.035 1.00 15.11 ? 98   SER Q O   1 
ATOM   18284 C  CB  . SER Q  1 98  ? 31.242  141.835 119.376 1.00 15.40 ? 98   SER Q CB  1 
ATOM   18285 O  OG  . SER Q  1 98  ? 29.935  141.440 119.752 1.00 14.77 ? 98   SER Q OG  1 
ATOM   18286 N  N   . ILE Q  1 99  ? 29.879  141.276 116.155 1.00 16.15 ? 99   ILE Q N   1 
ATOM   18287 C  CA  . ILE Q  1 99  ? 28.986  141.702 115.079 1.00 16.97 ? 99   ILE Q CA  1 
ATOM   18288 C  C   . ILE Q  1 99  ? 27.789  140.760 114.963 1.00 17.32 ? 99   ILE Q C   1 
ATOM   18289 O  O   . ILE Q  1 99  ? 27.905  139.574 115.266 1.00 16.58 ? 99   ILE Q O   1 
ATOM   18290 C  CB  . ILE Q  1 99  ? 29.772  141.643 113.734 1.00 18.20 ? 99   ILE Q CB  1 
ATOM   18291 C  CG1 . ILE Q  1 99  ? 30.737  142.834 113.594 1.00 17.60 ? 99   ILE Q CG1 1 
ATOM   18292 C  CG2 . ILE Q  1 99  ? 28.828  141.593 112.533 1.00 20.05 ? 99   ILE Q CG2 1 
ATOM   18293 C  CD1 . ILE Q  1 99  ? 31.839  142.603 112.498 1.00 15.94 ? 99   ILE Q CD1 1 
ATOM   18294 N  N   . GLU Q  1 100 ? 26.638  141.275 114.519 1.00 16.21 ? 100  GLU Q N   1 
ATOM   18295 C  CA  . GLU Q  1 100 ? 25.507  140.400 114.247 1.00 16.07 ? 100  GLU Q CA  1 
ATOM   18296 C  C   . GLU Q  1 100 ? 25.024  140.670 112.826 1.00 15.73 ? 100  GLU Q C   1 
ATOM   18297 O  O   . GLU Q  1 100 ? 24.892  141.829 112.417 1.00 15.75 ? 100  GLU Q O   1 
ATOM   18298 C  CB  . GLU Q  1 100 ? 24.395  140.597 115.293 1.00 17.29 ? 100  GLU Q CB  1 
ATOM   18299 C  CG  . GLU Q  1 100 ? 23.268  139.604 115.186 1.00 19.36 ? 100  GLU Q CG  1 
ATOM   18300 C  CD  . GLU Q  1 100 ? 22.154  139.913 116.182 1.00 24.93 ? 100  GLU Q CD  1 
ATOM   18301 O  OE1 . GLU Q  1 100 ? 22.353  139.650 117.392 1.00 26.06 ? 100  GLU Q OE1 1 
ATOM   18302 O  OE2 . GLU Q  1 100 ? 21.092  140.434 115.754 1.00 25.38 ? 100  GLU Q OE2 1 
ATOM   18303 N  N   . ASP Q  1 101 ? 24.766  139.621 112.055 1.00 15.36 ? 101  ASP Q N   1 
ATOM   18304 C  CA  . ASP Q  1 101 ? 24.417  139.810 110.641 1.00 16.66 ? 101  ASP Q CA  1 
ATOM   18305 C  C   . ASP Q  1 101 ? 23.356  138.821 110.176 1.00 17.31 ? 101  ASP Q C   1 
ATOM   18306 O  O   . ASP Q  1 101 ? 23.459  137.618 110.456 1.00 17.57 ? 101  ASP Q O   1 
ATOM   18307 C  CB  . ASP Q  1 101 ? 25.689  139.678 109.757 1.00 15.95 ? 101  ASP Q CB  1 
ATOM   18308 C  CG  . ASP Q  1 101 ? 25.455  140.114 108.321 1.00 16.09 ? 101  ASP Q CG  1 
ATOM   18309 O  OD1 . ASP Q  1 101 ? 25.500  141.343 108.086 1.00 16.63 ? 101  ASP Q OD1 1 
ATOM   18310 O  OD2 . ASP Q  1 101 ? 25.222  139.315 107.366 1.00 14.48 ? 101  ASP Q OD2 1 
ATOM   18311 N  N   . SER Q  1 102 ? 22.362  139.312 109.430 1.00 17.84 ? 102  SER Q N   1 
ATOM   18312 C  CA  . SER Q  1 102 ? 21.298  138.423 108.970 1.00 19.04 ? 102  SER Q CA  1 
ATOM   18313 C  C   . SER Q  1 102 ? 21.365  138.155 107.469 1.00 18.66 ? 102  SER Q C   1 
ATOM   18314 O  O   . SER Q  1 102 ? 20.445  137.557 106.902 1.00 18.96 ? 102  SER Q O   1 
ATOM   18315 C  CB  . SER Q  1 102 ? 19.920  138.952 109.335 1.00 19.46 ? 102  SER Q CB  1 
ATOM   18316 O  OG  . SER Q  1 102 ? 19.914  139.571 110.611 1.00 22.55 ? 102  SER Q OG  1 
ATOM   18317 N  N   . VAL Q  1 103 ? 22.449  138.575 106.832 1.00 16.54 ? 103  VAL Q N   1 
ATOM   18318 C  CA  . VAL Q  1 103 ? 22.617  138.286 105.417 1.00 15.86 ? 103  VAL Q CA  1 
ATOM   18319 C  C   . VAL Q  1 103 ? 23.459  136.999 105.262 1.00 14.84 ? 103  VAL Q C   1 
ATOM   18320 O  O   . VAL Q  1 103 ? 23.098  136.082 104.508 1.00 14.64 ? 103  VAL Q O   1 
ATOM   18321 C  CB  . VAL Q  1 103 ? 23.164  139.509 104.656 1.00 15.71 ? 103  VAL Q CB  1 
ATOM   18322 C  CG1 . VAL Q  1 103 ? 23.502  139.163 103.212 1.00 15.94 ? 103  VAL Q CG1 1 
ATOM   18323 C  CG2 . VAL Q  1 103 ? 22.140  140.652 104.727 1.00 16.95 ? 103  VAL Q CG2 1 
ATOM   18324 N  N   . ILE Q  1 104 ? 24.563  136.910 105.992 1.00 13.98 ? 104  ILE Q N   1 
ATOM   18325 C  CA  . ILE Q  1 104 ? 25.320  135.664 105.986 1.00 12.97 ? 104  ILE Q CA  1 
ATOM   18326 C  C   . ILE Q  1 104 ? 24.454  134.602 106.659 1.00 13.92 ? 104  ILE Q C   1 
ATOM   18327 O  O   . ILE Q  1 104 ? 23.532  134.922 107.412 1.00 12.99 ? 104  ILE Q O   1 
ATOM   18328 C  CB  . ILE Q  1 104 ? 26.652  135.798 106.761 1.00 13.32 ? 104  ILE Q CB  1 
ATOM   18329 C  CG1 . ILE Q  1 104 ? 26.405  136.190 108.213 1.00 10.36 ? 104  ILE Q CG1 1 
ATOM   18330 C  CG2 . ILE Q  1 104 ? 27.621  136.754 106.070 1.00 12.90 ? 104  ILE Q CG2 1 
ATOM   18331 C  CD1 . ILE Q  1 104 ? 27.639  136.064 109.067 1.00 12.70 ? 104  ILE Q CD1 1 
ATOM   18332 N  N   . SER Q  1 105 ? 24.728  133.336 106.355 1.00 13.97 ? 105  SER Q N   1 
ATOM   18333 C  CA  . SER Q  1 105 ? 24.047  132.231 106.999 1.00 14.78 ? 105  SER Q CA  1 
ATOM   18334 C  C   . SER Q  1 105 ? 24.975  131.015 107.131 1.00 15.62 ? 105  SER Q C   1 
ATOM   18335 O  O   . SER Q  1 105 ? 26.019  130.959 106.486 1.00 15.12 ? 105  SER Q O   1 
ATOM   18336 C  CB  . SER Q  1 105 ? 22.783  131.853 106.225 1.00 14.35 ? 105  SER Q CB  1 
ATOM   18337 O  OG  . SER Q  1 105 ? 22.073  130.846 106.916 1.00 14.87 ? 105  SER Q OG  1 
ATOM   18338 N  N   . LEU Q  1 106 ? 24.590  130.054 107.970 1.00 16.33 ? 106  LEU Q N   1 
ATOM   18339 C  CA  . LEU Q  1 106 ? 25.380  128.824 108.136 1.00 17.76 ? 106  LEU Q CA  1 
ATOM   18340 C  C   . LEU Q  1 106 ? 24.721  127.627 107.460 1.00 19.21 ? 106  LEU Q C   1 
ATOM   18341 O  O   . LEU Q  1 106 ? 25.180  126.478 107.586 1.00 18.75 ? 106  LEU Q O   1 
ATOM   18342 C  CB  . LEU Q  1 106 ? 25.679  128.527 109.609 1.00 16.92 ? 106  LEU Q CB  1 
ATOM   18343 C  CG  . LEU Q  1 106 ? 26.349  129.709 110.324 1.00 17.64 ? 106  LEU Q CG  1 
ATOM   18344 C  CD1 . LEU Q  1 106 ? 26.663  129.390 111.780 1.00 16.13 ? 106  LEU Q CD1 1 
ATOM   18345 C  CD2 . LEU Q  1 106 ? 27.604  130.186 109.574 1.00 13.48 ? 106  LEU Q CD2 1 
ATOM   18346 N  N   . SER Q  1 107 ? 23.657  127.920 106.718 1.00 20.61 ? 107  SER Q N   1 
ATOM   18347 C  CA  . SER Q  1 107 ? 22.934  126.919 105.941 1.00 22.61 ? 107  SER Q CA  1 
ATOM   18348 C  C   . SER Q  1 107 ? 22.190  127.667 104.836 1.00 23.56 ? 107  SER Q C   1 
ATOM   18349 O  O   . SER Q  1 107 ? 21.870  128.841 105.008 1.00 24.03 ? 107  SER Q O   1 
ATOM   18350 C  CB  . SER Q  1 107 ? 21.954  126.158 106.836 1.00 22.64 ? 107  SER Q CB  1 
ATOM   18351 O  OG  . SER Q  1 107 ? 21.259  127.041 107.705 1.00 23.50 ? 107  SER Q OG  1 
ATOM   18352 N  N   . GLY Q  1 108 ? 21.931  127.012 103.700 1.00 24.62 ? 108  GLY Q N   1 
ATOM   18353 C  CA  . GLY Q  1 108 ? 21.162  127.638 102.619 1.00 25.13 ? 108  GLY Q CA  1 
ATOM   18354 C  C   . GLY Q  1 108 ? 21.966  128.297 101.500 1.00 25.20 ? 108  GLY Q C   1 
ATOM   18355 O  O   . GLY Q  1 108 ? 23.178  128.086 101.394 1.00 24.93 ? 108  GLY Q O   1 
ATOM   18356 N  N   . ASP Q  1 109 ? 21.295  129.093 100.661 1.00 25.07 ? 109  ASP Q N   1 
ATOM   18357 C  CA  . ASP Q  1 109 ? 21.972  129.764 99.544  1.00 25.11 ? 109  ASP Q CA  1 
ATOM   18358 C  C   . ASP Q  1 109 ? 23.039  130.732 100.013 1.00 24.15 ? 109  ASP Q C   1 
ATOM   18359 O  O   . ASP Q  1 109 ? 24.014  130.981 99.303  1.00 24.33 ? 109  ASP Q O   1 
ATOM   18360 C  CB  . ASP Q  1 109 ? 20.993  130.525 98.644  1.00 25.92 ? 109  ASP Q CB  1 
ATOM   18361 C  CG  . ASP Q  1 109 ? 21.714  131.447 97.644  1.00 27.85 ? 109  ASP Q CG  1 
ATOM   18362 O  OD1 . ASP Q  1 109 ? 21.414  131.376 96.427  1.00 30.40 ? 109  ASP Q OD1 1 
ATOM   18363 O  OD2 . ASP Q  1 109 ? 22.599  132.271 97.980  1.00 29.30 ? 109  ASP Q OD2 1 
ATOM   18364 N  N   . HIS Q  1 110 ? 22.857  131.302 101.194 1.00 23.04 ? 110  HIS Q N   1 
ATOM   18365 C  CA  . HIS Q  1 110 ? 23.835  132.281 101.677 1.00 21.96 ? 110  HIS Q CA  1 
ATOM   18366 C  C   . HIS Q  1 110 ? 24.819  131.661 102.642 1.00 20.57 ? 110  HIS Q C   1 
ATOM   18367 O  O   . HIS Q  1 110 ? 25.469  132.364 103.397 1.00 20.94 ? 110  HIS Q O   1 
ATOM   18368 C  CB  . HIS Q  1 110 ? 23.124  133.429 102.382 1.00 22.11 ? 110  HIS Q CB  1 
ATOM   18369 C  CG  . HIS Q  1 110 ? 22.330  134.302 101.466 1.00 23.28 ? 110  HIS Q CG  1 
ATOM   18370 N  ND1 . HIS Q  1 110 ? 21.747  135.482 101.884 1.00 23.54 ? 110  HIS Q ND1 1 
ATOM   18371 C  CD2 . HIS Q  1 110 ? 22.019  134.170 100.155 1.00 23.80 ? 110  HIS Q CD2 1 
ATOM   18372 C  CE1 . HIS Q  1 110 ? 21.109  136.038 100.869 1.00 24.94 ? 110  HIS Q CE1 1 
ATOM   18373 N  NE2 . HIS Q  1 110 ? 21.258  135.264 99.808  1.00 25.43 ? 110  HIS Q NE2 1 
ATOM   18374 N  N   . CYS Q  1 111 ? 24.927  130.344 102.617 1.00 19.74 ? 111  CYS Q N   1 
ATOM   18375 C  CA  . CYS Q  1 111 ? 25.767  129.625 103.570 1.00 18.85 ? 111  CYS Q CA  1 
ATOM   18376 C  C   . CYS Q  1 111 ? 27.242  129.976 103.415 1.00 17.27 ? 111  CYS Q C   1 
ATOM   18377 O  O   . CYS Q  1 111 ? 27.740  130.011 102.299 1.00 16.77 ? 111  CYS Q O   1 
ATOM   18378 C  CB  . CYS Q  1 111 ? 25.562  128.124 103.402 1.00 19.24 ? 111  CYS Q CB  1 
ATOM   18379 S  SG  . CYS Q  1 111 ? 26.402  127.155 104.658 1.00 25.29 ? 111  CYS Q SG  1 
ATOM   18380 N  N   . ILE Q  1 112 ? 27.934  130.241 104.524 1.00 16.02 ? 112  ILE Q N   1 
ATOM   18381 C  CA  . ILE Q  1 112 ? 29.357  130.621 104.440 1.00 15.31 ? 112  ILE Q CA  1 
ATOM   18382 C  C   . ILE Q  1 112 ? 30.353  129.545 104.861 1.00 14.67 ? 112  ILE Q C   1 
ATOM   18383 O  O   . ILE Q  1 112 ? 31.575  129.779 104.854 1.00 12.69 ? 112  ILE Q O   1 
ATOM   18384 C  CB  . ILE Q  1 112 ? 29.646  131.938 105.177 1.00 15.74 ? 112  ILE Q CB  1 
ATOM   18385 C  CG1 . ILE Q  1 112 ? 29.356  131.815 106.674 1.00 16.12 ? 112  ILE Q CG1 1 
ATOM   18386 C  CG2 . ILE Q  1 112 ? 28.850  133.118 104.545 1.00 15.23 ? 112  ILE Q CG2 1 
ATOM   18387 C  CD1 . ILE Q  1 112 ? 29.778  133.055 107.445 1.00 16.44 ? 112  ILE Q CD1 1 
ATOM   18388 N  N   . ILE Q  1 113 ? 29.840  128.367 105.216 1.00 14.42 ? 113  ILE Q N   1 
ATOM   18389 C  CA  . ILE Q  1 113 ? 30.706  127.238 105.558 1.00 14.58 ? 113  ILE Q CA  1 
ATOM   18390 C  C   . ILE Q  1 113 ? 31.556  126.840 104.364 1.00 14.24 ? 113  ILE Q C   1 
ATOM   18391 O  O   . ILE Q  1 113 ? 31.030  126.652 103.264 1.00 13.14 ? 113  ILE Q O   1 
ATOM   18392 C  CB  . ILE Q  1 113 ? 29.892  126.003 105.955 1.00 15.08 ? 113  ILE Q CB  1 
ATOM   18393 C  CG1 . ILE Q  1 113 ? 28.938  126.287 107.121 1.00 17.29 ? 113  ILE Q CG1 1 
ATOM   18394 C  CG2 . ILE Q  1 113 ? 30.818  124.823 106.271 1.00 14.93 ? 113  ILE Q CG2 1 
ATOM   18395 C  CD1 . ILE Q  1 113 ? 29.600  126.883 108.312 1.00 19.40 ? 113  ILE Q CD1 1 
ATOM   18396 N  N   . GLY Q  1 114 ? 32.859  126.695 104.598 1.00 13.47 ? 114  GLY Q N   1 
ATOM   18397 C  CA  . GLY Q  1 114 ? 33.797  126.276 103.583 1.00 13.29 ? 114  GLY Q CA  1 
ATOM   18398 C  C   . GLY Q  1 114 ? 34.265  127.427 102.724 1.00 12.42 ? 114  GLY Q C   1 
ATOM   18399 O  O   . GLY Q  1 114 ? 34.934  127.218 101.720 1.00 12.19 ? 114  GLY Q O   1 
ATOM   18400 N  N   . ARG Q  1 115 ? 33.870  128.639 103.096 1.00 12.63 ? 115  ARG Q N   1 
ATOM   18401 C  CA  . ARG Q  1 115 ? 34.327  129.839 102.402 1.00 12.09 ? 115  ARG Q CA  1 
ATOM   18402 C  C   . ARG Q  1 115 ? 35.415  130.425 103.302 1.00 12.50 ? 115  ARG Q C   1 
ATOM   18403 O  O   . ARG Q  1 115 ? 35.767  129.798 104.301 1.00 12.96 ? 115  ARG Q O   1 
ATOM   18404 C  CB  . ARG Q  1 115 ? 33.152  130.775 102.095 1.00 12.34 ? 115  ARG Q CB  1 
ATOM   18405 C  CG  . ARG Q  1 115 ? 32.110  130.028 101.206 1.00 13.38 ? 115  ARG Q CG  1 
ATOM   18406 C  CD  . ARG Q  1 115 ? 31.021  130.911 100.563 1.00 14.66 ? 115  ARG Q CD  1 
ATOM   18407 N  NE  . ARG Q  1 115 ? 30.028  130.125 99.820  1.00 14.45 ? 115  ARG Q NE  1 
ATOM   18408 C  CZ  . ARG Q  1 115 ? 30.166  129.765 98.553  1.00 14.72 ? 115  ARG Q CZ  1 
ATOM   18409 N  NH1 . ARG Q  1 115 ? 31.276  130.095 97.900  1.00 12.69 ? 115  ARG Q NH1 1 
ATOM   18410 N  NH2 . ARG Q  1 115 ? 29.206  129.065 97.936  1.00 14.33 ? 115  ARG Q NH2 1 
ATOM   18411 N  N   . THR Q  1 116 ? 35.976  131.580 102.934 1.00 11.95 ? 116  THR Q N   1 
ATOM   18412 C  CA  . THR Q  1 116 ? 37.125  132.111 103.646 1.00 11.58 ? 116  THR Q CA  1 
ATOM   18413 C  C   . THR Q  1 116 ? 36.807  133.453 104.315 1.00 11.39 ? 116  THR Q C   1 
ATOM   18414 O  O   . THR Q  1 116 ? 36.263  134.353 103.662 1.00 12.78 ? 116  THR Q O   1 
ATOM   18415 C  CB  . THR Q  1 116 ? 38.310  132.270 102.651 1.00 11.03 ? 116  THR Q CB  1 
ATOM   18416 O  OG1 . THR Q  1 116 ? 38.876  130.994 102.336 1.00 12.58 ? 116  THR Q OG1 1 
ATOM   18417 C  CG2 . THR Q  1 116 ? 39.519  133.017 103.300 1.00 11.77 ? 116  THR Q CG2 1 
ATOM   18418 N  N   . LEU Q  1 117 ? 37.147  133.604 105.594 1.00 10.31 ? 117  LEU Q N   1 
ATOM   18419 C  CA  . LEU Q  1 117 ? 37.042  134.901 106.280 1.00 9.74  ? 117  LEU Q CA  1 
ATOM   18420 C  C   . LEU Q  1 117 ? 38.395  135.612 106.144 1.00 9.52  ? 117  LEU Q C   1 
ATOM   18421 O  O   . LEU Q  1 117 ? 39.432  134.977 106.364 1.00 10.02 ? 117  LEU Q O   1 
ATOM   18422 C  CB  . LEU Q  1 117 ? 36.732  134.693 107.764 1.00 10.10 ? 117  LEU Q CB  1 
ATOM   18423 C  CG  . LEU Q  1 117 ? 36.570  135.942 108.635 1.00 9.39  ? 117  LEU Q CG  1 
ATOM   18424 C  CD1 . LEU Q  1 117 ? 35.349  136.737 108.158 1.00 10.64 ? 117  LEU Q CD1 1 
ATOM   18425 C  CD2 . LEU Q  1 117 ? 36.345  135.478 110.112 1.00 9.80  ? 117  LEU Q CD2 1 
ATOM   18426 N  N   . VAL Q  1 118 ? 38.397  136.899 105.782 1.00 9.82  ? 118  VAL Q N   1 
ATOM   18427 C  CA  . VAL Q  1 118 ? 39.641  137.621 105.537 1.00 8.94  ? 118  VAL Q CA  1 
ATOM   18428 C  C   . VAL Q  1 118 ? 39.614  138.944 106.304 1.00 9.10  ? 118  VAL Q C   1 
ATOM   18429 O  O   . VAL Q  1 118 ? 38.567  139.597 106.359 1.00 9.91  ? 118  VAL Q O   1 
ATOM   18430 C  CB  . VAL Q  1 118 ? 39.776  138.000 104.054 1.00 9.40  ? 118  VAL Q CB  1 
ATOM   18431 C  CG1 . VAL Q  1 118 ? 41.009  138.871 103.847 1.00 10.66 ? 118  VAL Q CG1 1 
ATOM   18432 C  CG2 . VAL Q  1 118 ? 39.780  136.750 103.132 1.00 10.46 ? 118  VAL Q CG2 1 
ATOM   18433 N  N   . VAL Q  1 119 ? 40.709  139.269 106.977 1.00 9.27  ? 119  VAL Q N   1 
ATOM   18434 C  CA  . VAL Q  1 119 ? 40.862  140.595 107.591 1.00 8.85  ? 119  VAL Q CA  1 
ATOM   18435 C  C   . VAL Q  1 119 ? 41.926  141.344 106.754 1.00 9.91  ? 119  VAL Q C   1 
ATOM   18436 O  O   . VAL Q  1 119 ? 42.964  140.761 106.368 1.00 9.61  ? 119  VAL Q O   1 
ATOM   18437 C  CB  . VAL Q  1 119 ? 41.203  140.527 109.103 1.00 9.01  ? 119  VAL Q CB  1 
ATOM   18438 C  CG1 . VAL Q  1 119 ? 42.528  139.789 109.319 1.00 10.16 ? 119  VAL Q CG1 1 
ATOM   18439 C  CG2 . VAL Q  1 119 ? 41.251  142.009 109.723 1.00 6.58  ? 119  VAL Q CG2 1 
ATOM   18440 N  N   . HIS Q  1 120 ? 41.606  142.600 106.429 1.00 9.58  ? 120  HIS Q N   1 
ATOM   18441 C  CA  . HIS Q  1 120 ? 42.338  143.406 105.450 1.00 10.02 ? 120  HIS Q CA  1 
ATOM   18442 C  C   . HIS Q  1 120 ? 43.273  144.437 106.003 1.00 9.63  ? 120  HIS Q C   1 
ATOM   18443 O  O   . HIS Q  1 120 ? 43.160  144.835 107.159 1.00 9.39  ? 120  HIS Q O   1 
ATOM   18444 C  CB  . HIS Q  1 120 ? 41.337  144.132 104.558 1.00 8.93  ? 120  HIS Q CB  1 
ATOM   18445 C  CG  . HIS Q  1 120 ? 40.790  143.258 103.478 1.00 9.58  ? 120  HIS Q CG  1 
ATOM   18446 N  ND1 . HIS Q  1 120 ? 41.458  143.038 102.286 1.00 11.45 ? 120  HIS Q ND1 1 
ATOM   18447 C  CD2 . HIS Q  1 120 ? 39.646  142.534 103.410 1.00 10.52 ? 120  HIS Q CD2 1 
ATOM   18448 C  CE1 . HIS Q  1 120 ? 40.738  142.229 101.526 1.00 12.76 ? 120  HIS Q CE1 1 
ATOM   18449 N  NE2 . HIS Q  1 120 ? 39.642  141.906 102.183 1.00 11.77 ? 120  HIS Q NE2 1 
ATOM   18450 N  N   . GLU Q  1 121 ? 44.184  144.869 105.144 1.00 10.57 ? 121  GLU Q N   1 
ATOM   18451 C  CA  . GLU Q  1 121 ? 45.219  145.845 105.458 1.00 13.05 ? 121  GLU Q CA  1 
ATOM   18452 C  C   . GLU Q  1 121 ? 44.644  147.208 105.839 1.00 13.75 ? 121  GLU Q C   1 
ATOM   18453 O  O   . GLU Q  1 121 ? 45.138  147.867 106.761 1.00 14.53 ? 121  GLU Q O   1 
ATOM   18454 C  CB  . GLU Q  1 121 ? 46.067  146.033 104.187 1.00 12.46 ? 121  GLU Q CB  1 
ATOM   18455 C  CG  . GLU Q  1 121 ? 47.092  147.160 104.215 1.00 15.87 ? 121  GLU Q CG  1 
ATOM   18456 C  CD  . GLU Q  1 121 ? 47.582  147.549 102.813 1.00 19.25 ? 121  GLU Q CD  1 
ATOM   18457 O  OE1 . GLU Q  1 121 ? 46.989  147.122 101.788 1.00 17.97 ? 121  GLU Q OE1 1 
ATOM   18458 O  OE2 . GLU Q  1 121 ? 48.565  148.322 102.713 1.00 22.48 ? 121  GLU Q OE2 1 
ATOM   18459 N  N   . LYS Q  1 122 ? 43.609  147.636 105.122 1.00 13.65 ? 122  LYS Q N   1 
ATOM   18460 C  CA  . LYS Q  1 122 ? 43.051  148.963 105.340 1.00 13.93 ? 122  LYS Q CA  1 
ATOM   18461 C  C   . LYS Q  1 122 ? 41.560  148.912 105.703 1.00 12.81 ? 122  LYS Q C   1 
ATOM   18462 O  O   . LYS Q  1 122 ? 40.924  147.881 105.626 1.00 12.04 ? 122  LYS Q O   1 
ATOM   18463 C  CB  . LYS Q  1 122 ? 43.136  149.781 104.038 1.00 12.88 ? 122  LYS Q CB  1 
ATOM   18464 C  CG  . LYS Q  1 122 ? 44.482  149.771 103.333 1.00 17.61 ? 122  LYS Q CG  1 
ATOM   18465 C  CD  . LYS Q  1 122 ? 44.421  150.590 102.024 1.00 22.58 ? 122  LYS Q CD  1 
ATOM   18466 C  CE  . LYS Q  1 122 ? 45.768  150.686 101.321 1.00 28.03 ? 122  LYS Q CE  1 
ATOM   18467 N  NZ  . LYS Q  1 122 ? 45.670  151.450 100.015 1.00 31.66 ? 122  LYS Q NZ  1 
ATOM   18468 N  N   . ALA Q  1 123 ? 41.028  150.092 105.999 1.00 12.55 ? 123  ALA Q N   1 
ATOM   18469 C  CA  . ALA Q  1 123 ? 39.605  150.247 106.240 1.00 12.25 ? 123  ALA Q CA  1 
ATOM   18470 C  C   . ALA Q  1 123 ? 38.830  149.932 104.961 1.00 11.89 ? 123  ALA Q C   1 
ATOM   18471 O  O   . ALA Q  1 123 ? 39.236  150.287 103.857 1.00 11.35 ? 123  ALA Q O   1 
ATOM   18472 C  CB  . ALA Q  1 123 ? 39.295  151.665 106.667 1.00 12.66 ? 123  ALA Q CB  1 
ATOM   18473 N  N   . ASP Q  1 124 ? 37.703  149.277 105.122 1.00 10.35 ? 124  ASP Q N   1 
ATOM   18474 C  CA  . ASP Q  1 124 ? 36.719  149.124 104.053 1.00 10.06 ? 124  ASP Q CA  1 
ATOM   18475 C  C   . ASP Q  1 124 ? 35.935  150.446 103.924 1.00 10.37 ? 124  ASP Q C   1 
ATOM   18476 O  O   . ASP Q  1 124 ? 35.340  150.943 104.906 1.00 9.88  ? 124  ASP Q O   1 
ATOM   18477 C  CB  . ASP Q  1 124 ? 35.769  148.003 104.511 1.00 10.43 ? 124  ASP Q CB  1 
ATOM   18478 C  CG  . ASP Q  1 124 ? 34.762  147.596 103.480 1.00 10.39 ? 124  ASP Q CG  1 
ATOM   18479 O  OD1 . ASP Q  1 124 ? 34.349  148.355 102.590 1.00 8.47  ? 124  ASP Q OD1 1 
ATOM   18480 O  OD2 . ASP Q  1 124 ? 34.305  146.468 103.504 1.00 10.24 ? 124  ASP Q OD2 1 
ATOM   18481 N  N   . ASP Q  1 125 ? 35.900  151.024 102.732 1.00 8.71  ? 125  ASP Q N   1 
ATOM   18482 C  CA  . ASP Q  1 125 ? 35.139  152.287 102.577 1.00 8.56  ? 125  ASP Q CA  1 
ATOM   18483 C  C   . ASP Q  1 125 ? 33.622  152.068 102.392 1.00 9.32  ? 125  ASP Q C   1 
ATOM   18484 O  O   . ASP Q  1 125 ? 32.855  153.033 102.117 1.00 10.16 ? 125  ASP Q O   1 
ATOM   18485 C  CB  . ASP Q  1 125 ? 35.732  153.189 101.460 1.00 8.84  ? 125  ASP Q CB  1 
ATOM   18486 C  CG  . ASP Q  1 125 ? 35.542  152.626 100.067 1.00 10.38 ? 125  ASP Q CG  1 
ATOM   18487 O  OD1 . ASP Q  1 125 ? 34.711  151.707 99.841  1.00 10.56 ? 125  ASP Q OD1 1 
ATOM   18488 O  OD2 . ASP Q  1 125 ? 36.205  153.083 99.110  1.00 9.23  ? 125  ASP Q OD2 1 
ATOM   18489 N  N   . LEU Q  1 126 ? 33.189  150.809 102.532 1.00 10.20 ? 126  LEU Q N   1 
ATOM   18490 C  CA  . LEU Q  1 126 ? 31.780  150.447 102.518 1.00 10.39 ? 126  LEU Q CA  1 
ATOM   18491 C  C   . LEU Q  1 126 ? 31.100  150.803 101.200 1.00 9.71  ? 126  LEU Q C   1 
ATOM   18492 O  O   . LEU Q  1 126 ? 29.896  151.026 101.160 1.00 9.98  ? 126  LEU Q O   1 
ATOM   18493 C  CB  . LEU Q  1 126 ? 31.041  151.074 103.729 1.00 11.63 ? 126  LEU Q CB  1 
ATOM   18494 C  CG  . LEU Q  1 126 ? 31.683  150.794 105.104 1.00 12.90 ? 126  LEU Q CG  1 
ATOM   18495 C  CD1 . LEU Q  1 126 ? 30.864  151.470 106.260 1.00 12.02 ? 126  LEU Q CD1 1 
ATOM   18496 C  CD2 . LEU Q  1 126 ? 31.856  149.271 105.373 1.00 10.06 ? 126  LEU Q CD2 1 
ATOM   18497 N  N   . GLY Q  1 127 ? 31.891  150.820 100.125 1.00 9.62  ? 127  GLY Q N   1 
ATOM   18498 C  CA  . GLY Q  1 127 ? 31.393  151.075 98.796  1.00 9.00  ? 127  GLY Q CA  1 
ATOM   18499 C  C   . GLY Q  1 127 ? 31.104  152.525 98.500  1.00 9.60  ? 127  GLY Q C   1 
ATOM   18500 O  O   . GLY Q  1 127 ? 30.416  152.828 97.549  1.00 7.37  ? 127  GLY Q O   1 
ATOM   18501 N  N   . LYS Q  1 128 ? 31.635  153.408 99.328  1.00 8.65  ? 128  LYS Q N   1 
ATOM   18502 C  CA  . LYS Q  1 128 ? 31.382  154.835 99.208  1.00 10.51 ? 128  LYS Q CA  1 
ATOM   18503 C  C   . LYS Q  1 128 ? 32.543  155.605 98.650  1.00 9.05  ? 128  LYS Q C   1 
ATOM   18504 O  O   . LYS Q  1 128 ? 32.576  156.823 98.757  1.00 10.33 ? 128  LYS Q O   1 
ATOM   18505 C  CB  . LYS Q  1 128 ? 31.090  155.373 100.608 1.00 11.18 ? 128  LYS Q CB  1 
ATOM   18506 C  CG  . LYS Q  1 128 ? 29.793  154.783 101.155 1.00 15.27 ? 128  LYS Q CG  1 
ATOM   18507 C  CD  . LYS Q  1 128 ? 29.366  155.486 102.463 1.00 24.26 ? 128  LYS Q CD  1 
ATOM   18508 C  CE  . LYS Q  1 128 ? 27.937  155.124 102.812 1.00 30.95 ? 128  LYS Q CE  1 
ATOM   18509 N  NZ  . LYS Q  1 128 ? 27.392  155.930 103.966 1.00 36.25 ? 128  LYS Q NZ  1 
ATOM   18510 N  N   . GLY Q  1 129 ? 33.508  154.920 98.086  1.00 8.25  ? 129  GLY Q N   1 
ATOM   18511 C  CA  . GLY Q  1 129 ? 34.688  155.632 97.648  1.00 7.22  ? 129  GLY Q CA  1 
ATOM   18512 C  C   . GLY Q  1 129 ? 34.632  156.156 96.227  1.00 7.42  ? 129  GLY Q C   1 
ATOM   18513 O  O   . GLY Q  1 129 ? 35.602  156.773 95.793  1.00 5.74  ? 129  GLY Q O   1 
ATOM   18514 N  N   . GLY Q  1 130 ? 33.547  155.884 95.489  1.00 5.87  ? 130  GLY Q N   1 
ATOM   18515 C  CA  . GLY Q  1 130 ? 33.388  156.483 94.159  1.00 5.00  ? 130  GLY Q CA  1 
ATOM   18516 C  C   . GLY Q  1 130 ? 34.236  155.975 92.993  1.00 5.39  ? 130  GLY Q C   1 
ATOM   18517 O  O   . GLY Q  1 130 ? 34.082  156.484 91.874  1.00 5.51  ? 130  GLY Q O   1 
ATOM   18518 N  N   . ASN Q  1 131 ? 35.173  155.060 93.250  1.00 5.39  ? 131  ASN Q N   1 
ATOM   18519 C  CA  . ASN Q  1 131 ? 35.934  154.456 92.180  1.00 6.33  ? 131  ASN Q CA  1 
ATOM   18520 C  C   . ASN Q  1 131 ? 35.500  153.044 91.926  1.00 6.03  ? 131  ASN Q C   1 
ATOM   18521 O  O   . ASN Q  1 131 ? 34.726  152.452 92.721  1.00 8.09  ? 131  ASN Q O   1 
ATOM   18522 C  CB  . ASN Q  1 131 ? 37.473  154.536 92.366  1.00 5.20  ? 131  ASN Q CB  1 
ATOM   18523 C  CG  . ASN Q  1 131 ? 37.966  153.818 93.597  1.00 8.08  ? 131  ASN Q CG  1 
ATOM   18524 O  OD1 . ASN Q  1 131 ? 37.186  153.353 94.412  1.00 8.50  ? 131  ASN Q OD1 1 
ATOM   18525 N  ND2 . ASN Q  1 131 ? 39.286  153.797 93.769  1.00 8.71  ? 131  ASN Q ND2 1 
ATOM   18526 N  N   . GLU Q  1 132 ? 36.046  152.466 90.878  1.00 6.80  ? 132  GLU Q N   1 
ATOM   18527 C  CA  . GLU Q  1 132 ? 35.691  151.098 90.539  1.00 7.12  ? 132  GLU Q CA  1 
ATOM   18528 C  C   . GLU Q  1 132 ? 36.019  150.144 91.694  1.00 8.89  ? 132  GLU Q C   1 
ATOM   18529 O  O   . GLU Q  1 132 ? 35.244  149.236 91.995  1.00 8.85  ? 132  GLU Q O   1 
ATOM   18530 C  CB  . GLU Q  1 132 ? 36.438  150.644 89.277  1.00 7.13  ? 132  GLU Q CB  1 
ATOM   18531 C  CG  . GLU Q  1 132 ? 35.940  151.340 88.019  1.00 10.03 ? 132  GLU Q CG  1 
ATOM   18532 C  CD  . GLU Q  1 132 ? 36.656  150.863 86.769  1.00 13.72 ? 132  GLU Q CD  1 
ATOM   18533 O  OE1 . GLU Q  1 132 ? 37.169  149.732 86.766  1.00 18.32 ? 132  GLU Q OE1 1 
ATOM   18534 O  OE2 . GLU Q  1 132 ? 36.719  151.620 85.793  1.00 15.38 ? 132  GLU Q OE2 1 
ATOM   18535 N  N   . GLU Q  1 133 ? 37.188  150.335 92.293  1.00 9.36  ? 133  GLU Q N   1 
ATOM   18536 C  CA  . GLU Q  1 133 ? 37.645  149.444 93.369  1.00 11.35 ? 133  GLU Q CA  1 
ATOM   18537 C  C   . GLU Q  1 133 ? 36.690  149.473 94.567  1.00 10.75 ? 133  GLU Q C   1 
ATOM   18538 O  O   . GLU Q  1 133 ? 36.415  148.449 95.187  1.00 11.39 ? 133  GLU Q O   1 
ATOM   18539 C  CB  . GLU Q  1 133 ? 39.088  149.775 93.759  1.00 11.83 ? 133  GLU Q CB  1 
ATOM   18540 C  CG  . GLU Q  1 133 ? 39.747  148.704 94.620  1.00 13.91 ? 133  GLU Q CG  1 
ATOM   18541 C  CD  . GLU Q  1 133 ? 39.875  147.373 93.883  1.00 16.91 ? 133  GLU Q CD  1 
ATOM   18542 O  OE1 . GLU Q  1 133 ? 40.344  147.368 92.725  1.00 14.78 ? 133  GLU Q OE1 1 
ATOM   18543 O  OE2 . GLU Q  1 133 ? 39.493  146.329 94.456  1.00 18.20 ? 133  GLU Q OE2 1 
ATOM   18544 N  N   . SER Q  1 134 ? 36.135  150.632 94.875  1.00 11.22 ? 134  SER Q N   1 
ATOM   18545 C  CA  . SER Q  1 134 ? 35.199  150.680 95.991  1.00 10.83 ? 134  SER Q CA  1 
ATOM   18546 C  C   . SER Q  1 134 ? 34.008  149.733 95.791  1.00 11.27 ? 134  SER Q C   1 
ATOM   18547 O  O   . SER Q  1 134 ? 33.522  149.088 96.742  1.00 10.85 ? 134  SER Q O   1 
ATOM   18548 C  CB  . SER Q  1 134 ? 34.705  152.105 96.205  1.00 9.55  ? 134  SER Q CB  1 
ATOM   18549 O  OG  . SER Q  1 134 ? 33.780  152.108 97.283  1.00 10.12 ? 134  SER Q OG  1 
ATOM   18550 N  N   . THR Q  1 135 ? 33.544  149.610 94.557  1.00 11.91 ? 135  THR Q N   1 
ATOM   18551 C  CA  . THR Q  1 135 ? 32.368  148.792 94.302  1.00 12.07 ? 135  THR Q CA  1 
ATOM   18552 C  C   . THR Q  1 135 ? 32.698  147.317 94.319  1.00 12.60 ? 135  THR Q C   1 
ATOM   18553 O  O   . THR Q  1 135 ? 31.800  146.495 94.169  1.00 13.20 ? 135  THR Q O   1 
ATOM   18554 C  CB  . THR Q  1 135 ? 31.743  149.125 92.915  1.00 12.71 ? 135  THR Q CB  1 
ATOM   18555 O  OG1 . THR Q  1 135 ? 32.644  148.736 91.859  1.00 12.71 ? 135  THR Q OG1 1 
ATOM   18556 C  CG2 . THR Q  1 135 ? 31.597  150.628 92.726  1.00 13.39 ? 135  THR Q CG2 1 
ATOM   18557 N  N   . LYS Q  1 136 ? 33.984  146.988 94.451  1.00 12.34 ? 136  LYS Q N   1 
ATOM   18558 C  CA  . LYS Q  1 136 ? 34.431  145.603 94.463  1.00 12.80 ? 136  LYS Q CA  1 
ATOM   18559 C  C   . LYS Q  1 136 ? 34.906  145.125 95.830  1.00 12.42 ? 136  LYS Q C   1 
ATOM   18560 O  O   . LYS Q  1 136 ? 34.424  144.121 96.344  1.00 12.26 ? 136  LYS Q O   1 
ATOM   18561 C  CB  . LYS Q  1 136 ? 35.586  145.390 93.451  1.00 12.84 ? 136  LYS Q CB  1 
ATOM   18562 C  CG  . LYS Q  1 136 ? 35.133  145.458 91.992  1.00 16.46 ? 136  LYS Q CG  1 
ATOM   18563 C  CD  . LYS Q  1 136 ? 36.250  145.087 90.994  1.00 23.66 ? 136  LYS Q CD  1 
ATOM   18564 C  CE  . LYS Q  1 136 ? 36.910  146.329 90.414  1.00 25.41 ? 136  LYS Q CE  1 
ATOM   18565 N  NZ  . LYS Q  1 136 ? 37.130  146.190 88.932  1.00 28.71 ? 136  LYS Q NZ  1 
ATOM   18566 N  N   . THR Q  1 137 ? 35.855  145.850 96.393  1.00 12.64 ? 137  THR Q N   1 
ATOM   18567 C  CA  . THR Q  1 137 ? 36.491  145.437 97.646  1.00 13.35 ? 137  THR Q CA  1 
ATOM   18568 C  C   . THR Q  1 137 ? 36.398  146.480 98.739  1.00 12.94 ? 137  THR Q C   1 
ATOM   18569 O  O   . THR Q  1 137 ? 36.966  146.302 99.810  1.00 12.61 ? 137  THR Q O   1 
ATOM   18570 C  CB  . THR Q  1 137 ? 37.980  145.240 97.397  1.00 12.91 ? 137  THR Q CB  1 
ATOM   18571 O  OG1 . THR Q  1 137 ? 38.538  146.480 96.932  1.00 12.00 ? 137  THR Q OG1 1 
ATOM   18572 C  CG2 . THR Q  1 137 ? 38.237  144.237 96.246  1.00 16.07 ? 137  THR Q CG2 1 
ATOM   18573 N  N   . GLY Q  1 138 ? 35.728  147.589 98.485  1.00 12.00 ? 138  GLY Q N   1 
ATOM   18574 C  CA  . GLY Q  1 138 ? 35.795  148.670 99.447  1.00 11.00 ? 138  GLY Q CA  1 
ATOM   18575 C  C   . GLY Q  1 138 ? 37.179  149.324 99.588  1.00 10.79 ? 138  GLY Q C   1 
ATOM   18576 O  O   . GLY Q  1 138 ? 37.382  150.043 100.555 1.00 10.21 ? 138  GLY Q O   1 
ATOM   18577 N  N   . ASN Q  1 139 ? 38.104  149.141 98.630  1.00 9.17  ? 139  ASN Q N   1 
ATOM   18578 C  CA  . ASN Q  1 139 ? 39.437  149.682 98.777  1.00 9.38  ? 139  ASN Q CA  1 
ATOM   18579 C  C   . ASN Q  1 139 ? 40.118  149.212 100.092 1.00 9.46  ? 139  ASN Q C   1 
ATOM   18580 O  O   . ASN Q  1 139 ? 40.949  149.910 100.668 1.00 10.09 ? 139  ASN Q O   1 
ATOM   18581 C  CB  . ASN Q  1 139 ? 39.405  151.212 98.724  1.00 10.04 ? 139  ASN Q CB  1 
ATOM   18582 C  CG  . ASN Q  1 139 ? 39.105  151.742 97.322  1.00 12.11 ? 139  ASN Q CG  1 
ATOM   18583 O  OD1 . ASN Q  1 139 ? 39.906  151.551 96.412  1.00 10.58 ? 139  ASN Q OD1 1 
ATOM   18584 N  ND2 . ASN Q  1 139 ? 37.941  152.396 97.141  1.00 8.44  ? 139  ASN Q ND2 1 
ATOM   18585 N  N   . ALA Q  1 140 ? 39.786  148.013 100.548 1.00 8.77  ? 140  ALA Q N   1 
ATOM   18586 C  CA  . ALA Q  1 140 ? 40.361  147.514 101.798 1.00 10.21 ? 140  ALA Q CA  1 
ATOM   18587 C  C   . ALA Q  1 140 ? 41.804  146.993 101.714 1.00 10.94 ? 140  ALA Q C   1 
ATOM   18588 O  O   . ALA Q  1 140 ? 42.440  146.666 102.747 1.00 9.73  ? 140  ALA Q O   1 
ATOM   18589 C  CB  . ALA Q  1 140 ? 39.413  146.465 102.450 1.00 11.59 ? 140  ALA Q CB  1 
ATOM   18590 N  N   . GLY Q  1 141 ? 42.337  146.953 100.493 1.00 9.85  ? 141  GLY Q N   1 
ATOM   18591 C  CA  . GLY Q  1 141 ? 43.721  146.570 100.315 1.00 10.41 ? 141  GLY Q CA  1 
ATOM   18592 C  C   . GLY Q  1 141 ? 44.037  145.087 100.513 1.00 11.10 ? 141  GLY Q C   1 
ATOM   18593 O  O   . GLY Q  1 141 ? 43.190  144.213 100.314 1.00 10.62 ? 141  GLY Q O   1 
ATOM   18594 N  N   . SER Q  1 142 ? 45.262  144.814 100.948 1.00 12.25 ? 142  SER Q N   1 
ATOM   18595 C  CA  . SER Q  1 142 ? 45.747  143.437 100.936 1.00 12.83 ? 142  SER Q CA  1 
ATOM   18596 C  C   . SER Q  1 142 ? 45.101  142.585 102.027 1.00 13.00 ? 142  SER Q C   1 
ATOM   18597 O  O   . SER Q  1 142 ? 44.431  143.096 102.926 1.00 12.33 ? 142  SER Q O   1 
ATOM   18598 C  CB  . SER Q  1 142 ? 47.261  143.408 101.080 1.00 13.98 ? 142  SER Q CB  1 
ATOM   18599 O  OG  . SER Q  1 142 ? 47.603  143.641 102.430 1.00 15.93 ? 142  SER Q OG  1 
ATOM   18600 N  N   . ARG Q  1 143 ? 45.309  141.276 101.926 1.00 11.98 ? 143  ARG Q N   1 
ATOM   18601 C  CA  . ARG Q  1 143 ? 44.660  140.321 102.833 1.00 11.96 ? 143  ARG Q CA  1 
ATOM   18602 C  C   . ARG Q  1 143 ? 45.701  139.941 103.881 1.00 12.57 ? 143  ARG Q C   1 
ATOM   18603 O  O   . ARG Q  1 143 ? 46.692  139.263 103.549 1.00 12.91 ? 143  ARG Q O   1 
ATOM   18604 C  CB  . ARG Q  1 143 ? 44.222  139.110 102.023 1.00 11.52 ? 143  ARG Q CB  1 
ATOM   18605 C  CG  . ARG Q  1 143 ? 43.283  139.467 100.895 1.00 12.56 ? 143  ARG Q CG  1 
ATOM   18606 C  CD  . ARG Q  1 143 ? 42.972  138.378 99.892  1.00 14.65 ? 143  ARG Q CD  1 
ATOM   18607 N  NE  . ARG Q  1 143 ? 42.161  138.937 98.808  1.00 14.91 ? 143  ARG Q NE  1 
ATOM   18608 C  CZ  . ARG Q  1 143 ? 41.367  138.231 98.017  1.00 14.51 ? 143  ARG Q CZ  1 
ATOM   18609 N  NH1 . ARG Q  1 143 ? 41.254  136.920 98.173  1.00 13.53 ? 143  ARG Q NH1 1 
ATOM   18610 N  NH2 . ARG Q  1 143 ? 40.666  138.856 97.082  1.00 11.96 ? 143  ARG Q NH2 1 
ATOM   18611 N  N   . LEU Q  1 144 ? 45.503  140.380 105.125 1.00 10.44 ? 144  LEU Q N   1 
ATOM   18612 C  CA  . LEU Q  1 144 ? 46.506  140.158 106.149 1.00 10.09 ? 144  LEU Q CA  1 
ATOM   18613 C  C   . LEU Q  1 144 ? 46.437  138.785 106.760 1.00 9.95  ? 144  LEU Q C   1 
ATOM   18614 O  O   . LEU Q  1 144 ? 47.459  138.244 107.147 1.00 10.38 ? 144  LEU Q O   1 
ATOM   18615 C  CB  . LEU Q  1 144 ? 46.410  141.178 107.272 1.00 9.77  ? 144  LEU Q CB  1 
ATOM   18616 C  CG  . LEU Q  1 144 ? 46.556  142.639 106.816 1.00 11.71 ? 144  LEU Q CG  1 
ATOM   18617 C  CD1 . LEU Q  1 144 ? 46.528  143.545 108.050 1.00 14.68 ? 144  LEU Q CD1 1 
ATOM   18618 C  CD2 . LEU Q  1 144 ? 47.836  142.859 106.021 1.00 15.24 ? 144  LEU Q CD2 1 
ATOM   18619 N  N   . ALA Q  1 145 ? 45.238  138.264 106.935 1.00 9.70  ? 145  ALA Q N   1 
ATOM   18620 C  CA  . ALA Q  1 145 ? 45.103  136.914 107.468 1.00 9.21  ? 145  ALA Q CA  1 
ATOM   18621 C  C   . ALA Q  1 145 ? 43.770  136.358 107.035 1.00 10.17 ? 145  ALA Q C   1 
ATOM   18622 O  O   . ALA Q  1 145 ? 42.833  137.126 106.752 1.00 10.95 ? 145  ALA Q O   1 
ATOM   18623 C  CB  . ALA Q  1 145 ? 45.199  136.896 108.970 1.00 9.37  ? 145  ALA Q CB  1 
ATOM   18624 N  N   . CYS Q  1 146 ? 43.666  135.038 106.968 1.00 9.39  ? 146  CYS Q N   1 
ATOM   18625 C  CA  . CYS Q  1 146 ? 42.410  134.463 106.521 1.00 10.91 ? 146  CYS Q CA  1 
ATOM   18626 C  C   . CYS Q  1 146 ? 42.330  133.059 107.058 1.00 10.47 ? 146  CYS Q C   1 
ATOM   18627 O  O   . CYS Q  1 146 ? 43.330  132.501 107.583 1.00 10.86 ? 146  CYS Q O   1 
ATOM   18628 C  CB  . CYS Q  1 146 ? 42.311  134.455 104.978 1.00 11.41 ? 146  CYS Q CB  1 
ATOM   18629 S  SG  . CYS Q  1 146 ? 43.657  133.496 104.158 1.00 16.40 ? 146  CYS Q SG  1 
ATOM   18630 N  N   . GLY Q  1 147 ? 41.140  132.473 106.949 1.00 11.11 ? 147  GLY Q N   1 
ATOM   18631 C  CA  . GLY Q  1 147 ? 40.985  131.076 107.353 1.00 12.01 ? 147  GLY Q CA  1 
ATOM   18632 C  C   . GLY Q  1 147 ? 39.723  130.535 106.691 1.00 10.92 ? 147  GLY Q C   1 
ATOM   18633 O  O   . GLY Q  1 147 ? 38.866  131.311 106.299 1.00 11.30 ? 147  GLY Q O   1 
ATOM   18634 N  N   . VAL Q  1 148 ? 39.628  129.218 106.547 1.00 10.74 ? 148  VAL Q N   1 
ATOM   18635 C  CA  . VAL Q  1 148 ? 38.425  128.606 105.998 1.00 11.10 ? 148  VAL Q CA  1 
ATOM   18636 C  C   . VAL Q  1 148 ? 37.421  128.511 107.147 1.00 12.01 ? 148  VAL Q C   1 
ATOM   18637 O  O   . VAL Q  1 148 ? 37.792  128.123 108.248 1.00 12.34 ? 148  VAL Q O   1 
ATOM   18638 C  CB  . VAL Q  1 148 ? 38.734  127.192 105.422 1.00 11.63 ? 148  VAL Q CB  1 
ATOM   18639 C  CG1 . VAL Q  1 148 ? 37.454  126.551 104.821 1.00 11.50 ? 148  VAL Q CG1 1 
ATOM   18640 C  CG2 . VAL Q  1 148 ? 39.822  127.314 104.343 1.00 9.38  ? 148  VAL Q CG2 1 
ATOM   18641 N  N   . ILE Q  1 149 ? 36.158  128.855 106.890 1.00 12.43 ? 149  ILE Q N   1 
ATOM   18642 C  CA  . ILE Q  1 149 ? 35.123  128.786 107.913 1.00 11.75 ? 149  ILE Q CA  1 
ATOM   18643 C  C   . ILE Q  1 149 ? 34.640  127.325 107.992 1.00 12.53 ? 149  ILE Q C   1 
ATOM   18644 O  O   . ILE Q  1 149 ? 34.095  126.786 107.020 1.00 11.99 ? 149  ILE Q O   1 
ATOM   18645 C  CB  . ILE Q  1 149 ? 33.971  129.719 107.527 1.00 12.05 ? 149  ILE Q CB  1 
ATOM   18646 C  CG1 . ILE Q  1 149 ? 34.471  131.178 107.516 1.00 12.20 ? 149  ILE Q CG1 1 
ATOM   18647 C  CG2 . ILE Q  1 149 ? 32.834  129.573 108.503 1.00 10.73 ? 149  ILE Q CG2 1 
ATOM   18648 C  CD1 . ILE Q  1 149 ? 33.534  132.127 106.671 1.00 11.84 ? 149  ILE Q CD1 1 
ATOM   18649 N  N   . GLY Q  1 150 ? 34.848  126.705 109.145 1.00 11.69 ? 150  GLY Q N   1 
ATOM   18650 C  CA  . GLY Q  1 150 ? 34.514  125.307 109.313 1.00 12.33 ? 150  GLY Q CA  1 
ATOM   18651 C  C   . GLY Q  1 150 ? 33.442  125.104 110.373 1.00 13.58 ? 150  GLY Q C   1 
ATOM   18652 O  O   . GLY Q  1 150 ? 33.228  125.955 111.262 1.00 12.54 ? 150  GLY Q O   1 
ATOM   18653 N  N   . ILE Q  1 151 ? 32.754  123.980 110.253 1.00 13.04 ? 151  ILE Q N   1 
ATOM   18654 C  CA  . ILE Q  1 151 ? 31.698  123.600 111.203 1.00 14.11 ? 151  ILE Q CA  1 
ATOM   18655 C  C   . ILE Q  1 151 ? 32.307  123.378 112.581 1.00 14.54 ? 151  ILE Q C   1 
ATOM   18656 O  O   . ILE Q  1 151 ? 33.310  122.692 112.699 1.00 14.82 ? 151  ILE Q O   1 
ATOM   18657 C  CB  . ILE Q  1 151 ? 31.008  122.301 110.732 1.00 13.74 ? 151  ILE Q CB  1 
ATOM   18658 C  CG1 . ILE Q  1 151 ? 30.297  122.536 109.395 1.00 13.19 ? 151  ILE Q CG1 1 
ATOM   18659 C  CG2 . ILE Q  1 151 ? 30.005  121.811 111.792 1.00 13.77 ? 151  ILE Q CG2 1 
ATOM   18660 C  CD1 . ILE Q  1 151 ? 29.923  121.272 108.617 1.00 11.20 ? 151  ILE Q CD1 1 
ATOM   18661 N  N   . ALA Q  1 152 ? 31.689  123.932 113.620 1.00 15.79 ? 152  ALA Q N   1 
ATOM   18662 C  CA  . ALA Q  1 152 ? 32.189  123.791 114.982 1.00 16.73 ? 152  ALA Q CA  1 
ATOM   18663 C  C   . ALA Q  1 152 ? 31.228  123.021 115.863 1.00 19.01 ? 152  ALA Q C   1 
ATOM   18664 O  O   . ALA Q  1 152 ? 30.037  122.886 115.540 1.00 19.13 ? 152  ALA Q O   1 
ATOM   18665 C  CB  . ALA Q  1 152 ? 32.461  125.144 115.604 1.00 16.68 ? 152  ALA Q CB  1 
ATOM   18666 N  N   . GLN Q  1 153 ? 31.767  122.538 116.978 1.00 20.29 ? 153  GLN Q N   1 
ATOM   18667 C  CA  . GLN Q  1 153 ? 31.010  121.784 117.965 1.00 23.23 ? 153  GLN Q CA  1 
ATOM   18668 C  C   . GLN Q  1 153 ? 30.274  122.728 118.897 1.00 24.11 ? 153  GLN Q C   1 
ATOM   18669 O  O   . GLN Q  1 153 ? 30.767  123.819 119.186 1.00 25.06 ? 153  GLN Q O   1 
ATOM   18670 C  CB  . GLN Q  1 153 ? 31.950  120.899 118.780 1.00 23.06 ? 153  GLN Q CB  1 
ATOM   18671 C  CG  . GLN Q  1 153 ? 31.392  120.456 120.133 1.00 25.89 ? 153  GLN Q CG  1 
ATOM   18672 C  CD  . GLN Q  1 153 ? 32.235  119.380 120.783 1.00 29.23 ? 153  GLN Q CD  1 
ATOM   18673 O  OE1 . GLN Q  1 153 ? 33.218  119.675 121.473 1.00 31.48 ? 153  GLN Q OE1 1 
ATOM   18674 N  NE2 . GLN Q  1 153 ? 31.859  118.128 120.561 1.00 28.33 ? 153  GLN Q NE2 1 
ATOM   18675 O  OXT . GLN Q  1 153 ? 29.187  122.394 119.381 1.00 25.76 ? 153  GLN Q OXT 1 
ATOM   18676 N  N   . ALA R  1 1   ? 58.496  128.515 43.658  1.00 40.35 ? 1    ALA S N   1 
ATOM   18677 C  CA  . ALA R  1 1   ? 58.595  127.952 42.280  1.00 40.40 ? 1    ALA S CA  1 
ATOM   18678 C  C   . ALA R  1 1   ? 57.448  128.429 41.401  1.00 40.32 ? 1    ALA S C   1 
ATOM   18679 O  O   . ALA R  1 1   ? 56.285  128.388 41.807  1.00 40.48 ? 1    ALA S O   1 
ATOM   18680 C  CB  . ALA R  1 1   ? 58.617  126.426 42.328  1.00 40.49 ? 1    ALA S CB  1 
ATOM   18681 N  N   . THR R  1 2   ? 57.778  128.894 40.202  1.00 40.00 ? 2    THR S N   1 
ATOM   18682 C  CA  . THR R  1 2   ? 56.753  129.296 39.249  1.00 39.74 ? 2    THR S CA  1 
ATOM   18683 C  C   . THR R  1 2   ? 56.325  128.048 38.484  1.00 39.35 ? 2    THR S C   1 
ATOM   18684 O  O   . THR R  1 2   ? 57.155  127.207 38.126  1.00 39.32 ? 2    THR S O   1 
ATOM   18685 C  CB  . THR R  1 2   ? 57.277  130.395 38.303  1.00 39.87 ? 2    THR S CB  1 
ATOM   18686 O  OG1 . THR R  1 2   ? 56.564  130.344 37.060  1.00 40.18 ? 2    THR S OG1 1 
ATOM   18687 C  CG2 . THR R  1 2   ? 58.721  130.109 37.889  1.00 40.31 ? 2    THR S CG2 1 
ATOM   18688 N  N   . LYS R  1 3   ? 55.027  127.907 38.256  1.00 38.74 ? 3    LYS S N   1 
ATOM   18689 C  CA  . LYS R  1 3   ? 54.524  126.719 37.587  1.00 38.12 ? 3    LYS S CA  1 
ATOM   18690 C  C   . LYS R  1 3   ? 53.764  127.093 36.332  1.00 37.78 ? 3    LYS S C   1 
ATOM   18691 O  O   . LYS R  1 3   ? 53.167  128.165 36.259  1.00 37.65 ? 3    LYS S O   1 
ATOM   18692 C  CB  . LYS R  1 3   ? 53.612  125.929 38.527  1.00 38.35 ? 3    LYS S CB  1 
ATOM   18693 C  CG  . LYS R  1 3   ? 54.234  125.636 39.880  1.00 38.23 ? 3    LYS S CG  1 
ATOM   18694 C  CD  . LYS R  1 3   ? 53.186  125.256 40.915  1.00 38.89 ? 3    LYS S CD  1 
ATOM   18695 C  CE  . LYS R  1 3   ? 53.797  125.119 42.313  1.00 38.39 ? 3    LYS S CE  1 
ATOM   18696 N  NZ  . LYS R  1 3   ? 52.764  125.107 43.386  1.00 37.86 ? 3    LYS S NZ  1 
ATOM   18697 N  N   . ALA R  1 4   ? 53.794  126.201 35.349  1.00 37.18 ? 4    ALA S N   1 
ATOM   18698 C  CA  . ALA R  1 4   ? 53.081  126.412 34.095  1.00 36.65 ? 4    ALA S CA  1 
ATOM   18699 C  C   . ALA R  1 4   ? 52.354  125.142 33.670  1.00 36.37 ? 4    ALA S C   1 
ATOM   18700 O  O   . ALA R  1 4   ? 52.682  124.038 34.117  1.00 35.89 ? 4    ALA S O   1 
ATOM   18701 C  CB  . ALA R  1 4   ? 54.033  126.864 33.015  1.00 36.74 ? 4    ALA S CB  1 
ATOM   18702 N  N   . VAL R  1 5   ? 51.367  125.302 32.797  1.00 36.06 ? 5    VAL S N   1 
ATOM   18703 C  CA  . VAL R  1 5   ? 50.573  124.169 32.348  1.00 36.02 ? 5    VAL S CA  1 
ATOM   18704 C  C   . VAL R  1 5   ? 50.165  124.299 30.884  1.00 36.07 ? 5    VAL S C   1 
ATOM   18705 O  O   . VAL R  1 5   ? 49.973  125.407 30.377  1.00 35.52 ? 5    VAL S O   1 
ATOM   18706 C  CB  . VAL R  1 5   ? 49.304  124.005 33.210  1.00 35.98 ? 5    VAL S CB  1 
ATOM   18707 C  CG1 . VAL R  1 5   ? 48.278  125.085 32.871  1.00 35.91 ? 5    VAL S CG1 1 
ATOM   18708 C  CG2 . VAL R  1 5   ? 48.712  122.618 33.027  1.00 35.85 ? 5    VAL S CG2 1 
ATOM   18709 N  N   . CYS R  1 6   ? 50.036  123.158 30.213  1.00 36.32 ? 6    CYS S N   1 
ATOM   18710 C  CA  . CYS R  1 6   ? 49.625  123.144 28.815  1.00 36.89 ? 6    CYS S CA  1 
ATOM   18711 C  C   . CYS R  1 6   ? 48.657  122.001 28.502  1.00 37.47 ? 6    CYS S C   1 
ATOM   18712 O  O   . CYS R  1 6   ? 48.948  120.831 28.762  1.00 37.58 ? 6    CYS S O   1 
ATOM   18713 C  CB  . CYS R  1 6   ? 50.848  123.078 27.893  1.00 36.79 ? 6    CYS S CB  1 
ATOM   18714 S  SG  . CYS R  1 6   ? 50.448  123.198 26.130  1.00 35.64 ? 6    CYS S SG  1 
ATOM   18715 N  N   . VAL R  1 7   ? 47.499  122.364 27.957  1.00 38.23 ? 7    VAL S N   1 
ATOM   18716 C  CA  . VAL R  1 7   ? 46.474  121.412 27.541  1.00 38.69 ? 7    VAL S CA  1 
ATOM   18717 C  C   . VAL R  1 7   ? 46.593  121.223 26.028  1.00 39.25 ? 7    VAL S C   1 
ATOM   18718 O  O   . VAL R  1 7   ? 46.278  122.132 25.252  1.00 39.20 ? 7    VAL S O   1 
ATOM   18719 C  CB  . VAL R  1 7   ? 45.059  121.944 27.877  1.00 38.82 ? 7    VAL S CB  1 
ATOM   18720 C  CG1 . VAL R  1 7   ? 43.981  120.935 27.475  1.00 38.56 ? 7    VAL S CG1 1 
ATOM   18721 C  CG2 . VAL R  1 7   ? 44.952  122.305 29.368  1.00 38.66 ? 7    VAL S CG2 1 
ATOM   18722 N  N   . LEU R  1 8   ? 47.056  120.049 25.607  1.00 39.70 ? 8    LEU S N   1 
ATOM   18723 C  CA  . LEU R  1 8   ? 47.239  119.777 24.184  1.00 40.14 ? 8    LEU S CA  1 
ATOM   18724 C  C   . LEU R  1 8   ? 45.987  119.201 23.520  1.00 40.59 ? 8    LEU S C   1 
ATOM   18725 O  O   . LEU R  1 8   ? 45.415  118.208 23.988  1.00 40.25 ? 8    LEU S O   1 
ATOM   18726 C  CB  . LEU R  1 8   ? 48.433  118.848 23.956  1.00 40.17 ? 8    LEU S CB  1 
ATOM   18727 C  CG  . LEU R  1 8   ? 49.800  119.348 24.415  1.00 40.35 ? 8    LEU S CG  1 
ATOM   18728 C  CD1 . LEU R  1 8   ? 50.779  118.181 24.466  1.00 42.34 ? 8    LEU S CD1 1 
ATOM   18729 C  CD2 . LEU R  1 8   ? 50.316  120.432 23.499  1.00 41.08 ? 8    LEU S CD2 1 
ATOM   18730 N  N   . LYS R  1 9   ? 45.570  119.836 22.426  1.00 41.06 ? 9    LYS S N   1 
ATOM   18731 C  CA  . LYS R  1 9   ? 44.412  119.398 21.650  1.00 41.97 ? 9    LYS S CA  1 
ATOM   18732 C  C   . LYS R  1 9   ? 44.628  119.722 20.173  1.00 42.23 ? 9    LYS S C   1 
ATOM   18733 O  O   . LYS R  1 9   ? 45.374  120.643 19.842  1.00 42.06 ? 9    LYS S O   1 
ATOM   18734 C  CB  . LYS R  1 9   ? 43.123  120.062 22.157  1.00 42.06 ? 9    LYS S CB  1 
ATOM   18735 C  CG  . LYS R  1 9   ? 42.687  119.600 23.544  1.00 43.40 ? 9    LYS S CG  1 
ATOM   18736 C  CD  . LYS R  1 9   ? 41.273  120.052 23.916  1.00 45.10 ? 9    LYS S CD  1 
ATOM   18737 C  CE  . LYS R  1 9   ? 40.871  119.456 25.276  1.00 46.75 ? 9    LYS S CE  1 
ATOM   18738 N  NZ  . LYS R  1 9   ? 39.507  119.852 25.741  1.00 47.68 ? 9    LYS S NZ  1 
ATOM   18739 N  N   . GLY R  1 10  ? 43.980  118.959 19.293  1.00 42.82 ? 10   GLY S N   1 
ATOM   18740 C  CA  . GLY R  1 10  ? 44.093  119.171 17.857  1.00 43.42 ? 10   GLY S CA  1 
ATOM   18741 C  C   . GLY R  1 10  ? 42.871  118.705 17.084  1.00 43.99 ? 10   GLY S C   1 
ATOM   18742 O  O   . GLY R  1 10  ? 41.795  118.528 17.664  1.00 44.21 ? 10   GLY S O   1 
ATOM   18743 N  N   . ASP R  1 11  ? 43.036  118.501 15.777  1.00 44.32 ? 11   ASP S N   1 
ATOM   18744 C  CA  . ASP R  1 11  ? 41.940  118.061 14.902  1.00 44.81 ? 11   ASP S CA  1 
ATOM   18745 C  C   . ASP R  1 11  ? 41.601  116.587 15.074  1.00 44.55 ? 11   ASP S C   1 
ATOM   18746 O  O   . ASP R  1 11  ? 40.473  116.161 14.798  1.00 44.76 ? 11   ASP S O   1 
ATOM   18747 C  CB  . ASP R  1 11  ? 42.289  118.288 13.426  1.00 45.29 ? 11   ASP S CB  1 
ATOM   18748 C  CG  . ASP R  1 11  ? 42.348  119.753 13.052  1.00 46.80 ? 11   ASP S CG  1 
ATOM   18749 O  OD1 . ASP R  1 11  ? 41.508  120.535 13.558  1.00 47.71 ? 11   ASP S OD1 1 
ATOM   18750 O  OD2 . ASP R  1 11  ? 43.200  120.205 12.251  1.00 48.24 ? 11   ASP S OD2 1 
ATOM   18751 N  N   . GLY R  1 12  ? 42.586  115.807 15.506  1.00 44.08 ? 12   GLY S N   1 
ATOM   18752 C  CA  . GLY R  1 12  ? 42.406  114.380 15.671  1.00 43.51 ? 12   GLY S CA  1 
ATOM   18753 C  C   . GLY R  1 12  ? 42.207  113.962 17.113  1.00 43.20 ? 12   GLY S C   1 
ATOM   18754 O  O   . GLY R  1 12  ? 41.734  114.738 17.939  1.00 43.17 ? 12   GLY S O   1 
ATOM   18755 N  N   . PRO R  1 13  ? 42.598  112.731 17.417  1.00 42.85 ? 13   PRO S N   1 
ATOM   18756 C  CA  . PRO R  1 13  ? 42.407  112.155 18.751  1.00 42.55 ? 13   PRO S CA  1 
ATOM   18757 C  C   . PRO R  1 13  ? 43.564  112.381 19.726  1.00 41.95 ? 13   PRO S C   1 
ATOM   18758 O  O   . PRO R  1 13  ? 43.509  111.880 20.857  1.00 41.32 ? 13   PRO S O   1 
ATOM   18759 C  CB  . PRO R  1 13  ? 42.271  110.667 18.434  1.00 42.76 ? 13   PRO S CB  1 
ATOM   18760 C  CG  . PRO R  1 13  ? 43.252  110.468 17.285  1.00 42.74 ? 13   PRO S CG  1 
ATOM   18761 C  CD  . PRO R  1 13  ? 43.264  111.783 16.503  1.00 42.91 ? 13   PRO S CD  1 
ATOM   18762 N  N   . VAL R  1 14  ? 44.588  113.116 19.303  1.00 41.42 ? 14   VAL S N   1 
ATOM   18763 C  CA  . VAL R  1 14  ? 45.711  113.387 20.187  1.00 41.18 ? 14   VAL S CA  1 
ATOM   18764 C  C   . VAL R  1 14  ? 45.351  114.431 21.233  1.00 41.32 ? 14   VAL S C   1 
ATOM   18765 O  O   . VAL R  1 14  ? 44.976  115.561 20.912  1.00 40.96 ? 14   VAL S O   1 
ATOM   18766 C  CB  . VAL R  1 14  ? 46.963  113.815 19.433  1.00 41.03 ? 14   VAL S CB  1 
ATOM   18767 C  CG1 . VAL R  1 14  ? 48.104  114.010 20.419  1.00 40.29 ? 14   VAL S CG1 1 
ATOM   18768 C  CG2 . VAL R  1 14  ? 47.314  112.765 18.407  1.00 40.64 ? 14   VAL S CG2 1 
ATOM   18769 N  N   . GLN R  1 15  ? 45.476  114.024 22.488  1.00 41.41 ? 15   GLN S N   1 
ATOM   18770 C  CA  . GLN R  1 15  ? 45.121  114.850 23.629  1.00 41.86 ? 15   GLN S CA  1 
ATOM   18771 C  C   . GLN R  1 15  ? 46.134  114.641 24.737  1.00 41.58 ? 15   GLN S C   1 
ATOM   18772 O  O   . GLN R  1 15  ? 46.648  113.536 24.917  1.00 41.37 ? 15   GLN S O   1 
ATOM   18773 C  CB  . GLN R  1 15  ? 43.760  114.427 24.173  1.00 42.07 ? 15   GLN S CB  1 
ATOM   18774 C  CG  . GLN R  1 15  ? 42.555  115.146 23.614  1.00 43.72 ? 15   GLN S CG  1 
ATOM   18775 C  CD  . GLN R  1 15  ? 41.306  114.806 24.403  1.00 45.28 ? 15   GLN S CD  1 
ATOM   18776 O  OE1 . GLN R  1 15  ? 41.037  113.630 24.668  1.00 45.91 ? 15   GLN S OE1 1 
ATOM   18777 N  NE2 . GLN R  1 15  ? 40.553  115.829 24.802  1.00 46.68 ? 15   GLN S NE2 1 
ATOM   18778 N  N   . GLY R  1 16  ? 46.402  115.699 25.493  1.00 41.41 ? 16   GLY S N   1 
ATOM   18779 C  CA  . GLY R  1 16  ? 47.323  115.605 26.602  1.00 41.33 ? 16   GLY S CA  1 
ATOM   18780 C  C   . GLY R  1 16  ? 47.310  116.791 27.542  1.00 41.04 ? 16   GLY S C   1 
ATOM   18781 O  O   . GLY R  1 16  ? 46.681  117.820 27.288  1.00 40.83 ? 16   GLY S O   1 
ATOM   18782 N  N   . ILE R  1 17  ? 48.004  116.619 28.658  1.00 40.67 ? 17   ILE S N   1 
ATOM   18783 C  CA  . ILE R  1 17  ? 48.204  117.687 29.618  1.00 40.56 ? 17   ILE S CA  1 
ATOM   18784 C  C   . ILE R  1 17  ? 49.668  117.616 30.021  1.00 40.34 ? 17   ILE S C   1 
ATOM   18785 O  O   . ILE R  1 17  ? 50.172  116.539 30.346  1.00 40.33 ? 17   ILE S O   1 
ATOM   18786 C  CB  . ILE R  1 17  ? 47.280  117.521 30.843  1.00 40.69 ? 17   ILE S CB  1 
ATOM   18787 C  CG1 . ILE R  1 17  ? 45.827  117.831 30.463  1.00 40.65 ? 17   ILE S CG1 1 
ATOM   18788 C  CG2 . ILE R  1 17  ? 47.742  118.419 31.988  1.00 40.75 ? 17   ILE S CG2 1 
ATOM   18789 C  CD1 . ILE R  1 17  ? 44.847  117.673 31.614  1.00 41.83 ? 17   ILE S CD1 1 
ATOM   18790 N  N   . ILE R  1 18  ? 50.346  118.758 29.976  1.00 40.29 ? 18   ILE S N   1 
ATOM   18791 C  CA  . ILE R  1 18  ? 51.760  118.842 30.315  1.00 40.18 ? 18   ILE S CA  1 
ATOM   18792 C  C   . ILE R  1 18  ? 51.991  119.926 31.359  1.00 40.40 ? 18   ILE S C   1 
ATOM   18793 O  O   . ILE R  1 18  ? 51.478  121.038 31.229  1.00 40.35 ? 18   ILE S O   1 
ATOM   18794 C  CB  . ILE R  1 18  ? 52.615  119.148 29.049  1.00 40.16 ? 18   ILE S CB  1 
ATOM   18795 C  CG1 . ILE R  1 18  ? 52.485  118.030 28.009  1.00 39.94 ? 18   ILE S CG1 1 
ATOM   18796 C  CG2 . ILE R  1 18  ? 54.073  119.348 29.428  1.00 39.44 ? 18   ILE S CG2 1 
ATOM   18797 C  CD1 . ILE R  1 18  ? 53.187  116.724 28.397  1.00 39.90 ? 18   ILE S CD1 1 
ATOM   18798 N  N   . ASN R  1 19  ? 52.776  119.594 32.382  1.00 40.65 ? 19   ASN S N   1 
ATOM   18799 C  CA  . ASN R  1 19  ? 53.093  120.521 33.460  1.00 40.88 ? 19   ASN S CA  1 
ATOM   18800 C  C   . ASN R  1 19  ? 54.532  120.994 33.391  1.00 41.02 ? 19   ASN S C   1 
ATOM   18801 O  O   . ASN R  1 19  ? 55.402  120.269 32.924  1.00 40.98 ? 19   ASN S O   1 
ATOM   18802 C  CB  . ASN R  1 19  ? 52.874  119.847 34.815  1.00 41.03 ? 19   ASN S CB  1 
ATOM   18803 C  CG  . ASN R  1 19  ? 51.537  119.150 34.906  1.00 41.41 ? 19   ASN S CG  1 
ATOM   18804 O  OD1 . ASN R  1 19  ? 51.458  117.921 34.839  1.00 41.73 ? 19   ASN S OD1 1 
ATOM   18805 N  ND2 . ASN R  1 19  ? 50.471  119.934 35.055  1.00 41.09 ? 19   ASN S ND2 1 
ATOM   18806 N  N   . PHE R  1 20  ? 54.775  122.211 33.859  1.00 41.43 ? 20   PHE S N   1 
ATOM   18807 C  CA  . PHE R  1 20  ? 56.118  122.765 33.906  1.00 42.00 ? 20   PHE S CA  1 
ATOM   18808 C  C   . PHE R  1 20  ? 56.371  123.287 35.312  1.00 42.70 ? 20   PHE S C   1 
ATOM   18809 O  O   . PHE R  1 20  ? 55.503  123.925 35.907  1.00 42.44 ? 20   PHE S O   1 
ATOM   18810 C  CB  . PHE R  1 20  ? 56.264  123.939 32.941  1.00 42.14 ? 20   PHE S CB  1 
ATOM   18811 C  CG  . PHE R  1 20  ? 55.972  123.608 31.498  1.00 42.25 ? 20   PHE S CG  1 
ATOM   18812 C  CD1 . PHE R  1 20  ? 54.664  123.446 31.053  1.00 42.32 ? 20   PHE S CD1 1 
ATOM   18813 C  CD2 . PHE R  1 20  ? 57.004  123.508 30.577  1.00 42.42 ? 20   PHE S CD2 1 
ATOM   18814 C  CE1 . PHE R  1 20  ? 54.396  123.165 29.722  1.00 42.43 ? 20   PHE S CE1 1 
ATOM   18815 C  CE2 . PHE R  1 20  ? 56.738  123.231 29.246  1.00 42.20 ? 20   PHE S CE2 1 
ATOM   18816 C  CZ  . PHE R  1 20  ? 55.432  123.059 28.822  1.00 41.86 ? 20   PHE S CZ  1 
ATOM   18817 N  N   . GLU R  1 21  ? 57.556  123.023 35.846  1.00 43.47 ? 21   GLU S N   1 
ATOM   18818 C  CA  . GLU R  1 21  ? 57.909  123.562 37.148  1.00 44.47 ? 21   GLU S CA  1 
ATOM   18819 C  C   . GLU R  1 21  ? 59.372  123.978 37.196  1.00 45.06 ? 21   GLU S C   1 
ATOM   18820 O  O   . GLU R  1 21  ? 60.265  123.193 36.881  1.00 44.79 ? 21   GLU S O   1 
ATOM   18821 C  CB  . GLU R  1 21  ? 57.596  122.578 38.282  1.00 44.55 ? 21   GLU S CB  1 
ATOM   18822 C  CG  . GLU R  1 21  ? 57.920  123.141 39.661  1.00 45.20 ? 21   GLU S CG  1 
ATOM   18823 C  CD  . GLU R  1 21  ? 57.666  122.161 40.796  1.00 46.69 ? 21   GLU S CD  1 
ATOM   18824 O  OE1 . GLU R  1 21  ? 58.621  121.467 41.211  1.00 47.21 ? 21   GLU S OE1 1 
ATOM   18825 O  OE2 . GLU R  1 21  ? 56.519  122.094 41.290  1.00 47.02 ? 21   GLU S OE2 1 
ATOM   18826 N  N   . GLN R  1 22  ? 59.597  125.230 37.581  1.00 45.94 ? 22   GLN S N   1 
ATOM   18827 C  CA  . GLN R  1 22  ? 60.939  125.772 37.728  1.00 46.87 ? 22   GLN S CA  1 
ATOM   18828 C  C   . GLN R  1 22  ? 61.104  126.266 39.161  1.00 47.62 ? 22   GLN S C   1 
ATOM   18829 O  O   . GLN R  1 22  ? 60.556  127.301 39.545  1.00 47.64 ? 22   GLN S O   1 
ATOM   18830 C  CB  . GLN R  1 22  ? 61.166  126.912 36.739  1.00 46.80 ? 22   GLN S CB  1 
ATOM   18831 C  CG  . GLN R  1 22  ? 62.600  127.402 36.679  1.00 46.81 ? 22   GLN S CG  1 
ATOM   18832 C  CD  . GLN R  1 22  ? 62.786  128.523 35.676  1.00 46.49 ? 22   GLN S CD  1 
ATOM   18833 O  OE1 . GLN R  1 22  ? 61.838  129.239 35.362  1.00 46.39 ? 22   GLN S OE1 1 
ATOM   18834 N  NE2 . GLN R  1 22  ? 64.008  128.683 35.178  1.00 46.23 ? 22   GLN S NE2 1 
ATOM   18835 N  N   . LYS R  1 23  ? 61.862  125.515 39.951  1.00 48.62 ? 23   LYS S N   1 
ATOM   18836 C  CA  . LYS R  1 23  ? 62.045  125.822 41.367  1.00 49.56 ? 23   LYS S CA  1 
ATOM   18837 C  C   . LYS R  1 23  ? 62.952  127.013 41.675  1.00 50.04 ? 23   LYS S C   1 
ATOM   18838 O  O   . LYS R  1 23  ? 62.752  127.706 42.676  1.00 50.08 ? 23   LYS S O   1 
ATOM   18839 C  CB  . LYS R  1 23  ? 62.548  124.578 42.099  1.00 49.71 ? 23   LYS S CB  1 
ATOM   18840 C  CG  . LYS R  1 23  ? 61.455  123.563 42.374  1.00 50.71 ? 23   LYS S CG  1 
ATOM   18841 C  CD  . LYS R  1 23  ? 62.028  122.212 42.767  1.00 52.39 ? 23   LYS S CD  1 
ATOM   18842 C  CE  . LYS R  1 23  ? 61.169  121.540 43.839  1.00 53.26 ? 23   LYS S CE  1 
ATOM   18843 N  NZ  . LYS R  1 23  ? 59.702  121.672 43.587  1.00 53.92 ? 23   LYS S NZ  1 
ATOM   18844 N  N   . GLU R  1 24  ? 63.939  127.254 40.819  1.00 50.62 ? 24   GLU S N   1 
ATOM   18845 C  CA  . GLU R  1 24  ? 64.896  128.331 41.042  1.00 51.16 ? 24   GLU S CA  1 
ATOM   18846 C  C   . GLU R  1 24  ? 64.993  129.223 39.808  1.00 51.33 ? 24   GLU S C   1 
ATOM   18847 O  O   . GLU R  1 24  ? 64.776  128.766 38.684  1.00 51.42 ? 24   GLU S O   1 
ATOM   18848 C  CB  . GLU R  1 24  ? 66.275  127.741 41.353  1.00 51.24 ? 24   GLU S CB  1 
ATOM   18849 C  CG  . GLU R  1 24  ? 66.848  128.130 42.707  1.00 52.06 ? 24   GLU S CG  1 
ATOM   18850 C  CD  . GLU R  1 24  ? 66.671  127.040 43.753  1.00 52.75 ? 24   GLU S CD  1 
ATOM   18851 O  OE1 . GLU R  1 24  ? 66.718  125.847 43.380  1.00 53.22 ? 24   GLU S OE1 1 
ATOM   18852 O  OE2 . GLU R  1 24  ? 66.489  127.369 44.946  1.00 52.48 ? 24   GLU S OE2 1 
ATOM   18853 N  N   . SER R  1 25  ? 65.327  130.493 40.015  1.00 51.54 ? 25   SER S N   1 
ATOM   18854 C  CA  . SER R  1 25  ? 65.480  131.423 38.902  1.00 51.71 ? 25   SER S CA  1 
ATOM   18855 C  C   . SER R  1 25  ? 66.548  130.943 37.923  1.00 51.67 ? 25   SER S C   1 
ATOM   18856 O  O   . SER R  1 25  ? 67.679  130.652 38.318  1.00 51.76 ? 25   SER S O   1 
ATOM   18857 C  CB  . SER R  1 25  ? 65.844  132.818 39.405  1.00 51.84 ? 25   SER S CB  1 
ATOM   18858 O  OG  . SER R  1 25  ? 66.179  133.663 38.317  1.00 52.26 ? 25   SER S OG  1 
ATOM   18859 N  N   . ASN R  1 26  ? 66.177  130.857 36.649  1.00 51.57 ? 26   ASN S N   1 
ATOM   18860 C  CA  . ASN R  1 26  ? 67.102  130.426 35.604  1.00 51.40 ? 26   ASN S CA  1 
ATOM   18861 C  C   . ASN R  1 26  ? 67.552  128.969 35.767  1.00 51.04 ? 26   ASN S C   1 
ATOM   18862 O  O   . ASN R  1 26  ? 68.427  128.497 35.041  1.00 51.16 ? 26   ASN S O   1 
ATOM   18863 C  CB  . ASN R  1 26  ? 68.312  131.366 35.542  1.00 51.66 ? 26   ASN S CB  1 
ATOM   18864 C  CG  . ASN R  1 26  ? 69.118  131.206 34.265  1.00 52.09 ? 26   ASN S CG  1 
ATOM   18865 O  OD1 . ASN R  1 26  ? 68.568  130.922 33.201  1.00 52.89 ? 26   ASN S OD1 1 
ATOM   18866 N  ND2 . ASN R  1 26  ? 70.430  131.393 34.367  1.00 52.68 ? 26   ASN S ND2 1 
ATOM   18867 N  N   . GLY R  1 27  ? 66.944  128.258 36.714  1.00 50.47 ? 27   GLY S N   1 
ATOM   18868 C  CA  . GLY R  1 27  ? 67.277  126.863 36.958  1.00 49.62 ? 27   GLY S CA  1 
ATOM   18869 C  C   . GLY R  1 27  ? 66.560  125.896 36.027  1.00 48.96 ? 27   GLY S C   1 
ATOM   18870 O  O   . GLY R  1 27  ? 65.798  126.314 35.151  1.00 49.14 ? 27   GLY S O   1 
ATOM   18871 N  N   . PRO R  1 28  ? 66.806  124.600 36.211  1.00 48.21 ? 28   PRO S N   1 
ATOM   18872 C  CA  . PRO R  1 28  ? 66.194  123.557 35.377  1.00 47.48 ? 28   PRO S CA  1 
ATOM   18873 C  C   . PRO R  1 28  ? 64.672  123.551 35.450  1.00 46.72 ? 28   PRO S C   1 
ATOM   18874 O  O   . PRO R  1 28  ? 64.107  123.729 36.532  1.00 46.50 ? 28   PRO S O   1 
ATOM   18875 C  CB  . PRO R  1 28  ? 66.727  122.259 35.991  1.00 47.63 ? 28   PRO S CB  1 
ATOM   18876 C  CG  . PRO R  1 28  ? 67.958  122.654 36.729  1.00 47.98 ? 28   PRO S CG  1 
ATOM   18877 C  CD  . PRO R  1 28  ? 67.710  124.041 37.231  1.00 48.27 ? 28   PRO S CD  1 
ATOM   18878 N  N   . VAL R  1 29  ? 64.018  123.350 34.309  1.00 45.67 ? 29   VAL S N   1 
ATOM   18879 C  CA  . VAL R  1 29  ? 62.565  123.267 34.286  1.00 44.71 ? 29   VAL S CA  1 
ATOM   18880 C  C   . VAL R  1 29  ? 62.118  121.822 34.113  1.00 44.23 ? 29   VAL S C   1 
ATOM   18881 O  O   . VAL R  1 29  ? 62.497  121.152 33.150  1.00 43.84 ? 29   VAL S O   1 
ATOM   18882 C  CB  . VAL R  1 29  ? 61.944  124.119 33.167  1.00 44.67 ? 29   VAL S CB  1 
ATOM   18883 C  CG1 . VAL R  1 29  ? 60.435  123.869 33.082  1.00 44.42 ? 29   VAL S CG1 1 
ATOM   18884 C  CG2 . VAL R  1 29  ? 62.241  125.592 33.391  1.00 44.60 ? 29   VAL S CG2 1 
ATOM   18885 N  N   . LYS R  1 30  ? 61.317  121.342 35.059  1.00 43.47 ? 30   LYS S N   1 
ATOM   18886 C  CA  . LYS R  1 30  ? 60.779  119.993 34.976  1.00 42.87 ? 30   LYS S CA  1 
ATOM   18887 C  C   . LYS R  1 30  ? 59.531  120.009 34.109  1.00 42.24 ? 30   LYS S C   1 
ATOM   18888 O  O   . LYS R  1 30  ? 58.627  120.828 34.306  1.00 42.03 ? 30   LYS S O   1 
ATOM   18889 C  CB  . LYS R  1 30  ? 60.474  119.422 36.370  1.00 43.04 ? 30   LYS S CB  1 
ATOM   18890 C  CG  . LYS R  1 30  ? 61.702  119.299 37.261  1.00 43.81 ? 30   LYS S CG  1 
ATOM   18891 C  CD  . LYS R  1 30  ? 61.379  118.718 38.644  1.00 46.08 ? 30   LYS S CD  1 
ATOM   18892 C  CE  . LYS R  1 30  ? 61.893  117.287 38.790  1.00 46.80 ? 30   LYS S CE  1 
ATOM   18893 N  NZ  . LYS R  1 30  ? 61.763  116.784 40.189  1.00 47.07 ? 30   LYS S NZ  1 
ATOM   18894 N  N   . VAL R  1 31  ? 59.513  119.118 33.123  1.00 41.48 ? 31   VAL S N   1 
ATOM   18895 C  CA  . VAL R  1 31  ? 58.383  118.972 32.221  1.00 40.50 ? 31   VAL S CA  1 
ATOM   18896 C  C   . VAL R  1 31  ? 57.836  117.546 32.340  1.00 40.18 ? 31   VAL S C   1 
ATOM   18897 O  O   . VAL R  1 31  ? 58.574  116.575 32.181  1.00 40.27 ? 31   VAL S O   1 
ATOM   18898 C  CB  . VAL R  1 31  ? 58.797  119.285 30.777  1.00 40.50 ? 31   VAL S CB  1 
ATOM   18899 C  CG1 . VAL R  1 31  ? 57.588  119.258 29.859  1.00 39.82 ? 31   VAL S CG1 1 
ATOM   18900 C  CG2 . VAL R  1 31  ? 59.485  120.641 30.725  1.00 40.23 ? 31   VAL S CG2 1 
ATOM   18901 N  N   . TRP R  1 32  ? 56.550  117.421 32.648  1.00 39.63 ? 32   TRP S N   1 
ATOM   18902 C  CA  . TRP R  1 32  ? 55.944  116.108 32.838  1.00 39.08 ? 32   TRP S CA  1 
ATOM   18903 C  C   . TRP R  1 32  ? 54.435  116.119 32.623  1.00 38.43 ? 32   TRP S C   1 
ATOM   18904 O  O   . TRP R  1 32  ? 53.765  117.127 32.850  1.00 38.24 ? 32   TRP S O   1 
ATOM   18905 C  CB  . TRP R  1 32  ? 56.258  115.561 34.242  1.00 39.43 ? 32   TRP S CB  1 
ATOM   18906 C  CG  . TRP R  1 32  ? 55.359  116.098 35.331  1.00 40.13 ? 32   TRP S CG  1 
ATOM   18907 C  CD1 . TRP R  1 32  ? 54.254  115.485 35.861  1.00 41.39 ? 32   TRP S CD1 1 
ATOM   18908 C  CD2 . TRP R  1 32  ? 55.489  117.347 36.024  1.00 41.19 ? 32   TRP S CD2 1 
ATOM   18909 N  NE1 . TRP R  1 32  ? 53.693  116.275 36.837  1.00 41.63 ? 32   TRP S NE1 1 
ATOM   18910 C  CE2 . TRP R  1 32  ? 54.432  117.424 36.960  1.00 42.05 ? 32   TRP S CE2 1 
ATOM   18911 C  CE3 . TRP R  1 32  ? 56.399  118.410 35.958  1.00 41.71 ? 32   TRP S CE3 1 
ATOM   18912 C  CZ2 . TRP R  1 32  ? 54.257  118.520 37.810  1.00 42.09 ? 32   TRP S CZ2 1 
ATOM   18913 C  CZ3 . TRP R  1 32  ? 56.224  119.496 36.800  1.00 42.06 ? 32   TRP S CZ3 1 
ATOM   18914 C  CH2 . TRP R  1 32  ? 55.163  119.541 37.715  1.00 42.58 ? 32   TRP S CH2 1 
ATOM   18915 N  N   . GLY R  1 33  ? 53.909  114.974 32.203  1.00 37.68 ? 33   GLY S N   1 
ATOM   18916 C  CA  . GLY R  1 33  ? 52.491  114.829 31.953  1.00 36.86 ? 33   GLY S CA  1 
ATOM   18917 C  C   . GLY R  1 33  ? 52.226  113.621 31.082  1.00 36.28 ? 33   GLY S C   1 
ATOM   18918 O  O   . GLY R  1 33  ? 53.031  112.693 31.029  1.00 36.39 ? 33   GLY S O   1 
ATOM   18919 N  N   . SER R  1 34  ? 51.104  113.645 30.378  1.00 35.68 ? 34   SER S N   1 
ATOM   18920 C  CA  . SER R  1 34  ? 50.713  112.527 29.541  1.00 35.24 ? 34   SER S CA  1 
ATOM   18921 C  C   . SER R  1 34  ? 50.062  112.993 28.241  1.00 34.99 ? 34   SER S C   1 
ATOM   18922 O  O   . SER R  1 34  ? 49.405  114.035 28.208  1.00 34.82 ? 34   SER S O   1 
ATOM   18923 C  CB  . SER R  1 34  ? 49.733  111.644 30.308  1.00 35.47 ? 34   SER S CB  1 
ATOM   18924 O  OG  . SER R  1 34  ? 49.536  110.409 29.644  1.00 36.32 ? 34   SER S OG  1 
ATOM   18925 N  N   . ILE R  1 35  ? 50.253  112.216 27.177  1.00 34.48 ? 35   ILE S N   1 
ATOM   18926 C  CA  . ILE R  1 35  ? 49.624  112.489 25.880  1.00 34.32 ? 35   ILE S CA  1 
ATOM   18927 C  C   . ILE R  1 35  ? 49.055  111.189 25.301  1.00 33.89 ? 35   ILE S C   1 
ATOM   18928 O  O   . ILE R  1 35  ? 49.765  110.183 25.200  1.00 33.91 ? 35   ILE S O   1 
ATOM   18929 C  CB  . ILE R  1 35  ? 50.627  113.101 24.873  1.00 34.21 ? 35   ILE S CB  1 
ATOM   18930 C  CG1 . ILE R  1 35  ? 51.338  114.323 25.449  1.00 34.16 ? 35   ILE S CG1 1 
ATOM   18931 C  CG2 . ILE R  1 35  ? 49.909  113.508 23.600  1.00 34.64 ? 35   ILE S CG2 1 
ATOM   18932 C  CD1 . ILE R  1 35  ? 52.576  114.737 24.630  1.00 34.53 ? 35   ILE S CD1 1 
ATOM   18933 N  N   . LYS R  1 36  ? 47.786  111.216 24.900  1.00 33.24 ? 36   LYS S N   1 
ATOM   18934 C  CA  . LYS R  1 36  ? 47.129  110.026 24.368  1.00 32.65 ? 36   LYS S CA  1 
ATOM   18935 C  C   . LYS R  1 36  ? 46.641  110.189 22.928  1.00 32.20 ? 36   LYS S C   1 
ATOM   18936 O  O   . LYS R  1 36  ? 46.499  111.311 22.425  1.00 32.06 ? 36   LYS S O   1 
ATOM   18937 C  CB  . LYS R  1 36  ? 45.945  109.645 25.258  1.00 32.97 ? 36   LYS S CB  1 
ATOM   18938 C  CG  . LYS R  1 36  ? 44.779  110.614 25.172  1.00 33.45 ? 36   LYS S CG  1 
ATOM   18939 C  CD  . LYS R  1 36  ? 43.713  110.281 26.223  1.00 36.32 ? 36   LYS S CD  1 
ATOM   18940 C  CE  . LYS R  1 36  ? 42.365  110.857 25.826  1.00 37.56 ? 36   LYS S CE  1 
ATOM   18941 N  NZ  . LYS R  1 36  ? 41.703  110.053 24.749  1.00 38.61 ? 36   LYS S NZ  1 
ATOM   18942 N  N   . GLY R  1 37  ? 46.369  109.054 22.284  1.00 31.30 ? 37   GLY S N   1 
ATOM   18943 C  CA  . GLY R  1 37  ? 45.888  109.032 20.915  1.00 30.48 ? 37   GLY S CA  1 
ATOM   18944 C  C   . GLY R  1 37  ? 47.004  109.094 19.879  1.00 29.95 ? 37   GLY S C   1 
ATOM   18945 O  O   . GLY R  1 37  ? 46.743  109.351 18.699  1.00 30.00 ? 37   GLY S O   1 
ATOM   18946 N  N   . LEU R  1 38  ? 48.231  108.830 20.328  1.00 29.13 ? 38   LEU S N   1 
ATOM   18947 C  CA  . LEU R  1 38  ? 49.434  108.868 19.494  1.00 28.74 ? 38   LEU S CA  1 
ATOM   18948 C  C   . LEU R  1 38  ? 49.796  107.524 18.871  1.00 28.33 ? 38   LEU S C   1 
ATOM   18949 O  O   . LEU R  1 38  ? 49.508  106.471 19.450  1.00 28.33 ? 38   LEU S O   1 
ATOM   18950 C  CB  . LEU R  1 38  ? 50.611  109.279 20.364  1.00 28.74 ? 38   LEU S CB  1 
ATOM   18951 C  CG  . LEU R  1 38  ? 50.646  110.712 20.863  1.00 28.34 ? 38   LEU S CG  1 
ATOM   18952 C  CD1 . LEU R  1 38  ? 51.724  110.844 21.920  1.00 29.09 ? 38   LEU S CD1 1 
ATOM   18953 C  CD2 . LEU R  1 38  ? 50.876  111.673 19.679  1.00 27.93 ? 38   LEU S CD2 1 
ATOM   18954 N  N   . THR R  1 39  ? 50.432  107.545 17.700  1.00 27.45 ? 39   THR S N   1 
ATOM   18955 C  CA  . THR R  1 39  ? 50.916  106.291 17.122  1.00 26.96 ? 39   THR S CA  1 
ATOM   18956 C  C   . THR R  1 39  ? 52.120  105.807 17.930  1.00 27.06 ? 39   THR S C   1 
ATOM   18957 O  O   . THR R  1 39  ? 52.940  106.617 18.379  1.00 26.72 ? 39   THR S O   1 
ATOM   18958 C  CB  . THR R  1 39  ? 51.310  106.436 15.630  1.00 27.20 ? 39   THR S CB  1 
ATOM   18959 O  OG1 . THR R  1 39  ? 52.239  107.524 15.476  1.00 24.85 ? 39   THR S OG1 1 
ATOM   18960 C  CG2 . THR R  1 39  ? 50.105  106.838 14.774  1.00 27.12 ? 39   THR S CG2 1 
ATOM   18961 N  N   . GLU R  1 40  ? 52.235  104.493 18.114  1.00 27.07 ? 40   GLU S N   1 
ATOM   18962 C  CA  . GLU R  1 40  ? 53.374  103.953 18.852  1.00 27.57 ? 40   GLU S CA  1 
ATOM   18963 C  C   . GLU R  1 40  ? 54.681  104.448 18.249  1.00 27.25 ? 40   GLU S C   1 
ATOM   18964 O  O   . GLU R  1 40  ? 54.846  104.484 17.020  1.00 27.23 ? 40   GLU S O   1 
ATOM   18965 C  CB  . GLU R  1 40  ? 53.375  102.419 18.890  1.00 27.70 ? 40   GLU S CB  1 
ATOM   18966 C  CG  . GLU R  1 40  ? 54.506  101.869 19.746  1.00 29.74 ? 40   GLU S CG  1 
ATOM   18967 C  CD  . GLU R  1 40  ? 54.593  100.355 19.727  1.00 33.12 ? 40   GLU S CD  1 
ATOM   18968 O  OE1 . GLU R  1 40  ? 53.619  99.715  19.264  1.00 34.67 ? 40   GLU S OE1 1 
ATOM   18969 O  OE2 . GLU R  1 40  ? 55.631  99.807  20.179  1.00 33.27 ? 40   GLU S OE2 1 
ATOM   18970 N  N   . GLY R  1 41  ? 55.608  104.838 19.115  1.00 27.17 ? 41   GLY S N   1 
ATOM   18971 C  CA  . GLY R  1 41  ? 56.891  105.343 18.658  1.00 26.70 ? 41   GLY S CA  1 
ATOM   18972 C  C   . GLY R  1 41  ? 57.133  106.804 19.000  1.00 26.79 ? 41   GLY S C   1 
ATOM   18973 O  O   . GLY R  1 41  ? 56.388  107.406 19.785  1.00 25.75 ? 41   GLY S O   1 
ATOM   18974 N  N   . LEU R  1 42  ? 58.185  107.363 18.392  1.00 26.84 ? 42   LEU S N   1 
ATOM   18975 C  CA  . LEU R  1 42  ? 58.660  108.714 18.665  1.00 27.68 ? 42   LEU S CA  1 
ATOM   18976 C  C   . LEU R  1 42  ? 57.855  109.818 17.973  1.00 27.93 ? 42   LEU S C   1 
ATOM   18977 O  O   . LEU R  1 42  ? 57.471  109.693 16.805  1.00 28.05 ? 42   LEU S O   1 
ATOM   18978 C  CB  . LEU R  1 42  ? 60.126  108.845 18.209  1.00 27.59 ? 42   LEU S CB  1 
ATOM   18979 C  CG  . LEU R  1 42  ? 61.149  107.858 18.790  1.00 29.59 ? 42   LEU S CG  1 
ATOM   18980 C  CD1 . LEU R  1 42  ? 62.468  107.907 18.005  1.00 29.30 ? 42   LEU S CD1 1 
ATOM   18981 C  CD2 . LEU R  1 42  ? 61.363  108.088 20.296  1.00 29.13 ? 42   LEU S CD2 1 
ATOM   18982 N  N   . HIS R  1 43  ? 57.655  110.923 18.685  1.00 27.94 ? 43   HIS S N   1 
ATOM   18983 C  CA  . HIS R  1 43  ? 56.929  112.071 18.153  1.00 27.94 ? 43   HIS S CA  1 
ATOM   18984 C  C   . HIS R  1 43  ? 57.641  113.341 18.574  1.00 28.30 ? 43   HIS S C   1 
ATOM   18985 O  O   . HIS R  1 43  ? 57.874  113.562 19.764  1.00 27.07 ? 43   HIS S O   1 
ATOM   18986 C  CB  . HIS R  1 43  ? 55.501  112.099 18.688  1.00 28.30 ? 43   HIS S CB  1 
ATOM   18987 C  CG  . HIS R  1 43  ? 54.677  110.936 18.244  1.00 29.50 ? 43   HIS S CG  1 
ATOM   18988 N  ND1 . HIS R  1 43  ? 53.896  110.971 17.107  1.00 30.26 ? 43   HIS S ND1 1 
ATOM   18989 C  CD2 . HIS R  1 43  ? 54.540  109.690 18.762  1.00 28.79 ? 43   HIS S CD2 1 
ATOM   18990 C  CE1 . HIS R  1 43  ? 53.294  109.804 16.958  1.00 31.13 ? 43   HIS S CE1 1 
ATOM   18991 N  NE2 . HIS R  1 43  ? 53.669  109.009 17.948  1.00 29.50 ? 43   HIS S NE2 1 
ATOM   18992 N  N   . GLY R  1 44  ? 58.016  114.164 17.603  1.00 28.39 ? 44   GLY S N   1 
ATOM   18993 C  CA  . GLY R  1 44  ? 58.686  115.418 17.917  1.00 29.33 ? 44   GLY S CA  1 
ATOM   18994 C  C   . GLY R  1 44  ? 57.902  116.203 18.952  1.00 30.00 ? 44   GLY S C   1 
ATOM   18995 O  O   . GLY R  1 44  ? 56.672  116.246 18.889  1.00 30.55 ? 44   GLY S O   1 
ATOM   18996 N  N   . PHE R  1 45  ? 58.615  116.845 19.876  1.00 29.96 ? 45   PHE S N   1 
ATOM   18997 C  CA  . PHE R  1 45  ? 58.011  117.567 21.000  1.00 30.41 ? 45   PHE S CA  1 
ATOM   18998 C  C   . PHE R  1 45  ? 58.660  118.955 21.077  1.00 30.53 ? 45   PHE S C   1 
ATOM   18999 O  O   . PHE R  1 45  ? 59.842  119.063 21.430  1.00 30.67 ? 45   PHE S O   1 
ATOM   19000 C  CB  . PHE R  1 45  ? 58.313  116.768 22.269  1.00 29.82 ? 45   PHE S CB  1 
ATOM   19001 C  CG  . PHE R  1 45  ? 57.525  117.190 23.493  1.00 30.95 ? 45   PHE S CG  1 
ATOM   19002 C  CD1 . PHE R  1 45  ? 56.139  117.279 23.466  1.00 30.66 ? 45   PHE S CD1 1 
ATOM   19003 C  CD2 . PHE R  1 45  ? 58.182  117.454 24.688  1.00 30.82 ? 45   PHE S CD2 1 
ATOM   19004 C  CE1 . PHE R  1 45  ? 55.428  117.634 24.608  1.00 31.80 ? 45   PHE S CE1 1 
ATOM   19005 C  CE2 . PHE R  1 45  ? 57.473  117.817 25.833  1.00 32.07 ? 45   PHE S CE2 1 
ATOM   19006 C  CZ  . PHE R  1 45  ? 56.096  117.909 25.789  1.00 32.20 ? 45   PHE S CZ  1 
ATOM   19007 N  N   . HIS R  1 46  ? 57.922  120.015 20.741  1.00 30.58 ? 46   HIS S N   1 
ATOM   19008 C  CA  . HIS R  1 46  ? 58.538  121.353 20.742  1.00 30.66 ? 46   HIS S CA  1 
ATOM   19009 C  C   . HIS R  1 46  ? 57.707  122.510 21.286  1.00 30.78 ? 46   HIS S C   1 
ATOM   19010 O  O   . HIS R  1 46  ? 56.473  122.482 21.267  1.00 30.20 ? 46   HIS S O   1 
ATOM   19011 C  CB  . HIS R  1 46  ? 58.982  121.785 19.333  1.00 30.36 ? 46   HIS S CB  1 
ATOM   19012 C  CG  . HIS R  1 46  ? 59.647  120.715 18.531  1.00 30.59 ? 46   HIS S CG  1 
ATOM   19013 N  ND1 . HIS R  1 46  ? 59.134  120.272 17.330  1.00 32.25 ? 46   HIS S ND1 1 
ATOM   19014 C  CD2 . HIS R  1 46  ? 60.792  120.021 18.729  1.00 31.09 ? 46   HIS S CD2 1 
ATOM   19015 C  CE1 . HIS R  1 46  ? 59.920  119.335 16.832  1.00 31.18 ? 46   HIS S CE1 1 
ATOM   19016 N  NE2 . HIS R  1 46  ? 60.933  119.162 17.663  1.00 31.72 ? 46   HIS S NE2 1 
ATOM   19017 N  N   . VAL R  1 47  ? 58.429  123.538 21.738  1.00 30.84 ? 47   VAL S N   1 
ATOM   19018 C  CA  . VAL R  1 47  ? 57.847  124.816 22.124  1.00 30.85 ? 47   VAL S CA  1 
ATOM   19019 C  C   . VAL R  1 47  ? 58.007  125.762 20.939  1.00 31.39 ? 47   VAL S C   1 
ATOM   19020 O  O   . VAL R  1 47  ? 59.133  126.134 20.572  1.00 31.25 ? 47   VAL S O   1 
ATOM   19021 C  CB  . VAL R  1 47  ? 58.563  125.432 23.320  1.00 30.81 ? 47   VAL S CB  1 
ATOM   19022 C  CG1 . VAL R  1 47  ? 58.223  126.901 23.436  1.00 30.52 ? 47   VAL S CG1 1 
ATOM   19023 C  CG2 . VAL R  1 47  ? 58.188  124.677 24.602  1.00 30.98 ? 47   VAL S CG2 1 
ATOM   19024 N  N   . HIS R  1 48  ? 56.884  126.122 20.325  1.00 31.44 ? 48   HIS S N   1 
ATOM   19025 C  CA  . HIS R  1 48  ? 56.901  127.024 19.183  1.00 32.22 ? 48   HIS S CA  1 
ATOM   19026 C  C   . HIS R  1 48  ? 56.739  128.477 19.618  1.00 32.59 ? 48   HIS S C   1 
ATOM   19027 O  O   . HIS R  1 48  ? 56.216  128.766 20.703  1.00 33.00 ? 48   HIS S O   1 
ATOM   19028 C  CB  . HIS R  1 48  ? 55.880  126.609 18.123  1.00 31.61 ? 48   HIS S CB  1 
ATOM   19029 C  CG  . HIS R  1 48  ? 56.249  125.338 17.422  1.00 31.99 ? 48   HIS S CG  1 
ATOM   19030 N  ND1 . HIS R  1 48  ? 56.201  125.194 16.053  1.00 31.81 ? 48   HIS S ND1 1 
ATOM   19031 C  CD2 . HIS R  1 48  ? 56.700  124.156 17.909  1.00 30.97 ? 48   HIS S CD2 1 
ATOM   19032 C  CE1 . HIS R  1 48  ? 56.593  123.974 15.726  1.00 31.13 ? 48   HIS S CE1 1 
ATOM   19033 N  NE2 . HIS R  1 48  ? 56.897  123.324 16.836  1.00 30.45 ? 48   HIS S NE2 1 
ATOM   19034 N  N   . GLU R  1 49  ? 57.200  129.372 18.753  1.00 32.87 ? 49   GLU S N   1 
ATOM   19035 C  CA  . GLU R  1 49  ? 57.315  130.785 19.064  1.00 33.37 ? 49   GLU S CA  1 
ATOM   19036 C  C   . GLU R  1 49  ? 56.074  131.515 19.569  1.00 33.99 ? 49   GLU S C   1 
ATOM   19037 O  O   . GLU R  1 49  ? 56.137  132.223 20.580  1.00 33.74 ? 49   GLU S O   1 
ATOM   19038 C  CB  . GLU R  1 49  ? 57.882  131.529 17.861  1.00 33.45 ? 49   GLU S CB  1 
ATOM   19039 C  CG  . GLU R  1 49  ? 58.329  132.934 18.206  1.00 32.98 ? 49   GLU S CG  1 
ATOM   19040 C  CD  . GLU R  1 49  ? 58.849  133.702 17.008  1.00 33.26 ? 49   GLU S CD  1 
ATOM   19041 O  OE1 . GLU R  1 49  ? 58.897  133.125 15.888  1.00 32.69 ? 49   GLU S OE1 1 
ATOM   19042 O  OE2 . GLU R  1 49  ? 59.215  134.884 17.194  1.00 30.82 ? 49   GLU S OE2 1 
ATOM   19043 N  N   . PHE R  1 50  ? 54.953  131.363 18.872  1.00 34.67 ? 50   PHE S N   1 
ATOM   19044 C  CA  . PHE R  1 50  ? 53.759  132.144 19.219  1.00 35.57 ? 50   PHE S CA  1 
ATOM   19045 C  C   . PHE R  1 50  ? 52.647  131.331 19.884  1.00 35.59 ? 50   PHE S C   1 
ATOM   19046 O  O   . PHE R  1 50  ? 52.395  130.193 19.505  1.00 35.67 ? 50   PHE S O   1 
ATOM   19047 C  CB  . PHE R  1 50  ? 53.209  132.865 17.977  1.00 35.73 ? 50   PHE S CB  1 
ATOM   19048 C  CG  . PHE R  1 50  ? 54.249  133.646 17.196  1.00 37.10 ? 50   PHE S CG  1 
ATOM   19049 C  CD1 . PHE R  1 50  ? 54.875  134.759 17.750  1.00 38.15 ? 50   PHE S CD1 1 
ATOM   19050 C  CD2 . PHE R  1 50  ? 54.581  133.277 15.898  1.00 37.56 ? 50   PHE S CD2 1 
ATOM   19051 C  CE1 . PHE R  1 50  ? 55.828  135.485 17.021  1.00 38.56 ? 50   PHE S CE1 1 
ATOM   19052 C  CE2 . PHE R  1 50  ? 55.527  133.994 15.162  1.00 38.70 ? 50   PHE S CE2 1 
ATOM   19053 C  CZ  . PHE R  1 50  ? 56.155  135.097 15.724  1.00 38.74 ? 50   PHE S CZ  1 
ATOM   19054 N  N   . GLY R  1 51  ? 51.993  131.916 20.888  1.00 35.99 ? 51   GLY S N   1 
ATOM   19055 C  CA  . GLY R  1 51  ? 50.880  131.268 21.565  1.00 36.03 ? 51   GLY S CA  1 
ATOM   19056 C  C   . GLY R  1 51  ? 49.604  131.664 20.852  1.00 36.54 ? 51   GLY S C   1 
ATOM   19057 O  O   . GLY R  1 51  ? 48.654  132.166 21.459  1.00 36.34 ? 51   GLY S O   1 
ATOM   19058 N  N   . ASP R  1 52  ? 49.596  131.432 19.542  1.00 36.75 ? 52   ASP S N   1 
ATOM   19059 C  CA  . ASP R  1 52  ? 48.498  131.843 18.680  1.00 37.35 ? 52   ASP S CA  1 
ATOM   19060 C  C   . ASP R  1 52  ? 47.821  130.624 18.029  1.00 37.56 ? 52   ASP S C   1 
ATOM   19061 O  O   . ASP R  1 52  ? 48.406  129.950 17.185  1.00 37.59 ? 52   ASP S O   1 
ATOM   19062 C  CB  . ASP R  1 52  ? 49.043  132.828 17.639  1.00 37.40 ? 52   ASP S CB  1 
ATOM   19063 C  CG  . ASP R  1 52  ? 47.980  133.357 16.712  1.00 37.62 ? 52   ASP S CG  1 
ATOM   19064 O  OD1 . ASP R  1 52  ? 46.836  132.854 16.766  1.00 37.15 ? 52   ASP S OD1 1 
ATOM   19065 O  OD2 . ASP R  1 52  ? 48.210  134.273 15.893  1.00 36.79 ? 52   ASP S OD2 1 
ATOM   19066 N  N   . ASN R  1 53  ? 46.582  130.357 18.435  1.00 37.91 ? 53   ASN S N   1 
ATOM   19067 C  CA  . ASN R  1 53  ? 45.834  129.193 17.970  1.00 38.24 ? 53   ASN S CA  1 
ATOM   19068 C  C   . ASN R  1 53  ? 44.670  129.568 17.061  1.00 38.09 ? 53   ASN S C   1 
ATOM   19069 O  O   . ASN R  1 53  ? 43.724  128.796 16.905  1.00 37.87 ? 53   ASN S O   1 
ATOM   19070 C  CB  . ASN R  1 53  ? 45.313  128.409 19.185  1.00 38.93 ? 53   ASN S CB  1 
ATOM   19071 C  CG  . ASN R  1 53  ? 44.750  127.041 18.815  1.00 40.18 ? 53   ASN S CG  1 
ATOM   19072 O  OD1 . ASN R  1 53  ? 43.593  126.727 19.116  1.00 42.09 ? 53   ASN S OD1 1 
ATOM   19073 N  ND2 . ASN R  1 53  ? 45.573  126.216 18.193  1.00 40.60 ? 53   ASN S ND2 1 
ATOM   19074 N  N   . THR R  1 54  ? 44.739  130.754 16.459  1.00 37.87 ? 54   THR S N   1 
ATOM   19075 C  CA  . THR R  1 54  ? 43.669  131.217 15.567  1.00 37.87 ? 54   THR S CA  1 
ATOM   19076 C  C   . THR R  1 54  ? 43.496  130.321 14.333  1.00 37.79 ? 54   THR S C   1 
ATOM   19077 O  O   . THR R  1 54  ? 42.376  130.140 13.843  1.00 38.07 ? 54   THR S O   1 
ATOM   19078 C  CB  . THR R  1 54  ? 43.869  132.697 15.152  1.00 37.82 ? 54   THR S CB  1 
ATOM   19079 O  OG1 . THR R  1 54  ? 45.249  132.942 14.846  1.00 37.43 ? 54   THR S OG1 1 
ATOM   19080 C  CG2 . THR R  1 54  ? 43.608  133.613 16.324  1.00 38.18 ? 54   THR S CG2 1 
ATOM   19081 N  N   . ALA R  1 55  ? 44.603  129.794 13.823  1.00 37.32 ? 55   ALA S N   1 
ATOM   19082 C  CA  . ALA R  1 55  ? 44.575  128.850 12.703  1.00 37.43 ? 55   ALA S CA  1 
ATOM   19083 C  C   . ALA R  1 55  ? 45.073  127.502 13.204  1.00 37.25 ? 55   ALA S C   1 
ATOM   19084 O  O   . ALA R  1 55  ? 45.914  126.867 12.574  1.00 37.55 ? 55   ALA S O   1 
ATOM   19085 C  CB  . ALA R  1 55  ? 45.453  129.332 11.568  1.00 37.05 ? 55   ALA S CB  1 
ATOM   19086 N  N   . GLY R  1 56  ? 44.560  127.078 14.354  1.00 37.12 ? 56   GLY S N   1 
ATOM   19087 C  CA  . GLY R  1 56  ? 45.008  125.836 14.951  1.00 36.97 ? 56   GLY S CA  1 
ATOM   19088 C  C   . GLY R  1 56  ? 46.491  125.913 15.251  1.00 36.60 ? 56   GLY S C   1 
ATOM   19089 O  O   . GLY R  1 56  ? 47.027  126.996 15.506  1.00 36.65 ? 56   GLY S O   1 
ATOM   19090 N  N   . CYS R  1 57  ? 47.166  124.768 15.192  1.00 36.45 ? 57   CYS S N   1 
ATOM   19091 C  CA  . CYS R  1 57  ? 48.599  124.697 15.488  1.00 36.36 ? 57   CYS S CA  1 
ATOM   19092 C  C   . CYS R  1 57  ? 49.448  125.443 14.482  1.00 35.49 ? 57   CYS S C   1 
ATOM   19093 O  O   . CYS R  1 57  ? 50.600  125.775 14.746  1.00 35.02 ? 57   CYS S O   1 
ATOM   19094 C  CB  . CYS R  1 57  ? 49.053  123.239 15.557  1.00 36.32 ? 57   CYS S CB  1 
ATOM   19095 S  SG  . CYS R  1 57  ? 48.137  122.342 16.817  1.00 38.57 ? 57   CYS S SG  1 
ATOM   19096 N  N   . THR R  1 58  ? 48.866  125.707 13.325  1.00 35.57 ? 58   THR S N   1 
ATOM   19097 C  CA  . THR R  1 58  ? 49.577  126.376 12.248  1.00 35.38 ? 58   THR S CA  1 
ATOM   19098 C  C   . THR R  1 58  ? 50.062  127.765 12.626  1.00 35.47 ? 58   THR S C   1 
ATOM   19099 O  O   . THR R  1 58  ? 51.177  128.158 12.293  1.00 35.30 ? 58   THR S O   1 
ATOM   19100 C  CB  . THR R  1 58  ? 48.660  126.472 11.045  1.00 35.55 ? 58   THR S CB  1 
ATOM   19101 O  OG1 . THR R  1 58  ? 48.294  125.145 10.642  1.00 35.36 ? 58   THR S OG1 1 
ATOM   19102 C  CG2 . THR R  1 58  ? 49.416  127.050 9.856   1.00 35.99 ? 58   THR S CG2 1 
ATOM   19103 N  N   . SER R  1 59  ? 49.229  128.510 13.335  1.00 35.34 ? 59   SER S N   1 
ATOM   19104 C  CA  . SER R  1 59  ? 49.581  129.885 13.665  1.00 35.39 ? 59   SER S CA  1 
ATOM   19105 C  C   . SER R  1 59  ? 50.548  130.003 14.854  1.00 35.43 ? 59   SER S C   1 
ATOM   19106 O  O   . SER R  1 59  ? 50.763  131.096 15.382  1.00 35.30 ? 59   SER S O   1 
ATOM   19107 C  CB  . SER R  1 59  ? 48.310  130.707 13.890  1.00 35.28 ? 59   SER S CB  1 
ATOM   19108 O  OG  . SER R  1 59  ? 47.385  129.986 14.694  1.00 35.53 ? 59   SER S OG  1 
ATOM   19109 N  N   . ALA R  1 60  ? 51.140  128.883 15.271  1.00 35.35 ? 60   ALA S N   1 
ATOM   19110 C  CA  . ALA R  1 60  ? 52.078  128.907 16.402  1.00 35.17 ? 60   ALA S CA  1 
ATOM   19111 C  C   . ALA R  1 60  ? 53.486  129.302 15.933  1.00 35.10 ? 60   ALA S C   1 
ATOM   19112 O  O   . ALA R  1 60  ? 54.420  129.444 16.735  1.00 34.85 ? 60   ALA S O   1 
ATOM   19113 C  CB  . ALA R  1 60  ? 52.104  127.547 17.113  1.00 34.91 ? 60   ALA S CB  1 
ATOM   19114 N  N   . GLY R  1 61  ? 53.625  129.462 14.620  1.00 35.05 ? 61   GLY S N   1 
ATOM   19115 C  CA  . GLY R  1 61  ? 54.892  129.835 14.024  1.00 34.83 ? 61   GLY S CA  1 
ATOM   19116 C  C   . GLY R  1 61  ? 55.927  128.735 14.152  1.00 34.59 ? 61   GLY S C   1 
ATOM   19117 O  O   . GLY R  1 61  ? 55.594  127.575 14.407  1.00 34.83 ? 61   GLY S O   1 
ATOM   19118 N  N   . PRO R  1 62  ? 57.190  129.109 13.984  1.00 34.54 ? 62   PRO S N   1 
ATOM   19119 C  CA  . PRO R  1 62  ? 58.307  128.161 14.031  1.00 34.14 ? 62   PRO S CA  1 
ATOM   19120 C  C   . PRO R  1 62  ? 58.705  127.845 15.467  1.00 34.12 ? 62   PRO S C   1 
ATOM   19121 O  O   . PRO R  1 62  ? 58.015  128.253 16.399  1.00 34.08 ? 62   PRO S O   1 
ATOM   19122 C  CB  . PRO R  1 62  ? 59.439  128.935 13.359  1.00 34.52 ? 62   PRO S CB  1 
ATOM   19123 C  CG  . PRO R  1 62  ? 59.132  130.398 13.650  1.00 34.51 ? 62   PRO S CG  1 
ATOM   19124 C  CD  . PRO R  1 62  ? 57.636  130.502 13.764  1.00 34.55 ? 62   PRO S CD  1 
ATOM   19125 N  N   . HIS R  1 63  ? 59.809  127.125 15.638  1.00 33.62 ? 63   HIS S N   1 
ATOM   19126 C  CA  . HIS R  1 63  ? 60.292  126.786 16.971  1.00 33.17 ? 63   HIS S CA  1 
ATOM   19127 C  C   . HIS R  1 63  ? 60.787  128.046 17.643  1.00 32.91 ? 63   HIS S C   1 
ATOM   19128 O  O   . HIS R  1 63  ? 61.380  128.913 16.994  1.00 31.94 ? 63   HIS S O   1 
ATOM   19129 C  CB  . HIS R  1 63  ? 61.412  125.747 16.898  1.00 33.41 ? 63   HIS S CB  1 
ATOM   19130 C  CG  . HIS R  1 63  ? 60.966  124.428 16.348  1.00 34.52 ? 63   HIS S CG  1 
ATOM   19131 N  ND1 . HIS R  1 63  ? 61.818  123.356 16.189  1.00 34.13 ? 63   HIS S ND1 1 
ATOM   19132 C  CD2 . HIS R  1 63  ? 59.753  124.010 15.918  1.00 35.02 ? 63   HIS S CD2 1 
ATOM   19133 C  CE1 . HIS R  1 63  ? 61.148  122.333 15.693  1.00 35.36 ? 63   HIS S CE1 1 
ATOM   19134 N  NE2 . HIS R  1 63  ? 59.894  122.706 15.512  1.00 36.83 ? 63   HIS S NE2 1 
ATOM   19135 N  N   . PHE R  1 64  ? 60.522  128.158 18.940  1.00 32.44 ? 64   PHE S N   1 
ATOM   19136 C  CA  . PHE R  1 64  ? 60.990  129.306 19.693  1.00 32.52 ? 64   PHE S CA  1 
ATOM   19137 C  C   . PHE R  1 64  ? 62.510  129.309 19.554  1.00 32.10 ? 64   PHE S C   1 
ATOM   19138 O  O   . PHE R  1 64  ? 63.163  128.319 19.889  1.00 31.98 ? 64   PHE S O   1 
ATOM   19139 C  CB  . PHE R  1 64  ? 60.563  129.189 21.153  1.00 32.65 ? 64   PHE S CB  1 
ATOM   19140 C  CG  . PHE R  1 64  ? 60.955  130.370 21.998  1.00 33.20 ? 64   PHE S CG  1 
ATOM   19141 C  CD1 . PHE R  1 64  ? 60.882  131.659 21.493  1.00 33.89 ? 64   PHE S CD1 1 
ATOM   19142 C  CD2 . PHE R  1 64  ? 61.405  130.187 23.297  1.00 34.15 ? 64   PHE S CD2 1 
ATOM   19143 C  CE1 . PHE R  1 64  ? 61.254  132.760 22.278  1.00 35.06 ? 64   PHE S CE1 1 
ATOM   19144 C  CE2 . PHE R  1 64  ? 61.776  131.274 24.090  1.00 34.54 ? 64   PHE S CE2 1 
ATOM   19145 C  CZ  . PHE R  1 64  ? 61.699  132.563 23.579  1.00 35.23 ? 64   PHE S CZ  1 
ATOM   19146 N  N   . ASN R  1 65  ? 63.069  130.418 19.074  1.00 31.51 ? 65   ASN S N   1 
ATOM   19147 C  CA  . ASN R  1 65  ? 64.488  130.457 18.718  1.00 31.12 ? 65   ASN S CA  1 
ATOM   19148 C  C   . ASN R  1 65  ? 65.146  131.832 18.879  1.00 31.07 ? 65   ASN S C   1 
ATOM   19149 O  O   . ASN R  1 65  ? 65.758  132.354 17.947  1.00 30.65 ? 65   ASN S O   1 
ATOM   19150 C  CB  . ASN R  1 65  ? 64.619  129.976 17.261  1.00 30.72 ? 65   ASN S CB  1 
ATOM   19151 C  CG  . ASN R  1 65  ? 66.064  129.838 16.795  1.00 30.01 ? 65   ASN S CG  1 
ATOM   19152 O  OD1 . ASN R  1 65  ? 66.976  129.645 17.602  1.00 27.41 ? 65   ASN S OD1 1 
ATOM   19153 N  ND2 . ASN R  1 65  ? 66.273  129.916 15.468  1.00 27.16 ? 65   ASN S ND2 1 
ATOM   19154 N  N   . PRO R  1 66  ? 65.053  132.394 20.079  1.00 31.37 ? 66   PRO S N   1 
ATOM   19155 C  CA  . PRO R  1 66  ? 65.590  133.730 20.368  1.00 31.44 ? 66   PRO S CA  1 
ATOM   19156 C  C   . PRO R  1 66  ? 67.082  133.908 20.057  1.00 31.77 ? 66   PRO S C   1 
ATOM   19157 O  O   . PRO R  1 66  ? 67.528  135.050 19.835  1.00 31.63 ? 66   PRO S O   1 
ATOM   19158 C  CB  . PRO R  1 66  ? 65.375  133.850 21.880  1.00 31.51 ? 66   PRO S CB  1 
ATOM   19159 C  CG  . PRO R  1 66  ? 65.284  132.432 22.326  1.00 31.31 ? 66   PRO S CG  1 
ATOM   19160 C  CD  . PRO R  1 66  ? 64.436  131.793 21.274  1.00 31.00 ? 66   PRO S CD  1 
ATOM   19161 N  N   . LEU R  1 67  ? 67.844  132.815 20.052  1.00 31.70 ? 67   LEU S N   1 
ATOM   19162 C  CA  . LEU R  1 67  ? 69.278  132.907 19.802  1.00 32.00 ? 67   LEU S CA  1 
ATOM   19163 C  C   . LEU R  1 67  ? 69.630  132.615 18.351  1.00 32.35 ? 67   LEU S C   1 
ATOM   19164 O  O   . LEU R  1 67  ? 70.808  132.501 18.009  1.00 32.44 ? 67   LEU S O   1 
ATOM   19165 C  CB  . LEU R  1 67  ? 70.057  131.981 20.733  1.00 31.79 ? 67   LEU S CB  1 
ATOM   19166 C  CG  . LEU R  1 67  ? 70.118  132.416 22.201  1.00 31.82 ? 67   LEU S CG  1 
ATOM   19167 C  CD1 . LEU R  1 67  ? 70.878  131.407 23.047  1.00 31.85 ? 67   LEU S CD1 1 
ATOM   19168 C  CD2 . LEU R  1 67  ? 70.732  133.813 22.349  1.00 31.65 ? 67   LEU S CD2 1 
ATOM   19169 N  N   . SER R  1 68  ? 68.600  132.504 17.511  1.00 32.71 ? 68   SER S N   1 
ATOM   19170 C  CA  . SER R  1 68  ? 68.757  132.238 16.079  1.00 32.87 ? 68   SER S CA  1 
ATOM   19171 C  C   . SER R  1 68  ? 69.748  131.113 15.808  1.00 32.89 ? 68   SER S C   1 
ATOM   19172 O  O   . SER R  1 68  ? 70.736  131.304 15.110  1.00 33.26 ? 68   SER S O   1 
ATOM   19173 C  CB  . SER R  1 68  ? 69.205  133.502 15.326  1.00 32.97 ? 68   SER S CB  1 
ATOM   19174 O  OG  . SER R  1 68  ? 68.230  134.524 15.407  1.00 33.35 ? 68   SER S OG  1 
ATOM   19175 N  N   . ARG R  1 69  ? 69.498  129.935 16.354  1.00 32.80 ? 69   ARG S N   1 
ATOM   19176 C  CA  . ARG R  1 69  ? 70.418  128.835 16.113  1.00 32.66 ? 69   ARG S CA  1 
ATOM   19177 C  C   . ARG R  1 69  ? 69.747  127.733 15.317  1.00 32.07 ? 69   ARG S C   1 
ATOM   19178 O  O   . ARG R  1 69  ? 68.567  127.829 15.005  1.00 32.03 ? 69   ARG S O   1 
ATOM   19179 C  CB  . ARG R  1 69  ? 70.979  128.327 17.433  1.00 33.13 ? 69   ARG S CB  1 
ATOM   19180 C  CG  . ARG R  1 69  ? 71.696  129.438 18.179  1.00 34.55 ? 69   ARG S CG  1 
ATOM   19181 C  CD  . ARG R  1 69  ? 73.008  129.042 18.791  1.00 38.27 ? 69   ARG S CD  1 
ATOM   19182 N  NE  . ARG R  1 69  ? 72.867  128.887 20.233  1.00 41.97 ? 69   ARG S NE  1 
ATOM   19183 C  CZ  . ARG R  1 69  ? 73.541  129.597 21.126  1.00 43.82 ? 69   ARG S CZ  1 
ATOM   19184 N  NH1 . ARG R  1 69  ? 74.418  130.509 20.728  1.00 44.87 ? 69   ARG S NH1 1 
ATOM   19185 N  NH2 . ARG R  1 69  ? 73.346  129.390 22.422  1.00 45.33 ? 69   ARG S NH2 1 
ATOM   19186 N  N   . LYS R  1 70  ? 70.493  126.692 14.972  1.00 31.22 ? 70   LYS S N   1 
ATOM   19187 C  CA  . LYS R  1 70  ? 69.898  125.618 14.187  1.00 30.59 ? 70   LYS S CA  1 
ATOM   19188 C  C   . LYS R  1 70  ? 69.170  124.635 15.097  1.00 29.71 ? 70   LYS S C   1 
ATOM   19189 O  O   . LYS R  1 70  ? 69.402  124.596 16.309  1.00 29.53 ? 70   LYS S O   1 
ATOM   19190 C  CB  . LYS R  1 70  ? 70.937  124.930 13.300  1.00 30.98 ? 70   LYS S CB  1 
ATOM   19191 C  CG  . LYS R  1 70  ? 71.682  125.894 12.368  1.00 31.73 ? 70   LYS S CG  1 
ATOM   19192 C  CD  . LYS R  1 70  ? 70.906  126.182 11.103  1.00 35.37 ? 70   LYS S CD  1 
ATOM   19193 N  N   . HIS R  1 71  ? 68.260  123.871 14.506  1.00 28.69 ? 71   HIS S N   1 
ATOM   19194 C  CA  . HIS R  1 71  ? 67.496  122.901 15.262  1.00 28.16 ? 71   HIS S CA  1 
ATOM   19195 C  C   . HIS R  1 71  ? 68.400  121.757 15.725  1.00 27.84 ? 71   HIS S C   1 
ATOM   19196 O  O   . HIS R  1 71  ? 69.337  121.380 15.029  1.00 27.41 ? 71   HIS S O   1 
ATOM   19197 C  CB  . HIS R  1 71  ? 66.335  122.373 14.424  1.00 27.64 ? 71   HIS S CB  1 
ATOM   19198 C  CG  . HIS R  1 71  ? 65.585  121.253 15.069  1.00 28.09 ? 71   HIS S CG  1 
ATOM   19199 N  ND1 . HIS R  1 71  ? 64.495  121.458 15.889  1.00 27.70 ? 71   HIS S ND1 1 
ATOM   19200 C  CD2 . HIS R  1 71  ? 65.775  119.912 15.021  1.00 27.03 ? 71   HIS S CD2 1 
ATOM   19201 C  CE1 . HIS R  1 71  ? 64.048  120.293 16.322  1.00 27.94 ? 71   HIS S CE1 1 
ATOM   19202 N  NE2 . HIS R  1 71  ? 64.798  119.337 15.796  1.00 25.62 ? 71   HIS S NE2 1 
ATOM   19203 N  N   . GLY R  1 72  ? 68.127  121.223 16.911  1.00 27.55 ? 72   GLY S N   1 
ATOM   19204 C  CA  . GLY R  1 72  ? 68.897  120.107 17.438  1.00 27.08 ? 72   GLY S CA  1 
ATOM   19205 C  C   . GLY R  1 72  ? 68.071  119.376 18.488  1.00 27.70 ? 72   GLY S C   1 
ATOM   19206 O  O   . GLY R  1 72  ? 66.873  119.615 18.608  1.00 27.37 ? 72   GLY S O   1 
ATOM   19207 N  N   . GLY R  1 73  ? 68.699  118.470 19.229  1.00 27.61 ? 73   GLY S N   1 
ATOM   19208 C  CA  . GLY R  1 73  ? 68.025  117.777 20.311  1.00 28.69 ? 73   GLY S CA  1 
ATOM   19209 C  C   . GLY R  1 73  ? 68.248  118.520 21.620  1.00 29.50 ? 73   GLY S C   1 
ATOM   19210 O  O   . GLY R  1 73  ? 69.098  119.393 21.706  1.00 29.27 ? 73   GLY S O   1 
ATOM   19211 N  N   . PRO R  1 74  ? 67.499  118.172 22.655  1.00 30.47 ? 74   PRO S N   1 
ATOM   19212 C  CA  . PRO R  1 74  ? 67.649  118.830 23.961  1.00 31.58 ? 74   PRO S CA  1 
ATOM   19213 C  C   . PRO R  1 74  ? 69.089  118.888 24.484  1.00 32.51 ? 74   PRO S C   1 
ATOM   19214 O  O   . PRO R  1 74  ? 69.441  119.839 25.183  1.00 32.64 ? 74   PRO S O   1 
ATOM   19215 C  CB  . PRO R  1 74  ? 66.842  117.934 24.904  1.00 31.28 ? 74   PRO S CB  1 
ATOM   19216 C  CG  . PRO R  1 74  ? 65.874  117.241 24.042  1.00 31.54 ? 74   PRO S CG  1 
ATOM   19217 C  CD  . PRO R  1 74  ? 66.458  117.133 22.660  1.00 30.37 ? 74   PRO S CD  1 
ATOM   19218 N  N   . LYS R  1 75  ? 69.900  117.885 24.165  1.00 33.63 ? 75   LYS S N   1 
ATOM   19219 C  CA  . LYS R  1 75  ? 71.254  117.793 24.718  1.00 35.04 ? 75   LYS S CA  1 
ATOM   19220 C  C   . LYS R  1 75  ? 72.343  118.481 23.917  1.00 35.48 ? 75   LYS S C   1 
ATOM   19221 O  O   . LYS R  1 75  ? 73.495  118.540 24.357  1.00 35.58 ? 75   LYS S O   1 
ATOM   19222 C  CB  . LYS R  1 75  ? 71.639  116.330 24.893  1.00 35.20 ? 75   LYS S CB  1 
ATOM   19223 C  CG  . LYS R  1 75  ? 70.595  115.542 25.641  1.00 37.58 ? 75   LYS S CG  1 
ATOM   19224 C  CD  . LYS R  1 75  ? 71.132  114.212 26.122  1.00 39.77 ? 75   LYS S CD  1 
ATOM   19225 C  CE  . LYS R  1 75  ? 70.076  113.495 26.960  1.00 42.50 ? 75   LYS S CE  1 
ATOM   19226 N  NZ  . LYS R  1 75  ? 69.598  114.296 28.148  1.00 44.01 ? 75   LYS S NZ  1 
ATOM   19227 N  N   . ASP R  1 76  ? 71.984  118.995 22.747  1.00 36.02 ? 76   ASP S N   1 
ATOM   19228 C  CA  . ASP R  1 76  ? 72.962  119.618 21.865  1.00 36.46 ? 76   ASP S CA  1 
ATOM   19229 C  C   . ASP R  1 76  ? 73.313  121.049 22.251  1.00 36.68 ? 76   ASP S C   1 
ATOM   19230 O  O   . ASP R  1 76  ? 72.507  121.768 22.838  1.00 36.61 ? 76   ASP S O   1 
ATOM   19231 C  CB  . ASP R  1 76  ? 72.470  119.576 20.414  1.00 36.78 ? 76   ASP S CB  1 
ATOM   19232 C  CG  . ASP R  1 76  ? 72.385  118.163 19.876  1.00 37.91 ? 76   ASP S CG  1 
ATOM   19233 O  OD1 . ASP R  1 76  ? 73.317  117.367 20.143  1.00 39.58 ? 76   ASP S OD1 1 
ATOM   19234 O  OD2 . ASP R  1 76  ? 71.422  117.745 19.195  1.00 38.94 ? 76   ASP S OD2 1 
ATOM   19235 N  N   . GLU R  1 77  ? 74.536  121.449 21.920  1.00 37.03 ? 77   GLU S N   1 
ATOM   19236 C  CA  . GLU R  1 77  ? 74.974  122.813 22.140  1.00 37.18 ? 77   GLU S CA  1 
ATOM   19237 C  C   . GLU R  1 77  ? 74.236  123.686 21.122  1.00 36.86 ? 77   GLU S C   1 
ATOM   19238 O  O   . GLU R  1 77  ? 73.799  124.797 21.435  1.00 37.16 ? 77   GLU S O   1 
ATOM   19239 C  CB  . GLU R  1 77  ? 76.490  122.906 21.950  1.00 37.64 ? 77   GLU S CB  1 
ATOM   19240 C  CG  . GLU R  1 77  ? 77.163  124.086 22.628  1.00 39.20 ? 77   GLU S CG  1 
ATOM   19241 C  CD  . GLU R  1 77  ? 78.672  123.908 22.717  1.00 41.47 ? 77   GLU S CD  1 
ATOM   19242 O  OE1 . GLU R  1 77  ? 79.158  123.453 23.778  1.00 42.16 ? 77   GLU S OE1 1 
ATOM   19243 O  OE2 . GLU R  1 77  ? 79.372  124.216 21.726  1.00 42.14 ? 77   GLU S OE2 1 
ATOM   19244 N  N   . GLU R  1 78  ? 74.079  123.171 19.904  1.00 36.07 ? 78   GLU S N   1 
ATOM   19245 C  CA  . GLU R  1 78  ? 73.365  123.903 18.860  1.00 35.47 ? 78   GLU S CA  1 
ATOM   19246 C  C   . GLU R  1 78  ? 71.899  123.444 18.805  1.00 34.90 ? 78   GLU S C   1 
ATOM   19247 O  O   . GLU R  1 78  ? 71.588  122.369 18.290  1.00 35.28 ? 78   GLU S O   1 
ATOM   19248 C  CB  . GLU R  1 78  ? 74.055  123.727 17.497  1.00 35.00 ? 78   GLU S CB  1 
ATOM   19249 C  CG  . GLU R  1 78  ? 73.456  124.551 16.358  1.00 35.21 ? 78   GLU S CG  1 
ATOM   19250 C  CD  . GLU R  1 78  ? 73.856  126.021 16.390  1.00 34.84 ? 78   GLU S CD  1 
ATOM   19251 O  OE1 . GLU R  1 78  ? 74.567  126.449 17.333  1.00 34.87 ? 78   GLU S OE1 1 
ATOM   19252 O  OE2 . GLU R  1 78  ? 73.457  126.756 15.459  1.00 35.20 ? 78   GLU S OE2 1 
ATOM   19253 N  N   . ARG R  1 79  ? 71.001  124.261 19.341  1.00 33.97 ? 79   ARG S N   1 
ATOM   19254 C  CA  . ARG R  1 79  ? 69.586  123.923 19.339  1.00 33.35 ? 79   ARG S CA  1 
ATOM   19255 C  C   . ARG R  1 79  ? 68.734  125.162 19.505  1.00 32.72 ? 79   ARG S C   1 
ATOM   19256 O  O   . ARG R  1 79  ? 69.218  126.212 19.930  1.00 32.40 ? 79   ARG S O   1 
ATOM   19257 C  CB  . ARG R  1 79  ? 69.253  122.956 20.483  1.00 33.70 ? 79   ARG S CB  1 
ATOM   19258 C  CG  . ARG R  1 79  ? 69.468  123.565 21.880  1.00 34.29 ? 79   ARG S CG  1 
ATOM   19259 C  CD  . ARG R  1 79  ? 68.946  122.715 23.039  1.00 35.59 ? 79   ARG S CD  1 
ATOM   19260 N  NE  . ARG R  1 79  ? 67.652  123.181 23.522  1.00 35.67 ? 79   ARG S NE  1 
ATOM   19261 C  CZ  . ARG R  1 79  ? 67.102  122.790 24.662  1.00 36.52 ? 79   ARG S CZ  1 
ATOM   19262 N  NH1 . ARG R  1 79  ? 67.735  121.915 25.437  1.00 36.86 ? 79   ARG S NH1 1 
ATOM   19263 N  NH2 . ARG R  1 79  ? 65.920  123.271 25.037  1.00 35.37 ? 79   ARG S NH2 1 
ATOM   19264 N  N   . HIS R  1 80  ? 67.458  125.029 19.157  1.00 31.79 ? 80   HIS S N   1 
ATOM   19265 C  CA  . HIS R  1 80  ? 66.496  126.085 19.401  1.00 31.29 ? 80   HIS S CA  1 
ATOM   19266 C  C   . HIS R  1 80  ? 66.156  125.954 20.875  1.00 31.00 ? 80   HIS S C   1 
ATOM   19267 O  O   . HIS R  1 80  ? 66.259  124.866 21.432  1.00 31.04 ? 80   HIS S O   1 
ATOM   19268 C  CB  . HIS R  1 80  ? 65.232  125.854 18.576  1.00 31.13 ? 80   HIS S CB  1 
ATOM   19269 C  CG  . HIS R  1 80  ? 65.462  125.866 17.096  1.00 30.81 ? 80   HIS S CG  1 
ATOM   19270 N  ND1 . HIS R  1 80  ? 64.688  125.137 16.218  1.00 29.58 ? 80   HIS S ND1 1 
ATOM   19271 C  CD2 . HIS R  1 80  ? 66.366  126.534 16.337  1.00 29.45 ? 80   HIS S CD2 1 
ATOM   19272 C  CE1 . HIS R  1 80  ? 65.100  125.361 14.980  1.00 30.72 ? 80   HIS S CE1 1 
ATOM   19273 N  NE2 . HIS R  1 80  ? 66.120  126.201 15.026  1.00 28.15 ? 80   HIS S NE2 1 
ATOM   19274 N  N   . VAL R  1 81  ? 65.745  127.041 21.515  1.00 30.60 ? 81   VAL S N   1 
ATOM   19275 C  CA  . VAL R  1 81  ? 65.333  126.933 22.909  1.00 29.93 ? 81   VAL S CA  1 
ATOM   19276 C  C   . VAL R  1 81  ? 64.140  125.979 23.024  1.00 29.82 ? 81   VAL S C   1 
ATOM   19277 O  O   . VAL R  1 81  ? 64.005  125.254 24.007  1.00 29.19 ? 81   VAL S O   1 
ATOM   19278 C  CB  . VAL R  1 81  ? 64.940  128.296 23.492  1.00 30.02 ? 81   VAL S CB  1 
ATOM   19279 C  CG1 . VAL R  1 81  ? 64.330  128.122 24.871  1.00 29.12 ? 81   VAL S CG1 1 
ATOM   19280 C  CG2 . VAL R  1 81  ? 66.142  129.231 23.528  1.00 29.90 ? 81   VAL S CG2 1 
ATOM   19281 N  N   . GLY R  1 82  ? 63.286  125.964 22.000  1.00 29.78 ? 82   GLY S N   1 
ATOM   19282 C  CA  . GLY R  1 82  ? 62.085  125.143 22.039  1.00 29.66 ? 82   GLY S CA  1 
ATOM   19283 C  C   . GLY R  1 82  ? 62.301  123.658 21.803  1.00 29.51 ? 82   GLY S C   1 
ATOM   19284 O  O   . GLY R  1 82  ? 61.352  122.869 21.822  1.00 29.91 ? 82   GLY S O   1 
ATOM   19285 N  N   . ASP R  1 83  ? 63.552  123.271 21.586  1.00 29.15 ? 83   ASP S N   1 
ATOM   19286 C  CA  . ASP R  1 83  ? 63.869  121.903 21.179  1.00 28.62 ? 83   ASP S CA  1 
ATOM   19287 C  C   . ASP R  1 83  ? 63.853  120.877 22.297  1.00 28.75 ? 83   ASP S C   1 
ATOM   19288 O  O   . ASP R  1 83  ? 64.884  120.598 22.918  1.00 28.72 ? 83   ASP S O   1 
ATOM   19289 C  CB  . ASP R  1 83  ? 65.213  121.860 20.446  1.00 28.59 ? 83   ASP S CB  1 
ATOM   19290 C  CG  . ASP R  1 83  ? 65.113  122.406 19.027  1.00 28.19 ? 83   ASP S CG  1 
ATOM   19291 O  OD1 . ASP R  1 83  ? 63.966  122.593 18.543  1.00 26.22 ? 83   ASP S OD1 1 
ATOM   19292 O  OD2 . ASP R  1 83  ? 66.118  122.667 18.331  1.00 28.45 ? 83   ASP S OD2 1 
ATOM   19293 N  N   . LEU R  1 84  ? 62.689  120.289 22.523  1.00 27.92 ? 84   LEU S N   1 
ATOM   19294 C  CA  . LEU R  1 84  ? 62.560  119.296 23.578  1.00 28.28 ? 84   LEU S CA  1 
ATOM   19295 C  C   . LEU R  1 84  ? 62.642  117.854 23.066  1.00 28.39 ? 84   LEU S C   1 
ATOM   19296 O  O   . LEU R  1 84  ? 62.385  116.908 23.807  1.00 28.97 ? 84   LEU S O   1 
ATOM   19297 C  CB  . LEU R  1 84  ? 61.291  119.555 24.389  1.00 27.99 ? 84   LEU S CB  1 
ATOM   19298 C  CG  . LEU R  1 84  ? 61.298  120.935 25.057  1.00 27.64 ? 84   LEU S CG  1 
ATOM   19299 C  CD1 . LEU R  1 84  ? 59.951  121.248 25.674  1.00 25.92 ? 84   LEU S CD1 1 
ATOM   19300 C  CD2 . LEU R  1 84  ? 62.414  121.049 26.111  1.00 29.12 ? 84   LEU S CD2 1 
ATOM   19301 N  N   . GLY R  1 85  ? 63.011  117.693 21.800  1.00 28.38 ? 85   GLY S N   1 
ATOM   19302 C  CA  . GLY R  1 85  ? 63.217  116.373 21.218  1.00 28.25 ? 85   GLY S CA  1 
ATOM   19303 C  C   . GLY R  1 85  ? 61.992  115.516 20.944  1.00 27.91 ? 85   GLY S C   1 
ATOM   19304 O  O   . GLY R  1 85  ? 61.080  115.948 20.245  1.00 27.84 ? 85   GLY S O   1 
ATOM   19305 N  N   . ASN R  1 86  ? 61.976  114.301 21.506  1.00 27.37 ? 86   ASN S N   1 
ATOM   19306 C  CA  . ASN R  1 86  ? 60.901  113.348 21.256  1.00 27.06 ? 86   ASN S CA  1 
ATOM   19307 C  C   . ASN R  1 86  ? 60.283  112.781 22.520  1.00 26.82 ? 86   ASN S C   1 
ATOM   19308 O  O   . ASN R  1 86  ? 60.984  112.486 23.498  1.00 26.91 ? 86   ASN S O   1 
ATOM   19309 C  CB  . ASN R  1 86  ? 61.408  112.127 20.462  1.00 27.37 ? 86   ASN S CB  1 
ATOM   19310 C  CG  . ASN R  1 86  ? 61.938  112.484 19.093  1.00 28.23 ? 86   ASN S CG  1 
ATOM   19311 O  OD1 . ASN R  1 86  ? 61.197  112.974 18.237  1.00 32.60 ? 86   ASN S OD1 1 
ATOM   19312 N  ND2 . ASN R  1 86  ? 63.223  112.228 18.869  1.00 27.91 ? 86   ASN S ND2 1 
ATOM   19313 N  N   . VAL R  1 87  ? 58.973  112.614 22.497  1.00 26.30 ? 87   VAL S N   1 
ATOM   19314 C  CA  . VAL R  1 87  ? 58.330  111.850 23.553  1.00 26.77 ? 87   VAL S CA  1 
ATOM   19315 C  C   . VAL R  1 87  ? 58.118  110.492 22.907  1.00 26.80 ? 87   VAL S C   1 
ATOM   19316 O  O   . VAL R  1 87  ? 58.282  110.352 21.683  1.00 27.38 ? 87   VAL S O   1 
ATOM   19317 C  CB  . VAL R  1 87  ? 56.998  112.469 24.044  1.00 27.03 ? 87   VAL S CB  1 
ATOM   19318 C  CG1 . VAL R  1 87  ? 57.244  113.862 24.617  1.00 27.74 ? 87   VAL S CG1 1 
ATOM   19319 C  CG2 . VAL R  1 87  ? 55.956  112.504 22.937  1.00 27.12 ? 87   VAL S CG2 1 
ATOM   19320 N  N   . THR R  1 88  ? 57.772  109.489 23.702  1.00 26.47 ? 88   THR S N   1 
ATOM   19321 C  CA  . THR R  1 88  ? 57.614  108.141 23.172  1.00 26.34 ? 88   THR S CA  1 
ATOM   19322 C  C   . THR R  1 88  ? 56.246  107.544 23.529  1.00 26.01 ? 88   THR S C   1 
ATOM   19323 O  O   . THR R  1 88  ? 55.902  107.430 24.712  1.00 25.65 ? 88   THR S O   1 
ATOM   19324 C  CB  . THR R  1 88  ? 58.750  107.228 23.709  1.00 26.81 ? 88   THR S CB  1 
ATOM   19325 O  OG1 . THR R  1 88  ? 60.005  107.569 23.084  1.00 26.72 ? 88   THR S OG1 1 
ATOM   19326 C  CG2 . THR R  1 88  ? 58.523  105.777 23.290  1.00 27.79 ? 88   THR S CG2 1 
ATOM   19327 N  N   . ALA R  1 89  ? 55.478  107.165 22.510  1.00 25.13 ? 89   ALA S N   1 
ATOM   19328 C  CA  . ALA R  1 89  ? 54.175  106.529 22.724  1.00 24.77 ? 89   ALA S CA  1 
ATOM   19329 C  C   . ALA R  1 89  ? 54.313  105.014 22.795  1.00 25.12 ? 89   ALA S C   1 
ATOM   19330 O  O   . ALA R  1 89  ? 54.933  104.394 21.923  1.00 23.54 ? 89   ALA S O   1 
ATOM   19331 C  CB  . ALA R  1 89  ? 53.201  106.900 21.611  1.00 24.49 ? 89   ALA S CB  1 
ATOM   19332 N  N   . ASP R  1 90  ? 53.709  104.420 23.829  1.00 26.10 ? 90   ASP S N   1 
ATOM   19333 C  CA  . ASP R  1 90  ? 53.718  102.974 23.991  1.00 27.42 ? 90   ASP S CA  1 
ATOM   19334 C  C   . ASP R  1 90  ? 52.665  102.385 23.060  1.00 27.72 ? 90   ASP S C   1 
ATOM   19335 O  O   . ASP R  1 90  ? 52.087  103.109 22.237  1.00 27.78 ? 90   ASP S O   1 
ATOM   19336 C  CB  . ASP R  1 90  ? 53.474  102.563 25.459  1.00 27.63 ? 90   ASP S CB  1 
ATOM   19337 C  CG  . ASP R  1 90  ? 52.099  102.971 25.973  1.00 30.19 ? 90   ASP S CG  1 
ATOM   19338 O  OD1 . ASP R  1 90  ? 51.268  103.444 25.166  1.00 33.42 ? 90   ASP S OD1 1 
ATOM   19339 O  OD2 . ASP R  1 90  ? 51.749  102.851 27.176  1.00 33.10 ? 90   ASP S OD2 1 
ATOM   19340 N  N   . LYS R  1 91  ? 52.405  101.087 23.188  1.00 28.02 ? 91   LYS S N   1 
ATOM   19341 C  CA  . LYS R  1 91  ? 51.429  100.433 22.314  1.00 28.72 ? 91   LYS S CA  1 
ATOM   19342 C  C   . LYS R  1 91  ? 49.986  100.947 22.472  1.00 28.74 ? 91   LYS S C   1 
ATOM   19343 O  O   . LYS R  1 91  ? 49.170  100.777 21.570  1.00 28.35 ? 91   LYS S O   1 
ATOM   19344 C  CB  . LYS R  1 91  ? 51.507  98.898  22.398  1.00 28.62 ? 91   LYS S CB  1 
ATOM   19345 C  CG  . LYS R  1 91  ? 51.433  98.295  23.797  1.00 30.10 ? 91   LYS S CG  1 
ATOM   19346 C  CD  . LYS R  1 91  ? 50.941  96.840  23.745  1.00 31.58 ? 91   LYS S CD  1 
ATOM   19347 C  CE  . LYS R  1 91  ? 51.101  96.134  25.086  1.00 31.74 ? 91   LYS S CE  1 
ATOM   19348 N  NZ  . LYS R  1 91  ? 50.233  94.917  25.205  1.00 35.91 ? 91   LYS S NZ  1 
ATOM   19349 N  N   . ASP R  1 92  ? 49.682  101.584 23.600  1.00 29.38 ? 92   ASP S N   1 
ATOM   19350 C  CA  . ASP R  1 92  ? 48.350  102.155 23.820  1.00 30.35 ? 92   ASP S CA  1 
ATOM   19351 C  C   . ASP R  1 92  ? 48.187  103.529 23.212  1.00 30.22 ? 92   ASP S C   1 
ATOM   19352 O  O   . ASP R  1 92  ? 47.105  104.112 23.281  1.00 29.68 ? 92   ASP S O   1 
ATOM   19353 C  CB  . ASP R  1 92  ? 48.074  102.335 25.297  1.00 30.75 ? 92   ASP S CB  1 
ATOM   19354 C  CG  . ASP R  1 92  ? 48.327  101.117 26.058  1.00 32.79 ? 92   ASP S CG  1 
ATOM   19355 O  OD1 . ASP R  1 92  ? 47.890  100.058 25.575  1.00 36.44 ? 92   ASP S OD1 1 
ATOM   19356 O  OD2 . ASP R  1 92  ? 48.957  101.112 27.133  1.00 34.73 ? 92   ASP S OD2 1 
ATOM   19357 N  N   . GLY R  1 93  ? 49.267  104.069 22.668  1.00 30.57 ? 93   GLY S N   1 
ATOM   19358 C  CA  . GLY R  1 93  ? 49.219  105.409 22.115  1.00 31.47 ? 93   GLY S CA  1 
ATOM   19359 C  C   . GLY R  1 93  ? 49.394  106.456 23.200  1.00 32.24 ? 93   GLY S C   1 
ATOM   19360 O  O   . GLY R  1 93  ? 49.142  107.642 22.989  1.00 32.15 ? 93   GLY S O   1 
ATOM   19361 N  N   . VAL R  1 94  ? 49.819  106.011 24.378  1.00 33.00 ? 94   VAL S N   1 
ATOM   19362 C  CA  . VAL R  1 94  ? 50.046  106.926 25.484  1.00 34.01 ? 94   VAL S CA  1 
ATOM   19363 C  C   . VAL R  1 94  ? 51.526  107.201 25.663  1.00 34.69 ? 94   VAL S C   1 
ATOM   19364 O  O   . VAL R  1 94  ? 52.336  106.276 25.736  1.00 34.39 ? 94   VAL S O   1 
ATOM   19365 C  CB  . VAL R  1 94  ? 49.490  106.372 26.795  1.00 33.92 ? 94   VAL S CB  1 
ATOM   19366 C  CG1 . VAL R  1 94  ? 49.740  107.358 27.922  1.00 34.17 ? 94   VAL S CG1 1 
ATOM   19367 C  CG2 . VAL R  1 94  ? 48.007  106.073 26.649  1.00 34.48 ? 94   VAL S CG2 1 
ATOM   19368 N  N   . ALA R  1 95  ? 51.876  108.481 25.711  1.00 35.79 ? 95   ALA S N   1 
ATOM   19369 C  CA  . ALA R  1 95  ? 53.254  108.886 25.930  1.00 36.93 ? 95   ALA S CA  1 
ATOM   19370 C  C   . ALA R  1 95  ? 53.340  109.526 27.303  1.00 37.80 ? 95   ALA S C   1 
ATOM   19371 O  O   . ALA R  1 95  ? 52.719  110.558 27.538  1.00 37.72 ? 95   ALA S O   1 
ATOM   19372 C  CB  . ALA R  1 95  ? 53.696  109.870 24.852  1.00 36.44 ? 95   ALA S CB  1 
ATOM   19373 N  N   . ASP R  1 96  ? 54.073  108.891 28.218  1.00 39.17 ? 96   ASP S N   1 
ATOM   19374 C  CA  . ASP R  1 96  ? 54.262  109.439 29.561  1.00 40.60 ? 96   ASP S CA  1 
ATOM   19375 C  C   . ASP R  1 96  ? 55.498  110.334 29.558  1.00 41.07 ? 96   ASP S C   1 
ATOM   19376 O  O   . ASP R  1 96  ? 56.641  109.860 29.490  1.00 41.44 ? 96   ASP S O   1 
ATOM   19377 C  CB  . ASP R  1 96  ? 54.370  108.327 30.616  1.00 40.93 ? 96   ASP S CB  1 
ATOM   19378 C  CG  . ASP R  1 96  ? 53.032  107.635 30.873  1.00 42.82 ? 96   ASP S CG  1 
ATOM   19379 O  OD1 . ASP R  1 96  ? 53.018  106.390 31.007  1.00 44.66 ? 96   ASP S OD1 1 
ATOM   19380 O  OD2 . ASP R  1 96  ? 51.943  108.255 30.951  1.00 43.79 ? 96   ASP S OD2 1 
ATOM   19381 N  N   . VAL R  1 97  ? 55.257  111.637 29.631  1.00 41.51 ? 97   VAL S N   1 
ATOM   19382 C  CA  . VAL R  1 97  ? 56.328  112.619 29.542  1.00 41.90 ? 97   VAL S CA  1 
ATOM   19383 C  C   . VAL R  1 97  ? 56.943  112.973 30.891  1.00 42.07 ? 97   VAL S C   1 
ATOM   19384 O  O   . VAL R  1 97  ? 56.245  113.243 31.868  1.00 41.71 ? 97   VAL S O   1 
ATOM   19385 C  CB  . VAL R  1 97  ? 55.847  113.886 28.804  1.00 41.82 ? 97   VAL S CB  1 
ATOM   19386 C  CG1 . VAL R  1 97  ? 57.022  114.805 28.447  1.00 41.90 ? 97   VAL S CG1 1 
ATOM   19387 C  CG2 . VAL R  1 97  ? 55.093  113.479 27.555  1.00 42.15 ? 97   VAL S CG2 1 
ATOM   19388 N  N   . SER R  1 98  ? 58.271  112.930 30.917  1.00 42.69 ? 98   SER S N   1 
ATOM   19389 C  CA  . SER R  1 98  ? 59.073  113.290 32.077  1.00 43.00 ? 98   SER S CA  1 
ATOM   19390 C  C   . SER R  1 98  ? 60.406  113.787 31.517  1.00 43.18 ? 98   SER S C   1 
ATOM   19391 O  O   . SER R  1 98  ? 61.227  112.998 31.035  1.00 43.19 ? 98   SER S O   1 
ATOM   19392 C  CB  . SER R  1 98  ? 59.272  112.095 33.013  1.00 43.23 ? 98   SER S CB  1 
ATOM   19393 O  OG  . SER R  1 98  ? 59.526  112.520 34.345  1.00 42.85 ? 98   SER S OG  1 
ATOM   19394 N  N   . ILE R  1 99  ? 60.582  115.106 31.559  1.00 42.94 ? 99   ILE S N   1 
ATOM   19395 C  CA  . ILE R  1 99  ? 61.742  115.784 31.006  1.00 42.69 ? 99   ILE S CA  1 
ATOM   19396 C  C   . ILE R  1 99  ? 62.232  116.851 31.979  1.00 42.18 ? 99   ILE S C   1 
ATOM   19397 O  O   . ILE R  1 99  ? 61.445  117.443 32.716  1.00 42.07 ? 99   ILE S O   1 
ATOM   19398 C  CB  . ILE R  1 99  ? 61.348  116.465 29.668  1.00 42.76 ? 99   ILE S CB  1 
ATOM   19399 C  CG1 . ILE R  1 99  ? 61.012  115.419 28.598  1.00 43.02 ? 99   ILE S CG1 1 
ATOM   19400 C  CG2 . ILE R  1 99  ? 62.445  117.419 29.180  1.00 43.59 ? 99   ILE S CG2 1 
ATOM   19401 C  CD1 . ILE R  1 99  ? 60.490  116.014 27.291  1.00 42.46 ? 99   ILE S CD1 1 
ATOM   19402 N  N   . GLU R  1 100 ? 63.541  117.060 32.008  1.00 41.83 ? 100  GLU S N   1 
ATOM   19403 C  CA  . GLU R  1 100 ? 64.119  118.176 32.737  1.00 41.55 ? 100  GLU S CA  1 
ATOM   19404 C  C   . GLU R  1 100 ? 64.942  118.972 31.731  1.00 41.16 ? 100  GLU S C   1 
ATOM   19405 O  O   . GLU R  1 100 ? 65.789  118.409 31.032  1.00 40.82 ? 100  GLU S O   1 
ATOM   19406 C  CB  . GLU R  1 100 ? 64.990  117.715 33.908  1.00 41.74 ? 100  GLU S CB  1 
ATOM   19407 C  CG  . GLU R  1 100 ? 65.869  118.829 34.460  1.00 42.56 ? 100  GLU S CG  1 
ATOM   19408 C  CD  . GLU R  1 100 ? 66.417  118.534 35.842  1.00 43.26 ? 100  GLU S CD  1 
ATOM   19409 O  OE1 . GLU R  1 100 ? 65.609  118.380 36.790  1.00 42.98 ? 100  GLU S OE1 1 
ATOM   19410 O  OE2 . GLU R  1 100 ? 67.660  118.471 35.980  1.00 42.96 ? 100  GLU S OE2 1 
ATOM   19411 N  N   . ASP R  1 101 ? 64.677  120.272 31.638  1.00 40.77 ? 101  ASP S N   1 
ATOM   19412 C  CA  . ASP R  1 101 ? 65.399  121.115 30.695  1.00 40.57 ? 101  ASP S CA  1 
ATOM   19413 C  C   . ASP R  1 101 ? 65.851  122.419 31.327  1.00 40.17 ? 101  ASP S C   1 
ATOM   19414 O  O   . ASP R  1 101 ? 65.108  123.047 32.073  1.00 40.08 ? 101  ASP S O   1 
ATOM   19415 C  CB  . ASP R  1 101 ? 64.555  121.392 29.451  1.00 40.56 ? 101  ASP S CB  1 
ATOM   19416 C  CG  . ASP R  1 101 ? 65.389  121.919 28.293  1.00 40.86 ? 101  ASP S CG  1 
ATOM   19417 O  OD1 . ASP R  1 101 ? 66.104  121.096 27.669  1.00 40.55 ? 101  ASP S OD1 1 
ATOM   19418 O  OD2 . ASP R  1 101 ? 65.399  123.126 27.946  1.00 39.49 ? 101  ASP S OD2 1 
ATOM   19419 N  N   . SER R  1 102 ? 67.073  122.824 31.001  1.00 40.03 ? 102  SER S N   1 
ATOM   19420 C  CA  . SER R  1 102 ? 67.665  124.028 31.564  1.00 40.06 ? 102  SER S CA  1 
ATOM   19421 C  C   . SER R  1 102 ? 67.867  125.139 30.537  1.00 39.89 ? 102  SER S C   1 
ATOM   19422 O  O   . SER R  1 102 ? 68.374  126.207 30.868  1.00 39.97 ? 102  SER S O   1 
ATOM   19423 C  CB  . SER R  1 102 ? 69.004  123.691 32.225  1.00 40.16 ? 102  SER S CB  1 
ATOM   19424 O  OG  . SER R  1 102 ? 68.827  122.859 33.361  1.00 40.63 ? 102  SER S OG  1 
ATOM   19425 N  N   . VAL R  1 103 ? 67.496  124.890 29.287  1.00 39.74 ? 103  VAL S N   1 
ATOM   19426 C  CA  . VAL R  1 103 ? 67.620  125.929 28.273  1.00 39.73 ? 103  VAL S CA  1 
ATOM   19427 C  C   . VAL R  1 103 ? 66.340  126.750 28.275  1.00 39.67 ? 103  VAL S C   1 
ATOM   19428 O  O   . VAL R  1 103 ? 66.377  127.984 28.269  1.00 39.39 ? 103  VAL S O   1 
ATOM   19429 C  CB  . VAL R  1 103 ? 67.925  125.358 26.881  1.00 39.65 ? 103  VAL S CB  1 
ATOM   19430 C  CG1 . VAL R  1 103 ? 67.754  126.428 25.805  1.00 39.85 ? 103  VAL S CG1 1 
ATOM   19431 C  CG2 . VAL R  1 103 ? 69.333  124.805 26.848  1.00 39.87 ? 103  VAL S CG2 1 
ATOM   19432 N  N   . ILE R  1 104 ? 65.206  126.058 28.305  1.00 39.64 ? 104  ILE S N   1 
ATOM   19433 C  CA  . ILE R  1 104 ? 63.930  126.736 28.433  1.00 39.84 ? 104  ILE S CA  1 
ATOM   19434 C  C   . ILE R  1 104 ? 63.847  127.286 29.852  1.00 40.18 ? 104  ILE S C   1 
ATOM   19435 O  O   . ILE R  1 104 ? 64.562  126.833 30.752  1.00 39.48 ? 104  ILE S O   1 
ATOM   19436 C  CB  . ILE R  1 104 ? 62.759  125.767 28.191  1.00 39.84 ? 104  ILE S CB  1 
ATOM   19437 C  CG1 . ILE R  1 104 ? 62.775  124.648 29.237  1.00 39.66 ? 104  ILE S CG1 1 
ATOM   19438 C  CG2 . ILE R  1 104 ? 62.793  125.206 26.764  1.00 39.76 ? 104  ILE S CG2 1 
ATOM   19439 C  CD1 . ILE R  1 104 ? 61.586  123.732 29.173  1.00 39.77 ? 104  ILE S CD1 1 
ATOM   19440 N  N   . SER R  1 105 ? 62.974  128.265 30.047  1.00 40.80 ? 105  SER S N   1 
ATOM   19441 C  CA  . SER R  1 105 ? 62.782  128.861 31.363  1.00 41.40 ? 105  SER S CA  1 
ATOM   19442 C  C   . SER R  1 105 ? 61.348  129.365 31.488  1.00 42.03 ? 105  SER S C   1 
ATOM   19443 O  O   . SER R  1 105 ? 60.595  129.368 30.508  1.00 41.88 ? 105  SER S O   1 
ATOM   19444 C  CB  . SER R  1 105 ? 63.780  130.000 31.591  1.00 41.31 ? 105  SER S CB  1 
ATOM   19445 O  OG  . SER R  1 105 ? 63.703  130.489 32.918  1.00 41.05 ? 105  SER S OG  1 
ATOM   19446 N  N   . LEU R  1 106 ? 60.967  129.770 32.697  1.00 42.85 ? 106  LEU S N   1 
ATOM   19447 C  CA  . LEU R  1 106 ? 59.626  130.297 32.936  1.00 43.68 ? 106  LEU S CA  1 
ATOM   19448 C  C   . LEU R  1 106 ? 59.673  131.794 33.231  1.00 44.21 ? 106  LEU S C   1 
ATOM   19449 O  O   . LEU R  1 106 ? 58.674  132.387 33.643  1.00 44.26 ? 106  LEU S O   1 
ATOM   19450 C  CB  . LEU R  1 106 ? 58.929  129.536 34.067  1.00 43.58 ? 106  LEU S CB  1 
ATOM   19451 C  CG  . LEU R  1 106 ? 58.739  128.043 33.796  1.00 43.72 ? 106  LEU S CG  1 
ATOM   19452 C  CD1 . LEU R  1 106 ? 57.879  127.400 34.883  1.00 43.77 ? 106  LEU S CD1 1 
ATOM   19453 C  CD2 . LEU R  1 106 ? 58.128  127.832 32.411  1.00 43.15 ? 106  LEU S CD2 1 
ATOM   19454 N  N   . SER R  1 107 ? 60.847  132.386 33.013  1.00 45.01 ? 107  SER S N   1 
ATOM   19455 C  CA  . SER R  1 107 ? 61.068  133.823 33.177  1.00 45.77 ? 107  SER S CA  1 
ATOM   19456 C  C   . SER R  1 107 ? 62.313  134.235 32.391  1.00 46.11 ? 107  SER S C   1 
ATOM   19457 O  O   . SER R  1 107 ? 63.120  133.388 32.005  1.00 46.35 ? 107  SER S O   1 
ATOM   19458 C  CB  . SER R  1 107 ? 61.249  134.187 34.652  1.00 45.91 ? 107  SER S CB  1 
ATOM   19459 O  OG  . SER R  1 107 ? 62.592  133.993 35.068  1.00 46.50 ? 107  SER S OG  1 
ATOM   19460 N  N   . GLY R  1 108 ? 62.467  135.532 32.149  1.00 46.40 ? 108  GLY S N   1 
ATOM   19461 C  CA  . GLY R  1 108 ? 63.637  136.034 31.445  1.00 46.57 ? 108  GLY S CA  1 
ATOM   19462 C  C   . GLY R  1 108 ? 63.562  135.903 29.935  1.00 46.57 ? 108  GLY S C   1 
ATOM   19463 O  O   . GLY R  1 108 ? 62.478  135.736 29.380  1.00 46.86 ? 108  GLY S O   1 
ATOM   19464 N  N   . ASP R  1 109 ? 64.723  135.976 29.280  1.00 46.56 ? 109  ASP S N   1 
ATOM   19465 C  CA  . ASP R  1 109 ? 64.839  135.891 27.812  1.00 46.38 ? 109  ASP S CA  1 
ATOM   19466 C  C   . ASP R  1 109 ? 64.312  134.602 27.180  1.00 45.88 ? 109  ASP S C   1 
ATOM   19467 O  O   . ASP R  1 109 ? 63.801  134.619 26.056  1.00 45.71 ? 109  ASP S O   1 
ATOM   19468 C  CB  . ASP R  1 109 ? 66.300  136.068 27.377  1.00 46.70 ? 109  ASP S CB  1 
ATOM   19469 C  CG  . ASP R  1 109 ? 66.678  137.519 27.159  1.00 47.65 ? 109  ASP S CG  1 
ATOM   19470 O  OD1 . ASP R  1 109 ? 67.847  137.771 26.794  1.00 48.83 ? 109  ASP S OD1 1 
ATOM   19471 O  OD2 . ASP R  1 109 ? 65.885  138.471 27.324  1.00 48.50 ? 109  ASP S OD2 1 
ATOM   19472 N  N   . HIS R  1 110 ? 64.461  133.487 27.890  1.00 45.17 ? 110  HIS S N   1 
ATOM   19473 C  CA  . HIS R  1 110 ? 64.041  132.188 27.372  1.00 44.43 ? 110  HIS S CA  1 
ATOM   19474 C  C   . HIS R  1 110 ? 62.685  131.747 27.908  1.00 43.88 ? 110  HIS S C   1 
ATOM   19475 O  O   . HIS R  1 110 ? 62.393  130.552 27.952  1.00 43.68 ? 110  HIS S O   1 
ATOM   19476 C  CB  . HIS R  1 110 ? 65.095  131.130 27.684  1.00 44.46 ? 110  HIS S CB  1 
ATOM   19477 C  CG  . HIS R  1 110 ? 66.406  131.369 27.004  1.00 44.96 ? 110  HIS S CG  1 
ATOM   19478 N  ND1 . HIS R  1 110 ? 67.486  130.524 27.148  1.00 45.64 ? 110  HIS S ND1 1 
ATOM   19479 C  CD2 . HIS R  1 110 ? 66.810  132.357 26.170  1.00 45.61 ? 110  HIS S CD2 1 
ATOM   19480 C  CE1 . HIS R  1 110 ? 68.499  130.982 26.436  1.00 45.94 ? 110  HIS S CE1 1 
ATOM   19481 N  NE2 . HIS R  1 110 ? 68.116  132.094 25.834  1.00 46.27 ? 110  HIS S NE2 1 
ATOM   19482 N  N   . CYS R  1 111 ? 61.864  132.717 28.306  1.00 43.20 ? 111  CYS S N   1 
ATOM   19483 C  CA  . CYS R  1 111 ? 60.537  132.447 28.850  1.00 42.66 ? 111  CYS S CA  1 
ATOM   19484 C  C   . CYS R  1 111 ? 59.595  131.876 27.794  1.00 42.10 ? 111  CYS S C   1 
ATOM   19485 O  O   . CYS R  1 111 ? 59.451  132.435 26.707  1.00 41.93 ? 111  CYS S O   1 
ATOM   19486 C  CB  . CYS R  1 111 ? 59.938  133.715 29.450  1.00 42.74 ? 111  CYS S CB  1 
ATOM   19487 S  SG  . CYS R  1 111 ? 58.478  133.416 30.462  1.00 43.56 ? 111  CYS S SG  1 
ATOM   19488 N  N   . ILE R  1 112 ? 58.948  130.765 28.135  1.00 41.46 ? 112  ILE S N   1 
ATOM   19489 C  CA  . ILE R  1 112 ? 58.062  130.068 27.212  1.00 41.01 ? 112  ILE S CA  1 
ATOM   19490 C  C   . ILE R  1 112 ? 56.592  130.250 27.570  1.00 40.64 ? 112  ILE S C   1 
ATOM   19491 O  O   . ILE R  1 112 ? 55.708  129.709 26.901  1.00 40.64 ? 112  ILE S O   1 
ATOM   19492 C  CB  . ILE R  1 112 ? 58.420  128.566 27.147  1.00 41.07 ? 112  ILE S CB  1 
ATOM   19493 C  CG1 . ILE R  1 112 ? 58.233  127.905 28.517  1.00 41.14 ? 112  ILE S CG1 1 
ATOM   19494 C  CG2 . ILE R  1 112 ? 59.847  128.385 26.660  1.00 40.88 ? 112  ILE S CG2 1 
ATOM   19495 C  CD1 . ILE R  1 112 ? 58.573  126.426 28.533  1.00 41.36 ? 112  ILE S CD1 1 
ATOM   19496 N  N   . ILE R  1 113 ? 56.336  130.997 28.639  1.00 40.00 ? 113  ILE S N   1 
ATOM   19497 C  CA  . ILE R  1 113 ? 54.968  131.291 29.030  1.00 39.48 ? 113  ILE S CA  1 
ATOM   19498 C  C   . ILE R  1 113 ? 54.342  132.079 27.888  1.00 38.94 ? 113  ILE S C   1 
ATOM   19499 O  O   . ILE R  1 113 ? 54.968  132.991 27.348  1.00 39.08 ? 113  ILE S O   1 
ATOM   19500 C  CB  . ILE R  1 113 ? 54.941  132.124 30.327  1.00 39.45 ? 113  ILE S CB  1 
ATOM   19501 C  CG1 . ILE R  1 113 ? 55.662  131.389 31.454  1.00 39.64 ? 113  ILE S CG1 1 
ATOM   19502 C  CG2 . ILE R  1 113 ? 53.512  132.423 30.739  1.00 39.67 ? 113  ILE S CG2 1 
ATOM   19503 C  CD1 . ILE R  1 113 ? 54.814  130.343 32.144  1.00 41.12 ? 113  ILE S CD1 1 
ATOM   19504 N  N   . GLY R  1 114 ? 53.121  131.721 27.511  1.00 38.23 ? 114  GLY S N   1 
ATOM   19505 C  CA  . GLY R  1 114 ? 52.429  132.423 26.447  1.00 37.67 ? 114  GLY S CA  1 
ATOM   19506 C  C   . GLY R  1 114 ? 52.832  131.945 25.069  1.00 37.37 ? 114  GLY S C   1 
ATOM   19507 O  O   . GLY R  1 114 ? 52.385  132.497 24.063  1.00 37.37 ? 114  GLY S O   1 
ATOM   19508 N  N   . ARG R  1 115 ? 53.690  130.928 25.018  1.00 36.78 ? 115  ARG S N   1 
ATOM   19509 C  CA  . ARG R  1 115 ? 54.096  130.354 23.739  1.00 36.46 ? 115  ARG S CA  1 
ATOM   19510 C  C   . ARG R  1 115 ? 53.325  129.056 23.527  1.00 35.86 ? 115  ARG S C   1 
ATOM   19511 O  O   . ARG R  1 115 ? 52.372  128.786 24.259  1.00 35.44 ? 115  ARG S O   1 
ATOM   19512 C  CB  . ARG R  1 115 ? 55.614  130.154 23.675  1.00 36.76 ? 115  ARG S CB  1 
ATOM   19513 C  CG  . ARG R  1 115 ? 56.373  131.381 24.166  1.00 36.73 ? 115  ARG S CG  1 
ATOM   19514 C  CD  . ARG R  1 115 ? 57.706  131.638 23.480  1.00 36.68 ? 115  ARG S CD  1 
ATOM   19515 N  NE  . ARG R  1 115 ? 58.285  132.907 23.919  1.00 36.80 ? 115  ARG S NE  1 
ATOM   19516 C  CZ  . ARG R  1 115 ? 58.375  133.995 23.163  1.00 36.28 ? 115  ARG S CZ  1 
ATOM   19517 N  NH1 . ARG R  1 115 ? 57.932  133.971 21.910  1.00 35.29 ? 115  ARG S NH1 1 
ATOM   19518 N  NH2 . ARG R  1 115 ? 58.920  135.105 23.654  1.00 34.97 ? 115  ARG S NH2 1 
ATOM   19519 N  N   . THR R  1 116 ? 53.729  128.253 22.544  1.00 35.02 ? 116  THR S N   1 
ATOM   19520 C  CA  . THR R  1 116 ? 52.951  127.071 22.209  1.00 34.53 ? 116  THR S CA  1 
ATOM   19521 C  C   . THR R  1 116 ? 53.710  125.754 22.253  1.00 34.23 ? 116  THR S C   1 
ATOM   19522 O  O   . THR R  1 116 ? 54.762  125.602 21.628  1.00 34.23 ? 116  THR S O   1 
ATOM   19523 C  CB  . THR R  1 116 ? 52.324  127.236 20.807  1.00 34.66 ? 116  THR S CB  1 
ATOM   19524 O  OG1 . THR R  1 116 ? 51.466  128.384 20.791  1.00 35.54 ? 116  THR S OG1 1 
ATOM   19525 C  CG2 . THR R  1 116 ? 51.374  126.092 20.505  1.00 34.76 ? 116  THR S CG2 1 
ATOM   19526 N  N   . LEU R  1 117 ? 53.151  124.791 22.975  1.00 33.13 ? 117  LEU S N   1 
ATOM   19527 C  CA  . LEU R  1 117 ? 53.729  123.455 23.029  1.00 32.42 ? 117  LEU S CA  1 
ATOM   19528 C  C   . LEU R  1 117 ? 53.057  122.586 21.951  1.00 31.99 ? 117  LEU S C   1 
ATOM   19529 O  O   . LEU R  1 117 ? 51.823  122.518 21.873  1.00 31.81 ? 117  LEU S O   1 
ATOM   19530 C  CB  . LEU R  1 117 ? 53.515  122.862 24.415  1.00 32.34 ? 117  LEU S CB  1 
ATOM   19531 C  CG  . LEU R  1 117 ? 54.223  121.536 24.679  1.00 32.55 ? 117  LEU S CG  1 
ATOM   19532 C  CD1 . LEU R  1 117 ? 55.734  121.725 24.609  1.00 30.26 ? 117  LEU S CD1 1 
ATOM   19533 C  CD2 . LEU R  1 117 ? 53.784  120.975 26.034  1.00 30.60 ? 117  LEU S CD2 1 
ATOM   19534 N  N   . VAL R  1 118 ? 53.866  121.931 21.124  1.00 31.09 ? 118  VAL S N   1 
ATOM   19535 C  CA  . VAL R  1 118 ? 53.364  121.136 19.998  1.00 30.26 ? 118  VAL S CA  1 
ATOM   19536 C  C   . VAL R  1 118 ? 53.870  119.691 20.024  1.00 29.83 ? 118  VAL S C   1 
ATOM   19537 O  O   . VAL R  1 118 ? 55.047  119.442 20.324  1.00 28.98 ? 118  VAL S O   1 
ATOM   19538 C  CB  . VAL R  1 118 ? 53.821  121.769 18.670  1.00 30.52 ? 118  VAL S CB  1 
ATOM   19539 C  CG1 . VAL R  1 118 ? 53.448  120.878 17.458  1.00 31.06 ? 118  VAL S CG1 1 
ATOM   19540 C  CG2 . VAL R  1 118 ? 53.233  123.181 18.510  1.00 30.25 ? 118  VAL S CG2 1 
ATOM   19541 N  N   . VAL R  1 119 ? 52.981  118.738 19.741  1.00 28.93 ? 119  VAL S N   1 
ATOM   19542 C  CA  . VAL R  1 119 ? 53.409  117.350 19.587  1.00 28.54 ? 119  VAL S CA  1 
ATOM   19543 C  C   . VAL R  1 119 ? 53.241  116.955 18.105  1.00 28.32 ? 119  VAL S C   1 
ATOM   19544 O  O   . VAL R  1 119 ? 52.192  117.214 17.508  1.00 27.80 ? 119  VAL S O   1 
ATOM   19545 C  CB  . VAL R  1 119 ? 52.653  116.401 20.517  1.00 28.45 ? 119  VAL S CB  1 
ATOM   19546 C  CG1 . VAL R  1 119 ? 51.149  116.465 20.240  1.00 27.97 ? 119  VAL S CG1 1 
ATOM   19547 C  CG2 . VAL R  1 119 ? 53.204  114.984 20.383  1.00 29.21 ? 119  VAL S CG2 1 
ATOM   19548 N  N   . HIS R  1 120 ? 54.265  116.331 17.525  1.00 27.50 ? 120  HIS S N   1 
ATOM   19549 C  CA  . HIS R  1 120 ? 54.283  116.065 16.078  1.00 27.80 ? 120  HIS S CA  1 
ATOM   19550 C  C   . HIS R  1 120 ? 53.892  114.665 15.591  1.00 28.38 ? 120  HIS S C   1 
ATOM   19551 O  O   . HIS R  1 120 ? 53.879  113.703 16.349  1.00 28.28 ? 120  HIS S O   1 
ATOM   19552 C  CB  . HIS R  1 120 ? 55.658  116.423 15.509  1.00 27.24 ? 120  HIS S CB  1 
ATOM   19553 C  CG  . HIS R  1 120 ? 55.877  117.896 15.345  1.00 26.97 ? 120  HIS S CG  1 
ATOM   19554 N  ND1 . HIS R  1 120 ? 55.480  118.583 14.214  1.00 26.01 ? 120  HIS S ND1 1 
ATOM   19555 C  CD2 . HIS R  1 120 ? 56.455  118.816 16.160  1.00 26.03 ? 120  HIS S CD2 1 
ATOM   19556 C  CE1 . HIS R  1 120 ? 55.803  119.862 14.338  1.00 27.35 ? 120  HIS S CE1 1 
ATOM   19557 N  NE2 . HIS R  1 120 ? 56.394  120.029 15.510  1.00 25.94 ? 120  HIS S NE2 1 
ATOM   19558 N  N   . GLU R  1 121 ? 53.606  114.580 14.295  1.00 28.46 ? 121  GLU S N   1 
ATOM   19559 C  CA  . GLU R  1 121 ? 53.246  113.337 13.606  1.00 29.36 ? 121  GLU S CA  1 
ATOM   19560 C  C   . GLU R  1 121 ? 54.343  112.266 13.645  1.00 29.54 ? 121  GLU S C   1 
ATOM   19561 O  O   . GLU R  1 121 ? 54.067  111.062 13.832  1.00 29.24 ? 121  GLU S O   1 
ATOM   19562 C  CB  . GLU R  1 121 ? 52.953  113.666 12.118  1.00 29.34 ? 121  GLU S CB  1 
ATOM   19563 C  CG  . GLU R  1 121 ? 52.834  112.463 11.192  1.00 30.37 ? 121  GLU S CG  1 
ATOM   19564 C  CD  . GLU R  1 121 ? 52.970  112.821 9.711   1.00 31.61 ? 121  GLU S CD  1 
ATOM   19565 O  OE1 . GLU R  1 121 ? 53.214  114.008 9.383   1.00 30.12 ? 121  GLU S OE1 1 
ATOM   19566 O  OE2 . GLU R  1 121 ? 52.833  111.900 8.864   1.00 32.02 ? 121  GLU S OE2 1 
ATOM   19567 N  N   . LYS R  1 122 ? 55.579  112.734 13.449  1.00 30.04 ? 122  LYS S N   1 
ATOM   19568 C  CA  . LYS R  1 122 ? 56.758  111.896 13.259  1.00 30.34 ? 122  LYS S CA  1 
ATOM   19569 C  C   . LYS R  1 122 ? 57.883  112.182 14.246  1.00 29.22 ? 122  LYS S C   1 
ATOM   19570 O  O   . LYS R  1 122 ? 57.838  113.143 15.009  1.00 28.61 ? 122  LYS S O   1 
ATOM   19571 C  CB  . LYS R  1 122 ? 57.336  112.159 11.852  1.00 31.21 ? 122  LYS S CB  1 
ATOM   19572 C  CG  . LYS R  1 122 ? 56.474  111.696 10.684  1.00 35.05 ? 122  LYS S CG  1 
ATOM   19573 C  CD  . LYS R  1 122 ? 57.014  112.200 9.333   1.00 40.25 ? 122  LYS S CD  1 
ATOM   19574 C  CE  . LYS R  1 122 ? 58.376  111.614 8.988   1.00 42.16 ? 122  LYS S CE  1 
ATOM   19575 N  NZ  . LYS R  1 122 ? 58.703  111.794 7.532   1.00 44.38 ? 122  LYS S NZ  1 
ATOM   19576 N  N   . ALA R  1 123 ? 58.913  111.345 14.174  1.00 28.41 ? 123  ALA S N   1 
ATOM   19577 C  CA  . ALA R  1 123 ? 60.097  111.488 14.998  1.00 27.76 ? 123  ALA S CA  1 
ATOM   19578 C  C   . ALA R  1 123 ? 60.858  112.748 14.607  1.00 27.83 ? 123  ALA S C   1 
ATOM   19579 O  O   . ALA R  1 123 ? 60.936  113.080 13.431  1.00 27.66 ? 123  ALA S O   1 
ATOM   19580 C  CB  . ALA R  1 123 ? 60.989  110.277 14.826  1.00 27.78 ? 123  ALA S CB  1 
ATOM   19581 N  N   . ASP R  1 124 ? 61.392  113.444 15.609  1.00 27.22 ? 124  ASP S N   1 
ATOM   19582 C  CA  . ASP R  1 124 ? 62.276  114.600 15.409  1.00 26.64 ? 124  ASP S CA  1 
ATOM   19583 C  C   . ASP R  1 124 ? 63.631  113.951 15.158  1.00 26.36 ? 124  ASP S C   1 
ATOM   19584 O  O   . ASP R  1 124 ? 64.049  113.097 15.949  1.00 26.09 ? 124  ASP S O   1 
ATOM   19585 C  CB  . ASP R  1 124 ? 62.298  115.423 16.707  1.00 26.12 ? 124  ASP S CB  1 
ATOM   19586 C  CG  . ASP R  1 124 ? 63.128  116.703 16.614  1.00 27.78 ? 124  ASP S CG  1 
ATOM   19587 O  OD1 . ASP R  1 124 ? 64.121  116.752 15.841  1.00 26.26 ? 124  ASP S OD1 1 
ATOM   19588 O  OD2 . ASP R  1 124 ? 62.859  117.713 17.312  1.00 28.00 ? 124  ASP S OD2 1 
ATOM   19589 N  N   . ASP R  1 125 ? 64.312  114.317 14.064  1.00 25.82 ? 125  ASP S N   1 
ATOM   19590 C  CA  . ASP R  1 125 ? 65.601  113.690 13.753  1.00 25.64 ? 125  ASP S CA  1 
ATOM   19591 C  C   . ASP R  1 125 ? 66.762  114.377 14.481  1.00 25.58 ? 125  ASP S C   1 
ATOM   19592 O  O   . ASP R  1 125 ? 67.934  114.084 14.231  1.00 24.62 ? 125  ASP S O   1 
ATOM   19593 C  CB  . ASP R  1 125 ? 65.851  113.539 12.228  1.00 25.06 ? 125  ASP S CB  1 
ATOM   19594 C  CG  . ASP R  1 125 ? 65.967  114.870 11.499  1.00 25.10 ? 125  ASP S CG  1 
ATOM   19595 O  OD1 . ASP R  1 125 ? 66.228  115.905 12.162  1.00 22.83 ? 125  ASP S OD1 1 
ATOM   19596 O  OD2 . ASP R  1 125 ? 65.819  114.974 10.250  1.00 25.33 ? 125  ASP S OD2 1 
ATOM   19597 N  N   . LEU R  1 126 ? 66.404  115.293 15.381  1.00 25.80 ? 126  LEU S N   1 
ATOM   19598 C  CA  . LEU R  1 126 ? 67.362  116.013 16.226  1.00 26.24 ? 126  LEU S CA  1 
ATOM   19599 C  C   . LEU R  1 126 ? 68.413  116.816 15.448  1.00 26.25 ? 126  LEU S C   1 
ATOM   19600 O  O   . LEU R  1 126 ? 69.506  117.091 15.953  1.00 25.92 ? 126  LEU S O   1 
ATOM   19601 C  CB  . LEU R  1 126 ? 68.033  115.056 17.222  1.00 26.73 ? 126  LEU S CB  1 
ATOM   19602 C  CG  . LEU R  1 126 ? 67.054  114.099 17.906  1.00 27.51 ? 126  LEU S CG  1 
ATOM   19603 C  CD1 . LEU R  1 126 ? 67.774  113.057 18.794  1.00 28.54 ? 126  LEU S CD1 1 
ATOM   19604 C  CD2 . LEU R  1 126 ? 66.032  114.888 18.702  1.00 29.19 ? 126  LEU S CD2 1 
ATOM   19605 N  N   . GLY R  1 127 ? 68.075  117.200 14.222  1.00 26.00 ? 127  GLY S N   1 
ATOM   19606 C  CA  . GLY R  1 127 ? 68.960  118.058 13.450  1.00 26.61 ? 127  GLY S CA  1 
ATOM   19607 C  C   . GLY R  1 127 ? 70.038  117.339 12.659  1.00 26.84 ? 127  GLY S C   1 
ATOM   19608 O  O   . GLY R  1 127 ? 70.866  117.988 12.008  1.00 26.98 ? 127  GLY S O   1 
ATOM   19609 N  N   . LYS R  1 128 ? 70.010  116.009 12.676  1.00 27.44 ? 128  LYS S N   1 
ATOM   19610 C  CA  . LYS R  1 128 ? 71.035  115.213 12.007  1.00 28.17 ? 128  LYS S CA  1 
ATOM   19611 C  C   . LYS R  1 128 ? 70.538  114.575 10.698  1.00 27.96 ? 128  LYS S C   1 
ATOM   19612 O  O   . LYS R  1 128 ? 71.149  113.630 10.207  1.00 28.36 ? 128  LYS S O   1 
ATOM   19613 C  CB  . LYS R  1 128 ? 71.551  114.091 12.931  1.00 28.80 ? 128  LYS S CB  1 
ATOM   19614 C  CG  . LYS R  1 128 ? 71.660  114.390 14.422  1.00 30.82 ? 128  LYS S CG  1 
ATOM   19615 C  CD  . LYS R  1 128 ? 71.536  113.051 15.192  1.00 34.16 ? 128  LYS S CD  1 
ATOM   19616 C  CE  . LYS R  1 128 ? 71.271  113.203 16.677  1.00 36.53 ? 128  LYS S CE  1 
ATOM   19617 N  NZ  . LYS R  1 128 ? 70.834  111.891 17.286  1.00 38.74 ? 128  LYS S NZ  1 
ATOM   19618 N  N   . GLY R  1 129 ? 69.464  115.107 10.122  1.00 27.85 ? 129  GLY S N   1 
ATOM   19619 C  CA  . GLY R  1 129 ? 68.864  114.525 8.925   1.00 28.10 ? 129  GLY S CA  1 
ATOM   19620 C  C   . GLY R  1 129 ? 69.480  114.600 7.533   1.00 28.44 ? 129  GLY S C   1 
ATOM   19621 O  O   . GLY R  1 129 ? 68.968  113.967 6.606   1.00 29.31 ? 129  GLY S O   1 
ATOM   19622 N  N   . GLY R  1 130 ? 70.554  115.351 7.346   1.00 27.73 ? 130  GLY S N   1 
ATOM   19623 C  CA  . GLY R  1 130 ? 71.164  115.399 6.028   1.00 27.27 ? 130  GLY S CA  1 
ATOM   19624 C  C   . GLY R  1 130 ? 70.489  116.345 5.044   1.00 27.00 ? 130  GLY S C   1 
ATOM   19625 O  O   . GLY R  1 130 ? 70.963  116.522 3.923   1.00 26.51 ? 130  GLY S O   1 
ATOM   19626 N  N   . ASN R  1 131 ? 69.373  116.947 5.446   1.00 27.08 ? 131  ASN S N   1 
ATOM   19627 C  CA  . ASN R  1 131 ? 68.687  117.909 4.580   1.00 27.25 ? 131  ASN S CA  1 
ATOM   19628 C  C   . ASN R  1 131 ? 68.397  119.220 5.308   1.00 27.24 ? 131  ASN S C   1 
ATOM   19629 O  O   . ASN R  1 131 ? 68.434  119.300 6.541   1.00 25.83 ? 131  ASN S O   1 
ATOM   19630 C  CB  . ASN R  1 131 ? 67.397  117.310 3.980   1.00 27.28 ? 131  ASN S CB  1 
ATOM   19631 C  CG  . ASN R  1 131 ? 66.326  117.007 5.048   1.00 28.80 ? 131  ASN S CG  1 
ATOM   19632 O  OD1 . ASN R  1 131 ? 66.322  117.603 6.113   1.00 29.37 ? 131  ASN S OD1 1 
ATOM   19633 N  ND2 . ASN R  1 131 ? 65.405  116.096 4.740   1.00 29.51 ? 131  ASN S ND2 1 
ATOM   19634 N  N   . GLU R  1 132 ? 68.125  120.256 4.527   1.00 27.24 ? 132  GLU S N   1 
ATOM   19635 C  CA  . GLU R  1 132 ? 67.791  121.562 5.070   1.00 28.44 ? 132  GLU S CA  1 
ATOM   19636 C  C   . GLU R  1 132 ? 66.745  121.528 6.160   1.00 27.36 ? 132  GLU S C   1 
ATOM   19637 O  O   . GLU R  1 132 ? 66.938  122.056 7.251   1.00 26.83 ? 132  GLU S O   1 
ATOM   19638 C  CB  . GLU R  1 132 ? 67.264  122.435 3.948   1.00 28.69 ? 132  GLU S CB  1 
ATOM   19639 C  CG  . GLU R  1 132 ? 68.362  123.229 3.311   1.00 35.59 ? 132  GLU S CG  1 
ATOM   19640 C  CD  . GLU R  1 132 ? 68.826  124.330 4.229   1.00 42.45 ? 132  GLU S CD  1 
ATOM   19641 O  OE1 . GLU R  1 132 ? 68.033  125.284 4.445   1.00 45.82 ? 132  GLU S OE1 1 
ATOM   19642 O  OE2 . GLU R  1 132 ? 69.972  124.234 4.728   1.00 44.45 ? 132  GLU S OE2 1 
ATOM   19643 N  N   . GLU R  1 133 ? 65.625  120.899 5.846   1.00 27.15 ? 133  GLU S N   1 
ATOM   19644 C  CA  . GLU R  1 133 ? 64.522  120.827 6.774   1.00 26.31 ? 133  GLU S CA  1 
ATOM   19645 C  C   . GLU R  1 133 ? 64.962  120.335 8.154   1.00 25.98 ? 133  GLU S C   1 
ATOM   19646 O  O   . GLU R  1 133 ? 64.481  120.826 9.184   1.00 25.06 ? 133  GLU S O   1 
ATOM   19647 C  CB  . GLU R  1 133 ? 63.421  119.940 6.202   1.00 27.12 ? 133  GLU S CB  1 
ATOM   19648 C  CG  . GLU R  1 133 ? 62.128  120.010 7.002   1.00 28.96 ? 133  GLU S CG  1 
ATOM   19649 C  CD  . GLU R  1 133 ? 61.535  121.408 7.000   1.00 30.78 ? 133  GLU S CD  1 
ATOM   19650 O  OE1 . GLU R  1 133 ? 61.724  122.147 6.015   1.00 30.67 ? 133  GLU S OE1 1 
ATOM   19651 O  OE2 . GLU R  1 133 ? 60.875  121.773 7.987   1.00 32.99 ? 133  GLU S OE2 1 
ATOM   19652 N  N   . SER R  1 134 ? 65.880  119.371 8.181   1.00 25.53 ? 134  SER S N   1 
ATOM   19653 C  CA  . SER R  1 134 ? 66.376  118.861 9.461   1.00 25.18 ? 134  SER S CA  1 
ATOM   19654 C  C   . SER R  1 134 ? 66.853  119.984 10.366  1.00 25.44 ? 134  SER S C   1 
ATOM   19655 O  O   . SER R  1 134 ? 66.589  119.949 11.576  1.00 24.70 ? 134  SER S O   1 
ATOM   19656 C  CB  . SER R  1 134 ? 67.518  117.865 9.261   1.00 25.45 ? 134  SER S CB  1 
ATOM   19657 O  OG  . SER R  1 134 ? 67.907  117.292 10.507  1.00 23.23 ? 134  SER S OG  1 
ATOM   19658 N  N   . THR R  1 135 ? 67.539  120.981 9.791   1.00 25.81 ? 135  THR S N   1 
ATOM   19659 C  CA  . THR R  1 135 ? 68.064  122.112 10.584  1.00 26.39 ? 135  THR S CA  1 
ATOM   19660 C  C   . THR R  1 135 ? 67.018  123.142 11.006  1.00 27.29 ? 135  THR S C   1 
ATOM   19661 O  O   . THR R  1 135 ? 67.358  124.124 11.676  1.00 26.89 ? 135  THR S O   1 
ATOM   19662 C  CB  . THR R  1 135 ? 69.167  122.882 9.824   1.00 26.24 ? 135  THR S CB  1 
ATOM   19663 O  OG1 . THR R  1 135 ? 68.568  123.625 8.755   1.00 24.98 ? 135  THR S OG1 1 
ATOM   19664 C  CG2 . THR R  1 135 ? 70.152  121.927 9.155   1.00 25.34 ? 135  THR S CG2 1 
ATOM   19665 N  N   . LYS R  1 136 ? 65.771  122.951 10.580  1.00 28.36 ? 136  LYS S N   1 
ATOM   19666 C  CA  . LYS R  1 136 ? 64.693  123.865 10.934  1.00 29.39 ? 136  LYS S CA  1 
ATOM   19667 C  C   . LYS R  1 136 ? 63.657  123.233 11.855  1.00 29.47 ? 136  LYS S C   1 
ATOM   19668 O  O   . LYS R  1 136 ? 63.229  123.850 12.836  1.00 30.01 ? 136  LYS S O   1 
ATOM   19669 C  CB  . LYS R  1 136 ? 63.955  124.343 9.678   1.00 29.83 ? 136  LYS S CB  1 
ATOM   19670 C  CG  . LYS R  1 136 ? 64.830  124.828 8.561   1.00 32.42 ? 136  LYS S CG  1 
ATOM   19671 C  CD  . LYS R  1 136 ? 63.963  125.449 7.464   1.00 38.21 ? 136  LYS S CD  1 
ATOM   19672 C  CE  . LYS R  1 136 ? 62.504  124.947 7.506   1.00 38.98 ? 136  LYS S CE  1 
ATOM   19673 N  NZ  . LYS R  1 136 ? 61.739  125.318 6.260   1.00 40.66 ? 136  LYS S NZ  1 
ATOM   19674 N  N   . THR R  1 137 ? 63.240  122.008 11.529  1.00 29.34 ? 137  THR S N   1 
ATOM   19675 C  CA  . THR R  1 137 ? 62.174  121.333 12.273  1.00 28.94 ? 137  THR S CA  1 
ATOM   19676 C  C   . THR R  1 137 ? 62.519  119.939 12.765  1.00 28.68 ? 137  THR S C   1 
ATOM   19677 O  O   . THR R  1 137 ? 61.741  119.336 13.506  1.00 29.23 ? 137  THR S O   1 
ATOM   19678 C  CB  . THR R  1 137 ? 60.944  121.160 11.364  1.00 29.43 ? 137  THR S CB  1 
ATOM   19679 O  OG1 . THR R  1 137 ? 61.281  120.266 10.286  1.00 28.38 ? 137  THR S OG1 1 
ATOM   19680 C  CG2 . THR R  1 137 ? 60.596  122.478 10.650  1.00 29.16 ? 137  THR S CG2 1 
ATOM   19681 N  N   . GLY R  1 138 ? 63.638  119.385 12.321  1.00 27.81 ? 138  GLY S N   1 
ATOM   19682 C  CA  . GLY R  1 138 ? 63.946  118.011 12.665  1.00 26.59 ? 138  GLY S CA  1 
ATOM   19683 C  C   . GLY R  1 138 ? 63.104  117.030 11.854  1.00 26.55 ? 138  GLY S C   1 
ATOM   19684 O  O   . GLY R  1 138 ? 63.088  115.831 12.151  1.00 25.98 ? 138  GLY S O   1 
ATOM   19685 N  N   . ASN R  1 139 ? 62.391  117.535 10.846  1.00 25.99 ? 139  ASN S N   1 
ATOM   19686 C  CA  . ASN R  1 139 ? 61.564  116.689 9.975   1.00 26.13 ? 139  ASN S CA  1 
ATOM   19687 C  C   . ASN R  1 139 ? 60.481  115.907 10.724  1.00 26.08 ? 139  ASN S C   1 
ATOM   19688 O  O   . ASN R  1 139 ? 60.159  114.783 10.334  1.00 25.48 ? 139  ASN S O   1 
ATOM   19689 C  CB  . ASN R  1 139 ? 62.436  115.671 9.228   1.00 26.06 ? 139  ASN S CB  1 
ATOM   19690 C  CG  . ASN R  1 139 ? 63.256  116.303 8.095   1.00 25.93 ? 139  ASN S CG  1 
ATOM   19691 O  OD1 . ASN R  1 139 ? 62.708  116.870 7.148   1.00 25.17 ? 139  ASN S OD1 1 
ATOM   19692 N  ND2 . ASN R  1 139 ? 64.572  116.177 8.186   1.00 26.80 ? 139  ASN S ND2 1 
ATOM   19693 N  N   . ALA R  1 140 ? 59.939  116.483 11.797  1.00 26.42 ? 140  ALA S N   1 
ATOM   19694 C  CA  . ALA R  1 140 ? 58.954  115.781 12.637  1.00 26.93 ? 140  ALA S CA  1 
ATOM   19695 C  C   . ALA R  1 140 ? 57.536  115.734 12.065  1.00 27.54 ? 140  ALA S C   1 
ATOM   19696 O  O   . ALA R  1 140 ? 56.630  115.110 12.647  1.00 28.24 ? 140  ALA S O   1 
ATOM   19697 C  CB  . ALA R  1 140 ? 58.935  116.372 14.037  1.00 26.61 ? 140  ALA S CB  1 
ATOM   19698 N  N   . GLY R  1 141 ? 57.337  116.414 10.943  1.00 27.94 ? 141  GLY S N   1 
ATOM   19699 C  CA  . GLY R  1 141 ? 56.062  116.374 10.256  1.00 28.24 ? 141  GLY S CA  1 
ATOM   19700 C  C   . GLY R  1 141 ? 54.977  117.205 10.897  1.00 28.67 ? 141  GLY S C   1 
ATOM   19701 O  O   . GLY R  1 141 ? 55.243  118.159 11.630  1.00 28.34 ? 141  GLY S O   1 
ATOM   19702 N  N   . SER R  1 142 ? 53.745  116.807 10.611  1.00 29.25 ? 142  SER S N   1 
ATOM   19703 C  CA  . SER R  1 142 ? 52.530  117.452 11.106  1.00 30.65 ? 142  SER S CA  1 
ATOM   19704 C  C   . SER R  1 142 ? 52.524  117.815 12.587  1.00 30.52 ? 142  SER S C   1 
ATOM   19705 O  O   . SER R  1 142 ? 53.195  117.179 13.413  1.00 30.54 ? 142  SER S O   1 
ATOM   19706 C  CB  . SER R  1 142 ? 51.323  116.527 10.854  1.00 30.70 ? 142  SER S CB  1 
ATOM   19707 O  OG  . SER R  1 142 ? 51.530  115.702 9.718   1.00 34.22 ? 142  SER S OG  1 
ATOM   19708 N  N   . ARG R  1 143 ? 51.741  118.842 12.905  1.00 31.10 ? 143  ARG S N   1 
ATOM   19709 C  CA  . ARG R  1 143 ? 51.466  119.241 14.283  1.00 31.85 ? 143  ARG S CA  1 
ATOM   19710 C  C   . ARG R  1 143 ? 50.138  118.590 14.687  1.00 32.34 ? 143  ARG S C   1 
ATOM   19711 O  O   . ARG R  1 143 ? 49.061  119.100 14.357  1.00 32.22 ? 143  ARG S O   1 
ATOM   19712 C  CB  . ARG R  1 143 ? 51.373  120.765 14.373  1.00 31.93 ? 143  ARG S CB  1 
ATOM   19713 C  CG  . ARG R  1 143 ? 52.486  121.452 13.631  1.00 31.93 ? 143  ARG S CG  1 
ATOM   19714 C  CD  . ARG R  1 143 ? 52.508  122.959 13.791  1.00 32.74 ? 143  ARG S CD  1 
ATOM   19715 N  NE  . ARG R  1 143 ? 53.669  123.522 13.112  1.00 34.33 ? 143  ARG S NE  1 
ATOM   19716 C  CZ  . ARG R  1 143 ? 54.066  124.778 13.237  1.00 32.67 ? 143  ARG S CZ  1 
ATOM   19717 N  NH1 . ARG R  1 143 ? 53.385  125.605 14.016  1.00 33.17 ? 143  ARG S NH1 1 
ATOM   19718 N  NH2 . ARG R  1 143 ? 55.146  125.198 12.592  1.00 32.89 ? 143  ARG S NH2 1 
ATOM   19719 N  N   . LEU R  1 144 ? 50.217  117.457 15.388  1.00 32.65 ? 144  LEU S N   1 
ATOM   19720 C  CA  . LEU R  1 144 ? 49.034  116.679 15.741  1.00 32.99 ? 144  LEU S CA  1 
ATOM   19721 C  C   . LEU R  1 144 ? 48.159  117.321 16.814  1.00 33.35 ? 144  LEU S C   1 
ATOM   19722 O  O   . LEU R  1 144 ? 46.930  117.162 16.808  1.00 33.65 ? 144  LEU S O   1 
ATOM   19723 C  CB  . LEU R  1 144 ? 49.442  115.284 16.196  1.00 33.26 ? 144  LEU S CB  1 
ATOM   19724 C  CG  . LEU R  1 144 ? 50.276  114.471 15.212  1.00 33.80 ? 144  LEU S CG  1 
ATOM   19725 C  CD1 . LEU R  1 144 ? 50.484  113.077 15.785  1.00 35.19 ? 144  LEU S CD1 1 
ATOM   19726 C  CD2 . LEU R  1 144 ? 49.593  114.404 13.858  1.00 33.51 ? 144  LEU S CD2 1 
ATOM   19727 N  N   . ALA R  1 145 ? 48.788  118.021 17.749  1.00 33.10 ? 145  ALA S N   1 
ATOM   19728 C  CA  . ALA R  1 145 ? 48.039  118.713 18.781  1.00 33.51 ? 145  ALA S CA  1 
ATOM   19729 C  C   . ALA R  1 145 ? 48.926  119.767 19.410  1.00 33.87 ? 145  ALA S C   1 
ATOM   19730 O  O   . ALA R  1 145 ? 50.153  119.659 19.370  1.00 33.29 ? 145  ALA S O   1 
ATOM   19731 C  CB  . ALA R  1 145 ? 47.526  117.728 19.838  1.00 33.36 ? 145  ALA S CB  1 
ATOM   19732 N  N   . CYS R  1 146 ? 48.296  120.780 20.002  1.00 34.47 ? 146  CYS S N   1 
ATOM   19733 C  CA  . CYS R  1 146 ? 49.020  121.889 20.610  1.00 34.99 ? 146  CYS S CA  1 
ATOM   19734 C  C   . CYS R  1 146 ? 48.172  122.609 21.651  1.00 35.02 ? 146  CYS S C   1 
ATOM   19735 O  O   . CYS R  1 146 ? 46.991  122.294 21.833  1.00 34.58 ? 146  CYS S O   1 
ATOM   19736 C  CB  . CYS R  1 146 ? 49.434  122.904 19.542  1.00 35.31 ? 146  CYS S CB  1 
ATOM   19737 S  SG  . CYS R  1 146 ? 48.058  123.492 18.520  1.00 36.85 ? 146  CYS S SG  1 
ATOM   19738 N  N   . GLY R  1 147 ? 48.795  123.587 22.308  1.00 34.87 ? 147  GLY S N   1 
ATOM   19739 C  CA  . GLY R  1 147 ? 48.140  124.408 23.311  1.00 35.14 ? 147  GLY S CA  1 
ATOM   19740 C  C   . GLY R  1 147 ? 49.054  125.521 23.801  1.00 35.10 ? 147  GLY S C   1 
ATOM   19741 O  O   . GLY R  1 147 ? 50.277  125.390 23.765  1.00 34.72 ? 147  GLY S O   1 
ATOM   19742 N  N   . VAL R  1 148 ? 48.464  126.620 24.264  1.00 35.17 ? 148  VAL S N   1 
ATOM   19743 C  CA  . VAL R  1 148 ? 49.254  127.735 24.784  1.00 35.29 ? 148  VAL S CA  1 
ATOM   19744 C  C   . VAL R  1 148 ? 49.718  127.443 26.208  1.00 35.43 ? 148  VAL S C   1 
ATOM   19745 O  O   . VAL R  1 148 ? 48.964  126.915 27.024  1.00 35.04 ? 148  VAL S O   1 
ATOM   19746 C  CB  . VAL R  1 148 ? 48.480  129.069 24.756  1.00 35.11 ? 148  VAL S CB  1 
ATOM   19747 C  CG1 . VAL R  1 148 ? 49.347  130.194 25.291  1.00 35.08 ? 148  VAL S CG1 1 
ATOM   19748 C  CG2 . VAL R  1 148 ? 48.025  129.378 23.344  1.00 35.20 ? 148  VAL S CG2 1 
ATOM   19749 N  N   . ILE R  1 149 ? 50.974  127.769 26.486  1.00 35.80 ? 149  ILE S N   1 
ATOM   19750 C  CA  . ILE R  1 149 ? 51.535  127.559 27.809  1.00 36.34 ? 149  ILE S CA  1 
ATOM   19751 C  C   . ILE R  1 149 ? 51.118  128.709 28.714  1.00 36.47 ? 149  ILE S C   1 
ATOM   19752 O  O   . ILE R  1 149 ? 51.459  129.868 28.465  1.00 36.18 ? 149  ILE S O   1 
ATOM   19753 C  CB  . ILE R  1 149 ? 53.061  127.427 27.727  1.00 36.42 ? 149  ILE S CB  1 
ATOM   19754 C  CG1 . ILE R  1 149 ? 53.421  126.351 26.697  1.00 37.15 ? 149  ILE S CG1 1 
ATOM   19755 C  CG2 . ILE R  1 149 ? 53.643  127.086 29.101  1.00 36.63 ? 149  ILE S CG2 1 
ATOM   19756 C  CD1 . ILE R  1 149 ? 54.902  126.094 26.565  1.00 38.08 ? 149  ILE S CD1 1 
ATOM   19757 N  N   . GLY R  1 150 ? 50.361  128.378 29.755  1.00 36.82 ? 150  GLY S N   1 
ATOM   19758 C  CA  . GLY R  1 150 ? 49.852  129.376 30.678  1.00 37.20 ? 150  GLY S CA  1 
ATOM   19759 C  C   . GLY R  1 150 ? 50.309  129.192 32.113  1.00 37.52 ? 150  GLY S C   1 
ATOM   19760 O  O   . GLY R  1 150 ? 50.799  128.127 32.500  1.00 37.43 ? 150  GLY S O   1 
ATOM   19761 N  N   . ILE R  1 151 ? 50.139  130.246 32.904  1.00 37.85 ? 151  ILE S N   1 
ATOM   19762 C  CA  . ILE R  1 151 ? 50.534  130.234 34.309  1.00 38.23 ? 151  ILE S CA  1 
ATOM   19763 C  C   . ILE R  1 151 ? 49.670  129.258 35.104  1.00 38.41 ? 151  ILE S C   1 
ATOM   19764 O  O   . ILE R  1 151 ? 48.467  129.147 34.872  1.00 38.31 ? 151  ILE S O   1 
ATOM   19765 C  CB  . ILE R  1 151 ? 50.475  131.670 34.897  1.00 38.27 ? 151  ILE S CB  1 
ATOM   19766 C  CG1 . ILE R  1 151 ? 51.464  132.576 34.153  1.00 38.55 ? 151  ILE S CG1 1 
ATOM   19767 C  CG2 . ILE R  1 151 ? 50.773  131.667 36.396  1.00 38.00 ? 151  ILE S CG2 1 
ATOM   19768 C  CD1 . ILE R  1 151 ? 51.181  134.057 34.281  1.00 39.19 ? 151  ILE S CD1 1 
ATOM   19769 N  N   . ALA R  1 152 ? 50.302  128.535 36.025  1.00 38.95 ? 152  ALA S N   1 
ATOM   19770 C  CA  . ALA R  1 152 ? 49.608  127.565 36.866  1.00 39.30 ? 152  ALA S CA  1 
ATOM   19771 C  C   . ALA R  1 152 ? 49.702  127.941 38.339  1.00 39.55 ? 152  ALA S C   1 
ATOM   19772 O  O   . ALA R  1 152 ? 50.644  128.616 38.753  1.00 39.42 ? 152  ALA S O   1 
ATOM   19773 C  CB  . ALA R  1 152 ? 50.174  126.164 36.643  1.00 39.44 ? 152  ALA S CB  1 
ATOM   19774 N  N   . GLN R  1 153 ? 48.721  127.501 39.123  1.00 39.81 ? 153  GLN S N   1 
ATOM   19775 C  CA  . GLN R  1 153 ? 48.725  127.780 40.554  1.00 40.41 ? 153  GLN S CA  1 
ATOM   19776 C  C   . GLN R  1 153 ? 49.790  126.933 41.220  1.00 40.59 ? 153  GLN S C   1 
ATOM   19777 O  O   . GLN R  1 153 ? 49.806  125.720 41.007  1.00 40.81 ? 153  GLN S O   1 
ATOM   19778 C  CB  . GLN R  1 153 ? 47.359  127.494 41.190  1.00 40.32 ? 153  GLN S CB  1 
ATOM   19779 C  CG  . GLN R  1 153 ? 47.337  127.724 42.704  1.00 41.22 ? 153  GLN S CG  1 
ATOM   19780 C  CD  . GLN R  1 153 ? 45.933  127.737 43.302  1.00 41.79 ? 153  GLN S CD  1 
ATOM   19781 O  OE1 . GLN R  1 153 ? 45.117  126.863 43.007  1.00 42.43 ? 153  GLN S OE1 1 
ATOM   19782 N  NE2 . GLN R  1 153 ? 45.655  128.725 44.149  1.00 41.70 ? 153  GLN S NE2 1 
ATOM   19783 O  OXT . GLN R  1 153 ? 50.624  127.462 41.956  1.00 40.86 ? 153  GLN S OXT 1 
HETATM 19784 CU CU  . CU  S  2 .   ? 40.567  99.024  78.969  1.00 17.96 ? 154  CU  A CU  1 
HETATM 19785 ZN ZN  . ZN  T  3 .   ? 46.625  100.446 77.673  1.00 8.78  ? 155  ZN  A ZN  1 
HETATM 19786 CU CU  . CU  U  2 .   ? 2.709   74.480  19.983  1.00 15.11 ? 154  CU  B CU  1 
HETATM 19787 ZN ZN  . ZN  V  3 .   ? -3.232  73.464  17.676  1.00 5.72  ? 155  ZN  B ZN  1 
HETATM 19788 CU CU  . CU  W  2 .   ? 38.598  84.825  16.837  1.00 16.70 ? 154  CU  C CU  1 
HETATM 19789 ZN ZN  . ZN  X  3 .   ? 44.002  83.256  13.661  1.00 5.63  ? 155  ZN  C ZN  1 
HETATM 19790 CA CA  . CA  Y  4 .   ? 54.489  73.512  23.142  0.50 37.37 ? 156  CA  C CA  1 
HETATM 19791 CU CU  . CU  Z  2 .   ? 4.896   88.702  70.750  1.00 21.95 ? 154  CU  D CU  1 
HETATM 19792 ZN ZN  . ZN  AA 3 .   ? -0.147  90.443  67.062  1.00 10.06 ? 155  ZN  D ZN  1 
HETATM 19793 CA CA  . CA  BA 4 .   ? -11.351 100.241 75.677  1.00 47.38 ? 156  CA  D CA  1 
HETATM 19794 CU CU  . CU  CA 2 .   ? 44.876  119.578 56.237  1.00 20.96 ? 154  CU  E CU  1 
HETATM 19795 ZN ZN  . ZN  DA 3 .   ? 49.724  115.749 54.463  1.00 8.88  ? 155  ZN  E ZN  1 
HETATM 19796 CU CU  . CU  EA 2 .   ? 0.768   110.449 104.832 1.00 22.60 ? 154  CU  F CU  1 
HETATM 19797 ZN ZN  . ZN  FA 3 .   ? 6.766   108.406 105.592 1.00 12.27 ? 155  ZN  F ZN  1 
HETATM 19798 CU CU  . CU  GA 2 .   ? 16.681  149.766 55.241  1.00 27.46 ? 154  CU  G CU  1 
HETATM 19799 ZN ZN  . ZN  HA 3 .   ? 11.408  153.727 54.978  1.00 20.87 ? 155  ZN  G ZN  1 
HETATM 19800 CU CU  . CU  IA 2 .   ? 33.003  74.154  99.422  1.00 22.67 ? 154  CU  H CU  1 
HETATM 19801 ZN ZN  . ZN  JA 3 .   ? 37.619  70.645  102.158 1.00 10.25 ? 155  ZN  H ZN  1 
HETATM 19802 CU CU  . CU  KA 2 .   ? 8.106   99.173  41.251  1.00 17.68 ? 154  CU  I CU  1 
HETATM 19803 ZN ZN  . ZN  LA 3 .   ? 3.191   102.855 43.202  1.00 7.33  ? 155  ZN  I ZN  1 
HETATM 19804 CU CU  . CU  MA 2 .   ? 39.740  89.569  49.455  1.00 15.22 ? 154  CU  J CU  1 
HETATM 19805 ZN ZN  . ZN  NA 3 .   ? 45.308  88.892  52.601  1.00 6.91  ? 155  ZN  J ZN  1 
HETATM 19806 CU CU  . CU  OA 2 .   ? 0.719   83.921  103.092 1.00 13.88 ? 154  CU  K CU  1 
HETATM 19807 ZN ZN  . ZN  PA 3 .   ? -4.974  84.831  105.752 1.00 5.00  ? 155  ZN  K ZN  1 
HETATM 19808 CU CU  . CU  QA 2 .   ? 51.424  149.466 68.476  1.00 22.18 ? 154  CU  L CU  1 
HETATM 19809 ZN ZN  . ZN  RA 3 .   ? 57.646  151.525 68.853  1.00 9.48  ? 155  ZN  L ZN  1 
HETATM 19810 CU CU  . CU  SA 2 .   ? -7.780  140.450 115.547 1.00 23.23 ? 154  CU  M CU  1 
HETATM 19811 ZN ZN  . ZN  TA 3 .   ? -3.397  144.293 118.022 1.00 9.52  ? 155  ZN  M ZN  1 
HETATM 19812 CU CU  . CU  UA 2 .   ? 11.991  118.766 65.295  1.00 22.16 ? 154  CU  N CU  1 
HETATM 19813 ZN ZN  . ZN  VA 3 .   ? 6.125   116.675 66.868  1.00 11.76 ? 155  ZN  N ZN  1 
HETATM 19814 CU CU  . CU  WA 2 .   ? 41.251  110.085 111.374 1.00 29.67 ? 154  CU  O CU  1 
HETATM 19815 ZN ZN  . ZN  XA 3 .   ? 36.258  106.088 110.814 1.00 18.93 ? 155  ZN  O ZN  1 
HETATM 19816 CA CA  . CA  YA 4 .   ? 51.619  80.010  105.378 1.00 44.98 ? 156  CA  O CA  1 
HETATM 19817 CU CU  . CU  ZA 2 .   ? 35.517  136.690 35.301  1.00 69.29 ? 154  CU  P CU  1 
HETATM 19818 ZN ZN  . ZN  AB 3 .   ? 36.823  141.196 39.182  1.00 61.01 ? 155  ZN  P ZN  1 
HETATM 19819 CU CU  . CU  BB 2 .   ? 37.773  141.199 101.474 1.00 22.77 ? 154  CU  Q CU  1 
HETATM 19820 ZN ZN  . ZN  CB 3 .   ? 32.188  143.145 99.169  1.00 12.04 ? 155  ZN  Q ZN  1 
HETATM 19821 CU CU  . CU  DB 2 .   ? 57.761  121.585 16.262  1.00 46.78 ? 154  CU  S CU  1 
HETATM 19822 ZN ZN  . ZN  EB 3 .   ? 63.862  123.316 16.676  1.00 27.55 ? 155  ZN  S ZN  1 
HETATM 19823 O  O   . HOH FB 5 .   ? 22.156  91.598  73.054  1.00 55.91 ? 2001 HOH A O   1 
HETATM 19824 O  O   . HOH FB 5 .   ? 35.516  85.085  85.392  1.00 34.06 ? 2002 HOH A O   1 
HETATM 19825 O  O   . HOH FB 5 .   ? 33.361  77.312  77.666  1.00 52.03 ? 2003 HOH A O   1 
HETATM 19826 O  O   . HOH FB 5 .   ? 28.329  97.296  82.092  1.00 58.94 ? 2004 HOH A O   1 
HETATM 19827 O  O   . HOH FB 5 .   ? 25.929  91.656  80.571  1.00 53.18 ? 2005 HOH A O   1 
HETATM 19828 O  O   . HOH FB 5 .   ? 26.736  95.072  78.921  1.00 41.57 ? 2006 HOH A O   1 
HETATM 19829 O  O   . HOH FB 5 .   ? 22.928  89.832  74.796  1.00 53.65 ? 2007 HOH A O   1 
HETATM 19830 O  O   . HOH FB 5 .   ? 22.211  85.886  81.385  1.00 59.98 ? 2008 HOH A O   1 
HETATM 19831 O  O   . HOH FB 5 .   ? 23.737  98.031  71.987  1.00 61.27 ? 2009 HOH A O   1 
HETATM 19832 O  O   . HOH FB 5 .   ? 25.385  98.163  75.325  1.00 57.87 ? 2010 HOH A O   1 
HETATM 19833 O  O   . HOH FB 5 .   ? 33.515  81.077  74.477  1.00 50.21 ? 2011 HOH A O   1 
HETATM 19834 O  O   . HOH FB 5 .   ? 39.703  77.878  79.559  1.00 43.84 ? 2012 HOH A O   1 
HETATM 19835 O  O   . HOH FB 5 .   ? 35.537  77.976  78.882  1.00 46.64 ? 2013 HOH A O   1 
HETATM 19836 O  O   . HOH FB 5 .   ? 38.844  105.270 63.354  1.00 59.16 ? 2014 HOH A O   1 
HETATM 19837 O  O   . HOH FB 5 .   ? 49.579  78.074  73.920  1.00 57.93 ? 2015 HOH A O   1 
HETATM 19838 O  O   . HOH FB 5 .   ? 36.457  104.157 84.998  1.00 54.40 ? 2016 HOH A O   1 
HETATM 19839 O  O   . HOH FB 5 .   ? 44.977  95.796  67.552  1.00 46.29 ? 2017 HOH A O   1 
HETATM 19840 O  O   . HOH FB 5 .   ? 49.074  100.853 65.086  1.00 47.15 ? 2018 HOH A O   1 
HETATM 19841 O  O   . HOH FB 5 .   ? 54.836  103.856 69.388  1.00 55.53 ? 2019 HOH A O   1 
HETATM 19842 O  O   . HOH FB 5 .   ? 56.510  99.885  67.383  1.00 60.79 ? 2020 HOH A O   1 
HETATM 19843 O  O   . HOH FB 5 .   ? 26.329  96.498  73.466  1.00 52.91 ? 2021 HOH A O   1 
HETATM 19844 O  O   . HOH FB 5 .   ? 23.417  94.219  72.814  1.00 59.25 ? 2022 HOH A O   1 
HETATM 19845 O  O   . HOH FB 5 .   ? 24.288  93.693  69.739  1.00 52.17 ? 2023 HOH A O   1 
HETATM 19846 O  O   . HOH FB 5 .   ? 28.595  97.328  72.187  1.00 45.21 ? 2024 HOH A O   1 
HETATM 19847 O  O   . HOH FB 5 .   ? 25.282  95.759  65.857  1.00 52.05 ? 2025 HOH A O   1 
HETATM 19848 O  O   . HOH FB 5 .   ? 34.590  99.595  64.183  1.00 44.96 ? 2026 HOH A O   1 
HETATM 19849 O  O   . HOH FB 5 .   ? 33.169  100.237 67.374  1.00 50.22 ? 2027 HOH A O   1 
HETATM 19850 O  O   . HOH FB 5 .   ? 50.572  88.145  90.150  1.00 53.12 ? 2028 HOH A O   1 
HETATM 19851 O  O   . HOH FB 5 .   ? 38.843  106.596 67.861  1.00 49.61 ? 2029 HOH A O   1 
HETATM 19852 O  O   . HOH FB 5 .   ? 43.055  99.172  64.351  1.00 46.08 ? 2030 HOH A O   1 
HETATM 19853 O  O   . HOH FB 5 .   ? 42.483  105.462 64.791  1.00 46.40 ? 2031 HOH A O   1 
HETATM 19854 O  O   . HOH FB 5 .   ? 50.470  108.657 66.464  1.00 46.00 ? 2032 HOH A O   1 
HETATM 19855 O  O   . HOH FB 5 .   ? 49.368  111.026 67.236  1.00 40.13 ? 2033 HOH A O   1 
HETATM 19856 O  O   . HOH FB 5 .   ? 49.255  108.370 64.345  1.00 47.02 ? 2034 HOH A O   1 
HETATM 19857 O  O   . HOH FB 5 .   ? 42.305  102.464 61.539  1.00 53.53 ? 2035 HOH A O   1 
HETATM 19858 O  O   . HOH FB 5 .   ? 49.068  95.507  90.626  1.00 46.25 ? 2036 HOH A O   1 
HETATM 19859 O  O   . HOH FB 5 .   ? 47.266  101.685 89.952  1.00 49.96 ? 2037 HOH A O   1 
HETATM 19860 O  O   . HOH FB 5 .   ? 36.454  91.063  92.640  1.00 34.88 ? 2038 HOH A O   1 
HETATM 19861 O  O   . HOH FB 5 .   ? 36.020  94.439  87.860  1.00 42.86 ? 2039 HOH A O   1 
HETATM 19862 O  O   . HOH FB 5 .   ? 39.312  96.054  97.122  1.00 52.60 ? 2040 HOH A O   1 
HETATM 19863 O  O   . HOH FB 5 .   ? 29.640  93.668  91.681  1.00 60.39 ? 2041 HOH A O   1 
HETATM 19864 O  O   . HOH FB 5 .   ? 34.149  90.343  87.913  1.00 51.05 ? 2042 HOH A O   1 
HETATM 19865 O  O   . HOH FB 5 .   ? 43.759  105.892 82.943  1.00 57.43 ? 2043 HOH A O   1 
HETATM 19866 O  O   . HOH FB 5 .   ? 30.085  96.844  85.703  1.00 51.33 ? 2044 HOH A O   1 
HETATM 19867 O  O   . HOH FB 5 .   ? 38.598  102.932 87.067  1.00 46.85 ? 2045 HOH A O   1 
HETATM 19868 O  O   . HOH FB 5 .   ? 40.561  99.486  92.374  1.00 45.66 ? 2046 HOH A O   1 
HETATM 19869 O  O   . HOH FB 5 .   ? 40.300  101.563 79.691  1.00 38.54 ? 2047 HOH A O   1 
HETATM 19870 O  O   . HOH FB 5 .   ? 53.579  97.606  81.261  1.00 36.82 ? 2048 HOH A O   1 
HETATM 19871 O  O   . HOH FB 5 .   ? 49.781  98.019  86.623  1.00 44.62 ? 2049 HOH A O   1 
HETATM 19872 O  O   . HOH FB 5 .   ? 57.110  100.328 86.685  1.00 56.49 ? 2050 HOH A O   1 
HETATM 19873 O  O   . HOH FB 5 .   ? 61.585  97.537  80.627  1.00 51.40 ? 2051 HOH A O   1 
HETATM 19874 O  O   . HOH FB 5 .   ? 55.952  95.714  77.027  1.00 53.99 ? 2052 HOH A O   1 
HETATM 19875 O  O   . HOH FB 5 .   ? 53.837  113.831 75.463  1.00 59.37 ? 2053 HOH A O   1 
HETATM 19876 O  O   . HOH FB 5 .   ? 52.075  104.012 72.353  1.00 47.17 ? 2054 HOH A O   1 
HETATM 19877 O  O   . HOH FB 5 .   ? 54.757  94.244  71.276  1.00 55.00 ? 2055 HOH A O   1 
HETATM 19878 O  O   . HOH FB 5 .   ? 45.255  92.119  67.114  1.00 55.56 ? 2056 HOH A O   1 
HETATM 19879 O  O   . HOH FB 5 .   ? 49.040  96.887  67.320  1.00 35.22 ? 2057 HOH A O   1 
HETATM 19880 O  O   . HOH FB 5 .   ? 47.235  90.344  68.653  1.00 47.13 ? 2058 HOH A O   1 
HETATM 19881 O  O   . HOH FB 5 .   ? 47.219  95.693  66.350  1.00 51.35 ? 2059 HOH A O   1 
HETATM 19882 O  O   . HOH FB 5 .   ? 56.150  95.394  73.987  1.00 52.98 ? 2060 HOH A O   1 
HETATM 19883 O  O   . HOH FB 5 .   ? 49.772  102.096 67.568  1.00 38.35 ? 2061 HOH A O   1 
HETATM 19884 O  O   . HOH FB 5 .   ? 51.224  98.750  65.922  1.00 58.63 ? 2062 HOH A O   1 
HETATM 19885 O  O   . HOH FB 5 .   ? 64.564  99.762  73.497  1.00 52.37 ? 2063 HOH A O   1 
HETATM 19886 O  O   . HOH FB 5 .   ? 56.287  101.744 70.150  1.00 46.88 ? 2064 HOH A O   1 
HETATM 19887 O  O   . HOH FB 5 .   ? 55.831  107.034 75.524  1.00 63.58 ? 2065 HOH A O   1 
HETATM 19888 O  O   . HOH FB 5 .   ? 54.689  97.291  78.989  1.00 42.12 ? 2066 HOH A O   1 
HETATM 19889 O  O   . HOH FB 5 .   ? 49.526  105.200 80.467  1.00 41.44 ? 2067 HOH A O   1 
HETATM 19890 O  O   . HOH FB 5 .   ? 43.506  92.477  68.950  1.00 44.22 ? 2068 HOH A O   1 
HETATM 19891 O  O   . HOH FB 5 .   ? 37.410  89.616  67.544  1.00 39.07 ? 2069 HOH A O   1 
HETATM 19892 O  O   . HOH FB 5 .   ? 29.175  90.309  60.030  1.00 50.33 ? 2070 HOH A O   1 
HETATM 19893 O  O   . HOH FB 5 .   ? 24.905  89.094  69.994  1.00 46.33 ? 2071 HOH A O   1 
HETATM 19894 O  O   . HOH FB 5 .   ? 36.407  83.199  66.867  1.00 59.24 ? 2072 HOH A O   1 
HETATM 19895 O  O   . HOH FB 5 .   ? 44.480  88.076  65.978  1.00 54.49 ? 2073 HOH A O   1 
HETATM 19896 O  O   . HOH FB 5 .   ? 44.298  83.840  65.147  1.00 61.70 ? 2074 HOH A O   1 
HETATM 19897 O  O   . HOH FB 5 .   ? 46.967  87.909  67.669  1.00 49.25 ? 2075 HOH A O   1 
HETATM 19898 O  O   . HOH FB 5 .   ? 45.903  81.126  68.081  1.00 53.79 ? 2076 HOH A O   1 
HETATM 19899 O  O   . HOH FB 5 .   ? 49.105  90.399  70.449  1.00 42.09 ? 2077 HOH A O   1 
HETATM 19900 O  O   . HOH FB 5 .   ? 52.360  86.244  70.537  1.00 47.22 ? 2078 HOH A O   1 
HETATM 19901 O  O   . HOH FB 5 .   ? 52.948  89.563  71.293  1.00 47.17 ? 2079 HOH A O   1 
HETATM 19902 O  O   . HOH FB 5 .   ? 57.598  88.061  76.169  1.00 40.15 ? 2080 HOH A O   1 
HETATM 19903 O  O   . HOH FB 5 .   ? 56.604  86.819  77.568  1.00 42.67 ? 2081 HOH A O   1 
HETATM 19904 O  O   . HOH FB 5 .   ? 55.981  87.239  82.822  1.00 53.49 ? 2082 HOH A O   1 
HETATM 19905 O  O   . HOH FB 5 .   ? 50.244  92.715  91.859  1.00 48.82 ? 2083 HOH A O   1 
HETATM 19906 O  O   . HOH FB 5 .   ? 51.361  90.025  87.909  1.00 41.30 ? 2084 HOH A O   1 
HETATM 19907 O  O   . HOH FB 5 .   ? 29.341  100.144 71.909  1.00 46.67 ? 2085 HOH A O   1 
HETATM 19908 O  O   . HOH FB 5 .   ? 37.498  105.218 69.878  1.00 40.59 ? 2086 HOH A O   1 
HETATM 19909 O  O   . HOH FB 5 .   ? 41.969  101.512 66.016  1.00 46.02 ? 2087 HOH A O   1 
HETATM 19910 O  O   . HOH FB 5 .   ? 45.696  98.043  72.940  1.00 31.21 ? 2088 HOH A O   1 
HETATM 19911 O  O   . HOH FB 5 .   ? 40.671  108.273 68.863  1.00 37.20 ? 2089 HOH A O   1 
HETATM 19912 O  O   . HOH FB 5 .   ? 44.014  103.832 65.519  1.00 41.15 ? 2090 HOH A O   1 
HETATM 19913 O  O   . HOH FB 5 .   ? 50.902  107.430 71.035  1.00 56.75 ? 2091 HOH A O   1 
HETATM 19914 O  O   . HOH FB 5 .   ? 51.255  106.698 67.924  1.00 51.36 ? 2092 HOH A O   1 
HETATM 19915 O  O   . HOH FB 5 .   ? 48.204  110.149 69.719  1.00 32.54 ? 2093 HOH A O   1 
HETATM 19916 O  O   . HOH FB 5 .   ? 47.040  110.160 64.290  1.00 55.14 ? 2094 HOH A O   1 
HETATM 19917 O  O   . HOH FB 5 .   ? 49.608  104.887 60.365  1.00 59.41 ? 2095 HOH A O   1 
HETATM 19918 O  O   . HOH FB 5 .   ? 45.654  103.803 60.356  1.00 59.82 ? 2096 HOH A O   1 
HETATM 19919 O  O   . HOH FB 5 .   ? 44.646  108.384 64.042  1.00 44.72 ? 2097 HOH A O   1 
HETATM 19920 O  O   . HOH FB 5 .   ? 39.557  113.121 76.375  1.00 52.57 ? 2098 HOH A O   1 
HETATM 19921 O  O   . HOH FB 5 .   ? 48.855  118.423 77.544  1.00 57.18 ? 2099 HOH A O   1 
HETATM 19922 O  O   . HOH FB 5 .   ? 42.303  113.580 76.435  1.00 41.94 ? 2100 HOH A O   1 
HETATM 19923 O  O   . HOH FB 5 .   ? 43.072  112.105 79.974  1.00 61.59 ? 2101 HOH A O   1 
HETATM 19924 O  O   . HOH FB 5 .   ? 44.839  102.703 81.402  1.00 37.87 ? 2102 HOH A O   1 
HETATM 19925 O  O   . HOH FB 5 .   ? 38.563  103.448 78.725  1.00 40.85 ? 2103 HOH A O   1 
HETATM 19926 O  O   . HOH FB 5 .   ? 37.965  106.435 76.635  1.00 52.49 ? 2104 HOH A O   1 
HETATM 19927 O  O   . HOH FB 5 .   ? 42.022  102.412 81.932  1.00 38.66 ? 2105 HOH A O   1 
HETATM 19928 O  O   . HOH FB 5 .   ? 40.792  103.309 86.127  1.00 41.37 ? 2106 HOH A O   1 
HETATM 19929 O  O   . HOH FB 5 .   ? 32.769  102.408 82.368  1.00 43.00 ? 2107 HOH A O   1 
HETATM 19930 O  O   . HOH FB 5 .   ? 37.870  103.113 81.393  1.00 47.57 ? 2108 HOH A O   1 
HETATM 19931 O  O   . HOH FB 5 .   ? 41.341  104.195 83.511  1.00 48.94 ? 2109 HOH A O   1 
HETATM 19932 O  O   . HOH FB 5 .   ? 31.968  90.900  86.318  1.00 45.55 ? 2110 HOH A O   1 
HETATM 19933 O  O   . HOH FB 5 .   ? 34.761  87.297  87.501  1.00 37.88 ? 2111 HOH A O   1 
HETATM 19934 O  O   . HOH FB 5 .   ? 37.358  68.717  88.776  1.00 57.93 ? 2112 HOH A O   1 
HETATM 19935 O  O   . HOH FB 5 .   ? 35.729  70.757  87.620  1.00 61.00 ? 2113 HOH A O   1 
HETATM 19936 O  O   . HOH GB 5 .   ? -2.213  97.967  24.619  1.00 49.91 ? 2001 HOH B O   1 
HETATM 19937 O  O   . HOH GB 5 .   ? 9.383   87.754  29.127  1.00 46.65 ? 2002 HOH B O   1 
HETATM 19938 O  O   . HOH GB 5 .   ? 13.717  83.105  30.685  1.00 62.28 ? 2003 HOH B O   1 
HETATM 19939 O  O   . HOH GB 5 .   ? 13.797  95.578  20.845  1.00 56.59 ? 2004 HOH B O   1 
HETATM 19940 O  O   . HOH GB 5 .   ? 16.981  75.240  21.170  1.00 48.59 ? 2005 HOH B O   1 
HETATM 19941 O  O   . HOH GB 5 .   ? 21.843  83.048  15.860  1.00 40.68 ? 2006 HOH B O   1 
HETATM 19942 O  O   . HOH GB 5 .   ? 10.538  85.687  27.905  1.00 43.67 ? 2007 HOH B O   1 
HETATM 19943 O  O   . HOH GB 5 .   ? 15.166  90.371  23.955  1.00 55.58 ? 2008 HOH B O   1 
HETATM 19944 O  O   . HOH GB 5 .   ? 5.455   97.579  21.583  1.00 48.75 ? 2009 HOH B O   1 
HETATM 19945 O  O   . HOH GB 5 .   ? 7.436   98.154  18.797  1.00 62.69 ? 2010 HOH B O   1 
HETATM 19946 O  O   . HOH GB 5 .   ? 11.244  95.540  19.906  1.00 57.17 ? 2011 HOH B O   1 
HETATM 19947 O  O   . HOH GB 5 .   ? 16.046  81.267  28.732  1.00 60.04 ? 2012 HOH B O   1 
HETATM 19948 O  O   . HOH GB 5 .   ? 19.494  79.852  25.978  1.00 47.17 ? 2013 HOH B O   1 
HETATM 19949 O  O   . HOH GB 5 .   ? 13.148  72.937  28.496  1.00 56.82 ? 2014 HOH B O   1 
HETATM 19950 O  O   . HOH GB 5 .   ? 17.607  77.011  31.626  1.00 61.45 ? 2015 HOH B O   1 
HETATM 19951 O  O   . HOH GB 5 .   ? 16.471  77.726  22.041  1.00 36.39 ? 2016 HOH B O   1 
HETATM 19952 O  O   . HOH GB 5 .   ? -8.945  96.272  11.956  1.00 47.70 ? 2017 HOH B O   1 
HETATM 19953 O  O   . HOH GB 5 .   ? 21.128  82.878  18.845  1.00 35.11 ? 2018 HOH B O   1 
HETATM 19954 O  O   . HOH GB 5 .   ? 17.167  81.275  23.781  1.00 36.62 ? 2019 HOH B O   1 
HETATM 19955 O  O   . HOH GB 5 .   ? 17.923  83.416  25.381  1.00 43.01 ? 2020 HOH B O   1 
HETATM 19956 O  O   . HOH GB 5 .   ? 17.601  74.914  18.708  1.00 51.19 ? 2021 HOH B O   1 
HETATM 19957 O  O   . HOH GB 5 .   ? 14.696  88.582  22.542  1.00 46.53 ? 2022 HOH B O   1 
HETATM 19958 O  O   . HOH GB 5 .   ? 11.212  92.124  16.499  1.00 45.42 ? 2023 HOH B O   1 
HETATM 19959 O  O   . HOH GB 5 .   ? 4.533   95.450  20.720  1.00 38.63 ? 2024 HOH B O   1 
HETATM 19960 O  O   . HOH GB 5 .   ? 8.531   95.404  20.640  1.00 41.48 ? 2025 HOH B O   1 
HETATM 19961 O  O   . HOH GB 5 .   ? 10.141  94.482  17.399  1.00 42.28 ? 2026 HOH B O   1 
HETATM 19962 O  O   . HOH GB 5 .   ? 3.272   71.020  2.405   1.00 46.10 ? 2027 HOH B O   1 
HETATM 19963 O  O   . HOH GB 5 .   ? 2.654   96.134  19.271  1.00 46.22 ? 2028 HOH B O   1 
HETATM 19964 O  O   . HOH GB 5 .   ? 0.175   77.324  39.266  1.00 53.53 ? 2029 HOH B O   1 
HETATM 19965 O  O   . HOH GB 5 .   ? 8.425   84.271  32.240  1.00 41.96 ? 2030 HOH B O   1 
HETATM 19966 O  O   . HOH GB 5 .   ? -4.438  68.107  24.536  1.00 60.81 ? 2031 HOH B O   1 
HETATM 19967 O  O   . HOH GB 5 .   ? -8.731  94.699  21.327  1.00 59.92 ? 2032 HOH B O   1 
HETATM 19968 O  O   . HOH GB 5 .   ? -9.654  77.008  27.190  1.00 56.75 ? 2033 HOH B O   1 
HETATM 19969 O  O   . HOH GB 5 .   ? -10.261 70.726  8.384   1.00 56.03 ? 2034 HOH B O   1 
HETATM 19970 O  O   . HOH GB 5 .   ? -9.752  88.919  16.260  1.00 48.34 ? 2035 HOH B O   1 
HETATM 19971 O  O   . HOH GB 5 .   ? -4.854  95.325  13.619  1.00 46.48 ? 2036 HOH B O   1 
HETATM 19972 O  O   . HOH GB 5 .   ? -8.394  94.985  14.327  1.00 42.66 ? 2037 HOH B O   1 
HETATM 19973 O  O   . HOH GB 5 .   ? -6.536  80.751  1.757   1.00 51.91 ? 2038 HOH B O   1 
HETATM 19974 O  O   . HOH GB 5 .   ? -3.511  72.970  4.979   1.00 37.72 ? 2039 HOH B O   1 
HETATM 19975 O  O   . HOH GB 5 .   ? -5.737  76.689  3.305   1.00 44.44 ? 2040 HOH B O   1 
HETATM 19976 O  O   . HOH GB 5 .   ? -12.371 78.923  15.791  1.00 55.55 ? 2041 HOH B O   1 
HETATM 19977 O  O   . HOH GB 5 .   ? 0.015   81.661  7.709   1.00 41.52 ? 2042 HOH B O   1 
HETATM 19978 O  O   . HOH GB 5 .   ? 2.808   74.280  5.325   1.00 57.17 ? 2043 HOH B O   1 
HETATM 19979 O  O   . HOH GB 5 .   ? 14.497  89.751  17.701  1.00 53.44 ? 2044 HOH B O   1 
HETATM 19980 O  O   . HOH GB 5 .   ? 20.966  86.420  13.545  1.00 54.02 ? 2045 HOH B O   1 
HETATM 19981 O  O   . HOH GB 5 .   ? 17.861  76.216  16.433  1.00 35.88 ? 2046 HOH B O   1 
HETATM 19982 O  O   . HOH GB 5 .   ? 20.566  78.601  12.936  1.00 53.19 ? 2047 HOH B O   1 
HETATM 19983 O  O   . HOH GB 5 .   ? -0.117  89.863  6.618   1.00 53.23 ? 2048 HOH B O   1 
HETATM 19984 O  O   . HOH GB 5 .   ? 14.135  73.400  9.933   1.00 52.16 ? 2049 HOH B O   1 
HETATM 19985 O  O   . HOH GB 5 .   ? 15.652  75.617  15.083  1.00 31.08 ? 2050 HOH B O   1 
HETATM 19986 O  O   . HOH GB 5 .   ? -2.252  83.130  8.225   1.00 46.92 ? 2051 HOH B O   1 
HETATM 19987 O  O   . HOH GB 5 .   ? 19.854  76.283  9.191   1.00 48.45 ? 2052 HOH B O   1 
HETATM 19988 O  O   . HOH GB 5 .   ? 11.620  72.558  9.562   1.00 43.26 ? 2053 HOH B O   1 
HETATM 19989 O  O   . HOH GB 5 .   ? 10.871  73.343  6.464   1.00 46.39 ? 2054 HOH B O   1 
HETATM 19990 O  O   . HOH GB 5 .   ? 5.602   66.909  8.997   1.00 45.54 ? 2055 HOH B O   1 
HETATM 19991 O  O   . HOH GB 5 .   ? 4.251   68.728  6.948   1.00 42.44 ? 2056 HOH B O   1 
HETATM 19992 O  O   . HOH GB 5 .   ? 1.799   71.830  4.997   1.00 54.39 ? 2057 HOH B O   1 
HETATM 19993 O  O   . HOH GB 5 .   ? 0.970   67.510  3.552   1.00 38.29 ? 2058 HOH B O   1 
HETATM 19994 O  O   . HOH GB 5 .   ? -4.562  65.486  4.039   1.00 45.52 ? 2059 HOH B O   1 
HETATM 19995 O  O   . HOH GB 5 .   ? -1.152  72.104  3.536   1.00 51.47 ? 2060 HOH B O   1 
HETATM 19996 O  O   . HOH GB 5 .   ? -7.260  78.761  30.314  1.00 42.55 ? 2061 HOH B O   1 
HETATM 19997 O  O   . HOH GB 5 .   ? -5.612  72.284  29.645  1.00 46.40 ? 2062 HOH B O   1 
HETATM 19998 O  O   . HOH GB 5 .   ? -4.860  62.810  7.200   1.00 43.35 ? 2063 HOH B O   1 
HETATM 19999 O  O   . HOH GB 5 .   ? 2.649   60.065  18.093  1.00 53.55 ? 2064 HOH B O   1 
HETATM 20000 O  O   . HOH GB 5 .   ? 5.104   82.214  33.993  1.00 27.23 ? 2065 HOH B O   1 
HETATM 20001 O  O   . HOH GB 5 .   ? -2.430  68.772  23.153  1.00 57.77 ? 2066 HOH B O   1 
HETATM 20002 O  O   . HOH GB 5 .   ? 2.283   76.757  38.327  1.00 49.85 ? 2067 HOH B O   1 
HETATM 20003 O  O   . HOH GB 5 .   ? 2.696   74.460  36.368  1.00 57.76 ? 2068 HOH B O   1 
HETATM 20004 O  O   . HOH GB 5 .   ? -0.106  76.340  35.004  1.00 34.46 ? 2069 HOH B O   1 
HETATM 20005 O  O   . HOH GB 5 .   ? 5.964   78.989  29.362  1.00 42.88 ? 2070 HOH B O   1 
HETATM 20006 O  O   . HOH GB 5 .   ? 11.280  80.465  33.025  1.00 46.04 ? 2071 HOH B O   1 
HETATM 20007 O  O   . HOH GB 5 .   ? 8.731   83.095  29.917  1.00 45.66 ? 2072 HOH B O   1 
HETATM 20008 O  O   . HOH GB 5 .   ? 11.555  79.563  28.575  1.00 52.89 ? 2073 HOH B O   1 
HETATM 20009 O  O   . HOH GB 5 .   ? 10.715  83.219  32.436  1.00 44.19 ? 2074 HOH B O   1 
HETATM 20010 O  O   . HOH GB 5 .   ? 7.066   81.630  29.421  1.00 61.07 ? 2075 HOH B O   1 
HETATM 20011 O  O   . HOH GB 5 .   ? 8.210   68.015  27.793  1.00 55.59 ? 2076 HOH B O   1 
HETATM 20012 O  O   . HOH GB 5 .   ? 6.084   73.664  36.948  1.00 33.35 ? 2077 HOH B O   1 
HETATM 20013 O  O   . HOH GB 5 .   ? 12.089  75.823  28.141  1.00 51.34 ? 2078 HOH B O   1 
HETATM 20014 O  O   . HOH GB 5 .   ? 6.648   70.252  32.761  1.00 40.12 ? 2079 HOH B O   1 
HETATM 20015 O  O   . HOH GB 5 .   ? 4.326   71.250  33.466  1.00 46.66 ? 2080 HOH B O   1 
HETATM 20016 O  O   . HOH GB 5 .   ? 2.657   71.937  29.334  1.00 53.73 ? 2081 HOH B O   1 
HETATM 20017 O  O   . HOH GB 5 .   ? 0.811   74.246  33.353  1.00 36.05 ? 2082 HOH B O   1 
HETATM 20018 O  O   . HOH GB 5 .   ? 2.565   72.063  20.470  1.00 33.77 ? 2083 HOH B O   1 
HETATM 20019 O  O   . HOH GB 5 .   ? -5.393  72.208  22.663  1.00 50.59 ? 2084 HOH B O   1 
HETATM 20020 O  O   . HOH GB 5 .   ? -7.515  75.857  25.769  1.00 43.23 ? 2085 HOH B O   1 
HETATM 20021 O  O   . HOH GB 5 .   ? -7.374  70.775  23.315  1.00 55.77 ? 2086 HOH B O   1 
HETATM 20022 O  O   . HOH GB 5 .   ? -10.409 76.708  20.165  1.00 36.88 ? 2087 HOH B O   1 
HETATM 20023 O  O   . HOH GB 5 .   ? -8.182  70.467  11.318  1.00 50.58 ? 2088 HOH B O   1 
HETATM 20024 O  O   . HOH GB 5 .   ? -6.960  83.245  9.168   1.00 55.87 ? 2089 HOH B O   1 
HETATM 20025 O  O   . HOH GB 5 .   ? -4.855  83.579  1.794   1.00 53.78 ? 2090 HOH B O   1 
HETATM 20026 O  O   . HOH GB 5 .   ? -3.522  77.251  7.245   1.00 33.09 ? 2091 HOH B O   1 
HETATM 20027 O  O   . HOH GB 5 .   ? -4.674  71.863  7.241   1.00 36.40 ? 2092 HOH B O   1 
HETATM 20028 O  O   . HOH GB 5 .   ? -4.770  75.464  5.537   1.00 43.60 ? 2093 HOH B O   1 
HETATM 20029 O  O   . HOH GB 5 .   ? -9.978  80.065  10.446  1.00 51.23 ? 2094 HOH B O   1 
HETATM 20030 O  O   . HOH GB 5 .   ? -11.570 75.177  6.263   1.00 52.55 ? 2095 HOH B O   1 
HETATM 20031 O  O   . HOH GB 5 .   ? -11.564 73.020  8.548   1.00 40.79 ? 2096 HOH B O   1 
HETATM 20032 O  O   . HOH GB 5 .   ? -11.146 77.408  17.531  1.00 36.32 ? 2097 HOH B O   1 
HETATM 20033 O  O   . HOH GB 5 .   ? -6.938  68.978  19.940  1.00 45.26 ? 2098 HOH B O   1 
HETATM 20034 O  O   . HOH GB 5 .   ? 1.591   80.908  9.628   1.00 32.94 ? 2099 HOH B O   1 
HETATM 20035 O  O   . HOH GB 5 .   ? 2.920   76.166  6.580   1.00 42.16 ? 2100 HOH B O   1 
HETATM 20036 O  O   . HOH GB 5 .   ? 11.381  84.893  7.340   1.00 37.92 ? 2101 HOH B O   1 
HETATM 20037 O  O   . HOH GB 5 .   ? 7.936   83.667  9.209   1.00 34.12 ? 2102 HOH B O   1 
HETATM 20038 O  O   . HOH GB 5 .   ? 13.520  79.081  4.339   1.00 52.02 ? 2103 HOH B O   1 
HETATM 20039 O  O   . HOH GB 5 .   ? 19.347  86.696  7.347   1.00 51.05 ? 2104 HOH B O   1 
HETATM 20040 O  O   . HOH GB 5 .   ? 17.366  81.749  2.866   1.00 49.91 ? 2105 HOH B O   1 
HETATM 20041 O  O   . HOH GB 5 .   ? 20.132  83.518  13.526  1.00 40.05 ? 2106 HOH B O   1 
HETATM 20042 O  O   . HOH GB 5 .   ? 8.347   91.160  10.287  1.00 42.46 ? 2107 HOH B O   1 
HETATM 20043 O  O   . HOH GB 5 .   ? 2.092   90.151  6.016   1.00 44.04 ? 2108 HOH B O   1 
HETATM 20044 O  O   . HOH GB 5 .   ? 1.397   91.369  10.194  1.00 45.09 ? 2109 HOH B O   1 
HETATM 20045 O  O   . HOH GB 5 .   ? 1.540   85.683  6.703   1.00 36.57 ? 2110 HOH B O   1 
HETATM 20046 O  O   . HOH GB 5 .   ? 5.222   93.354  9.130   1.00 53.50 ? 2111 HOH B O   1 
HETATM 20047 O  O   . HOH GB 5 .   ? -1.208  85.965  7.742   1.00 35.65 ? 2112 HOH B O   1 
HETATM 20048 O  O   . HOH GB 5 .   ? -4.046  83.763  10.147  1.00 41.72 ? 2113 HOH B O   1 
HETATM 20049 O  O   . HOH GB 5 .   ? -8.113  84.601  10.648  1.00 45.16 ? 2114 HOH B O   1 
HETATM 20050 O  O   . HOH GB 5 .   ? -12.065 88.044  15.818  1.00 38.61 ? 2115 HOH B O   1 
HETATM 20051 O  O   . HOH GB 5 .   ? -13.121 86.434  14.669  1.00 54.99 ? 2116 HOH B O   1 
HETATM 20052 O  O   . HOH GB 5 .   ? -12.485 89.787  20.509  1.00 57.10 ? 2117 HOH B O   1 
HETATM 20053 O  O   . HOH GB 5 .   ? -7.355  93.412  26.710  1.00 51.55 ? 2118 HOH B O   1 
HETATM 20054 O  O   . HOH GB 5 .   ? -11.999 87.181  21.855  1.00 58.71 ? 2119 HOH B O   1 
HETATM 20055 O  O   . HOH GB 5 .   ? -8.909  84.269  27.189  1.00 41.66 ? 2120 HOH B O   1 
HETATM 20056 O  O   . HOH GB 5 .   ? -8.713  81.243  31.104  1.00 52.73 ? 2121 HOH B O   1 
HETATM 20057 O  O   . HOH GB 5 .   ? 14.899  72.876  14.805  1.00 34.18 ? 2122 HOH B O   1 
HETATM 20058 O  O   . HOH GB 5 .   ? 6.683   68.121  11.321  1.00 37.80 ? 2123 HOH B O   1 
HETATM 20059 O  O   . HOH GB 5 .   ? 10.173  70.049  9.999   1.00 47.31 ? 2124 HOH B O   1 
HETATM 20060 O  O   . HOH GB 5 .   ? -1.213  75.812  13.319  1.00 29.51 ? 2125 HOH B O   1 
HETATM 20061 O  O   . HOH GB 5 .   ? 3.046   71.941  7.025   1.00 48.29 ? 2126 HOH B O   1 
HETATM 20062 O  O   . HOH GB 5 .   ? 0.889   69.990  5.939   1.00 48.18 ? 2127 HOH B O   1 
HETATM 20063 O  O   . HOH GB 5 .   ? -6.953  66.932  9.870   1.00 58.82 ? 2128 HOH B O   1 
HETATM 20064 O  O   . HOH GB 5 .   ? -0.055  65.197  4.394   1.00 41.16 ? 2129 HOH B O   1 
HETATM 20065 O  O   . HOH GB 5 .   ? -2.732  63.859  4.125   1.00 47.39 ? 2130 HOH B O   1 
HETATM 20066 O  O   . HOH GB 5 .   ? -4.089  68.894  0.309   1.00 48.69 ? 2131 HOH B O   1 
HETATM 20067 O  O   . HOH GB 5 .   ? -0.705  69.738  2.467   1.00 62.81 ? 2132 HOH B O   1 
HETATM 20068 O  O   . HOH GB 5 .   ? -4.121  63.622  9.684   1.00 33.46 ? 2133 HOH B O   1 
HETATM 20069 O  O   . HOH GB 5 .   ? 3.283   58.635  14.796  1.00 34.09 ? 2134 HOH B O   1 
HETATM 20070 O  O   . HOH GB 5 .   ? 0.330   60.133  17.328  1.00 40.67 ? 2135 HOH B O   1 
HETATM 20071 O  O   . HOH GB 5 .   ? 3.128   61.495  20.124  1.00 53.50 ? 2136 HOH B O   1 
HETATM 20072 O  O   . HOH GB 5 .   ? -2.230  71.026  21.636  1.00 34.39 ? 2137 HOH B O   1 
HETATM 20073 O  O   . HOH GB 5 .   ? 5.055   66.984  18.157  1.00 47.94 ? 2138 HOH B O   1 
HETATM 20074 O  O   . HOH GB 5 .   ? 4.575   69.863  19.827  1.00 40.56 ? 2139 HOH B O   1 
HETATM 20075 O  O   . HOH GB 5 .   ? 9.691   70.927  24.497  1.00 33.63 ? 2140 HOH B O   1 
HETATM 20076 O  O   . HOH GB 5 .   ? 12.830  75.507  25.695  1.00 53.34 ? 2141 HOH B O   1 
HETATM 20077 O  O   . HOH GB 5 .   ? 4.695   70.573  22.566  1.00 44.63 ? 2142 HOH B O   1 
HETATM 20078 O  O   . HOH GB 5 .   ? 7.061   70.607  26.170  1.00 46.01 ? 2143 HOH B O   1 
HETATM 20079 O  O   . HOH GB 5 .   ? 0.597   71.328  22.514  1.00 35.95 ? 2144 HOH B O   1 
HETATM 20080 O  O   . HOH GB 5 .   ? 1.095   70.147  26.972  1.00 43.03 ? 2145 HOH B O   1 
HETATM 20081 O  O   . HOH GB 5 .   ? 1.192   69.276  24.070  1.00 49.52 ? 2146 HOH B O   1 
HETATM 20082 O  O   . HOH GB 5 .   ? 10.899  73.375  26.272  1.00 43.12 ? 2147 HOH B O   1 
HETATM 20083 O  O   . HOH GB 5 .   ? 10.540  82.462  28.456  1.00 44.55 ? 2148 HOH B O   1 
HETATM 20084 O  O   . HOH GB 5 .   ? 7.357   88.232  27.117  1.00 24.67 ? 2149 HOH B O   1 
HETATM 20085 O  O   . HOH GB 5 .   ? 7.844   85.896  29.384  1.00 33.30 ? 2150 HOH B O   1 
HETATM 20086 O  O   . HOH GB 5 .   ? 4.739   99.773  22.889  1.00 51.02 ? 2151 HOH B O   1 
HETATM 20087 O  O   . HOH GB 5 .   ? -0.511  102.464 26.578  1.00 53.19 ? 2152 HOH B O   1 
HETATM 20088 O  O   . HOH HB 5 .   ? 48.838  71.880  37.276  1.00 58.85 ? 2001 HOH C O   1 
HETATM 20089 O  O   . HOH HB 5 .   ? 52.985  72.071  33.005  1.00 59.45 ? 2002 HOH C O   1 
HETATM 20090 O  O   . HOH HB 5 .   ? 24.361  86.777  19.543  1.00 61.31 ? 2003 HOH C O   1 
HETATM 20091 O  O   . HOH HB 5 .   ? 35.189  85.674  33.893  1.00 36.93 ? 2004 HOH C O   1 
HETATM 20092 O  O   . HOH HB 5 .   ? 26.061  88.537  20.102  1.00 49.09 ? 2005 HOH C O   1 
HETATM 20093 O  O   . HOH HB 5 .   ? 24.581  84.440  20.741  1.00 51.07 ? 2006 HOH C O   1 
HETATM 20094 O  O   . HOH HB 5 .   ? 33.567  85.838  31.783  1.00 41.42 ? 2007 HOH C O   1 
HETATM 20095 O  O   . HOH HB 5 .   ? 29.894  73.596  32.194  1.00 49.41 ? 2008 HOH C O   1 
HETATM 20096 O  O   . HOH HB 5 .   ? 31.195  75.506  6.986   1.00 53.57 ? 2009 HOH C O   1 
HETATM 20097 O  O   . HOH HB 5 .   ? 31.715  89.822  26.985  1.00 53.00 ? 2010 HOH C O   1 
HETATM 20098 O  O   . HOH HB 5 .   ? 30.057  82.615  36.265  1.00 51.55 ? 2011 HOH C O   1 
HETATM 20099 O  O   . HOH HB 5 .   ? 33.109  73.766  35.923  1.00 51.99 ? 2012 HOH C O   1 
HETATM 20100 O  O   . HOH HB 5 .   ? 27.382  88.317  22.353  1.00 40.44 ? 2013 HOH C O   1 
HETATM 20101 O  O   . HOH HB 5 .   ? 25.721  85.154  23.108  1.00 36.59 ? 2014 HOH C O   1 
HETATM 20102 O  O   . HOH HB 5 .   ? 21.845  79.276  27.074  1.00 54.50 ? 2015 HOH C O   1 
HETATM 20103 O  O   . HOH HB 5 .   ? 26.051  84.896  27.340  1.00 40.54 ? 2016 HOH C O   1 
HETATM 20104 O  O   . HOH HB 5 .   ? 29.007  80.027  31.950  1.00 48.05 ? 2017 HOH C O   1 
HETATM 20105 O  O   . HOH HB 5 .   ? 32.206  72.940  31.172  1.00 38.44 ? 2018 HOH C O   1 
HETATM 20106 O  O   . HOH HB 5 .   ? 30.156  71.234  9.152   1.00 52.52 ? 2019 HOH C O   1 
HETATM 20107 O  O   . HOH HB 5 .   ? 29.367  75.753  8.631   1.00 48.63 ? 2020 HOH C O   1 
HETATM 20108 O  O   . HOH HB 5 .   ? 33.723  72.163  33.314  1.00 40.13 ? 2021 HOH C O   1 
HETATM 20109 O  O   . HOH HB 5 .   ? 40.101  74.160  34.879  1.00 34.21 ? 2022 HOH C O   1 
HETATM 20110 O  O   . HOH HB 5 .   ? 35.878  74.345  35.811  1.00 37.74 ? 2023 HOH C O   1 
HETATM 20111 O  O   . HOH HB 5 .   ? 24.038  86.112  17.065  1.00 48.39 ? 2024 HOH C O   1 
HETATM 20112 O  O   . HOH HB 5 .   ? 41.797  72.547  34.196  1.00 53.57 ? 2025 HOH C O   1 
HETATM 20113 O  O   . HOH HB 5 .   ? 40.779  100.830 26.997  1.00 61.04 ? 2026 HOH C O   1 
HETATM 20114 O  O   . HOH HB 5 .   ? 44.494  99.366  28.830  1.00 52.74 ? 2027 HOH C O   1 
HETATM 20115 O  O   . HOH HB 5 .   ? 33.425  97.644  31.624  1.00 58.57 ? 2028 HOH C O   1 
HETATM 20116 O  O   . HOH HB 5 .   ? 46.517  67.156  30.817  1.00 59.23 ? 2029 HOH C O   1 
HETATM 20117 O  O   . HOH HB 5 .   ? 51.681  68.570  28.865  1.00 38.81 ? 2030 HOH C O   1 
HETATM 20118 O  O   . HOH HB 5 .   ? 52.184  65.942  28.530  1.00 56.23 ? 2031 HOH C O   1 
HETATM 20119 O  O   . HOH HB 5 .   ? 57.150  69.350  26.728  1.00 55.67 ? 2032 HOH C O   1 
HETATM 20120 O  O   . HOH HB 5 .   ? 51.974  89.152  20.895  1.00 54.48 ? 2033 HOH C O   1 
HETATM 20121 O  O   . HOH HB 5 .   ? 61.175  74.927  24.373  1.00 59.71 ? 2034 HOH C O   1 
HETATM 20122 O  O   . HOH HB 5 .   ? 53.770  71.286  22.949  1.00 70.30 ? 2035 HOH C O   1 
HETATM 20123 O  O   . HOH HB 5 .   ? 56.952  72.473  20.986  1.00 61.59 ? 2036 HOH C O   1 
HETATM 20124 O  O   . HOH HB 5 .   ? 54.453  75.703  23.001  1.00 58.04 ? 2037 HOH C O   1 
HETATM 20125 O  O   . HOH HB 5 .   ? 52.633  73.751  24.692  1.00 40.07 ? 2038 HOH C O   1 
HETATM 20126 O  O   . HOH HB 5 .   ? 48.289  67.996  29.228  1.00 40.08 ? 2039 HOH C O   1 
HETATM 20127 O  O   . HOH HB 5 .   ? 41.460  71.616  12.819  1.00 43.58 ? 2040 HOH C O   1 
HETATM 20128 O  O   . HOH HB 5 .   ? 35.920  68.515  33.819  1.00 60.58 ? 2041 HOH C O   1 
HETATM 20129 O  O   . HOH HB 5 .   ? 40.695  70.449  16.501  1.00 49.32 ? 2042 HOH C O   1 
HETATM 20130 O  O   . HOH HB 5 .   ? 34.988  70.599  9.136   1.00 45.70 ? 2043 HOH C O   1 
HETATM 20131 O  O   . HOH HB 5 .   ? 36.557  72.631  8.834   1.00 55.75 ? 2044 HOH C O   1 
HETATM 20132 O  O   . HOH HB 5 .   ? 21.644  73.478  26.694  1.00 53.54 ? 2045 HOH C O   1 
HETATM 20133 O  O   . HOH HB 5 .   ? 23.638  81.819  19.677  1.00 29.82 ? 2046 HOH C O   1 
HETATM 20134 O  O   . HOH HB 5 .   ? 21.406  74.452  18.027  1.00 45.71 ? 2047 HOH C O   1 
HETATM 20135 O  O   . HOH HB 5 .   ? 25.228  80.563  17.759  1.00 28.88 ? 2048 HOH C O   1 
HETATM 20136 O  O   . HOH HB 5 .   ? 25.754  77.419  12.855  1.00 48.52 ? 2049 HOH C O   1 
HETATM 20137 O  O   . HOH HB 5 .   ? 43.082  70.313  17.310  1.00 56.41 ? 2050 HOH C O   1 
HETATM 20138 O  O   . HOH HB 5 .   ? 19.376  72.539  15.633  1.00 46.00 ? 2051 HOH C O   1 
HETATM 20139 O  O   . HOH HB 5 .   ? 20.264  74.749  15.760  1.00 39.78 ? 2052 HOH C O   1 
HETATM 20140 O  O   . HOH HB 5 .   ? 20.381  67.695  13.308  1.00 62.12 ? 2053 HOH C O   1 
HETATM 20141 O  O   . HOH HB 5 .   ? 28.549  74.277  10.261  1.00 37.00 ? 2054 HOH C O   1 
HETATM 20142 O  O   . HOH HB 5 .   ? 28.018  77.479  11.863  1.00 40.02 ? 2055 HOH C O   1 
HETATM 20143 O  O   . HOH HB 5 .   ? 24.311  83.863  15.554  1.00 43.92 ? 2056 HOH C O   1 
HETATM 20144 O  O   . HOH HB 5 .   ? 33.479  78.242  6.307   1.00 47.68 ? 2057 HOH C O   1 
HETATM 20145 O  O   . HOH HB 5 .   ? 37.089  75.085  3.278   1.00 42.56 ? 2058 HOH C O   1 
HETATM 20146 O  O   . HOH HB 5 .   ? 47.752  93.816  18.429  1.00 46.94 ? 2059 HOH C O   1 
HETATM 20147 O  O   . HOH HB 5 .   ? 50.615  94.033  20.879  1.00 54.56 ? 2060 HOH C O   1 
HETATM 20148 O  O   . HOH HB 5 .   ? 48.910  90.712  17.570  1.00 59.92 ? 2061 HOH C O   1 
HETATM 20149 O  O   . HOH HB 5 .   ? 39.448  92.569  4.118   1.00 59.75 ? 2062 HOH C O   1 
HETATM 20150 O  O   . HOH HB 5 .   ? 39.421  92.577  31.131  1.00 26.04 ? 2063 HOH C O   1 
HETATM 20151 O  O   . HOH HB 5 .   ? 44.544  90.042  12.410  1.00 55.93 ? 2064 HOH C O   1 
HETATM 20152 O  O   . HOH HB 5 .   ? 42.293  98.733  28.494  1.00 43.08 ? 2065 HOH C O   1 
HETATM 20153 O  O   . HOH HB 5 .   ? 43.926  96.317  25.745  1.00 33.63 ? 2066 HOH C O   1 
HETATM 20154 O  O   . HOH HB 5 .   ? 32.619  94.786  30.021  1.00 57.53 ? 2067 HOH C O   1 
HETATM 20155 O  O   . HOH HB 5 .   ? 31.426  91.819  14.667  1.00 58.70 ? 2068 HOH C O   1 
HETATM 20156 O  O   . HOH HB 5 .   ? 30.881  91.198  24.263  1.00 48.83 ? 2069 HOH C O   1 
HETATM 20157 O  O   . HOH HB 5 .   ? 38.242  93.979  17.872  1.00 41.42 ? 2070 HOH C O   1 
HETATM 20158 O  O   . HOH HB 5 .   ? 32.274  93.870  21.981  1.00 49.39 ? 2071 HOH C O   1 
HETATM 20159 O  O   . HOH HB 5 .   ? 34.095  92.270  18.130  1.00 53.05 ? 2072 HOH C O   1 
HETATM 20160 O  O   . HOH HB 5 .   ? 42.420  96.283  23.329  1.00 43.36 ? 2073 HOH C O   1 
HETATM 20161 O  O   . HOH HB 5 .   ? 38.473  86.624  15.075  1.00 34.99 ? 2074 HOH C O   1 
HETATM 20162 O  O   . HOH HB 5 .   ? 46.757  88.335  14.891  1.00 56.81 ? 2075 HOH C O   1 
HETATM 20163 O  O   . HOH HB 5 .   ? 51.888  83.435  16.199  1.00 37.66 ? 2076 HOH C O   1 
HETATM 20164 O  O   . HOH HB 5 .   ? 49.702  88.637  19.434  1.00 40.23 ? 2077 HOH C O   1 
HETATM 20165 O  O   . HOH HB 5 .   ? 57.302  87.806  15.569  1.00 53.07 ? 2078 HOH C O   1 
HETATM 20166 O  O   . HOH HB 5 .   ? 53.470  78.468  15.808  1.00 54.18 ? 2079 HOH C O   1 
HETATM 20167 O  O   . HOH HB 5 .   ? 43.758  72.386  11.256  1.00 36.23 ? 2080 HOH C O   1 
HETATM 20168 O  O   . HOH HB 5 .   ? 44.083  75.126  7.284   1.00 43.87 ? 2081 HOH C O   1 
HETATM 20169 O  O   . HOH HB 5 .   ? 50.601  73.383  14.017  1.00 57.62 ? 2082 HOH C O   1 
HETATM 20170 O  O   . HOH HB 5 .   ? 52.547  75.452  14.306  1.00 63.99 ? 2083 HOH C O   1 
HETATM 20171 O  O   . HOH HB 5 .   ? 52.437  80.881  15.274  1.00 39.47 ? 2084 HOH C O   1 
HETATM 20172 O  O   . HOH HB 5 .   ? 47.199  87.224  10.198  1.00 41.91 ? 2085 HOH C O   1 
HETATM 20173 O  O   . HOH HB 5 .   ? 39.349  72.501  16.700  1.00 33.05 ? 2086 HOH C O   1 
HETATM 20174 O  O   . HOH HB 5 .   ? 37.017  72.553  11.329  1.00 41.96 ? 2087 HOH C O   1 
HETATM 20175 O  O   . HOH HB 5 .   ? 29.455  68.891  20.711  1.00 33.64 ? 2088 HOH C O   1 
HETATM 20176 O  O   . HOH HB 5 .   ? 26.413  69.281  14.682  1.00 47.79 ? 2089 HOH C O   1 
HETATM 20177 O  O   . HOH HB 5 .   ? 24.445  65.538  21.227  1.00 52.09 ? 2090 HOH C O   1 
HETATM 20178 O  O   . HOH HB 5 .   ? 23.602  67.815  24.102  1.00 57.82 ? 2091 HOH C O   1 
HETATM 20179 O  O   . HOH HB 5 .   ? 23.366  66.596  17.067  1.00 49.68 ? 2092 HOH C O   1 
HETATM 20180 O  O   . HOH HB 5 .   ? 22.077  75.073  24.117  1.00 29.19 ? 2093 HOH C O   1 
HETATM 20181 O  O   . HOH HB 5 .   ? 18.695  73.056  23.991  1.00 58.28 ? 2094 HOH C O   1 
HETATM 20182 O  O   . HOH HB 5 .   ? 27.561  67.379  22.031  1.00 37.79 ? 2095 HOH C O   1 
HETATM 20183 O  O   . HOH HB 5 .   ? 29.959  64.669  23.668  1.00 41.31 ? 2096 HOH C O   1 
HETATM 20184 O  O   . HOH HB 5 .   ? 31.637  68.705  27.792  1.00 49.82 ? 2097 HOH C O   1 
HETATM 20185 O  O   . HOH HB 5 .   ? 26.250  66.907  25.915  1.00 52.02 ? 2098 HOH C O   1 
HETATM 20186 O  O   . HOH HB 5 .   ? 34.017  68.149  26.680  1.00 41.91 ? 2099 HOH C O   1 
HETATM 20187 O  O   . HOH HB 5 .   ? 39.765  67.445  19.084  1.00 51.67 ? 2100 HOH C O   1 
HETATM 20188 O  O   . HOH HB 5 .   ? 40.750  65.397  22.484  1.00 52.63 ? 2101 HOH C O   1 
HETATM 20189 O  O   . HOH HB 5 .   ? 40.548  63.243  25.687  1.00 57.69 ? 2102 HOH C O   1 
HETATM 20190 O  O   . HOH HB 5 .   ? 41.016  67.454  25.666  1.00 52.63 ? 2103 HOH C O   1 
HETATM 20191 O  O   . HOH HB 5 .   ? 45.307  71.120  18.165  1.00 43.24 ? 2104 HOH C O   1 
HETATM 20192 O  O   . HOH HB 5 .   ? 42.654  68.557  19.105  1.00 40.28 ? 2105 HOH C O   1 
HETATM 20193 O  O   . HOH HB 5 .   ? 55.454  74.260  20.747  1.00 47.15 ? 2106 HOH C O   1 
HETATM 20194 O  O   . HOH HB 5 .   ? 53.311  72.140  18.074  1.00 52.34 ? 2107 HOH C O   1 
HETATM 20195 O  O   . HOH HB 5 .   ? 49.553  71.090  18.282  1.00 53.23 ? 2108 HOH C O   1 
HETATM 20196 O  O   . HOH HB 5 .   ? 55.745  76.713  26.419  1.00 50.62 ? 2109 HOH C O   1 
HETATM 20197 O  O   . HOH HB 5 .   ? 55.195  79.205  25.546  1.00 50.27 ? 2110 HOH C O   1 
HETATM 20198 O  O   . HOH HB 5 .   ? 52.398  85.034  26.312  1.00 40.14 ? 2111 HOH C O   1 
HETATM 20199 O  O   . HOH HB 5 .   ? 50.340  90.811  23.877  1.00 42.81 ? 2112 HOH C O   1 
HETATM 20200 O  O   . HOH HB 5 .   ? 24.286  84.887  12.604  1.00 53.28 ? 2113 HOH C O   1 
HETATM 20201 O  O   . HOH HB 5 .   ? 25.753  81.613  15.217  1.00 33.51 ? 2114 HOH C O   1 
HETATM 20202 O  O   . HOH HB 5 .   ? 33.019  80.577  7.464   1.00 50.68 ? 2115 HOH C O   1 
HETATM 20203 O  O   . HOH HB 5 .   ? 29.383  78.877  9.242   1.00 46.84 ? 2116 HOH C O   1 
HETATM 20204 O  O   . HOH HB 5 .   ? 36.093  75.258  7.832   1.00 45.70 ? 2117 HOH C O   1 
HETATM 20205 O  O   . HOH HB 5 .   ? 41.892  78.386  13.729  1.00 30.16 ? 2118 HOH C O   1 
HETATM 20206 O  O   . HOH HB 5 .   ? 38.262  75.189  5.555   1.00 41.45 ? 2119 HOH C O   1 
HETATM 20207 O  O   . HOH HB 5 .   ? 35.233  81.706  4.265   1.00 41.93 ? 2120 HOH C O   1 
HETATM 20208 O  O   . HOH HB 5 .   ? 45.287  77.300  5.725   1.00 43.94 ? 2121 HOH C O   1 
HETATM 20209 O  O   . HOH HB 5 .   ? 42.921  81.414  1.595   1.00 32.23 ? 2122 HOH C O   1 
HETATM 20210 O  O   . HOH HB 5 .   ? 39.910  72.622  5.805   1.00 57.84 ? 2123 HOH C O   1 
HETATM 20211 O  O   . HOH HB 5 .   ? 41.891  76.447  -0.508  1.00 58.10 ? 2124 HOH C O   1 
HETATM 20212 O  O   . HOH HB 5 .   ? 34.736  84.694  3.141   1.00 59.13 ? 2125 HOH C O   1 
HETATM 20213 O  O   . HOH HB 5 .   ? 40.098  89.867  0.110   1.00 32.01 ? 2126 HOH C O   1 
HETATM 20214 O  O   . HOH HB 5 .   ? 38.707  89.658  2.778   1.00 39.33 ? 2127 HOH C O   1 
HETATM 20215 O  O   . HOH HB 5 .   ? 43.203  88.019  13.888  1.00 37.82 ? 2128 HOH C O   1 
HETATM 20216 O  O   . HOH HB 5 .   ? 33.643  86.938  6.673   1.00 51.96 ? 2129 HOH C O   1 
HETATM 20217 O  O   . HOH HB 5 .   ? 35.906  87.246  13.174  1.00 37.39 ? 2130 HOH C O   1 
HETATM 20218 O  O   . HOH HB 5 .   ? 34.384  87.342  9.678   1.00 48.72 ? 2131 HOH C O   1 
HETATM 20219 O  O   . HOH HB 5 .   ? 31.326  90.373  12.292  1.00 55.37 ? 2132 HOH C O   1 
HETATM 20220 O  O   . HOH HB 5 .   ? 35.818  92.898  16.690  1.00 47.42 ? 2133 HOH C O   1 
HETATM 20221 O  O   . HOH HB 5 .   ? 40.561  92.862  16.591  1.00 36.30 ? 2134 HOH C O   1 
HETATM 20222 O  O   . HOH HB 5 .   ? 40.600  88.631  14.989  1.00 37.25 ? 2135 HOH C O   1 
HETATM 20223 O  O   . HOH HB 5 .   ? 36.007  89.342  15.141  1.00 45.64 ? 2136 HOH C O   1 
HETATM 20224 O  O   . HOH HB 5 .   ? 31.856  90.767  17.335  1.00 33.76 ? 2137 HOH C O   1 
HETATM 20225 O  O   . HOH HB 5 .   ? 33.099  87.783  29.384  1.00 42.34 ? 2138 HOH C O   1 
HETATM 20226 O  O   . HOH HB 5 .   ? 36.534  87.008  32.028  1.00 31.91 ? 2139 HOH C O   1 
HETATM 20227 O  O   . HOH HB 5 .   ? 37.056  83.653  32.786  1.00 24.22 ? 2140 HOH C O   1 
HETATM 20228 O  O   . HOH HB 5 .   ? 47.235  75.761  37.905  1.00 46.18 ? 2141 HOH C O   1 
HETATM 20229 O  O   . HOH HB 5 .   ? 40.365  74.007  39.723  1.00 45.82 ? 2142 HOH C O   1 
HETATM 20230 O  O   . HOH HB 5 .   ? 40.294  77.033  40.580  1.00 37.36 ? 2143 HOH C O   1 
HETATM 20231 O  O   . HOH HB 5 .   ? 42.074  77.155  47.944  1.00 52.34 ? 2144 HOH C O   1 
HETATM 20232 O  O   . HOH IB 5 .   ? -10.033 96.263  88.717  1.00 59.89 ? 2001 HOH D O   1 
HETATM 20233 O  O   . HOH IB 5 .   ? -10.298 99.184  85.159  1.00 49.70 ? 2002 HOH D O   1 
HETATM 20234 O  O   . HOH IB 5 .   ? -5.430  98.063  91.008  1.00 45.32 ? 2003 HOH D O   1 
HETATM 20235 O  O   . HOH IB 5 .   ? 6.716   87.540  87.788  1.00 45.69 ? 2004 HOH D O   1 
HETATM 20236 O  O   . HOH IB 5 .   ? 17.964  87.303  76.135  1.00 61.14 ? 2005 HOH D O   1 
HETATM 20237 O  O   . HOH IB 5 .   ? 8.509   87.587  85.907  1.00 41.81 ? 2006 HOH D O   1 
HETATM 20238 O  O   . HOH IB 5 .   ? 3.014   99.843  91.308  1.00 48.49 ? 2007 HOH D O   1 
HETATM 20239 O  O   . HOH IB 5 .   ? 16.902  87.815  78.454  1.00 57.01 ? 2008 HOH D O   1 
HETATM 20240 O  O   . HOH IB 5 .   ? -8.780  108.331 81.238  1.00 53.36 ? 2009 HOH D O   1 
HETATM 20241 O  O   . HOH IB 5 .   ? 20.469  93.304  82.764  1.00 57.95 ? 2010 HOH D O   1 
HETATM 20242 O  O   . HOH IB 5 .   ? 16.355  88.031  82.152  1.00 46.58 ? 2011 HOH D O   1 
HETATM 20243 O  O   . HOH IB 5 .   ? 20.692  94.734  66.239  1.00 57.14 ? 2012 HOH D O   1 
HETATM 20244 O  O   . HOH IB 5 .   ? 13.737  97.771  85.781  1.00 58.53 ? 2013 HOH D O   1 
HETATM 20245 O  O   . HOH IB 5 .   ? 14.707  97.504  63.556  1.00 57.43 ? 2014 HOH D O   1 
HETATM 20246 O  O   . HOH IB 5 .   ? 6.482   99.102  89.833  1.00 46.02 ? 2015 HOH D O   1 
HETATM 20247 O  O   . HOH IB 5 .   ? 2.022   99.480  88.580  1.00 39.30 ? 2016 HOH D O   1 
HETATM 20248 O  O   . HOH IB 5 .   ? 8.273   101.466 87.615  1.00 49.88 ? 2017 HOH D O   1 
HETATM 20249 O  O   . HOH IB 5 .   ? 0.299   101.158 87.898  1.00 46.70 ? 2018 HOH D O   1 
HETATM 20250 O  O   . HOH IB 5 .   ? 10.465  99.665  58.341  1.00 51.76 ? 2019 HOH D O   1 
HETATM 20251 O  O   . HOH IB 5 .   ? -3.494  106.632 83.773  1.00 61.12 ? 2020 HOH D O   1 
HETATM 20252 O  O   . HOH IB 5 .   ? -2.577  74.343  82.080  1.00 51.11 ? 2021 HOH D O   1 
HETATM 20253 O  O   . HOH IB 5 .   ? -10.679 101.751 85.652  1.00 54.64 ? 2022 HOH D O   1 
HETATM 20254 O  O   . HOH IB 5 .   ? -17.481 103.375 80.191  1.00 47.83 ? 2023 HOH D O   1 
HETATM 20255 O  O   . HOH IB 5 .   ? -9.585  100.141 77.345  1.00 40.79 ? 2024 HOH D O   1 
HETATM 20256 O  O   . HOH IB 5 .   ? -5.509  105.826 82.266  1.00 41.16 ? 2025 HOH D O   1 
HETATM 20257 O  O   . HOH IB 5 .   ? -8.662  105.419 81.566  1.00 37.86 ? 2026 HOH D O   1 
HETATM 20258 O  O   . HOH IB 5 .   ? 6.750   104.746 87.635  1.00 60.75 ? 2027 HOH D O   1 
HETATM 20259 O  O   . HOH IB 5 .   ? 10.314  100.323 85.574  1.00 45.82 ? 2028 HOH D O   1 
HETATM 20260 O  O   . HOH IB 5 .   ? 20.928  97.566  79.131  1.00 49.45 ? 2029 HOH D O   1 
HETATM 20261 O  O   . HOH IB 5 .   ? 18.030  92.382  72.814  1.00 46.87 ? 2030 HOH D O   1 
HETATM 20262 O  O   . HOH IB 5 .   ? 17.517  95.820  67.698  1.00 64.48 ? 2031 HOH D O   1 
HETATM 20263 O  O   . HOH IB 5 .   ? 20.939  97.248  67.256  1.00 56.37 ? 2032 HOH D O   1 
HETATM 20264 O  O   . HOH IB 5 .   ? 15.725  98.861  65.402  1.00 61.32 ? 2033 HOH D O   1 
HETATM 20265 O  O   . HOH IB 5 .   ? 15.614  95.771  66.049  1.00 55.73 ? 2034 HOH D O   1 
HETATM 20266 O  O   . HOH IB 5 .   ? 8.315   98.269  57.905  1.00 49.67 ? 2035 HOH D O   1 
HETATM 20267 O  O   . HOH IB 5 .   ? 2.037   97.407  53.993  1.00 54.89 ? 2036 HOH D O   1 
HETATM 20268 O  O   . HOH IB 5 .   ? -4.265  79.796  71.377  1.00 46.84 ? 2037 HOH D O   1 
HETATM 20269 O  O   . HOH IB 5 .   ? 1.786   93.970  53.173  1.00 39.02 ? 2038 HOH D O   1 
HETATM 20270 O  O   . HOH IB 5 .   ? 2.375   80.873  84.796  1.00 29.68 ? 2039 HOH D O   1 
HETATM 20271 O  O   . HOH IB 5 .   ? 0.213   83.483  65.770  1.00 48.93 ? 2040 HOH D O   1 
HETATM 20272 O  O   . HOH IB 5 .   ? 5.113   82.688  79.723  1.00 47.41 ? 2041 HOH D O   1 
HETATM 20273 O  O   . HOH IB 5 .   ? -0.083  74.600  81.858  1.00 49.12 ? 2042 HOH D O   1 
HETATM 20274 O  O   . HOH IB 5 .   ? 6.405   84.560  83.899  1.00 46.18 ? 2043 HOH D O   1 
HETATM 20275 O  O   . HOH IB 5 .   ? 8.178   82.337  86.393  1.00 50.03 ? 2044 HOH D O   1 
HETATM 20276 O  O   . HOH IB 5 .   ? 10.896  83.329  82.084  1.00 62.33 ? 2045 HOH D O   1 
HETATM 20277 O  O   . HOH IB 5 .   ? 10.351  76.210  76.217  1.00 53.84 ? 2046 HOH D O   1 
HETATM 20278 O  O   . HOH IB 5 .   ? 4.650   79.513  71.748  1.00 51.38 ? 2047 HOH D O   1 
HETATM 20279 O  O   . HOH IB 5 .   ? -0.153  77.377  76.650  1.00 48.48 ? 2048 HOH D O   1 
HETATM 20280 O  O   . HOH IB 5 .   ? 5.091   86.776  68.871  1.00 44.31 ? 2049 HOH D O   1 
HETATM 20281 O  O   . HOH IB 5 .   ? -8.177  90.539  68.931  1.00 43.24 ? 2050 HOH D O   1 
HETATM 20282 O  O   . HOH IB 5 .   ? -6.514  85.030  72.104  1.00 45.82 ? 2051 HOH D O   1 
HETATM 20283 O  O   . HOH IB 5 .   ? -13.740 89.898  64.861  1.00 55.41 ? 2052 HOH D O   1 
HETATM 20284 O  O   . HOH IB 5 .   ? 0.827   101.233 64.735  1.00 41.07 ? 2053 HOH D O   1 
HETATM 20285 O  O   . HOH IB 5 .   ? 3.171   103.151 70.103  1.00 52.81 ? 2054 HOH D O   1 
HETATM 20286 O  O   . HOH IB 5 .   ? 0.882   103.334 71.147  1.00 54.28 ? 2055 HOH D O   1 
HETATM 20287 O  O   . HOH IB 5 .   ? 2.504   102.009 65.976  1.00 53.35 ? 2056 HOH D O   1 
HETATM 20288 O  O   . HOH IB 5 .   ? 0.675   98.610  60.475  1.00 50.83 ? 2057 HOH D O   1 
HETATM 20289 O  O   . HOH IB 5 .   ? -8.903  97.531  66.858  1.00 59.05 ? 2058 HOH D O   1 
HETATM 20290 O  O   . HOH IB 5 .   ? -3.105  94.745  60.221  1.00 50.02 ? 2059 HOH D O   1 
HETATM 20291 O  O   . HOH IB 5 .   ? -8.671  93.196  67.915  1.00 45.50 ? 2060 HOH D O   1 
HETATM 20292 O  O   . HOH IB 5 .   ? -2.888  86.707  63.318  1.00 52.61 ? 2061 HOH D O   1 
HETATM 20293 O  O   . HOH IB 5 .   ? 4.363   101.059 70.484  1.00 42.64 ? 2062 HOH D O   1 
HETATM 20294 O  O   . HOH IB 5 .   ? 13.873  104.288 75.433  1.00 42.33 ? 2063 HOH D O   1 
HETATM 20295 O  O   . HOH IB 5 .   ? 11.939  104.455 67.380  1.00 42.51 ? 2064 HOH D O   1 
HETATM 20296 O  O   . HOH IB 5 .   ? 17.564  103.810 69.929  1.00 54.90 ? 2065 HOH D O   1 
HETATM 20297 O  O   . HOH IB 5 .   ? 9.049   105.348 80.981  1.00 46.14 ? 2066 HOH D O   1 
HETATM 20298 O  O   . HOH IB 5 .   ? 4.872   106.362 73.182  1.00 59.48 ? 2067 HOH D O   1 
HETATM 20299 O  O   . HOH IB 5 .   ? -5.276  109.903 78.908  1.00 59.97 ? 2068 HOH D O   1 
HETATM 20300 O  O   . HOH IB 5 .   ? -1.546  102.372 71.567  1.00 50.44 ? 2069 HOH D O   1 
HETATM 20301 O  O   . HOH IB 5 .   ? -5.735  102.842 71.423  1.00 51.60 ? 2070 HOH D O   1 
HETATM 20302 O  O   . HOH IB 5 .   ? -5.265  105.321 73.928  1.00 48.71 ? 2071 HOH D O   1 
HETATM 20303 O  O   . HOH IB 5 .   ? -11.034 97.927  75.688  1.00 46.53 ? 2072 HOH D O   1 
HETATM 20304 O  O   . HOH IB 5 .   ? -13.048 97.623  79.096  1.00 47.93 ? 2073 HOH D O   1 
HETATM 20305 O  O   . HOH IB 5 .   ? -11.746 98.683  82.353  1.00 47.45 ? 2074 HOH D O   1 
HETATM 20306 O  O   . HOH IB 5 .   ? -11.420 96.582  70.056  1.00 55.24 ? 2075 HOH D O   1 
HETATM 20307 O  O   . HOH IB 5 .   ? -9.636  88.750  78.878  1.00 41.45 ? 2076 HOH D O   1 
HETATM 20308 O  O   . HOH IB 5 .   ? -7.633  83.136  76.687  1.00 48.99 ? 2077 HOH D O   1 
HETATM 20309 O  O   . HOH IB 5 .   ? 4.892   84.264  81.773  1.00 47.50 ? 2078 HOH D O   1 
HETATM 20310 O  O   . HOH IB 5 .   ? 17.910  91.422  70.402  1.00 49.89 ? 2079 HOH D O   1 
HETATM 20311 O  O   . HOH IB 5 .   ? 11.523  92.263  62.040  1.00 51.29 ? 2080 HOH D O   1 
HETATM 20312 O  O   . HOH IB 5 .   ? 14.856  94.197  64.250  1.00 50.79 ? 2081 HOH D O   1 
HETATM 20313 O  O   . HOH IB 5 .   ? 2.143   95.209  67.335  1.00 36.89 ? 2082 HOH D O   1 
HETATM 20314 O  O   . HOH IB 5 .   ? 8.334   98.497  62.264  1.00 49.76 ? 2083 HOH D O   1 
HETATM 20315 O  O   . HOH IB 5 .   ? 6.619   98.357  59.663  1.00 44.52 ? 2084 HOH D O   1 
HETATM 20316 O  O   . HOH IB 5 .   ? 4.541   96.831  52.983  1.00 51.05 ? 2085 HOH D O   1 
HETATM 20317 O  O   . HOH IB 5 .   ? 2.520   103.255 55.781  1.00 51.21 ? 2086 HOH D O   1 
HETATM 20318 O  O   . HOH IB 5 .   ? 5.148   101.124 59.828  1.00 57.89 ? 2087 HOH D O   1 
HETATM 20319 O  O   . HOH IB 5 .   ? 2.551   92.191  55.106  1.00 38.59 ? 2088 HOH D O   1 
HETATM 20320 O  O   . HOH IB 5 .   ? 5.270   83.488  54.151  1.00 37.88 ? 2089 HOH D O   1 
HETATM 20321 O  O   . HOH IB 5 .   ? 6.341   83.624  56.753  1.00 39.12 ? 2090 HOH D O   1 
HETATM 20322 O  O   . HOH IB 5 .   ? 0.508   85.591  67.352  1.00 42.12 ? 2091 HOH D O   1 
HETATM 20323 O  O   . HOH IB 5 .   ? 10.429  88.846  57.865  1.00 55.82 ? 2092 HOH D O   1 
HETATM 20324 O  O   . HOH IB 5 .   ? 7.715   86.060  67.370  1.00 45.70 ? 2093 HOH D O   1 
HETATM 20325 O  O   . HOH IB 5 .   ? 11.420  82.427  71.926  1.00 45.67 ? 2094 HOH D O   1 
HETATM 20326 O  O   . HOH IB 5 .   ? 3.080   84.780  68.827  1.00 43.28 ? 2095 HOH D O   1 
HETATM 20327 O  O   . HOH IB 5 .   ? 7.176   80.605  70.725  1.00 50.16 ? 2096 HOH D O   1 
HETATM 20328 O  O   . HOH IB 5 .   ? 7.094   84.262  69.299  1.00 49.96 ? 2097 HOH D O   1 
HETATM 20329 O  O   . HOH IB 5 .   ? 3.479   82.369  67.965  1.00 58.70 ? 2098 HOH D O   1 
HETATM 20330 O  O   . HOH IB 5 .   ? 2.705   80.723  70.156  1.00 41.60 ? 2099 HOH D O   1 
HETATM 20331 O  O   . HOH IB 5 .   ? 15.127  84.536  77.238  1.00 54.57 ? 2100 HOH D O   1 
HETATM 20332 O  O   . HOH IB 5 .   ? 9.019   85.409  83.661  1.00 46.40 ? 2101 HOH D O   1 
HETATM 20333 O  O   . HOH IB 5 .   ? 5.041   89.773  86.742  1.00 25.14 ? 2102 HOH D O   1 
HETATM 20334 O  O   . HOH IB 5 .   ? 5.447   86.425  85.969  1.00 34.69 ? 2103 HOH D O   1 
HETATM 20335 O  O   . HOH IB 5 .   ? 1.974   99.211  93.549  1.00 35.75 ? 2104 HOH D O   1 
HETATM 20336 O  O   . HOH IB 5 .   ? -3.498  102.550 94.635  1.00 46.94 ? 2105 HOH D O   1 
HETATM 20337 O  O   . HOH IB 5 .   ? -5.015  98.749  96.015  1.00 51.30 ? 2106 HOH D O   1 
HETATM 20338 O  O   . HOH IB 5 .   ? -0.133  102.625 94.385  1.00 57.33 ? 2107 HOH D O   1 
HETATM 20339 O  O   . HOH JB 5 .   ? 42.936  132.963 64.172  1.00 42.43 ? 2001 HOH E O   1 
HETATM 20340 O  O   . HOH JB 5 .   ? 45.914  129.747 76.543  1.00 50.24 ? 2002 HOH E O   1 
HETATM 20341 O  O   . HOH JB 5 .   ? 52.000  130.852 75.343  1.00 50.65 ? 2003 HOH E O   1 
HETATM 20342 O  O   . HOH JB 5 .   ? 36.073  133.634 62.321  1.00 51.89 ? 2004 HOH E O   1 
HETATM 20343 O  O   . HOH JB 5 .   ? 34.812  127.252 58.938  1.00 47.90 ? 2005 HOH E O   1 
HETATM 20344 O  O   . HOH JB 5 .   ? 28.755  129.409 65.136  1.00 56.06 ? 2006 HOH E O   1 
HETATM 20345 O  O   . HOH JB 5 .   ? 34.923  129.379 64.695  1.00 39.96 ? 2007 HOH E O   1 
HETATM 20346 O  O   . HOH JB 5 .   ? 41.685  127.074 75.859  1.00 50.22 ? 2008 HOH E O   1 
HETATM 20347 O  O   . HOH JB 5 .   ? 28.613  120.352 65.116  1.00 50.70 ? 2009 HOH E O   1 
HETATM 20348 O  O   . HOH JB 5 .   ? 46.108  126.998 76.318  1.00 45.24 ? 2010 HOH E O   1 
HETATM 20349 O  O   . HOH JB 5 .   ? 51.844  128.837 73.715  1.00 40.91 ? 2011 HOH E O   1 
HETATM 20350 O  O   . HOH JB 5 .   ? 48.096  130.021 75.162  1.00 41.85 ? 2012 HOH E O   1 
HETATM 20351 O  O   . HOH JB 5 .   ? 40.620  103.492 59.597  1.00 64.20 ? 2013 HOH E O   1 
HETATM 20352 O  O   . HOH JB 5 .   ? 64.425  124.639 66.775  1.00 67.72 ? 2014 HOH E O   1 
HETATM 20353 O  O   . HOH JB 5 .   ? 42.843  126.289 46.791  1.00 53.54 ? 2015 HOH E O   1 
HETATM 20354 O  O   . HOH JB 5 .   ? 62.776  120.078 72.231  1.00 45.75 ? 2016 HOH E O   1 
HETATM 20355 O  O   . HOH JB 5 .   ? 59.687  120.150 73.894  1.00 46.62 ? 2017 HOH E O   1 
HETATM 20356 O  O   . HOH JB 5 .   ? 44.017  125.514 75.118  1.00 43.15 ? 2018 HOH E O   1 
HETATM 20357 O  O   . HOH JB 5 .   ? 37.436  124.807 75.057  1.00 57.08 ? 2019 HOH E O   1 
HETATM 20358 O  O   . HOH JB 5 .   ? 36.686  121.057 78.542  1.00 60.46 ? 2020 HOH E O   1 
HETATM 20359 O  O   . HOH JB 5 .   ? 32.653  123.040 74.751  1.00 56.35 ? 2021 HOH E O   1 
HETATM 20360 O  O   . HOH JB 5 .   ? 31.525  120.932 64.373  1.00 46.30 ? 2022 HOH E O   1 
HETATM 20361 O  O   . HOH JB 5 .   ? 39.741  114.162 80.043  1.00 59.48 ? 2023 HOH E O   1 
HETATM 20362 O  O   . HOH JB 5 .   ? 29.287  119.681 69.109  1.00 59.00 ? 2024 HOH E O   1 
HETATM 20363 O  O   . HOH JB 5 .   ? 33.209  118.988 63.721  1.00 38.87 ? 2025 HOH E O   1 
HETATM 20364 O  O   . HOH JB 5 .   ? 51.866  111.774 67.544  1.00 49.14 ? 2026 HOH E O   1 
HETATM 20365 O  O   . HOH JB 5 .   ? 28.898  114.924 68.281  1.00 56.66 ? 2027 HOH E O   1 
HETATM 20366 O  O   . HOH JB 5 .   ? 28.488  112.544 69.738  1.00 52.45 ? 2028 HOH E O   1 
HETATM 20367 O  O   . HOH JB 5 .   ? 35.936  109.007 64.615  1.00 50.29 ? 2029 HOH E O   1 
HETATM 20368 O  O   . HOH JB 5 .   ? 31.088  119.738 60.503  1.00 59.66 ? 2030 HOH E O   1 
HETATM 20369 O  O   . HOH JB 5 .   ? 35.927  109.714 57.774  1.00 52.25 ? 2031 HOH E O   1 
HETATM 20370 O  O   . HOH JB 5 .   ? 39.047  106.850 55.764  1.00 60.11 ? 2032 HOH E O   1 
HETATM 20371 O  O   . HOH JB 5 .   ? 40.378  106.795 60.205  1.00 45.62 ? 2033 HOH E O   1 
HETATM 20372 O  O   . HOH JB 5 .   ? 41.795  103.967 57.443  1.00 52.52 ? 2034 HOH E O   1 
HETATM 20373 O  O   . HOH JB 5 .   ? 49.147  102.056 51.985  1.00 41.81 ? 2035 HOH E O   1 
HETATM 20374 O  O   . HOH JB 5 .   ? 47.588  100.656 54.183  1.00 40.34 ? 2036 HOH E O   1 
HETATM 20375 O  O   . HOH JB 5 .   ? 56.467  127.851 51.689  1.00 47.55 ? 2037 HOH E O   1 
HETATM 20376 O  O   . HOH JB 5 .   ? 47.299  102.206 50.022  1.00 40.02 ? 2038 HOH E O   1 
HETATM 20377 O  O   . HOH JB 5 .   ? 46.866  135.752 56.932  1.00 34.26 ? 2039 HOH E O   1 
HETATM 20378 O  O   . HOH JB 5 .   ? 47.903  118.507 48.207  1.00 49.45 ? 2040 HOH E O   1 
HETATM 20379 O  O   . HOH JB 5 .   ? 47.952  136.639 49.803  1.00 54.45 ? 2041 HOH E O   1 
HETATM 20380 O  O   . HOH JB 5 .   ? 44.032  130.418 56.567  1.00 43.60 ? 2042 HOH E O   1 
HETATM 20381 O  O   . HOH JB 5 .   ? 49.332  132.936 49.938  1.00 45.59 ? 2043 HOH E O   1 
HETATM 20382 O  O   . HOH JB 5 .   ? 44.127  132.793 60.387  1.00 44.55 ? 2044 HOH E O   1 
HETATM 20383 O  O   . HOH JB 5 .   ? 41.824  136.050 60.493  1.00 47.36 ? 2045 HOH E O   1 
HETATM 20384 O  O   . HOH JB 5 .   ? 39.189  131.508 59.185  1.00 51.05 ? 2046 HOH E O   1 
HETATM 20385 O  O   . HOH JB 5 .   ? 32.461  124.467 61.295  1.00 54.14 ? 2047 HOH E O   1 
HETATM 20386 O  O   . HOH JB 5 .   ? 37.438  129.826 56.981  1.00 54.49 ? 2048 HOH E O   1 
HETATM 20387 O  O   . HOH JB 5 .   ? 43.088  125.370 49.387  1.00 43.86 ? 2049 HOH E O   1 
HETATM 20388 O  O   . HOH JB 5 .   ? 43.112  130.636 48.039  1.00 60.33 ? 2050 HOH E O   1 
HETATM 20389 O  O   . HOH JB 5 .   ? 47.481  130.742 49.326  1.00 46.64 ? 2051 HOH E O   1 
HETATM 20390 O  O   . HOH JB 5 .   ? 43.985  119.073 53.783  1.00 40.13 ? 2052 HOH E O   1 
HETATM 20391 O  O   . HOH JB 5 .   ? 55.290  123.141 51.458  1.00 47.53 ? 2053 HOH E O   1 
HETATM 20392 O  O   . HOH JB 5 .   ? 57.671  117.322 53.639  1.00 45.80 ? 2054 HOH E O   1 
HETATM 20393 O  O   . HOH JB 5 .   ? 63.599  110.905 56.833  1.00 63.76 ? 2055 HOH E O   1 
HETATM 20394 O  O   . HOH JB 5 .   ? 48.582  113.196 58.989  1.00 32.67 ? 2056 HOH E O   1 
HETATM 20395 O  O   . HOH JB 5 .   ? 50.976  107.630 62.193  1.00 35.90 ? 2057 HOH E O   1 
HETATM 20396 O  O   . HOH JB 5 .   ? 55.628  103.575 58.325  1.00 56.63 ? 2058 HOH E O   1 
HETATM 20397 O  O   . HOH JB 5 .   ? 58.130  110.265 60.974  1.00 55.30 ? 2059 HOH E O   1 
HETATM 20398 O  O   . HOH JB 5 .   ? 49.829  105.793 57.911  1.00 41.61 ? 2060 HOH E O   1 
HETATM 20399 O  O   . HOH JB 5 .   ? 59.288  111.484 58.433  1.00 50.61 ? 2061 HOH E O   1 
HETATM 20400 O  O   . HOH JB 5 .   ? 57.609  110.918 47.646  1.00 53.61 ? 2062 HOH E O   1 
HETATM 20401 O  O   . HOH JB 5 .   ? 52.723  107.596 53.700  1.00 39.17 ? 2063 HOH E O   1 
HETATM 20402 O  O   . HOH JB 5 .   ? 56.615  105.582 55.335  1.00 51.42 ? 2064 HOH E O   1 
HETATM 20403 O  O   . HOH JB 5 .   ? 58.528  115.280 55.069  1.00 42.66 ? 2065 HOH E O   1 
HETATM 20404 O  O   . HOH JB 5 .   ? 51.343  114.772 48.592  1.00 49.65 ? 2066 HOH E O   1 
HETATM 20405 O  O   . HOH JB 5 .   ? 47.759  112.641 65.989  1.00 37.32 ? 2067 HOH E O   1 
HETATM 20406 O  O   . HOH JB 5 .   ? 39.887  114.922 73.666  1.00 34.62 ? 2068 HOH E O   1 
HETATM 20407 O  O   . HOH JB 5 .   ? 35.773  110.223 71.207  1.00 55.52 ? 2069 HOH E O   1 
HETATM 20408 O  O   . HOH JB 5 .   ? 35.237  118.016 77.780  1.00 55.29 ? 2070 HOH E O   1 
HETATM 20409 O  O   . HOH JB 5 .   ? 38.478  115.461 75.912  1.00 43.32 ? 2071 HOH E O   1 
HETATM 20410 O  O   . HOH JB 5 .   ? 33.431  111.188 75.281  1.00 50.74 ? 2072 HOH E O   1 
HETATM 20411 O  O   . HOH JB 5 .   ? 32.324  121.726 72.456  1.00 42.10 ? 2073 HOH E O   1 
HETATM 20412 O  O   . HOH JB 5 .   ? 41.411  115.142 78.601  1.00 56.86 ? 2074 HOH E O   1 
HETATM 20413 O  O   . HOH JB 5 .   ? 43.496  120.838 76.961  1.00 44.74 ? 2075 HOH E O   1 
HETATM 20414 O  O   . HOH JB 5 .   ? 45.464  119.077 76.006  1.00 48.65 ? 2076 HOH E O   1 
HETATM 20415 O  O   . HOH JB 5 .   ? 48.656  111.692 72.005  1.00 42.53 ? 2077 HOH E O   1 
HETATM 20416 O  O   . HOH JB 5 .   ? 51.625  117.313 74.426  1.00 53.09 ? 2078 HOH E O   1 
HETATM 20417 O  O   . HOH JB 5 .   ? 53.985  112.879 66.301  1.00 41.15 ? 2079 HOH E O   1 
HETATM 20418 O  O   . HOH JB 5 .   ? 52.259  112.355 70.127  1.00 47.40 ? 2080 HOH E O   1 
HETATM 20419 O  O   . HOH JB 5 .   ? 58.049  112.626 65.587  1.00 45.82 ? 2081 HOH E O   1 
HETATM 20420 O  O   . HOH JB 5 .   ? 63.407  117.639 64.310  1.00 45.64 ? 2082 HOH E O   1 
HETATM 20421 O  O   . HOH JB 5 .   ? 61.879  119.246 65.533  1.00 47.15 ? 2083 HOH E O   1 
HETATM 20422 O  O   . HOH JB 5 .   ? 60.006  126.896 57.123  1.00 48.80 ? 2084 HOH E O   1 
HETATM 20423 O  O   . HOH JB 5 .   ? 45.221  131.051 58.720  1.00 51.66 ? 2085 HOH E O   1 
HETATM 20424 O  O   . HOH JB 5 .   ? 30.074  115.978 57.939  1.00 48.40 ? 2086 HOH E O   1 
HETATM 20425 O  O   . HOH JB 5 .   ? 32.763  117.280 61.476  1.00 39.22 ? 2087 HOH E O   1 
HETATM 20426 O  O   . HOH JB 5 .   ? 35.548  111.028 59.669  1.00 51.18 ? 2088 HOH E O   1 
HETATM 20427 O  O   . HOH JB 5 .   ? 38.201  110.159 56.172  1.00 40.87 ? 2089 HOH E O   1 
HETATM 20428 O  O   . HOH JB 5 .   ? 42.654  106.996 60.405  1.00 44.98 ? 2090 HOH E O   1 
HETATM 20429 O  O   . HOH JB 5 .   ? 39.856  106.966 53.343  1.00 38.15 ? 2091 HOH E O   1 
HETATM 20430 O  O   . HOH JB 5 .   ? 43.768  105.037 58.405  1.00 40.10 ? 2092 HOH E O   1 
HETATM 20431 O  O   . HOH JB 5 .   ? 50.320  104.447 52.432  1.00 49.32 ? 2093 HOH E O   1 
HETATM 20432 O  O   . HOH JB 5 .   ? 45.866  99.937  60.809  1.00 51.82 ? 2094 HOH E O   1 
HETATM 20433 O  O   . HOH JB 5 .   ? 45.164  100.611 52.602  1.00 45.10 ? 2095 HOH E O   1 
HETATM 20434 O  O   . HOH JB 5 .   ? 43.154  101.425 55.011  1.00 41.69 ? 2096 HOH E O   1 
HETATM 20435 O  O   . HOH JB 5 .   ? 46.516  104.819 49.924  1.00 32.89 ? 2097 HOH E O   1 
HETATM 20436 O  O   . HOH JB 5 .   ? 41.380  110.718 44.727  1.00 42.11 ? 2098 HOH E O   1 
HETATM 20437 O  O   . HOH JB 5 .   ? 48.085  118.605 50.864  1.00 35.49 ? 2099 HOH E O   1 
HETATM 20438 O  O   . HOH JB 5 .   ? 41.216  118.137 53.161  1.00 41.40 ? 2100 HOH E O   1 
HETATM 20439 O  O   . HOH JB 5 .   ? 37.343  123.791 53.500  1.00 38.04 ? 2101 HOH E O   1 
HETATM 20440 O  O   . HOH JB 5 .   ? 45.166  123.679 48.896  1.00 46.63 ? 2102 HOH E O   1 
HETATM 20441 O  O   . HOH JB 5 .   ? 45.611  120.186 51.655  1.00 40.21 ? 2103 HOH E O   1 
HETATM 20442 O  O   . HOH JB 5 .   ? 44.707  120.885 49.315  1.00 50.01 ? 2104 HOH E O   1 
HETATM 20443 O  O   . HOH JB 5 .   ? 40.851  124.029 50.038  1.00 52.46 ? 2105 HOH E O   1 
HETATM 20444 O  O   . HOH JB 5 .   ? 41.264  120.942 51.954  1.00 52.48 ? 2106 HOH E O   1 
HETATM 20445 O  O   . HOH JB 5 .   ? 33.899  126.217 62.487  1.00 41.86 ? 2107 HOH E O   1 
HETATM 20446 O  O   . HOH JB 5 .   ? 41.366  131.923 61.268  1.00 47.26 ? 2108 HOH E O   1 
HETATM 20447 O  O   . HOH JB 5 .   ? 46.848  132.585 65.753  1.00 27.52 ? 2109 HOH E O   1 
HETATM 20448 O  O   . HOH JB 5 .   ? 45.408  133.671 62.961  1.00 35.55 ? 2110 HOH E O   1 
HETATM 20449 O  O   . HOH JB 5 .   ? 59.327  131.894 72.306  1.00 57.21 ? 2111 HOH E O   1 
HETATM 20450 O  O   . HOH JB 5 .   ? 59.513  134.994 71.933  1.00 59.87 ? 2112 HOH E O   1 
HETATM 20451 O  O   . HOH JB 5 .   ? 57.772  132.080 78.304  1.00 64.96 ? 2113 HOH E O   1 
HETATM 20452 O  O   . HOH JB 5 .   ? 53.821  132.455 76.304  1.00 48.94 ? 2114 HOH E O   1 
HETATM 20453 O  O   . HOH KB 5 .   ? 3.301   123.369 123.389 1.00 45.14 ? 2001 HOH F O   1 
HETATM 20454 O  O   . HOH KB 5 .   ? -17.552 115.458 98.650  1.00 59.31 ? 2002 HOH F O   1 
HETATM 20455 O  O   . HOH KB 5 .   ? -8.287  122.302 110.018 1.00 45.49 ? 2003 HOH F O   1 
HETATM 20456 O  O   . HOH KB 5 .   ? -16.152 117.581 104.883 1.00 46.07 ? 2004 HOH F O   1 
HETATM 20457 O  O   . HOH KB 5 .   ? -18.176 113.930 101.276 1.00 42.62 ? 2005 HOH F O   1 
HETATM 20458 O  O   . HOH KB 5 .   ? -18.551 112.599 111.041 1.00 52.88 ? 2006 HOH F O   1 
HETATM 20459 O  O   . HOH KB 5 .   ? -14.209 116.221 107.536 1.00 37.67 ? 2007 HOH F O   1 
HETATM 20460 O  O   . HOH KB 5 .   ? -14.407 108.599 104.371 1.00 44.73 ? 2008 HOH F O   1 
HETATM 20461 O  O   . HOH KB 5 .   ? -5.231  96.722  108.022 1.00 60.94 ? 2009 HOH F O   1 
HETATM 20462 O  O   . HOH KB 5 .   ? -7.698  120.456 122.474 1.00 50.57 ? 2010 HOH F O   1 
HETATM 20463 O  O   . HOH KB 5 .   ? -3.249  121.245 122.639 1.00 46.97 ? 2011 HOH F O   1 
HETATM 20464 O  O   . HOH KB 5 .   ? -0.892  94.588  105.604 1.00 54.56 ? 2012 HOH F O   1 
HETATM 20465 O  O   . HOH KB 5 .   ? 9.623   116.231 126.300 1.00 48.91 ? 2013 HOH F O   1 
HETATM 20466 O  O   . HOH KB 5 .   ? 15.319  109.977 111.903 1.00 48.85 ? 2014 HOH F O   1 
HETATM 20467 O  O   . HOH KB 5 .   ? 3.988   105.273 118.031 1.00 48.68 ? 2015 HOH F O   1 
HETATM 20468 O  O   . HOH KB 5 .   ? -0.868  100.106 115.024 1.00 55.69 ? 2016 HOH F O   1 
HETATM 20469 O  O   . HOH KB 5 .   ? 0.715   97.278  111.906 1.00 54.21 ? 2017 HOH F O   1 
HETATM 20470 O  O   . HOH KB 5 .   ? -14.612 107.285 106.620 1.00 43.56 ? 2018 HOH F O   1 
HETATM 20471 O  O   . HOH KB 5 .   ? -12.156 105.943 107.034 1.00 42.62 ? 2019 HOH F O   1 
HETATM 20472 O  O   . HOH KB 5 .   ? -16.039 100.429 109.372 1.00 55.11 ? 2020 HOH F O   1 
HETATM 20473 O  O   . HOH KB 5 .   ? -8.024  100.057 107.236 1.00 52.10 ? 2021 HOH F O   1 
HETATM 20474 O  O   . HOH KB 5 .   ? -7.196  97.544  109.567 1.00 44.07 ? 2022 HOH F O   1 
HETATM 20475 O  O   . HOH KB 5 .   ? 1.215   94.393  104.025 1.00 48.41 ? 2023 HOH F O   1 
HETATM 20476 O  O   . HOH KB 5 .   ? 8.760   118.383 98.859  1.00 48.75 ? 2024 HOH F O   1 
HETATM 20477 O  O   . HOH KB 5 .   ? -2.786  126.327 104.500 1.00 33.85 ? 2025 HOH F O   1 
HETATM 20478 O  O   . HOH KB 5 .   ? 2.957   124.717 99.188  1.00 42.44 ? 2026 HOH F O   1 
HETATM 20479 O  O   . HOH KB 5 .   ? 0.102   127.675 97.567  1.00 49.61 ? 2027 HOH F O   1 
HETATM 20480 O  O   . HOH KB 5 .   ? -3.275  120.580 103.599 1.00 46.59 ? 2028 HOH F O   1 
HETATM 20481 O  O   . HOH KB 5 .   ? -9.272  124.458 101.362 1.00 52.89 ? 2029 HOH F O   1 
HETATM 20482 O  O   . HOH KB 5 .   ? -9.008  119.763 103.672 1.00 53.91 ? 2030 HOH F O   1 
HETATM 20483 O  O   . HOH KB 5 .   ? -5.731  122.468 106.787 1.00 47.82 ? 2031 HOH F O   1 
HETATM 20484 O  O   . HOH KB 5 .   ? -13.438 111.069 103.708 1.00 43.25 ? 2032 HOH F O   1 
HETATM 20485 O  O   . HOH KB 5 .   ? -2.764  125.377 95.438  1.00 55.36 ? 2033 HOH F O   1 
HETATM 20486 O  O   . HOH KB 5 .   ? -3.983  119.626 93.537  1.00 56.56 ? 2034 HOH F O   1 
HETATM 20487 O  O   . HOH KB 5 .   ? -9.025  117.832 101.673 1.00 57.42 ? 2035 HOH F O   1 
HETATM 20488 O  O   . HOH KB 5 .   ? -6.894  117.370 98.358  1.00 54.12 ? 2036 HOH F O   1 
HETATM 20489 O  O   . HOH KB 5 .   ? 0.234   115.651 97.165  1.00 42.02 ? 2037 HOH F O   1 
HETATM 20490 O  O   . HOH KB 5 .   ? -1.595  120.352 95.265  1.00 50.36 ? 2038 HOH F O   1 
HETATM 20491 O  O   . HOH KB 5 .   ? 2.211   122.314 98.134  1.00 43.32 ? 2039 HOH F O   1 
HETATM 20492 O  O   . HOH KB 5 .   ? 1.186   109.867 102.208 1.00 42.66 ? 2040 HOH F O   1 
HETATM 20493 O  O   . HOH KB 5 .   ? 13.562  112.650 107.807 1.00 44.85 ? 2041 HOH F O   1 
HETATM 20494 O  O   . HOH KB 5 .   ? 10.473  117.150 104.084 1.00 49.35 ? 2042 HOH F O   1 
HETATM 20495 O  O   . HOH KB 5 .   ? 18.452  115.647 103.252 1.00 57.12 ? 2043 HOH F O   1 
HETATM 20496 O  O   . HOH KB 5 .   ? 10.460  101.418 103.281 1.00 45.19 ? 2044 HOH F O   1 
HETATM 20497 O  O   . HOH KB 5 .   ? 6.975   101.025 113.980 1.00 42.25 ? 2045 HOH F O   1 
HETATM 20498 O  O   . HOH KB 5 .   ? 14.229  106.766 114.136 1.00 57.81 ? 2046 HOH F O   1 
HETATM 20499 O  O   . HOH KB 5 .   ? 12.206  101.957 106.579 1.00 45.32 ? 2047 HOH F O   1 
HETATM 20500 O  O   . HOH KB 5 .   ? 14.517  110.816 109.550 1.00 50.27 ? 2048 HOH F O   1 
HETATM 20501 O  O   . HOH KB 5 .   ? 10.759  107.931 101.197 1.00 48.04 ? 2049 HOH F O   1 
HETATM 20502 O  O   . HOH KB 5 .   ? 1.836   105.561 116.292 1.00 46.48 ? 2050 HOH F O   1 
HETATM 20503 O  O   . HOH KB 5 .   ? 1.520   102.911 115.034 1.00 50.95 ? 2051 HOH F O   1 
HETATM 20504 O  O   . HOH KB 5 .   ? -1.015  105.017 117.211 1.00 54.91 ? 2052 HOH F O   1 
HETATM 20505 O  O   . HOH KB 5 .   ? 0.566   99.767  113.183 1.00 45.80 ? 2053 HOH F O   1 
HETATM 20506 O  O   . HOH KB 5 .   ? -5.352  104.702 117.822 1.00 50.47 ? 2054 HOH F O   1 
HETATM 20507 O  O   . HOH KB 5 .   ? -4.967  98.146  116.612 1.00 58.48 ? 2055 HOH F O   1 
HETATM 20508 O  O   . HOH KB 5 .   ? -17.289 107.817 114.657 1.00 52.12 ? 2056 HOH F O   1 
HETATM 20509 O  O   . HOH KB 5 .   ? -0.310  110.355 124.979 1.00 53.36 ? 2057 HOH F O   1 
HETATM 20510 O  O   . HOH KB 5 .   ? -2.891  105.930 118.620 1.00 53.41 ? 2058 HOH F O   1 
HETATM 20511 O  O   . HOH KB 5 .   ? 6.483   106.867 118.357 1.00 51.31 ? 2059 HOH F O   1 
HETATM 20512 O  O   . HOH KB 5 .   ? 10.163  107.581 119.417 1.00 58.30 ? 2060 HOH F O   1 
HETATM 20513 O  O   . HOH KB 5 .   ? 11.733  115.310 119.974 1.00 49.47 ? 2061 HOH F O   1 
HETATM 20514 O  O   . HOH KB 5 .   ? 14.015  119.343 115.953 1.00 63.02 ? 2062 HOH F O   1 
HETATM 20515 O  O   . HOH KB 5 .   ? 10.968  122.134 110.628 1.00 44.81 ? 2063 HOH F O   1 
HETATM 20516 O  O   . HOH KB 5 .   ? 9.680   122.244 104.397 1.00 57.58 ? 2064 HOH F O   1 
HETATM 20517 O  O   . HOH KB 5 .   ? -3.418  121.576 105.699 1.00 56.78 ? 2065 HOH F O   1 
HETATM 20518 O  O   . HOH KB 5 .   ? -10.173 101.683 101.256 1.00 54.84 ? 2066 HOH F O   1 
HETATM 20519 O  O   . HOH KB 5 .   ? -11.024 104.402 105.003 1.00 49.87 ? 2067 HOH F O   1 
HETATM 20520 O  O   . HOH KB 5 .   ? 0.499   97.808  109.158 1.00 64.31 ? 2068 HOH F O   1 
HETATM 20521 O  O   . HOH KB 5 .   ? 4.614   105.519 109.614 1.00 40.00 ? 2069 HOH F O   1 
HETATM 20522 O  O   . HOH KB 5 .   ? 1.487   96.289  101.850 1.00 43.86 ? 2070 HOH F O   1 
HETATM 20523 O  O   . HOH KB 5 .   ? 9.354   97.173  101.830 1.00 43.93 ? 2071 HOH F O   1 
HETATM 20524 O  O   . HOH KB 5 .   ? 12.304  97.474  105.987 1.00 64.08 ? 2072 HOH F O   1 
HETATM 20525 O  O   . HOH KB 5 .   ? 2.402   95.294  99.637  1.00 36.71 ? 2073 HOH F O   1 
HETATM 20526 O  O   . HOH KB 5 .   ? 7.593   98.770  92.969  1.00 48.56 ? 2074 HOH F O   1 
HETATM 20527 O  O   . HOH KB 5 .   ? 0.306   106.478 98.828  1.00 54.69 ? 2075 HOH F O   1 
HETATM 20528 O  O   . HOH KB 5 .   ? 5.385   105.191 94.230  1.00 61.75 ? 2076 HOH F O   1 
HETATM 20529 O  O   . HOH KB 5 .   ? 4.936   100.990 94.053  1.00 45.05 ? 2077 HOH F O   1 
HETATM 20530 O  O   . HOH KB 5 .   ? 5.853   110.618 101.267 1.00 37.06 ? 2078 HOH F O   1 
HETATM 20531 O  O   . HOH KB 5 .   ? -0.651  102.375 97.286  1.00 40.97 ? 2079 HOH F O   1 
HETATM 20532 O  O   . HOH KB 5 .   ? -1.013  104.621 98.744  1.00 41.43 ? 2080 HOH F O   1 
HETATM 20533 O  O   . HOH KB 5 .   ? -0.587  107.962 100.717 1.00 39.81 ? 2081 HOH F O   1 
HETATM 20534 O  O   . HOH KB 5 .   ? 2.551   111.471 98.289  1.00 59.18 ? 2082 HOH F O   1 
HETATM 20535 O  O   . HOH KB 5 .   ? 2.636   114.468 97.773  1.00 44.07 ? 2083 HOH F O   1 
HETATM 20536 O  O   . HOH KB 5 .   ? -9.072  115.184 101.268 1.00 68.15 ? 2084 HOH F O   1 
HETATM 20537 O  O   . HOH KB 5 .   ? -1.121  110.658 99.654  1.00 50.51 ? 2085 HOH F O   1 
HETATM 20538 O  O   . HOH KB 5 .   ? -5.966  112.167 98.876  1.00 46.08 ? 2086 HOH F O   1 
HETATM 20539 O  O   . HOH KB 5 .   ? 3.129   111.312 100.931 1.00 47.80 ? 2087 HOH F O   1 
HETATM 20540 O  O   . HOH KB 5 .   ? -13.317 113.150 105.611 1.00 42.14 ? 2088 HOH F O   1 
HETATM 20541 O  O   . HOH KB 5 .   ? -11.333 114.176 102.601 1.00 46.68 ? 2089 HOH F O   1 
HETATM 20542 O  O   . HOH KB 5 .   ? -8.105  120.856 106.862 1.00 45.87 ? 2090 HOH F O   1 
HETATM 20543 O  O   . HOH KB 5 .   ? -5.974  123.603 109.776 1.00 37.04 ? 2091 HOH F O   1 
HETATM 20544 O  O   . HOH KB 5 .   ? -5.267  122.956 112.919 1.00 33.07 ? 2092 HOH F O   1 
HETATM 20545 O  O   . HOH KB 5 .   ? 3.313   126.499 123.364 1.00 52.88 ? 2093 HOH F O   1 
HETATM 20546 O  O   . HOH KB 5 .   ? -3.572  124.984 125.036 1.00 53.22 ? 2094 HOH F O   1 
HETATM 20547 O  O   . HOH LB 5 .   ? 5.164   135.653 71.881  1.00 54.93 ? 2001 HOH G O   1 
HETATM 20548 O  O   . HOH LB 5 .   ? 20.348  135.688 61.410  1.00 45.81 ? 2002 HOH G O   1 
HETATM 20549 O  O   . HOH LB 5 .   ? 28.790  142.985 58.717  1.00 54.12 ? 2003 HOH G O   1 
HETATM 20550 O  O   . HOH LB 5 .   ? 28.029  139.390 60.813  1.00 44.89 ? 2004 HOH G O   1 
HETATM 20551 O  O   . HOH LB 5 .   ? 13.111  138.214 73.003  1.00 49.39 ? 2005 HOH G O   1 
HETATM 20552 O  O   . HOH LB 5 .   ? 31.170  147.481 60.258  1.00 37.73 ? 2006 HOH G O   1 
HETATM 20553 O  O   . HOH LB 5 .   ? 33.481  151.842 66.420  1.00 52.33 ? 2007 HOH G O   1 
HETATM 20554 O  O   . HOH LB 5 .   ? 29.724  149.829 60.451  1.00 43.62 ? 2008 HOH G O   1 
HETATM 20555 O  O   . HOH LB 5 .   ? 34.450  154.270 64.157  1.00 59.45 ? 2009 HOH G O   1 
HETATM 20556 O  O   . HOH LB 5 .   ? 16.659  148.553 56.780  1.00 62.17 ? 2010 HOH G O   1 
HETATM 20557 O  O   . HOH LB 5 .   ? 6.228   147.091 51.115  1.00 56.46 ? 2011 HOH G O   1 
HETATM 20558 O  O   . HOH LB 5 .   ? 14.517  133.702 54.503  1.00 39.28 ? 2012 HOH G O   1 
HETATM 20559 O  O   . HOH LB 5 .   ? 10.790  137.125 48.439  1.00 53.43 ? 2013 HOH G O   1 
HETATM 20560 O  O   . HOH LB 5 .   ? 12.392  133.410 47.379  1.00 48.22 ? 2014 HOH G O   1 
HETATM 20561 O  O   . HOH LB 5 .   ? 21.490  132.793 52.479  1.00 59.26 ? 2015 HOH G O   1 
HETATM 20562 O  O   . HOH LB 5 .   ? 18.766  135.696 57.853  1.00 51.29 ? 2016 HOH G O   1 
HETATM 20563 O  O   . HOH LB 5 .   ? 20.000  132.906 57.074  1.00 55.68 ? 2017 HOH G O   1 
HETATM 20564 O  O   . HOH LB 5 .   ? 17.259  137.700 56.605  1.00 57.90 ? 2018 HOH G O   1 
HETATM 20565 O  O   . HOH LB 5 .   ? 16.764  144.917 47.706  1.00 51.62 ? 2019 HOH G O   1 
HETATM 20566 O  O   . HOH LB 5 .   ? 12.434  139.319 47.805  1.00 53.37 ? 2020 HOH G O   1 
HETATM 20567 O  O   . HOH LB 5 .   ? 14.904  149.816 51.140  1.00 58.75 ? 2021 HOH G O   1 
HETATM 20568 O  O   . HOH LB 5 .   ? 16.640  150.438 53.348  1.00 45.99 ? 2022 HOH G O   1 
HETATM 20569 O  O   . HOH LB 5 .   ? 11.769  160.483 64.131  1.00 57.93 ? 2023 HOH G O   1 
HETATM 20570 O  O   . HOH LB 5 .   ? 8.182   161.281 55.783  1.00 53.79 ? 2024 HOH G O   1 
HETATM 20571 O  O   . HOH LB 5 .   ? 8.481   155.377 49.970  1.00 57.44 ? 2025 HOH G O   1 
HETATM 20572 O  O   . HOH LB 5 .   ? 17.253  154.684 67.914  1.00 55.57 ? 2026 HOH G O   1 
HETATM 20573 O  O   . HOH LB 5 .   ? 16.295  157.798 64.868  1.00 60.35 ? 2027 HOH G O   1 
HETATM 20574 O  O   . HOH LB 5 .   ? 28.467  157.289 69.481  1.00 50.60 ? 2028 HOH G O   1 
HETATM 20575 O  O   . HOH LB 5 .   ? 27.716  152.071 74.852  1.00 47.22 ? 2029 HOH G O   1 
HETATM 20576 O  O   . HOH LB 5 .   ? 30.803  149.772 74.585  1.00 52.04 ? 2030 HOH G O   1 
HETATM 20577 O  O   . HOH LB 5 .   ? 38.090  152.855 70.290  1.00 58.22 ? 2031 HOH G O   1 
HETATM 20578 O  O   . HOH LB 5 .   ? 33.207  161.613 74.292  1.00 44.49 ? 2032 HOH G O   1 
HETATM 20579 O  O   . HOH LB 5 .   ? 35.221  146.846 70.402  1.00 54.56 ? 2033 HOH G O   1 
HETATM 20580 O  O   . HOH LB 5 .   ? 26.232  151.875 72.758  1.00 55.99 ? 2034 HOH G O   1 
HETATM 20581 O  O   . HOH LB 5 .   ? 18.171  152.941 69.859  1.00 52.19 ? 2035 HOH G O   1 
HETATM 20582 O  O   . HOH LB 5 .   ? -0.248  153.753 63.948  1.00 59.64 ? 2036 HOH G O   1 
HETATM 20583 O  O   . HOH LB 5 .   ? 4.177   141.661 52.602  1.00 58.60 ? 2037 HOH G O   1 
HETATM 20584 O  O   . HOH LB 5 .   ? 29.603  151.806 58.238  1.00 51.33 ? 2038 HOH G O   1 
HETATM 20585 O  O   . HOH LB 5 .   ? 13.761  155.738 59.421  1.00 43.17 ? 2039 HOH G O   1 
HETATM 20586 O  O   . HOH LB 5 .   ? 23.604  145.991 50.558  1.00 46.51 ? 2040 HOH G O   1 
HETATM 20587 O  O   . HOH LB 5 .   ? 20.893  137.098 58.410  1.00 54.52 ? 2041 HOH G O   1 
HETATM 20588 O  O   . HOH LB 5 .   ? 16.502  135.949 63.436  1.00 32.79 ? 2042 HOH G O   1 
HETATM 20589 O  O   . HOH LB 5 .   ? 17.065  135.091 60.228  1.00 43.26 ? 2043 HOH G O   1 
HETATM 20590 O  O   . HOH MB 5 .   ? 50.326  97.403  103.122 1.00 56.22 ? 2001 HOH H O   1 
HETATM 20591 O  O   . HOH MB 5 .   ? 47.999  92.954  96.255  1.00 47.46 ? 2002 HOH H O   1 
HETATM 20592 O  O   . HOH MB 5 .   ? 53.498  87.321  110.961 1.00 61.04 ? 2003 HOH H O   1 
HETATM 20593 O  O   . HOH MB 5 .   ? 31.264  87.452  91.305  1.00 50.80 ? 2004 HOH H O   1 
HETATM 20594 O  O   . HOH MB 5 .   ? 51.658  89.038  109.644 1.00 47.04 ? 2005 HOH H O   1 
HETATM 20595 O  O   . HOH MB 5 .   ? 59.146  82.622  99.058  1.00 56.01 ? 2006 HOH H O   1 
HETATM 20596 O  O   . HOH MB 5 .   ? 48.722  89.529  109.959 1.00 51.80 ? 2007 HOH H O   1 
HETATM 20597 O  O   . HOH MB 5 .   ? 23.511  86.414  94.347  1.00 45.32 ? 2008 HOH H O   1 
HETATM 20598 O  O   . HOH MB 5 .   ? 32.738  93.892  102.709 1.00 51.05 ? 2009 HOH H O   1 
HETATM 20599 O  O   . HOH MB 5 .   ? 40.315  94.147  99.433  1.00 43.91 ? 2010 HOH H O   1 
HETATM 20600 O  O   . HOH MB 5 .   ? 16.860  76.413  101.398 1.00 55.90 ? 2011 HOH H O   1 
HETATM 20601 O  O   . HOH MB 5 .   ? 42.256  93.372  100.640 1.00 47.65 ? 2012 HOH H O   1 
HETATM 20602 O  O   . HOH MB 5 .   ? 46.458  91.615  107.570 1.00 51.44 ? 2013 HOH H O   1 
HETATM 20603 O  O   . HOH MB 5 .   ? 52.988  89.309  101.611 1.00 54.07 ? 2014 HOH H O   1 
HETATM 20604 O  O   . HOH MB 5 .   ? 53.484  94.451  104.856 1.00 51.20 ? 2015 HOH H O   1 
HETATM 20605 O  O   . HOH MB 5 .   ? 50.723  96.399  105.743 1.00 62.18 ? 2016 HOH H O   1 
HETATM 20606 O  O   . HOH MB 5 .   ? 51.115  87.941  107.090 1.00 36.06 ? 2017 HOH H O   1 
HETATM 20607 O  O   . HOH MB 5 .   ? 53.208  91.390  110.154 1.00 56.57 ? 2018 HOH H O   1 
HETATM 20608 O  O   . HOH MB 5 .   ? 57.471  89.420  104.036 1.00 47.25 ? 2019 HOH H O   1 
HETATM 20609 O  O   . HOH MB 5 .   ? 59.211  83.855  101.358 1.00 50.85 ? 2020 HOH H O   1 
HETATM 20610 O  O   . HOH MB 5 .   ? 55.603  84.361  107.536 1.00 47.63 ? 2021 HOH H O   1 
HETATM 20611 O  O   . HOH MB 5 .   ? 48.372  89.491  107.307 1.00 38.54 ? 2022 HOH H O   1 
HETATM 20612 O  O   . HOH MB 5 .   ? 36.921  76.156  113.050 1.00 53.06 ? 2023 HOH H O   1 
HETATM 20613 O  O   . HOH MB 5 .   ? 37.197  79.573  112.146 1.00 41.07 ? 2024 HOH H O   1 
HETATM 20614 O  O   . HOH MB 5 .   ? 25.257  78.970  114.933 1.00 56.28 ? 2025 HOH H O   1 
HETATM 20615 O  O   . HOH MB 5 .   ? 27.830  77.929  116.035 1.00 53.05 ? 2026 HOH H O   1 
HETATM 20616 O  O   . HOH MB 5 .   ? 24.079  81.075  115.589 1.00 53.98 ? 2027 HOH H O   1 
HETATM 20617 O  O   . HOH MB 5 .   ? 19.716  82.529  101.523 1.00 51.82 ? 2028 HOH H O   1 
HETATM 20618 O  O   . HOH MB 5 .   ? 21.156  80.681  103.057 1.00 45.91 ? 2029 HOH H O   1 
HETATM 20619 O  O   . HOH MB 5 .   ? 17.090  83.066  108.651 1.00 52.73 ? 2030 HOH H O   1 
HETATM 20620 O  O   . HOH MB 5 .   ? 23.635  76.699  112.275 1.00 60.24 ? 2031 HOH H O   1 
HETATM 20621 O  O   . HOH MB 5 .   ? 22.938  76.481  108.576 1.00 53.74 ? 2032 HOH H O   1 
HETATM 20622 O  O   . HOH MB 5 .   ? 48.601  79.680  91.279  1.00 58.58 ? 2033 HOH H O   1 
HETATM 20623 O  O   . HOH MB 5 .   ? 18.332  76.992  104.116 1.00 55.65 ? 2034 HOH H O   1 
HETATM 20624 O  O   . HOH MB 5 .   ? 25.084  67.403  107.847 1.00 52.92 ? 2035 HOH H O   1 
HETATM 20625 O  O   . HOH MB 5 .   ? 26.416  68.197  110.288 1.00 50.37 ? 2036 HOH H O   1 
HETATM 20626 O  O   . HOH MB 5 .   ? 31.667  73.941  113.829 1.00 48.12 ? 2037 HOH H O   1 
HETATM 20627 O  O   . HOH MB 5 .   ? 33.939  60.420  112.261 1.00 45.47 ? 2038 HOH H O   1 
HETATM 20628 O  O   . HOH MB 5 .   ? 40.151  68.744  90.230  1.00 55.64 ? 2039 HOH H O   1 
HETATM 20629 O  O   . HOH MB 5 .   ? 44.686  73.671  90.233  1.00 51.38 ? 2040 HOH H O   1 
HETATM 20630 O  O   . HOH MB 5 .   ? 35.847  82.086  85.442  1.00 39.05 ? 2041 HOH H O   1 
HETATM 20631 O  O   . HOH MB 5 .   ? 36.039  76.279  81.025  1.00 49.44 ? 2042 HOH H O   1 
HETATM 20632 O  O   . HOH MB 5 .   ? 38.148  74.956  84.590  1.00 53.37 ? 2043 HOH H O   1 
HETATM 20633 O  O   . HOH MB 5 .   ? 32.620  79.305  89.811  1.00 51.34 ? 2044 HOH H O   1 
HETATM 20634 O  O   . HOH MB 5 .   ? 32.425  84.308  89.476  1.00 45.60 ? 2045 HOH H O   1 
HETATM 20635 O  O   . HOH MB 5 .   ? 27.748  82.814  89.768  1.00 54.01 ? 2046 HOH H O   1 
HETATM 20636 O  O   . HOH MB 5 .   ? 28.332  80.328  80.767  1.00 59.07 ? 2047 HOH H O   1 
HETATM 20637 O  O   . HOH MB 5 .   ? 27.921  72.955  92.357  1.00 61.65 ? 2048 HOH H O   1 
HETATM 20638 O  O   . HOH MB 5 .   ? 31.542  70.889  90.958  1.00 50.16 ? 2049 HOH H O   1 
HETATM 20639 O  O   . HOH MB 5 .   ? 32.250  71.735  98.390  1.00 50.98 ? 2050 HOH H O   1 
HETATM 20640 O  O   . HOH MB 5 .   ? 43.268  71.225  94.362  1.00 47.03 ? 2051 HOH H O   1 
HETATM 20641 O  O   . HOH MB 5 .   ? 45.650  70.450  100.396 1.00 40.06 ? 2052 HOH H O   1 
HETATM 20642 O  O   . HOH MB 5 .   ? 48.994  68.994  93.621  1.00 64.98 ? 2053 HOH H O   1 
HETATM 20643 O  O   . HOH MB 5 .   ? 49.690  66.165  96.238  1.00 53.47 ? 2054 HOH H O   1 
HETATM 20644 O  O   . HOH MB 5 .   ? 39.964  80.077  111.858 1.00 46.11 ? 2055 HOH H O   1 
HETATM 20645 O  O   . HOH MB 5 .   ? 38.450  74.033  112.823 1.00 35.64 ? 2056 HOH H O   1 
HETATM 20646 O  O   . HOH MB 5 .   ? 43.488  79.060  113.458 1.00 54.90 ? 2057 HOH H O   1 
HETATM 20647 O  O   . HOH MB 5 .   ? 37.494  68.070  112.554 1.00 51.88 ? 2058 HOH H O   1 
HETATM 20648 O  O   . HOH MB 5 .   ? 44.843  68.709  114.321 1.00 56.45 ? 2059 HOH H O   1 
HETATM 20649 O  O   . HOH MB 5 .   ? 46.365  70.766  103.038 1.00 43.45 ? 2060 HOH H O   1 
HETATM 20650 O  O   . HOH MB 5 .   ? 39.182  65.111  100.072 1.00 50.78 ? 2061 HOH H O   1 
HETATM 20651 O  O   . HOH MB 5 .   ? 35.669  79.493  109.910 1.00 38.94 ? 2062 HOH H O   1 
HETATM 20652 O  O   . HOH MB 5 .   ? 30.815  84.796  110.087 1.00 35.87 ? 2063 HOH H O   1 
HETATM 20653 O  O   . HOH MB 5 .   ? 28.457  80.234  115.065 1.00 44.87 ? 2064 HOH H O   1 
HETATM 20654 O  O   . HOH MB 5 .   ? 28.742  86.890  111.515 1.00 38.83 ? 2065 HOH H O   1 
HETATM 20655 O  O   . HOH MB 5 .   ? 23.493  83.239  114.201 1.00 47.91 ? 2066 HOH H O   1 
HETATM 20656 O  O   . HOH MB 5 .   ? 22.573  92.388  110.953 1.00 51.12 ? 2067 HOH H O   1 
HETATM 20657 O  O   . HOH MB 5 .   ? 21.201  87.535  115.509 1.00 53.30 ? 2068 HOH H O   1 
HETATM 20658 O  O   . HOH MB 5 .   ? 20.376  89.633  104.652 1.00 46.01 ? 2069 HOH H O   1 
HETATM 20659 O  O   . HOH MB 5 .   ? 26.931  88.595  111.450 1.00 62.41 ? 2070 HOH H O   1 
HETATM 20660 O  O   . HOH MB 5 .   ? 33.938  91.536  109.139 1.00 51.72 ? 2071 HOH H O   1 
HETATM 20661 O  O   . HOH MB 5 .   ? 38.976  87.980  113.878 1.00 47.76 ? 2072 HOH H O   1 
HETATM 20662 O  O   . HOH MB 5 .   ? 37.493  83.772  113.213 1.00 37.85 ? 2073 HOH H O   1 
HETATM 20663 O  O   . HOH MB 5 .   ? 40.378  88.879  109.893 1.00 40.77 ? 2074 HOH H O   1 
HETATM 20664 O  O   . HOH MB 5 .   ? 40.134  82.843  112.453 1.00 35.74 ? 2075 HOH H O   1 
HETATM 20665 O  O   . HOH MB 5 .   ? 45.323  88.300  114.547 1.00 60.22 ? 2076 HOH H O   1 
HETATM 20666 O  O   . HOH MB 5 .   ? 48.101  88.453  112.195 1.00 50.63 ? 2077 HOH H O   1 
HETATM 20667 O  O   . HOH MB 5 .   ? 43.783  81.625  113.221 1.00 49.71 ? 2078 HOH H O   1 
HETATM 20668 O  O   . HOH MB 5 .   ? 41.908  79.648  110.254 1.00 37.23 ? 2079 HOH H O   1 
HETATM 20669 O  O   . HOH MB 5 .   ? 52.069  81.987  109.622 1.00 54.24 ? 2080 HOH H O   1 
HETATM 20670 O  O   . HOH MB 5 .   ? 52.009  77.676  105.982 1.00 52.19 ? 2081 HOH H O   1 
HETATM 20671 O  O   . HOH MB 5 .   ? 46.809  82.195  111.218 1.00 52.43 ? 2082 HOH H O   1 
HETATM 20672 O  O   . HOH MB 5 .   ? 46.211  78.675  110.159 1.00 38.73 ? 2083 HOH H O   1 
HETATM 20673 O  O   . HOH MB 5 .   ? 50.905  78.927  103.364 1.00 41.14 ? 2084 HOH H O   1 
HETATM 20674 O  O   . HOH MB 5 .   ? 50.247  81.755  104.462 1.00 35.40 ? 2085 HOH H O   1 
HETATM 20675 O  O   . HOH MB 5 .   ? 53.138  81.336  101.036 1.00 49.95 ? 2086 HOH H O   1 
HETATM 20676 O  O   . HOH MB 5 .   ? 53.153  84.976  100.705 1.00 42.94 ? 2087 HOH H O   1 
HETATM 20677 O  O   . HOH MB 5 .   ? 52.033  79.039  99.382  1.00 47.52 ? 2088 HOH H O   1 
HETATM 20678 O  O   . HOH MB 5 .   ? 46.802  75.187  89.503  1.00 52.18 ? 2089 HOH H O   1 
HETATM 20679 O  O   . HOH MB 5 .   ? 48.292  77.828  93.805  1.00 41.56 ? 2090 HOH H O   1 
HETATM 20680 O  O   . HOH MB 5 .   ? 33.579  81.608  89.997  1.00 49.33 ? 2091 HOH H O   1 
HETATM 20681 O  O   . HOH MB 5 .   ? 19.187  74.066  104.431 1.00 60.41 ? 2092 HOH H O   1 
HETATM 20682 O  O   . HOH MB 5 .   ? 20.752  78.097  103.339 1.00 47.21 ? 2093 HOH H O   1 
HETATM 20683 O  O   . HOH MB 5 .   ? 25.717  70.214  107.657 1.00 44.36 ? 2094 HOH H O   1 
HETATM 20684 O  O   . HOH MB 5 .   ? 36.409  73.606  106.486 1.00 33.57 ? 2095 HOH H O   1 
HETATM 20685 O  O   . HOH MB 5 .   ? 30.070  72.322  112.320 1.00 44.74 ? 2096 HOH H O   1 
HETATM 20686 O  O   . HOH MB 5 .   ? 31.500  69.432  113.211 1.00 56.22 ? 2097 HOH H O   1 
HETATM 20687 O  O   . HOH MB 5 .   ? 27.333  66.028  109.231 1.00 40.26 ? 2098 HOH H O   1 
HETATM 20688 O  O   . HOH MB 5 .   ? 38.287  66.093  111.037 1.00 53.89 ? 2099 HOH H O   1 
HETATM 20689 O  O   . HOH MB 5 .   ? 33.994  61.464  110.153 1.00 40.91 ? 2100 HOH H O   1 
HETATM 20690 O  O   . HOH MB 5 .   ? 32.014  62.285  115.077 1.00 44.38 ? 2101 HOH H O   1 
HETATM 20691 O  O   . HOH MB 5 .   ? 30.248  64.825  114.886 1.00 44.80 ? 2102 HOH H O   1 
HETATM 20692 O  O   . HOH MB 5 .   ? 26.753  60.850  101.943 1.00 50.29 ? 2103 HOH H O   1 
HETATM 20693 O  O   . HOH MB 5 .   ? 25.000  59.985  104.986 1.00 42.99 ? 2104 HOH H O   1 
HETATM 20694 O  O   . HOH MB 5 .   ? 36.171  57.130  105.709 1.00 56.65 ? 2105 HOH H O   1 
HETATM 20695 O  O   . HOH MB 5 .   ? 29.767  57.342  103.003 1.00 46.18 ? 2106 HOH H O   1 
HETATM 20696 O  O   . HOH MB 5 .   ? 28.903  59.915  102.077 1.00 36.99 ? 2107 HOH H O   1 
HETATM 20697 O  O   . HOH MB 5 .   ? 36.104  68.838  98.102  1.00 43.96 ? 2108 HOH H O   1 
HETATM 20698 O  O   . HOH MB 5 .   ? 33.754  70.322  96.802  1.00 47.09 ? 2109 HOH H O   1 
HETATM 20699 O  O   . HOH MB 5 .   ? 33.030  68.593  95.001  1.00 55.73 ? 2110 HOH H O   1 
HETATM 20700 O  O   . HOH MB 5 .   ? 33.408  69.499  92.516  1.00 49.71 ? 2111 HOH H O   1 
HETATM 20701 O  O   . HOH MB 5 .   ? 25.289  73.942  94.154  1.00 40.43 ? 2112 HOH H O   1 
HETATM 20702 O  O   . HOH MB 5 .   ? 29.108  71.483  96.348  1.00 50.55 ? 2113 HOH H O   1 
HETATM 20703 O  O   . HOH MB 5 .   ? 29.720  84.786  90.677  1.00 51.03 ? 2114 HOH H O   1 
HETATM 20704 O  O   . HOH MB 5 .   ? 35.444  88.513  92.499  1.00 29.22 ? 2115 HOH H O   1 
HETATM 20705 O  O   . HOH MB 5 .   ? 34.022  86.424  89.964  1.00 39.34 ? 2116 HOH H O   1 
HETATM 20706 O  O   . HOH MB 5 .   ? 41.668  97.810  97.118  1.00 51.90 ? 2117 HOH H O   1 
HETATM 20707 O  O   . HOH MB 5 .   ? 41.382  97.096  94.338  1.00 44.28 ? 2118 HOH H O   1 
HETATM 20708 O  O   . HOH NB 5 .   ? 18.028  84.214  36.804  1.00 55.00 ? 2001 HOH I O   1 
HETATM 20709 O  O   . HOH NB 5 .   ? 10.571  85.405  33.491  1.00 40.32 ? 2002 HOH I O   1 
HETATM 20710 O  O   . HOH NB 5 .   ? 15.393  78.461  50.198  1.00 49.30 ? 2003 HOH I O   1 
HETATM 20711 O  O   . HOH NB 5 .   ? 18.533  92.750  37.071  1.00 44.73 ? 2004 HOH I O   1 
HETATM 20712 O  O   . HOH NB 5 .   ? 18.116  93.537  31.641  1.00 51.97 ? 2005 HOH I O   1 
HETATM 20713 O  O   . HOH NB 5 .   ? 21.421  86.285  35.980  1.00 52.83 ? 2006 HOH I O   1 
HETATM 20714 O  O   . HOH NB 5 .   ? 19.069  90.114  39.552  1.00 39.95 ? 2007 HOH I O   1 
HETATM 20715 O  O   . HOH NB 5 .   ? 20.127  83.123  42.593  1.00 52.89 ? 2008 HOH I O   1 
HETATM 20716 O  O   . HOH NB 5 .   ? 17.967  86.524  38.044  1.00 37.91 ? 2009 HOH I O   1 
HETATM 20717 O  O   . HOH NB 5 .   ? 13.548  80.415  44.127  1.00 49.60 ? 2010 HOH I O   1 
HETATM 20718 O  O   . HOH NB 5 .   ? 15.391  79.877  48.217  1.00 55.87 ? 2011 HOH I O   1 
HETATM 20719 O  O   . HOH NB 5 .   ? 18.480  80.615  48.428  1.00 44.02 ? 2012 HOH I O   1 
HETATM 20720 O  O   . HOH NB 5 .   ? 7.859   79.953  44.845  1.00 39.89 ? 2013 HOH I O   1 
HETATM 20721 O  O   . HOH NB 5 .   ? 13.681  99.812  55.339  1.00 58.25 ? 2014 HOH I O   1 
HETATM 20722 O  O   . HOH NB 5 .   ? 4.000   77.690  40.579  1.00 38.23 ? 2015 HOH I O   1 
HETATM 20723 O  O   . HOH NB 5 .   ? 0.358   79.564  40.350  1.00 38.06 ? 2016 HOH I O   1 
HETATM 20724 O  O   . HOH NB 5 .   ? 5.854   78.337  43.918  1.00 40.14 ? 2017 HOH I O   1 
HETATM 20725 O  O   . HOH NB 5 .   ? 5.983   104.543 30.479  1.00 52.18 ? 2018 HOH I O   1 
HETATM 20726 O  O   . HOH NB 5 .   ? -3.637  102.015 33.105  1.00 54.60 ? 2019 HOH I O   1 
HETATM 20727 O  O   . HOH NB 5 .   ? 9.998   98.617  22.191  1.00 63.95 ? 2020 HOH I O   1 
HETATM 20728 O  O   . HOH NB 5 .   ? -12.262 84.480  40.574  1.00 49.20 ? 2021 HOH I O   1 
HETATM 20729 O  O   . HOH NB 5 .   ? 14.501  98.043  22.899  1.00 57.81 ? 2022 HOH I O   1 
HETATM 20730 O  O   . HOH NB 5 .   ? 11.832  104.313 31.178  1.00 47.79 ? 2023 HOH I O   1 
HETATM 20731 O  O   . HOH NB 5 .   ? 13.192  102.622 34.876  1.00 51.72 ? 2024 HOH I O   1 
HETATM 20732 O  O   . HOH NB 5 .   ? 15.189  101.234 27.747  1.00 46.82 ? 2025 HOH I O   1 
HETATM 20733 O  O   . HOH NB 5 .   ? -11.188 85.857  46.238  1.00 37.34 ? 2026 HOH I O   1 
HETATM 20734 O  O   . HOH NB 5 .   ? -16.298 88.901  46.767  1.00 60.02 ? 2027 HOH I O   1 
HETATM 20735 O  O   . HOH NB 5 .   ? -12.275 84.752  48.604  1.00 49.87 ? 2028 HOH I O   1 
HETATM 20736 O  O   . HOH NB 5 .   ? -18.333 90.201  42.638  1.00 42.58 ? 2029 HOH I O   1 
HETATM 20737 O  O   . HOH NB 5 .   ? -11.973 92.741  40.232  1.00 43.91 ? 2030 HOH I O   1 
HETATM 20738 O  O   . HOH NB 5 .   ? -9.784  91.984  43.935  1.00 39.60 ? 2031 HOH I O   1 
HETATM 20739 O  O   . HOH NB 5 .   ? -8.353  84.075  47.011  1.00 43.91 ? 2032 HOH I O   1 
HETATM 20740 O  O   . HOH NB 5 .   ? 7.237   99.510  55.903  1.00 51.09 ? 2033 HOH I O   1 
HETATM 20741 O  O   . HOH NB 5 .   ? 10.495  80.629  44.224  1.00 42.48 ? 2034 HOH I O   1 
HETATM 20742 O  O   . HOH NB 5 .   ? 13.462  81.069  46.769  1.00 51.45 ? 2035 HOH I O   1 
HETATM 20743 O  O   . HOH NB 5 .   ? 15.224  79.576  52.437  1.00 56.57 ? 2036 HOH I O   1 
HETATM 20744 O  O   . HOH NB 5 .   ? 20.898  91.056  45.254  1.00 43.25 ? 2037 HOH I O   1 
HETATM 20745 O  O   . HOH NB 5 .   ? 19.531  83.744  48.352  1.00 37.75 ? 2038 HOH I O   1 
HETATM 20746 O  O   . HOH NB 5 .   ? 6.252   79.543  54.570  1.00 54.53 ? 2039 HOH I O   1 
HETATM 20747 O  O   . HOH NB 5 .   ? 21.888  87.915  50.441  1.00 58.41 ? 2040 HOH I O   1 
HETATM 20748 O  O   . HOH NB 5 .   ? 19.039  92.647  46.668  1.00 34.07 ? 2041 HOH I O   1 
HETATM 20749 O  O   . HOH NB 5 .   ? 22.308  90.621  52.853  1.00 45.37 ? 2042 HOH I O   1 
HETATM 20750 O  O   . HOH NB 5 .   ? 16.905  89.214  59.124  1.00 55.19 ? 2043 HOH I O   1 
HETATM 20751 O  O   . HOH NB 5 .   ? 16.387  97.116  52.047  1.00 47.57 ? 2044 HOH I O   1 
HETATM 20752 O  O   . HOH NB 5 .   ? 15.183  96.903  55.142  1.00 45.91 ? 2045 HOH I O   1 
HETATM 20753 O  O   . HOH NB 5 .   ? 21.710  95.890  45.799  1.00 56.76 ? 2046 HOH I O   1 
HETATM 20754 O  O   . HOH NB 5 .   ? 12.009  105.838 53.723  1.00 59.20 ? 2047 HOH I O   1 
HETATM 20755 O  O   . HOH NB 5 .   ? 9.811   105.197 55.833  1.00 48.16 ? 2048 HOH I O   1 
HETATM 20756 O  O   . HOH NB 5 .   ? 4.970   112.880 53.647  1.00 40.67 ? 2049 HOH I O   1 
HETATM 20757 O  O   . HOH NB 5 .   ? 3.912   110.371 56.673  1.00 50.29 ? 2050 HOH I O   1 
HETATM 20758 O  O   . HOH NB 5 .   ? 2.615   104.978 31.124  1.00 47.33 ? 2051 HOH I O   1 
HETATM 20759 O  O   . HOH NB 5 .   ? -2.080  99.958  30.509  1.00 49.36 ? 2052 HOH I O   1 
HETATM 20760 O  O   . HOH NB 5 .   ? 14.481  112.232 44.452  1.00 48.79 ? 2053 HOH I O   1 
HETATM 20761 O  O   . HOH NB 5 .   ? 7.356   90.963  27.150  1.00 28.65 ? 2054 HOH I O   1 
HETATM 20762 O  O   . HOH NB 5 .   ? 9.769   93.827  31.866  1.00 40.63 ? 2055 HOH I O   1 
HETATM 20763 O  O   . HOH NB 5 .   ? 9.031   99.766  25.672  1.00 57.51 ? 2056 HOH I O   1 
HETATM 20764 O  O   . HOH NB 5 .   ? 7.753   97.072  22.734  1.00 43.22 ? 2057 HOH I O   1 
HETATM 20765 O  O   . HOH NB 5 .   ? 5.544   98.642  25.974  1.00 38.74 ? 2058 HOH I O   1 
HETATM 20766 O  O   . HOH NB 5 .   ? 9.794   88.979  31.626  1.00 42.28 ? 2059 HOH I O   1 
HETATM 20767 O  O   . HOH NB 5 .   ? 11.884  87.420  29.076  1.00 41.06 ? 2060 HOH I O   1 
HETATM 20768 O  O   . HOH NB 5 .   ? 14.357  91.075  32.622  1.00 48.23 ? 2061 HOH I O   1 
HETATM 20769 O  O   . HOH NB 5 .   ? 12.013  98.104  23.919  1.00 48.34 ? 2062 HOH I O   1 
HETATM 20770 O  O   . HOH NB 5 .   ? 16.148  93.016  33.598  1.00 56.10 ? 2063 HOH I O   1 
HETATM 20771 O  O   . HOH NB 5 .   ? 15.999  97.040  32.266  1.00 55.39 ? 2064 HOH I O   1 
HETATM 20772 O  O   . HOH NB 5 .   ? 11.169  102.454 33.182  1.00 44.25 ? 2065 HOH I O   1 
HETATM 20773 O  O   . HOH NB 5 .   ? 12.268  100.990 27.973  1.00 47.99 ? 2066 HOH I O   1 
HETATM 20774 O  O   . HOH NB 5 .   ? 7.371   100.195 27.740  1.00 36.06 ? 2067 HOH I O   1 
HETATM 20775 O  O   . HOH NB 5 .   ? 8.057   102.090 29.461  1.00 56.08 ? 2068 HOH I O   1 
HETATM 20776 O  O   . HOH NB 5 .   ? 9.244   101.710 40.533  1.00 35.86 ? 2069 HOH I O   1 
HETATM 20777 O  O   . HOH NB 5 .   ? -1.281  102.418 34.711  1.00 41.04 ? 2070 HOH I O   1 
HETATM 20778 O  O   . HOH NB 5 .   ? -4.505  103.161 40.344  1.00 35.88 ? 2071 HOH I O   1 
HETATM 20779 O  O   . HOH NB 5 .   ? -7.952  104.001 33.364  1.00 56.01 ? 2072 HOH I O   1 
HETATM 20780 O  O   . HOH NB 5 .   ? 3.101   116.327 46.935  1.00 56.16 ? 2073 HOH I O   1 
HETATM 20781 O  O   . HOH NB 5 .   ? -0.199  107.704 49.254  1.00 46.37 ? 2074 HOH I O   1 
HETATM 20782 O  O   . HOH NB 5 .   ? 0.437   99.851  53.593  1.00 41.88 ? 2075 HOH I O   1 
HETATM 20783 O  O   . HOH NB 5 .   ? -0.772  93.501  52.550  1.00 48.72 ? 2076 HOH I O   1 
HETATM 20784 O  O   . HOH NB 5 .   ? 1.618   105.061 53.463  1.00 45.11 ? 2077 HOH I O   1 
HETATM 20785 O  O   . HOH NB 5 .   ? -5.904  104.932 54.050  1.00 53.35 ? 2078 HOH I O   1 
HETATM 20786 O  O   . HOH NB 5 .   ? -4.346  107.228 51.717  1.00 41.07 ? 2079 HOH I O   1 
HETATM 20787 O  O   . HOH NB 5 .   ? -4.465  111.690 43.536  1.00 55.19 ? 2080 HOH I O   1 
HETATM 20788 O  O   . HOH NB 5 .   ? -5.673  103.040 42.758  1.00 39.92 ? 2081 HOH I O   1 
HETATM 20789 O  O   . HOH NB 5 .   ? 1.982   108.567 40.844  1.00 47.78 ? 2082 HOH I O   1 
HETATM 20790 O  O   . HOH NB 5 .   ? 3.566   94.098  51.328  1.00 35.14 ? 2083 HOH I O   1 
HETATM 20791 O  O   . HOH NB 5 .   ? 6.408   97.713  54.410  1.00 47.58 ? 2084 HOH I O   1 
HETATM 20792 O  O   . HOH NB 5 .   ? 8.261   88.836  52.326  1.00 38.65 ? 2085 HOH I O   1 
HETATM 20793 O  O   . HOH NB 5 .   ? 9.767   93.029  57.662  1.00 51.50 ? 2086 HOH I O   1 
HETATM 20794 O  O   . HOH NB 5 .   ? 10.242  86.573  54.172  1.00 40.57 ? 2087 HOH I O   1 
HETATM 20795 O  O   . HOH NB 5 .   ? 15.155  90.059  57.367  1.00 49.82 ? 2088 HOH I O   1 
HETATM 20796 O  O   . HOH NB 5 .   ? 16.931  85.957  59.022  1.00 51.46 ? 2089 HOH I O   1 
HETATM 20797 O  O   . HOH NB 5 .   ? 16.797  80.803  54.451  1.00 60.32 ? 2090 HOH I O   1 
HETATM 20798 O  O   . HOH NB 5 .   ? 12.501  83.613  54.336  1.00 64.33 ? 2091 HOH I O   1 
HETATM 20799 O  O   . HOH NB 5 .   ? 6.849   82.343  52.721  1.00 65.40 ? 2092 HOH I O   1 
HETATM 20800 O  O   . HOH NB 5 .   ? 5.322   81.896  51.043  1.00 49.77 ? 2093 HOH I O   1 
HETATM 20801 O  O   . HOH NB 5 .   ? -0.353  85.425  54.669  1.00 45.00 ? 2094 HOH I O   1 
HETATM 20802 O  O   . HOH NB 5 .   ? 1.041   81.478  51.734  1.00 54.17 ? 2095 HOH I O   1 
HETATM 20803 O  O   . HOH NB 5 .   ? 1.403   89.559  54.314  1.00 39.02 ? 2096 HOH I O   1 
HETATM 20804 O  O   . HOH NB 5 .   ? -1.250  90.747  53.223  1.00 38.09 ? 2097 HOH I O   1 
HETATM 20805 O  O   . HOH NB 5 .   ? -5.118  91.659  53.428  1.00 58.16 ? 2098 HOH I O   1 
HETATM 20806 O  O   . HOH NB 5 .   ? -2.465  94.022  50.605  1.00 43.68 ? 2099 HOH I O   1 
HETATM 20807 O  O   . HOH NB 5 .   ? -6.219  95.216  49.968  1.00 47.16 ? 2100 HOH I O   1 
HETATM 20808 O  O   . HOH NB 5 .   ? -7.428  91.469  51.000  1.00 52.25 ? 2101 HOH I O   1 
HETATM 20809 O  O   . HOH NB 5 .   ? -12.003 88.526  39.717  1.00 43.77 ? 2102 HOH I O   1 
HETATM 20810 O  O   . HOH NB 5 .   ? -14.255 91.690  37.656  1.00 54.05 ? 2103 HOH I O   1 
HETATM 20811 O  O   . HOH NB 5 .   ? -10.617 94.816  38.595  1.00 49.23 ? 2104 HOH I O   1 
HETATM 20812 O  O   . HOH NB 5 .   ? -6.210  95.728  33.228  1.00 41.06 ? 2105 HOH I O   1 
HETATM 20813 O  O   . HOH NB 5 .   ? -4.762  98.331  29.615  1.00 52.55 ? 2106 HOH I O   1 
HETATM 20814 O  O   . HOH NB 5 .   ? 8.641   91.730  32.255  1.00 46.45 ? 2107 HOH I O   1 
HETATM 20815 O  O   . HOH NB 5 .   ? 19.454  95.448  47.086  1.00 37.96 ? 2108 HOH I O   1 
HETATM 20816 O  O   . HOH NB 5 .   ? 13.942  103.373 50.379  1.00 38.90 ? 2109 HOH I O   1 
HETATM 20817 O  O   . HOH NB 5 .   ? 16.344  99.703  51.411  1.00 55.16 ? 2110 HOH I O   1 
HETATM 20818 O  O   . HOH NB 5 .   ? 8.976   101.242 54.315  1.00 44.85 ? 2111 HOH I O   1 
HETATM 20819 O  O   . HOH NB 5 .   ? 3.563   99.911  47.634  1.00 31.24 ? 2112 HOH I O   1 
HETATM 20820 O  O   . HOH NB 5 .   ? 7.630   104.160 55.035  1.00 43.81 ? 2113 HOH I O   1 
HETATM 20821 O  O   . HOH NB 5 .   ? 12.279  107.474 51.699  1.00 42.10 ? 2114 HOH I O   1 
HETATM 20822 O  O   . HOH NB 5 .   ? 5.771   111.906 51.469  1.00 37.15 ? 2115 HOH I O   1 
HETATM 20823 O  O   . HOH NB 5 .   ? 6.541   111.289 56.783  1.00 53.74 ? 2116 HOH I O   1 
HETATM 20824 O  O   . HOH NB 5 .   ? 8.679   108.760 56.868  1.00 45.67 ? 2117 HOH I O   1 
HETATM 20825 O  O   . HOH NB 5 .   ? 10.935  116.156 45.016  1.00 36.84 ? 2118 HOH I O   1 
HETATM 20826 O  O   . HOH NB 5 .   ? 11.798  113.455 44.196  1.00 39.23 ? 2119 HOH I O   1 
HETATM 20827 O  O   . HOH NB 5 .   ? 10.738  112.186 40.638  1.00 62.37 ? 2120 HOH I O   1 
HETATM 20828 O  O   . HOH NB 5 .   ? 10.440  108.152 38.825  1.00 52.38 ? 2121 HOH I O   1 
HETATM 20829 O  O   . HOH NB 5 .   ? 14.346  110.814 41.946  1.00 50.72 ? 2122 HOH I O   1 
HETATM 20830 O  O   . HOH NB 5 .   ? 5.385   104.572 39.343  1.00 35.11 ? 2123 HOH I O   1 
HETATM 20831 O  O   . HOH NB 5 .   ? 13.024  105.063 43.143  1.00 47.22 ? 2124 HOH I O   1 
HETATM 20832 O  O   . HOH NB 5 .   ? 9.715   101.786 43.030  1.00 57.42 ? 2125 HOH I O   1 
HETATM 20833 O  O   . HOH NB 5 .   ? 11.887  102.500 41.473  1.00 40.03 ? 2126 HOH I O   1 
HETATM 20834 O  O   . HOH NB 5 .   ? 20.950  97.411  42.968  1.00 58.08 ? 2127 HOH I O   1 
HETATM 20835 O  O   . HOH NB 5 .   ? 19.481  96.746  38.205  1.00 58.32 ? 2128 HOH I O   1 
HETATM 20836 O  O   . HOH NB 5 .   ? 16.218  99.391  37.237  1.00 33.77 ? 2129 HOH I O   1 
HETATM 20837 O  O   . HOH NB 5 .   ? 12.312  101.989 38.562  1.00 49.27 ? 2130 HOH I O   1 
HETATM 20838 O  O   . HOH NB 5 .   ? 9.181   104.642 37.142  1.00 43.91 ? 2131 HOH I O   1 
HETATM 20839 O  O   . HOH NB 5 .   ? 9.019   103.651 34.291  1.00 36.95 ? 2132 HOH I O   1 
HETATM 20840 O  O   . HOH NB 5 .   ? 7.744   103.113 38.487  1.00 41.26 ? 2133 HOH I O   1 
HETATM 20841 O  O   . HOH NB 5 .   ? 11.935  88.304  33.256  1.00 44.71 ? 2134 HOH I O   1 
HETATM 20842 O  O   . HOH NB 5 .   ? 8.070   86.856  31.764  1.00 31.98 ? 2135 HOH I O   1 
HETATM 20843 O  O   . HOH NB 5 .   ? 6.319   84.756  34.150  1.00 23.96 ? 2136 HOH I O   1 
HETATM 20844 O  O   . HOH NB 5 .   ? -6.797  80.276  35.975  1.00 39.83 ? 2137 HOH I O   1 
HETATM 20845 O  O   . HOH NB 5 .   ? -1.064  75.344  37.597  1.00 49.12 ? 2138 HOH I O   1 
HETATM 20846 O  O   . HOH NB 5 .   ? -6.126  74.818  39.238  1.00 56.67 ? 2139 HOH I O   1 
HETATM 20847 O  O   . HOH NB 5 .   ? -3.764  70.679  29.956  1.00 62.15 ? 2140 HOH I O   1 
HETATM 20848 O  O   . HOH NB 5 .   ? -7.400  76.009  34.222  1.00 50.74 ? 2141 HOH I O   1 
HETATM 20849 O  O   . HOH OB 5 .   ? 51.246  94.385  28.359  1.00 42.88 ? 2001 HOH J O   1 
HETATM 20850 O  O   . HOH OB 5 .   ? 34.675  90.534  34.801  1.00 38.96 ? 2002 HOH J O   1 
HETATM 20851 O  O   . HOH OB 5 .   ? 24.656  98.262  50.601  1.00 55.04 ? 2003 HOH J O   1 
HETATM 20852 O  O   . HOH OB 5 .   ? 23.016  96.120  50.614  1.00 52.68 ? 2004 HOH J O   1 
HETATM 20853 O  O   . HOH OB 5 .   ? 39.009  101.904 30.432  1.00 49.90 ? 2005 HOH J O   1 
HETATM 20854 O  O   . HOH OB 5 .   ? 21.410  92.281  42.901  1.00 44.95 ? 2006 HOH J O   1 
HETATM 20855 O  O   . HOH OB 5 .   ? 27.823  94.015  43.107  1.00 48.58 ? 2007 HOH J O   1 
HETATM 20856 O  O   . HOH OB 5 .   ? 49.913  99.197  61.658  1.00 56.43 ? 2008 HOH J O   1 
HETATM 20857 O  O   . HOH OB 5 .   ? 57.693  89.885  48.877  1.00 59.97 ? 2009 HOH J O   1 
HETATM 20858 O  O   . HOH OB 5 .   ? 28.084  94.351  39.063  1.00 41.61 ? 2010 HOH J O   1 
HETATM 20859 O  O   . HOH OB 5 .   ? 26.382  96.288  46.962  1.00 44.18 ? 2011 HOH J O   1 
HETATM 20860 O  O   . HOH OB 5 .   ? 24.583  99.743  48.267  1.00 47.57 ? 2012 HOH J O   1 
HETATM 20861 O  O   . HOH OB 5 .   ? 32.789  97.623  34.421  1.00 49.68 ? 2013 HOH J O   1 
HETATM 20862 O  O   . HOH OB 5 .   ? 26.937  96.284  49.934  1.00 60.55 ? 2014 HOH J O   1 
HETATM 20863 O  O   . HOH OB 5 .   ? 51.139  108.287 38.955  1.00 62.67 ? 2015 HOH J O   1 
HETATM 20864 O  O   . HOH OB 5 .   ? 48.807  106.939 36.835  1.00 64.39 ? 2016 HOH J O   1 
HETATM 20865 O  O   . HOH OB 5 .   ? 38.546  103.161 35.097  1.00 39.24 ? 2017 HOH J O   1 
HETATM 20866 O  O   . HOH OB 5 .   ? 36.060  106.684 55.418  1.00 57.88 ? 2018 HOH J O   1 
HETATM 20867 O  O   . HOH OB 5 .   ? 39.983  103.257 33.006  1.00 41.92 ? 2019 HOH J O   1 
HETATM 20868 O  O   . HOH OB 5 .   ? 44.937  98.974  31.448  1.00 38.50 ? 2020 HOH J O   1 
HETATM 20869 O  O   . HOH OB 5 .   ? 43.613  102.906 30.121  1.00 62.80 ? 2021 HOH J O   1 
HETATM 20870 O  O   . HOH OB 5 .   ? 41.081  100.508 30.613  1.00 40.86 ? 2022 HOH J O   1 
HETATM 20871 O  O   . HOH OB 5 .   ? 47.521  100.092 32.169  1.00 52.89 ? 2023 HOH J O   1 
HETATM 20872 O  O   . HOH OB 5 .   ? 50.437  80.510  44.664  1.00 50.99 ? 2024 HOH J O   1 
HETATM 20873 O  O   . HOH OB 5 .   ? 56.577  93.255  34.576  1.00 55.96 ? 2025 HOH J O   1 
HETATM 20874 O  O   . HOH OB 5 .   ? 57.522  95.660  33.333  1.00 52.22 ? 2026 HOH J O   1 
HETATM 20875 O  O   . HOH OB 5 .   ? 58.725  91.085  38.522  1.00 42.46 ? 2027 HOH J O   1 
HETATM 20876 O  O   . HOH OB 5 .   ? 57.568  99.762  37.279  1.00 47.49 ? 2028 HOH J O   1 
HETATM 20877 O  O   . HOH OB 5 .   ? 50.085  95.743  61.852  1.00 53.36 ? 2029 HOH J O   1 
HETATM 20878 O  O   . HOH OB 5 .   ? 55.697  90.089  50.629  1.00 55.78 ? 2030 HOH J O   1 
HETATM 20879 O  O   . HOH OB 5 .   ? 34.587  102.443 35.727  1.00 53.96 ? 2031 HOH J O   1 
HETATM 20880 O  O   . HOH OB 5 .   ? 27.010  98.726  46.990  1.00 43.34 ? 2032 HOH J O   1 
HETATM 20881 O  O   . HOH OB 5 .   ? 24.944  101.232 44.928  1.00 50.72 ? 2033 HOH J O   1 
HETATM 20882 O  O   . HOH OB 5 .   ? 43.243  109.769 40.413  1.00 54.45 ? 2034 HOH J O   1 
HETATM 20883 O  O   . HOH OB 5 .   ? 26.231  104.475 46.617  1.00 58.51 ? 2035 HOH J O   1 
HETATM 20884 O  O   . HOH OB 5 .   ? 50.473  106.524 40.697  1.00 58.86 ? 2036 HOH J O   1 
HETATM 20885 O  O   . HOH OB 5 .   ? 29.215  98.731  48.500  1.00 36.76 ? 2037 HOH J O   1 
HETATM 20886 O  O   . HOH OB 5 .   ? 49.617  101.728 48.954  1.00 51.76 ? 2038 HOH J O   1 
HETATM 20887 O  O   . HOH OB 5 .   ? 51.193  101.129 50.560  1.00 60.98 ? 2039 HOH J O   1 
HETATM 20888 O  O   . HOH OB 5 .   ? 26.796  105.119 51.283  1.00 56.55 ? 2040 HOH J O   1 
HETATM 20889 O  O   . HOH OB 5 .   ? 52.610  89.287  29.942  1.00 57.60 ? 2041 HOH J O   1 
HETATM 20890 O  O   . HOH OB 5 .   ? 32.814  100.370 54.447  1.00 53.66 ? 2042 HOH J O   1 
HETATM 20891 O  O   . HOH OB 5 .   ? 34.995  103.644 55.967  1.00 44.55 ? 2043 HOH J O   1 
HETATM 20892 O  O   . HOH OB 5 .   ? 51.732  82.694  36.849  1.00 53.19 ? 2044 HOH J O   1 
HETATM 20893 O  O   . HOH OB 5 .   ? 36.804  96.182  60.977  1.00 41.09 ? 2045 HOH J O   1 
HETATM 20894 O  O   . HOH OB 5 .   ? 39.318  100.025 59.046  1.00 60.11 ? 2046 HOH J O   1 
HETATM 20895 O  O   . HOH OB 5 .   ? 47.082  80.146  48.689  1.00 61.32 ? 2047 HOH J O   1 
HETATM 20896 O  O   . HOH OB 5 .   ? 48.314  79.708  42.601  1.00 46.84 ? 2048 HOH J O   1 
HETATM 20897 O  O   . HOH OB 5 .   ? 47.737  77.007  46.140  1.00 53.87 ? 2049 HOH J O   1 
HETATM 20898 O  O   . HOH OB 5 .   ? 44.278  77.883  47.912  1.00 50.62 ? 2050 HOH J O   1 
HETATM 20899 O  O   . HOH OB 5 .   ? 36.257  84.922  40.201  1.00 43.85 ? 2051 HOH J O   1 
HETATM 20900 O  O   . HOH OB 5 .   ? 36.374  76.366  41.017  1.00 51.70 ? 2052 HOH J O   1 
HETATM 20901 O  O   . HOH OB 5 .   ? 30.979  87.444  39.581  1.00 60.65 ? 2053 HOH J O   1 
HETATM 20902 O  O   . HOH OB 5 .   ? 37.266  82.217  35.185  1.00 26.94 ? 2054 HOH J O   1 
HETATM 20903 O  O   . HOH OB 5 .   ? 30.807  88.416  37.167  1.00 48.34 ? 2055 HOH J O   1 
HETATM 20904 O  O   . HOH OB 5 .   ? 35.443  87.085  36.222  1.00 42.31 ? 2056 HOH J O   1 
HETATM 20905 O  O   . HOH OB 5 .   ? 32.702  85.985  34.104  1.00 45.06 ? 2057 HOH J O   1 
HETATM 20906 O  O   . HOH OB 5 .   ? 39.569  78.894  49.990  1.00 62.21 ? 2058 HOH J O   1 
HETATM 20907 O  O   . HOH OB 5 .   ? 30.040  86.633  42.431  1.00 45.44 ? 2059 HOH J O   1 
HETATM 20908 O  O   . HOH OB 5 .   ? 43.008  100.495 24.691  1.00 59.56 ? 2060 HOH J O   1 
HETATM 20909 O  O   . HOH OB 5 .   ? 36.055  81.150  48.422  1.00 44.83 ? 2061 HOH J O   1 
HETATM 20910 O  O   . HOH OB 5 .   ? 30.388  83.940  44.315  1.00 55.68 ? 2062 HOH J O   1 
HETATM 20911 O  O   . HOH OB 5 .   ? 38.965  77.736  42.952  1.00 45.37 ? 2063 HOH J O   1 
HETATM 20912 O  O   . HOH OB 5 .   ? 38.835  87.946  51.317  1.00 39.39 ? 2064 HOH J O   1 
HETATM 20913 O  O   . HOH OB 5 .   ? 45.794  82.726  50.926  1.00 52.17 ? 2065 HOH J O   1 
HETATM 20914 O  O   . HOH OB 5 .   ? 48.629  81.773  46.658  1.00 38.55 ? 2066 HOH J O   1 
HETATM 20915 O  O   . HOH OB 5 .   ? 52.540  85.849  49.867  1.00 36.47 ? 2067 HOH J O   1 
HETATM 20916 O  O   . HOH OB 5 .   ? 47.551  88.765  60.346  1.00 40.45 ? 2068 HOH J O   1 
HETATM 20917 O  O   . HOH OB 5 .   ? 50.542  102.138 58.647  1.00 54.71 ? 2069 HOH J O   1 
HETATM 20918 O  O   . HOH OB 5 .   ? 49.008  99.043  55.114  1.00 35.38 ? 2070 HOH J O   1 
HETATM 20919 O  O   . HOH OB 5 .   ? 50.749  105.786 54.727  1.00 45.62 ? 2071 HOH J O   1 
HETATM 20920 O  O   . HOH OB 5 .   ? 48.431  96.276  59.651  1.00 43.06 ? 2072 HOH J O   1 
HETATM 20921 O  O   . HOH OB 5 .   ? 55.143  95.465  52.254  1.00 49.45 ? 2073 HOH J O   1 
HETATM 20922 O  O   . HOH OB 5 .   ? 55.722  95.776  59.018  1.00 53.08 ? 2074 HOH J O   1 
HETATM 20923 O  O   . HOH OB 5 .   ? 54.412  93.096  59.573  1.00 41.01 ? 2075 HOH J O   1 
HETATM 20924 O  O   . HOH OB 5 .   ? 50.125  91.049  59.262  1.00 41.38 ? 2076 HOH J O   1 
HETATM 20925 O  O   . HOH OB 5 .   ? 53.930  87.845  50.847  1.00 38.26 ? 2077 HOH J O   1 
HETATM 20926 O  O   . HOH OB 5 .   ? 46.827  83.702  55.721  1.00 48.22 ? 2078 HOH J O   1 
HETATM 20927 O  O   . HOH OB 5 .   ? 45.202  100.570 49.829  1.00 36.04 ? 2079 HOH J O   1 
HETATM 20928 O  O   . HOH OB 5 .   ? 37.775  107.752 45.757  1.00 40.60 ? 2080 HOH J O   1 
HETATM 20929 O  O   . HOH OB 5 .   ? 39.943  104.534 46.209  1.00 40.55 ? 2081 HOH J O   1 
HETATM 20930 O  O   . HOH OB 5 .   ? 32.789  112.440 49.246  1.00 53.81 ? 2082 HOH J O   1 
HETATM 20931 O  O   . HOH OB 5 .   ? 28.228  105.233 42.361  1.00 47.46 ? 2083 HOH J O   1 
HETATM 20932 O  O   . HOH OB 5 .   ? 42.446  108.769 42.853  1.00 38.98 ? 2084 HOH J O   1 
HETATM 20933 O  O   . HOH OB 5 .   ? 36.718  110.026 44.077  1.00 48.20 ? 2085 HOH J O   1 
HETATM 20934 O  O   . HOH OB 5 .   ? 41.915  106.825 39.790  1.00 43.70 ? 2086 HOH J O   1 
HETATM 20935 O  O   . HOH OB 5 .   ? 48.405  104.924 40.635  1.00 46.56 ? 2087 HOH J O   1 
HETATM 20936 O  O   . HOH OB 5 .   ? 47.288  105.473 47.305  1.00 40.91 ? 2088 HOH J O   1 
HETATM 20937 O  O   . HOH OB 5 .   ? 49.860  103.442 47.016  1.00 39.44 ? 2089 HOH J O   1 
HETATM 20938 O  O   . HOH OB 5 .   ? 50.955  99.515  48.157  1.00 39.72 ? 2090 HOH J O   1 
HETATM 20939 O  O   . HOH OB 5 .   ? 55.077  100.746 45.674  1.00 52.39 ? 2091 HOH J O   1 
HETATM 20940 O  O   . HOH OB 5 .   ? 54.623  98.322  48.142  1.00 43.94 ? 2092 HOH J O   1 
HETATM 20941 O  O   . HOH OB 5 .   ? 59.602  99.915  44.458  1.00 60.69 ? 2093 HOH J O   1 
HETATM 20942 O  O   . HOH OB 5 .   ? 59.036  96.014  43.112  1.00 55.06 ? 2094 HOH J O   1 
HETATM 20943 O  O   . HOH OB 5 .   ? 57.020  94.162  41.509  1.00 53.60 ? 2095 HOH J O   1 
HETATM 20944 O  O   . HOH OB 5 .   ? 53.905  89.013  32.069  1.00 53.85 ? 2096 HOH J O   1 
HETATM 20945 O  O   . HOH OB 5 .   ? 56.904  85.883  34.172  1.00 46.03 ? 2097 HOH J O   1 
HETATM 20946 O  O   . HOH OB 5 .   ? 58.779  84.248  45.757  1.00 56.35 ? 2098 HOH J O   1 
HETATM 20947 O  O   . HOH OB 5 .   ? 53.843  82.360  41.910  1.00 52.04 ? 2099 HOH J O   1 
HETATM 20948 O  O   . HOH OB 5 .   ? 57.480  88.669  40.595  1.00 37.39 ? 2100 HOH J O   1 
HETATM 20949 O  O   . HOH OB 5 .   ? 52.364  84.051  39.712  1.00 37.03 ? 2101 HOH J O   1 
HETATM 20950 O  O   . HOH OB 5 .   ? 49.839  84.714  37.624  1.00 48.07 ? 2102 HOH J O   1 
HETATM 20951 O  O   . HOH OB 5 .   ? 49.962  79.106  40.381  1.00 48.63 ? 2103 HOH J O   1 
HETATM 20952 O  O   . HOH OB 5 .   ? 37.062  86.220  38.470  1.00 44.54 ? 2104 HOH J O   1 
HETATM 20953 O  O   . HOH OB 5 .   ? 30.902  98.470  54.527  1.00 59.15 ? 2105 HOH J O   1 
HETATM 20954 O  O   . HOH OB 5 .   ? 29.067  97.490  51.177  1.00 41.71 ? 2106 HOH J O   1 
HETATM 20955 O  O   . HOH OB 5 .   ? 33.167  90.201  57.975  1.00 60.91 ? 2107 HOH J O   1 
HETATM 20956 O  O   . HOH OB 5 .   ? 35.811  95.294  58.643  1.00 40.23 ? 2108 HOH J O   1 
HETATM 20957 O  O   . HOH OB 5 .   ? 41.162  99.285  58.379  1.00 45.90 ? 2109 HOH J O   1 
HETATM 20958 O  O   . HOH OB 5 .   ? 45.317  94.237  52.647  1.00 31.81 ? 2110 HOH J O   1 
HETATM 20959 O  O   . HOH OB 5 .   ? 43.057  98.423  60.748  1.00 46.91 ? 2111 HOH J O   1 
HETATM 20960 O  O   . HOH OB 5 .   ? 37.761  94.006  62.131  1.00 37.11 ? 2112 HOH J O   1 
HETATM 20961 O  O   . HOH OB 5 .   ? 42.947  97.093  66.137  1.00 39.91 ? 2113 HOH J O   1 
HETATM 20962 O  O   . HOH OB 5 .   ? 44.445  91.004  65.287  1.00 37.95 ? 2114 HOH J O   1 
HETATM 20963 O  O   . HOH OB 5 .   ? 34.484  88.022  65.302  1.00 39.99 ? 2115 HOH J O   1 
HETATM 20964 O  O   . HOH OB 5 .   ? 39.320  80.593  65.057  1.00 59.31 ? 2116 HOH J O   1 
HETATM 20965 O  O   . HOH OB 5 .   ? 38.300  83.602  65.441  1.00 45.32 ? 2117 HOH J O   1 
HETATM 20966 O  O   . HOH OB 5 .   ? 37.456  84.526  63.068  1.00 37.40 ? 2118 HOH J O   1 
HETATM 20967 O  O   . HOH OB 5 .   ? 46.060  82.931  58.154  1.00 59.48 ? 2119 HOH J O   1 
HETATM 20968 O  O   . HOH OB 5 .   ? 42.731  84.831  52.259  1.00 32.73 ? 2120 HOH J O   1 
HETATM 20969 O  O   . HOH OB 5 .   ? 35.137  88.704  56.297  1.00 44.22 ? 2121 HOH J O   1 
HETATM 20970 O  O   . HOH OB 5 .   ? 36.361  88.174  52.951  1.00 40.74 ? 2122 HOH J O   1 
HETATM 20971 O  O   . HOH OB 5 .   ? 38.326  81.295  49.610  1.00 43.46 ? 2123 HOH J O   1 
HETATM 20972 O  O   . HOH OB 5 .   ? 39.978  85.136  51.069  1.00 40.67 ? 2124 HOH J O   1 
HETATM 20973 O  O   . HOH OB 5 .   ? 31.108  86.735  48.756  1.00 33.83 ? 2125 HOH J O   1 
HETATM 20974 O  O   . HOH OB 5 .   ? 29.332  89.281  43.703  1.00 44.62 ? 2126 HOH J O   1 
HETATM 20975 O  O   . HOH OB 5 .   ? 35.674  86.299  51.081  1.00 50.68 ? 2127 HOH J O   1 
HETATM 20976 O  O   . HOH OB 5 .   ? 38.609  83.087  51.865  1.00 41.28 ? 2128 HOH J O   1 
HETATM 20977 O  O   . HOH OB 5 .   ? 33.432  88.905  37.029  1.00 36.13 ? 2129 HOH J O   1 
HETATM 20978 O  O   . HOH OB 5 .   ? 36.884  88.640  34.184  1.00 34.45 ? 2130 HOH J O   1 
HETATM 20979 O  O   . HOH OB 5 .   ? 38.606  91.402  33.471  1.00 23.74 ? 2131 HOH J O   1 
HETATM 20980 O  O   . HOH OB 5 .   ? 51.124  99.779  25.804  1.00 61.32 ? 2132 HOH J O   1 
HETATM 20981 O  O   . HOH OB 5 .   ? 44.725  99.147  26.286  1.00 50.76 ? 2133 HOH J O   1 
HETATM 20982 O  O   . HOH PB 5 .   ? -8.997  79.722  81.145  1.00 49.82 ? 2001 HOH K O   1 
HETATM 20983 O  O   . HOH PB 5 .   ? 14.237  77.576  91.494  1.00 60.48 ? 2002 HOH K O   1 
HETATM 20984 O  O   . HOH PB 5 .   ? 7.021   82.675  88.791  1.00 43.97 ? 2003 HOH K O   1 
HETATM 20985 O  O   . HOH PB 5 .   ? 15.268  75.100  105.892 1.00 50.61 ? 2004 HOH K O   1 
HETATM 20986 O  O   . HOH PB 5 .   ? 2.295   71.051  84.189  1.00 54.53 ? 2005 HOH K O   1 
HETATM 20987 O  O   . HOH PB 5 .   ? 19.127  80.847  99.704  1.00 62.79 ? 2006 HOH K O   1 
HETATM 20988 O  O   . HOH PB 5 .   ? 12.943  78.732  98.018  1.00 47.53 ? 2007 HOH K O   1 
HETATM 20989 O  O   . HOH PB 5 .   ? 13.021  78.844  93.735  1.00 41.58 ? 2008 HOH K O   1 
HETATM 20990 O  O   . HOH PB 5 .   ? 15.440  73.431  103.074 1.00 47.57 ? 2009 HOH K O   1 
HETATM 20991 O  O   . HOH PB 5 .   ? 13.964  76.955  101.876 1.00 54.29 ? 2010 HOH K O   1 
HETATM 20992 O  O   . HOH PB 5 .   ? 2.822   68.036  110.859 1.00 57.98 ? 2011 HOH K O   1 
HETATM 20993 O  O   . HOH PB 5 .   ? 0.540   73.126  83.980  1.00 46.33 ? 2012 HOH K O   1 
HETATM 20994 O  O   . HOH PB 5 .   ? 1.242   70.250  86.557  1.00 48.45 ? 2013 HOH K O   1 
HETATM 20995 O  O   . HOH PB 5 .   ? -3.289  74.730  84.598  1.00 36.48 ? 2014 HOH K O   1 
HETATM 20996 O  O   . HOH PB 5 .   ? 1.853   72.933  112.844 1.00 58.88 ? 2015 HOH K O   1 
HETATM 20997 O  O   . HOH PB 5 .   ? -9.402  93.287  98.398  1.00 49.51 ? 2016 HOH K O   1 
HETATM 20998 O  O   . HOH PB 5 .   ? -2.423  93.153  107.097 1.00 61.01 ? 2017 HOH K O   1 
HETATM 20999 O  O   . HOH PB 5 .   ? -15.070 80.280  86.265  1.00 60.74 ? 2018 HOH K O   1 
HETATM 21000 O  O   . HOH PB 5 .   ? -12.632 71.342  88.066  1.00 62.09 ? 2019 HOH K O   1 
HETATM 21001 O  O   . HOH PB 5 .   ? -15.752 79.678  93.549  1.00 38.97 ? 2020 HOH K O   1 
HETATM 21002 O  O   . HOH PB 5 .   ? -16.690 74.544  89.606  1.00 42.12 ? 2021 HOH K O   1 
HETATM 21003 O  O   . HOH PB 5 .   ? -14.000 72.583  89.339  1.00 42.49 ? 2022 HOH K O   1 
HETATM 21004 O  O   . HOH PB 5 .   ? -14.720 69.135  105.789 1.00 55.68 ? 2023 HOH K O   1 
HETATM 21005 O  O   . HOH PB 5 .   ? -16.390 91.228  110.924 1.00 53.48 ? 2024 HOH K O   1 
HETATM 21006 O  O   . HOH PB 5 .   ? -7.292  71.652  102.638 1.00 42.40 ? 2025 HOH K O   1 
HETATM 21007 O  O   . HOH PB 5 .   ? -2.529  69.725  110.417 1.00 43.49 ? 2026 HOH K O   1 
HETATM 21008 O  O   . HOH PB 5 .   ? 2.884   70.329  88.900  1.00 39.25 ? 2027 HOH K O   1 
HETATM 21009 O  O   . HOH PB 5 .   ? 6.817   71.107  89.668  1.00 52.83 ? 2028 HOH K O   1 
HETATM 21010 O  O   . HOH PB 5 .   ? 13.148  74.440  101.613 1.00 48.47 ? 2029 HOH K O   1 
HETATM 21011 O  O   . HOH PB 5 .   ? 10.864  74.403  103.064 1.00 30.48 ? 2030 HOH K O   1 
HETATM 21012 O  O   . HOH PB 5 .   ? -11.469 73.377  103.205 1.00 45.73 ? 2031 HOH K O   1 
HETATM 21013 O  O   . HOH PB 5 .   ? 10.956  68.912  108.423 1.00 46.78 ? 2032 HOH K O   1 
HETATM 21014 O  O   . HOH PB 5 .   ? 12.569  65.056  106.480 1.00 47.63 ? 2033 HOH K O   1 
HETATM 21015 O  O   . HOH PB 5 .   ? 10.308  61.106  107.339 1.00 51.31 ? 2034 HOH K O   1 
HETATM 21016 O  O   . HOH PB 5 .   ? 12.841  67.830  105.941 1.00 53.29 ? 2035 HOH K O   1 
HETATM 21017 O  O   . HOH PB 5 .   ? 4.961   70.169  109.949 1.00 41.80 ? 2036 HOH K O   1 
HETATM 21018 O  O   . HOH PB 5 .   ? 6.724   72.851  108.695 1.00 41.34 ? 2037 HOH K O   1 
HETATM 21019 O  O   . HOH PB 5 .   ? -10.176 90.963  89.995  1.00 53.24 ? 2038 HOH K O   1 
HETATM 21020 O  O   . HOH PB 5 .   ? 12.806  75.626  107.437 1.00 54.51 ? 2039 HOH K O   1 
HETATM 21021 O  O   . HOH PB 5 .   ? 13.381  77.453  104.699 1.00 54.04 ? 2040 HOH K O   1 
HETATM 21022 O  O   . HOH PB 5 .   ? 2.316   77.173  114.832 1.00 38.02 ? 2041 HOH K O   1 
HETATM 21023 O  O   . HOH PB 5 .   ? -0.125  75.113  114.317 1.00 53.68 ? 2042 HOH K O   1 
HETATM 21024 O  O   . HOH PB 5 .   ? -7.858  78.623  119.082 1.00 43.51 ? 2043 HOH K O   1 
HETATM 21025 O  O   . HOH PB 5 .   ? -3.643  95.782  101.314 1.00 45.91 ? 2044 HOH K O   1 
HETATM 21026 O  O   . HOH PB 5 .   ? -6.884  94.204  95.526  1.00 39.49 ? 2045 HOH K O   1 
HETATM 21027 O  O   . HOH PB 5 .   ? -7.359  95.825  99.483  1.00 53.56 ? 2046 HOH K O   1 
HETATM 21028 O  O   . HOH PB 5 .   ? 6.781   86.485  113.475 1.00 54.09 ? 2047 HOH K O   1 
HETATM 21029 O  O   . HOH PB 5 .   ? -1.675  90.947  107.042 1.00 48.91 ? 2048 HOH K O   1 
HETATM 21030 O  O   . HOH PB 5 .   ? 5.176   98.098  91.925  1.00 36.02 ? 2049 HOH K O   1 
HETATM 21031 O  O   . HOH PB 5 .   ? 1.802   96.591  93.873  1.00 34.49 ? 2050 HOH K O   1 
HETATM 21032 O  O   . HOH PB 5 .   ? 9.192   87.394  88.415  1.00 57.38 ? 2051 HOH K O   1 
HETATM 21033 O  O   . HOH PB 5 .   ? 5.387   88.432  94.273  1.00 42.50 ? 2052 HOH K O   1 
HETATM 21034 O  O   . HOH PB 5 .   ? 4.619   91.235  89.005  1.00 29.84 ? 2053 HOH K O   1 
HETATM 21035 O  O   . HOH PB 5 .   ? 9.948   85.590  93.285  1.00 57.20 ? 2054 HOH K O   1 
HETATM 21036 O  O   . HOH PB 5 .   ? 6.009   86.210  90.276  1.00 41.53 ? 2055 HOH K O   1 
HETATM 21037 O  O   . HOH PB 5 .   ? 11.561  90.016  90.990  1.00 54.35 ? 2056 HOH K O   1 
HETATM 21038 O  O   . HOH PB 5 .   ? 11.086  86.404  96.949  1.00 45.36 ? 2057 HOH K O   1 
HETATM 21039 O  O   . HOH PB 5 .   ? 4.849   92.089  102.353 1.00 42.55 ? 2058 HOH K O   1 
HETATM 21040 O  O   . HOH PB 5 .   ? 8.094   88.812  102.480 1.00 43.21 ? 2059 HOH K O   1 
HETATM 21041 O  O   . HOH PB 5 .   ? 9.622   87.315  100.057 1.00 51.19 ? 2060 HOH K O   1 
HETATM 21042 O  O   . HOH PB 5 .   ? 2.681   95.641  96.296  1.00 34.99 ? 2061 HOH K O   1 
HETATM 21043 O  O   . HOH PB 5 .   ? -5.666  92.159  101.802 1.00 54.92 ? 2062 HOH K O   1 
HETATM 21044 O  O   . HOH PB 5 .   ? 1.552   85.612  104.954 1.00 35.71 ? 2063 HOH K O   1 
HETATM 21045 O  O   . HOH PB 5 .   ? -6.565  92.349  105.089 1.00 49.90 ? 2064 HOH K O   1 
HETATM 21046 O  O   . HOH PB 5 .   ? -11.870 88.066  102.427 1.00 30.35 ? 2065 HOH K O   1 
HETATM 21047 O  O   . HOH PB 5 .   ? -7.638  92.045  99.691  1.00 37.11 ? 2066 HOH K O   1 
HETATM 21048 O  O   . HOH PB 5 .   ? -15.296 84.082  103.141 1.00 48.56 ? 2067 HOH K O   1 
HETATM 21049 O  O   . HOH PB 5 .   ? -17.094 90.039  106.212 1.00 51.29 ? 2068 HOH K O   1 
HETATM 21050 O  O   . HOH PB 5 .   ? -8.893  92.840  108.683 1.00 56.49 ? 2069 HOH K O   1 
HETATM 21051 O  O   . HOH PB 5 .   ? -7.917  85.299  113.204 1.00 43.61 ? 2070 HOH K O   1 
HETATM 21052 O  O   . HOH PB 5 .   ? -14.875 76.678  102.879 1.00 56.39 ? 2071 HOH K O   1 
HETATM 21053 O  O   . HOH PB 5 .   ? -11.400 68.119  106.767 1.00 47.73 ? 2072 HOH K O   1 
HETATM 21054 O  O   . HOH PB 5 .   ? -9.367  74.883  107.958 1.00 32.62 ? 2073 HOH K O   1 
HETATM 21055 O  O   . HOH PB 5 .   ? -15.201 78.811  104.449 1.00 43.28 ? 2074 HOH K O   1 
HETATM 21056 O  O   . HOH PB 5 .   ? -8.858  77.593  112.219 1.00 39.44 ? 2075 HOH K O   1 
HETATM 21057 O  O   . HOH PB 5 .   ? -11.786 75.236  111.099 1.00 57.40 ? 2076 HOH K O   1 
HETATM 21058 O  O   . HOH PB 5 .   ? -14.679 77.481  112.249 1.00 50.91 ? 2077 HOH K O   1 
HETATM 21059 O  O   . HOH PB 5 .   ? -15.639 81.677  104.616 1.00 44.98 ? 2078 HOH K O   1 
HETATM 21060 O  O   . HOH PB 5 .   ? -18.027 78.358  106.078 1.00 58.34 ? 2079 HOH K O   1 
HETATM 21061 O  O   . HOH PB 5 .   ? -16.719 78.604  110.948 1.00 44.16 ? 2080 HOH K O   1 
HETATM 21062 O  O   . HOH PB 5 .   ? -15.128 80.872  111.797 1.00 35.04 ? 2081 HOH K O   1 
HETATM 21063 O  O   . HOH PB 5 .   ? -10.459 82.752  112.023 1.00 32.13 ? 2082 HOH K O   1 
HETATM 21064 O  O   . HOH PB 5 .   ? -17.239 85.052  109.773 1.00 49.65 ? 2083 HOH K O   1 
HETATM 21065 O  O   . HOH PB 5 .   ? -14.071 90.169  110.722 1.00 51.11 ? 2084 HOH K O   1 
HETATM 21066 O  O   . HOH PB 5 .   ? -16.686 88.729  109.938 1.00 52.24 ? 2085 HOH K O   1 
HETATM 21067 O  O   . HOH PB 5 .   ? -13.441 86.175  103.469 1.00 35.48 ? 2086 HOH K O   1 
HETATM 21068 O  O   . HOH PB 5 .   ? -6.477  90.028  108.863 1.00 38.76 ? 2087 HOH K O   1 
HETATM 21069 O  O   . HOH PB 5 .   ? -5.089  73.101  102.814 1.00 34.95 ? 2088 HOH K O   1 
HETATM 21070 O  O   . HOH PB 5 .   ? -3.398  72.044  108.429 1.00 37.32 ? 2089 HOH K O   1 
HETATM 21071 O  O   . HOH PB 5 .   ? -0.204  66.771  106.943 1.00 41.97 ? 2090 HOH K O   1 
HETATM 21072 O  O   . HOH PB 5 .   ? 7.902   61.976  96.527  1.00 47.33 ? 2091 HOH K O   1 
HETATM 21073 O  O   . HOH PB 5 .   ? 5.030   60.437  99.285  1.00 56.42 ? 2092 HOH K O   1 
HETATM 21074 O  O   . HOH PB 5 .   ? 6.975   60.859  103.425 1.00 52.11 ? 2093 HOH K O   1 
HETATM 21075 O  O   . HOH PB 5 .   ? 14.047  61.940  100.666 1.00 45.19 ? 2094 HOH K O   1 
HETATM 21076 O  O   . HOH PB 5 .   ? 12.186  68.034  96.540  1.00 40.81 ? 2095 HOH K O   1 
HETATM 21077 O  O   . HOH PB 5 .   ? 5.202   65.168  92.366  1.00 49.15 ? 2096 HOH K O   1 
HETATM 21078 O  O   . HOH PB 5 .   ? 3.974   63.491  98.091  1.00 40.55 ? 2097 HOH K O   1 
HETATM 21079 O  O   . HOH PB 5 .   ? -1.212  66.803  93.038  1.00 43.44 ? 2098 HOH K O   1 
HETATM 21080 O  O   . HOH PB 5 .   ? -5.792  67.798  100.523 1.00 42.71 ? 2099 HOH K O   1 
HETATM 21081 O  O   . HOH PB 5 .   ? -12.270 68.298  94.168  1.00 58.73 ? 2100 HOH K O   1 
HETATM 21082 O  O   . HOH PB 5 .   ? -9.467  70.706  99.937  1.00 39.63 ? 2101 HOH K O   1 
HETATM 21083 O  O   . HOH PB 5 .   ? -12.395 71.202  100.501 1.00 53.88 ? 2102 HOH K O   1 
HETATM 21084 O  O   . HOH PB 5 .   ? -10.662 74.508  100.879 1.00 40.31 ? 2103 HOH K O   1 
HETATM 21085 O  O   . HOH PB 5 .   ? -17.711 80.275  95.227  1.00 43.00 ? 2104 HOH K O   1 
HETATM 21086 O  O   . HOH PB 5 .   ? -14.165 75.745  100.684 1.00 50.78 ? 2105 HOH K O   1 
HETATM 21087 O  O   . HOH PB 5 .   ? -16.338 81.845  88.307  1.00 48.85 ? 2106 HOH K O   1 
HETATM 21088 O  O   . HOH PB 5 .   ? -12.147 89.229  86.543  1.00 47.38 ? 2107 HOH K O   1 
HETATM 21089 O  O   . HOH PB 5 .   ? -12.526 91.866  94.737  1.00 55.77 ? 2108 HOH K O   1 
HETATM 21090 O  O   . HOH PB 5 .   ? -15.922 85.540  92.830  1.00 44.63 ? 2109 HOH K O   1 
HETATM 21091 O  O   . HOH PB 5 .   ? -10.791 89.863  92.431  1.00 35.46 ? 2110 HOH K O   1 
HETATM 21092 O  O   . HOH PB 5 .   ? -8.506  94.412  93.004  1.00 45.17 ? 2111 HOH K O   1 
HETATM 21093 O  O   . HOH PB 5 .   ? 4.486   87.264  92.164  1.00 54.53 ? 2112 HOH K O   1 
HETATM 21094 O  O   . HOH PB 5 .   ? 10.883  75.682  105.607 1.00 36.46 ? 2113 HOH K O   1 
HETATM 21095 O  O   . HOH PB 5 .   ? 13.416  77.927  108.443 1.00 59.38 ? 2114 HOH K O   1 
HETATM 21096 O  O   . HOH PB 5 .   ? 12.375  81.103  111.091 1.00 54.92 ? 2115 HOH K O   1 
HETATM 21097 O  O   . HOH PB 5 .   ? 6.086   74.440  110.871 1.00 46.47 ? 2116 HOH K O   1 
HETATM 21098 O  O   . HOH PB 5 .   ? 3.915   78.001  112.509 1.00 38.15 ? 2117 HOH K O   1 
HETATM 21099 O  O   . HOH PB 5 .   ? -5.189  79.501  105.765 1.00 29.63 ? 2118 HOH K O   1 
HETATM 21100 O  O   . HOH PB 5 .   ? -1.494  74.188  111.763 1.00 53.08 ? 2119 HOH K O   1 
HETATM 21101 O  O   . HOH PB 5 .   ? -4.233  75.029  113.985 1.00 39.88 ? 2120 HOH K O   1 
HETATM 21102 O  O   . HOH PB 5 .   ? 1.313   79.369  115.953 1.00 35.61 ? 2121 HOH K O   1 
HETATM 21103 O  O   . HOH PB 5 .   ? -9.532  80.441  113.429 1.00 55.39 ? 2122 HOH K O   1 
HETATM 21104 O  O   . HOH PB 5 .   ? -5.342  82.911  117.992 1.00 32.88 ? 2123 HOH K O   1 
HETATM 21105 O  O   . HOH PB 5 .   ? -5.291  77.791  120.130 1.00 44.43 ? 2124 HOH K O   1 
HETATM 21106 O  O   . HOH PB 5 .   ? -6.889  74.014  113.719 1.00 47.83 ? 2125 HOH K O   1 
HETATM 21107 O  O   . HOH PB 5 .   ? 4.516   87.635  116.650 1.00 44.90 ? 2126 HOH K O   1 
HETATM 21108 O  O   . HOH PB 5 .   ? 4.393   84.797  116.441 1.00 48.20 ? 2127 HOH K O   1 
HETATM 21109 O  O   . HOH PB 5 .   ? 0.487   92.685  118.752 1.00 56.44 ? 2128 HOH K O   1 
HETATM 21110 O  O   . HOH PB 5 .   ? 0.782   89.688  119.151 1.00 41.48 ? 2129 HOH K O   1 
HETATM 21111 O  O   . HOH PB 5 .   ? 5.466   88.733  114.127 1.00 62.35 ? 2130 HOH K O   1 
HETATM 21112 O  O   . HOH PB 5 .   ? 2.070   88.767  116.871 1.00 37.21 ? 2131 HOH K O   1 
HETATM 21113 O  O   . HOH PB 5 .   ? 1.550   91.099  113.535 1.00 62.76 ? 2132 HOH K O   1 
HETATM 21114 O  O   . HOH PB 5 .   ? -6.000  91.110  114.621 1.00 55.19 ? 2133 HOH K O   1 
HETATM 21115 O  O   . HOH PB 5 .   ? -2.201  88.809  105.647 1.00 31.42 ? 2134 HOH K O   1 
HETATM 21116 O  O   . HOH PB 5 .   ? 4.588   84.631  110.153 1.00 40.78 ? 2135 HOH K O   1 
HETATM 21117 O  O   . HOH PB 5 .   ? 3.852   85.149  106.772 1.00 37.52 ? 2136 HOH K O   1 
HETATM 21118 O  O   . HOH PB 5 .   ? 11.400  83.898  98.241  1.00 41.55 ? 2137 HOH K O   1 
HETATM 21119 O  O   . HOH PB 5 .   ? 4.782   87.033  104.990 1.00 44.47 ? 2138 HOH K O   1 
HETATM 21120 O  O   . HOH PB 5 .   ? 9.668   86.334  103.018 1.00 32.64 ? 2139 HOH K O   1 
HETATM 21121 O  O   . HOH PB 5 .   ? 1.781   90.385  105.481 1.00 40.71 ? 2140 HOH K O   1 
HETATM 21122 O  O   . HOH PB 5 .   ? 0.454   88.201  104.571 1.00 36.47 ? 2141 HOH K O   1 
HETATM 21123 O  O   . HOH PB 5 .   ? 6.438   90.437  103.930 1.00 52.46 ? 2142 HOH K O   1 
HETATM 21124 O  O   . HOH PB 5 .   ? 2.346   92.035  103.472 1.00 36.89 ? 2143 HOH K O   1 
HETATM 21125 O  O   . HOH PB 5 .   ? 8.050   84.503  91.188  1.00 41.39 ? 2144 HOH K O   1 
HETATM 21126 O  O   . HOH PB 5 .   ? 4.739   84.742  88.063  1.00 41.20 ? 2145 HOH K O   1 
HETATM 21127 O  O   . HOH PB 5 .   ? 3.049   82.119  87.140  1.00 26.88 ? 2146 HOH K O   1 
HETATM 21128 O  O   . HOH PB 5 .   ? -1.653  77.497  79.002  1.00 49.17 ? 2147 HOH K O   1 
HETATM 21129 O  O   . HOH PB 5 .   ? -2.811  74.609  79.431  1.00 54.19 ? 2148 HOH K O   1 
HETATM 21130 O  O   . HOH QB 5 .   ? 57.152  133.629 50.525  1.00 48.66 ? 2001 HOH L O   1 
HETATM 21131 O  O   . HOH QB 5 .   ? 31.801  144.246 71.037  1.00 54.48 ? 2002 HOH L O   1 
HETATM 21132 O  O   . HOH QB 5 .   ? 36.375  141.767 61.746  1.00 49.75 ? 2003 HOH L O   1 
HETATM 21133 O  O   . HOH QB 5 .   ? 39.532  141.388 58.277  1.00 51.40 ? 2004 HOH L O   1 
HETATM 21134 O  O   . HOH QB 5 .   ? 32.034  146.231 68.451  1.00 37.59 ? 2005 HOH L O   1 
HETATM 21135 O  O   . HOH QB 5 .   ? 32.647  141.547 66.903  1.00 59.00 ? 2006 HOH L O   1 
HETATM 21136 O  O   . HOH QB 5 .   ? 65.047  145.225 46.457  1.00 54.35 ? 2007 HOH L O   1 
HETATM 21137 O  O   . HOH QB 5 .   ? 33.739  147.645 58.803  1.00 52.54 ? 2008 HOH L O   1 
HETATM 21138 O  O   . HOH QB 5 .   ? 37.060  143.817 63.130  1.00 41.38 ? 2009 HOH L O   1 
HETATM 21139 O  O   . HOH QB 5 .   ? 50.776  163.110 57.762  1.00 58.74 ? 2010 HOH L O   1 
HETATM 21140 O  O   . HOH QB 5 .   ? 48.799  132.898 77.632  1.00 62.50 ? 2011 HOH L O   1 
HETATM 21141 O  O   . HOH QB 5 .   ? 44.944  140.280 78.897  1.00 53.32 ? 2012 HOH L O   1 
HETATM 21142 O  O   . HOH QB 5 .   ? 59.667  150.168 75.526  1.00 49.94 ? 2013 HOH L O   1 
HETATM 21143 O  O   . HOH QB 5 .   ? 67.473  145.497 56.289  1.00 46.52 ? 2014 HOH L O   1 
HETATM 21144 O  O   . HOH QB 5 .   ? 64.009  162.804 70.401  1.00 45.74 ? 2015 HOH L O   1 
HETATM 21145 O  O   . HOH QB 5 .   ? 64.307  143.595 48.870  1.00 48.46 ? 2016 HOH L O   1 
HETATM 21146 O  O   . HOH QB 5 .   ? 56.502  159.026 59.495  1.00 54.77 ? 2017 HOH L O   1 
HETATM 21147 O  O   . HOH QB 5 .   ? 57.111  154.540 56.098  1.00 44.63 ? 2018 HOH L O   1 
HETATM 21148 O  O   . HOH QB 5 .   ? 50.583  154.365 54.412  1.00 55.91 ? 2019 HOH L O   1 
HETATM 21149 O  O   . HOH QB 5 .   ? 51.763  160.303 58.070  1.00 57.10 ? 2020 HOH L O   1 
HETATM 21150 O  O   . HOH QB 5 .   ? 52.950  162.851 61.780  1.00 45.78 ? 2021 HOH L O   1 
HETATM 21151 O  O   . HOH QB 5 .   ? 36.954  152.907 63.848  1.00 51.71 ? 2022 HOH L O   1 
HETATM 21152 O  O   . HOH QB 5 .   ? 34.787  154.768 59.576  1.00 55.51 ? 2023 HOH L O   1 
HETATM 21153 O  O   . HOH QB 5 .   ? 39.440  154.185 64.055  1.00 41.14 ? 2024 HOH L O   1 
HETATM 21154 O  O   . HOH QB 5 .   ? 41.429  159.874 64.182  1.00 67.47 ? 2025 HOH L O   1 
HETATM 21155 O  O   . HOH QB 5 .   ? 44.944  162.461 62.843  1.00 53.43 ? 2026 HOH L O   1 
HETATM 21156 O  O   . HOH QB 5 .   ? 43.688  160.107 64.560  1.00 56.75 ? 2027 HOH L O   1 
HETATM 21157 O  O   . HOH QB 5 .   ? 64.290  138.877 68.628  1.00 55.48 ? 2028 HOH L O   1 
HETATM 21158 O  O   . HOH QB 5 .   ? 49.701  163.557 65.645  1.00 51.37 ? 2029 HOH L O   1 
HETATM 21159 O  O   . HOH QB 5 .   ? 58.431  141.521 75.794  1.00 45.38 ? 2030 HOH L O   1 
HETATM 21160 O  O   . HOH QB 5 .   ? 60.332  137.471 70.688  1.00 51.64 ? 2031 HOH L O   1 
HETATM 21161 O  O   . HOH QB 5 .   ? 47.933  133.699 67.994  1.00 30.08 ? 2032 HOH L O   1 
HETATM 21162 O  O   . HOH QB 5 .   ? 56.997  149.212 75.514  1.00 49.92 ? 2033 HOH L O   1 
HETATM 21163 O  O   . HOH QB 5 .   ? 47.200  139.550 68.996  1.00 43.64 ? 2034 HOH L O   1 
HETATM 21164 O  O   . HOH QB 5 .   ? 49.573  132.331 75.183  1.00 44.50 ? 2035 HOH L O   1 
HETATM 21165 O  O   . HOH QB 5 .   ? 52.716  135.137 74.163  1.00 37.37 ? 2036 HOH L O   1 
HETATM 21166 O  O   . HOH QB 5 .   ? 44.786  137.347 64.918  1.00 49.14 ? 2037 HOH L O   1 
HETATM 21167 O  O   . HOH QB 5 .   ? 42.601  135.003 65.602  1.00 51.66 ? 2038 HOH L O   1 
HETATM 21168 O  O   . HOH QB 5 .   ? 41.701  140.072 67.613  1.00 52.64 ? 2039 HOH L O   1 
HETATM 21169 O  O   . HOH QB 5 .   ? 54.379  149.325 77.077  1.00 52.11 ? 2040 HOH L O   1 
HETATM 21170 O  O   . HOH QB 5 .   ? 37.206  149.107 67.109  1.00 49.33 ? 2041 HOH L O   1 
HETATM 21171 O  O   . HOH QB 5 .   ? 46.444  134.614 77.079  1.00 54.20 ? 2042 HOH L O   1 
HETATM 21172 O  O   . HOH QB 5 .   ? 41.549  142.693 70.389  1.00 55.36 ? 2043 HOH L O   1 
HETATM 21173 O  O   . HOH QB 5 .   ? 49.836  144.467 75.926  1.00 43.61 ? 2044 HOH L O   1 
HETATM 21174 O  O   . HOH QB 5 .   ? 43.055  142.764 73.666  1.00 49.08 ? 2045 HOH L O   1 
HETATM 21175 O  O   . HOH QB 5 .   ? 45.566  145.834 74.055  1.00 58.37 ? 2046 HOH L O   1 
HETATM 21176 O  O   . HOH QB 5 .   ? 47.578  139.453 77.396  1.00 46.33 ? 2047 HOH L O   1 
HETATM 21177 O  O   . HOH QB 5 .   ? 51.871  137.682 75.214  1.00 38.55 ? 2048 HOH L O   1 
HETATM 21178 O  O   . HOH QB 5 .   ? 51.286  149.976 71.584  1.00 43.14 ? 2049 HOH L O   1 
HETATM 21179 O  O   . HOH QB 5 .   ? 60.947  147.597 74.307  1.00 46.82 ? 2050 HOH L O   1 
HETATM 21180 O  O   . HOH QB 5 .   ? 64.618  147.275 67.954  1.00 40.36 ? 2051 HOH L O   1 
HETATM 21181 O  O   . HOH QB 5 .   ? 64.408  149.042 75.183  1.00 55.81 ? 2052 HOH L O   1 
HETATM 21182 O  O   . HOH QB 5 .   ? 61.174  142.928 70.794  1.00 40.94 ? 2053 HOH L O   1 
HETATM 21183 O  O   . HOH QB 5 .   ? 70.880  149.327 69.605  1.00 62.99 ? 2054 HOH L O   1 
HETATM 21184 O  O   . HOH QB 5 .   ? 63.482  151.722 75.493  1.00 55.59 ? 2055 HOH L O   1 
HETATM 21185 O  O   . HOH QB 5 .   ? 65.922  158.399 76.006  1.00 48.03 ? 2056 HOH L O   1 
HETATM 21186 O  O   . HOH QB 5 .   ? 63.467  159.482 72.613  1.00 38.67 ? 2057 HOH L O   1 
HETATM 21187 O  O   . HOH QB 5 .   ? 64.699  159.825 69.533  1.00 56.47 ? 2058 HOH L O   1 
HETATM 21188 O  O   . HOH QB 5 .   ? 61.273  158.178 71.768  1.00 35.28 ? 2059 HOH L O   1 
HETATM 21189 O  O   . HOH QB 5 .   ? 59.274  158.979 60.668  1.00 39.28 ? 2060 HOH L O   1 
HETATM 21190 O  O   . HOH QB 5 .   ? 65.955  153.753 60.640  1.00 55.20 ? 2061 HOH L O   1 
HETATM 21191 O  O   . HOH QB 5 .   ? 63.168  158.090 68.667  1.00 42.86 ? 2062 HOH L O   1 
HETATM 21192 O  O   . HOH QB 5 .   ? 66.995  158.880 65.598  1.00 47.46 ? 2063 HOH L O   1 
HETATM 21193 O  O   . HOH QB 5 .   ? 65.613  149.131 66.057  1.00 41.81 ? 2064 HOH L O   1 
HETATM 21194 O  O   . HOH QB 5 .   ? 54.794  154.656 57.441  1.00 45.56 ? 2065 HOH L O   1 
HETATM 21195 O  O   . HOH QB 5 .   ? 53.009  160.283 60.716  1.00 44.92 ? 2066 HOH L O   1 
HETATM 21196 O  O   . HOH QB 5 .   ? 54.341  156.953 58.602  1.00 47.30 ? 2067 HOH L O   1 
HETATM 21197 O  O   . HOH QB 5 .   ? 52.252  154.981 56.242  1.00 46.63 ? 2068 HOH L O   1 
HETATM 21198 O  O   . HOH QB 5 .   ? 48.082  155.451 54.878  1.00 46.94 ? 2069 HOH L O   1 
HETATM 21199 O  O   . HOH QB 5 .   ? 50.042  158.022 56.988  1.00 49.12 ? 2070 HOH L O   1 
HETATM 21200 O  O   . HOH QB 5 .   ? 35.666  152.206 55.431  1.00 51.09 ? 2071 HOH L O   1 
HETATM 21201 O  O   . HOH QB 5 .   ? 47.755  150.557 48.498  1.00 56.77 ? 2072 HOH L O   1 
HETATM 21202 O  O   . HOH QB 5 .   ? 59.494  153.113 56.064  1.00 44.85 ? 2073 HOH L O   1 
HETATM 21203 O  O   . HOH QB 5 .   ? 62.980  151.347 49.803  1.00 51.09 ? 2074 HOH L O   1 
HETATM 21204 O  O   . HOH QB 5 .   ? 60.646  154.528 52.525  1.00 55.12 ? 2075 HOH L O   1 
HETATM 21205 O  O   . HOH QB 5 .   ? 63.612  152.241 56.129  1.00 58.28 ? 2076 HOH L O   1 
HETATM 21206 O  O   . HOH QB 5 .   ? 63.022  151.044 52.385  1.00 56.87 ? 2077 HOH L O   1 
HETATM 21207 O  O   . HOH QB 5 .   ? 66.793  144.266 58.481  1.00 52.64 ? 2078 HOH L O   1 
HETATM 21208 O  O   . HOH QB 5 .   ? 65.209  144.560 55.540  1.00 42.85 ? 2079 HOH L O   1 
HETATM 21209 O  O   . HOH QB 5 .   ? 66.856  140.632 59.712  1.00 57.12 ? 2080 HOH L O   1 
HETATM 21210 O  O   . HOH QB 5 .   ? 62.810  137.850 64.454  1.00 43.66 ? 2081 HOH L O   1 
HETATM 21211 O  O   . HOH QB 5 .   ? 62.512  136.805 69.349  1.00 60.49 ? 2082 HOH L O   1 
HETATM 21212 O  O   . HOH QB 5 .   ? 47.657  138.461 66.678  1.00 54.84 ? 2083 HOH L O   1 
HETATM 21213 O  O   . HOH QB 5 .   ? 39.934  155.846 66.428  1.00 50.05 ? 2084 HOH L O   1 
HETATM 21214 O  O   . HOH QB 5 .   ? 48.422  160.706 69.762  1.00 53.74 ? 2085 HOH L O   1 
HETATM 21215 O  O   . HOH QB 5 .   ? 45.119  161.160 66.840  1.00 56.08 ? 2086 HOH L O   1 
HETATM 21216 O  O   . HOH QB 5 .   ? 52.220  162.295 64.634  1.00 46.60 ? 2087 HOH L O   1 
HETATM 21217 O  O   . HOH QB 5 .   ? 56.167  154.425 64.541  1.00 34.92 ? 2088 HOH L O   1 
HETATM 21218 O  O   . HOH QB 5 .   ? 51.612  162.672 72.265  1.00 41.71 ? 2089 HOH L O   1 
HETATM 21219 O  O   . HOH QB 5 .   ? 62.655  161.953 71.917  1.00 55.55 ? 2090 HOH L O   1 
HETATM 21220 O  O   . HOH QB 5 .   ? 61.909  159.933 67.687  1.00 62.50 ? 2091 HOH L O   1 
HETATM 21221 O  O   . HOH QB 5 .   ? 56.474  164.629 80.467  1.00 50.07 ? 2092 HOH L O   1 
HETATM 21222 O  O   . HOH QB 5 .   ? 59.253  162.046 73.601  1.00 32.78 ? 2093 HOH L O   1 
HETATM 21223 O  O   . HOH QB 5 .   ? 53.522  165.349 78.094  1.00 63.66 ? 2094 HOH L O   1 
HETATM 21224 O  O   . HOH QB 5 .   ? 56.440  160.910 81.601  1.00 46.77 ? 2095 HOH L O   1 
HETATM 21225 O  O   . HOH QB 5 .   ? 60.394  153.892 80.293  1.00 50.94 ? 2096 HOH L O   1 
HETATM 21226 O  O   . HOH QB 5 .   ? 59.677  154.099 84.483  1.00 51.89 ? 2097 HOH L O   1 
HETATM 21227 O  O   . HOH QB 5 .   ? 54.245  159.107 80.068  1.00 42.98 ? 2098 HOH L O   1 
HETATM 21228 O  O   . HOH QB 5 .   ? 54.597  154.508 80.186  1.00 56.54 ? 2099 HOH L O   1 
HETATM 21229 O  O   . HOH QB 5 .   ? 61.748  155.077 77.942  1.00 43.24 ? 2100 HOH L O   1 
HETATM 21230 O  O   . HOH QB 5 .   ? 60.886  151.966 74.064  1.00 37.86 ? 2101 HOH L O   1 
HETATM 21231 O  O   . HOH QB 5 .   ? 56.063  149.273 72.921  1.00 34.75 ? 2102 HOH L O   1 
HETATM 21232 O  O   . HOH QB 5 .   ? 49.636  154.297 74.068  1.00 52.85 ? 2103 HOH L O   1 
HETATM 21233 O  O   . HOH QB 5 .   ? 50.811  160.145 77.492  1.00 51.70 ? 2104 HOH L O   1 
HETATM 21234 O  O   . HOH QB 5 .   ? 49.447  152.144 72.397  1.00 41.93 ? 2105 HOH L O   1 
HETATM 21235 O  O   . HOH QB 5 .   ? 53.369  148.618 72.927  1.00 41.45 ? 2106 HOH L O   1 
HETATM 21236 O  O   . HOH QB 5 .   ? 52.705  148.048 75.484  1.00 44.76 ? 2107 HOH L O   1 
HETATM 21237 O  O   . HOH QB 5 .   ? 43.858  147.864 73.343  1.00 40.48 ? 2108 HOH L O   1 
HETATM 21238 O  O   . HOH QB 5 .   ? 47.945  149.327 73.435  1.00 56.28 ? 2109 HOH L O   1 
HETATM 21239 O  O   . HOH QB 5 .   ? 52.172  145.500 75.614  1.00 35.33 ? 2110 HOH L O   1 
HETATM 21240 O  O   . HOH QB 5 .   ? 37.773  147.059 65.375  1.00 42.86 ? 2111 HOH L O   1 
HETATM 21241 O  O   . HOH QB 5 .   ? 38.978  145.854 68.612  1.00 40.77 ? 2112 HOH L O   1 
HETATM 21242 O  O   . HOH QB 5 .   ? 42.987  139.236 64.953  1.00 47.86 ? 2113 HOH L O   1 
HETATM 21243 O  O   . HOH QB 5 .   ? 45.785  136.333 62.628  1.00 36.49 ? 2114 HOH L O   1 
HETATM 21244 O  O   . HOH QB 5 .   ? 46.801  137.085 59.340  1.00 31.25 ? 2115 HOH L O   1 
HETATM 21245 O  O   . HOH RB 5 .   ? 9.021   128.183 102.530 1.00 46.48 ? 2001 HOH M O   1 
HETATM 21246 O  O   . HOH RB 5 .   ? -8.696  126.949 107.441 1.00 44.41 ? 2002 HOH M O   1 
HETATM 21247 O  O   . HOH RB 5 .   ? -14.518 127.891 102.080 1.00 65.55 ? 2003 HOH M O   1 
HETATM 21248 O  O   . HOH RB 5 .   ? -3.510  130.275 95.656  1.00 55.16 ? 2004 HOH M O   1 
HETATM 21249 O  O   . HOH RB 5 .   ? -17.036 128.478 115.169 1.00 49.76 ? 2005 HOH M O   1 
HETATM 21250 O  O   . HOH RB 5 .   ? -16.207 130.459 105.625 1.00 42.35 ? 2006 HOH M O   1 
HETATM 21251 O  O   . HOH RB 5 .   ? -10.602 129.383 100.800 1.00 58.91 ? 2007 HOH M O   1 
HETATM 21252 O  O   . HOH RB 5 .   ? 1.968   131.028 99.553  1.00 42.22 ? 2008 HOH M O   1 
HETATM 21253 O  O   . HOH RB 5 .   ? -3.137  132.941 95.798  1.00 44.42 ? 2009 HOH M O   1 
HETATM 21254 O  O   . HOH RB 5 .   ? -1.620  129.895 97.557  1.00 37.41 ? 2010 HOH M O   1 
HETATM 21255 O  O   . HOH RB 5 .   ? -23.472 143.573 109.531 1.00 59.81 ? 2011 HOH M O   1 
HETATM 21256 O  O   . HOH RB 5 .   ? 12.258  140.102 102.524 1.00 47.33 ? 2012 HOH M O   1 
HETATM 21257 O  O   . HOH RB 5 .   ? 9.481   139.834 100.644 1.00 60.66 ? 2013 HOH M O   1 
HETATM 21258 O  O   . HOH RB 5 .   ? 6.973   145.659 117.139 1.00 57.18 ? 2014 HOH M O   1 
HETATM 21259 O  O   . HOH RB 5 .   ? -5.693  134.147 96.811  1.00 44.22 ? 2015 HOH M O   1 
HETATM 21260 O  O   . HOH RB 5 .   ? -9.212  133.119 97.527  1.00 52.29 ? 2016 HOH M O   1 
HETATM 21261 O  O   . HOH RB 5 .   ? -13.084 151.320 100.978 1.00 49.99 ? 2017 HOH M O   1 
HETATM 21262 O  O   . HOH RB 5 .   ? -17.147 136.501 95.404  1.00 47.68 ? 2018 HOH M O   1 
HETATM 21263 O  O   . HOH RB 5 .   ? -19.787 138.773 105.636 1.00 42.68 ? 2019 HOH M O   1 
HETATM 21264 O  O   . HOH RB 5 .   ? -18.105 140.838 106.425 1.00 37.75 ? 2020 HOH M O   1 
HETATM 21265 O  O   . HOH RB 5 .   ? -18.160 146.884 106.005 1.00 45.36 ? 2021 HOH M O   1 
HETATM 21266 O  O   . HOH RB 5 .   ? -21.275 144.977 101.018 1.00 48.34 ? 2022 HOH M O   1 
HETATM 21267 O  O   . HOH RB 5 .   ? -15.258 150.874 105.946 1.00 41.65 ? 2023 HOH M O   1 
HETATM 21268 O  O   . HOH RB 5 .   ? -21.358 141.656 109.082 1.00 62.11 ? 2024 HOH M O   1 
HETATM 21269 O  O   . HOH RB 5 .   ? -16.566 150.155 112.770 1.00 52.23 ? 2025 HOH M O   1 
HETATM 21270 O  O   . HOH RB 5 .   ? -14.265 152.217 115.372 1.00 47.00 ? 2026 HOH M O   1 
HETATM 21271 O  O   . HOH RB 5 .   ? -4.250  158.064 119.954 1.00 37.16 ? 2027 HOH M O   1 
HETATM 21272 O  O   . HOH RB 5 .   ? -5.735  159.203 117.835 1.00 37.31 ? 2028 HOH M O   1 
HETATM 21273 O  O   . HOH RB 5 .   ? -1.909  134.976 125.757 1.00 48.44 ? 2029 HOH M O   1 
HETATM 21274 O  O   . HOH RB 5 .   ? 2.506   132.256 122.137 1.00 51.32 ? 2030 HOH M O   1 
HETATM 21275 O  O   . HOH RB 5 .   ? -5.693  124.354 115.362 1.00 36.54 ? 2031 HOH M O   1 
HETATM 21276 O  O   . HOH RB 5 .   ? -4.634  127.191 122.828 1.00 45.60 ? 2032 HOH M O   1 
HETATM 21277 O  O   . HOH RB 5 .   ? -8.496  129.680 115.500 1.00 60.10 ? 2033 HOH M O   1 
HETATM 21278 O  O   . HOH RB 5 .   ? -9.924  124.066 111.191 1.00 41.19 ? 2034 HOH M O   1 
HETATM 21279 O  O   . HOH RB 5 .   ? -8.305  127.003 111.173 1.00 45.40 ? 2035 HOH M O   1 
HETATM 21280 O  O   . HOH RB 5 .   ? -7.522  128.400 113.180 1.00 57.28 ? 2036 HOH M O   1 
HETATM 21281 O  O   . HOH RB 5 .   ? -19.224 135.339 108.540 1.00 51.22 ? 2037 HOH M O   1 
HETATM 21282 O  O   . HOH RB 5 .   ? -14.976 130.353 114.039 1.00 49.08 ? 2038 HOH M O   1 
HETATM 21283 O  O   . HOH RB 5 .   ? -14.905 130.620 117.916 1.00 54.61 ? 2039 HOH M O   1 
HETATM 21284 O  O   . HOH RB 5 .   ? -8.678  136.563 122.842 1.00 44.13 ? 2040 HOH M O   1 
HETATM 21285 O  O   . HOH RB 5 .   ? -9.045  140.927 117.791 1.00 44.78 ? 2041 HOH M O   1 
HETATM 21286 O  O   . HOH RB 5 .   ? 4.246   142.732 120.456 1.00 48.16 ? 2042 HOH M O   1 
HETATM 21287 O  O   . HOH RB 5 .   ? 1.553   137.280 122.188 1.00 47.94 ? 2043 HOH M O   1 
HETATM 21288 O  O   . HOH RB 5 .   ? -0.891  152.436 110.549 1.00 36.54 ? 2044 HOH M O   1 
HETATM 21289 O  O   . HOH RB 5 .   ? -2.658  154.296 114.383 1.00 40.66 ? 2045 HOH M O   1 
HETATM 21290 O  O   . HOH RB 5 .   ? 3.100   156.404 115.012 1.00 48.56 ? 2046 HOH M O   1 
HETATM 21291 O  O   . HOH RB 5 .   ? 3.706   154.665 118.275 1.00 47.52 ? 2047 HOH M O   1 
HETATM 21292 O  O   . HOH RB 5 .   ? -0.528  152.531 119.109 1.00 47.47 ? 2048 HOH M O   1 
HETATM 21293 O  O   . HOH RB 5 .   ? 6.649   151.625 120.951 1.00 58.16 ? 2049 HOH M O   1 
HETATM 21294 O  O   . HOH RB 5 .   ? 5.376   144.841 118.849 1.00 48.53 ? 2050 HOH M O   1 
HETATM 21295 O  O   . HOH RB 5 .   ? -3.025  145.142 124.193 1.00 41.91 ? 2051 HOH M O   1 
HETATM 21296 O  O   . HOH RB 5 .   ? -3.494  147.321 106.257 1.00 41.10 ? 2052 HOH M O   1 
HETATM 21297 O  O   . HOH RB 5 .   ? -10.517 151.337 102.111 1.00 31.21 ? 2053 HOH M O   1 
HETATM 21298 O  O   . HOH RB 5 .   ? -14.421 149.348 98.945  1.00 49.79 ? 2054 HOH M O   1 
HETATM 21299 O  O   . HOH RB 5 .   ? -14.097 141.991 92.664  1.00 53.14 ? 2055 HOH M O   1 
HETATM 21300 O  O   . HOH RB 5 .   ? -13.633 145.510 92.515  1.00 58.46 ? 2056 HOH M O   1 
HETATM 21301 O  O   . HOH RB 5 .   ? -16.268 148.464 94.597  1.00 48.14 ? 2057 HOH M O   1 
HETATM 21302 O  O   . HOH RB 5 .   ? -17.932 138.026 97.605  1.00 43.86 ? 2058 HOH M O   1 
HETATM 21303 O  O   . HOH RB 5 .   ? -11.015 144.033 95.122  1.00 40.01 ? 2059 HOH M O   1 
HETATM 21304 O  O   . HOH RB 5 .   ? -4.823  144.284 95.543  1.00 42.38 ? 2060 HOH M O   1 
HETATM 21305 O  O   . HOH RB 5 .   ? -3.962  140.648 95.973  1.00 45.58 ? 2061 HOH M O   1 
HETATM 21306 O  O   . HOH RB 5 .   ? -1.325  148.239 100.792 1.00 51.59 ? 2062 HOH M O   1 
HETATM 21307 O  O   . HOH RB 5 .   ? 0.352   142.206 95.645  1.00 62.16 ? 2063 HOH M O   1 
HETATM 21308 O  O   . HOH RB 5 .   ? 1.452   147.661 102.918 1.00 42.33 ? 2064 HOH M O   1 
HETATM 21309 O  O   . HOH RB 5 .   ? 2.490   147.028 107.011 1.00 43.89 ? 2065 HOH M O   1 
HETATM 21310 O  O   . HOH RB 5 .   ? 11.666  142.534 110.377 1.00 38.08 ? 2066 HOH M O   1 
HETATM 21311 O  O   . HOH RB 5 .   ? 12.560  144.509 109.690 1.00 50.86 ? 2067 HOH M O   1 
HETATM 21312 O  O   . HOH RB 5 .   ? 6.254   147.538 108.419 1.00 49.99 ? 2068 HOH M O   1 
HETATM 21313 O  O   . HOH RB 5 .   ? 7.769   146.825 105.025 1.00 52.53 ? 2069 HOH M O   1 
HETATM 21314 O  O   . HOH RB 5 .   ? 13.305  135.709 108.530 1.00 55.44 ? 2070 HOH M O   1 
HETATM 21315 O  O   . HOH RB 5 .   ? 11.518  137.996 114.123 1.00 53.01 ? 2071 HOH M O   1 
HETATM 21316 O  O   . HOH RB 5 .   ? 7.111   133.507 117.439 1.00 50.29 ? 2072 HOH M O   1 
HETATM 21317 O  O   . HOH RB 5 .   ? -18.932 142.555 108.450 1.00 38.05 ? 2073 HOH M O   1 
HETATM 21318 O  O   . HOH RB 5 .   ? -14.509 149.574 114.487 1.00 38.35 ? 2074 HOH M O   1 
HETATM 21319 O  O   . HOH RB 5 .   ? -16.653 148.807 110.451 1.00 42.67 ? 2075 HOH M O   1 
HETATM 21320 O  O   . HOH RB 5 .   ? -3.702  146.853 113.223 1.00 33.30 ? 2076 HOH M O   1 
HETATM 21321 O  O   . HOH RB 5 .   ? -8.336  154.919 113.108 1.00 41.38 ? 2077 HOH M O   1 
HETATM 21322 O  O   . HOH RB 5 .   ? -2.867  155.786 119.968 1.00 45.35 ? 2078 HOH M O   1 
HETATM 21323 O  O   . HOH RB 5 .   ? -7.086  155.234 121.642 1.00 34.48 ? 2079 HOH M O   1 
HETATM 21324 O  O   . HOH RB 5 .   ? -4.185  161.161 113.612 1.00 44.93 ? 2080 HOH M O   1 
HETATM 21325 O  O   . HOH RB 5 .   ? -8.290  159.412 119.021 1.00 36.52 ? 2081 HOH M O   1 
HETATM 21326 O  O   . HOH RB 5 .   ? -15.878 148.447 124.356 1.00 46.63 ? 2082 HOH M O   1 
HETATM 21327 O  O   . HOH RB 5 .   ? -16.175 151.733 125.095 1.00 32.50 ? 2083 HOH M O   1 
HETATM 21328 O  O   . HOH RB 5 .   ? -15.216 145.773 124.663 1.00 49.67 ? 2084 HOH M O   1 
HETATM 21329 O  O   . HOH RB 5 .   ? -13.853 149.440 125.844 1.00 37.81 ? 2085 HOH M O   1 
HETATM 21330 O  O   . HOH RB 5 .   ? -5.581  141.464 121.219 1.00 40.66 ? 2086 HOH M O   1 
HETATM 21331 O  O   . HOH RB 5 .   ? -11.963 141.902 117.963 1.00 43.53 ? 2087 HOH M O   1 
HETATM 21332 O  O   . HOH RB 5 .   ? -13.733 144.639 119.141 1.00 49.61 ? 2088 HOH M O   1 
HETATM 21333 O  O   . HOH RB 5 .   ? -15.808 136.155 117.010 1.00 42.28 ? 2089 HOH M O   1 
HETATM 21334 O  O   . HOH RB 5 .   ? -7.762  139.791 120.140 1.00 37.61 ? 2090 HOH M O   1 
HETATM 21335 O  O   . HOH RB 5 .   ? -11.610 139.268 118.975 1.00 46.78 ? 2091 HOH M O   1 
HETATM 21336 O  O   . HOH RB 5 .   ? -9.436  139.268 122.208 1.00 50.43 ? 2092 HOH M O   1 
HETATM 21337 O  O   . HOH RB 5 .   ? -18.476 136.157 113.376 1.00 56.58 ? 2093 HOH M O   1 
HETATM 21338 O  O   . HOH RB 5 .   ? -17.595 133.667 107.720 1.00 42.34 ? 2094 HOH M O   1 
HETATM 21339 O  O   . HOH RB 5 .   ? -17.410 132.861 111.315 1.00 47.74 ? 2095 HOH M O   1 
HETATM 21340 O  O   . HOH RB 5 .   ? -10.304 127.848 109.679 1.00 52.36 ? 2096 HOH M O   1 
HETATM 21341 O  O   . HOH RB 5 .   ? -4.320  127.370 106.671 1.00 31.04 ? 2097 HOH M O   1 
HETATM 21342 O  O   . HOH RB 5 .   ? -6.153  126.222 109.464 1.00 34.70 ? 2098 HOH M O   1 
HETATM 21343 O  O   . HOH RB 5 .   ? 4.395   127.148 97.371  1.00 53.24 ? 2099 HOH M O   1 
HETATM 21344 O  O   . HOH SB 5 .   ? -0.183  137.142 52.990  1.00 62.12 ? 2001 HOH N O   1 
HETATM 21345 O  O   . HOH SB 5 .   ? 18.758  130.934 58.498  1.00 44.56 ? 2002 HOH N O   1 
HETATM 21346 O  O   . HOH SB 5 .   ? 25.145  128.634 60.191  1.00 58.53 ? 2003 HOH N O   1 
HETATM 21347 O  O   . HOH SB 5 .   ? 31.280  122.506 62.125  1.00 42.78 ? 2004 HOH N O   1 
HETATM 21348 O  O   . HOH SB 5 .   ? 24.883  121.229 59.569  1.00 43.39 ? 2005 HOH N O   1 
HETATM 21349 O  O   . HOH SB 5 .   ? 30.918  120.841 58.269  1.00 59.90 ? 2006 HOH N O   1 
HETATM 21350 O  O   . HOH SB 5 .   ? 24.947  124.836 57.867  1.00 46.38 ? 2007 HOH N O   1 
HETATM 21351 O  O   . HOH SB 5 .   ? 22.009  126.177 50.748  1.00 60.33 ? 2008 HOH N O   1 
HETATM 21352 O  O   . HOH SB 5 .   ? 25.849  116.812 59.854  1.00 46.00 ? 2009 HOH N O   1 
HETATM 21353 O  O   . HOH SB 5 .   ? 15.268  125.333 47.002  1.00 47.54 ? 2010 HOH N O   1 
HETATM 21354 O  O   . HOH SB 5 .   ? 13.272  130.754 47.417  1.00 47.23 ? 2011 HOH N O   1 
HETATM 21355 O  O   . HOH SB 5 .   ? 9.174   130.925 48.468  1.00 49.34 ? 2012 HOH N O   1 
HETATM 21356 O  O   . HOH SB 5 .   ? 14.108  127.119 45.856  1.00 51.88 ? 2013 HOH N O   1 
HETATM 21357 O  O   . HOH SB 5 .   ? 22.929  128.082 63.212  1.00 59.69 ? 2014 HOH N O   1 
HETATM 21358 O  O   . HOH SB 5 .   ? -5.908  115.848 73.415  1.00 64.93 ? 2015 HOH N O   1 
HETATM 21359 O  O   . HOH SB 5 .   ? 25.322  115.715 57.777  1.00 41.88 ? 2016 HOH N O   1 
HETATM 21360 O  O   . HOH SB 5 .   ? 27.905  116.324 54.707  1.00 53.24 ? 2017 HOH N O   1 
HETATM 21361 O  O   . HOH SB 5 .   ? 26.362  112.613 52.035  1.00 58.71 ? 2018 HOH N O   1 
HETATM 21362 O  O   . HOH SB 5 .   ? 22.832  114.411 57.868  1.00 39.74 ? 2019 HOH N O   1 
HETATM 21363 O  O   . HOH SB 5 .   ? 24.760  104.076 50.501  1.00 50.74 ? 2020 HOH N O   1 
HETATM 21364 O  O   . HOH SB 5 .   ? 25.611  109.006 53.856  1.00 53.29 ? 2021 HOH N O   1 
HETATM 21365 O  O   . HOH SB 5 .   ? 19.367  106.332 48.162  1.00 59.49 ? 2022 HOH N O   1 
HETATM 21366 O  O   . HOH SB 5 .   ? 16.687  106.208 56.348  1.00 46.81 ? 2023 HOH N O   1 
HETATM 21367 O  O   . HOH SB 5 .   ? 18.634  108.732 58.955  1.00 47.77 ? 2024 HOH N O   1 
HETATM 21368 O  O   . HOH SB 5 .   ? 24.962  114.437 61.411  1.00 52.41 ? 2025 HOH N O   1 
HETATM 21369 O  O   . HOH SB 5 .   ? 9.845   102.986 63.155  1.00 56.94 ? 2026 HOH N O   1 
HETATM 21370 O  O   . HOH SB 5 .   ? 4.027   130.052 70.662  1.00 52.82 ? 2027 HOH N O   1 
HETATM 21371 O  O   . HOH SB 5 .   ? 15.702  134.470 65.832  1.00 40.53 ? 2028 HOH N O   1 
HETATM 21372 O  O   . HOH SB 5 .   ? 16.471  128.650 65.810  1.00 48.00 ? 2029 HOH N O   1 
HETATM 21373 O  O   . HOH SB 5 .   ? 15.174  135.154 73.205  1.00 50.63 ? 2030 HOH N O   1 
HETATM 21374 O  O   . HOH SB 5 .   ? 12.472  132.361 72.714  1.00 51.16 ? 2031 HOH N O   1 
HETATM 21375 O  O   . HOH SB 5 .   ? 17.525  131.266 62.129  1.00 48.50 ? 2032 HOH N O   1 
HETATM 21376 O  O   . HOH SB 5 .   ? 22.498  131.816 61.044  1.00 56.45 ? 2033 HOH N O   1 
HETATM 21377 O  O   . HOH SB 5 .   ? 18.968  132.803 73.889  1.00 56.98 ? 2034 HOH N O   1 
HETATM 21378 O  O   . HOH SB 5 .   ? 22.472  125.692 65.120  1.00 58.04 ? 2035 HOH N O   1 
HETATM 21379 O  O   . HOH SB 5 .   ? 15.769  122.870 72.744  1.00 44.64 ? 2036 HOH N O   1 
HETATM 21380 O  O   . HOH SB 5 .   ? 13.073  129.916 72.992  1.00 58.02 ? 2037 HOH N O   1 
HETATM 21381 O  O   . HOH SB 5 .   ? 12.631  117.762 67.661  1.00 47.97 ? 2038 HOH N O   1 
HETATM 21382 O  O   . HOH SB 5 .   ? -0.784  121.113 67.951  1.00 47.94 ? 2039 HOH N O   1 
HETATM 21383 O  O   . HOH SB 5 .   ? 0.619   110.097 67.464  1.00 49.47 ? 2040 HOH N O   1 
HETATM 21384 O  O   . HOH SB 5 .   ? 2.366   110.082 58.719  1.00 44.79 ? 2041 HOH N O   1 
HETATM 21385 O  O   . HOH SB 5 .   ? 3.209   111.214 54.483  1.00 50.45 ? 2042 HOH N O   1 
HETATM 21386 O  O   . HOH SB 5 .   ? 2.919   114.488 53.626  1.00 52.86 ? 2043 HOH N O   1 
HETATM 21387 O  O   . HOH SB 5 .   ? 2.426   107.781 62.970  1.00 49.17 ? 2044 HOH N O   1 
HETATM 21388 O  O   . HOH SB 5 .   ? -3.301  114.088 73.276  1.00 52.98 ? 2045 HOH N O   1 
HETATM 21389 O  O   . HOH SB 5 .   ? -2.235  119.242 66.315  1.00 47.03 ? 2046 HOH N O   1 
HETATM 21390 O  O   . HOH SB 5 .   ? 4.205   116.212 72.826  1.00 55.57 ? 2047 HOH N O   1 
HETATM 21391 O  O   . HOH SB 5 .   ? 7.133   113.765 55.209  1.00 40.66 ? 2048 HOH N O   1 
HETATM 21392 O  O   . HOH SB 5 .   ? 12.804  114.813 50.687  1.00 41.25 ? 2049 HOH N O   1 
HETATM 21393 O  O   . HOH SB 5 .   ? 26.400  107.889 51.030  1.00 52.71 ? 2050 HOH N O   1 
HETATM 21394 O  O   . HOH SB 5 .   ? 20.219  107.563 46.276  1.00 57.54 ? 2051 HOH N O   1 
HETATM 21395 O  O   . HOH SB 5 .   ? 25.039  117.136 49.513  1.00 47.77 ? 2052 HOH N O   1 
HETATM 21396 O  O   . HOH SB 5 .   ? 24.124  112.823 43.357  1.00 56.77 ? 2053 HOH N O   1 
HETATM 21397 O  O   . HOH SB 5 .   ? 20.714  114.576 43.414  1.00 58.99 ? 2054 HOH N O   1 
HETATM 21398 O  O   . HOH SB 5 .   ? 16.566  113.991 45.059  1.00 49.64 ? 2055 HOH N O   1 
HETATM 21399 O  O   . HOH SB 5 .   ? 15.262  113.715 47.659  1.00 35.62 ? 2056 HOH N O   1 
HETATM 21400 O  O   . HOH SB 5 .   ? 11.598  119.752 45.309  1.00 47.82 ? 2057 HOH N O   1 
HETATM 21401 O  O   . HOH SB 5 .   ? 5.204   120.339 47.078  1.00 53.35 ? 2058 HOH N O   1 
HETATM 21402 O  O   . HOH SB 5 .   ? 5.437   114.104 49.427  1.00 54.76 ? 2059 HOH N O   1 
HETATM 21403 O  O   . HOH SB 5 .   ? 3.007   115.448 50.965  1.00 42.27 ? 2060 HOH N O   1 
HETATM 21404 O  O   . HOH SB 5 .   ? 1.357   116.481 54.854  1.00 53.06 ? 2061 HOH N O   1 
HETATM 21405 O  O   . HOH SB 5 .   ? -5.739  124.051 56.725  1.00 48.52 ? 2062 HOH N O   1 
HETATM 21406 O  O   . HOH SB 5 .   ? -2.660  118.500 52.112  1.00 60.90 ? 2063 HOH N O   1 
HETATM 21407 O  O   . HOH SB 5 .   ? -4.257  128.696 61.042  1.00 61.45 ? 2064 HOH N O   1 
HETATM 21408 O  O   . HOH SB 5 .   ? 0.413   130.714 64.984  1.00 54.97 ? 2065 HOH N O   1 
HETATM 21409 O  O   . HOH SB 5 .   ? 22.702  112.840 60.125  1.00 45.44 ? 2066 HOH N O   1 
HETATM 21410 O  O   . HOH SB 5 .   ? 17.629  107.379 61.069  1.00 51.75 ? 2067 HOH N O   1 
HETATM 21411 O  O   . HOH SB 5 .   ? 14.826  107.398 64.391  1.00 52.24 ? 2068 HOH N O   1 
HETATM 21412 O  O   . HOH SB 5 .   ? 6.305   114.275 62.102  1.00 37.47 ? 2069 HOH N O   1 
HETATM 21413 O  O   . HOH SB 5 .   ? 10.250  106.423 60.530  1.00 58.59 ? 2070 HOH N O   1 
HETATM 21414 O  O   . HOH SB 5 .   ? 8.158   104.865 62.481  1.00 50.09 ? 2071 HOH N O   1 
HETATM 21415 O  O   . HOH SB 5 .   ? 4.912   105.237 70.563  1.00 38.94 ? 2072 HOH N O   1 
HETATM 21416 O  O   . HOH SB 5 .   ? 4.635   100.883 67.602  1.00 56.51 ? 2073 HOH N O   1 
HETATM 21417 O  O   . HOH SB 5 .   ? 14.868  107.557 74.768  1.00 55.24 ? 2074 HOH N O   1 
HETATM 21418 O  O   . HOH SB 5 .   ? 12.427  107.776 75.794  1.00 53.87 ? 2075 HOH N O   1 
HETATM 21419 O  O   . HOH SB 5 .   ? 12.097  114.383 74.428  1.00 59.55 ? 2076 HOH N O   1 
HETATM 21420 O  O   . HOH SB 5 .   ? 8.612   118.529 70.588  1.00 44.36 ? 2077 HOH N O   1 
HETATM 21421 O  O   . HOH SB 5 .   ? 12.949  113.148 79.066  1.00 64.15 ? 2078 HOH N O   1 
HETATM 21422 O  O   . HOH SB 5 .   ? 14.988  115.824 68.409  1.00 48.09 ? 2079 HOH N O   1 
HETATM 21423 O  O   . HOH SB 5 .   ? 20.521  119.552 68.375  1.00 43.68 ? 2080 HOH N O   1 
HETATM 21424 O  O   . HOH SB 5 .   ? 13.055  121.992 72.935  1.00 44.22 ? 2081 HOH N O   1 
HETATM 21425 O  O   . HOH SB 5 .   ? 11.211  119.230 69.950  1.00 49.56 ? 2082 HOH N O   1 
HETATM 21426 O  O   . HOH SB 5 .   ? 22.983  123.187 64.188  1.00 53.31 ? 2083 HOH N O   1 
HETATM 21427 O  O   . HOH SB 5 .   ? 12.956  119.176 72.336  1.00 54.31 ? 2084 HOH N O   1 
HETATM 21428 O  O   . HOH SB 5 .   ? 15.639  118.281 69.446  1.00 58.64 ? 2085 HOH N O   1 
HETATM 21429 O  O   . HOH SB 5 .   ? 19.424  129.765 60.838  1.00 43.36 ? 2086 HOH N O   1 
HETATM 21430 O  O   . HOH SB 5 .   ? 16.483  132.580 59.442  1.00 38.55 ? 2087 HOH N O   1 
HETATM 21431 O  O   . HOH SB 5 .   ? 15.094  132.029 56.749  1.00 33.14 ? 2088 HOH N O   1 
HETATM 21432 O  O   . HOH SB 5 .   ? 3.302   136.248 50.665  1.00 53.57 ? 2089 HOH N O   1 
HETATM 21433 O  O   . HOH SB 5 .   ? 9.715   135.499 46.041  1.00 53.90 ? 2090 HOH N O   1 
HETATM 21434 O  O   . HOH TB 5 .   ? 43.627  126.115 105.160 1.00 46.74 ? 2001 HOH O O   1 
HETATM 21435 O  O   . HOH TB 5 .   ? 55.077  114.697 110.923 1.00 46.72 ? 2002 HOH O O   1 
HETATM 21436 O  O   . HOH TB 5 .   ? 45.683  124.107 106.434 1.00 46.87 ? 2003 HOH O O   1 
HETATM 21437 O  O   . HOH TB 5 .   ? 50.805  122.327 101.065 1.00 55.42 ? 2004 HOH O O   1 
HETATM 21438 O  O   . HOH TB 5 .   ? 51.977  117.539 113.308 1.00 54.27 ? 2005 HOH O O   1 
HETATM 21439 O  O   . HOH TB 5 .   ? 53.808  116.956 110.196 1.00 50.70 ? 2006 HOH O O   1 
HETATM 21440 O  O   . HOH TB 5 .   ? 53.310  120.809 108.109 1.00 49.24 ? 2007 HOH O O   1 
HETATM 21441 O  O   . HOH TB 5 .   ? 44.269  122.759 94.036  1.00 57.77 ? 2008 HOH O O   1 
HETATM 21442 O  O   . HOH TB 5 .   ? 53.915  116.564 97.287  1.00 60.35 ? 2009 HOH O O   1 
HETATM 21443 O  O   . HOH TB 5 .   ? 54.315  103.174 96.720  1.00 62.42 ? 2010 HOH O O   1 
HETATM 21444 O  O   . HOH TB 5 .   ? 56.085  112.585 109.172 1.00 38.82 ? 2011 HOH O O   1 
HETATM 21445 O  O   . HOH TB 5 .   ? 59.588  108.456 103.357 1.00 48.85 ? 2012 HOH O O   1 
HETATM 21446 O  O   . HOH TB 5 .   ? 55.046  110.140 108.645 1.00 40.68 ? 2013 HOH O O   1 
HETATM 21447 O  O   . HOH TB 5 .   ? 58.433  103.565 106.555 1.00 48.52 ? 2014 HOH O O   1 
HETATM 21448 O  O   . HOH TB 5 .   ? 61.669  104.778 103.475 1.00 49.83 ? 2015 HOH O O   1 
HETATM 21449 O  O   . HOH TB 5 .   ? 60.854  100.776 99.227  1.00 59.14 ? 2016 HOH O O   1 
HETATM 21450 O  O   . HOH TB 5 .   ? 52.682  100.587 105.918 1.00 44.27 ? 2017 HOH O O   1 
HETATM 21451 O  O   . HOH TB 5 .   ? 39.004  126.181 112.095 1.00 38.38 ? 2018 HOH O O   1 
HETATM 21452 O  O   . HOH TB 5 .   ? 34.438  122.596 117.620 1.00 52.48 ? 2019 HOH O O   1 
HETATM 21453 O  O   . HOH TB 5 .   ? 43.800  124.342 109.366 1.00 46.38 ? 2020 HOH O O   1 
HETATM 21454 O  O   . HOH TB 5 .   ? 41.306  121.265 112.546 1.00 53.94 ? 2021 HOH O O   1 
HETATM 21455 O  O   . HOH TB 5 .   ? 47.932  120.002 115.240 1.00 55.67 ? 2022 HOH O O   1 
HETATM 21456 O  O   . HOH TB 5 .   ? 35.826  120.283 118.320 1.00 56.45 ? 2023 HOH O O   1 
HETATM 21457 O  O   . HOH TB 5 .   ? 38.728  109.923 115.231 1.00 58.57 ? 2024 HOH O O   1 
HETATM 21458 O  O   . HOH TB 5 .   ? 28.261  107.697 108.704 1.00 53.42 ? 2025 HOH O O   1 
HETATM 21459 O  O   . HOH TB 5 .   ? 38.548  99.524  101.797 1.00 56.95 ? 2026 HOH O O   1 
HETATM 21460 O  O   . HOH TB 5 .   ? 40.406  100.662 100.726 1.00 57.47 ? 2027 HOH O O   1 
HETATM 21461 O  O   . HOH TB 5 .   ? 29.387  102.196 102.963 1.00 61.90 ? 2028 HOH O O   1 
HETATM 21462 O  O   . HOH TB 5 .   ? 33.358  98.135  109.174 1.00 55.95 ? 2029 HOH O O   1 
HETATM 21463 O  O   . HOH TB 5 .   ? 33.914  106.006 115.323 1.00 62.49 ? 2030 HOH O O   1 
HETATM 21464 O  O   . HOH TB 5 .   ? 41.733  105.261 99.960  1.00 63.46 ? 2031 HOH O O   1 
HETATM 21465 O  O   . HOH TB 5 .   ? 44.302  100.411 102.853 1.00 47.84 ? 2032 HOH O O   1 
HETATM 21466 O  O   . HOH TB 5 .   ? 42.370  102.886 101.140 1.00 55.35 ? 2033 HOH O O   1 
HETATM 21467 O  O   . HOH TB 5 .   ? 49.575  100.598 98.723  1.00 61.48 ? 2034 HOH O O   1 
HETATM 21468 O  O   . HOH TB 5 .   ? 55.628  102.847 98.962  1.00 63.83 ? 2035 HOH O O   1 
HETATM 21469 O  O   . HOH TB 5 .   ? 58.882  103.966 96.534  1.00 52.70 ? 2036 HOH O O   1 
HETATM 21470 O  O   . HOH TB 5 .   ? 47.919  106.930 97.908  1.00 52.01 ? 2037 HOH O O   1 
HETATM 21471 O  O   . HOH TB 5 .   ? 20.767  114.519 102.747 1.00 64.34 ? 2038 HOH O O   1 
HETATM 21472 O  O   . HOH TB 5 .   ? 39.006  104.135 106.644 1.00 46.93 ? 2039 HOH O O   1 
HETATM 21473 O  O   . HOH TB 5 .   ? 45.890  98.035  106.983 1.00 56.79 ? 2040 HOH O O   1 
HETATM 21474 O  O   . HOH TB 5 .   ? 45.372  97.324  114.189 1.00 48.52 ? 2041 HOH O O   1 
HETATM 21475 O  O   . HOH TB 5 .   ? 35.128  98.161  113.092 1.00 55.44 ? 2042 HOH O O   1 
HETATM 21476 O  O   . HOH TB 5 .   ? 44.735  95.882  107.243 1.00 53.62 ? 2043 HOH O O   1 
HETATM 21477 O  O   . HOH TB 5 .   ? 37.106  94.804  109.597 1.00 64.61 ? 2044 HOH O O   1 
HETATM 21478 O  O   . HOH TB 5 .   ? 41.149  99.415  121.936 1.00 56.33 ? 2045 HOH O O   1 
HETATM 21479 O  O   . HOH TB 5 .   ? 47.301  113.798 117.119 1.00 44.71 ? 2046 HOH O O   1 
HETATM 21480 O  O   . HOH TB 5 .   ? 45.997  123.187 108.787 1.00 46.96 ? 2047 HOH O O   1 
HETATM 21481 O  O   . HOH TB 5 .   ? 42.503  124.975 107.088 1.00 35.34 ? 2048 HOH O O   1 
HETATM 21482 O  O   . HOH TB 5 .   ? 42.318  124.104 103.652 1.00 36.13 ? 2049 HOH O O   1 
HETATM 21483 O  O   . HOH TB 5 .   ? 39.287  127.888 93.999  1.00 59.36 ? 2050 HOH O O   1 
HETATM 21484 O  O   . HOH UB 5 .   ? 40.141  141.915 15.174  1.00 65.46 ? 2001 HOH P O   1 
HETATM 21485 O  O   . HOH UB 5 .   ? 46.415  139.605 49.736  1.00 49.74 ? 2002 HOH P O   1 
HETATM 21486 O  O   . HOH VB 5 .   ? 56.075  139.353 109.710 1.00 54.29 ? 2001 HOH Q O   1 
HETATM 21487 O  O   . HOH VB 5 .   ? 43.784  128.996 109.041 1.00 44.52 ? 2002 HOH Q O   1 
HETATM 21488 O  O   . HOH VB 5 .   ? 32.797  128.980 121.304 1.00 61.61 ? 2003 HOH Q O   1 
HETATM 21489 O  O   . HOH VB 5 .   ? 56.538  137.541 107.537 1.00 45.56 ? 2004 HOH Q O   1 
HETATM 21490 O  O   . HOH VB 5 .   ? 48.908  137.241 104.440 1.00 55.70 ? 2005 HOH Q O   1 
HETATM 21491 O  O   . HOH VB 5 .   ? 50.136  133.825 100.784 1.00 58.01 ? 2006 HOH Q O   1 
HETATM 21492 O  O   . HOH VB 5 .   ? 53.719  134.001 108.773 1.00 63.26 ? 2007 HOH Q O   1 
HETATM 21493 O  O   . HOH VB 5 .   ? 49.771  138.720 108.827 1.00 54.06 ? 2008 HOH Q O   1 
HETATM 21494 O  O   . HOH VB 5 .   ? 49.545  135.144 110.759 1.00 48.24 ? 2009 HOH Q O   1 
HETATM 21495 O  O   . HOH VB 5 .   ? 45.823  133.884 117.344 1.00 55.91 ? 2010 HOH Q O   1 
HETATM 21496 O  O   . HOH VB 5 .   ? 50.667  143.381 108.563 1.00 54.01 ? 2011 HOH Q O   1 
HETATM 21497 O  O   . HOH VB 5 .   ? 38.590  134.376 119.984 1.00 45.95 ? 2012 HOH Q O   1 
HETATM 21498 O  O   . HOH VB 5 .   ? 33.292  128.586 117.906 1.00 54.99 ? 2013 HOH Q O   1 
HETATM 21499 O  O   . HOH VB 5 .   ? 19.599  132.605 114.372 1.00 58.67 ? 2014 HOH Q O   1 
HETATM 21500 O  O   . HOH VB 5 .   ? 27.385  152.429 105.277 1.00 54.05 ? 2015 HOH Q O   1 
HETATM 21501 O  O   . HOH VB 5 .   ? 44.340  138.313 120.017 1.00 59.92 ? 2016 HOH Q O   1 
HETATM 21502 O  O   . HOH VB 5 .   ? 49.886  144.341 110.921 1.00 46.71 ? 2017 HOH Q O   1 
HETATM 21503 O  O   . HOH VB 5 .   ? 47.620  145.587 110.108 1.00 40.46 ? 2018 HOH Q O   1 
HETATM 21504 O  O   . HOH VB 5 .   ? 48.330  155.458 118.561 1.00 48.00 ? 2019 HOH Q O   1 
HETATM 21505 O  O   . HOH VB 5 .   ? 50.036  150.460 115.073 1.00 52.32 ? 2020 HOH Q O   1 
HETATM 21506 O  O   . HOH VB 5 .   ? 42.851  153.330 119.610 1.00 55.66 ? 2021 HOH Q O   1 
HETATM 21507 O  O   . HOH VB 5 .   ? 40.860  153.739 111.267 1.00 49.01 ? 2022 HOH Q O   1 
HETATM 21508 O  O   . HOH VB 5 .   ? 43.166  151.189 109.340 1.00 54.05 ? 2023 HOH Q O   1 
HETATM 21509 O  O   . HOH VB 5 .   ? 38.162  153.963 103.831 1.00 42.04 ? 2024 HOH Q O   1 
HETATM 21510 O  O   . HOH VB 5 .   ? 32.579  153.280 108.573 1.00 47.84 ? 2025 HOH Q O   1 
HETATM 21511 O  O   . HOH VB 5 .   ? 37.867  156.112 102.122 1.00 38.08 ? 2026 HOH Q O   1 
HETATM 21512 O  O   . HOH VB 5 .   ? 27.777  155.976 97.677  1.00 50.45 ? 2027 HOH Q O   1 
HETATM 21513 O  O   . HOH VB 5 .   ? 31.112  130.014 94.842  1.00 55.06 ? 2028 HOH Q O   1 
HETATM 21514 O  O   . HOH VB 5 .   ? 42.530  131.385 101.471 1.00 42.83 ? 2029 HOH Q O   1 
HETATM 21515 O  O   . HOH VB 5 .   ? 42.863  124.993 93.424  1.00 56.13 ? 2030 HOH Q O   1 
HETATM 21516 O  O   . HOH VB 5 .   ? 43.116  150.022 97.403  1.00 59.58 ? 2031 HOH Q O   1 
HETATM 21517 O  O   . HOH VB 5 .   ? 42.089  125.515 101.160 1.00 38.66 ? 2032 HOH Q O   1 
HETATM 21518 O  O   . HOH VB 5 .   ? 43.047  128.866 105.178 1.00 47.93 ? 2033 HOH Q O   1 
HETATM 21519 O  O   . HOH VB 5 .   ? 47.008  132.096 104.573 1.00 53.14 ? 2034 HOH Q O   1 
HETATM 21520 O  O   . HOH VB 5 .   ? 47.137  126.353 105.325 1.00 60.36 ? 2035 HOH Q O   1 
HETATM 21521 O  O   . HOH VB 5 .   ? 48.130  134.410 102.559 1.00 49.15 ? 2036 HOH Q O   1 
HETATM 21522 O  O   . HOH VB 5 .   ? 42.638  137.204 94.550  1.00 50.04 ? 2037 HOH Q O   1 
HETATM 21523 O  O   . HOH VB 5 .   ? 45.364  138.494 97.895  1.00 56.01 ? 2038 HOH Q O   1 
HETATM 21524 O  O   . HOH VB 5 .   ? 40.520  130.512 93.644  1.00 53.09 ? 2039 HOH Q O   1 
HETATM 21525 O  O   . HOH VB 5 .   ? 38.767  142.176 99.119  1.00 42.21 ? 2040 HOH Q O   1 
HETATM 21526 O  O   . HOH VB 5 .   ? 25.481  138.707 97.170  1.00 55.22 ? 2041 HOH Q O   1 
HETATM 21527 O  O   . HOH VB 5 .   ? 27.199  149.538 107.047 1.00 45.72 ? 2042 HOH Q O   1 
HETATM 21528 O  O   . HOH VB 5 .   ? 27.869  151.883 102.774 1.00 44.88 ? 2043 HOH Q O   1 
HETATM 21529 O  O   . HOH VB 5 .   ? 26.440  149.397 98.234  1.00 46.08 ? 2044 HOH Q O   1 
HETATM 21530 O  O   . HOH VB 5 .   ? 23.855  140.397 98.293  1.00 50.81 ? 2045 HOH Q O   1 
HETATM 21531 O  O   . HOH VB 5 .   ? 31.200  145.871 110.843 1.00 49.75 ? 2046 HOH Q O   1 
HETATM 21532 O  O   . HOH VB 5 .   ? 40.597  146.117 123.192 1.00 55.20 ? 2047 HOH Q O   1 
HETATM 21533 O  O   . HOH VB 5 .   ? 42.384  144.771 124.617 1.00 47.02 ? 2048 HOH Q O   1 
HETATM 21534 O  O   . HOH VB 5 .   ? 47.760  142.811 119.351 1.00 62.62 ? 2049 HOH Q O   1 
HETATM 21535 O  O   . HOH VB 5 .   ? 36.077  144.993 116.131 1.00 43.71 ? 2050 HOH Q O   1 
HETATM 21536 O  O   . HOH VB 5 .   ? 33.982  139.718 121.080 1.00 49.38 ? 2051 HOH Q O   1 
HETATM 21537 O  O   . HOH VB 5 .   ? 29.181  145.656 116.326 1.00 41.65 ? 2052 HOH Q O   1 
HETATM 21538 O  O   . HOH VB 5 .   ? 25.864  143.007 110.199 1.00 49.01 ? 2053 HOH Q O   1 
HETATM 21539 O  O   . HOH VB 5 .   ? 21.958  142.192 109.677 1.00 58.75 ? 2054 HOH Q O   1 
HETATM 21540 O  O   . HOH VB 5 .   ? 26.827  128.922 99.478  1.00 52.17 ? 2055 HOH Q O   1 
HETATM 21541 O  O   . HOH VB 5 .   ? 41.425  130.190 103.388 1.00 48.26 ? 2056 HOH Q O   1 
HETATM 21542 O  O   . HOH VB 5 .   ? 47.465  147.326 107.950 1.00 41.18 ? 2057 HOH Q O   1 
HETATM 21543 O  O   . HOH VB 5 .   ? 40.443  152.360 102.262 1.00 47.52 ? 2058 HOH Q O   1 
HETATM 21544 O  O   . HOH VB 5 .   ? 42.824  152.315 106.468 1.00 50.59 ? 2059 HOH Q O   1 
HETATM 21545 O  O   . HOH VB 5 .   ? 31.718  145.397 103.954 1.00 35.13 ? 2060 HOH Q O   1 
HETATM 21546 O  O   . HOH VB 5 .   ? 34.882  153.462 106.339 1.00 53.55 ? 2061 HOH Q O   1 
HETATM 21547 O  O   . HOH VB 5 .   ? 37.993  155.168 99.480  1.00 34.63 ? 2062 HOH Q O   1 
HETATM 21548 O  O   . HOH VB 5 .   ? 33.423  155.085 104.081 1.00 37.69 ? 2063 HOH Q O   1 
HETATM 21549 O  O   . HOH VB 5 .   ? 31.126  154.575 95.600  1.00 30.69 ? 2064 HOH Q O   1 
HETATM 21550 O  O   . HOH VB 5 .   ? 27.314  153.149 97.503  1.00 57.29 ? 2065 HOH Q O   1 
HETATM 21551 O  O   . HOH VB 5 .   ? 30.664  158.910 98.399  1.00 44.31 ? 2066 HOH Q O   1 
HETATM 21552 O  O   . HOH VB 5 .   ? 26.629  158.618 103.840 1.00 45.91 ? 2067 HOH Q O   1 
HETATM 21553 O  O   . HOH VB 5 .   ? 41.801  151.736 92.163  1.00 41.54 ? 2068 HOH Q O   1 
HETATM 21554 O  O   . HOH VB 5 .   ? 39.218  151.965 90.960  1.00 36.13 ? 2069 HOH Q O   1 
HETATM 21555 O  O   . HOH VB 5 .   ? 30.951  144.137 93.030  1.00 53.02 ? 2070 HOH Q O   1 
HETATM 21556 O  O   . HOH VB 5 .   ? 35.140  141.465 95.809  1.00 42.42 ? 2071 HOH Q O   1 
HETATM 21557 O  O   . HOH VB 5 .   ? 39.268  148.191 89.931  1.00 59.15 ? 2072 HOH Q O   1 
HETATM 21558 O  O   . HOH VB 5 .   ? 41.285  146.964 97.624  1.00 46.00 ? 2073 HOH Q O   1 
HETATM 21559 O  O   . HOH VB 5 .   ? 41.976  152.900 94.978  1.00 46.68 ? 2074 HOH Q O   1 
HETATM 21560 O  O   . HOH VB 5 .   ? 40.895  144.135 98.863  1.00 41.47 ? 2075 HOH Q O   1 
HETATM 21561 O  O   . HOH VB 5 .   ? 37.820  140.633 96.718  1.00 43.48 ? 2076 HOH Q O   1 
HETATM 21562 O  O   . HOH VB 5 .   ? 46.706  140.385 99.626  1.00 45.65 ? 2077 HOH Q O   1 
HETATM 21563 O  O   . HOH VB 5 .   ? 40.178  137.865 94.096  1.00 52.07 ? 2078 HOH Q O   1 
HETATM 21564 O  O   . HOH VB 5 .   ? 39.370  140.943 94.635  1.00 53.18 ? 2079 HOH Q O   1 
HETATM 21565 O  O   . HOH VB 5 .   ? 41.713  141.707 97.763  1.00 59.49 ? 2080 HOH Q O   1 
HETATM 21566 O  O   . HOH VB 5 .   ? 44.888  130.316 106.780 1.00 46.03 ? 2081 HOH Q O   1 
HETATM 21567 O  O   . HOH VB 5 .   ? 39.696  127.801 110.155 1.00 34.88 ? 2082 HOH Q O   1 
HETATM 21568 O  O   . HOH VB 5 .   ? 41.627  127.430 107.824 1.00 38.46 ? 2083 HOH Q O   1 
HETATM 21569 O  O   . HOH WB 5 .   ? 44.972  114.749 16.902  1.00 62.07 ? 2001 HOH S O   1 
HETATM 21570 O  O   . HOH WB 5 .   ? 64.948  115.831 27.432  1.00 53.38 ? 2002 HOH S O   1 
HETATM 21571 O  O   . HOH WB 5 .   ? 49.590  109.819 15.951  1.00 60.63 ? 2003 HOH S O   1 
HETATM 21572 O  O   . HOH WB 5 .   ? 50.046  122.970 11.565  1.00 55.11 ? 2004 HOH S O   1 
HETATM 21573 O  O   . HOH WB 5 .   ? 67.421  129.967 20.415  1.00 53.20 ? 2005 HOH S O   1 
HETATM 21574 O  O   . HOH WB 5 .   ? 66.585  126.824 12.392  1.00 55.34 ? 2006 HOH S O   1 
HETATM 21575 O  O   . HOH WB 5 .   ? 62.931  115.065 25.612  1.00 49.77 ? 2007 HOH S O   1 
HETATM 21576 O  O   . HOH WB 5 .   ? 51.297  110.232 13.536  1.00 63.54 ? 2008 HOH S O   1 
HETATM 21577 O  O   . HOH WB 5 .   ? 64.337  118.570 19.383  1.00 52.68 ? 2009 HOH S O   1 
HETATM 21578 O  O   . HOH WB 5 .   ? 65.070  110.724 13.734  1.00 75.41 ? 2010 HOH S O   1 
HETATM 21579 O  O   . HOH WB 5 .   ? 74.482  113.958 10.899  1.00 60.01 ? 2011 HOH S O   1 
HETATM 21580 O  O   . HOH WB 5 .   ? 71.209  118.451 1.624   1.00 52.37 ? 2012 HOH S O   1 
HETATM 21581 O  O   . HOH WB 5 .   ? 70.972  121.796 3.770   1.00 50.34 ? 2013 HOH S O   1 
HETATM 21582 O  O   . HOH WB 5 .   ? 65.026  120.145 3.044   1.00 50.81 ? 2014 HOH S O   1 
HETATM 21583 O  O   . HOH WB 5 .   ? 61.546  125.960 13.311  1.00 49.54 ? 2015 HOH S O   1 
HETATM 21584 O  O   . HOH WB 5 .   ? 58.839  118.658 9.265   1.00 64.52 ? 2016 HOH S O   1 
HETATM 21585 O  O   . HOH WB 5 .   ? 60.799  112.129 10.682  1.00 57.42 ? 2017 HOH S O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   1   1   ALA ALA A . n 
A 1 2   THR 2   2   2   THR THR A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   ALA 4   4   4   ALA ALA A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   CYS 6   6   6   CYS CYS A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  TRP 32  32  32  TRP TRP A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  HIS 43  43  43  HIS HIS A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  HIS 46  46  46  HIS HIS A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  HIS 48  48  48  HIS HIS A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  PHE 50  50  50  PHE PHE A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  CYS 57  57  57  CYS CYS A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  PRO 62  62  62  PRO PRO A . n 
A 1 63  HIS 63  63  63  HIS HIS A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 HIS 110 110 110 HIS HIS A . n 
A 1 111 CYS 111 111 111 CYS CYS A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 CYS 146 146 146 CYS CYS A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 GLN 153 153 153 GLN GLN A . n 
B 1 1   ALA 1   1   1   ALA ALA B . n 
B 1 2   THR 2   2   2   THR THR B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   ALA 4   4   4   ALA ALA B . n 
B 1 5   VAL 5   5   5   VAL VAL B . n 
B 1 6   CYS 6   6   6   CYS CYS B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   LEU 8   8   8   LEU LEU B . n 
B 1 9   LYS 9   9   9   LYS LYS B . n 
B 1 10  GLY 10  10  10  GLY GLY B . n 
B 1 11  ASP 11  11  11  ASP ASP B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  PRO 13  13  13  PRO PRO B . n 
B 1 14  VAL 14  14  14  VAL VAL B . n 
B 1 15  GLN 15  15  15  GLN GLN B . n 
B 1 16  GLY 16  16  16  GLY GLY B . n 
B 1 17  ILE 17  17  17  ILE ILE B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  ASN 19  19  19  ASN ASN B . n 
B 1 20  PHE 20  20  20  PHE PHE B . n 
B 1 21  GLU 21  21  21  GLU GLU B . n 
B 1 22  GLN 22  22  22  GLN GLN B . n 
B 1 23  LYS 23  23  23  LYS LYS B . n 
B 1 24  GLU 24  24  24  GLU GLU B . n 
B 1 25  SER 25  25  25  SER SER B . n 
B 1 26  ASN 26  26  26  ASN ASN B . n 
B 1 27  GLY 27  27  27  GLY GLY B . n 
B 1 28  PRO 28  28  28  PRO PRO B . n 
B 1 29  VAL 29  29  29  VAL VAL B . n 
B 1 30  LYS 30  30  30  LYS LYS B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  TRP 32  32  32  TRP TRP B . n 
B 1 33  GLY 33  33  33  GLY GLY B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  ILE 35  35  35  ILE ILE B . n 
B 1 36  LYS 36  36  36  LYS LYS B . n 
B 1 37  GLY 37  37  37  GLY GLY B . n 
B 1 38  LEU 38  38  38  LEU LEU B . n 
B 1 39  THR 39  39  39  THR THR B . n 
B 1 40  GLU 40  40  40  GLU GLU B . n 
B 1 41  GLY 41  41  41  GLY GLY B . n 
B 1 42  LEU 42  42  42  LEU LEU B . n 
B 1 43  HIS 43  43  43  HIS HIS B . n 
B 1 44  GLY 44  44  44  GLY GLY B . n 
B 1 45  PHE 45  45  45  PHE PHE B . n 
B 1 46  HIS 46  46  46  HIS HIS B . n 
B 1 47  VAL 47  47  47  VAL VAL B . n 
B 1 48  HIS 48  48  48  HIS HIS B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  PHE 50  50  50  PHE PHE B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  THR 54  54  54  THR THR B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  GLY 56  56  56  GLY GLY B . n 
B 1 57  CYS 57  57  57  CYS CYS B . n 
B 1 58  THR 58  58  58  THR THR B . n 
B 1 59  SER 59  59  59  SER SER B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  PRO 62  62  62  PRO PRO B . n 
B 1 63  HIS 63  63  63  HIS HIS B . n 
B 1 64  PHE 64  64  64  PHE PHE B . n 
B 1 65  ASN 65  65  65  ASN ASN B . n 
B 1 66  PRO 66  66  66  PRO PRO B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  SER 68  68  68  SER SER B . n 
B 1 69  ARG 69  69  69  ARG ARG B . n 
B 1 70  LYS 70  70  70  LYS LYS B . n 
B 1 71  HIS 71  71  71  HIS HIS B . n 
B 1 72  GLY 72  72  72  GLY GLY B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LYS 75  75  75  LYS LYS B . n 
B 1 76  ASP 76  76  76  ASP ASP B . n 
B 1 77  GLU 77  77  77  GLU GLU B . n 
B 1 78  GLU 78  78  78  GLU GLU B . n 
B 1 79  ARG 79  79  79  ARG ARG B . n 
B 1 80  HIS 80  80  80  HIS HIS B . n 
B 1 81  VAL 81  81  81  VAL VAL B . n 
B 1 82  GLY 82  82  82  GLY GLY B . n 
B 1 83  ASP 83  83  83  ASP ASP B . n 
B 1 84  LEU 84  84  84  LEU LEU B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  ASN 86  86  86  ASN ASN B . n 
B 1 87  VAL 87  87  87  VAL VAL B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  ASP 90  90  90  ASP ASP B . n 
B 1 91  LYS 91  91  91  LYS LYS B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  GLY 93  93  93  GLY GLY B . n 
B 1 94  VAL 94  94  94  VAL VAL B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  ASP 96  96  96  ASP ASP B . n 
B 1 97  VAL 97  97  97  VAL VAL B . n 
B 1 98  SER 98  98  98  SER SER B . n 
B 1 99  ILE 99  99  99  ILE ILE B . n 
B 1 100 GLU 100 100 100 GLU GLU B . n 
B 1 101 ASP 101 101 101 ASP ASP B . n 
B 1 102 SER 102 102 102 SER SER B . n 
B 1 103 VAL 103 103 103 VAL VAL B . n 
B 1 104 ILE 104 104 104 ILE ILE B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 SER 107 107 107 SER SER B . n 
B 1 108 GLY 108 108 108 GLY GLY B . n 
B 1 109 ASP 109 109 109 ASP ASP B . n 
B 1 110 HIS 110 110 110 HIS HIS B . n 
B 1 111 CYS 111 111 111 CYS CYS B . n 
B 1 112 ILE 112 112 112 ILE ILE B . n 
B 1 113 ILE 113 113 113 ILE ILE B . n 
B 1 114 GLY 114 114 114 GLY GLY B . n 
B 1 115 ARG 115 115 115 ARG ARG B . n 
B 1 116 THR 116 116 116 THR THR B . n 
B 1 117 LEU 117 117 117 LEU LEU B . n 
B 1 118 VAL 118 118 118 VAL VAL B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 HIS 120 120 120 HIS HIS B . n 
B 1 121 GLU 121 121 121 GLU GLU B . n 
B 1 122 LYS 122 122 122 LYS LYS B . n 
B 1 123 ALA 123 123 123 ALA ALA B . n 
B 1 124 ASP 124 124 124 ASP ASP B . n 
B 1 125 ASP 125 125 125 ASP ASP B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 GLY 127 127 127 GLY GLY B . n 
B 1 128 LYS 128 128 128 LYS LYS B . n 
B 1 129 GLY 129 129 129 GLY GLY B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ASN 131 131 131 ASN ASN B . n 
B 1 132 GLU 132 132 132 GLU GLU B . n 
B 1 133 GLU 133 133 133 GLU GLU B . n 
B 1 134 SER 134 134 134 SER SER B . n 
B 1 135 THR 135 135 135 THR THR B . n 
B 1 136 LYS 136 136 136 LYS LYS B . n 
B 1 137 THR 137 137 137 THR THR B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 ASN 139 139 139 ASN ASN B . n 
B 1 140 ALA 140 140 140 ALA ALA B . n 
B 1 141 GLY 141 141 141 GLY GLY B . n 
B 1 142 SER 142 142 142 SER SER B . n 
B 1 143 ARG 143 143 143 ARG ARG B . n 
B 1 144 LEU 144 144 144 LEU LEU B . n 
B 1 145 ALA 145 145 145 ALA ALA B . n 
B 1 146 CYS 146 146 146 CYS CYS B . n 
B 1 147 GLY 147 147 147 GLY GLY B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 ILE 149 149 149 ILE ILE B . n 
B 1 150 GLY 150 150 150 GLY GLY B . n 
B 1 151 ILE 151 151 151 ILE ILE B . n 
B 1 152 ALA 152 152 152 ALA ALA B . n 
B 1 153 GLN 153 153 153 GLN GLN B . n 
C 1 1   ALA 1   1   1   ALA ALA C . n 
C 1 2   THR 2   2   2   THR THR C . n 
C 1 3   LYS 3   3   3   LYS LYS C . n 
C 1 4   ALA 4   4   4   ALA ALA C . n 
C 1 5   VAL 5   5   5   VAL VAL C . n 
C 1 6   CYS 6   6   6   CYS CYS C . n 
C 1 7   VAL 7   7   7   VAL VAL C . n 
C 1 8   LEU 8   8   8   LEU LEU C . n 
C 1 9   LYS 9   9   9   LYS LYS C . n 
C 1 10  GLY 10  10  10  GLY GLY C . n 
C 1 11  ASP 11  11  11  ASP ASP C . n 
C 1 12  GLY 12  12  12  GLY GLY C . n 
C 1 13  PRO 13  13  13  PRO PRO C . n 
C 1 14  VAL 14  14  14  VAL VAL C . n 
C 1 15  GLN 15  15  15  GLN GLN C . n 
C 1 16  GLY 16  16  16  GLY GLY C . n 
C 1 17  ILE 17  17  17  ILE ILE C . n 
C 1 18  ILE 18  18  18  ILE ILE C . n 
C 1 19  ASN 19  19  19  ASN ASN C . n 
C 1 20  PHE 20  20  20  PHE PHE C . n 
C 1 21  GLU 21  21  21  GLU GLU C . n 
C 1 22  GLN 22  22  22  GLN GLN C . n 
C 1 23  LYS 23  23  23  LYS LYS C . n 
C 1 24  GLU 24  24  24  GLU GLU C . n 
C 1 25  SER 25  25  25  SER SER C . n 
C 1 26  ASN 26  26  26  ASN ASN C . n 
C 1 27  GLY 27  27  27  GLY GLY C . n 
C 1 28  PRO 28  28  28  PRO PRO C . n 
C 1 29  VAL 29  29  29  VAL VAL C . n 
C 1 30  LYS 30  30  30  LYS LYS C . n 
C 1 31  VAL 31  31  31  VAL VAL C . n 
C 1 32  TRP 32  32  32  TRP TRP C . n 
C 1 33  GLY 33  33  33  GLY GLY C . n 
C 1 34  SER 34  34  34  SER SER C . n 
C 1 35  ILE 35  35  35  ILE ILE C . n 
C 1 36  LYS 36  36  36  LYS LYS C . n 
C 1 37  GLY 37  37  37  GLY GLY C . n 
C 1 38  LEU 38  38  38  LEU LEU C . n 
C 1 39  THR 39  39  39  THR THR C . n 
C 1 40  GLU 40  40  40  GLU GLU C . n 
C 1 41  GLY 41  41  41  GLY GLY C . n 
C 1 42  LEU 42  42  42  LEU LEU C . n 
C 1 43  HIS 43  43  43  HIS HIS C . n 
C 1 44  GLY 44  44  44  GLY GLY C . n 
C 1 45  PHE 45  45  45  PHE PHE C . n 
C 1 46  HIS 46  46  46  HIS HIS C . n 
C 1 47  VAL 47  47  47  VAL VAL C . n 
C 1 48  HIS 48  48  48  HIS HIS C . n 
C 1 49  GLU 49  49  49  GLU GLU C . n 
C 1 50  PHE 50  50  50  PHE PHE C . n 
C 1 51  GLY 51  51  51  GLY GLY C . n 
C 1 52  ASP 52  52  52  ASP ASP C . n 
C 1 53  ASN 53  53  53  ASN ASN C . n 
C 1 54  THR 54  54  54  THR THR C . n 
C 1 55  ALA 55  55  55  ALA ALA C . n 
C 1 56  GLY 56  56  56  GLY GLY C . n 
C 1 57  CYS 57  57  57  CYS CYS C . n 
C 1 58  THR 58  58  58  THR THR C . n 
C 1 59  SER 59  59  59  SER SER C . n 
C 1 60  ALA 60  60  60  ALA ALA C . n 
C 1 61  GLY 61  61  61  GLY GLY C . n 
C 1 62  PRO 62  62  62  PRO PRO C . n 
C 1 63  HIS 63  63  63  HIS HIS C . n 
C 1 64  PHE 64  64  64  PHE PHE C . n 
C 1 65  ASN 65  65  65  ASN ASN C . n 
C 1 66  PRO 66  66  66  PRO PRO C . n 
C 1 67  LEU 67  67  67  LEU LEU C . n 
C 1 68  SER 68  68  68  SER SER C . n 
C 1 69  ARG 69  69  69  ARG ARG C . n 
C 1 70  LYS 70  70  70  LYS LYS C . n 
C 1 71  HIS 71  71  71  HIS HIS C . n 
C 1 72  GLY 72  72  72  GLY GLY C . n 
C 1 73  GLY 73  73  73  GLY GLY C . n 
C 1 74  PRO 74  74  74  PRO PRO C . n 
C 1 75  LYS 75  75  75  LYS LYS C . n 
C 1 76  ASP 76  76  76  ASP ASP C . n 
C 1 77  GLU 77  77  77  GLU GLU C . n 
C 1 78  GLU 78  78  78  GLU GLU C . n 
C 1 79  ARG 79  79  79  ARG ARG C . n 
C 1 80  HIS 80  80  80  HIS HIS C . n 
C 1 81  VAL 81  81  81  VAL VAL C . n 
C 1 82  GLY 82  82  82  GLY GLY C . n 
C 1 83  ASP 83  83  83  ASP ASP C . n 
C 1 84  LEU 84  84  84  LEU LEU C . n 
C 1 85  GLY 85  85  85  GLY GLY C . n 
C 1 86  ASN 86  86  86  ASN ASN C . n 
C 1 87  VAL 87  87  87  VAL VAL C . n 
C 1 88  THR 88  88  88  THR THR C . n 
C 1 89  ALA 89  89  89  ALA ALA C . n 
C 1 90  ASP 90  90  90  ASP ASP C . n 
C 1 91  LYS 91  91  91  LYS LYS C . n 
C 1 92  ASP 92  92  92  ASP ASP C . n 
C 1 93  GLY 93  93  93  GLY GLY C . n 
C 1 94  VAL 94  94  94  VAL VAL C . n 
C 1 95  ALA 95  95  95  ALA ALA C . n 
C 1 96  ASP 96  96  96  ASP ASP C . n 
C 1 97  VAL 97  97  97  VAL VAL C . n 
C 1 98  SER 98  98  98  SER SER C . n 
C 1 99  ILE 99  99  99  ILE ILE C . n 
C 1 100 GLU 100 100 100 GLU GLU C . n 
C 1 101 ASP 101 101 101 ASP ASP C . n 
C 1 102 SER 102 102 102 SER SER C . n 
C 1 103 VAL 103 103 103 VAL VAL C . n 
C 1 104 ILE 104 104 104 ILE ILE C . n 
C 1 105 SER 105 105 105 SER SER C . n 
C 1 106 LEU 106 106 106 LEU LEU C . n 
C 1 107 SER 107 107 107 SER SER C . n 
C 1 108 GLY 108 108 108 GLY GLY C . n 
C 1 109 ASP 109 109 109 ASP ASP C . n 
C 1 110 HIS 110 110 110 HIS HIS C . n 
C 1 111 CYS 111 111 111 CYS CYS C . n 
C 1 112 ILE 112 112 112 ILE ILE C . n 
C 1 113 ILE 113 113 113 ILE ILE C . n 
C 1 114 GLY 114 114 114 GLY GLY C . n 
C 1 115 ARG 115 115 115 ARG ARG C . n 
C 1 116 THR 116 116 116 THR THR C . n 
C 1 117 LEU 117 117 117 LEU LEU C . n 
C 1 118 VAL 118 118 118 VAL VAL C . n 
C 1 119 VAL 119 119 119 VAL VAL C . n 
C 1 120 HIS 120 120 120 HIS HIS C . n 
C 1 121 GLU 121 121 121 GLU GLU C . n 
C 1 122 LYS 122 122 122 LYS LYS C . n 
C 1 123 ALA 123 123 123 ALA ALA C . n 
C 1 124 ASP 124 124 124 ASP ASP C . n 
C 1 125 ASP 125 125 125 ASP ASP C . n 
C 1 126 LEU 126 126 126 LEU LEU C . n 
C 1 127 GLY 127 127 127 GLY GLY C . n 
C 1 128 LYS 128 128 128 LYS LYS C . n 
C 1 129 GLY 129 129 129 GLY GLY C . n 
C 1 130 GLY 130 130 130 GLY GLY C . n 
C 1 131 ASN 131 131 131 ASN ASN C . n 
C 1 132 GLU 132 132 132 GLU GLU C . n 
C 1 133 GLU 133 133 133 GLU GLU C . n 
C 1 134 SER 134 134 134 SER SER C . n 
C 1 135 THR 135 135 135 THR THR C . n 
C 1 136 LYS 136 136 136 LYS LYS C . n 
C 1 137 THR 137 137 137 THR THR C . n 
C 1 138 GLY 138 138 138 GLY GLY C . n 
C 1 139 ASN 139 139 139 ASN ASN C . n 
C 1 140 ALA 140 140 140 ALA ALA C . n 
C 1 141 GLY 141 141 141 GLY GLY C . n 
C 1 142 SER 142 142 142 SER SER C . n 
C 1 143 ARG 143 143 143 ARG ARG C . n 
C 1 144 LEU 144 144 144 LEU LEU C . n 
C 1 145 ALA 145 145 145 ALA ALA C . n 
C 1 146 CYS 146 146 146 CYS CYS C . n 
C 1 147 GLY 147 147 147 GLY GLY C . n 
C 1 148 VAL 148 148 148 VAL VAL C . n 
C 1 149 ILE 149 149 149 ILE ILE C . n 
C 1 150 GLY 150 150 150 GLY GLY C . n 
C 1 151 ILE 151 151 151 ILE ILE C . n 
C 1 152 ALA 152 152 152 ALA ALA C . n 
C 1 153 GLN 153 153 153 GLN GLN C . n 
D 1 1   ALA 1   1   1   ALA ALA D . n 
D 1 2   THR 2   2   2   THR THR D . n 
D 1 3   LYS 3   3   3   LYS LYS D . n 
D 1 4   ALA 4   4   4   ALA ALA D . n 
D 1 5   VAL 5   5   5   VAL VAL D . n 
D 1 6   CYS 6   6   6   CYS CYS D . n 
D 1 7   VAL 7   7   7   VAL VAL D . n 
D 1 8   LEU 8   8   8   LEU LEU D . n 
D 1 9   LYS 9   9   9   LYS LYS D . n 
D 1 10  GLY 10  10  10  GLY GLY D . n 
D 1 11  ASP 11  11  11  ASP ASP D . n 
D 1 12  GLY 12  12  12  GLY GLY D . n 
D 1 13  PRO 13  13  13  PRO PRO D . n 
D 1 14  VAL 14  14  14  VAL VAL D . n 
D 1 15  GLN 15  15  15  GLN GLN D . n 
D 1 16  GLY 16  16  16  GLY GLY D . n 
D 1 17  ILE 17  17  17  ILE ILE D . n 
D 1 18  ILE 18  18  18  ILE ILE D . n 
D 1 19  ASN 19  19  19  ASN ASN D . n 
D 1 20  PHE 20  20  20  PHE PHE D . n 
D 1 21  GLU 21  21  21  GLU GLU D . n 
D 1 22  GLN 22  22  22  GLN GLN D . n 
D 1 23  LYS 23  23  23  LYS LYS D . n 
D 1 24  GLU 24  24  24  GLU GLU D . n 
D 1 25  SER 25  25  25  SER SER D . n 
D 1 26  ASN 26  26  26  ASN ASN D . n 
D 1 27  GLY 27  27  27  GLY GLY D . n 
D 1 28  PRO 28  28  28  PRO PRO D . n 
D 1 29  VAL 29  29  29  VAL VAL D . n 
D 1 30  LYS 30  30  30  LYS LYS D . n 
D 1 31  VAL 31  31  31  VAL VAL D . n 
D 1 32  TRP 32  32  32  TRP TRP D . n 
D 1 33  GLY 33  33  33  GLY GLY D . n 
D 1 34  SER 34  34  34  SER SER D . n 
D 1 35  ILE 35  35  35  ILE ILE D . n 
D 1 36  LYS 36  36  36  LYS LYS D . n 
D 1 37  GLY 37  37  37  GLY GLY D . n 
D 1 38  LEU 38  38  38  LEU LEU D . n 
D 1 39  THR 39  39  39  THR THR D . n 
D 1 40  GLU 40  40  40  GLU GLU D . n 
D 1 41  GLY 41  41  41  GLY GLY D . n 
D 1 42  LEU 42  42  42  LEU LEU D . n 
D 1 43  HIS 43  43  43  HIS HIS D . n 
D 1 44  GLY 44  44  44  GLY GLY D . n 
D 1 45  PHE 45  45  45  PHE PHE D . n 
D 1 46  HIS 46  46  46  HIS HIS D . n 
D 1 47  VAL 47  47  47  VAL VAL D . n 
D 1 48  HIS 48  48  48  HIS HIS D . n 
D 1 49  GLU 49  49  49  GLU GLU D . n 
D 1 50  PHE 50  50  50  PHE PHE D . n 
D 1 51  GLY 51  51  51  GLY GLY D . n 
D 1 52  ASP 52  52  52  ASP ASP D . n 
D 1 53  ASN 53  53  53  ASN ASN D . n 
D 1 54  THR 54  54  54  THR THR D . n 
D 1 55  ALA 55  55  55  ALA ALA D . n 
D 1 56  GLY 56  56  56  GLY GLY D . n 
D 1 57  CYS 57  57  57  CYS CYS D . n 
D 1 58  THR 58  58  58  THR THR D . n 
D 1 59  SER 59  59  59  SER SER D . n 
D 1 60  ALA 60  60  60  ALA ALA D . n 
D 1 61  GLY 61  61  61  GLY GLY D . n 
D 1 62  PRO 62  62  62  PRO PRO D . n 
D 1 63  HIS 63  63  63  HIS HIS D . n 
D 1 64  PHE 64  64  64  PHE PHE D . n 
D 1 65  ASN 65  65  65  ASN ASN D . n 
D 1 66  PRO 66  66  66  PRO PRO D . n 
D 1 67  LEU 67  67  67  LEU LEU D . n 
D 1 68  SER 68  68  68  SER SER D . n 
D 1 69  ARG 69  69  69  ARG ARG D . n 
D 1 70  LYS 70  70  70  LYS LYS D . n 
D 1 71  HIS 71  71  71  HIS HIS D . n 
D 1 72  GLY 72  72  72  GLY GLY D . n 
D 1 73  GLY 73  73  73  GLY GLY D . n 
D 1 74  PRO 74  74  74  PRO PRO D . n 
D 1 75  LYS 75  75  75  LYS LYS D . n 
D 1 76  ASP 76  76  76  ASP ASP D . n 
D 1 77  GLU 77  77  77  GLU GLU D . n 
D 1 78  GLU 78  78  78  GLU GLU D . n 
D 1 79  ARG 79  79  79  ARG ARG D . n 
D 1 80  HIS 80  80  80  HIS HIS D . n 
D 1 81  VAL 81  81  81  VAL VAL D . n 
D 1 82  GLY 82  82  82  GLY GLY D . n 
D 1 83  ASP 83  83  83  ASP ASP D . n 
D 1 84  LEU 84  84  84  LEU LEU D . n 
D 1 85  GLY 85  85  85  GLY GLY D . n 
D 1 86  ASN 86  86  86  ASN ASN D . n 
D 1 87  VAL 87  87  87  VAL VAL D . n 
D 1 88  THR 88  88  88  THR THR D . n 
D 1 89  ALA 89  89  89  ALA ALA D . n 
D 1 90  ASP 90  90  90  ASP ASP D . n 
D 1 91  LYS 91  91  91  LYS LYS D . n 
D 1 92  ASP 92  92  92  ASP ASP D . n 
D 1 93  GLY 93  93  93  GLY GLY D . n 
D 1 94  VAL 94  94  94  VAL VAL D . n 
D 1 95  ALA 95  95  95  ALA ALA D . n 
D 1 96  ASP 96  96  96  ASP ASP D . n 
D 1 97  VAL 97  97  97  VAL VAL D . n 
D 1 98  SER 98  98  98  SER SER D . n 
D 1 99  ILE 99  99  99  ILE ILE D . n 
D 1 100 GLU 100 100 100 GLU GLU D . n 
D 1 101 ASP 101 101 101 ASP ASP D . n 
D 1 102 SER 102 102 102 SER SER D . n 
D 1 103 VAL 103 103 103 VAL VAL D . n 
D 1 104 ILE 104 104 104 ILE ILE D . n 
D 1 105 SER 105 105 105 SER SER D . n 
D 1 106 LEU 106 106 106 LEU LEU D . n 
D 1 107 SER 107 107 107 SER SER D . n 
D 1 108 GLY 108 108 108 GLY GLY D . n 
D 1 109 ASP 109 109 109 ASP ASP D . n 
D 1 110 HIS 110 110 110 HIS HIS D . n 
D 1 111 CYS 111 111 111 CYS CYS D . n 
D 1 112 ILE 112 112 112 ILE ILE D . n 
D 1 113 ILE 113 113 113 ILE ILE D . n 
D 1 114 GLY 114 114 114 GLY GLY D . n 
D 1 115 ARG 115 115 115 ARG ARG D . n 
D 1 116 THR 116 116 116 THR THR D . n 
D 1 117 LEU 117 117 117 LEU LEU D . n 
D 1 118 VAL 118 118 118 VAL VAL D . n 
D 1 119 VAL 119 119 119 VAL VAL D . n 
D 1 120 HIS 120 120 120 HIS HIS D . n 
D 1 121 GLU 121 121 121 GLU GLU D . n 
D 1 122 LYS 122 122 122 LYS LYS D . n 
D 1 123 ALA 123 123 123 ALA ALA D . n 
D 1 124 ASP 124 124 124 ASP ASP D . n 
D 1 125 ASP 125 125 125 ASP ASP D . n 
D 1 126 LEU 126 126 126 LEU LEU D . n 
D 1 127 GLY 127 127 127 GLY GLY D . n 
D 1 128 LYS 128 128 128 LYS LYS D . n 
D 1 129 GLY 129 129 129 GLY GLY D . n 
D 1 130 GLY 130 130 130 GLY GLY D . n 
D 1 131 ASN 131 131 131 ASN ASN D . n 
D 1 132 GLU 132 132 132 GLU GLU D . n 
D 1 133 GLU 133 133 133 GLU GLU D . n 
D 1 134 SER 134 134 134 SER SER D . n 
D 1 135 THR 135 135 135 THR THR D . n 
D 1 136 LYS 136 136 136 LYS LYS D . n 
D 1 137 THR 137 137 137 THR THR D . n 
D 1 138 GLY 138 138 138 GLY GLY D . n 
D 1 139 ASN 139 139 139 ASN ASN D . n 
D 1 140 ALA 140 140 140 ALA ALA D . n 
D 1 141 GLY 141 141 141 GLY GLY D . n 
D 1 142 SER 142 142 142 SER SER D . n 
D 1 143 ARG 143 143 143 ARG ARG D . n 
D 1 144 LEU 144 144 144 LEU LEU D . n 
D 1 145 ALA 145 145 145 ALA ALA D . n 
D 1 146 CYS 146 146 146 CYS CYS D . n 
D 1 147 GLY 147 147 147 GLY GLY D . n 
D 1 148 VAL 148 148 148 VAL VAL D . n 
D 1 149 ILE 149 149 149 ILE ILE D . n 
D 1 150 GLY 150 150 150 GLY GLY D . n 
D 1 151 ILE 151 151 151 ILE ILE D . n 
D 1 152 ALA 152 152 152 ALA ALA D . n 
D 1 153 GLN 153 153 153 GLN GLN D . n 
E 1 1   ALA 1   1   1   ALA ALA E . n 
E 1 2   THR 2   2   2   THR THR E . n 
E 1 3   LYS 3   3   3   LYS LYS E . n 
E 1 4   ALA 4   4   4   ALA ALA E . n 
E 1 5   VAL 5   5   5   VAL VAL E . n 
E 1 6   CYS 6   6   6   CYS CYS E . n 
E 1 7   VAL 7   7   7   VAL VAL E . n 
E 1 8   LEU 8   8   8   LEU LEU E . n 
E 1 9   LYS 9   9   9   LYS LYS E . n 
E 1 10  GLY 10  10  10  GLY GLY E . n 
E 1 11  ASP 11  11  11  ASP ASP E . n 
E 1 12  GLY 12  12  12  GLY GLY E . n 
E 1 13  PRO 13  13  13  PRO PRO E . n 
E 1 14  VAL 14  14  14  VAL VAL E . n 
E 1 15  GLN 15  15  15  GLN GLN E . n 
E 1 16  GLY 16  16  16  GLY GLY E . n 
E 1 17  ILE 17  17  17  ILE ILE E . n 
E 1 18  ILE 18  18  18  ILE ILE E . n 
E 1 19  ASN 19  19  19  ASN ASN E . n 
E 1 20  PHE 20  20  20  PHE PHE E . n 
E 1 21  GLU 21  21  21  GLU GLU E . n 
E 1 22  GLN 22  22  22  GLN GLN E . n 
E 1 23  LYS 23  23  23  LYS LYS E . n 
E 1 24  GLU 24  24  24  GLU GLU E . n 
E 1 25  SER 25  25  25  SER SER E . n 
E 1 26  ASN 26  26  26  ASN ASN E . n 
E 1 27  GLY 27  27  27  GLY GLY E . n 
E 1 28  PRO 28  28  28  PRO PRO E . n 
E 1 29  VAL 29  29  29  VAL VAL E . n 
E 1 30  LYS 30  30  30  LYS LYS E . n 
E 1 31  VAL 31  31  31  VAL VAL E . n 
E 1 32  TRP 32  32  32  TRP TRP E . n 
E 1 33  GLY 33  33  33  GLY GLY E . n 
E 1 34  SER 34  34  34  SER SER E . n 
E 1 35  ILE 35  35  35  ILE ILE E . n 
E 1 36  LYS 36  36  36  LYS LYS E . n 
E 1 37  GLY 37  37  37  GLY GLY E . n 
E 1 38  LEU 38  38  38  LEU LEU E . n 
E 1 39  THR 39  39  39  THR THR E . n 
E 1 40  GLU 40  40  40  GLU GLU E . n 
E 1 41  GLY 41  41  41  GLY GLY E . n 
E 1 42  LEU 42  42  42  LEU LEU E . n 
E 1 43  HIS 43  43  43  HIS HIS E . n 
E 1 44  GLY 44  44  44  GLY GLY E . n 
E 1 45  PHE 45  45  45  PHE PHE E . n 
E 1 46  HIS 46  46  46  HIS HIS E . n 
E 1 47  VAL 47  47  47  VAL VAL E . n 
E 1 48  HIS 48  48  48  HIS HIS E . n 
E 1 49  GLU 49  49  49  GLU GLU E . n 
E 1 50  PHE 50  50  50  PHE PHE E . n 
E 1 51  GLY 51  51  51  GLY GLY E . n 
E 1 52  ASP 52  52  52  ASP ASP E . n 
E 1 53  ASN 53  53  53  ASN ASN E . n 
E 1 54  THR 54  54  54  THR THR E . n 
E 1 55  ALA 55  55  55  ALA ALA E . n 
E 1 56  GLY 56  56  56  GLY GLY E . n 
E 1 57  CYS 57  57  57  CYS CYS E . n 
E 1 58  THR 58  58  58  THR THR E . n 
E 1 59  SER 59  59  59  SER SER E . n 
E 1 60  ALA 60  60  60  ALA ALA E . n 
E 1 61  GLY 61  61  61  GLY GLY E . n 
E 1 62  PRO 62  62  62  PRO PRO E . n 
E 1 63  HIS 63  63  63  HIS HIS E . n 
E 1 64  PHE 64  64  64  PHE PHE E . n 
E 1 65  ASN 65  65  65  ASN ASN E . n 
E 1 66  PRO 66  66  66  PRO PRO E . n 
E 1 67  LEU 67  67  67  LEU LEU E . n 
E 1 68  SER 68  68  68  SER SER E . n 
E 1 69  ARG 69  69  69  ARG ARG E . n 
E 1 70  LYS 70  70  70  LYS LYS E . n 
E 1 71  HIS 71  71  71  HIS HIS E . n 
E 1 72  GLY 72  72  72  GLY GLY E . n 
E 1 73  GLY 73  73  73  GLY GLY E . n 
E 1 74  PRO 74  74  74  PRO PRO E . n 
E 1 75  LYS 75  75  75  LYS LYS E . n 
E 1 76  ASP 76  76  76  ASP ASP E . n 
E 1 77  GLU 77  77  77  GLU GLU E . n 
E 1 78  GLU 78  78  78  GLU GLU E . n 
E 1 79  ARG 79  79  79  ARG ARG E . n 
E 1 80  HIS 80  80  80  HIS HIS E . n 
E 1 81  VAL 81  81  81  VAL VAL E . n 
E 1 82  GLY 82  82  82  GLY GLY E . n 
E 1 83  ASP 83  83  83  ASP ASP E . n 
E 1 84  LEU 84  84  84  LEU LEU E . n 
E 1 85  GLY 85  85  85  GLY GLY E . n 
E 1 86  ASN 86  86  86  ASN ASN E . n 
E 1 87  VAL 87  87  87  VAL VAL E . n 
E 1 88  THR 88  88  88  THR THR E . n 
E 1 89  ALA 89  89  89  ALA ALA E . n 
E 1 90  ASP 90  90  90  ASP ASP E . n 
E 1 91  LYS 91  91  91  LYS LYS E . n 
E 1 92  ASP 92  92  92  ASP ASP E . n 
E 1 93  GLY 93  93  93  GLY GLY E . n 
E 1 94  VAL 94  94  94  VAL VAL E . n 
E 1 95  ALA 95  95  95  ALA ALA E . n 
E 1 96  ASP 96  96  96  ASP ASP E . n 
E 1 97  VAL 97  97  97  VAL VAL E . n 
E 1 98  SER 98  98  98  SER SER E . n 
E 1 99  ILE 99  99  99  ILE ILE E . n 
E 1 100 GLU 100 100 100 GLU GLU E . n 
E 1 101 ASP 101 101 101 ASP ASP E . n 
E 1 102 SER 102 102 102 SER SER E . n 
E 1 103 VAL 103 103 103 VAL VAL E . n 
E 1 104 ILE 104 104 104 ILE ILE E . n 
E 1 105 SER 105 105 105 SER SER E . n 
E 1 106 LEU 106 106 106 LEU LEU E . n 
E 1 107 SER 107 107 107 SER SER E . n 
E 1 108 GLY 108 108 ?   ?   ?   E . n 
E 1 109 ASP 109 109 ?   ?   ?   E . n 
E 1 110 HIS 110 110 110 HIS HIS E . n 
E 1 111 CYS 111 111 111 CYS CYS E . n 
E 1 112 ILE 112 112 112 ILE ILE E . n 
E 1 113 ILE 113 113 113 ILE ILE E . n 
E 1 114 GLY 114 114 114 GLY GLY E . n 
E 1 115 ARG 115 115 115 ARG ARG E . n 
E 1 116 THR 116 116 116 THR THR E . n 
E 1 117 LEU 117 117 117 LEU LEU E . n 
E 1 118 VAL 118 118 118 VAL VAL E . n 
E 1 119 VAL 119 119 119 VAL VAL E . n 
E 1 120 HIS 120 120 120 HIS HIS E . n 
E 1 121 GLU 121 121 121 GLU GLU E . n 
E 1 122 LYS 122 122 122 LYS LYS E . n 
E 1 123 ALA 123 123 123 ALA ALA E . n 
E 1 124 ASP 124 124 124 ASP ASP E . n 
E 1 125 ASP 125 125 125 ASP ASP E . n 
E 1 126 LEU 126 126 126 LEU LEU E . n 
E 1 127 GLY 127 127 127 GLY GLY E . n 
E 1 128 LYS 128 128 128 LYS LYS E . n 
E 1 129 GLY 129 129 129 GLY GLY E . n 
E 1 130 GLY 130 130 130 GLY GLY E . n 
E 1 131 ASN 131 131 131 ASN ASN E . n 
E 1 132 GLU 132 132 132 GLU GLU E . n 
E 1 133 GLU 133 133 133 GLU GLU E . n 
E 1 134 SER 134 134 134 SER SER E . n 
E 1 135 THR 135 135 135 THR THR E . n 
E 1 136 LYS 136 136 136 LYS LYS E . n 
E 1 137 THR 137 137 137 THR THR E . n 
E 1 138 GLY 138 138 138 GLY GLY E . n 
E 1 139 ASN 139 139 139 ASN ASN E . n 
E 1 140 ALA 140 140 140 ALA ALA E . n 
E 1 141 GLY 141 141 141 GLY GLY E . n 
E 1 142 SER 142 142 142 SER SER E . n 
E 1 143 ARG 143 143 143 ARG ARG E . n 
E 1 144 LEU 144 144 144 LEU LEU E . n 
E 1 145 ALA 145 145 145 ALA ALA E . n 
E 1 146 CYS 146 146 146 CYS CYS E . n 
E 1 147 GLY 147 147 147 GLY GLY E . n 
E 1 148 VAL 148 148 148 VAL VAL E . n 
E 1 149 ILE 149 149 149 ILE ILE E . n 
E 1 150 GLY 150 150 150 GLY GLY E . n 
E 1 151 ILE 151 151 151 ILE ILE E . n 
E 1 152 ALA 152 152 152 ALA ALA E . n 
E 1 153 GLN 153 153 153 GLN GLN E . n 
F 1 1   ALA 1   1   ?   ?   ?   F . n 
F 1 2   THR 2   2   ?   ?   ?   F . n 
F 1 3   LYS 3   3   3   LYS LYS F . n 
F 1 4   ALA 4   4   4   ALA ALA F . n 
F 1 5   VAL 5   5   5   VAL VAL F . n 
F 1 6   CYS 6   6   6   CYS CYS F . n 
F 1 7   VAL 7   7   7   VAL VAL F . n 
F 1 8   LEU 8   8   8   LEU LEU F . n 
F 1 9   LYS 9   9   9   LYS LYS F . n 
F 1 10  GLY 10  10  10  GLY GLY F . n 
F 1 11  ASP 11  11  11  ASP ASP F . n 
F 1 12  GLY 12  12  12  GLY GLY F . n 
F 1 13  PRO 13  13  13  PRO PRO F . n 
F 1 14  VAL 14  14  14  VAL VAL F . n 
F 1 15  GLN 15  15  15  GLN GLN F . n 
F 1 16  GLY 16  16  16  GLY GLY F . n 
F 1 17  ILE 17  17  17  ILE ILE F . n 
F 1 18  ILE 18  18  18  ILE ILE F . n 
F 1 19  ASN 19  19  19  ASN ASN F . n 
F 1 20  PHE 20  20  20  PHE PHE F . n 
F 1 21  GLU 21  21  21  GLU GLU F . n 
F 1 22  GLN 22  22  ?   ?   ?   F . n 
F 1 23  LYS 23  23  ?   ?   ?   F . n 
F 1 24  GLU 24  24  ?   ?   ?   F . n 
F 1 25  SER 25  25  ?   ?   ?   F . n 
F 1 26  ASN 26  26  ?   ?   ?   F . n 
F 1 27  GLY 27  27  ?   ?   ?   F . n 
F 1 28  PRO 28  28  28  PRO PRO F . n 
F 1 29  VAL 29  29  29  VAL VAL F . n 
F 1 30  LYS 30  30  30  LYS LYS F . n 
F 1 31  VAL 31  31  31  VAL VAL F . n 
F 1 32  TRP 32  32  32  TRP TRP F . n 
F 1 33  GLY 33  33  33  GLY GLY F . n 
F 1 34  SER 34  34  34  SER SER F . n 
F 1 35  ILE 35  35  35  ILE ILE F . n 
F 1 36  LYS 36  36  36  LYS LYS F . n 
F 1 37  GLY 37  37  37  GLY GLY F . n 
F 1 38  LEU 38  38  38  LEU LEU F . n 
F 1 39  THR 39  39  39  THR THR F . n 
F 1 40  GLU 40  40  40  GLU GLU F . n 
F 1 41  GLY 41  41  41  GLY GLY F . n 
F 1 42  LEU 42  42  42  LEU LEU F . n 
F 1 43  HIS 43  43  43  HIS HIS F . n 
F 1 44  GLY 44  44  44  GLY GLY F . n 
F 1 45  PHE 45  45  45  PHE PHE F . n 
F 1 46  HIS 46  46  46  HIS HIS F . n 
F 1 47  VAL 47  47  47  VAL VAL F . n 
F 1 48  HIS 48  48  48  HIS HIS F . n 
F 1 49  GLU 49  49  49  GLU GLU F . n 
F 1 50  PHE 50  50  50  PHE PHE F . n 
F 1 51  GLY 51  51  51  GLY GLY F . n 
F 1 52  ASP 52  52  52  ASP ASP F . n 
F 1 53  ASN 53  53  53  ASN ASN F . n 
F 1 54  THR 54  54  54  THR THR F . n 
F 1 55  ALA 55  55  55  ALA ALA F . n 
F 1 56  GLY 56  56  56  GLY GLY F . n 
F 1 57  CYS 57  57  57  CYS CYS F . n 
F 1 58  THR 58  58  58  THR THR F . n 
F 1 59  SER 59  59  59  SER SER F . n 
F 1 60  ALA 60  60  60  ALA ALA F . n 
F 1 61  GLY 61  61  61  GLY GLY F . n 
F 1 62  PRO 62  62  62  PRO PRO F . n 
F 1 63  HIS 63  63  63  HIS HIS F . n 
F 1 64  PHE 64  64  64  PHE PHE F . n 
F 1 65  ASN 65  65  65  ASN ASN F . n 
F 1 66  PRO 66  66  66  PRO PRO F . n 
F 1 67  LEU 67  67  67  LEU LEU F . n 
F 1 68  SER 68  68  68  SER SER F . n 
F 1 69  ARG 69  69  69  ARG ARG F . n 
F 1 70  LYS 70  70  70  LYS LYS F . n 
F 1 71  HIS 71  71  71  HIS HIS F . n 
F 1 72  GLY 72  72  72  GLY GLY F . n 
F 1 73  GLY 73  73  73  GLY GLY F . n 
F 1 74  PRO 74  74  74  PRO PRO F . n 
F 1 75  LYS 75  75  75  LYS LYS F . n 
F 1 76  ASP 76  76  76  ASP ASP F . n 
F 1 77  GLU 77  77  77  GLU GLU F . n 
F 1 78  GLU 78  78  78  GLU GLU F . n 
F 1 79  ARG 79  79  79  ARG ARG F . n 
F 1 80  HIS 80  80  80  HIS HIS F . n 
F 1 81  VAL 81  81  81  VAL VAL F . n 
F 1 82  GLY 82  82  82  GLY GLY F . n 
F 1 83  ASP 83  83  83  ASP ASP F . n 
F 1 84  LEU 84  84  84  LEU LEU F . n 
F 1 85  GLY 85  85  85  GLY GLY F . n 
F 1 86  ASN 86  86  86  ASN ASN F . n 
F 1 87  VAL 87  87  87  VAL VAL F . n 
F 1 88  THR 88  88  88  THR THR F . n 
F 1 89  ALA 89  89  89  ALA ALA F . n 
F 1 90  ASP 90  90  90  ASP ASP F . n 
F 1 91  LYS 91  91  91  LYS LYS F . n 
F 1 92  ASP 92  92  92  ASP ASP F . n 
F 1 93  GLY 93  93  93  GLY GLY F . n 
F 1 94  VAL 94  94  94  VAL VAL F . n 
F 1 95  ALA 95  95  95  ALA ALA F . n 
F 1 96  ASP 96  96  96  ASP ASP F . n 
F 1 97  VAL 97  97  97  VAL VAL F . n 
F 1 98  SER 98  98  98  SER SER F . n 
F 1 99  ILE 99  99  99  ILE ILE F . n 
F 1 100 GLU 100 100 100 GLU GLU F . n 
F 1 101 ASP 101 101 101 ASP ASP F . n 
F 1 102 SER 102 102 102 SER SER F . n 
F 1 103 VAL 103 103 103 VAL VAL F . n 
F 1 104 ILE 104 104 104 ILE ILE F . n 
F 1 105 SER 105 105 105 SER SER F . n 
F 1 106 LEU 106 106 106 LEU LEU F . n 
F 1 107 SER 107 107 107 SER SER F . n 
F 1 108 GLY 108 108 108 GLY GLY F . n 
F 1 109 ASP 109 109 109 ASP ASP F . n 
F 1 110 HIS 110 110 110 HIS HIS F . n 
F 1 111 CYS 111 111 111 CYS CYS F . n 
F 1 112 ILE 112 112 112 ILE ILE F . n 
F 1 113 ILE 113 113 113 ILE ILE F . n 
F 1 114 GLY 114 114 114 GLY GLY F . n 
F 1 115 ARG 115 115 115 ARG ARG F . n 
F 1 116 THR 116 116 116 THR THR F . n 
F 1 117 LEU 117 117 117 LEU LEU F . n 
F 1 118 VAL 118 118 118 VAL VAL F . n 
F 1 119 VAL 119 119 119 VAL VAL F . n 
F 1 120 HIS 120 120 120 HIS HIS F . n 
F 1 121 GLU 121 121 121 GLU GLU F . n 
F 1 122 LYS 122 122 122 LYS LYS F . n 
F 1 123 ALA 123 123 123 ALA ALA F . n 
F 1 124 ASP 124 124 124 ASP ASP F . n 
F 1 125 ASP 125 125 125 ASP ASP F . n 
F 1 126 LEU 126 126 126 LEU LEU F . n 
F 1 127 GLY 127 127 127 GLY GLY F . n 
F 1 128 LYS 128 128 128 LYS LYS F . n 
F 1 129 GLY 129 129 129 GLY GLY F . n 
F 1 130 GLY 130 130 130 GLY GLY F . n 
F 1 131 ASN 131 131 131 ASN ASN F . n 
F 1 132 GLU 132 132 132 GLU GLU F . n 
F 1 133 GLU 133 133 133 GLU GLU F . n 
F 1 134 SER 134 134 134 SER SER F . n 
F 1 135 THR 135 135 135 THR THR F . n 
F 1 136 LYS 136 136 136 LYS LYS F . n 
F 1 137 THR 137 137 137 THR THR F . n 
F 1 138 GLY 138 138 138 GLY GLY F . n 
F 1 139 ASN 139 139 139 ASN ASN F . n 
F 1 140 ALA 140 140 140 ALA ALA F . n 
F 1 141 GLY 141 141 141 GLY GLY F . n 
F 1 142 SER 142 142 142 SER SER F . n 
F 1 143 ARG 143 143 143 ARG ARG F . n 
F 1 144 LEU 144 144 144 LEU LEU F . n 
F 1 145 ALA 145 145 145 ALA ALA F . n 
F 1 146 CYS 146 146 146 CYS CYS F . n 
F 1 147 GLY 147 147 147 GLY GLY F . n 
F 1 148 VAL 148 148 148 VAL VAL F . n 
F 1 149 ILE 149 149 149 ILE ILE F . n 
F 1 150 GLY 150 150 150 GLY GLY F . n 
F 1 151 ILE 151 151 151 ILE ILE F . n 
F 1 152 ALA 152 152 152 ALA ALA F . n 
F 1 153 GLN 153 153 153 GLN GLN F . n 
G 1 1   ALA 1   1   1   ALA ALA G . n 
G 1 2   THR 2   2   2   THR THR G . n 
G 1 3   LYS 3   3   3   LYS LYS G . n 
G 1 4   ALA 4   4   4   ALA ALA G . n 
G 1 5   VAL 5   5   5   VAL VAL G . n 
G 1 6   CYS 6   6   6   CYS CYS G . n 
G 1 7   VAL 7   7   7   VAL VAL G . n 
G 1 8   LEU 8   8   8   LEU LEU G . n 
G 1 9   LYS 9   9   9   LYS LYS G . n 
G 1 10  GLY 10  10  10  GLY GLY G . n 
G 1 11  ASP 11  11  11  ASP ASP G . n 
G 1 12  GLY 12  12  12  GLY GLY G . n 
G 1 13  PRO 13  13  13  PRO PRO G . n 
G 1 14  VAL 14  14  14  VAL VAL G . n 
G 1 15  GLN 15  15  15  GLN GLN G . n 
G 1 16  GLY 16  16  16  GLY GLY G . n 
G 1 17  ILE 17  17  17  ILE ILE G . n 
G 1 18  ILE 18  18  18  ILE ILE G . n 
G 1 19  ASN 19  19  19  ASN ASN G . n 
G 1 20  PHE 20  20  20  PHE PHE G . n 
G 1 21  GLU 21  21  21  GLU GLU G . n 
G 1 22  GLN 22  22  22  GLN GLN G . n 
G 1 23  LYS 23  23  23  LYS LYS G . n 
G 1 24  GLU 24  24  24  GLU GLU G . n 
G 1 25  SER 25  25  25  SER SER G . n 
G 1 26  ASN 26  26  26  ASN ASN G . n 
G 1 27  GLY 27  27  27  GLY GLY G . n 
G 1 28  PRO 28  28  28  PRO PRO G . n 
G 1 29  VAL 29  29  29  VAL VAL G . n 
G 1 30  LYS 30  30  30  LYS LYS G . n 
G 1 31  VAL 31  31  31  VAL VAL G . n 
G 1 32  TRP 32  32  32  TRP TRP G . n 
G 1 33  GLY 33  33  33  GLY GLY G . n 
G 1 34  SER 34  34  34  SER SER G . n 
G 1 35  ILE 35  35  35  ILE ILE G . n 
G 1 36  LYS 36  36  36  LYS LYS G . n 
G 1 37  GLY 37  37  37  GLY GLY G . n 
G 1 38  LEU 38  38  38  LEU LEU G . n 
G 1 39  THR 39  39  39  THR THR G . n 
G 1 40  GLU 40  40  40  GLU GLU G . n 
G 1 41  GLY 41  41  41  GLY GLY G . n 
G 1 42  LEU 42  42  42  LEU LEU G . n 
G 1 43  HIS 43  43  43  HIS HIS G . n 
G 1 44  GLY 44  44  44  GLY GLY G . n 
G 1 45  PHE 45  45  45  PHE PHE G . n 
G 1 46  HIS 46  46  46  HIS HIS G . n 
G 1 47  VAL 47  47  47  VAL VAL G . n 
G 1 48  HIS 48  48  48  HIS HIS G . n 
G 1 49  GLU 49  49  49  GLU GLU G . n 
G 1 50  PHE 50  50  50  PHE PHE G . n 
G 1 51  GLY 51  51  51  GLY GLY G . n 
G 1 52  ASP 52  52  52  ASP ASP G . n 
G 1 53  ASN 53  53  53  ASN ASN G . n 
G 1 54  THR 54  54  54  THR THR G . n 
G 1 55  ALA 55  55  55  ALA ALA G . n 
G 1 56  GLY 56  56  56  GLY GLY G . n 
G 1 57  CYS 57  57  57  CYS CYS G . n 
G 1 58  THR 58  58  58  THR THR G . n 
G 1 59  SER 59  59  59  SER SER G . n 
G 1 60  ALA 60  60  60  ALA ALA G . n 
G 1 61  GLY 61  61  61  GLY GLY G . n 
G 1 62  PRO 62  62  62  PRO PRO G . n 
G 1 63  HIS 63  63  63  HIS HIS G . n 
G 1 64  PHE 64  64  64  PHE PHE G . n 
G 1 65  ASN 65  65  65  ASN ASN G . n 
G 1 66  PRO 66  66  66  PRO PRO G . n 
G 1 67  LEU 67  67  67  LEU LEU G . n 
G 1 68  SER 68  68  68  SER SER G . n 
G 1 69  ARG 69  69  69  ARG ARG G . n 
G 1 70  LYS 70  70  70  LYS LYS G . n 
G 1 71  HIS 71  71  71  HIS HIS G . n 
G 1 72  GLY 72  72  72  GLY GLY G . n 
G 1 73  GLY 73  73  73  GLY GLY G . n 
G 1 74  PRO 74  74  74  PRO PRO G . n 
G 1 75  LYS 75  75  75  LYS LYS G . n 
G 1 76  ASP 76  76  76  ASP ASP G . n 
G 1 77  GLU 77  77  77  GLU GLU G . n 
G 1 78  GLU 78  78  78  GLU GLU G . n 
G 1 79  ARG 79  79  79  ARG ARG G . n 
G 1 80  HIS 80  80  80  HIS HIS G . n 
G 1 81  VAL 81  81  81  VAL VAL G . n 
G 1 82  GLY 82  82  82  GLY GLY G . n 
G 1 83  ASP 83  83  83  ASP ASP G . n 
G 1 84  LEU 84  84  84  LEU LEU G . n 
G 1 85  GLY 85  85  85  GLY GLY G . n 
G 1 86  ASN 86  86  86  ASN ASN G . n 
G 1 87  VAL 87  87  87  VAL VAL G . n 
G 1 88  THR 88  88  88  THR THR G . n 
G 1 89  ALA 89  89  89  ALA ALA G . n 
G 1 90  ASP 90  90  90  ASP ASP G . n 
G 1 91  LYS 91  91  91  LYS LYS G . n 
G 1 92  ASP 92  92  92  ASP ASP G . n 
G 1 93  GLY 93  93  93  GLY GLY G . n 
G 1 94  VAL 94  94  94  VAL VAL G . n 
G 1 95  ALA 95  95  95  ALA ALA G . n 
G 1 96  ASP 96  96  96  ASP ASP G . n 
G 1 97  VAL 97  97  97  VAL VAL G . n 
G 1 98  SER 98  98  98  SER SER G . n 
G 1 99  ILE 99  99  99  ILE ILE G . n 
G 1 100 GLU 100 100 100 GLU GLU G . n 
G 1 101 ASP 101 101 101 ASP ASP G . n 
G 1 102 SER 102 102 102 SER SER G . n 
G 1 103 VAL 103 103 103 VAL VAL G . n 
G 1 104 ILE 104 104 104 ILE ILE G . n 
G 1 105 SER 105 105 105 SER SER G . n 
G 1 106 LEU 106 106 106 LEU LEU G . n 
G 1 107 SER 107 107 107 SER SER G . n 
G 1 108 GLY 108 108 108 GLY GLY G . n 
G 1 109 ASP 109 109 109 ASP ASP G . n 
G 1 110 HIS 110 110 110 HIS HIS G . n 
G 1 111 CYS 111 111 111 CYS CYS G . n 
G 1 112 ILE 112 112 112 ILE ILE G . n 
G 1 113 ILE 113 113 113 ILE ILE G . n 
G 1 114 GLY 114 114 114 GLY GLY G . n 
G 1 115 ARG 115 115 115 ARG ARG G . n 
G 1 116 THR 116 116 116 THR THR G . n 
G 1 117 LEU 117 117 117 LEU LEU G . n 
G 1 118 VAL 118 118 118 VAL VAL G . n 
G 1 119 VAL 119 119 119 VAL VAL G . n 
G 1 120 HIS 120 120 120 HIS HIS G . n 
G 1 121 GLU 121 121 121 GLU GLU G . n 
G 1 122 LYS 122 122 122 LYS LYS G . n 
G 1 123 ALA 123 123 123 ALA ALA G . n 
G 1 124 ASP 124 124 124 ASP ASP G . n 
G 1 125 ASP 125 125 125 ASP ASP G . n 
G 1 126 LEU 126 126 126 LEU LEU G . n 
G 1 127 GLY 127 127 127 GLY GLY G . n 
G 1 128 LYS 128 128 128 LYS LYS G . n 
G 1 129 GLY 129 129 129 GLY GLY G . n 
G 1 130 GLY 130 130 130 GLY GLY G . n 
G 1 131 ASN 131 131 131 ASN ASN G . n 
G 1 132 GLU 132 132 132 GLU GLU G . n 
G 1 133 GLU 133 133 133 GLU GLU G . n 
G 1 134 SER 134 134 134 SER SER G . n 
G 1 135 THR 135 135 135 THR THR G . n 
G 1 136 LYS 136 136 136 LYS LYS G . n 
G 1 137 THR 137 137 137 THR THR G . n 
G 1 138 GLY 138 138 138 GLY GLY G . n 
G 1 139 ASN 139 139 139 ASN ASN G . n 
G 1 140 ALA 140 140 140 ALA ALA G . n 
G 1 141 GLY 141 141 141 GLY GLY G . n 
G 1 142 SER 142 142 142 SER SER G . n 
G 1 143 ARG 143 143 143 ARG ARG G . n 
G 1 144 LEU 144 144 144 LEU LEU G . n 
G 1 145 ALA 145 145 145 ALA ALA G . n 
G 1 146 CYS 146 146 146 CYS CYS G . n 
G 1 147 GLY 147 147 147 GLY GLY G . n 
G 1 148 VAL 148 148 148 VAL VAL G . n 
G 1 149 ILE 149 149 149 ILE ILE G . n 
G 1 150 GLY 150 150 150 GLY GLY G . n 
G 1 151 ILE 151 151 151 ILE ILE G . n 
G 1 152 ALA 152 152 152 ALA ALA G . n 
G 1 153 GLN 153 153 153 GLN GLN G . n 
H 1 1   ALA 1   1   1   ALA ALA H . n 
H 1 2   THR 2   2   2   THR THR H . n 
H 1 3   LYS 3   3   3   LYS LYS H . n 
H 1 4   ALA 4   4   4   ALA ALA H . n 
H 1 5   VAL 5   5   5   VAL VAL H . n 
H 1 6   CYS 6   6   6   CYS CYS H . n 
H 1 7   VAL 7   7   7   VAL VAL H . n 
H 1 8   LEU 8   8   8   LEU LEU H . n 
H 1 9   LYS 9   9   9   LYS LYS H . n 
H 1 10  GLY 10  10  10  GLY GLY H . n 
H 1 11  ASP 11  11  11  ASP ASP H . n 
H 1 12  GLY 12  12  12  GLY GLY H . n 
H 1 13  PRO 13  13  13  PRO PRO H . n 
H 1 14  VAL 14  14  14  VAL VAL H . n 
H 1 15  GLN 15  15  15  GLN GLN H . n 
H 1 16  GLY 16  16  16  GLY GLY H . n 
H 1 17  ILE 17  17  17  ILE ILE H . n 
H 1 18  ILE 18  18  18  ILE ILE H . n 
H 1 19  ASN 19  19  19  ASN ASN H . n 
H 1 20  PHE 20  20  20  PHE PHE H . n 
H 1 21  GLU 21  21  21  GLU GLU H . n 
H 1 22  GLN 22  22  22  GLN GLN H . n 
H 1 23  LYS 23  23  23  LYS LYS H . n 
H 1 24  GLU 24  24  24  GLU GLU H . n 
H 1 25  SER 25  25  25  SER SER H . n 
H 1 26  ASN 26  26  26  ASN ASN H . n 
H 1 27  GLY 27  27  27  GLY GLY H . n 
H 1 28  PRO 28  28  28  PRO PRO H . n 
H 1 29  VAL 29  29  29  VAL VAL H . n 
H 1 30  LYS 30  30  30  LYS LYS H . n 
H 1 31  VAL 31  31  31  VAL VAL H . n 
H 1 32  TRP 32  32  32  TRP TRP H . n 
H 1 33  GLY 33  33  33  GLY GLY H . n 
H 1 34  SER 34  34  34  SER SER H . n 
H 1 35  ILE 35  35  35  ILE ILE H . n 
H 1 36  LYS 36  36  36  LYS LYS H . n 
H 1 37  GLY 37  37  37  GLY GLY H . n 
H 1 38  LEU 38  38  38  LEU LEU H . n 
H 1 39  THR 39  39  39  THR THR H . n 
H 1 40  GLU 40  40  40  GLU GLU H . n 
H 1 41  GLY 41  41  41  GLY GLY H . n 
H 1 42  LEU 42  42  42  LEU LEU H . n 
H 1 43  HIS 43  43  43  HIS HIS H . n 
H 1 44  GLY 44  44  44  GLY GLY H . n 
H 1 45  PHE 45  45  45  PHE PHE H . n 
H 1 46  HIS 46  46  46  HIS HIS H . n 
H 1 47  VAL 47  47  47  VAL VAL H . n 
H 1 48  HIS 48  48  48  HIS HIS H . n 
H 1 49  GLU 49  49  49  GLU GLU H . n 
H 1 50  PHE 50  50  50  PHE PHE H . n 
H 1 51  GLY 51  51  51  GLY GLY H . n 
H 1 52  ASP 52  52  52  ASP ASP H . n 
H 1 53  ASN 53  53  53  ASN ASN H . n 
H 1 54  THR 54  54  54  THR THR H . n 
H 1 55  ALA 55  55  55  ALA ALA H . n 
H 1 56  GLY 56  56  56  GLY GLY H . n 
H 1 57  CYS 57  57  57  CYS CYS H . n 
H 1 58  THR 58  58  58  THR THR H . n 
H 1 59  SER 59  59  59  SER SER H . n 
H 1 60  ALA 60  60  60  ALA ALA H . n 
H 1 61  GLY 61  61  61  GLY GLY H . n 
H 1 62  PRO 62  62  62  PRO PRO H . n 
H 1 63  HIS 63  63  63  HIS HIS H . n 
H 1 64  PHE 64  64  64  PHE PHE H . n 
H 1 65  ASN 65  65  65  ASN ASN H . n 
H 1 66  PRO 66  66  66  PRO PRO H . n 
H 1 67  LEU 67  67  67  LEU LEU H . n 
H 1 68  SER 68  68  68  SER SER H . n 
H 1 69  ARG 69  69  69  ARG ARG H . n 
H 1 70  LYS 70  70  70  LYS LYS H . n 
H 1 71  HIS 71  71  71  HIS HIS H . n 
H 1 72  GLY 72  72  72  GLY GLY H . n 
H 1 73  GLY 73  73  73  GLY GLY H . n 
H 1 74  PRO 74  74  74  PRO PRO H . n 
H 1 75  LYS 75  75  75  LYS LYS H . n 
H 1 76  ASP 76  76  76  ASP ASP H . n 
H 1 77  GLU 77  77  77  GLU GLU H . n 
H 1 78  GLU 78  78  78  GLU GLU H . n 
H 1 79  ARG 79  79  79  ARG ARG H . n 
H 1 80  HIS 80  80  80  HIS HIS H . n 
H 1 81  VAL 81  81  81  VAL VAL H . n 
H 1 82  GLY 82  82  82  GLY GLY H . n 
H 1 83  ASP 83  83  83  ASP ASP H . n 
H 1 84  LEU 84  84  84  LEU LEU H . n 
H 1 85  GLY 85  85  85  GLY GLY H . n 
H 1 86  ASN 86  86  86  ASN ASN H . n 
H 1 87  VAL 87  87  87  VAL VAL H . n 
H 1 88  THR 88  88  88  THR THR H . n 
H 1 89  ALA 89  89  89  ALA ALA H . n 
H 1 90  ASP 90  90  90  ASP ASP H . n 
H 1 91  LYS 91  91  91  LYS LYS H . n 
H 1 92  ASP 92  92  92  ASP ASP H . n 
H 1 93  GLY 93  93  93  GLY GLY H . n 
H 1 94  VAL 94  94  94  VAL VAL H . n 
H 1 95  ALA 95  95  95  ALA ALA H . n 
H 1 96  ASP 96  96  96  ASP ASP H . n 
H 1 97  VAL 97  97  97  VAL VAL H . n 
H 1 98  SER 98  98  98  SER SER H . n 
H 1 99  ILE 99  99  99  ILE ILE H . n 
H 1 100 GLU 100 100 100 GLU GLU H . n 
H 1 101 ASP 101 101 101 ASP ASP H . n 
H 1 102 SER 102 102 102 SER SER H . n 
H 1 103 VAL 103 103 103 VAL VAL H . n 
H 1 104 ILE 104 104 104 ILE ILE H . n 
H 1 105 SER 105 105 105 SER SER H . n 
H 1 106 LEU 106 106 106 LEU LEU H . n 
H 1 107 SER 107 107 107 SER SER H . n 
H 1 108 GLY 108 108 108 GLY GLY H . n 
H 1 109 ASP 109 109 109 ASP ASP H . n 
H 1 110 HIS 110 110 110 HIS HIS H . n 
H 1 111 CYS 111 111 111 CYS CYS H . n 
H 1 112 ILE 112 112 112 ILE ILE H . n 
H 1 113 ILE 113 113 113 ILE ILE H . n 
H 1 114 GLY 114 114 114 GLY GLY H . n 
H 1 115 ARG 115 115 115 ARG ARG H . n 
H 1 116 THR 116 116 116 THR THR H . n 
H 1 117 LEU 117 117 117 LEU LEU H . n 
H 1 118 VAL 118 118 118 VAL VAL H . n 
H 1 119 VAL 119 119 119 VAL VAL H . n 
H 1 120 HIS 120 120 120 HIS HIS H . n 
H 1 121 GLU 121 121 121 GLU GLU H . n 
H 1 122 LYS 122 122 122 LYS LYS H . n 
H 1 123 ALA 123 123 123 ALA ALA H . n 
H 1 124 ASP 124 124 124 ASP ASP H . n 
H 1 125 ASP 125 125 125 ASP ASP H . n 
H 1 126 LEU 126 126 126 LEU LEU H . n 
H 1 127 GLY 127 127 127 GLY GLY H . n 
H 1 128 LYS 128 128 128 LYS LYS H . n 
H 1 129 GLY 129 129 129 GLY GLY H . n 
H 1 130 GLY 130 130 130 GLY GLY H . n 
H 1 131 ASN 131 131 131 ASN ASN H . n 
H 1 132 GLU 132 132 132 GLU GLU H . n 
H 1 133 GLU 133 133 133 GLU GLU H . n 
H 1 134 SER 134 134 134 SER SER H . n 
H 1 135 THR 135 135 135 THR THR H . n 
H 1 136 LYS 136 136 136 LYS LYS H . n 
H 1 137 THR 137 137 137 THR THR H . n 
H 1 138 GLY 138 138 138 GLY GLY H . n 
H 1 139 ASN 139 139 139 ASN ASN H . n 
H 1 140 ALA 140 140 140 ALA ALA H . n 
H 1 141 GLY 141 141 141 GLY GLY H . n 
H 1 142 SER 142 142 142 SER SER H . n 
H 1 143 ARG 143 143 143 ARG ARG H . n 
H 1 144 LEU 144 144 144 LEU LEU H . n 
H 1 145 ALA 145 145 145 ALA ALA H . n 
H 1 146 CYS 146 146 146 CYS CYS H . n 
H 1 147 GLY 147 147 147 GLY GLY H . n 
H 1 148 VAL 148 148 148 VAL VAL H . n 
H 1 149 ILE 149 149 149 ILE ILE H . n 
H 1 150 GLY 150 150 150 GLY GLY H . n 
H 1 151 ILE 151 151 151 ILE ILE H . n 
H 1 152 ALA 152 152 152 ALA ALA H . n 
H 1 153 GLN 153 153 153 GLN GLN H . n 
I 1 1   ALA 1   1   1   ALA ALA I . n 
I 1 2   THR 2   2   2   THR THR I . n 
I 1 3   LYS 3   3   3   LYS LYS I . n 
I 1 4   ALA 4   4   4   ALA ALA I . n 
I 1 5   VAL 5   5   5   VAL VAL I . n 
I 1 6   CYS 6   6   6   CYS CYS I . n 
I 1 7   VAL 7   7   7   VAL VAL I . n 
I 1 8   LEU 8   8   8   LEU LEU I . n 
I 1 9   LYS 9   9   9   LYS LYS I . n 
I 1 10  GLY 10  10  10  GLY GLY I . n 
I 1 11  ASP 11  11  11  ASP ASP I . n 
I 1 12  GLY 12  12  12  GLY GLY I . n 
I 1 13  PRO 13  13  13  PRO PRO I . n 
I 1 14  VAL 14  14  14  VAL VAL I . n 
I 1 15  GLN 15  15  15  GLN GLN I . n 
I 1 16  GLY 16  16  16  GLY GLY I . n 
I 1 17  ILE 17  17  17  ILE ILE I . n 
I 1 18  ILE 18  18  18  ILE ILE I . n 
I 1 19  ASN 19  19  19  ASN ASN I . n 
I 1 20  PHE 20  20  20  PHE PHE I . n 
I 1 21  GLU 21  21  21  GLU GLU I . n 
I 1 22  GLN 22  22  22  GLN GLN I . n 
I 1 23  LYS 23  23  23  LYS LYS I . n 
I 1 24  GLU 24  24  24  GLU GLU I . n 
I 1 25  SER 25  25  25  SER SER I . n 
I 1 26  ASN 26  26  26  ASN ASN I . n 
I 1 27  GLY 27  27  27  GLY GLY I . n 
I 1 28  PRO 28  28  28  PRO PRO I . n 
I 1 29  VAL 29  29  29  VAL VAL I . n 
I 1 30  LYS 30  30  30  LYS LYS I . n 
I 1 31  VAL 31  31  31  VAL VAL I . n 
I 1 32  TRP 32  32  32  TRP TRP I . n 
I 1 33  GLY 33  33  33  GLY GLY I . n 
I 1 34  SER 34  34  34  SER SER I . n 
I 1 35  ILE 35  35  35  ILE ILE I . n 
I 1 36  LYS 36  36  36  LYS LYS I . n 
I 1 37  GLY 37  37  37  GLY GLY I . n 
I 1 38  LEU 38  38  38  LEU LEU I . n 
I 1 39  THR 39  39  39  THR THR I . n 
I 1 40  GLU 40  40  40  GLU GLU I . n 
I 1 41  GLY 41  41  41  GLY GLY I . n 
I 1 42  LEU 42  42  42  LEU LEU I . n 
I 1 43  HIS 43  43  43  HIS HIS I . n 
I 1 44  GLY 44  44  44  GLY GLY I . n 
I 1 45  PHE 45  45  45  PHE PHE I . n 
I 1 46  HIS 46  46  46  HIS HIS I . n 
I 1 47  VAL 47  47  47  VAL VAL I . n 
I 1 48  HIS 48  48  48  HIS HIS I . n 
I 1 49  GLU 49  49  49  GLU GLU I . n 
I 1 50  PHE 50  50  50  PHE PHE I . n 
I 1 51  GLY 51  51  51  GLY GLY I . n 
I 1 52  ASP 52  52  52  ASP ASP I . n 
I 1 53  ASN 53  53  53  ASN ASN I . n 
I 1 54  THR 54  54  54  THR THR I . n 
I 1 55  ALA 55  55  55  ALA ALA I . n 
I 1 56  GLY 56  56  56  GLY GLY I . n 
I 1 57  CYS 57  57  57  CYS CYS I . n 
I 1 58  THR 58  58  58  THR THR I . n 
I 1 59  SER 59  59  59  SER SER I . n 
I 1 60  ALA 60  60  60  ALA ALA I . n 
I 1 61  GLY 61  61  61  GLY GLY I . n 
I 1 62  PRO 62  62  62  PRO PRO I . n 
I 1 63  HIS 63  63  63  HIS HIS I . n 
I 1 64  PHE 64  64  64  PHE PHE I . n 
I 1 65  ASN 65  65  65  ASN ASN I . n 
I 1 66  PRO 66  66  66  PRO PRO I . n 
I 1 67  LEU 67  67  67  LEU LEU I . n 
I 1 68  SER 68  68  68  SER SER I . n 
I 1 69  ARG 69  69  69  ARG ARG I . n 
I 1 70  LYS 70  70  70  LYS LYS I . n 
I 1 71  HIS 71  71  71  HIS HIS I . n 
I 1 72  GLY 72  72  72  GLY GLY I . n 
I 1 73  GLY 73  73  73  GLY GLY I . n 
I 1 74  PRO 74  74  74  PRO PRO I . n 
I 1 75  LYS 75  75  75  LYS LYS I . n 
I 1 76  ASP 76  76  76  ASP ASP I . n 
I 1 77  GLU 77  77  77  GLU GLU I . n 
I 1 78  GLU 78  78  78  GLU GLU I . n 
I 1 79  ARG 79  79  79  ARG ARG I . n 
I 1 80  HIS 80  80  80  HIS HIS I . n 
I 1 81  VAL 81  81  81  VAL VAL I . n 
I 1 82  GLY 82  82  82  GLY GLY I . n 
I 1 83  ASP 83  83  83  ASP ASP I . n 
I 1 84  LEU 84  84  84  LEU LEU I . n 
I 1 85  GLY 85  85  85  GLY GLY I . n 
I 1 86  ASN 86  86  86  ASN ASN I . n 
I 1 87  VAL 87  87  87  VAL VAL I . n 
I 1 88  THR 88  88  88  THR THR I . n 
I 1 89  ALA 89  89  89  ALA ALA I . n 
I 1 90  ASP 90  90  90  ASP ASP I . n 
I 1 91  LYS 91  91  91  LYS LYS I . n 
I 1 92  ASP 92  92  92  ASP ASP I . n 
I 1 93  GLY 93  93  93  GLY GLY I . n 
I 1 94  VAL 94  94  94  VAL VAL I . n 
I 1 95  ALA 95  95  95  ALA ALA I . n 
I 1 96  ASP 96  96  96  ASP ASP I . n 
I 1 97  VAL 97  97  97  VAL VAL I . n 
I 1 98  SER 98  98  98  SER SER I . n 
I 1 99  ILE 99  99  99  ILE ILE I . n 
I 1 100 GLU 100 100 100 GLU GLU I . n 
I 1 101 ASP 101 101 101 ASP ASP I . n 
I 1 102 SER 102 102 102 SER SER I . n 
I 1 103 VAL 103 103 103 VAL VAL I . n 
I 1 104 ILE 104 104 104 ILE ILE I . n 
I 1 105 SER 105 105 105 SER SER I . n 
I 1 106 LEU 106 106 106 LEU LEU I . n 
I 1 107 SER 107 107 107 SER SER I . n 
I 1 108 GLY 108 108 108 GLY GLY I . n 
I 1 109 ASP 109 109 109 ASP ASP I . n 
I 1 110 HIS 110 110 110 HIS HIS I . n 
I 1 111 CYS 111 111 111 CYS CYS I . n 
I 1 112 ILE 112 112 112 ILE ILE I . n 
I 1 113 ILE 113 113 113 ILE ILE I . n 
I 1 114 GLY 114 114 114 GLY GLY I . n 
I 1 115 ARG 115 115 115 ARG ARG I . n 
I 1 116 THR 116 116 116 THR THR I . n 
I 1 117 LEU 117 117 117 LEU LEU I . n 
I 1 118 VAL 118 118 118 VAL VAL I . n 
I 1 119 VAL 119 119 119 VAL VAL I . n 
I 1 120 HIS 120 120 120 HIS HIS I . n 
I 1 121 GLU 121 121 121 GLU GLU I . n 
I 1 122 LYS 122 122 122 LYS LYS I . n 
I 1 123 ALA 123 123 123 ALA ALA I . n 
I 1 124 ASP 124 124 124 ASP ASP I . n 
I 1 125 ASP 125 125 125 ASP ASP I . n 
I 1 126 LEU 126 126 126 LEU LEU I . n 
I 1 127 GLY 127 127 127 GLY GLY I . n 
I 1 128 LYS 128 128 128 LYS LYS I . n 
I 1 129 GLY 129 129 129 GLY GLY I . n 
I 1 130 GLY 130 130 130 GLY GLY I . n 
I 1 131 ASN 131 131 131 ASN ASN I . n 
I 1 132 GLU 132 132 132 GLU GLU I . n 
I 1 133 GLU 133 133 133 GLU GLU I . n 
I 1 134 SER 134 134 134 SER SER I . n 
I 1 135 THR 135 135 135 THR THR I . n 
I 1 136 LYS 136 136 136 LYS LYS I . n 
I 1 137 THR 137 137 137 THR THR I . n 
I 1 138 GLY 138 138 138 GLY GLY I . n 
I 1 139 ASN 139 139 139 ASN ASN I . n 
I 1 140 ALA 140 140 140 ALA ALA I . n 
I 1 141 GLY 141 141 141 GLY GLY I . n 
I 1 142 SER 142 142 142 SER SER I . n 
I 1 143 ARG 143 143 143 ARG ARG I . n 
I 1 144 LEU 144 144 144 LEU LEU I . n 
I 1 145 ALA 145 145 145 ALA ALA I . n 
I 1 146 CYS 146 146 146 CYS CYS I . n 
I 1 147 GLY 147 147 147 GLY GLY I . n 
I 1 148 VAL 148 148 148 VAL VAL I . n 
I 1 149 ILE 149 149 149 ILE ILE I . n 
I 1 150 GLY 150 150 150 GLY GLY I . n 
I 1 151 ILE 151 151 151 ILE ILE I . n 
I 1 152 ALA 152 152 152 ALA ALA I . n 
I 1 153 GLN 153 153 153 GLN GLN I . n 
J 1 1   ALA 1   1   1   ALA ALA J . n 
J 1 2   THR 2   2   2   THR THR J . n 
J 1 3   LYS 3   3   3   LYS LYS J . n 
J 1 4   ALA 4   4   4   ALA ALA J . n 
J 1 5   VAL 5   5   5   VAL VAL J . n 
J 1 6   CYS 6   6   6   CYS CYS J . n 
J 1 7   VAL 7   7   7   VAL VAL J . n 
J 1 8   LEU 8   8   8   LEU LEU J . n 
J 1 9   LYS 9   9   9   LYS LYS J . n 
J 1 10  GLY 10  10  10  GLY GLY J . n 
J 1 11  ASP 11  11  11  ASP ASP J . n 
J 1 12  GLY 12  12  12  GLY GLY J . n 
J 1 13  PRO 13  13  13  PRO PRO J . n 
J 1 14  VAL 14  14  14  VAL VAL J . n 
J 1 15  GLN 15  15  15  GLN GLN J . n 
J 1 16  GLY 16  16  16  GLY GLY J . n 
J 1 17  ILE 17  17  17  ILE ILE J . n 
J 1 18  ILE 18  18  18  ILE ILE J . n 
J 1 19  ASN 19  19  19  ASN ASN J . n 
J 1 20  PHE 20  20  20  PHE PHE J . n 
J 1 21  GLU 21  21  21  GLU GLU J . n 
J 1 22  GLN 22  22  22  GLN GLN J . n 
J 1 23  LYS 23  23  23  LYS LYS J . n 
J 1 24  GLU 24  24  24  GLU GLU J . n 
J 1 25  SER 25  25  25  SER SER J . n 
J 1 26  ASN 26  26  26  ASN ASN J . n 
J 1 27  GLY 27  27  27  GLY GLY J . n 
J 1 28  PRO 28  28  28  PRO PRO J . n 
J 1 29  VAL 29  29  29  VAL VAL J . n 
J 1 30  LYS 30  30  30  LYS LYS J . n 
J 1 31  VAL 31  31  31  VAL VAL J . n 
J 1 32  TRP 32  32  32  TRP TRP J . n 
J 1 33  GLY 33  33  33  GLY GLY J . n 
J 1 34  SER 34  34  34  SER SER J . n 
J 1 35  ILE 35  35  35  ILE ILE J . n 
J 1 36  LYS 36  36  36  LYS LYS J . n 
J 1 37  GLY 37  37  37  GLY GLY J . n 
J 1 38  LEU 38  38  38  LEU LEU J . n 
J 1 39  THR 39  39  39  THR THR J . n 
J 1 40  GLU 40  40  40  GLU GLU J . n 
J 1 41  GLY 41  41  41  GLY GLY J . n 
J 1 42  LEU 42  42  42  LEU LEU J . n 
J 1 43  HIS 43  43  43  HIS HIS J . n 
J 1 44  GLY 44  44  44  GLY GLY J . n 
J 1 45  PHE 45  45  45  PHE PHE J . n 
J 1 46  HIS 46  46  46  HIS HIS J . n 
J 1 47  VAL 47  47  47  VAL VAL J . n 
J 1 48  HIS 48  48  48  HIS HIS J . n 
J 1 49  GLU 49  49  49  GLU GLU J . n 
J 1 50  PHE 50  50  50  PHE PHE J . n 
J 1 51  GLY 51  51  51  GLY GLY J . n 
J 1 52  ASP 52  52  52  ASP ASP J . n 
J 1 53  ASN 53  53  53  ASN ASN J . n 
J 1 54  THR 54  54  54  THR THR J . n 
J 1 55  ALA 55  55  55  ALA ALA J . n 
J 1 56  GLY 56  56  56  GLY GLY J . n 
J 1 57  CYS 57  57  57  CYS CYS J . n 
J 1 58  THR 58  58  58  THR THR J . n 
J 1 59  SER 59  59  59  SER SER J . n 
J 1 60  ALA 60  60  60  ALA ALA J . n 
J 1 61  GLY 61  61  61  GLY GLY J . n 
J 1 62  PRO 62  62  62  PRO PRO J . n 
J 1 63  HIS 63  63  63  HIS HIS J . n 
J 1 64  PHE 64  64  64  PHE PHE J . n 
J 1 65  ASN 65  65  65  ASN ASN J . n 
J 1 66  PRO 66  66  66  PRO PRO J . n 
J 1 67  LEU 67  67  67  LEU LEU J . n 
J 1 68  SER 68  68  68  SER SER J . n 
J 1 69  ARG 69  69  69  ARG ARG J . n 
J 1 70  LYS 70  70  70  LYS LYS J . n 
J 1 71  HIS 71  71  71  HIS HIS J . n 
J 1 72  GLY 72  72  72  GLY GLY J . n 
J 1 73  GLY 73  73  73  GLY GLY J . n 
J 1 74  PRO 74  74  74  PRO PRO J . n 
J 1 75  LYS 75  75  75  LYS LYS J . n 
J 1 76  ASP 76  76  76  ASP ASP J . n 
J 1 77  GLU 77  77  77  GLU GLU J . n 
J 1 78  GLU 78  78  78  GLU GLU J . n 
J 1 79  ARG 79  79  79  ARG ARG J . n 
J 1 80  HIS 80  80  80  HIS HIS J . n 
J 1 81  VAL 81  81  81  VAL VAL J . n 
J 1 82  GLY 82  82  82  GLY GLY J . n 
J 1 83  ASP 83  83  83  ASP ASP J . n 
J 1 84  LEU 84  84  84  LEU LEU J . n 
J 1 85  GLY 85  85  85  GLY GLY J . n 
J 1 86  ASN 86  86  86  ASN ASN J . n 
J 1 87  VAL 87  87  87  VAL VAL J . n 
J 1 88  THR 88  88  88  THR THR J . n 
J 1 89  ALA 89  89  89  ALA ALA J . n 
J 1 90  ASP 90  90  90  ASP ASP J . n 
J 1 91  LYS 91  91  91  LYS LYS J . n 
J 1 92  ASP 92  92  92  ASP ASP J . n 
J 1 93  GLY 93  93  93  GLY GLY J . n 
J 1 94  VAL 94  94  94  VAL VAL J . n 
J 1 95  ALA 95  95  95  ALA ALA J . n 
J 1 96  ASP 96  96  96  ASP ASP J . n 
J 1 97  VAL 97  97  97  VAL VAL J . n 
J 1 98  SER 98  98  98  SER SER J . n 
J 1 99  ILE 99  99  99  ILE ILE J . n 
J 1 100 GLU 100 100 100 GLU GLU J . n 
J 1 101 ASP 101 101 101 ASP ASP J . n 
J 1 102 SER 102 102 102 SER SER J . n 
J 1 103 VAL 103 103 103 VAL VAL J . n 
J 1 104 ILE 104 104 104 ILE ILE J . n 
J 1 105 SER 105 105 105 SER SER J . n 
J 1 106 LEU 106 106 106 LEU LEU J . n 
J 1 107 SER 107 107 107 SER SER J . n 
J 1 108 GLY 108 108 108 GLY GLY J . n 
J 1 109 ASP 109 109 109 ASP ASP J . n 
J 1 110 HIS 110 110 110 HIS HIS J . n 
J 1 111 CYS 111 111 111 CYS CYS J . n 
J 1 112 ILE 112 112 112 ILE ILE J . n 
J 1 113 ILE 113 113 113 ILE ILE J . n 
J 1 114 GLY 114 114 114 GLY GLY J . n 
J 1 115 ARG 115 115 115 ARG ARG J . n 
J 1 116 THR 116 116 116 THR THR J . n 
J 1 117 LEU 117 117 117 LEU LEU J . n 
J 1 118 VAL 118 118 118 VAL VAL J . n 
J 1 119 VAL 119 119 119 VAL VAL J . n 
J 1 120 HIS 120 120 120 HIS HIS J . n 
J 1 121 GLU 121 121 121 GLU GLU J . n 
J 1 122 LYS 122 122 122 LYS LYS J . n 
J 1 123 ALA 123 123 123 ALA ALA J . n 
J 1 124 ASP 124 124 124 ASP ASP J . n 
J 1 125 ASP 125 125 125 ASP ASP J . n 
J 1 126 LEU 126 126 126 LEU LEU J . n 
J 1 127 GLY 127 127 127 GLY GLY J . n 
J 1 128 LYS 128 128 128 LYS LYS J . n 
J 1 129 GLY 129 129 129 GLY GLY J . n 
J 1 130 GLY 130 130 130 GLY GLY J . n 
J 1 131 ASN 131 131 131 ASN ASN J . n 
J 1 132 GLU 132 132 132 GLU GLU J . n 
J 1 133 GLU 133 133 133 GLU GLU J . n 
J 1 134 SER 134 134 134 SER SER J . n 
J 1 135 THR 135 135 135 THR THR J . n 
J 1 136 LYS 136 136 136 LYS LYS J . n 
J 1 137 THR 137 137 137 THR THR J . n 
J 1 138 GLY 138 138 138 GLY GLY J . n 
J 1 139 ASN 139 139 139 ASN ASN J . n 
J 1 140 ALA 140 140 140 ALA ALA J . n 
J 1 141 GLY 141 141 141 GLY GLY J . n 
J 1 142 SER 142 142 142 SER SER J . n 
J 1 143 ARG 143 143 143 ARG ARG J . n 
J 1 144 LEU 144 144 144 LEU LEU J . n 
J 1 145 ALA 145 145 145 ALA ALA J . n 
J 1 146 CYS 146 146 146 CYS CYS J . n 
J 1 147 GLY 147 147 147 GLY GLY J . n 
J 1 148 VAL 148 148 148 VAL VAL J . n 
J 1 149 ILE 149 149 149 ILE ILE J . n 
J 1 150 GLY 150 150 150 GLY GLY J . n 
J 1 151 ILE 151 151 151 ILE ILE J . n 
J 1 152 ALA 152 152 152 ALA ALA J . n 
J 1 153 GLN 153 153 153 GLN GLN J . n 
K 1 1   ALA 1   1   1   ALA ALA K . n 
K 1 2   THR 2   2   2   THR THR K . n 
K 1 3   LYS 3   3   3   LYS LYS K . n 
K 1 4   ALA 4   4   4   ALA ALA K . n 
K 1 5   VAL 5   5   5   VAL VAL K . n 
K 1 6   CYS 6   6   6   CYS CYS K . n 
K 1 7   VAL 7   7   7   VAL VAL K . n 
K 1 8   LEU 8   8   8   LEU LEU K . n 
K 1 9   LYS 9   9   9   LYS LYS K . n 
K 1 10  GLY 10  10  10  GLY GLY K . n 
K 1 11  ASP 11  11  11  ASP ASP K . n 
K 1 12  GLY 12  12  12  GLY GLY K . n 
K 1 13  PRO 13  13  13  PRO PRO K . n 
K 1 14  VAL 14  14  14  VAL VAL K . n 
K 1 15  GLN 15  15  15  GLN GLN K . n 
K 1 16  GLY 16  16  16  GLY GLY K . n 
K 1 17  ILE 17  17  17  ILE ILE K . n 
K 1 18  ILE 18  18  18  ILE ILE K . n 
K 1 19  ASN 19  19  19  ASN ASN K . n 
K 1 20  PHE 20  20  20  PHE PHE K . n 
K 1 21  GLU 21  21  21  GLU GLU K . n 
K 1 22  GLN 22  22  22  GLN GLN K . n 
K 1 23  LYS 23  23  23  LYS LYS K . n 
K 1 24  GLU 24  24  24  GLU GLU K . n 
K 1 25  SER 25  25  25  SER SER K . n 
K 1 26  ASN 26  26  26  ASN ASN K . n 
K 1 27  GLY 27  27  27  GLY GLY K . n 
K 1 28  PRO 28  28  28  PRO PRO K . n 
K 1 29  VAL 29  29  29  VAL VAL K . n 
K 1 30  LYS 30  30  30  LYS LYS K . n 
K 1 31  VAL 31  31  31  VAL VAL K . n 
K 1 32  TRP 32  32  32  TRP TRP K . n 
K 1 33  GLY 33  33  33  GLY GLY K . n 
K 1 34  SER 34  34  34  SER SER K . n 
K 1 35  ILE 35  35  35  ILE ILE K . n 
K 1 36  LYS 36  36  36  LYS LYS K . n 
K 1 37  GLY 37  37  37  GLY GLY K . n 
K 1 38  LEU 38  38  38  LEU LEU K . n 
K 1 39  THR 39  39  39  THR THR K . n 
K 1 40  GLU 40  40  40  GLU GLU K . n 
K 1 41  GLY 41  41  41  GLY GLY K . n 
K 1 42  LEU 42  42  42  LEU LEU K . n 
K 1 43  HIS 43  43  43  HIS HIS K . n 
K 1 44  GLY 44  44  44  GLY GLY K . n 
K 1 45  PHE 45  45  45  PHE PHE K . n 
K 1 46  HIS 46  46  46  HIS HIS K . n 
K 1 47  VAL 47  47  47  VAL VAL K . n 
K 1 48  HIS 48  48  48  HIS HIS K . n 
K 1 49  GLU 49  49  49  GLU GLU K . n 
K 1 50  PHE 50  50  50  PHE PHE K . n 
K 1 51  GLY 51  51  51  GLY GLY K . n 
K 1 52  ASP 52  52  52  ASP ASP K . n 
K 1 53  ASN 53  53  53  ASN ASN K . n 
K 1 54  THR 54  54  54  THR THR K . n 
K 1 55  ALA 55  55  55  ALA ALA K . n 
K 1 56  GLY 56  56  56  GLY GLY K . n 
K 1 57  CYS 57  57  57  CYS CYS K . n 
K 1 58  THR 58  58  58  THR THR K . n 
K 1 59  SER 59  59  59  SER SER K . n 
K 1 60  ALA 60  60  60  ALA ALA K . n 
K 1 61  GLY 61  61  61  GLY GLY K . n 
K 1 62  PRO 62  62  62  PRO PRO K . n 
K 1 63  HIS 63  63  63  HIS HIS K . n 
K 1 64  PHE 64  64  64  PHE PHE K . n 
K 1 65  ASN 65  65  65  ASN ASN K . n 
K 1 66  PRO 66  66  66  PRO PRO K . n 
K 1 67  LEU 67  67  67  LEU LEU K . n 
K 1 68  SER 68  68  68  SER SER K . n 
K 1 69  ARG 69  69  69  ARG ARG K . n 
K 1 70  LYS 70  70  70  LYS LYS K . n 
K 1 71  HIS 71  71  71  HIS HIS K . n 
K 1 72  GLY 72  72  72  GLY GLY K . n 
K 1 73  GLY 73  73  73  GLY GLY K . n 
K 1 74  PRO 74  74  74  PRO PRO K . n 
K 1 75  LYS 75  75  75  LYS LYS K . n 
K 1 76  ASP 76  76  76  ASP ASP K . n 
K 1 77  GLU 77  77  77  GLU GLU K . n 
K 1 78  GLU 78  78  78  GLU GLU K . n 
K 1 79  ARG 79  79  79  ARG ARG K . n 
K 1 80  HIS 80  80  80  HIS HIS K . n 
K 1 81  VAL 81  81  81  VAL VAL K . n 
K 1 82  GLY 82  82  82  GLY GLY K . n 
K 1 83  ASP 83  83  83  ASP ASP K . n 
K 1 84  LEU 84  84  84  LEU LEU K . n 
K 1 85  GLY 85  85  85  GLY GLY K . n 
K 1 86  ASN 86  86  86  ASN ASN K . n 
K 1 87  VAL 87  87  87  VAL VAL K . n 
K 1 88  THR 88  88  88  THR THR K . n 
K 1 89  ALA 89  89  89  ALA ALA K . n 
K 1 90  ASP 90  90  90  ASP ASP K . n 
K 1 91  LYS 91  91  91  LYS LYS K . n 
K 1 92  ASP 92  92  92  ASP ASP K . n 
K 1 93  GLY 93  93  93  GLY GLY K . n 
K 1 94  VAL 94  94  94  VAL VAL K . n 
K 1 95  ALA 95  95  95  ALA ALA K . n 
K 1 96  ASP 96  96  96  ASP ASP K . n 
K 1 97  VAL 97  97  97  VAL VAL K . n 
K 1 98  SER 98  98  98  SER SER K . n 
K 1 99  ILE 99  99  99  ILE ILE K . n 
K 1 100 GLU 100 100 100 GLU GLU K . n 
K 1 101 ASP 101 101 101 ASP ASP K . n 
K 1 102 SER 102 102 102 SER SER K . n 
K 1 103 VAL 103 103 103 VAL VAL K . n 
K 1 104 ILE 104 104 104 ILE ILE K . n 
K 1 105 SER 105 105 105 SER SER K . n 
K 1 106 LEU 106 106 106 LEU LEU K . n 
K 1 107 SER 107 107 107 SER SER K . n 
K 1 108 GLY 108 108 108 GLY GLY K . n 
K 1 109 ASP 109 109 109 ASP ASP K . n 
K 1 110 HIS 110 110 110 HIS HIS K . n 
K 1 111 CYS 111 111 111 CYS CYS K . n 
K 1 112 ILE 112 112 112 ILE ILE K . n 
K 1 113 ILE 113 113 113 ILE ILE K . n 
K 1 114 GLY 114 114 114 GLY GLY K . n 
K 1 115 ARG 115 115 115 ARG ARG K . n 
K 1 116 THR 116 116 116 THR THR K . n 
K 1 117 LEU 117 117 117 LEU LEU K . n 
K 1 118 VAL 118 118 118 VAL VAL K . n 
K 1 119 VAL 119 119 119 VAL VAL K . n 
K 1 120 HIS 120 120 120 HIS HIS K . n 
K 1 121 GLU 121 121 121 GLU GLU K . n 
K 1 122 LYS 122 122 122 LYS LYS K . n 
K 1 123 ALA 123 123 123 ALA ALA K . n 
K 1 124 ASP 124 124 124 ASP ASP K . n 
K 1 125 ASP 125 125 125 ASP ASP K . n 
K 1 126 LEU 126 126 126 LEU LEU K . n 
K 1 127 GLY 127 127 127 GLY GLY K . n 
K 1 128 LYS 128 128 128 LYS LYS K . n 
K 1 129 GLY 129 129 129 GLY GLY K . n 
K 1 130 GLY 130 130 130 GLY GLY K . n 
K 1 131 ASN 131 131 131 ASN ASN K . n 
K 1 132 GLU 132 132 132 GLU GLU K . n 
K 1 133 GLU 133 133 133 GLU GLU K . n 
K 1 134 SER 134 134 134 SER SER K . n 
K 1 135 THR 135 135 135 THR THR K . n 
K 1 136 LYS 136 136 136 LYS LYS K . n 
K 1 137 THR 137 137 137 THR THR K . n 
K 1 138 GLY 138 138 138 GLY GLY K . n 
K 1 139 ASN 139 139 139 ASN ASN K . n 
K 1 140 ALA 140 140 140 ALA ALA K . n 
K 1 141 GLY 141 141 141 GLY GLY K . n 
K 1 142 SER 142 142 142 SER SER K . n 
K 1 143 ARG 143 143 143 ARG ARG K . n 
K 1 144 LEU 144 144 144 LEU LEU K . n 
K 1 145 ALA 145 145 145 ALA ALA K . n 
K 1 146 CYS 146 146 146 CYS CYS K . n 
K 1 147 GLY 147 147 147 GLY GLY K . n 
K 1 148 VAL 148 148 148 VAL VAL K . n 
K 1 149 ILE 149 149 149 ILE ILE K . n 
K 1 150 GLY 150 150 150 GLY GLY K . n 
K 1 151 ILE 151 151 151 ILE ILE K . n 
K 1 152 ALA 152 152 152 ALA ALA K . n 
K 1 153 GLN 153 153 153 GLN GLN K . n 
L 1 1   ALA 1   1   ?   ?   ?   L . n 
L 1 2   THR 2   2   2   THR THR L . n 
L 1 3   LYS 3   3   3   LYS LYS L . n 
L 1 4   ALA 4   4   4   ALA ALA L . n 
L 1 5   VAL 5   5   5   VAL VAL L . n 
L 1 6   CYS 6   6   6   CYS CYS L . n 
L 1 7   VAL 7   7   7   VAL VAL L . n 
L 1 8   LEU 8   8   8   LEU LEU L . n 
L 1 9   LYS 9   9   9   LYS LYS L . n 
L 1 10  GLY 10  10  10  GLY GLY L . n 
L 1 11  ASP 11  11  11  ASP ASP L . n 
L 1 12  GLY 12  12  12  GLY GLY L . n 
L 1 13  PRO 13  13  13  PRO PRO L . n 
L 1 14  VAL 14  14  14  VAL VAL L . n 
L 1 15  GLN 15  15  15  GLN GLN L . n 
L 1 16  GLY 16  16  16  GLY GLY L . n 
L 1 17  ILE 17  17  17  ILE ILE L . n 
L 1 18  ILE 18  18  18  ILE ILE L . n 
L 1 19  ASN 19  19  19  ASN ASN L . n 
L 1 20  PHE 20  20  20  PHE PHE L . n 
L 1 21  GLU 21  21  21  GLU GLU L . n 
L 1 22  GLN 22  22  22  GLN GLN L . n 
L 1 23  LYS 23  23  23  LYS LYS L . n 
L 1 24  GLU 24  24  24  GLU GLU L . n 
L 1 25  SER 25  25  25  SER SER L . n 
L 1 26  ASN 26  26  26  ASN ASN L . n 
L 1 27  GLY 27  27  27  GLY GLY L . n 
L 1 28  PRO 28  28  28  PRO PRO L . n 
L 1 29  VAL 29  29  29  VAL VAL L . n 
L 1 30  LYS 30  30  30  LYS LYS L . n 
L 1 31  VAL 31  31  31  VAL VAL L . n 
L 1 32  TRP 32  32  32  TRP TRP L . n 
L 1 33  GLY 33  33  33  GLY GLY L . n 
L 1 34  SER 34  34  34  SER SER L . n 
L 1 35  ILE 35  35  35  ILE ILE L . n 
L 1 36  LYS 36  36  36  LYS LYS L . n 
L 1 37  GLY 37  37  37  GLY GLY L . n 
L 1 38  LEU 38  38  38  LEU LEU L . n 
L 1 39  THR 39  39  39  THR THR L . n 
L 1 40  GLU 40  40  40  GLU GLU L . n 
L 1 41  GLY 41  41  41  GLY GLY L . n 
L 1 42  LEU 42  42  42  LEU LEU L . n 
L 1 43  HIS 43  43  43  HIS HIS L . n 
L 1 44  GLY 44  44  44  GLY GLY L . n 
L 1 45  PHE 45  45  45  PHE PHE L . n 
L 1 46  HIS 46  46  46  HIS HIS L . n 
L 1 47  VAL 47  47  47  VAL VAL L . n 
L 1 48  HIS 48  48  48  HIS HIS L . n 
L 1 49  GLU 49  49  49  GLU GLU L . n 
L 1 50  PHE 50  50  50  PHE PHE L . n 
L 1 51  GLY 51  51  51  GLY GLY L . n 
L 1 52  ASP 52  52  52  ASP ASP L . n 
L 1 53  ASN 53  53  53  ASN ASN L . n 
L 1 54  THR 54  54  54  THR THR L . n 
L 1 55  ALA 55  55  55  ALA ALA L . n 
L 1 56  GLY 56  56  56  GLY GLY L . n 
L 1 57  CYS 57  57  57  CYS CYS L . n 
L 1 58  THR 58  58  58  THR THR L . n 
L 1 59  SER 59  59  59  SER SER L . n 
L 1 60  ALA 60  60  60  ALA ALA L . n 
L 1 61  GLY 61  61  61  GLY GLY L . n 
L 1 62  PRO 62  62  62  PRO PRO L . n 
L 1 63  HIS 63  63  63  HIS HIS L . n 
L 1 64  PHE 64  64  64  PHE PHE L . n 
L 1 65  ASN 65  65  65  ASN ASN L . n 
L 1 66  PRO 66  66  66  PRO PRO L . n 
L 1 67  LEU 67  67  67  LEU LEU L . n 
L 1 68  SER 68  68  68  SER SER L . n 
L 1 69  ARG 69  69  69  ARG ARG L . n 
L 1 70  LYS 70  70  70  LYS LYS L . n 
L 1 71  HIS 71  71  71  HIS HIS L . n 
L 1 72  GLY 72  72  72  GLY GLY L . n 
L 1 73  GLY 73  73  73  GLY GLY L . n 
L 1 74  PRO 74  74  74  PRO PRO L . n 
L 1 75  LYS 75  75  75  LYS LYS L . n 
L 1 76  ASP 76  76  76  ASP ASP L . n 
L 1 77  GLU 77  77  77  GLU GLU L . n 
L 1 78  GLU 78  78  78  GLU GLU L . n 
L 1 79  ARG 79  79  79  ARG ARG L . n 
L 1 80  HIS 80  80  80  HIS HIS L . n 
L 1 81  VAL 81  81  81  VAL VAL L . n 
L 1 82  GLY 82  82  82  GLY GLY L . n 
L 1 83  ASP 83  83  83  ASP ASP L . n 
L 1 84  LEU 84  84  84  LEU LEU L . n 
L 1 85  GLY 85  85  85  GLY GLY L . n 
L 1 86  ASN 86  86  86  ASN ASN L . n 
L 1 87  VAL 87  87  87  VAL VAL L . n 
L 1 88  THR 88  88  88  THR THR L . n 
L 1 89  ALA 89  89  89  ALA ALA L . n 
L 1 90  ASP 90  90  90  ASP ASP L . n 
L 1 91  LYS 91  91  91  LYS LYS L . n 
L 1 92  ASP 92  92  92  ASP ASP L . n 
L 1 93  GLY 93  93  93  GLY GLY L . n 
L 1 94  VAL 94  94  94  VAL VAL L . n 
L 1 95  ALA 95  95  95  ALA ALA L . n 
L 1 96  ASP 96  96  96  ASP ASP L . n 
L 1 97  VAL 97  97  97  VAL VAL L . n 
L 1 98  SER 98  98  98  SER SER L . n 
L 1 99  ILE 99  99  99  ILE ILE L . n 
L 1 100 GLU 100 100 100 GLU GLU L . n 
L 1 101 ASP 101 101 101 ASP ASP L . n 
L 1 102 SER 102 102 102 SER SER L . n 
L 1 103 VAL 103 103 103 VAL VAL L . n 
L 1 104 ILE 104 104 104 ILE ILE L . n 
L 1 105 SER 105 105 105 SER SER L . n 
L 1 106 LEU 106 106 106 LEU LEU L . n 
L 1 107 SER 107 107 107 SER SER L . n 
L 1 108 GLY 108 108 108 GLY GLY L . n 
L 1 109 ASP 109 109 109 ASP ASP L . n 
L 1 110 HIS 110 110 110 HIS HIS L . n 
L 1 111 CYS 111 111 111 CYS CYS L . n 
L 1 112 ILE 112 112 112 ILE ILE L . n 
L 1 113 ILE 113 113 113 ILE ILE L . n 
L 1 114 GLY 114 114 114 GLY GLY L . n 
L 1 115 ARG 115 115 115 ARG ARG L . n 
L 1 116 THR 116 116 116 THR THR L . n 
L 1 117 LEU 117 117 117 LEU LEU L . n 
L 1 118 VAL 118 118 118 VAL VAL L . n 
L 1 119 VAL 119 119 119 VAL VAL L . n 
L 1 120 HIS 120 120 120 HIS HIS L . n 
L 1 121 GLU 121 121 121 GLU GLU L . n 
L 1 122 LYS 122 122 122 LYS LYS L . n 
L 1 123 ALA 123 123 123 ALA ALA L . n 
L 1 124 ASP 124 124 124 ASP ASP L . n 
L 1 125 ASP 125 125 125 ASP ASP L . n 
L 1 126 LEU 126 126 126 LEU LEU L . n 
L 1 127 GLY 127 127 127 GLY GLY L . n 
L 1 128 LYS 128 128 128 LYS LYS L . n 
L 1 129 GLY 129 129 129 GLY GLY L . n 
L 1 130 GLY 130 130 130 GLY GLY L . n 
L 1 131 ASN 131 131 131 ASN ASN L . n 
L 1 132 GLU 132 132 132 GLU GLU L . n 
L 1 133 GLU 133 133 133 GLU GLU L . n 
L 1 134 SER 134 134 134 SER SER L . n 
L 1 135 THR 135 135 135 THR THR L . n 
L 1 136 LYS 136 136 136 LYS LYS L . n 
L 1 137 THR 137 137 137 THR THR L . n 
L 1 138 GLY 138 138 138 GLY GLY L . n 
L 1 139 ASN 139 139 139 ASN ASN L . n 
L 1 140 ALA 140 140 140 ALA ALA L . n 
L 1 141 GLY 141 141 141 GLY GLY L . n 
L 1 142 SER 142 142 142 SER SER L . n 
L 1 143 ARG 143 143 143 ARG ARG L . n 
L 1 144 LEU 144 144 144 LEU LEU L . n 
L 1 145 ALA 145 145 145 ALA ALA L . n 
L 1 146 CYS 146 146 146 CYS CYS L . n 
L 1 147 GLY 147 147 147 GLY GLY L . n 
L 1 148 VAL 148 148 148 VAL VAL L . n 
L 1 149 ILE 149 149 149 ILE ILE L . n 
L 1 150 GLY 150 150 150 GLY GLY L . n 
L 1 151 ILE 151 151 151 ILE ILE L . n 
L 1 152 ALA 152 152 152 ALA ALA L . n 
L 1 153 GLN 153 153 153 GLN GLN L . n 
M 1 1   ALA 1   1   ?   ?   ?   M . n 
M 1 2   THR 2   2   2   THR THR M . n 
M 1 3   LYS 3   3   3   LYS LYS M . n 
M 1 4   ALA 4   4   4   ALA ALA M . n 
M 1 5   VAL 5   5   5   VAL VAL M . n 
M 1 6   CYS 6   6   6   CYS CYS M . n 
M 1 7   VAL 7   7   7   VAL VAL M . n 
M 1 8   LEU 8   8   8   LEU LEU M . n 
M 1 9   LYS 9   9   9   LYS LYS M . n 
M 1 10  GLY 10  10  10  GLY GLY M . n 
M 1 11  ASP 11  11  11  ASP ASP M . n 
M 1 12  GLY 12  12  12  GLY GLY M . n 
M 1 13  PRO 13  13  13  PRO PRO M . n 
M 1 14  VAL 14  14  14  VAL VAL M . n 
M 1 15  GLN 15  15  15  GLN GLN M . n 
M 1 16  GLY 16  16  16  GLY GLY M . n 
M 1 17  ILE 17  17  17  ILE ILE M . n 
M 1 18  ILE 18  18  18  ILE ILE M . n 
M 1 19  ASN 19  19  19  ASN ASN M . n 
M 1 20  PHE 20  20  20  PHE PHE M . n 
M 1 21  GLU 21  21  21  GLU GLU M . n 
M 1 22  GLN 22  22  22  GLN GLN M . n 
M 1 23  LYS 23  23  23  LYS LYS M . n 
M 1 24  GLU 24  24  24  GLU GLU M . n 
M 1 25  SER 25  25  25  SER SER M . n 
M 1 26  ASN 26  26  26  ASN ASN M . n 
M 1 27  GLY 27  27  27  GLY GLY M . n 
M 1 28  PRO 28  28  28  PRO PRO M . n 
M 1 29  VAL 29  29  29  VAL VAL M . n 
M 1 30  LYS 30  30  30  LYS LYS M . n 
M 1 31  VAL 31  31  31  VAL VAL M . n 
M 1 32  TRP 32  32  32  TRP TRP M . n 
M 1 33  GLY 33  33  33  GLY GLY M . n 
M 1 34  SER 34  34  34  SER SER M . n 
M 1 35  ILE 35  35  35  ILE ILE M . n 
M 1 36  LYS 36  36  36  LYS LYS M . n 
M 1 37  GLY 37  37  37  GLY GLY M . n 
M 1 38  LEU 38  38  38  LEU LEU M . n 
M 1 39  THR 39  39  39  THR THR M . n 
M 1 40  GLU 40  40  40  GLU GLU M . n 
M 1 41  GLY 41  41  41  GLY GLY M . n 
M 1 42  LEU 42  42  42  LEU LEU M . n 
M 1 43  HIS 43  43  43  HIS HIS M . n 
M 1 44  GLY 44  44  44  GLY GLY M . n 
M 1 45  PHE 45  45  45  PHE PHE M . n 
M 1 46  HIS 46  46  46  HIS HIS M . n 
M 1 47  VAL 47  47  47  VAL VAL M . n 
M 1 48  HIS 48  48  48  HIS HIS M . n 
M 1 49  GLU 49  49  49  GLU GLU M . n 
M 1 50  PHE 50  50  50  PHE PHE M . n 
M 1 51  GLY 51  51  51  GLY GLY M . n 
M 1 52  ASP 52  52  52  ASP ASP M . n 
M 1 53  ASN 53  53  53  ASN ASN M . n 
M 1 54  THR 54  54  54  THR THR M . n 
M 1 55  ALA 55  55  55  ALA ALA M . n 
M 1 56  GLY 56  56  56  GLY GLY M . n 
M 1 57  CYS 57  57  57  CYS CYS M . n 
M 1 58  THR 58  58  58  THR THR M . n 
M 1 59  SER 59  59  59  SER SER M . n 
M 1 60  ALA 60  60  60  ALA ALA M . n 
M 1 61  GLY 61  61  61  GLY GLY M . n 
M 1 62  PRO 62  62  62  PRO PRO M . n 
M 1 63  HIS 63  63  63  HIS HIS M . n 
M 1 64  PHE 64  64  64  PHE PHE M . n 
M 1 65  ASN 65  65  65  ASN ASN M . n 
M 1 66  PRO 66  66  66  PRO PRO M . n 
M 1 67  LEU 67  67  67  LEU LEU M . n 
M 1 68  SER 68  68  68  SER SER M . n 
M 1 69  ARG 69  69  69  ARG ARG M . n 
M 1 70  LYS 70  70  70  LYS LYS M . n 
M 1 71  HIS 71  71  71  HIS HIS M . n 
M 1 72  GLY 72  72  72  GLY GLY M . n 
M 1 73  GLY 73  73  73  GLY GLY M . n 
M 1 74  PRO 74  74  74  PRO PRO M . n 
M 1 75  LYS 75  75  75  LYS LYS M . n 
M 1 76  ASP 76  76  76  ASP ASP M . n 
M 1 77  GLU 77  77  77  GLU GLU M . n 
M 1 78  GLU 78  78  78  GLU GLU M . n 
M 1 79  ARG 79  79  79  ARG ARG M . n 
M 1 80  HIS 80  80  80  HIS HIS M . n 
M 1 81  VAL 81  81  81  VAL VAL M . n 
M 1 82  GLY 82  82  82  GLY GLY M . n 
M 1 83  ASP 83  83  83  ASP ASP M . n 
M 1 84  LEU 84  84  84  LEU LEU M . n 
M 1 85  GLY 85  85  85  GLY GLY M . n 
M 1 86  ASN 86  86  86  ASN ASN M . n 
M 1 87  VAL 87  87  87  VAL VAL M . n 
M 1 88  THR 88  88  88  THR THR M . n 
M 1 89  ALA 89  89  89  ALA ALA M . n 
M 1 90  ASP 90  90  90  ASP ASP M . n 
M 1 91  LYS 91  91  91  LYS LYS M . n 
M 1 92  ASP 92  92  92  ASP ASP M . n 
M 1 93  GLY 93  93  93  GLY GLY M . n 
M 1 94  VAL 94  94  94  VAL VAL M . n 
M 1 95  ALA 95  95  95  ALA ALA M . n 
M 1 96  ASP 96  96  96  ASP ASP M . n 
M 1 97  VAL 97  97  97  VAL VAL M . n 
M 1 98  SER 98  98  98  SER SER M . n 
M 1 99  ILE 99  99  99  ILE ILE M . n 
M 1 100 GLU 100 100 100 GLU GLU M . n 
M 1 101 ASP 101 101 101 ASP ASP M . n 
M 1 102 SER 102 102 102 SER SER M . n 
M 1 103 VAL 103 103 103 VAL VAL M . n 
M 1 104 ILE 104 104 104 ILE ILE M . n 
M 1 105 SER 105 105 105 SER SER M . n 
M 1 106 LEU 106 106 106 LEU LEU M . n 
M 1 107 SER 107 107 107 SER SER M . n 
M 1 108 GLY 108 108 108 GLY GLY M . n 
M 1 109 ASP 109 109 109 ASP ASP M . n 
M 1 110 HIS 110 110 110 HIS HIS M . n 
M 1 111 CYS 111 111 111 CYS CYS M . n 
M 1 112 ILE 112 112 112 ILE ILE M . n 
M 1 113 ILE 113 113 113 ILE ILE M . n 
M 1 114 GLY 114 114 114 GLY GLY M . n 
M 1 115 ARG 115 115 115 ARG ARG M . n 
M 1 116 THR 116 116 116 THR THR M . n 
M 1 117 LEU 117 117 117 LEU LEU M . n 
M 1 118 VAL 118 118 118 VAL VAL M . n 
M 1 119 VAL 119 119 119 VAL VAL M . n 
M 1 120 HIS 120 120 120 HIS HIS M . n 
M 1 121 GLU 121 121 121 GLU GLU M . n 
M 1 122 LYS 122 122 122 LYS LYS M . n 
M 1 123 ALA 123 123 123 ALA ALA M . n 
M 1 124 ASP 124 124 124 ASP ASP M . n 
M 1 125 ASP 125 125 125 ASP ASP M . n 
M 1 126 LEU 126 126 126 LEU LEU M . n 
M 1 127 GLY 127 127 127 GLY GLY M . n 
M 1 128 LYS 128 128 128 LYS LYS M . n 
M 1 129 GLY 129 129 129 GLY GLY M . n 
M 1 130 GLY 130 130 130 GLY GLY M . n 
M 1 131 ASN 131 131 131 ASN ASN M . n 
M 1 132 GLU 132 132 132 GLU GLU M . n 
M 1 133 GLU 133 133 133 GLU GLU M . n 
M 1 134 SER 134 134 134 SER SER M . n 
M 1 135 THR 135 135 135 THR THR M . n 
M 1 136 LYS 136 136 136 LYS LYS M . n 
M 1 137 THR 137 137 137 THR THR M . n 
M 1 138 GLY 138 138 138 GLY GLY M . n 
M 1 139 ASN 139 139 139 ASN ASN M . n 
M 1 140 ALA 140 140 140 ALA ALA M . n 
M 1 141 GLY 141 141 141 GLY GLY M . n 
M 1 142 SER 142 142 142 SER SER M . n 
M 1 143 ARG 143 143 143 ARG ARG M . n 
M 1 144 LEU 144 144 144 LEU LEU M . n 
M 1 145 ALA 145 145 145 ALA ALA M . n 
M 1 146 CYS 146 146 146 CYS CYS M . n 
M 1 147 GLY 147 147 147 GLY GLY M . n 
M 1 148 VAL 148 148 148 VAL VAL M . n 
M 1 149 ILE 149 149 149 ILE ILE M . n 
M 1 150 GLY 150 150 150 GLY GLY M . n 
M 1 151 ILE 151 151 151 ILE ILE M . n 
M 1 152 ALA 152 152 152 ALA ALA M . n 
M 1 153 GLN 153 153 153 GLN GLN M . n 
N 1 1   ALA 1   1   1   ALA ALA N . n 
N 1 2   THR 2   2   2   THR THR N . n 
N 1 3   LYS 3   3   3   LYS LYS N . n 
N 1 4   ALA 4   4   4   ALA ALA N . n 
N 1 5   VAL 5   5   5   VAL VAL N . n 
N 1 6   CYS 6   6   6   CYS CYS N . n 
N 1 7   VAL 7   7   7   VAL VAL N . n 
N 1 8   LEU 8   8   8   LEU LEU N . n 
N 1 9   LYS 9   9   9   LYS LYS N . n 
N 1 10  GLY 10  10  10  GLY GLY N . n 
N 1 11  ASP 11  11  11  ASP ASP N . n 
N 1 12  GLY 12  12  12  GLY GLY N . n 
N 1 13  PRO 13  13  13  PRO PRO N . n 
N 1 14  VAL 14  14  14  VAL VAL N . n 
N 1 15  GLN 15  15  15  GLN GLN N . n 
N 1 16  GLY 16  16  16  GLY GLY N . n 
N 1 17  ILE 17  17  17  ILE ILE N . n 
N 1 18  ILE 18  18  18  ILE ILE N . n 
N 1 19  ASN 19  19  19  ASN ASN N . n 
N 1 20  PHE 20  20  20  PHE PHE N . n 
N 1 21  GLU 21  21  21  GLU GLU N . n 
N 1 22  GLN 22  22  22  GLN GLN N . n 
N 1 23  LYS 23  23  23  LYS LYS N . n 
N 1 24  GLU 24  24  24  GLU GLU N . n 
N 1 25  SER 25  25  25  SER SER N . n 
N 1 26  ASN 26  26  26  ASN ASN N . n 
N 1 27  GLY 27  27  27  GLY GLY N . n 
N 1 28  PRO 28  28  28  PRO PRO N . n 
N 1 29  VAL 29  29  29  VAL VAL N . n 
N 1 30  LYS 30  30  30  LYS LYS N . n 
N 1 31  VAL 31  31  31  VAL VAL N . n 
N 1 32  TRP 32  32  32  TRP TRP N . n 
N 1 33  GLY 33  33  33  GLY GLY N . n 
N 1 34  SER 34  34  34  SER SER N . n 
N 1 35  ILE 35  35  35  ILE ILE N . n 
N 1 36  LYS 36  36  36  LYS LYS N . n 
N 1 37  GLY 37  37  37  GLY GLY N . n 
N 1 38  LEU 38  38  38  LEU LEU N . n 
N 1 39  THR 39  39  39  THR THR N . n 
N 1 40  GLU 40  40  40  GLU GLU N . n 
N 1 41  GLY 41  41  41  GLY GLY N . n 
N 1 42  LEU 42  42  42  LEU LEU N . n 
N 1 43  HIS 43  43  43  HIS HIS N . n 
N 1 44  GLY 44  44  44  GLY GLY N . n 
N 1 45  PHE 45  45  45  PHE PHE N . n 
N 1 46  HIS 46  46  46  HIS HIS N . n 
N 1 47  VAL 47  47  47  VAL VAL N . n 
N 1 48  HIS 48  48  48  HIS HIS N . n 
N 1 49  GLU 49  49  49  GLU GLU N . n 
N 1 50  PHE 50  50  50  PHE PHE N . n 
N 1 51  GLY 51  51  51  GLY GLY N . n 
N 1 52  ASP 52  52  52  ASP ASP N . n 
N 1 53  ASN 53  53  53  ASN ASN N . n 
N 1 54  THR 54  54  54  THR THR N . n 
N 1 55  ALA 55  55  55  ALA ALA N . n 
N 1 56  GLY 56  56  56  GLY GLY N . n 
N 1 57  CYS 57  57  57  CYS CYS N . n 
N 1 58  THR 58  58  58  THR THR N . n 
N 1 59  SER 59  59  59  SER SER N . n 
N 1 60  ALA 60  60  60  ALA ALA N . n 
N 1 61  GLY 61  61  61  GLY GLY N . n 
N 1 62  PRO 62  62  62  PRO PRO N . n 
N 1 63  HIS 63  63  63  HIS HIS N . n 
N 1 64  PHE 64  64  64  PHE PHE N . n 
N 1 65  ASN 65  65  65  ASN ASN N . n 
N 1 66  PRO 66  66  66  PRO PRO N . n 
N 1 67  LEU 67  67  67  LEU LEU N . n 
N 1 68  SER 68  68  68  SER SER N . n 
N 1 69  ARG 69  69  69  ARG ARG N . n 
N 1 70  LYS 70  70  70  LYS LYS N . n 
N 1 71  HIS 71  71  71  HIS HIS N . n 
N 1 72  GLY 72  72  72  GLY GLY N . n 
N 1 73  GLY 73  73  73  GLY GLY N . n 
N 1 74  PRO 74  74  74  PRO PRO N . n 
N 1 75  LYS 75  75  75  LYS LYS N . n 
N 1 76  ASP 76  76  76  ASP ASP N . n 
N 1 77  GLU 77  77  77  GLU GLU N . n 
N 1 78  GLU 78  78  78  GLU GLU N . n 
N 1 79  ARG 79  79  79  ARG ARG N . n 
N 1 80  HIS 80  80  80  HIS HIS N . n 
N 1 81  VAL 81  81  81  VAL VAL N . n 
N 1 82  GLY 82  82  82  GLY GLY N . n 
N 1 83  ASP 83  83  83  ASP ASP N . n 
N 1 84  LEU 84  84  84  LEU LEU N . n 
N 1 85  GLY 85  85  85  GLY GLY N . n 
N 1 86  ASN 86  86  86  ASN ASN N . n 
N 1 87  VAL 87  87  87  VAL VAL N . n 
N 1 88  THR 88  88  88  THR THR N . n 
N 1 89  ALA 89  89  89  ALA ALA N . n 
N 1 90  ASP 90  90  90  ASP ASP N . n 
N 1 91  LYS 91  91  91  LYS LYS N . n 
N 1 92  ASP 92  92  92  ASP ASP N . n 
N 1 93  GLY 93  93  93  GLY GLY N . n 
N 1 94  VAL 94  94  94  VAL VAL N . n 
N 1 95  ALA 95  95  95  ALA ALA N . n 
N 1 96  ASP 96  96  96  ASP ASP N . n 
N 1 97  VAL 97  97  97  VAL VAL N . n 
N 1 98  SER 98  98  98  SER SER N . n 
N 1 99  ILE 99  99  99  ILE ILE N . n 
N 1 100 GLU 100 100 100 GLU GLU N . n 
N 1 101 ASP 101 101 101 ASP ASP N . n 
N 1 102 SER 102 102 102 SER SER N . n 
N 1 103 VAL 103 103 103 VAL VAL N . n 
N 1 104 ILE 104 104 104 ILE ILE N . n 
N 1 105 SER 105 105 105 SER SER N . n 
N 1 106 LEU 106 106 106 LEU LEU N . n 
N 1 107 SER 107 107 107 SER SER N . n 
N 1 108 GLY 108 108 108 GLY GLY N . n 
N 1 109 ASP 109 109 109 ASP ASP N . n 
N 1 110 HIS 110 110 110 HIS HIS N . n 
N 1 111 CYS 111 111 111 CYS CYS N . n 
N 1 112 ILE 112 112 112 ILE ILE N . n 
N 1 113 ILE 113 113 113 ILE ILE N . n 
N 1 114 GLY 114 114 114 GLY GLY N . n 
N 1 115 ARG 115 115 115 ARG ARG N . n 
N 1 116 THR 116 116 116 THR THR N . n 
N 1 117 LEU 117 117 117 LEU LEU N . n 
N 1 118 VAL 118 118 118 VAL VAL N . n 
N 1 119 VAL 119 119 119 VAL VAL N . n 
N 1 120 HIS 120 120 120 HIS HIS N . n 
N 1 121 GLU 121 121 121 GLU GLU N . n 
N 1 122 LYS 122 122 122 LYS LYS N . n 
N 1 123 ALA 123 123 123 ALA ALA N . n 
N 1 124 ASP 124 124 124 ASP ASP N . n 
N 1 125 ASP 125 125 125 ASP ASP N . n 
N 1 126 LEU 126 126 126 LEU LEU N . n 
N 1 127 GLY 127 127 127 GLY GLY N . n 
N 1 128 LYS 128 128 128 LYS LYS N . n 
N 1 129 GLY 129 129 129 GLY GLY N . n 
N 1 130 GLY 130 130 130 GLY GLY N . n 
N 1 131 ASN 131 131 131 ASN ASN N . n 
N 1 132 GLU 132 132 132 GLU GLU N . n 
N 1 133 GLU 133 133 133 GLU GLU N . n 
N 1 134 SER 134 134 134 SER SER N . n 
N 1 135 THR 135 135 135 THR THR N . n 
N 1 136 LYS 136 136 136 LYS LYS N . n 
N 1 137 THR 137 137 137 THR THR N . n 
N 1 138 GLY 138 138 138 GLY GLY N . n 
N 1 139 ASN 139 139 139 ASN ASN N . n 
N 1 140 ALA 140 140 140 ALA ALA N . n 
N 1 141 GLY 141 141 141 GLY GLY N . n 
N 1 142 SER 142 142 142 SER SER N . n 
N 1 143 ARG 143 143 143 ARG ARG N . n 
N 1 144 LEU 144 144 144 LEU LEU N . n 
N 1 145 ALA 145 145 145 ALA ALA N . n 
N 1 146 CYS 146 146 146 CYS CYS N . n 
N 1 147 GLY 147 147 147 GLY GLY N . n 
N 1 148 VAL 148 148 148 VAL VAL N . n 
N 1 149 ILE 149 149 149 ILE ILE N . n 
N 1 150 GLY 150 150 150 GLY GLY N . n 
N 1 151 ILE 151 151 151 ILE ILE N . n 
N 1 152 ALA 152 152 152 ALA ALA N . n 
N 1 153 GLN 153 153 153 GLN GLN N . n 
O 1 1   ALA 1   1   1   ALA ALA O . n 
O 1 2   THR 2   2   2   THR THR O . n 
O 1 3   LYS 3   3   3   LYS LYS O . n 
O 1 4   ALA 4   4   4   ALA ALA O . n 
O 1 5   VAL 5   5   5   VAL VAL O . n 
O 1 6   CYS 6   6   6   CYS CYS O . n 
O 1 7   VAL 7   7   7   VAL VAL O . n 
O 1 8   LEU 8   8   8   LEU LEU O . n 
O 1 9   LYS 9   9   9   LYS LYS O . n 
O 1 10  GLY 10  10  10  GLY GLY O . n 
O 1 11  ASP 11  11  11  ASP ASP O . n 
O 1 12  GLY 12  12  12  GLY GLY O . n 
O 1 13  PRO 13  13  13  PRO PRO O . n 
O 1 14  VAL 14  14  14  VAL VAL O . n 
O 1 15  GLN 15  15  15  GLN GLN O . n 
O 1 16  GLY 16  16  16  GLY GLY O . n 
O 1 17  ILE 17  17  17  ILE ILE O . n 
O 1 18  ILE 18  18  18  ILE ILE O . n 
O 1 19  ASN 19  19  19  ASN ASN O . n 
O 1 20  PHE 20  20  20  PHE PHE O . n 
O 1 21  GLU 21  21  21  GLU GLU O . n 
O 1 22  GLN 22  22  22  GLN GLN O . n 
O 1 23  LYS 23  23  23  LYS LYS O . n 
O 1 24  GLU 24  24  24  GLU GLU O . n 
O 1 25  SER 25  25  25  SER SER O . n 
O 1 26  ASN 26  26  26  ASN ASN O . n 
O 1 27  GLY 27  27  27  GLY GLY O . n 
O 1 28  PRO 28  28  28  PRO PRO O . n 
O 1 29  VAL 29  29  29  VAL VAL O . n 
O 1 30  LYS 30  30  30  LYS LYS O . n 
O 1 31  VAL 31  31  31  VAL VAL O . n 
O 1 32  TRP 32  32  32  TRP TRP O . n 
O 1 33  GLY 33  33  33  GLY GLY O . n 
O 1 34  SER 34  34  34  SER SER O . n 
O 1 35  ILE 35  35  35  ILE ILE O . n 
O 1 36  LYS 36  36  36  LYS LYS O . n 
O 1 37  GLY 37  37  37  GLY GLY O . n 
O 1 38  LEU 38  38  38  LEU LEU O . n 
O 1 39  THR 39  39  39  THR THR O . n 
O 1 40  GLU 40  40  40  GLU GLU O . n 
O 1 41  GLY 41  41  41  GLY GLY O . n 
O 1 42  LEU 42  42  42  LEU LEU O . n 
O 1 43  HIS 43  43  43  HIS HIS O . n 
O 1 44  GLY 44  44  44  GLY GLY O . n 
O 1 45  PHE 45  45  45  PHE PHE O . n 
O 1 46  HIS 46  46  46  HIS HIS O . n 
O 1 47  VAL 47  47  47  VAL VAL O . n 
O 1 48  HIS 48  48  48  HIS HIS O . n 
O 1 49  GLU 49  49  49  GLU GLU O . n 
O 1 50  PHE 50  50  50  PHE PHE O . n 
O 1 51  GLY 51  51  51  GLY GLY O . n 
O 1 52  ASP 52  52  52  ASP ASP O . n 
O 1 53  ASN 53  53  53  ASN ASN O . n 
O 1 54  THR 54  54  54  THR THR O . n 
O 1 55  ALA 55  55  55  ALA ALA O . n 
O 1 56  GLY 56  56  56  GLY GLY O . n 
O 1 57  CYS 57  57  57  CYS CYS O . n 
O 1 58  THR 58  58  58  THR THR O . n 
O 1 59  SER 59  59  59  SER SER O . n 
O 1 60  ALA 60  60  60  ALA ALA O . n 
O 1 61  GLY 61  61  61  GLY GLY O . n 
O 1 62  PRO 62  62  62  PRO PRO O . n 
O 1 63  HIS 63  63  63  HIS HIS O . n 
O 1 64  PHE 64  64  64  PHE PHE O . n 
O 1 65  ASN 65  65  65  ASN ASN O . n 
O 1 66  PRO 66  66  66  PRO PRO O . n 
O 1 67  LEU 67  67  67  LEU LEU O . n 
O 1 68  SER 68  68  68  SER SER O . n 
O 1 69  ARG 69  69  69  ARG ARG O . n 
O 1 70  LYS 70  70  70  LYS LYS O . n 
O 1 71  HIS 71  71  71  HIS HIS O . n 
O 1 72  GLY 72  72  72  GLY GLY O . n 
O 1 73  GLY 73  73  73  GLY GLY O . n 
O 1 74  PRO 74  74  74  PRO PRO O . n 
O 1 75  LYS 75  75  75  LYS LYS O . n 
O 1 76  ASP 76  76  76  ASP ASP O . n 
O 1 77  GLU 77  77  77  GLU GLU O . n 
O 1 78  GLU 78  78  78  GLU GLU O . n 
O 1 79  ARG 79  79  79  ARG ARG O . n 
O 1 80  HIS 80  80  80  HIS HIS O . n 
O 1 81  VAL 81  81  81  VAL VAL O . n 
O 1 82  GLY 82  82  82  GLY GLY O . n 
O 1 83  ASP 83  83  83  ASP ASP O . n 
O 1 84  LEU 84  84  84  LEU LEU O . n 
O 1 85  GLY 85  85  85  GLY GLY O . n 
O 1 86  ASN 86  86  86  ASN ASN O . n 
O 1 87  VAL 87  87  87  VAL VAL O . n 
O 1 88  THR 88  88  88  THR THR O . n 
O 1 89  ALA 89  89  89  ALA ALA O . n 
O 1 90  ASP 90  90  90  ASP ASP O . n 
O 1 91  LYS 91  91  91  LYS LYS O . n 
O 1 92  ASP 92  92  92  ASP ASP O . n 
O 1 93  GLY 93  93  93  GLY GLY O . n 
O 1 94  VAL 94  94  94  VAL VAL O . n 
O 1 95  ALA 95  95  95  ALA ALA O . n 
O 1 96  ASP 96  96  96  ASP ASP O . n 
O 1 97  VAL 97  97  97  VAL VAL O . n 
O 1 98  SER 98  98  98  SER SER O . n 
O 1 99  ILE 99  99  99  ILE ILE O . n 
O 1 100 GLU 100 100 100 GLU GLU O . n 
O 1 101 ASP 101 101 101 ASP ASP O . n 
O 1 102 SER 102 102 102 SER SER O . n 
O 1 103 VAL 103 103 103 VAL VAL O . n 
O 1 104 ILE 104 104 104 ILE ILE O . n 
O 1 105 SER 105 105 105 SER SER O . n 
O 1 106 LEU 106 106 106 LEU LEU O . n 
O 1 107 SER 107 107 107 SER SER O . n 
O 1 108 GLY 108 108 108 GLY GLY O . n 
O 1 109 ASP 109 109 109 ASP ASP O . n 
O 1 110 HIS 110 110 110 HIS HIS O . n 
O 1 111 CYS 111 111 111 CYS CYS O . n 
O 1 112 ILE 112 112 112 ILE ILE O . n 
O 1 113 ILE 113 113 113 ILE ILE O . n 
O 1 114 GLY 114 114 114 GLY GLY O . n 
O 1 115 ARG 115 115 115 ARG ARG O . n 
O 1 116 THR 116 116 116 THR THR O . n 
O 1 117 LEU 117 117 117 LEU LEU O . n 
O 1 118 VAL 118 118 118 VAL VAL O . n 
O 1 119 VAL 119 119 119 VAL VAL O . n 
O 1 120 HIS 120 120 120 HIS HIS O . n 
O 1 121 GLU 121 121 121 GLU GLU O . n 
O 1 122 LYS 122 122 122 LYS LYS O . n 
O 1 123 ALA 123 123 123 ALA ALA O . n 
O 1 124 ASP 124 124 124 ASP ASP O . n 
O 1 125 ASP 125 125 125 ASP ASP O . n 
O 1 126 LEU 126 126 126 LEU LEU O . n 
O 1 127 GLY 127 127 127 GLY GLY O . n 
O 1 128 LYS 128 128 128 LYS LYS O . n 
O 1 129 GLY 129 129 129 GLY GLY O . n 
O 1 130 GLY 130 130 130 GLY GLY O . n 
O 1 131 ASN 131 131 131 ASN ASN O . n 
O 1 132 GLU 132 132 132 GLU GLU O . n 
O 1 133 GLU 133 133 133 GLU GLU O . n 
O 1 134 SER 134 134 134 SER SER O . n 
O 1 135 THR 135 135 135 THR THR O . n 
O 1 136 LYS 136 136 136 LYS LYS O . n 
O 1 137 THR 137 137 137 THR THR O . n 
O 1 138 GLY 138 138 138 GLY GLY O . n 
O 1 139 ASN 139 139 139 ASN ASN O . n 
O 1 140 ALA 140 140 140 ALA ALA O . n 
O 1 141 GLY 141 141 141 GLY GLY O . n 
O 1 142 SER 142 142 142 SER SER O . n 
O 1 143 ARG 143 143 143 ARG ARG O . n 
O 1 144 LEU 144 144 144 LEU LEU O . n 
O 1 145 ALA 145 145 145 ALA ALA O . n 
O 1 146 CYS 146 146 146 CYS CYS O . n 
O 1 147 GLY 147 147 147 GLY GLY O . n 
O 1 148 VAL 148 148 148 VAL VAL O . n 
O 1 149 ILE 149 149 149 ILE ILE O . n 
O 1 150 GLY 150 150 150 GLY GLY O . n 
O 1 151 ILE 151 151 151 ILE ILE O . n 
O 1 152 ALA 152 152 152 ALA ALA O . n 
O 1 153 GLN 153 153 153 GLN GLN O . n 
P 1 1   ALA 1   1   1   ALA ALA P . n 
P 1 2   THR 2   2   2   THR THR P . n 
P 1 3   LYS 3   3   3   LYS LYS P . n 
P 1 4   ALA 4   4   4   ALA ALA P . n 
P 1 5   VAL 5   5   5   VAL VAL P . n 
P 1 6   CYS 6   6   6   CYS CYS P . n 
P 1 7   VAL 7   7   7   VAL VAL P . n 
P 1 8   LEU 8   8   8   LEU LEU P . n 
P 1 9   LYS 9   9   9   LYS LYS P . n 
P 1 10  GLY 10  10  10  GLY GLY P . n 
P 1 11  ASP 11  11  11  ASP ASP P . n 
P 1 12  GLY 12  12  12  GLY GLY P . n 
P 1 13  PRO 13  13  13  PRO PRO P . n 
P 1 14  VAL 14  14  14  VAL VAL P . n 
P 1 15  GLN 15  15  15  GLN GLN P . n 
P 1 16  GLY 16  16  16  GLY GLY P . n 
P 1 17  ILE 17  17  17  ILE ILE P . n 
P 1 18  ILE 18  18  18  ILE ILE P . n 
P 1 19  ASN 19  19  19  ASN ASN P . n 
P 1 20  PHE 20  20  20  PHE PHE P . n 
P 1 21  GLU 21  21  21  GLU GLU P . n 
P 1 22  GLN 22  22  22  GLN GLN P . n 
P 1 23  LYS 23  23  23  LYS LYS P . n 
P 1 24  GLU 24  24  24  GLU GLU P . n 
P 1 25  SER 25  25  25  SER SER P . n 
P 1 26  ASN 26  26  26  ASN ASN P . n 
P 1 27  GLY 27  27  27  GLY GLY P . n 
P 1 28  PRO 28  28  28  PRO PRO P . n 
P 1 29  VAL 29  29  29  VAL VAL P . n 
P 1 30  LYS 30  30  30  LYS LYS P . n 
P 1 31  VAL 31  31  31  VAL VAL P . n 
P 1 32  TRP 32  32  32  TRP TRP P . n 
P 1 33  GLY 33  33  33  GLY GLY P . n 
P 1 34  SER 34  34  34  SER SER P . n 
P 1 35  ILE 35  35  35  ILE ILE P . n 
P 1 36  LYS 36  36  36  LYS LYS P . n 
P 1 37  GLY 37  37  37  GLY GLY P . n 
P 1 38  LEU 38  38  38  LEU LEU P . n 
P 1 39  THR 39  39  39  THR THR P . n 
P 1 40  GLU 40  40  40  GLU GLU P . n 
P 1 41  GLY 41  41  41  GLY GLY P . n 
P 1 42  LEU 42  42  42  LEU LEU P . n 
P 1 43  HIS 43  43  43  HIS HIS P . n 
P 1 44  GLY 44  44  44  GLY GLY P . n 
P 1 45  PHE 45  45  45  PHE PHE P . n 
P 1 46  HIS 46  46  46  HIS HIS P . n 
P 1 47  VAL 47  47  47  VAL VAL P . n 
P 1 48  HIS 48  48  48  HIS HIS P . n 
P 1 49  GLU 49  49  49  GLU GLU P . n 
P 1 50  PHE 50  50  50  PHE PHE P . n 
P 1 51  GLY 51  51  51  GLY GLY P . n 
P 1 52  ASP 52  52  52  ASP ASP P . n 
P 1 53  ASN 53  53  53  ASN ASN P . n 
P 1 54  THR 54  54  54  THR THR P . n 
P 1 55  ALA 55  55  55  ALA ALA P . n 
P 1 56  GLY 56  56  56  GLY GLY P . n 
P 1 57  CYS 57  57  57  CYS CYS P . n 
P 1 58  THR 58  58  58  THR THR P . n 
P 1 59  SER 59  59  59  SER SER P . n 
P 1 60  ALA 60  60  60  ALA ALA P . n 
P 1 61  GLY 61  61  61  GLY GLY P . n 
P 1 62  PRO 62  62  62  PRO PRO P . n 
P 1 63  HIS 63  63  63  HIS HIS P . n 
P 1 64  PHE 64  64  64  PHE PHE P . n 
P 1 65  ASN 65  65  65  ASN ASN P . n 
P 1 66  PRO 66  66  66  PRO PRO P . n 
P 1 67  LEU 67  67  67  LEU LEU P . n 
P 1 68  SER 68  68  68  SER SER P . n 
P 1 69  ARG 69  69  69  ARG ARG P . n 
P 1 70  LYS 70  70  70  LYS LYS P . n 
P 1 71  HIS 71  71  71  HIS HIS P . n 
P 1 72  GLY 72  72  72  GLY GLY P . n 
P 1 73  GLY 73  73  73  GLY GLY P . n 
P 1 74  PRO 74  74  74  PRO PRO P . n 
P 1 75  LYS 75  75  75  LYS LYS P . n 
P 1 76  ASP 76  76  76  ASP ASP P . n 
P 1 77  GLU 77  77  77  GLU GLU P . n 
P 1 78  GLU 78  78  78  GLU GLU P . n 
P 1 79  ARG 79  79  79  ARG ARG P . n 
P 1 80  HIS 80  80  80  HIS HIS P . n 
P 1 81  VAL 81  81  81  VAL VAL P . n 
P 1 82  GLY 82  82  82  GLY GLY P . n 
P 1 83  ASP 83  83  83  ASP ASP P . n 
P 1 84  LEU 84  84  84  LEU LEU P . n 
P 1 85  GLY 85  85  85  GLY GLY P . n 
P 1 86  ASN 86  86  86  ASN ASN P . n 
P 1 87  VAL 87  87  87  VAL VAL P . n 
P 1 88  THR 88  88  88  THR THR P . n 
P 1 89  ALA 89  89  89  ALA ALA P . n 
P 1 90  ASP 90  90  90  ASP ASP P . n 
P 1 91  LYS 91  91  91  LYS LYS P . n 
P 1 92  ASP 92  92  92  ASP ASP P . n 
P 1 93  GLY 93  93  93  GLY GLY P . n 
P 1 94  VAL 94  94  94  VAL VAL P . n 
P 1 95  ALA 95  95  95  ALA ALA P . n 
P 1 96  ASP 96  96  96  ASP ASP P . n 
P 1 97  VAL 97  97  97  VAL VAL P . n 
P 1 98  SER 98  98  98  SER SER P . n 
P 1 99  ILE 99  99  99  ILE ILE P . n 
P 1 100 GLU 100 100 100 GLU GLU P . n 
P 1 101 ASP 101 101 101 ASP ASP P . n 
P 1 102 SER 102 102 102 SER SER P . n 
P 1 103 VAL 103 103 103 VAL VAL P . n 
P 1 104 ILE 104 104 104 ILE ILE P . n 
P 1 105 SER 105 105 105 SER SER P . n 
P 1 106 LEU 106 106 106 LEU LEU P . n 
P 1 107 SER 107 107 107 SER SER P . n 
P 1 108 GLY 108 108 108 GLY GLY P . n 
P 1 109 ASP 109 109 109 ASP ASP P . n 
P 1 110 HIS 110 110 110 HIS HIS P . n 
P 1 111 CYS 111 111 111 CYS CYS P . n 
P 1 112 ILE 112 112 112 ILE ILE P . n 
P 1 113 ILE 113 113 113 ILE ILE P . n 
P 1 114 GLY 114 114 114 GLY GLY P . n 
P 1 115 ARG 115 115 115 ARG ARG P . n 
P 1 116 THR 116 116 116 THR THR P . n 
P 1 117 LEU 117 117 117 LEU LEU P . n 
P 1 118 VAL 118 118 118 VAL VAL P . n 
P 1 119 VAL 119 119 119 VAL VAL P . n 
P 1 120 HIS 120 120 120 HIS HIS P . n 
P 1 121 GLU 121 121 121 GLU GLU P . n 
P 1 122 LYS 122 122 122 LYS LYS P . n 
P 1 123 ALA 123 123 123 ALA ALA P . n 
P 1 124 ASP 124 124 124 ASP ASP P . n 
P 1 125 ASP 125 125 125 ASP ASP P . n 
P 1 126 LEU 126 126 126 LEU LEU P . n 
P 1 127 GLY 127 127 127 GLY GLY P . n 
P 1 128 LYS 128 128 128 LYS LYS P . n 
P 1 129 GLY 129 129 129 GLY GLY P . n 
P 1 130 GLY 130 130 130 GLY GLY P . n 
P 1 131 ASN 131 131 131 ASN ASN P . n 
P 1 132 GLU 132 132 132 GLU GLU P . n 
P 1 133 GLU 133 133 133 GLU GLU P . n 
P 1 134 SER 134 134 134 SER SER P . n 
P 1 135 THR 135 135 135 THR THR P . n 
P 1 136 LYS 136 136 136 LYS LYS P . n 
P 1 137 THR 137 137 137 THR THR P . n 
P 1 138 GLY 138 138 138 GLY GLY P . n 
P 1 139 ASN 139 139 139 ASN ASN P . n 
P 1 140 ALA 140 140 140 ALA ALA P . n 
P 1 141 GLY 141 141 141 GLY GLY P . n 
P 1 142 SER 142 142 142 SER SER P . n 
P 1 143 ARG 143 143 143 ARG ARG P . n 
P 1 144 LEU 144 144 144 LEU LEU P . n 
P 1 145 ALA 145 145 145 ALA ALA P . n 
P 1 146 CYS 146 146 146 CYS CYS P . n 
P 1 147 GLY 147 147 147 GLY GLY P . n 
P 1 148 VAL 148 148 148 VAL VAL P . n 
P 1 149 ILE 149 149 149 ILE ILE P . n 
P 1 150 GLY 150 150 150 GLY GLY P . n 
P 1 151 ILE 151 151 151 ILE ILE P . n 
P 1 152 ALA 152 152 152 ALA ALA P . n 
P 1 153 GLN 153 153 153 GLN GLN P . n 
Q 1 1   ALA 1   1   1   ALA ALA Q . n 
Q 1 2   THR 2   2   2   THR THR Q . n 
Q 1 3   LYS 3   3   3   LYS LYS Q . n 
Q 1 4   ALA 4   4   4   ALA ALA Q . n 
Q 1 5   VAL 5   5   5   VAL VAL Q . n 
Q 1 6   CYS 6   6   6   CYS CYS Q . n 
Q 1 7   VAL 7   7   7   VAL VAL Q . n 
Q 1 8   LEU 8   8   8   LEU LEU Q . n 
Q 1 9   LYS 9   9   9   LYS LYS Q . n 
Q 1 10  GLY 10  10  10  GLY GLY Q . n 
Q 1 11  ASP 11  11  11  ASP ASP Q . n 
Q 1 12  GLY 12  12  12  GLY GLY Q . n 
Q 1 13  PRO 13  13  13  PRO PRO Q . n 
Q 1 14  VAL 14  14  14  VAL VAL Q . n 
Q 1 15  GLN 15  15  15  GLN GLN Q . n 
Q 1 16  GLY 16  16  16  GLY GLY Q . n 
Q 1 17  ILE 17  17  17  ILE ILE Q . n 
Q 1 18  ILE 18  18  18  ILE ILE Q . n 
Q 1 19  ASN 19  19  19  ASN ASN Q . n 
Q 1 20  PHE 20  20  20  PHE PHE Q . n 
Q 1 21  GLU 21  21  21  GLU GLU Q . n 
Q 1 22  GLN 22  22  22  GLN GLN Q . n 
Q 1 23  LYS 23  23  23  LYS LYS Q . n 
Q 1 24  GLU 24  24  24  GLU GLU Q . n 
Q 1 25  SER 25  25  25  SER SER Q . n 
Q 1 26  ASN 26  26  26  ASN ASN Q . n 
Q 1 27  GLY 27  27  27  GLY GLY Q . n 
Q 1 28  PRO 28  28  28  PRO PRO Q . n 
Q 1 29  VAL 29  29  29  VAL VAL Q . n 
Q 1 30  LYS 30  30  30  LYS LYS Q . n 
Q 1 31  VAL 31  31  31  VAL VAL Q . n 
Q 1 32  TRP 32  32  32  TRP TRP Q . n 
Q 1 33  GLY 33  33  33  GLY GLY Q . n 
Q 1 34  SER 34  34  34  SER SER Q . n 
Q 1 35  ILE 35  35  35  ILE ILE Q . n 
Q 1 36  LYS 36  36  36  LYS LYS Q . n 
Q 1 37  GLY 37  37  37  GLY GLY Q . n 
Q 1 38  LEU 38  38  38  LEU LEU Q . n 
Q 1 39  THR 39  39  39  THR THR Q . n 
Q 1 40  GLU 40  40  40  GLU GLU Q . n 
Q 1 41  GLY 41  41  41  GLY GLY Q . n 
Q 1 42  LEU 42  42  42  LEU LEU Q . n 
Q 1 43  HIS 43  43  43  HIS HIS Q . n 
Q 1 44  GLY 44  44  44  GLY GLY Q . n 
Q 1 45  PHE 45  45  45  PHE PHE Q . n 
Q 1 46  HIS 46  46  46  HIS HIS Q . n 
Q 1 47  VAL 47  47  47  VAL VAL Q . n 
Q 1 48  HIS 48  48  48  HIS HIS Q . n 
Q 1 49  GLU 49  49  49  GLU GLU Q . n 
Q 1 50  PHE 50  50  50  PHE PHE Q . n 
Q 1 51  GLY 51  51  51  GLY GLY Q . n 
Q 1 52  ASP 52  52  52  ASP ASP Q . n 
Q 1 53  ASN 53  53  53  ASN ASN Q . n 
Q 1 54  THR 54  54  54  THR THR Q . n 
Q 1 55  ALA 55  55  55  ALA ALA Q . n 
Q 1 56  GLY 56  56  56  GLY GLY Q . n 
Q 1 57  CYS 57  57  57  CYS CYS Q . n 
Q 1 58  THR 58  58  58  THR THR Q . n 
Q 1 59  SER 59  59  59  SER SER Q . n 
Q 1 60  ALA 60  60  60  ALA ALA Q . n 
Q 1 61  GLY 61  61  61  GLY GLY Q . n 
Q 1 62  PRO 62  62  62  PRO PRO Q . n 
Q 1 63  HIS 63  63  63  HIS HIS Q . n 
Q 1 64  PHE 64  64  64  PHE PHE Q . n 
Q 1 65  ASN 65  65  65  ASN ASN Q . n 
Q 1 66  PRO 66  66  66  PRO PRO Q . n 
Q 1 67  LEU 67  67  67  LEU LEU Q . n 
Q 1 68  SER 68  68  68  SER SER Q . n 
Q 1 69  ARG 69  69  69  ARG ARG Q . n 
Q 1 70  LYS 70  70  70  LYS LYS Q . n 
Q 1 71  HIS 71  71  71  HIS HIS Q . n 
Q 1 72  GLY 72  72  72  GLY GLY Q . n 
Q 1 73  GLY 73  73  73  GLY GLY Q . n 
Q 1 74  PRO 74  74  74  PRO PRO Q . n 
Q 1 75  LYS 75  75  75  LYS LYS Q . n 
Q 1 76  ASP 76  76  76  ASP ASP Q . n 
Q 1 77  GLU 77  77  77  GLU GLU Q . n 
Q 1 78  GLU 78  78  78  GLU GLU Q . n 
Q 1 79  ARG 79  79  79  ARG ARG Q . n 
Q 1 80  HIS 80  80  80  HIS HIS Q . n 
Q 1 81  VAL 81  81  81  VAL VAL Q . n 
Q 1 82  GLY 82  82  82  GLY GLY Q . n 
Q 1 83  ASP 83  83  83  ASP ASP Q . n 
Q 1 84  LEU 84  84  84  LEU LEU Q . n 
Q 1 85  GLY 85  85  85  GLY GLY Q . n 
Q 1 86  ASN 86  86  86  ASN ASN Q . n 
Q 1 87  VAL 87  87  87  VAL VAL Q . n 
Q 1 88  THR 88  88  88  THR THR Q . n 
Q 1 89  ALA 89  89  89  ALA ALA Q . n 
Q 1 90  ASP 90  90  90  ASP ASP Q . n 
Q 1 91  LYS 91  91  91  LYS LYS Q . n 
Q 1 92  ASP 92  92  92  ASP ASP Q . n 
Q 1 93  GLY 93  93  93  GLY GLY Q . n 
Q 1 94  VAL 94  94  94  VAL VAL Q . n 
Q 1 95  ALA 95  95  95  ALA ALA Q . n 
Q 1 96  ASP 96  96  96  ASP ASP Q . n 
Q 1 97  VAL 97  97  97  VAL VAL Q . n 
Q 1 98  SER 98  98  98  SER SER Q . n 
Q 1 99  ILE 99  99  99  ILE ILE Q . n 
Q 1 100 GLU 100 100 100 GLU GLU Q . n 
Q 1 101 ASP 101 101 101 ASP ASP Q . n 
Q 1 102 SER 102 102 102 SER SER Q . n 
Q 1 103 VAL 103 103 103 VAL VAL Q . n 
Q 1 104 ILE 104 104 104 ILE ILE Q . n 
Q 1 105 SER 105 105 105 SER SER Q . n 
Q 1 106 LEU 106 106 106 LEU LEU Q . n 
Q 1 107 SER 107 107 107 SER SER Q . n 
Q 1 108 GLY 108 108 108 GLY GLY Q . n 
Q 1 109 ASP 109 109 109 ASP ASP Q . n 
Q 1 110 HIS 110 110 110 HIS HIS Q . n 
Q 1 111 CYS 111 111 111 CYS CYS Q . n 
Q 1 112 ILE 112 112 112 ILE ILE Q . n 
Q 1 113 ILE 113 113 113 ILE ILE Q . n 
Q 1 114 GLY 114 114 114 GLY GLY Q . n 
Q 1 115 ARG 115 115 115 ARG ARG Q . n 
Q 1 116 THR 116 116 116 THR THR Q . n 
Q 1 117 LEU 117 117 117 LEU LEU Q . n 
Q 1 118 VAL 118 118 118 VAL VAL Q . n 
Q 1 119 VAL 119 119 119 VAL VAL Q . n 
Q 1 120 HIS 120 120 120 HIS HIS Q . n 
Q 1 121 GLU 121 121 121 GLU GLU Q . n 
Q 1 122 LYS 122 122 122 LYS LYS Q . n 
Q 1 123 ALA 123 123 123 ALA ALA Q . n 
Q 1 124 ASP 124 124 124 ASP ASP Q . n 
Q 1 125 ASP 125 125 125 ASP ASP Q . n 
Q 1 126 LEU 126 126 126 LEU LEU Q . n 
Q 1 127 GLY 127 127 127 GLY GLY Q . n 
Q 1 128 LYS 128 128 128 LYS LYS Q . n 
Q 1 129 GLY 129 129 129 GLY GLY Q . n 
Q 1 130 GLY 130 130 130 GLY GLY Q . n 
Q 1 131 ASN 131 131 131 ASN ASN Q . n 
Q 1 132 GLU 132 132 132 GLU GLU Q . n 
Q 1 133 GLU 133 133 133 GLU GLU Q . n 
Q 1 134 SER 134 134 134 SER SER Q . n 
Q 1 135 THR 135 135 135 THR THR Q . n 
Q 1 136 LYS 136 136 136 LYS LYS Q . n 
Q 1 137 THR 137 137 137 THR THR Q . n 
Q 1 138 GLY 138 138 138 GLY GLY Q . n 
Q 1 139 ASN 139 139 139 ASN ASN Q . n 
Q 1 140 ALA 140 140 140 ALA ALA Q . n 
Q 1 141 GLY 141 141 141 GLY GLY Q . n 
Q 1 142 SER 142 142 142 SER SER Q . n 
Q 1 143 ARG 143 143 143 ARG ARG Q . n 
Q 1 144 LEU 144 144 144 LEU LEU Q . n 
Q 1 145 ALA 145 145 145 ALA ALA Q . n 
Q 1 146 CYS 146 146 146 CYS CYS Q . n 
Q 1 147 GLY 147 147 147 GLY GLY Q . n 
Q 1 148 VAL 148 148 148 VAL VAL Q . n 
Q 1 149 ILE 149 149 149 ILE ILE Q . n 
Q 1 150 GLY 150 150 150 GLY GLY Q . n 
Q 1 151 ILE 151 151 151 ILE ILE Q . n 
Q 1 152 ALA 152 152 152 ALA ALA Q . n 
Q 1 153 GLN 153 153 153 GLN GLN Q . n 
R 1 1   ALA 1   1   1   ALA ALA S . n 
R 1 2   THR 2   2   2   THR THR S . n 
R 1 3   LYS 3   3   3   LYS LYS S . n 
R 1 4   ALA 4   4   4   ALA ALA S . n 
R 1 5   VAL 5   5   5   VAL VAL S . n 
R 1 6   CYS 6   6   6   CYS CYS S . n 
R 1 7   VAL 7   7   7   VAL VAL S . n 
R 1 8   LEU 8   8   8   LEU LEU S . n 
R 1 9   LYS 9   9   9   LYS LYS S . n 
R 1 10  GLY 10  10  10  GLY GLY S . n 
R 1 11  ASP 11  11  11  ASP ASP S . n 
R 1 12  GLY 12  12  12  GLY GLY S . n 
R 1 13  PRO 13  13  13  PRO PRO S . n 
R 1 14  VAL 14  14  14  VAL VAL S . n 
R 1 15  GLN 15  15  15  GLN GLN S . n 
R 1 16  GLY 16  16  16  GLY GLY S . n 
R 1 17  ILE 17  17  17  ILE ILE S . n 
R 1 18  ILE 18  18  18  ILE ILE S . n 
R 1 19  ASN 19  19  19  ASN ASN S . n 
R 1 20  PHE 20  20  20  PHE PHE S . n 
R 1 21  GLU 21  21  21  GLU GLU S . n 
R 1 22  GLN 22  22  22  GLN GLN S . n 
R 1 23  LYS 23  23  23  LYS LYS S . n 
R 1 24  GLU 24  24  24  GLU GLU S . n 
R 1 25  SER 25  25  25  SER SER S . n 
R 1 26  ASN 26  26  26  ASN ASN S . n 
R 1 27  GLY 27  27  27  GLY GLY S . n 
R 1 28  PRO 28  28  28  PRO PRO S . n 
R 1 29  VAL 29  29  29  VAL VAL S . n 
R 1 30  LYS 30  30  30  LYS LYS S . n 
R 1 31  VAL 31  31  31  VAL VAL S . n 
R 1 32  TRP 32  32  32  TRP TRP S . n 
R 1 33  GLY 33  33  33  GLY GLY S . n 
R 1 34  SER 34  34  34  SER SER S . n 
R 1 35  ILE 35  35  35  ILE ILE S . n 
R 1 36  LYS 36  36  36  LYS LYS S . n 
R 1 37  GLY 37  37  37  GLY GLY S . n 
R 1 38  LEU 38  38  38  LEU LEU S . n 
R 1 39  THR 39  39  39  THR THR S . n 
R 1 40  GLU 40  40  40  GLU GLU S . n 
R 1 41  GLY 41  41  41  GLY GLY S . n 
R 1 42  LEU 42  42  42  LEU LEU S . n 
R 1 43  HIS 43  43  43  HIS HIS S . n 
R 1 44  GLY 44  44  44  GLY GLY S . n 
R 1 45  PHE 45  45  45  PHE PHE S . n 
R 1 46  HIS 46  46  46  HIS HIS S . n 
R 1 47  VAL 47  47  47  VAL VAL S . n 
R 1 48  HIS 48  48  48  HIS HIS S . n 
R 1 49  GLU 49  49  49  GLU GLU S . n 
R 1 50  PHE 50  50  50  PHE PHE S . n 
R 1 51  GLY 51  51  51  GLY GLY S . n 
R 1 52  ASP 52  52  52  ASP ASP S . n 
R 1 53  ASN 53  53  53  ASN ASN S . n 
R 1 54  THR 54  54  54  THR THR S . n 
R 1 55  ALA 55  55  55  ALA ALA S . n 
R 1 56  GLY 56  56  56  GLY GLY S . n 
R 1 57  CYS 57  57  57  CYS CYS S . n 
R 1 58  THR 58  58  58  THR THR S . n 
R 1 59  SER 59  59  59  SER SER S . n 
R 1 60  ALA 60  60  60  ALA ALA S . n 
R 1 61  GLY 61  61  61  GLY GLY S . n 
R 1 62  PRO 62  62  62  PRO PRO S . n 
R 1 63  HIS 63  63  63  HIS HIS S . n 
R 1 64  PHE 64  64  64  PHE PHE S . n 
R 1 65  ASN 65  65  65  ASN ASN S . n 
R 1 66  PRO 66  66  66  PRO PRO S . n 
R 1 67  LEU 67  67  67  LEU LEU S . n 
R 1 68  SER 68  68  68  SER SER S . n 
R 1 69  ARG 69  69  69  ARG ARG S . n 
R 1 70  LYS 70  70  70  LYS LYS S . n 
R 1 71  HIS 71  71  71  HIS HIS S . n 
R 1 72  GLY 72  72  72  GLY GLY S . n 
R 1 73  GLY 73  73  73  GLY GLY S . n 
R 1 74  PRO 74  74  74  PRO PRO S . n 
R 1 75  LYS 75  75  75  LYS LYS S . n 
R 1 76  ASP 76  76  76  ASP ASP S . n 
R 1 77  GLU 77  77  77  GLU GLU S . n 
R 1 78  GLU 78  78  78  GLU GLU S . n 
R 1 79  ARG 79  79  79  ARG ARG S . n 
R 1 80  HIS 80  80  80  HIS HIS S . n 
R 1 81  VAL 81  81  81  VAL VAL S . n 
R 1 82  GLY 82  82  82  GLY GLY S . n 
R 1 83  ASP 83  83  83  ASP ASP S . n 
R 1 84  LEU 84  84  84  LEU LEU S . n 
R 1 85  GLY 85  85  85  GLY GLY S . n 
R 1 86  ASN 86  86  86  ASN ASN S . n 
R 1 87  VAL 87  87  87  VAL VAL S . n 
R 1 88  THR 88  88  88  THR THR S . n 
R 1 89  ALA 89  89  89  ALA ALA S . n 
R 1 90  ASP 90  90  90  ASP ASP S . n 
R 1 91  LYS 91  91  91  LYS LYS S . n 
R 1 92  ASP 92  92  92  ASP ASP S . n 
R 1 93  GLY 93  93  93  GLY GLY S . n 
R 1 94  VAL 94  94  94  VAL VAL S . n 
R 1 95  ALA 95  95  95  ALA ALA S . n 
R 1 96  ASP 96  96  96  ASP ASP S . n 
R 1 97  VAL 97  97  97  VAL VAL S . n 
R 1 98  SER 98  98  98  SER SER S . n 
R 1 99  ILE 99  99  99  ILE ILE S . n 
R 1 100 GLU 100 100 100 GLU GLU S . n 
R 1 101 ASP 101 101 101 ASP ASP S . n 
R 1 102 SER 102 102 102 SER SER S . n 
R 1 103 VAL 103 103 103 VAL VAL S . n 
R 1 104 ILE 104 104 104 ILE ILE S . n 
R 1 105 SER 105 105 105 SER SER S . n 
R 1 106 LEU 106 106 106 LEU LEU S . n 
R 1 107 SER 107 107 107 SER SER S . n 
R 1 108 GLY 108 108 108 GLY GLY S . n 
R 1 109 ASP 109 109 109 ASP ASP S . n 
R 1 110 HIS 110 110 110 HIS HIS S . n 
R 1 111 CYS 111 111 111 CYS CYS S . n 
R 1 112 ILE 112 112 112 ILE ILE S . n 
R 1 113 ILE 113 113 113 ILE ILE S . n 
R 1 114 GLY 114 114 114 GLY GLY S . n 
R 1 115 ARG 115 115 115 ARG ARG S . n 
R 1 116 THR 116 116 116 THR THR S . n 
R 1 117 LEU 117 117 117 LEU LEU S . n 
R 1 118 VAL 118 118 118 VAL VAL S . n 
R 1 119 VAL 119 119 119 VAL VAL S . n 
R 1 120 HIS 120 120 120 HIS HIS S . n 
R 1 121 GLU 121 121 121 GLU GLU S . n 
R 1 122 LYS 122 122 122 LYS LYS S . n 
R 1 123 ALA 123 123 123 ALA ALA S . n 
R 1 124 ASP 124 124 124 ASP ASP S . n 
R 1 125 ASP 125 125 125 ASP ASP S . n 
R 1 126 LEU 126 126 126 LEU LEU S . n 
R 1 127 GLY 127 127 127 GLY GLY S . n 
R 1 128 LYS 128 128 128 LYS LYS S . n 
R 1 129 GLY 129 129 129 GLY GLY S . n 
R 1 130 GLY 130 130 130 GLY GLY S . n 
R 1 131 ASN 131 131 131 ASN ASN S . n 
R 1 132 GLU 132 132 132 GLU GLU S . n 
R 1 133 GLU 133 133 133 GLU GLU S . n 
R 1 134 SER 134 134 134 SER SER S . n 
R 1 135 THR 135 135 135 THR THR S . n 
R 1 136 LYS 136 136 136 LYS LYS S . n 
R 1 137 THR 137 137 137 THR THR S . n 
R 1 138 GLY 138 138 138 GLY GLY S . n 
R 1 139 ASN 139 139 139 ASN ASN S . n 
R 1 140 ALA 140 140 140 ALA ALA S . n 
R 1 141 GLY 141 141 141 GLY GLY S . n 
R 1 142 SER 142 142 142 SER SER S . n 
R 1 143 ARG 143 143 143 ARG ARG S . n 
R 1 144 LEU 144 144 144 LEU LEU S . n 
R 1 145 ALA 145 145 145 ALA ALA S . n 
R 1 146 CYS 146 146 146 CYS CYS S . n 
R 1 147 GLY 147 147 147 GLY GLY S . n 
R 1 148 VAL 148 148 148 VAL VAL S . n 
R 1 149 ILE 149 149 149 ILE ILE S . n 
R 1 150 GLY 150 150 150 GLY GLY S . n 
R 1 151 ILE 151 151 151 ILE ILE S . n 
R 1 152 ALA 152 152 152 ALA ALA S . n 
R 1 153 GLN 153 153 153 GLN GLN S . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
S  2 CU  1   154  154  CU  CU  A . 
T  3 ZN  1   155  155  ZN  ZN  A . 
U  2 CU  1   154  154  CU  CU  B . 
V  3 ZN  1   155  155  ZN  ZN  B . 
W  2 CU  1   154  154  CU  CU  C . 
X  3 ZN  1   155  155  ZN  ZN  C . 
Y  4 CA  1   156  156  CA  CA  C . 
Z  2 CU  1   154  154  CU  CU  D . 
AA 3 ZN  1   155  155  ZN  ZN  D . 
BA 4 CA  1   156  156  CA  CA  D . 
CA 2 CU  1   154  154  CU  CU  E . 
DA 3 ZN  1   155  155  ZN  ZN  E . 
EA 2 CU  1   154  154  CU  CU  F . 
FA 3 ZN  1   155  155  ZN  ZN  F . 
GA 2 CU  1   154  154  CU  CU  G . 
HA 3 ZN  1   155  155  ZN  ZN  G . 
IA 2 CU  1   154  154  CU  CU  H . 
JA 3 ZN  1   155  155  ZN  ZN  H . 
KA 2 CU  1   154  154  CU  CU  I . 
LA 3 ZN  1   155  155  ZN  ZN  I . 
MA 2 CU  1   154  154  CU  CU  J . 
NA 3 ZN  1   155  155  ZN  ZN  J . 
OA 2 CU  1   154  154  CU  CU  K . 
PA 3 ZN  1   155  155  ZN  ZN  K . 
QA 2 CU  1   154  154  CU  CU  L . 
RA 3 ZN  1   155  155  ZN  ZN  L . 
SA 2 CU  1   154  154  CU  CU  M . 
TA 3 ZN  1   155  155  ZN  ZN  M . 
UA 2 CU  1   154  154  CU  CU  N . 
VA 3 ZN  1   155  155  ZN  ZN  N . 
WA 2 CU  1   154  154  CU  CU  O . 
XA 3 ZN  1   155  155  ZN  ZN  O . 
YA 4 CA  1   156  156  CA  CA  O . 
ZA 2 CU  1   154  154  CU  CU  P . 
AB 3 ZN  1   155  155  ZN  ZN  P . 
BB 2 CU  1   154  154  CU  CU  Q . 
CB 3 ZN  1   155  155  ZN  ZN  Q . 
DB 2 CU  1   154  154  CU  CU  S . 
EB 3 ZN  1   155  155  ZN  ZN  S . 
FB 5 HOH 1   2001 2001 HOH HOH A . 
FB 5 HOH 2   2002 2002 HOH HOH A . 
FB 5 HOH 3   2003 2003 HOH HOH A . 
FB 5 HOH 4   2004 2004 HOH HOH A . 
FB 5 HOH 5   2005 2005 HOH HOH A . 
FB 5 HOH 6   2006 2006 HOH HOH A . 
FB 5 HOH 7   2007 2007 HOH HOH A . 
FB 5 HOH 8   2008 2008 HOH HOH A . 
FB 5 HOH 9   2009 2009 HOH HOH A . 
FB 5 HOH 10  2010 2010 HOH HOH A . 
FB 5 HOH 11  2011 2011 HOH HOH A . 
FB 5 HOH 12  2012 2012 HOH HOH A . 
FB 5 HOH 13  2013 2013 HOH HOH A . 
FB 5 HOH 14  2014 2014 HOH HOH A . 
FB 5 HOH 15  2015 2015 HOH HOH A . 
FB 5 HOH 16  2016 2016 HOH HOH A . 
FB 5 HOH 17  2017 2017 HOH HOH A . 
FB 5 HOH 18  2018 2018 HOH HOH A . 
FB 5 HOH 19  2019 2019 HOH HOH A . 
FB 5 HOH 20  2020 2020 HOH HOH A . 
FB 5 HOH 21  2021 2021 HOH HOH A . 
FB 5 HOH 22  2022 2022 HOH HOH A . 
FB 5 HOH 23  2023 2023 HOH HOH A . 
FB 5 HOH 24  2024 2024 HOH HOH A . 
FB 5 HOH 25  2025 2025 HOH HOH A . 
FB 5 HOH 26  2026 2026 HOH HOH A . 
FB 5 HOH 27  2027 2027 HOH HOH A . 
FB 5 HOH 28  2028 2028 HOH HOH A . 
FB 5 HOH 29  2029 2029 HOH HOH A . 
FB 5 HOH 30  2030 2030 HOH HOH A . 
FB 5 HOH 31  2031 2031 HOH HOH A . 
FB 5 HOH 32  2032 2032 HOH HOH A . 
FB 5 HOH 33  2033 2033 HOH HOH A . 
FB 5 HOH 34  2034 2034 HOH HOH A . 
FB 5 HOH 35  2035 2035 HOH HOH A . 
FB 5 HOH 36  2036 2036 HOH HOH A . 
FB 5 HOH 37  2037 2037 HOH HOH A . 
FB 5 HOH 38  2038 2038 HOH HOH A . 
FB 5 HOH 39  2039 2039 HOH HOH A . 
FB 5 HOH 40  2040 2040 HOH HOH A . 
FB 5 HOH 41  2041 2041 HOH HOH A . 
FB 5 HOH 42  2042 2042 HOH HOH A . 
FB 5 HOH 43  2043 2043 HOH HOH A . 
FB 5 HOH 44  2044 2044 HOH HOH A . 
FB 5 HOH 45  2045 2045 HOH HOH A . 
FB 5 HOH 46  2046 2046 HOH HOH A . 
FB 5 HOH 47  2047 2047 HOH HOH A . 
FB 5 HOH 48  2048 2048 HOH HOH A . 
FB 5 HOH 49  2049 2049 HOH HOH A . 
FB 5 HOH 50  2050 2050 HOH HOH A . 
FB 5 HOH 51  2051 2051 HOH HOH A . 
FB 5 HOH 52  2052 2052 HOH HOH A . 
FB 5 HOH 53  2053 2053 HOH HOH A . 
FB 5 HOH 54  2054 2054 HOH HOH A . 
FB 5 HOH 55  2055 2055 HOH HOH A . 
FB 5 HOH 56  2056 2056 HOH HOH A . 
FB 5 HOH 57  2057 2057 HOH HOH A . 
FB 5 HOH 58  2058 2058 HOH HOH A . 
FB 5 HOH 59  2059 2059 HOH HOH A . 
FB 5 HOH 60  2060 2060 HOH HOH A . 
FB 5 HOH 61  2061 2061 HOH HOH A . 
FB 5 HOH 62  2062 2062 HOH HOH A . 
FB 5 HOH 63  2063 2063 HOH HOH A . 
FB 5 HOH 64  2064 2064 HOH HOH A . 
FB 5 HOH 65  2065 2065 HOH HOH A . 
FB 5 HOH 66  2066 2066 HOH HOH A . 
FB 5 HOH 67  2067 2067 HOH HOH A . 
FB 5 HOH 68  2068 2068 HOH HOH A . 
FB 5 HOH 69  2069 2069 HOH HOH A . 
FB 5 HOH 70  2070 2070 HOH HOH A . 
FB 5 HOH 71  2071 2071 HOH HOH A . 
FB 5 HOH 72  2072 2072 HOH HOH A . 
FB 5 HOH 73  2073 2073 HOH HOH A . 
FB 5 HOH 74  2074 2074 HOH HOH A . 
FB 5 HOH 75  2075 2075 HOH HOH A . 
FB 5 HOH 76  2076 2076 HOH HOH A . 
FB 5 HOH 77  2077 2077 HOH HOH A . 
FB 5 HOH 78  2078 2078 HOH HOH A . 
FB 5 HOH 79  2079 2079 HOH HOH A . 
FB 5 HOH 80  2080 2080 HOH HOH A . 
FB 5 HOH 81  2081 2081 HOH HOH A . 
FB 5 HOH 82  2082 2082 HOH HOH A . 
FB 5 HOH 83  2083 2083 HOH HOH A . 
FB 5 HOH 84  2084 2084 HOH HOH A . 
FB 5 HOH 85  2085 2085 HOH HOH A . 
FB 5 HOH 86  2086 2086 HOH HOH A . 
FB 5 HOH 87  2087 2087 HOH HOH A . 
FB 5 HOH 88  2088 2088 HOH HOH A . 
FB 5 HOH 89  2089 2089 HOH HOH A . 
FB 5 HOH 90  2090 2090 HOH HOH A . 
FB 5 HOH 91  2091 2091 HOH HOH A . 
FB 5 HOH 92  2092 2092 HOH HOH A . 
FB 5 HOH 93  2093 2093 HOH HOH A . 
FB 5 HOH 94  2094 2094 HOH HOH A . 
FB 5 HOH 95  2095 2095 HOH HOH A . 
FB 5 HOH 96  2096 2096 HOH HOH A . 
FB 5 HOH 97  2097 2097 HOH HOH A . 
FB 5 HOH 98  2098 2098 HOH HOH A . 
FB 5 HOH 99  2099 2099 HOH HOH A . 
FB 5 HOH 100 2100 2100 HOH HOH A . 
FB 5 HOH 101 2101 2101 HOH HOH A . 
FB 5 HOH 102 2102 2102 HOH HOH A . 
FB 5 HOH 103 2103 2103 HOH HOH A . 
FB 5 HOH 104 2104 2104 HOH HOH A . 
FB 5 HOH 105 2105 2105 HOH HOH A . 
FB 5 HOH 106 2106 2106 HOH HOH A . 
FB 5 HOH 107 2107 2107 HOH HOH A . 
FB 5 HOH 108 2108 2108 HOH HOH A . 
FB 5 HOH 109 2109 2109 HOH HOH A . 
FB 5 HOH 110 2110 2110 HOH HOH A . 
FB 5 HOH 111 2111 2111 HOH HOH A . 
FB 5 HOH 112 2112 2112 HOH HOH A . 
FB 5 HOH 113 2113 2113 HOH HOH A . 
GB 5 HOH 1   2001 2001 HOH HOH B . 
GB 5 HOH 2   2002 2002 HOH HOH B . 
GB 5 HOH 3   2003 2003 HOH HOH B . 
GB 5 HOH 4   2004 2004 HOH HOH B . 
GB 5 HOH 5   2005 2005 HOH HOH B . 
GB 5 HOH 6   2006 2006 HOH HOH B . 
GB 5 HOH 7   2007 2007 HOH HOH B . 
GB 5 HOH 8   2008 2008 HOH HOH B . 
GB 5 HOH 9   2009 2009 HOH HOH B . 
GB 5 HOH 10  2010 2010 HOH HOH B . 
GB 5 HOH 11  2011 2011 HOH HOH B . 
GB 5 HOH 12  2012 2012 HOH HOH B . 
GB 5 HOH 13  2013 2013 HOH HOH B . 
GB 5 HOH 14  2014 2014 HOH HOH B . 
GB 5 HOH 15  2015 2015 HOH HOH B . 
GB 5 HOH 16  2016 2016 HOH HOH B . 
GB 5 HOH 17  2017 2017 HOH HOH B . 
GB 5 HOH 18  2018 2018 HOH HOH B . 
GB 5 HOH 19  2019 2019 HOH HOH B . 
GB 5 HOH 20  2020 2020 HOH HOH B . 
GB 5 HOH 21  2021 2021 HOH HOH B . 
GB 5 HOH 22  2022 2022 HOH HOH B . 
GB 5 HOH 23  2023 2023 HOH HOH B . 
GB 5 HOH 24  2024 2024 HOH HOH B . 
GB 5 HOH 25  2025 2025 HOH HOH B . 
GB 5 HOH 26  2026 2026 HOH HOH B . 
GB 5 HOH 27  2027 2027 HOH HOH B . 
GB 5 HOH 28  2028 2028 HOH HOH B . 
GB 5 HOH 29  2029 2029 HOH HOH B . 
GB 5 HOH 30  2030 2030 HOH HOH B . 
GB 5 HOH 31  2031 2031 HOH HOH B . 
GB 5 HOH 32  2032 2032 HOH HOH B . 
GB 5 HOH 33  2033 2033 HOH HOH B . 
GB 5 HOH 34  2034 2034 HOH HOH B . 
GB 5 HOH 35  2035 2035 HOH HOH B . 
GB 5 HOH 36  2036 2036 HOH HOH B . 
GB 5 HOH 37  2037 2037 HOH HOH B . 
GB 5 HOH 38  2038 2038 HOH HOH B . 
GB 5 HOH 39  2039 2039 HOH HOH B . 
GB 5 HOH 40  2040 2040 HOH HOH B . 
GB 5 HOH 41  2041 2041 HOH HOH B . 
GB 5 HOH 42  2042 2042 HOH HOH B . 
GB 5 HOH 43  2043 2043 HOH HOH B . 
GB 5 HOH 44  2044 2044 HOH HOH B . 
GB 5 HOH 45  2045 2045 HOH HOH B . 
GB 5 HOH 46  2046 2046 HOH HOH B . 
GB 5 HOH 47  2047 2047 HOH HOH B . 
GB 5 HOH 48  2048 2048 HOH HOH B . 
GB 5 HOH 49  2049 2049 HOH HOH B . 
GB 5 HOH 50  2050 2050 HOH HOH B . 
GB 5 HOH 51  2051 2051 HOH HOH B . 
GB 5 HOH 52  2052 2052 HOH HOH B . 
GB 5 HOH 53  2053 2053 HOH HOH B . 
GB 5 HOH 54  2054 2054 HOH HOH B . 
GB 5 HOH 55  2055 2055 HOH HOH B . 
GB 5 HOH 56  2056 2056 HOH HOH B . 
GB 5 HOH 57  2057 2057 HOH HOH B . 
GB 5 HOH 58  2058 2058 HOH HOH B . 
GB 5 HOH 59  2059 2059 HOH HOH B . 
GB 5 HOH 60  2060 2060 HOH HOH B . 
GB 5 HOH 61  2061 2061 HOH HOH B . 
GB 5 HOH 62  2062 2062 HOH HOH B . 
GB 5 HOH 63  2063 2063 HOH HOH B . 
GB 5 HOH 64  2064 2064 HOH HOH B . 
GB 5 HOH 65  2065 2065 HOH HOH B . 
GB 5 HOH 66  2066 2066 HOH HOH B . 
GB 5 HOH 67  2067 2067 HOH HOH B . 
GB 5 HOH 68  2068 2068 HOH HOH B . 
GB 5 HOH 69  2069 2069 HOH HOH B . 
GB 5 HOH 70  2070 2070 HOH HOH B . 
GB 5 HOH 71  2071 2071 HOH HOH B . 
GB 5 HOH 72  2072 2072 HOH HOH B . 
GB 5 HOH 73  2073 2073 HOH HOH B . 
GB 5 HOH 74  2074 2074 HOH HOH B . 
GB 5 HOH 75  2075 2075 HOH HOH B . 
GB 5 HOH 76  2076 2076 HOH HOH B . 
GB 5 HOH 77  2077 2077 HOH HOH B . 
GB 5 HOH 78  2078 2078 HOH HOH B . 
GB 5 HOH 79  2079 2079 HOH HOH B . 
GB 5 HOH 80  2080 2080 HOH HOH B . 
GB 5 HOH 81  2081 2081 HOH HOH B . 
GB 5 HOH 82  2082 2082 HOH HOH B . 
GB 5 HOH 83  2083 2083 HOH HOH B . 
GB 5 HOH 84  2084 2084 HOH HOH B . 
GB 5 HOH 85  2085 2085 HOH HOH B . 
GB 5 HOH 86  2086 2086 HOH HOH B . 
GB 5 HOH 87  2087 2087 HOH HOH B . 
GB 5 HOH 88  2088 2088 HOH HOH B . 
GB 5 HOH 89  2089 2089 HOH HOH B . 
GB 5 HOH 90  2090 2090 HOH HOH B . 
GB 5 HOH 91  2091 2091 HOH HOH B . 
GB 5 HOH 92  2092 2092 HOH HOH B . 
GB 5 HOH 93  2093 2093 HOH HOH B . 
GB 5 HOH 94  2094 2094 HOH HOH B . 
GB 5 HOH 95  2095 2095 HOH HOH B . 
GB 5 HOH 96  2096 2096 HOH HOH B . 
GB 5 HOH 97  2097 2097 HOH HOH B . 
GB 5 HOH 98  2098 2098 HOH HOH B . 
GB 5 HOH 99  2099 2099 HOH HOH B . 
GB 5 HOH 100 2100 2100 HOH HOH B . 
GB 5 HOH 101 2101 2101 HOH HOH B . 
GB 5 HOH 102 2102 2102 HOH HOH B . 
GB 5 HOH 103 2103 2103 HOH HOH B . 
GB 5 HOH 104 2104 2104 HOH HOH B . 
GB 5 HOH 105 2105 2105 HOH HOH B . 
GB 5 HOH 106 2106 2106 HOH HOH B . 
GB 5 HOH 107 2107 2107 HOH HOH B . 
GB 5 HOH 108 2108 2108 HOH HOH B . 
GB 5 HOH 109 2109 2109 HOH HOH B . 
GB 5 HOH 110 2110 2110 HOH HOH B . 
GB 5 HOH 111 2111 2111 HOH HOH B . 
GB 5 HOH 112 2112 2112 HOH HOH B . 
GB 5 HOH 113 2113 2113 HOH HOH B . 
GB 5 HOH 114 2114 2114 HOH HOH B . 
GB 5 HOH 115 2115 2115 HOH HOH B . 
GB 5 HOH 116 2116 2116 HOH HOH B . 
GB 5 HOH 117 2117 2117 HOH HOH B . 
GB 5 HOH 118 2118 2118 HOH HOH B . 
GB 5 HOH 119 2119 2119 HOH HOH B . 
GB 5 HOH 120 2120 2120 HOH HOH B . 
GB 5 HOH 121 2121 2121 HOH HOH B . 
GB 5 HOH 122 2122 2122 HOH HOH B . 
GB 5 HOH 123 2123 2123 HOH HOH B . 
GB 5 HOH 124 2124 2124 HOH HOH B . 
GB 5 HOH 125 2125 2125 HOH HOH B . 
GB 5 HOH 126 2126 2126 HOH HOH B . 
GB 5 HOH 127 2127 2127 HOH HOH B . 
GB 5 HOH 128 2128 2128 HOH HOH B . 
GB 5 HOH 129 2129 2129 HOH HOH B . 
GB 5 HOH 130 2130 2130 HOH HOH B . 
GB 5 HOH 131 2131 2131 HOH HOH B . 
GB 5 HOH 132 2132 2132 HOH HOH B . 
GB 5 HOH 133 2133 2133 HOH HOH B . 
GB 5 HOH 134 2134 2134 HOH HOH B . 
GB 5 HOH 135 2135 2135 HOH HOH B . 
GB 5 HOH 136 2136 2136 HOH HOH B . 
GB 5 HOH 137 2137 2137 HOH HOH B . 
GB 5 HOH 138 2138 2138 HOH HOH B . 
GB 5 HOH 139 2139 2139 HOH HOH B . 
GB 5 HOH 140 2140 2140 HOH HOH B . 
GB 5 HOH 141 2141 2141 HOH HOH B . 
GB 5 HOH 142 2142 2142 HOH HOH B . 
GB 5 HOH 143 2143 2143 HOH HOH B . 
GB 5 HOH 144 2144 2144 HOH HOH B . 
GB 5 HOH 145 2145 2145 HOH HOH B . 
GB 5 HOH 146 2146 2146 HOH HOH B . 
GB 5 HOH 147 2147 2147 HOH HOH B . 
GB 5 HOH 148 2148 2148 HOH HOH B . 
GB 5 HOH 149 2149 2149 HOH HOH B . 
GB 5 HOH 150 2150 2150 HOH HOH B . 
GB 5 HOH 151 2151 2151 HOH HOH B . 
GB 5 HOH 152 2152 2152 HOH HOH B . 
HB 5 HOH 1   2001 2001 HOH HOH C . 
HB 5 HOH 2   2002 2002 HOH HOH C . 
HB 5 HOH 3   2003 2003 HOH HOH C . 
HB 5 HOH 4   2004 2004 HOH HOH C . 
HB 5 HOH 5   2005 2005 HOH HOH C . 
HB 5 HOH 6   2006 2006 HOH HOH C . 
HB 5 HOH 7   2007 2007 HOH HOH C . 
HB 5 HOH 8   2008 2008 HOH HOH C . 
HB 5 HOH 9   2009 2009 HOH HOH C . 
HB 5 HOH 10  2010 2010 HOH HOH C . 
HB 5 HOH 11  2011 2011 HOH HOH C . 
HB 5 HOH 12  2012 2012 HOH HOH C . 
HB 5 HOH 13  2013 2013 HOH HOH C . 
HB 5 HOH 14  2014 2014 HOH HOH C . 
HB 5 HOH 15  2015 2015 HOH HOH C . 
HB 5 HOH 16  2016 2016 HOH HOH C . 
HB 5 HOH 17  2017 2017 HOH HOH C . 
HB 5 HOH 18  2018 2018 HOH HOH C . 
HB 5 HOH 19  2019 2019 HOH HOH C . 
HB 5 HOH 20  2020 2020 HOH HOH C . 
HB 5 HOH 21  2021 2021 HOH HOH C . 
HB 5 HOH 22  2022 2022 HOH HOH C . 
HB 5 HOH 23  2023 2023 HOH HOH C . 
HB 5 HOH 24  2024 2024 HOH HOH C . 
HB 5 HOH 25  2025 2025 HOH HOH C . 
HB 5 HOH 26  2026 2026 HOH HOH C . 
HB 5 HOH 27  2027 2027 HOH HOH C . 
HB 5 HOH 28  2028 2028 HOH HOH C . 
HB 5 HOH 29  2029 2029 HOH HOH C . 
HB 5 HOH 30  2030 2030 HOH HOH C . 
HB 5 HOH 31  2031 2031 HOH HOH C . 
HB 5 HOH 32  2032 2032 HOH HOH C . 
HB 5 HOH 33  2033 2033 HOH HOH C . 
HB 5 HOH 34  2034 2034 HOH HOH C . 
HB 5 HOH 35  2035 2035 HOH HOH C . 
HB 5 HOH 36  2036 2036 HOH HOH C . 
HB 5 HOH 37  2037 2037 HOH HOH C . 
HB 5 HOH 38  2038 2038 HOH HOH C . 
HB 5 HOH 39  2039 2039 HOH HOH C . 
HB 5 HOH 40  2040 2040 HOH HOH C . 
HB 5 HOH 41  2041 2041 HOH HOH C . 
HB 5 HOH 42  2042 2042 HOH HOH C . 
HB 5 HOH 43  2043 2043 HOH HOH C . 
HB 5 HOH 44  2044 2044 HOH HOH C . 
HB 5 HOH 45  2045 2045 HOH HOH C . 
HB 5 HOH 46  2046 2046 HOH HOH C . 
HB 5 HOH 47  2047 2047 HOH HOH C . 
HB 5 HOH 48  2048 2048 HOH HOH C . 
HB 5 HOH 49  2049 2049 HOH HOH C . 
HB 5 HOH 50  2050 2050 HOH HOH C . 
HB 5 HOH 51  2051 2051 HOH HOH C . 
HB 5 HOH 52  2052 2052 HOH HOH C . 
HB 5 HOH 53  2053 2053 HOH HOH C . 
HB 5 HOH 54  2054 2054 HOH HOH C . 
HB 5 HOH 55  2055 2055 HOH HOH C . 
HB 5 HOH 56  2056 2056 HOH HOH C . 
HB 5 HOH 57  2057 2057 HOH HOH C . 
HB 5 HOH 58  2058 2058 HOH HOH C . 
HB 5 HOH 59  2059 2059 HOH HOH C . 
HB 5 HOH 60  2060 2060 HOH HOH C . 
HB 5 HOH 61  2061 2061 HOH HOH C . 
HB 5 HOH 62  2062 2062 HOH HOH C . 
HB 5 HOH 63  2063 2063 HOH HOH C . 
HB 5 HOH 64  2064 2064 HOH HOH C . 
HB 5 HOH 65  2065 2065 HOH HOH C . 
HB 5 HOH 66  2066 2066 HOH HOH C . 
HB 5 HOH 67  2067 2067 HOH HOH C . 
HB 5 HOH 68  2068 2068 HOH HOH C . 
HB 5 HOH 69  2069 2069 HOH HOH C . 
HB 5 HOH 70  2070 2070 HOH HOH C . 
HB 5 HOH 71  2071 2071 HOH HOH C . 
HB 5 HOH 72  2072 2072 HOH HOH C . 
HB 5 HOH 73  2073 2073 HOH HOH C . 
HB 5 HOH 74  2074 2074 HOH HOH C . 
HB 5 HOH 75  2075 2075 HOH HOH C . 
HB 5 HOH 76  2076 2076 HOH HOH C . 
HB 5 HOH 77  2077 2077 HOH HOH C . 
HB 5 HOH 78  2078 2078 HOH HOH C . 
HB 5 HOH 79  2079 2079 HOH HOH C . 
HB 5 HOH 80  2080 2080 HOH HOH C . 
HB 5 HOH 81  2081 2081 HOH HOH C . 
HB 5 HOH 82  2082 2082 HOH HOH C . 
HB 5 HOH 83  2083 2083 HOH HOH C . 
HB 5 HOH 84  2084 2084 HOH HOH C . 
HB 5 HOH 85  2085 2085 HOH HOH C . 
HB 5 HOH 86  2086 2086 HOH HOH C . 
HB 5 HOH 87  2087 2087 HOH HOH C . 
HB 5 HOH 88  2088 2088 HOH HOH C . 
HB 5 HOH 89  2089 2089 HOH HOH C . 
HB 5 HOH 90  2090 2090 HOH HOH C . 
HB 5 HOH 91  2091 2091 HOH HOH C . 
HB 5 HOH 92  2092 2092 HOH HOH C . 
HB 5 HOH 93  2093 2093 HOH HOH C . 
HB 5 HOH 94  2094 2094 HOH HOH C . 
HB 5 HOH 95  2095 2095 HOH HOH C . 
HB 5 HOH 96  2096 2096 HOH HOH C . 
HB 5 HOH 97  2097 2097 HOH HOH C . 
HB 5 HOH 98  2098 2098 HOH HOH C . 
HB 5 HOH 99  2099 2099 HOH HOH C . 
HB 5 HOH 100 2100 2100 HOH HOH C . 
HB 5 HOH 101 2101 2101 HOH HOH C . 
HB 5 HOH 102 2102 2102 HOH HOH C . 
HB 5 HOH 103 2103 2103 HOH HOH C . 
HB 5 HOH 104 2104 2104 HOH HOH C . 
HB 5 HOH 105 2105 2105 HOH HOH C . 
HB 5 HOH 106 2106 2106 HOH HOH C . 
HB 5 HOH 107 2107 2107 HOH HOH C . 
HB 5 HOH 108 2108 2108 HOH HOH C . 
HB 5 HOH 109 2109 2109 HOH HOH C . 
HB 5 HOH 110 2110 2110 HOH HOH C . 
HB 5 HOH 111 2111 2111 HOH HOH C . 
HB 5 HOH 112 2112 2112 HOH HOH C . 
HB 5 HOH 113 2113 2113 HOH HOH C . 
HB 5 HOH 114 2114 2114 HOH HOH C . 
HB 5 HOH 115 2115 2115 HOH HOH C . 
HB 5 HOH 116 2116 2116 HOH HOH C . 
HB 5 HOH 117 2117 2117 HOH HOH C . 
HB 5 HOH 118 2118 2118 HOH HOH C . 
HB 5 HOH 119 2119 2119 HOH HOH C . 
HB 5 HOH 120 2120 2120 HOH HOH C . 
HB 5 HOH 121 2121 2121 HOH HOH C . 
HB 5 HOH 122 2122 2122 HOH HOH C . 
HB 5 HOH 123 2123 2123 HOH HOH C . 
HB 5 HOH 124 2124 2124 HOH HOH C . 
HB 5 HOH 125 2125 2125 HOH HOH C . 
HB 5 HOH 126 2126 2126 HOH HOH C . 
HB 5 HOH 127 2127 2127 HOH HOH C . 
HB 5 HOH 128 2128 2128 HOH HOH C . 
HB 5 HOH 129 2129 2129 HOH HOH C . 
HB 5 HOH 130 2130 2130 HOH HOH C . 
HB 5 HOH 131 2131 2131 HOH HOH C . 
HB 5 HOH 132 2132 2132 HOH HOH C . 
HB 5 HOH 133 2133 2133 HOH HOH C . 
HB 5 HOH 134 2134 2134 HOH HOH C . 
HB 5 HOH 135 2135 2135 HOH HOH C . 
HB 5 HOH 136 2136 2136 HOH HOH C . 
HB 5 HOH 137 2137 2137 HOH HOH C . 
HB 5 HOH 138 2138 2138 HOH HOH C . 
HB 5 HOH 139 2139 2139 HOH HOH C . 
HB 5 HOH 140 2140 2140 HOH HOH C . 
HB 5 HOH 141 2141 2141 HOH HOH C . 
HB 5 HOH 142 2142 2142 HOH HOH C . 
HB 5 HOH 143 2143 2143 HOH HOH C . 
HB 5 HOH 144 2144 2144 HOH HOH C . 
IB 5 HOH 1   2001 2001 HOH HOH D . 
IB 5 HOH 2   2002 2002 HOH HOH D . 
IB 5 HOH 3   2003 2003 HOH HOH D . 
IB 5 HOH 4   2004 2004 HOH HOH D . 
IB 5 HOH 5   2005 2005 HOH HOH D . 
IB 5 HOH 6   2006 2006 HOH HOH D . 
IB 5 HOH 7   2007 2007 HOH HOH D . 
IB 5 HOH 8   2008 2008 HOH HOH D . 
IB 5 HOH 9   2009 2009 HOH HOH D . 
IB 5 HOH 10  2010 2010 HOH HOH D . 
IB 5 HOH 11  2011 2011 HOH HOH D . 
IB 5 HOH 12  2012 2012 HOH HOH D . 
IB 5 HOH 13  2013 2013 HOH HOH D . 
IB 5 HOH 14  2014 2014 HOH HOH D . 
IB 5 HOH 15  2015 2015 HOH HOH D . 
IB 5 HOH 16  2016 2016 HOH HOH D . 
IB 5 HOH 17  2017 2017 HOH HOH D . 
IB 5 HOH 18  2018 2018 HOH HOH D . 
IB 5 HOH 19  2019 2019 HOH HOH D . 
IB 5 HOH 20  2020 2020 HOH HOH D . 
IB 5 HOH 21  2021 2021 HOH HOH D . 
IB 5 HOH 22  2022 2022 HOH HOH D . 
IB 5 HOH 23  2023 2023 HOH HOH D . 
IB 5 HOH 24  2024 2024 HOH HOH D . 
IB 5 HOH 25  2025 2025 HOH HOH D . 
IB 5 HOH 26  2026 2026 HOH HOH D . 
IB 5 HOH 27  2027 2027 HOH HOH D . 
IB 5 HOH 28  2028 2028 HOH HOH D . 
IB 5 HOH 29  2029 2029 HOH HOH D . 
IB 5 HOH 30  2030 2030 HOH HOH D . 
IB 5 HOH 31  2031 2031 HOH HOH D . 
IB 5 HOH 32  2032 2032 HOH HOH D . 
IB 5 HOH 33  2033 2033 HOH HOH D . 
IB 5 HOH 34  2034 2034 HOH HOH D . 
IB 5 HOH 35  2035 2035 HOH HOH D . 
IB 5 HOH 36  2036 2036 HOH HOH D . 
IB 5 HOH 37  2037 2037 HOH HOH D . 
IB 5 HOH 38  2038 2038 HOH HOH D . 
IB 5 HOH 39  2039 2039 HOH HOH D . 
IB 5 HOH 40  2040 2040 HOH HOH D . 
IB 5 HOH 41  2041 2041 HOH HOH D . 
IB 5 HOH 42  2042 2042 HOH HOH D . 
IB 5 HOH 43  2043 2043 HOH HOH D . 
IB 5 HOH 44  2044 2044 HOH HOH D . 
IB 5 HOH 45  2045 2045 HOH HOH D . 
IB 5 HOH 46  2046 2046 HOH HOH D . 
IB 5 HOH 47  2047 2047 HOH HOH D . 
IB 5 HOH 48  2048 2048 HOH HOH D . 
IB 5 HOH 49  2049 2049 HOH HOH D . 
IB 5 HOH 50  2050 2050 HOH HOH D . 
IB 5 HOH 51  2051 2051 HOH HOH D . 
IB 5 HOH 52  2052 2052 HOH HOH D . 
IB 5 HOH 53  2053 2053 HOH HOH D . 
IB 5 HOH 54  2054 2054 HOH HOH D . 
IB 5 HOH 55  2055 2055 HOH HOH D . 
IB 5 HOH 56  2056 2056 HOH HOH D . 
IB 5 HOH 57  2057 2057 HOH HOH D . 
IB 5 HOH 58  2058 2058 HOH HOH D . 
IB 5 HOH 59  2059 2059 HOH HOH D . 
IB 5 HOH 60  2060 2060 HOH HOH D . 
IB 5 HOH 61  2061 2061 HOH HOH D . 
IB 5 HOH 62  2062 2062 HOH HOH D . 
IB 5 HOH 63  2063 2063 HOH HOH D . 
IB 5 HOH 64  2064 2064 HOH HOH D . 
IB 5 HOH 65  2065 2065 HOH HOH D . 
IB 5 HOH 66  2066 2066 HOH HOH D . 
IB 5 HOH 67  2067 2067 HOH HOH D . 
IB 5 HOH 68  2068 2068 HOH HOH D . 
IB 5 HOH 69  2069 2069 HOH HOH D . 
IB 5 HOH 70  2070 2070 HOH HOH D . 
IB 5 HOH 71  2071 2071 HOH HOH D . 
IB 5 HOH 72  2072 2072 HOH HOH D . 
IB 5 HOH 73  2073 2073 HOH HOH D . 
IB 5 HOH 74  2074 2074 HOH HOH D . 
IB 5 HOH 75  2075 2075 HOH HOH D . 
IB 5 HOH 76  2076 2076 HOH HOH D . 
IB 5 HOH 77  2077 2077 HOH HOH D . 
IB 5 HOH 78  2078 2078 HOH HOH D . 
IB 5 HOH 79  2079 2079 HOH HOH D . 
IB 5 HOH 80  2080 2080 HOH HOH D . 
IB 5 HOH 81  2081 2081 HOH HOH D . 
IB 5 HOH 82  2082 2082 HOH HOH D . 
IB 5 HOH 83  2083 2083 HOH HOH D . 
IB 5 HOH 84  2084 2084 HOH HOH D . 
IB 5 HOH 85  2085 2085 HOH HOH D . 
IB 5 HOH 86  2086 2086 HOH HOH D . 
IB 5 HOH 87  2087 2087 HOH HOH D . 
IB 5 HOH 88  2088 2088 HOH HOH D . 
IB 5 HOH 89  2089 2089 HOH HOH D . 
IB 5 HOH 90  2090 2090 HOH HOH D . 
IB 5 HOH 91  2091 2091 HOH HOH D . 
IB 5 HOH 92  2092 2092 HOH HOH D . 
IB 5 HOH 93  2093 2093 HOH HOH D . 
IB 5 HOH 94  2094 2094 HOH HOH D . 
IB 5 HOH 95  2095 2095 HOH HOH D . 
IB 5 HOH 96  2096 2096 HOH HOH D . 
IB 5 HOH 97  2097 2097 HOH HOH D . 
IB 5 HOH 98  2098 2098 HOH HOH D . 
IB 5 HOH 99  2099 2099 HOH HOH D . 
IB 5 HOH 100 2100 2100 HOH HOH D . 
IB 5 HOH 101 2101 2101 HOH HOH D . 
IB 5 HOH 102 2102 2102 HOH HOH D . 
IB 5 HOH 103 2103 2103 HOH HOH D . 
IB 5 HOH 104 2104 2104 HOH HOH D . 
IB 5 HOH 105 2105 2105 HOH HOH D . 
IB 5 HOH 106 2106 2106 HOH HOH D . 
IB 5 HOH 107 2107 2107 HOH HOH D . 
JB 5 HOH 1   2001 2001 HOH HOH E . 
JB 5 HOH 2   2002 2002 HOH HOH E . 
JB 5 HOH 3   2003 2003 HOH HOH E . 
JB 5 HOH 4   2004 2004 HOH HOH E . 
JB 5 HOH 5   2005 2005 HOH HOH E . 
JB 5 HOH 6   2006 2006 HOH HOH E . 
JB 5 HOH 7   2007 2007 HOH HOH E . 
JB 5 HOH 8   2008 2008 HOH HOH E . 
JB 5 HOH 9   2009 2009 HOH HOH E . 
JB 5 HOH 10  2010 2010 HOH HOH E . 
JB 5 HOH 11  2011 2011 HOH HOH E . 
JB 5 HOH 12  2012 2012 HOH HOH E . 
JB 5 HOH 13  2013 2013 HOH HOH E . 
JB 5 HOH 14  2014 2014 HOH HOH E . 
JB 5 HOH 15  2015 2015 HOH HOH E . 
JB 5 HOH 16  2016 2016 HOH HOH E . 
JB 5 HOH 17  2017 2017 HOH HOH E . 
JB 5 HOH 18  2018 2018 HOH HOH E . 
JB 5 HOH 19  2019 2019 HOH HOH E . 
JB 5 HOH 20  2020 2020 HOH HOH E . 
JB 5 HOH 21  2021 2021 HOH HOH E . 
JB 5 HOH 22  2022 2022 HOH HOH E . 
JB 5 HOH 23  2023 2023 HOH HOH E . 
JB 5 HOH 24  2024 2024 HOH HOH E . 
JB 5 HOH 25  2025 2025 HOH HOH E . 
JB 5 HOH 26  2026 2026 HOH HOH E . 
JB 5 HOH 27  2027 2027 HOH HOH E . 
JB 5 HOH 28  2028 2028 HOH HOH E . 
JB 5 HOH 29  2029 2029 HOH HOH E . 
JB 5 HOH 30  2030 2030 HOH HOH E . 
JB 5 HOH 31  2031 2031 HOH HOH E . 
JB 5 HOH 32  2032 2032 HOH HOH E . 
JB 5 HOH 33  2033 2033 HOH HOH E . 
JB 5 HOH 34  2034 2034 HOH HOH E . 
JB 5 HOH 35  2035 2035 HOH HOH E . 
JB 5 HOH 36  2036 2036 HOH HOH E . 
JB 5 HOH 37  2037 2037 HOH HOH E . 
JB 5 HOH 38  2038 2038 HOH HOH E . 
JB 5 HOH 39  2039 2039 HOH HOH E . 
JB 5 HOH 40  2040 2040 HOH HOH E . 
JB 5 HOH 41  2041 2041 HOH HOH E . 
JB 5 HOH 42  2042 2042 HOH HOH E . 
JB 5 HOH 43  2043 2043 HOH HOH E . 
JB 5 HOH 44  2044 2044 HOH HOH E . 
JB 5 HOH 45  2045 2045 HOH HOH E . 
JB 5 HOH 46  2046 2046 HOH HOH E . 
JB 5 HOH 47  2047 2047 HOH HOH E . 
JB 5 HOH 48  2048 2048 HOH HOH E . 
JB 5 HOH 49  2049 2049 HOH HOH E . 
JB 5 HOH 50  2050 2050 HOH HOH E . 
JB 5 HOH 51  2051 2051 HOH HOH E . 
JB 5 HOH 52  2052 2052 HOH HOH E . 
JB 5 HOH 53  2053 2053 HOH HOH E . 
JB 5 HOH 54  2054 2054 HOH HOH E . 
JB 5 HOH 55  2055 2055 HOH HOH E . 
JB 5 HOH 56  2056 2056 HOH HOH E . 
JB 5 HOH 57  2057 2057 HOH HOH E . 
JB 5 HOH 58  2058 2058 HOH HOH E . 
JB 5 HOH 59  2059 2059 HOH HOH E . 
JB 5 HOH 60  2060 2060 HOH HOH E . 
JB 5 HOH 61  2061 2061 HOH HOH E . 
JB 5 HOH 62  2062 2062 HOH HOH E . 
JB 5 HOH 63  2063 2063 HOH HOH E . 
JB 5 HOH 64  2064 2064 HOH HOH E . 
JB 5 HOH 65  2065 2065 HOH HOH E . 
JB 5 HOH 66  2066 2066 HOH HOH E . 
JB 5 HOH 67  2067 2067 HOH HOH E . 
JB 5 HOH 68  2068 2068 HOH HOH E . 
JB 5 HOH 69  2069 2069 HOH HOH E . 
JB 5 HOH 70  2070 2070 HOH HOH E . 
JB 5 HOH 71  2071 2071 HOH HOH E . 
JB 5 HOH 72  2072 2072 HOH HOH E . 
JB 5 HOH 73  2073 2073 HOH HOH E . 
JB 5 HOH 74  2074 2074 HOH HOH E . 
JB 5 HOH 75  2075 2075 HOH HOH E . 
JB 5 HOH 76  2076 2076 HOH HOH E . 
JB 5 HOH 77  2077 2077 HOH HOH E . 
JB 5 HOH 78  2078 2078 HOH HOH E . 
JB 5 HOH 79  2079 2079 HOH HOH E . 
JB 5 HOH 80  2080 2080 HOH HOH E . 
JB 5 HOH 81  2081 2081 HOH HOH E . 
JB 5 HOH 82  2082 2082 HOH HOH E . 
JB 5 HOH 83  2083 2083 HOH HOH E . 
JB 5 HOH 84  2084 2084 HOH HOH E . 
JB 5 HOH 85  2085 2085 HOH HOH E . 
JB 5 HOH 86  2086 2086 HOH HOH E . 
JB 5 HOH 87  2087 2087 HOH HOH E . 
JB 5 HOH 88  2088 2088 HOH HOH E . 
JB 5 HOH 89  2089 2089 HOH HOH E . 
JB 5 HOH 90  2090 2090 HOH HOH E . 
JB 5 HOH 91  2091 2091 HOH HOH E . 
JB 5 HOH 92  2092 2092 HOH HOH E . 
JB 5 HOH 93  2093 2093 HOH HOH E . 
JB 5 HOH 94  2094 2094 HOH HOH E . 
JB 5 HOH 95  2095 2095 HOH HOH E . 
JB 5 HOH 96  2096 2096 HOH HOH E . 
JB 5 HOH 97  2097 2097 HOH HOH E . 
JB 5 HOH 98  2098 2098 HOH HOH E . 
JB 5 HOH 99  2099 2099 HOH HOH E . 
JB 5 HOH 100 2100 2100 HOH HOH E . 
JB 5 HOH 101 2101 2101 HOH HOH E . 
JB 5 HOH 102 2102 2102 HOH HOH E . 
JB 5 HOH 103 2103 2103 HOH HOH E . 
JB 5 HOH 104 2104 2104 HOH HOH E . 
JB 5 HOH 105 2105 2105 HOH HOH E . 
JB 5 HOH 106 2106 2106 HOH HOH E . 
JB 5 HOH 107 2107 2107 HOH HOH E . 
JB 5 HOH 108 2108 2108 HOH HOH E . 
JB 5 HOH 109 2109 2109 HOH HOH E . 
JB 5 HOH 110 2110 2110 HOH HOH E . 
JB 5 HOH 111 2111 2111 HOH HOH E . 
JB 5 HOH 112 2112 2112 HOH HOH E . 
JB 5 HOH 113 2113 2113 HOH HOH E . 
JB 5 HOH 114 2114 2114 HOH HOH E . 
KB 5 HOH 1   2001 2001 HOH HOH F . 
KB 5 HOH 2   2002 2002 HOH HOH F . 
KB 5 HOH 3   2003 2003 HOH HOH F . 
KB 5 HOH 4   2004 2004 HOH HOH F . 
KB 5 HOH 5   2005 2005 HOH HOH F . 
KB 5 HOH 6   2006 2006 HOH HOH F . 
KB 5 HOH 7   2007 2007 HOH HOH F . 
KB 5 HOH 8   2008 2008 HOH HOH F . 
KB 5 HOH 9   2009 2009 HOH HOH F . 
KB 5 HOH 10  2010 2010 HOH HOH F . 
KB 5 HOH 11  2011 2011 HOH HOH F . 
KB 5 HOH 12  2012 2012 HOH HOH F . 
KB 5 HOH 13  2013 2013 HOH HOH F . 
KB 5 HOH 14  2014 2014 HOH HOH F . 
KB 5 HOH 15  2015 2015 HOH HOH F . 
KB 5 HOH 16  2016 2016 HOH HOH F . 
KB 5 HOH 17  2017 2017 HOH HOH F . 
KB 5 HOH 18  2018 2018 HOH HOH F . 
KB 5 HOH 19  2019 2019 HOH HOH F . 
KB 5 HOH 20  2020 2020 HOH HOH F . 
KB 5 HOH 21  2021 2021 HOH HOH F . 
KB 5 HOH 22  2022 2022 HOH HOH F . 
KB 5 HOH 23  2023 2023 HOH HOH F . 
KB 5 HOH 24  2024 2024 HOH HOH F . 
KB 5 HOH 25  2025 2025 HOH HOH F . 
KB 5 HOH 26  2026 2026 HOH HOH F . 
KB 5 HOH 27  2027 2027 HOH HOH F . 
KB 5 HOH 28  2028 2028 HOH HOH F . 
KB 5 HOH 29  2029 2029 HOH HOH F . 
KB 5 HOH 30  2030 2030 HOH HOH F . 
KB 5 HOH 31  2031 2031 HOH HOH F . 
KB 5 HOH 32  2032 2032 HOH HOH F . 
KB 5 HOH 33  2033 2033 HOH HOH F . 
KB 5 HOH 34  2034 2034 HOH HOH F . 
KB 5 HOH 35  2035 2035 HOH HOH F . 
KB 5 HOH 36  2036 2036 HOH HOH F . 
KB 5 HOH 37  2037 2037 HOH HOH F . 
KB 5 HOH 38  2038 2038 HOH HOH F . 
KB 5 HOH 39  2039 2039 HOH HOH F . 
KB 5 HOH 40  2040 2040 HOH HOH F . 
KB 5 HOH 41  2041 2041 HOH HOH F . 
KB 5 HOH 42  2042 2042 HOH HOH F . 
KB 5 HOH 43  2043 2043 HOH HOH F . 
KB 5 HOH 44  2044 2044 HOH HOH F . 
KB 5 HOH 45  2045 2045 HOH HOH F . 
KB 5 HOH 46  2046 2046 HOH HOH F . 
KB 5 HOH 47  2047 2047 HOH HOH F . 
KB 5 HOH 48  2048 2048 HOH HOH F . 
KB 5 HOH 49  2049 2049 HOH HOH F . 
KB 5 HOH 50  2050 2050 HOH HOH F . 
KB 5 HOH 51  2051 2051 HOH HOH F . 
KB 5 HOH 52  2052 2052 HOH HOH F . 
KB 5 HOH 53  2053 2053 HOH HOH F . 
KB 5 HOH 54  2054 2054 HOH HOH F . 
KB 5 HOH 55  2055 2055 HOH HOH F . 
KB 5 HOH 56  2056 2056 HOH HOH F . 
KB 5 HOH 57  2057 2057 HOH HOH F . 
KB 5 HOH 58  2058 2058 HOH HOH F . 
KB 5 HOH 59  2059 2059 HOH HOH F . 
KB 5 HOH 60  2060 2060 HOH HOH F . 
KB 5 HOH 61  2061 2061 HOH HOH F . 
KB 5 HOH 62  2062 2062 HOH HOH F . 
KB 5 HOH 63  2063 2063 HOH HOH F . 
KB 5 HOH 64  2064 2064 HOH HOH F . 
KB 5 HOH 65  2065 2065 HOH HOH F . 
KB 5 HOH 66  2066 2066 HOH HOH F . 
KB 5 HOH 67  2067 2067 HOH HOH F . 
KB 5 HOH 68  2068 2068 HOH HOH F . 
KB 5 HOH 69  2069 2069 HOH HOH F . 
KB 5 HOH 70  2070 2070 HOH HOH F . 
KB 5 HOH 71  2071 2071 HOH HOH F . 
KB 5 HOH 72  2072 2072 HOH HOH F . 
KB 5 HOH 73  2073 2073 HOH HOH F . 
KB 5 HOH 74  2074 2074 HOH HOH F . 
KB 5 HOH 75  2075 2075 HOH HOH F . 
KB 5 HOH 76  2076 2076 HOH HOH F . 
KB 5 HOH 77  2077 2077 HOH HOH F . 
KB 5 HOH 78  2078 2078 HOH HOH F . 
KB 5 HOH 79  2079 2079 HOH HOH F . 
KB 5 HOH 80  2080 2080 HOH HOH F . 
KB 5 HOH 81  2081 2081 HOH HOH F . 
KB 5 HOH 82  2082 2082 HOH HOH F . 
KB 5 HOH 83  2083 2083 HOH HOH F . 
KB 5 HOH 84  2084 2084 HOH HOH F . 
KB 5 HOH 85  2085 2085 HOH HOH F . 
KB 5 HOH 86  2086 2086 HOH HOH F . 
KB 5 HOH 87  2087 2087 HOH HOH F . 
KB 5 HOH 88  2088 2088 HOH HOH F . 
KB 5 HOH 89  2089 2089 HOH HOH F . 
KB 5 HOH 90  2090 2090 HOH HOH F . 
KB 5 HOH 91  2091 2091 HOH HOH F . 
KB 5 HOH 92  2092 2092 HOH HOH F . 
KB 5 HOH 93  2093 2093 HOH HOH F . 
KB 5 HOH 94  2094 2094 HOH HOH F . 
LB 5 HOH 1   2001 2001 HOH HOH G . 
LB 5 HOH 2   2002 2002 HOH HOH G . 
LB 5 HOH 3   2003 2003 HOH HOH G . 
LB 5 HOH 4   2004 2004 HOH HOH G . 
LB 5 HOH 5   2005 2005 HOH HOH G . 
LB 5 HOH 6   2006 2006 HOH HOH G . 
LB 5 HOH 7   2007 2007 HOH HOH G . 
LB 5 HOH 8   2008 2008 HOH HOH G . 
LB 5 HOH 9   2009 2009 HOH HOH G . 
LB 5 HOH 10  2010 2010 HOH HOH G . 
LB 5 HOH 11  2011 2011 HOH HOH G . 
LB 5 HOH 12  2012 2012 HOH HOH G . 
LB 5 HOH 13  2013 2013 HOH HOH G . 
LB 5 HOH 14  2014 2014 HOH HOH G . 
LB 5 HOH 15  2015 2015 HOH HOH G . 
LB 5 HOH 16  2016 2016 HOH HOH G . 
LB 5 HOH 17  2017 2017 HOH HOH G . 
LB 5 HOH 18  2018 2018 HOH HOH G . 
LB 5 HOH 19  2019 2019 HOH HOH G . 
LB 5 HOH 20  2020 2020 HOH HOH G . 
LB 5 HOH 21  2021 2021 HOH HOH G . 
LB 5 HOH 22  2022 2022 HOH HOH G . 
LB 5 HOH 23  2023 2023 HOH HOH G . 
LB 5 HOH 24  2024 2024 HOH HOH G . 
LB 5 HOH 25  2025 2025 HOH HOH G . 
LB 5 HOH 26  2026 2026 HOH HOH G . 
LB 5 HOH 27  2027 2027 HOH HOH G . 
LB 5 HOH 28  2028 2028 HOH HOH G . 
LB 5 HOH 29  2029 2029 HOH HOH G . 
LB 5 HOH 30  2030 2030 HOH HOH G . 
LB 5 HOH 31  2031 2031 HOH HOH G . 
LB 5 HOH 32  2032 2032 HOH HOH G . 
LB 5 HOH 33  2033 2033 HOH HOH G . 
LB 5 HOH 34  2034 2034 HOH HOH G . 
LB 5 HOH 35  2035 2035 HOH HOH G . 
LB 5 HOH 36  2036 2036 HOH HOH G . 
LB 5 HOH 37  2037 2037 HOH HOH G . 
LB 5 HOH 38  2038 2038 HOH HOH G . 
LB 5 HOH 39  2039 2039 HOH HOH G . 
LB 5 HOH 40  2040 2040 HOH HOH G . 
LB 5 HOH 41  2041 2041 HOH HOH G . 
LB 5 HOH 42  2042 2042 HOH HOH G . 
LB 5 HOH 43  2043 2043 HOH HOH G . 
MB 5 HOH 1   2001 2001 HOH HOH H . 
MB 5 HOH 2   2002 2002 HOH HOH H . 
MB 5 HOH 3   2003 2003 HOH HOH H . 
MB 5 HOH 4   2004 2004 HOH HOH H . 
MB 5 HOH 5   2005 2005 HOH HOH H . 
MB 5 HOH 6   2006 2006 HOH HOH H . 
MB 5 HOH 7   2007 2007 HOH HOH H . 
MB 5 HOH 8   2008 2008 HOH HOH H . 
MB 5 HOH 9   2009 2009 HOH HOH H . 
MB 5 HOH 10  2010 2010 HOH HOH H . 
MB 5 HOH 11  2011 2011 HOH HOH H . 
MB 5 HOH 12  2012 2012 HOH HOH H . 
MB 5 HOH 13  2013 2013 HOH HOH H . 
MB 5 HOH 14  2014 2014 HOH HOH H . 
MB 5 HOH 15  2015 2015 HOH HOH H . 
MB 5 HOH 16  2016 2016 HOH HOH H . 
MB 5 HOH 17  2017 2017 HOH HOH H . 
MB 5 HOH 18  2018 2018 HOH HOH H . 
MB 5 HOH 19  2019 2019 HOH HOH H . 
MB 5 HOH 20  2020 2020 HOH HOH H . 
MB 5 HOH 21  2021 2021 HOH HOH H . 
MB 5 HOH 22  2022 2022 HOH HOH H . 
MB 5 HOH 23  2023 2023 HOH HOH H . 
MB 5 HOH 24  2024 2024 HOH HOH H . 
MB 5 HOH 25  2025 2025 HOH HOH H . 
MB 5 HOH 26  2026 2026 HOH HOH H . 
MB 5 HOH 27  2027 2027 HOH HOH H . 
MB 5 HOH 28  2028 2028 HOH HOH H . 
MB 5 HOH 29  2029 2029 HOH HOH H . 
MB 5 HOH 30  2030 2030 HOH HOH H . 
MB 5 HOH 31  2031 2031 HOH HOH H . 
MB 5 HOH 32  2032 2032 HOH HOH H . 
MB 5 HOH 33  2033 2033 HOH HOH H . 
MB 5 HOH 34  2034 2034 HOH HOH H . 
MB 5 HOH 35  2035 2035 HOH HOH H . 
MB 5 HOH 36  2036 2036 HOH HOH H . 
MB 5 HOH 37  2037 2037 HOH HOH H . 
MB 5 HOH 38  2038 2038 HOH HOH H . 
MB 5 HOH 39  2039 2039 HOH HOH H . 
MB 5 HOH 40  2040 2040 HOH HOH H . 
MB 5 HOH 41  2041 2041 HOH HOH H . 
MB 5 HOH 42  2042 2042 HOH HOH H . 
MB 5 HOH 43  2043 2043 HOH HOH H . 
MB 5 HOH 44  2044 2044 HOH HOH H . 
MB 5 HOH 45  2045 2045 HOH HOH H . 
MB 5 HOH 46  2046 2046 HOH HOH H . 
MB 5 HOH 47  2047 2047 HOH HOH H . 
MB 5 HOH 48  2048 2048 HOH HOH H . 
MB 5 HOH 49  2049 2049 HOH HOH H . 
MB 5 HOH 50  2050 2050 HOH HOH H . 
MB 5 HOH 51  2051 2051 HOH HOH H . 
MB 5 HOH 52  2052 2052 HOH HOH H . 
MB 5 HOH 53  2053 2053 HOH HOH H . 
MB 5 HOH 54  2054 2054 HOH HOH H . 
MB 5 HOH 55  2055 2055 HOH HOH H . 
MB 5 HOH 56  2056 2056 HOH HOH H . 
MB 5 HOH 57  2057 2057 HOH HOH H . 
MB 5 HOH 58  2058 2058 HOH HOH H . 
MB 5 HOH 59  2059 2059 HOH HOH H . 
MB 5 HOH 60  2060 2060 HOH HOH H . 
MB 5 HOH 61  2061 2061 HOH HOH H . 
MB 5 HOH 62  2062 2062 HOH HOH H . 
MB 5 HOH 63  2063 2063 HOH HOH H . 
MB 5 HOH 64  2064 2064 HOH HOH H . 
MB 5 HOH 65  2065 2065 HOH HOH H . 
MB 5 HOH 66  2066 2066 HOH HOH H . 
MB 5 HOH 67  2067 2067 HOH HOH H . 
MB 5 HOH 68  2068 2068 HOH HOH H . 
MB 5 HOH 69  2069 2069 HOH HOH H . 
MB 5 HOH 70  2070 2070 HOH HOH H . 
MB 5 HOH 71  2071 2071 HOH HOH H . 
MB 5 HOH 72  2072 2072 HOH HOH H . 
MB 5 HOH 73  2073 2073 HOH HOH H . 
MB 5 HOH 74  2074 2074 HOH HOH H . 
MB 5 HOH 75  2075 2075 HOH HOH H . 
MB 5 HOH 76  2076 2076 HOH HOH H . 
MB 5 HOH 77  2077 2077 HOH HOH H . 
MB 5 HOH 78  2078 2078 HOH HOH H . 
MB 5 HOH 79  2079 2079 HOH HOH H . 
MB 5 HOH 80  2080 2080 HOH HOH H . 
MB 5 HOH 81  2081 2081 HOH HOH H . 
MB 5 HOH 82  2082 2082 HOH HOH H . 
MB 5 HOH 83  2083 2083 HOH HOH H . 
MB 5 HOH 84  2084 2084 HOH HOH H . 
MB 5 HOH 85  2085 2085 HOH HOH H . 
MB 5 HOH 86  2086 2086 HOH HOH H . 
MB 5 HOH 87  2087 2087 HOH HOH H . 
MB 5 HOH 88  2088 2088 HOH HOH H . 
MB 5 HOH 89  2089 2089 HOH HOH H . 
MB 5 HOH 90  2090 2090 HOH HOH H . 
MB 5 HOH 91  2091 2091 HOH HOH H . 
MB 5 HOH 92  2092 2092 HOH HOH H . 
MB 5 HOH 93  2093 2093 HOH HOH H . 
MB 5 HOH 94  2094 2094 HOH HOH H . 
MB 5 HOH 95  2095 2095 HOH HOH H . 
MB 5 HOH 96  2096 2096 HOH HOH H . 
MB 5 HOH 97  2097 2097 HOH HOH H . 
MB 5 HOH 98  2098 2098 HOH HOH H . 
MB 5 HOH 99  2099 2099 HOH HOH H . 
MB 5 HOH 100 2100 2100 HOH HOH H . 
MB 5 HOH 101 2101 2101 HOH HOH H . 
MB 5 HOH 102 2102 2102 HOH HOH H . 
MB 5 HOH 103 2103 2103 HOH HOH H . 
MB 5 HOH 104 2104 2104 HOH HOH H . 
MB 5 HOH 105 2105 2105 HOH HOH H . 
MB 5 HOH 106 2106 2106 HOH HOH H . 
MB 5 HOH 107 2107 2107 HOH HOH H . 
MB 5 HOH 108 2108 2108 HOH HOH H . 
MB 5 HOH 109 2109 2109 HOH HOH H . 
MB 5 HOH 110 2110 2110 HOH HOH H . 
MB 5 HOH 111 2111 2111 HOH HOH H . 
MB 5 HOH 112 2112 2112 HOH HOH H . 
MB 5 HOH 113 2113 2113 HOH HOH H . 
MB 5 HOH 114 2114 2114 HOH HOH H . 
MB 5 HOH 115 2115 2115 HOH HOH H . 
MB 5 HOH 116 2116 2116 HOH HOH H . 
MB 5 HOH 117 2117 2117 HOH HOH H . 
MB 5 HOH 118 2118 2118 HOH HOH H . 
NB 5 HOH 1   2001 2001 HOH HOH I . 
NB 5 HOH 2   2002 2002 HOH HOH I . 
NB 5 HOH 3   2003 2003 HOH HOH I . 
NB 5 HOH 4   2004 2004 HOH HOH I . 
NB 5 HOH 5   2005 2005 HOH HOH I . 
NB 5 HOH 6   2006 2006 HOH HOH I . 
NB 5 HOH 7   2007 2007 HOH HOH I . 
NB 5 HOH 8   2008 2008 HOH HOH I . 
NB 5 HOH 9   2009 2009 HOH HOH I . 
NB 5 HOH 10  2010 2010 HOH HOH I . 
NB 5 HOH 11  2011 2011 HOH HOH I . 
NB 5 HOH 12  2012 2012 HOH HOH I . 
NB 5 HOH 13  2013 2013 HOH HOH I . 
NB 5 HOH 14  2014 2014 HOH HOH I . 
NB 5 HOH 15  2015 2015 HOH HOH I . 
NB 5 HOH 16  2016 2016 HOH HOH I . 
NB 5 HOH 17  2017 2017 HOH HOH I . 
NB 5 HOH 18  2018 2018 HOH HOH I . 
NB 5 HOH 19  2019 2019 HOH HOH I . 
NB 5 HOH 20  2020 2020 HOH HOH I . 
NB 5 HOH 21  2021 2021 HOH HOH I . 
NB 5 HOH 22  2022 2022 HOH HOH I . 
NB 5 HOH 23  2023 2023 HOH HOH I . 
NB 5 HOH 24  2024 2024 HOH HOH I . 
NB 5 HOH 25  2025 2025 HOH HOH I . 
NB 5 HOH 26  2026 2026 HOH HOH I . 
NB 5 HOH 27  2027 2027 HOH HOH I . 
NB 5 HOH 28  2028 2028 HOH HOH I . 
NB 5 HOH 29  2029 2029 HOH HOH I . 
NB 5 HOH 30  2030 2030 HOH HOH I . 
NB 5 HOH 31  2031 2031 HOH HOH I . 
NB 5 HOH 32  2032 2032 HOH HOH I . 
NB 5 HOH 33  2033 2033 HOH HOH I . 
NB 5 HOH 34  2034 2034 HOH HOH I . 
NB 5 HOH 35  2035 2035 HOH HOH I . 
NB 5 HOH 36  2036 2036 HOH HOH I . 
NB 5 HOH 37  2037 2037 HOH HOH I . 
NB 5 HOH 38  2038 2038 HOH HOH I . 
NB 5 HOH 39  2039 2039 HOH HOH I . 
NB 5 HOH 40  2040 2040 HOH HOH I . 
NB 5 HOH 41  2041 2041 HOH HOH I . 
NB 5 HOH 42  2042 2042 HOH HOH I . 
NB 5 HOH 43  2043 2043 HOH HOH I . 
NB 5 HOH 44  2044 2044 HOH HOH I . 
NB 5 HOH 45  2045 2045 HOH HOH I . 
NB 5 HOH 46  2046 2046 HOH HOH I . 
NB 5 HOH 47  2047 2047 HOH HOH I . 
NB 5 HOH 48  2048 2048 HOH HOH I . 
NB 5 HOH 49  2049 2049 HOH HOH I . 
NB 5 HOH 50  2050 2050 HOH HOH I . 
NB 5 HOH 51  2051 2051 HOH HOH I . 
NB 5 HOH 52  2052 2052 HOH HOH I . 
NB 5 HOH 53  2053 2053 HOH HOH I . 
NB 5 HOH 54  2054 2054 HOH HOH I . 
NB 5 HOH 55  2055 2055 HOH HOH I . 
NB 5 HOH 56  2056 2056 HOH HOH I . 
NB 5 HOH 57  2057 2057 HOH HOH I . 
NB 5 HOH 58  2058 2058 HOH HOH I . 
NB 5 HOH 59  2059 2059 HOH HOH I . 
NB 5 HOH 60  2060 2060 HOH HOH I . 
NB 5 HOH 61  2061 2061 HOH HOH I . 
NB 5 HOH 62  2062 2062 HOH HOH I . 
NB 5 HOH 63  2063 2063 HOH HOH I . 
NB 5 HOH 64  2064 2064 HOH HOH I . 
NB 5 HOH 65  2065 2065 HOH HOH I . 
NB 5 HOH 66  2066 2066 HOH HOH I . 
NB 5 HOH 67  2067 2067 HOH HOH I . 
NB 5 HOH 68  2068 2068 HOH HOH I . 
NB 5 HOH 69  2069 2069 HOH HOH I . 
NB 5 HOH 70  2070 2070 HOH HOH I . 
NB 5 HOH 71  2071 2071 HOH HOH I . 
NB 5 HOH 72  2072 2072 HOH HOH I . 
NB 5 HOH 73  2073 2073 HOH HOH I . 
NB 5 HOH 74  2074 2074 HOH HOH I . 
NB 5 HOH 75  2075 2075 HOH HOH I . 
NB 5 HOH 76  2076 2076 HOH HOH I . 
NB 5 HOH 77  2077 2077 HOH HOH I . 
NB 5 HOH 78  2078 2078 HOH HOH I . 
NB 5 HOH 79  2079 2079 HOH HOH I . 
NB 5 HOH 80  2080 2080 HOH HOH I . 
NB 5 HOH 81  2081 2081 HOH HOH I . 
NB 5 HOH 82  2082 2082 HOH HOH I . 
NB 5 HOH 83  2083 2083 HOH HOH I . 
NB 5 HOH 84  2084 2084 HOH HOH I . 
NB 5 HOH 85  2085 2085 HOH HOH I . 
NB 5 HOH 86  2086 2086 HOH HOH I . 
NB 5 HOH 87  2087 2087 HOH HOH I . 
NB 5 HOH 88  2088 2088 HOH HOH I . 
NB 5 HOH 89  2089 2089 HOH HOH I . 
NB 5 HOH 90  2090 2090 HOH HOH I . 
NB 5 HOH 91  2091 2091 HOH HOH I . 
NB 5 HOH 92  2092 2092 HOH HOH I . 
NB 5 HOH 93  2093 2093 HOH HOH I . 
NB 5 HOH 94  2094 2094 HOH HOH I . 
NB 5 HOH 95  2095 2095 HOH HOH I . 
NB 5 HOH 96  2096 2096 HOH HOH I . 
NB 5 HOH 97  2097 2097 HOH HOH I . 
NB 5 HOH 98  2098 2098 HOH HOH I . 
NB 5 HOH 99  2099 2099 HOH HOH I . 
NB 5 HOH 100 2100 2100 HOH HOH I . 
NB 5 HOH 101 2101 2101 HOH HOH I . 
NB 5 HOH 102 2102 2102 HOH HOH I . 
NB 5 HOH 103 2103 2103 HOH HOH I . 
NB 5 HOH 104 2104 2104 HOH HOH I . 
NB 5 HOH 105 2105 2105 HOH HOH I . 
NB 5 HOH 106 2106 2106 HOH HOH I . 
NB 5 HOH 107 2107 2107 HOH HOH I . 
NB 5 HOH 108 2108 2108 HOH HOH I . 
NB 5 HOH 109 2109 2109 HOH HOH I . 
NB 5 HOH 110 2110 2110 HOH HOH I . 
NB 5 HOH 111 2111 2111 HOH HOH I . 
NB 5 HOH 112 2112 2112 HOH HOH I . 
NB 5 HOH 113 2113 2113 HOH HOH I . 
NB 5 HOH 114 2114 2114 HOH HOH I . 
NB 5 HOH 115 2115 2115 HOH HOH I . 
NB 5 HOH 116 2116 2116 HOH HOH I . 
NB 5 HOH 117 2117 2117 HOH HOH I . 
NB 5 HOH 118 2118 2118 HOH HOH I . 
NB 5 HOH 119 2119 2119 HOH HOH I . 
NB 5 HOH 120 2120 2120 HOH HOH I . 
NB 5 HOH 121 2121 2121 HOH HOH I . 
NB 5 HOH 122 2122 2122 HOH HOH I . 
NB 5 HOH 123 2123 2123 HOH HOH I . 
NB 5 HOH 124 2124 2124 HOH HOH I . 
NB 5 HOH 125 2125 2125 HOH HOH I . 
NB 5 HOH 126 2126 2126 HOH HOH I . 
NB 5 HOH 127 2127 2127 HOH HOH I . 
NB 5 HOH 128 2128 2128 HOH HOH I . 
NB 5 HOH 129 2129 2129 HOH HOH I . 
NB 5 HOH 130 2130 2130 HOH HOH I . 
NB 5 HOH 131 2131 2131 HOH HOH I . 
NB 5 HOH 132 2132 2132 HOH HOH I . 
NB 5 HOH 133 2133 2133 HOH HOH I . 
NB 5 HOH 134 2134 2134 HOH HOH I . 
NB 5 HOH 135 2135 2135 HOH HOH I . 
NB 5 HOH 136 2136 2136 HOH HOH I . 
NB 5 HOH 137 2137 2137 HOH HOH I . 
NB 5 HOH 138 2138 2138 HOH HOH I . 
NB 5 HOH 139 2139 2139 HOH HOH I . 
NB 5 HOH 140 2140 2140 HOH HOH I . 
NB 5 HOH 141 2141 2141 HOH HOH I . 
OB 5 HOH 1   2001 2001 HOH HOH J . 
OB 5 HOH 2   2002 2002 HOH HOH J . 
OB 5 HOH 3   2003 2003 HOH HOH J . 
OB 5 HOH 4   2004 2004 HOH HOH J . 
OB 5 HOH 5   2005 2005 HOH HOH J . 
OB 5 HOH 6   2006 2006 HOH HOH J . 
OB 5 HOH 7   2007 2007 HOH HOH J . 
OB 5 HOH 8   2008 2008 HOH HOH J . 
OB 5 HOH 9   2009 2009 HOH HOH J . 
OB 5 HOH 10  2010 2010 HOH HOH J . 
OB 5 HOH 11  2011 2011 HOH HOH J . 
OB 5 HOH 12  2012 2012 HOH HOH J . 
OB 5 HOH 13  2013 2013 HOH HOH J . 
OB 5 HOH 14  2014 2014 HOH HOH J . 
OB 5 HOH 15  2015 2015 HOH HOH J . 
OB 5 HOH 16  2016 2016 HOH HOH J . 
OB 5 HOH 17  2017 2017 HOH HOH J . 
OB 5 HOH 18  2018 2018 HOH HOH J . 
OB 5 HOH 19  2019 2019 HOH HOH J . 
OB 5 HOH 20  2020 2020 HOH HOH J . 
OB 5 HOH 21  2021 2021 HOH HOH J . 
OB 5 HOH 22  2022 2022 HOH HOH J . 
OB 5 HOH 23  2023 2023 HOH HOH J . 
OB 5 HOH 24  2024 2024 HOH HOH J . 
OB 5 HOH 25  2025 2025 HOH HOH J . 
OB 5 HOH 26  2026 2026 HOH HOH J . 
OB 5 HOH 27  2027 2027 HOH HOH J . 
OB 5 HOH 28  2028 2028 HOH HOH J . 
OB 5 HOH 29  2029 2029 HOH HOH J . 
OB 5 HOH 30  2030 2030 HOH HOH J . 
OB 5 HOH 31  2031 2031 HOH HOH J . 
OB 5 HOH 32  2032 2032 HOH HOH J . 
OB 5 HOH 33  2033 2033 HOH HOH J . 
OB 5 HOH 34  2034 2034 HOH HOH J . 
OB 5 HOH 35  2035 2035 HOH HOH J . 
OB 5 HOH 36  2036 2036 HOH HOH J . 
OB 5 HOH 37  2037 2037 HOH HOH J . 
OB 5 HOH 38  2038 2038 HOH HOH J . 
OB 5 HOH 39  2039 2039 HOH HOH J . 
OB 5 HOH 40  2040 2040 HOH HOH J . 
OB 5 HOH 41  2041 2041 HOH HOH J . 
OB 5 HOH 42  2042 2042 HOH HOH J . 
OB 5 HOH 43  2043 2043 HOH HOH J . 
OB 5 HOH 44  2044 2044 HOH HOH J . 
OB 5 HOH 45  2045 2045 HOH HOH J . 
OB 5 HOH 46  2046 2046 HOH HOH J . 
OB 5 HOH 47  2047 2047 HOH HOH J . 
OB 5 HOH 48  2048 2048 HOH HOH J . 
OB 5 HOH 49  2049 2049 HOH HOH J . 
OB 5 HOH 50  2050 2050 HOH HOH J . 
OB 5 HOH 51  2051 2051 HOH HOH J . 
OB 5 HOH 52  2052 2052 HOH HOH J . 
OB 5 HOH 53  2053 2053 HOH HOH J . 
OB 5 HOH 54  2054 2054 HOH HOH J . 
OB 5 HOH 55  2055 2055 HOH HOH J . 
OB 5 HOH 56  2056 2056 HOH HOH J . 
OB 5 HOH 57  2057 2057 HOH HOH J . 
OB 5 HOH 58  2058 2058 HOH HOH J . 
OB 5 HOH 59  2059 2059 HOH HOH J . 
OB 5 HOH 60  2060 2060 HOH HOH J . 
OB 5 HOH 61  2061 2061 HOH HOH J . 
OB 5 HOH 62  2062 2062 HOH HOH J . 
OB 5 HOH 63  2063 2063 HOH HOH J . 
OB 5 HOH 64  2064 2064 HOH HOH J . 
OB 5 HOH 65  2065 2065 HOH HOH J . 
OB 5 HOH 66  2066 2066 HOH HOH J . 
OB 5 HOH 67  2067 2067 HOH HOH J . 
OB 5 HOH 68  2068 2068 HOH HOH J . 
OB 5 HOH 69  2069 2069 HOH HOH J . 
OB 5 HOH 70  2070 2070 HOH HOH J . 
OB 5 HOH 71  2071 2071 HOH HOH J . 
OB 5 HOH 72  2072 2072 HOH HOH J . 
OB 5 HOH 73  2073 2073 HOH HOH J . 
OB 5 HOH 74  2074 2074 HOH HOH J . 
OB 5 HOH 75  2075 2075 HOH HOH J . 
OB 5 HOH 76  2076 2076 HOH HOH J . 
OB 5 HOH 77  2077 2077 HOH HOH J . 
OB 5 HOH 78  2078 2078 HOH HOH J . 
OB 5 HOH 79  2079 2079 HOH HOH J . 
OB 5 HOH 80  2080 2080 HOH HOH J . 
OB 5 HOH 81  2081 2081 HOH HOH J . 
OB 5 HOH 82  2082 2082 HOH HOH J . 
OB 5 HOH 83  2083 2083 HOH HOH J . 
OB 5 HOH 84  2084 2084 HOH HOH J . 
OB 5 HOH 85  2085 2085 HOH HOH J . 
OB 5 HOH 86  2086 2086 HOH HOH J . 
OB 5 HOH 87  2087 2087 HOH HOH J . 
OB 5 HOH 88  2088 2088 HOH HOH J . 
OB 5 HOH 89  2089 2089 HOH HOH J . 
OB 5 HOH 90  2090 2090 HOH HOH J . 
OB 5 HOH 91  2091 2091 HOH HOH J . 
OB 5 HOH 92  2092 2092 HOH HOH J . 
OB 5 HOH 93  2093 2093 HOH HOH J . 
OB 5 HOH 94  2094 2094 HOH HOH J . 
OB 5 HOH 95  2095 2095 HOH HOH J . 
OB 5 HOH 96  2096 2096 HOH HOH J . 
OB 5 HOH 97  2097 2097 HOH HOH J . 
OB 5 HOH 98  2098 2098 HOH HOH J . 
OB 5 HOH 99  2099 2099 HOH HOH J . 
OB 5 HOH 100 2100 2100 HOH HOH J . 
OB 5 HOH 101 2101 2101 HOH HOH J . 
OB 5 HOH 102 2102 2102 HOH HOH J . 
OB 5 HOH 103 2103 2103 HOH HOH J . 
OB 5 HOH 104 2104 2104 HOH HOH J . 
OB 5 HOH 105 2105 2105 HOH HOH J . 
OB 5 HOH 106 2106 2106 HOH HOH J . 
OB 5 HOH 107 2107 2107 HOH HOH J . 
OB 5 HOH 108 2108 2108 HOH HOH J . 
OB 5 HOH 109 2109 2109 HOH HOH J . 
OB 5 HOH 110 2110 2110 HOH HOH J . 
OB 5 HOH 111 2111 2111 HOH HOH J . 
OB 5 HOH 112 2112 2112 HOH HOH J . 
OB 5 HOH 113 2113 2113 HOH HOH J . 
OB 5 HOH 114 2114 2114 HOH HOH J . 
OB 5 HOH 115 2115 2115 HOH HOH J . 
OB 5 HOH 116 2116 2116 HOH HOH J . 
OB 5 HOH 117 2117 2117 HOH HOH J . 
OB 5 HOH 118 2118 2118 HOH HOH J . 
OB 5 HOH 119 2119 2119 HOH HOH J . 
OB 5 HOH 120 2120 2120 HOH HOH J . 
OB 5 HOH 121 2121 2121 HOH HOH J . 
OB 5 HOH 122 2122 2122 HOH HOH J . 
OB 5 HOH 123 2123 2123 HOH HOH J . 
OB 5 HOH 124 2124 2124 HOH HOH J . 
OB 5 HOH 125 2125 2125 HOH HOH J . 
OB 5 HOH 126 2126 2126 HOH HOH J . 
OB 5 HOH 127 2127 2127 HOH HOH J . 
OB 5 HOH 128 2128 2128 HOH HOH J . 
OB 5 HOH 129 2129 2129 HOH HOH J . 
OB 5 HOH 130 2130 2130 HOH HOH J . 
OB 5 HOH 131 2131 2131 HOH HOH J . 
OB 5 HOH 132 2132 2132 HOH HOH J . 
OB 5 HOH 133 2133 2133 HOH HOH J . 
PB 5 HOH 1   2001 2001 HOH HOH K . 
PB 5 HOH 2   2002 2002 HOH HOH K . 
PB 5 HOH 3   2003 2003 HOH HOH K . 
PB 5 HOH 4   2004 2004 HOH HOH K . 
PB 5 HOH 5   2005 2005 HOH HOH K . 
PB 5 HOH 6   2006 2006 HOH HOH K . 
PB 5 HOH 7   2007 2007 HOH HOH K . 
PB 5 HOH 8   2008 2008 HOH HOH K . 
PB 5 HOH 9   2009 2009 HOH HOH K . 
PB 5 HOH 10  2010 2010 HOH HOH K . 
PB 5 HOH 11  2011 2011 HOH HOH K . 
PB 5 HOH 12  2012 2012 HOH HOH K . 
PB 5 HOH 13  2013 2013 HOH HOH K . 
PB 5 HOH 14  2014 2014 HOH HOH K . 
PB 5 HOH 15  2015 2015 HOH HOH K . 
PB 5 HOH 16  2016 2016 HOH HOH K . 
PB 5 HOH 17  2017 2017 HOH HOH K . 
PB 5 HOH 18  2018 2018 HOH HOH K . 
PB 5 HOH 19  2019 2019 HOH HOH K . 
PB 5 HOH 20  2020 2020 HOH HOH K . 
PB 5 HOH 21  2021 2021 HOH HOH K . 
PB 5 HOH 22  2022 2022 HOH HOH K . 
PB 5 HOH 23  2023 2023 HOH HOH K . 
PB 5 HOH 24  2024 2024 HOH HOH K . 
PB 5 HOH 25  2025 2025 HOH HOH K . 
PB 5 HOH 26  2026 2026 HOH HOH K . 
PB 5 HOH 27  2027 2027 HOH HOH K . 
PB 5 HOH 28  2028 2028 HOH HOH K . 
PB 5 HOH 29  2029 2029 HOH HOH K . 
PB 5 HOH 30  2030 2030 HOH HOH K . 
PB 5 HOH 31  2031 2031 HOH HOH K . 
PB 5 HOH 32  2032 2032 HOH HOH K . 
PB 5 HOH 33  2033 2033 HOH HOH K . 
PB 5 HOH 34  2034 2034 HOH HOH K . 
PB 5 HOH 35  2035 2035 HOH HOH K . 
PB 5 HOH 36  2036 2036 HOH HOH K . 
PB 5 HOH 37  2037 2037 HOH HOH K . 
PB 5 HOH 38  2038 2038 HOH HOH K . 
PB 5 HOH 39  2039 2039 HOH HOH K . 
PB 5 HOH 40  2040 2040 HOH HOH K . 
PB 5 HOH 41  2041 2041 HOH HOH K . 
PB 5 HOH 42  2042 2042 HOH HOH K . 
PB 5 HOH 43  2043 2043 HOH HOH K . 
PB 5 HOH 44  2044 2044 HOH HOH K . 
PB 5 HOH 45  2045 2045 HOH HOH K . 
PB 5 HOH 46  2046 2046 HOH HOH K . 
PB 5 HOH 47  2047 2047 HOH HOH K . 
PB 5 HOH 48  2048 2048 HOH HOH K . 
PB 5 HOH 49  2049 2049 HOH HOH K . 
PB 5 HOH 50  2050 2050 HOH HOH K . 
PB 5 HOH 51  2051 2051 HOH HOH K . 
PB 5 HOH 52  2052 2052 HOH HOH K . 
PB 5 HOH 53  2053 2053 HOH HOH K . 
PB 5 HOH 54  2054 2054 HOH HOH K . 
PB 5 HOH 55  2055 2055 HOH HOH K . 
PB 5 HOH 56  2056 2056 HOH HOH K . 
PB 5 HOH 57  2057 2057 HOH HOH K . 
PB 5 HOH 58  2058 2058 HOH HOH K . 
PB 5 HOH 59  2059 2059 HOH HOH K . 
PB 5 HOH 60  2060 2060 HOH HOH K . 
PB 5 HOH 61  2061 2061 HOH HOH K . 
PB 5 HOH 62  2062 2062 HOH HOH K . 
PB 5 HOH 63  2063 2063 HOH HOH K . 
PB 5 HOH 64  2064 2064 HOH HOH K . 
PB 5 HOH 65  2065 2065 HOH HOH K . 
PB 5 HOH 66  2066 2066 HOH HOH K . 
PB 5 HOH 67  2067 2067 HOH HOH K . 
PB 5 HOH 68  2068 2068 HOH HOH K . 
PB 5 HOH 69  2069 2069 HOH HOH K . 
PB 5 HOH 70  2070 2070 HOH HOH K . 
PB 5 HOH 71  2071 2071 HOH HOH K . 
PB 5 HOH 72  2072 2072 HOH HOH K . 
PB 5 HOH 73  2073 2073 HOH HOH K . 
PB 5 HOH 74  2074 2074 HOH HOH K . 
PB 5 HOH 75  2075 2075 HOH HOH K . 
PB 5 HOH 76  2076 2076 HOH HOH K . 
PB 5 HOH 77  2077 2077 HOH HOH K . 
PB 5 HOH 78  2078 2078 HOH HOH K . 
PB 5 HOH 79  2079 2079 HOH HOH K . 
PB 5 HOH 80  2080 2080 HOH HOH K . 
PB 5 HOH 81  2081 2081 HOH HOH K . 
PB 5 HOH 82  2082 2082 HOH HOH K . 
PB 5 HOH 83  2083 2083 HOH HOH K . 
PB 5 HOH 84  2084 2084 HOH HOH K . 
PB 5 HOH 85  2085 2085 HOH HOH K . 
PB 5 HOH 86  2086 2086 HOH HOH K . 
PB 5 HOH 87  2087 2087 HOH HOH K . 
PB 5 HOH 88  2088 2088 HOH HOH K . 
PB 5 HOH 89  2089 2089 HOH HOH K . 
PB 5 HOH 90  2090 2090 HOH HOH K . 
PB 5 HOH 91  2091 2091 HOH HOH K . 
PB 5 HOH 92  2092 2092 HOH HOH K . 
PB 5 HOH 93  2093 2093 HOH HOH K . 
PB 5 HOH 94  2094 2094 HOH HOH K . 
PB 5 HOH 95  2095 2095 HOH HOH K . 
PB 5 HOH 96  2096 2096 HOH HOH K . 
PB 5 HOH 97  2097 2097 HOH HOH K . 
PB 5 HOH 98  2098 2098 HOH HOH K . 
PB 5 HOH 99  2099 2099 HOH HOH K . 
PB 5 HOH 100 2100 2100 HOH HOH K . 
PB 5 HOH 101 2101 2101 HOH HOH K . 
PB 5 HOH 102 2102 2102 HOH HOH K . 
PB 5 HOH 103 2103 2103 HOH HOH K . 
PB 5 HOH 104 2104 2104 HOH HOH K . 
PB 5 HOH 105 2105 2105 HOH HOH K . 
PB 5 HOH 106 2106 2106 HOH HOH K . 
PB 5 HOH 107 2107 2107 HOH HOH K . 
PB 5 HOH 108 2108 2108 HOH HOH K . 
PB 5 HOH 109 2109 2109 HOH HOH K . 
PB 5 HOH 110 2110 2110 HOH HOH K . 
PB 5 HOH 111 2111 2111 HOH HOH K . 
PB 5 HOH 112 2112 2112 HOH HOH K . 
PB 5 HOH 113 2113 2113 HOH HOH K . 
PB 5 HOH 114 2114 2114 HOH HOH K . 
PB 5 HOH 115 2115 2115 HOH HOH K . 
PB 5 HOH 116 2116 2116 HOH HOH K . 
PB 5 HOH 117 2117 2117 HOH HOH K . 
PB 5 HOH 118 2118 2118 HOH HOH K . 
PB 5 HOH 119 2119 2119 HOH HOH K . 
PB 5 HOH 120 2120 2120 HOH HOH K . 
PB 5 HOH 121 2121 2121 HOH HOH K . 
PB 5 HOH 122 2122 2122 HOH HOH K . 
PB 5 HOH 123 2123 2123 HOH HOH K . 
PB 5 HOH 124 2124 2124 HOH HOH K . 
PB 5 HOH 125 2125 2125 HOH HOH K . 
PB 5 HOH 126 2126 2126 HOH HOH K . 
PB 5 HOH 127 2127 2127 HOH HOH K . 
PB 5 HOH 128 2128 2128 HOH HOH K . 
PB 5 HOH 129 2129 2129 HOH HOH K . 
PB 5 HOH 130 2130 2130 HOH HOH K . 
PB 5 HOH 131 2131 2131 HOH HOH K . 
PB 5 HOH 132 2132 2132 HOH HOH K . 
PB 5 HOH 133 2133 2133 HOH HOH K . 
PB 5 HOH 134 2134 2134 HOH HOH K . 
PB 5 HOH 135 2135 2135 HOH HOH K . 
PB 5 HOH 136 2136 2136 HOH HOH K . 
PB 5 HOH 137 2137 2137 HOH HOH K . 
PB 5 HOH 138 2138 2138 HOH HOH K . 
PB 5 HOH 139 2139 2139 HOH HOH K . 
PB 5 HOH 140 2140 2140 HOH HOH K . 
PB 5 HOH 141 2141 2141 HOH HOH K . 
PB 5 HOH 142 2142 2142 HOH HOH K . 
PB 5 HOH 143 2143 2143 HOH HOH K . 
PB 5 HOH 144 2144 2144 HOH HOH K . 
PB 5 HOH 145 2145 2145 HOH HOH K . 
PB 5 HOH 146 2146 2146 HOH HOH K . 
PB 5 HOH 147 2147 2147 HOH HOH K . 
PB 5 HOH 148 2148 2148 HOH HOH K . 
QB 5 HOH 1   2001 2001 HOH HOH L . 
QB 5 HOH 2   2002 2002 HOH HOH L . 
QB 5 HOH 3   2003 2003 HOH HOH L . 
QB 5 HOH 4   2004 2004 HOH HOH L . 
QB 5 HOH 5   2005 2005 HOH HOH L . 
QB 5 HOH 6   2006 2006 HOH HOH L . 
QB 5 HOH 7   2007 2007 HOH HOH L . 
QB 5 HOH 8   2008 2008 HOH HOH L . 
QB 5 HOH 9   2009 2009 HOH HOH L . 
QB 5 HOH 10  2010 2010 HOH HOH L . 
QB 5 HOH 11  2011 2011 HOH HOH L . 
QB 5 HOH 12  2012 2012 HOH HOH L . 
QB 5 HOH 13  2013 2013 HOH HOH L . 
QB 5 HOH 14  2014 2014 HOH HOH L . 
QB 5 HOH 15  2015 2015 HOH HOH L . 
QB 5 HOH 16  2016 2016 HOH HOH L . 
QB 5 HOH 17  2017 2017 HOH HOH L . 
QB 5 HOH 18  2018 2018 HOH HOH L . 
QB 5 HOH 19  2019 2019 HOH HOH L . 
QB 5 HOH 20  2020 2020 HOH HOH L . 
QB 5 HOH 21  2021 2021 HOH HOH L . 
QB 5 HOH 22  2022 2022 HOH HOH L . 
QB 5 HOH 23  2023 2023 HOH HOH L . 
QB 5 HOH 24  2024 2024 HOH HOH L . 
QB 5 HOH 25  2025 2025 HOH HOH L . 
QB 5 HOH 26  2026 2026 HOH HOH L . 
QB 5 HOH 27  2027 2027 HOH HOH L . 
QB 5 HOH 28  2028 2028 HOH HOH L . 
QB 5 HOH 29  2029 2029 HOH HOH L . 
QB 5 HOH 30  2030 2030 HOH HOH L . 
QB 5 HOH 31  2031 2031 HOH HOH L . 
QB 5 HOH 32  2032 2032 HOH HOH L . 
QB 5 HOH 33  2033 2033 HOH HOH L . 
QB 5 HOH 34  2034 2034 HOH HOH L . 
QB 5 HOH 35  2035 2035 HOH HOH L . 
QB 5 HOH 36  2036 2036 HOH HOH L . 
QB 5 HOH 37  2037 2037 HOH HOH L . 
QB 5 HOH 38  2038 2038 HOH HOH L . 
QB 5 HOH 39  2039 2039 HOH HOH L . 
QB 5 HOH 40  2040 2040 HOH HOH L . 
QB 5 HOH 41  2041 2041 HOH HOH L . 
QB 5 HOH 42  2042 2042 HOH HOH L . 
QB 5 HOH 43  2043 2043 HOH HOH L . 
QB 5 HOH 44  2044 2044 HOH HOH L . 
QB 5 HOH 45  2045 2045 HOH HOH L . 
QB 5 HOH 46  2046 2046 HOH HOH L . 
QB 5 HOH 47  2047 2047 HOH HOH L . 
QB 5 HOH 48  2048 2048 HOH HOH L . 
QB 5 HOH 49  2049 2049 HOH HOH L . 
QB 5 HOH 50  2050 2050 HOH HOH L . 
QB 5 HOH 51  2051 2051 HOH HOH L . 
QB 5 HOH 52  2052 2052 HOH HOH L . 
QB 5 HOH 53  2053 2053 HOH HOH L . 
QB 5 HOH 54  2054 2054 HOH HOH L . 
QB 5 HOH 55  2055 2055 HOH HOH L . 
QB 5 HOH 56  2056 2056 HOH HOH L . 
QB 5 HOH 57  2057 2057 HOH HOH L . 
QB 5 HOH 58  2058 2058 HOH HOH L . 
QB 5 HOH 59  2059 2059 HOH HOH L . 
QB 5 HOH 60  2060 2060 HOH HOH L . 
QB 5 HOH 61  2061 2061 HOH HOH L . 
QB 5 HOH 62  2062 2062 HOH HOH L . 
QB 5 HOH 63  2063 2063 HOH HOH L . 
QB 5 HOH 64  2064 2064 HOH HOH L . 
QB 5 HOH 65  2065 2065 HOH HOH L . 
QB 5 HOH 66  2066 2066 HOH HOH L . 
QB 5 HOH 67  2067 2067 HOH HOH L . 
QB 5 HOH 68  2068 2068 HOH HOH L . 
QB 5 HOH 69  2069 2069 HOH HOH L . 
QB 5 HOH 70  2070 2070 HOH HOH L . 
QB 5 HOH 71  2071 2071 HOH HOH L . 
QB 5 HOH 72  2072 2072 HOH HOH L . 
QB 5 HOH 73  2073 2073 HOH HOH L . 
QB 5 HOH 74  2074 2074 HOH HOH L . 
QB 5 HOH 75  2075 2075 HOH HOH L . 
QB 5 HOH 76  2076 2076 HOH HOH L . 
QB 5 HOH 77  2077 2077 HOH HOH L . 
QB 5 HOH 78  2078 2078 HOH HOH L . 
QB 5 HOH 79  2079 2079 HOH HOH L . 
QB 5 HOH 80  2080 2080 HOH HOH L . 
QB 5 HOH 81  2081 2081 HOH HOH L . 
QB 5 HOH 82  2082 2082 HOH HOH L . 
QB 5 HOH 83  2083 2083 HOH HOH L . 
QB 5 HOH 84  2084 2084 HOH HOH L . 
QB 5 HOH 85  2085 2085 HOH HOH L . 
QB 5 HOH 86  2086 2086 HOH HOH L . 
QB 5 HOH 87  2087 2087 HOH HOH L . 
QB 5 HOH 88  2088 2088 HOH HOH L . 
QB 5 HOH 89  2089 2089 HOH HOH L . 
QB 5 HOH 90  2090 2090 HOH HOH L . 
QB 5 HOH 91  2091 2091 HOH HOH L . 
QB 5 HOH 92  2092 2092 HOH HOH L . 
QB 5 HOH 93  2093 2093 HOH HOH L . 
QB 5 HOH 94  2094 2094 HOH HOH L . 
QB 5 HOH 95  2095 2095 HOH HOH L . 
QB 5 HOH 96  2096 2096 HOH HOH L . 
QB 5 HOH 97  2097 2097 HOH HOH L . 
QB 5 HOH 98  2098 2098 HOH HOH L . 
QB 5 HOH 99  2099 2099 HOH HOH L . 
QB 5 HOH 100 2100 2100 HOH HOH L . 
QB 5 HOH 101 2101 2101 HOH HOH L . 
QB 5 HOH 102 2102 2102 HOH HOH L . 
QB 5 HOH 103 2103 2103 HOH HOH L . 
QB 5 HOH 104 2104 2104 HOH HOH L . 
QB 5 HOH 105 2105 2105 HOH HOH L . 
QB 5 HOH 106 2106 2106 HOH HOH L . 
QB 5 HOH 107 2107 2107 HOH HOH L . 
QB 5 HOH 108 2108 2108 HOH HOH L . 
QB 5 HOH 109 2109 2109 HOH HOH L . 
QB 5 HOH 110 2110 2110 HOH HOH L . 
QB 5 HOH 111 2111 2111 HOH HOH L . 
QB 5 HOH 112 2112 2112 HOH HOH L . 
QB 5 HOH 113 2113 2113 HOH HOH L . 
QB 5 HOH 114 2114 2114 HOH HOH L . 
QB 5 HOH 115 2115 2115 HOH HOH L . 
RB 5 HOH 1   2001 2001 HOH HOH M . 
RB 5 HOH 2   2002 2002 HOH HOH M . 
RB 5 HOH 3   2003 2003 HOH HOH M . 
RB 5 HOH 4   2004 2004 HOH HOH M . 
RB 5 HOH 5   2005 2005 HOH HOH M . 
RB 5 HOH 6   2006 2006 HOH HOH M . 
RB 5 HOH 7   2007 2007 HOH HOH M . 
RB 5 HOH 8   2008 2008 HOH HOH M . 
RB 5 HOH 9   2009 2009 HOH HOH M . 
RB 5 HOH 10  2010 2010 HOH HOH M . 
RB 5 HOH 11  2011 2011 HOH HOH M . 
RB 5 HOH 12  2012 2012 HOH HOH M . 
RB 5 HOH 13  2013 2013 HOH HOH M . 
RB 5 HOH 14  2014 2014 HOH HOH M . 
RB 5 HOH 15  2015 2015 HOH HOH M . 
RB 5 HOH 16  2016 2016 HOH HOH M . 
RB 5 HOH 17  2017 2017 HOH HOH M . 
RB 5 HOH 18  2018 2018 HOH HOH M . 
RB 5 HOH 19  2019 2019 HOH HOH M . 
RB 5 HOH 20  2020 2020 HOH HOH M . 
RB 5 HOH 21  2021 2021 HOH HOH M . 
RB 5 HOH 22  2022 2022 HOH HOH M . 
RB 5 HOH 23  2023 2023 HOH HOH M . 
RB 5 HOH 24  2024 2024 HOH HOH M . 
RB 5 HOH 25  2025 2025 HOH HOH M . 
RB 5 HOH 26  2026 2026 HOH HOH M . 
RB 5 HOH 27  2027 2027 HOH HOH M . 
RB 5 HOH 28  2028 2028 HOH HOH M . 
RB 5 HOH 29  2029 2029 HOH HOH M . 
RB 5 HOH 30  2030 2030 HOH HOH M . 
RB 5 HOH 31  2031 2031 HOH HOH M . 
RB 5 HOH 32  2032 2032 HOH HOH M . 
RB 5 HOH 33  2033 2033 HOH HOH M . 
RB 5 HOH 34  2034 2034 HOH HOH M . 
RB 5 HOH 35  2035 2035 HOH HOH M . 
RB 5 HOH 36  2036 2036 HOH HOH M . 
RB 5 HOH 37  2037 2037 HOH HOH M . 
RB 5 HOH 38  2038 2038 HOH HOH M . 
RB 5 HOH 39  2039 2039 HOH HOH M . 
RB 5 HOH 40  2040 2040 HOH HOH M . 
RB 5 HOH 41  2041 2041 HOH HOH M . 
RB 5 HOH 42  2042 2042 HOH HOH M . 
RB 5 HOH 43  2043 2043 HOH HOH M . 
RB 5 HOH 44  2044 2044 HOH HOH M . 
RB 5 HOH 45  2045 2045 HOH HOH M . 
RB 5 HOH 46  2046 2046 HOH HOH M . 
RB 5 HOH 47  2047 2047 HOH HOH M . 
RB 5 HOH 48  2048 2048 HOH HOH M . 
RB 5 HOH 49  2049 2049 HOH HOH M . 
RB 5 HOH 50  2050 2050 HOH HOH M . 
RB 5 HOH 51  2051 2051 HOH HOH M . 
RB 5 HOH 52  2052 2052 HOH HOH M . 
RB 5 HOH 53  2053 2053 HOH HOH M . 
RB 5 HOH 54  2054 2054 HOH HOH M . 
RB 5 HOH 55  2055 2055 HOH HOH M . 
RB 5 HOH 56  2056 2056 HOH HOH M . 
RB 5 HOH 57  2057 2057 HOH HOH M . 
RB 5 HOH 58  2058 2058 HOH HOH M . 
RB 5 HOH 59  2059 2059 HOH HOH M . 
RB 5 HOH 60  2060 2060 HOH HOH M . 
RB 5 HOH 61  2061 2061 HOH HOH M . 
RB 5 HOH 62  2062 2062 HOH HOH M . 
RB 5 HOH 63  2063 2063 HOH HOH M . 
RB 5 HOH 64  2064 2064 HOH HOH M . 
RB 5 HOH 65  2065 2065 HOH HOH M . 
RB 5 HOH 66  2066 2066 HOH HOH M . 
RB 5 HOH 67  2067 2067 HOH HOH M . 
RB 5 HOH 68  2068 2068 HOH HOH M . 
RB 5 HOH 69  2069 2069 HOH HOH M . 
RB 5 HOH 70  2070 2070 HOH HOH M . 
RB 5 HOH 71  2071 2071 HOH HOH M . 
RB 5 HOH 72  2072 2072 HOH HOH M . 
RB 5 HOH 73  2073 2073 HOH HOH M . 
RB 5 HOH 74  2074 2074 HOH HOH M . 
RB 5 HOH 75  2075 2075 HOH HOH M . 
RB 5 HOH 76  2076 2076 HOH HOH M . 
RB 5 HOH 77  2077 2077 HOH HOH M . 
RB 5 HOH 78  2078 2078 HOH HOH M . 
RB 5 HOH 79  2079 2079 HOH HOH M . 
RB 5 HOH 80  2080 2080 HOH HOH M . 
RB 5 HOH 81  2081 2081 HOH HOH M . 
RB 5 HOH 82  2082 2082 HOH HOH M . 
RB 5 HOH 83  2083 2083 HOH HOH M . 
RB 5 HOH 84  2084 2084 HOH HOH M . 
RB 5 HOH 85  2085 2085 HOH HOH M . 
RB 5 HOH 86  2086 2086 HOH HOH M . 
RB 5 HOH 87  2087 2087 HOH HOH M . 
RB 5 HOH 88  2088 2088 HOH HOH M . 
RB 5 HOH 89  2089 2089 HOH HOH M . 
RB 5 HOH 90  2090 2090 HOH HOH M . 
RB 5 HOH 91  2091 2091 HOH HOH M . 
RB 5 HOH 92  2092 2092 HOH HOH M . 
RB 5 HOH 93  2093 2093 HOH HOH M . 
RB 5 HOH 94  2094 2094 HOH HOH M . 
RB 5 HOH 95  2095 2095 HOH HOH M . 
RB 5 HOH 96  2096 2096 HOH HOH M . 
RB 5 HOH 97  2097 2097 HOH HOH M . 
RB 5 HOH 98  2098 2098 HOH HOH M . 
RB 5 HOH 99  2099 2099 HOH HOH M . 
SB 5 HOH 1   2001 2001 HOH HOH N . 
SB 5 HOH 2   2002 2002 HOH HOH N . 
SB 5 HOH 3   2003 2003 HOH HOH N . 
SB 5 HOH 4   2004 2004 HOH HOH N . 
SB 5 HOH 5   2005 2005 HOH HOH N . 
SB 5 HOH 6   2006 2006 HOH HOH N . 
SB 5 HOH 7   2007 2007 HOH HOH N . 
SB 5 HOH 8   2008 2008 HOH HOH N . 
SB 5 HOH 9   2009 2009 HOH HOH N . 
SB 5 HOH 10  2010 2010 HOH HOH N . 
SB 5 HOH 11  2011 2011 HOH HOH N . 
SB 5 HOH 12  2012 2012 HOH HOH N . 
SB 5 HOH 13  2013 2013 HOH HOH N . 
SB 5 HOH 14  2014 2014 HOH HOH N . 
SB 5 HOH 15  2015 2015 HOH HOH N . 
SB 5 HOH 16  2016 2016 HOH HOH N . 
SB 5 HOH 17  2017 2017 HOH HOH N . 
SB 5 HOH 18  2018 2018 HOH HOH N . 
SB 5 HOH 19  2019 2019 HOH HOH N . 
SB 5 HOH 20  2020 2020 HOH HOH N . 
SB 5 HOH 21  2021 2021 HOH HOH N . 
SB 5 HOH 22  2022 2022 HOH HOH N . 
SB 5 HOH 23  2023 2023 HOH HOH N . 
SB 5 HOH 24  2024 2024 HOH HOH N . 
SB 5 HOH 25  2025 2025 HOH HOH N . 
SB 5 HOH 26  2026 2026 HOH HOH N . 
SB 5 HOH 27  2027 2027 HOH HOH N . 
SB 5 HOH 28  2028 2028 HOH HOH N . 
SB 5 HOH 29  2029 2029 HOH HOH N . 
SB 5 HOH 30  2030 2030 HOH HOH N . 
SB 5 HOH 31  2031 2031 HOH HOH N . 
SB 5 HOH 32  2032 2032 HOH HOH N . 
SB 5 HOH 33  2033 2033 HOH HOH N . 
SB 5 HOH 34  2034 2034 HOH HOH N . 
SB 5 HOH 35  2035 2035 HOH HOH N . 
SB 5 HOH 36  2036 2036 HOH HOH N . 
SB 5 HOH 37  2037 2037 HOH HOH N . 
SB 5 HOH 38  2038 2038 HOH HOH N . 
SB 5 HOH 39  2039 2039 HOH HOH N . 
SB 5 HOH 40  2040 2040 HOH HOH N . 
SB 5 HOH 41  2041 2041 HOH HOH N . 
SB 5 HOH 42  2042 2042 HOH HOH N . 
SB 5 HOH 43  2043 2043 HOH HOH N . 
SB 5 HOH 44  2044 2044 HOH HOH N . 
SB 5 HOH 45  2045 2045 HOH HOH N . 
SB 5 HOH 46  2046 2046 HOH HOH N . 
SB 5 HOH 47  2047 2047 HOH HOH N . 
SB 5 HOH 48  2048 2048 HOH HOH N . 
SB 5 HOH 49  2049 2049 HOH HOH N . 
SB 5 HOH 50  2050 2050 HOH HOH N . 
SB 5 HOH 51  2051 2051 HOH HOH N . 
SB 5 HOH 52  2052 2052 HOH HOH N . 
SB 5 HOH 53  2053 2053 HOH HOH N . 
SB 5 HOH 54  2054 2054 HOH HOH N . 
SB 5 HOH 55  2055 2055 HOH HOH N . 
SB 5 HOH 56  2056 2056 HOH HOH N . 
SB 5 HOH 57  2057 2057 HOH HOH N . 
SB 5 HOH 58  2058 2058 HOH HOH N . 
SB 5 HOH 59  2059 2059 HOH HOH N . 
SB 5 HOH 60  2060 2060 HOH HOH N . 
SB 5 HOH 61  2061 2061 HOH HOH N . 
SB 5 HOH 62  2062 2062 HOH HOH N . 
SB 5 HOH 63  2063 2063 HOH HOH N . 
SB 5 HOH 64  2064 2064 HOH HOH N . 
SB 5 HOH 65  2065 2065 HOH HOH N . 
SB 5 HOH 66  2066 2066 HOH HOH N . 
SB 5 HOH 67  2067 2067 HOH HOH N . 
SB 5 HOH 68  2068 2068 HOH HOH N . 
SB 5 HOH 69  2069 2069 HOH HOH N . 
SB 5 HOH 70  2070 2070 HOH HOH N . 
SB 5 HOH 71  2071 2071 HOH HOH N . 
SB 5 HOH 72  2072 2072 HOH HOH N . 
SB 5 HOH 73  2073 2073 HOH HOH N . 
SB 5 HOH 74  2074 2074 HOH HOH N . 
SB 5 HOH 75  2075 2075 HOH HOH N . 
SB 5 HOH 76  2076 2076 HOH HOH N . 
SB 5 HOH 77  2077 2077 HOH HOH N . 
SB 5 HOH 78  2078 2078 HOH HOH N . 
SB 5 HOH 79  2079 2079 HOH HOH N . 
SB 5 HOH 80  2080 2080 HOH HOH N . 
SB 5 HOH 81  2081 2081 HOH HOH N . 
SB 5 HOH 82  2082 2082 HOH HOH N . 
SB 5 HOH 83  2083 2083 HOH HOH N . 
SB 5 HOH 84  2084 2084 HOH HOH N . 
SB 5 HOH 85  2085 2085 HOH HOH N . 
SB 5 HOH 86  2086 2086 HOH HOH N . 
SB 5 HOH 87  2087 2087 HOH HOH N . 
SB 5 HOH 88  2088 2088 HOH HOH N . 
SB 5 HOH 89  2089 2089 HOH HOH N . 
SB 5 HOH 90  2090 2090 HOH HOH N . 
TB 5 HOH 1   2001 2001 HOH HOH O . 
TB 5 HOH 2   2002 2002 HOH HOH O . 
TB 5 HOH 3   2003 2003 HOH HOH O . 
TB 5 HOH 4   2004 2004 HOH HOH O . 
TB 5 HOH 5   2005 2005 HOH HOH O . 
TB 5 HOH 6   2006 2006 HOH HOH O . 
TB 5 HOH 7   2007 2007 HOH HOH O . 
TB 5 HOH 8   2008 2008 HOH HOH O . 
TB 5 HOH 9   2009 2009 HOH HOH O . 
TB 5 HOH 10  2010 2010 HOH HOH O . 
TB 5 HOH 11  2011 2011 HOH HOH O . 
TB 5 HOH 12  2012 2012 HOH HOH O . 
TB 5 HOH 13  2013 2013 HOH HOH O . 
TB 5 HOH 14  2014 2014 HOH HOH O . 
TB 5 HOH 15  2015 2015 HOH HOH O . 
TB 5 HOH 16  2016 2016 HOH HOH O . 
TB 5 HOH 17  2017 2017 HOH HOH O . 
TB 5 HOH 18  2018 2018 HOH HOH O . 
TB 5 HOH 19  2019 2019 HOH HOH O . 
TB 5 HOH 20  2020 2020 HOH HOH O . 
TB 5 HOH 21  2021 2021 HOH HOH O . 
TB 5 HOH 22  2022 2022 HOH HOH O . 
TB 5 HOH 23  2023 2023 HOH HOH O . 
TB 5 HOH 24  2024 2024 HOH HOH O . 
TB 5 HOH 25  2025 2025 HOH HOH O . 
TB 5 HOH 26  2026 2026 HOH HOH O . 
TB 5 HOH 27  2027 2027 HOH HOH O . 
TB 5 HOH 28  2028 2028 HOH HOH O . 
TB 5 HOH 29  2029 2029 HOH HOH O . 
TB 5 HOH 30  2030 2030 HOH HOH O . 
TB 5 HOH 31  2031 2031 HOH HOH O . 
TB 5 HOH 32  2032 2032 HOH HOH O . 
TB 5 HOH 33  2033 2033 HOH HOH O . 
TB 5 HOH 34  2034 2034 HOH HOH O . 
TB 5 HOH 35  2035 2035 HOH HOH O . 
TB 5 HOH 36  2036 2036 HOH HOH O . 
TB 5 HOH 37  2037 2037 HOH HOH O . 
TB 5 HOH 38  2038 2038 HOH HOH O . 
TB 5 HOH 39  2039 2039 HOH HOH O . 
TB 5 HOH 40  2040 2040 HOH HOH O . 
TB 5 HOH 41  2041 2041 HOH HOH O . 
TB 5 HOH 42  2042 2042 HOH HOH O . 
TB 5 HOH 43  2043 2043 HOH HOH O . 
TB 5 HOH 44  2044 2044 HOH HOH O . 
TB 5 HOH 45  2045 2045 HOH HOH O . 
TB 5 HOH 46  2046 2046 HOH HOH O . 
TB 5 HOH 47  2047 2047 HOH HOH O . 
TB 5 HOH 48  2048 2048 HOH HOH O . 
TB 5 HOH 49  2049 2049 HOH HOH O . 
TB 5 HOH 50  2050 2050 HOH HOH O . 
UB 5 HOH 1   2001 2001 HOH HOH P . 
UB 5 HOH 2   2002 2002 HOH HOH P . 
VB 5 HOH 1   2001 2001 HOH HOH Q . 
VB 5 HOH 2   2002 2002 HOH HOH Q . 
VB 5 HOH 3   2003 2003 HOH HOH Q . 
VB 5 HOH 4   2004 2004 HOH HOH Q . 
VB 5 HOH 5   2005 2005 HOH HOH Q . 
VB 5 HOH 6   2006 2006 HOH HOH Q . 
VB 5 HOH 7   2007 2007 HOH HOH Q . 
VB 5 HOH 8   2008 2008 HOH HOH Q . 
VB 5 HOH 9   2009 2009 HOH HOH Q . 
VB 5 HOH 10  2010 2010 HOH HOH Q . 
VB 5 HOH 11  2011 2011 HOH HOH Q . 
VB 5 HOH 12  2012 2012 HOH HOH Q . 
VB 5 HOH 13  2013 2013 HOH HOH Q . 
VB 5 HOH 14  2014 2014 HOH HOH Q . 
VB 5 HOH 15  2015 2015 HOH HOH Q . 
VB 5 HOH 16  2016 2016 HOH HOH Q . 
VB 5 HOH 17  2017 2017 HOH HOH Q . 
VB 5 HOH 18  2018 2018 HOH HOH Q . 
VB 5 HOH 19  2019 2019 HOH HOH Q . 
VB 5 HOH 20  2020 2020 HOH HOH Q . 
VB 5 HOH 21  2021 2021 HOH HOH Q . 
VB 5 HOH 22  2022 2022 HOH HOH Q . 
VB 5 HOH 23  2023 2023 HOH HOH Q . 
VB 5 HOH 24  2024 2024 HOH HOH Q . 
VB 5 HOH 25  2025 2025 HOH HOH Q . 
VB 5 HOH 26  2026 2026 HOH HOH Q . 
VB 5 HOH 27  2027 2027 HOH HOH Q . 
VB 5 HOH 28  2028 2028 HOH HOH Q . 
VB 5 HOH 29  2029 2029 HOH HOH Q . 
VB 5 HOH 30  2030 2030 HOH HOH Q . 
VB 5 HOH 31  2031 2031 HOH HOH Q . 
VB 5 HOH 32  2032 2032 HOH HOH Q . 
VB 5 HOH 33  2033 2033 HOH HOH Q . 
VB 5 HOH 34  2034 2034 HOH HOH Q . 
VB 5 HOH 35  2035 2035 HOH HOH Q . 
VB 5 HOH 36  2036 2036 HOH HOH Q . 
VB 5 HOH 37  2037 2037 HOH HOH Q . 
VB 5 HOH 38  2038 2038 HOH HOH Q . 
VB 5 HOH 39  2039 2039 HOH HOH Q . 
VB 5 HOH 40  2040 2040 HOH HOH Q . 
VB 5 HOH 41  2041 2041 HOH HOH Q . 
VB 5 HOH 42  2042 2042 HOH HOH Q . 
VB 5 HOH 43  2043 2043 HOH HOH Q . 
VB 5 HOH 44  2044 2044 HOH HOH Q . 
VB 5 HOH 45  2045 2045 HOH HOH Q . 
VB 5 HOH 46  2046 2046 HOH HOH Q . 
VB 5 HOH 47  2047 2047 HOH HOH Q . 
VB 5 HOH 48  2048 2048 HOH HOH Q . 
VB 5 HOH 49  2049 2049 HOH HOH Q . 
VB 5 HOH 50  2050 2050 HOH HOH Q . 
VB 5 HOH 51  2051 2051 HOH HOH Q . 
VB 5 HOH 52  2052 2052 HOH HOH Q . 
VB 5 HOH 53  2053 2053 HOH HOH Q . 
VB 5 HOH 54  2054 2054 HOH HOH Q . 
VB 5 HOH 55  2055 2055 HOH HOH Q . 
VB 5 HOH 56  2056 2056 HOH HOH Q . 
VB 5 HOH 57  2057 2057 HOH HOH Q . 
VB 5 HOH 58  2058 2058 HOH HOH Q . 
VB 5 HOH 59  2059 2059 HOH HOH Q . 
VB 5 HOH 60  2060 2060 HOH HOH Q . 
VB 5 HOH 61  2061 2061 HOH HOH Q . 
VB 5 HOH 62  2062 2062 HOH HOH Q . 
VB 5 HOH 63  2063 2063 HOH HOH Q . 
VB 5 HOH 64  2064 2064 HOH HOH Q . 
VB 5 HOH 65  2065 2065 HOH HOH Q . 
VB 5 HOH 66  2066 2066 HOH HOH Q . 
VB 5 HOH 67  2067 2067 HOH HOH Q . 
VB 5 HOH 68  2068 2068 HOH HOH Q . 
VB 5 HOH 69  2069 2069 HOH HOH Q . 
VB 5 HOH 70  2070 2070 HOH HOH Q . 
VB 5 HOH 71  2071 2071 HOH HOH Q . 
VB 5 HOH 72  2072 2072 HOH HOH Q . 
VB 5 HOH 73  2073 2073 HOH HOH Q . 
VB 5 HOH 74  2074 2074 HOH HOH Q . 
VB 5 HOH 75  2075 2075 HOH HOH Q . 
VB 5 HOH 76  2076 2076 HOH HOH Q . 
VB 5 HOH 77  2077 2077 HOH HOH Q . 
VB 5 HOH 78  2078 2078 HOH HOH Q . 
VB 5 HOH 79  2079 2079 HOH HOH Q . 
VB 5 HOH 80  2080 2080 HOH HOH Q . 
VB 5 HOH 81  2081 2081 HOH HOH Q . 
VB 5 HOH 82  2082 2082 HOH HOH Q . 
VB 5 HOH 83  2083 2083 HOH HOH Q . 
WB 5 HOH 1   2001 2001 HOH HOH S . 
WB 5 HOH 2   2002 2002 HOH HOH S . 
WB 5 HOH 3   2003 2003 HOH HOH S . 
WB 5 HOH 4   2004 2004 HOH HOH S . 
WB 5 HOH 5   2005 2005 HOH HOH S . 
WB 5 HOH 6   2006 2006 HOH HOH S . 
WB 5 HOH 7   2007 2007 HOH HOH S . 
WB 5 HOH 8   2008 2008 HOH HOH S . 
WB 5 HOH 9   2009 2009 HOH HOH S . 
WB 5 HOH 10  2010 2010 HOH HOH S . 
WB 5 HOH 11  2011 2011 HOH HOH S . 
WB 5 HOH 12  2012 2012 HOH HOH S . 
WB 5 HOH 13  2013 2013 HOH HOH S . 
WB 5 HOH 14  2014 2014 HOH HOH S . 
WB 5 HOH 15  2015 2015 HOH HOH S . 
WB 5 HOH 16  2016 2016 HOH HOH S . 
WB 5 HOH 17  2017 2017 HOH HOH S . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PQS dimeric 2 
2 author_and_software_defined_assembly PQS dimeric 2 
3 author_and_software_defined_assembly PQS dimeric 2 
4 author_and_software_defined_assembly PQS dimeric 2 
5 author_and_software_defined_assembly PQS dimeric 2 
6 author_and_software_defined_assembly PQS dimeric 2 
7 author_and_software_defined_assembly PQS dimeric 2 
8 author_and_software_defined_assembly PQS dimeric 2 
9 author_and_software_defined_assembly PQS dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,H,S,T,IA,JA,FB,MB      
2 1 B,I,U,V,KA,LA,GB,NB      
3 1 C,J,W,X,Y,MA,NA,HB,OB    
4 1 D,K,Z,AA,BA,OA,PA,IB,PB  
5 1 E,L,CA,DA,QA,RA,JB,QB    
6 1 F,M,EA,FA,SA,TA,KB,RB    
7 1 G,N,GA,HA,UA,VA,LB,SB    
8 1 O,Q,WA,XA,YA,BB,CB,TB,VB 
9 1 P,R,ZA,AB,DB,EB,UB,WB    
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1   NE2 ? A  HIS 120 ? A HIS 120  ? 1_555 CU ? S  CU . ? A CU 154 ? 1_555 ND1 ? A  HIS 46  ? A HIS 46   ? 1_555 95.8  ? 
2   NE2 ? A  HIS 120 ? A HIS 120  ? 1_555 CU ? S  CU . ? A CU 154 ? 1_555 NE2 ? A  HIS 48  ? A HIS 48   ? 1_555 111.6 ? 
3   ND1 ? A  HIS 46  ? A HIS 46   ? 1_555 CU ? S  CU . ? A CU 154 ? 1_555 NE2 ? A  HIS 48  ? A HIS 48   ? 1_555 132.5 ? 
4   NE2 ? A  HIS 120 ? A HIS 120  ? 1_555 CU ? S  CU . ? A CU 154 ? 1_555 NE2 ? A  HIS 63  ? A HIS 63   ? 1_555 141.3 ? 
5   ND1 ? A  HIS 46  ? A HIS 46   ? 1_555 CU ? S  CU . ? A CU 154 ? 1_555 NE2 ? A  HIS 63  ? A HIS 63   ? 1_555 78.0  ? 
6   NE2 ? A  HIS 48  ? A HIS 48   ? 1_555 CU ? S  CU . ? A CU 154 ? 1_555 NE2 ? A  HIS 63  ? A HIS 63   ? 1_555 99.7  ? 
7   NE2 ? A  HIS 120 ? A HIS 120  ? 1_555 CU ? S  CU . ? A CU 154 ? 1_555 O   ? FB HOH .   ? A HOH 2047 ? 1_555 83.1  ? 
8   ND1 ? A  HIS 46  ? A HIS 46   ? 1_555 CU ? S  CU . ? A CU 154 ? 1_555 O   ? FB HOH .   ? A HOH 2047 ? 1_555 124.2 ? 
9   NE2 ? A  HIS 48  ? A HIS 48   ? 1_555 CU ? S  CU . ? A CU 154 ? 1_555 O   ? FB HOH .   ? A HOH 2047 ? 1_555 97.8  ? 
10  NE2 ? A  HIS 63  ? A HIS 63   ? 1_555 CU ? S  CU . ? A CU 154 ? 1_555 O   ? FB HOH .   ? A HOH 2047 ? 1_555 70.2  ? 
11  ND1 ? A  HIS 63  ? A HIS 63   ? 1_555 ZN ? T  ZN . ? A ZN 155 ? 1_555 OD1 ? A  ASP 83  ? A ASP 83   ? 1_555 104.7 ? 
12  ND1 ? A  HIS 63  ? A HIS 63   ? 1_555 ZN ? T  ZN . ? A ZN 155 ? 1_555 ND1 ? A  HIS 71  ? A HIS 71   ? 1_555 106.6 ? 
13  OD1 ? A  ASP 83  ? A ASP 83   ? 1_555 ZN ? T  ZN . ? A ZN 155 ? 1_555 ND1 ? A  HIS 71  ? A HIS 71   ? 1_555 95.7  ? 
14  ND1 ? A  HIS 63  ? A HIS 63   ? 1_555 ZN ? T  ZN . ? A ZN 155 ? 1_555 ND1 ? A  HIS 80  ? A HIS 80   ? 1_555 112.5 ? 
15  OD1 ? A  ASP 83  ? A ASP 83   ? 1_555 ZN ? T  ZN . ? A ZN 155 ? 1_555 ND1 ? A  HIS 80  ? A HIS 80   ? 1_555 114.1 ? 
16  ND1 ? A  HIS 71  ? A HIS 71   ? 1_555 ZN ? T  ZN . ? A ZN 155 ? 1_555 ND1 ? A  HIS 80  ? A HIS 80   ? 1_555 121.0 ? 
17  NE2 ? B  HIS 120 ? B HIS 120  ? 1_555 CU ? U  CU . ? B CU 154 ? 1_555 ND1 ? B  HIS 46  ? B HIS 46   ? 1_555 93.8  ? 
18  NE2 ? B  HIS 120 ? B HIS 120  ? 1_555 CU ? U  CU . ? B CU 154 ? 1_555 NE2 ? B  HIS 63  ? B HIS 63   ? 1_555 141.8 ? 
19  ND1 ? B  HIS 46  ? B HIS 46   ? 1_555 CU ? U  CU . ? B CU 154 ? 1_555 NE2 ? B  HIS 63  ? B HIS 63   ? 1_555 76.3  ? 
20  NE2 ? B  HIS 120 ? B HIS 120  ? 1_555 CU ? U  CU . ? B CU 154 ? 1_555 O   ? GB HOH .   ? B HOH 2083 ? 1_555 87.8  ? 
21  ND1 ? B  HIS 46  ? B HIS 46   ? 1_555 CU ? U  CU . ? B CU 154 ? 1_555 O   ? GB HOH .   ? B HOH 2083 ? 1_555 117.6 ? 
22  NE2 ? B  HIS 63  ? B HIS 63   ? 1_555 CU ? U  CU . ? B CU 154 ? 1_555 O   ? GB HOH .   ? B HOH 2083 ? 1_555 65.9  ? 
23  NE2 ? B  HIS 120 ? B HIS 120  ? 1_555 CU ? U  CU . ? B CU 154 ? 1_555 NE2 ? B  HIS 48  ? B HIS 48   ? 1_555 113.4 ? 
24  ND1 ? B  HIS 46  ? B HIS 46   ? 1_555 CU ? U  CU . ? B CU 154 ? 1_555 NE2 ? B  HIS 48  ? B HIS 48   ? 1_555 131.2 ? 
25  NE2 ? B  HIS 63  ? B HIS 63   ? 1_555 CU ? U  CU . ? B CU 154 ? 1_555 NE2 ? B  HIS 48  ? B HIS 48   ? 1_555 100.0 ? 
26  O   ? GB HOH .   ? B HOH 2083 ? 1_555 CU ? U  CU . ? B CU 154 ? 1_555 NE2 ? B  HIS 48  ? B HIS 48   ? 1_555 103.8 ? 
27  ND1 ? B  HIS 71  ? B HIS 71   ? 1_555 ZN ? V  ZN . ? B ZN 155 ? 1_555 ND1 ? B  HIS 80  ? B HIS 80   ? 1_555 120.6 ? 
28  ND1 ? B  HIS 71  ? B HIS 71   ? 1_555 ZN ? V  ZN . ? B ZN 155 ? 1_555 OD1 ? B  ASP 83  ? B ASP 83   ? 1_555 96.0  ? 
29  ND1 ? B  HIS 80  ? B HIS 80   ? 1_555 ZN ? V  ZN . ? B ZN 155 ? 1_555 OD1 ? B  ASP 83  ? B ASP 83   ? 1_555 114.4 ? 
30  ND1 ? B  HIS 71  ? B HIS 71   ? 1_555 ZN ? V  ZN . ? B ZN 155 ? 1_555 ND1 ? B  HIS 63  ? B HIS 63   ? 1_555 106.5 ? 
31  ND1 ? B  HIS 80  ? B HIS 80   ? 1_555 ZN ? V  ZN . ? B ZN 155 ? 1_555 ND1 ? B  HIS 63  ? B HIS 63   ? 1_555 111.8 ? 
32  OD1 ? B  ASP 83  ? B ASP 83   ? 1_555 ZN ? V  ZN . ? B ZN 155 ? 1_555 ND1 ? B  HIS 63  ? B HIS 63   ? 1_555 105.7 ? 
33  ND1 ? C  HIS 46  ? C HIS 46   ? 1_555 CU ? W  CU . ? C CU 154 ? 1_555 NE2 ? C  HIS 48  ? C HIS 48   ? 1_555 133.8 ? 
34  ND1 ? C  HIS 46  ? C HIS 46   ? 1_555 CU ? W  CU . ? C CU 154 ? 1_555 NE2 ? C  HIS 120 ? C HIS 120  ? 1_555 96.9  ? 
35  NE2 ? C  HIS 48  ? C HIS 48   ? 1_555 CU ? W  CU . ? C CU 154 ? 1_555 NE2 ? C  HIS 120 ? C HIS 120  ? 1_555 112.4 ? 
36  ND1 ? C  HIS 46  ? C HIS 46   ? 1_555 CU ? W  CU . ? C CU 154 ? 1_555 O   ? HB HOH .   ? C HOH 2074 ? 1_555 118.2 ? 
37  NE2 ? C  HIS 48  ? C HIS 48   ? 1_555 CU ? W  CU . ? C CU 154 ? 1_555 O   ? HB HOH .   ? C HOH 2074 ? 1_555 99.2  ? 
38  NE2 ? C  HIS 120 ? C HIS 120  ? 1_555 CU ? W  CU . ? C CU 154 ? 1_555 O   ? HB HOH .   ? C HOH 2074 ? 1_555 86.5  ? 
39  ND1 ? C  HIS 46  ? C HIS 46   ? 1_555 CU ? W  CU . ? C CU 154 ? 1_555 NE2 ? C  HIS 63  ? C HIS 63   ? 1_555 78.0  ? 
40  NE2 ? C  HIS 48  ? C HIS 48   ? 1_555 CU ? W  CU . ? C CU 154 ? 1_555 NE2 ? C  HIS 63  ? C HIS 63   ? 1_555 97.2  ? 
41  NE2 ? C  HIS 120 ? C HIS 120  ? 1_555 CU ? W  CU . ? C CU 154 ? 1_555 NE2 ? C  HIS 63  ? C HIS 63   ? 1_555 141.3 ? 
42  O   ? HB HOH .   ? C HOH 2074 ? 1_555 CU ? W  CU . ? C CU 154 ? 1_555 NE2 ? C  HIS 63  ? C HIS 63   ? 1_555 64.0  ? 
43  ND1 ? C  HIS 71  ? C HIS 71   ? 1_555 ZN ? X  ZN . ? C ZN 155 ? 1_555 ND1 ? C  HIS 63  ? C HIS 63   ? 1_555 107.7 ? 
44  ND1 ? C  HIS 71  ? C HIS 71   ? 1_555 ZN ? X  ZN . ? C ZN 155 ? 1_555 OD1 ? C  ASP 83  ? C ASP 83   ? 1_555 95.7  ? 
45  ND1 ? C  HIS 63  ? C HIS 63   ? 1_555 ZN ? X  ZN . ? C ZN 155 ? 1_555 OD1 ? C  ASP 83  ? C ASP 83   ? 1_555 104.5 ? 
46  ND1 ? C  HIS 71  ? C HIS 71   ? 1_555 ZN ? X  ZN . ? C ZN 155 ? 1_555 ND1 ? C  HIS 80  ? C HIS 80   ? 1_555 120.6 ? 
47  ND1 ? C  HIS 63  ? C HIS 63   ? 1_555 ZN ? X  ZN . ? C ZN 155 ? 1_555 ND1 ? C  HIS 80  ? C HIS 80   ? 1_555 111.5 ? 
48  OD1 ? C  ASP 83  ? C ASP 83   ? 1_555 ZN ? X  ZN . ? C ZN 155 ? 1_555 ND1 ? C  HIS 80  ? C HIS 80   ? 1_555 114.8 ? 
49  O   ? HB HOH .   ? C HOH 2037 ? 1_555 CA ? Y  CA . ? C CA 156 ? 1_555 O   ? HB HOH .   ? C HOH 2106 ? 1_555 70.8  ? 
50  O   ? HB HOH .   ? C HOH 2037 ? 1_555 CA ? Y  CA . ? C CA 156 ? 1_555 O   ? HB HOH .   ? C HOH 2038 ? 1_555 86.0  ? 
51  O   ? HB HOH .   ? C HOH 2106 ? 1_555 CA ? Y  CA . ? C CA 156 ? 1_555 O   ? HB HOH .   ? C HOH 2038 ? 1_555 144.6 ? 
52  O   ? HB HOH .   ? C HOH 2037 ? 1_555 CA ? Y  CA . ? C CA 156 ? 1_555 O   ? HB HOH .   ? C HOH 2035 ? 1_555 159.4 ? 
53  O   ? HB HOH .   ? C HOH 2106 ? 1_555 CA ? Y  CA . ? C CA 156 ? 1_555 O   ? HB HOH .   ? C HOH 2035 ? 1_555 107.5 ? 
54  O   ? HB HOH .   ? C HOH 2038 ? 1_555 CA ? Y  CA . ? C CA 156 ? 1_555 O   ? HB HOH .   ? C HOH 2035 ? 1_555 84.9  ? 
55  O   ? HB HOH .   ? C HOH 2037 ? 1_555 CA ? Y  CA . ? C CA 156 ? 1_555 O   ? C  SER 102 ? C SER 102  ? 1_555 87.9  ? 
56  O   ? HB HOH .   ? C HOH 2106 ? 1_555 CA ? Y  CA . ? C CA 156 ? 1_555 O   ? C  SER 102 ? C SER 102  ? 1_555 69.7  ? 
57  O   ? HB HOH .   ? C HOH 2038 ? 1_555 CA ? Y  CA . ? C CA 156 ? 1_555 O   ? C  SER 102 ? C SER 102  ? 1_555 83.5  ? 
58  O   ? HB HOH .   ? C HOH 2035 ? 1_555 CA ? Y  CA . ? C CA 156 ? 1_555 O   ? C  SER 102 ? C SER 102  ? 1_555 72.7  ? 
59  O   ? HB HOH .   ? C HOH 2037 ? 1_555 CA ? Y  CA . ? C CA 156 ? 1_555 O   ? C  ASN 26  ? C ASN 26   ? 1_555 131.6 ? 
60  O   ? HB HOH .   ? C HOH 2106 ? 1_555 CA ? Y  CA . ? C CA 156 ? 1_555 O   ? C  ASN 26  ? C ASN 26   ? 1_555 139.6 ? 
61  O   ? HB HOH .   ? C HOH 2038 ? 1_555 CA ? Y  CA . ? C CA 156 ? 1_555 O   ? C  ASN 26  ? C ASN 26   ? 1_555 75.7  ? 
62  O   ? HB HOH .   ? C HOH 2035 ? 1_555 CA ? Y  CA . ? C CA 156 ? 1_555 O   ? C  ASN 26  ? C ASN 26   ? 1_555 63.4  ? 
63  O   ? C  SER 102 ? C SER 102  ? 1_555 CA ? Y  CA . ? C CA 156 ? 1_555 O   ? C  ASN 26  ? C ASN 26   ? 1_555 132.5 ? 
64  O   ? HB HOH .   ? C HOH 2037 ? 1_555 CA ? Y  CA . ? C CA 156 ? 1_555 OD1 ? C  ASN 26  ? C ASN 26   ? 1_555 83.4  ? 
65  O   ? HB HOH .   ? C HOH 2106 ? 1_555 CA ? Y  CA . ? C CA 156 ? 1_555 OD1 ? C  ASN 26  ? C ASN 26   ? 1_555 91.0  ? 
66  O   ? HB HOH .   ? C HOH 2038 ? 1_555 CA ? Y  CA . ? C CA 156 ? 1_555 OD1 ? C  ASN 26  ? C ASN 26   ? 1_555 113.1 ? 
67  O   ? HB HOH .   ? C HOH 2035 ? 1_555 CA ? Y  CA . ? C CA 156 ? 1_555 OD1 ? C  ASN 26  ? C ASN 26   ? 1_555 117.2 ? 
68  O   ? C  SER 102 ? C SER 102  ? 1_555 CA ? Y  CA . ? C CA 156 ? 1_555 OD1 ? C  ASN 26  ? C ASN 26   ? 1_555 160.6 ? 
69  O   ? C  ASN 26  ? C ASN 26   ? 1_555 CA ? Y  CA . ? C CA 156 ? 1_555 OD1 ? C  ASN 26  ? C ASN 26   ? 1_555 64.4  ? 
70  NE2 ? D  HIS 48  ? D HIS 48   ? 1_555 CU ? Z  CU . ? D CU 154 ? 1_555 NE2 ? D  HIS 120 ? D HIS 120  ? 1_555 111.4 ? 
71  NE2 ? D  HIS 48  ? D HIS 48   ? 1_555 CU ? Z  CU . ? D CU 154 ? 1_555 NE2 ? D  HIS 63  ? D HIS 63   ? 1_555 96.4  ? 
72  NE2 ? D  HIS 120 ? D HIS 120  ? 1_555 CU ? Z  CU . ? D CU 154 ? 1_555 NE2 ? D  HIS 63  ? D HIS 63   ? 1_555 138.9 ? 
73  NE2 ? D  HIS 48  ? D HIS 48   ? 1_555 CU ? Z  CU . ? D CU 154 ? 1_555 O   ? IB HOH .   ? D HOH 2049 ? 1_555 95.6  ? 
74  NE2 ? D  HIS 120 ? D HIS 120  ? 1_555 CU ? Z  CU . ? D CU 154 ? 1_555 O   ? IB HOH .   ? D HOH 2049 ? 1_555 82.9  ? 
75  NE2 ? D  HIS 63  ? D HIS 63   ? 1_555 CU ? Z  CU . ? D CU 154 ? 1_555 O   ? IB HOH .   ? D HOH 2049 ? 1_555 64.1  ? 
76  NE2 ? D  HIS 48  ? D HIS 48   ? 1_555 CU ? Z  CU . ? D CU 154 ? 1_555 ND1 ? D  HIS 46  ? D HIS 46   ? 1_555 134.3 ? 
77  NE2 ? D  HIS 120 ? D HIS 120  ? 1_555 CU ? Z  CU . ? D CU 154 ? 1_555 ND1 ? D  HIS 46  ? D HIS 46   ? 1_555 101.3 ? 
78  NE2 ? D  HIS 63  ? D HIS 63   ? 1_555 CU ? Z  CU . ? D CU 154 ? 1_555 ND1 ? D  HIS 46  ? D HIS 46   ? 1_555 77.2  ? 
79  O   ? IB HOH .   ? D HOH 2049 ? 1_555 CU ? Z  CU . ? D CU 154 ? 1_555 ND1 ? D  HIS 46  ? D HIS 46   ? 1_555 120.0 ? 
80  ND1 ? D  HIS 71  ? D HIS 71   ? 1_555 ZN ? AA ZN . ? D ZN 155 ? 1_555 ND1 ? D  HIS 80  ? D HIS 80   ? 1_555 123.1 ? 
81  ND1 ? D  HIS 71  ? D HIS 71   ? 1_555 ZN ? AA ZN . ? D ZN 155 ? 1_555 ND1 ? D  HIS 63  ? D HIS 63   ? 1_555 103.4 ? 
82  ND1 ? D  HIS 80  ? D HIS 80   ? 1_555 ZN ? AA ZN . ? D ZN 155 ? 1_555 ND1 ? D  HIS 63  ? D HIS 63   ? 1_555 111.7 ? 
83  ND1 ? D  HIS 71  ? D HIS 71   ? 1_555 ZN ? AA ZN . ? D ZN 155 ? 1_555 OD1 ? D  ASP 83  ? D ASP 83   ? 1_555 96.1  ? 
84  ND1 ? D  HIS 80  ? D HIS 80   ? 1_555 ZN ? AA ZN . ? D ZN 155 ? 1_555 OD1 ? D  ASP 83  ? D ASP 83   ? 1_555 115.3 ? 
85  ND1 ? D  HIS 63  ? D HIS 63   ? 1_555 ZN ? AA ZN . ? D ZN 155 ? 1_555 OD1 ? D  ASP 83  ? D ASP 83   ? 1_555 104.9 ? 
86  O   ? D  SER 102 ? D SER 102  ? 1_555 CA ? BA CA . ? D CA 156 ? 1_555 O   ? IB HOH .   ? D HOH 2072 ? 1_555 87.4  ? 
87  O   ? D  SER 102 ? D SER 102  ? 1_555 CA ? BA CA . ? D CA 156 ? 1_555 O   ? D  ASN 26  ? D ASN 26   ? 1_555 123.1 ? 
88  O   ? IB HOH .   ? D HOH 2072 ? 1_555 CA ? BA CA . ? D CA 156 ? 1_555 O   ? D  ASN 26  ? D ASN 26   ? 1_555 138.0 ? 
89  O   ? D  SER 102 ? D SER 102  ? 1_555 CA ? BA CA . ? D CA 156 ? 1_555 OD1 ? D  ASN 26  ? D ASN 26   ? 1_555 163.2 ? 
90  O   ? IB HOH .   ? D HOH 2072 ? 1_555 CA ? BA CA . ? D CA 156 ? 1_555 OD1 ? D  ASN 26  ? D ASN 26   ? 1_555 79.2  ? 
91  O   ? D  ASN 26  ? D ASN 26   ? 1_555 CA ? BA CA . ? D CA 156 ? 1_555 OD1 ? D  ASN 26  ? D ASN 26   ? 1_555 73.6  ? 
92  O   ? D  SER 102 ? D SER 102  ? 1_555 CA ? BA CA . ? D CA 156 ? 1_555 O   ? IB HOH .   ? D HOH 2024 ? 1_555 80.6  ? 
93  O   ? IB HOH .   ? D HOH 2072 ? 1_555 CA ? BA CA . ? D CA 156 ? 1_555 O   ? IB HOH .   ? D HOH 2024 ? 1_555 81.8  ? 
94  O   ? D  ASN 26  ? D ASN 26   ? 1_555 CA ? BA CA . ? D CA 156 ? 1_555 O   ? IB HOH .   ? D HOH 2024 ? 1_555 76.6  ? 
95  OD1 ? D  ASN 26  ? D ASN 26   ? 1_555 CA ? BA CA . ? D CA 156 ? 1_555 O   ? IB HOH .   ? D HOH 2024 ? 1_555 107.3 ? 
96  O   ? D  SER 102 ? D SER 102  ? 1_555 CA ? BA CA . ? D CA 156 ? 1_555 O   ? FB HOH .   ? A HOH 2063 ? 1_455 77.6  ? 
97  O   ? IB HOH .   ? D HOH 2072 ? 1_555 CA ? BA CA . ? D CA 156 ? 1_555 O   ? FB HOH .   ? A HOH 2063 ? 1_455 82.1  ? 
98  O   ? D  ASN 26  ? D ASN 26   ? 1_555 CA ? BA CA . ? D CA 156 ? 1_555 O   ? FB HOH .   ? A HOH 2063 ? 1_455 128.6 ? 
99  OD1 ? D  ASN 26  ? D ASN 26   ? 1_555 CA ? BA CA . ? D CA 156 ? 1_555 O   ? FB HOH .   ? A HOH 2063 ? 1_455 90.3  ? 
100 O   ? IB HOH .   ? D HOH 2024 ? 1_555 CA ? BA CA . ? D CA 156 ? 1_555 O   ? FB HOH .   ? A HOH 2063 ? 1_455 153.4 ? 
101 O   ? JB HOH .   ? E HOH 2052 ? 1_555 CU ? CA CU . ? E CU 154 ? 1_555 ND1 ? E  HIS 46  ? E HIS 46   ? 1_555 120.3 ? 
102 O   ? JB HOH .   ? E HOH 2052 ? 1_555 CU ? CA CU . ? E CU 154 ? 1_555 NE2 ? E  HIS 120 ? E HIS 120  ? 1_555 85.9  ? 
103 ND1 ? E  HIS 46  ? E HIS 46   ? 1_555 CU ? CA CU . ? E CU 154 ? 1_555 NE2 ? E  HIS 120 ? E HIS 120  ? 1_555 94.0  ? 
104 O   ? JB HOH .   ? E HOH 2052 ? 1_555 CU ? CA CU . ? E CU 154 ? 1_555 NE2 ? E  HIS 63  ? E HIS 63   ? 1_555 66.6  ? 
105 ND1 ? E  HIS 46  ? E HIS 46   ? 1_555 CU ? CA CU . ? E CU 154 ? 1_555 NE2 ? E  HIS 63  ? E HIS 63   ? 1_555 79.6  ? 
106 NE2 ? E  HIS 120 ? E HIS 120  ? 1_555 CU ? CA CU . ? E CU 154 ? 1_555 NE2 ? E  HIS 63  ? E HIS 63   ? 1_555 142.4 ? 
107 O   ? JB HOH .   ? E HOH 2052 ? 1_555 CU ? CA CU . ? E CU 154 ? 1_555 NE2 ? E  HIS 48  ? E HIS 48   ? 1_555 98.5  ? 
108 ND1 ? E  HIS 46  ? E HIS 46   ? 1_555 CU ? CA CU . ? E CU 154 ? 1_555 NE2 ? E  HIS 48  ? E HIS 48   ? 1_555 134.0 ? 
109 NE2 ? E  HIS 120 ? E HIS 120  ? 1_555 CU ? CA CU . ? E CU 154 ? 1_555 NE2 ? E  HIS 48  ? E HIS 48   ? 1_555 113.7 ? 
110 NE2 ? E  HIS 63  ? E HIS 63   ? 1_555 CU ? CA CU . ? E CU 154 ? 1_555 NE2 ? E  HIS 48  ? E HIS 48   ? 1_555 96.1  ? 
111 ND1 ? E  HIS 71  ? E HIS 71   ? 1_555 ZN ? DA ZN . ? E ZN 155 ? 1_555 ND1 ? E  HIS 80  ? E HIS 80   ? 1_555 120.4 ? 
112 ND1 ? E  HIS 71  ? E HIS 71   ? 1_555 ZN ? DA ZN . ? E ZN 155 ? 1_555 OD1 ? E  ASP 83  ? E ASP 83   ? 1_555 98.0  ? 
113 ND1 ? E  HIS 80  ? E HIS 80   ? 1_555 ZN ? DA ZN . ? E ZN 155 ? 1_555 OD1 ? E  ASP 83  ? E ASP 83   ? 1_555 114.3 ? 
114 ND1 ? E  HIS 71  ? E HIS 71   ? 1_555 ZN ? DA ZN . ? E ZN 155 ? 1_555 ND1 ? E  HIS 63  ? E HIS 63   ? 1_555 106.0 ? 
115 ND1 ? E  HIS 80  ? E HIS 80   ? 1_555 ZN ? DA ZN . ? E ZN 155 ? 1_555 ND1 ? E  HIS 63  ? E HIS 63   ? 1_555 113.5 ? 
116 OD1 ? E  ASP 83  ? E ASP 83   ? 1_555 ZN ? DA ZN . ? E ZN 155 ? 1_555 ND1 ? E  HIS 63  ? E HIS 63   ? 1_555 102.2 ? 
117 NE2 ? F  HIS 63  ? F HIS 63   ? 1_555 CU ? EA CU . ? F CU 154 ? 1_555 NE2 ? F  HIS 120 ? F HIS 120  ? 1_555 142.0 ? 
118 NE2 ? F  HIS 63  ? F HIS 63   ? 1_555 CU ? EA CU . ? F CU 154 ? 1_555 NE2 ? F  HIS 48  ? F HIS 48   ? 1_555 97.6  ? 
119 NE2 ? F  HIS 120 ? F HIS 120  ? 1_555 CU ? EA CU . ? F CU 154 ? 1_555 NE2 ? F  HIS 48  ? F HIS 48   ? 1_555 111.3 ? 
120 NE2 ? F  HIS 63  ? F HIS 63   ? 1_555 CU ? EA CU . ? F CU 154 ? 1_555 O   ? KB HOH .   ? F HOH 2040 ? 1_555 66.2  ? 
121 NE2 ? F  HIS 120 ? F HIS 120  ? 1_555 CU ? EA CU . ? F CU 154 ? 1_555 O   ? KB HOH .   ? F HOH 2040 ? 1_555 86.8  ? 
122 NE2 ? F  HIS 48  ? F HIS 48   ? 1_555 CU ? EA CU . ? F CU 154 ? 1_555 O   ? KB HOH .   ? F HOH 2040 ? 1_555 94.5  ? 
123 NE2 ? F  HIS 63  ? F HIS 63   ? 1_555 CU ? EA CU . ? F CU 154 ? 1_555 ND1 ? F  HIS 46  ? F HIS 46   ? 1_555 77.9  ? 
124 NE2 ? F  HIS 120 ? F HIS 120  ? 1_555 CU ? EA CU . ? F CU 154 ? 1_555 ND1 ? F  HIS 46  ? F HIS 46   ? 1_555 96.0  ? 
125 NE2 ? F  HIS 48  ? F HIS 48   ? 1_555 CU ? EA CU . ? F CU 154 ? 1_555 ND1 ? F  HIS 46  ? F HIS 46   ? 1_555 136.3 ? 
126 O   ? KB HOH .   ? F HOH 2040 ? 1_555 CU ? EA CU . ? F CU 154 ? 1_555 ND1 ? F  HIS 46  ? F HIS 46   ? 1_555 121.4 ? 
127 ND1 ? F  HIS 63  ? F HIS 63   ? 1_555 ZN ? FA ZN . ? F ZN 155 ? 1_555 ND1 ? F  HIS 71  ? F HIS 71   ? 1_555 107.1 ? 
128 ND1 ? F  HIS 63  ? F HIS 63   ? 1_555 ZN ? FA ZN . ? F ZN 155 ? 1_555 ND1 ? F  HIS 80  ? F HIS 80   ? 1_555 108.5 ? 
129 ND1 ? F  HIS 71  ? F HIS 71   ? 1_555 ZN ? FA ZN . ? F ZN 155 ? 1_555 ND1 ? F  HIS 80  ? F HIS 80   ? 1_555 121.4 ? 
130 ND1 ? F  HIS 63  ? F HIS 63   ? 1_555 ZN ? FA ZN . ? F ZN 155 ? 1_555 OD1 ? F  ASP 83  ? F ASP 83   ? 1_555 107.1 ? 
131 ND1 ? F  HIS 71  ? F HIS 71   ? 1_555 ZN ? FA ZN . ? F ZN 155 ? 1_555 OD1 ? F  ASP 83  ? F ASP 83   ? 1_555 94.8  ? 
132 ND1 ? F  HIS 80  ? F HIS 80   ? 1_555 ZN ? FA ZN . ? F ZN 155 ? 1_555 OD1 ? F  ASP 83  ? F ASP 83   ? 1_555 116.5 ? 
133 NE2 ? G  HIS 63  ? G HIS 63   ? 1_555 CU ? GA CU . ? G CU 154 ? 1_555 NE2 ? G  HIS 48  ? G HIS 48   ? 1_555 93.1  ? 
134 NE2 ? G  HIS 63  ? G HIS 63   ? 1_555 CU ? GA CU . ? G CU 154 ? 1_555 O   ? LB HOH .   ? G HOH 2022 ? 1_555 56.6  ? 
135 NE2 ? G  HIS 48  ? G HIS 48   ? 1_555 CU ? GA CU . ? G CU 154 ? 1_555 O   ? LB HOH .   ? G HOH 2022 ? 1_555 96.2  ? 
136 NE2 ? G  HIS 63  ? G HIS 63   ? 1_555 CU ? GA CU . ? G CU 154 ? 1_555 ND1 ? G  HIS 46  ? G HIS 46   ? 1_555 75.7  ? 
137 NE2 ? G  HIS 48  ? G HIS 48   ? 1_555 CU ? GA CU . ? G CU 154 ? 1_555 ND1 ? G  HIS 46  ? G HIS 46   ? 1_555 132.7 ? 
138 O   ? LB HOH .   ? G HOH 2022 ? 1_555 CU ? GA CU . ? G CU 154 ? 1_555 ND1 ? G  HIS 46  ? G HIS 46   ? 1_555 113.3 ? 
139 NE2 ? G  HIS 63  ? G HIS 63   ? 1_555 CU ? GA CU . ? G CU 154 ? 1_555 NE2 ? G  HIS 120 ? G HIS 120  ? 1_555 146.2 ? 
140 NE2 ? G  HIS 48  ? G HIS 48   ? 1_555 CU ? GA CU . ? G CU 154 ? 1_555 NE2 ? G  HIS 120 ? G HIS 120  ? 1_555 116.6 ? 
141 O   ? LB HOH .   ? G HOH 2022 ? 1_555 CU ? GA CU . ? G CU 154 ? 1_555 NE2 ? G  HIS 120 ? G HIS 120  ? 1_555 101.7 ? 
142 ND1 ? G  HIS 46  ? G HIS 46   ? 1_555 CU ? GA CU . ? G CU 154 ? 1_555 NE2 ? G  HIS 120 ? G HIS 120  ? 1_555 93.4  ? 
143 NE2 ? G  HIS 63  ? G HIS 63   ? 1_555 CU ? GA CU . ? G CU 154 ? 1_555 O   ? LB HOH .   ? G HOH 2010 ? 1_555 127.8 ? 
144 NE2 ? G  HIS 48  ? G HIS 48   ? 1_555 CU ? GA CU . ? G CU 154 ? 1_555 O   ? LB HOH .   ? G HOH 2010 ? 1_555 66.3  ? 
145 O   ? LB HOH .   ? G HOH 2022 ? 1_555 CU ? GA CU . ? G CU 154 ? 1_555 O   ? LB HOH .   ? G HOH 2010 ? 1_555 161.2 ? 
146 ND1 ? G  HIS 46  ? G HIS 46   ? 1_555 CU ? GA CU . ? G CU 154 ? 1_555 O   ? LB HOH .   ? G HOH 2010 ? 1_555 84.7  ? 
147 NE2 ? G  HIS 120 ? G HIS 120  ? 1_555 CU ? GA CU . ? G CU 154 ? 1_555 O   ? LB HOH .   ? G HOH 2010 ? 1_555 81.6  ? 
148 OD1 ? G  ASP 83  ? G ASP 83   ? 1_555 ZN ? HA ZN . ? G ZN 155 ? 1_555 ND1 ? G  HIS 71  ? G HIS 71   ? 1_555 94.0  ? 
149 OD1 ? G  ASP 83  ? G ASP 83   ? 1_555 ZN ? HA ZN . ? G ZN 155 ? 1_555 ND1 ? G  HIS 80  ? G HIS 80   ? 1_555 118.8 ? 
150 ND1 ? G  HIS 71  ? G HIS 71   ? 1_555 ZN ? HA ZN . ? G ZN 155 ? 1_555 ND1 ? G  HIS 80  ? G HIS 80   ? 1_555 121.2 ? 
151 OD1 ? G  ASP 83  ? G ASP 83   ? 1_555 ZN ? HA ZN . ? G ZN 155 ? 1_555 ND1 ? G  HIS 63  ? G HIS 63   ? 1_555 105.7 ? 
152 ND1 ? G  HIS 71  ? G HIS 71   ? 1_555 ZN ? HA ZN . ? G ZN 155 ? 1_555 ND1 ? G  HIS 63  ? G HIS 63   ? 1_555 107.2 ? 
153 ND1 ? G  HIS 80  ? G HIS 80   ? 1_555 ZN ? HA ZN . ? G ZN 155 ? 1_555 ND1 ? G  HIS 63  ? G HIS 63   ? 1_555 108.3 ? 
154 OD1 ? G  ASP 83  ? G ASP 83   ? 1_555 ZN ? HA ZN . ? G ZN 155 ? 1_555 OD2 ? G  ASP 83  ? G ASP 83   ? 1_555 52.9  ? 
155 ND1 ? G  HIS 71  ? G HIS 71   ? 1_555 ZN ? HA ZN . ? G ZN 155 ? 1_555 OD2 ? G  ASP 83  ? G ASP 83   ? 1_555 70.0  ? 
156 ND1 ? G  HIS 80  ? G HIS 80   ? 1_555 ZN ? HA ZN . ? G ZN 155 ? 1_555 OD2 ? G  ASP 83  ? G ASP 83   ? 1_555 91.7  ? 
157 ND1 ? G  HIS 63  ? G HIS 63   ? 1_555 ZN ? HA ZN . ? G ZN 155 ? 1_555 OD2 ? G  ASP 83  ? G ASP 83   ? 1_555 156.9 ? 
158 ND1 ? H  HIS 46  ? H HIS 46   ? 1_555 CU ? IA CU . ? H CU 154 ? 1_555 NE2 ? H  HIS 120 ? H HIS 120  ? 1_555 94.3  ? 
159 ND1 ? H  HIS 46  ? H HIS 46   ? 1_555 CU ? IA CU . ? H CU 154 ? 1_555 NE2 ? H  HIS 63  ? H HIS 63   ? 1_555 82.7  ? 
160 NE2 ? H  HIS 120 ? H HIS 120  ? 1_555 CU ? IA CU . ? H CU 154 ? 1_555 NE2 ? H  HIS 63  ? H HIS 63   ? 1_555 141.5 ? 
161 ND1 ? H  HIS 46  ? H HIS 46   ? 1_555 CU ? IA CU . ? H CU 154 ? 1_555 NE2 ? H  HIS 48  ? H HIS 48   ? 1_555 138.5 ? 
162 NE2 ? H  HIS 120 ? H HIS 120  ? 1_555 CU ? IA CU . ? H CU 154 ? 1_555 NE2 ? H  HIS 48  ? H HIS 48   ? 1_555 110.9 ? 
163 NE2 ? H  HIS 63  ? H HIS 63   ? 1_555 CU ? IA CU . ? H CU 154 ? 1_555 NE2 ? H  HIS 48  ? H HIS 48   ? 1_555 95.3  ? 
164 ND1 ? H  HIS 46  ? H HIS 46   ? 1_555 CU ? IA CU . ? H CU 154 ? 1_555 O   ? MB HOH .   ? H HOH 2050 ? 1_555 127.2 ? 
165 NE2 ? H  HIS 120 ? H HIS 120  ? 1_555 CU ? IA CU . ? H CU 154 ? 1_555 O   ? MB HOH .   ? H HOH 2050 ? 1_555 88.0  ? 
166 NE2 ? H  HIS 63  ? H HIS 63   ? 1_555 CU ? IA CU . ? H CU 154 ? 1_555 O   ? MB HOH .   ? H HOH 2050 ? 1_555 65.0  ? 
167 NE2 ? H  HIS 48  ? H HIS 48   ? 1_555 CU ? IA CU . ? H CU 154 ? 1_555 O   ? MB HOH .   ? H HOH 2050 ? 1_555 87.4  ? 
168 OD1 ? H  ASP 83  ? H ASP 83   ? 1_555 ZN ? JA ZN . ? H ZN 155 ? 1_555 ND1 ? H  HIS 71  ? H HIS 71   ? 1_555 97.0  ? 
169 OD1 ? H  ASP 83  ? H ASP 83   ? 1_555 ZN ? JA ZN . ? H ZN 155 ? 1_555 ND1 ? H  HIS 80  ? H HIS 80   ? 1_555 112.6 ? 
170 ND1 ? H  HIS 71  ? H HIS 71   ? 1_555 ZN ? JA ZN . ? H ZN 155 ? 1_555 ND1 ? H  HIS 80  ? H HIS 80   ? 1_555 123.3 ? 
171 OD1 ? H  ASP 83  ? H ASP 83   ? 1_555 ZN ? JA ZN . ? H ZN 155 ? 1_555 ND1 ? H  HIS 63  ? H HIS 63   ? 1_555 107.0 ? 
172 ND1 ? H  HIS 71  ? H HIS 71   ? 1_555 ZN ? JA ZN . ? H ZN 155 ? 1_555 ND1 ? H  HIS 63  ? H HIS 63   ? 1_555 105.1 ? 
173 ND1 ? H  HIS 80  ? H HIS 80   ? 1_555 ZN ? JA ZN . ? H ZN 155 ? 1_555 ND1 ? H  HIS 63  ? H HIS 63   ? 1_555 110.2 ? 
174 NE2 ? I  HIS 63  ? I HIS 63   ? 1_555 CU ? KA CU . ? I CU 154 ? 1_555 ND1 ? I  HIS 46  ? I HIS 46   ? 1_555 76.6  ? 
175 NE2 ? I  HIS 63  ? I HIS 63   ? 1_555 CU ? KA CU . ? I CU 154 ? 1_555 NE2 ? I  HIS 120 ? I HIS 120  ? 1_555 140.2 ? 
176 ND1 ? I  HIS 46  ? I HIS 46   ? 1_555 CU ? KA CU . ? I CU 154 ? 1_555 NE2 ? I  HIS 120 ? I HIS 120  ? 1_555 95.9  ? 
177 NE2 ? I  HIS 63  ? I HIS 63   ? 1_555 CU ? KA CU . ? I CU 154 ? 1_555 NE2 ? I  HIS 48  ? I HIS 48   ? 1_555 97.9  ? 
178 ND1 ? I  HIS 46  ? I HIS 46   ? 1_555 CU ? KA CU . ? I CU 154 ? 1_555 NE2 ? I  HIS 48  ? I HIS 48   ? 1_555 137.8 ? 
179 NE2 ? I  HIS 120 ? I HIS 120  ? 1_555 CU ? KA CU . ? I CU 154 ? 1_555 NE2 ? I  HIS 48  ? I HIS 48   ? 1_555 112.1 ? 
180 ND1 ? I  HIS 80  ? I HIS 80   ? 1_555 ZN ? LA ZN . ? I ZN 155 ? 1_555 ND1 ? I  HIS 71  ? I HIS 71   ? 1_555 123.3 ? 
181 ND1 ? I  HIS 80  ? I HIS 80   ? 1_555 ZN ? LA ZN . ? I ZN 155 ? 1_555 OD1 ? I  ASP 83  ? I ASP 83   ? 1_555 114.7 ? 
182 ND1 ? I  HIS 71  ? I HIS 71   ? 1_555 ZN ? LA ZN . ? I ZN 155 ? 1_555 OD1 ? I  ASP 83  ? I ASP 83   ? 1_555 98.2  ? 
183 ND1 ? I  HIS 80  ? I HIS 80   ? 1_555 ZN ? LA ZN . ? I ZN 155 ? 1_555 ND1 ? I  HIS 63  ? I HIS 63   ? 1_555 108.5 ? 
184 ND1 ? I  HIS 71  ? I HIS 71   ? 1_555 ZN ? LA ZN . ? I ZN 155 ? 1_555 ND1 ? I  HIS 63  ? I HIS 63   ? 1_555 106.7 ? 
185 OD1 ? I  ASP 83  ? I ASP 83   ? 1_555 ZN ? LA ZN . ? I ZN 155 ? 1_555 ND1 ? I  HIS 63  ? I HIS 63   ? 1_555 103.4 ? 
186 NE2 ? J  HIS 63  ? J HIS 63   ? 1_555 CU ? MA CU . ? J CU 154 ? 1_555 ND1 ? J  HIS 46  ? J HIS 46   ? 1_555 76.7  ? 
187 NE2 ? J  HIS 63  ? J HIS 63   ? 1_555 CU ? MA CU . ? J CU 154 ? 1_555 NE2 ? J  HIS 48  ? J HIS 48   ? 1_555 96.9  ? 
188 ND1 ? J  HIS 46  ? J HIS 46   ? 1_555 CU ? MA CU . ? J CU 154 ? 1_555 NE2 ? J  HIS 48  ? J HIS 48   ? 1_555 134.1 ? 
189 NE2 ? J  HIS 63  ? J HIS 63   ? 1_555 CU ? MA CU . ? J CU 154 ? 1_555 O   ? OB HOH .   ? J HOH 2064 ? 1_555 68.7  ? 
190 ND1 ? J  HIS 46  ? J HIS 46   ? 1_555 CU ? MA CU . ? J CU 154 ? 1_555 O   ? OB HOH .   ? J HOH 2064 ? 1_555 119.3 ? 
191 NE2 ? J  HIS 48  ? J HIS 48   ? 1_555 CU ? MA CU . ? J CU 154 ? 1_555 O   ? OB HOH .   ? J HOH 2064 ? 1_555 99.1  ? 
192 NE2 ? J  HIS 63  ? J HIS 63   ? 1_555 CU ? MA CU . ? J CU 154 ? 1_555 NE2 ? J  HIS 120 ? J HIS 120  ? 1_555 142.7 ? 
193 ND1 ? J  HIS 46  ? J HIS 46   ? 1_555 CU ? MA CU . ? J CU 154 ? 1_555 NE2 ? J  HIS 120 ? J HIS 120  ? 1_555 96.3  ? 
194 NE2 ? J  HIS 48  ? J HIS 48   ? 1_555 CU ? MA CU . ? J CU 154 ? 1_555 NE2 ? J  HIS 120 ? J HIS 120  ? 1_555 112.8 ? 
195 O   ? OB HOH .   ? J HOH 2064 ? 1_555 CU ? MA CU . ? J CU 154 ? 1_555 NE2 ? J  HIS 120 ? J HIS 120  ? 1_555 84.1  ? 
196 OD1 ? J  ASP 83  ? J ASP 83   ? 1_555 ZN ? NA ZN . ? J ZN 155 ? 1_555 ND1 ? J  HIS 63  ? J HIS 63   ? 1_555 108.1 ? 
197 OD1 ? J  ASP 83  ? J ASP 83   ? 1_555 ZN ? NA ZN . ? J ZN 155 ? 1_555 ND1 ? J  HIS 71  ? J HIS 71   ? 1_555 98.2  ? 
198 ND1 ? J  HIS 63  ? J HIS 63   ? 1_555 ZN ? NA ZN . ? J ZN 155 ? 1_555 ND1 ? J  HIS 71  ? J HIS 71   ? 1_555 109.0 ? 
199 OD1 ? J  ASP 83  ? J ASP 83   ? 1_555 ZN ? NA ZN . ? J ZN 155 ? 1_555 ND1 ? J  HIS 80  ? J HIS 80   ? 1_555 111.9 ? 
200 ND1 ? J  HIS 63  ? J HIS 63   ? 1_555 ZN ? NA ZN . ? J ZN 155 ? 1_555 ND1 ? J  HIS 80  ? J HIS 80   ? 1_555 110.7 ? 
201 ND1 ? J  HIS 71  ? J HIS 71   ? 1_555 ZN ? NA ZN . ? J ZN 155 ? 1_555 ND1 ? J  HIS 80  ? J HIS 80   ? 1_555 118.0 ? 
202 O   ? PB HOH .   ? K HOH 2063 ? 1_555 CU ? OA CU . ? K CU 154 ? 1_555 NE2 ? K  HIS 120 ? K HIS 120  ? 1_555 85.7  ? 
203 O   ? PB HOH .   ? K HOH 2063 ? 1_555 CU ? OA CU . ? K CU 154 ? 1_555 NE2 ? K  HIS 63  ? K HIS 63   ? 1_555 68.5  ? 
204 NE2 ? K  HIS 120 ? K HIS 120  ? 1_555 CU ? OA CU . ? K CU 154 ? 1_555 NE2 ? K  HIS 63  ? K HIS 63   ? 1_555 144.0 ? 
205 O   ? PB HOH .   ? K HOH 2063 ? 1_555 CU ? OA CU . ? K CU 154 ? 1_555 ND1 ? K  HIS 46  ? K HIS 46   ? 1_555 122.8 ? 
206 NE2 ? K  HIS 120 ? K HIS 120  ? 1_555 CU ? OA CU . ? K CU 154 ? 1_555 ND1 ? K  HIS 46  ? K HIS 46   ? 1_555 95.6  ? 
207 NE2 ? K  HIS 63  ? K HIS 63   ? 1_555 CU ? OA CU . ? K CU 154 ? 1_555 ND1 ? K  HIS 46  ? K HIS 46   ? 1_555 79.3  ? 
208 O   ? PB HOH .   ? K HOH 2063 ? 1_555 CU ? OA CU . ? K CU 154 ? 1_555 NE2 ? K  HIS 48  ? K HIS 48   ? 1_555 98.0  ? 
209 NE2 ? K  HIS 120 ? K HIS 120  ? 1_555 CU ? OA CU . ? K CU 154 ? 1_555 NE2 ? K  HIS 48  ? K HIS 48   ? 1_555 111.2 ? 
210 NE2 ? K  HIS 63  ? K HIS 63   ? 1_555 CU ? OA CU . ? K CU 154 ? 1_555 NE2 ? K  HIS 48  ? K HIS 48   ? 1_555 97.4  ? 
211 ND1 ? K  HIS 46  ? K HIS 46   ? 1_555 CU ? OA CU . ? K CU 154 ? 1_555 NE2 ? K  HIS 48  ? K HIS 48   ? 1_555 133.0 ? 
212 ND1 ? K  HIS 63  ? K HIS 63   ? 1_555 ZN ? PA ZN . ? K ZN 155 ? 1_555 ND1 ? K  HIS 71  ? K HIS 71   ? 1_555 107.6 ? 
213 ND1 ? K  HIS 63  ? K HIS 63   ? 1_555 ZN ? PA ZN . ? K ZN 155 ? 1_555 ND1 ? K  HIS 80  ? K HIS 80   ? 1_555 110.8 ? 
214 ND1 ? K  HIS 71  ? K HIS 71   ? 1_555 ZN ? PA ZN . ? K ZN 155 ? 1_555 ND1 ? K  HIS 80  ? K HIS 80   ? 1_555 121.1 ? 
215 ND1 ? K  HIS 63  ? K HIS 63   ? 1_555 ZN ? PA ZN . ? K ZN 155 ? 1_555 OD1 ? K  ASP 83  ? K ASP 83   ? 1_555 105.3 ? 
216 ND1 ? K  HIS 71  ? K HIS 71   ? 1_555 ZN ? PA ZN . ? K ZN 155 ? 1_555 OD1 ? K  ASP 83  ? K ASP 83   ? 1_555 98.0  ? 
217 ND1 ? K  HIS 80  ? K HIS 80   ? 1_555 ZN ? PA ZN . ? K ZN 155 ? 1_555 OD1 ? K  ASP 83  ? K ASP 83   ? 1_555 112.4 ? 
218 NE2 ? L  HIS 48  ? L HIS 48   ? 1_555 CU ? QA CU . ? L CU 154 ? 1_555 ND1 ? L  HIS 46  ? L HIS 46   ? 1_555 134.1 ? 
219 NE2 ? L  HIS 48  ? L HIS 48   ? 1_555 CU ? QA CU . ? L CU 154 ? 1_555 NE2 ? L  HIS 120 ? L HIS 120  ? 1_555 115.9 ? 
220 ND1 ? L  HIS 46  ? L HIS 46   ? 1_555 CU ? QA CU . ? L CU 154 ? 1_555 NE2 ? L  HIS 120 ? L HIS 120  ? 1_555 100.0 ? 
221 ND1 ? L  HIS 63  ? L HIS 63   ? 1_555 ZN ? RA ZN . ? L ZN 155 ? 1_555 ND1 ? L  HIS 71  ? L HIS 71   ? 1_555 105.9 ? 
222 ND1 ? L  HIS 63  ? L HIS 63   ? 1_555 ZN ? RA ZN . ? L ZN 155 ? 1_555 OD1 ? L  ASP 83  ? L ASP 83   ? 1_555 105.0 ? 
223 ND1 ? L  HIS 71  ? L HIS 71   ? 1_555 ZN ? RA ZN . ? L ZN 155 ? 1_555 OD1 ? L  ASP 83  ? L ASP 83   ? 1_555 97.9  ? 
224 ND1 ? L  HIS 63  ? L HIS 63   ? 1_555 ZN ? RA ZN . ? L ZN 155 ? 1_555 ND1 ? L  HIS 80  ? L HIS 80   ? 1_555 112.7 ? 
225 ND1 ? L  HIS 71  ? L HIS 71   ? 1_555 ZN ? RA ZN . ? L ZN 155 ? 1_555 ND1 ? L  HIS 80  ? L HIS 80   ? 1_555 119.1 ? 
226 OD1 ? L  ASP 83  ? L ASP 83   ? 1_555 ZN ? RA ZN . ? L ZN 155 ? 1_555 ND1 ? L  HIS 80  ? L HIS 80   ? 1_555 114.5 ? 
227 NE2 ? M  HIS 63  ? M HIS 63   ? 1_555 CU ? SA CU . ? M CU 154 ? 1_555 ND1 ? M  HIS 46  ? M HIS 46   ? 1_555 78.9  ? 
228 NE2 ? M  HIS 63  ? M HIS 63   ? 1_555 CU ? SA CU . ? M CU 154 ? 1_555 NE2 ? M  HIS 48  ? M HIS 48   ? 1_555 97.7  ? 
229 ND1 ? M  HIS 46  ? M HIS 46   ? 1_555 CU ? SA CU . ? M CU 154 ? 1_555 NE2 ? M  HIS 48  ? M HIS 48   ? 1_555 136.5 ? 
230 NE2 ? M  HIS 63  ? M HIS 63   ? 1_555 CU ? SA CU . ? M CU 154 ? 1_555 O   ? RB HOH .   ? M HOH 2041 ? 1_555 66.4  ? 
231 ND1 ? M  HIS 46  ? M HIS 46   ? 1_555 CU ? SA CU . ? M CU 154 ? 1_555 O   ? RB HOH .   ? M HOH 2041 ? 1_555 120.3 ? 
232 NE2 ? M  HIS 48  ? M HIS 48   ? 1_555 CU ? SA CU . ? M CU 154 ? 1_555 O   ? RB HOH .   ? M HOH 2041 ? 1_555 96.4  ? 
233 NE2 ? M  HIS 63  ? M HIS 63   ? 1_555 CU ? SA CU . ? M CU 154 ? 1_555 NE2 ? M  HIS 120 ? M HIS 120  ? 1_555 142.6 ? 
234 ND1 ? M  HIS 46  ? M HIS 46   ? 1_555 CU ? SA CU . ? M CU 154 ? 1_555 NE2 ? M  HIS 120 ? M HIS 120  ? 1_555 95.7  ? 
235 NE2 ? M  HIS 48  ? M HIS 48   ? 1_555 CU ? SA CU . ? M CU 154 ? 1_555 NE2 ? M  HIS 120 ? M HIS 120  ? 1_555 110.5 ? 
236 O   ? RB HOH .   ? M HOH 2041 ? 1_555 CU ? SA CU . ? M CU 154 ? 1_555 NE2 ? M  HIS 120 ? M HIS 120  ? 1_555 86.0  ? 
237 ND1 ? M  HIS 63  ? M HIS 63   ? 1_555 ZN ? TA ZN . ? M ZN 155 ? 1_555 ND1 ? M  HIS 71  ? M HIS 71   ? 1_555 106.5 ? 
238 ND1 ? M  HIS 63  ? M HIS 63   ? 1_555 ZN ? TA ZN . ? M ZN 155 ? 1_555 ND1 ? M  HIS 80  ? M HIS 80   ? 1_555 112.8 ? 
239 ND1 ? M  HIS 71  ? M HIS 71   ? 1_555 ZN ? TA ZN . ? M ZN 155 ? 1_555 ND1 ? M  HIS 80  ? M HIS 80   ? 1_555 122.2 ? 
240 ND1 ? M  HIS 63  ? M HIS 63   ? 1_555 ZN ? TA ZN . ? M ZN 155 ? 1_555 OD1 ? M  ASP 83  ? M ASP 83   ? 1_555 104.5 ? 
241 ND1 ? M  HIS 71  ? M HIS 71   ? 1_555 ZN ? TA ZN . ? M ZN 155 ? 1_555 OD1 ? M  ASP 83  ? M ASP 83   ? 1_555 96.0  ? 
242 ND1 ? M  HIS 80  ? M HIS 80   ? 1_555 ZN ? TA ZN . ? M ZN 155 ? 1_555 OD1 ? M  ASP 83  ? M ASP 83   ? 1_555 112.5 ? 
243 O   ? SB HOH .   ? N HOH 2038 ? 1_555 CU ? UA CU . ? N CU 154 ? 1_555 NE2 ? N  HIS 120 ? N HIS 120  ? 1_555 85.6  ? 
244 O   ? SB HOH .   ? N HOH 2038 ? 1_555 CU ? UA CU . ? N CU 154 ? 1_555 NE2 ? N  HIS 63  ? N HIS 63   ? 1_555 63.9  ? 
245 NE2 ? N  HIS 120 ? N HIS 120  ? 1_555 CU ? UA CU . ? N CU 154 ? 1_555 NE2 ? N  HIS 63  ? N HIS 63   ? 1_555 140.2 ? 
246 O   ? SB HOH .   ? N HOH 2038 ? 1_555 CU ? UA CU . ? N CU 154 ? 1_555 NE2 ? N  HIS 48  ? N HIS 48   ? 1_555 96.3  ? 
247 NE2 ? N  HIS 120 ? N HIS 120  ? 1_555 CU ? UA CU . ? N CU 154 ? 1_555 NE2 ? N  HIS 48  ? N HIS 48   ? 1_555 114.9 ? 
248 NE2 ? N  HIS 63  ? N HIS 63   ? 1_555 CU ? UA CU . ? N CU 154 ? 1_555 NE2 ? N  HIS 48  ? N HIS 48   ? 1_555 94.4  ? 
249 O   ? SB HOH .   ? N HOH 2038 ? 1_555 CU ? UA CU . ? N CU 154 ? 1_555 ND1 ? N  HIS 46  ? N HIS 46   ? 1_555 116.3 ? 
250 NE2 ? N  HIS 120 ? N HIS 120  ? 1_555 CU ? UA CU . ? N CU 154 ? 1_555 ND1 ? N  HIS 46  ? N HIS 46   ? 1_555 95.9  ? 
251 NE2 ? N  HIS 63  ? N HIS 63   ? 1_555 CU ? UA CU . ? N CU 154 ? 1_555 ND1 ? N  HIS 46  ? N HIS 46   ? 1_555 77.4  ? 
252 NE2 ? N  HIS 48  ? N HIS 48   ? 1_555 CU ? UA CU . ? N CU 154 ? 1_555 ND1 ? N  HIS 46  ? N HIS 46   ? 1_555 137.0 ? 
253 ND1 ? N  HIS 71  ? N HIS 71   ? 1_555 ZN ? VA ZN . ? N ZN 155 ? 1_555 OD1 ? N  ASP 83  ? N ASP 83   ? 1_555 98.3  ? 
254 ND1 ? N  HIS 71  ? N HIS 71   ? 1_555 ZN ? VA ZN . ? N ZN 155 ? 1_555 ND1 ? N  HIS 63  ? N HIS 63   ? 1_555 110.0 ? 
255 OD1 ? N  ASP 83  ? N ASP 83   ? 1_555 ZN ? VA ZN . ? N ZN 155 ? 1_555 ND1 ? N  HIS 63  ? N HIS 63   ? 1_555 102.5 ? 
256 ND1 ? N  HIS 71  ? N HIS 71   ? 1_555 ZN ? VA ZN . ? N ZN 155 ? 1_555 ND1 ? N  HIS 80  ? N HIS 80   ? 1_555 120.9 ? 
257 OD1 ? N  ASP 83  ? N ASP 83   ? 1_555 ZN ? VA ZN . ? N ZN 155 ? 1_555 ND1 ? N  HIS 80  ? N HIS 80   ? 1_555 114.2 ? 
258 ND1 ? N  HIS 63  ? N HIS 63   ? 1_555 ZN ? VA ZN . ? N ZN 155 ? 1_555 ND1 ? N  HIS 80  ? N HIS 80   ? 1_555 109.2 ? 
259 NE2 ? O  HIS 48  ? O HIS 48   ? 1_555 CU ? WA CU . ? O CU 154 ? 1_555 NE2 ? O  HIS 120 ? O HIS 120  ? 1_555 106.9 ? 
260 NE2 ? O  HIS 48  ? O HIS 48   ? 1_555 CU ? WA CU . ? O CU 154 ? 1_555 ND1 ? O  HIS 46  ? O HIS 46   ? 1_555 144.3 ? 
261 NE2 ? O  HIS 120 ? O HIS 120  ? 1_555 CU ? WA CU . ? O CU 154 ? 1_555 ND1 ? O  HIS 46  ? O HIS 46   ? 1_555 98.7  ? 
262 NE2 ? O  HIS 48  ? O HIS 48   ? 1_555 CU ? WA CU . ? O CU 154 ? 1_555 NE2 ? O  HIS 63  ? O HIS 63   ? 1_555 99.0  ? 
263 NE2 ? O  HIS 120 ? O HIS 120  ? 1_555 CU ? WA CU . ? O CU 154 ? 1_555 NE2 ? O  HIS 63  ? O HIS 63   ? 1_555 136.6 ? 
264 ND1 ? O  HIS 46  ? O HIS 46   ? 1_555 CU ? WA CU . ? O CU 154 ? 1_555 NE2 ? O  HIS 63  ? O HIS 63   ? 1_555 77.5  ? 
265 OD1 ? O  ASP 83  ? O ASP 83   ? 1_555 ZN ? XA ZN . ? O ZN 155 ? 1_555 ND1 ? O  HIS 63  ? O HIS 63   ? 1_555 105.9 ? 
266 OD1 ? O  ASP 83  ? O ASP 83   ? 1_555 ZN ? XA ZN . ? O ZN 155 ? 1_555 ND1 ? O  HIS 80  ? O HIS 80   ? 1_555 109.4 ? 
267 ND1 ? O  HIS 63  ? O HIS 63   ? 1_555 ZN ? XA ZN . ? O ZN 155 ? 1_555 ND1 ? O  HIS 80  ? O HIS 80   ? 1_555 113.6 ? 
268 OD1 ? O  ASP 83  ? O ASP 83   ? 1_555 ZN ? XA ZN . ? O ZN 155 ? 1_555 ND1 ? O  HIS 71  ? O HIS 71   ? 1_555 98.4  ? 
269 ND1 ? O  HIS 63  ? O HIS 63   ? 1_555 ZN ? XA ZN . ? O ZN 155 ? 1_555 ND1 ? O  HIS 71  ? O HIS 71   ? 1_555 106.4 ? 
270 ND1 ? O  HIS 80  ? O HIS 80   ? 1_555 ZN ? XA ZN . ? O ZN 155 ? 1_555 ND1 ? O  HIS 71  ? O HIS 71   ? 1_555 121.0 ? 
271 O   ? H  SER 102 ? H SER 102  ? 1_555 CA ? YA CA . ? O CA 156 ? 1_555 O   ? MB HOH .   ? H HOH 2085 ? 1_555 84.3  ? 
272 O   ? H  SER 102 ? H SER 102  ? 1_555 CA ? YA CA . ? O CA 156 ? 1_555 OD1 ? H  ASN 26  ? H ASN 26   ? 1_555 160.5 ? 
273 O   ? MB HOH .   ? H HOH 2085 ? 1_555 CA ? YA CA . ? O CA 156 ? 1_555 OD1 ? H  ASN 26  ? H ASN 26   ? 1_555 102.0 ? 
274 O   ? H  SER 102 ? H SER 102  ? 1_555 CA ? YA CA . ? O CA 156 ? 1_555 O   ? MB HOH .   ? H HOH 2081 ? 1_555 73.9  ? 
275 O   ? MB HOH .   ? H HOH 2085 ? 1_555 CA ? YA CA . ? O CA 156 ? 1_555 O   ? MB HOH .   ? H HOH 2081 ? 1_555 151.6 ? 
276 OD1 ? H  ASN 26  ? H ASN 26   ? 1_555 CA ? YA CA . ? O CA 156 ? 1_555 O   ? MB HOH .   ? H HOH 2081 ? 1_555 93.5  ? 
277 O   ? H  SER 102 ? H SER 102  ? 1_555 CA ? YA CA . ? O CA 156 ? 1_555 O   ? MB HOH .   ? H HOH 2084 ? 1_555 85.7  ? 
278 O   ? MB HOH .   ? H HOH 2085 ? 1_555 CA ? YA CA . ? O CA 156 ? 1_555 O   ? MB HOH .   ? H HOH 2084 ? 1_555 80.7  ? 
279 OD1 ? H  ASN 26  ? H ASN 26   ? 1_555 CA ? YA CA . ? O CA 156 ? 1_555 O   ? MB HOH .   ? H HOH 2084 ? 1_555 77.3  ? 
280 O   ? MB HOH .   ? H HOH 2081 ? 1_555 CA ? YA CA . ? O CA 156 ? 1_555 O   ? MB HOH .   ? H HOH 2084 ? 1_555 79.8  ? 
281 O   ? H  SER 102 ? H SER 102  ? 1_555 CA ? YA CA . ? O CA 156 ? 1_555 O   ? H  ASN 26  ? H ASN 26   ? 1_555 130.5 ? 
282 O   ? MB HOH .   ? H HOH 2085 ? 1_555 CA ? YA CA . ? O CA 156 ? 1_555 O   ? H  ASN 26  ? H ASN 26   ? 1_555 76.6  ? 
283 OD1 ? H  ASN 26  ? H ASN 26   ? 1_555 CA ? YA CA . ? O CA 156 ? 1_555 O   ? H  ASN 26  ? H ASN 26   ? 1_555 68.9  ? 
284 O   ? MB HOH .   ? H HOH 2081 ? 1_555 CA ? YA CA . ? O CA 156 ? 1_555 O   ? H  ASN 26  ? H ASN 26   ? 1_555 131.6 ? 
285 O   ? MB HOH .   ? H HOH 2084 ? 1_555 CA ? YA CA . ? O CA 156 ? 1_555 O   ? H  ASN 26  ? H ASN 26   ? 1_555 133.6 ? 
286 NE2 ? P  HIS 63  ? P HIS 63   ? 1_555 CU ? ZA CU . ? P CU 154 ? 1_555 NE2 ? P  HIS 120 ? P HIS 120  ? 1_555 126.2 ? 
287 NE2 ? P  HIS 63  ? P HIS 63   ? 1_555 CU ? ZA CU . ? P CU 154 ? 1_555 ND1 ? P  HIS 46  ? P HIS 46   ? 1_555 87.7  ? 
288 NE2 ? P  HIS 120 ? P HIS 120  ? 1_555 CU ? ZA CU . ? P CU 154 ? 1_555 ND1 ? P  HIS 46  ? P HIS 46   ? 1_555 96.5  ? 
289 NE2 ? P  HIS 63  ? P HIS 63   ? 1_555 CU ? ZA CU . ? P CU 154 ? 1_555 NE2 ? P  HIS 48  ? P HIS 48   ? 1_555 105.4 ? 
290 NE2 ? P  HIS 120 ? P HIS 120  ? 1_555 CU ? ZA CU . ? P CU 154 ? 1_555 NE2 ? P  HIS 48  ? P HIS 48   ? 1_555 92.3  ? 
291 ND1 ? P  HIS 46  ? P HIS 46   ? 1_555 CU ? ZA CU . ? P CU 154 ? 1_555 NE2 ? P  HIS 48  ? P HIS 48   ? 1_555 155.5 ? 
292 OD2 ? P  ASP 83  ? P ASP 83   ? 1_555 ZN ? AB ZN . ? P ZN 155 ? 1_555 OD1 ? P  ASP 83  ? P ASP 83   ? 1_555 52.2  ? 
293 OD2 ? P  ASP 83  ? P ASP 83   ? 1_555 ZN ? AB ZN . ? P ZN 155 ? 1_555 ND1 ? P  HIS 71  ? P HIS 71   ? 1_555 83.7  ? 
294 OD1 ? P  ASP 83  ? P ASP 83   ? 1_555 ZN ? AB ZN . ? P ZN 155 ? 1_555 ND1 ? P  HIS 71  ? P HIS 71   ? 1_555 98.4  ? 
295 OD2 ? P  ASP 83  ? P ASP 83   ? 1_555 ZN ? AB ZN . ? P ZN 155 ? 1_555 ND1 ? P  HIS 80  ? P HIS 80   ? 1_555 89.2  ? 
296 OD1 ? P  ASP 83  ? P ASP 83   ? 1_555 ZN ? AB ZN . ? P ZN 155 ? 1_555 ND1 ? P  HIS 80  ? P HIS 80   ? 1_555 123.4 ? 
297 ND1 ? P  HIS 71  ? P HIS 71   ? 1_555 ZN ? AB ZN . ? P ZN 155 ? 1_555 ND1 ? P  HIS 80  ? P HIS 80   ? 1_555 118.9 ? 
298 OD2 ? P  ASP 83  ? P ASP 83   ? 1_555 ZN ? AB ZN . ? P ZN 155 ? 1_555 ND1 ? P  HIS 63  ? P HIS 63   ? 1_555 158.6 ? 
299 OD1 ? P  ASP 83  ? P ASP 83   ? 1_555 ZN ? AB ZN . ? P ZN 155 ? 1_555 ND1 ? P  HIS 63  ? P HIS 63   ? 1_555 106.6 ? 
300 ND1 ? P  HIS 71  ? P HIS 71   ? 1_555 ZN ? AB ZN . ? P ZN 155 ? 1_555 ND1 ? P  HIS 63  ? P HIS 63   ? 1_555 104.6 ? 
301 ND1 ? P  HIS 80  ? P HIS 80   ? 1_555 ZN ? AB ZN . ? P ZN 155 ? 1_555 ND1 ? P  HIS 63  ? P HIS 63   ? 1_555 103.2 ? 
302 NE2 ? Q  HIS 120 ? Q HIS 120  ? 1_555 CU ? BB CU . ? Q CU 154 ? 1_555 O   ? VB HOH .   ? Q HOH 2040 ? 1_555 81.3  ? 
303 NE2 ? Q  HIS 120 ? Q HIS 120  ? 1_555 CU ? BB CU . ? Q CU 154 ? 1_555 NE2 ? Q  HIS 63  ? Q HIS 63   ? 1_555 137.4 ? 
304 O   ? VB HOH .   ? Q HOH 2040 ? 1_555 CU ? BB CU . ? Q CU 154 ? 1_555 NE2 ? Q  HIS 63  ? Q HIS 63   ? 1_555 65.4  ? 
305 NE2 ? Q  HIS 120 ? Q HIS 120  ? 1_555 CU ? BB CU . ? Q CU 154 ? 1_555 ND1 ? Q  HIS 46  ? Q HIS 46   ? 1_555 99.0  ? 
306 O   ? VB HOH .   ? Q HOH 2040 ? 1_555 CU ? BB CU . ? Q CU 154 ? 1_555 ND1 ? Q  HIS 46  ? Q HIS 46   ? 1_555 121.5 ? 
307 NE2 ? Q  HIS 63  ? Q HIS 63   ? 1_555 CU ? BB CU . ? Q CU 154 ? 1_555 ND1 ? Q  HIS 46  ? Q HIS 46   ? 1_555 78.5  ? 
308 NE2 ? Q  HIS 120 ? Q HIS 120  ? 1_555 CU ? BB CU . ? Q CU 154 ? 1_555 NE2 ? Q  HIS 48  ? Q HIS 48   ? 1_555 112.3 ? 
309 O   ? VB HOH .   ? Q HOH 2040 ? 1_555 CU ? BB CU . ? Q CU 154 ? 1_555 NE2 ? Q  HIS 48  ? Q HIS 48   ? 1_555 98.2  ? 
310 NE2 ? Q  HIS 63  ? Q HIS 63   ? 1_555 CU ? BB CU . ? Q CU 154 ? 1_555 NE2 ? Q  HIS 48  ? Q HIS 48   ? 1_555 98.7  ? 
311 ND1 ? Q  HIS 46  ? Q HIS 46   ? 1_555 CU ? BB CU . ? Q CU 154 ? 1_555 NE2 ? Q  HIS 48  ? Q HIS 48   ? 1_555 132.7 ? 
312 ND1 ? Q  HIS 63  ? Q HIS 63   ? 1_555 ZN ? CB ZN . ? Q ZN 155 ? 1_555 OD1 ? Q  ASP 83  ? Q ASP 83   ? 1_555 103.8 ? 
313 ND1 ? Q  HIS 63  ? Q HIS 63   ? 1_555 ZN ? CB ZN . ? Q ZN 155 ? 1_555 ND1 ? Q  HIS 80  ? Q HIS 80   ? 1_555 111.0 ? 
314 OD1 ? Q  ASP 83  ? Q ASP 83   ? 1_555 ZN ? CB ZN . ? Q ZN 155 ? 1_555 ND1 ? Q  HIS 80  ? Q HIS 80   ? 1_555 112.2 ? 
315 ND1 ? Q  HIS 63  ? Q HIS 63   ? 1_555 ZN ? CB ZN . ? Q ZN 155 ? 1_555 ND1 ? Q  HIS 71  ? Q HIS 71   ? 1_555 110.2 ? 
316 OD1 ? Q  ASP 83  ? Q ASP 83   ? 1_555 ZN ? CB ZN . ? Q ZN 155 ? 1_555 ND1 ? Q  HIS 71  ? Q HIS 71   ? 1_555 99.3  ? 
317 ND1 ? Q  HIS 80  ? Q HIS 80   ? 1_555 ZN ? CB ZN . ? Q ZN 155 ? 1_555 ND1 ? Q  HIS 71  ? Q HIS 71   ? 1_555 118.7 ? 
318 NE2 ? R  HIS 63  ? S HIS 63   ? 1_555 CU ? DB CU . ? S CU 154 ? 1_555 ND1 ? R  HIS 46  ? S HIS 46   ? 1_555 83.2  ? 
319 NE2 ? R  HIS 63  ? S HIS 63   ? 1_555 CU ? DB CU . ? S CU 154 ? 1_555 NE2 ? R  HIS 48  ? S HIS 48   ? 1_555 93.6  ? 
320 ND1 ? R  HIS 46  ? S HIS 46   ? 1_555 CU ? DB CU . ? S CU 154 ? 1_555 NE2 ? R  HIS 48  ? S HIS 48   ? 1_555 130.3 ? 
321 NE2 ? R  HIS 63  ? S HIS 63   ? 1_555 CU ? DB CU . ? S CU 154 ? 1_555 NE2 ? R  HIS 120 ? S HIS 120  ? 1_555 137.4 ? 
322 ND1 ? R  HIS 46  ? S HIS 46   ? 1_555 CU ? DB CU . ? S CU 154 ? 1_555 NE2 ? R  HIS 120 ? S HIS 120  ? 1_555 97.6  ? 
323 NE2 ? R  HIS 48  ? S HIS 48   ? 1_555 CU ? DB CU . ? S CU 154 ? 1_555 NE2 ? R  HIS 120 ? S HIS 120  ? 1_555 116.0 ? 
324 ND1 ? R  HIS 80  ? S HIS 80   ? 1_555 ZN ? EB ZN . ? S ZN 155 ? 1_555 OD1 ? R  ASP 83  ? S ASP 83   ? 1_555 120.5 ? 
325 ND1 ? R  HIS 80  ? S HIS 80   ? 1_555 ZN ? EB ZN . ? S ZN 155 ? 1_555 ND1 ? R  HIS 71  ? S HIS 71   ? 1_555 125.2 ? 
326 OD1 ? R  ASP 83  ? S ASP 83   ? 1_555 ZN ? EB ZN . ? S ZN 155 ? 1_555 ND1 ? R  HIS 71  ? S HIS 71   ? 1_555 90.8  ? 
327 ND1 ? R  HIS 80  ? S HIS 80   ? 1_555 ZN ? EB ZN . ? S ZN 155 ? 1_555 ND1 ? R  HIS 63  ? S HIS 63   ? 1_555 108.8 ? 
328 OD1 ? R  ASP 83  ? S ASP 83   ? 1_555 ZN ? EB ZN . ? S ZN 155 ? 1_555 ND1 ? R  HIS 63  ? S HIS 63   ? 1_555 105.8 ? 
329 ND1 ? R  HIS 71  ? S HIS 71   ? 1_555 ZN ? EB ZN . ? S ZN 155 ? 1_555 ND1 ? R  HIS 63  ? S HIS 63   ? 1_555 102.8 ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2003-05-08 
2 'Structure model' 1 1 2011-07-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' Advisory                    
2 2 'Structure model' 'Version format compliance' 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1  ? refined 41.9990 92.7450  77.5010  0.2738 0.3268 0.2285 -0.0297 0.0231  0.0235  0.3939 1.7203 2.4501  
0.3695  -0.3914 -0.6319 0.0155  0.0176  0.0329  0.0771  -0.0672 -0.0479 0.1542  -0.0681 0.0517  
'X-RAY DIFFRACTION' 2  ? refined 1.8230  80.8690  18.2360  0.2560 0.3025 0.2784 0.0048  0.0016  0.0244  0.4364 1.0334 1.9486  
0.2720  0.4686  0.7495  0.0165  0.0149  -0.0093 -0.0539 0.0235  0.0374  -0.0721 -0.1209 -0.0400 
'X-RAY DIFFRACTION' 3  ? refined 40.2020 79.9080  21.0390  0.2572 0.3237 0.2667 0.0115  0.0036  -0.0035 0.3464 0.8679 1.7061  
0.1293  0.1464  0.3582  -0.0020 0.0380  -0.0468 -0.0301 0.0157  -0.0558 0.0473  0.1287  -0.0138 
'X-RAY DIFFRACTION' 4  ? refined 3.0630  93.6740  74.8370  0.2818 0.3293 0.2494 -0.0206 0.0451  0.0321  0.4916 0.8767 2.6184  
-0.0501 -0.5955 -0.4587 0.0509  0.0662  0.1022  -0.1570 0.0401  -0.1000 0.0299  -0.1038 -0.0910 
'X-RAY DIFFRACTION' 5  ? refined 47.9430 120.4050 62.0100  0.2553 0.2944 0.2748 -0.0007 -0.0046 -0.0229 0.4642 2.8620 0.8262  
0.2942  0.2706  0.5787  -0.0397 -0.0420 -0.0332 -0.1147 0.0608  -0.1131 0.0056  0.0490  -0.0212 
'X-RAY DIFFRACTION' 6  ? refined 0.4560  111.6250 110.1710 0.3467 0.2167 0.3269 0.0330  -0.0607 -0.0106 0.4729 3.1975 0.6928  
-0.8700 -0.2605 0.6916  -0.0166 -0.0216 -0.0197 0.3467  0.1034  -0.1312 0.1893  0.0453  -0.0867 
'X-RAY DIFFRACTION' 7  ? refined 14.3640 148.3970 61.3980  0.2854 0.2483 0.6222 0.0851  -0.1576 -0.2325 1.1128 4.4067 1.2002  
1.7735  0.8128  0.8956  -0.2732 -0.3441 0.6269  -0.3784 -0.2746 0.9741  -0.3241 -0.1849 0.5478  
'X-RAY DIFFRACTION' 8  ? refined 40.1180 111.6310 105.0200 0.2499 0.2039 0.4878 -0.0187 -0.0778 0.0295  0.0761 6.0838 0.8752  
-1.0256 -0.1423 -0.3385 0.0746  0.0198  -0.2476 -0.2759 0.1527  0.8359  0.1165  -0.0899 -0.2273 
'X-RAY DIFFRACTION' 9  ? refined 57.9290 121.2110 22.9610  0.4754 0.3928 0.1742 0.0564  0.0342  0.0722  4.2152 1.8234 4.1287  
-0.9906 0.0157  -1.5566 -0.2512 -0.7339 -0.1908 0.2698  0.2220  -0.0985 -0.7130 -0.2469 0.0291  
'X-RAY DIFFRACTION' 10 ? refined 38.4320 139.6630 30.5920  0.7806 1.2086 0.0690 0.8109  -0.1603 -0.2814 6.0487 6.4738 11.4578 
-1.6345 -0.9648 2.9661  -0.3925 -1.3673 0.5828  -0.4773 -0.1079 0.4313  -1.2460 -1.7686 0.5005  
'X-RAY DIFFRACTION' 11 ? refined 34.5020 138.8560 106.5970 0.2163 0.2577 0.3483 0.0142  0.0220  0.0237  1.3408 6.2236 1.1933  
-2.4308 0.3864  -1.4006 -0.0852 0.0309  -0.3318 0.1640  0.2546  0.5813  -0.0673 -0.0760 -0.1694 
'X-RAY DIFFRACTION' 12 ? refined 36.3140 79.5130  101.4640 0.3363 0.3116 0.2280 -0.0757 0.0272  0.0103  0.7127 1.3878 2.1333  
0.5072  -0.7318 -0.9628 -0.1679 0.0920  0.0556  -0.2056 0.1427  -0.0094 0.3755  -0.1983 0.0253  
'X-RAY DIFFRACTION' 13 ? refined 4.3570  93.9820  42.8170  0.2748 0.2988 0.2817 -0.0076 0.0376  0.0043  0.5541 1.1616 1.1983  
0.3217  0.1261  0.5121  0.0836  -0.0690 0.0100  0.0553  -0.0486 0.0149  -0.1109 -0.0794 -0.0350 
'X-RAY DIFFRACTION' 14 ? refined 43.0100 93.5360  45.2220  0.2429 0.3125 0.2646 0.0004  0.0045  -0.0052 0.6400 1.1254 2.0804  
0.2251  0.3216  0.6816  0.0013  -0.0196 0.0683  0.0852  -0.0039 0.0047  0.0269  0.0291  0.0026  
'X-RAY DIFFRACTION' 15 ? refined -2.3960 80.0770  98.5420  0.2647 0.2987 0.2771 -0.0088 -0.0144 0.0271  0.4975 1.2445 1.5452  
0.2732  -0.3589 -0.4334 -0.0106 0.0381  -0.0258 -0.0029 0.1030  0.0164  0.0964  -0.1063 -0.0925 
'X-RAY DIFFRACTION' 16 ? refined 52.9600 148.0460 62.4030  0.2947 0.2789 0.2908 -0.0273 -0.0225 -0.0200 0.7298 2.5633 0.6707  
0.8405  0.0257  0.6937  -0.0812 0.0371  0.0803  -0.2901 0.0942  -0.0203 -0.0679 0.0490  -0.0130 
'X-RAY DIFFRACTION' 17 ? refined -4.2370 139.6470 110.6090 0.2764 0.2448 0.3060 0.0229  -0.0236 -0.0213 0.5893 3.2359 0.7857  
-0.2782 -0.1541 0.3645  0.0038  0.0075  -0.0058 0.2012  -0.0117 -0.1268 0.0239  0.0224  0.0079  
'X-RAY DIFFRACTION' 18 ? refined 9.3360  120.9760 59.7200  0.2026 0.3138 0.2948 -0.0036 0.0290  -0.0780 1.9343 3.5719 1.6670  
1.5771  0.5156  0.3822  -0.0159 -0.3621 0.2038  -0.1528 -0.1964 0.2927  0.0223  -0.1673 0.2122  
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1  1  A 1 ? ? A 153 ? ? ? ? 
'X-RAY DIFFRACTION' 2  2  B 1 ? ? B 153 ? ? ? ? 
'X-RAY DIFFRACTION' 3  3  C 1 ? ? C 153 ? ? ? ? 
'X-RAY DIFFRACTION' 4  4  D 1 ? ? D 153 ? ? ? ? 
'X-RAY DIFFRACTION' 5  5  E 1 ? ? E 153 ? ? ? ? 
'X-RAY DIFFRACTION' 6  6  F 3 ? ? F 153 ? ? ? ? 
'X-RAY DIFFRACTION' 7  7  G 1 ? ? G 153 ? ? ? ? 
'X-RAY DIFFRACTION' 8  8  O 1 ? ? O 153 ? ? ? ? 
'X-RAY DIFFRACTION' 9  9  S 1 ? ? S 153 ? ? ? ? 
'X-RAY DIFFRACTION' 10 10 P 1 ? ? P 153 ? ? ? ? 
'X-RAY DIFFRACTION' 11 11 Q 1 ? ? Q 153 ? ? ? ? 
'X-RAY DIFFRACTION' 12 12 H 1 ? ? H 153 ? ? ? ? 
'X-RAY DIFFRACTION' 13 13 I 1 ? ? I 153 ? ? ? ? 
'X-RAY DIFFRACTION' 14 14 J 1 ? ? J 153 ? ? ? ? 
'X-RAY DIFFRACTION' 15 15 K 1 ? ? K 153 ? ? ? ? 
'X-RAY DIFFRACTION' 16 16 L 2 ? ? L 153 ? ? ? ? 
'X-RAY DIFFRACTION' 17 17 M 2 ? ? M 153 ? ? ? ? 
'X-RAY DIFFRACTION' 18 18 N 1 ? ? N 153 ? ? ? ? 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC   refinement       5.0 ? 1 
HKL-2000 'data reduction' .   ? 2 
HKL-2000 'data scaling'   .   ? 3 
MOLREP   phasing          .   ? 4 
# 
_pdbx_database_remark.id     700 
_pdbx_database_remark.text   
;
SHEET
DETERMINATION METHOD: DSSP
THE SHEETS PRESENTED AS "FA" IN EACH CHAIN ON SHEET RECORDS
BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY
A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
ARE IDENTICAL.

THE SHEETS PRESENTED AS "PA" IN EACH CHAIN ON SHEET RECORDS
BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY
A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
ARE IDENTICAL.
;
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 OD1 N ASP 90   ? ? OD1 N ASP 92   ? ? 1.47 
2  1 O   J GLN 153  ? ? OD1 S ASP 92   ? ? 1.68 
3  1 OD1 B ASN 53   ? ? O   B HOH 2071 ? ? 1.76 
4  1 NZ  J LYS 3    ? ? OD2 S ASP 92   ? ? 1.97 
5  1 NH1 B ARG 69   ? ? OE1 B GLU 78   ? ? 2.06 
6  1 NH2 B ARG 69   ? ? OE2 B GLU 77   ? ? 2.07 
7  1 OE2 N GLU 133  ? ? O   N HOH 2076 ? ? 2.08 
8  1 O   J HOH 2046 ? ? O   J HOH 2109 ? ? 2.10 
9  1 O   A HOH 2080 ? ? O   A HOH 2081 ? ? 2.12 
10 1 NH2 O ARG 79   ? ? OD1 O ASP 101  ? ? 2.17 
11 1 O   O GLU 24   ? ? N   O ASN 26   ? ? 2.18 
12 1 OE1 K GLU 100  ? ? O   K HOH 2100 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O  M THR 54   ? ? 1_555 OE2 S GLU 132  ? ? 1_456 1.86 
2 1 NZ B LYS 122  ? ? 1_555 OE2 M GLU 40   ? ? 2_546 1.92 
3 1 O  C HOH 2120 ? ? 1_555 O   H HOH 2064 ? ? 1_554 2.06 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 CB  A ASP 96  ? ? CG A ASP 96  ? ? OD2 A ASP 96  ? ? 124.31 118.30 6.01  0.90 N 
2  1 CB  A ASP 109 ? ? CG A ASP 109 ? ? OD2 A ASP 109 ? ? 124.54 118.30 6.24  0.90 N 
3  1 CG1 B VAL 31  ? ? CB B VAL 31  ? ? CG2 B VAL 31  ? ? 121.57 110.90 10.67 1.60 N 
4  1 CB  B ASP 109 ? ? CG B ASP 109 ? ? OD2 B ASP 109 ? ? 123.91 118.30 5.61  0.90 N 
5  1 CB  C ASP 101 ? ? CG C ASP 101 ? ? OD2 C ASP 101 ? ? 124.40 118.30 6.10  0.90 N 
6  1 CG1 D VAL 31  ? ? CB D VAL 31  ? ? CG2 D VAL 31  ? ? 122.08 110.90 11.18 1.60 N 
7  1 NE  D ARG 79  ? ? CZ D ARG 79  ? ? NH1 D ARG 79  ? ? 123.73 120.30 3.43  0.50 N 
8  1 NE  D ARG 79  ? ? CZ D ARG 79  ? ? NH2 D ARG 79  ? ? 114.37 120.30 -5.93 0.50 N 
9  1 NE  F ARG 79  ? ? CZ F ARG 79  ? ? NH1 F ARG 79  ? ? 123.49 120.30 3.19  0.50 N 
10 1 NE  F ARG 79  ? ? CZ F ARG 79  ? ? NH2 F ARG 79  ? ? 115.62 120.30 -4.68 0.50 N 
11 1 CB  F ASP 101 ? ? CG F ASP 101 ? ? OD2 F ASP 101 ? ? 125.07 118.30 6.77  0.90 N 
12 1 CB  G ASP 83  ? ? CG G ASP 83  ? ? OD2 G ASP 83  ? ? 123.73 118.30 5.43  0.90 N 
13 1 CB  I ASP 96  ? ? CG I ASP 96  ? ? OD2 I ASP 96  ? ? 124.58 118.30 6.28  0.90 N 
14 1 CB  I ASP 101 ? ? CG I ASP 101 ? ? OD2 I ASP 101 ? ? 124.18 118.30 5.88  0.90 N 
15 1 CB  I ASP 109 ? ? CG I ASP 109 ? ? OD2 I ASP 109 ? ? 123.94 118.30 5.64  0.90 N 
16 1 CB  L ASP 76  ? ? CG L ASP 76  ? ? OD2 L ASP 76  ? ? 124.44 118.30 6.14  0.90 N 
17 1 CB  L ASP 92  ? ? CG L ASP 92  ? ? OD2 L ASP 92  ? ? 123.77 118.30 5.47  0.90 N 
18 1 CB  M ASP 109 ? ? CG M ASP 109 ? ? OD2 M ASP 109 ? ? 123.87 118.30 5.57  0.90 N 
19 1 CB  M ASP 124 ? ? CG M ASP 124 ? ? OD1 M ASP 124 ? ? 123.95 118.30 5.65  0.90 N 
20 1 NE  N ARG 79  ? ? CZ N ARG 79  ? ? NH2 N ARG 79  ? ? 116.93 120.30 -3.37 0.50 N 
21 1 CB  O ASP 83  ? ? CG O ASP 83  ? ? OD2 O ASP 83  ? ? 123.78 118.30 5.48  0.90 N 
22 1 NE  Q ARG 79  ? ? CZ Q ARG 79  ? ? NH1 Q ARG 79  ? ? 123.43 120.30 3.13  0.50 N 
23 1 NE  Q ARG 79  ? ? CZ Q ARG 79  ? ? NH2 Q ARG 79  ? ? 114.96 120.30 -5.34 0.50 N 
24 1 CB  Q ASP 101 ? ? CG Q ASP 101 ? ? OD2 Q ASP 101 ? ? 124.06 118.30 5.76  0.90 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 65  ? ? -154.33 65.58   
2  1 ASN C 26  ? ? 67.09   -4.95   
3  1 ASN D 26  ? ? 58.69   4.68    
4  1 ASN D 65  ? ? -151.65 65.73   
5  1 ASN E 26  ? ? 70.71   -0.19   
6  1 ASN E 65  ? ? -151.64 67.36   
7  1 ASN G 65  ? ? -160.29 73.36   
8  1 ASN G 131 ? ? 1.84    155.03  
9  1 SER G 142 ? ? -49.95  156.12  
10 1 ASN H 65  ? ? -150.80 60.76   
11 1 ASN K 26  ? ? 59.47   5.04    
12 1 SER O 25  ? ? -49.53  35.77   
13 1 ASN O 26  ? ? 169.07  -5.59   
14 1 ASN O 65  ? ? -153.18 77.53   
15 1 ASP P 90  ? ? -79.64  -169.18 
16 1 THR Q 2   ? ? -23.76  129.50  
17 1 GLU Q 24  ? ? -116.15 -122.30 
18 1 ASN S 65  ? ? -150.09 55.60   
19 1 ARG S 115 ? ? -101.87 -167.74 
20 1 SER S 142 ? ? -44.88  153.02  
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 2014 ? 6.66 . 
2 1 O ? B HOH 2027 ? 7.08 . 
3 1 O ? D HOH 2019 ? 6.53 . 
4 1 O ? E HOH 2013 ? 6.24 . 
5 1 O ? K HOH 2017 ? 6.16 . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 C LYS 30  ? NZ  ? C LYS 30  NZ  
2   1 Y 1 D ASP 11  ? CG  ? D ASP 11  CG  
3   1 Y 1 D ASP 11  ? OD1 ? D ASP 11  OD1 
4   1 Y 1 D ASP 11  ? OD2 ? D ASP 11  OD2 
5   1 Y 1 D GLN 15  ? OE1 ? D GLN 15  OE1 
6   1 Y 1 D GLU 24  ? CG  ? D GLU 24  CG  
7   1 Y 1 D GLU 24  ? CD  ? D GLU 24  CD  
8   1 Y 1 D GLU 24  ? OE1 ? D GLU 24  OE1 
9   1 Y 1 D GLU 24  ? OE2 ? D GLU 24  OE2 
10  1 Y 1 D LYS 30  ? NZ  ? D LYS 30  NZ  
11  1 Y 1 D LYS 70  ? CD  ? D LYS 70  CD  
12  1 Y 1 D LYS 70  ? CE  ? D LYS 70  CE  
13  1 Y 1 D LYS 70  ? NZ  ? D LYS 70  NZ  
14  1 Y 1 D LYS 122 ? CE  ? D LYS 122 CE  
15  1 Y 1 D LYS 122 ? NZ  ? D LYS 122 NZ  
16  1 Y 1 D LYS 136 ? CE  ? D LYS 136 CE  
17  1 Y 1 D LYS 136 ? NZ  ? D LYS 136 NZ  
18  1 Y 1 E LYS 3   ? CE  ? E LYS 3   CE  
19  1 Y 1 E LYS 3   ? NZ  ? E LYS 3   NZ  
20  1 Y 1 E GLN 15  ? OE1 ? E GLN 15  OE1 
21  1 Y 1 E GLN 15  ? NE2 ? E GLN 15  NE2 
22  1 Y 1 E LYS 23  ? CE  ? E LYS 23  CE  
23  1 Y 1 E LYS 23  ? NZ  ? E LYS 23  NZ  
24  1 Y 1 E LYS 70  ? NZ  ? E LYS 70  NZ  
25  1 Y 1 E LYS 75  ? CE  ? E LYS 75  CE  
26  1 Y 1 E LYS 75  ? NZ  ? E LYS 75  NZ  
27  1 Y 1 E GLU 77  ? OE1 ? E GLU 77  OE1 
28  1 Y 1 E GLU 77  ? OE2 ? E GLU 77  OE2 
29  1 Y 1 E LYS 91  ? NZ  ? E LYS 91  NZ  
30  1 Y 1 E SER 107 ? OG  ? E SER 107 OG  
31  1 Y 1 E GLU 132 ? CD  ? E GLU 132 CD  
32  1 Y 1 E GLU 132 ? OE1 ? E GLU 132 OE1 
33  1 Y 1 E GLU 132 ? OE2 ? E GLU 132 OE2 
34  1 Y 1 F LYS 3   ? N   ? F LYS 3   N   
35  1 Y 1 F LYS 3   ? CA  ? F LYS 3   CA  
36  1 Y 1 F LYS 3   ? CB  ? F LYS 3   CB  
37  1 Y 1 F LYS 3   ? CG  ? F LYS 3   CG  
38  1 Y 1 F LYS 3   ? CD  ? F LYS 3   CD  
39  1 Y 1 F LYS 3   ? CE  ? F LYS 3   CE  
40  1 Y 1 F LYS 3   ? NZ  ? F LYS 3   NZ  
41  1 Y 1 F GLN 15  ? CD  ? F GLN 15  CD  
42  1 Y 1 F GLN 15  ? OE1 ? F GLN 15  OE1 
43  1 Y 1 F GLN 15  ? NE2 ? F GLN 15  NE2 
44  1 Y 1 F GLU 21  ? C   ? F GLU 21  C   
45  1 Y 1 F GLU 21  ? O   ? F GLU 21  O   
46  1 Y 1 F GLU 21  ? CD  ? F GLU 21  CD  
47  1 Y 1 F GLU 21  ? OE1 ? F GLU 21  OE1 
48  1 Y 1 F GLU 21  ? OE2 ? F GLU 21  OE2 
49  1 Y 1 F LYS 36  ? CG  ? F LYS 36  CG  
50  1 Y 1 F LYS 36  ? CD  ? F LYS 36  CD  
51  1 Y 1 F LYS 36  ? CE  ? F LYS 36  CE  
52  1 Y 1 F LYS 36  ? NZ  ? F LYS 36  NZ  
53  1 Y 1 F LYS 70  ? CD  ? F LYS 70  CD  
54  1 Y 1 F LYS 70  ? CE  ? F LYS 70  CE  
55  1 Y 1 F LYS 70  ? NZ  ? F LYS 70  NZ  
56  1 Y 1 J LYS 23  ? CD  ? J LYS 23  CD  
57  1 Y 1 J LYS 23  ? CE  ? J LYS 23  CE  
58  1 Y 1 J LYS 23  ? NZ  ? J LYS 23  NZ  
59  1 Y 1 J LYS 30  ? CE  ? J LYS 30  CE  
60  1 Y 1 J LYS 30  ? NZ  ? J LYS 30  NZ  
61  1 Y 1 J LYS 128 ? NZ  ? J LYS 128 NZ  
62  1 Y 1 J LYS 136 ? CE  ? J LYS 136 CE  
63  1 Y 1 J LYS 136 ? NZ  ? J LYS 136 NZ  
64  1 Y 1 K GLN 15  ? CD  ? K GLN 15  CD  
65  1 Y 1 K GLN 15  ? OE1 ? K GLN 15  OE1 
66  1 Y 1 K GLN 15  ? NE2 ? K GLN 15  NE2 
67  1 Y 1 K LYS 136 ? NZ  ? K LYS 136 NZ  
68  1 Y 1 L LYS 3   ? CD  ? L LYS 3   CD  
69  1 Y 1 L LYS 3   ? CE  ? L LYS 3   CE  
70  1 Y 1 L LYS 3   ? NZ  ? L LYS 3   NZ  
71  1 Y 1 L LYS 9   ? NZ  ? L LYS 9   NZ  
72  1 Y 1 L GLN 15  ? CD  ? L GLN 15  CD  
73  1 Y 1 L GLN 15  ? OE1 ? L GLN 15  OE1 
74  1 Y 1 L GLN 15  ? NE2 ? L GLN 15  NE2 
75  1 Y 1 L LYS 91  ? CE  ? L LYS 91  CE  
76  1 Y 1 L LYS 91  ? NZ  ? L LYS 91  NZ  
77  1 Y 1 M THR 2   ? N   ? M THR 2   N   
78  1 Y 1 M THR 2   ? CA  ? M THR 2   CA  
79  1 Y 1 M THR 2   ? CB  ? M THR 2   CB  
80  1 Y 1 M THR 2   ? OG1 ? M THR 2   OG1 
81  1 Y 1 M THR 2   ? CG2 ? M THR 2   CG2 
82  1 Y 1 M GLN 15  ? OE1 ? M GLN 15  OE1 
83  1 Y 1 M GLN 15  ? NE2 ? M GLN 15  NE2 
84  1 Y 1 M GLU 24  ? CA  ? M GLU 24  CA  
85  1 Y 1 M GLU 24  ? CB  ? M GLU 24  CB  
86  1 Y 1 M GLU 24  ? CG  ? M GLU 24  CG  
87  1 Y 1 M GLU 24  ? CD  ? M GLU 24  CD  
88  1 Y 1 M GLU 24  ? OE1 ? M GLU 24  OE1 
89  1 Y 1 M GLU 24  ? OE2 ? M GLU 24  OE2 
90  1 Y 1 M SER 25  ? CB  ? M SER 25  CB  
91  1 Y 1 M SER 25  ? OG  ? M SER 25  OG  
92  1 Y 1 M ASN 26  ? CB  ? M ASN 26  CB  
93  1 Y 1 M ASN 26  ? CG  ? M ASN 26  CG  
94  1 Y 1 M ASN 26  ? OD1 ? M ASN 26  OD1 
95  1 Y 1 M ASN 26  ? ND2 ? M ASN 26  ND2 
96  1 Y 1 M LYS 30  ? CE  ? M LYS 30  CE  
97  1 Y 1 M LYS 30  ? NZ  ? M LYS 30  NZ  
98  1 Y 1 M LYS 36  ? CE  ? M LYS 36  CE  
99  1 Y 1 M LYS 36  ? NZ  ? M LYS 36  NZ  
100 1 Y 1 M LYS 70  ? CD  ? M LYS 70  CD  
101 1 Y 1 M LYS 70  ? CE  ? M LYS 70  CE  
102 1 Y 1 M LYS 70  ? NZ  ? M LYS 70  NZ  
103 1 Y 1 M LYS 75  ? CD  ? M LYS 75  CD  
104 1 Y 1 M LYS 75  ? CE  ? M LYS 75  CE  
105 1 Y 1 M LYS 75  ? NZ  ? M LYS 75  NZ  
106 1 Y 1 M LYS 136 ? NZ  ? M LYS 136 NZ  
107 1 Y 1 P LYS 75  ? CE  ? P LYS 75  CE  
108 1 Y 1 P LYS 75  ? NZ  ? P LYS 75  NZ  
109 1 Y 1 P LYS 122 ? NZ  ? P LYS 122 NZ  
110 1 Y 1 P GLU 132 ? CA  ? P GLU 132 CA  
111 1 Y 1 P GLU 132 ? CB  ? P GLU 132 CB  
112 1 Y 1 P GLU 132 ? CG  ? P GLU 132 CG  
113 1 Y 1 P GLU 132 ? CD  ? P GLU 132 CD  
114 1 Y 1 P GLU 132 ? OE1 ? P GLU 132 OE1 
115 1 Y 1 P GLU 132 ? OE2 ? P GLU 132 OE2 
116 1 Y 1 S LYS 70  ? CE  ? R LYS 70  CE  
117 1 Y 1 S LYS 70  ? NZ  ? R LYS 70  NZ  
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 E GLY 108 ? E GLY 108 
2  1 Y 1 E ASP 109 ? E ASP 109 
3  1 Y 1 F ALA 1   ? F ALA 1   
4  1 Y 1 F THR 2   ? F THR 2   
5  1 Y 1 F GLN 22  ? F GLN 22  
6  1 Y 1 F LYS 23  ? F LYS 23  
7  1 Y 1 F GLU 24  ? F GLU 24  
8  1 Y 1 F SER 25  ? F SER 25  
9  1 Y 1 F ASN 26  ? F ASN 26  
10 1 Y 1 F GLY 27  ? F GLY 27  
11 1 Y 1 L ALA 1   ? L ALA 1   
12 1 Y 1 M ALA 1   ? M ALA 1   
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'COPPER (II) ION' CU  
3 'ZINC ION'        ZN  
4 'CALCIUM ION'     CA  
5 water             HOH 
# 
