data_3KH3
# 
_entry.id   3KH3 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.281 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3KH3         
RCSB  RCSB055984   
WWPDB D_1000055984 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          3KH4 
_pdbx_database_related.details        'P6522 crystal form' 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.entry_id                        3KH3 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.recvd_initial_deposition_date   2009-10-30 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Gazdag, E.M.'     1 
'Blankenfeldt, W.' 2 
# 
_citation.id                        primary 
_citation.title                     
'Purification and crystallization of human Cu/Zn superoxide dismutase recombinantly produced in the protozoan Leishmania tarentolae.' 
_citation.journal_abbrev            'Acta Crystallogr.,Sect.F' 
_citation.journal_volume            66 
_citation.page_first                871 
_citation.page_last                 877 
_citation.year                      2010 
_citation.journal_id_ASTM           ? 
_citation.country                   DK 
_citation.journal_id_ISSN           1744-3091 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   20693657 
_citation.pdbx_database_id_DOI      10.1107/S1744309110019330 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Gazdag, E.M.'     1 
primary 'Cirstea, I.C.'    2 
primary 'Breitling, R.'    3 
primary 'Lukes, J.'        4 
primary 'Blankenfeldt, W.' 5 
primary 'Alexandrov, K.'   6 
# 
_cell.entry_id           3KH3 
_cell.length_a           75.500 
_cell.length_b           166.610 
_cell.length_c           174.980 
_cell.angle_alpha        90.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.pdbx_unique_axis   ? 
_cell.Z_PDB              48 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         3KH3 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.space_group_name_Hall            ? 
# 
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 [Cu-Zn]' 15827.561 12 1.15.1.1 ? ? ? 
2 non-polymer syn 'COPPER (II) ION'              63.546    12 ?        ? ? ? 
3 non-polymer syn 'ZINC ION'                     65.409    12 ?        ? ? ? 
4 non-polymer syn 'SULFATE ION'                  96.063    3  ?        ? ? ? 
# 
_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 
_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                 SOD1 
_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      'Leishmania tarentolae' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     5689 
_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               P10 
_entity_src_gen.pdbx_host_org_variant              ? 
_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          'chromosomal integration' 
_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.pdbx_db_accession          P00441 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_struct_ref.pdbx_align_begin           2 
_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 3KH3 A 1 ? 153 ? P00441 2 ? 154 ? 2 154 
2  1 3KH3 B 1 ? 153 ? P00441 2 ? 154 ? 2 154 
3  1 3KH3 C 1 ? 153 ? P00441 2 ? 154 ? 2 154 
4  1 3KH3 D 1 ? 153 ? P00441 2 ? 154 ? 2 154 
5  1 3KH3 E 1 ? 153 ? P00441 2 ? 154 ? 2 154 
6  1 3KH3 F 1 ? 153 ? P00441 2 ? 154 ? 2 154 
7  1 3KH3 G 1 ? 153 ? P00441 2 ? 154 ? 2 154 
8  1 3KH3 H 1 ? 153 ? P00441 2 ? 154 ? 2 154 
9  1 3KH3 I 1 ? 153 ? P00441 2 ? 154 ? 2 154 
10 1 3KH3 J 1 ? 153 ? P00441 2 ? 154 ? 2 154 
11 1 3KH3 K 1 ? 153 ? P00441 2 ? 154 ? 2 154 
12 1 3KH3 L 1 ? 153 ? P00441 2 ? 154 ? 2 154 
# 
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 
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 
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 
SO4 non-polymer         . 'SULFATE ION'     ? 'O4 S -2'        96.063  
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.crystals_number   1 
_exptl.entry_id          3KH3 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_percent_sol   57.55 
_exptl_crystal.density_Matthews      2.90 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    
'21-25% (w/v) PEG4000, 0.1 M NaOAc, pH 4.2-5.2, vapor diffusion, hanging drop, temperature 292K' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   4.2-5.2 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'MARMOSAIC 225 mm CCD' 
_diffrn_detector.pdbx_collection_date   2008-10-11 
_diffrn_detector.details                'SI(111)' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    'SI(111) MONOCHROMATOR' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9797 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SLS BEAMLINE X10SA' 
_diffrn_source.pdbx_wavelength_list        0.9797 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_site       SLS 
_diffrn_source.pdbx_synchrotron_beamline   X10SA 
# 
_reflns.entry_id                     3KH3 
_reflns.d_resolution_high            3.500 
_reflns.number_obs                   28607 
_reflns.pdbx_Rmerge_I_obs            0.189 
_reflns.pdbx_netI_over_sigmaI        11.160 
_reflns.percent_possible_obs         99.900 
_reflns.B_iso_Wilson_estimate        42.624 
_reflns.observed_criterion_sigma_I   -3.00 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             50.00 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_redundancy              ? 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.number_unique_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
3.50  3.60  14373 ? 2306 0.575 4.3  ? ? ? ? ? 100.00 ? 1  
3.60  3.70  12416 ? 1999 0.463 5.4  ? ? ? ? ? 100.00 ? 2  
3.70  3.80  11683 ? 1874 0.424 5.6  ? ? ? ? ? 99.90  ? 3  
3.80  3.90  10119 ? 1630 0.365 6.5  ? ? ? ? ? 100.00 ? 4  
3.90  4.00  9253  ? 1485 0.289 7.9  ? ? ? ? ? 100.00 ? 5  
4.00  5.00  57461 ? 9267 0.192 10.6 ? ? ? ? ? 99.90  ? 6  
5.00  6.00  25323 ? 4128 0.157 11.9 ? ? ? ? ? 100.00 ? 7  
6.00  8.00  20271 ? 3353 0.120 14.5 ? ? ? ? ? 100.00 ? 8  
8.00  10.00 7169  ? 1212 0.067 22.1 ? ? ? ? ? 99.90  ? 9  
10.00 15.00 5378  ? 937  0.046 30.0 ? ? ? ? ? 100.00 ? 10 
15.00 30.00 1893  ? 360  0.039 35.2 ? ? ? ? ? 99.70  ? 11 
30.00 50.00 198   ? 47   0.029 36.5 ? ? ? ? ? 95.90  ? 12 
50.00 ?     25    ? 9    0.042 28.9 ? ? ? ? ? 60.00  ? 13 
# 
_refine.entry_id                                 3KH3 
_refine.ls_d_res_high                            3.500 
_refine.ls_d_res_low                             47.780 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.ls_percent_reflns_obs                    99.960 
_refine.ls_number_reflns_obs                     28597 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  
;HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
 U VALUES: RESIDUAL ONLY
;
_refine.ls_R_factor_obs                          0.244 
_refine.ls_R_factor_R_work                       0.243 
_refine.ls_R_factor_R_free                       0.277 
_refine.ls_percent_reflns_R_free                 5.100 
_refine.ls_number_reflns_R_free                  1446 
_refine.B_iso_mean                               75.883 
_refine.aniso_B[1][1]                            0.380 
_refine.aniso_B[2][2]                            4.590 
_refine.aniso_B[3][3]                            -4.970 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.862 
_refine.correlation_coeff_Fo_to_Fc_free          0.811 
_refine.pdbx_overall_ESU_R_Free                  0.692 
_refine.overall_SU_ML                            0.491 
_refine.overall_SU_B                             70.354 
_refine.solvent_model_details                    'BABINET MODEL WITH MASK' 
_refine.pdbx_solvent_vdw_probe_radii             1.400 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.B_iso_max                                277.39 
_refine.B_iso_min                                20.56 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            1.00 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_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        13312 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         39 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               13351 
_refine_hist.d_res_high                       3.500 
_refine_hist.d_res_low                        47.780 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d       13552 0.013  0.021  ? 'X-RAY DIFFRACTION' ? 
r_bond_other_d         8952  0.000  0.020  ? 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg    18296 1.173  1.946  ? 'X-RAY DIFFRACTION' ? 
r_angle_other_deg      22042 4.443  3.000  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg 1824  6.284  5.000  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg 575   39.026 25.652 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg 2216  16.443 15.000 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg 47    10.638 15.000 ? 'X-RAY DIFFRACTION' ? 
r_chiral_restr         2015  0.062  0.200  ? 'X-RAY DIFFRACTION' ? 
r_gen_planes_refined   15631 0.004  0.020  ? 'X-RAY DIFFRACTION' ? 
r_gen_planes_other     2444  0.003  0.020  ? 'X-RAY DIFFRACTION' ? 
r_mcbond_it            8940  0.147  1.500  ? 'X-RAY DIFFRACTION' ? 
r_mcbond_other         3900  0.000  1.500  ? 'X-RAY DIFFRACTION' ? 
r_mcangle_it           14205 0.270  2.000  ? 'X-RAY DIFFRACTION' ? 
r_scbond_it            4612  0.368  3.000  ? 'X-RAY DIFFRACTION' ? 
r_scangle_it           4091  0.651  4.500  ? 'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_ens_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.weight_B_iso 
1 1 'MEDIUM POSITIONAL' A 1825 0.030 0.500 1  'X-RAY DIFFRACTION' ? ? ? 
1 1 'MEDIUM POSITIONAL' B 1825 0.030 0.500 2  'X-RAY DIFFRACTION' ? ? ? 
1 1 'MEDIUM POSITIONAL' C 1825 0.040 0.500 3  'X-RAY DIFFRACTION' ? ? ? 
1 1 'MEDIUM POSITIONAL' E 1825 0.040 0.500 4  'X-RAY DIFFRACTION' ? ? ? 
1 1 'MEDIUM POSITIONAL' F 1825 0.030 0.500 5  'X-RAY DIFFRACTION' ? ? ? 
1 1 'MEDIUM POSITIONAL' G 1825 0.040 0.500 6  'X-RAY DIFFRACTION' ? ? ? 
1 1 'MEDIUM POSITIONAL' H 1825 0.040 0.500 7  'X-RAY DIFFRACTION' ? ? ? 
1 1 'MEDIUM POSITIONAL' I 1825 0.030 0.500 8  'X-RAY DIFFRACTION' ? ? ? 
1 1 'MEDIUM POSITIONAL' J 1825 0.040 0.500 9  'X-RAY DIFFRACTION' ? ? ? 
1 1 'MEDIUM POSITIONAL' K 1825 0.040 0.500 10 'X-RAY DIFFRACTION' ? ? ? 
1 1 'MEDIUM POSITIONAL' L 1825 0.030 0.500 11 'X-RAY DIFFRACTION' ? ? ? 
1 1 'MEDIUM THERMAL'    A 1825 0.060 2.000 12 'X-RAY DIFFRACTION' ? ? ? 
1 1 'MEDIUM THERMAL'    B 1825 0.080 2.000 13 'X-RAY DIFFRACTION' ? ? ? 
1 1 'MEDIUM THERMAL'    C 1825 0.070 2.000 14 'X-RAY DIFFRACTION' ? ? ? 
1 1 'MEDIUM THERMAL'    E 1825 0.100 2.000 15 'X-RAY DIFFRACTION' ? ? ? 
1 1 'MEDIUM THERMAL'    F 1825 0.070 2.000 16 'X-RAY DIFFRACTION' ? ? ? 
1 1 'MEDIUM THERMAL'    G 1825 0.080 2.000 17 'X-RAY DIFFRACTION' ? ? ? 
1 1 'MEDIUM THERMAL'    H 1825 0.070 2.000 18 'X-RAY DIFFRACTION' ? ? ? 
1 1 'MEDIUM THERMAL'    I 1825 0.060 2.000 19 'X-RAY DIFFRACTION' ? ? ? 
1 1 'MEDIUM THERMAL'    J 1825 0.080 2.000 20 'X-RAY DIFFRACTION' ? ? ? 
1 1 'MEDIUM THERMAL'    K 1825 0.090 2.000 21 'X-RAY DIFFRACTION' ? ? ? 
1 1 'MEDIUM THERMAL'    L 1825 0.060 2.000 22 'X-RAY DIFFRACTION' ? ? ? 
# 
_refine_ls_shell.d_res_high                       3.500 
_refine_ls_shell.d_res_low                        3.590 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               100.000 
_refine_ls_shell.number_reflns_R_work             1993 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.281 
_refine_ls_shell.R_factor_R_free                  0.311 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             107 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                2100 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
loop_
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.id 
_struct_ncs_dom.details 
1 1  A 
1 2  B 
1 3  C 
1 4  E 
1 5  F 
1 6  G 
1 7  H 
1 8  I 
1 9  J 
1 10 K 
1 11 L 
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.selection_details 
1 1  1 A 3 A 155 4 . . . . A 3 A 155 ? 
1 2  1 B 3 B 155 4 . . . . B 3 B 155 ? 
1 3  1 C 3 C 155 4 . . . . C 3 C 155 ? 
1 4  1 E 3 E 155 4 . . . . E 3 E 155 ? 
1 5  1 F 3 F 155 4 . . . . F 3 F 155 ? 
1 6  1 G 3 G 155 4 . . . . G 3 G 155 ? 
1 7  1 H 3 H 155 4 . . . . H 3 H 155 ? 
1 8  1 I 3 I 155 4 . . . . I 3 I 155 ? 
1 9  1 J 3 J 155 4 . . . . J 3 J 155 ? 
1 10 1 K 3 K 155 4 . . . . K 3 K 155 ? 
1 11 1 L 3 L 155 4 . . . . L 3 L 155 ? 
# 
_struct_ncs_ens.id        1 
_struct_ncs_ens.details   ? 
# 
_struct.entry_id                  3KH3 
_struct.title                     
;Crystal structure of human Cu/Zn superoxide dismutase recombinantly produced in Leishmania tarantolae; P212121 crystal form containing 12 chains in the asymmetric unit
;
_struct.pdbx_descriptor           'Superoxide dismutase [Cu-Zn] (E.C.1.15.1.1)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3KH3 
_struct_keywords.text            
;eukaryotic expression, Leishmania tarantolae, Amyotrophic lateral sclerosis, Antioxidant, Disease mutation, Disulfide bond, Metal-binding, Neurodegeneration, Oxidoreductase, Phosphoprotein
;
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
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 2 ? 
N  N N 3 ? 
O  N N 2 ? 
P  N N 3 ? 
Q  N N 4 ? 
R  N N 4 ? 
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 2 ? 
Z  N N 3 ? 
AA N N 2 ? 
BA N N 3 ? 
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 4 ? 
JA N N 2 ? 
KA N N 3 ? 
LA N N 2 ? 
MA N N 3 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
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  CYS A 57  ? GLY A 61  ? CYS A 58  GLY A 62  5 ? 5 
HELX_P HELX_P2  2  GLU A 132 ? LYS A 136 ? GLU A 133 LYS A 137 5 ? 5 
HELX_P HELX_P3  3  CYS B 57  ? GLY B 61  ? CYS B 58  GLY B 62  5 ? 5 
HELX_P HELX_P4  4  GLU B 132 ? LYS B 136 ? GLU B 133 LYS B 137 5 ? 5 
HELX_P HELX_P5  5  CYS C 57  ? GLY C 61  ? CYS C 58  GLY C 62  5 ? 5 
HELX_P HELX_P6  6  GLU C 132 ? LYS C 136 ? GLU C 133 LYS C 137 5 ? 5 
HELX_P HELX_P7  7  GLY D 56  ? GLY D 61  ? GLY D 57  GLY D 62  1 ? 6 
HELX_P HELX_P8  8  ALA E 55  ? GLY E 61  ? ALA E 56  GLY E 62  5 ? 7 
HELX_P HELX_P9  9  GLU E 132 ? LYS E 136 ? GLU E 133 LYS E 137 5 ? 5 
HELX_P HELX_P10 10 CYS F 57  ? GLY F 61  ? CYS F 58  GLY F 62  5 ? 5 
HELX_P HELX_P11 11 GLU F 132 ? LYS F 136 ? GLU F 133 LYS F 137 5 ? 5 
HELX_P HELX_P12 12 CYS G 57  ? GLY G 61  ? CYS G 58  GLY G 62  5 ? 5 
HELX_P HELX_P13 13 GLU G 132 ? LYS G 136 ? GLU G 133 LYS G 137 5 ? 5 
HELX_P HELX_P14 14 CYS H 57  ? GLY H 61  ? CYS H 58  GLY H 62  5 ? 5 
HELX_P HELX_P15 15 GLU H 132 ? LYS H 136 ? GLU H 133 LYS H 137 5 ? 5 
HELX_P HELX_P16 16 CYS I 57  ? GLY I 61  ? CYS I 58  GLY I 62  5 ? 5 
HELX_P HELX_P17 17 GLU I 132 ? LYS I 136 ? GLU I 133 LYS I 137 5 ? 5 
HELX_P HELX_P18 18 ALA J 55  ? GLY J 61  ? ALA J 56  GLY J 62  5 ? 7 
HELX_P HELX_P19 19 GLU J 132 ? LYS J 136 ? GLU J 133 LYS J 137 5 ? 5 
HELX_P HELX_P20 20 CYS K 57  ? GLY K 61  ? CYS K 58  GLY K 62  5 ? 5 
HELX_P HELX_P21 21 GLU K 132 ? LYS K 136 ? GLU K 133 LYS K 137 5 ? 5 
HELX_P HELX_P22 22 CYS L 57  ? GLY L 61  ? CYS L 58  GLY L 62  5 ? 5 
HELX_P HELX_P23 23 GLU L 132 ? LYS L 136 ? GLU L 133 LYS L 137 5 ? 5 
# 
_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 58  A CYS 147 1_555 ? ? ? ? ? ? ? 2.030 ? 
disulf2  disulf ? ? B CYS 57  SG  ? ? ? 1_555 B  CYS 146 SG ? ? B CYS 58  B CYS 147 1_555 ? ? ? ? ? ? ? 2.026 ? 
disulf3  disulf ? ? C CYS 57  SG  ? ? ? 1_555 C  CYS 146 SG ? ? C CYS 58  C CYS 147 1_555 ? ? ? ? ? ? ? 2.022 ? 
disulf4  disulf ? ? D CYS 57  SG  ? ? ? 1_555 D  CYS 146 SG ? ? D CYS 58  D CYS 147 1_555 ? ? ? ? ? ? ? 2.070 ? 
disulf5  disulf ? ? E CYS 57  SG  ? ? ? 1_555 E  CYS 146 SG ? ? E CYS 58  E CYS 147 1_555 ? ? ? ? ? ? ? 2.058 ? 
disulf6  disulf ? ? F CYS 57  SG  ? ? ? 1_555 F  CYS 146 SG ? ? F CYS 58  F CYS 147 1_555 ? ? ? ? ? ? ? 2.011 ? 
disulf7  disulf ? ? G CYS 57  SG  ? ? ? 1_555 G  CYS 146 SG ? ? G CYS 58  G CYS 147 1_555 ? ? ? ? ? ? ? 2.060 ? 
disulf8  disulf ? ? H CYS 57  SG  ? ? ? 1_555 H  CYS 146 SG ? ? H CYS 58  H CYS 147 1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf9  disulf ? ? I CYS 57  SG  ? ? ? 1_555 I  CYS 146 SG ? ? I CYS 58  I CYS 147 1_555 ? ? ? ? ? ? ? 2.020 ? 
disulf10 disulf ? ? J CYS 57  SG  ? ? ? 1_555 J  CYS 146 SG ? ? J CYS 58  J CYS 147 1_555 ? ? ? ? ? ? ? 2.019 ? 
disulf11 disulf ? ? K CYS 57  SG  ? ? ? 1_555 K  CYS 146 SG ? ? K CYS 58  K CYS 147 1_555 ? ? ? ? ? ? ? 2.055 ? 
disulf12 disulf ? ? L CYS 57  SG  ? ? ? 1_555 L  CYS 146 SG ? ? L CYS 58  L CYS 147 1_555 ? ? ? ? ? ? ? 2.025 ? 
metalc1  metalc ? ? A HIS 48  NE2 ? ? ? 1_555 M  CU  .   CU A ? A HIS 49  A CU  155 1_555 ? ? ? ? ? ? ? 2.356 ? 
metalc2  metalc ? ? A HIS 63  ND1 ? ? ? 1_555 N  ZN  .   ZN ? ? A HIS 64  A ZN  156 1_555 ? ? ? ? ? ? ? 1.993 ? 
metalc3  metalc ? ? A HIS 71  ND1 ? ? ? 1_555 N  ZN  .   ZN ? ? A HIS 72  A ZN  156 1_555 ? ? ? ? ? ? ? 2.163 ? 
metalc4  metalc ? ? A HIS 80  ND1 ? ? ? 1_555 N  ZN  .   ZN ? ? A HIS 81  A ZN  156 1_555 ? ? ? ? ? ? ? 1.953 ? 
metalc5  metalc ? ? A ASP 83  OD1 ? ? ? 1_555 N  ZN  .   ZN ? ? A ASP 84  A ZN  156 1_555 ? ? ? ? ? ? ? 1.865 ? 
metalc6  metalc ? ? A HIS 120 NE2 ? ? ? 1_555 M  CU  .   CU A ? A HIS 121 A CU  155 1_555 ? ? ? ? ? ? ? 2.378 ? 
metalc7  metalc ? ? B HIS 46  ND1 ? ? ? 1_555 O  CU  .   CU A ? B HIS 47  B CU  155 1_555 ? ? ? ? ? ? ? 2.326 ? 
metalc8  metalc ? ? B HIS 63  ND1 ? ? ? 1_555 P  ZN  .   ZN ? ? B HIS 64  B ZN  156 1_555 ? ? ? ? ? ? ? 1.995 ? 
metalc9  metalc ? ? B HIS 71  ND1 ? ? ? 1_555 P  ZN  .   ZN ? ? B HIS 72  B ZN  156 1_555 ? ? ? ? ? ? ? 2.040 ? 
metalc10 metalc ? ? B HIS 80  ND1 ? ? ? 1_555 P  ZN  .   ZN ? ? B HIS 81  B ZN  156 1_555 ? ? ? ? ? ? ? 2.098 ? 
metalc11 metalc ? ? B HIS 120 NE2 ? ? ? 1_555 O  CU  .   CU A ? B HIS 121 B CU  155 1_555 ? ? ? ? ? ? ? 2.294 ? 
metalc12 metalc ? ? C HIS 46  ND1 ? ? ? 1_555 S  CU  .   CU A ? C HIS 47  C CU  155 1_555 ? ? ? ? ? ? ? 2.034 ? 
metalc13 metalc ? ? C HIS 63  ND1 ? ? ? 1_555 T  ZN  .   ZN ? ? C HIS 64  C ZN  156 1_555 ? ? ? ? ? ? ? 2.167 ? 
metalc14 metalc ? ? C HIS 71  ND1 ? ? ? 1_555 T  ZN  .   ZN ? ? C HIS 72  C ZN  156 1_555 ? ? ? ? ? ? ? 1.991 ? 
metalc15 metalc ? ? C HIS 80  ND1 ? ? ? 1_555 T  ZN  .   ZN ? ? C HIS 81  C ZN  156 1_555 ? ? ? ? ? ? ? 2.030 ? 
metalc16 metalc ? ? C ASP 83  OD1 ? ? ? 1_555 T  ZN  .   ZN ? ? C ASP 84  C ZN  156 1_555 ? ? ? ? ? ? ? 1.815 ? 
metalc17 metalc ? ? D HIS 48  NE2 ? ? ? 1_555 U  CU  .   CU A ? D HIS 49  D CU  155 1_555 ? ? ? ? ? ? ? 2.108 ? 
metalc18 metalc ? ? E HIS 46  ND1 ? ? ? 1_555 W  CU  .   CU A ? E HIS 47  E CU  155 1_555 ? ? ? ? ? ? ? 2.276 ? 
metalc19 metalc ? ? E HIS 80  ND1 ? ? ? 1_555 X  ZN  .   ZN ? ? E HIS 81  E ZN  156 1_555 ? ? ? ? ? ? ? 1.865 ? 
metalc20 metalc ? ? E ASP 83  OD2 ? ? ? 1_555 X  ZN  .   ZN ? ? E ASP 84  E ZN  156 1_555 ? ? ? ? ? ? ? 2.055 ? 
metalc21 metalc ? ? F HIS 46  ND1 ? ? ? 1_555 Y  CU  .   CU A ? F HIS 47  F CU  155 1_555 ? ? ? ? ? ? ? 2.261 ? 
metalc22 metalc ? ? F HIS 63  ND1 ? ? ? 1_555 Z  ZN  .   ZN ? ? F HIS 64  F ZN  156 1_555 ? ? ? ? ? ? ? 2.150 ? 
metalc23 metalc ? ? F HIS 71  ND1 ? ? ? 1_555 Z  ZN  .   ZN ? ? F HIS 72  F ZN  156 1_555 ? ? ? ? ? ? ? 1.830 ? 
metalc24 metalc ? ? F HIS 80  ND1 ? ? ? 1_555 Z  ZN  .   ZN ? ? F HIS 81  F ZN  156 1_555 ? ? ? ? ? ? ? 2.073 ? 
metalc25 metalc ? ? F ASP 83  OD1 ? ? ? 1_555 Z  ZN  .   ZN ? ? F ASP 84  F ZN  156 1_555 ? ? ? ? ? ? ? 1.949 ? 
metalc26 metalc ? ? F HIS 120 NE2 ? ? ? 1_555 Y  CU  .   CU A ? F HIS 121 F CU  155 1_555 ? ? ? ? ? ? ? 2.233 ? 
metalc27 metalc ? ? G HIS 46  ND1 ? ? ? 1_555 AA CU  .   CU A ? G HIS 47  G CU  155 1_555 ? ? ? ? ? ? ? 2.201 ? 
metalc28 metalc ? ? G HIS 63  ND1 ? ? ? 1_555 BA ZN  .   ZN ? ? G HIS 64  G ZN  156 1_555 ? ? ? ? ? ? ? 2.106 ? 
metalc29 metalc ? ? G HIS 71  ND1 ? ? ? 1_555 BA ZN  .   ZN ? ? G HIS 72  G ZN  156 1_555 ? ? ? ? ? ? ? 2.247 ? 
metalc30 metalc ? ? G HIS 80  ND1 ? ? ? 1_555 BA ZN  .   ZN ? ? G HIS 81  G ZN  156 1_555 ? ? ? ? ? ? ? 1.940 ? 
metalc31 metalc ? ? G ASP 83  OD1 ? ? ? 1_555 BA ZN  .   ZN ? ? G ASP 84  G ZN  156 1_555 ? ? ? ? ? ? ? 1.798 ? 
metalc32 metalc ? ? G HIS 120 NE2 ? ? ? 1_555 AA CU  .   CU A ? G HIS 121 G CU  155 1_555 ? ? ? ? ? ? ? 2.326 ? 
metalc33 metalc ? ? H HIS 46  ND1 ? ? ? 1_555 CA CU  .   CU A ? H HIS 47  H CU  155 1_555 ? ? ? ? ? ? ? 2.277 ? 
metalc34 metalc ? ? H HIS 63  ND1 ? ? ? 1_555 DA ZN  .   ZN ? ? H HIS 64  H ZN  156 1_555 ? ? ? ? ? ? ? 2.101 ? 
metalc35 metalc ? ? H HIS 71  ND1 ? ? ? 1_555 DA ZN  .   ZN ? ? H HIS 72  H ZN  156 1_555 ? ? ? ? ? ? ? 1.909 ? 
metalc36 metalc ? ? H HIS 80  ND1 ? ? ? 1_555 DA ZN  .   ZN ? ? H HIS 81  H ZN  156 1_555 ? ? ? ? ? ? ? 2.042 ? 
metalc37 metalc ? ? H ASP 83  OD1 ? ? ? 1_555 DA ZN  .   ZN ? ? H ASP 84  H ZN  156 1_555 ? ? ? ? ? ? ? 2.025 ? 
metalc38 metalc ? ? H HIS 120 NE2 ? ? ? 1_555 CA CU  .   CU A ? H HIS 121 H CU  155 1_555 ? ? ? ? ? ? ? 2.365 ? 
metalc39 metalc ? ? I HIS 46  ND1 ? ? ? 1_555 EA CU  .   CU A ? I HIS 47  I CU  155 1_555 ? ? ? ? ? ? ? 2.264 ? 
metalc40 metalc ? ? I HIS 63  ND1 ? ? ? 1_555 FA ZN  .   ZN ? ? I HIS 64  I ZN  156 1_555 ? ? ? ? ? ? ? 2.174 ? 
metalc41 metalc ? ? I HIS 71  ND1 ? ? ? 1_555 FA ZN  .   ZN ? ? I HIS 72  I ZN  156 1_555 ? ? ? ? ? ? ? 2.013 ? 
metalc42 metalc ? ? I HIS 80  ND1 ? ? ? 1_555 FA ZN  .   ZN ? ? I HIS 81  I ZN  156 1_555 ? ? ? ? ? ? ? 1.984 ? 
metalc43 metalc ? ? I ASP 83  OD1 ? ? ? 1_555 FA ZN  .   ZN ? ? I ASP 84  I ZN  156 1_555 ? ? ? ? ? ? ? 1.881 ? 
metalc44 metalc ? ? I HIS 120 NE2 ? ? ? 1_555 EA CU  .   CU A ? I HIS 121 I CU  155 1_555 ? ? ? ? ? ? ? 2.351 ? 
metalc45 metalc ? ? J HIS 46  ND1 ? ? ? 1_555 GA CU  .   CU A ? J HIS 47  J CU  155 1_555 ? ? ? ? ? ? ? 2.176 ? 
metalc46 metalc ? ? J HIS 63  ND1 ? ? ? 1_555 HA ZN  .   ZN ? ? J HIS 64  J ZN  156 1_555 ? ? ? ? ? ? ? 2.108 ? 
metalc47 metalc ? ? J HIS 71  ND1 ? ? ? 1_555 HA ZN  .   ZN ? ? J HIS 72  J ZN  156 1_555 ? ? ? ? ? ? ? 2.012 ? 
metalc48 metalc ? ? J HIS 80  ND1 ? ? ? 1_555 HA ZN  .   ZN ? ? J HIS 81  J ZN  156 1_555 ? ? ? ? ? ? ? 1.992 ? 
metalc49 metalc ? ? J ASP 83  OD1 ? ? ? 1_555 HA ZN  .   ZN ? ? J ASP 84  J ZN  156 1_555 ? ? ? ? ? ? ? 1.825 ? 
metalc50 metalc ? ? J HIS 120 NE2 ? ? ? 1_555 GA CU  .   CU A ? J HIS 121 J CU  155 1_555 ? ? ? ? ? ? ? 2.387 ? 
metalc51 metalc ? ? K HIS 46  ND1 ? ? ? 1_555 JA CU  .   CU A ? K HIS 47  K CU  155 1_555 ? ? ? ? ? ? ? 2.347 ? 
metalc52 metalc ? ? K HIS 63  ND1 ? ? ? 1_555 KA ZN  .   ZN ? ? K HIS 64  K ZN  156 1_555 ? ? ? ? ? ? ? 2.107 ? 
metalc53 metalc ? ? K HIS 71  ND1 ? ? ? 1_555 KA ZN  .   ZN ? ? K HIS 72  K ZN  156 1_555 ? ? ? ? ? ? ? 2.121 ? 
metalc54 metalc ? ? K HIS 80  ND1 ? ? ? 1_555 KA ZN  .   ZN ? ? K HIS 81  K ZN  156 1_555 ? ? ? ? ? ? ? 1.868 ? 
metalc55 metalc ? ? L HIS 46  ND1 ? ? ? 1_555 LA CU  .   CU A ? L HIS 47  L CU  155 1_555 ? ? ? ? ? ? ? 2.294 ? 
metalc56 metalc ? ? L HIS 48  NE2 ? ? ? 1_555 LA CU  .   CU A ? L HIS 49  L CU  155 1_555 ? ? ? ? ? ? ? 2.297 ? 
metalc57 metalc ? ? L HIS 63  ND1 ? ? ? 1_555 MA ZN  .   ZN ? ? L HIS 64  L ZN  156 1_555 ? ? ? ? ? ? ? 2.001 ? 
metalc58 metalc ? ? L HIS 71  ND1 ? ? ? 1_555 MA ZN  .   ZN ? ? L HIS 72  L ZN  156 1_555 ? ? ? ? ? ? ? 2.010 ? 
metalc59 metalc ? ? L HIS 80  ND1 ? ? ? 1_555 MA ZN  .   ZN ? ? L HIS 81  L ZN  156 1_555 ? ? ? ? ? ? ? 2.153 ? 
metalc60 metalc ? ? L ASP 83  OD1 ? ? ? 1_555 MA ZN  .   ZN ? ? L ASP 84  L ZN  156 1_555 ? ? ? ? ? ? ? 1.704 ? 
metalc61 metalc ? ? B ASP 83  OD1 ? ? ? 1_555 P  ZN  .   ZN ? ? B ASP 84  B ZN  156 1_555 ? ? ? ? ? ? ? 1.727 ? 
metalc62 metalc ? ? E HIS 71  ND1 ? ? ? 1_555 X  ZN  .   ZN ? ? E HIS 72  E ZN  156 1_555 ? ? ? ? ? ? ? 2.400 ? 
metalc63 metalc ? ? D HIS 80  ND1 ? ? ? 1_555 V  ZN  .   ZN ? ? D HIS 81  D ZN  156 1_555 ? ? ? ? ? ? ? 2.427 ? 
metalc64 metalc ? ? A HIS 46  ND1 ? ? ? 1_555 M  CU  .   CU A ? A HIS 47  A CU  155 1_555 ? ? ? ? ? ? ? 2.440 ? 
metalc65 metalc ? ? B HIS 48  NE2 ? ? ? 1_555 O  CU  .   CU A ? B HIS 49  B CU  155 1_555 ? ? ? ? ? ? ? 2.449 ? 
metalc66 metalc ? ? E HIS 48  NE2 ? ? ? 1_555 W  CU  .   CU A ? E HIS 49  E CU  155 1_555 ? ? ? ? ? ? ? 2.461 ? 
metalc67 metalc ? ? C HIS 120 NE2 ? ? ? 1_555 S  CU  .   CU A ? C HIS 121 C CU  155 1_555 ? ? ? ? ? ? ? 2.468 ? 
metalc68 metalc ? ? F HIS 48  NE2 ? ? ? 1_555 Y  CU  .   CU A ? F HIS 49  F CU  155 1_555 ? ? ? ? ? ? ? 2.482 ? 
metalc69 metalc ? ? D ASP 83  OD1 ? ? ? 1_555 V  ZN  .   ZN ? ? D ASP 84  D ZN  156 1_555 ? ? ? ? ? ? ? 2.484 ? 
metalc70 metalc ? ? K ASP 83  OD1 ? ? ? 1_555 KA ZN  .   ZN ? ? K ASP 84  K ZN  156 1_555 ? ? ? ? ? ? ? 2.488 ? 
metalc71 metalc ? ? L HIS 120 NE2 ? ? ? 1_555 LA CU  .   CU A ? L HIS 121 L CU  155 1_555 ? ? ? ? ? ? ? 2.507 ? 
metalc72 metalc ? ? C ASP 83  OD2 ? ? ? 1_555 T  ZN  .   ZN ? ? C ASP 84  C ZN  156 1_555 ? ? ? ? ? ? ? 2.511 ? 
metalc73 metalc ? ? I ASP 83  OD2 ? ? ? 1_555 FA ZN  .   ZN ? ? I ASP 84  I ZN  156 1_555 ? ? ? ? ? ? ? 2.518 ? 
metalc74 metalc ? ? K HIS 120 NE2 ? ? ? 1_555 JA CU  .   CU A ? K HIS 121 K CU  155 1_555 ? ? ? ? ? ? ? 2.524 ? 
metalc75 metalc ? ? F ASP 83  OD2 ? ? ? 1_555 Z  ZN  .   ZN ? ? F ASP 84  F ZN  156 1_555 ? ? ? ? ? ? ? 2.542 ? 
metalc76 metalc ? ? L ASP 83  OD2 ? ? ? 1_555 MA ZN  .   ZN ? ? L ASP 84  L ZN  156 1_555 ? ? ? ? ? ? ? 2.550 ? 
metalc77 metalc ? ? H HIS 48  NE2 ? ? ? 1_555 CA CU  .   CU A ? H HIS 49  H CU  155 1_555 ? ? ? ? ? ? ? 2.554 ? 
metalc78 metalc ? ? J ASP 83  OD2 ? ? ? 1_555 HA ZN  .   ZN ? ? J ASP 84  J ZN  156 1_555 ? ? ? ? ? ? ? 2.555 ? 
metalc79 metalc ? ? J HIS 48  NE2 ? ? ? 1_555 GA CU  .   CU A ? J HIS 49  J CU  155 1_555 ? ? ? ? ? ? ? 2.557 ? 
metalc80 metalc ? ? B ASP 83  OD2 ? ? ? 1_555 P  ZN  .   ZN ? ? B ASP 84  B ZN  156 1_555 ? ? ? ? ? ? ? 2.588 ? 
metalc81 metalc ? ? I HIS 48  NE2 ? ? ? 1_555 EA CU  .   CU A ? I HIS 49  I CU  155 1_555 ? ? ? ? ? ? ? 2.588 ? 
metalc82 metalc ? ? E HIS 120 NE2 ? ? ? 1_555 W  CU  .   CU A ? E HIS 121 E CU  155 1_555 ? ? ? ? ? ? ? 2.596 ? 
metalc83 metalc ? ? G ASP 83  OD2 ? ? ? 1_555 BA ZN  .   ZN ? ? G ASP 84  G ZN  156 1_555 ? ? ? ? ? ? ? 2.608 ? 
metalc84 metalc ? ? K HIS 48  NE2 ? ? ? 1_555 JA CU  .   CU A ? K HIS 49  K CU  155 1_555 ? ? ? ? ? ? ? 2.624 ? 
metalc85 metalc ? ? E HIS 63  ND1 ? ? ? 1_555 X  ZN  .   ZN ? ? E HIS 64  E ZN  156 1_555 ? ? ? ? ? ? ? 2.638 ? 
metalc86 metalc ? ? K HIS 63  NE2 ? ? ? 1_555 JA CU  .   CU A ? K HIS 64  K CU  155 1_555 ? ? ? ? ? ? ? 2.658 ? 
metalc87 metalc ? ? A ASP 83  OD2 ? ? ? 1_555 N  ZN  .   ZN ? ? A ASP 84  A ZN  156 1_555 ? ? ? ? ? ? ? 2.697 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLY 
_struct_mon_prot_cis.label_seq_id           12 
_struct_mon_prot_cis.label_asym_id          D 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           GLY 
_struct_mon_prot_cis.auth_seq_id            13 
_struct_mon_prot_cis.auth_asym_id           D 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    13 
_struct_mon_prot_cis.pdbx_label_asym_id_2   D 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     14 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    D 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -14.19 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 5 ? 
B ? 4 ? 
C ? 5 ? 
D ? 4 ? 
E ? 5 ? 
F ? 4 ? 
G ? 3 ? 
H ? 3 ? 
I ? 5 ? 
J ? 4 ? 
K ? 5 ? 
L ? 4 ? 
M ? 5 ? 
N ? 4 ? 
O ? 5 ? 
P ? 4 ? 
Q ? 5 ? 
R ? 4 ? 
S ? 5 ? 
T ? 4 ? 
U ? 5 ? 
V ? 4 ? 
W ? 5 ? 
X ? 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 
A 1 2 ? anti-parallel 
A 2 3 ? anti-parallel 
A 3 4 ? anti-parallel 
A 4 5 ? anti-parallel 
B 1 2 ? anti-parallel 
B 2 3 ? anti-parallel 
B 3 4 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? anti-parallel 
C 3 4 ? anti-parallel 
C 4 5 ? anti-parallel 
D 1 2 ? anti-parallel 
D 2 3 ? anti-parallel 
D 3 4 ? anti-parallel 
E 1 2 ? anti-parallel 
E 2 3 ? anti-parallel 
E 3 4 ? anti-parallel 
E 4 5 ? anti-parallel 
F 1 2 ? anti-parallel 
F 2 3 ? anti-parallel 
F 3 4 ? anti-parallel 
G 1 2 ? anti-parallel 
G 2 3 ? anti-parallel 
H 1 2 ? anti-parallel 
H 2 3 ? anti-parallel 
I 1 2 ? anti-parallel 
I 2 3 ? anti-parallel 
I 3 4 ? anti-parallel 
I 4 5 ? anti-parallel 
J 1 2 ? anti-parallel 
J 2 3 ? anti-parallel 
J 3 4 ? anti-parallel 
K 1 2 ? anti-parallel 
K 2 3 ? anti-parallel 
K 3 4 ? anti-parallel 
K 4 5 ? anti-parallel 
L 1 2 ? anti-parallel 
L 2 3 ? anti-parallel 
L 3 4 ? anti-parallel 
M 1 2 ? anti-parallel 
M 2 3 ? anti-parallel 
M 3 4 ? anti-parallel 
M 4 5 ? anti-parallel 
N 1 2 ? anti-parallel 
N 2 3 ? anti-parallel 
N 3 4 ? anti-parallel 
O 1 2 ? anti-parallel 
O 2 3 ? anti-parallel 
O 3 4 ? anti-parallel 
O 4 5 ? anti-parallel 
P 1 2 ? anti-parallel 
P 2 3 ? anti-parallel 
P 3 4 ? anti-parallel 
Q 1 2 ? anti-parallel 
Q 2 3 ? anti-parallel 
Q 3 4 ? anti-parallel 
Q 4 5 ? anti-parallel 
R 1 2 ? anti-parallel 
R 2 3 ? anti-parallel 
R 3 4 ? anti-parallel 
S 1 2 ? anti-parallel 
S 2 3 ? anti-parallel 
S 3 4 ? anti-parallel 
S 4 5 ? anti-parallel 
T 1 2 ? anti-parallel 
T 2 3 ? anti-parallel 
T 3 4 ? anti-parallel 
U 1 2 ? anti-parallel 
U 2 3 ? anti-parallel 
U 3 4 ? anti-parallel 
U 4 5 ? anti-parallel 
V 1 2 ? anti-parallel 
V 2 3 ? anti-parallel 
V 3 4 ? anti-parallel 
W 1 2 ? anti-parallel 
W 2 3 ? anti-parallel 
W 3 4 ? anti-parallel 
W 4 5 ? anti-parallel 
X 1 2 ? anti-parallel 
X 2 3 ? anti-parallel 
X 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 
A 1 ALA A 95  ? ASP A 101 ? ALA A 96  ASP A 102 
A 2 VAL A 29  ? LYS A 36  ? VAL A 30  LYS A 37  
A 3 GLN A 15  ? GLN A 22  ? GLN A 16  GLN A 23  
A 4 THR A 2   ? LEU A 8   ? THR A 3   LEU A 9   
A 5 GLY A 150 ? ILE A 151 ? GLY A 151 ILE A 152 
B 1 ASP A 83  ? ALA A 89  ? ASP A 84  ALA A 90  
B 2 GLY A 41  ? HIS A 48  ? GLY A 42  HIS A 49  
B 3 THR A 116 ? HIS A 120 ? THR A 117 HIS A 121 
B 4 ARG A 143 ? VAL A 148 ? ARG A 144 VAL A 149 
C 1 ALA B 95  ? ASP B 101 ? ALA B 96  ASP B 102 
C 2 VAL B 29  ? LYS B 36  ? VAL B 30  LYS B 37  
C 3 GLN B 15  ? GLN B 22  ? GLN B 16  GLN B 23  
C 4 THR B 2   ? LEU B 8   ? THR B 3   LEU B 9   
C 5 GLY B 150 ? ILE B 151 ? GLY B 151 ILE B 152 
D 1 ASP B 83  ? ALA B 89  ? ASP B 84  ALA B 90  
D 2 GLY B 41  ? HIS B 48  ? GLY B 42  HIS B 49  
D 3 THR B 116 ? HIS B 120 ? THR B 117 HIS B 121 
D 4 ARG B 143 ? VAL B 148 ? ARG B 144 VAL B 149 
E 1 ALA C 95  ? ASP C 101 ? ALA C 96  ASP C 102 
E 2 VAL C 29  ? LYS C 36  ? VAL C 30  LYS C 37  
E 3 GLN C 15  ? GLN C 22  ? GLN C 16  GLN C 23  
E 4 THR C 2   ? LEU C 8   ? THR C 3   LEU C 9   
E 5 GLY C 150 ? ILE C 151 ? GLY C 151 ILE C 152 
F 1 ASP C 83  ? ALA C 89  ? ASP C 84  ALA C 90  
F 2 GLY C 41  ? HIS C 48  ? GLY C 42  HIS C 49  
F 3 THR C 116 ? HIS C 120 ? THR C 117 HIS C 121 
F 4 ARG C 143 ? VAL C 148 ? ARG C 144 VAL C 149 
G 1 ILE D 17  ? PHE D 20  ? ILE D 18  PHE D 21  
G 2 ALA D 4   ? VAL D 7   ? ALA D 5   VAL D 8   
G 3 ILE D 149 ? ILE D 151 ? ILE D 150 ILE D 152 
H 1 ASP D 83  ? ALA D 89  ? ASP D 84  ALA D 90  
H 2 GLY D 41  ? HIS D 48  ? GLY D 42  HIS D 49  
H 3 THR D 116 ? VAL D 119 ? THR D 117 VAL D 120 
I 1 ASP E 96  ? ASP E 101 ? ASP E 97  ASP E 102 
I 2 VAL E 29  ? LYS E 36  ? VAL E 30  LYS E 37  
I 3 GLN E 15  ? GLN E 22  ? GLN E 16  GLN E 23  
I 4 LYS E 3   ? LEU E 8   ? LYS E 4   LEU E 9   
I 5 GLY E 150 ? ILE E 151 ? GLY E 151 ILE E 152 
J 1 ASP E 83  ? ALA E 89  ? ASP E 84  ALA E 90  
J 2 GLY E 41  ? HIS E 48  ? GLY E 42  HIS E 49  
J 3 THR E 116 ? HIS E 120 ? THR E 117 HIS E 121 
J 4 ARG E 143 ? VAL E 148 ? ARG E 144 VAL E 149 
K 1 ALA F 95  ? ASP F 101 ? ALA F 96  ASP F 102 
K 2 VAL F 29  ? LYS F 36  ? VAL F 30  LYS F 37  
K 3 GLN F 15  ? GLN F 22  ? GLN F 16  GLN F 23  
K 4 THR F 2   ? LEU F 8   ? THR F 3   LEU F 9   
K 5 GLY F 150 ? ILE F 151 ? GLY F 151 ILE F 152 
L 1 ASP F 83  ? ALA F 89  ? ASP F 84  ALA F 90  
L 2 GLY F 41  ? HIS F 48  ? GLY F 42  HIS F 49  
L 3 THR F 116 ? HIS F 120 ? THR F 117 HIS F 121 
L 4 ARG F 143 ? VAL F 148 ? ARG F 144 VAL F 149 
M 1 ALA G 95  ? ASP G 101 ? ALA G 96  ASP G 102 
M 2 VAL G 29  ? LYS G 36  ? VAL G 30  LYS G 37  
M 3 GLN G 15  ? GLN G 22  ? GLN G 16  GLN G 23  
M 4 THR G 2   ? LEU G 8   ? THR G 3   LEU G 9   
M 5 GLY G 150 ? ILE G 151 ? GLY G 151 ILE G 152 
N 1 ASP G 83  ? ALA G 89  ? ASP G 84  ALA G 90  
N 2 GLY G 41  ? HIS G 48  ? GLY G 42  HIS G 49  
N 3 THR G 116 ? HIS G 120 ? THR G 117 HIS G 121 
N 4 ARG G 143 ? VAL G 148 ? ARG G 144 VAL G 149 
O 1 ALA H 95  ? ASP H 101 ? ALA H 96  ASP H 102 
O 2 VAL H 29  ? LYS H 36  ? VAL H 30  LYS H 37  
O 3 GLN H 15  ? GLN H 22  ? GLN H 16  GLN H 23  
O 4 LYS H 3   ? LEU H 8   ? LYS H 4   LEU H 9   
O 5 GLY H 150 ? ILE H 151 ? GLY H 151 ILE H 152 
P 1 ASP H 83  ? ALA H 89  ? ASP H 84  ALA H 90  
P 2 GLY H 41  ? HIS H 48  ? GLY H 42  HIS H 49  
P 3 THR H 116 ? HIS H 120 ? THR H 117 HIS H 121 
P 4 ARG H 143 ? VAL H 148 ? ARG H 144 VAL H 149 
Q 1 ALA I 95  ? ASP I 101 ? ALA I 96  ASP I 102 
Q 2 VAL I 29  ? LYS I 36  ? VAL I 30  LYS I 37  
Q 3 GLN I 15  ? GLN I 22  ? GLN I 16  GLN I 23  
Q 4 THR I 2   ? LEU I 8   ? THR I 3   LEU I 9   
Q 5 GLY I 150 ? ILE I 151 ? GLY I 151 ILE I 152 
R 1 ASP I 83  ? ALA I 89  ? ASP I 84  ALA I 90  
R 2 GLY I 41  ? HIS I 48  ? GLY I 42  HIS I 49  
R 3 THR I 116 ? HIS I 120 ? THR I 117 HIS I 121 
R 4 ARG I 143 ? VAL I 148 ? ARG I 144 VAL I 149 
S 1 ALA J 95  ? ASP J 101 ? ALA J 96  ASP J 102 
S 2 VAL J 29  ? LYS J 36  ? VAL J 30  LYS J 37  
S 3 GLN J 15  ? GLN J 22  ? GLN J 16  GLN J 23  
S 4 THR J 2   ? LEU J 8   ? THR J 3   LEU J 9   
S 5 GLY J 150 ? ILE J 151 ? GLY J 151 ILE J 152 
T 1 ASP J 83  ? ALA J 89  ? ASP J 84  ALA J 90  
T 2 GLY J 41  ? HIS J 48  ? GLY J 42  HIS J 49  
T 3 THR J 116 ? HIS J 120 ? THR J 117 HIS J 121 
T 4 ARG J 143 ? VAL J 148 ? ARG J 144 VAL J 149 
U 1 ALA K 95  ? ASP K 101 ? ALA K 96  ASP K 102 
U 2 VAL K 29  ? LYS K 36  ? VAL K 30  LYS K 37  
U 3 GLN K 15  ? GLN K 22  ? GLN K 16  GLN K 23  
U 4 THR K 2   ? LEU K 8   ? THR K 3   LEU K 9   
U 5 GLY K 150 ? ILE K 151 ? GLY K 151 ILE K 152 
V 1 ASP K 83  ? ALA K 89  ? ASP K 84  ALA K 90  
V 2 GLY K 41  ? HIS K 48  ? GLY K 42  HIS K 49  
V 3 THR K 116 ? HIS K 120 ? THR K 117 HIS K 121 
V 4 ARG K 143 ? VAL K 148 ? ARG K 144 VAL K 149 
W 1 ALA L 95  ? ASP L 101 ? ALA L 96  ASP L 102 
W 2 VAL L 29  ? LYS L 36  ? VAL L 30  LYS L 37  
W 3 GLN L 15  ? GLN L 22  ? GLN L 16  GLN L 23  
W 4 THR L 2   ? LEU L 8   ? THR L 3   LEU L 9   
W 5 GLY L 150 ? ILE L 151 ? GLY L 151 ILE L 152 
X 1 ASP L 83  ? ALA L 89  ? ASP L 84  ALA L 90  
X 2 GLY L 41  ? HIS L 48  ? GLY L 42  HIS L 49  
X 3 THR L 116 ? HIS L 120 ? THR L 117 HIS L 121 
X 4 ARG L 143 ? VAL L 148 ? ARG L 144 VAL L 149 
# 
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 
A 1 2 O ALA A 95  ? O ALA A 96  N ILE A 35  ? N ILE A 36  
A 2 3 O TRP A 32  ? O TRP A 33  N ASN A 19  ? N ASN A 20  
A 3 4 O PHE A 20  ? O PHE A 21  N ALA A 4   ? N ALA A 5   
A 4 5 N VAL A 5   ? N VAL A 6   O GLY A 150 ? O GLY A 151 
B 1 2 O ALA A 89  ? O ALA A 90  N GLY A 41  ? N GLY A 42  
B 2 3 N HIS A 48  ? N HIS A 49  O THR A 116 ? O THR A 117 
B 3 4 N LEU A 117 ? N LEU A 118 O GLY A 147 ? O GLY A 148 
C 1 2 O ALA B 95  ? O ALA B 96  N ILE B 35  ? N ILE B 36  
C 2 3 O TRP B 32  ? O TRP B 33  N ASN B 19  ? N ASN B 20  
C 3 4 O PHE B 20  ? O PHE B 21  N ALA B 4   ? N ALA B 5   
C 4 5 N VAL B 5   ? N VAL B 6   O GLY B 150 ? O GLY B 151 
D 1 2 O ALA B 89  ? O ALA B 90  N GLY B 41  ? N GLY B 42  
D 2 3 N HIS B 48  ? N HIS B 49  O THR B 116 ? O THR B 117 
D 3 4 N LEU B 117 ? N LEU B 118 O GLY B 147 ? O GLY B 148 
E 1 2 O ASP C 101 ? O ASP C 102 N VAL C 29  ? N VAL C 30  
E 2 3 O TRP C 32  ? O TRP C 33  N ASN C 19  ? N ASN C 20  
E 3 4 O PHE C 20  ? O PHE C 21  N ALA C 4   ? N ALA C 5   
E 4 5 N VAL C 5   ? N VAL C 6   O GLY C 150 ? O GLY C 151 
F 1 2 O ALA C 89  ? O ALA C 90  N GLY C 41  ? N GLY C 42  
F 2 3 N HIS C 48  ? N HIS C 49  O THR C 116 ? O THR C 117 
F 3 4 N VAL C 119 ? N VAL C 120 O ALA C 145 ? O ALA C 146 
G 1 2 O PHE D 20  ? O PHE D 21  N ALA D 4   ? N ALA D 5   
G 2 3 N VAL D 5   ? N VAL D 6   O GLY D 150 ? O GLY D 151 
H 1 2 O ALA D 89  ? O ALA D 90  N GLY D 41  ? N GLY D 42  
H 2 3 N HIS D 48  ? N HIS D 49  O THR D 116 ? O THR D 117 
I 1 2 O ASP E 101 ? O ASP E 102 N VAL E 29  ? N VAL E 30  
I 2 3 O TRP E 32  ? O TRP E 33  N ASN E 19  ? N ASN E 20  
I 3 4 O PHE E 20  ? O PHE E 21  N ALA E 4   ? N ALA E 5   
I 4 5 N VAL E 5   ? N VAL E 6   O GLY E 150 ? O GLY E 151 
J 1 2 O ALA E 89  ? O ALA E 90  N GLY E 41  ? N GLY E 42  
J 2 3 N HIS E 48  ? N HIS E 49  O THR E 116 ? O THR E 117 
J 3 4 N LEU E 117 ? N LEU E 118 O GLY E 147 ? O GLY E 148 
K 1 2 O ALA F 95  ? O ALA F 96  N ILE F 35  ? N ILE F 36  
K 2 3 O TRP F 32  ? O TRP F 33  N ASN F 19  ? N ASN F 20  
K 3 4 O PHE F 20  ? O PHE F 21  N ALA F 4   ? N ALA F 5   
K 4 5 N VAL F 5   ? N VAL F 6   O GLY F 150 ? O GLY F 151 
L 1 2 O ALA F 89  ? O ALA F 90  N GLY F 41  ? N GLY F 42  
L 2 3 N HIS F 48  ? N HIS F 49  O THR F 116 ? O THR F 117 
L 3 4 N VAL F 119 ? N VAL F 120 O ALA F 145 ? O ALA F 146 
M 1 2 O ALA G 95  ? O ALA G 96  N ILE G 35  ? N ILE G 36  
M 2 3 O TRP G 32  ? O TRP G 33  N ASN G 19  ? N ASN G 20  
M 3 4 O ILE G 18  ? O ILE G 19  N CYS G 6   ? N CYS G 7   
M 4 5 N VAL G 5   ? N VAL G 6   O GLY G 150 ? O GLY G 151 
N 1 2 O ALA G 89  ? O ALA G 90  N GLY G 41  ? N GLY G 42  
N 2 3 N HIS G 48  ? N HIS G 49  O THR G 116 ? O THR G 117 
N 3 4 N LEU G 117 ? N LEU G 118 O GLY G 147 ? O GLY G 148 
O 1 2 O ALA H 95  ? O ALA H 96  N ILE H 35  ? N ILE H 36  
O 2 3 O TRP H 32  ? O TRP H 33  N ASN H 19  ? N ASN H 20  
O 3 4 O PHE H 20  ? O PHE H 21  N ALA H 4   ? N ALA H 5   
O 4 5 N VAL H 5   ? N VAL H 6   O GLY H 150 ? O GLY H 151 
P 1 2 O ALA H 89  ? O ALA H 90  N GLY H 41  ? N GLY H 42  
P 2 3 N HIS H 48  ? N HIS H 49  O THR H 116 ? O THR H 117 
P 3 4 N LEU H 117 ? N LEU H 118 O GLY H 147 ? O GLY H 148 
Q 1 2 O ASP I 101 ? O ASP I 102 N VAL I 29  ? N VAL I 30  
Q 2 3 O TRP I 32  ? O TRP I 33  N ASN I 19  ? N ASN I 20  
Q 3 4 O PHE I 20  ? O PHE I 21  N ALA I 4   ? N ALA I 5   
Q 4 5 N VAL I 5   ? N VAL I 6   O GLY I 150 ? O GLY I 151 
R 1 2 O ALA I 89  ? O ALA I 90  N GLY I 41  ? N GLY I 42  
R 2 3 N HIS I 48  ? N HIS I 49  O THR I 116 ? O THR I 117 
R 3 4 N LEU I 117 ? N LEU I 118 O GLY I 147 ? O GLY I 148 
S 1 2 O ASP J 101 ? O ASP J 102 N VAL J 29  ? N VAL J 30  
S 2 3 O TRP J 32  ? O TRP J 33  N ASN J 19  ? N ASN J 20  
S 3 4 O ILE J 18  ? O ILE J 19  N CYS J 6   ? N CYS J 7   
S 4 5 N VAL J 5   ? N VAL J 6   O GLY J 150 ? O GLY J 151 
T 1 2 O ALA J 89  ? O ALA J 90  N GLY J 41  ? N GLY J 42  
T 2 3 N HIS J 48  ? N HIS J 49  O THR J 116 ? O THR J 117 
T 3 4 N LEU J 117 ? N LEU J 118 O GLY J 147 ? O GLY J 148 
U 1 2 O ALA K 95  ? O ALA K 96  N ILE K 35  ? N ILE K 36  
U 2 3 O TRP K 32  ? O TRP K 33  N ASN K 19  ? N ASN K 20  
U 3 4 O ILE K 18  ? O ILE K 19  N CYS K 6   ? N CYS K 7   
U 4 5 N VAL K 5   ? N VAL K 6   O GLY K 150 ? O GLY K 151 
V 1 2 O ALA K 89  ? O ALA K 90  N GLY K 41  ? N GLY K 42  
V 2 3 N HIS K 48  ? N HIS K 49  O THR K 116 ? O THR K 117 
V 3 4 N LEU K 117 ? N LEU K 118 O GLY K 147 ? O GLY K 148 
W 1 2 O ALA L 95  ? O ALA L 96  N ILE L 35  ? N ILE L 36  
W 2 3 O TRP L 32  ? O TRP L 33  N ASN L 19  ? N ASN L 20  
W 3 4 O PHE L 20  ? O PHE L 21  N ALA L 4   ? N ALA L 5   
W 4 5 N VAL L 5   ? N VAL L 6   O GLY L 150 ? O GLY L 151 
X 1 2 O ALA L 89  ? O ALA L 90  N GLY L 41  ? N GLY L 42  
X 2 3 N HIS L 48  ? N HIS L 49  O THR L 116 ? O THR L 117 
X 3 4 N LEU L 117 ? N LEU L 118 O GLY L 147 ? O GLY L 148 
# 
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 ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU A 155'  
AC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN A 156'  
AC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU B 155'  
AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN B 156'  
AC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU C 155'  
AC6 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN C 156'  
AC7 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU D 155'  
AC8 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN D 156'  
AC9 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU E 155'  
BC1 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN E 156'  
BC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU F 155'  
BC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN F 156'  
BC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU G 155'  
BC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN G 156'  
BC6 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU H 155'  
BC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN H 156'  
BC8 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU I 155'  
BC9 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN I 156'  
CC1 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU J 155'  
CC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN J 156'  
CC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU K 155'  
CC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN K 156'  
CC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU L 155'  
CC6 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN L 156'  
CC7 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE SO4 B 1'   
CC8 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE SO4 J 157' 
CC9 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE SO4 B 157' 
# 
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 4 HIS A 46  ? HIS A 47  . ? 1_555 ? 
2   AC1 4 HIS A 48  ? HIS A 49  . ? 1_555 ? 
3   AC1 4 HIS A 63  ? HIS A 64  . ? 1_555 ? 
4   AC1 4 HIS A 120 ? HIS A 121 . ? 1_555 ? 
5   AC2 4 HIS A 63  ? HIS A 64  . ? 1_555 ? 
6   AC2 4 HIS A 71  ? HIS A 72  . ? 1_555 ? 
7   AC2 4 HIS A 80  ? HIS A 81  . ? 1_555 ? 
8   AC2 4 ASP A 83  ? ASP A 84  . ? 1_555 ? 
9   AC3 4 HIS B 46  ? HIS B 47  . ? 1_555 ? 
10  AC3 4 HIS B 48  ? HIS B 49  . ? 1_555 ? 
11  AC3 4 HIS B 63  ? HIS B 64  . ? 1_555 ? 
12  AC3 4 HIS B 120 ? HIS B 121 . ? 1_555 ? 
13  AC4 4 HIS B 63  ? HIS B 64  . ? 1_555 ? 
14  AC4 4 HIS B 71  ? HIS B 72  . ? 1_555 ? 
15  AC4 4 HIS B 80  ? HIS B 81  . ? 1_555 ? 
16  AC4 4 ASP B 83  ? ASP B 84  . ? 1_555 ? 
17  AC5 4 HIS C 46  ? HIS C 47  . ? 1_555 ? 
18  AC5 4 HIS C 48  ? HIS C 49  . ? 1_555 ? 
19  AC5 4 HIS C 63  ? HIS C 64  . ? 1_555 ? 
20  AC5 4 HIS C 120 ? HIS C 121 . ? 1_555 ? 
21  AC6 4 HIS C 63  ? HIS C 64  . ? 1_555 ? 
22  AC6 4 HIS C 71  ? HIS C 72  . ? 1_555 ? 
23  AC6 4 HIS C 80  ? HIS C 81  . ? 1_555 ? 
24  AC6 4 ASP C 83  ? ASP C 84  . ? 1_555 ? 
25  AC7 4 HIS D 46  ? HIS D 47  . ? 1_555 ? 
26  AC7 4 HIS D 48  ? HIS D 49  . ? 1_555 ? 
27  AC7 4 VAL D 118 ? VAL D 119 . ? 1_555 ? 
28  AC7 4 HIS D 120 ? HIS D 121 . ? 1_555 ? 
29  AC8 4 HIS D 63  ? HIS D 64  . ? 1_555 ? 
30  AC8 4 HIS D 71  ? HIS D 72  . ? 1_555 ? 
31  AC8 4 HIS D 80  ? HIS D 81  . ? 1_555 ? 
32  AC8 4 ASP D 83  ? ASP D 84  . ? 1_555 ? 
33  AC9 4 HIS E 46  ? HIS E 47  . ? 1_555 ? 
34  AC9 4 HIS E 48  ? HIS E 49  . ? 1_555 ? 
35  AC9 4 HIS E 63  ? HIS E 64  . ? 1_555 ? 
36  AC9 4 HIS E 120 ? HIS E 121 . ? 1_555 ? 
37  BC1 4 HIS E 63  ? HIS E 64  . ? 1_555 ? 
38  BC1 4 HIS E 71  ? HIS E 72  . ? 1_555 ? 
39  BC1 4 HIS E 80  ? HIS E 81  . ? 1_555 ? 
40  BC1 4 ASP E 83  ? ASP E 84  . ? 1_555 ? 
41  BC2 4 HIS F 46  ? HIS F 47  . ? 1_555 ? 
42  BC2 4 HIS F 48  ? HIS F 49  . ? 1_555 ? 
43  BC2 4 HIS F 63  ? HIS F 64  . ? 1_555 ? 
44  BC2 4 HIS F 120 ? HIS F 121 . ? 1_555 ? 
45  BC3 5 HIS F 63  ? HIS F 64  . ? 1_555 ? 
46  BC3 5 HIS F 71  ? HIS F 72  . ? 1_555 ? 
47  BC3 5 HIS F 80  ? HIS F 81  . ? 1_555 ? 
48  BC3 5 ASP F 83  ? ASP F 84  . ? 1_555 ? 
49  BC3 5 LYS F 136 ? LYS F 137 . ? 1_555 ? 
50  BC4 4 HIS G 46  ? HIS G 47  . ? 1_555 ? 
51  BC4 4 HIS G 48  ? HIS G 49  . ? 1_555 ? 
52  BC4 4 HIS G 63  ? HIS G 64  . ? 1_555 ? 
53  BC4 4 HIS G 120 ? HIS G 121 . ? 1_555 ? 
54  BC5 4 HIS G 63  ? HIS G 64  . ? 1_555 ? 
55  BC5 4 HIS G 71  ? HIS G 72  . ? 1_555 ? 
56  BC5 4 HIS G 80  ? HIS G 81  . ? 1_555 ? 
57  BC5 4 ASP G 83  ? ASP G 84  . ? 1_555 ? 
58  BC6 4 HIS H 46  ? HIS H 47  . ? 1_555 ? 
59  BC6 4 HIS H 48  ? HIS H 49  . ? 1_555 ? 
60  BC6 4 HIS H 63  ? HIS H 64  . ? 1_555 ? 
61  BC6 4 HIS H 120 ? HIS H 121 . ? 1_555 ? 
62  BC7 5 HIS H 63  ? HIS H 64  . ? 1_555 ? 
63  BC7 5 HIS H 71  ? HIS H 72  . ? 1_555 ? 
64  BC7 5 HIS H 80  ? HIS H 81  . ? 1_555 ? 
65  BC7 5 ASP H 83  ? ASP H 84  . ? 1_555 ? 
66  BC7 5 LYS H 136 ? LYS H 137 . ? 1_555 ? 
67  BC8 4 HIS I 46  ? HIS I 47  . ? 1_555 ? 
68  BC8 4 HIS I 48  ? HIS I 49  . ? 1_555 ? 
69  BC8 4 HIS I 63  ? HIS I 64  . ? 1_555 ? 
70  BC8 4 HIS I 120 ? HIS I 121 . ? 1_555 ? 
71  BC9 4 HIS I 63  ? HIS I 64  . ? 1_555 ? 
72  BC9 4 HIS I 71  ? HIS I 72  . ? 1_555 ? 
73  BC9 4 HIS I 80  ? HIS I 81  . ? 1_555 ? 
74  BC9 4 ASP I 83  ? ASP I 84  . ? 1_555 ? 
75  CC1 4 HIS J 46  ? HIS J 47  . ? 1_555 ? 
76  CC1 4 HIS J 48  ? HIS J 49  . ? 1_555 ? 
77  CC1 4 HIS J 63  ? HIS J 64  . ? 1_555 ? 
78  CC1 4 HIS J 120 ? HIS J 121 . ? 1_555 ? 
79  CC2 4 HIS J 63  ? HIS J 64  . ? 1_555 ? 
80  CC2 4 HIS J 71  ? HIS J 72  . ? 1_555 ? 
81  CC2 4 HIS J 80  ? HIS J 81  . ? 1_555 ? 
82  CC2 4 ASP J 83  ? ASP J 84  . ? 1_555 ? 
83  CC3 4 HIS K 46  ? HIS K 47  . ? 1_555 ? 
84  CC3 4 HIS K 48  ? HIS K 49  . ? 1_555 ? 
85  CC3 4 HIS K 63  ? HIS K 64  . ? 1_555 ? 
86  CC3 4 HIS K 120 ? HIS K 121 . ? 1_555 ? 
87  CC4 5 HIS K 63  ? HIS K 64  . ? 1_555 ? 
88  CC4 5 HIS K 71  ? HIS K 72  . ? 1_555 ? 
89  CC4 5 HIS K 80  ? HIS K 81  . ? 1_555 ? 
90  CC4 5 ASP K 83  ? ASP K 84  . ? 1_555 ? 
91  CC4 5 LYS K 136 ? LYS K 137 . ? 1_555 ? 
92  CC5 4 HIS L 46  ? HIS L 47  . ? 1_555 ? 
93  CC5 4 HIS L 48  ? HIS L 49  . ? 1_555 ? 
94  CC5 4 HIS L 63  ? HIS L 64  . ? 1_555 ? 
95  CC5 4 HIS L 120 ? HIS L 121 . ? 1_555 ? 
96  CC6 4 HIS L 63  ? HIS L 64  . ? 1_555 ? 
97  CC6 4 HIS L 71  ? HIS L 72  . ? 1_555 ? 
98  CC6 4 HIS L 80  ? HIS L 81  . ? 1_555 ? 
99  CC6 4 ASP L 83  ? ASP L 84  . ? 1_555 ? 
100 CC7 3 LYS B 128 ? LYS B 129 . ? 1_555 ? 
101 CC7 3 LYS C 128 ? LYS C 129 . ? 1_555 ? 
102 CC7 3 LYS F 128 ? LYS F 129 . ? 1_555 ? 
103 CC8 3 LYS H 128 ? LYS H 129 . ? 1_555 ? 
104 CC8 3 LYS J 128 ? LYS J 129 . ? 1_555 ? 
105 CC8 3 LYS L 128 ? LYS L 129 . ? 1_555 ? 
106 CC9 4 HIS B 48  ? HIS B 49  . ? 1_555 ? 
107 CC9 4 HIS B 120 ? HIS B 121 . ? 1_555 ? 
108 CC9 4 THR B 137 ? THR B 138 . ? 1_555 ? 
109 CC9 4 ARG B 143 ? ARG B 144 . ? 1_555 ? 
# 
_atom_sites.entry_id                    3KH3 
_atom_sites.fract_transf_matrix[1][1]   0.013245 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006002 
_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]   0.005715 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
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   ? 37.904 -35.561  -12.671  1.00 72.86  ? 2   ALA A N   1 
ATOM   2     C  CA  . ALA A  1 1   ? 36.521 -35.412  -12.157  1.00 70.97  ? 2   ALA A CA  1 
ATOM   3     C  C   . ALA A  1 1   ? 35.539 -35.016  -13.280  1.00 66.85  ? 2   ALA A C   1 
ATOM   4     O  O   . ALA A  1 1   ? 34.845 -33.999  -13.178  1.00 66.75  ? 2   ALA A O   1 
ATOM   5     C  CB  . ALA A  1 1   ? 36.476 -34.399  -10.973  1.00 74.03  ? 2   ALA A CB  1 
ATOM   6     N  N   . THR A  1 2   ? 35.500 -35.832  -14.340  1.00 64.38  ? 3   THR A N   1 
ATOM   7     C  CA  . THR A  1 2   ? 34.455 -35.779  -15.397  1.00 60.19  ? 3   THR A CA  1 
ATOM   8     C  C   . THR A  1 2   ? 33.201 -36.504  -14.949  1.00 58.09  ? 3   THR A C   1 
ATOM   9     O  O   . THR A  1 2   ? 33.267 -37.573  -14.354  1.00 58.69  ? 3   THR A O   1 
ATOM   10    C  CB  . THR A  1 2   ? 34.877 -36.469  -16.735  1.00 58.72  ? 3   THR A CB  1 
ATOM   11    O  OG1 . THR A  1 2   ? 36.305 -36.483  -16.866  1.00 61.84  ? 3   THR A OG1 1 
ATOM   12    C  CG2 . THR A  1 2   ? 34.235 -35.765  -17.975  1.00 55.77  ? 3   THR A CG2 1 
ATOM   13    N  N   . LYS A  1 3   ? 32.059 -35.902  -15.255  1.00 56.04  ? 4   LYS A N   1 
ATOM   14    C  CA  . LYS A  1 3   ? 30.736 -36.453  -14.914  1.00 54.47  ? 4   LYS A CA  1 
ATOM   15    C  C   . LYS A  1 3   ? 29.839 -36.444  -16.139  1.00 51.18  ? 4   LYS A C   1 
ATOM   16    O  O   . LYS A  1 3   ? 29.948 -35.571  -16.999  1.00 50.59  ? 4   LYS A O   1 
ATOM   17    C  CB  . LYS A  1 3   ? 30.047 -35.645  -13.789  1.00 56.22  ? 4   LYS A CB  1 
ATOM   18    C  CG  . LYS A  1 3   ? 30.734 -35.705  -12.408  1.00 60.07  ? 4   LYS A CG  1 
ATOM   19    C  CD  . LYS A  1 3   ? 29.843 -35.106  -11.312  1.00 61.93  ? 4   LYS A CD  1 
ATOM   20    C  CE  . LYS A  1 3   ? 30.650 -34.605  -10.114  1.00 66.25  ? 4   LYS A CE  1 
ATOM   21    N  NZ  . LYS A  1 3   ? 29.870 -33.617  -9.303   1.00 67.91  ? 4   LYS A NZ  1 
ATOM   22    N  N   . ALA A  1 4   ? 28.950 -37.422  -16.213  1.00 49.55  ? 5   ALA A N   1 
ATOM   23    C  CA  . ALA A  1 4   ? 27.934 -37.443  -17.262  1.00 47.05  ? 5   ALA A CA  1 
ATOM   24    C  C   . ALA A  1 4   ? 26.602 -37.865  -16.665  1.00 46.67  ? 5   ALA A C   1 
ATOM   25    O  O   . ALA A  1 4   ? 26.554 -38.322  -15.526  1.00 48.30  ? 5   ALA A O   1 
ATOM   26    C  CB  . ALA A  1 4   ? 28.340 -38.362  -18.383  1.00 45.55  ? 5   ALA A CB  1 
ATOM   27    N  N   . VAL A  1 5   ? 25.528 -37.667  -17.422  1.00 45.02  ? 6   VAL A N   1 
ATOM   28    C  CA  . VAL A  1 5   ? 24.192 -38.064  -16.990  1.00 45.08  ? 6   VAL A CA  1 
ATOM   29    C  C   . VAL A  1 5   ? 23.317 -38.395  -18.170  1.00 43.23  ? 6   VAL A C   1 
ATOM   30    O  O   . VAL A  1 5   ? 23.553 -37.907  -19.265  1.00 42.15  ? 6   VAL A O   1 
ATOM   31    C  CB  . VAL A  1 5   ? 23.498 -36.970  -16.224  1.00 46.75  ? 6   VAL A CB  1 
ATOM   32    C  CG1 . VAL A  1 5   ? 22.969 -35.936  -17.169  1.00 46.45  ? 6   VAL A CG1 1 
ATOM   33    C  CG2 . VAL A  1 5   ? 22.355 -37.531  -15.432  1.00 47.97  ? 6   VAL A CG2 1 
ATOM   34    N  N   . CYS A  1 6   ? 22.308 -39.226  -17.933  1.00 43.35  ? 7   CYS A N   1 
ATOM   35    C  CA  . CYS A  1 6   ? 21.411 -39.683  -18.985  1.00 42.32  ? 7   CYS A CA  1 
ATOM   36    C  C   . CYS A  1 6   ? 20.002 -39.950  -18.486  1.00 43.44  ? 7   CYS A C   1 
ATOM   37    O  O   . CYS A  1 6   ? 19.812 -40.716  -17.569  1.00 44.53  ? 7   CYS A O   1 
ATOM   38    C  CB  . CYS A  1 6   ? 21.934 -40.965  -19.632  1.00 41.31  ? 7   CYS A CB  1 
ATOM   39    S  SG  . CYS A  1 6   ? 20.768 -41.680  -20.831  1.00 40.37  ? 7   CYS A SG  1 
ATOM   40    N  N   . VAL A  1 7   ? 19.022 -39.325  -19.130  1.00 43.67  ? 8   VAL A N   1 
ATOM   41    C  CA  . VAL A  1 7   ? 17.600 -39.532  -18.835  1.00 45.09  ? 8   VAL A CA  1 
ATOM   42    C  C   . VAL A  1 7   ? 17.006 -40.593  -19.765  1.00 44.42  ? 8   VAL A C   1 
ATOM   43    O  O   . VAL A  1 7   ? 16.777 -40.356  -20.953  1.00 43.49  ? 8   VAL A O   1 
ATOM   44    C  CB  . VAL A  1 7   ? 16.779 -38.218  -18.966  1.00 46.28  ? 8   VAL A CB  1 
ATOM   45    C  CG1 . VAL A  1 7   ? 15.300 -38.487  -18.826  1.00 48.15  ? 8   VAL A CG1 1 
ATOM   46    C  CG2 . VAL A  1 7   ? 17.212 -37.220  -17.933  1.00 47.61  ? 8   VAL A CG2 1 
ATOM   47    N  N   . LEU A  1 8   ? 16.762 -41.766  -19.195  1.00 45.19  ? 9   LEU A N   1 
ATOM   48    C  CA  . LEU A  1 8   ? 16.175 -42.891  -19.913  1.00 44.99  ? 9   LEU A CA  1 
ATOM   49    C  C   . LEU A  1 8   ? 14.685 -42.692  -20.039  1.00 46.75  ? 9   LEU A C   1 
ATOM   50    O  O   . LEU A  1 8   ? 14.017 -42.455  -19.052  1.00 48.79  ? 9   LEU A O   1 
ATOM   51    C  CB  . LEU A  1 8   ? 16.457 -44.194  -19.170  1.00 45.60  ? 9   LEU A CB  1 
ATOM   52    C  CG  . LEU A  1 8   ? 17.914 -44.663  -19.192  1.00 44.07  ? 9   LEU A CG  1 
ATOM   53    C  CD1 . LEU A  1 8   ? 18.169 -45.667  -18.126  1.00 45.32  ? 9   LEU A CD1 1 
ATOM   54    C  CD2 . LEU A  1 8   ? 18.259 -45.239  -20.522  1.00 42.83  ? 9   LEU A CD2 1 
ATOM   55    N  N   . LYS A  1 9   ? 14.184 -42.772  -21.264  1.00 46.49  ? 10  LYS A N   1 
ATOM   56    C  CA  . LYS A  1 9   ? 12.749 -42.636  -21.569  1.00 48.80  ? 10  LYS A CA  1 
ATOM   57    C  C   . LYS A  1 9   ? 12.335 -43.513  -22.735  1.00 48.84  ? 10  LYS A C   1 
ATOM   58    O  O   . LYS A  1 9   ? 13.171 -43.938  -23.515  1.00 47.28  ? 10  LYS A O   1 
ATOM   59    C  CB  . LYS A  1 9   ? 12.384 -41.194  -21.917  1.00 49.45  ? 10  LYS A CB  1 
ATOM   60    C  CG  . LYS A  1 9   ? 12.099 -40.304  -20.694  1.00 51.77  ? 10  LYS A CG  1 
ATOM   61    C  CD  . LYS A  1 9   ? 11.138 -39.137  -21.048  1.00 54.16  ? 10  LYS A CD  1 
ATOM   62    C  CE  . LYS A  1 9   ? 11.102 -38.042  -19.968  1.00 55.52  ? 10  LYS A CE  1 
ATOM   63    N  NZ  . LYS A  1 9   ? 10.178 -38.382  -18.840  1.00 58.47  ? 10  LYS A NZ  1 
ATOM   64    N  N   . GLY A  1 10  ? 11.040 -43.783  -22.857  1.00 51.32  ? 11  GLY A N   1 
ATOM   65    C  CA  . GLY A  1 10  ? 10.551 -44.632  -23.942  1.00 51.97  ? 11  GLY A CA  1 
ATOM   66    C  C   . GLY A  1 10  ? 9.060  -44.580  -24.215  1.00 55.32  ? 11  GLY A C   1 
ATOM   67    O  O   . GLY A  1 10  ? 8.326  -43.806  -23.614  1.00 57.36  ? 11  GLY A O   1 
ATOM   68    N  N   . ASP A  1 11  ? 8.618  -45.438  -25.128  1.00 56.38  ? 12  ASP A N   1 
ATOM   69    C  CA  . ASP A  1 11  ? 7.205  -45.522  -25.522  1.00 59.97  ? 12  ASP A CA  1 
ATOM   70    C  C   . ASP A  1 11  ? 6.266  -45.972  -24.406  1.00 62.89  ? 12  ASP A C   1 
ATOM   71    O  O   . ASP A  1 11  ? 5.114  -45.561  -24.357  1.00 66.27  ? 12  ASP A O   1 
ATOM   72    C  CB  . ASP A  1 11  ? 7.037  -46.471  -26.705  1.00 60.66  ? 12  ASP A CB  1 
ATOM   73    C  CG  . ASP A  1 11  ? 7.139  -45.761  -28.022  1.00 60.90  ? 12  ASP A CG  1 
ATOM   74    O  OD1 . ASP A  1 11  ? 6.489  -44.697  -28.163  1.00 62.92  ? 12  ASP A OD1 1 
ATOM   75    O  OD2 . ASP A  1 11  ? 7.864  -46.268  -28.918  1.00 60.05  ? 12  ASP A OD2 1 
ATOM   76    N  N   . GLY A  1 12  ? 6.764  -46.823  -23.521  1.00 62.08  ? 13  GLY A N   1 
ATOM   77    C  CA  . GLY A  1 12  ? 5.968  -47.360  -22.415  1.00 65.13  ? 13  GLY A CA  1 
ATOM   78    C  C   . GLY A  1 12  ? 6.366  -46.792  -21.053  1.00 64.78  ? 13  GLY A C   1 
ATOM   79    O  O   . GLY A  1 12  ? 7.012  -45.746  -20.985  1.00 62.77  ? 13  GLY A O   1 
ATOM   80    N  N   . PRO A  1 13  ? 6.008  -47.496  -19.960  1.00 67.06  ? 14  PRO A N   1 
ATOM   81    C  CA  . PRO A  1 13  ? 6.101  -46.979  -18.598  1.00 68.22  ? 14  PRO A CA  1 
ATOM   82    C  C   . PRO A  1 13  ? 7.524  -46.907  -18.052  1.00 64.92  ? 14  PRO A C   1 
ATOM   83    O  O   . PRO A  1 13  ? 7.755  -46.270  -17.027  1.00 65.48  ? 14  PRO A O   1 
ATOM   84    C  CB  . PRO A  1 13  ? 5.308  -48.010  -17.796  1.00 72.11  ? 14  PRO A CB  1 
ATOM   85    C  CG  . PRO A  1 13  ? 5.551  -49.289  -18.513  1.00 70.99  ? 14  PRO A CG  1 
ATOM   86    C  CD  . PRO A  1 13  ? 5.746  -48.946  -19.964  1.00 68.59  ? 14  PRO A CD  1 
ATOM   87    N  N   . VAL A  1 14  ? 8.451  -47.574  -18.729  1.00 61.99  ? 15  VAL A N   1 
ATOM   88    C  CA  . VAL A  1 14  ? 9.835  -47.624  -18.292  1.00 59.23  ? 15  VAL A CA  1 
ATOM   89    C  C   . VAL A  1 14  ? 10.463 -46.237  -18.434  1.00 57.05  ? 15  VAL A C   1 
ATOM   90    O  O   . VAL A  1 14  ? 10.407 -45.606  -19.508  1.00 55.59  ? 15  VAL A O   1 
ATOM   91    C  CB  . VAL A  1 14  ? 10.665 -48.645  -19.092  1.00 57.02  ? 15  VAL A CB  1 
ATOM   92    C  CG1 . VAL A  1 14  ? 12.052 -48.755  -18.485  1.00 55.01  ? 15  VAL A CG1 1 
ATOM   93    C  CG2 . VAL A  1 14  ? 9.970  -50.001  -19.121  1.00 59.43  ? 15  VAL A CG2 1 
ATOM   94    N  N   . GLN A  1 15  ? 11.022 -45.764  -17.319  1.00 57.19  ? 16  GLN A N   1 
ATOM   95    C  CA  . GLN A  1 15  ? 11.755 -44.500  -17.269  1.00 55.45  ? 16  GLN A CA  1 
ATOM   96    C  C   . GLN A  1 15  ? 12.699 -44.445  -16.086  1.00 55.37  ? 16  GLN A C   1 
ATOM   97    O  O   . GLN A  1 15  ? 12.548 -45.171  -15.114  1.00 57.37  ? 16  GLN A O   1 
ATOM   98    C  CB  . GLN A  1 15  ? 10.807 -43.295  -17.232  1.00 57.46  ? 16  GLN A CB  1 
ATOM   99    C  CG  . GLN A  1 15  ? 9.767  -43.322  -16.128  1.00 61.79  ? 16  GLN A CG  1 
ATOM   100   C  CD  . GLN A  1 15  ? 8.995  -42.017  -16.012  1.00 64.22  ? 16  GLN A CD  1 
ATOM   101   O  OE1 . GLN A  1 15  ? 8.517  -41.669  -14.933  1.00 67.61  ? 16  GLN A OE1 1 
ATOM   102   N  NE2 . GLN A  1 15  ? 8.871  -41.289  -17.124  1.00 62.84  ? 16  GLN A NE2 1 
ATOM   103   N  N   . GLY A  1 16  ? 13.685 -43.566  -16.196  1.00 53.53  ? 17  GLY A N   1 
ATOM   104   C  CA  . GLY A  1 16  ? 14.728 -43.443  -15.179  1.00 53.65  ? 17  GLY A CA  1 
ATOM   105   C  C   . GLY A  1 16  ? 15.832 -42.440  -15.483  1.00 51.44  ? 17  GLY A C   1 
ATOM   106   O  O   . GLY A  1 16  ? 15.867 -41.817  -16.546  1.00 49.53  ? 17  GLY A O   1 
ATOM   107   N  N   . ILE A  1 17  ? 16.721 -42.297  -14.506  1.00 52.11  ? 18  ILE A N   1 
ATOM   108   C  CA  . ILE A  1 17  ? 17.882 -41.416  -14.579  1.00 50.82  ? 18  ILE A CA  1 
ATOM   109   C  C   . ILE A  1 17  ? 19.121 -42.212  -14.194  1.00 50.46  ? 18  ILE A C   1 
ATOM   110   O  O   . ILE A  1 17  ? 19.122 -42.890  -13.186  1.00 52.67  ? 18  ILE A O   1 
ATOM   111   C  CB  . ILE A  1 17  ? 17.765 -40.243  -13.584  1.00 53.12  ? 18  ILE A CB  1 
ATOM   112   C  CG1 . ILE A  1 17  ? 16.908 -39.115  -14.149  1.00 53.38  ? 18  ILE A CG1 1 
ATOM   113   C  CG2 . ILE A  1 17  ? 19.127 -39.699  -13.240  1.00 52.83  ? 18  ILE A CG2 1 
ATOM   114   C  CD1 . ILE A  1 17  ? 17.029 -37.828  -13.355  1.00 55.50  ? 18  ILE A CD1 1 
ATOM   115   N  N   . ILE A  1 18  ? 20.169 -42.127  -14.999  1.00 48.32  ? 19  ILE A N   1 
ATOM   116   C  CA  . ILE A  1 18  ? 21.430 -42.813  -14.713  1.00 48.37  ? 19  ILE A CA  1 
ATOM   117   C  C   . ILE A  1 18  ? 22.595 -41.839  -14.770  1.00 48.11  ? 19  ILE A C   1 
ATOM   118   O  O   . ILE A  1 18  ? 22.773 -41.120  -15.759  1.00 46.55  ? 19  ILE A O   1 
ATOM   119   C  CB  . ILE A  1 18  ? 21.725 -43.936  -15.729  1.00 46.70  ? 19  ILE A CB  1 
ATOM   120   C  CG1 . ILE A  1 18  ? 20.713 -45.064  -15.591  1.00 47.65  ? 19  ILE A CG1 1 
ATOM   121   C  CG2 . ILE A  1 18  ? 23.132 -44.482  -15.544  1.00 46.97  ? 19  ILE A CG2 1 
ATOM   122   C  CD1 . ILE A  1 18  ? 20.814 -45.807  -14.316  1.00 50.50  ? 19  ILE A CD1 1 
ATOM   123   N  N   . ASN A  1 19  ? 23.410 -41.852  -13.723  1.00 50.11  ? 20  ASN A N   1 
ATOM   124   C  CA  . ASN A  1 19  ? 24.587 -40.987  -13.622  1.00 50.50  ? 20  ASN A CA  1 
ATOM   125   C  C   . ASN A  1 19  ? 25.883 -41.695  -13.937  1.00 50.37  ? 20  ASN A C   1 
ATOM   126   O  O   . ASN A  1 19  ? 26.014 -42.880  -13.681  1.00 51.26  ? 20  ASN A O   1 
ATOM   127   C  CB  . ASN A  1 19  ? 24.699 -40.445  -12.214  1.00 53.57  ? 20  ASN A CB  1 
ATOM   128   C  CG  . ASN A  1 19  ? 23.529 -39.589  -11.838  1.00 54.43  ? 20  ASN A CG  1 
ATOM   129   O  OD1 . ASN A  1 19  ? 22.636 -40.024  -11.121  1.00 56.27  ? 20  ASN A OD1 1 
ATOM   130   N  ND2 . ASN A  1 19  ? 23.519 -38.365  -12.328  1.00 53.65  ? 20  ASN A ND2 1 
ATOM   131   N  N   . PHE A  1 20  ? 26.846 -40.937  -14.457  1.00 50.01  ? 21  PHE A N   1 
ATOM   132   C  CA  . PHE A  1 20  ? 28.217 -41.416  -14.706  1.00 50.59  ? 21  PHE A CA  1 
ATOM   133   C  C   . PHE A  1 20  ? 29.218 -40.517  -13.986  1.00 52.98  ? 21  PHE A C   1 
ATOM   134   O  O   . PHE A  1 20  ? 29.004 -39.298  -13.871  1.00 53.20  ? 21  PHE A O   1 
ATOM   135   C  CB  . PHE A  1 20  ? 28.552 -41.412  -16.200  1.00 48.32  ? 21  PHE A CB  1 
ATOM   136   C  CG  . PHE A  1 20  ? 27.671 -42.294  -17.024  1.00 46.25  ? 21  PHE A CG  1 
ATOM   137   C  CD1 . PHE A  1 20  ? 26.407 -41.878  -17.376  1.00 44.92  ? 21  PHE A CD1 1 
ATOM   138   C  CD2 . PHE A  1 20  ? 28.109 -43.533  -17.451  1.00 46.12  ? 21  PHE A CD2 1 
ATOM   139   C  CE1 . PHE A  1 20  ? 25.600 -42.679  -18.128  1.00 43.62  ? 21  PHE A CE1 1 
ATOM   140   C  CE2 . PHE A  1 20  ? 27.310 -44.340  -18.205  1.00 44.60  ? 21  PHE A CE2 1 
ATOM   141   C  CZ  . PHE A  1 20  ? 26.056 -43.919  -18.547  1.00 43.57  ? 21  PHE A CZ  1 
ATOM   142   N  N   . GLU A  1 21  ? 30.304 -41.121  -13.504  1.00 55.19  ? 22  GLU A N   1 
ATOM   143   C  CA  . GLU A  1 21  ? 31.385 -40.369  -12.860  1.00 57.99  ? 22  GLU A CA  1 
ATOM   144   C  C   . GLU A  1 21  ? 32.741 -41.061  -12.973  1.00 59.82  ? 22  GLU A C   1 
ATOM   145   O  O   . GLU A  1 21  ? 32.981 -42.101  -12.370  1.00 61.56  ? 22  GLU A O   1 
ATOM   146   C  CB  . GLU A  1 21  ? 31.073 -40.098  -11.398  1.00 60.82  ? 22  GLU A CB  1 
ATOM   147   C  CG  . GLU A  1 21  ? 32.162 -39.275  -10.733  1.00 64.58  ? 22  GLU A CG  1 
ATOM   148   C  CD  . GLU A  1 21  ? 31.772 -38.782  -9.350   1.00 68.29  ? 22  GLU A CD  1 
ATOM   149   O  OE1 . GLU A  1 21  ? 30.784 -39.352  -8.768   1.00 68.50  ? 22  GLU A OE1 1 
ATOM   150   O  OE2 . GLU A  1 21  ? 32.477 -37.830  -8.864   1.00 70.93  ? 22  GLU A OE2 1 
ATOM   151   N  N   . GLN A  1 22  ? 33.620 -40.454  -13.756  1.00 59.90  ? 23  GLN A N   1 
ATOM   152   C  CA  . GLN A  1 22  ? 34.987 -40.939  -13.955  1.00 62.23  ? 23  GLN A CA  1 
ATOM   153   C  C   . GLN A  1 22  ? 35.937 -39.955  -13.268  1.00 65.76  ? 23  GLN A C   1 
ATOM   154   O  O   . GLN A  1 22  ? 36.151 -38.831  -13.750  1.00 65.46  ? 23  GLN A O   1 
ATOM   155   C  CB  . GLN A  1 22  ? 35.308 -41.031  -15.449  1.00 60.22  ? 23  GLN A CB  1 
ATOM   156   C  CG  . GLN A  1 22  ? 36.630 -41.691  -15.782  1.00 62.63  ? 23  GLN A CG  1 
ATOM   157   C  CD  . GLN A  1 22  ? 36.895 -41.750  -17.282  1.00 61.14  ? 23  GLN A CD  1 
ATOM   158   O  OE1 . GLN A  1 22  ? 36.624 -40.803  -18.015  1.00 59.70  ? 23  GLN A OE1 1 
ATOM   159   N  NE2 . GLN A  1 22  ? 37.435 -42.862  -17.741  1.00 62.14  ? 23  GLN A NE2 1 
ATOM   160   N  N   . LYS A  1 23  ? 36.502 -40.370  -12.139  1.00 69.49  ? 24  LYS A N   1 
ATOM   161   C  CA  . LYS A  1 23  ? 37.378 -39.485  -11.362  1.00 73.45  ? 24  LYS A CA  1 
ATOM   162   C  C   . LYS A  1 23  ? 38.655 -39.139  -12.114  1.00 75.02  ? 24  LYS A C   1 
ATOM   163   O  O   . LYS A  1 23  ? 39.134 -38.015  -12.034  1.00 76.78  ? 24  LYS A O   1 
ATOM   164   C  CB  . LYS A  1 23  ? 37.742 -40.103  -10.009  1.00 77.71  ? 24  LYS A CB  1 
ATOM   165   C  CG  . LYS A  1 23  ? 36.547 -40.269  -9.066   1.00 77.69  ? 24  LYS A CG  1 
ATOM   166   C  CD  . LYS A  1 23  ? 36.964 -40.188  -7.582   1.00 83.09  ? 24  LYS A CD  1 
ATOM   167   C  CE  . LYS A  1 23  ? 35.960 -40.929  -6.667   1.00 83.71  ? 24  LYS A CE  1 
ATOM   168   N  NZ  . LYS A  1 23  ? 36.465 -41.100  -5.256   1.00 89.31  ? 24  LYS A NZ  1 
ATOM   169   N  N   . GLU A  1 24  ? 39.196 -40.108  -12.845  1.00 74.88  ? 25  GLU A N   1 
ATOM   170   C  CA  . GLU A  1 24  ? 40.461 -39.918  -13.541  1.00 77.23  ? 25  GLU A CA  1 
ATOM   171   C  C   . GLU A  1 24  ? 40.436 -40.469  -14.956  1.00 74.53  ? 25  GLU A C   1 
ATOM   172   O  O   . GLU A  1 24  ? 39.954 -41.566  -15.199  1.00 72.80  ? 25  GLU A O   1 
ATOM   173   C  CB  . GLU A  1 24  ? 41.587 -40.555  -12.749  1.00 82.46  ? 25  GLU A CB  1 
ATOM   174   C  CG  . GLU A  1 24  ? 41.631 -40.044  -11.319  1.00 86.03  ? 25  GLU A CG  1 
ATOM   175   C  CD  . GLU A  1 24  ? 42.938 -40.381  -10.607  1.00 92.85  ? 25  GLU A CD  1 
ATOM   176   O  OE1 . GLU A  1 24  ? 43.380 -41.566  -10.678  1.00 94.69  ? 25  GLU A OE1 1 
ATOM   177   O  OE2 . GLU A  1 24  ? 43.518 -39.460  -9.974   1.00 96.48  ? 25  GLU A OE2 1 
ATOM   178   N  N   . SER A  1 25  ? 40.995 -39.688  -15.872  1.00 74.79  ? 26  SER A N   1 
ATOM   179   C  CA  . SER A  1 25  ? 40.930 -39.953  -17.308  1.00 72.66  ? 26  SER A CA  1 
ATOM   180   C  C   . SER A  1 25  ? 41.293 -41.386  -17.674  1.00 73.47  ? 26  SER A C   1 
ATOM   181   O  O   . SER A  1 25  ? 40.692 -41.978  -18.572  1.00 70.83  ? 26  SER A O   1 
ATOM   182   C  CB  . SER A  1 25  ? 41.844 -38.979  -18.060  1.00 74.84  ? 26  SER A CB  1 
ATOM   183   O  OG  . SER A  1 25  ? 43.087 -38.830  -17.392  1.00 80.36  ? 26  SER A OG  1 
ATOM   184   N  N   . ASN A  1 26  ? 42.279 -41.934  -16.981  1.00 77.71  ? 27  ASN A N   1 
ATOM   185   C  CA  . ASN A  1 26  ? 42.741 -43.309  -17.216  1.00 79.51  ? 27  ASN A CA  1 
ATOM   186   C  C   . ASN A  1 26  ? 41.986 -44.366  -16.362  1.00 78.65  ? 27  ASN A C   1 
ATOM   187   O  O   . ASN A  1 26  ? 42.274 -45.570  -16.424  1.00 80.32  ? 27  ASN A O   1 
ATOM   188   C  CB  . ASN A  1 26  ? 44.261 -43.409  -16.973  1.00 85.35  ? 27  ASN A CB  1 
ATOM   189   C  CG  . ASN A  1 26  ? 44.651 -43.243  -15.489  1.00 89.11  ? 27  ASN A CG  1 
ATOM   190   O  OD1 . ASN A  1 26  ? 44.145 -42.360  -14.767  1.00 87.93  ? 27  ASN A OD1 1 
ATOM   191   N  ND2 . ASN A  1 26  ? 45.567 -44.088  -15.040  1.00 93.56  ? 27  ASN A ND2 1 
ATOM   192   N  N   . GLY A  1 27  ? 41.015 -43.916  -15.575  1.00 76.38  ? 28  GLY A N   1 
ATOM   193   C  CA  . GLY A  1 27  ? 40.434 -44.751  -14.525  1.00 76.66  ? 28  GLY A CA  1 
ATOM   194   C  C   . GLY A  1 27  ? 39.051 -45.285  -14.825  1.00 72.30  ? 28  GLY A C   1 
ATOM   195   O  O   . GLY A  1 27  ? 38.508 -45.062  -15.900  1.00 68.93  ? 28  GLY A O   1 
ATOM   196   N  N   . PRO A  1 28  ? 38.462 -45.995  -13.858  1.00 72.78  ? 29  PRO A N   1 
ATOM   197   C  CA  . PRO A  1 28  ? 37.176 -46.606  -14.075  1.00 69.34  ? 29  PRO A CA  1 
ATOM   198   C  C   . PRO A  1 28  ? 36.042 -45.596  -13.943  1.00 66.19  ? 29  PRO A C   1 
ATOM   199   O  O   . PRO A  1 28  ? 36.223 -44.530  -13.338  1.00 67.28  ? 29  PRO A O   1 
ATOM   200   C  CB  . PRO A  1 28  ? 37.104 -47.637  -12.945  1.00 72.31  ? 29  PRO A CB  1 
ATOM   201   C  CG  . PRO A  1 28  ? 37.831 -46.999  -11.824  1.00 75.96  ? 29  PRO A CG  1 
ATOM   202   C  CD  . PRO A  1 28  ? 38.925 -46.179  -12.469  1.00 77.02  ? 29  PRO A CD  1 
ATOM   203   N  N   . VAL A  1 29  ? 34.885 -45.961  -14.498  1.00 62.73  ? 30  VAL A N   1 
ATOM   204   C  CA  . VAL A  1 29  ? 33.679 -45.128  -14.499  1.00 59.62  ? 30  VAL A CA  1 
ATOM   205   C  C   . VAL A  1 29  ? 32.604 -45.722  -13.610  1.00 59.55  ? 30  VAL A C   1 
ATOM   206   O  O   . VAL A  1 29  ? 32.096 -46.791  -13.881  1.00 58.92  ? 30  VAL A O   1 
ATOM   207   C  CB  . VAL A  1 29  ? 33.078 -45.039  -15.917  1.00 56.05  ? 30  VAL A CB  1 
ATOM   208   C  CG1 . VAL A  1 29  ? 31.798 -44.248  -15.890  1.00 53.52  ? 30  VAL A CG1 1 
ATOM   209   C  CG2 . VAL A  1 29  ? 34.079 -44.450  -16.908  1.00 56.15  ? 30  VAL A CG2 1 
ATOM   210   N  N   . LYS A  1 30  ? 32.240 -45.020  -12.554  1.00 60.81  ? 31  LYS A N   1 
ATOM   211   C  CA  . LYS A  1 30  ? 31.103 -45.448  -11.734  1.00 61.20  ? 31  LYS A CA  1 
ATOM   212   C  C   . LYS A  1 30  ? 29.801 -45.082  -12.425  1.00 57.65  ? 31  LYS A C   1 
ATOM   213   O  O   . LYS A  1 30  ? 29.629 -43.949  -12.879  1.00 56.11  ? 31  LYS A O   1 
ATOM   214   C  CB  . LYS A  1 30  ? 31.148 -44.822  -10.340  1.00 64.35  ? 31  LYS A CB  1 
ATOM   215   C  CG  . LYS A  1 30  ? 32.255 -45.411  -9.480   1.00 69.05  ? 31  LYS A CG  1 
ATOM   216   C  CD  . LYS A  1 30  ? 32.109 -45.082  -8.007   1.00 73.23  ? 31  LYS A CD  1 
ATOM   217   C  CE  . LYS A  1 30  ? 33.244 -45.733  -7.210   1.00 77.86  ? 31  LYS A CE  1 
ATOM   218   N  NZ  . LYS A  1 30  ? 33.056 -45.568  -5.747   1.00 82.54  ? 31  LYS A NZ  1 
ATOM   219   N  N   . VAL A  1 31  ? 28.889 -46.042  -12.494  1.00 56.79  ? 32  VAL A N   1 
ATOM   220   C  CA  . VAL A  1 31  ? 27.593 -45.819  -13.096  1.00 54.10  ? 32  VAL A CA  1 
ATOM   221   C  C   . VAL A  1 31  ? 26.541 -46.050  -12.048  1.00 55.67  ? 32  VAL A C   1 
ATOM   222   O  O   . VAL A  1 31  ? 26.510 -47.086  -11.453  1.00 57.88  ? 32  VAL A O   1 
ATOM   223   C  CB  . VAL A  1 31  ? 27.379 -46.776  -14.259  1.00 52.10  ? 32  VAL A CB  1 
ATOM   224   C  CG1 . VAL A  1 31  ? 26.053 -46.472  -14.974  1.00 49.52  ? 32  VAL A CG1 1 
ATOM   225   C  CG2 . VAL A  1 31  ? 28.561 -46.700  -15.199  1.00 51.53  ? 32  VAL A CG2 1 
ATOM   226   N  N   . TRP A  1 32  ? 25.686 -45.088  -11.789  1.00 55.34  ? 33  TRP A N   1 
ATOM   227   C  CA  . TRP A  1 32  ? 24.634 -45.323  -10.818  1.00 57.55  ? 33  TRP A CA  1 
ATOM   228   C  C   . TRP A  1 32  ? 23.390 -44.527  -11.070  1.00 56.50  ? 33  TRP A C   1 
ATOM   229   O  O   . TRP A  1 32  ? 23.418 -43.512  -11.759  1.00 54.84  ? 33  TRP A O   1 
ATOM   230   C  CB  . TRP A  1 32  ? 25.120 -45.010  -9.423   1.00 61.37  ? 33  TRP A CB  1 
ATOM   231   C  CG  . TRP A  1 32  ? 24.998 -43.545  -9.009   1.00 62.15  ? 33  TRP A CG  1 
ATOM   232   C  CD1 . TRP A  1 32  ? 24.019 -42.975  -8.231   1.00 64.22  ? 33  TRP A CD1 1 
ATOM   233   C  CD2 . TRP A  1 32  ? 25.907 -42.505  -9.312   1.00 61.45  ? 33  TRP A CD2 1 
ATOM   234   N  NE1 . TRP A  1 32  ? 24.270 -41.643  -8.037   1.00 64.26  ? 33  TRP A NE1 1 
ATOM   235   C  CE2 . TRP A  1 32  ? 25.424 -41.326  -8.691   1.00 62.82  ? 33  TRP A CE2 1 
ATOM   236   C  CE3 . TRP A  1 32  ? 27.086 -42.447  -10.057  1.00 60.59  ? 33  TRP A CE3 1 
ATOM   237   C  CZ2 . TRP A  1 32  ? 26.084 -40.106  -8.790   1.00 63.40  ? 33  TRP A CZ2 1 
ATOM   238   C  CZ3 . TRP A  1 32  ? 27.753 -41.225  -10.161  1.00 61.07  ? 33  TRP A CZ3 1 
ATOM   239   C  CH2 . TRP A  1 32  ? 27.249 -40.069  -9.524   1.00 62.37  ? 33  TRP A CH2 1 
ATOM   240   N  N   . GLY A  1 33  ? 22.293 -44.988  -10.486  1.00 58.08  ? 34  GLY A N   1 
ATOM   241   C  CA  . GLY A  1 33  ? 21.010 -44.312  -10.639  1.00 57.91  ? 34  GLY A CA  1 
ATOM   242   C  C   . GLY A  1 33  ? 19.837 -45.219  -10.337  1.00 59.46  ? 34  GLY A C   1 
ATOM   243   O  O   . GLY A  1 33  ? 19.998 -46.259  -9.710   1.00 61.57  ? 34  GLY A O   1 
ATOM   244   N  N   . SER A  1 34  ? 18.662 -44.827  -10.813  1.00 58.83  ? 35  SER A N   1 
ATOM   245   C  CA  . SER A  1 34  ? 17.449 -45.564  -10.549  1.00 60.74  ? 35  SER A CA  1 
ATOM   246   C  C   . SER A  1 34  ? 16.515 -45.587  -11.775  1.00 58.73  ? 35  SER A C   1 
ATOM   247   O  O   . SER A  1 34  ? 16.071 -44.544  -12.267  1.00 57.72  ? 35  SER A O   1 
ATOM   248   C  CB  . SER A  1 34  ? 16.752 -44.946  -9.347   1.00 64.51  ? 35  SER A CB  1 
ATOM   249   O  OG  . SER A  1 34  ? 15.742 -45.798  -8.869   1.00 67.54  ? 35  SER A OG  1 
ATOM   250   N  N   . ILE A  1 35  ? 16.238 -46.796  -12.268  1.00 58.52  ? 36  ILE A N   1 
ATOM   251   C  CA  . ILE A  1 35  ? 15.244 -47.024  -13.330  1.00 57.46  ? 36  ILE A CA  1 
ATOM   252   C  C   . ILE A  1 35  ? 14.002 -47.680  -12.757  1.00 60.85  ? 36  ILE A C   1 
ATOM   253   O  O   . ILE A  1 35  ? 14.087 -48.531  -11.885  1.00 63.18  ? 36  ILE A O   1 
ATOM   254   C  CB  . ILE A  1 35  ? 15.749 -47.956  -14.423  1.00 55.05  ? 36  ILE A CB  1 
ATOM   255   C  CG1 . ILE A  1 35  ? 17.103 -47.497  -14.954  1.00 52.46  ? 36  ILE A CG1 1 
ATOM   256   C  CG2 . ILE A  1 35  ? 14.739 -48.004  -15.554  1.00 54.01  ? 36  ILE A CG2 1 
ATOM   257   C  CD1 . ILE A  1 35  ? 17.693 -48.464  -15.955  1.00 50.99  ? 36  ILE A CD1 1 
ATOM   258   N  N   . LYS A  1 36  ? 12.847 -47.287  -13.269  1.00 61.59  ? 37  LYS A N   1 
ATOM   259   C  CA  . LYS A  1 36  ? 11.569 -47.819  -12.783  1.00 65.32  ? 37  LYS A CA  1 
ATOM   260   C  C   . LYS A  1 36  ? 10.581 -48.159  -13.907  1.00 65.06  ? 37  LYS A C   1 
ATOM   261   O  O   . LYS A  1 36  ? 10.801 -47.846  -15.080  1.00 62.14  ? 37  LYS A O   1 
ATOM   262   C  CB  . LYS A  1 36  ? 10.928 -46.858  -11.771  1.00 68.57  ? 37  LYS A CB  1 
ATOM   263   C  CG  . LYS A  1 36  ? 10.631 -45.458  -12.290  1.00 67.62  ? 37  LYS A CG  1 
ATOM   264   C  CD  . LYS A  1 36  ? 9.589  -44.776  -11.409  1.00 72.32  ? 37  LYS A CD  1 
ATOM   265   C  CE  . LYS A  1 36  ? 9.369  -43.318  -11.792  1.00 71.87  ? 37  LYS A CE  1 
ATOM   266   N  NZ  . LYS A  1 36  ? 8.176  -42.739  -11.112  1.00 76.51  ? 37  LYS A NZ  1 
ATOM   267   N  N   . GLY A  1 37  ? 9.498  -48.826  -13.526  1.00 68.70  ? 38  GLY A N   1 
ATOM   268   C  CA  . GLY A  1 37  ? 8.496  -49.335  -14.481  1.00 69.51  ? 38  GLY A CA  1 
ATOM   269   C  C   . GLY A  1 37  ? 8.925  -50.643  -15.144  1.00 68.19  ? 38  GLY A C   1 
ATOM   270   O  O   . GLY A  1 37  ? 8.374  -51.050  -16.173  1.00 67.89  ? 38  GLY A O   1 
ATOM   271   N  N   . LEU A  1 38  ? 9.903  -51.310  -14.532  1.00 67.73  ? 39  LEU A N   1 
ATOM   272   C  CA  . LEU A  1 38  ? 10.528 -52.495  -15.113  1.00 66.42  ? 39  LEU A CA  1 
ATOM   273   C  C   . LEU A  1 38  ? 9.848  -53.765  -14.639  1.00 70.12  ? 39  LEU A C   1 
ATOM   274   O  O   . LEU A  1 38  ? 9.430  -53.878  -13.491  1.00 73.29  ? 39  LEU A O   1 
ATOM   275   C  CB  . LEU A  1 38  ? 12.026 -52.557  -14.780  1.00 64.22  ? 39  LEU A CB  1 
ATOM   276   C  CG  . LEU A  1 38  ? 12.969 -51.767  -15.683  1.00 59.92  ? 39  LEU A CG  1 
ATOM   277   C  CD1 . LEU A  1 38  ? 14.322 -51.613  -15.032  1.00 58.81  ? 39  LEU A CD1 1 
ATOM   278   C  CD2 . LEU A  1 38  ? 13.118 -52.437  -17.009  1.00 58.15  ? 39  LEU A CD2 1 
ATOM   279   N  N   . THR A  1 39  ? 9.761  -54.725  -15.552  1.00 69.89  ? 40  THR A N   1 
ATOM   280   C  CA  . THR A  1 39  ? 9.257  -56.069  -15.245  1.00 73.35  ? 40  THR A CA  1 
ATOM   281   C  C   . THR A  1 39  ? 10.249 -56.713  -14.260  1.00 74.12  ? 40  THR A C   1 
ATOM   282   O  O   . THR A  1 39  ? 11.472 -56.593  -14.424  1.00 71.28  ? 40  THR A O   1 
ATOM   283   C  CB  . THR A  1 39  ? 9.076  -56.960  -16.530  1.00 72.84  ? 40  THR A CB  1 
ATOM   284   O  OG1 . THR A  1 39  ? 10.150 -57.892  -16.645  1.00 72.06  ? 40  THR A OG1 1 
ATOM   285   C  CG2 . THR A  1 39  ? 9.009  -56.133  -17.822  1.00 69.86  ? 40  THR A CG2 1 
ATOM   286   N  N   . GLU A  1 40  ? 9.742  -57.376  -13.226  1.00 78.45  ? 41  GLU A N   1 
ATOM   287   C  CA  . GLU A  1 40  ? 10.623 -57.911  -12.182  1.00 79.86  ? 41  GLU A CA  1 
ATOM   288   C  C   . GLU A  1 40  ? 11.671 -58.842  -12.772  1.00 78.08  ? 41  GLU A C   1 
ATOM   289   O  O   . GLU A  1 40  ? 11.368 -59.703  -13.602  1.00 78.39  ? 41  GLU A O   1 
ATOM   290   C  CB  . GLU A  1 40  ? 9.844  -58.671  -11.108  1.00 85.56  ? 41  GLU A CB  1 
ATOM   291   C  CG  . GLU A  1 40  ? 10.757 -59.286  -10.012  1.00 88.08  ? 41  GLU A CG  1 
ATOM   292   C  CD  . GLU A  1 40  ? 9.993  -60.126  -8.973   1.00 94.60  ? 41  GLU A CD  1 
ATOM   293   O  OE1 . GLU A  1 40  ? 9.145  -60.958  -9.378   1.00 96.90  ? 41  GLU A OE1 1 
ATOM   294   O  OE2 . GLU A  1 40  ? 10.255 -59.970  -7.755   1.00 97.20  ? 41  GLU A OE2 1 
ATOM   295   N  N   . GLY A  1 41  ? 12.906 -58.665  -12.326  1.00 76.74  ? 42  GLY A N   1 
ATOM   296   C  CA  . GLY A  1 41  ? 14.013 -59.541  -12.719  1.00 75.84  ? 42  GLY A CA  1 
ATOM   297   C  C   . GLY A  1 41  ? 15.144 -58.840  -13.462  1.00 71.36  ? 42  GLY A C   1 
ATOM   298   O  O   . GLY A  1 41  ? 15.325 -57.612  -13.381  1.00 69.04  ? 42  GLY A O   1 
ATOM   299   N  N   . LEU A  1 42  ? 15.913 -59.644  -14.187  1.00 70.43  ? 43  LEU A N   1 
ATOM   300   C  CA  . LEU A  1 42  ? 17.090 -59.143  -14.897  1.00 67.02  ? 43  LEU A CA  1 
ATOM   301   C  C   . LEU A  1 42  ? 16.720 -58.377  -16.190  1.00 63.74  ? 43  LEU A C   1 
ATOM   302   O  O   . LEU A  1 42  ? 15.758 -58.730  -16.898  1.00 64.29  ? 43  LEU A O   1 
ATOM   303   C  CB  . LEU A  1 42  ? 18.071 -60.278  -15.237  1.00 67.80  ? 43  LEU A CB  1 
ATOM   304   C  CG  . LEU A  1 42  ? 18.929 -60.794  -14.078  1.00 70.38  ? 43  LEU A CG  1 
ATOM   305   C  CD1 . LEU A  1 42  ? 18.496 -62.207  -13.698  1.00 74.67  ? 43  LEU A CD1 1 
ATOM   306   C  CD2 . LEU A  1 42  ? 20.403 -60.759  -14.432  1.00 69.06  ? 43  LEU A CD2 1 
ATOM   307   N  N   . HIS A  1 43  ? 17.500 -57.335  -16.490  1.00 60.68  ? 44  HIS A N   1 
ATOM   308   C  CA  . HIS A  1 43  ? 17.350 -56.593  -17.730  1.00 57.53  ? 44  HIS A CA  1 
ATOM   309   C  C   . HIS A  1 43  ? 18.697 -56.255  -18.322  1.00 55.27  ? 44  HIS A C   1 
ATOM   310   O  O   . HIS A  1 43  ? 19.611 -55.857  -17.602  1.00 55.20  ? 44  HIS A O   1 
ATOM   311   C  CB  . HIS A  1 43  ? 16.563 -55.328  -17.484  1.00 56.58  ? 44  HIS A CB  1 
ATOM   312   C  CG  . HIS A  1 43  ? 15.118 -55.577  -17.236  1.00 58.97  ? 44  HIS A CG  1 
ATOM   313   N  ND1 . HIS A  1 43  ? 14.220 -55.799  -18.256  1.00 59.29  ? 44  HIS A ND1 1 
ATOM   314   C  CD2 . HIS A  1 43  ? 14.412 -55.656  -16.084  1.00 61.96  ? 44  HIS A CD2 1 
ATOM   315   C  CE1 . HIS A  1 43  ? 13.015 -55.989  -17.745  1.00 62.15  ? 44  HIS A CE1 1 
ATOM   316   N  NE2 . HIS A  1 43  ? 13.105 -55.909  -16.429  1.00 63.85  ? 44  HIS A NE2 1 
ATOM   317   N  N   . GLY A  1 44  ? 18.803 -56.427  -19.638  1.00 53.84  ? 45  GLY A N   1 
ATOM   318   C  CA  . GLY A  1 44  ? 19.984 -56.040  -20.397  1.00 51.89  ? 45  GLY A CA  1 
ATOM   319   C  C   . GLY A  1 44  ? 20.212 -54.545  -20.331  1.00 49.67  ? 45  GLY A C   1 
ATOM   320   O  O   . GLY A  1 44  ? 19.272 -53.764  -20.218  1.00 49.26  ? 45  GLY A O   1 
ATOM   321   N  N   . PHE A  1 45  ? 21.470 -54.138  -20.401  1.00 48.76  ? 46  PHE A N   1 
ATOM   322   C  CA  . PHE A  1 45  ? 21.841 -52.759  -20.100  1.00 47.23  ? 46  PHE A CA  1 
ATOM   323   C  C   . PHE A  1 45  ? 23.109 -52.394  -20.834  1.00 46.16  ? 46  PHE A C   1 
ATOM   324   O  O   . PHE A  1 45  ? 24.196 -52.727  -20.390  1.00 47.36  ? 46  PHE A O   1 
ATOM   325   C  CB  . PHE A  1 45  ? 22.059 -52.636  -18.590  1.00 48.80  ? 46  PHE A CB  1 
ATOM   326   C  CG  . PHE A  1 45  ? 22.209 -51.230  -18.093  1.00 47.74  ? 46  PHE A CG  1 
ATOM   327   C  CD1 . PHE A  1 45  ? 21.281 -50.266  -18.415  1.00 46.58  ? 46  PHE A CD1 1 
ATOM   328   C  CD2 . PHE A  1 45  ? 23.248 -50.889  -17.256  1.00 48.55  ? 46  PHE A CD2 1 
ATOM   329   C  CE1 . PHE A  1 45  ? 21.407 -48.986  -17.936  1.00 46.05  ? 46  PHE A CE1 1 
ATOM   330   C  CE2 . PHE A  1 45  ? 23.371 -49.611  -16.776  1.00 48.17  ? 46  PHE A CE2 1 
ATOM   331   C  CZ  . PHE A  1 45  ? 22.448 -48.662  -17.116  1.00 46.94  ? 46  PHE A CZ  1 
ATOM   332   N  N   . HIS A  1 46  ? 22.976 -51.697  -21.949  1.00 44.42  ? 47  HIS A N   1 
ATOM   333   C  CA  . HIS A  1 46  ? 24.118 -51.446  -22.811  1.00 43.94  ? 47  HIS A CA  1 
ATOM   334   C  C   . HIS A  1 46  ? 24.218 -50.021  -23.326  1.00 42.35  ? 47  HIS A C   1 
ATOM   335   O  O   . HIS A  1 46  ? 23.242 -49.309  -23.396  1.00 41.58  ? 47  HIS A O   1 
ATOM   336   C  CB  . HIS A  1 46  ? 24.058 -52.386  -23.995  1.00 44.57  ? 47  HIS A CB  1 
ATOM   337   C  CG  . HIS A  1 46  ? 23.620 -53.768  -23.645  1.00 46.10  ? 47  HIS A CG  1 
ATOM   338   N  ND1 . HIS A  1 46  ? 22.362 -54.242  -23.925  1.00 46.54  ? 47  HIS A ND1 1 
ATOM   339   C  CD2 . HIS A  1 46  ? 24.273 -54.781  -23.042  1.00 48.47  ? 47  HIS A CD2 1 
ATOM   340   C  CE1 . HIS A  1 46  ? 22.257 -55.488  -23.515  1.00 48.59  ? 47  HIS A CE1 1 
ATOM   341   N  NE2 . HIS A  1 46  ? 23.406 -55.840  -22.972  1.00 49.74  ? 47  HIS A NE2 1 
ATOM   342   N  N   . VAL A  1 47  ? 25.428 -49.616  -23.674  1.00 42.42  ? 48  VAL A N   1 
ATOM   343   C  CA  . VAL A  1 47  ? 25.662 -48.362  -24.371  1.00 41.30  ? 48  VAL A CA  1 
ATOM   344   C  C   . VAL A  1 47  ? 25.716 -48.663  -25.854  1.00 41.46  ? 48  VAL A C   1 
ATOM   345   O  O   . VAL A  1 47  ? 26.546 -49.443  -26.290  1.00 42.69  ? 48  VAL A O   1 
ATOM   346   C  CB  . VAL A  1 47  ? 26.995 -47.726  -23.964  1.00 41.81  ? 48  VAL A CB  1 
ATOM   347   C  CG1 . VAL A  1 47  ? 27.310 -46.554  -24.848  1.00 41.07  ? 48  VAL A CG1 1 
ATOM   348   C  CG2 . VAL A  1 47  ? 26.963 -47.290  -22.531  1.00 42.21  ? 48  VAL A CG2 1 
ATOM   349   N  N   . HIS A  1 48  ? 24.823 -48.047  -26.618  1.00 40.71  ? 49  HIS A N   1 
ATOM   350   C  CA  . HIS A  1 48  ? 24.761 -48.231  -28.074  1.00 41.34  ? 49  HIS A CA  1 
ATOM   351   C  C   . HIS A  1 48  ? 25.516 -47.154  -28.824  1.00 41.41  ? 49  HIS A C   1 
ATOM   352   O  O   . HIS A  1 48  ? 25.794 -46.099  -28.284  1.00 40.99  ? 49  HIS A O   1 
ATOM   353   C  CB  . HIS A  1 48  ? 23.314 -48.228  -28.551  1.00 41.18  ? 49  HIS A CB  1 
ATOM   354   C  CG  . HIS A  1 48  ? 22.547 -49.448  -28.158  1.00 41.88  ? 49  HIS A CG  1 
ATOM   355   N  ND1 . HIS A  1 48  ? 21.930 -50.266  -29.078  1.00 43.04  ? 49  HIS A ND1 1 
ATOM   356   C  CD2 . HIS A  1 48  ? 22.306 -49.997  -26.946  1.00 41.67  ? 49  HIS A CD2 1 
ATOM   357   C  CE1 . HIS A  1 48  ? 21.338 -51.263  -28.447  1.00 43.62  ? 49  HIS A CE1 1 
ATOM   358   N  NE2 . HIS A  1 48  ? 21.548 -51.120  -27.153  1.00 42.83  ? 49  HIS A NE2 1 
ATOM   359   N  N   . GLU A  1 49  ? 25.801 -47.405  -30.091  1.00 42.53  ? 50  GLU A N   1 
ATOM   360   C  CA  . GLU A  1 49  ? 26.733 -46.569  -30.852  1.00 43.38  ? 50  GLU A CA  1 
ATOM   361   C  C   . GLU A  1 49  ? 26.309 -45.118  -31.000  1.00 42.41  ? 50  GLU A C   1 
ATOM   362   O  O   . GLU A  1 49  ? 27.075 -44.219  -30.710  1.00 42.31  ? 50  GLU A O   1 
ATOM   363   C  CB  . GLU A  1 49  ? 26.975 -47.162  -32.242  1.00 45.46  ? 50  GLU A CB  1 
ATOM   364   C  CG  . GLU A  1 49  ? 28.108 -46.491  -33.033  1.00 47.02  ? 50  GLU A CG  1 
ATOM   365   C  CD  . GLU A  1 49  ? 28.489 -47.222  -34.305  1.00 49.46  ? 50  GLU A CD  1 
ATOM   366   O  OE1 . GLU A  1 49  ? 28.127 -48.390  -34.491  1.00 49.94  ? 50  GLU A OE1 1 
ATOM   367   O  OE2 . GLU A  1 49  ? 29.170 -46.613  -35.136  1.00 51.34  ? 50  GLU A OE2 1 
ATOM   368   N  N   . PHE A  1 50  ? 25.092 -44.902  -31.461  1.00 42.11  ? 51  PHE A N   1 
ATOM   369   C  CA  . PHE A  1 50  ? 24.646 -43.567  -31.856  1.00 42.06  ? 51  PHE A CA  1 
ATOM   370   C  C   . PHE A  1 50  ? 23.733 -42.856  -30.862  1.00 40.68  ? 51  PHE A C   1 
ATOM   371   O  O   . PHE A  1 50  ? 22.827 -43.439  -30.294  1.00 40.05  ? 51  PHE A O   1 
ATOM   372   C  CB  . PHE A  1 50  ? 23.924 -43.640  -33.201  1.00 43.50  ? 51  PHE A CB  1 
ATOM   373   C  CG  . PHE A  1 50  ? 24.719 -44.310  -34.281  1.00 45.44  ? 51  PHE A CG  1 
ATOM   374   C  CD1 . PHE A  1 50  ? 25.956 -43.809  -34.661  1.00 46.53  ? 51  PHE A CD1 1 
ATOM   375   C  CD2 . PHE A  1 50  ? 24.226 -45.436  -34.922  1.00 46.83  ? 51  PHE A CD2 1 
ATOM   376   C  CE1 . PHE A  1 50  ? 26.688 -44.419  -35.656  1.00 48.98  ? 51  PHE A CE1 1 
ATOM   377   C  CE2 . PHE A  1 50  ? 24.958 -46.056  -35.919  1.00 49.05  ? 51  PHE A CE2 1 
ATOM   378   C  CZ  . PHE A  1 50  ? 26.193 -45.547  -36.286  1.00 50.16  ? 51  PHE A CZ  1 
ATOM   379   N  N   . GLY A  1 51  ? 23.975 -41.565  -30.693  1.00 40.67  ? 52  GLY A N   1 
ATOM   380   C  CA  . GLY A  1 51  ? 23.098 -40.692  -29.917  1.00 40.14  ? 52  GLY A CA  1 
ATOM   381   C  C   . GLY A  1 51  ? 21.918 -40.187  -30.728  1.00 40.93  ? 52  GLY A C   1 
ATOM   382   O  O   . GLY A  1 51  ? 21.522 -39.031  -30.637  1.00 41.21  ? 52  GLY A O   1 
ATOM   383   N  N   . ASP A  1 52  ? 21.350 -41.074  -31.525  1.00 41.65  ? 53  ASP A N   1 
ATOM   384   C  CA  . ASP A  1 52  ? 20.297 -40.725  -32.463  1.00 42.97  ? 53  ASP A CA  1 
ATOM   385   C  C   . ASP A  1 52  ? 18.985 -41.230  -31.899  1.00 42.94  ? 53  ASP A C   1 
ATOM   386   O  O   . ASP A  1 52  ? 18.820 -42.406  -31.616  1.00 42.65  ? 53  ASP A O   1 
ATOM   387   C  CB  . ASP A  1 52  ? 20.586 -41.372  -33.815  1.00 44.53  ? 53  ASP A CB  1 
ATOM   388   C  CG  . ASP A  1 52  ? 19.676 -40.891  -34.896  1.00 46.62  ? 53  ASP A CG  1 
ATOM   389   O  OD1 . ASP A  1 52  ? 18.514 -40.567  -34.587  1.00 46.96  ? 53  ASP A OD1 1 
ATOM   390   O  OD2 . ASP A  1 52  ? 20.126 -40.866  -36.062  1.00 48.30  ? 53  ASP A OD2 1 
ATOM   391   N  N   . ASN A  1 53  ? 18.051 -40.317  -31.720  1.00 43.84  ? 54  ASN A N   1 
ATOM   392   C  CA  . ASN A  1 53  ? 16.719 -40.645  -31.189  1.00 44.47  ? 54  ASN A CA  1 
ATOM   393   C  C   . ASN A  1 53  ? 15.610 -40.344  -32.196  1.00 46.65  ? 54  ASN A C   1 
ATOM   394   O  O   . ASN A  1 53  ? 14.431 -40.317  -31.844  1.00 47.56  ? 54  ASN A O   1 
ATOM   395   C  CB  . ASN A  1 53  ? 16.466 -39.859  -29.907  1.00 43.98  ? 54  ASN A CB  1 
ATOM   396   C  CG  . ASN A  1 53  ? 15.961 -40.718  -28.805  1.00 43.92  ? 54  ASN A CG  1 
ATOM   397   O  OD1 . ASN A  1 53  ? 16.663 -41.610  -28.342  1.00 43.29  ? 54  ASN A OD1 1 
ATOM   398   N  ND2 . ASN A  1 53  ? 14.747 -40.457  -28.360  1.00 45.37  ? 54  ASN A ND2 1 
ATOM   399   N  N   . THR A  1 54  ? 16.022 -40.113  -33.442  1.00 47.67  ? 55  THR A N   1 
ATOM   400   C  CA  . THR A  1 54  ? 15.137 -39.751  -34.546  1.00 50.51  ? 55  THR A CA  1 
ATOM   401   C  C   . THR A  1 54  ? 13.868 -40.599  -34.601  1.00 52.15  ? 55  THR A C   1 
ATOM   402   O  O   . THR A  1 54  ? 12.759 -40.090  -34.420  1.00 53.73  ? 55  THR A O   1 
ATOM   403   C  CB  . THR A  1 54  ? 15.906 -39.899  -35.877  1.00 51.72  ? 55  THR A CB  1 
ATOM   404   O  OG1 . THR A  1 54  ? 16.896 -38.862  -35.945  1.00 51.16  ? 55  THR A OG1 1 
ATOM   405   C  CG2 . THR A  1 54  ? 14.954 -39.855  -37.112  1.00 55.29  ? 55  THR A CG2 1 
ATOM   406   N  N   . ALA A  1 55  ? 14.068 -41.894  -34.859  1.00 52.07  ? 56  ALA A N   1 
ATOM   407   C  CA  . ALA A  1 55  ? 12.997 -42.898  -34.907  1.00 53.69  ? 56  ALA A CA  1 
ATOM   408   C  C   . ALA A  1 55  ? 12.971 -43.739  -33.617  1.00 51.84  ? 56  ALA A C   1 
ATOM   409   O  O   . ALA A  1 55  ? 12.897 -44.960  -33.642  1.00 52.16  ? 56  ALA A O   1 
ATOM   410   C  CB  . ALA A  1 55  ? 13.147 -43.788  -36.142  1.00 55.42  ? 56  ALA A CB  1 
ATOM   411   N  N   . GLY A  1 56  ? 13.026 -43.055  -32.484  1.00 50.41  ? 57  GLY A N   1 
ATOM   412   C  CA  . GLY A  1 56  ? 12.942 -43.701  -31.179  1.00 49.27  ? 57  GLY A CA  1 
ATOM   413   C  C   . GLY A  1 56  ? 14.256 -44.276  -30.701  1.00 46.72  ? 57  GLY A C   1 
ATOM   414   O  O   . GLY A  1 56  ? 15.316 -43.751  -30.995  1.00 45.59  ? 57  GLY A O   1 
ATOM   415   N  N   . CYS A  1 57  ? 14.178 -45.348  -29.936  1.00 46.36  ? 58  CYS A N   1 
ATOM   416   C  CA  . CYS A  1 57  ? 15.375 -46.033  -29.474  1.00 44.70  ? 58  CYS A CA  1 
ATOM   417   C  C   . CYS A  1 57  ? 16.057 -46.826  -30.583  1.00 45.13  ? 58  CYS A C   1 
ATOM   418   O  O   . CYS A  1 57  ? 17.254 -47.098  -30.476  1.00 44.05  ? 58  CYS A O   1 
ATOM   419   C  CB  . CYS A  1 57  ? 15.068 -46.999  -28.332  1.00 44.82  ? 58  CYS A CB  1 
ATOM   420   S  SG  . CYS A  1 57  ? 14.638 -46.256  -26.727  1.00 44.70  ? 58  CYS A SG  1 
ATOM   421   N  N   . THR A  1 58  ? 15.307 -47.210  -31.626  1.00 47.12  ? 59  THR A N   1 
ATOM   422   C  CA  . THR A  1 58  ? 15.855 -48.015  -32.749  1.00 48.05  ? 59  THR A CA  1 
ATOM   423   C  C   . THR A  1 58  ? 16.970 -47.320  -33.515  1.00 47.50  ? 59  THR A C   1 
ATOM   424   O  O   . THR A  1 58  ? 17.840 -47.979  -34.060  1.00 47.96  ? 59  THR A O   1 
ATOM   425   C  CB  . THR A  1 58  ? 14.802 -48.342  -33.794  1.00 50.79  ? 59  THR A CB  1 
ATOM   426   O  OG1 . THR A  1 58  ? 13.587 -48.727  -33.145  1.00 52.08  ? 59  THR A OG1 1 
ATOM   427   C  CG2 . THR A  1 58  ? 15.295 -49.463  -34.691  1.00 52.20  ? 59  THR A CG2 1 
ATOM   428   N  N   . SER A  1 59  ? 16.915 -45.993  -33.559  1.00 47.07  ? 60  SER A N   1 
ATOM   429   C  CA  . SER A  1 59  ? 17.910 -45.167  -34.230  1.00 46.87  ? 60  SER A CA  1 
ATOM   430   C  C   . SER A  1 59  ? 19.281 -45.246  -33.593  1.00 45.10  ? 60  SER A C   1 
ATOM   431   O  O   . SER A  1 59  ? 20.274 -44.971  -34.248  1.00 45.68  ? 60  SER A O   1 
ATOM   432   C  CB  . SER A  1 59  ? 17.471 -43.714  -34.211  1.00 46.99  ? 60  SER A CB  1 
ATOM   433   O  OG  . SER A  1 59  ? 16.112 -43.615  -34.535  1.00 49.30  ? 60  SER A OG  1 
ATOM   434   N  N   . ALA A  1 60  ? 19.336 -45.609  -32.320  1.00 43.50  ? 61  ALA A N   1 
ATOM   435   C  CA  . ALA A  1 60  ? 20.592 -45.707  -31.586  1.00 42.23  ? 61  ALA A CA  1 
ATOM   436   C  C   . ALA A  1 60  ? 21.587 -46.671  -32.189  1.00 43.04  ? 61  ALA A C   1 
ATOM   437   O  O   . ALA A  1 60  ? 22.755 -46.628  -31.858  1.00 42.70  ? 61  ALA A O   1 
ATOM   438   C  CB  . ALA A  1 60  ? 20.316 -46.102  -30.167  1.00 41.33  ? 61  ALA A CB  1 
ATOM   439   N  N   . GLY A  1 61  ? 21.119 -47.553  -33.058  1.00 44.73  ? 62  GLY A N   1 
ATOM   440   C  CA  . GLY A  1 61  ? 21.978 -48.531  -33.735  1.00 46.24  ? 62  GLY A CA  1 
ATOM   441   C  C   . GLY A  1 61  ? 22.377 -49.668  -32.805  1.00 45.97  ? 62  GLY A C   1 
ATOM   442   O  O   . GLY A  1 61  ? 21.691 -49.932  -31.812  1.00 45.05  ? 62  GLY A O   1 
ATOM   443   N  N   . PRO A  1 62  ? 23.497 -50.344  -33.106  1.00 47.05  ? 63  PRO A N   1 
ATOM   444   C  CA  . PRO A  1 62  ? 23.908 -51.513  -32.348  1.00 47.40  ? 63  PRO A CA  1 
ATOM   445   C  C   . PRO A  1 62  ? 24.725 -51.182  -31.136  1.00 46.10  ? 63  PRO A C   1 
ATOM   446   O  O   . PRO A  1 62  ? 24.954 -50.014  -30.849  1.00 44.85  ? 63  PRO A O   1 
ATOM   447   C  CB  . PRO A  1 62  ? 24.781 -52.259  -33.337  1.00 49.86  ? 63  PRO A CB  1 
ATOM   448   C  CG  . PRO A  1 62  ? 25.405 -51.191  -34.116  1.00 50.07  ? 63  PRO A CG  1 
ATOM   449   C  CD  . PRO A  1 62  ? 24.388 -50.103  -34.247  1.00 48.65  ? 63  PRO A CD  1 
ATOM   450   N  N   . HIS A  1 63  ? 25.156 -52.228  -30.441  1.00 46.90  ? 64  HIS A N   1 
ATOM   451   C  CA  . HIS A  1 63  ? 26.004 -52.109  -29.257  1.00 46.47  ? 64  HIS A CA  1 
ATOM   452   C  C   . HIS A  1 63  ? 27.278 -51.384  -29.607  1.00 46.88  ? 64  HIS A C   1 
ATOM   453   O  O   . HIS A  1 63  ? 27.880 -51.711  -30.618  1.00 48.73  ? 64  HIS A O   1 
ATOM   454   C  CB  . HIS A  1 63  ? 26.386 -53.490  -28.747  1.00 48.27  ? 64  HIS A CB  1 
ATOM   455   C  CG  . HIS A  1 63  ? 25.271 -54.222  -28.075  1.00 48.09  ? 64  HIS A CG  1 
ATOM   456   N  ND1 . HIS A  1 63  ? 25.478 -55.081  -27.016  1.00 48.95  ? 64  HIS A ND1 1 
ATOM   457   C  CD2 . HIS A  1 63  ? 23.938 -54.218  -28.302  1.00 47.52  ? 64  HIS A CD2 1 
ATOM   458   C  CE1 . HIS A  1 63  ? 24.317 -55.566  -26.613  1.00 49.16  ? 64  HIS A CE1 1 
ATOM   459   N  NE2 . HIS A  1 63  ? 23.369 -55.068  -27.384  1.00 48.25  ? 64  HIS A NE2 1 
ATOM   460   N  N   . PHE A  1 64  ? 27.700 -50.424  -28.782  1.00 45.70  ? 65  PHE A N   1 
ATOM   461   C  CA  . PHE A  1 64  ? 28.912 -49.635  -29.072  1.00 46.42  ? 65  PHE A CA  1 
ATOM   462   C  C   . PHE A  1 64  ? 30.127 -50.556  -29.113  1.00 48.86  ? 65  PHE A C   1 
ATOM   463   O  O   . PHE A  1 64  ? 30.468 -51.201  -28.135  1.00 49.37  ? 65  PHE A O   1 
ATOM   464   C  CB  . PHE A  1 64  ? 29.097 -48.511  -28.046  1.00 45.23  ? 65  PHE A CB  1 
ATOM   465   C  CG  . PHE A  1 64  ? 30.326 -47.660  -28.265  1.00 46.08  ? 65  PHE A CG  1 
ATOM   466   C  CD1 . PHE A  1 64  ? 30.688 -47.234  -29.535  1.00 47.03  ? 65  PHE A CD1 1 
ATOM   467   C  CD2 . PHE A  1 64  ? 31.103 -47.263  -27.181  1.00 46.72  ? 65  PHE A CD2 1 
ATOM   468   C  CE1 . PHE A  1 64  ? 31.808 -46.450  -29.729  1.00 48.67  ? 65  PHE A CE1 1 
ATOM   469   C  CE2 . PHE A  1 64  ? 32.223 -46.474  -27.367  1.00 48.31  ? 65  PHE A CE2 1 
ATOM   470   C  CZ  . PHE A  1 64  ? 32.577 -46.064  -28.648  1.00 49.25  ? 65  PHE A CZ  1 
ATOM   471   N  N   . ASN A  1 65  ? 30.770 -50.619  -30.266  1.00 50.80  ? 66  ASN A N   1 
ATOM   472   C  CA  . ASN A  1 65  ? 31.766 -51.657  -30.528  1.00 53.95  ? 66  ASN A CA  1 
ATOM   473   C  C   . ASN A  1 65  ? 32.906 -51.186  -31.445  1.00 56.42  ? 66  ASN A C   1 
ATOM   474   O  O   . ASN A  1 65  ? 33.036 -51.638  -32.586  1.00 58.49  ? 66  ASN A O   1 
ATOM   475   C  CB  . ASN A  1 65  ? 31.055 -52.864  -31.149  1.00 54.85  ? 66  ASN A CB  1 
ATOM   476   C  CG  . ASN A  1 65  ? 31.965 -54.050  -31.341  1.00 58.19  ? 66  ASN A CG  1 
ATOM   477   O  OD1 . ASN A  1 65  ? 33.103 -54.071  -30.888  1.00 60.13  ? 66  ASN A OD1 1 
ATOM   478   N  ND2 . ASN A  1 65  ? 31.460 -55.053  -32.018  1.00 59.62  ? 66  ASN A ND2 1 
ATOM   479   N  N   . PRO A  1 66  ? 33.749 -50.284  -30.941  1.00 56.59  ? 67  PRO A N   1 
ATOM   480   C  CA  . PRO A  1 66  ? 34.783 -49.684  -31.750  1.00 59.01  ? 67  PRO A CA  1 
ATOM   481   C  C   . PRO A  1 66  ? 35.966 -50.608  -31.967  1.00 63.16  ? 67  PRO A C   1 
ATOM   482   O  O   . PRO A  1 66  ? 36.687 -50.432  -32.948  1.00 66.18  ? 67  PRO A O   1 
ATOM   483   C  CB  . PRO A  1 66  ? 35.211 -48.479  -30.921  1.00 58.04  ? 67  PRO A CB  1 
ATOM   484   C  CG  . PRO A  1 66  ? 34.961 -48.882  -29.539  1.00 56.72  ? 67  PRO A CG  1 
ATOM   485   C  CD  . PRO A  1 66  ? 33.757 -49.766  -29.568  1.00 55.01  ? 67  PRO A CD  1 
ATOM   486   N  N   . LEU A  1 67  ? 36.179 -51.569  -31.064  1.00 63.90  ? 68  LEU A N   1 
ATOM   487   C  CA  . LEU A  1 67  ? 37.288 -52.538  -31.214  1.00 68.19  ? 68  LEU A CA  1 
ATOM   488   C  C   . LEU A  1 67  ? 36.875 -53.808  -31.995  1.00 69.72  ? 68  LEU A C   1 
ATOM   489   O  O   . LEU A  1 67  ? 37.605 -54.802  -32.041  1.00 73.16  ? 68  LEU A O   1 
ATOM   490   C  CB  . LEU A  1 67  ? 37.875 -52.891  -29.845  1.00 69.09  ? 68  LEU A CB  1 
ATOM   491   C  CG  . LEU A  1 67  ? 38.438 -51.716  -29.016  1.00 68.66  ? 68  LEU A CG  1 
ATOM   492   C  CD1 . LEU A  1 67  ? 39.198 -52.223  -27.798  1.00 70.87  ? 68  LEU A CD1 1 
ATOM   493   C  CD2 . LEU A  1 67  ? 39.350 -50.782  -29.834  1.00 70.69  ? 68  LEU A CD2 1 
ATOM   494   N  N   . SER A  1 68  ? 35.690 -53.751  -32.608  1.00 67.47  ? 69  SER A N   1 
ATOM   495   C  CA  . SER A  1 68  ? 35.215 -54.766  -33.554  1.00 69.06  ? 69  SER A CA  1 
ATOM   496   C  C   . SER A  1 68  ? 35.220 -56.171  -32.975  1.00 70.50  ? 69  SER A C   1 
ATOM   497   O  O   . SER A  1 68  ? 35.667 -57.100  -33.629  1.00 74.06  ? 69  SER A O   1 
ATOM   498   C  CB  . SER A  1 68  ? 36.066 -54.731  -34.827  1.00 73.13  ? 69  SER A CB  1 
ATOM   499   O  OG  . SER A  1 68  ? 36.254 -53.404  -35.287  1.00 72.62  ? 69  SER A OG  1 
ATOM   500   N  N   . ARG A  1 69  ? 34.720 -56.311  -31.753  1.00 68.09  ? 70  ARG A N   1 
ATOM   501   C  CA  . ARG A  1 69  ? 34.714 -57.592  -31.059  1.00 69.92  ? 70  ARG A CA  1 
ATOM   502   C  C   . ARG A  1 69  ? 33.318 -58.184  -30.993  1.00 67.79  ? 70  ARG A C   1 
ATOM   503   O  O   . ARG A  1 69  ? 32.370 -57.597  -31.487  1.00 65.22  ? 70  ARG A O   1 
ATOM   504   C  CB  . ARG A  1 69  ? 35.277 -57.433  -29.646  1.00 69.89  ? 70  ARG A CB  1 
ATOM   505   C  CG  . ARG A  1 69  ? 36.706 -56.922  -29.605  1.00 74.21  ? 70  ARG A CG  1 
ATOM   506   C  CD  . ARG A  1 69  ? 37.727 -57.976  -29.160  1.00 81.39  ? 70  ARG A CD  1 
ATOM   507   N  NE  . ARG A  1 69  ? 39.112 -57.462  -29.195  1.00 87.14  ? 70  ARG A NE  1 
ATOM   508   C  CZ  . ARG A  1 69  ? 39.684 -56.655  -28.280  1.00 87.14  ? 70  ARG A CZ  1 
ATOM   509   N  NH1 . ARG A  1 69  ? 39.027 -56.235  -27.199  1.00 83.31  ? 70  ARG A NH1 1 
ATOM   510   N  NH2 . ARG A  1 69  ? 40.940 -56.253  -28.455  1.00 90.51  ? 70  ARG A NH2 1 
ATOM   511   N  N   . LYS A  1 70  ? 33.226 -59.374  -30.395  1.00 69.54  ? 71  LYS A N   1 
ATOM   512   C  CA  . LYS A  1 70  ? 31.962 -60.106  -30.191  1.00 68.38  ? 71  LYS A CA  1 
ATOM   513   C  C   . LYS A  1 70  ? 31.299 -59.705  -28.884  1.00 65.28  ? 71  LYS A C   1 
ATOM   514   O  O   . LYS A  1 70  ? 31.966 -59.219  -27.977  1.00 64.81  ? 71  LYS A O   1 
ATOM   515   C  CB  . LYS A  1 70  ? 32.212 -61.620  -30.150  1.00 72.21  ? 71  LYS A CB  1 
ATOM   516   C  CG  . LYS A  1 70  ? 32.918 -62.202  -31.380  1.00 76.35  ? 71  LYS A CG  1 
ATOM   517   C  CD  . LYS A  1 70  ? 31.908 -62.745  -32.391  1.00 77.06  ? 71  LYS A CD  1 
ATOM   518   C  CE  . LYS A  1 70  ? 32.563 -63.443  -33.576  1.00 81.74  ? 71  LYS A CE  1 
ATOM   519   N  NZ  . LYS A  1 70  ? 31.503 -64.002  -34.506  1.00 82.12  ? 71  LYS A NZ  1 
ATOM   520   N  N   . HIS A  1 71  ? 29.988 -59.934  -28.791  1.00 63.54  ? 72  HIS A N   1 
ATOM   521   C  CA  . HIS A  1 71  ? 29.232 -59.586  -27.576  1.00 61.20  ? 72  HIS A CA  1 
ATOM   522   C  C   . HIS A  1 71  ? 29.717 -60.392  -26.396  1.00 63.17  ? 72  HIS A C   1 
ATOM   523   O  O   . HIS A  1 71  ? 30.241 -61.479  -26.560  1.00 66.50  ? 72  HIS A O   1 
ATOM   524   C  CB  . HIS A  1 71  ? 27.713 -59.780  -27.747  1.00 59.78  ? 72  HIS A CB  1 
ATOM   525   C  CG  . HIS A  1 71  ? 26.902 -59.374  -26.542  1.00 57.79  ? 72  HIS A CG  1 
ATOM   526   N  ND1 . HIS A  1 71  ? 26.744 -58.060  -26.154  1.00 55.05  ? 72  HIS A ND1 1 
ATOM   527   C  CD2 . HIS A  1 71  ? 26.205 -60.114  -25.648  1.00 58.42  ? 72  HIS A CD2 1 
ATOM   528   C  CE1 . HIS A  1 71  ? 25.992 -58.013  -25.069  1.00 54.23  ? 72  HIS A CE1 1 
ATOM   529   N  NE2 . HIS A  1 71  ? 25.647 -59.245  -24.746  1.00 55.97  ? 72  HIS A NE2 1 
ATOM   530   N  N   . GLY A  1 72  ? 29.553 -59.844  -25.205  1.00 61.64  ? 73  GLY A N   1 
ATOM   531   C  CA  . GLY A  1 72  ? 29.909 -60.558  -23.996  1.00 63.94  ? 73  GLY A CA  1 
ATOM   532   C  C   . GLY A  1 72  ? 29.443 -59.877  -22.725  1.00 62.27  ? 73  GLY A C   1 
ATOM   533   O  O   . GLY A  1 72  ? 28.781 -58.846  -22.751  1.00 59.31  ? 73  GLY A O   1 
ATOM   534   N  N   . GLY A  1 73  ? 29.786 -60.488  -21.601  1.00 64.74  ? 74  GLY A N   1 
ATOM   535   C  CA  . GLY A  1 73  ? 29.499 -59.919  -20.293  1.00 64.18  ? 74  GLY A CA  1 
ATOM   536   C  C   . GLY A  1 73  ? 30.556 -58.883  -19.972  1.00 63.94  ? 74  GLY A C   1 
ATOM   537   O  O   . GLY A  1 73  ? 31.631 -58.891  -20.571  1.00 65.34  ? 74  GLY A O   1 
ATOM   538   N  N   . PRO A  1 74  ? 30.273 -57.983  -19.019  1.00 62.80  ? 75  PRO A N   1 
ATOM   539   C  CA  . PRO A  1 74  ? 31.231 -56.897  -18.733  1.00 62.58  ? 75  PRO A CA  1 
ATOM   540   C  C   . PRO A  1 74  ? 32.577 -57.391  -18.217  1.00 66.48  ? 75  PRO A C   1 
ATOM   541   O  O   . PRO A  1 74  ? 33.610 -56.845  -18.585  1.00 67.13  ? 75  PRO A O   1 
ATOM   542   C  CB  . PRO A  1 74  ? 30.519 -56.065  -17.663  1.00 61.31  ? 75  PRO A CB  1 
ATOM   543   C  CG  . PRO A  1 74  ? 29.498 -56.976  -17.082  1.00 62.42  ? 75  PRO A CG  1 
ATOM   544   C  CD  . PRO A  1 74  ? 29.086 -57.932  -18.149  1.00 62.07  ? 75  PRO A CD  1 
ATOM   545   N  N   . LYS A  1 75  ? 32.554 -58.433  -17.394  1.00 69.58  ? 76  LYS A N   1 
ATOM   546   C  CA  . LYS A  1 75  ? 33.783 -59.035  -16.884  1.00 73.99  ? 76  LYS A CA  1 
ATOM   547   C  C   . LYS A  1 75  ? 34.565 -59.757  -17.972  1.00 75.65  ? 76  LYS A C   1 
ATOM   548   O  O   . LYS A  1 75  ? 35.778 -59.857  -17.890  1.00 78.86  ? 76  LYS A O   1 
ATOM   549   C  CB  . LYS A  1 75  ? 33.485 -60.051  -15.793  1.00 77.39  ? 76  LYS A CB  1 
ATOM   550   C  CG  . LYS A  1 75  ? 32.534 -59.584  -14.714  1.00 76.85  ? 76  LYS A CG  1 
ATOM   551   C  CD  . LYS A  1 75  ? 32.762 -60.404  -13.436  1.00 81.79  ? 76  LYS A CD  1 
ATOM   552   C  CE  . LYS A  1 75  ? 31.654 -60.164  -12.398  1.00 81.60  ? 76  LYS A CE  1 
ATOM   553   N  NZ  . LYS A  1 75  ? 31.673 -61.178  -11.306  1.00 86.37  ? 76  LYS A NZ  1 
ATOM   554   N  N   . ASP A  1 76  ? 33.870 -60.291  -18.968  1.00 74.12  ? 77  ASP A N   1 
ATOM   555   C  CA  . ASP A  1 76  ? 34.543 -60.941  -20.088  1.00 76.05  ? 77  ASP A CA  1 
ATOM   556   C  C   . ASP A  1 76  ? 35.534 -59.977  -20.758  1.00 75.79  ? 77  ASP A C   1 
ATOM   557   O  O   . ASP A  1 76  ? 35.286 -58.762  -20.834  1.00 72.69  ? 77  ASP A O   1 
ATOM   558   C  CB  . ASP A  1 76  ? 33.525 -61.477  -21.106  1.00 74.21  ? 77  ASP A CB  1 
ATOM   559   C  CG  . ASP A  1 76  ? 32.776 -62.680  -20.585  1.00 76.11  ? 77  ASP A CG  1 
ATOM   560   O  OD1 . ASP A  1 76  ? 33.339 -63.387  -19.730  1.00 80.02  ? 77  ASP A OD1 1 
ATOM   561   O  OD2 . ASP A  1 76  ? 31.631 -62.919  -21.025  1.00 74.45  ? 77  ASP A OD2 1 
ATOM   562   N  N   . GLU A  1 77  ? 36.676 -60.504  -21.202  1.00 79.56  ? 78  GLU A N   1 
ATOM   563   C  CA  . GLU A  1 77  ? 37.612 -59.697  -21.984  1.00 79.88  ? 78  GLU A CA  1 
ATOM   564   C  C   . GLU A  1 77  ? 37.043 -59.470  -23.377  1.00 77.10  ? 78  GLU A C   1 
ATOM   565   O  O   . GLU A  1 77  ? 37.003 -58.328  -23.844  1.00 74.42  ? 78  GLU A O   1 
ATOM   566   C  CB  . GLU A  1 77  ? 38.990 -60.348  -22.090  1.00 85.44  ? 78  GLU A CB  1 
ATOM   567   C  CG  . GLU A  1 77  ? 39.815 -59.759  -23.267  1.00 86.63  ? 78  GLU A CG  1 
ATOM   568   C  CD  . GLU A  1 77  ? 41.287 -60.089  -23.213  1.00 93.03  ? 78  GLU A CD  1 
ATOM   569   O  OE1 . GLU A  1 77  ? 41.641 -61.216  -22.747  1.00 97.17  ? 78  GLU A OE1 1 
ATOM   570   O  OE2 . GLU A  1 77  ? 42.081 -59.215  -23.662  1.00 93.92  ? 78  GLU A OE2 1 
ATOM   571   N  N   . GLU A  1 78  ? 36.638 -60.571  -24.026  1.00 78.19  ? 79  GLU A N   1 
ATOM   572   C  CA  . GLU A  1 78  ? 35.950 -60.519  -25.327  1.00 76.02  ? 79  GLU A CA  1 
ATOM   573   C  C   . GLU A  1 78  ? 34.533 -60.010  -25.120  1.00 71.42  ? 79  GLU A C   1 
ATOM   574   O  O   . GLU A  1 78  ? 33.598 -60.795  -24.910  1.00 71.04  ? 79  GLU A O   1 
ATOM   575   C  CB  . GLU A  1 78  ? 35.930 -61.885  -26.031  1.00 79.17  ? 79  GLU A CB  1 
ATOM   576   C  CG  . GLU A  1 78  ? 35.356 -61.863  -27.470  1.00 77.98  ? 79  GLU A CG  1 
ATOM   577   C  CD  . GLU A  1 78  ? 36.327 -61.287  -28.525  1.00 79.86  ? 79  GLU A CD  1 
ATOM   578   O  OE1 . GLU A  1 78  ? 37.455 -60.871  -28.154  1.00 82.18  ? 79  GLU A OE1 1 
ATOM   579   O  OE2 . GLU A  1 78  ? 35.967 -61.253  -29.733  1.00 79.40  ? 79  GLU A OE2 1 
ATOM   580   N  N   . ARG A  1 79  ? 34.414 -58.680  -25.168  1.00 68.38  ? 80  ARG A N   1 
ATOM   581   C  CA  . ARG A  1 79  ? 33.141 -57.965  -25.045  1.00 64.17  ? 80  ARG A CA  1 
ATOM   582   C  C   . ARG A  1 79  ? 33.099 -56.742  -25.958  1.00 61.85  ? 80  ARG A C   1 
ATOM   583   O  O   . ARG A  1 79  ? 34.133 -56.292  -26.475  1.00 63.19  ? 80  ARG A O   1 
ATOM   584   C  CB  . ARG A  1 79  ? 32.927 -57.499  -23.611  1.00 63.05  ? 80  ARG A CB  1 
ATOM   585   C  CG  . ARG A  1 79  ? 34.038 -56.612  -23.085  1.00 63.86  ? 80  ARG A CG  1 
ATOM   586   C  CD  . ARG A  1 79  ? 33.688 -56.001  -21.733  1.00 62.89  ? 80  ARG A CD  1 
ATOM   587   N  NE  . ARG A  1 79  ? 32.917 -54.764  -21.859  1.00 59.29  ? 80  ARG A NE  1 
ATOM   588   C  CZ  . ARG A  1 79  ? 32.691 -53.906  -20.867  1.00 58.17  ? 80  ARG A CZ  1 
ATOM   589   N  NH1 . ARG A  1 79  ? 33.158 -54.135  -19.645  1.00 60.44  ? 80  ARG A NH1 1 
ATOM   590   N  NH2 . ARG A  1 79  ? 31.988 -52.809  -21.097  1.00 55.42  ? 80  ARG A NH2 1 
ATOM   591   N  N   . HIS A  1 80  ? 31.892 -56.209  -26.150  1.00 58.76  ? 81  HIS A N   1 
ATOM   592   C  CA  . HIS A  1 80  ? 31.733 -54.885  -26.753  1.00 56.31  ? 81  HIS A CA  1 
ATOM   593   C  C   . HIS A  1 80  ? 32.068 -53.840  -25.700  1.00 55.22  ? 81  HIS A C   1 
ATOM   594   O  O   . HIS A  1 80  ? 31.790 -54.031  -24.518  1.00 55.19  ? 81  HIS A O   1 
ATOM   595   C  CB  . HIS A  1 80  ? 30.311 -54.639  -27.229  1.00 53.68  ? 81  HIS A CB  1 
ATOM   596   C  CG  . HIS A  1 80  ? 29.843 -55.586  -28.276  1.00 54.65  ? 81  HIS A CG  1 
ATOM   597   N  ND1 . HIS A  1 80  ? 28.526 -55.969  -28.387  1.00 53.40  ? 81  HIS A ND1 1 
ATOM   598   C  CD2 . HIS A  1 80  ? 30.507 -56.207  -29.273  1.00 57.24  ? 81  HIS A CD2 1 
ATOM   599   C  CE1 . HIS A  1 80  ? 28.401 -56.784  -29.416  1.00 55.39  ? 81  HIS A CE1 1 
ATOM   600   N  NE2 . HIS A  1 80  ? 29.590 -56.951  -29.965  1.00 57.64  ? 81  HIS A NE2 1 
ATOM   601   N  N   . VAL A  1 81  ? 32.643 -52.724  -26.124  1.00 54.76  ? 82  VAL A N   1 
ATOM   602   C  CA  . VAL A  1 81  ? 32.941 -51.627  -25.196  1.00 53.77  ? 82  VAL A CA  1 
ATOM   603   C  C   . VAL A  1 81  ? 31.685 -51.232  -24.435  1.00 50.89  ? 82  VAL A C   1 
ATOM   604   O  O   . VAL A  1 81  ? 31.724 -50.967  -23.261  1.00 50.94  ? 82  VAL A O   1 
ATOM   605   C  CB  . VAL A  1 81  ? 33.516 -50.390  -25.927  1.00 53.53  ? 82  VAL A CB  1 
ATOM   606   C  CG1 . VAL A  1 81  ? 33.619 -49.203  -24.990  1.00 52.34  ? 82  VAL A CG1 1 
ATOM   607   C  CG2 . VAL A  1 81  ? 34.890 -50.721  -26.525  1.00 57.18  ? 82  VAL A CG2 1 
ATOM   608   N  N   . GLY A  1 82  ? 30.560 -51.233  -25.116  1.00 49.05  ? 83  GLY A N   1 
ATOM   609   C  CA  . GLY A  1 82  ? 29.303 -50.812  -24.523  1.00 47.02  ? 83  GLY A CA  1 
ATOM   610   C  C   . GLY A  1 82  ? 28.515 -51.864  -23.784  1.00 47.47  ? 83  GLY A C   1 
ATOM   611   O  O   . GLY A  1 82  ? 27.399 -51.595  -23.351  1.00 46.13  ? 83  GLY A O   1 
ATOM   612   N  N   . ASP A  1 83  ? 29.075 -53.064  -23.645  1.00 49.74  ? 84  ASP A N   1 
ATOM   613   C  CA  . ASP A  1 83  ? 28.393 -54.157  -22.950  1.00 50.55  ? 84  ASP A CA  1 
ATOM   614   C  C   . ASP A  1 83  ? 28.526 -53.997  -21.452  1.00 51.36  ? 84  ASP A C   1 
ATOM   615   O  O   . ASP A  1 83  ? 29.503 -54.446  -20.885  1.00 53.79  ? 84  ASP A O   1 
ATOM   616   C  CB  . ASP A  1 83  ? 28.967 -55.508  -23.365  1.00 52.98  ? 84  ASP A CB  1 
ATOM   617   C  CG  . ASP A  1 83  ? 28.547 -55.926  -24.742  1.00 52.56  ? 84  ASP A CG  1 
ATOM   618   O  OD1 . ASP A  1 83  ? 27.552 -55.433  -25.273  1.00 50.32  ? 84  ASP A OD1 1 
ATOM   619   O  OD2 . ASP A  1 83  ? 29.208 -56.785  -25.322  1.00 55.06  ? 84  ASP A OD2 1 
ATOM   620   N  N   . LEU A  1 84  ? 27.549 -53.357  -20.818  1.00 49.93  ? 85  LEU A N   1 
ATOM   621   C  CA  . LEU A  1 84  ? 27.541 -53.196  -19.357  1.00 51.16  ? 85  LEU A CA  1 
ATOM   622   C  C   . LEU A  1 84  ? 26.737 -54.278  -18.633  1.00 52.86  ? 85  LEU A C   1 
ATOM   623   O  O   . LEU A  1 84  ? 26.482 -54.169  -17.431  1.00 54.11  ? 85  LEU A O   1 
ATOM   624   C  CB  . LEU A  1 84  ? 27.012 -51.824  -18.962  1.00 49.39  ? 85  LEU A CB  1 
ATOM   625   C  CG  . LEU A  1 84  ? 28.007 -50.690  -19.180  1.00 48.68  ? 85  LEU A CG  1 
ATOM   626   C  CD1 . LEU A  1 84  ? 27.369 -49.358  -18.856  1.00 47.08  ? 85  LEU A CD1 1 
ATOM   627   C  CD2 . LEU A  1 84  ? 29.259 -50.909  -18.348  1.00 50.98  ? 85  LEU A CD2 1 
ATOM   628   N  N   . GLY A  1 85  ? 26.341 -55.317  -19.358  1.00 53.30  ? 86  GLY A N   1 
ATOM   629   C  CA  . GLY A  1 85  ? 25.724 -56.486  -18.747  1.00 55.49  ? 86  GLY A CA  1 
ATOM   630   C  C   . GLY A  1 85  ? 24.278 -56.259  -18.339  1.00 54.83  ? 86  GLY A C   1 
ATOM   631   O  O   . GLY A  1 85  ? 23.503 -55.720  -19.120  1.00 52.91  ? 86  GLY A O   1 
ATOM   632   N  N   . ASN A  1 86  ? 23.920 -56.674  -17.119  1.00 56.95  ? 87  ASN A N   1 
ATOM   633   C  CA  . ASN A  1 86  ? 22.525 -56.651  -16.648  1.00 57.14  ? 87  ASN A CA  1 
ATOM   634   C  C   . ASN A  1 86  ? 22.267 -55.704  -15.497  1.00 57.51  ? 87  ASN A C   1 
ATOM   635   O  O   . ASN A  1 86  ? 23.193 -55.318  -14.771  1.00 58.34  ? 87  ASN A O   1 
ATOM   636   C  CB  . ASN A  1 86  ? 22.077 -58.034  -16.213  1.00 60.14  ? 87  ASN A CB  1 
ATOM   637   C  CG  . ASN A  1 86  ? 21.790 -58.942  -17.378  1.00 60.19  ? 87  ASN A CG  1 
ATOM   638   O  OD1 . ASN A  1 86  ? 20.995 -58.622  -18.259  1.00 58.68  ? 87  ASN A OD1 1 
ATOM   639   N  ND2 . ASN A  1 86  ? 22.426 -60.094  -17.383  1.00 62.72  ? 87  ASN A ND2 1 
ATOM   640   N  N   . VAL A  1 87  ? 20.997 -55.314  -15.369  1.00 57.30  ? 88  VAL A N   1 
ATOM   641   C  CA  . VAL A  1 87  ? 20.494 -54.568  -14.206  1.00 58.60  ? 88  VAL A CA  1 
ATOM   642   C  C   . VAL A  1 87  ? 19.296 -55.305  -13.637  1.00 61.34  ? 88  VAL A C   1 
ATOM   643   O  O   . VAL A  1 87  ? 18.462 -55.803  -14.392  1.00 60.99  ? 88  VAL A O   1 
ATOM   644   C  CB  . VAL A  1 87  ? 20.046 -53.130  -14.541  1.00 56.09  ? 88  VAL A CB  1 
ATOM   645   C  CG1 . VAL A  1 87  ? 21.236 -52.273  -14.927  1.00 53.95  ? 88  VAL A CG1 1 
ATOM   646   C  CG2 . VAL A  1 87  ? 19.006 -53.139  -15.634  1.00 54.66  ? 88  VAL A CG2 1 
ATOM   647   N  N   . THR A  1 88  ? 19.204 -55.344  -12.307  1.00 64.47  ? 89  THR A N   1 
ATOM   648   C  CA  . THR A  1 88  ? 18.179 -56.148  -11.616  1.00 68.05  ? 89  THR A CA  1 
ATOM   649   C  C   . THR A  1 88  ? 17.002 -55.328  -11.055  1.00 69.17  ? 89  THR A C   1 
ATOM   650   O  O   . THR A  1 88  ? 17.183 -54.366  -10.295  1.00 69.54  ? 89  THR A O   1 
ATOM   651   C  CB  . THR A  1 88  ? 18.793 -56.978  -10.466  1.00 71.87  ? 89  THR A CB  1 
ATOM   652   O  OG1 . THR A  1 88  ? 19.678 -57.959  -11.005  1.00 71.92  ? 89  THR A OG1 1 
ATOM   653   C  CG2 . THR A  1 88  ? 17.692 -57.688  -9.673   1.00 76.07  ? 89  THR A CG2 1 
ATOM   654   N  N   . ALA A  1 89  ? 15.797 -55.739  -11.428  1.00 70.09  ? 90  ALA A N   1 
ATOM   655   C  CA  . ALA A  1 89  ? 14.572 -55.037  -11.036  1.00 71.61  ? 90  ALA A CA  1 
ATOM   656   C  C   . ALA A  1 89  ? 13.853 -55.781  -9.936   1.00 76.60  ? 90  ALA A C   1 
ATOM   657   O  O   . ALA A  1 89  ? 13.629 -56.979  -10.044  1.00 78.63  ? 90  ALA A O   1 
ATOM   658   C  CB  . ALA A  1 89  ? 13.642 -54.881  -12.239  1.00 69.84  ? 90  ALA A CB  1 
ATOM   659   N  N   . ASP A  1 90  ? 13.474 -55.064  -8.886   1.00 79.13  ? 91  ASP A N   1 
ATOM   660   C  CA  . ASP A  1 90  ? 12.748 -55.670  -7.754   1.00 84.59  ? 91  ASP A CA  1 
ATOM   661   C  C   . ASP A  1 90  ? 11.210 -55.610  -7.925   1.00 86.76  ? 91  ASP A C   1 
ATOM   662   O  O   . ASP A  1 90  ? 10.704 -54.867  -8.758   1.00 84.27  ? 91  ASP A O   1 
ATOM   663   C  CB  . ASP A  1 90  ? 13.224 -55.071  -6.405   1.00 87.20  ? 91  ASP A CB  1 
ATOM   664   C  CG  . ASP A  1 90  ? 12.771 -53.640  -6.175   1.00 86.90  ? 91  ASP A CG  1 
ATOM   665   O  OD1 . ASP A  1 90  ? 13.069 -53.130  -5.082   1.00 89.63  ? 91  ASP A OD1 1 
ATOM   666   O  OD2 . ASP A  1 90  ? 12.122 -53.025  -7.052   1.00 84.62  ? 91  ASP A OD2 1 
ATOM   667   N  N   . LYS A  1 91  ? 10.506 -56.425  -7.137   1.00 91.91  ? 92  LYS A N   1 
ATOM   668   C  CA  . LYS A  1 91  ? 9.017  -56.531  -7.111   1.00 95.48  ? 92  LYS A CA  1 
ATOM   669   C  C   . LYS A  1 91  ? 8.266  -55.353  -7.722   1.00 93.64  ? 92  LYS A C   1 
ATOM   670   O  O   . LYS A  1 91  ? 7.559  -55.512  -8.718   1.00 92.61  ? 92  LYS A O   1 
ATOM   671   C  CB  . LYS A  1 91  ? 8.456  -56.694  -5.673   1.00 101.94 ? 92  LYS A CB  1 
ATOM   672   C  CG  . LYS A  1 91  ? 9.380  -57.275  -4.605   1.00 104.79 ? 92  LYS A CG  1 
ATOM   673   C  CD  . LYS A  1 91  ? 9.641  -58.778  -4.826   1.00 106.42 ? 92  LYS A CD  1 
ATOM   674   C  CE  . LYS A  1 91  ? 10.137 -59.496  -3.546   1.00 111.19 ? 92  LYS A CE  1 
ATOM   675   N  NZ  . LYS A  1 91  ? 9.018  -60.024  -2.698   1.00 118.07 ? 92  LYS A NZ  1 
ATOM   676   N  N   . ASP A  1 92  ? 8.418  -54.179  -7.099   1.00 93.74  ? 93  ASP A N   1 
ATOM   677   C  CA  . ASP A  1 92  ? 7.636  -52.966  -7.453   1.00 93.26  ? 93  ASP A CA  1 
ATOM   678   C  C   . ASP A  1 92  ? 8.214  -52.232  -8.690   1.00 87.27  ? 93  ASP A C   1 
ATOM   679   O  O   . ASP A  1 92  ? 7.897  -51.063  -8.947   1.00 86.42  ? 93  ASP A O   1 
ATOM   680   C  CB  . ASP A  1 92  ? 7.424  -51.995  -6.246   1.00 96.79  ? 93  ASP A CB  1 
ATOM   681   C  CG  . ASP A  1 92  ? 8.160  -52.432  -4.947   1.00 100.14 ? 93  ASP A CG  1 
ATOM   682   O  OD1 . ASP A  1 92  ? 9.418  -52.446  -4.920   1.00 97.26  ? 93  ASP A OD1 1 
ATOM   683   O  OD2 . ASP A  1 92  ? 7.466  -52.741  -3.942   1.00 105.85 ? 93  ASP A OD2 1 
ATOM   684   N  N   . GLY A  1 93  ? 9.052  -52.937  -9.451   1.00 83.73  ? 94  GLY A N   1 
ATOM   685   C  CA  . GLY A  1 93  ? 9.501  -52.495  -10.773  1.00 78.50  ? 94  GLY A CA  1 
ATOM   686   C  C   . GLY A  1 93  ? 10.745 -51.635  -10.779  1.00 74.77  ? 94  GLY A C   1 
ATOM   687   O  O   . GLY A  1 93  ? 11.166 -51.171  -11.828  1.00 70.85  ? 94  GLY A O   1 
ATOM   688   N  N   . VAL A  1 94  ? 11.334 -51.414  -9.614   1.00 76.13  ? 95  VAL A N   1 
ATOM   689   C  CA  . VAL A  1 94  ? 12.418 -50.466  -9.501   1.00 73.43  ? 95  VAL A CA  1 
ATOM   690   C  C   . VAL A  1 94  ? 13.767 -51.174  -9.510   1.00 72.07  ? 95  VAL A C   1 
ATOM   691   O  O   . VAL A  1 94  ? 13.947 -52.211  -8.869   1.00 74.82  ? 95  VAL A O   1 
ATOM   692   C  CB  . VAL A  1 94  ? 12.246 -49.620  -8.257   1.00 76.51  ? 95  VAL A CB  1 
ATOM   693   C  CG1 . VAL A  1 94  ? 13.560 -48.947  -7.886   1.00 74.67  ? 95  VAL A CG1 1 
ATOM   694   C  CG2 . VAL A  1 94  ? 11.128 -48.619  -8.498   1.00 76.66  ? 95  VAL A CG2 1 
ATOM   695   N  N   . ALA A  1 95  ? 14.707 -50.607  -10.265  1.00 68.36  ? 96  ALA A N   1 
ATOM   696   C  CA  . ALA A  1 95  ? 16.047 -51.185  -10.442  1.00 66.68  ? 96  ALA A CA  1 
ATOM   697   C  C   . ALA A  1 95  ? 17.052 -50.168  -9.942   1.00 65.87  ? 96  ALA A C   1 
ATOM   698   O  O   . ALA A  1 95  ? 17.291 -49.156  -10.583  1.00 63.12  ? 96  ALA A O   1 
ATOM   699   C  CB  . ALA A  1 95  ? 16.325 -51.538  -11.912  1.00 62.93  ? 96  ALA A CB  1 
ATOM   700   N  N   . ASP A  1 96  ? 17.633 -50.438  -8.786   1.00 68.77  ? 97  ASP A N   1 
ATOM   701   C  CA  . ASP A  1 96  ? 18.631 -49.539  -8.213   1.00 68.94  ? 97  ASP A CA  1 
ATOM   702   C  C   . ASP A  1 96  ? 20.029 -49.831  -8.772   1.00 66.57  ? 97  ASP A C   1 
ATOM   703   O  O   . ASP A  1 96  ? 20.784 -50.632  -8.227   1.00 68.68  ? 97  ASP A O   1 
ATOM   704   C  CB  . ASP A  1 96  ? 18.616 -49.628  -6.685   1.00 73.86  ? 97  ASP A CB  1 
ATOM   705   C  CG  . ASP A  1 96  ? 17.490 -48.823  -6.070   1.00 76.77  ? 97  ASP A CG  1 
ATOM   706   O  OD1 . ASP A  1 96  ? 17.343 -47.631  -6.438   1.00 75.07  ? 97  ASP A OD1 1 
ATOM   707   O  OD2 . ASP A  1 96  ? 16.759 -49.380  -5.216   1.00 81.19  ? 97  ASP A OD2 1 
ATOM   708   N  N   . VAL A  1 97  ? 20.361 -49.158  -9.865   1.00 62.68  ? 98  VAL A N   1 
ATOM   709   C  CA  . VAL A  1 97  ? 21.595 -49.432  -10.593  1.00 60.57  ? 98  VAL A CA  1 
ATOM   710   C  C   . VAL A  1 97  ? 22.819 -48.972  -9.827   1.00 62.12  ? 98  VAL A C   1 
ATOM   711   O  O   . VAL A  1 97  ? 22.864 -47.835  -9.355   1.00 62.67  ? 98  VAL A O   1 
ATOM   712   C  CB  . VAL A  1 97  ? 21.624 -48.728  -11.955  1.00 56.58  ? 98  VAL A CB  1 
ATOM   713   C  CG1 . VAL A  1 97  ? 22.883 -49.081  -12.695  1.00 55.09  ? 98  VAL A CG1 1 
ATOM   714   C  CG2 . VAL A  1 97  ? 20.437 -49.126  -12.780  1.00 55.64  ? 98  VAL A CG2 1 
ATOM   715   N  N   . SER A  1 98  ? 23.807 -49.856  -9.716   1.00 63.27  ? 99  SER A N   1 
ATOM   716   C  CA  . SER A  1 98  ? 25.126 -49.501  -9.168   1.00 64.96  ? 99  SER A CA  1 
ATOM   717   C  C   . SER A  1 98  ? 26.235 -50.373  -9.752   1.00 64.80  ? 99  SER A C   1 
ATOM   718   O  O   . SER A  1 98  ? 26.620 -51.386  -9.196   1.00 67.75  ? 99  SER A O   1 
ATOM   719   C  CB  . SER A  1 98  ? 25.162 -49.579  -7.639   1.00 69.59  ? 99  SER A CB  1 
ATOM   720   O  OG  . SER A  1 98  ? 26.475 -49.312  -7.148   1.00 71.28  ? 99  SER A OG  1 
ATOM   721   N  N   . ILE A  1 99  ? 26.753 -49.941  -10.882  1.00 61.87  ? 100 ILE A N   1 
ATOM   722   C  CA  . ILE A  1 99  ? 27.819 -50.635  -11.584  1.00 61.73  ? 100 ILE A CA  1 
ATOM   723   C  C   . ILE A  1 99  ? 29.123 -49.836  -11.441  1.00 62.59  ? 100 ILE A C   1 
ATOM   724   O  O   . ILE A  1 99  ? 29.130 -48.639  -11.127  1.00 62.35  ? 100 ILE A O   1 
ATOM   725   C  CB  . ILE A  1 99  ? 27.444 -50.832  -13.104  1.00 58.15  ? 100 ILE A CB  1 
ATOM   726   C  CG1 . ILE A  1 99  ? 26.216 -51.748  -13.237  1.00 57.94  ? 100 ILE A CG1 1 
ATOM   727   C  CG2 . ILE A  1 99  ? 28.624 -51.385  -13.910  1.00 58.27  ? 100 ILE A CG2 1 
ATOM   728   C  CD1 . ILE A  1 99  ? 26.051 -52.375  -14.613  1.00 55.82  ? 100 ILE A CD1 1 
ATOM   729   N  N   . GLU A  1 100 ? 30.231 -50.526  -11.642  1.00 64.21  ? 101 GLU A N   1 
ATOM   730   C  CA  . GLU A  1 100 ? 31.515 -49.874  -11.820  1.00 64.95  ? 101 GLU A CA  1 
ATOM   731   C  C   . GLU A  1 100 ? 32.237 -50.595  -12.936  1.00 64.38  ? 101 GLU A C   1 
ATOM   732   O  O   . GLU A  1 100 ? 32.363 -51.802  -12.895  1.00 66.22  ? 101 GLU A O   1 
ATOM   733   C  CB  . GLU A  1 100 ? 32.335 -49.924  -10.532  1.00 69.55  ? 101 GLU A CB  1 
ATOM   734   C  CG  . GLU A  1 100 ? 33.661 -49.148  -10.615  1.00 71.44  ? 101 GLU A CG  1 
ATOM   735   C  CD  . GLU A  1 100 ? 34.352 -48.956  -9.271   1.00 76.62  ? 101 GLU A CD  1 
ATOM   736   O  OE1 . GLU A  1 100 ? 35.344 -48.197  -9.240   1.00 77.88  ? 101 GLU A OE1 1 
ATOM   737   O  OE2 . GLU A  1 100 ? 33.901 -49.545  -8.255   1.00 79.29  ? 101 GLU A OE2 1 
ATOM   738   N  N   . ASP A  1 101 ? 32.700 -49.857  -13.935  1.00 62.41  ? 102 ASP A N   1 
ATOM   739   C  CA  . ASP A  1 101 ? 33.265 -50.461  -15.144  1.00 61.83  ? 102 ASP A CA  1 
ATOM   740   C  C   . ASP A  1 101 ? 34.534 -49.789  -15.617  1.00 62.86  ? 102 ASP A C   1 
ATOM   741   O  O   . ASP A  1 101 ? 34.704 -48.600  -15.451  1.00 62.33  ? 102 ASP A O   1 
ATOM   742   C  CB  . ASP A  1 101 ? 32.244 -50.445  -16.272  1.00 58.07  ? 102 ASP A CB  1 
ATOM   743   C  CG  . ASP A  1 101 ? 32.637 -51.340  -17.398  1.00 58.15  ? 102 ASP A CG  1 
ATOM   744   O  OD1 . ASP A  1 101 ? 32.677 -52.579  -17.200  1.00 59.97  ? 102 ASP A OD1 1 
ATOM   745   O  OD2 . ASP A  1 101 ? 32.934 -50.798  -18.477  1.00 56.70  ? 102 ASP A OD2 1 
ATOM   746   N  N   . SER A  1 102 ? 35.410 -50.571  -16.236  1.00 64.82  ? 103 SER A N   1 
ATOM   747   C  CA  . SER A  1 102 ? 36.747 -50.114  -16.646  1.00 66.93  ? 103 SER A CA  1 
ATOM   748   C  C   . SER A  1 102 ? 36.989 -50.046  -18.139  1.00 65.40  ? 103 SER A C   1 
ATOM   749   O  O   . SER A  1 102 ? 37.965 -49.452  -18.559  1.00 66.87  ? 103 SER A O   1 
ATOM   750   C  CB  . SER A  1 102 ? 37.790 -51.034  -16.051  1.00 71.66  ? 103 SER A CB  1 
ATOM   751   O  OG  . SER A  1 102 ? 37.572 -51.136  -14.658  1.00 73.87  ? 103 SER A OG  1 
ATOM   752   N  N   . VAL A  1 103 ? 36.115 -50.657  -18.934  1.00 63.01  ? 104 VAL A N   1 
ATOM   753   C  CA  . VAL A  1 103 ? 36.239 -50.615  -20.399  1.00 61.88  ? 104 VAL A CA  1 
ATOM   754   C  C   . VAL A  1 103 ? 35.662 -49.309  -20.972  1.00 58.73  ? 104 VAL A C   1 
ATOM   755   O  O   . VAL A  1 103 ? 36.295 -48.670  -21.823  1.00 59.15  ? 104 VAL A O   1 
ATOM   756   C  CB  . VAL A  1 103 ? 35.545 -51.812  -21.080  1.00 61.03  ? 104 VAL A CB  1 
ATOM   757   C  CG1 . VAL A  1 103 ? 35.741 -51.749  -22.586  1.00 60.40  ? 104 VAL A CG1 1 
ATOM   758   C  CG2 . VAL A  1 103 ? 36.085 -53.112  -20.545  1.00 64.69  ? 104 VAL A CG2 1 
ATOM   759   N  N   . ILE A  1 104 ? 34.461 -48.927  -20.523  1.00 55.91  ? 105 ILE A N   1 
ATOM   760   C  CA  . ILE A  1 104 ? 33.857 -47.671  -20.968  1.00 53.20  ? 105 ILE A CA  1 
ATOM   761   C  C   . ILE A  1 104 ? 34.662 -46.490  -20.441  1.00 54.51  ? 105 ILE A C   1 
ATOM   762   O  O   . ILE A  1 104 ? 35.412 -46.621  -19.468  1.00 56.98  ? 105 ILE A O   1 
ATOM   763   C  CB  . ILE A  1 104 ? 32.378 -47.502  -20.527  1.00 50.65  ? 105 ILE A CB  1 
ATOM   764   C  CG1 . ILE A  1 104 ? 32.240 -47.415  -18.998  1.00 51.87  ? 105 ILE A CG1 1 
ATOM   765   C  CG2 . ILE A  1 104 ? 31.536 -48.627  -21.087  1.00 49.60  ? 105 ILE A CG2 1 
ATOM   766   C  CD1 . ILE A  1 104 ? 30.932 -46.784  -18.520  1.00 49.46  ? 105 ILE A CD1 1 
ATOM   767   N  N   . SER A  1 105 ? 34.496 -45.340  -21.086  1.00 53.08  ? 106 SER A N   1 
ATOM   768   C  CA  . SER A  1 105 ? 35.148 -44.111  -20.629  1.00 54.29  ? 106 SER A CA  1 
ATOM   769   C  C   . SER A  1 105 ? 34.434 -42.840  -21.056  1.00 52.07  ? 106 SER A C   1 
ATOM   770   O  O   . SER A  1 105 ? 33.759 -42.812  -22.088  1.00 50.11  ? 106 SER A O   1 
ATOM   771   C  CB  . SER A  1 105 ? 36.584 -44.036  -21.137  1.00 57.26  ? 106 SER A CB  1 
ATOM   772   O  OG  . SER A  1 105 ? 37.291 -42.990  -20.482  1.00 58.96  ? 106 SER A OG  1 
ATOM   773   N  N   . LEU A  1 106 ? 34.620 -41.788  -20.257  1.00 52.78  ? 107 LEU A N   1 
ATOM   774   C  CA  . LEU A  1 106 ? 34.052 -40.480  -20.534  1.00 51.30  ? 107 LEU A CA  1 
ATOM   775   C  C   . LEU A  1 106 ? 35.044 -39.597  -21.276  1.00 52.91  ? 107 LEU A C   1 
ATOM   776   O  O   . LEU A  1 106 ? 34.892 -38.379  -21.302  1.00 52.88  ? 107 LEU A O   1 
ATOM   777   C  CB  . LEU A  1 106 ? 33.623 -39.805  -19.236  1.00 51.66  ? 107 LEU A CB  1 
ATOM   778   C  CG  . LEU A  1 106 ? 32.578 -40.549  -18.401  1.00 50.43  ? 107 LEU A CG  1 
ATOM   779   C  CD1 . LEU A  1 106 ? 32.225 -39.747  -17.160  1.00 51.66  ? 107 LEU A CD1 1 
ATOM   780   C  CD2 . LEU A  1 106 ? 31.334 -40.825  -19.198  1.00 47.33  ? 107 LEU A CD2 1 
ATOM   781   N  N   . SER A  1 107 ? 36.055 -40.212  -21.886  1.00 54.81  ? 108 SER A N   1 
ATOM   782   C  CA  . SER A  1 107 ? 37.069 -39.488  -22.678  1.00 56.77  ? 108 SER A CA  1 
ATOM   783   C  C   . SER A  1 107 ? 37.886 -40.401  -23.596  1.00 58.55  ? 108 SER A C   1 
ATOM   784   O  O   . SER A  1 107 ? 38.269 -41.507  -23.214  1.00 59.80  ? 108 SER A O   1 
ATOM   785   C  CB  . SER A  1 107 ? 38.021 -38.727  -21.771  1.00 59.68  ? 108 SER A CB  1 
ATOM   786   O  OG  . SER A  1 107 ? 38.650 -39.579  -20.839  1.00 61.78  ? 108 SER A OG  1 
ATOM   787   N  N   . GLY A  1 108 ? 38.132 -39.931  -24.817  1.00 59.15  ? 109 GLY A N   1 
ATOM   788   C  CA  . GLY A  1 108 ? 38.996 -40.628  -25.785  1.00 61.67  ? 109 GLY A CA  1 
ATOM   789   C  C   . GLY A  1 108 ? 38.334 -41.575  -26.788  1.00 60.24  ? 109 GLY A C   1 
ATOM   790   O  O   . GLY A  1 108 ? 37.187 -41.393  -27.208  1.00 57.29  ? 109 GLY A O   1 
ATOM   791   N  N   . ASP A  1 109 ? 39.087 -42.601  -27.172  1.00 62.90  ? 110 ASP A N   1 
ATOM   792   C  CA  . ASP A  1 109 ? 38.626 -43.652  -28.122  1.00 62.42  ? 110 ASP A CA  1 
ATOM   793   C  C   . ASP A  1 109 ? 37.310 -44.328  -27.684  1.00 58.65  ? 110 ASP A C   1 
ATOM   794   O  O   . ASP A  1 109 ? 36.394 -44.548  -28.480  1.00 56.44  ? 110 ASP A O   1 
ATOM   795   C  CB  . ASP A  1 109 ? 39.716 -44.757  -28.273  1.00 66.42  ? 110 ASP A CB  1 
ATOM   796   C  CG  . ASP A  1 109 ? 39.665 -45.463  -29.654  1.00 67.86  ? 110 ASP A CG  1 
ATOM   797   O  OD1 . ASP A  1 109 ? 38.971 -46.515  -29.805  1.00 66.26  ? 110 ASP A OD1 1 
ATOM   798   O  OD2 . ASP A  1 109 ? 40.327 -44.931  -30.586  1.00 70.73  ? 110 ASP A OD2 1 
ATOM   799   N  N   . HIS A  1 110 ? 37.270 -44.661  -26.398  1.00 58.25  ? 111 HIS A N   1 
ATOM   800   C  CA  . HIS A  1 110 ? 36.153 -45.376  -25.781  1.00 55.81  ? 111 HIS A CA  1 
ATOM   801   C  C   . HIS A  1 110 ? 35.035 -44.430  -25.309  1.00 52.71  ? 111 HIS A C   1 
ATOM   802   O  O   . HIS A  1 110 ? 34.110 -44.863  -24.597  1.00 50.94  ? 111 HIS A O   1 
ATOM   803   C  CB  . HIS A  1 110 ? 36.669 -46.188  -24.566  1.00 57.69  ? 111 HIS A CB  1 
ATOM   804   C  CG  . HIS A  1 110 ? 37.555 -47.354  -24.924  1.00 61.01  ? 111 HIS A CG  1 
ATOM   805   N  ND1 . HIS A  1 110 ? 37.900 -48.336  -24.010  1.00 62.81  ? 111 HIS A ND1 1 
ATOM   806   C  CD2 . HIS A  1 110 ? 38.154 -47.699  -26.091  1.00 62.99  ? 111 HIS A CD2 1 
ATOM   807   C  CE1 . HIS A  1 110 ? 38.684 -49.223  -24.597  1.00 65.66  ? 111 HIS A CE1 1 
ATOM   808   N  NE2 . HIS A  1 110 ? 38.842 -48.867  -25.861  1.00 66.07  ? 111 HIS A NE2 1 
ATOM   809   N  N   . CYS A  1 111 ? 35.133 -43.151  -25.687  1.00 52.39  ? 112 CYS A N   1 
ATOM   810   C  CA  . CYS A  1 111 ? 34.234 -42.108  -25.171  1.00 50.11  ? 112 CYS A CA  1 
ATOM   811   C  C   . CYS A  1 111 ? 32.780 -42.466  -25.464  1.00 47.34  ? 112 CYS A C   1 
ATOM   812   O  O   . CYS A  1 111 ? 32.390 -42.594  -26.629  1.00 46.73  ? 112 CYS A O   1 
ATOM   813   C  CB  . CYS A  1 111 ? 34.591 -40.747  -25.786  1.00 50.80  ? 112 CYS A CB  1 
ATOM   814   S  SG  . CYS A  1 111 ? 33.734 -39.270  -25.182  1.00 49.10  ? 112 CYS A SG  1 
ATOM   815   N  N   . ILE A  1 112 ? 32.000 -42.651  -24.401  1.00 45.97  ? 113 ILE A N   1 
ATOM   816   C  CA  . ILE A  1 112 ? 30.583 -42.966  -24.528  1.00 43.92  ? 113 ILE A CA  1 
ATOM   817   C  C   . ILE A  1 112 ? 29.700 -41.717  -24.569  1.00 42.66  ? 113 ILE A C   1 
ATOM   818   O  O   . ILE A  1 112 ? 28.514 -41.796  -24.853  1.00 41.45  ? 113 ILE A O   1 
ATOM   819   C  CB  . ILE A  1 112 ? 30.085 -43.901  -23.395  1.00 43.76  ? 113 ILE A CB  1 
ATOM   820   C  CG1 . ILE A  1 112 ? 30.232 -43.263  -22.029  1.00 44.25  ? 113 ILE A CG1 1 
ATOM   821   C  CG2 . ILE A  1 112 ? 30.831 -45.226  -23.422  1.00 45.38  ? 113 ILE A CG2 1 
ATOM   822   C  CD1 . ILE A  1 112 ? 29.285 -43.836  -21.011  1.00 43.95  ? 113 ILE A CD1 1 
ATOM   823   N  N   . ILE A  1 113 ? 30.271 -40.562  -24.283  1.00 43.45  ? 114 ILE A N   1 
ATOM   824   C  CA  . ILE A  1 113 ? 29.506 -39.318  -24.263  1.00 42.54  ? 114 ILE A CA  1 
ATOM   825   C  C   . ILE A  1 113 ? 29.017 -39.001  -25.641  1.00 41.81  ? 114 ILE A C   1 
ATOM   826   O  O   . ILE A  1 113 ? 29.769 -39.071  -26.598  1.00 42.61  ? 114 ILE A O   1 
ATOM   827   C  CB  . ILE A  1 113 ? 30.344 -38.140  -23.742  1.00 44.03  ? 114 ILE A CB  1 
ATOM   828   C  CG1 . ILE A  1 113 ? 30.527 -38.274  -22.236  1.00 44.89  ? 114 ILE A CG1 1 
ATOM   829   C  CG2 . ILE A  1 113 ? 29.683 -36.824  -24.051  1.00 43.54  ? 114 ILE A CG2 1 
ATOM   830   C  CD1 . ILE A  1 113 ? 31.477 -37.293  -21.671  1.00 47.23  ? 114 ILE A CD1 1 
ATOM   831   N  N   . GLY A  1 114 ? 27.746 -38.646  -25.721  1.00 40.74  ? 115 GLY A N   1 
ATOM   832   C  CA  . GLY A  1 114 ? 27.098 -38.359  -26.996  1.00 40.65  ? 115 GLY A CA  1 
ATOM   833   C  C   . GLY A  1 114 ? 26.493 -39.596  -27.632  1.00 39.98  ? 115 GLY A C   1 
ATOM   834   O  O   . GLY A  1 114 ? 25.972 -39.538  -28.736  1.00 40.22  ? 115 GLY A O   1 
ATOM   835   N  N   . ARG A  1 115 ? 26.574 -40.716  -26.934  1.00 39.60  ? 116 ARG A N   1 
ATOM   836   C  CA  . ARG A  1 115 ? 25.990 -41.957  -27.404  1.00 39.42  ? 116 ARG A CA  1 
ATOM   837   C  C   . ARG A  1 115 ? 24.795 -42.320  -26.532  1.00 38.70  ? 116 ARG A C   1 
ATOM   838   O  O   . ARG A  1 115 ? 24.525 -41.667  -25.537  1.00 38.52  ? 116 ARG A O   1 
ATOM   839   C  CB  . ARG A  1 115 ? 27.032 -43.070  -27.415  1.00 40.19  ? 116 ARG A CB  1 
ATOM   840   C  CG  . ARG A  1 115 ? 28.251 -42.709  -28.230  1.00 41.76  ? 116 ARG A CG  1 
ATOM   841   C  CD  . ARG A  1 115 ? 29.250 -43.841  -28.344  1.00 43.28  ? 116 ARG A CD  1 
ATOM   842   N  NE  . ARG A  1 115 ? 30.515 -43.403  -28.961  1.00 44.96  ? 116 ARG A NE  1 
ATOM   843   C  CZ  . ARG A  1 115 ? 30.744 -43.322  -30.273  1.00 46.13  ? 116 ARG A CZ  1 
ATOM   844   N  NH1 . ARG A  1 115 ? 29.803 -43.646  -31.159  1.00 45.77  ? 116 ARG A NH1 1 
ATOM   845   N  NH2 . ARG A  1 115 ? 31.926 -42.915  -30.708  1.00 48.39  ? 116 ARG A NH2 1 
ATOM   846   N  N   . THR A  1 116 ? 24.067 -43.354  -26.931  1.00 38.70  ? 117 THR A N   1 
ATOM   847   C  CA  . THR A  1 116 ? 22.809 -43.732  -26.281  1.00 38.37  ? 117 THR A CA  1 
ATOM   848   C  C   . THR A  1 116 ? 22.957 -44.894  -25.290  1.00 38.71  ? 117 THR A C   1 
ATOM   849   O  O   . THR A  1 116 ? 23.562 -45.915  -25.591  1.00 39.24  ? 117 THR A O   1 
ATOM   850   C  CB  . THR A  1 116 ? 21.759 -44.139  -27.317  1.00 38.68  ? 117 THR A CB  1 
ATOM   851   O  OG1 . THR A  1 116 ? 21.432 -43.024  -28.152  1.00 38.56  ? 117 THR A OG1 1 
ATOM   852   C  CG2 . THR A  1 116 ? 20.509 -44.620  -26.636  1.00 38.99  ? 117 THR A CG2 1 
ATOM   853   N  N   . LEU A  1 117 ? 22.403 -44.709  -24.097  1.00 38.90  ? 118 LEU A N   1 
ATOM   854   C  CA  . LEU A  1 117 ? 22.249 -45.777  -23.105  1.00 39.49  ? 118 LEU A CA  1 
ATOM   855   C  C   . LEU A  1 117 ? 20.890 -46.399  -23.336  1.00 39.85  ? 118 LEU A C   1 
ATOM   856   O  O   . LEU A  1 117 ? 19.962 -45.714  -23.731  1.00 39.90  ? 118 LEU A O   1 
ATOM   857   C  CB  . LEU A  1 117 ? 22.321 -45.223  -21.679  1.00 40.05  ? 118 LEU A CB  1 
ATOM   858   C  CG  . LEU A  1 117 ? 22.279 -46.242  -20.548  1.00 41.07  ? 118 LEU A CG  1 
ATOM   859   C  CD1 . LEU A  1 117 ? 23.439 -47.178  -20.667  1.00 41.64  ? 118 LEU A CD1 1 
ATOM   860   C  CD2 . LEU A  1 117 ? 22.296 -45.553  -19.213  1.00 41.97  ? 118 LEU A CD2 1 
ATOM   861   N  N   . VAL A  1 118 ? 20.768 -47.694  -23.082  1.00 40.71  ? 119 VAL A N   1 
ATOM   862   C  CA  . VAL A  1 118 ? 19.550 -48.446  -23.424  1.00 41.39  ? 119 VAL A CA  1 
ATOM   863   C  C   . VAL A  1 118 ? 19.270 -49.578  -22.439  1.00 42.89  ? 119 VAL A C   1 
ATOM   864   O  O   . VAL A  1 118 ? 20.094 -50.454  -22.231  1.00 43.54  ? 119 VAL A O   1 
ATOM   865   C  CB  . VAL A  1 118 ? 19.663 -49.072  -24.820  1.00 41.25  ? 119 VAL A CB  1 
ATOM   866   C  CG1 . VAL A  1 118 ? 18.554 -50.032  -25.036  1.00 42.69  ? 119 VAL A CG1 1 
ATOM   867   C  CG2 . VAL A  1 118 ? 19.654 -48.013  -25.885  1.00 40.53  ? 119 VAL A CG2 1 
ATOM   868   N  N   . VAL A  1 119 ? 18.099 -49.553  -21.828  1.00 44.06  ? 120 VAL A N   1 
ATOM   869   C  CA  . VAL A  1 119 ? 17.667 -50.647  -20.960  1.00 46.02  ? 120 VAL A CA  1 
ATOM   870   C  C   . VAL A  1 119 ? 16.724 -51.536  -21.777  1.00 47.08  ? 120 VAL A C   1 
ATOM   871   O  O   . VAL A  1 119 ? 15.986 -51.050  -22.641  1.00 46.68  ? 120 VAL A O   1 
ATOM   872   C  CB  . VAL A  1 119 ? 16.981 -50.127  -19.669  1.00 47.40  ? 120 VAL A CB  1 
ATOM   873   C  CG1 . VAL A  1 119 ? 15.582 -49.608  -19.971  1.00 48.37  ? 120 VAL A CG1 1 
ATOM   874   C  CG2 . VAL A  1 119 ? 16.939 -51.210  -18.599  1.00 49.62  ? 120 VAL A CG2 1 
ATOM   875   N  N   . HIS A  1 120 ? 16.756 -52.835  -21.492  1.00 48.76  ? 121 HIS A N   1 
ATOM   876   C  CA  . HIS A  1 120 ? 16.194 -53.853  -22.397  1.00 49.97  ? 121 HIS A CA  1 
ATOM   877   C  C   . HIS A  1 120 ? 15.022 -54.682  -21.852  1.00 52.76  ? 121 HIS A C   1 
ATOM   878   O  O   . HIS A  1 120 ? 14.799 -54.784  -20.642  1.00 54.08  ? 121 HIS A O   1 
ATOM   879   C  CB  . HIS A  1 120 ? 17.309 -54.794  -22.866  1.00 49.87  ? 121 HIS A CB  1 
ATOM   880   C  CG  . HIS A  1 120 ? 18.024 -54.306  -24.074  1.00 47.85  ? 121 HIS A CG  1 
ATOM   881   N  ND1 . HIS A  1 120 ? 17.856 -54.871  -25.317  1.00 48.81  ? 121 HIS A ND1 1 
ATOM   882   C  CD2 . HIS A  1 120 ? 18.877 -53.276  -24.243  1.00 45.92  ? 121 HIS A CD2 1 
ATOM   883   C  CE1 . HIS A  1 120 ? 18.590 -54.221  -26.200  1.00 47.31  ? 121 HIS A CE1 1 
ATOM   884   N  NE2 . HIS A  1 120 ? 19.214 -53.243  -25.574  1.00 45.69  ? 121 HIS A NE2 1 
ATOM   885   N  N   . GLU A  1 121 ? 14.303 -55.294  -22.786  1.00 53.95  ? 122 GLU A N   1 
ATOM   886   C  CA  . GLU A  1 121 ? 13.123 -56.112  -22.488  1.00 57.07  ? 122 GLU A CA  1 
ATOM   887   C  C   . GLU A  1 121 ? 13.444 -57.303  -21.598  1.00 59.04  ? 122 GLU A C   1 
ATOM   888   O  O   . GLU A  1 121 ? 12.937 -57.402  -20.495  1.00 60.82  ? 122 GLU A O   1 
ATOM   889   C  CB  . GLU A  1 121 ? 12.502 -56.614  -23.802  1.00 58.22  ? 122 GLU A CB  1 
ATOM   890   C  CG  . GLU A  1 121 ? 11.314 -57.571  -23.631  1.00 62.07  ? 122 GLU A CG  1 
ATOM   891   C  CD  . GLU A  1 121 ? 10.829 -58.186  -24.948  1.00 63.81  ? 122 GLU A CD  1 
ATOM   892   O  OE1 . GLU A  1 121 ? 11.514 -58.035  -25.984  1.00 62.07  ? 122 GLU A OE1 1 
ATOM   893   O  OE2 . GLU A  1 121 ? 9.755  -58.831  -24.933  1.00 66.99  ? 122 GLU A OE2 1 
ATOM   894   N  N   . LYS A  1 122 ? 14.281 -58.201  -22.120  1.00 59.17  ? 123 LYS A N   1 
ATOM   895   C  CA  . LYS A  1 122 ? 14.707 -59.430  -21.440  1.00 61.32  ? 123 LYS A CA  1 
ATOM   896   C  C   . LYS A  1 122 ? 16.080 -59.235  -20.815  1.00 59.93  ? 123 LYS A C   1 
ATOM   897   O  O   . LYS A  1 122 ? 16.663 -58.160  -20.899  1.00 57.45  ? 123 LYS A O   1 
ATOM   898   C  CB  . LYS A  1 122 ? 14.800 -60.602  -22.433  1.00 62.87  ? 123 LYS A CB  1 
ATOM   899   C  CG  . LYS A  1 122 ? 13.588 -60.815  -23.329  1.00 64.59  ? 123 LYS A CG  1 
ATOM   900   C  CD  . LYS A  1 122 ? 13.794 -61.987  -24.308  1.00 66.60  ? 123 LYS A CD  1 
ATOM   901   C  CE  . LYS A  1 122 ? 12.659 -62.059  -25.365  1.00 68.13  ? 123 LYS A CE  1 
ATOM   902   N  NZ  . LYS A  1 122 ? 12.686 -63.300  -26.177  1.00 70.74  ? 123 LYS A NZ  1 
ATOM   903   N  N   . ALA A  1 123 ? 16.602 -60.295  -20.207  1.00 62.00  ? 124 ALA A N   1 
ATOM   904   C  CA  . ALA A  1 123 ? 17.955 -60.283  -19.637  1.00 61.42  ? 124 ALA A CA  1 
ATOM   905   C  C   . ALA A  1 123 ? 19.007 -60.578  -20.691  1.00 60.27  ? 124 ALA A C   1 
ATOM   906   O  O   . ALA A  1 123 ? 18.763 -61.345  -21.612  1.00 61.03  ? 124 ALA A O   1 
ATOM   907   C  CB  . ALA A  1 123 ? 18.067 -61.285  -18.505  1.00 64.72  ? 124 ALA A CB  1 
ATOM   908   N  N   . ASP A  1 124 ? 20.171 -59.952  -20.530  1.00 58.80  ? 125 ASP A N   1 
ATOM   909   C  CA  . ASP A  1 124 ? 21.349 -60.195  -21.382  1.00 58.53  ? 125 ASP A CA  1 
ATOM   910   C  C   . ASP A  1 124 ? 22.011 -61.530  -20.979  1.00 61.83  ? 125 ASP A C   1 
ATOM   911   O  O   . ASP A  1 124 ? 22.432 -61.689  -19.825  1.00 63.37  ? 125 ASP A O   1 
ATOM   912   C  CB  . ASP A  1 124 ? 22.364 -59.036  -21.243  1.00 56.29  ? 125 ASP A CB  1 
ATOM   913   C  CG  . ASP A  1 124 ? 23.595 -59.176  -22.162  1.00 56.17  ? 125 ASP A CG  1 
ATOM   914   O  OD1 . ASP A  1 124 ? 23.682 -60.155  -22.924  1.00 57.76  ? 125 ASP A OD1 1 
ATOM   915   O  OD2 . ASP A  1 124 ? 24.483 -58.294  -22.122  1.00 54.63  ? 125 ASP A OD2 1 
ATOM   916   N  N   . ASP A  1 125 ? 22.124 -62.470  -21.927  1.00 63.14  ? 126 ASP A N   1 
ATOM   917   C  CA  . ASP A  1 125 ? 22.676 -63.803  -21.635  1.00 66.47  ? 126 ASP A CA  1 
ATOM   918   C  C   . ASP A  1 125 ? 24.206 -63.815  -21.574  1.00 67.13  ? 126 ASP A C   1 
ATOM   919   O  O   . ASP A  1 125 ? 24.833 -64.878  -21.501  1.00 70.15  ? 126 ASP A O   1 
ATOM   920   C  CB  . ASP A  1 125 ? 22.158 -64.852  -22.637  1.00 68.43  ? 126 ASP A CB  1 
ATOM   921   C  CG  . ASP A  1 125 ? 22.833 -64.778  -24.012  1.00 67.76  ? 126 ASP A CG  1 
ATOM   922   O  OD1 . ASP A  1 125 ? 23.987 -64.289  -24.111  1.00 66.89  ? 126 ASP A OD1 1 
ATOM   923   O  OD2 . ASP A  1 125 ? 22.207 -65.248  -24.997  1.00 68.06  ? 126 ASP A OD2 1 
ATOM   924   N  N   . LEU A  1 126 ? 24.795 -62.622  -21.625  1.00 64.60  ? 127 LEU A N   1 
ATOM   925   C  CA  . LEU A  1 126 ? 26.252 -62.416  -21.502  1.00 65.29  ? 127 LEU A CA  1 
ATOM   926   C  C   . LEU A  1 126 ? 27.057 -63.233  -22.516  1.00 67.33  ? 127 LEU A C   1 
ATOM   927   O  O   . LEU A  1 126 ? 28.192 -63.632  -22.234  1.00 69.88  ? 127 LEU A O   1 
ATOM   928   C  CB  . LEU A  1 126 ? 26.739 -62.686  -20.063  1.00 67.49  ? 127 LEU A CB  1 
ATOM   929   C  CG  . LEU A  1 126 ? 25.944 -61.990  -18.940  1.00 66.27  ? 127 LEU A CG  1 
ATOM   930   C  CD1 . LEU A  1 126 ? 26.633 -62.174  -17.587  1.00 69.23  ? 127 LEU A CD1 1 
ATOM   931   C  CD2 . LEU A  1 126 ? 25.715 -60.518  -19.230  1.00 62.43  ? 127 LEU A CD2 1 
ATOM   932   N  N   . GLY A  1 127 ? 26.461 -63.465  -23.688  1.00 66.73  ? 128 GLY A N   1 
ATOM   933   C  CA  . GLY A  1 127 ? 27.142 -64.142  -24.791  1.00 68.89  ? 128 GLY A CA  1 
ATOM   934   C  C   . GLY A  1 127 ? 27.261 -65.656  -24.676  1.00 73.13  ? 128 GLY A C   1 
ATOM   935   O  O   . GLY A  1 127 ? 27.767 -66.319  -25.590  1.00 75.31  ? 128 GLY A O   1 
ATOM   936   N  N   . LYS A  1 128 ? 26.782 -66.212  -23.560  1.00 74.59  ? 129 LYS A N   1 
ATOM   937   C  CA  . LYS A  1 128 ? 26.890 -67.661  -23.292  1.00 78.95  ? 129 LYS A CA  1 
ATOM   938   C  C   . LYS A  1 128 ? 25.652 -68.437  -23.785  1.00 79.93  ? 129 LYS A C   1 
ATOM   939   O  O   . LYS A  1 128 ? 25.351 -69.542  -23.285  1.00 83.25  ? 129 LYS A O   1 
ATOM   940   C  CB  . LYS A  1 128 ? 27.088 -67.912  -21.786  1.00 80.72  ? 129 LYS A CB  1 
ATOM   941   C  CG  . LYS A  1 128 ? 28.235 -67.121  -21.162  1.00 80.44  ? 129 LYS A CG  1 
ATOM   942   C  CD  . LYS A  1 128 ? 28.702 -67.751  -19.842  1.00 84.55  ? 129 LYS A CD  1 
ATOM   943   C  CE  . LYS A  1 128 ? 29.745 -66.866  -19.128  1.00 84.38  ? 129 LYS A CE  1 
ATOM   944   N  NZ  . LYS A  1 128 ? 30.494 -67.592  -18.053  1.00 88.94  ? 129 LYS A NZ  1 
ATOM   945   N  N   . GLY A  1 129 ? 24.947 -67.862  -24.761  1.00 77.39  ? 130 GLY A N   1 
ATOM   946   C  CA  . GLY A  1 129 ? 23.637 -68.367  -25.187  1.00 78.03  ? 130 GLY A CA  1 
ATOM   947   C  C   . GLY A  1 129 ? 23.712 -69.542  -26.133  1.00 81.43  ? 130 GLY A C   1 
ATOM   948   O  O   . GLY A  1 129 ? 22.783 -70.348  -26.210  1.00 83.39  ? 130 GLY A O   1 
ATOM   949   N  N   . GLY A  1 130 ? 24.812 -69.615  -26.872  1.00 82.36  ? 131 GLY A N   1 
ATOM   950   C  CA  . GLY A  1 130 ? 25.046 -70.724  -27.798  1.00 86.45  ? 131 GLY A CA  1 
ATOM   951   C  C   . GLY A  1 130 ? 24.542 -70.459  -29.211  1.00 85.83  ? 131 GLY A C   1 
ATOM   952   O  O   . GLY A  1 130 ? 25.079 -70.986  -30.179  1.00 88.51  ? 131 GLY A O   1 
ATOM   953   N  N   . ASN A  1 131 ? 23.497 -69.652  -29.335  1.00 82.76  ? 132 ASN A N   1 
ATOM   954   C  CA  . ASN A  1 131 ? 22.965 -69.310  -30.651  1.00 82.41  ? 132 ASN A CA  1 
ATOM   955   C  C   . ASN A  1 131 ? 23.727 -68.179  -31.296  1.00 80.01  ? 132 ASN A C   1 
ATOM   956   O  O   . ASN A  1 131 ? 24.601 -67.568  -30.678  1.00 78.20  ? 132 ASN A O   1 
ATOM   957   C  CB  . ASN A  1 131 ? 21.464 -68.994  -30.590  1.00 81.11  ? 132 ASN A CB  1 
ATOM   958   C  CG  . ASN A  1 131 ? 21.158 -67.603  -30.089  1.00 76.68  ? 132 ASN A CG  1 
ATOM   959   O  OD1 . ASN A  1 131 ? 22.048 -66.825  -29.774  1.00 74.39  ? 132 ASN A OD1 1 
ATOM   960   N  ND2 . ASN A  1 131 ? 19.871 -67.286  -30.008  1.00 76.07  ? 132 ASN A ND2 1 
ATOM   961   N  N   . GLU A  1 132 ? 23.387 -67.902  -32.547  1.00 80.36  ? 133 GLU A N   1 
ATOM   962   C  CA  . GLU A  1 132 ? 24.058 -66.862  -33.332  1.00 78.73  ? 133 GLU A CA  1 
ATOM   963   C  C   . GLU A  1 132 ? 23.887 -65.481  -32.716  1.00 74.03  ? 133 GLU A C   1 
ATOM   964   O  O   . GLU A  1 132 ? 24.853 -64.732  -32.575  1.00 72.36  ? 133 GLU A O   1 
ATOM   965   C  CB  . GLU A  1 132 ? 23.486 -66.848  -34.750  1.00 80.53  ? 133 GLU A CB  1 
ATOM   966   C  CG  . GLU A  1 132 ? 23.836 -65.586  -35.567  1.00 79.18  ? 133 GLU A CG  1 
ATOM   967   C  CD  . GLU A  1 132 ? 25.280 -65.573  -36.171  1.00 81.54  ? 133 GLU A CD  1 
ATOM   968   O  OE1 . GLU A  1 132 ? 26.089 -66.490  -35.885  1.00 84.29  ? 133 GLU A OE1 1 
ATOM   969   O  OE2 . GLU A  1 132 ? 25.613 -64.623  -36.929  1.00 80.67  ? 133 GLU A OE2 1 
ATOM   970   N  N   . GLU A  1 133 ? 22.638 -65.168  -32.372  1.00 72.36  ? 134 GLU A N   1 
ATOM   971   C  CA  . GLU A  1 133 ? 22.236 -63.831  -31.899  1.00 68.39  ? 134 GLU A CA  1 
ATOM   972   C  C   . GLU A  1 133 ? 22.844 -63.466  -30.542  1.00 66.31  ? 134 GLU A C   1 
ATOM   973   O  O   . GLU A  1 133 ? 23.097 -62.292  -30.278  1.00 63.45  ? 134 GLU A O   1 
ATOM   974   C  CB  . GLU A  1 133 ? 20.706 -63.735  -31.819  1.00 68.11  ? 134 GLU A CB  1 
ATOM   975   C  CG  . GLU A  1 133 ? 20.141 -62.312  -31.756  1.00 65.01  ? 134 GLU A CG  1 
ATOM   976   C  CD  . GLU A  1 133 ? 20.269 -61.531  -33.080  1.00 65.04  ? 134 GLU A CD  1 
ATOM   977   O  OE1 . GLU A  1 133 ? 20.678 -62.099  -34.118  1.00 67.64  ? 134 GLU A OE1 1 
ATOM   978   O  OE2 . GLU A  1 133 ? 19.942 -60.327  -33.070  1.00 62.55  ? 134 GLU A OE2 1 
ATOM   979   N  N   . SER A  1 134 ? 23.108 -64.467  -29.701  1.00 68.19  ? 135 SER A N   1 
ATOM   980   C  CA  . SER A  1 134 ? 23.724 -64.232  -28.379  1.00 67.04  ? 135 SER A CA  1 
ATOM   981   C  C   . SER A  1 134 ? 25.115 -63.629  -28.474  1.00 66.32  ? 135 SER A C   1 
ATOM   982   O  O   . SER A  1 134 ? 25.560 -62.982  -27.544  1.00 64.71  ? 135 SER A O   1 
ATOM   983   C  CB  . SER A  1 134 ? 23.848 -65.513  -27.574  1.00 70.14  ? 135 SER A CB  1 
ATOM   984   O  OG  . SER A  1 134 ? 24.579 -65.245  -26.388  1.00 69.34  ? 135 SER A OG  1 
ATOM   985   N  N   . THR A  1 135 ? 25.794 -63.891  -29.584  1.00 68.10  ? 136 THR A N   1 
ATOM   986   C  CA  . THR A  1 135 ? 27.086 -63.282  -29.905  1.00 68.12  ? 136 THR A CA  1 
ATOM   987   C  C   . THR A  1 135 ? 27.007 -61.799  -30.350  1.00 64.98  ? 136 THR A C   1 
ATOM   988   O  O   . THR A  1 135 ? 28.032 -61.101  -30.439  1.00 64.61  ? 136 THR A O   1 
ATOM   989   C  CB  . THR A  1 135 ? 27.765 -64.117  -30.991  1.00 71.75  ? 136 THR A CB  1 
ATOM   990   O  OG1 . THR A  1 135 ? 28.328 -65.260  -30.361  1.00 75.03  ? 136 THR A OG1 1 
ATOM   991   C  CG2 . THR A  1 135 ? 28.861 -63.357  -31.719  1.00 71.94  ? 136 THR A CG2 1 
ATOM   992   N  N   . LYS A  1 136 ? 25.791 -61.322  -30.604  1.00 62.99  ? 137 LYS A N   1 
ATOM   993   C  CA  . LYS A  1 136 ? 25.578 -59.981  -31.106  1.00 60.45  ? 137 LYS A CA  1 
ATOM   994   C  C   . LYS A  1 136 ? 24.838 -59.109  -30.104  1.00 57.32  ? 137 LYS A C   1 
ATOM   995   O  O   . LYS A  1 136 ? 25.370 -58.113  -29.614  1.00 55.52  ? 137 LYS A O   1 
ATOM   996   C  CB  . LYS A  1 136 ? 24.764 -60.034  -32.390  1.00 61.42  ? 137 LYS A CB  1 
ATOM   997   C  CG  . LYS A  1 136 ? 25.514 -60.507  -33.621  1.00 64.66  ? 137 LYS A CG  1 
ATOM   998   C  CD  . LYS A  1 136 ? 24.574 -60.480  -34.833  1.00 66.18  ? 137 LYS A CD  1 
ATOM   999   C  CE  . LYS A  1 136 ? 25.339 -60.397  -36.169  1.00 68.69  ? 137 LYS A CE  1 
ATOM   1000  N  NZ  . LYS A  1 136 ? 25.758 -61.740  -36.663  1.00 72.82  ? 137 LYS A NZ  1 
ATOM   1001  N  N   . THR A  1 137 ? 23.597 -59.473  -29.820  1.00 57.10  ? 138 THR A N   1 
ATOM   1002  C  CA  . THR A  1 137 ? 22.705 -58.628  -29.019  1.00 54.81  ? 138 THR A CA  1 
ATOM   1003  C  C   . THR A  1 137 ? 22.625 -59.061  -27.564  1.00 54.88  ? 138 THR A C   1 
ATOM   1004  O  O   . THR A  1 137 ? 22.177 -58.298  -26.713  1.00 53.17  ? 138 THR A O   1 
ATOM   1005  C  CB  . THR A  1 137 ? 21.279 -58.608  -29.615  1.00 55.05  ? 138 THR A CB  1 
ATOM   1006  O  OG1 . THR A  1 137 ? 20.630 -59.866  -29.391  1.00 57.41  ? 138 THR A OG1 1 
ATOM   1007  C  CG2 . THR A  1 137 ? 21.334 -58.330  -31.096  1.00 55.78  ? 138 THR A CG2 1 
ATOM   1008  N  N   . GLY A  1 138 ? 23.066 -60.282  -27.300  1.00 57.25  ? 139 GLY A N   1 
ATOM   1009  C  CA  . GLY A  1 138 ? 22.928 -60.894  -25.991  1.00 58.40  ? 139 GLY A CA  1 
ATOM   1010  C  C   . GLY A  1 138 ? 21.557 -61.512  -25.753  1.00 59.51  ? 139 GLY A C   1 
ATOM   1011  O  O   . GLY A  1 138 ? 21.237 -61.922  -24.632  1.00 60.47  ? 139 GLY A O   1 
ATOM   1012  N  N   . ASN A  1 139 ? 20.752 -61.588  -26.810  1.00 59.78  ? 140 ASN A N   1 
ATOM   1013  C  CA  . ASN A  1 139 ? 19.373 -62.093  -26.732  1.00 61.41  ? 140 ASN A CA  1 
ATOM   1014  C  C   . ASN A  1 139 ? 18.485 -61.374  -25.712  1.00 60.24  ? 140 ASN A C   1 
ATOM   1015  O  O   . ASN A  1 139 ? 17.474 -61.928  -25.244  1.00 62.03  ? 140 ASN A O   1 
ATOM   1016  C  CB  . ASN A  1 139 ? 19.362 -63.612  -26.453  1.00 65.06  ? 140 ASN A CB  1 
ATOM   1017  C  CG  . ASN A  1 139 ? 19.667 -64.452  -27.700  1.00 67.10  ? 140 ASN A CG  1 
ATOM   1018  O  OD1 . ASN A  1 139 ? 20.212 -65.546  -27.583  1.00 69.80  ? 140 ASN A OD1 1 
ATOM   1019  N  ND2 . ASN A  1 139 ? 19.317 -63.942  -28.886  1.00 65.99  ? 140 ASN A ND2 1 
ATOM   1020  N  N   . ALA A  1 140 ? 18.850 -60.127  -25.411  1.00 57.59  ? 141 ALA A N   1 
ATOM   1021  C  CA  . ALA A  1 140 ? 18.193 -59.326  -24.358  1.00 56.46  ? 141 ALA A CA  1 
ATOM   1022  C  C   . ALA A  1 140 ? 16.923 -58.647  -24.839  1.00 55.88  ? 141 ALA A C   1 
ATOM   1023  O  O   . ALA A  1 140 ? 16.260 -57.977  -24.073  1.00 55.36  ? 141 ALA A O   1 
ATOM   1024  C  CB  . ALA A  1 140 ? 19.144 -58.303  -23.801  1.00 54.25  ? 141 ALA A CB  1 
ATOM   1025  N  N   . GLY A  1 141 ? 16.601 -58.817  -26.111  1.00 56.45  ? 142 GLY A N   1 
ATOM   1026  C  CA  . GLY A  1 141 ? 15.301 -58.431  -26.634  1.00 57.17  ? 142 GLY A CA  1 
ATOM   1027  C  C   . GLY A  1 141 ? 15.166 -56.963  -26.969  1.00 54.97  ? 142 GLY A C   1 
ATOM   1028  O  O   . GLY A  1 141 ? 16.167 -56.282  -27.219  1.00 52.86  ? 142 GLY A O   1 
ATOM   1029  N  N   . SER A  1 142 ? 13.914 -56.487  -26.972  1.00 55.90  ? 143 SER A N   1 
ATOM   1030  C  CA  . SER A  1 142 ? 13.559 -55.128  -27.460  1.00 54.49  ? 143 SER A CA  1 
ATOM   1031  C  C   . SER A  1 142 ? 14.065 -54.014  -26.566  1.00 52.09  ? 143 SER A C   1 
ATOM   1032  O  O   . SER A  1 142 ? 14.510 -54.257  -25.434  1.00 51.81  ? 143 SER A O   1 
ATOM   1033  C  CB  . SER A  1 142 ? 12.041 -54.978  -27.620  1.00 56.75  ? 143 SER A CB  1 
ATOM   1034  O  OG  . SER A  1 142 ? 11.395 -54.832  -26.359  1.00 57.62  ? 143 SER A OG  1 
ATOM   1035  N  N   . ARG A  1 143 ? 13.962 -52.793  -27.078  1.00 50.68  ? 144 ARG A N   1 
ATOM   1036  C  CA  . ARG A  1 143 ? 14.451 -51.622  -26.361  1.00 48.72  ? 144 ARG A CA  1 
ATOM   1037  C  C   . ARG A  1 143 ? 13.316 -50.890  -25.630  1.00 49.65  ? 144 ARG A C   1 
ATOM   1038  O  O   . ARG A  1 143 ? 12.489 -50.230  -26.231  1.00 50.50  ? 144 ARG A O   1 
ATOM   1039  C  CB  . ARG A  1 143 ? 15.174 -50.708  -27.330  1.00 47.05  ? 144 ARG A CB  1 
ATOM   1040  C  CG  . ARG A  1 143 ? 16.354 -51.391  -27.978  1.00 46.71  ? 144 ARG A CG  1 
ATOM   1041  C  CD  . ARG A  1 143 ? 16.979 -50.555  -29.076  1.00 45.96  ? 144 ARG A CD  1 
ATOM   1042  N  NE  . ARG A  1 143 ? 17.993 -51.316  -29.805  1.00 46.10  ? 144 ARG A NE  1 
ATOM   1043  C  CZ  . ARG A  1 143 ? 18.758 -50.814  -30.767  1.00 45.98  ? 144 ARG A CZ  1 
ATOM   1044  N  NH1 . ARG A  1 143 ? 18.634 -49.553  -31.135  1.00 45.60  ? 144 ARG A NH1 1 
ATOM   1045  N  NH2 . ARG A  1 143 ? 19.654 -51.575  -31.368  1.00 47.25  ? 144 ARG A NH2 1 
ATOM   1046  N  N   . LEU A  1 144 ? 13.282 -51.022  -24.318  1.00 49.98  ? 145 LEU A N   1 
ATOM   1047  C  CA  . LEU A  1 144 ? 12.174 -50.492  -23.535  1.00 51.73  ? 145 LEU A CA  1 
ATOM   1048  C  C   . LEU A  1 144 ? 12.268 -48.990  -23.374  1.00 50.47  ? 145 LEU A C   1 
ATOM   1049  O  O   . LEU A  1 144 ? 11.314 -48.282  -23.628  1.00 51.74  ? 145 LEU A O   1 
ATOM   1050  C  CB  . LEU A  1 144 ? 12.130 -51.142  -22.140  1.00 53.26  ? 145 LEU A CB  1 
ATOM   1051  C  CG  . LEU A  1 144 ? 11.731 -52.621  -22.075  1.00 55.60  ? 145 LEU A CG  1 
ATOM   1052  C  CD1 . LEU A  1 144 ? 11.544 -53.097  -20.630  1.00 57.43  ? 145 LEU A CD1 1 
ATOM   1053  C  CD2 . LEU A  1 144 ? 10.459 -52.875  -22.886  1.00 57.82  ? 145 LEU A CD2 1 
ATOM   1054  N  N   . ALA A  1 145 ? 13.424 -48.525  -22.911  1.00 48.55  ? 146 ALA A N   1 
ATOM   1055  C  CA  . ALA A  1 145 ? 13.666 -47.100  -22.647  1.00 47.45  ? 146 ALA A CA  1 
ATOM   1056  C  C   . ALA A  1 145 ? 15.121 -46.757  -22.907  1.00 45.03  ? 146 ALA A C   1 
ATOM   1057  O  O   . ALA A  1 145 ? 16.013 -47.564  -22.657  1.00 44.69  ? 146 ALA A O   1 
ATOM   1058  C  CB  . ALA A  1 145 ? 13.302 -46.758  -21.228  1.00 48.75  ? 146 ALA A CB  1 
ATOM   1059  N  N   . CYS A  1 146 ? 15.360 -45.558  -23.405  1.00 43.91  ? 147 CYS A N   1 
ATOM   1060  C  CA  . CYS A  1 146 ? 16.715 -45.132  -23.728  1.00 42.05  ? 147 CYS A CA  1 
ATOM   1061  C  C   . CYS A  1 146 ? 16.897 -43.627  -23.638  1.00 41.72  ? 147 CYS A C   1 
ATOM   1062  O  O   . CYS A  1 146 ? 15.943 -42.877  -23.492  1.00 43.08  ? 147 CYS A O   1 
ATOM   1063  C  CB  . CYS A  1 146 ? 17.074 -45.590  -25.120  1.00 41.48  ? 147 CYS A CB  1 
ATOM   1064  S  SG  . CYS A  1 146 ? 16.066 -44.859  -26.365  1.00 41.97  ? 147 CYS A SG  1 
ATOM   1065  N  N   . GLY A  1 147 ? 18.139 -43.185  -23.718  1.00 40.55  ? 148 GLY A N   1 
ATOM   1066  C  CA  . GLY A  1 147 ? 18.442 -41.757  -23.665  1.00 40.45  ? 148 GLY A CA  1 
ATOM   1067  C  C   . GLY A  1 147 ? 19.873 -41.461  -24.090  1.00 39.44  ? 148 GLY A C   1 
ATOM   1068  O  O   . GLY A  1 147 ? 20.756 -42.311  -23.952  1.00 39.00  ? 148 GLY A O   1 
ATOM   1069  N  N   . VAL A  1 148 ? 20.101 -40.258  -24.618  1.00 39.31  ? 149 VAL A N   1 
ATOM   1070  C  CA  . VAL A  1 148 ? 21.435 -39.856  -25.048  1.00 38.64  ? 149 VAL A CA  1 
ATOM   1071  C  C   . VAL A  1 148 ? 22.245 -39.439  -23.846  1.00 38.84  ? 149 VAL A C   1 
ATOM   1072  O  O   . VAL A  1 148 ? 21.747 -38.712  -22.994  1.00 39.39  ? 149 VAL A O   1 
ATOM   1073  C  CB  . VAL A  1 148 ? 21.380 -38.706  -26.024  1.00 38.86  ? 149 VAL A CB  1 
ATOM   1074  C  CG1 . VAL A  1 148 ? 22.759 -38.272  -26.401  1.00 38.83  ? 149 VAL A CG1 1 
ATOM   1075  C  CG2 . VAL A  1 148 ? 20.629 -39.131  -27.232  1.00 39.31  ? 149 VAL A CG2 1 
ATOM   1076  N  N   . ILE A  1 149 ? 23.493 -39.905  -23.787  1.00 38.85  ? 150 ILE A N   1 
ATOM   1077  C  CA  . ILE A  1 149 ? 24.410 -39.638  -22.650  1.00 39.49  ? 150 ILE A CA  1 
ATOM   1078  C  C   . ILE A  1 149 ? 25.027 -38.262  -22.762  1.00 39.96  ? 150 ILE A C   1 
ATOM   1079  O  O   . ILE A  1 149 ? 25.697 -37.958  -23.744  1.00 40.05  ? 150 ILE A O   1 
ATOM   1080  C  CB  . ILE A  1 149 ? 25.574 -40.648  -22.574  1.00 39.73  ? 150 ILE A CB  1 
ATOM   1081  C  CG1 . ILE A  1 149 ? 25.059 -42.028  -22.196  1.00 39.67  ? 150 ILE A CG1 1 
ATOM   1082  C  CG2 . ILE A  1 149 ? 26.593 -40.199  -21.570  1.00 40.74  ? 150 ILE A CG2 1 
ATOM   1083  C  CD1 . ILE A  1 149 ? 26.092 -43.102  -22.335  1.00 40.21  ? 150 ILE A CD1 1 
ATOM   1084  N  N   . GLY A  1 150 ? 24.834 -37.450  -21.735  1.00 40.78  ? 151 GLY A N   1 
ATOM   1085  C  CA  . GLY A  1 150 ? 25.201 -36.042  -21.799  1.00 41.75  ? 151 GLY A CA  1 
ATOM   1086  C  C   . GLY A  1 150 ? 26.165 -35.592  -20.722  1.00 43.18  ? 151 GLY A C   1 
ATOM   1087  O  O   . GLY A  1 150 ? 26.234 -36.190  -19.650  1.00 43.80  ? 151 GLY A O   1 
ATOM   1088  N  N   . ILE A  1 151 ? 26.910 -34.531  -21.027  1.00 44.09  ? 152 ILE A N   1 
ATOM   1089  C  CA  . ILE A  1 151 ? 27.891 -33.979  -20.106  1.00 45.88  ? 152 ILE A CA  1 
ATOM   1090  C  C   . ILE A  1 151 ? 27.133 -33.334  -18.966  1.00 47.01  ? 152 ILE A C   1 
ATOM   1091  O  O   . ILE A  1 151 ? 26.179 -32.612  -19.190  1.00 47.02  ? 152 ILE A O   1 
ATOM   1092  C  CB  . ILE A  1 151 ? 28.796 -32.930  -20.771  1.00 46.95  ? 152 ILE A CB  1 
ATOM   1093  C  CG1 . ILE A  1 151 ? 29.606 -33.551  -21.891  1.00 46.52  ? 152 ILE A CG1 1 
ATOM   1094  C  CG2 . ILE A  1 151 ? 29.747 -32.350  -19.762  1.00 49.26  ? 152 ILE A CG2 1 
ATOM   1095  C  CD1 . ILE A  1 151 ? 30.496 -32.567  -22.574  1.00 48.17  ? 152 ILE A CD1 1 
ATOM   1096  N  N   . ALA A  1 152 ? 27.562 -33.610  -17.744  1.00 48.55  ? 153 ALA A N   1 
ATOM   1097  C  CA  . ALA A  1 152 ? 26.876 -33.129  -16.551  1.00 50.18  ? 153 ALA A CA  1 
ATOM   1098  C  C   . ALA A  1 152 ? 27.763 -32.211  -15.710  1.00 53.12  ? 153 ALA A C   1 
ATOM   1099  O  O   . ALA A  1 152 ? 28.997 -32.207  -15.851  1.00 53.84  ? 153 ALA A O   1 
ATOM   1100  C  CB  . ALA A  1 152 ? 26.438 -34.286  -15.732  1.00 50.36  ? 153 ALA A CB  1 
ATOM   1101  N  N   . GLN A  1 153 ? 27.127 -31.430  -14.832  1.00 55.14  ? 154 GLN A N   1 
ATOM   1102  C  CA  . GLN A  1 153 ? 27.862 -30.475  -13.989  1.00 58.44  ? 154 GLN A CA  1 
ATOM   1103  C  C   . GLN A  1 153 ? 28.553 -31.184  -12.863  1.00 60.45  ? 154 GLN A C   1 
ATOM   1104  O  O   . GLN A  1 153 ? 27.922 -32.024  -12.224  1.00 60.50  ? 154 GLN A O   1 
ATOM   1105  C  CB  . GLN A  1 153 ? 26.953 -29.398  -13.399  1.00 60.50  ? 154 GLN A CB  1 
ATOM   1106  C  CG  . GLN A  1 153 ? 27.725 -28.360  -12.556  1.00 64.21  ? 154 GLN A CG  1 
ATOM   1107  C  CD  . GLN A  1 153 ? 26.853 -27.217  -12.072  1.00 66.74  ? 154 GLN A CD  1 
ATOM   1108  O  OE1 . GLN A  1 153 ? 26.353 -26.437  -12.873  1.00 66.32  ? 154 GLN A OE1 1 
ATOM   1109  N  NE2 . GLN A  1 153 ? 26.672 -27.107  -10.756  1.00 69.76  ? 154 GLN A NE2 1 
ATOM   1110  O  OXT . GLN A  1 153 ? 29.719 -30.908  -12.580  1.00 62.48  ? 154 GLN A OXT 1 
ATOM   1111  N  N   . ALA B  1 1   ? 34.760 -36.917  -41.405  1.00 66.88  ? 2   ALA B N   1 
ATOM   1112  C  CA  . ALA B  1 1   ? 33.371 -36.872  -41.954  1.00 64.55  ? 2   ALA B CA  1 
ATOM   1113  C  C   . ALA B  1 1   ? 32.346 -37.067  -40.815  1.00 60.53  ? 2   ALA B C   1 
ATOM   1114  O  O   . ALA B  1 1   ? 31.456 -37.917  -40.915  1.00 60.74  ? 2   ALA B O   1 
ATOM   1115  C  CB  . ALA B  1 1   ? 33.194 -37.940  -43.088  1.00 67.50  ? 2   ALA B CB  1 
ATOM   1116  N  N   . THR B  1 2   ? 32.477 -36.259  -39.755  1.00 57.44  ? 3   THR B N   1 
ATOM   1117  C  CA  . THR B  1 2   ? 31.696 -36.398  -38.502  1.00 53.95  ? 3   THR B CA  1 
ATOM   1118  C  C   . THR B  1 2   ? 30.300 -35.836  -38.681  1.00 50.98  ? 3   THR B C   1 
ATOM   1119  O  O   . THR B  1 2   ? 30.113 -34.820  -39.349  1.00 50.31  ? 3   THR B O   1 
ATOM   1120  C  CB  . THR B  1 2   ? 32.356 -35.675  -37.293  1.00 52.90  ? 3   THR B CB  1 
ATOM   1121  O  OG1 . THR B  1 2   ? 33.759 -35.550  -37.511  1.00 56.17  ? 3   THR B OG1 1 
ATOM   1122  C  CG2 . THR B  1 2   ? 32.120 -36.436  -35.983  1.00 51.58  ? 3   THR B CG2 1 
ATOM   1123  N  N   . LYS B  1 3   ? 29.330 -36.521  -38.081  1.00 49.45  ? 4   LYS B N   1 
ATOM   1124  C  CA  . LYS B  1 3   ? 27.936 -36.091  -38.073  1.00 47.09  ? 4   LYS B CA  1 
ATOM   1125  C  C   . LYS B  1 3   ? 27.375 -36.165  -36.661  1.00 44.84  ? 4   LYS B C   1 
ATOM   1126  O  O   . LYS B  1 3   ? 27.790 -36.981  -35.862  1.00 45.60  ? 4   LYS B O   1 
ATOM   1127  C  CB  . LYS B  1 3   ? 27.091 -36.974  -38.998  1.00 48.52  ? 4   LYS B CB  1 
ATOM   1128  C  CG  . LYS B  1 3   ? 27.423 -36.865  -40.496  1.00 51.18  ? 4   LYS B CG  1 
ATOM   1129  C  CD  . LYS B  1 3   ? 26.360 -37.574  -41.370  1.00 52.57  ? 4   LYS B CD  1 
ATOM   1130  C  CE  . LYS B  1 3   ? 26.895 -38.023  -42.728  1.00 56.06  ? 4   LYS B CE  1 
ATOM   1131  N  NZ  . LYS B  1 3   ? 26.067 -39.116  -43.309  1.00 57.61  ? 4   LYS B NZ  1 
ATOM   1132  N  N   . ALA B  1 4   ? 26.429 -35.298  -36.357  1.00 42.53  ? 5   ALA B N   1 
ATOM   1133  C  CA  . ALA B  1 4   ? 25.699 -35.370  -35.099  1.00 40.87  ? 5   ALA B CA  1 
ATOM   1134  C  C   . ALA B  1 4   ? 24.232 -35.053  -35.356  1.00 39.73  ? 5   ALA B C   1 
ATOM   1135  O  O   . ALA B  1 4   ? 23.880 -34.561  -36.432  1.00 39.92  ? 5   ALA B O   1 
ATOM   1136  C  CB  . ALA B  1 4   ? 26.271 -34.418  -34.102  1.00 39.70  ? 5   ALA B CB  1 
ATOM   1137  N  N   . VAL B  1 5   ? 23.385 -35.360  -34.371  1.00 38.94  ? 6   VAL B N   1 
ATOM   1138  C  CA  . VAL B  1 5   ? 21.938 -35.122  -34.453  1.00 38.26  ? 6   VAL B CA  1 
ATOM   1139  C  C   . VAL B  1 5   ? 21.357 -34.836  -33.082  1.00 37.11  ? 6   VAL B C   1 
ATOM   1140  O  O   . VAL B  1 5   ? 21.920 -35.239  -32.077  1.00 37.20  ? 6   VAL B O   1 
ATOM   1141  C  CB  . VAL B  1 5   ? 21.182 -36.320  -35.047  1.00 39.99  ? 6   VAL B CB  1 
ATOM   1142  C  CG1 . VAL B  1 5   ? 21.024 -37.415  -34.017  1.00 40.97  ? 6   VAL B CG1 1 
ATOM   1143  C  CG2 . VAL B  1 5   ? 19.821 -35.885  -35.570  1.00 40.02  ? 6   VAL B CG2 1 
ATOM   1144  N  N   . CYS B  1 6   ? 20.230 -34.132  -33.056  1.00 36.46  ? 7   CYS B N   1 
ATOM   1145  C  CA  . CYS B  1 6   ? 19.579 -33.774  -31.805  1.00 35.93  ? 7   CYS B CA  1 
ATOM   1146  C  C   . CYS B  1 6   ? 18.093 -33.673  -31.960  1.00 36.42  ? 7   CYS B C   1 
ATOM   1147  O  O   . CYS B  1 6   ? 17.629 -32.961  -32.828  1.00 36.23  ? 7   CYS B O   1 
ATOM   1148  C  CB  . CYS B  1 6   ? 20.081 -32.432  -31.311  1.00 34.56  ? 7   CYS B CB  1 
ATOM   1149  S  SG  . CYS B  1 6   ? 19.112 -31.816  -29.949  1.00 33.94  ? 7   CYS B SG  1 
ATOM   1150  N  N   . VAL B  1 7   ? 17.355 -34.374  -31.106  1.00 37.57  ? 8   VAL B N   1 
ATOM   1151  C  CA  . VAL B  1 7   ? 15.891 -34.285  -31.079  1.00 38.50  ? 8   VAL B CA  1 
ATOM   1152  C  C   . VAL B  1 7   ? 15.402 -33.279  -30.036  1.00 37.93  ? 8   VAL B C   1 
ATOM   1153  O  O   . VAL B  1 7   ? 15.437 -33.536  -28.836  1.00 38.26  ? 8   VAL B O   1 
ATOM   1154  C  CB  . VAL B  1 7   ? 15.264 -35.638  -30.797  1.00 40.57  ? 8   VAL B CB  1 
ATOM   1155  C  CG1 . VAL B  1 7   ? 13.786 -35.486  -30.591  1.00 42.07  ? 8   VAL B CG1 1 
ATOM   1156  C  CG2 . VAL B  1 7   ? 15.548 -36.569  -31.931  1.00 41.57  ? 8   VAL B CG2 1 
ATOM   1157  N  N   . LEU B  1 8   ? 14.930 -32.136  -30.519  1.00 37.24  ? 9   LEU B N   1 
ATOM   1158  C  CA  . LEU B  1 8   ? 14.419 -31.070  -29.665  1.00 37.01  ? 9   LEU B CA  1 
ATOM   1159  C  C   . LEU B  1 8   ? 13.024 -31.414  -29.183  1.00 39.15  ? 9   LEU B C   1 
ATOM   1160  O  O   . LEU B  1 8   ? 12.154 -31.723  -29.994  1.00 40.50  ? 9   LEU B O   1 
ATOM   1161  C  CB  . LEU B  1 8   ? 14.365 -29.752  -30.428  1.00 35.89  ? 9   LEU B CB  1 
ATOM   1162  C  CG  . LEU B  1 8   ? 15.707 -29.111  -30.730  1.00 34.12  ? 9   LEU B CG  1 
ATOM   1163  C  CD1 . LEU B  1 8   ? 15.559 -28.089  -31.822  1.00 33.46  ? 9   LEU B CD1 1 
ATOM   1164  C  CD2 . LEU B  1 8   ? 16.287 -28.491  -29.489  1.00 33.59  ? 9   LEU B CD2 1 
ATOM   1165  N  N   . LYS B  1 9   ? 12.817 -31.363  -27.868  1.00 39.97  ? 10  LYS B N   1 
ATOM   1166  C  CA  . LYS B  1 9   ? 11.505 -31.630  -27.241  1.00 42.49  ? 10  LYS B CA  1 
ATOM   1167  C  C   . LYS B  1 9   ? 11.287 -30.782  -26.009  1.00 42.98  ? 10  LYS B C   1 
ATOM   1168  O  O   . LYS B  1 9   ? 12.225 -30.283  -25.425  1.00 41.97  ? 10  LYS B O   1 
ATOM   1169  C  CB  . LYS B  1 9   ? 11.378 -33.101  -26.835  1.00 44.43  ? 10  LYS B CB  1 
ATOM   1170  C  CG  . LYS B  1 9   ? 10.911 -34.034  -27.960  1.00 46.11  ? 10  LYS B CG  1 
ATOM   1171  C  CD  . LYS B  1 9   ? 10.177 -35.279  -27.395  1.00 49.49  ? 10  LYS B CD  1 
ATOM   1172  C  CE  . LYS B  1 9   ? 9.980  -36.395  -28.443  1.00 50.64  ? 10  LYS B CE  1 
ATOM   1173  N  NZ  . LYS B  1 9   ? 8.750  -36.190  -29.298  1.00 52.39  ? 10  LYS B NZ  1 
ATOM   1174  N  N   . GLY B  1 10  ? 10.045 -30.638  -25.593  1.00 45.34  ? 11  GLY B N   1 
ATOM   1175  C  CA  . GLY B  1 10  ? 9.754  -29.836  -24.420  1.00 46.52  ? 11  GLY B CA  1 
ATOM   1176  C  C   . GLY B  1 10  ? 8.377  -30.038  -23.815  1.00 50.16  ? 11  GLY B C   1 
ATOM   1177  O  O   . GLY B  1 10  ? 7.610  -30.892  -24.236  1.00 51.96  ? 11  GLY B O   1 
ATOM   1178  N  N   . ASP B  1 11  ? 8.083  -29.220  -22.806  1.00 51.62  ? 12  ASP B N   1 
ATOM   1179  C  CA  . ASP B  1 11  ? 6.812  -29.272  -22.063  1.00 55.53  ? 12  ASP B CA  1 
ATOM   1180  C  C   . ASP B  1 11  ? 5.587  -28.949  -22.920  1.00 57.10  ? 12  ASP B C   1 
ATOM   1181  O  O   . ASP B  1 11  ? 4.500  -29.482  -22.682  1.00 60.70  ? 12  ASP B O   1 
ATOM   1182  C  CB  . ASP B  1 11  ? 6.851  -28.318  -20.854  1.00 56.67  ? 12  ASP B CB  1 
ATOM   1183  C  CG  . ASP B  1 11  ? 7.362  -28.991  -19.600  1.00 58.44  ? 12  ASP B CG  1 
ATOM   1184  O  OD1 . ASP B  1 11  ? 6.890  -30.111  -19.283  1.00 61.40  ? 12  ASP B OD1 1 
ATOM   1185  O  OD2 . ASP B  1 11  ? 8.230  -28.398  -18.923  1.00 57.95  ? 12  ASP B OD2 1 
ATOM   1186  N  N   . GLY B  1 12  ? 5.773  -28.071  -23.902  1.00 54.80  ? 13  GLY B N   1 
ATOM   1187  C  CA  . GLY B  1 12  ? 4.685  -27.627  -24.765  1.00 56.27  ? 13  GLY B CA  1 
ATOM   1188  C  C   . GLY B  1 12  ? 4.784  -28.169  -26.174  1.00 54.87  ? 13  GLY B C   1 
ATOM   1189  O  O   . GLY B  1 12  ? 5.468  -29.157  -26.401  1.00 53.51  ? 13  GLY B O   1 
ATOM   1190  N  N   . PRO B  1 13  ? 4.128  -27.492  -27.135  1.00 55.46  ? 14  PRO B N   1 
ATOM   1191  C  CA  . PRO B  1 13  ? 3.956  -27.996  -28.492  1.00 55.54  ? 14  PRO B CA  1 
ATOM   1192  C  C   . PRO B  1 13  ? 5.195  -27.935  -29.369  1.00 51.91  ? 14  PRO B C   1 
ATOM   1193  O  O   . PRO B  1 13  ? 5.204  -28.547  -30.434  1.00 52.09  ? 14  PRO B O   1 
ATOM   1194  C  CB  . PRO B  1 13  ? 2.916  -27.044  -29.077  1.00 57.54  ? 14  PRO B CB  1 
ATOM   1195  C  CG  . PRO B  1 13  ? 3.189  -25.767  -28.429  1.00 56.17  ? 14  PRO B CG  1 
ATOM   1196  C  CD  . PRO B  1 13  ? 3.734  -26.073  -27.054  1.00 55.78  ? 14  PRO B CD  1 
ATOM   1197  N  N   . VAL B  1 14  ? 6.206  -27.177  -28.938  1.00 49.16  ? 15  VAL B N   1 
ATOM   1198  C  CA  . VAL B  1 14  ? 7.441  -27.001  -29.695  1.00 45.69  ? 15  VAL B CA  1 
ATOM   1199  C  C   . VAL B  1 14  ? 8.231  -28.312  -29.718  1.00 44.83  ? 15  VAL B C   1 
ATOM   1200  O  O   . VAL B  1 14  ? 8.532  -28.906  -28.680  1.00 45.04  ? 15  VAL B O   1 
ATOM   1201  C  CB  . VAL B  1 14  ? 8.320  -25.907  -29.114  1.00 43.44  ? 15  VAL B CB  1 
ATOM   1202  C  CG1 . VAL B  1 14  ? 9.475  -25.671  -30.023  1.00 40.84  ? 15  VAL B CG1 1 
ATOM   1203  C  CG2 . VAL B  1 14  ? 7.539  -24.629  -28.942  1.00 44.79  ? 15  VAL B CG2 1 
ATOM   1204  N  N   . GLN B  1 15  ? 8.528  -28.767  -30.924  1.00 44.22  ? 16  GLN B N   1 
ATOM   1205  C  CA  . GLN B  1 15  ? 9.350  -29.942  -31.143  1.00 43.48  ? 16  GLN B CA  1 
ATOM   1206  C  C   . GLN B  1 15  ? 10.019 -29.895  -32.524  1.00 42.23  ? 16  GLN B C   1 
ATOM   1207  O  O   . GLN B  1 15  ? 9.619  -29.150  -33.414  1.00 42.48  ? 16  GLN B O   1 
ATOM   1208  C  CB  . GLN B  1 15  ? 8.539  -31.224  -30.963  1.00 46.23  ? 16  GLN B CB  1 
ATOM   1209  C  CG  . GLN B  1 15  ? 7.285  -31.299  -31.795  1.00 49.36  ? 16  GLN B CG  1 
ATOM   1210  C  CD  . GLN B  1 15  ? 6.637  -32.667  -31.768  1.00 52.72  ? 16  GLN B CD  1 
ATOM   1211  O  OE1 . GLN B  1 15  ? 5.890  -33.022  -32.684  1.00 55.17  ? 16  GLN B OE1 1 
ATOM   1212  N  NE2 . GLN B  1 15  ? 6.906  -33.441  -30.709  1.00 52.93  ? 16  GLN B NE2 1 
ATOM   1213  N  N   . GLY B  1 16  ? 11.067 -30.687  -32.680  1.00 41.23  ? 17  GLY B N   1 
ATOM   1214  C  CA  . GLY B  1 16  ? 11.826 -30.719  -33.928  1.00 40.39  ? 17  GLY B CA  1 
ATOM   1215  C  C   . GLY B  1 16  ? 13.063 -31.602  -33.917  1.00 39.46  ? 17  GLY B C   1 
ATOM   1216  O  O   . GLY B  1 16  ? 13.435 -32.188  -32.897  1.00 39.25  ? 17  GLY B O   1 
ATOM   1217  N  N   . ILE B  1 17  ? 13.699 -31.681  -35.074  1.00 39.20  ? 18  ILE B N   1 
ATOM   1218  C  CA  . ILE B  1 17  ? 14.928 -32.434  -35.262  1.00 38.74  ? 18  ILE B CA  1 
ATOM   1219  C  C   . ILE B  1 17  ? 15.952 -31.527  -35.911  1.00 37.41  ? 18  ILE B C   1 
ATOM   1220  O  O   . ILE B  1 17  ? 15.644 -30.879  -36.896  1.00 37.97  ? 18  ILE B O   1 
ATOM   1221  C  CB  . ILE B  1 17  ? 14.703 -33.617  -36.205  1.00 41.02  ? 18  ILE B CB  1 
ATOM   1222  C  CG1 . ILE B  1 17  ? 14.113 -34.814  -35.459  1.00 42.67  ? 18  ILE B CG1 1 
ATOM   1223  C  CG2 . ILE B  1 17  ? 16.003 -34.025  -36.895  1.00 40.86  ? 18  ILE B CG2 1 
ATOM   1224  C  CD1 . ILE B  1 17  ? 14.191 -36.107  -36.255  1.00 44.92  ? 18  ILE B CD1 1 
ATOM   1225  N  N   . ILE B  1 18  ? 17.168 -31.488  -35.373  1.00 36.25  ? 19  ILE B N   1 
ATOM   1226  C  CA  . ILE B  1 18  ? 18.262 -30.678  -35.943  1.00 35.36  ? 19  ILE B CA  1 
ATOM   1227  C  C   . ILE B  1 18  ? 19.501 -31.503  -36.188  1.00 35.87  ? 19  ILE B C   1 
ATOM   1228  O  O   . ILE B  1 18  ? 19.955 -32.197  -35.297  1.00 35.83  ? 19  ILE B O   1 
ATOM   1229  C  CB  . ILE B  1 18  ? 18.679 -29.547  -35.018  1.00 33.73  ? 19  ILE B CB  1 
ATOM   1230  C  CG1 . ILE B  1 18  ? 17.571 -28.513  -34.883  1.00 33.54  ? 19  ILE B CG1 1 
ATOM   1231  C  CG2 . ILE B  1 18  ? 19.900 -28.893  -35.559  1.00 33.48  ? 19  ILE B CG2 1 
ATOM   1232  C  CD1 . ILE B  1 18  ? 17.331 -27.731  -36.115  1.00 34.38  ? 19  ILE B CD1 1 
ATOM   1233  N  N   . ASN B  1 19  ? 20.038 -31.420  -37.401  1.00 36.85  ? 20  ASN B N   1 
ATOM   1234  C  CA  . ASN B  1 19  ? 21.222 -32.190  -37.803  1.00 38.09  ? 20  ASN B CA  1 
ATOM   1235  C  C   . ASN B  1 19  ? 22.501 -31.370  -37.811  1.00 37.76  ? 20  ASN B C   1 
ATOM   1236  O  O   . ASN B  1 19  ? 22.465 -30.176  -38.079  1.00 37.30  ? 20  ASN B O   1 
ATOM   1237  C  CB  . ASN B  1 19  ? 21.039 -32.750  -39.203  1.00 40.23  ? 20  ASN B CB  1 
ATOM   1238  C  CG  . ASN B  1 19  ? 19.896 -33.722  -39.293  1.00 41.38  ? 20  ASN B CG  1 
ATOM   1239  O  OD1 . ASN B  1 19  ? 18.841 -33.396  -39.812  1.00 42.05  ? 20  ASN B OD1 1 
ATOM   1240  N  ND2 . ASN B  1 19  ? 20.092 -34.920  -38.772  1.00 41.96  ? 20  ASN B ND2 1 
ATOM   1241  N  N   . PHE B  1 20  ? 23.626 -32.025  -37.541  1.00 38.46  ? 21  PHE B N   1 
ATOM   1242  C  CA  . PHE B  1 20  ? 24.939 -31.398  -37.613  1.00 38.78  ? 21  PHE B CA  1 
ATOM   1243  C  C   . PHE B  1 20  ? 25.824 -32.182  -38.558  1.00 41.27  ? 21  PHE B C   1 
ATOM   1244  O  O   . PHE B  1 20  ? 25.732 -33.406  -38.627  1.00 42.52  ? 21  PHE B O   1 
ATOM   1245  C  CB  . PHE B  1 20  ? 25.600 -31.359  -36.244  1.00 37.94  ? 21  PHE B CB  1 
ATOM   1246  C  CG  . PHE B  1 20  ? 24.857 -30.552  -35.234  1.00 35.94  ? 21  PHE B CG  1 
ATOM   1247  C  CD1 . PHE B  1 20  ? 23.780 -31.082  -34.571  1.00 35.37  ? 21  PHE B CD1 1 
ATOM   1248  C  CD2 . PHE B  1 20  ? 25.245 -29.272  -34.927  1.00 35.22  ? 21  PHE B CD2 1 
ATOM   1249  C  CE1 . PHE B  1 20  ? 23.099 -30.355  -33.628  1.00 33.90  ? 21  PHE B CE1 1 
ATOM   1250  C  CE2 . PHE B  1 20  ? 24.564 -28.545  -33.990  1.00 33.78  ? 21  PHE B CE2 1 
ATOM   1251  C  CZ  . PHE B  1 20  ? 23.488 -29.093  -33.343  1.00 33.25  ? 21  PHE B CZ  1 
ATOM   1252  N  N   . GLU B  1 21  ? 26.686 -31.479  -39.282  1.00 42.45  ? 22  GLU B N   1 
ATOM   1253  C  CA  . GLU B  1 21  ? 27.658 -32.130  -40.164  1.00 45.46  ? 22  GLU B CA  1 
ATOM   1254  C  C   . GLU B  1 21  ? 28.943 -31.307  -40.369  1.00 46.86  ? 22  GLU B C   1 
ATOM   1255  O  O   . GLU B  1 21  ? 28.936 -30.259  -41.017  1.00 47.02  ? 22  GLU B O   1 
ATOM   1256  C  CB  . GLU B  1 21  ? 27.047 -32.466  -41.523  1.00 47.20  ? 22  GLU B CB  1 
ATOM   1257  C  CG  . GLU B  1 21  ? 28.023 -33.202  -42.449  1.00 51.09  ? 22  GLU B CG  1 
ATOM   1258  C  CD  . GLU B  1 21  ? 27.375 -33.741  -43.696  1.00 53.61  ? 22  GLU B CD  1 
ATOM   1259  O  OE1 . GLU B  1 21  ? 26.311 -33.230  -44.080  1.00 52.91  ? 22  GLU B OE1 1 
ATOM   1260  O  OE2 . GLU B  1 21  ? 27.946 -34.664  -44.307  1.00 56.60  ? 22  GLU B OE2 1 
ATOM   1261  N  N   . GLN B  1 22  ? 30.046 -31.825  -39.829  1.00 48.21  ? 23  GLN B N   1 
ATOM   1262  C  CA  . GLN B  1 22  ? 31.357 -31.205  -39.958  1.00 50.18  ? 23  GLN B CA  1 
ATOM   1263  C  C   . GLN B  1 22  ? 32.180 -32.087  -40.872  1.00 53.88  ? 23  GLN B C   1 
ATOM   1264  O  O   . GLN B  1 22  ? 32.523 -33.207  -40.504  1.00 55.07  ? 23  GLN B O   1 
ATOM   1265  C  CB  . GLN B  1 22  ? 32.016 -31.089  -38.579  1.00 49.52  ? 23  GLN B CB  1 
ATOM   1266  C  CG  . GLN B  1 22  ? 33.324 -30.303  -38.552  1.00 51.61  ? 23  GLN B CG  1 
ATOM   1267  C  CD  . GLN B  1 22  ? 33.943 -30.209  -37.154  1.00 51.30  ? 23  GLN B CD  1 
ATOM   1268  O  OE1 . GLN B  1 22  ? 34.022 -31.190  -36.413  1.00 51.46  ? 23  GLN B OE1 1 
ATOM   1269  N  NE2 . GLN B  1 22  ? 34.387 -29.020  -36.797  1.00 51.47  ? 23  GLN B NE2 1 
ATOM   1270  N  N   . LYS B  1 23  ? 32.466 -31.607  -42.076  1.00 56.19  ? 24  LYS B N   1 
ATOM   1271  C  CA  . LYS B  1 23  ? 33.206 -32.419  -43.049  1.00 60.30  ? 24  LYS B CA  1 
ATOM   1272  C  C   . LYS B  1 23  ? 34.644 -32.641  -42.631  1.00 62.82  ? 24  LYS B C   1 
ATOM   1273  O  O   . LYS B  1 23  ? 35.204 -33.713  -42.869  1.00 65.64  ? 24  LYS B O   1 
ATOM   1274  C  CB  . LYS B  1 23  ? 33.168 -31.804  -44.450  1.00 62.59  ? 24  LYS B CB  1 
ATOM   1275  C  CG  . LYS B  1 23  ? 31.787 -31.779  -45.077  1.00 61.44  ? 24  LYS B CG  1 
ATOM   1276  C  CD  . LYS B  1 23  ? 31.855 -31.831  -46.600  1.00 65.42  ? 24  LYS B CD  1 
ATOM   1277  C  CE  . LYS B  1 23  ? 30.615 -31.193  -47.239  1.00 64.42  ? 24  LYS B CE  1 
ATOM   1278  N  NZ  . LYS B  1 23  ? 30.847 -30.921  -48.702  1.00 68.36  ? 24  LYS B NZ  1 
ATOM   1279  N  N   . GLU B  1 24  ? 35.240 -31.627  -42.020  1.00 62.34  ? 25  GLU B N   1 
ATOM   1280  C  CA  . GLU B  1 24  ? 36.657 -31.693  -41.659  1.00 65.58  ? 25  GLU B CA  1 
ATOM   1281  C  C   . GLU B  1 24  ? 36.912 -31.173  -40.271  1.00 63.58  ? 25  GLU B C   1 
ATOM   1282  O  O   . GLU B  1 24  ? 36.353 -30.183  -39.873  1.00 61.03  ? 25  GLU B O   1 
ATOM   1283  C  CB  . GLU B  1 24  ? 37.488 -30.935  -42.679  1.00 69.24  ? 25  GLU B CB  1 
ATOM   1284  C  CG  . GLU B  1 24  ? 37.211 -31.449  -44.077  1.00 72.00  ? 25  GLU B CG  1 
ATOM   1285  C  CD  . GLU B  1 24  ? 38.190 -30.962  -45.113  1.00 77.57  ? 25  GLU B CD  1 
ATOM   1286  O  OE1 . GLU B  1 24  ? 38.459 -29.730  -45.124  1.00 78.03  ? 25  GLU B OE1 1 
ATOM   1287  O  OE2 . GLU B  1 24  ? 38.664 -31.810  -45.931  1.00 81.69  ? 25  GLU B OE2 1 
ATOM   1288  N  N   . SER B  1 25  ? 37.766 -31.861  -39.535  1.00 65.37  ? 26  SER B N   1 
ATOM   1289  C  CA  . SER B  1 25  ? 38.004 -31.565  -38.106  1.00 64.24  ? 26  SER B CA  1 
ATOM   1290  C  C   . SER B  1 25  ? 38.285 -30.093  -37.788  1.00 63.85  ? 26  SER B C   1 
ATOM   1291  O  O   . SER B  1 25  ? 37.847 -29.551  -36.776  1.00 61.18  ? 26  SER B O   1 
ATOM   1292  C  CB  . SER B  1 25  ? 39.169 -32.421  -37.581  1.00 67.81  ? 26  SER B CB  1 
ATOM   1293  O  OG  . SER B  1 25  ? 40.262 -32.400  -38.474  1.00 72.90  ? 26  SER B OG  1 
ATOM   1294  N  N   . ASN B  1 26  ? 39.027 -29.457  -38.672  1.00 66.99  ? 27  ASN B N   1 
ATOM   1295  C  CA  . ASN B  1 26  ? 39.384 -28.051  -38.527  1.00 67.41  ? 27  ASN B CA  1 
ATOM   1296  C  C   . ASN B  1 26  ? 38.316 -27.083  -39.113  1.00 64.57  ? 27  ASN B C   1 
ATOM   1297  O  O   . ASN B  1 26  ? 38.432 -25.866  -38.997  1.00 64.67  ? 27  ASN B O   1 
ATOM   1298  C  CB  . ASN B  1 26  ? 40.760 -27.824  -39.194  1.00 72.78  ? 27  ASN B CB  1 
ATOM   1299  C  CG  . ASN B  1 26  ? 40.726 -27.984  -40.765  1.00 75.19  ? 27  ASN B CG  1 
ATOM   1300  O  OD1 . ASN B  1 26  ? 40.183 -28.966  -41.312  1.00 74.34  ? 27  ASN B OD1 1 
ATOM   1301  N  ND2 . ASN B  1 26  ? 41.317 -27.004  -41.477  1.00 78.00  ? 27  ASN B ND2 1 
ATOM   1302  N  N   . GLY B  1 27  ? 37.274 -27.627  -39.734  1.00 62.41  ? 28  GLY B N   1 
ATOM   1303  C  CA  . GLY B  1 27  ? 36.397 -26.853  -40.630  1.00 60.92  ? 28  GLY B CA  1 
ATOM   1304  C  C   . GLY B  1 27  ? 35.079 -26.446  -40.002  1.00 56.40  ? 28  GLY B C   1 
ATOM   1305  O  O   . GLY B  1 27  ? 34.853 -26.682  -38.811  1.00 54.32  ? 28  GLY B O   1 
ATOM   1306  N  N   . PRO B  1 28  ? 34.186 -25.846  -40.809  1.00 55.15  ? 29  PRO B N   1 
ATOM   1307  C  CA  . PRO B  1 28  ? 32.922 -25.371  -40.298  1.00 51.34  ? 29  PRO B CA  1 
ATOM   1308  C  C   . PRO B  1 28  ? 31.896 -26.493  -40.164  1.00 49.15  ? 29  PRO B C   1 
ATOM   1309  O  O   . PRO B  1 28  ? 32.035 -27.547  -40.788  1.00 50.66  ? 29  PRO B O   1 
ATOM   1310  C  CB  . PRO B  1 28  ? 32.491 -24.362  -41.362  1.00 51.85  ? 29  PRO B CB  1 
ATOM   1311  C  CG  . PRO B  1 28  ? 32.982 -24.946  -42.620  1.00 55.01  ? 29  PRO B CG  1 
ATOM   1312  C  CD  . PRO B  1 28  ? 34.279 -25.644  -42.265  1.00 57.69  ? 29  PRO B CD  1 
ATOM   1313  N  N   . VAL B  1 29  ? 30.881 -26.231  -39.345  1.00 45.93  ? 30  VAL B N   1 
ATOM   1314  C  CA  . VAL B  1 29  ? 29.810 -27.178  -39.066  1.00 43.93  ? 30  VAL B CA  1 
ATOM   1315  C  C   . VAL B  1 29  ? 28.501 -26.712  -39.655  1.00 42.41  ? 30  VAL B C   1 
ATOM   1316  O  O   . VAL B  1 29  ? 27.998 -25.683  -39.273  1.00 40.98  ? 30  VAL B O   1 
ATOM   1317  C  CB  . VAL B  1 29  ? 29.575 -27.305  -37.570  1.00 41.86  ? 30  VAL B CB  1 
ATOM   1318  C  CG1 . VAL B  1 29  ? 28.411 -28.221  -37.320  1.00 40.11  ? 30  VAL B CG1 1 
ATOM   1319  C  CG2 . VAL B  1 29  ? 30.833 -27.794  -36.889  1.00 43.54  ? 30  VAL B CG2 1 
ATOM   1320  N  N   . LYS B  1 30  ? 27.951 -27.467  -40.590  1.00 43.30  ? 31  LYS B N   1 
ATOM   1321  C  CA  . LYS B  1 30  ? 26.625 -27.168  -41.121  1.00 42.32  ? 31  LYS B CA  1 
ATOM   1322  C  C   . LYS B  1 30  ? 25.581 -27.658  -40.152  1.00 39.93  ? 31  LYS B C   1 
ATOM   1323  O  O   . LYS B  1 30  ? 25.654 -28.774  -39.680  1.00 40.13  ? 31  LYS B O   1 
ATOM   1324  C  CB  . LYS B  1 30  ? 26.406 -27.799  -42.496  1.00 44.67  ? 31  LYS B CB  1 
ATOM   1325  C  CG  . LYS B  1 30  ? 27.224 -27.126  -43.586  1.00 47.75  ? 31  LYS B CG  1 
ATOM   1326  C  CD  . LYS B  1 30  ? 26.771 -27.483  -44.985  1.00 50.69  ? 31  LYS B CD  1 
ATOM   1327  C  CE  . LYS B  1 30  ? 27.624 -26.762  -46.028  1.00 53.71  ? 31  LYS B CE  1 
ATOM   1328  N  NZ  . LYS B  1 30  ? 27.160 -26.976  -47.413  1.00 56.87  ? 31  LYS B NZ  1 
ATOM   1329  N  N   . VAL B  1 31  ? 24.615 -26.803  -39.862  1.00 38.27  ? 32  VAL B N   1 
ATOM   1330  C  CA  . VAL B  1 31  ? 23.517 -27.120  -38.965  1.00 36.55  ? 32  VAL B CA  1 
ATOM   1331  C  C   . VAL B  1 31  ? 22.206 -26.968  -39.704  1.00 36.74  ? 32  VAL B C   1 
ATOM   1332  O  O   . VAL B  1 31  ? 21.896 -25.912  -40.199  1.00 37.00  ? 32  VAL B O   1 
ATOM   1333  C  CB  . VAL B  1 31  ? 23.486 -26.166  -37.764  1.00 34.83  ? 32  VAL B CB  1 
ATOM   1334  C  CG1 . VAL B  1 31  ? 22.416 -26.597  -36.773  1.00 33.41  ? 32  VAL B CG1 1 
ATOM   1335  C  CG2 . VAL B  1 31  ? 24.843 -26.108  -37.094  1.00 35.28  ? 32  VAL B CG2 1 
ATOM   1336  N  N   . TRP B  1 32  ? 21.431 -28.025  -39.795  1.00 37.27  ? 33  TRP B N   1 
ATOM   1337  C  CA  . TRP B  1 32  ? 20.163 -27.937  -40.510  1.00 38.17  ? 33  TRP B CA  1 
ATOM   1338  C  C   . TRP B  1 32  ? 19.105 -28.896  -39.960  1.00 38.16  ? 33  TRP B C   1 
ATOM   1339  O  O   . TRP B  1 32  ? 19.403 -29.905  -39.307  1.00 38.09  ? 33  TRP B O   1 
ATOM   1340  C  CB  . TRP B  1 32  ? 20.351 -28.172  -42.020  1.00 40.68  ? 33  TRP B CB  1 
ATOM   1341  C  CG  . TRP B  1 32  ? 20.291 -29.619  -42.430  1.00 42.56  ? 33  TRP B CG  1 
ATOM   1342  C  CD1 . TRP B  1 32  ? 19.230 -30.275  -42.972  1.00 44.32  ? 33  TRP B CD1 1 
ATOM   1343  C  CD2 . TRP B  1 32  ? 21.338 -30.585  -42.314  1.00 43.22  ? 33  TRP B CD2 1 
ATOM   1344  N  NE1 . TRP B  1 32  ? 19.550 -31.589  -43.204  1.00 45.69  ? 33  TRP B NE1 1 
ATOM   1345  C  CE2 . TRP B  1 32  ? 20.836 -31.808  -42.802  1.00 45.11  ? 33  TRP B CE2 1 
ATOM   1346  C  CE3 . TRP B  1 32  ? 22.651 -30.531  -41.850  1.00 43.06  ? 33  TRP B CE3 1 
ATOM   1347  C  CZ2 . TRP B  1 32  ? 21.599 -32.972  -42.836  1.00 46.79  ? 33  TRP B CZ2 1 
ATOM   1348  C  CZ3 . TRP B  1 32  ? 23.407 -31.677  -41.885  1.00 44.80  ? 33  TRP B CZ3 1 
ATOM   1349  C  CH2 . TRP B  1 32  ? 22.879 -32.891  -42.375  1.00 46.54  ? 33  TRP B CH2 1 
ATOM   1350  N  N   . GLY B  1 33  ? 17.856 -28.550  -40.230  1.00 38.56  ? 34  GLY B N   1 
ATOM   1351  C  CA  . GLY B  1 33  ? 16.730 -29.330  -39.763  1.00 39.03  ? 34  GLY B CA  1 
ATOM   1352  C  C   . GLY B  1 33  ? 15.464 -28.518  -39.737  1.00 39.26  ? 34  GLY B C   1 
ATOM   1353  O  O   . GLY B  1 33  ? 15.401 -27.450  -40.323  1.00 39.55  ? 34  GLY B O   1 
ATOM   1354  N  N   . SER B  1 34  ? 14.459 -29.019  -39.034  1.00 39.63  ? 35  SER B N   1 
ATOM   1355  C  CA  . SER B  1 34  ? 13.138 -28.387  -39.021  1.00 40.60  ? 35  SER B CA  1 
ATOM   1356  C  C   . SER B  1 34  ? 12.495 -28.406  -37.645  1.00 39.88  ? 35  SER B C   1 
ATOM   1357  O  O   . SER B  1 34  ? 12.251 -29.459  -37.097  1.00 40.67  ? 35  SER B O   1 
ATOM   1358  C  CB  . SER B  1 34  ? 12.228 -29.090  -40.021  1.00 43.52  ? 35  SER B CB  1 
ATOM   1359  O  OG  . SER B  1 34  ? 11.048 -28.348  -40.206  1.00 44.94  ? 35  SER B OG  1 
ATOM   1360  N  N   . ILE B  1 35  ? 12.245 -27.238  -37.078  1.00 38.94  ? 36  ILE B N   1 
ATOM   1361  C  CA  . ILE B  1 35  ? 11.542 -27.137  -35.794  1.00 39.00  ? 36  ILE B CA  1 
ATOM   1362  C  C   . ILE B  1 35  ? 10.141 -26.627  -36.040  1.00 41.13  ? 36  ILE B C   1 
ATOM   1363  O  O   . ILE B  1 35  ? 9.940  -25.784  -36.905  1.00 41.65  ? 36  ILE B O   1 
ATOM   1364  C  CB  . ILE B  1 35  ? 12.201 -26.154  -34.831  1.00 37.01  ? 36  ILE B CB  1 
ATOM   1365  C  CG1 . ILE B  1 35  ? 13.671 -26.481  -34.633  1.00 35.35  ? 36  ILE B CG1 1 
ATOM   1366  C  CG2 . ILE B  1 35  ? 11.484 -26.182  -33.501  1.00 37.21  ? 36  ILE B CG2 1 
ATOM   1367  C  CD1 . ILE B  1 35  ? 14.374 -25.475  -33.795  1.00 34.12  ? 36  ILE B CD1 1 
ATOM   1368  N  N   . LYS B  1 36  ? 9.176  -27.114  -35.267  1.00 42.72  ? 37  LYS B N   1 
ATOM   1369  C  CA  . LYS B  1 36  ? 7.779  -26.701  -35.442  1.00 45.33  ? 37  LYS B CA  1 
ATOM   1370  C  C   . LYS B  1 36  ? 7.055  -26.423  -34.136  1.00 46.08  ? 37  LYS B C   1 
ATOM   1371  O  O   . LYS B  1 36  ? 7.564  -26.691  -33.055  1.00 44.90  ? 37  LYS B O   1 
ATOM   1372  C  CB  . LYS B  1 36  ? 7.012  -27.732  -36.270  1.00 48.27  ? 37  LYS B CB  1 
ATOM   1373  C  CG  . LYS B  1 36  ? 6.991  -29.142  -35.711  1.00 49.31  ? 37  LYS B CG  1 
ATOM   1374  C  CD  . LYS B  1 36  ? 5.816  -29.929  -36.318  1.00 53.66  ? 37  LYS B CD  1 
ATOM   1375  C  CE  . LYS B  1 36  ? 5.823  -31.401  -35.914  1.00 54.92  ? 37  LYS B CE  1 
ATOM   1376  N  NZ  . LYS B  1 36  ? 4.554  -32.064  -36.342  1.00 58.98  ? 37  LYS B NZ  1 
ATOM   1377  N  N   . GLY B  1 37  ? 5.861  -25.862  -34.246  1.00 48.53  ? 38  GLY B N   1 
ATOM   1378  C  CA  . GLY B  1 37  ? 5.088  -25.461  -33.060  1.00 50.06  ? 38  GLY B CA  1 
ATOM   1379  C  C   . GLY B  1 37  ? 5.533  -24.116  -32.483  1.00 48.24  ? 38  GLY B C   1 
ATOM   1380  O  O   . GLY B  1 37  ? 5.226  -23.758  -31.328  1.00 48.67  ? 38  GLY B O   1 
ATOM   1381  N  N   . LEU B  1 38  ? 6.242  -23.358  -33.313  1.00 46.42  ? 39  LEU B N   1 
ATOM   1382  C  CA  . LEU B  1 38  ? 6.889  -22.115  -32.875  1.00 44.60  ? 39  LEU B CA  1 
ATOM   1383  C  C   . LEU B  1 38  ? 6.051  -20.903  -33.172  1.00 46.23  ? 39  LEU B C   1 
ATOM   1384  O  O   . LEU B  1 38  ? 5.455  -20.819  -34.243  1.00 47.76  ? 39  LEU B O   1 
ATOM   1385  C  CB  . LEU B  1 38  ? 8.253  -21.925  -33.559  1.00 41.87  ? 39  LEU B CB  1 
ATOM   1386  C  CG  . LEU B  1 38  ? 9.443  -22.639  -32.911  1.00 39.44  ? 39  LEU B CG  1 
ATOM   1387  C  CD1 . LEU B  1 38  ? 10.594 -22.708  -33.849  1.00 37.69  ? 39  LEU B CD1 1 
ATOM   1388  C  CD2 . LEU B  1 38  ? 9.842  -21.961  -31.649  1.00 38.61  ? 39  LEU B CD2 1 
ATOM   1389  N  N   . THR B  1 39  ? 6.044  -19.957  -32.230  1.00 46.12  ? 40  THR B N   1 
ATOM   1390  C  CA  . THR B  1 39  ? 5.326  -18.681  -32.383  1.00 47.75  ? 40  THR B CA  1 
ATOM   1391  C  C   . THR B  1 39  ? 5.979  -17.911  -33.519  1.00 46.40  ? 40  THR B C   1 
ATOM   1392  O  O   . THR B  1 39  ? 7.206  -17.851  -33.583  1.00 43.83  ? 40  THR B O   1 
ATOM   1393  C  CB  . THR B  1 39  ? 5.368  -17.822  -31.110  1.00 47.93  ? 40  THR B CB  1 
ATOM   1394  O  OG1 . THR B  1 39  ? 6.337  -16.795  -31.269  1.00 46.31  ? 40  THR B OG1 1 
ATOM   1395  C  CG2 . THR B  1 39  ? 5.742  -18.631  -29.872  1.00 47.44  ? 40  THR B CG2 1 
ATOM   1396  N  N   . GLU B  1 40  ? 5.179  -17.334  -34.417  1.00 48.66  ? 41  GLU B N   1 
ATOM   1397  C  CA  . GLU B  1 40  ? 5.723  -16.725  -35.659  1.00 47.99  ? 41  GLU B CA  1 
ATOM   1398  C  C   . GLU B  1 40  ? 6.775  -15.689  -35.374  1.00 45.73  ? 41  GLU B C   1 
ATOM   1399  O  O   . GLU B  1 40  ? 6.591  -14.848  -34.513  1.00 46.09  ? 41  GLU B O   1 
ATOM   1400  C  CB  . GLU B  1 40  ? 4.642  -16.057  -36.504  1.00 51.25  ? 41  GLU B CB  1 
ATOM   1401  C  CG  . GLU B  1 40  ? 5.189  -15.372  -37.782  1.00 51.31  ? 41  GLU B CG  1 
ATOM   1402  C  CD  . GLU B  1 40  ? 4.097  -14.609  -38.588  1.00 55.21  ? 41  GLU B CD  1 
ATOM   1403  O  OE1 . GLU B  1 40  ? 3.301  -13.866  -37.968  1.00 56.70  ? 41  GLU B OE1 1 
ATOM   1404  O  OE2 . GLU B  1 40  ? 4.052  -14.746  -39.841  1.00 56.24  ? 41  GLU B OE2 1 
ATOM   1405  N  N   . GLY B  1 41  ? 7.874  -15.753  -36.111  1.00 43.85  ? 42  GLY B N   1 
ATOM   1406  C  CA  . GLY B  1 41  ? 8.947  -14.778  -35.981  1.00 42.24  ? 42  GLY B CA  1 
ATOM   1407  C  C   . GLY B  1 41  ? 10.259 -15.369  -35.506  1.00 39.67  ? 42  GLY B C   1 
ATOM   1408  O  O   . GLY B  1 41  ? 10.468 -16.574  -35.598  1.00 38.99  ? 42  GLY B O   1 
ATOM   1409  N  N   . LEU B  1 42  ? 11.125 -14.508  -34.968  1.00 38.58  ? 43  LEU B N   1 
ATOM   1410  C  CA  . LEU B  1 42  ? 12.496 -14.880  -34.572  1.00 36.52  ? 43  LEU B CA  1 
ATOM   1411  C  C   . LEU B  1 42  ? 12.545 -15.661  -33.273  1.00 35.80  ? 43  LEU B C   1 
ATOM   1412  O  O   . LEU B  1 42  ? 11.781 -15.391  -32.371  1.00 37.01  ? 43  LEU B O   1 
ATOM   1413  C  CB  . LEU B  1 42  ? 13.397 -13.635  -34.446  1.00 36.24  ? 43  LEU B CB  1 
ATOM   1414  C  CG  . LEU B  1 42  ? 13.904 -13.015  -35.753  1.00 36.48  ? 43  LEU B CG  1 
ATOM   1415  C  CD1 . LEU B  1 42  ? 13.277 -11.648  -35.976  1.00 38.26  ? 43  LEU B CD1 1 
ATOM   1416  C  CD2 . LEU B  1 42  ? 15.390 -12.914  -35.763  1.00 35.45  ? 43  LEU B CD2 1 
ATOM   1417  N  N   . HIS B  1 43  ? 13.460 -16.616  -33.182  1.00 34.35  ? 44  HIS B N   1 
ATOM   1418  C  CA  . HIS B  1 43  ? 13.683 -17.358  -31.947  1.00 33.89  ? 44  HIS B CA  1 
ATOM   1419  C  C   . HIS B  1 43  ? 15.163 -17.530  -31.655  1.00 32.56  ? 44  HIS B C   1 
ATOM   1420  O  O   . HIS B  1 43  ? 15.950 -17.792  -32.535  1.00 32.10  ? 44  HIS B O   1 
ATOM   1421  C  CB  . HIS B  1 43  ? 12.981 -18.714  -31.990  1.00 34.18  ? 44  HIS B CB  1 
ATOM   1422  C  CG  . HIS B  1 43  ? 11.497 -18.610  -31.891  1.00 36.11  ? 44  HIS B CG  1 
ATOM   1423  N  ND1 . HIS B  1 43  ? 10.847 -18.465  -30.689  1.00 37.45  ? 44  HIS B ND1 1 
ATOM   1424  C  CD2 . HIS B  1 43  ? 10.537 -18.585  -32.844  1.00 37.54  ? 44  HIS B CD2 1 
ATOM   1425  C  CE1 . HIS B  1 43  ? 9.548  -18.373  -30.902  1.00 39.61  ? 44  HIS B CE1 1 
ATOM   1426  N  NE2 . HIS B  1 43  ? 9.335  -18.440  -32.204  1.00 39.66  ? 44  HIS B NE2 1 
ATOM   1427  N  N   . GLY B  1 44  ? 15.540 -17.350  -30.406  1.00 32.50  ? 45  GLY B N   1 
ATOM   1428  C  CA  . GLY B  1 44  ? 16.898 -17.606  -29.979  1.00 31.81  ? 45  GLY B CA  1 
ATOM   1429  C  C   . GLY B  1 44  ? 17.264 -19.060  -30.101  1.00 31.07  ? 45  GLY B C   1 
ATOM   1430  O  O   . GLY B  1 44  ? 16.435 -19.907  -29.939  1.00 31.58  ? 45  GLY B O   1 
ATOM   1431  N  N   . PHE B  1 45  ? 18.526 -19.346  -30.347  1.00 30.58  ? 46  PHE B N   1 
ATOM   1432  C  CA  . PHE B  1 45  ? 18.950 -20.684  -30.735  1.00 30.23  ? 46  PHE B CA  1 
ATOM   1433  C  C   . PHE B  1 45  ? 20.402 -20.950  -30.341  1.00 30.23  ? 46  PHE B C   1 
ATOM   1434  O  O   . PHE B  1 45  ? 21.314 -20.578  -31.055  1.00 30.39  ? 46  PHE B O   1 
ATOM   1435  C  CB  . PHE B  1 45  ? 18.790 -20.814  -32.249  1.00 30.25  ? 46  PHE B CB  1 
ATOM   1436  C  CG  . PHE B  1 45  ? 18.956 -22.215  -32.781  1.00 30.18  ? 46  PHE B CG  1 
ATOM   1437  C  CD1 . PHE B  1 45  ? 18.226 -23.265  -32.254  1.00 30.36  ? 46  PHE B CD1 1 
ATOM   1438  C  CD2 . PHE B  1 45  ? 19.804 -22.463  -33.843  1.00 30.31  ? 46  PHE B CD2 1 
ATOM   1439  C  CE1 . PHE B  1 45  ? 18.368 -24.526  -32.743  1.00 30.57  ? 46  PHE B CE1 1 
ATOM   1440  C  CE2 . PHE B  1 45  ? 19.943 -23.712  -34.341  1.00 30.75  ? 46  PHE B CE2 1 
ATOM   1441  C  CZ  . PHE B  1 45  ? 19.225 -24.754  -33.788  1.00 31.03  ? 46  PHE B CZ  1 
ATOM   1442  N  N   . HIS B  1 46  ? 20.608 -21.615  -29.214  1.00 30.47  ? 47  HIS B N   1 
ATOM   1443  C  CA  . HIS B  1 46  ? 21.931 -21.741  -28.627  1.00 30.93  ? 47  HIS B CA  1 
ATOM   1444  C  C   . HIS B  1 46  ? 22.279 -23.136  -28.140  1.00 31.23  ? 47  HIS B C   1 
ATOM   1445  O  O   . HIS B  1 46  ? 21.426 -23.901  -27.779  1.00 31.31  ? 47  HIS B O   1 
ATOM   1446  C  CB  . HIS B  1 46  ? 22.046 -20.791  -27.451  1.00 31.71  ? 47  HIS B CB  1 
ATOM   1447  C  CG  . HIS B  1 46  ? 21.415 -19.461  -27.687  1.00 31.47  ? 47  HIS B CG  1 
ATOM   1448  N  ND1 . HIS B  1 46  ? 20.219 -19.106  -27.122  1.00 31.94  ? 47  HIS B ND1 1 
ATOM   1449  C  CD2 . HIS B  1 46  ? 21.807 -18.401  -28.425  1.00 31.99  ? 47  HIS B CD2 1 
ATOM   1450  C  CE1 . HIS B  1 46  ? 19.907 -17.879  -27.487  1.00 32.24  ? 47  HIS B CE1 1 
ATOM   1451  N  NE2 . HIS B  1 46  ? 20.855 -17.428  -28.282  1.00 31.99  ? 47  HIS B NE2 1 
ATOM   1452  N  N   . VAL B  1 47  ? 23.563 -23.446  -28.130  1.00 31.93  ? 48  VAL B N   1 
ATOM   1453  C  CA  . VAL B  1 47  ? 24.081 -24.671  -27.529  1.00 32.49  ? 48  VAL B CA  1 
ATOM   1454  C  C   . VAL B  1 47  ? 24.469 -24.366  -26.109  1.00 33.78  ? 48  VAL B C   1 
ATOM   1455  O  O   . VAL B  1 47  ? 25.331 -23.536  -25.873  1.00 34.64  ? 48  VAL B O   1 
ATOM   1456  C  CB  . VAL B  1 47  ? 25.341 -25.157  -28.237  1.00 33.05  ? 48  VAL B CB  1 
ATOM   1457  C  CG1 . VAL B  1 47  ? 25.979 -26.256  -27.477  1.00 34.10  ? 48  VAL B CG1 1 
ATOM   1458  C  CG2 . VAL B  1 47  ? 25.020 -25.626  -29.604  1.00 32.66  ? 48  VAL B CG2 1 
ATOM   1459  N  N   . HIS B  1 48  ? 23.835 -25.037  -25.161  1.00 34.35  ? 49  HIS B N   1 
ATOM   1460  C  CA  . HIS B  1 48  ? 24.117 -24.826  -23.732  1.00 36.09  ? 49  HIS B CA  1 
ATOM   1461  C  C   . HIS B  1 48  ? 25.125 -25.818  -23.195  1.00 37.50  ? 49  HIS B C   1 
ATOM   1462  O  O   . HIS B  1 48  ? 25.375 -26.836  -23.802  1.00 37.35  ? 49  HIS B O   1 
ATOM   1463  C  CB  . HIS B  1 48  ? 22.841 -24.931  -22.911  1.00 36.52  ? 49  HIS B CB  1 
ATOM   1464  C  CG  . HIS B  1 48  ? 21.906 -23.777  -23.092  1.00 35.85  ? 49  HIS B CG  1 
ATOM   1465  N  ND1 . HIS B  1 48  ? 21.453 -23.015  -22.040  1.00 37.12  ? 49  HIS B ND1 1 
ATOM   1466  C  CD2 . HIS B  1 48  ? 21.336 -23.264  -24.203  1.00 34.15  ? 49  HIS B CD2 1 
ATOM   1467  C  CE1 . HIS B  1 48  ? 20.635 -22.088  -22.495  1.00 36.49  ? 49  HIS B CE1 1 
ATOM   1468  N  NE2 . HIS B  1 48  ? 20.546 -22.220  -23.805  1.00 34.72  ? 49  HIS B NE2 1 
ATOM   1469  N  N   . GLU B  1 49  ? 25.673 -25.528  -22.027  1.00 39.42  ? 50  GLU B N   1 
ATOM   1470  C  CA  . GLU B  1 49  ? 26.846 -26.245  -21.517  1.00 41.41  ? 50  GLU B CA  1 
ATOM   1471  C  C   . GLU B  1 49  ? 26.611 -27.721  -21.275  1.00 41.68  ? 50  GLU B C   1 
ATOM   1472  O  O   . GLU B  1 49  ? 27.378 -28.544  -21.732  1.00 42.04  ? 50  GLU B O   1 
ATOM   1473  C  CB  . GLU B  1 49  ? 27.367 -25.602  -20.224  1.00 44.06  ? 50  GLU B CB  1 
ATOM   1474  C  CG  . GLU B  1 49  ? 28.720 -26.131  -19.749  1.00 46.42  ? 50  GLU B CG  1 
ATOM   1475  C  CD  . GLU B  1 49  ? 29.284 -25.338  -18.600  1.00 49.16  ? 50  GLU B CD  1 
ATOM   1476  O  OE1 . GLU B  1 49  ? 28.797 -24.238  -18.304  1.00 48.84  ? 50  GLU B OE1 1 
ATOM   1477  O  OE2 . GLU B  1 49  ? 30.221 -25.831  -17.971  1.00 52.04  ? 50  GLU B OE2 1 
ATOM   1478  N  N   . PHE B  1 50  ? 25.561 -28.047  -20.543  1.00 41.95  ? 51  PHE B N   1 
ATOM   1479  C  CA  . PHE B  1 50  ? 25.368 -29.406  -20.062  1.00 43.07  ? 51  PHE B CA  1 
ATOM   1480  C  C   . PHE B  1 50  ? 24.316 -30.208  -20.801  1.00 41.63  ? 51  PHE B C   1 
ATOM   1481  O  O   . PHE B  1 50  ? 23.242 -29.729  -21.090  1.00 40.44  ? 51  PHE B O   1 
ATOM   1482  C  CB  . PHE B  1 50  ? 24.989 -29.383  -18.597  1.00 45.38  ? 51  PHE B CB  1 
ATOM   1483  C  CG  . PHE B  1 50  ? 25.946 -28.626  -17.747  1.00 47.50  ? 51  PHE B CG  1 
ATOM   1484  C  CD1 . PHE B  1 50  ? 27.268 -28.998  -17.683  1.00 48.98  ? 51  PHE B CD1 1 
ATOM   1485  C  CD2 . PHE B  1 50  ? 25.519 -27.537  -17.002  1.00 48.77  ? 51  PHE B CD2 1 
ATOM   1486  C  CE1 . PHE B  1 50  ? 28.153 -28.292  -16.892  1.00 51.73  ? 51  PHE B CE1 1 
ATOM   1487  C  CE2 . PHE B  1 50  ? 26.397 -26.824  -16.217  1.00 51.03  ? 51  PHE B CE2 1 
ATOM   1488  C  CZ  . PHE B  1 50  ? 27.715 -27.198  -16.160  1.00 52.59  ? 51  PHE B CZ  1 
ATOM   1489  N  N   . GLY B  1 51  ? 24.638 -31.467  -21.060  1.00 42.27  ? 52  GLY B N   1 
ATOM   1490  C  CA  . GLY B  1 51  ? 23.696 -32.427  -21.624  1.00 41.66  ? 52  GLY B CA  1 
ATOM   1491  C  C   . GLY B  1 51  ? 22.832 -33.032  -20.549  1.00 43.31  ? 52  GLY B C   1 
ATOM   1492  O  O   . GLY B  1 51  ? 22.570 -34.218  -20.551  1.00 44.28  ? 52  GLY B O   1 
ATOM   1493  N  N   . ASP B  1 52  ? 22.375 -32.202  -19.634  1.00 44.08  ? 53  ASP B N   1 
ATOM   1494  C  CA  . ASP B  1 52  ? 21.616 -32.659  -18.489  1.00 46.34  ? 53  ASP B CA  1 
ATOM   1495  C  C   . ASP B  1 52  ? 20.167 -32.311  -18.728  1.00 45.74  ? 53  ASP B C   1 
ATOM   1496  O  O   . ASP B  1 52  ? 19.836 -31.156  -18.934  1.00 44.59  ? 53  ASP B O   1 
ATOM   1497  C  CB  . ASP B  1 52  ? 22.141 -31.965  -17.233  1.00 48.53  ? 53  ASP B CB  1 
ATOM   1498  C  CG  . ASP B  1 52  ? 21.589 -32.545  -15.957  1.00 51.61  ? 53  ASP B CG  1 
ATOM   1499  O  OD1 . ASP B  1 52  ? 20.415 -32.950  -15.953  1.00 52.13  ? 53  ASP B OD1 1 
ATOM   1500  O  OD2 . ASP B  1 52  ? 22.333 -32.566  -14.951  1.00 53.89  ? 53  ASP B OD2 1 
ATOM   1501  N  N   . ASN B  1 53  ? 19.309 -33.324  -18.700  1.00 46.93  ? 54  ASN B N   1 
ATOM   1502  C  CA  . ASN B  1 53  ? 17.858 -33.141  -18.876  1.00 47.18  ? 54  ASN B CA  1 
ATOM   1503  C  C   . ASN B  1 53  ? 17.048 -33.536  -17.635  1.00 50.24  ? 54  ASN B C   1 
ATOM   1504  O  O   . ASN B  1 53  ? 15.833 -33.670  -17.714  1.00 50.97  ? 54  ASN B O   1 
ATOM   1505  C  CB  . ASN B  1 53  ? 17.373 -33.943  -20.076  1.00 46.17  ? 54  ASN B CB  1 
ATOM   1506  C  CG  . ASN B  1 53  ? 16.520 -33.116  -21.030  1.00 44.91  ? 54  ASN B CG  1 
ATOM   1507  O  OD1 . ASN B  1 53  ? 17.013 -32.180  -21.665  1.00 43.34  ? 54  ASN B OD1 1 
ATOM   1508  N  ND2 . ASN B  1 53  ? 15.250 -33.471  -21.156  1.00 46.13  ? 54  ASN B ND2 1 
ATOM   1509  N  N   . THR B  1 54  ? 17.750 -33.693  -16.506  1.00 52.22  ? 55  THR B N   1 
ATOM   1510  C  CA  . THR B  1 54  ? 17.196 -34.118  -15.214  1.00 55.85  ? 55  THR B CA  1 
ATOM   1511  C  C   . THR B  1 54  ? 15.921 -33.397  -14.850  1.00 57.29  ? 55  THR B C   1 
ATOM   1512  O  O   . THR B  1 54  ? 14.868 -34.011  -14.721  1.00 59.18  ? 55  THR B O   1 
ATOM   1513  C  CB  . THR B  1 54  ? 18.213 -33.866  -14.097  1.00 57.72  ? 55  THR B CB  1 
ATOM   1514  O  OG1 . THR B  1 54  ? 19.282 -34.795  -14.237  1.00 57.85  ? 55  THR B OG1 1 
ATOM   1515  C  CG2 . THR B  1 54  ? 17.594 -34.014  -12.718  1.00 61.98  ? 55  THR B CG2 1 
ATOM   1516  N  N   . ALA B  1 55  ? 16.042 -32.088  -14.674  1.00 56.70  ? 56  ALA B N   1 
ATOM   1517  C  CA  . ALA B  1 55  ? 14.925 -31.218  -14.352  1.00 57.99  ? 56  ALA B CA  1 
ATOM   1518  C  C   . ALA B  1 55  ? 14.543 -30.401  -15.575  1.00 54.86  ? 56  ALA B C   1 
ATOM   1519  O  O   . ALA B  1 55  ? 14.395 -29.184  -15.507  1.00 54.64  ? 56  ALA B O   1 
ATOM   1520  C  CB  . ALA B  1 55  ? 15.290 -30.319  -13.196  1.00 60.20  ? 56  ALA B CB  1 
ATOM   1521  N  N   . GLY B  1 56  ? 14.382 -31.088  -16.697  1.00 52.92  ? 57  GLY B N   1 
ATOM   1522  C  CA  . GLY B  1 56  ? 13.909 -30.467  -17.937  1.00 50.57  ? 57  GLY B CA  1 
ATOM   1523  C  C   . GLY B  1 56  ? 15.010 -29.758  -18.697  1.00 47.35  ? 57  GLY B C   1 
ATOM   1524  O  O   . GLY B  1 56  ? 16.155 -30.163  -18.640  1.00 46.70  ? 57  GLY B O   1 
ATOM   1525  N  N   . CYS B  1 57  ? 14.654 -28.699  -19.417  1.00 45.76  ? 58  CYS B N   1 
ATOM   1526  C  CA  . CYS B  1 57  ? 15.633 -27.903  -20.137  1.00 43.04  ? 58  CYS B CA  1 
ATOM   1527  C  C   . CYS B  1 57  ? 16.473 -27.053  -19.197  1.00 43.79  ? 58  CYS B C   1 
ATOM   1528  O  O   . CYS B  1 57  ? 17.592 -26.703  -19.544  1.00 42.45  ? 58  CYS B O   1 
ATOM   1529  C  CB  . CYS B  1 57  ? 14.959 -26.990  -21.156  1.00 41.63  ? 58  CYS B CB  1 
ATOM   1530  S  SG  . CYS B  1 57  ? 14.281 -27.809  -22.607  1.00 40.74  ? 58  CYS B SG  1 
ATOM   1531  N  N   . THR B  1 58  ? 15.943 -26.708  -18.022  1.00 46.39  ? 59  THR B N   1 
ATOM   1532  C  CA  . THR B  1 58  ? 16.660 -25.837  -17.066  1.00 47.69  ? 59  THR B CA  1 
ATOM   1533  C  C   . THR B  1 58  ? 18.009 -26.407  -16.635  1.00 48.06  ? 59  THR B C   1 
ATOM   1534  O  O   . THR B  1 58  ? 18.953 -25.664  -16.372  1.00 48.16  ? 59  THR B O   1 
ATOM   1535  C  CB  . THR B  1 58  ? 15.865 -25.621  -15.789  1.00 51.13  ? 59  THR B CB  1 
ATOM   1536  O  OG1 . THR B  1 58  ? 14.507 -25.389  -16.122  1.00 51.77  ? 59  THR B OG1 1 
ATOM   1537  C  CG2 . THR B  1 58  ? 16.412 -24.434  -15.011  1.00 52.57  ? 59  THR B CG2 1 
ATOM   1538  N  N   . SER B  1 59  ? 18.076 -27.733  -16.561  1.00 48.57  ? 60  SER B N   1 
ATOM   1539  C  CA  . SER B  1 59  ? 19.272 -28.452  -16.136  1.00 49.28  ? 60  SER B CA  1 
ATOM   1540  C  C   . SER B  1 59  ? 20.439 -28.250  -17.054  1.00 46.98  ? 60  SER B C   1 
ATOM   1541  O  O   . SER B  1 59  ? 21.567 -28.439  -16.631  1.00 48.13  ? 60  SER B O   1 
ATOM   1542  C  CB  . SER B  1 59  ? 18.991 -29.936  -16.068  1.00 50.14  ? 60  SER B CB  1 
ATOM   1543  O  OG  . SER B  1 59  ? 17.766 -30.146  -15.416  1.00 52.95  ? 60  SER B OG  1 
ATOM   1544  N  N   . ALA B  1 60  ? 20.165 -27.879  -18.307  1.00 44.38  ? 61  ALA B N   1 
ATOM   1545  C  CA  . ALA B  1 60  ? 21.198 -27.645  -19.354  1.00 42.24  ? 61  ALA B CA  1 
ATOM   1546  C  C   . ALA B  1 60  ? 22.212 -26.562  -19.003  1.00 42.66  ? 61  ALA B C   1 
ATOM   1547  O  O   . ALA B  1 60  ? 23.279 -26.472  -19.599  1.00 41.82  ? 61  ALA B O   1 
ATOM   1548  C  CB  . ALA B  1 60  ? 20.529 -27.298  -20.692  1.00 39.74  ? 61  ALA B CB  1 
ATOM   1549  N  N   . GLY B  1 61  ? 21.858 -25.731  -18.039  1.00 44.36  ? 62  GLY B N   1 
ATOM   1550  C  CA  . GLY B  1 61  ? 22.743 -24.688  -17.574  1.00 45.54  ? 62  GLY B CA  1 
ATOM   1551  C  C   . GLY B  1 61  ? 22.780 -23.524  -18.538  1.00 43.66  ? 62  GLY B C   1 
ATOM   1552  O  O   . GLY B  1 61  ? 21.852 -23.331  -19.314  1.00 41.90  ? 62  GLY B O   1 
ATOM   1553  N  N   . PRO B  1 62  ? 23.859 -22.731  -18.492  1.00 44.43  ? 63  PRO B N   1 
ATOM   1554  C  CA  . PRO B  1 62  ? 23.975 -21.548  -19.320  1.00 43.13  ? 63  PRO B CA  1 
ATOM   1555  C  C   . PRO B  1 62  ? 24.512 -21.815  -20.719  1.00 40.95  ? 63  PRO B C   1 
ATOM   1556  O  O   . PRO B  1 62  ? 24.769 -22.949  -21.090  1.00 40.43  ? 63  PRO B O   1 
ATOM   1557  C  CB  . PRO B  1 62  ? 24.987 -20.717  -18.553  1.00 45.57  ? 63  PRO B CB  1 
ATOM   1558  C  CG  . PRO B  1 62  ? 25.897 -21.706  -17.970  1.00 47.11  ? 63  PRO B CG  1 
ATOM   1559  C  CD  . PRO B  1 62  ? 25.037 -22.883  -17.617  1.00 47.01  ? 63  PRO B CD  1 
ATOM   1560  N  N   . HIS B  1 63  ? 24.669 -20.749  -21.483  1.00 40.09  ? 64  HIS B N   1 
ATOM   1561  C  CA  . HIS B  1 63  ? 25.223 -20.828  -22.825  1.00 38.59  ? 64  HIS B CA  1 
ATOM   1562  C  C   . HIS B  1 63  ? 26.607 -21.432  -22.783  1.00 39.72  ? 64  HIS B C   1 
ATOM   1563  O  O   . HIS B  1 63  ? 27.392 -21.081  -21.924  1.00 41.98  ? 64  HIS B O   1 
ATOM   1564  C  CB  . HIS B  1 63  ? 25.331 -19.432  -23.413  1.00 38.55  ? 64  HIS B CB  1 
ATOM   1565  C  CG  . HIS B  1 63  ? 24.022 -18.831  -23.779  1.00 37.12  ? 64  HIS B CG  1 
ATOM   1566  N  ND1 . HIS B  1 63  ? 23.886 -17.960  -24.832  1.00 36.07  ? 64  HIS B ND1 1 
ATOM   1567  C  CD2 . HIS B  1 63  ? 22.791 -18.969  -23.233  1.00 37.02  ? 64  HIS B CD2 1 
ATOM   1568  C  CE1 . HIS B  1 63  ? 22.621 -17.587  -24.921  1.00 35.77  ? 64  HIS B CE1 1 
ATOM   1569  N  NE2 . HIS B  1 63  ? 21.937 -18.182  -23.959  1.00 36.15  ? 64  HIS B NE2 1 
ATOM   1570  N  N   . PHE B  1 64  ? 26.913 -22.330  -23.712  1.00 38.66  ? 65  PHE B N   1 
ATOM   1571  C  CA  . PHE B  1 64  ? 28.228 -22.986  -23.733  1.00 40.16  ? 65  PHE B CA  1 
ATOM   1572  C  C   . PHE B  1 64  ? 29.301 -21.961  -23.993  1.00 41.49  ? 65  PHE B C   1 
ATOM   1573  O  O   . PHE B  1 64  ? 29.332 -21.364  -25.056  1.00 40.35  ? 65  PHE B O   1 
ATOM   1574  C  CB  . PHE B  1 64  ? 28.280 -24.090  -24.788  1.00 39.11  ? 65  PHE B CB  1 
ATOM   1575  C  CG  . PHE B  1 64  ? 29.603 -24.815  -24.876  1.00 40.65  ? 65  PHE B CG  1 
ATOM   1576  C  CD1 . PHE B  1 64  ? 30.279 -25.199  -23.745  1.00 42.94  ? 65  PHE B CD1 1 
ATOM   1577  C  CD2 . PHE B  1 64  ? 30.142 -25.146  -26.111  1.00 40.71  ? 65  PHE B CD2 1 
ATOM   1578  C  CE1 . PHE B  1 64  ? 31.480 -25.872  -23.838  1.00 45.27  ? 65  PHE B CE1 1 
ATOM   1579  C  CE2 . PHE B  1 64  ? 31.335 -25.823  -26.213  1.00 42.88  ? 65  PHE B CE2 1 
ATOM   1580  C  CZ  . PHE B  1 64  ? 32.006 -26.188  -25.074  1.00 45.18  ? 65  PHE B CZ  1 
ATOM   1581  N  N   . ASN B  1 65  ? 30.185 -21.789  -23.012  1.00 44.31  ? 66  ASN B N   1 
ATOM   1582  C  CA  . ASN B  1 65  ? 31.130 -20.651  -22.962  1.00 46.53  ? 66  ASN B CA  1 
ATOM   1583  C  C   . ASN B  1 65  ? 32.516 -20.989  -22.371  1.00 49.89  ? 66  ASN B C   1 
ATOM   1584  O  O   . ASN B  1 65  ? 32.885 -20.493  -21.315  1.00 52.40  ? 66  ASN B O   1 
ATOM   1585  C  CB  . ASN B  1 65  ? 30.484 -19.510  -22.163  1.00 46.94  ? 66  ASN B CB  1 
ATOM   1586  C  CG  . ASN B  1 65  ? 31.308 -18.252  -22.169  1.00 48.95  ? 66  ASN B CG  1 
ATOM   1587  O  OD1 . ASN B  1 65  ? 32.292 -18.164  -22.860  1.00 50.21  ? 66  ASN B OD1 1 
ATOM   1588  N  ND2 . ASN B  1 65  ? 30.909 -17.278  -21.390  1.00 50.09  ? 66  ASN B ND2 1 
ATOM   1589  N  N   . PRO B  1 66  ? 33.295 -21.828  -23.065  1.00 50.37  ? 67  PRO B N   1 
ATOM   1590  C  CA  . PRO B  1 66  ? 34.547 -22.320  -22.531  1.00 53.77  ? 67  PRO B CA  1 
ATOM   1591  C  C   . PRO B  1 66  ? 35.656 -21.309  -22.588  1.00 57.06  ? 67  PRO B C   1 
ATOM   1592  O  O   . PRO B  1 66  ? 36.610 -21.447  -21.827  1.00 60.91  ? 67  PRO B O   1 
ATOM   1593  C  CB  . PRO B  1 66  ? 34.884 -23.487  -23.449  1.00 53.13  ? 67  PRO B CB  1 
ATOM   1594  C  CG  . PRO B  1 66  ? 34.262 -23.141  -24.716  1.00 50.42  ? 67  PRO B CG  1 
ATOM   1595  C  CD  . PRO B  1 66  ? 33.021 -22.386  -24.394  1.00 48.18  ? 67  PRO B CD  1 
ATOM   1596  N  N   . LEU B  1 67  ? 35.550 -20.320  -23.483  1.00 56.17  ? 68  LEU B N   1 
ATOM   1597  C  CA  . LEU B  1 67  ? 36.550 -19.242  -23.588  1.00 59.18  ? 68  LEU B CA  1 
ATOM   1598  C  C   . LEU B  1 67  ? 36.169 -18.027  -22.737  1.00 59.93  ? 68  LEU B C   1 
ATOM   1599  O  O   . LEU B  1 67  ? 36.732 -16.960  -22.895  1.00 62.12  ? 68  LEU B O   1 
ATOM   1600  C  CB  . LEU B  1 67  ? 36.760 -18.835  -25.047  1.00 58.52  ? 68  LEU B CB  1 
ATOM   1601  C  CG  . LEU B  1 67  ? 37.212 -19.950  -26.006  1.00 58.61  ? 68  LEU B CG  1 
ATOM   1602  C  CD1 . LEU B  1 67  ? 37.606 -19.373  -27.385  1.00 59.09  ? 68  LEU B CD1 1 
ATOM   1603  C  CD2 . LEU B  1 67  ? 38.350 -20.807  -25.427  1.00 61.96  ? 68  LEU B CD2 1 
ATOM   1604  N  N   . SER B  1 68  ? 35.194 -18.197  -21.849  1.00 58.55  ? 69  SER B N   1 
ATOM   1605  C  CA  . SER B  1 68  ? 34.865 -17.208  -20.811  1.00 60.11  ? 69  SER B CA  1 
ATOM   1606  C  C   . SER B  1 68  ? 34.599 -15.796  -21.341  1.00 59.70  ? 69  SER B C   1 
ATOM   1607  O  O   . SER B  1 68  ? 35.061 -14.805  -20.777  1.00 62.54  ? 69  SER B O   1 
ATOM   1608  C  CB  . SER B  1 68  ? 35.978 -17.164  -19.768  1.00 64.97  ? 69  SER B CB  1 
ATOM   1609  O  OG  . SER B  1 68  ? 36.374 -18.477  -19.405  1.00 65.87  ? 69  SER B OG  1 
ATOM   1610  N  N   . ARG B  1 69  ? 33.830 -15.717  -22.413  1.00 56.36  ? 70  ARG B N   1 
ATOM   1611  C  CA  . ARG B  1 69  ? 33.518 -14.440  -23.043  1.00 55.97  ? 70  ARG B CA  1 
ATOM   1612  C  C   . ARG B  1 69  ? 32.093 -13.991  -22.777  1.00 53.54  ? 70  ARG B C   1 
ATOM   1613  O  O   . ARG B  1 69  ? 31.354 -14.654  -22.062  1.00 52.43  ? 70  ARG B O   1 
ATOM   1614  C  CB  . ARG B  1 69  ? 33.823 -14.504  -24.530  1.00 54.90  ? 70  ARG B CB  1 
ATOM   1615  C  CG  . ARG B  1 69  ? 35.252 -14.079  -24.771  1.00 58.29  ? 70  ARG B CG  1 
ATOM   1616  C  CD  . ARG B  1 69  ? 35.662 -14.203  -26.209  1.00 57.96  ? 70  ARG B CD  1 
ATOM   1617  N  NE  . ARG B  1 69  ? 36.843 -15.039  -26.347  1.00 60.58  ? 70  ARG B NE  1 
ATOM   1618  C  CZ  . ARG B  1 69  ? 37.527 -15.206  -27.468  1.00 61.58  ? 70  ARG B CZ  1 
ATOM   1619  N  NH1 . ARG B  1 69  ? 37.176 -14.570  -28.581  1.00 61.02  ? 70  ARG B NH1 1 
ATOM   1620  N  NH2 . ARG B  1 69  ? 38.585 -16.003  -27.462  1.00 64.47  ? 70  ARG B NH2 1 
ATOM   1621  N  N   . LYS B  1 70  ? 31.745 -12.837  -23.332  1.00 53.24  ? 71  LYS B N   1 
ATOM   1622  C  CA  . LYS B  1 70  ? 30.406 -12.255  -23.224  1.00 51.42  ? 71  LYS B CA  1 
ATOM   1623  C  C   . LYS B  1 70  ? 29.495 -12.733  -24.354  1.00 47.78  ? 71  LYS B C   1 
ATOM   1624  O  O   . LYS B  1 70  ? 29.969 -13.145  -25.416  1.00 46.86  ? 71  LYS B O   1 
ATOM   1625  C  CB  . LYS B  1 70  ? 30.489 -10.730  -23.303  1.00 53.39  ? 71  LYS B CB  1 
ATOM   1626  C  CG  . LYS B  1 70  ? 31.414 -10.063  -22.275  1.00 57.83  ? 71  LYS B CG  1 
ATOM   1627  C  CD  . LYS B  1 70  ? 30.642 -9.617   -21.038  1.00 59.18  ? 71  LYS B CD  1 
ATOM   1628  C  CE  . LYS B  1 70  ? 31.523 -8.857   -20.042  1.00 63.91  ? 71  LYS B CE  1 
ATOM   1629  N  NZ  . LYS B  1 70  ? 30.735 -8.427   -18.833  1.00 65.29  ? 71  LYS B NZ  1 
ATOM   1630  N  N   . HIS B  1 71  ? 28.181 -12.648  -24.129  1.00 46.06  ? 72  HIS B N   1 
ATOM   1631  C  CA  . HIS B  1 71  ? 27.199 -13.083  -25.131  1.00 43.02  ? 72  HIS B CA  1 
ATOM   1632  C  C   . HIS B  1 71  ? 27.307 -12.212  -26.373  1.00 42.77  ? 72  HIS B C   1 
ATOM   1633  O  O   . HIS B  1 71  ? 27.728 -11.055  -26.304  1.00 44.61  ? 72  HIS B O   1 
ATOM   1634  C  CB  . HIS B  1 71  ? 25.763 -13.054  -24.593  1.00 41.88  ? 72  HIS B CB  1 
ATOM   1635  C  CG  . HIS B  1 71  ? 24.741 -13.550  -25.571  1.00 39.33  ? 72  HIS B CG  1 
ATOM   1636  N  ND1 . HIS B  1 71  ? 24.640 -14.873  -25.937  1.00 37.66  ? 72  HIS B ND1 1 
ATOM   1637  C  CD2 . HIS B  1 71  ? 23.782 -12.891  -26.270  1.00 38.38  ? 72  HIS B CD2 1 
ATOM   1638  C  CE1 . HIS B  1 71  ? 23.665 -15.002  -26.823  1.00 36.07  ? 72  HIS B CE1 1 
ATOM   1639  N  NE2 . HIS B  1 71  ? 23.125 -13.817  -27.036  1.00 36.07  ? 72  HIS B NE2 1 
ATOM   1640  N  N   . GLY B  1 72  ? 26.931 -12.786  -27.510  1.00 40.74  ? 73  GLY B N   1 
ATOM   1641  C  CA  . GLY B  1 72  ? 26.906 -12.053  -28.768  1.00 40.58  ? 73  GLY B CA  1 
ATOM   1642  C  C   . GLY B  1 72  ? 26.241 -12.797  -29.902  1.00 38.45  ? 73  GLY B C   1 
ATOM   1643  O  O   . GLY B  1 72  ? 25.718 -13.887  -29.727  1.00 37.12  ? 73  GLY B O   1 
ATOM   1644  N  N   . GLY B  1 73  ? 26.251 -12.184  -31.070  1.00 38.69  ? 74  GLY B N   1 
ATOM   1645  C  CA  . GLY B  1 73  ? 25.714 -12.804  -32.269  1.00 37.47  ? 74  GLY B CA  1 
ATOM   1646  C  C   . GLY B  1 73  ? 26.743 -13.729  -32.855  1.00 37.92  ? 74  GLY B C   1 
ATOM   1647  O  O   . GLY B  1 73  ? 27.897 -13.594  -32.548  1.00 39.80  ? 74  GLY B O   1 
ATOM   1648  N  N   . PRO B  1 74  ? 26.337 -14.669  -33.710  1.00 36.94  ? 75  PRO B N   1 
ATOM   1649  C  CA  . PRO B  1 74  ? 27.285 -15.646  -34.224  1.00 37.74  ? 75  PRO B CA  1 
ATOM   1650  C  C   . PRO B  1 74  ? 28.397 -15.028  -35.059  1.00 40.09  ? 75  PRO B C   1 
ATOM   1651  O  O   . PRO B  1 74  ? 29.515 -15.497  -35.020  1.00 41.70  ? 75  PRO B O   1 
ATOM   1652  C  CB  . PRO B  1 74  ? 26.416 -16.568  -35.084  1.00 36.44  ? 75  PRO B CB  1 
ATOM   1653  C  CG  . PRO B  1 74  ? 25.224 -15.794  -35.396  1.00 35.80  ? 75  PRO B CG  1 
ATOM   1654  C  CD  . PRO B  1 74  ? 24.994 -14.870  -34.263  1.00 35.61  ? 75  PRO B CD  1 
ATOM   1655  N  N   . LYS B  1 75  ? 28.087 -13.984  -35.807  1.00 40.80  ? 76  LYS B N   1 
ATOM   1656  C  CA  . LYS B  1 75  ? 29.096 -13.296  -36.604  1.00 43.60  ? 76  LYS B CA  1 
ATOM   1657  C  C   . LYS B  1 75  ? 30.053 -12.506  -35.746  1.00 45.42  ? 76  LYS B C   1 
ATOM   1658  O  O   . LYS B  1 75  ? 31.189 -12.279  -36.142  1.00 48.07  ? 76  LYS B O   1 
ATOM   1659  C  CB  . LYS B  1 75  ? 28.456 -12.313  -37.571  1.00 44.28  ? 76  LYS B CB  1 
ATOM   1660  C  CG  . LYS B  1 75  ? 27.336 -12.875  -38.412  1.00 43.36  ? 76  LYS B CG  1 
ATOM   1661  C  CD  . LYS B  1 75  ? 27.184 -12.044  -39.698  1.00 45.37  ? 76  LYS B CD  1 
ATOM   1662  C  CE  . LYS B  1 75  ? 25.910 -12.367  -40.475  1.00 44.66  ? 76  LYS B CE  1 
ATOM   1663  N  NZ  . LYS B  1 75  ? 25.627 -11.291  -41.511  1.00 46.33  ? 76  LYS B NZ  1 
ATOM   1664  N  N   . ASP B  1 76  ? 29.571 -12.046  -34.594  1.00 44.55  ? 77  ASP B N   1 
ATOM   1665  C  CA  . ASP B  1 76  ? 30.402 -11.306  -33.638  1.00 46.59  ? 77  ASP B CA  1 
ATOM   1666  C  C   . ASP B  1 76  ? 31.612 -12.165  -33.204  1.00 48.09  ? 77  ASP B C   1 
ATOM   1667  O  O   . ASP B  1 76  ? 31.505 -13.385  -33.054  1.00 46.54  ? 77  ASP B O   1 
ATOM   1668  C  CB  . ASP B  1 76  ? 29.582 -10.835  -32.404  1.00 45.36  ? 77  ASP B CB  1 
ATOM   1669  C  CG  . ASP B  1 76  ? 28.594 -9.677   -32.723  1.00 44.97  ? 77  ASP B CG  1 
ATOM   1670  O  OD1 . ASP B  1 76  ? 28.842 -8.888   -33.637  1.00 46.76  ? 77  ASP B OD1 1 
ATOM   1671  O  OD2 . ASP B  1 76  ? 27.568 -9.517   -32.043  1.00 43.71  ? 77  ASP B OD2 1 
ATOM   1672  N  N   . GLU B  1 77  ? 32.771 -11.518  -33.054  1.00 51.49  ? 78  GLU B N   1 
ATOM   1673  C  CA  . GLU B  1 77  ? 33.957 -12.194  -32.532  1.00 53.57  ? 78  GLU B CA  1 
ATOM   1674  C  C   . GLU B  1 77  ? 33.790 -12.430  -31.056  1.00 52.79  ? 78  GLU B C   1 
ATOM   1675  O  O   . GLU B  1 77  ? 34.023 -13.533  -30.587  1.00 52.40  ? 78  GLU B O   1 
ATOM   1676  C  CB  . GLU B  1 77  ? 35.238 -11.398  -32.762  1.00 57.88  ? 78  GLU B CB  1 
ATOM   1677  C  CG  . GLU B  1 77  ? 36.381 -11.886  -31.849  1.00 60.99  ? 78  GLU B CG  1 
ATOM   1678  C  CD  . GLU B  1 77  ? 37.782 -11.428  -32.281  1.00 66.52  ? 78  GLU B CD  1 
ATOM   1679  O  OE1 . GLU B  1 77  ? 37.941 -10.297  -32.821  1.00 68.48  ? 78  GLU B OE1 1 
ATOM   1680  O  OE2 . GLU B  1 77  ? 38.737 -12.214  -32.057  1.00 68.88  ? 78  GLU B OE2 1 
ATOM   1681  N  N   . GLU B  1 78  ? 33.419 -11.379  -30.333  1.00 53.00  ? 79  GLU B N   1 
ATOM   1682  C  CA  . GLU B  1 78  ? 33.071 -11.512  -28.915  1.00 52.53  ? 79  GLU B CA  1 
ATOM   1683  C  C   . GLU B  1 78  ? 31.711 -12.175  -28.761  1.00 48.76  ? 79  GLU B C   1 
ATOM   1684  O  O   . GLU B  1 78  ? 30.683 -11.505  -28.706  1.00 47.42  ? 79  GLU B O   1 
ATOM   1685  C  CB  . GLU B  1 78  ? 33.086 -10.155  -28.203  1.00 54.68  ? 79  GLU B CB  1 
ATOM   1686  C  CG  . GLU B  1 78  ? 32.887 -10.220  -26.664  1.00 55.21  ? 79  GLU B CG  1 
ATOM   1687  C  CD  . GLU B  1 78  ? 34.123 -10.722  -25.884  1.00 58.43  ? 79  GLU B CD  1 
ATOM   1688  O  OE1 . GLU B  1 78  ? 35.174 -11.043  -26.488  1.00 60.48  ? 79  GLU B OE1 1 
ATOM   1689  O  OE2 . GLU B  1 78  ? 34.047 -10.785  -24.641  1.00 59.30  ? 79  GLU B OE2 1 
ATOM   1690  N  N   . ARG B  1 79  ? 31.737 -13.502  -28.697  1.00 47.45  ? 80  ARG B N   1 
ATOM   1691  C  CA  . ARG B  1 79  ? 30.548 -14.327  -28.526  1.00 44.43  ? 80  ARG B CA  1 
ATOM   1692  C  C   . ARG B  1 79  ? 30.822 -15.534  -27.656  1.00 44.48  ? 80  ARG B C   1 
ATOM   1693  O  O   . ARG B  1 79  ? 31.969 -15.893  -27.429  1.00 46.65  ? 80  ARG B O   1 
ATOM   1694  C  CB  . ARG B  1 79  ? 30.058 -14.837  -29.878  1.00 42.57  ? 80  ARG B CB  1 
ATOM   1695  C  CG  . ARG B  1 79  ? 31.089 -15.631  -30.664  1.00 43.64  ? 80  ARG B CG  1 
ATOM   1696  C  CD  . ARG B  1 79  ? 30.493 -16.282  -31.906  1.00 42.06  ? 80  ARG B CD  1 
ATOM   1697  N  NE  . ARG B  1 79  ? 29.897 -17.582  -31.628  1.00 40.25  ? 80  ARG B NE  1 
ATOM   1698  C  CZ  . ARG B  1 79  ? 29.499 -18.454  -32.555  1.00 39.23  ? 80  ARG B CZ  1 
ATOM   1699  N  NH1 . ARG B  1 79  ? 29.622 -18.188  -33.845  1.00 39.75  ? 80  ARG B NH1 1 
ATOM   1700  N  NH2 . ARG B  1 79  ? 28.981 -19.620  -32.186  1.00 38.17  ? 80  ARG B NH2 1 
ATOM   1701  N  N   . HIS B  1 80  ? 29.756 -16.176  -27.187  1.00 42.48  ? 81  HIS B N   1 
ATOM   1702  C  CA  . HIS B  1 80  ? 29.874 -17.497  -26.581  1.00 42.18  ? 81  HIS B CA  1 
ATOM   1703  C  C   . HIS B  1 80  ? 30.080 -18.519  -27.698  1.00 41.24  ? 81  HIS B C   1 
ATOM   1704  O  O   . HIS B  1 80  ? 29.561 -18.348  -28.785  1.00 40.06  ? 81  HIS B O   1 
ATOM   1705  C  CB  . HIS B  1 80  ? 28.625 -17.879  -25.787  1.00 40.56  ? 81  HIS B CB  1 
ATOM   1706  C  CG  . HIS B  1 80  ? 28.322 -16.979  -24.632  1.00 41.67  ? 81  HIS B CG  1 
ATOM   1707  N  ND1 . HIS B  1 80  ? 27.038 -16.719  -24.208  1.00 40.45  ? 81  HIS B ND1 1 
ATOM   1708  C  CD2 . HIS B  1 80  ? 29.137 -16.302  -23.793  1.00 44.37  ? 81  HIS B CD2 1 
ATOM   1709  C  CE1 . HIS B  1 80  ? 27.077 -15.919  -23.160  1.00 42.37  ? 81  HIS B CE1 1 
ATOM   1710  N  NE2 . HIS B  1 80  ? 28.337 -15.650  -22.888  1.00 44.70  ? 81  HIS B NE2 1 
ATOM   1711  N  N   . VAL B  1 81  ? 30.831 -19.578  -27.435  1.00 42.18  ? 82  VAL B N   1 
ATOM   1712  C  CA  . VAL B  1 81  ? 31.008 -20.644  -28.416  1.00 41.46  ? 82  VAL B CA  1 
ATOM   1713  C  C   . VAL B  1 81  ? 29.664 -21.159  -28.861  1.00 38.58  ? 82  VAL B C   1 
ATOM   1714  O  O   . VAL B  1 81  ? 29.446 -21.399  -30.023  1.00 37.79  ? 82  VAL B O   1 
ATOM   1715  C  CB  . VAL B  1 81  ? 31.850 -21.803  -27.849  1.00 43.11  ? 82  VAL B CB  1 
ATOM   1716  C  CG1 . VAL B  1 81  ? 31.860 -23.001  -28.775  1.00 42.18  ? 82  VAL B CG1 1 
ATOM   1717  C  CG2 . VAL B  1 81  ? 33.268 -21.313  -27.592  1.00 46.65  ? 82  VAL B CG2 1 
ATOM   1718  N  N   . GLY B  1 82  ? 28.743 -21.288  -27.930  1.00 37.58  ? 83  GLY B N   1 
ATOM   1719  C  CA  . GLY B  1 82  ? 27.413 -21.824  -28.234  1.00 35.63  ? 83  GLY B CA  1 
ATOM   1720  C  C   . GLY B  1 82  ? 26.374 -20.864  -28.802  1.00 34.32  ? 83  GLY B C   1 
ATOM   1721  O  O   . GLY B  1 82  ? 25.240 -21.249  -29.032  1.00 32.96  ? 83  GLY B O   1 
ATOM   1722  N  N   . ASP B  1 83  ? 26.748 -19.611  -29.016  1.00 35.11  ? 84  ASP B N   1 
ATOM   1723  C  CA  . ASP B  1 83  ? 25.819 -18.600  -29.503  1.00 34.12  ? 84  ASP B CA  1 
ATOM   1724  C  C   . ASP B  1 83  ? 25.621 -18.740  -30.995  1.00 33.60  ? 84  ASP B C   1 
ATOM   1725  O  O   . ASP B  1 83  ? 26.375 -18.171  -31.773  1.00 34.64  ? 84  ASP B O   1 
ATOM   1726  C  CB  . ASP B  1 83  ? 26.335 -17.199  -29.203  1.00 35.39  ? 84  ASP B CB  1 
ATOM   1727  C  CG  . ASP B  1 83  ? 26.218 -16.823  -27.746  1.00 36.01  ? 84  ASP B CG  1 
ATOM   1728  O  OD1 . ASP B  1 83  ? 25.506 -17.474  -26.976  1.00 35.11  ? 84  ASP B OD1 1 
ATOM   1729  O  OD2 . ASP B  1 83  ? 26.843 -15.843  -27.338  1.00 37.89  ? 84  ASP B OD2 1 
ATOM   1730  N  N   . LEU B  1 84  ? 24.600 -19.501  -31.386  1.00 32.49  ? 85  LEU B N   1 
ATOM   1731  C  CA  . LEU B  1 84  ? 24.248 -19.698  -32.796  1.00 32.20  ? 85  LEU B CA  1 
ATOM   1732  C  C   . LEU B  1 84  ? 23.199 -18.700  -33.288  1.00 31.89  ? 85  LEU B C   1 
ATOM   1733  O  O   . LEU B  1 84  ? 22.709 -18.823  -34.404  1.00 31.95  ? 85  LEU B O   1 
ATOM   1734  C  CB  . LEU B  1 84  ? 23.772 -21.129  -33.042  1.00 31.57  ? 85  LEU B CB  1 
ATOM   1735  C  CG  . LEU B  1 84  ? 24.872 -22.173  -33.039  1.00 32.04  ? 85  LEU B CG  1 
ATOM   1736  C  CD1 . LEU B  1 84  ? 24.316 -23.542  -33.209  1.00 31.67  ? 85  LEU B CD1 1 
ATOM   1737  C  CD2 . LEU B  1 84  ? 25.838 -21.872  -34.130  1.00 33.31  ? 85  LEU B CD2 1 
ATOM   1738  N  N   . GLY B  1 85  ? 22.861 -17.712  -32.466  1.00 31.96  ? 86  GLY B N   1 
ATOM   1739  C  CA  . GLY B  1 85  ? 22.006 -16.608  -32.898  1.00 32.17  ? 86  GLY B CA  1 
ATOM   1740  C  C   . GLY B  1 85  ? 20.532 -16.943  -32.947  1.00 31.54  ? 86  GLY B C   1 
ATOM   1741  O  O   . GLY B  1 85  ? 20.009 -17.504  -31.995  1.00 31.30  ? 86  GLY B O   1 
ATOM   1742  N  N   . ASN B  1 86  ? 19.863 -16.604  -34.053  1.00 31.75  ? 87  ASN B N   1 
ATOM   1743  C  CA  . ASN B  1 86  ? 18.406 -16.792  -34.182  1.00 31.56  ? 87  ASN B CA  1 
ATOM   1744  C  C   . ASN B  1 86  ? 17.985 -17.789  -35.248  1.00 31.66  ? 87  ASN B C   1 
ATOM   1745  O  O   . ASN B  1 86  ? 18.741 -18.081  -36.154  1.00 31.99  ? 87  ASN B O   1 
ATOM   1746  C  CB  . ASN B  1 86  ? 17.733 -15.469  -34.480  1.00 32.27  ? 87  ASN B CB  1 
ATOM   1747  C  CG  . ASN B  1 86  ? 17.633 -14.610  -33.281  1.00 32.51  ? 87  ASN B CG  1 
ATOM   1748  O  OD1 . ASN B  1 86  ? 17.150 -15.038  -32.254  1.00 32.64  ? 87  ASN B OD1 1 
ATOM   1749  N  ND2 . ASN B  1 86  ? 18.088 -13.389  -33.391  1.00 33.54  ? 87  ASN B ND2 1 
ATOM   1750  N  N   . VAL B  1 87  ? 16.776 -18.317  -35.101  1.00 31.88  ? 88  VAL B N   1 
ATOM   1751  C  CA  . VAL B  1 87  ? 16.102 -19.099  -36.138  1.00 32.71  ? 88  VAL B CA  1 
ATOM   1752  C  C   . VAL B  1 87  ? 14.746 -18.465  -36.393  1.00 33.88  ? 88  VAL B C   1 
ATOM   1753  O  O   . VAL B  1 87  ? 14.117 -17.979  -35.476  1.00 34.02  ? 88  VAL B O   1 
ATOM   1754  C  CB  . VAL B  1 87  ? 15.894 -20.576  -35.745  1.00 32.41  ? 88  VAL B CB  1 
ATOM   1755  C  CG1 . VAL B  1 87  ? 17.204 -21.292  -35.637  1.00 31.60  ? 88  VAL B CG1 1 
ATOM   1756  C  CG2 . VAL B  1 87  ? 15.150 -20.688  -34.455  1.00 32.54  ? 88  VAL B CG2 1 
ATOM   1757  N  N   . THR B  1 88  ? 14.297 -18.478  -37.638  1.00 35.27  ? 89  THR B N   1 
ATOM   1758  C  CA  . THR B  1 88  ? 13.070 -17.781  -38.033  1.00 36.98  ? 89  THR B CA  1 
ATOM   1759  C  C   . THR B  1 88  ? 11.915 -18.732  -38.318  1.00 38.42  ? 89  THR B C   1 
ATOM   1760  O  O   . THR B  1 88  ? 12.040 -19.659  -39.099  1.00 38.96  ? 89  THR B O   1 
ATOM   1761  C  CB  . THR B  1 88  ? 13.292 -16.871  -39.261  1.00 38.21  ? 89  THR B CB  1 
ATOM   1762  O  OG1 . THR B  1 88  ? 14.144 -15.768  -38.905  1.00 37.45  ? 89  THR B OG1 1 
ATOM   1763  C  CG2 . THR B  1 88  ? 11.974 -16.314  -39.782  1.00 40.39  ? 89  THR B CG2 1 
ATOM   1764  N  N   . ALA B  1 89  ? 10.784 -18.458  -37.675  1.00 39.51  ? 90  ALA B N   1 
ATOM   1765  C  CA  . ALA B  1 89  ? 9.574  -19.269  -37.775  1.00 41.43  ? 90  ALA B CA  1 
ATOM   1766  C  C   . ALA B  1 89  ? 8.494  -18.600  -38.649  1.00 44.16  ? 90  ALA B C   1 
ATOM   1767  O  O   . ALA B  1 89  ? 8.149  -17.431  -38.449  1.00 44.88  ? 90  ALA B O   1 
ATOM   1768  C  CB  . ALA B  1 89  ? 9.030  -19.542  -36.386  1.00 41.43  ? 90  ALA B CB  1 
ATOM   1769  N  N   . ASP B  1 90  ? 7.948  -19.358  -39.600  1.00 46.17  ? 91  ASP B N   1 
ATOM   1770  C  CA  . ASP B  1 90  ? 6.913  -18.854  -40.526  1.00 49.26  ? 91  ASP B CA  1 
ATOM   1771  C  C   . ASP B  1 90  ? 5.491  -19.110  -40.050  1.00 51.87  ? 91  ASP B C   1 
ATOM   1772  O  O   . ASP B  1 90  ? 5.249  -19.972  -39.203  1.00 51.68  ? 91  ASP B O   1 
ATOM   1773  C  CB  . ASP B  1 90  ? 7.094  -19.431  -41.932  1.00 50.73  ? 91  ASP B CB  1 
ATOM   1774  C  CG  . ASP B  1 90  ? 6.715  -20.896  -42.032  1.00 51.93  ? 91  ASP B CG  1 
ATOM   1775  O  OD1 . ASP B  1 90  ? 6.781  -21.439  -43.148  1.00 53.88  ? 91  ASP B OD1 1 
ATOM   1776  O  OD2 . ASP B  1 90  ? 6.359  -21.517  -41.021  1.00 51.39  ? 91  ASP B OD2 1 
ATOM   1777  N  N   . LYS B  1 91  ? 4.562  -18.345  -40.617  1.00 54.76  ? 92  LYS B N   1 
ATOM   1778  C  CA  . LYS B  1 91  ? 3.109  -18.387  -40.278  1.00 58.19  ? 92  LYS B CA  1 
ATOM   1779  C  C   . LYS B  1 91  ? 2.667  -19.609  -39.508  1.00 58.63  ? 92  LYS B C   1 
ATOM   1780  O  O   . LYS B  1 91  ? 2.244  -19.498  -38.363  1.00 58.74  ? 92  LYS B O   1 
ATOM   1781  C  CB  . LYS B  1 91  ? 2.199  -18.311  -41.524  1.00 62.28  ? 92  LYS B CB  1 
ATOM   1782  C  CG  . LYS B  1 91  ? 2.765  -17.637  -42.763  1.00 62.81  ? 92  LYS B CG  1 
ATOM   1783  C  CD  . LYS B  1 91  ? 2.920  -16.094  -42.571  1.00 62.73  ? 92  LYS B CD  1 
ATOM   1784  C  CE  . LYS B  1 91  ? 3.011  -15.325  -43.926  1.00 64.57  ? 92  LYS B CE  1 
ATOM   1785  N  NZ  . LYS B  1 91  ? 1.681  -14.905  -44.475  1.00 69.22  ? 92  LYS B NZ  1 
ATOM   1786  N  N   . ASP B  1 92  ? 2.770  -20.767  -40.156  1.00 59.28  ? 93  ASP B N   1 
ATOM   1787  C  CA  . ASP B  1 92  ? 2.219  -22.026  -39.625  1.00 60.71  ? 93  ASP B CA  1 
ATOM   1788  C  C   . ASP B  1 92  ? 3.141  -22.680  -38.574  1.00 57.24  ? 93  ASP B C   1 
ATOM   1789  O  O   . ASP B  1 92  ? 2.995  -23.862  -38.248  1.00 57.99  ? 93  ASP B O   1 
ATOM   1790  C  CB  . ASP B  1 92  ? 1.815  -23.007  -40.753  1.00 63.66  ? 93  ASP B CB  1 
ATOM   1791  C  CG  . ASP B  1 92  ? 2.161  -22.503  -42.151  1.00 64.41  ? 93  ASP B CG  1 
ATOM   1792  O  OD1 . ASP B  1 92  ? 3.347  -22.399  -42.478  1.00 61.83  ? 93  ASP B OD1 1 
ATOM   1793  O  OD2 . ASP B  1 92  ? 1.253  -22.235  -42.936  1.00 68.03  ? 93  ASP B OD2 1 
ATOM   1794  N  N   . GLY B  1 93  ? 4.066  -21.889  -38.032  1.00 53.90  ? 94  GLY B N   1 
ATOM   1795  C  CA  . GLY B  1 93  ? 4.845  -22.276  -36.859  1.00 51.08  ? 94  GLY B CA  1 
ATOM   1796  C  C   . GLY B  1 93  ? 6.104  -23.064  -37.136  1.00 48.46  ? 94  GLY B C   1 
ATOM   1797  O  O   . GLY B  1 93  ? 6.755  -23.507  -36.209  1.00 46.51  ? 94  GLY B O   1 
ATOM   1798  N  N   . VAL B  1 94  ? 6.428  -23.272  -38.409  1.00 48.68  ? 95  VAL B N   1 
ATOM   1799  C  CA  . VAL B  1 94  ? 7.606  -24.043  -38.810  1.00 46.62  ? 95  VAL B CA  1 
ATOM   1800  C  C   . VAL B  1 94  ? 8.803  -23.129  -38.891  1.00 44.44  ? 95  VAL B C   1 
ATOM   1801  O  O   . VAL B  1 94  ? 8.688  -21.989  -39.318  1.00 45.53  ? 95  VAL B O   1 
ATOM   1802  C  CB  . VAL B  1 94  ? 7.428  -24.654  -40.206  1.00 48.56  ? 95  VAL B CB  1 
ATOM   1803  C  CG1 . VAL B  1 94  ? 8.748  -25.101  -40.778  1.00 46.30  ? 95  VAL B CG1 1 
ATOM   1804  C  CG2 . VAL B  1 94  ? 6.456  -25.807  -40.166  1.00 51.81  ? 95  VAL B CG2 1 
ATOM   1805  N  N   . ALA B  1 95  ? 9.962  -23.636  -38.510  1.00 42.33  ? 96  ALA B N   1 
ATOM   1806  C  CA  . ALA B  1 95  ? 11.217 -22.916  -38.686  1.00 40.16  ? 96  ALA B CA  1 
ATOM   1807  C  C   . ALA B  1 95  ? 12.170 -23.834  -39.437  1.00 39.96  ? 96  ALA B C   1 
ATOM   1808  O  O   . ALA B  1 95  ? 12.640 -24.825  -38.889  1.00 39.20  ? 96  ALA B O   1 
ATOM   1809  C  CB  . ALA B  1 95  ? 11.780 -22.536  -37.355  1.00 37.94  ? 96  ALA B CB  1 
ATOM   1810  N  N   . ASP B  1 96  ? 12.430 -23.530  -40.702  1.00 41.05  ? 97  ASP B N   1 
ATOM   1811  C  CA  . ASP B  1 96  ? 13.323 -24.363  -41.517  1.00 41.58  ? 97  ASP B CA  1 
ATOM   1812  C  C   . ASP B  1 96  ? 14.792 -23.977  -41.334  1.00 39.70  ? 97  ASP B C   1 
ATOM   1813  O  O   . ASP B  1 96  ? 15.323 -23.164  -42.079  1.00 40.34  ? 97  ASP B O   1 
ATOM   1814  C  CB  . ASP B  1 96  ? 12.910 -24.297  -42.994  1.00 44.50  ? 97  ASP B CB  1 
ATOM   1815  C  CG  . ASP B  1 96  ? 11.727 -25.240  -43.317  1.00 47.55  ? 97  ASP B CG  1 
ATOM   1816  O  OD1 . ASP B  1 96  ? 11.766 -26.417  -42.877  1.00 47.56  ? 97  ASP B OD1 1 
ATOM   1817  O  OD2 . ASP B  1 96  ? 10.761 -24.821  -44.000  1.00 50.07  ? 97  ASP B OD2 1 
ATOM   1818  N  N   . VAL B  1 97  ? 15.445 -24.583  -40.348  1.00 37.85  ? 98  VAL B N   1 
ATOM   1819  C  CA  . VAL B  1 97  ? 16.775 -24.162  -39.928  1.00 36.26  ? 98  VAL B CA  1 
ATOM   1820  C  C   . VAL B  1 97  ? 17.829 -24.500  -40.937  1.00 37.33  ? 98  VAL B C   1 
ATOM   1821  O  O   . VAL B  1 97  ? 17.890 -25.618  -41.392  1.00 38.61  ? 98  VAL B O   1 
ATOM   1822  C  CB  . VAL B  1 97  ? 17.197 -24.848  -38.642  1.00 34.80  ? 98  VAL B CB  1 
ATOM   1823  C  CG1 . VAL B  1 97  ? 18.549 -24.352  -38.209  1.00 33.85  ? 98  VAL B CG1 1 
ATOM   1824  C  CG2 . VAL B  1 97  ? 16.214 -24.589  -37.559  1.00 34.51  ? 98  VAL B CG2 1 
ATOM   1825  N  N   . SER B  1 98  ? 18.667 -23.529  -41.276  1.00 37.43  ? 99  SER B N   1 
ATOM   1826  C  CA  . SER B  1 98  ? 19.850 -23.748  -42.127  1.00 38.79  ? 99  SER B CA  1 
ATOM   1827  C  C   . SER B  1 98  ? 20.927 -22.739  -41.768  1.00 38.12  ? 99  SER B C   1 
ATOM   1828  O  O   . SER B  1 98  ? 20.998 -21.671  -42.340  1.00 38.96  ? 99  SER B O   1 
ATOM   1829  C  CB  . SER B  1 98  ? 19.520 -23.661  -43.625  1.00 41.34  ? 99  SER B CB  1 
ATOM   1830  O  OG  . SER B  1 98  ? 20.675 -23.764  -44.444  1.00 42.67  ? 99  SER B OG  1 
ATOM   1831  N  N   . ILE B  1 99  ? 21.760 -23.107  -40.812  1.00 37.00  ? 100 ILE B N   1 
ATOM   1832  C  CA  . ILE B  1 99  ? 22.879 -22.297  -40.380  1.00 36.77  ? 100 ILE B CA  1 
ATOM   1833  C  C   . ILE B  1 99  ? 24.180 -22.954  -40.831  1.00 38.39  ? 100 ILE B C   1 
ATOM   1834  O  O   . ILE B  1 99  ? 24.189 -24.130  -41.144  1.00 39.30  ? 100 ILE B O   1 
ATOM   1835  C  CB  . ILE B  1 99  ? 22.864 -22.153  -38.856  1.00 34.80  ? 100 ILE B CB  1 
ATOM   1836  C  CG1 . ILE B  1 99  ? 21.638 -21.362  -38.425  1.00 33.77  ? 100 ILE B CG1 1 
ATOM   1837  C  CG2 . ILE B  1 99  ? 24.121 -21.481  -38.363  1.00 35.21  ? 100 ILE B CG2 1 
ATOM   1838  C  CD1 . ILE B  1 99  ? 21.753 -20.781  -37.048  1.00 32.50  ? 100 ILE B CD1 1 
ATOM   1839  N  N   . GLU B  1 100 ? 25.253 -22.174  -40.926  1.00 39.39  ? 101 GLU B N   1 
ATOM   1840  C  CA  . GLU B  1 100 ? 26.604 -22.695  -41.098  1.00 41.02  ? 101 GLU B CA  1 
ATOM   1841  C  C   . GLU B  1 100 ? 27.493 -21.903  -40.182  1.00 40.82  ? 101 GLU B C   1 
ATOM   1842  O  O   . GLU B  1 100 ? 27.506 -20.696  -40.254  1.00 41.24  ? 101 GLU B O   1 
ATOM   1843  C  CB  . GLU B  1 100 ? 27.071 -22.565  -42.544  1.00 43.91  ? 101 GLU B CB  1 
ATOM   1844  C  CG  . GLU B  1 100 ? 28.431 -23.194  -42.805  1.00 46.94  ? 101 GLU B CG  1 
ATOM   1845  C  CD  . GLU B  1 100 ? 28.785 -23.314  -44.292  1.00 50.77  ? 101 GLU B CD  1 
ATOM   1846  O  OE1 . GLU B  1 100 ? 29.811 -23.973  -44.604  1.00 52.99  ? 101 GLU B OE1 1 
ATOM   1847  O  OE2 . GLU B  1 100 ? 28.041 -22.762  -45.140  1.00 51.36  ? 101 GLU B OE2 1 
ATOM   1848  N  N   . ASP B  1 101 ? 28.230 -22.580  -39.311  1.00 40.83  ? 102 ASP B N   1 
ATOM   1849  C  CA  . ASP B  1 101 ? 29.018 -21.910  -38.258  1.00 40.86  ? 102 ASP B CA  1 
ATOM   1850  C  C   . ASP B  1 101 ? 30.428 -22.482  -38.091  1.00 43.06  ? 102 ASP B C   1 
ATOM   1851  O  O   . ASP B  1 101 ? 30.646 -23.687  -38.236  1.00 43.45  ? 102 ASP B O   1 
ATOM   1852  C  CB  . ASP B  1 101 ? 28.299 -21.992  -36.919  1.00 38.37  ? 102 ASP B CB  1 
ATOM   1853  C  CG  . ASP B  1 101 ? 28.837 -21.012  -35.914  1.00 38.40  ? 102 ASP B CG  1 
ATOM   1854  O  OD1 . ASP B  1 101 ? 28.673 -19.799  -36.134  1.00 38.37  ? 102 ASP B OD1 1 
ATOM   1855  O  OD2 . ASP B  1 101 ? 29.427 -21.448  -34.905  1.00 38.62  ? 102 ASP B OD2 1 
ATOM   1856  N  N   . SER B  1 102 ? 31.359 -21.592  -37.738  1.00 44.68  ? 103 SER B N   1 
ATOM   1857  C  CA  . SER B  1 102 ? 32.794 -21.897  -37.657  1.00 47.50  ? 103 SER B CA  1 
ATOM   1858  C  C   . SER B  1 102 ? 33.373 -21.911  -36.244  1.00 47.49  ? 103 SER B C   1 
ATOM   1859  O  O   . SER B  1 102 ? 34.472 -22.396  -36.058  1.00 50.00  ? 103 SER B O   1 
ATOM   1860  C  CB  . SER B  1 102 ? 33.569 -20.888  -38.482  1.00 50.35  ? 103 SER B CB  1 
ATOM   1861  O  OG  . SER B  1 102 ? 33.046 -20.849  -39.795  1.00 51.08  ? 103 SER B OG  1 
ATOM   1862  N  N   . VAL B  1 103 ? 32.651 -21.386  -35.259  1.00 45.18  ? 104 VAL B N   1 
ATOM   1863  C  CA  . VAL B  1 103 ? 33.121 -21.402  -33.886  1.00 45.46  ? 104 VAL B CA  1 
ATOM   1864  C  C   . VAL B  1 103 ? 32.830 -22.737  -33.236  1.00 44.50  ? 104 VAL B C   1 
ATOM   1865  O  O   . VAL B  1 103 ? 33.709 -23.314  -32.627  1.00 46.49  ? 104 VAL B O   1 
ATOM   1866  C  CB  . VAL B  1 103 ? 32.491 -20.322  -33.054  1.00 44.07  ? 104 VAL B CB  1 
ATOM   1867  C  CG1 . VAL B  1 103 ? 33.063 -20.358  -31.661  1.00 45.11  ? 104 VAL B CG1 1 
ATOM   1868  C  CG2 . VAL B  1 103 ? 32.758 -18.987  -33.665  1.00 45.79  ? 104 VAL B CG2 1 
ATOM   1869  N  N   . ILE B  1 104 ? 31.604 -23.238  -33.348  1.00 41.96  ? 105 ILE B N   1 
ATOM   1870  C  CA  . ILE B  1 104 ? 31.264 -24.541  -32.755  1.00 40.93  ? 105 ILE B CA  1 
ATOM   1871  C  C   . ILE B  1 104 ? 32.059 -25.625  -33.450  1.00 42.84  ? 105 ILE B C   1 
ATOM   1872  O  O   . ILE B  1 104 ? 32.593 -25.413  -34.533  1.00 44.35  ? 105 ILE B O   1 
ATOM   1873  C  CB  . ILE B  1 104 ? 29.750 -24.876  -32.835  1.00 38.28  ? 105 ILE B CB  1 
ATOM   1874  C  CG1 . ILE B  1 104 ? 29.268 -24.976  -34.290  1.00 38.30  ? 105 ILE B CG1 1 
ATOM   1875  C  CG2 . ILE B  1 104 ? 28.940 -23.863  -32.090  1.00 36.59  ? 105 ILE B CG2 1 
ATOM   1876  C  CD1 . ILE B  1 104 ? 27.947 -25.726  -34.445  1.00 36.28  ? 105 ILE B CD1 1 
ATOM   1877  N  N   . SER B  1 105 ? 32.140 -26.789  -32.825  1.00 43.14  ? 106 SER B N   1 
ATOM   1878  C  CA  . SER B  1 105 ? 32.760 -27.962  -33.467  1.00 45.10  ? 106 SER B CA  1 
ATOM   1879  C  C   . SER B  1 105 ? 32.263 -29.289  -32.918  1.00 44.36  ? 106 SER B C   1 
ATOM   1880  O  O   . SER B  1 105 ? 31.785 -29.366  -31.793  1.00 43.22  ? 106 SER B O   1 
ATOM   1881  C  CB  . SER B  1 105 ? 34.280 -27.917  -33.330  1.00 48.51  ? 106 SER B CB  1 
ATOM   1882  O  OG  . SER B  1 105 ? 34.892 -28.914  -34.133  1.00 50.44  ? 106 SER B OG  1 
ATOM   1883  N  N   . LEU B  1 106 ? 32.402 -30.330  -33.729  1.00 45.42  ? 107 LEU B N   1 
ATOM   1884  C  CA  . LEU B  1 106 ? 32.055 -31.688  -33.326  1.00 45.38  ? 107 LEU B CA  1 
ATOM   1885  C  C   . LEU B  1 106 ? 33.269 -32.461  -32.839  1.00 48.12  ? 107 LEU B C   1 
ATOM   1886  O  O   . LEU B  1 106 ? 33.244 -33.673  -32.779  1.00 48.94  ? 107 LEU B O   1 
ATOM   1887  C  CB  . LEU B  1 106 ? 31.405 -32.427  -34.491  1.00 45.32  ? 107 LEU B CB  1 
ATOM   1888  C  CG  . LEU B  1 106 ? 30.128 -31.785  -35.046  1.00 42.72  ? 107 LEU B CG  1 
ATOM   1889  C  CD1 . LEU B  1 106 ? 29.561 -32.614  -36.173  1.00 43.47  ? 107 LEU B CD1 1 
ATOM   1890  C  CD2 . LEU B  1 106 ? 29.096 -31.592  -33.965  1.00 40.16  ? 107 LEU B CD2 1 
ATOM   1891  N  N   . SER B  1 107 ? 34.330 -31.742  -32.497  1.00 50.03  ? 108 SER B N   1 
ATOM   1892  C  CA  . SER B  1 107 ? 35.582 -32.336  -31.988  1.00 53.16  ? 108 SER B CA  1 
ATOM   1893  C  C   . SER B  1 107 ? 36.498 -31.329  -31.261  1.00 54.73  ? 108 SER B C   1 
ATOM   1894  O  O   . SER B  1 107 ? 36.657 -30.181  -31.685  1.00 54.63  ? 108 SER B O   1 
ATOM   1895  C  CB  . SER B  1 107 ? 36.365 -33.011  -33.119  1.00 55.98  ? 108 SER B CB  1 
ATOM   1896  O  OG  . SER B  1 107 ? 36.673 -32.120  -34.169  1.00 56.56  ? 108 SER B OG  1 
ATOM   1897  N  N   . GLY B  1 108 ? 37.081 -31.767  -30.152  1.00 56.47  ? 109 GLY B N   1 
ATOM   1898  C  CA  . GLY B  1 108 ? 38.075 -30.969  -29.441  1.00 59.11  ? 109 GLY B CA  1 
ATOM   1899  C  C   . GLY B  1 108 ? 37.579 -30.046  -28.345  1.00 57.56  ? 109 GLY B C   1 
ATOM   1900  O  O   . GLY B  1 108 ? 36.595 -30.334  -27.683  1.00 55.19  ? 109 GLY B O   1 
ATOM   1901  N  N   . ASP B  1 109 ? 38.307 -28.949  -28.137  1.00 59.47  ? 110 ASP B N   1 
ATOM   1902  C  CA  . ASP B  1 109 ? 38.010 -27.963  -27.079  1.00 59.00  ? 110 ASP B CA  1 
ATOM   1903  C  C   . ASP B  1 109 ? 36.584 -27.400  -27.155  1.00 54.62  ? 110 ASP B C   1 
ATOM   1904  O  O   . ASP B  1 109 ? 35.886 -27.233  -26.146  1.00 52.95  ? 110 ASP B O   1 
ATOM   1905  C  CB  . ASP B  1 109 ? 39.017 -26.800  -27.180  1.00 62.07  ? 110 ASP B CB  1 
ATOM   1906  C  CG  . ASP B  1 109 ? 39.281 -26.102  -25.820  1.00 64.31  ? 110 ASP B CG  1 
ATOM   1907  O  OD1 . ASP B  1 109 ? 38.545 -25.117  -25.460  1.00 62.31  ? 110 ASP B OD1 1 
ATOM   1908  O  OD2 . ASP B  1 109 ? 40.250 -26.540  -25.126  1.00 68.18  ? 110 ASP B OD2 1 
ATOM   1909  N  N   . HIS B  1 110 ? 36.190 -27.108  -28.383  1.00 52.97  ? 111 HIS B N   1 
ATOM   1910  C  CA  . HIS B  1 110 ? 34.896 -26.541  -28.707  1.00 49.61  ? 111 HIS B CA  1 
ATOM   1911  C  C   . HIS B  1 110 ? 33.796 -27.603  -28.933  1.00 47.16  ? 111 HIS B C   1 
ATOM   1912  O  O   . HIS B  1 110 ? 32.710 -27.287  -29.401  1.00 44.65  ? 111 HIS B O   1 
ATOM   1913  C  CB  . HIS B  1 110 ? 35.044 -25.712  -29.988  1.00 49.74  ? 111 HIS B CB  1 
ATOM   1914  C  CG  . HIS B  1 110 ? 35.874 -24.468  -29.834  1.00 52.05  ? 111 HIS B CG  1 
ATOM   1915  N  ND1 . HIS B  1 110 ? 35.907 -23.475  -30.793  1.00 52.11  ? 111 HIS B ND1 1 
ATOM   1916  C  CD2 . HIS B  1 110 ? 36.658 -24.032  -28.822  1.00 54.51  ? 111 HIS B CD2 1 
ATOM   1917  C  CE1 . HIS B  1 110 ? 36.681 -22.488  -30.382  1.00 54.41  ? 111 HIS B CE1 1 
ATOM   1918  N  NE2 . HIS B  1 110 ? 37.147 -22.799  -29.186  1.00 56.11  ? 111 HIS B NE2 1 
ATOM   1919  N  N   . CYS B  1 111 ? 34.081 -28.858  -28.602  1.00 48.22  ? 112 CYS B N   1 
ATOM   1920  C  CA  . CYS B  1 111 ? 33.175 -29.975  -28.894  1.00 46.40  ? 112 CYS B CA  1 
ATOM   1921  C  C   . CYS B  1 111 ? 31.821 -29.764  -28.247  1.00 43.77  ? 112 CYS B C   1 
ATOM   1922  O  O   . CYS B  1 111 ? 31.723 -29.673  -27.028  1.00 44.07  ? 112 CYS B O   1 
ATOM   1923  C  CB  . CYS B  1 111 ? 33.771 -31.291  -28.403  1.00 48.49  ? 112 CYS B CB  1 
ATOM   1924  S  SG  . CYS B  1 111 ? 32.855 -32.743  -28.885  1.00 47.17  ? 112 CYS B SG  1 
ATOM   1925  N  N   . ILE B  1 112 ? 30.783 -29.674  -29.073  1.00 41.59  ? 113 ILE B N   1 
ATOM   1926  C  CA  . ILE B  1 112 ? 29.411 -29.502  -28.590  1.00 39.40  ? 113 ILE B CA  1 
ATOM   1927  C  C   . ILE B  1 112 ? 28.710 -30.820  -28.336  1.00 39.17  ? 113 ILE B C   1 
ATOM   1928  O  O   . ILE B  1 112 ? 27.653 -30.839  -27.751  1.00 38.17  ? 113 ILE B O   1 
ATOM   1929  C  CB  . ILE B  1 112 ? 28.546 -28.660  -29.551  1.00 37.57  ? 113 ILE B CB  1 
ATOM   1930  C  CG1 . ILE B  1 112 ? 28.471 -29.278  -30.951  1.00 37.54  ? 113 ILE B CG1 1 
ATOM   1931  C  CG2 . ILE B  1 112 ? 29.086 -27.268  -29.636  1.00 38.05  ? 113 ILE B CG2 1 
ATOM   1932  C  CD1 . ILE B  1 112 ? 27.275 -28.803  -31.751  1.00 35.91  ? 113 ILE B CD1 1 
ATOM   1933  N  N   . ILE B  1 113 ? 29.294 -31.920  -28.784  1.00 40.55  ? 114 ILE B N   1 
ATOM   1934  C  CA  . ILE B  1 113 ? 28.669 -33.235  -28.644  1.00 40.62  ? 114 ILE B CA  1 
ATOM   1935  C  C   . ILE B  1 113 ? 28.551 -33.580  -27.180  1.00 41.20  ? 114 ILE B C   1 
ATOM   1936  O  O   . ILE B  1 113 ? 29.493 -33.380  -26.430  1.00 42.72  ? 114 ILE B O   1 
ATOM   1937  C  CB  . ILE B  1 113 ? 29.465 -34.344  -29.367  1.00 42.47  ? 114 ILE B CB  1 
ATOM   1938  C  CG1 . ILE B  1 113 ? 29.278 -34.211  -30.880  1.00 42.20  ? 114 ILE B CG1 1 
ATOM   1939  C  CG2 . ILE B  1 113 ? 29.016 -35.729  -28.918  1.00 43.00  ? 114 ILE B CG2 1 
ATOM   1940  C  CD1 . ILE B  1 113 ? 30.177 -35.135  -31.714  1.00 44.73  ? 114 ILE B CD1 1 
ATOM   1941  N  N   . GLY B  1 114 ? 27.387 -34.086  -26.790  1.00 40.36  ? 115 GLY B N   1 
ATOM   1942  C  CA  . GLY B  1 114 ? 27.101 -34.428  -25.411  1.00 41.15  ? 115 GLY B CA  1 
ATOM   1943  C  C   . GLY B  1 114 ? 26.558 -33.253  -24.649  1.00 40.24  ? 115 GLY B C   1 
ATOM   1944  O  O   . GLY B  1 114 ? 26.343 -33.341  -23.475  1.00 41.22  ? 115 GLY B O   1 
ATOM   1945  N  N   . ARG B  1 115 ? 26.351 -32.140  -25.324  1.00 38.81  ? 116 ARG B N   1 
ATOM   1946  C  CA  . ARG B  1 115 ? 25.766 -30.949  -24.711  1.00 38.25  ? 116 ARG B CA  1 
ATOM   1947  C  C   . ARG B  1 115 ? 24.371 -30.678  -25.283  1.00 36.66  ? 116 ARG B C   1 
ATOM   1948  O  O   . ARG B  1 115 ? 23.950 -31.315  -26.241  1.00 36.15  ? 116 ARG B O   1 
ATOM   1949  C  CB  . ARG B  1 115 ? 26.671 -29.742  -24.932  1.00 38.22  ? 116 ARG B CB  1 
ATOM   1950  C  CG  . ARG B  1 115 ? 28.083 -29.972  -24.451  1.00 40.49  ? 116 ARG B CG  1 
ATOM   1951  C  CD  . ARG B  1 115 ? 28.954 -28.733  -24.558  1.00 41.24  ? 116 ARG B CD  1 
ATOM   1952  N  NE  . ARG B  1 115 ? 30.361 -29.027  -24.258  1.00 43.52  ? 116 ARG B NE  1 
ATOM   1953  C  CZ  . ARG B  1 115 ? 30.898 -29.062  -23.042  1.00 45.56  ? 116 ARG B CZ  1 
ATOM   1954  N  NH1 . ARG B  1 115 ? 30.168 -28.812  -21.953  1.00 45.55  ? 116 ARG B NH1 1 
ATOM   1955  N  NH2 . ARG B  1 115 ? 32.187 -29.344  -22.919  1.00 48.32  ? 116 ARG B NH2 1 
ATOM   1956  N  N   . THR B  1 116 ? 23.664 -29.718  -24.701  1.00 36.24  ? 117 THR B N   1 
ATOM   1957  C  CA  . THR B  1 116 ? 22.259 -29.458  -25.038  1.00 35.22  ? 117 THR B CA  1 
ATOM   1958  C  C   . THR B  1 116 ? 22.056 -28.322  -26.037  1.00 33.83  ? 117 THR B C   1 
ATOM   1959  O  O   . THR B  1 116 ? 22.583 -27.238  -25.863  1.00 33.82  ? 117 THR B O   1 
ATOM   1960  C  CB  . THR B  1 116 ? 21.439 -29.107  -23.774  1.00 36.12  ? 117 THR B CB  1 
ATOM   1961  O  OG1 . THR B  1 116 ? 21.396 -30.219  -22.871  1.00 37.55  ? 117 THR B OG1 1 
ATOM   1962  C  CG2 . THR B  1 116 ? 20.038 -28.733  -24.135  1.00 35.55  ? 117 THR B CG2 1 
ATOM   1963  N  N   . LEU B  1 117 ? 21.276 -28.590  -27.078  1.00 33.18  ? 118 LEU B N   1 
ATOM   1964  C  CA  . LEU B  1 117 ? 20.756 -27.560  -27.989  1.00 32.10  ? 118 LEU B CA  1 
ATOM   1965  C  C   . LEU B  1 117 ? 19.423 -27.063  -27.448  1.00 32.20  ? 118 LEU B C   1 
ATOM   1966  O  O   . LEU B  1 117 ? 18.686 -27.826  -26.873  1.00 33.23  ? 118 LEU B O   1 
ATOM   1967  C  CB  . LEU B  1 117 ? 20.535 -28.129  -29.388  1.00 31.78  ? 118 LEU B CB  1 
ATOM   1968  C  CG  . LEU B  1 117 ? 20.110 -27.138  -30.472  1.00 30.93  ? 118 LEU B CG  1 
ATOM   1969  C  CD1 . LEU B  1 117 ? 21.151 -26.101  -30.643  1.00 30.79  ? 118 LEU B CD1 1 
ATOM   1970  C  CD2 . LEU B  1 117 ? 19.873 -27.800  -31.794  1.00 31.09  ? 118 LEU B CD2 1 
ATOM   1971  N  N   . VAL B  1 118 ? 19.111 -25.787  -27.642  1.00 31.66  ? 119 VAL B N   1 
ATOM   1972  C  CA  . VAL B  1 118 ? 17.937 -25.162  -27.007  1.00 32.14  ? 119 VAL B CA  1 
ATOM   1973  C  C   . VAL B  1 118 ? 17.310 -24.070  -27.847  1.00 31.64  ? 119 VAL B C   1 
ATOM   1974  O  O   . VAL B  1 118 ? 17.955 -23.133  -28.212  1.00 31.31  ? 119 VAL B O   1 
ATOM   1975  C  CB  . VAL B  1 118 ? 18.309 -24.520  -25.670  1.00 32.90  ? 119 VAL B CB  1 
ATOM   1976  C  CG1 . VAL B  1 118 ? 17.205 -23.655  -25.189  1.00 33.77  ? 119 VAL B CG1 1 
ATOM   1977  C  CG2 . VAL B  1 118 ? 18.622 -25.568  -24.639  1.00 34.15  ? 119 VAL B CG2 1 
ATOM   1978  N  N   . VAL B  1 119 ? 16.041 -24.198  -28.161  1.00 32.26  ? 120 VAL B N   1 
ATOM   1979  C  CA  . VAL B  1 119 ? 15.333 -23.172  -28.909  1.00 32.31  ? 120 VAL B CA  1 
ATOM   1980  C  C   . VAL B  1 119 ? 14.556 -22.375  -27.900  1.00 33.49  ? 120 VAL B C   1 
ATOM   1981  O  O   . VAL B  1 119 ? 14.142 -22.912  -26.904  1.00 34.70  ? 120 VAL B O   1 
ATOM   1982  C  CB  . VAL B  1 119 ? 14.410 -23.767  -29.985  1.00 32.83  ? 120 VAL B CB  1 
ATOM   1983  C  CG1 . VAL B  1 119 ? 13.209 -24.422  -29.374  1.00 34.73  ? 120 VAL B CG1 1 
ATOM   1984  C  CG2 . VAL B  1 119 ? 13.985 -22.706  -30.956  1.00 32.92  ? 120 VAL B CG2 1 
ATOM   1985  N  N   . HIS B  1 120 ? 14.358 -21.091  -28.156  1.00 33.69  ? 121 HIS B N   1 
ATOM   1986  C  CA  . HIS B  1 120 ? 13.937 -20.143  -27.117  1.00 34.82  ? 121 HIS B CA  1 
ATOM   1987  C  C   . HIS B  1 120 ? 12.632 -19.421  -27.366  1.00 36.21  ? 121 HIS B C   1 
ATOM   1988  O  O   . HIS B  1 120 ? 12.179 -19.299  -28.486  1.00 36.09  ? 121 HIS B O   1 
ATOM   1989  C  CB  . HIS B  1 120 ? 15.033 -19.098  -26.927  1.00 34.29  ? 121 HIS B CB  1 
ATOM   1990  C  CG  . HIS B  1 120 ? 16.075 -19.497  -25.937  1.00 33.97  ? 121 HIS B CG  1 
ATOM   1991  N  ND1 . HIS B  1 120 ? 16.170 -18.925  -24.690  1.00 35.65  ? 121 HIS B ND1 1 
ATOM   1992  C  CD2 . HIS B  1 120 ? 17.054 -20.420  -26.000  1.00 33.02  ? 121 HIS B CD2 1 
ATOM   1993  C  CE1 . HIS B  1 120 ? 17.161 -19.483  -24.025  1.00 35.52  ? 121 HIS B CE1 1 
ATOM   1994  N  NE2 . HIS B  1 120 ? 17.713 -20.396  -24.798  1.00 33.97  ? 121 HIS B NE2 1 
ATOM   1995  N  N   . GLU B  1 121 ? 12.072 -18.890  -26.290  1.00 37.97  ? 122 GLU B N   1 
ATOM   1996  C  CA  . GLU B  1 121 ? 10.783 -18.189  -26.302  1.00 40.04  ? 122 GLU B CA  1 
ATOM   1997  C  C   . GLU B  1 121 ? 10.798 -16.996  -27.229  1.00 39.53  ? 122 GLU B C   1 
ATOM   1998  O  O   . GLU B  1 121 ? 10.076 -16.972  -28.190  1.00 39.93  ? 122 GLU B O   1 
ATOM   1999  C  CB  . GLU B  1 121 ? 10.425 -17.725  -24.879  1.00 42.37  ? 122 GLU B CB  1 
ATOM   2000  C  CG  . GLU B  1 121 ? 9.151  -16.871  -24.751  1.00 45.03  ? 122 GLU B CG  1 
ATOM   2001  C  CD  . GLU B  1 121 ? 8.966  -16.252  -23.370  1.00 47.58  ? 122 GLU B CD  1 
ATOM   2002  O  OE1 . GLU B  1 121 ? 9.846  -16.362  -22.497  1.00 47.28  ? 122 GLU B OE1 1 
ATOM   2003  O  OE2 . GLU B  1 121 ? 7.918  -15.638  -23.164  1.00 50.21  ? 122 GLU B OE2 1 
ATOM   2004  N  N   . LYS B  1 122 ? 11.624 -16.011  -26.901  1.00 39.23  ? 123 LYS B N   1 
ATOM   2005  C  CA  . LYS B  1 122 ? 11.749 -14.750  -27.638  1.00 39.18  ? 123 LYS B CA  1 
ATOM   2006  C  C   . LYS B  1 122 ? 12.965 -14.791  -28.555  1.00 37.07  ? 123 LYS B C   1 
ATOM   2007  O  O   . LYS B  1 122 ? 13.700 -15.762  -28.578  1.00 35.88  ? 123 LYS B O   1 
ATOM   2008  C  CB  . LYS B  1 122 ? 11.936 -13.555  -26.678  1.00 40.55  ? 123 LYS B CB  1 
ATOM   2009  C  CG  . LYS B  1 122 ? 10.948 -13.430  -25.531  1.00 43.37  ? 123 LYS B CG  1 
ATOM   2010  C  CD  . LYS B  1 122 ? 11.267 -12.221  -24.629  1.00 45.08  ? 123 LYS B CD  1 
ATOM   2011  C  CE  . LYS B  1 122 ? 10.426 -12.226  -23.339  1.00 48.13  ? 123 LYS B CE  1 
ATOM   2012  N  NZ  . LYS B  1 122 ? 10.532 -10.934  -22.606  1.00 50.03  ? 123 LYS B NZ  1 
ATOM   2013  N  N   . ALA B  1 123 ? 13.191 -13.706  -29.283  1.00 36.98  ? 124 ALA B N   1 
ATOM   2014  C  CA  . ALA B  1 123 ? 14.340 -13.585  -30.158  1.00 35.44  ? 124 ALA B CA  1 
ATOM   2015  C  C   . ALA B  1 123 ? 15.568 -13.182  -29.390  1.00 35.17  ? 124 ALA B C   1 
ATOM   2016  O  O   . ALA B  1 123 ? 15.472 -12.415  -28.462  1.00 36.26  ? 124 ALA B O   1 
ATOM   2017  C  CB  . ALA B  1 123 ? 14.066 -12.562  -31.215  1.00 36.12  ? 124 ALA B CB  1 
ATOM   2018  N  N   . ASP B  1 124 ? 16.725 -13.686  -29.811  1.00 34.19  ? 125 ASP B N   1 
ATOM   2019  C  CA  . ASP B  1 124 ? 18.046 -13.316  -29.248  1.00 34.29  ? 125 ASP B CA  1 
ATOM   2020  C  C   . ASP B  1 124 ? 18.463 -11.953  -29.787  1.00 35.20  ? 125 ASP B C   1 
ATOM   2021  O  O   . ASP B  1 124 ? 18.568 -11.780  -30.995  1.00 35.09  ? 125 ASP B O   1 
ATOM   2022  C  CB  . ASP B  1 124 ? 19.099 -14.368  -29.627  1.00 33.21  ? 125 ASP B CB  1 
ATOM   2023  C  CG  . ASP B  1 124 ? 20.467 -14.112  -29.007  1.00 33.84  ? 125 ASP B CG  1 
ATOM   2024  O  OD1 . ASP B  1 124 ? 20.642 -13.072  -28.346  1.00 35.03  ? 125 ASP B OD1 1 
ATOM   2025  O  OD2 . ASP B  1 124 ? 21.382 -14.959  -29.200  1.00 33.27  ? 125 ASP B OD2 1 
ATOM   2026  N  N   . ASP B  1 125 ? 18.705 -10.989  -28.901  1.00 36.51  ? 126 ASP B N   1 
ATOM   2027  C  CA  . ASP B  1 125 ? 19.032 -9.609   -29.311  1.00 37.62  ? 126 ASP B CA  1 
ATOM   2028  C  C   . ASP B  1 125 ? 20.490 -9.467   -29.756  1.00 37.78  ? 126 ASP B C   1 
ATOM   2029  O  O   . ASP B  1 125 ? 20.947 -8.366   -30.010  1.00 39.13  ? 126 ASP B O   1 
ATOM   2030  C  CB  . ASP B  1 125 ? 18.668 -8.585   -28.208  1.00 39.42  ? 126 ASP B CB  1 
ATOM   2031  C  CG  . ASP B  1 125 ? 19.631 -8.581   -27.026  1.00 40.20  ? 126 ASP B CG  1 
ATOM   2032  O  OD1 . ASP B  1 125 ? 20.794 -8.945   -27.178  1.00 40.01  ? 126 ASP B OD1 1 
ATOM   2033  O  OD2 . ASP B  1 125 ? 19.230 -8.175   -25.930  1.00 41.23  ? 126 ASP B OD2 1 
ATOM   2034  N  N   . LEU B  1 126 ? 21.206 -10.587  -29.833  1.00 36.72  ? 127 LEU B N   1 
ATOM   2035  C  CA  . LEU B  1 126 ? 22.600 -10.648  -30.292  1.00 37.17  ? 127 LEU B CA  1 
ATOM   2036  C  C   . LEU B  1 126 ? 23.559 -9.776   -29.493  1.00 39.19  ? 127 LEU B C   1 
ATOM   2037  O  O   . LEU B  1 126 ? 24.571 -9.323   -30.003  1.00 40.64  ? 127 LEU B O   1 
ATOM   2038  C  CB  . LEU B  1 126 ? 22.698 -10.325  -31.787  1.00 37.17  ? 127 LEU B CB  1 
ATOM   2039  C  CG  . LEU B  1 126 ? 21.743 -11.078  -32.716  1.00 35.90  ? 127 LEU B CG  1 
ATOM   2040  C  CD1 . LEU B  1 126 ? 22.106 -10.831  -34.177  1.00 36.84  ? 127 LEU B CD1 1 
ATOM   2041  C  CD2 . LEU B  1 126 ? 21.719 -12.556  -32.446  1.00 34.61  ? 127 LEU B CD2 1 
ATOM   2042  N  N   . GLY B  1 127 ? 23.235 -9.546   -28.233  1.00 39.97  ? 128 GLY B N   1 
ATOM   2043  C  CA  . GLY B  1 127 ? 24.088 -8.771   -27.332  1.00 42.26  ? 128 GLY B CA  1 
ATOM   2044  C  C   . GLY B  1 127 ? 23.969 -7.261   -27.450  1.00 44.07  ? 128 GLY B C   1 
ATOM   2045  O  O   . GLY B  1 127 ? 24.550 -6.533   -26.657  1.00 46.30  ? 128 GLY B O   1 
ATOM   2046  N  N   . LYS B  1 128 ? 23.190 -6.782   -28.412  1.00 43.37  ? 129 LYS B N   1 
ATOM   2047  C  CA  . LYS B  1 128 ? 23.080 -5.347   -28.669  1.00 45.29  ? 129 LYS B CA  1 
ATOM   2048  C  C   . LYS B  1 128 ? 21.915 -4.715   -27.906  1.00 46.04  ? 129 LYS B C   1 
ATOM   2049  O  O   . LYS B  1 128 ? 21.363 -3.692   -28.326  1.00 46.99  ? 129 LYS B O   1 
ATOM   2050  C  CB  . LYS B  1 128 ? 22.900 -5.077   -30.164  1.00 44.82  ? 129 LYS B CB  1 
ATOM   2051  C  CG  . LYS B  1 128 ? 23.907 -5.747   -31.066  1.00 44.64  ? 129 LYS B CG  1 
ATOM   2052  C  CD  . LYS B  1 128 ? 23.952 -5.096   -32.453  1.00 45.75  ? 129 LYS B CD  1 
ATOM   2053  C  CE  . LYS B  1 128 ? 24.876 -5.898   -33.404  1.00 45.98  ? 129 LYS B CE  1 
ATOM   2054  N  NZ  . LYS B  1 128 ? 25.245 -5.137   -34.660  1.00 47.83  ? 129 LYS B NZ  1 
ATOM   2055  N  N   . GLY B  1 129 ? 21.550 -5.309   -26.778  1.00 46.02  ? 130 GLY B N   1 
ATOM   2056  C  CA  . GLY B  1 129 ? 20.344 -4.907   -26.039  1.00 46.84  ? 130 GLY B CA  1 
ATOM   2057  C  C   . GLY B  1 129 ? 20.529 -3.715   -25.129  1.00 49.71  ? 130 GLY B C   1 
ATOM   2058  O  O   . GLY B  1 129 ? 19.577 -2.993   -24.844  1.00 50.82  ? 130 GLY B O   1 
ATOM   2059  N  N   . GLY B  1 130 ? 21.756 -3.526   -24.653  1.00 51.20  ? 131 GLY B N   1 
ATOM   2060  C  CA  . GLY B  1 130 ? 22.085 -2.381   -23.794  1.00 54.70  ? 131 GLY B CA  1 
ATOM   2061  C  C   . GLY B  1 130 ? 21.938 -2.637   -22.300  1.00 56.43  ? 131 GLY B C   1 
ATOM   2062  O  O   . GLY B  1 130 ? 22.577 -1.997   -21.477  1.00 59.39  ? 131 GLY B O   1 
ATOM   2063  N  N   . ASN B  1 131 ? 21.078 -3.574   -21.945  1.00 55.07  ? 132 ASN B N   1 
ATOM   2064  C  CA  . ASN B  1 131 ? 20.918 -3.963   -20.551  1.00 56.88  ? 132 ASN B CA  1 
ATOM   2065  C  C   . ASN B  1 131 ? 21.946 -5.012   -20.113  1.00 56.37  ? 132 ASN B C   1 
ATOM   2066  O  O   . ASN B  1 131 ? 22.713 -5.533   -20.920  1.00 54.29  ? 132 ASN B O   1 
ATOM   2067  C  CB  . ASN B  1 131 ? 19.470 -4.431   -20.268  1.00 56.35  ? 132 ASN B CB  1 
ATOM   2068  C  CG  . ASN B  1 131 ? 19.184 -5.844   -20.766  1.00 53.20  ? 132 ASN B CG  1 
ATOM   2069  O  OD1 . ASN B  1 131 ? 20.042 -6.521   -21.350  1.00 51.10  ? 132 ASN B OD1 1 
ATOM   2070  N  ND2 . ASN B  1 131 ? 17.963 -6.294   -20.532  1.00 53.25  ? 132 ASN B ND2 1 
ATOM   2071  N  N   . GLU B  1 132 ? 21.935 -5.305   -18.820  1.00 58.54  ? 133 GLU B N   1 
ATOM   2072  C  CA  . GLU B  1 132 ? 22.842 -6.264   -18.229  1.00 58.94  ? 133 GLU B CA  1 
ATOM   2073  C  C   . GLU B  1 132 ? 22.652 -7.650   -18.806  1.00 55.49  ? 133 GLU B C   1 
ATOM   2074  O  O   . GLU B  1 132 ? 23.631 -8.313   -19.158  1.00 54.46  ? 133 GLU B O   1 
ATOM   2075  C  CB  . GLU B  1 132 ? 22.602 -6.323   -16.717  1.00 62.52  ? 133 GLU B CB  1 
ATOM   2076  C  CG  . GLU B  1 132 ? 23.237 -7.549   -15.977  1.00 63.50  ? 133 GLU B CG  1 
ATOM   2077  C  CD  . GLU B  1 132 ? 24.736 -7.396   -15.671  1.00 66.12  ? 133 GLU B CD  1 
ATOM   2078  O  OE1 . GLU B  1 132 ? 25.359 -6.365   -16.050  1.00 67.56  ? 133 GLU B OE1 1 
ATOM   2079  O  OE2 . GLU B  1 132 ? 25.282 -8.333   -15.042  1.00 66.88  ? 133 GLU B OE2 1 
ATOM   2080  N  N   . GLU B  1 133 ? 21.391 -8.090   -18.857  1.00 54.08  ? 134 GLU B N   1 
ATOM   2081  C  CA  . GLU B  1 133 ? 21.032 -9.463   -19.236  1.00 51.31  ? 134 GLU B CA  1 
ATOM   2082  C  C   . GLU B  1 133 ? 21.379 -9.769   -20.695  1.00 48.07  ? 134 GLU B C   1 
ATOM   2083  O  O   . GLU B  1 133 ? 21.734 -10.885  -21.033  1.00 46.29  ? 134 GLU B O   1 
ATOM   2084  C  CB  . GLU B  1 133 ? 19.543 -9.717   -18.948  1.00 51.44  ? 134 GLU B CB  1 
ATOM   2085  C  CG  . GLU B  1 133 ? 19.118 -11.186  -18.900  1.00 50.05  ? 134 GLU B CG  1 
ATOM   2086  C  CD  . GLU B  1 133 ? 19.688 -11.933  -17.697  1.00 52.33  ? 134 GLU B CD  1 
ATOM   2087  O  OE1 . GLU B  1 133 ? 20.198 -11.287  -16.754  1.00 55.51  ? 134 GLU B OE1 1 
ATOM   2088  O  OE2 . GLU B  1 133 ? 19.647 -13.183  -17.698  1.00 51.09  ? 134 GLU B OE2 1 
ATOM   2089  N  N   . SER B  1 134 ? 21.329 -8.761   -21.552  1.00 47.78  ? 135 SER B N   1 
ATOM   2090  C  CA  . SER B  1 134 ? 21.627 -8.954   -22.974  1.00 45.35  ? 135 SER B CA  1 
ATOM   2091  C  C   . SER B  1 134 ? 23.028 -9.451   -23.197  1.00 45.09  ? 135 SER B C   1 
ATOM   2092  O  O   . SER B  1 134 ? 23.296 -10.094  -24.174  1.00 43.21  ? 135 SER B O   1 
ATOM   2093  C  CB  . SER B  1 134 ? 21.445 -7.668   -23.759  1.00 45.79  ? 135 SER B CB  1 
ATOM   2094  O  OG  . SER B  1 134 ? 21.898 -7.854   -25.077  1.00 43.78  ? 135 SER B OG  1 
ATOM   2095  N  N   . THR B  1 135 ? 23.920 -9.113   -22.289  1.00 47.62  ? 136 THR B N   1 
ATOM   2096  C  CA  . THR B  1 135 ? 25.304 -9.575   -22.316  1.00 48.32  ? 136 THR B CA  1 
ATOM   2097  C  C   . THR B  1 135 ? 25.481 -11.019  -21.865  1.00 47.55  ? 136 THR B C   1 
ATOM   2098  O  O   . THR B  1 135 ? 26.563 -11.585  -21.999  1.00 47.97  ? 136 THR B O   1 
ATOM   2099  C  CB  . THR B  1 135 ? 26.146 -8.679   -21.439  1.00 51.78  ? 136 THR B CB  1 
ATOM   2100  O  OG1 . THR B  1 135 ? 26.425 -7.492   -22.171  1.00 52.59  ? 136 THR B OG1 1 
ATOM   2101  C  CG2 . THR B  1 135 ? 27.439 -9.341   -21.034  1.00 53.19  ? 136 THR B CG2 1 
ATOM   2102  N  N   . LYS B  1 136 ? 24.415 -11.616  -21.351  1.00 46.74  ? 137 LYS B N   1 
ATOM   2103  C  CA  . LYS B  1 136 ? 24.461 -12.984  -20.847  1.00 46.31  ? 137 LYS B CA  1 
ATOM   2104  C  C   . LYS B  1 136 ? 23.588 -13.947  -21.670  1.00 43.23  ? 137 LYS B C   1 
ATOM   2105  O  O   . LYS B  1 136 ? 24.083 -14.853  -22.329  1.00 41.86  ? 137 LYS B O   1 
ATOM   2106  C  CB  . LYS B  1 136 ? 23.984 -13.013  -19.395  1.00 48.72  ? 137 LYS B CB  1 
ATOM   2107  C  CG  . LYS B  1 136 ? 24.954 -12.458  -18.359  1.00 52.42  ? 137 LYS B CG  1 
ATOM   2108  C  CD  . LYS B  1 136 ? 24.319 -12.565  -16.949  1.00 55.35  ? 137 LYS B CD  1 
ATOM   2109  C  CE  . LYS B  1 136 ? 25.355 -12.548  -15.818  1.00 58.94  ? 137 LYS B CE  1 
ATOM   2110  N  NZ  . LYS B  1 136 ? 25.650 -11.159  -15.346  1.00 62.20  ? 137 LYS B NZ  1 
ATOM   2111  N  N   . THR B  1 137 ? 22.285 -13.738  -21.620  1.00 42.59  ? 138 THR B N   1 
ATOM   2112  C  CA  . THR B  1 137 ? 21.332 -14.678  -22.184  1.00 40.61  ? 138 THR B CA  1 
ATOM   2113  C  C   . THR B  1 137 ? 20.856 -14.272  -23.561  1.00 38.84  ? 138 THR B C   1 
ATOM   2114  O  O   . THR B  1 137 ? 20.271 -15.093  -24.270  1.00 37.20  ? 138 THR B O   1 
ATOM   2115  C  CB  . THR B  1 137 ? 20.111 -14.832  -21.261  1.00 41.80  ? 138 THR B CB  1 
ATOM   2116  O  OG1 . THR B  1 137 ? 19.289 -13.662  -21.297  1.00 42.81  ? 138 THR B OG1 1 
ATOM   2117  C  CG2 . THR B  1 137 ? 20.567 -15.053  -19.846  1.00 44.38  ? 138 THR B CG2 1 
ATOM   2118  N  N   . GLY B  1 138 ? 21.098 -13.008  -23.912  1.00 39.45  ? 139 GLY B N   1 
ATOM   2119  C  CA  . GLY B  1 138 ? 20.605 -12.407  -25.140  1.00 38.38  ? 139 GLY B CA  1 
ATOM   2120  C  C   . GLY B  1 138 ? 19.176 -11.909  -25.024  1.00 38.83  ? 139 GLY B C   1 
ATOM   2121  O  O   . GLY B  1 138 ? 18.583 -11.541  -26.017  1.00 38.28  ? 139 GLY B O   1 
ATOM   2122  N  N   . ASN B  1 139 ? 18.623 -11.897  -23.819  1.00 40.34  ? 140 ASN B N   1 
ATOM   2123  C  CA  . ASN B  1 139 ? 17.218 -11.542  -23.583  1.00 41.48  ? 140 ASN B CA  1 
ATOM   2124  C  C   . ASN B  1 139 ? 16.228 -12.374  -24.399  1.00 40.11  ? 140 ASN B C   1 
ATOM   2125  O  O   . ASN B  1 139 ? 15.116 -11.927  -24.679  1.00 40.85  ? 140 ASN B O   1 
ATOM   2126  C  CB  . ASN B  1 139 ? 16.962 -10.042  -23.841  1.00 42.89  ? 140 ASN B CB  1 
ATOM   2127  C  CG  . ASN B  1 139 ? 17.392 -9.153   -22.695  1.00 45.25  ? 140 ASN B CG  1 
ATOM   2128  O  OD1 . ASN B  1 139 ? 17.719 -7.990   -22.902  1.00 46.26  ? 140 ASN B OD1 1 
ATOM   2129  N  ND2 . ASN B  1 139 ? 17.379 -9.687   -21.485  1.00 46.32  ? 140 ASN B ND2 1 
ATOM   2130  N  N   . ALA B  1 140 ? 16.626 -13.592  -24.751  1.00 38.55  ? 141 ALA B N   1 
ATOM   2131  C  CA  . ALA B  1 140 ? 15.830 -14.463  -25.619  1.00 37.38  ? 141 ALA B CA  1 
ATOM   2132  C  C   . ALA B  1 140 ? 14.777 -15.245  -24.867  1.00 38.44  ? 141 ALA B C   1 
ATOM   2133  O  O   . ALA B  1 140 ? 14.016 -15.971  -25.471  1.00 38.03  ? 141 ALA B O   1 
ATOM   2134  C  CB  . ALA B  1 140 ? 16.719 -15.406  -26.351  1.00 35.58  ? 141 ALA B CB  1 
ATOM   2135  N  N   . GLY B  1 141 ? 14.740 -15.111  -23.551  1.00 40.30  ? 142 GLY B N   1 
ATOM   2136  C  CA  . GLY B  1 141 ? 13.629 -15.629  -22.752  1.00 42.12  ? 142 GLY B CA  1 
ATOM   2137  C  C   . GLY B  1 141 ? 13.703 -17.112  -22.434  1.00 41.77  ? 142 GLY B C   1 
ATOM   2138  O  O   . GLY B  1 141 ? 14.773 -17.721  -22.480  1.00 40.37  ? 142 GLY B O   1 
ATOM   2139  N  N   . SER B  1 142 ? 12.544 -17.686  -22.110  1.00 43.40  ? 143 SER B N   1 
ATOM   2140  C  CA  . SER B  1 142 ? 12.447 -19.051  -21.567  1.00 43.86  ? 143 SER B CA  1 
ATOM   2141  C  C   . SER B  1 142 ? 12.838 -20.114  -22.582  1.00 41.56  ? 143 SER B C   1 
ATOM   2142  O  O   . SER B  1 142 ? 12.987 -19.833  -23.772  1.00 39.92  ? 143 SER B O   1 
ATOM   2143  C  CB  . SER B  1 142 ? 11.037 -19.333  -21.035  1.00 46.57  ? 143 SER B CB  1 
ATOM   2144  O  OG  . SER B  1 142 ? 10.120 -19.529  -22.081  1.00 46.20  ? 143 SER B OG  1 
ATOM   2145  N  N   . ARG B  1 143 ? 12.993 -21.339  -22.094  1.00 41.82  ? 144 ARG B N   1 
ATOM   2146  C  CA  . ARG B  1 143 ? 13.427 -22.471  -22.911  1.00 39.97  ? 144 ARG B CA  1 
ATOM   2147  C  C   . ARG B  1 143 ? 12.242 -23.316  -23.355  1.00 40.85  ? 144 ARG B C   1 
ATOM   2148  O  O   . ARG B  1 143 ? 11.664 -24.049  -22.580  1.00 42.96  ? 144 ARG B O   1 
ATOM   2149  C  CB  . ARG B  1 143 ? 14.431 -23.310  -22.130  1.00 39.99  ? 144 ARG B CB  1 
ATOM   2150  C  CG  . ARG B  1 143 ? 15.656 -22.525  -21.763  1.00 39.66  ? 144 ARG B CG  1 
ATOM   2151  C  CD  . ARG B  1 143 ? 16.603 -23.275  -20.853  1.00 40.51  ? 144 ARG B CD  1 
ATOM   2152  N  NE  . ARG B  1 143 ? 17.694 -22.410  -20.388  1.00 40.65  ? 144 ARG B NE  1 
ATOM   2153  C  CZ  . ARG B  1 143 ? 18.716 -22.809  -19.642  1.00 41.62  ? 144 ARG B CZ  1 
ATOM   2154  N  NH1 . ARG B  1 143 ? 18.805 -24.066  -19.248  1.00 42.59  ? 144 ARG B NH1 1 
ATOM   2155  N  NH2 . ARG B  1 143 ? 19.658 -21.949  -19.294  1.00 42.55  ? 144 ARG B NH2 1 
ATOM   2156  N  N   . LEU B  1 144 ? 11.882 -23.203  -24.618  1.00 39.77  ? 145 LEU B N   1 
ATOM   2157  C  CA  . LEU B  1 144 ? 10.691 -23.845  -25.126  1.00 41.23  ? 145 LEU B CA  1 
ATOM   2158  C  C   . LEU B  1 144 ? 10.884 -25.321  -25.337  1.00 41.08  ? 145 LEU B C   1 
ATOM   2159  O  O   . LEU B  1 144 ? 10.077 -26.123  -24.890  1.00 43.40  ? 145 LEU B O   1 
ATOM   2160  C  CB  . LEU B  1 144 ? 10.253 -23.211  -26.448  1.00 40.72  ? 145 LEU B CB  1 
ATOM   2161  C  CG  . LEU B  1 144 ? 9.697  -21.783  -26.388  1.00 41.71  ? 145 LEU B CG  1 
ATOM   2162  C  CD1 . LEU B  1 144 ? 9.108  -21.407  -27.745  1.00 41.60  ? 145 LEU B CD1 1 
ATOM   2163  C  CD2 . LEU B  1 144 ? 8.637  -21.604  -25.296  1.00 44.63  ? 145 LEU B CD2 1 
ATOM   2164  N  N   . ALA B  1 145 ? 11.935 -25.674  -26.056  1.00 38.92  ? 146 ALA B N   1 
ATOM   2165  C  CA  . ALA B  1 145 ? 12.226 -27.069  -26.371  1.00 38.87  ? 146 ALA B CA  1 
ATOM   2166  C  C   . ALA B  1 145 ? 13.719 -27.275  -26.421  1.00 36.97  ? 146 ALA B C   1 
ATOM   2167  O  O   . ALA B  1 145 ? 14.437 -26.387  -26.813  1.00 35.84  ? 146 ALA B O   1 
ATOM   2168  C  CB  . ALA B  1 145 ? 11.593 -27.453  -27.689  1.00 39.00  ? 146 ALA B CB  1 
ATOM   2169  N  N   . CYS B  1 146 ? 14.185 -28.445  -26.020  1.00 37.27  ? 147 CYS B N   1 
ATOM   2170  C  CA  . CYS B  1 146 ? 15.605 -28.737  -26.033  1.00 35.99  ? 147 CYS B CA  1 
ATOM   2171  C  C   . CYS B  1 146 ? 15.893 -30.213  -26.186  1.00 36.61  ? 147 CYS B C   1 
ATOM   2172  O  O   . CYS B  1 146 ? 15.005 -31.036  -26.114  1.00 38.20  ? 147 CYS B O   1 
ATOM   2173  C  CB  . CYS B  1 146 ? 16.257 -28.222  -24.768  1.00 36.29  ? 147 CYS B CB  1 
ATOM   2174  S  SG  . CYS B  1 146 ? 15.747 -29.020  -23.306  1.00 38.20  ? 147 CYS B SG  1 
ATOM   2175  N  N   . GLY B  1 147 ? 17.155 -30.535  -26.414  1.00 35.89  ? 148 GLY B N   1 
ATOM   2176  C  CA  . GLY B  1 147 ? 17.586 -31.921  -26.549  1.00 36.67  ? 148 GLY B CA  1 
ATOM   2177  C  C   . GLY B  1 147 ? 19.087 -32.072  -26.493  1.00 36.08  ? 148 GLY B C   1 
ATOM   2178  O  O   . GLY B  1 147 ? 19.799 -31.157  -26.862  1.00 35.02  ? 148 GLY B O   1 
ATOM   2179  N  N   . VAL B  1 148 ? 19.563 -33.235  -26.048  1.00 37.22  ? 149 VAL B N   1 
ATOM   2180  C  CA  . VAL B  1 148 ? 21.013 -33.516  -25.976  1.00 37.21  ? 149 VAL B CA  1 
ATOM   2181  C  C   . VAL B  1 148 ? 21.593 -33.882  -27.335  1.00 36.65  ? 149 VAL B C   1 
ATOM   2182  O  O   . VAL B  1 148 ? 21.028 -34.671  -28.057  1.00 37.06  ? 149 VAL B O   1 
ATOM   2183  C  CB  . VAL B  1 148 ? 21.328 -34.643  -25.001  1.00 38.86  ? 149 VAL B CB  1 
ATOM   2184  C  CG1 . VAL B  1 148 ? 22.782 -34.896  -24.967  1.00 39.20  ? 149 VAL B CG1 1 
ATOM   2185  C  CG2 . VAL B  1 148 ? 20.839 -34.293  -23.629  1.00 39.95  ? 149 VAL B CG2 1 
ATOM   2186  N  N   . ILE B  1 149 ? 22.725 -33.290  -27.676  1.00 36.23  ? 150 ILE B N   1 
ATOM   2187  C  CA  . ILE B  1 149 ? 23.331 -33.467  -28.992  1.00 36.15  ? 150 ILE B CA  1 
ATOM   2188  C  C   . ILE B  1 149 ? 24.056 -34.776  -29.026  1.00 37.63  ? 150 ILE B C   1 
ATOM   2189  O  O   . ILE B  1 149 ? 24.909 -35.018  -28.213  1.00 38.75  ? 150 ILE B O   1 
ATOM   2190  C  CB  . ILE B  1 149 ? 24.339 -32.344  -29.323  1.00 35.71  ? 150 ILE B CB  1 
ATOM   2191  C  CG1 . ILE B  1 149 ? 23.606 -31.017  -29.556  1.00 34.33  ? 150 ILE B CG1 1 
ATOM   2192  C  CG2 . ILE B  1 149 ? 25.160 -32.713  -30.540  1.00 36.31  ? 150 ILE B CG2 1 
ATOM   2193  C  CD1 . ILE B  1 149 ? 24.498 -29.837  -29.667  1.00 34.06  ? 150 ILE B CD1 1 
ATOM   2194  N  N   . GLY B  1 150 ? 23.744 -35.612  -29.995  1.00 38.27  ? 151 GLY B N   1 
ATOM   2195  C  CA  . GLY B  1 150 ? 24.277 -36.974  -30.027  1.00 40.08  ? 151 GLY B CA  1 
ATOM   2196  C  C   . GLY B  1 150 ? 25.007 -37.341  -31.299  1.00 41.00  ? 151 GLY B C   1 
ATOM   2197  O  O   . GLY B  1 150 ? 24.784 -36.764  -32.350  1.00 40.57  ? 151 GLY B O   1 
ATOM   2198  N  N   . ILE B  1 151 ? 25.886 -38.320  -31.199  1.00 42.76  ? 152 ILE B N   1 
ATOM   2199  C  CA  . ILE B  1 151 ? 26.642 -38.785  -32.351  1.00 44.27  ? 152 ILE B CA  1 
ATOM   2200  C  C   . ILE B  1 151 ? 25.722 -39.520  -33.299  1.00 44.84  ? 152 ILE B C   1 
ATOM   2201  O  O   . ILE B  1 151 ? 24.957 -40.353  -32.880  1.00 45.42  ? 152 ILE B O   1 
ATOM   2202  C  CB  . ILE B  1 151 ? 27.783 -39.726  -31.939  1.00 46.54  ? 152 ILE B CB  1 
ATOM   2203  C  CG1 . ILE B  1 151 ? 28.768 -38.995  -31.020  1.00 46.47  ? 152 ILE B CG1 1 
ATOM   2204  C  CG2 . ILE B  1 151 ? 28.488 -40.261  -33.183  1.00 48.49  ? 152 ILE B CG2 1 
ATOM   2205  C  CD1 . ILE B  1 151 ? 29.886 -39.856  -30.554  1.00 49.11  ? 152 ILE B CD1 1 
ATOM   2206  N  N   . ALA B  1 152 ? 25.810 -39.207  -34.577  1.00 45.28  ? 153 ALA B N   1 
ATOM   2207  C  CA  . ALA B  1 152 ? 24.906 -39.763  -35.579  1.00 46.29  ? 153 ALA B CA  1 
ATOM   2208  C  C   . ALA B  1 152 ? 25.637 -40.610  -36.602  1.00 49.12  ? 153 ALA B C   1 
ATOM   2209  O  O   . ALA B  1 152 ? 26.832 -40.472  -36.779  1.00 50.17  ? 153 ALA B O   1 
ATOM   2210  C  CB  . ALA B  1 152 ? 24.196 -38.654  -36.278  1.00 45.05  ? 153 ALA B CB  1 
ATOM   2211  N  N   . GLN B  1 153 ? 24.913 -41.473  -37.298  1.00 50.87  ? 154 GLN B N   1 
ATOM   2212  C  CA  . GLN B  1 153 ? 25.532 -42.344  -38.302  1.00 54.20  ? 154 GLN B CA  1 
ATOM   2213  C  C   . GLN B  1 153 ? 25.871 -41.568  -39.560  1.00 54.94  ? 154 GLN B C   1 
ATOM   2214  O  O   . GLN B  1 153 ? 25.039 -40.826  -40.079  1.00 54.02  ? 154 GLN B O   1 
ATOM   2215  C  CB  . GLN B  1 153 ? 24.620 -43.522  -38.676  1.00 56.46  ? 154 GLN B CB  1 
ATOM   2216  C  CG  . GLN B  1 153 ? 25.256 -44.515  -39.692  1.00 60.26  ? 154 GLN B CG  1 
ATOM   2217  C  CD  . GLN B  1 153 ? 24.397 -45.747  -39.972  1.00 62.73  ? 154 GLN B CD  1 
ATOM   2218  O  OE1 . GLN B  1 153 ? 24.120 -46.546  -39.077  1.00 62.97  ? 154 GLN B OE1 1 
ATOM   2219  N  NE2 . GLN B  1 153 ? 23.981 -45.904  -41.223  1.00 64.79  ? 154 GLN B NE2 1 
ATOM   2220  O  OXT . GLN B  1 153 ? 26.969 -41.704  -40.100  1.00 56.97  ? 154 GLN B OXT 1 
ATOM   2221  N  N   . ALA C  1 1   ? 41.734 7.238    -13.356  1.00 128.26 ? 2   ALA C N   1 
ATOM   2222  C  CA  . ALA C  1 1   ? 40.877 6.875    -12.183  1.00 131.07 ? 2   ALA C CA  1 
ATOM   2223  C  C   . ALA C  1 1   ? 39.742 7.911    -12.041  1.00 127.20 ? 2   ALA C C   1 
ATOM   2224  O  O   . ALA C  1 1   ? 39.476 8.461    -10.949  1.00 132.16 ? 2   ALA C O   1 
ATOM   2225  C  CB  . ALA C  1 1   ? 41.720 6.760    -10.876  1.00 141.01 ? 2   ALA C CB  1 
ATOM   2226  N  N   . THR C  1 2   ? 39.072 8.131    -13.170  1.00 118.78 ? 3   THR C N   1 
ATOM   2227  C  CA  . THR C  1 2   ? 37.976 9.111    -13.316  1.00 114.56 ? 3   THR C CA  1 
ATOM   2228  C  C   . THR C  1 2   ? 36.566 8.487    -13.292  1.00 110.64 ? 3   THR C C   1 
ATOM   2229  O  O   . THR C  1 2   ? 36.339 7.406    -13.865  1.00 107.27 ? 3   THR C O   1 
ATOM   2230  C  CB  . THR C  1 2   ? 38.104 9.865    -14.656  1.00 109.11 ? 3   THR C CB  1 
ATOM   2231  O  OG1 . THR C  1 2   ? 39.458 9.791    -15.109  1.00 111.37 ? 3   THR C OG1 1 
ATOM   2232  C  CG2 . THR C  1 2   ? 37.660 11.336   -14.516  1.00 108.88 ? 3   THR C CG2 1 
ATOM   2233  N  N   . LYS C  1 3   ? 35.635 9.191    -12.642  1.00 111.46 ? 4   LYS C N   1 
ATOM   2234  C  CA  . LYS C  1 3   ? 34.238 8.761    -12.548  1.00 108.79 ? 4   LYS C CA  1 
ATOM   2235  C  C   . LYS C  1 3   ? 33.351 9.925    -12.895  1.00 105.97 ? 4   LYS C C   1 
ATOM   2236  O  O   . LYS C  1 3   ? 33.719 11.068   -12.674  1.00 108.64 ? 4   LYS C O   1 
ATOM   2237  C  CB  . LYS C  1 3   ? 33.889 8.276    -11.123  1.00 115.31 ? 4   LYS C CB  1 
ATOM   2238  C  CG  . LYS C  1 3   ? 34.593 6.960    -10.665  1.00 119.20 ? 4   LYS C CG  1 
ATOM   2239  C  CD  . LYS C  1 3   ? 33.988 6.424    -9.335   1.00 125.38 ? 4   LYS C CD  1 
ATOM   2240  C  CE  . LYS C  1 3   ? 34.985 5.572    -8.529   1.00 132.30 ? 4   LYS C CE  1 
ATOM   2241  N  NZ  . LYS C  1 3   ? 34.660 5.528    -7.063   1.00 139.75 ? 4   LYS C NZ  1 
ATOM   2242  N  N   . ALA C  1 4   ? 32.180 9.623    -13.434  1.00 101.42 ? 5   ALA C N   1 
ATOM   2243  C  CA  . ALA C  1 4   ? 31.167 10.636   -13.686  1.00 99.79  ? 5   ALA C CA  1 
ATOM   2244  C  C   . ALA C  1 4   ? 29.799 10.069   -13.359  1.00 99.44  ? 5   ALA C C   1 
ATOM   2245  O  O   . ALA C  1 4   ? 29.659 8.874    -13.170  1.00 99.34  ? 5   ALA C O   1 
ATOM   2246  C  CB  . ALA C  1 4   ? 31.244 11.098   -15.131  1.00 93.97  ? 5   ALA C CB  1 
ATOM   2247  N  N   . VAL C  1 5   ? 28.800 10.934   -13.281  1.00 100.05 ? 6   VAL C N   1 
ATOM   2248  C  CA  . VAL C  1 5   ? 27.434 10.516   -13.003  1.00 100.59 ? 6   VAL C CA  1 
ATOM   2249  C  C   . VAL C  1 5   ? 26.443 11.472   -13.657  1.00 98.79  ? 6   VAL C C   1 
ATOM   2250  O  O   . VAL C  1 5   ? 26.768 12.624   -13.925  1.00 99.28  ? 6   VAL C O   1 
ATOM   2251  C  CB  . VAL C  1 5   ? 27.151 10.460   -11.478  1.00 108.13 ? 6   VAL C CB  1 
ATOM   2252  C  CG1 . VAL C  1 5   ? 26.938 11.862   -10.914  1.00 113.27 ? 6   VAL C CG1 1 
ATOM   2253  C  CG2 . VAL C  1 5   ? 25.927 9.575    -11.178  1.00 108.94 ? 6   VAL C CG2 1 
ATOM   2254  N  N   . CYS C  1 6   ? 25.225 10.988   -13.888  1.00 97.54  ? 7   CYS C N   1 
ATOM   2255  C  CA  . CYS C  1 6   ? 24.160 11.784   -14.499  1.00 96.77  ? 7   CYS C CA  1 
ATOM   2256  C  C   . CYS C  1 6   ? 22.774 11.374   -14.032  1.00 99.56  ? 7   CYS C C   1 
ATOM   2257  O  O   . CYS C  1 6   ? 22.376 10.215   -14.139  1.00 97.73  ? 7   CYS C O   1 
ATOM   2258  C  CB  . CYS C  1 6   ? 24.184 11.663   -16.027  1.00 90.14  ? 7   CYS C CB  1 
ATOM   2259  S  SG  . CYS C  1 6   ? 22.709 12.529   -16.842  1.00 89.75  ? 7   CYS C SG  1 
ATOM   2260  N  N   . VAL C  1 7   ? 22.018 12.352   -13.568  1.00 104.55 ? 8   VAL C N   1 
ATOM   2261  C  CA  . VAL C  1 7   ? 20.618 12.133   -13.195  1.00 108.07 ? 8   VAL C CA  1 
ATOM   2262  C  C   . VAL C  1 7   ? 19.672 12.474   -14.350  1.00 105.09 ? 8   VAL C C   1 
ATOM   2263  O  O   . VAL C  1 7   ? 19.459 13.638   -14.703  1.00 106.47 ? 8   VAL C O   1 
ATOM   2264  C  CB  . VAL C  1 7   ? 20.226 12.948   -11.946  1.00 116.63 ? 8   VAL C CB  1 
ATOM   2265  C  CG1 . VAL C  1 7   ? 18.702 12.863   -11.694  1.00 120.85 ? 8   VAL C CG1 1 
ATOM   2266  C  CG2 . VAL C  1 7   ? 21.015 12.443   -10.731  1.00 120.36 ? 8   VAL C CG2 1 
ATOM   2267  N  N   . LEU C  1 8   ? 19.106 11.428   -14.922  1.00 101.59 ? 9   LEU C N   1 
ATOM   2268  C  CA  . LEU C  1 8   ? 18.148 11.565   -16.009  1.00 99.40  ? 9   LEU C CA  1 
ATOM   2269  C  C   . LEU C  1 8   ? 16.786 11.984   -15.450  1.00 105.94 ? 9   LEU C C   1 
ATOM   2270  O  O   . LEU C  1 8   ? 16.274 11.373   -14.494  1.00 110.14 ? 9   LEU C O   1 
ATOM   2271  C  CB  . LEU C  1 8   ? 18.045 10.238   -16.798  1.00 93.92  ? 9   LEU C CB  1 
ATOM   2272  C  CG  . LEU C  1 8   ? 19.279 9.844    -17.627  1.00 87.41  ? 9   LEU C CG  1 
ATOM   2273  C  CD1 . LEU C  1 8   ? 19.323 8.345    -17.901  1.00 83.76  ? 9   LEU C CD1 1 
ATOM   2274  C  CD2 . LEU C  1 8   ? 19.301 10.675   -18.934  1.00 84.06  ? 9   LEU C CD2 1 
ATOM   2275  N  N   . LYS C  1 9   ? 16.223 13.032   -16.042  1.00 107.34 ? 10  LYS C N   1 
ATOM   2276  C  CA  . LYS C  1 9   ? 14.890 13.492   -15.677  1.00 114.32 ? 10  LYS C CA  1 
ATOM   2277  C  C   . LYS C  1 9   ? 14.166 14.103   -16.853  1.00 113.67 ? 10  LYS C C   1 
ATOM   2278  O  O   . LYS C  1 9   ? 14.798 14.475   -17.820  1.00 109.26 ? 10  LYS C O   1 
ATOM   2279  C  CB  . LYS C  1 9   ? 14.976 14.536   -14.578  1.00 121.88 ? 10  LYS C CB  1 
ATOM   2280  C  CG  . LYS C  1 9   ? 15.041 13.965   -13.159  1.00 127.21 ? 10  LYS C CG  1 
ATOM   2281  C  CD  . LYS C  1 9   ? 14.467 14.977   -12.107  1.00 137.48 ? 10  LYS C CD  1 
ATOM   2282  C  CE  . LYS C  1 9   ? 14.839 14.599   -10.644  1.00 142.55 ? 10  LYS C CE  1 
ATOM   2283  N  NZ  . LYS C  1 9   ? 13.909 13.564   -10.031  1.00 146.12 ? 10  LYS C NZ  1 
ATOM   2284  N  N   . GLY C  1 10  ? 12.847 14.236   -16.769  1.00 119.12 ? 11  GLY C N   1 
ATOM   2285  C  CA  . GLY C  1 10  ? 12.087 14.810   -17.880  1.00 119.60 ? 11  GLY C CA  1 
ATOM   2286  C  C   . GLY C  1 10  ? 10.676 15.225   -17.550  1.00 128.22 ? 11  GLY C C   1 
ATOM   2287  O  O   . GLY C  1 10  ? 10.251 15.147   -16.404  1.00 134.38 ? 11  GLY C O   1 
ATOM   2288  N  N   . ASP C  1 11  ? 9.951  15.651   -18.583  1.00 129.13 ? 12  ASP C N   1 
ATOM   2289  C  CA  . ASP C  1 11  ? 8.564  16.117   -18.432  1.00 138.05 ? 12  ASP C CA  1 
ATOM   2290  C  C   . ASP C  1 11  ? 7.598  15.041   -17.933  1.00 140.96 ? 12  ASP C C   1 
ATOM   2291  O  O   . ASP C  1 11  ? 6.639  15.341   -17.211  1.00 149.95 ? 12  ASP C O   1 
ATOM   2292  C  CB  . ASP C  1 11  ? 8.031  16.680   -19.754  1.00 138.32 ? 12  ASP C CB  1 
ATOM   2293  C  CG  . ASP C  1 11  ? 8.248  18.171   -19.878  1.00 143.23 ? 12  ASP C CG  1 
ATOM   2294  O  OD1 . ASP C  1 11  ? 7.937  18.906   -18.910  1.00 151.60 ? 12  ASP C OD1 1 
ATOM   2295  O  OD2 . ASP C  1 11  ? 8.723  18.612   -20.949  1.00 139.83 ? 12  ASP C OD2 1 
ATOM   2296  N  N   . GLY C  1 12  ? 7.843  13.795   -18.325  1.00 134.05 ? 13  GLY C N   1 
ATOM   2297  C  CA  . GLY C  1 12  ? 6.960  12.684   -17.967  1.00 136.32 ? 13  GLY C CA  1 
ATOM   2298  C  C   . GLY C  1 12  ? 7.593  11.759   -16.939  1.00 134.44 ? 13  GLY C C   1 
ATOM   2299  O  O   . GLY C  1 12  ? 8.592  12.140   -16.289  1.00 133.22 ? 13  GLY C O   1 
ATOM   2300  N  N   . PRO C  1 13  ? 7.047  10.512   -16.830  1.00 134.27 ? 14  PRO C N   1 
ATOM   2301  C  CA  . PRO C  1 13  ? 7.380  9.568    -15.743  1.00 134.82 ? 14  PRO C CA  1 
ATOM   2302  C  C   . PRO C  1 13  ? 8.803  8.989    -15.811  1.00 126.64 ? 14  PRO C C   1 
ATOM   2303  O  O   . PRO C  1 13  ? 9.292  8.441    -14.807  1.00 127.81 ? 14  PRO C O   1 
ATOM   2304  C  CB  . PRO C  1 13  ? 6.364  8.446    -15.953  1.00 136.41 ? 14  PRO C CB  1 
ATOM   2305  C  CG  . PRO C  1 13  ? 6.155  8.404    -17.455  1.00 131.04 ? 14  PRO C CG  1 
ATOM   2306  C  CD  . PRO C  1 13  ? 6.350  9.823    -17.950  1.00 131.47 ? 14  PRO C CD  1 
ATOM   2307  N  N   . VAL C  1 14  ? 9.439  9.117    -16.982  1.00 119.23 ? 15  VAL C N   1 
ATOM   2308  C  CA  . VAL C  1 14  ? 10.762 8.557    -17.209  1.00 111.62 ? 15  VAL C CA  1 
ATOM   2309  C  C   . VAL C  1 14  ? 11.782 9.289    -16.340  1.00 112.53 ? 15  VAL C C   1 
ATOM   2310  O  O   . VAL C  1 14  ? 11.867 10.519   -16.341  1.00 114.77 ? 15  VAL C O   1 
ATOM   2311  C  CB  . VAL C  1 14  ? 11.179 8.619    -18.695  1.00 104.53 ? 15  VAL C CB  1 
ATOM   2312  C  CG1 . VAL C  1 14  ? 12.509 7.869    -18.905  1.00 97.49  ? 15  VAL C CG1 1 
ATOM   2313  C  CG2 . VAL C  1 14  ? 10.079 8.032    -19.593  1.00 104.54 ? 15  VAL C CG2 1 
ATOM   2314  N  N   . GLN C  1 15  ? 12.511 8.505    -15.567  1.00 111.61 ? 16  GLN C N   1 
ATOM   2315  C  CA  . GLN C  1 15  ? 13.599 9.017    -14.749  1.00 112.57 ? 16  GLN C CA  1 
ATOM   2316  C  C   . GLN C  1 15  ? 14.595 7.912    -14.388  1.00 109.26 ? 16  GLN C C   1 
ATOM   2317  O  O   . GLN C  1 15  ? 14.304 6.709    -14.501  1.00 107.92 ? 16  GLN C O   1 
ATOM   2318  C  CB  . GLN C  1 15  ? 13.065 9.690    -13.476  1.00 121.74 ? 16  GLN C CB  1 
ATOM   2319  C  CG  . GLN C  1 15  ? 12.099 8.827    -12.640  1.00 127.92 ? 16  GLN C CG  1 
ATOM   2320  C  CD  . GLN C  1 15  ? 11.784 9.439    -11.285  1.00 137.60 ? 16  GLN C CD  1 
ATOM   2321  O  OE1 . GLN C  1 15  ? 11.417 8.723    -10.344  1.00 142.95 ? 16  GLN C OE1 1 
ATOM   2322  N  NE2 . GLN C  1 15  ? 11.936 10.769   -11.174  1.00 140.35 ? 16  GLN C NE2 1 
ATOM   2323  N  N   . GLY C  1 16  ? 15.779 8.334    -13.966  1.00 108.46 ? 17  GLY C N   1 
ATOM   2324  C  CA  . GLY C  1 16  ? 16.839 7.393    -13.637  1.00 106.06 ? 17  GLY C CA  1 
ATOM   2325  C  C   . GLY C  1 16  ? 18.173 8.028    -13.268  1.00 105.68 ? 17  GLY C C   1 
ATOM   2326  O  O   . GLY C  1 16  ? 18.340 9.255    -13.293  1.00 106.88 ? 17  GLY C O   1 
ATOM   2327  N  N   . ILE C  1 17  ? 19.120 7.153    -12.932  1.00 104.47 ? 18  ILE C N   1 
ATOM   2328  C  CA  . ILE C  1 17  ? 20.511 7.506    -12.611  1.00 104.12 ? 18  ILE C CA  1 
ATOM   2329  C  C   . ILE C  1 17  ? 21.484 6.625    -13.398  1.00 98.21  ? 18  ILE C C   1 
ATOM   2330  O  O   . ILE C  1 17  ? 21.373 5.397    -13.374  1.00 97.77  ? 18  ILE C O   1 
ATOM   2331  C  CB  . ILE C  1 17  ? 20.823 7.244    -11.124  1.00 111.19 ? 18  ILE C CB  1 
ATOM   2332  C  CG1 . ILE C  1 17  ? 20.282 8.379    -10.248  1.00 117.97 ? 18  ILE C CG1 1 
ATOM   2333  C  CG2 . ILE C  1 17  ? 22.364 7.036    -10.896  1.00 110.22 ? 18  ILE C CG2 1 
ATOM   2334  C  CD1 . ILE C  1 17  ? 20.810 8.298    -8.801   1.00 125.24 ? 18  ILE C CD1 1 
ATOM   2335  N  N   . ILE C  1 18  ? 22.444 7.248    -14.070  1.00 94.56  ? 19  ILE C N   1 
ATOM   2336  C  CA  . ILE C  1 18  ? 23.446 6.517    -14.843  1.00 89.66  ? 19  ILE C CA  1 
ATOM   2337  C  C   . ILE C  1 18  ? 24.841 6.904    -14.415  1.00 91.15  ? 19  ILE C C   1 
ATOM   2338  O  O   . ILE C  1 18  ? 25.183 8.070    -14.341  1.00 92.34  ? 19  ILE C O   1 
ATOM   2339  C  CB  . ILE C  1 18  ? 23.339 6.797    -16.345  1.00 83.58  ? 19  ILE C CB  1 
ATOM   2340  C  CG1 . ILE C  1 18  ? 22.035 6.224    -16.913  1.00 82.20  ? 19  ILE C CG1 1 
ATOM   2341  C  CG2 . ILE C  1 18  ? 24.519 6.147    -17.059  1.00 79.73  ? 19  ILE C CG2 1 
ATOM   2342  C  CD1 . ILE C  1 18  ? 22.014 4.674    -16.908  1.00 81.62  ? 19  ILE C CD1 1 
ATOM   2343  N  N   . ASN C  1 19  ? 25.659 5.903    -14.168  1.00 91.77  ? 20  ASN C N   1 
ATOM   2344  C  CA  . ASN C  1 19  ? 27.056 6.110    -13.768  1.00 93.91  ? 20  ASN C CA  1 
ATOM   2345  C  C   . ASN C  1 19  ? 28.047 5.912    -14.904  1.00 89.22  ? 20  ASN C C   1 
ATOM   2346  O  O   . ASN C  1 19  ? 27.784 5.157    -15.840  1.00 85.13  ? 20  ASN C O   1 
ATOM   2347  C  CB  . ASN C  1 19  ? 27.435 5.132    -12.659  1.00 99.22  ? 20  ASN C CB  1 
ATOM   2348  C  CG  . ASN C  1 19  ? 26.626 5.328    -11.418  1.00 105.49 ? 20  ASN C CG  1 
ATOM   2349  O  OD1 . ASN C  1 19  ? 25.698 4.543    -11.136  1.00 106.88 ? 20  ASN C OD1 1 
ATOM   2350  N  ND2 . ASN C  1 19  ? 26.959 6.389    -10.655  1.00 109.81 ? 20  ASN C ND2 1 
ATOM   2351  N  N   . PHE C  1 20  ? 29.192 6.587    -14.795  1.00 90.66  ? 21  PHE C N   1 
ATOM   2352  C  CA  . PHE C  1 20  ? 30.319 6.399    -15.710  1.00 87.64  ? 21  PHE C CA  1 
ATOM   2353  C  C   . PHE C  1 20  ? 31.570 6.108    -14.926  1.00 92.49  ? 21  PHE C C   1 
ATOM   2354  O  O   . PHE C  1 20  ? 31.760 6.612    -13.827  1.00 97.70  ? 21  PHE C O   1 
ATOM   2355  C  CB  . PHE C  1 20  ? 30.545 7.644    -16.552  1.00 84.83  ? 21  PHE C CB  1 
ATOM   2356  C  CG  . PHE C  1 20  ? 29.380 8.011    -17.425  1.00 80.45  ? 21  PHE C CG  1 
ATOM   2357  C  CD1 . PHE C  1 20  ? 28.293 8.699    -16.905  1.00 82.27  ? 21  PHE C CD1 1 
ATOM   2358  C  CD2 . PHE C  1 20  ? 29.384 7.691    -18.768  1.00 75.34  ? 21  PHE C CD2 1 
ATOM   2359  C  CE1 . PHE C  1 20  ? 27.230 9.055    -17.704  1.00 79.17  ? 21  PHE C CE1 1 
ATOM   2360  C  CE2 . PHE C  1 20  ? 28.320 8.038    -19.571  1.00 72.09  ? 21  PHE C CE2 1 
ATOM   2361  C  CZ  . PHE C  1 20  ? 27.237 8.726    -19.039  1.00 74.12  ? 21  PHE C CZ  1 
ATOM   2362  N  N   . GLU C  1 21  ? 32.421 5.279    -15.503  1.00 91.57  ? 22  GLU C N   1 
ATOM   2363  C  CA  . GLU C  1 21  ? 33.710 4.951    -14.884  1.00 96.99  ? 22  GLU C CA  1 
ATOM   2364  C  C   . GLU C  1 21  ? 34.812 4.552    -15.887  1.00 95.30  ? 22  GLU C C   1 
ATOM   2365  O  O   . GLU C  1 21  ? 34.796 3.471    -16.486  1.00 93.34  ? 22  GLU C O   1 
ATOM   2366  C  CB  . GLU C  1 21  ? 33.575 3.853    -13.815  1.00 102.09 ? 22  GLU C CB  1 
ATOM   2367  C  CG  . GLU C  1 21  ? 34.924 3.539    -13.120  1.00 109.12 ? 22  GLU C CG  1 
ATOM   2368  C  CD  . GLU C  1 21  ? 34.790 2.637    -11.900  1.00 116.07 ? 22  GLU C CD  1 
ATOM   2369  O  OE1 . GLU C  1 21  ? 33.743 1.958    -11.776  1.00 115.11 ? 22  GLU C OE1 1 
ATOM   2370  O  OE2 . GLU C  1 21  ? 35.743 2.609    -11.075  1.00 122.85 ? 22  GLU C OE2 1 
ATOM   2371  N  N   . GLN C  1 22  ? 35.789 5.444    -16.017  1.00 96.87  ? 23  GLN C N   1 
ATOM   2372  C  CA  . GLN C  1 22  ? 36.945 5.231    -16.872  1.00 96.76  ? 23  GLN C CA  1 
ATOM   2373  C  C   . GLN C  1 22  ? 38.150 5.009    -15.966  1.00 104.07 ? 23  GLN C C   1 
ATOM   2374  O  O   . GLN C  1 22  ? 38.613 5.922    -15.282  1.00 107.75 ? 23  GLN C O   1 
ATOM   2375  C  CB  . GLN C  1 22  ? 37.148 6.445    -17.806  1.00 93.45  ? 23  GLN C CB  1 
ATOM   2376  C  CG  . GLN C  1 22  ? 38.188 6.247    -18.936  1.00 92.50  ? 23  GLN C CG  1 
ATOM   2377  C  CD  . GLN C  1 22  ? 38.298 7.479    -19.843  1.00 89.62  ? 23  GLN C CD  1 
ATOM   2378  O  OE1 . GLN C  1 22  ? 38.252 8.626    -19.372  1.00 91.11  ? 23  GLN C OE1 1 
ATOM   2379  N  NE2 . GLN C  1 22  ? 38.425 7.243    -21.146  1.00 86.04  ? 23  GLN C NE2 1 
ATOM   2380  N  N   . LYS C  1 23  ? 38.632 3.776    -15.952  1.00 106.85 ? 24  LYS C N   1 
ATOM   2381  C  CA  . LYS C  1 23  ? 39.781 3.423    -15.111  1.00 114.96 ? 24  LYS C CA  1 
ATOM   2382  C  C   . LYS C  1 23  ? 41.075 4.065    -15.571  1.00 117.24 ? 24  LYS C C   1 
ATOM   2383  O  O   . LYS C  1 23  ? 41.908 4.431    -14.745  1.00 123.84 ? 24  LYS C O   1 
ATOM   2384  C  CB  . LYS C  1 23  ? 40.007 1.907    -15.056  1.00 118.03 ? 24  LYS C CB  1 
ATOM   2385  C  CG  . LYS C  1 23  ? 38.874 1.153    -14.364  1.00 118.43 ? 24  LYS C CG  1 
ATOM   2386  C  CD  . LYS C  1 23  ? 39.368 -0.132   -13.677  1.00 125.73 ? 24  LYS C CD  1 
ATOM   2387  C  CE  . LYS C  1 23  ? 38.233 -1.166   -13.530  1.00 124.39 ? 24  LYS C CE  1 
ATOM   2388  N  NZ  . LYS C  1 23  ? 38.709 -2.533   -13.144  1.00 130.85 ? 24  LYS C NZ  1 
ATOM   2389  N  N   . GLU C  1 24  ? 41.247 4.180    -16.886  1.00 112.58 ? 25  GLU C N   1 
ATOM   2390  C  CA  . GLU C  1 24  ? 42.475 4.735    -17.464  1.00 114.93 ? 25  GLU C CA  1 
ATOM   2391  C  C   . GLU C  1 24  ? 42.175 5.699    -18.605  1.00 108.82 ? 25  GLU C C   1 
ATOM   2392  O  O   . GLU C  1 24  ? 41.327 5.427    -19.469  1.00 102.80 ? 25  GLU C O   1 
ATOM   2393  C  CB  . GLU C  1 24  ? 43.377 3.615    -17.931  1.00 118.45 ? 25  GLU C CB  1 
ATOM   2394  C  CG  . GLU C  1 24  ? 43.625 2.632    -16.818  1.00 125.49 ? 25  GLU C CG  1 
ATOM   2395  C  CD  . GLU C  1 24  ? 44.770 1.689    -17.126  1.00 132.28 ? 25  GLU C CD  1 
ATOM   2396  O  OE1 . GLU C  1 24  ? 44.804 1.136    -18.262  1.00 129.54 ? 25  GLU C OE1 1 
ATOM   2397  O  OE2 . GLU C  1 24  ? 45.636 1.502    -16.226  1.00 140.82 ? 25  GLU C OE2 1 
ATOM   2398  N  N   . SER C  1 25  ? 42.890 6.824    -18.594  1.00 111.24 ? 26  SER C N   1 
ATOM   2399  C  CA  . SER C  1 25  ? 42.677 7.949    -19.540  1.00 106.85 ? 26  SER C CA  1 
ATOM   2400  C  C   . SER C  1 25  ? 42.536 7.523    -21.028  1.00 101.88 ? 26  SER C C   1 
ATOM   2401  O  O   . SER C  1 25  ? 41.706 8.076    -21.781  1.00 96.18  ? 26  SER C O   1 
ATOM   2402  C  CB  . SER C  1 25  ? 43.840 8.964    -19.407  1.00 112.14 ? 26  SER C CB  1 
ATOM   2403  O  OG  . SER C  1 25  ? 45.132 8.321    -19.369  1.00 118.68 ? 26  SER C OG  1 
ATOM   2404  N  N   . ASN C  1 26  ? 43.357 6.541    -21.421  1.00 104.76 ? 27  ASN C N   1 
ATOM   2405  C  CA  . ASN C  1 26  ? 43.367 6.009    -22.787  1.00 101.56 ? 27  ASN C CA  1 
ATOM   2406  C  C   . ASN C  1 26  ? 42.370 4.847    -22.987  1.00 97.57  ? 27  ASN C C   1 
ATOM   2407  O  O   . ASN C  1 26  ? 42.255 4.306    -24.090  1.00 95.05  ? 27  ASN C O   1 
ATOM   2408  C  CB  . ASN C  1 26  ? 44.792 5.545    -23.148  1.00 107.77 ? 27  ASN C CB  1 
ATOM   2409  C  CG  . ASN C  1 26  ? 45.239 4.294    -22.348  1.00 113.46 ? 27  ASN C CG  1 
ATOM   2410  O  OD1 . ASN C  1 26  ? 45.053 4.217    -21.108  1.00 115.76 ? 27  ASN C OD1 1 
ATOM   2411  N  ND2 . ASN C  1 26  ? 45.821 3.309    -23.063  1.00 115.65 ? 27  ASN C ND2 1 
ATOM   2412  N  N   . GLY C  1 27  ? 41.651 4.479    -21.925  1.00 97.52  ? 28  GLY C N   1 
ATOM   2413  C  CA  . GLY C  1 27  ? 40.886 3.223    -21.887  1.00 95.80  ? 28  GLY C CA  1 
ATOM   2414  C  C   . GLY C  1 27  ? 39.378 3.383    -22.028  1.00 89.36  ? 28  GLY C C   1 
ATOM   2415  O  O   . GLY C  1 27  ? 38.876 4.504    -22.157  1.00 86.23  ? 28  GLY C O   1 
ATOM   2416  N  N   . PRO C  1 28  ? 38.644 2.253    -21.973  1.00 88.02  ? 29  PRO C N   1 
ATOM   2417  C  CA  . PRO C  1 28  ? 37.217 2.270    -22.204  1.00 82.47  ? 29  PRO C CA  1 
ATOM   2418  C  C   . PRO C  1 28  ? 36.455 2.768    -21.007  1.00 82.92  ? 29  PRO C C   1 
ATOM   2419  O  O   . PRO C  1 28  ? 36.959 2.736    -19.898  1.00 88.05  ? 29  PRO C O   1 
ATOM   2420  C  CB  . PRO C  1 28  ? 36.896 0.796    -22.442  1.00 82.77  ? 29  PRO C CB  1 
ATOM   2421  C  CG  . PRO C  1 28  ? 37.842 0.066    -21.570  1.00 89.36  ? 29  PRO C CG  1 
ATOM   2422  C  CD  . PRO C  1 28  ? 39.109 0.910    -21.564  1.00 92.74  ? 29  PRO C CD  1 
ATOM   2423  N  N   . VAL C  1 29  ? 35.234 3.201    -21.248  1.00 78.29  ? 30  VAL C N   1 
ATOM   2424  C  CA  . VAL C  1 29  ? 34.386 3.747    -20.214  1.00 78.89  ? 30  VAL C CA  1 
ATOM   2425  C  C   . VAL C  1 29  ? 33.243 2.813    -19.932  1.00 77.87  ? 30  VAL C C   1 
ATOM   2426  O  O   . VAL C  1 29  ? 32.423 2.575    -20.800  1.00 73.91  ? 30  VAL C O   1 
ATOM   2427  C  CB  . VAL C  1 29  ? 33.772 5.068    -20.674  1.00 75.55  ? 30  VAL C CB  1 
ATOM   2428  C  CG1 . VAL C  1 29  ? 32.763 5.588    -19.624  1.00 76.69  ? 30  VAL C CG1 1 
ATOM   2429  C  CG2 . VAL C  1 29  ? 34.882 6.080    -20.987  1.00 76.84  ? 30  VAL C CG2 1 
ATOM   2430  N  N   . LYS C  1 30  ? 33.153 2.304    -18.716  1.00 82.21  ? 31  LYS C N   1 
ATOM   2431  C  CA  . LYS C  1 30  ? 31.962 1.538    -18.316  1.00 81.99  ? 31  LYS C CA  1 
ATOM   2432  C  C   . LYS C  1 30  ? 30.800 2.474    -18.004  1.00 80.18  ? 31  LYS C C   1 
ATOM   2433  O  O   . LYS C  1 30  ? 30.963 3.483    -17.333  1.00 82.46  ? 31  LYS C O   1 
ATOM   2434  C  CB  . LYS C  1 30  ? 32.259 0.637    -17.122  1.00 88.08  ? 31  LYS C CB  1 
ATOM   2435  C  CG  . LYS C  1 30  ? 33.184 -0.515   -17.486  1.00 90.71  ? 31  LYS C CG  1 
ATOM   2436  C  CD  . LYS C  1 30  ? 33.224 -1.614   -16.410  1.00 97.40  ? 31  LYS C CD  1 
ATOM   2437  C  CE  . LYS C  1 30  ? 34.140 -2.777   -16.844  1.00 100.13 ? 31  LYS C CE  1 
ATOM   2438  N  NZ  . LYS C  1 30  ? 34.080 -3.954   -15.924  1.00 106.55 ? 31  LYS C NZ  1 
ATOM   2439  N  N   . VAL C  1 31  ? 29.636 2.139    -18.526  1.00 76.78  ? 32  VAL C N   1 
ATOM   2440  C  CA  . VAL C  1 31  ? 28.436 2.915    -18.284  1.00 76.03  ? 32  VAL C CA  1 
ATOM   2441  C  C   . VAL C  1 31  ? 27.414 2.004    -17.669  1.00 78.02  ? 32  VAL C C   1 
ATOM   2442  O  O   . VAL C  1 31  ? 27.045 1.003    -18.263  1.00 76.33  ? 32  VAL C O   1 
ATOM   2443  C  CB  . VAL C  1 31  ? 27.851 3.487    -19.578  1.00 70.78  ? 32  VAL C CB  1 
ATOM   2444  C  CG1 . VAL C  1 31  ? 26.642 4.369    -19.281  1.00 70.64  ? 32  VAL C CG1 1 
ATOM   2445  C  CG2 . VAL C  1 31  ? 28.935 4.250    -20.334  1.00 69.31  ? 32  VAL C CG2 1 
ATOM   2446  N  N   . TRP C  1 32  ? 26.947 2.343    -16.476  1.00 82.38  ? 33  TRP C N   1 
ATOM   2447  C  CA  . TRP C  1 32  ? 25.924 1.522    -15.820  1.00 85.25  ? 33  TRP C CA  1 
ATOM   2448  C  C   . TRP C  1 32  ? 24.950 2.307    -14.933  1.00 88.57  ? 33  TRP C C   1 
ATOM   2449  O  O   . TRP C  1 32  ? 25.244 3.397    -14.444  1.00 90.66  ? 33  TRP C O   1 
ATOM   2450  C  CB  . TRP C  1 32  ? 26.559 0.376    -15.028  1.00 89.79  ? 33  TRP C CB  1 
ATOM   2451  C  CG  . TRP C  1 32  ? 26.919 0.727    -13.627  1.00 96.35  ? 33  TRP C CG  1 
ATOM   2452  C  CD1 . TRP C  1 32  ? 26.211 0.441    -12.499  1.00 102.04 ? 33  TRP C CD1 1 
ATOM   2453  C  CD2 . TRP C  1 32  ? 28.083 1.431    -13.198  1.00 98.71  ? 33  TRP C CD2 1 
ATOM   2454  N  NE1 . TRP C  1 32  ? 26.868 0.925    -11.388  1.00 107.39 ? 33  TRP C NE1 1 
ATOM   2455  C  CE2 . TRP C  1 32  ? 28.019 1.538    -11.791  1.00 105.56 ? 33  TRP C CE2 1 
ATOM   2456  C  CE3 . TRP C  1 32  ? 29.174 1.989    -13.869  1.00 96.51  ? 33  TRP C CE3 1 
ATOM   2457  C  CZ2 . TRP C  1 32  ? 29.000 2.183    -11.042  1.00 110.26 ? 33  TRP C CZ2 1 
ATOM   2458  C  CZ3 . TRP C  1 32  ? 30.163 2.624    -13.125  1.00 101.04 ? 33  TRP C CZ3 1 
ATOM   2459  C  CH2 . TRP C  1 32  ? 30.066 2.718    -11.722  1.00 107.85 ? 33  TRP C CH2 1 
ATOM   2460  N  N   . GLY C  1 33  ? 23.777 1.728    -14.738  1.00 89.72  ? 34  GLY C N   1 
ATOM   2461  C  CA  . GLY C  1 33  ? 22.767 2.349    -13.919  1.00 93.71  ? 34  GLY C CA  1 
ATOM   2462  C  C   . GLY C  1 33  ? 21.399 1.770    -14.173  1.00 93.58  ? 34  GLY C C   1 
ATOM   2463  O  O   . GLY C  1 33  ? 21.267 0.705    -14.786  1.00 91.30  ? 34  GLY C O   1 
ATOM   2464  N  N   . SER C  1 34  ? 20.382 2.495    -13.709  1.00 96.65  ? 35  SER C N   1 
ATOM   2465  C  CA  . SER C  1 34  ? 19.001 2.040    -13.806  1.00 98.01  ? 35  SER C CA  1 
ATOM   2466  C  C   . SER C  1 34  ? 18.019 3.178    -14.182  1.00 97.82  ? 35  SER C C   1 
ATOM   2467  O  O   . SER C  1 34  ? 17.846 4.140    -13.445  1.00 101.93 ? 35  SER C O   1 
ATOM   2468  C  CB  . SER C  1 34  ? 18.603 1.376    -12.486  1.00 105.15 ? 35  SER C CB  1 
ATOM   2469  O  OG  . SER C  1 34  ? 17.422 0.617    -12.631  1.00 106.74 ? 35  SER C OG  1 
ATOM   2470  N  N   . ILE C  1 35  ? 17.390 3.051    -15.342  1.00 93.64  ? 36  ILE C N   1 
ATOM   2471  C  CA  . ILE C  1 35  ? 16.347 3.981    -15.755  1.00 94.42  ? 36  ILE C CA  1 
ATOM   2472  C  C   . ILE C  1 35  ? 15.029 3.288    -15.599  1.00 98.02  ? 36  ILE C C   1 
ATOM   2473  O  O   . ILE C  1 35  ? 14.944 2.063    -15.814  1.00 96.87  ? 36  ILE C O   1 
ATOM   2474  C  CB  . ILE C  1 35  ? 16.467 4.399    -17.237  1.00 88.39  ? 36  ILE C CB  1 
ATOM   2475  C  CG1 . ILE C  1 35  ? 17.893 4.905    -17.535  1.00 84.72  ? 36  ILE C CG1 1 
ATOM   2476  C  CG2 . ILE C  1 35  ? 15.375 5.454    -17.600  1.00 89.87  ? 36  ILE C CG2 1 
ATOM   2477  C  CD1 . ILE C  1 35  ? 18.139 5.235    -19.012  1.00 79.15  ? 36  ILE C CD1 1 
ATOM   2478  N  N   . LYS C  1 36  ? 14.002 4.068    -15.255  1.00 102.89 ? 37  LYS C N   1 
ATOM   2479  C  CA  . LYS C  1 36  ? 12.634 3.531    -15.078  1.00 107.45 ? 37  LYS C CA  1 
ATOM   2480  C  C   . LYS C  1 36  ? 11.522 4.431    -15.645  1.00 109.20 ? 37  LYS C C   1 
ATOM   2481  O  O   . LYS C  1 36  ? 11.778 5.565    -16.058  1.00 107.64 ? 37  LYS C O   1 
ATOM   2482  C  CB  . LYS C  1 36  ? 12.379 3.184    -13.600  1.00 114.99 ? 37  LYS C CB  1 
ATOM   2483  C  CG  . LYS C  1 36  ? 12.532 4.341    -12.632  1.00 120.33 ? 37  LYS C CG  1 
ATOM   2484  C  CD  . LYS C  1 36  ? 11.787 4.031    -11.319  1.00 129.91 ? 37  LYS C CD  1 
ATOM   2485  C  CE  . LYS C  1 36  ? 11.981 5.119    -10.248  1.00 136.17 ? 37  LYS C CE  1 
ATOM   2486  N  NZ  . LYS C  1 36  ? 11.054 4.950    -9.071   1.00 145.82 ? 37  LYS C NZ  1 
ATOM   2487  N  N   . GLY C  1 37  ? 10.302 3.883    -15.671  1.00 113.01 ? 38  GLY C N   1 
ATOM   2488  C  CA  . GLY C  1 37  ? 9.124  4.557    -16.251  1.00 115.87 ? 38  GLY C CA  1 
ATOM   2489  C  C   . GLY C  1 37  ? 9.082  4.435    -17.769  1.00 109.75 ? 38  GLY C C   1 
ATOM   2490  O  O   . GLY C  1 37  ? 8.347  5.185    -18.449  1.00 111.02 ? 38  GLY C O   1 
ATOM   2491  N  N   . LEU C  1 38  ? 9.867  3.480    -18.290  1.00 103.72 ? 39  LEU C N   1 
ATOM   2492  C  CA  . LEU C  1 38  ? 10.074 3.308    -19.743  1.00 97.49  ? 39  LEU C CA  1 
ATOM   2493  C  C   . LEU C  1 38  ? 9.049  2.353    -20.390  1.00 98.34  ? 39  LEU C C   1 
ATOM   2494  O  O   . LEU C  1 38  ? 8.683  1.324    -19.801  1.00 101.02 ? 39  LEU C O   1 
ATOM   2495  C  CB  . LEU C  1 38  ? 11.507 2.801    -20.033  1.00 91.04  ? 39  LEU C CB  1 
ATOM   2496  C  CG  . LEU C  1 38  ? 12.609 3.869    -20.093  1.00 88.02  ? 39  LEU C CG  1 
ATOM   2497  C  CD1 . LEU C  1 38  ? 13.996 3.204    -19.978  1.00 83.59  ? 39  LEU C CD1 1 
ATOM   2498  C  CD2 . LEU C  1 38  ? 12.481 4.737    -21.383  1.00 84.99  ? 39  LEU C CD2 1 
ATOM   2499  N  N   . THR C  1 39  ? 8.610  2.700    -21.603  1.00 96.34  ? 40  THR C N   1 
ATOM   2500  C  CA  . THR C  1 39  ? 7.732  1.821    -22.381  1.00 96.83  ? 40  THR C CA  1 
ATOM   2501  C  C   . THR C  1 39  ? 8.535  0.545    -22.697  1.00 92.04  ? 40  THR C C   1 
ATOM   2502  O  O   . THR C  1 39  ? 9.719  0.620    -23.045  1.00 86.71  ? 40  THR C O   1 
ATOM   2503  C  CB  . THR C  1 39  ? 7.206  2.490    -23.678  1.00 95.98  ? 40  THR C CB  1 
ATOM   2504  O  OG1 . THR C  1 39  ? 7.897  1.973    -24.813  1.00 90.12  ? 40  THR C OG1 1 
ATOM   2505  C  CG2 . THR C  1 39  ? 7.374  3.996    -23.638  1.00 97.13  ? 40  THR C CG2 1 
ATOM   2506  N  N   . GLU C  1 40  ? 7.918  -0.627   -22.541  1.00 94.70  ? 41  GLU C N   1 
ATOM   2507  C  CA  . GLU C  1 40  ? 8.649  -1.902   -22.693  1.00 91.37  ? 41  GLU C CA  1 
ATOM   2508  C  C   . GLU C  1 40  ? 9.335  -1.966   -24.053  1.00 85.10  ? 41  GLU C C   1 
ATOM   2509  O  O   . GLU C  1 40  ? 8.740  -1.625   -25.090  1.00 84.54  ? 41  GLU C O   1 
ATOM   2510  C  CB  . GLU C  1 40  ? 7.732  -3.125   -22.543  1.00 95.69  ? 41  GLU C CB  1 
ATOM   2511  C  CG  . GLU C  1 40  ? 8.468  -4.479   -22.775  1.00 93.22  ? 41  GLU C CG  1 
ATOM   2512  C  CD  . GLU C  1 40  ? 7.543  -5.709   -22.754  1.00 98.10  ? 41  GLU C CD  1 
ATOM   2513  O  OE1 . GLU C  1 40  ? 6.481  -5.672   -23.432  1.00 100.13 ? 41  GLU C OE1 1 
ATOM   2514  O  OE2 . GLU C  1 40  ? 7.891  -6.718   -22.073  1.00 99.65  ? 41  GLU C OE2 1 
ATOM   2515  N  N   . GLY C  1 41  ? 10.588 -2.410   -24.034  1.00 81.03  ? 42  GLY C N   1 
ATOM   2516  C  CA  . GLY C  1 41  ? 11.338 -2.651   -25.267  1.00 75.84  ? 42  GLY C CA  1 
ATOM   2517  C  C   . GLY C  1 41  ? 12.604 -1.833   -25.396  1.00 71.57  ? 42  GLY C C   1 
ATOM   2518  O  O   . GLY C  1 41  ? 13.188 -1.412   -24.396  1.00 72.16  ? 42  GLY C O   1 
ATOM   2519  N  N   . LEU C  1 42  ? 13.029 -1.631   -26.643  1.00 67.70  ? 43  LEU C N   1 
ATOM   2520  C  CA  . LEU C  1 42  ? 14.268 -0.915   -26.937  1.00 63.80  ? 43  LEU C CA  1 
ATOM   2521  C  C   . LEU C  1 42  ? 14.108 0.591    -26.876  1.00 64.20  ? 43  LEU C C   1 
ATOM   2522  O  O   . LEU C  1 42  ? 13.093 1.141    -27.277  1.00 66.36  ? 43  LEU C O   1 
ATOM   2523  C  CB  . LEU C  1 42  ? 14.799 -1.285   -28.325  1.00 60.36  ? 43  LEU C CB  1 
ATOM   2524  C  CG  . LEU C  1 42  ? 15.490 -2.646   -28.452  1.00 59.37  ? 43  LEU C CG  1 
ATOM   2525  C  CD1 . LEU C  1 42  ? 14.656 -3.647   -29.280  1.00 60.62  ? 43  LEU C CD1 1 
ATOM   2526  C  CD2 . LEU C  1 42  ? 16.873 -2.465   -29.071  1.00 56.03  ? 43  LEU C CD2 1 
ATOM   2527  N  N   . HIS C  1 43  ? 15.143 1.257    -26.397  1.00 62.72  ? 44  HIS C N   1 
ATOM   2528  C  CA  . HIS C  1 43  ? 15.173 2.706    -26.391  1.00 63.19  ? 44  HIS C CA  1 
ATOM   2529  C  C   . HIS C  1 43  ? 16.534 3.255    -26.807  1.00 59.69  ? 44  HIS C C   1 
ATOM   2530  O  O   . HIS C  1 43  ? 17.580 2.770    -26.358  1.00 58.22  ? 44  HIS C O   1 
ATOM   2531  C  CB  . HIS C  1 43  ? 14.809 3.230    -25.013  1.00 67.23  ? 44  HIS C CB  1 
ATOM   2532  C  CG  . HIS C  1 43  ? 13.359 3.071    -24.678  1.00 71.90  ? 44  HIS C CG  1 
ATOM   2533  N  ND1 . HIS C  1 43  ? 12.382 3.936    -25.137  1.00 74.74  ? 44  HIS C ND1 1 
ATOM   2534  C  CD2 . HIS C  1 43  ? 12.719 2.147    -23.922  1.00 75.07  ? 44  HIS C CD2 1 
ATOM   2535  C  CE1 . HIS C  1 43  ? 11.203 3.553    -24.673  1.00 79.31  ? 44  HIS C CE1 1 
ATOM   2536  N  NE2 . HIS C  1 43  ? 11.381 2.468    -23.937  1.00 79.60  ? 44  HIS C NE2 1 
ATOM   2537  N  N   . GLY C  1 44  ? 16.496 4.280    -27.658  1.00 58.87  ? 45  GLY C N   1 
ATOM   2538  C  CA  . GLY C  1 44  ? 17.693 4.989    -28.075  1.00 56.39  ? 45  GLY C CA  1 
ATOM   2539  C  C   . GLY C  1 44  ? 18.371 5.655    -26.897  1.00 57.64  ? 45  GLY C C   1 
ATOM   2540  O  O   . GLY C  1 44  ? 17.719 6.080    -25.963  1.00 61.20  ? 45  GLY C O   1 
ATOM   2541  N  N   . PHE C  1 45  ? 19.685 5.772    -26.954  1.00 55.52  ? 46  PHE C N   1 
ATOM   2542  C  CA  . PHE C  1 45  ? 20.467 6.154    -25.794  1.00 56.95  ? 46  PHE C CA  1 
ATOM   2543  C  C   . PHE C  1 45  ? 21.764 6.810    -26.207  1.00 55.40  ? 46  PHE C C   1 
ATOM   2544  O  O   . PHE C  1 45  ? 22.750 6.124    -26.513  1.00 53.49  ? 46  PHE C O   1 
ATOM   2545  C  CB  . PHE C  1 45  ? 20.778 4.905    -24.998  1.00 57.41  ? 46  PHE C CB  1 
ATOM   2546  C  CG  . PHE C  1 45  ? 21.374 5.166    -23.651  1.00 60.14  ? 46  PHE C CG  1 
ATOM   2547  C  CD1 . PHE C  1 45  ? 20.764 6.045    -22.759  1.00 63.67  ? 46  PHE C CD1 1 
ATOM   2548  C  CD2 . PHE C  1 45  ? 22.521 4.472    -23.240  1.00 59.94  ? 46  PHE C CD2 1 
ATOM   2549  C  CE1 . PHE C  1 45  ? 21.309 6.256    -21.496  1.00 66.88  ? 46  PHE C CE1 1 
ATOM   2550  C  CE2 . PHE C  1 45  ? 23.069 4.673    -21.977  1.00 63.16  ? 46  PHE C CE2 1 
ATOM   2551  C  CZ  . PHE C  1 45  ? 22.468 5.567    -21.103  1.00 66.59  ? 46  PHE C CZ  1 
ATOM   2552  N  N   . HIS C  1 46  ? 21.770 8.140    -26.195  1.00 56.90  ? 47  HIS C N   1 
ATOM   2553  C  CA  . HIS C  1 46  ? 22.881 8.920    -26.767  1.00 55.86  ? 47  HIS C CA  1 
ATOM   2554  C  C   . HIS C  1 46  ? 23.398 10.084   -25.912  1.00 58.59  ? 47  HIS C C   1 
ATOM   2555  O  O   . HIS C  1 46  ? 22.661 10.690   -25.158  1.00 61.81  ? 47  HIS C O   1 
ATOM   2556  C  CB  . HIS C  1 46  ? 22.467 9.478    -28.122  1.00 54.78  ? 47  HIS C CB  1 
ATOM   2557  C  CG  . HIS C  1 46  ? 21.653 8.529    -28.938  1.00 53.04  ? 47  HIS C CG  1 
ATOM   2558  N  ND1 . HIS C  1 46  ? 20.298 8.678    -29.110  1.00 54.93  ? 47  HIS C ND1 1 
ATOM   2559  C  CD2 . HIS C  1 46  ? 21.997 7.414    -29.624  1.00 51.04  ? 47  HIS C CD2 1 
ATOM   2560  C  CE1 . HIS C  1 46  ? 19.839 7.707    -29.878  1.00 53.43  ? 47  HIS C CE1 1 
ATOM   2561  N  NE2 . HIS C  1 46  ? 20.850 6.923    -30.203  1.00 51.00  ? 47  HIS C NE2 1 
ATOM   2562  N  N   . VAL C  1 47  ? 24.677 10.392   -26.071  1.00 57.88  ? 48  VAL C N   1 
ATOM   2563  C  CA  . VAL C  1 47  ? 25.242 11.581   -25.495  1.00 60.58  ? 48  VAL C CA  1 
ATOM   2564  C  C   . VAL C  1 47  ? 25.092 12.682   -26.518  1.00 60.99  ? 48  VAL C C   1 
ATOM   2565  O  O   . VAL C  1 47  ? 25.590 12.560   -27.633  1.00 58.74  ? 48  VAL C O   1 
ATOM   2566  C  CB  . VAL C  1 47  ? 26.711 11.398   -25.175  1.00 60.57  ? 48  VAL C CB  1 
ATOM   2567  C  CG1 . VAL C  1 47  ? 27.351 12.723   -24.775  1.00 63.59  ? 48  VAL C CG1 1 
ATOM   2568  C  CG2 . VAL C  1 47  ? 26.859 10.397   -24.073  1.00 61.74  ? 48  VAL C CG2 1 
ATOM   2569  N  N   . HIS C  1 48  ? 24.394 13.750   -26.138  1.00 64.48  ? 49  HIS C N   1 
ATOM   2570  C  CA  . HIS C  1 48  ? 24.233 14.930   -26.992  1.00 66.11  ? 49  HIS C CA  1 
ATOM   2571  C  C   . HIS C  1 48  ? 25.270 16.019   -26.693  1.00 68.70  ? 49  HIS C C   1 
ATOM   2572  O  O   . HIS C  1 48  ? 25.933 16.003   -25.652  1.00 69.97  ? 49  HIS C O   1 
ATOM   2573  C  CB  . HIS C  1 48  ? 22.848 15.510   -26.834  1.00 69.37  ? 49  HIS C CB  1 
ATOM   2574  C  CG  . HIS C  1 48  ? 21.779 14.654   -27.407  1.00 67.59  ? 49  HIS C CG  1 
ATOM   2575  N  ND1 . HIS C  1 48  ? 20.891 15.114   -28.353  1.00 69.01  ? 49  HIS C ND1 1 
ATOM   2576  C  CD2 . HIS C  1 48  ? 21.446 13.368   -27.166  1.00 64.91  ? 49  HIS C CD2 1 
ATOM   2577  C  CE1 . HIS C  1 48  ? 20.045 14.152   -28.666  1.00 67.38  ? 49  HIS C CE1 1 
ATOM   2578  N  NE2 . HIS C  1 48  ? 20.359 13.084   -27.955  1.00 65.07  ? 49  HIS C NE2 1 
ATOM   2579  N  N   . GLU C  1 49  ? 25.383 16.973   -27.621  1.00 70.02  ? 50  GLU C N   1 
ATOM   2580  C  CA  . GLU C  1 49  ? 26.493 17.939   -27.628  1.00 72.17  ? 50  GLU C CA  1 
ATOM   2581  C  C   . GLU C  1 49  ? 26.520 18.842   -26.404  1.00 76.64  ? 50  GLU C C   1 
ATOM   2582  O  O   . GLU C  1 49  ? 27.536 18.936   -25.714  1.00 77.51  ? 50  GLU C O   1 
ATOM   2583  C  CB  . GLU C  1 49  ? 26.458 18.801   -28.901  1.00 73.51  ? 50  GLU C CB  1 
ATOM   2584  C  CG  . GLU C  1 49  ? 27.719 19.677   -29.087  1.00 75.64  ? 50  GLU C CG  1 
ATOM   2585  C  CD  . GLU C  1 49  ? 27.792 20.340   -30.446  1.00 76.74  ? 50  GLU C CD  1 
ATOM   2586  O  OE1 . GLU C  1 49  ? 27.031 19.940   -31.364  1.00 74.83  ? 50  GLU C OE1 1 
ATOM   2587  O  OE2 . GLU C  1 49  ? 28.622 21.260   -30.581  1.00 79.88  ? 50  GLU C OE2 1 
ATOM   2588  N  N   . PHE C  1 50  ? 25.398 19.499   -26.140  1.00 80.09  ? 51  PHE C N   1 
ATOM   2589  C  CA  . PHE C  1 50  ? 25.360 20.549   -25.124  1.00 85.68  ? 51  PHE C CA  1 
ATOM   2590  C  C   . PHE C  1 50  ? 24.780 20.127   -23.788  1.00 87.55  ? 51  PHE C C   1 
ATOM   2591  O  O   . PHE C  1 50  ? 23.737 19.464   -23.738  1.00 86.52  ? 51  PHE C O   1 
ATOM   2592  C  CB  . PHE C  1 50  ? 24.571 21.739   -25.641  1.00 90.02  ? 51  PHE C CB  1 
ATOM   2593  C  CG  . PHE C  1 50  ? 25.066 22.245   -26.951  1.00 89.57  ? 51  PHE C CG  1 
ATOM   2594  C  CD1 . PHE C  1 50  ? 26.393 22.669   -27.097  1.00 89.75  ? 51  PHE C CD1 1 
ATOM   2595  C  CD2 . PHE C  1 50  ? 24.220 22.290   -28.051  1.00 89.64  ? 51  PHE C CD2 1 
ATOM   2596  C  CE1 . PHE C  1 50  ? 26.867 23.124   -28.315  1.00 89.86  ? 51  PHE C CE1 1 
ATOM   2597  C  CE2 . PHE C  1 50  ? 24.679 22.758   -29.276  1.00 89.72  ? 51  PHE C CE2 1 
ATOM   2598  C  CZ  . PHE C  1 50  ? 26.012 23.172   -29.410  1.00 89.83  ? 51  PHE C CZ  1 
ATOM   2599  N  N   . GLY C  1 51  ? 25.456 20.553   -22.713  1.00 90.95  ? 52  GLY C N   1 
ATOM   2600  C  CA  . GLY C  1 51  ? 24.932 20.458   -21.333  1.00 94.82  ? 52  GLY C CA  1 
ATOM   2601  C  C   . GLY C  1 51  ? 23.936 21.586   -20.997  1.00 101.26 ? 52  GLY C C   1 
ATOM   2602  O  O   . GLY C  1 51  ? 23.943 22.164   -19.899  1.00 106.66 ? 52  GLY C O   1 
ATOM   2603  N  N   . ASP C  1 52  ? 23.066 21.881   -21.958  1.00 101.15 ? 53  ASP C N   1 
ATOM   2604  C  CA  . ASP C  1 52  ? 22.123 22.969   -21.858  1.00 107.64 ? 53  ASP C CA  1 
ATOM   2605  C  C   . ASP C  1 52  ? 20.751 22.395   -21.599  1.00 108.80 ? 53  ASP C C   1 
ATOM   2606  O  O   . ASP C  1 52  ? 20.228 21.622   -22.409  1.00 104.60 ? 53  ASP C O   1 
ATOM   2607  C  CB  . ASP C  1 52  ? 22.113 23.747   -23.174  1.00 107.97 ? 53  ASP C CB  1 
ATOM   2608  C  CG  . ASP C  1 52  ? 21.333 25.026   -23.090  1.00 115.88 ? 53  ASP C CG  1 
ATOM   2609  O  OD1 . ASP C  1 52  ? 20.318 25.026   -22.374  1.00 120.19 ? 53  ASP C OD1 1 
ATOM   2610  O  OD2 . ASP C  1 52  ? 21.737 26.018   -23.746  1.00 118.32 ? 53  ASP C OD2 1 
ATOM   2611  N  N   . ASN C  1 53  ? 20.166 22.794   -20.471  1.00 115.29 ? 54  ASN C N   1 
ATOM   2612  C  CA  . ASN C  1 53  ? 18.810 22.337   -20.074  1.00 118.09 ? 54  ASN C CA  1 
ATOM   2613  C  C   . ASN C  1 53  ? 17.773 23.473   -20.029  1.00 126.15 ? 54  ASN C C   1 
ATOM   2614  O  O   . ASN C  1 53  ? 16.666 23.309   -19.524  1.00 130.24 ? 54  ASN C O   1 
ATOM   2615  C  CB  . ASN C  1 53  ? 18.880 21.618   -18.714  1.00 119.27 ? 54  ASN C CB  1 
ATOM   2616  C  CG  . ASN C  1 53  ? 18.174 20.270   -18.739  1.00 115.88 ? 54  ASN C CG  1 
ATOM   2617  O  OD1 . ASN C  1 53  ? 18.625 19.332   -19.423  1.00 109.22 ? 54  ASN C OD1 1 
ATOM   2618  N  ND2 . ASN C  1 53  ? 17.067 20.162   -17.998  1.00 121.22 ? 54  ASN C ND2 1 
ATOM   2619  N  N   . THR C  1 54  ? 18.173 24.610   -20.583  1.00 128.73 ? 55  THR C N   1 
ATOM   2620  C  CA  . THR C  1 54  ? 17.375 25.835   -20.618  1.00 137.55 ? 55  THR C CA  1 
ATOM   2621  C  C   . THR C  1 54  ? 15.915 25.561   -20.977  1.00 140.26 ? 55  THR C C   1 
ATOM   2622  O  O   . THR C  1 54  ? 15.006 25.726   -20.151  1.00 147.00 ? 55  THR C O   1 
ATOM   2623  C  CB  . THR C  1 54  ? 17.981 26.843   -21.668  1.00 138.06 ? 55  THR C CB  1 
ATOM   2624  O  OG1 . THR C  1 54  ? 19.216 27.361   -21.145  1.00 138.51 ? 55  THR C OG1 1 
ATOM   2625  C  CG2 . THR C  1 54  ? 17.007 28.008   -22.046  1.00 146.86 ? 55  THR C CG2 1 
ATOM   2626  N  N   . ALA C  1 55  ? 15.717 25.144   -22.222  1.00 135.46 ? 56  ALA C N   1 
ATOM   2627  C  CA  . ALA C  1 55  ? 14.394 24.824   -22.749  1.00 137.63 ? 56  ALA C CA  1 
ATOM   2628  C  C   . ALA C  1 55  ? 14.227 23.292   -22.794  1.00 130.28 ? 56  ALA C C   1 
ATOM   2629  O  O   . ALA C  1 55  ? 13.883 22.702   -23.830  1.00 126.18 ? 56  ALA C O   1 
ATOM   2630  C  CB  . ALA C  1 55  ? 14.185 25.462   -24.141  1.00 138.67 ? 56  ALA C CB  1 
ATOM   2631  N  N   . GLY C  1 56  ? 14.496 22.667   -21.644  1.00 129.28 ? 57  GLY C N   1 
ATOM   2632  C  CA  . GLY C  1 56  ? 14.255 21.228   -21.430  1.00 124.17 ? 57  GLY C CA  1 
ATOM   2633  C  C   . GLY C  1 56  ? 15.363 20.372   -22.000  1.00 114.83 ? 57  GLY C C   1 
ATOM   2634  O  O   . GLY C  1 56  ? 16.540 20.789   -22.000  1.00 112.73 ? 57  GLY C O   1 
ATOM   2635  N  N   . CYS C  1 57  ? 14.986 19.189   -22.499  1.00 109.84 ? 58  CYS C N   1 
ATOM   2636  C  CA  . CYS C  1 57  ? 15.919 18.313   -23.219  1.00 101.35 ? 58  CYS C CA  1 
ATOM   2637  C  C   . CYS C  1 57  ? 16.267 18.847   -24.625  1.00 99.14  ? 58  CYS C C   1 
ATOM   2638  O  O   . CYS C  1 57  ? 17.376 18.612   -25.112  1.00 94.13  ? 58  CYS C O   1 
ATOM   2639  C  CB  . CYS C  1 57  ? 15.379 16.884   -23.331  1.00 97.48  ? 58  CYS C CB  1 
ATOM   2640  S  SG  . CYS C  1 57  ? 15.310 15.928   -21.783  1.00 98.42  ? 58  CYS C SG  1 
ATOM   2641  N  N   . THR C  1 58  ? 15.362 19.585   -25.260  1.00 103.63 ? 59  THR C N   1 
ATOM   2642  C  CA  . THR C  1 58  ? 15.606 20.068   -26.624  1.00 102.45 ? 59  THR C CA  1 
ATOM   2643  C  C   . THR C  1 58  ? 16.881 20.907   -26.748  1.00 101.74 ? 59  THR C C   1 
ATOM   2644  O  O   . THR C  1 58  ? 17.544 20.895   -27.785  1.00 98.22  ? 59  THR C O   1 
ATOM   2645  C  CB  . THR C  1 58  ? 14.449 20.932   -27.118  1.00 109.66 ? 59  THR C CB  1 
ATOM   2646  O  OG1 . THR C  1 58  ? 13.206 20.320   -26.736  1.00 112.40 ? 59  THR C OG1 1 
ATOM   2647  C  CG2 . THR C  1 58  ? 14.528 21.127   -28.661  1.00 107.99 ? 59  THR C CG2 1 
ATOM   2648  N  N   . SER C  1 59  ? 17.202 21.636   -25.681  1.00 105.83 ? 60  SER C N   1 
ATOM   2649  C  CA  . SER C  1 59  ? 18.367 22.539   -25.638  1.00 106.59 ? 60  SER C CA  1 
ATOM   2650  C  C   . SER C  1 59  ? 19.682 21.809   -25.777  1.00 99.54  ? 60  SER C C   1 
ATOM   2651  O  O   . SER C  1 59  ? 20.675 22.423   -26.154  1.00 99.38  ? 60  SER C O   1 
ATOM   2652  C  CB  . SER C  1 59  ? 18.414 23.323   -24.317  1.00 112.64 ? 60  SER C CB  1 
ATOM   2653  O  OG  . SER C  1 59  ? 17.143 23.837   -23.973  1.00 120.33 ? 60  SER C OG  1 
ATOM   2654  N  N   . ALA C  1 60  ? 19.691 20.511   -25.457  1.00 94.69  ? 61  ALA C N   1 
ATOM   2655  C  CA  . ALA C  1 60  ? 20.920 19.657   -25.539  1.00 88.51  ? 61  ALA C CA  1 
ATOM   2656  C  C   . ALA C  1 60  ? 21.544 19.581   -26.952  1.00 84.59  ? 61  ALA C C   1 
ATOM   2657  O  O   . ALA C  1 60  ? 22.723 19.201   -27.121  1.00 80.73  ? 61  ALA C O   1 
ATOM   2658  C  CB  . ALA C  1 60  ? 20.632 18.238   -25.014  1.00 84.79  ? 61  ALA C CB  1 
ATOM   2659  N  N   . GLY C  1 61  ? 20.743 19.958   -27.952  1.00 86.19  ? 62  GLY C N   1 
ATOM   2660  C  CA  . GLY C  1 61  ? 21.201 20.011   -29.330  1.00 83.97  ? 62  GLY C CA  1 
ATOM   2661  C  C   . GLY C  1 61  ? 21.263 18.610   -29.878  1.00 78.20  ? 62  GLY C C   1 
ATOM   2662  O  O   . GLY C  1 61  ? 20.598 17.727   -29.330  1.00 76.93  ? 62  GLY C O   1 
ATOM   2663  N  N   . PRO C  1 62  ? 22.083 18.388   -30.938  1.00 75.28  ? 63  PRO C N   1 
ATOM   2664  C  CA  . PRO C  1 62  ? 22.174 17.086   -31.610  1.00 70.30  ? 63  PRO C CA  1 
ATOM   2665  C  C   . PRO C  1 62  ? 23.121 16.087   -30.930  1.00 66.26  ? 63  PRO C C   1 
ATOM   2666  O  O   . PRO C  1 62  ? 23.705 16.363   -29.877  1.00 67.17  ? 63  PRO C O   1 
ATOM   2667  C  CB  . PRO C  1 62  ? 22.717 17.468   -32.987  1.00 70.32  ? 63  PRO C CB  1 
ATOM   2668  C  CG  . PRO C  1 62  ? 23.632 18.617   -32.695  1.00 73.03  ? 63  PRO C CG  1 
ATOM   2669  C  CD  . PRO C  1 62  ? 22.989 19.377   -31.566  1.00 77.04  ? 63  PRO C CD  1 
ATOM   2670  N  N   . HIS C  1 63  ? 23.252 14.932   -31.558  1.00 62.45  ? 64  HIS C N   1 
ATOM   2671  C  CA  . HIS C  1 63  ? 24.170 13.908   -31.112  1.00 59.31  ? 64  HIS C CA  1 
ATOM   2672  C  C   . HIS C  1 63  ? 25.591 14.473   -31.045  1.00 59.75  ? 64  HIS C C   1 
ATOM   2673  O  O   . HIS C  1 63  ? 26.015 15.192   -31.943  1.00 60.94  ? 64  HIS C O   1 
ATOM   2674  C  CB  . HIS C  1 63  ? 24.128 12.731   -32.088  1.00 56.28  ? 64  HIS C CB  1 
ATOM   2675  C  CG  . HIS C  1 63  ? 22.874 11.925   -32.016  1.00 55.47  ? 64  HIS C CG  1 
ATOM   2676  N  ND1 . HIS C  1 63  ? 22.857 10.566   -32.227  1.00 52.72  ? 64  HIS C ND1 1 
ATOM   2677  C  CD2 . HIS C  1 63  ? 21.598 12.279   -31.744  1.00 57.77  ? 64  HIS C CD2 1 
ATOM   2678  C  CE1 . HIS C  1 63  ? 21.622 10.117   -32.092  1.00 53.40  ? 64  HIS C CE1 1 
ATOM   2679  N  NE2 . HIS C  1 63  ? 20.839 11.136   -31.798  1.00 56.35  ? 64  HIS C NE2 1 
ATOM   2680  N  N   . PHE C  1 64  ? 26.328 14.146   -29.991  1.00 59.35  ? 65  PHE C N   1 
ATOM   2681  C  CA  . PHE C  1 64  ? 27.700 14.637   -29.852  1.00 60.45  ? 65  PHE C CA  1 
ATOM   2682  C  C   . PHE C  1 64  ? 28.554 14.058   -30.961  1.00 58.50  ? 65  PHE C C   1 
ATOM   2683  O  O   . PHE C  1 64  ? 28.737 12.847   -31.045  1.00 55.93  ? 65  PHE C O   1 
ATOM   2684  C  CB  . PHE C  1 64  ? 28.275 14.275   -28.480  1.00 61.21  ? 65  PHE C CB  1 
ATOM   2685  C  CG  . PHE C  1 64  ? 29.685 14.736   -28.254  1.00 62.77  ? 65  PHE C CG  1 
ATOM   2686  C  CD1 . PHE C  1 64  ? 30.086 15.996   -28.646  1.00 65.51  ? 65  PHE C CD1 1 
ATOM   2687  C  CD2 . PHE C  1 64  ? 30.604 13.914   -27.602  1.00 62.74  ? 65  PHE C CD2 1 
ATOM   2688  C  CE1 . PHE C  1 64  ? 31.390 16.419   -28.426  1.00 68.08  ? 65  PHE C CE1 1 
ATOM   2689  C  CE2 . PHE C  1 64  ? 31.908 14.330   -27.366  1.00 65.26  ? 65  PHE C CE2 1 
ATOM   2690  C  CZ  . PHE C  1 64  ? 32.308 15.581   -27.779  1.00 67.88  ? 65  PHE C CZ  1 
ATOM   2691  N  N   . ASN C  1 65  ? 29.080 14.940   -31.805  1.00 60.36  ? 66  ASN C N   1 
ATOM   2692  C  CA  . ASN C  1 65  ? 29.705 14.536   -33.072  1.00 59.51  ? 66  ASN C CA  1 
ATOM   2693  C  C   . ASN C  1 65  ? 30.906 15.394   -33.492  1.00 62.29  ? 66  ASN C C   1 
ATOM   2694  O  O   . ASN C  1 65  ? 30.867 16.058   -34.513  1.00 64.03  ? 66  ASN C O   1 
ATOM   2695  C  CB  . ASN C  1 65  ? 28.633 14.566   -34.163  1.00 59.10  ? 66  ASN C CB  1 
ATOM   2696  C  CG  . ASN C  1 65  ? 29.120 14.031   -35.465  1.00 58.43  ? 66  ASN C CG  1 
ATOM   2697  O  OD1 . ASN C  1 65  ? 30.197 13.456   -35.543  1.00 58.22  ? 66  ASN C OD1 1 
ATOM   2698  N  ND2 . ASN C  1 65  ? 28.330 14.215   -36.504  1.00 59.16  ? 66  ASN C ND2 1 
ATOM   2699  N  N   . PRO C  1 66  ? 31.994 15.360   -32.713  1.00 63.39  ? 67  PRO C N   1 
ATOM   2700  C  CA  . PRO C  1 66  ? 33.146 16.223   -32.961  1.00 66.74  ? 67  PRO C CA  1 
ATOM   2701  C  C   . PRO C  1 66  ? 33.970 15.820   -34.175  1.00 67.24  ? 67  PRO C C   1 
ATOM   2702  O  O   . PRO C  1 66  ? 34.669 16.660   -34.721  1.00 70.74  ? 67  PRO C O   1 
ATOM   2703  C  CB  . PRO C  1 66  ? 33.980 16.065   -31.687  1.00 67.79  ? 67  PRO C CB  1 
ATOM   2704  C  CG  . PRO C  1 66  ? 33.675 14.715   -31.215  1.00 64.75  ? 67  PRO C CG  1 
ATOM   2705  C  CD  . PRO C  1 66  ? 32.233 14.447   -31.585  1.00 62.11  ? 67  PRO C CD  1 
ATOM   2706  N  N   . LEU C  1 67  ? 33.903 14.555   -34.581  1.00 64.59  ? 68  LEU C N   1 
ATOM   2707  C  CA  . LEU C  1 67  ? 34.645 14.082   -35.748  1.00 65.47  ? 68  LEU C CA  1 
ATOM   2708  C  C   . LEU C  1 67  ? 33.822 14.182   -37.031  1.00 65.02  ? 68  LEU C C   1 
ATOM   2709  O  O   . LEU C  1 67  ? 34.187 13.637   -38.065  1.00 65.59  ? 68  LEU C O   1 
ATOM   2710  C  CB  . LEU C  1 67  ? 35.146 12.650   -35.515  1.00 64.11  ? 68  LEU C CB  1 
ATOM   2711  C  CG  . LEU C  1 67  ? 36.078 12.434   -34.309  1.00 65.66  ? 68  LEU C CG  1 
ATOM   2712  C  CD1 . LEU C  1 67  ? 36.715 11.024   -34.368  1.00 65.55  ? 68  LEU C CD1 1 
ATOM   2713  C  CD2 . LEU C  1 67  ? 37.169 13.526   -34.197  1.00 69.81  ? 68  LEU C CD2 1 
ATOM   2714  N  N   . SER C  1 68  ? 32.695 14.869   -36.949  1.00 64.70  ? 69  SER C N   1 
ATOM   2715  C  CA  . SER C  1 68  ? 31.894 15.217   -38.126  1.00 65.72  ? 69  SER C CA  1 
ATOM   2716  C  C   . SER C  1 68  ? 31.491 14.021   -38.984  1.00 63.64  ? 69  SER C C   1 
ATOM   2717  O  O   . SER C  1 68  ? 31.564 14.088   -40.207  1.00 65.59  ? 69  SER C O   1 
ATOM   2718  C  CB  . SER C  1 68  ? 32.648 16.222   -39.004  1.00 70.15  ? 69  SER C CB  1 
ATOM   2719  O  OG  . SER C  1 68  ? 33.273 17.231   -38.228  1.00 72.90  ? 69  SER C OG  1 
ATOM   2720  N  N   . ARG C  1 69  ? 31.047 12.945   -38.343  1.00 60.32  ? 70  ARG C N   1 
ATOM   2721  C  CA  . ARG C  1 69  ? 30.663 11.721   -39.049  1.00 58.73  ? 70  ARG C CA  1 
ATOM   2722  C  C   . ARG C  1 69  ? 29.144 11.533   -39.105  1.00 57.13  ? 70  ARG C C   1 
ATOM   2723  O  O   . ARG C  1 69  ? 28.381 12.375   -38.627  1.00 57.64  ? 70  ARG C O   1 
ATOM   2724  C  CB  . ARG C  1 69  ? 31.332 10.503   -38.409  1.00 57.09  ? 70  ARG C CB  1 
ATOM   2725  C  CG  . ARG C  1 69  ? 32.844 10.624   -38.304  1.00 59.43  ? 70  ARG C CG  1 
ATOM   2726  C  CD  . ARG C  1 69  ? 33.551 9.281    -38.456  1.00 59.88  ? 70  ARG C CD  1 
ATOM   2727  N  NE  . ARG C  1 69  ? 34.728 9.141    -37.586  1.00 61.85  ? 70  ARG C NE  1 
ATOM   2728  C  CZ  . ARG C  1 69  ? 35.667 8.193    -37.710  1.00 64.52  ? 70  ARG C CZ  1 
ATOM   2729  N  NH1 . ARG C  1 69  ? 35.604 7.271    -38.683  1.00 64.65  ? 70  ARG C NH1 1 
ATOM   2730  N  NH2 . ARG C  1 69  ? 36.690 8.165    -36.854  1.00 66.62  ? 70  ARG C NH2 1 
ATOM   2731  N  N   . LYS C  1 70  ? 28.725 10.428   -39.723  1.00 55.89  ? 71  LYS C N   1 
ATOM   2732  C  CA  . LYS C  1 70  ? 27.312 10.044   -39.827  1.00 54.72  ? 71  LYS C CA  1 
ATOM   2733  C  C   . LYS C  1 70  ? 26.873 9.189    -38.645  1.00 51.82  ? 71  LYS C C   1 
ATOM   2734  O  O   . LYS C  1 70  ? 27.702 8.548    -38.001  1.00 50.58  ? 71  LYS C O   1 
ATOM   2735  C  CB  . LYS C  1 70  ? 27.077 9.235    -41.104  1.00 55.51  ? 71  LYS C CB  1 
ATOM   2736  C  CG  . LYS C  1 70  ? 27.494 9.915    -42.401  1.00 59.22  ? 71  LYS C CG  1 
ATOM   2737  C  CD  . LYS C  1 70  ? 26.315 10.633   -43.062  1.00 61.63  ? 71  LYS C CD  1 
ATOM   2738  C  CE  . LYS C  1 70  ? 26.688 11.229   -44.419  1.00 66.00  ? 71  LYS C CE  1 
ATOM   2739  N  NZ  . LYS C  1 70  ? 25.510 11.885   -45.069  1.00 68.74  ? 71  LYS C NZ  1 
ATOM   2740  N  N   . HIS C  1 71  ? 25.562 9.157    -38.389  1.00 51.35  ? 72  HIS C N   1 
ATOM   2741  C  CA  . HIS C  1 71  ? 25.006 8.364    -37.275  1.00 49.41  ? 72  HIS C CA  1 
ATOM   2742  C  C   . HIS C  1 71  ? 25.271 6.883    -37.500  1.00 47.85  ? 72  HIS C C   1 
ATOM   2743  O  O   . HIS C  1 71  ? 25.426 6.437    -38.634  1.00 48.41  ? 72  HIS C O   1 
ATOM   2744  C  CB  . HIS C  1 71  ? 23.490 8.606    -37.063  1.00 50.11  ? 72  HIS C CB  1 
ATOM   2745  C  CG  . HIS C  1 71  ? 22.907 7.861    -35.887  1.00 48.80  ? 72  HIS C CG  1 
ATOM   2746  N  ND1 . HIS C  1 71  ? 23.184 8.192    -34.579  1.00 48.53  ? 72  HIS C ND1 1 
ATOM   2747  C  CD2 . HIS C  1 71  ? 22.074 6.794    -35.832  1.00 47.96  ? 72  HIS C CD2 1 
ATOM   2748  C  CE1 . HIS C  1 71  ? 22.552 7.359    -33.773  1.00 47.86  ? 72  HIS C CE1 1 
ATOM   2749  N  NE2 . HIS C  1 71  ? 21.868 6.504    -34.507  1.00 47.14  ? 72  HIS C NE2 1 
ATOM   2750  N  N   . GLY C  1 72  ? 25.336 6.139    -36.402  1.00 46.52  ? 73  GLY C N   1 
ATOM   2751  C  CA  . GLY C  1 72  ? 25.495 4.696    -36.460  1.00 45.71  ? 73  GLY C CA  1 
ATOM   2752  C  C   . GLY C  1 72  ? 25.312 3.997    -35.130  1.00 44.91  ? 73  GLY C C   1 
ATOM   2753  O  O   . GLY C  1 72  ? 24.983 4.605    -34.119  1.00 45.04  ? 73  GLY C O   1 
ATOM   2754  N  N   . GLY C  1 73  ? 25.538 2.699    -35.146  1.00 44.84  ? 74  GLY C N   1 
ATOM   2755  C  CA  . GLY C  1 73  ? 25.533 1.903    -33.933  1.00 45.03  ? 74  GLY C CA  1 
ATOM   2756  C  C   . GLY C  1 73  ? 26.868 2.010    -33.229  1.00 45.83  ? 74  GLY C C   1 
ATOM   2757  O  O   . GLY C  1 73  ? 27.837 2.377    -33.832  1.00 46.60  ? 74  GLY C O   1 
ATOM   2758  N  N   . PRO C  1 74  ? 26.937 1.678    -31.945  1.00 46.60  ? 75  PRO C N   1 
ATOM   2759  C  CA  . PRO C  1 74  ? 28.185 1.856    -31.212  1.00 48.14  ? 75  PRO C CA  1 
ATOM   2760  C  C   . PRO C  1 74  ? 29.316 1.006    -31.742  1.00 49.59  ? 75  PRO C C   1 
ATOM   2761  O  O   . PRO C  1 74  ? 30.448 1.442    -31.757  1.00 51.14  ? 75  PRO C O   1 
ATOM   2762  C  CB  . PRO C  1 74  ? 27.823 1.437    -29.785  1.00 49.31  ? 75  PRO C CB  1 
ATOM   2763  C  CG  . PRO C  1 74  ? 26.607 0.621    -29.912  1.00 48.79  ? 75  PRO C CG  1 
ATOM   2764  C  CD  . PRO C  1 74  ? 25.875 1.114    -31.105  1.00 46.89  ? 75  PRO C CD  1 
ATOM   2765  N  N   . LYS C  1 75  ? 29.008 -0.195   -32.184  1.00 49.97  ? 76  LYS C N   1 
ATOM   2766  C  CA  . LYS C  1 75  ? 30.021 -1.075   -32.745  1.00 52.37  ? 76  LYS C CA  1 
ATOM   2767  C  C   . LYS C  1 75  ? 30.505 -0.613   -34.104  1.00 52.27  ? 76  LYS C C   1 
ATOM   2768  O  O   . LYS C  1 75  ? 31.599 -0.946   -34.509  1.00 54.78  ? 76  LYS C O   1 
ATOM   2769  C  CB  . LYS C  1 75  ? 29.479 -2.490   -32.926  1.00 53.54  ? 76  LYS C CB  1 
ATOM   2770  C  CG  . LYS C  1 75  ? 28.782 -3.098   -31.732  1.00 54.32  ? 76  LYS C CG  1 
ATOM   2771  C  CD  . LYS C  1 75  ? 28.836 -4.624   -31.834  1.00 57.24  ? 76  LYS C CD  1 
ATOM   2772  C  CE  . LYS C  1 75  ? 27.929 -5.316   -30.816  1.00 58.38  ? 76  LYS C CE  1 
ATOM   2773  N  NZ  . LYS C  1 75  ? 27.707 -6.797   -31.155  1.00 60.72  ? 76  LYS C NZ  1 
ATOM   2774  N  N   . ASP C  1 76  ? 29.656 0.088    -34.837  1.00 50.23  ? 77  ASP C N   1 
ATOM   2775  C  CA  . ASP C  1 76  ? 30.037 0.637    -36.138  1.00 50.71  ? 77  ASP C CA  1 
ATOM   2776  C  C   . ASP C  1 76  ? 31.223 1.586    -35.974  1.00 52.06  ? 77  ASP C C   1 
ATOM   2777  O  O   . ASP C  1 76  ? 31.345 2.298    -34.973  1.00 51.63  ? 77  ASP C O   1 
ATOM   2778  C  CB  . ASP C  1 76  ? 28.846 1.359    -36.808  1.00 48.89  ? 77  ASP C CB  1 
ATOM   2779  C  CG  . ASP C  1 76  ? 27.761 0.392    -37.299  1.00 48.65  ? 77  ASP C CG  1 
ATOM   2780  O  OD1 . ASP C  1 76  ? 28.088 -0.783   -37.568  1.00 50.42  ? 77  ASP C OD1 1 
ATOM   2781  O  OD2 . ASP C  1 76  ? 26.575 0.796    -37.412  1.00 47.65  ? 77  ASP C OD2 1 
ATOM   2782  N  N   . GLU C  1 77  ? 32.124 1.570    -36.943  1.00 54.42  ? 78  GLU C N   1 
ATOM   2783  C  CA  . GLU C  1 77  ? 33.222 2.539    -36.959  1.00 56.33  ? 78  GLU C CA  1 
ATOM   2784  C  C   . GLU C  1 77  ? 32.699 3.916    -37.353  1.00 54.78  ? 78  GLU C C   1 
ATOM   2785  O  O   . GLU C  1 77  ? 33.013 4.897    -36.705  1.00 54.82  ? 78  GLU C O   1 
ATOM   2786  C  CB  . GLU C  1 77  ? 34.330 2.126    -37.926  1.00 60.22  ? 78  GLU C CB  1 
ATOM   2787  C  CG  . GLU C  1 77  ? 35.247 3.305    -38.309  1.00 62.83  ? 78  GLU C CG  1 
ATOM   2788  C  CD  . GLU C  1 77  ? 36.571 2.874    -38.962  1.00 68.33  ? 78  GLU C CD  1 
ATOM   2789  O  OE1 . GLU C  1 77  ? 36.577 1.871    -39.723  1.00 69.94  ? 78  GLU C OE1 1 
ATOM   2790  O  OE2 . GLU C  1 77  ? 37.605 3.559    -38.713  1.00 71.18  ? 78  GLU C OE2 1 
ATOM   2791  N  N   . GLU C  1 78  ? 31.935 3.972    -38.444  1.00 54.16  ? 79  GLU C N   1 
ATOM   2792  C  CA  . GLU C  1 78  ? 31.228 5.193    -38.848  1.00 53.26  ? 79  GLU C CA  1 
ATOM   2793  C  C   . GLU C  1 78  ? 30.034 5.440    -37.914  1.00 50.56  ? 79  GLU C C   1 
ATOM   2794  O  O   . GLU C  1 78  ? 28.915 4.982    -38.157  1.00 49.19  ? 79  GLU C O   1 
ATOM   2795  C  CB  . GLU C  1 78  ? 30.770 5.123    -40.311  1.00 54.41  ? 79  GLU C CB  1 
ATOM   2796  C  CG  . GLU C  1 78  ? 30.164 6.442    -40.864  1.00 54.92  ? 79  GLU C CG  1 
ATOM   2797  C  CD  . GLU C  1 78  ? 31.188 7.537    -41.179  1.00 57.62  ? 79  GLU C CD  1 
ATOM   2798  O  OE1 . GLU C  1 78  ? 32.397 7.317    -41.001  1.00 59.54  ? 79  GLU C OE1 1 
ATOM   2799  O  OE2 . GLU C  1 78  ? 30.775 8.634    -41.602  1.00 58.47  ? 79  GLU C OE2 1 
ATOM   2800  N  N   . ARG C  1 79  ? 30.318 6.162    -36.833  1.00 50.38  ? 80  ARG C N   1 
ATOM   2801  C  CA  . ARG C  1 79  ? 29.331 6.551    -35.821  1.00 48.77  ? 80  ARG C CA  1 
ATOM   2802  C  C   . ARG C  1 79  ? 29.610 7.942    -35.271  1.00 49.80  ? 80  ARG C C   1 
ATOM   2803  O  O   . ARG C  1 79  ? 30.687 8.501    -35.476  1.00 51.61  ? 80  ARG C O   1 
ATOM   2804  C  CB  . ARG C  1 79  ? 29.364 5.571    -34.651  1.00 48.06  ? 80  ARG C CB  1 
ATOM   2805  C  CG  . ARG C  1 79  ? 30.728 5.428    -33.980  1.00 49.71  ? 80  ARG C CG  1 
ATOM   2806  C  CD  . ARG C  1 79  ? 30.669 4.610    -32.698  1.00 49.88  ? 80  ARG C CD  1 
ATOM   2807  N  NE  . ARG C  1 79  ? 30.318 5.421    -31.529  1.00 50.06  ? 80  ARG C NE  1 
ATOM   2808  C  CZ  . ARG C  1 79  ? 30.386 5.005    -30.262  1.00 50.99  ? 80  ARG C CZ  1 
ATOM   2809  N  NH1 . ARG C  1 79  ? 30.800 3.780    -29.963  1.00 51.90  ? 80  ARG C NH1 1 
ATOM   2810  N  NH2 . ARG C  1 79  ? 30.042 5.822    -29.276  1.00 51.89  ? 80  ARG C NH2 1 
ATOM   2811  N  N   . HIS C  1 80  ? 28.634 8.499    -34.567  1.00 49.32  ? 81  HIS C N   1 
ATOM   2812  C  CA  . HIS C  1 80  ? 28.873 9.702    -33.768  1.00 50.74  ? 81  HIS C CA  1 
ATOM   2813  C  C   . HIS C  1 80  ? 29.585 9.270    -32.504  1.00 50.99  ? 81  HIS C C   1 
ATOM   2814  O  O   . HIS C  1 80  ? 29.368 8.177    -32.016  1.00 50.01  ? 81  HIS C O   1 
ATOM   2815  C  CB  . HIS C  1 80  ? 27.576 10.418   -33.388  1.00 51.01  ? 81  HIS C CB  1 
ATOM   2816  C  CG  . HIS C  1 80  ? 26.783 10.916   -34.553  1.00 51.47  ? 81  HIS C CG  1 
ATOM   2817  N  ND1 . HIS C  1 80  ? 25.406 10.972   -34.544  1.00 51.47  ? 81  HIS C ND1 1 
ATOM   2818  C  CD2 . HIS C  1 80  ? 27.170 11.381   -35.763  1.00 52.63  ? 81  HIS C CD2 1 
ATOM   2819  C  CE1 . HIS C  1 80  ? 24.981 11.454   -35.697  1.00 52.89  ? 81  HIS C CE1 1 
ATOM   2820  N  NE2 . HIS C  1 80  ? 26.032 11.705   -36.456  1.00 53.48  ? 81  HIS C NE2 1 
ATOM   2821  N  N   . VAL C  1 81  ? 30.440 10.127   -31.973  1.00 52.97  ? 82  VAL C N   1 
ATOM   2822  C  CA  . VAL C  1 81  ? 31.123 9.822    -30.718  1.00 54.04  ? 82  VAL C CA  1 
ATOM   2823  C  C   . VAL C  1 81  ? 30.099 9.494    -29.649  1.00 53.32  ? 82  VAL C C   1 
ATOM   2824  O  O   . VAL C  1 81  ? 30.286 8.594    -28.854  1.00 53.50  ? 82  VAL C O   1 
ATOM   2825  C  CB  . VAL C  1 81  ? 32.016 10.996   -30.246  1.00 56.96  ? 82  VAL C CB  1 
ATOM   2826  C  CG1 . VAL C  1 81  ? 32.574 10.742   -28.859  1.00 58.55  ? 82  VAL C CG1 1 
ATOM   2827  C  CG2 . VAL C  1 81  ? 33.163 11.195   -31.207  1.00 58.53  ? 82  VAL C CG2 1 
ATOM   2828  N  N   . GLY C  1 82  ? 28.994 10.218   -29.652  1.00 53.29  ? 83  GLY C N   1 
ATOM   2829  C  CA  . GLY C  1 82  ? 27.958 10.051   -28.624  1.00 53.70  ? 83  GLY C CA  1 
ATOM   2830  C  C   . GLY C  1 82  ? 26.933 8.966    -28.855  1.00 51.72  ? 83  GLY C C   1 
ATOM   2831  O  O   . GLY C  1 82  ? 26.027 8.811    -28.056  1.00 52.43  ? 83  GLY C O   1 
ATOM   2832  N  N   . ASP C  1 83  ? 27.064 8.225    -29.947  1.00 49.85  ? 84  ASP C N   1 
ATOM   2833  C  CA  . ASP C  1 83  ? 26.110 7.171    -30.278  1.00 48.35  ? 84  ASP C CA  1 
ATOM   2834  C  C   . ASP C  1 83  ? 26.356 5.931    -29.436  1.00 48.49  ? 84  ASP C C   1 
ATOM   2835  O  O   . ASP C  1 83  ? 27.185 5.094    -29.794  1.00 48.20  ? 84  ASP C O   1 
ATOM   2836  C  CB  . ASP C  1 83  ? 26.210 6.791    -31.755  1.00 47.00  ? 84  ASP C CB  1 
ATOM   2837  C  CG  . ASP C  1 83  ? 25.613 7.824    -32.672  1.00 47.20  ? 84  ASP C CG  1 
ATOM   2838  O  OD1 . ASP C  1 83  ? 24.888 8.717    -32.209  1.00 48.14  ? 84  ASP C OD1 1 
ATOM   2839  O  OD2 . ASP C  1 83  ? 25.867 7.749    -33.885  1.00 47.05  ? 84  ASP C OD2 1 
ATOM   2840  N  N   . LEU C  1 84  ? 25.641 5.818    -28.318  1.00 49.67  ? 85  LEU C N   1 
ATOM   2841  C  CA  . LEU C  1 84  ? 25.768 4.654    -27.434  1.00 50.59  ? 85  LEU C CA  1 
ATOM   2842  C  C   . LEU C  1 84  ? 24.732 3.585    -27.728  1.00 49.88  ? 85  LEU C C   1 
ATOM   2843  O  O   . LEU C  1 84  ? 24.625 2.603    -27.007  1.00 51.14  ? 85  LEU C O   1 
ATOM   2844  C  CB  . LEU C  1 84  ? 25.705 5.063    -25.958  1.00 53.26  ? 85  LEU C CB  1 
ATOM   2845  C  CG  . LEU C  1 84  ? 26.989 5.692    -25.404  1.00 54.82  ? 85  LEU C CG  1 
ATOM   2846  C  CD1 . LEU C  1 84  ? 26.802 6.119    -23.961  1.00 57.83  ? 85  LEU C CD1 1 
ATOM   2847  C  CD2 . LEU C  1 84  ? 28.175 4.742    -25.525  1.00 54.83  ? 85  LEU C CD2 1 
ATOM   2848  N  N   . GLY C  1 85  ? 23.984 3.757    -28.805  1.00 48.53  ? 86  GLY C N   1 
ATOM   2849  C  CA  . GLY C  1 85  ? 23.064 2.714    -29.266  1.00 48.17  ? 86  GLY C CA  1 
ATOM   2850  C  C   . GLY C  1 85  ? 21.768 2.614    -28.479  1.00 49.78  ? 86  GLY C C   1 
ATOM   2851  O  O   . GLY C  1 85  ? 21.113 3.617    -28.250  1.00 51.03  ? 86  GLY C O   1 
ATOM   2852  N  N   . ASN C  1 86  ? 21.393 1.406    -28.069  1.00 50.58  ? 87  ASN C N   1 
ATOM   2853  C  CA  . ASN C  1 86  ? 20.103 1.186    -27.406  1.00 52.62  ? 87  ASN C CA  1 
ATOM   2854  C  C   . ASN C  1 86  ? 20.211 0.721    -25.977  1.00 55.19  ? 87  ASN C C   1 
ATOM   2855  O  O   . ASN C  1 86  ? 21.234 0.183    -25.575  1.00 55.38  ? 87  ASN C O   1 
ATOM   2856  C  CB  . ASN C  1 86  ? 19.280 0.166    -28.179  1.00 52.39  ? 87  ASN C CB  1 
ATOM   2857  C  CG  . ASN C  1 86  ? 18.661 0.751    -29.425  1.00 51.51  ? 87  ASN C CG  1 
ATOM   2858  O  OD1 . ASN C  1 86  ? 17.962 1.777    -29.380  1.00 52.79  ? 87  ASN C OD1 1 
ATOM   2859  N  ND2 . ASN C  1 86  ? 18.904 0.098    -30.553  1.00 50.25  ? 87  ASN C ND2 1 
ATOM   2860  N  N   . VAL C  1 87  ? 19.144 0.956    -25.220  1.00 57.91  ? 88  VAL C N   1 
ATOM   2861  C  CA  . VAL C  1 87  ? 18.961 0.356    -23.896  1.00 61.51  ? 88  VAL C CA  1 
ATOM   2862  C  C   . VAL C  1 87  ? 17.619 -0.366   -23.868  1.00 63.85  ? 88  VAL C C   1 
ATOM   2863  O  O   . VAL C  1 87  ? 16.634 0.112    -24.460  1.00 63.94  ? 88  VAL C O   1 
ATOM   2864  C  CB  . VAL C  1 87  ? 18.960 1.390    -22.769  1.00 64.27  ? 88  VAL C CB  1 
ATOM   2865  C  CG1 . VAL C  1 87  ? 20.348 2.007    -22.602  1.00 63.04  ? 88  VAL C CG1 1 
ATOM   2866  C  CG2 . VAL C  1 87  ? 17.904 2.448    -23.027  1.00 65.29  ? 88  VAL C CG2 1 
ATOM   2867  N  N   . THR C  1 88  ? 17.578 -1.507   -23.176  1.00 66.36  ? 89  THR C N   1 
ATOM   2868  C  CA  . THR C  1 88  ? 16.393 -2.381   -23.183  1.00 68.90  ? 89  THR C CA  1 
ATOM   2869  C  C   . THR C  1 88  ? 15.563 -2.307   -21.884  1.00 74.14  ? 89  THR C C   1 
ATOM   2870  O  O   . THR C  1 88  ? 16.061 -2.531   -20.767  1.00 76.77  ? 89  THR C O   1 
ATOM   2871  C  CB  . THR C  1 88  ? 16.770 -3.864   -23.493  1.00 68.78  ? 89  THR C CB  1 
ATOM   2872  O  OG1 . THR C  1 88  ? 17.280 -3.980   -24.831  1.00 64.81  ? 89  THR C OG1 1 
ATOM   2873  C  CG2 . THR C  1 88  ? 15.546 -4.783   -23.360  1.00 72.32  ? 89  THR C CG2 1 
ATOM   2874  N  N   . ALA C  1 89  ? 14.274 -2.032   -22.070  1.00 76.21  ? 90  ALA C N   1 
ATOM   2875  C  CA  . ALA C  1 89  ? 13.324 -1.897   -20.973  1.00 81.97  ? 90  ALA C CA  1 
ATOM   2876  C  C   . ALA C  1 89  ? 12.436 -3.149   -20.813  1.00 85.60  ? 90  ALA C C   1 
ATOM   2877  O  O   . ALA C  1 89  ? 11.781 -3.584   -21.776  1.00 84.69  ? 90  ALA C O   1 
ATOM   2878  C  CB  . ALA C  1 89  ? 12.442 -0.656   -21.203  1.00 83.28  ? 90  ALA C CB  1 
ATOM   2879  N  N   . ASP C  1 90  ? 12.395 -3.689   -19.587  1.00 90.35  ? 91  ASP C N   1 
ATOM   2880  C  CA  . ASP C  1 90  ? 11.568 -4.879   -19.251  1.00 94.92  ? 91  ASP C CA  1 
ATOM   2881  C  C   . ASP C  1 90  ? 10.128 -4.533   -18.804  1.00 100.66 ? 91  ASP C C   1 
ATOM   2882  O  O   . ASP C  1 90  ? 9.844  -3.400   -18.411  1.00 102.41 ? 91  ASP C O   1 
ATOM   2883  C  CB  . ASP C  1 90  ? 12.271 -5.782   -18.200  1.00 98.01  ? 91  ASP C CB  1 
ATOM   2884  C  CG  . ASP C  1 90  ? 12.268 -5.200   -16.762  1.00 103.25 ? 91  ASP C CG  1 
ATOM   2885  O  OD1 . ASP C  1 90  ? 12.878 -5.850   -15.886  1.00 106.35 ? 91  ASP C OD1 1 
ATOM   2886  O  OD2 . ASP C  1 90  ? 11.668 -4.127   -16.493  1.00 104.96 ? 91  ASP C OD2 1 
ATOM   2887  N  N   . LYS C  1 91  ? 9.245  -5.529   -18.883  1.00 104.15 ? 92  LYS C N   1 
ATOM   2888  C  CA  . LYS C  1 91  ? 7.795  -5.412   -18.542  1.00 110.59 ? 92  LYS C CA  1 
ATOM   2889  C  C   . LYS C  1 91  ? 7.405  -4.212   -17.689  1.00 114.59 ? 92  LYS C C   1 
ATOM   2890  O  O   . LYS C  1 91  ? 6.632  -3.341   -18.138  1.00 115.41 ? 92  LYS C O   1 
ATOM   2891  C  CB  . LYS C  1 91  ? 7.283  -6.654   -17.789  1.00 116.86 ? 92  LYS C CB  1 
ATOM   2892  C  CG  . LYS C  1 91  ? 8.038  -7.971   -18.011  1.00 115.20 ? 92  LYS C CG  1 
ATOM   2893  C  CD  . LYS C  1 91  ? 7.801  -8.545   -19.417  1.00 111.69 ? 92  LYS C CD  1 
ATOM   2894  C  CE  . LYS C  1 91  ? 8.102  -10.049  -19.474  1.00 112.88 ? 92  LYS C CE  1 
ATOM   2895  N  NZ  . LYS C  1 91  ? 6.928  -10.882  -19.124  1.00 119.97 ? 92  LYS C NZ  1 
ATOM   2896  N  N   . ASP C  1 92  ? 7.955  -4.186   -16.466  1.00 117.60 ? 93  ASP C N   1 
ATOM   2897  C  CA  . ASP C  1 92  ? 7.582  -3.184   -15.433  1.00 123.30 ? 93  ASP C CA  1 
ATOM   2898  C  C   . ASP C  1 92  ? 8.300  -1.827   -15.611  1.00 119.22 ? 93  ASP C C   1 
ATOM   2899  O  O   . ASP C  1 92  ? 8.359  -1.011   -14.681  1.00 123.32 ? 93  ASP C O   1 
ATOM   2900  C  CB  . ASP C  1 92  ? 7.745  -3.724   -13.973  1.00 129.94 ? 93  ASP C CB  1 
ATOM   2901  C  CG  . ASP C  1 92  ? 8.377  -5.136   -13.898  1.00 129.12 ? 93  ASP C CG  1 
ATOM   2902  O  OD1 . ASP C  1 92  ? 9.554  -5.276   -14.306  1.00 123.27 ? 93  ASP C OD1 1 
ATOM   2903  O  OD2 . ASP C  1 92  ? 7.698  -6.086   -13.424  1.00 134.74 ? 93  ASP C OD2 1 
ATOM   2904  N  N   . GLY C  1 93  ? 8.833  -1.607   -16.815  1.00 111.85 ? 94  GLY C N   1 
ATOM   2905  C  CA  . GLY C  1 93  ? 9.327  -0.296   -17.264  1.00 108.00 ? 94  GLY C CA  1 
ATOM   2906  C  C   . GLY C  1 93  ? 10.788 -0.040   -16.964  1.00 103.93 ? 94  GLY C C   1 
ATOM   2907  O  O   . GLY C  1 93  ? 11.324 1.015    -17.284  1.00 100.83 ? 94  GLY C O   1 
ATOM   2908  N  N   . VAL C  1 94  ? 11.422 -1.028   -16.354  1.00 104.51 ? 95  VAL C N   1 
ATOM   2909  C  CA  . VAL C  1 94  ? 12.768 -0.885   -15.844  1.00 103.23 ? 95  VAL C CA  1 
ATOM   2910  C  C   . VAL C  1 94  ? 13.767 -1.110   -16.986  1.00 95.87  ? 95  VAL C C   1 
ATOM   2911  O  O   . VAL C  1 94  ? 13.565 -1.975   -17.838  1.00 93.99  ? 95  VAL C O   1 
ATOM   2912  C  CB  . VAL C  1 94  ? 13.027 -1.930   -14.690  1.00 108.50 ? 95  VAL C CB  1 
ATOM   2913  C  CG1 . VAL C  1 94  ? 14.489 -1.854   -14.158  1.00 107.16 ? 95  VAL C CG1 1 
ATOM   2914  C  CG2 . VAL C  1 94  ? 11.956 -1.801   -13.552  1.00 116.86 ? 95  VAL C CG2 1 
ATOM   2915  N  N   . ALA C  1 95  ? 14.854 -0.355   -17.012  1.00 92.39  ? 96  ALA C N   1 
ATOM   2916  C  CA  . ALA C  1 95  ? 15.921 -0.651   -17.953  1.00 86.24  ? 96  ALA C CA  1 
ATOM   2917  C  C   . ALA C  1 95  ? 17.238 -0.716   -17.203  1.00 86.68  ? 96  ALA C C   1 
ATOM   2918  O  O   . ALA C  1 95  ? 17.758 0.308    -16.789  1.00 87.10  ? 96  ALA C O   1 
ATOM   2919  C  CB  . ALA C  1 95  ? 15.956 0.416    -19.029  1.00 81.76  ? 96  ALA C CB  1 
ATOM   2920  N  N   . ASP C  1 96  ? 17.763 -1.919   -17.009  1.00 87.33  ? 97  ASP C N   1 
ATOM   2921  C  CA  . ASP C  1 96  ? 19.002 -2.076   -16.237  1.00 89.24  ? 97  ASP C CA  1 
ATOM   2922  C  C   . ASP C  1 96  ? 20.212 -1.915   -17.125  1.00 84.13  ? 97  ASP C C   1 
ATOM   2923  O  O   . ASP C  1 96  ? 20.717 -2.905   -17.667  1.00 82.85  ? 97  ASP C O   1 
ATOM   2924  C  CB  . ASP C  1 96  ? 19.043 -3.425   -15.504  1.00 94.01  ? 97  ASP C CB  1 
ATOM   2925  C  CG  . ASP C  1 96  ? 18.252 -3.396   -14.176  1.00 101.69 ? 97  ASP C CG  1 
ATOM   2926  O  OD1 . ASP C  1 96  ? 18.499 -2.469   -13.349  1.00 104.42 ? 97  ASP C OD1 1 
ATOM   2927  O  OD2 . ASP C  1 96  ? 17.380 -4.288   -13.966  1.00 105.29 ? 97  ASP C OD2 1 
ATOM   2928  N  N   . VAL C  1 97  ? 20.688 -0.670   -17.240  1.00 82.07  ? 98  VAL C N   1 
ATOM   2929  C  CA  . VAL C  1 97  ? 21.756 -0.310   -18.189  1.00 77.25  ? 98  VAL C CA  1 
ATOM   2930  C  C   . VAL C  1 97  ? 23.119 -0.877   -17.800  1.00 78.62  ? 98  VAL C C   1 
ATOM   2931  O  O   . VAL C  1 97  ? 23.530 -0.757   -16.664  1.00 83.13  ? 98  VAL C O   1 
ATOM   2932  C  CB  . VAL C  1 97  ? 21.908 1.206    -18.317  1.00 75.75  ? 98  VAL C CB  1 
ATOM   2933  C  CG1 . VAL C  1 97  ? 22.956 1.530    -19.340  1.00 71.52  ? 98  VAL C CG1 1 
ATOM   2934  C  CG2 . VAL C  1 97  ? 20.592 1.839    -18.720  1.00 75.37  ? 98  VAL C CG2 1 
ATOM   2935  N  N   . SER C  1 98  ? 23.793 -1.515   -18.747  1.00 75.66  ? 99  SER C N   1 
ATOM   2936  C  CA  . SER C  1 98  ? 25.175 -1.990   -18.560  1.00 77.30  ? 99  SER C CA  1 
ATOM   2937  C  C   . SER C  1 98  ? 25.941 -2.056   -19.892  1.00 73.16  ? 99  SER C C   1 
ATOM   2938  O  O   . SER C  1 98  ? 26.107 -3.126   -20.529  1.00 72.62  ? 99  SER C O   1 
ATOM   2939  C  CB  . SER C  1 98  ? 25.233 -3.364   -17.876  1.00 81.93  ? 99  SER C CB  1 
ATOM   2940  O  OG  . SER C  1 98  ? 26.560 -3.876   -17.887  1.00 83.27  ? 99  SER C OG  1 
ATOM   2941  N  N   . ILE C  1 99  ? 26.445 -0.896   -20.285  1.00 70.80  ? 100 ILE C N   1 
ATOM   2942  C  CA  . ILE C  1 99  ? 27.215 -0.759   -21.524  1.00 67.30  ? 100 ILE C CA  1 
ATOM   2943  C  C   . ILE C  1 99  ? 28.722 -0.619   -21.228  1.00 69.56  ? 100 ILE C C   1 
ATOM   2944  O  O   . ILE C  1 99  ? 29.128 -0.215   -20.143  1.00 73.36  ? 100 ILE C O   1 
ATOM   2945  C  CB  . ILE C  1 99  ? 26.727 0.463    -22.319  1.00 63.27  ? 100 ILE C CB  1 
ATOM   2946  C  CG1 . ILE C  1 99  ? 25.282 0.274    -22.747  1.00 61.41  ? 100 ILE C CG1 1 
ATOM   2947  C  CG2 . ILE C  1 99  ? 27.604 0.679    -23.536  1.00 60.66  ? 100 ILE C CG2 1 
ATOM   2948  C  CD1 . ILE C  1 99  ? 24.880 1.166    -23.844  1.00 57.99  ? 100 ILE C CD1 1 
ATOM   2949  N  N   . GLU C  1 100 ? 29.549 -0.984   -22.181  1.00 68.18  ? 101 GLU C N   1 
ATOM   2950  C  CA  . GLU C  1 100 ? 30.953 -0.664   -22.094  1.00 70.40  ? 101 GLU C CA  1 
ATOM   2951  C  C   . GLU C  1 100 ? 31.391 -0.123   -23.459  1.00 66.96  ? 101 GLU C C   1 
ATOM   2952  O  O   . GLU C  1 100 ? 31.199 -0.774   -24.480  1.00 65.14  ? 101 GLU C O   1 
ATOM   2953  C  CB  . GLU C  1 100 ? 31.763 -1.892   -21.686  1.00 75.02  ? 101 GLU C CB  1 
ATOM   2954  C  CG  . GLU C  1 100 ? 33.254 -1.590   -21.477  1.00 79.16  ? 101 GLU C CG  1 
ATOM   2955  C  CD  . GLU C  1 100 ? 34.042 -2.768   -20.876  1.00 85.76  ? 101 GLU C CD  1 
ATOM   2956  O  OE1 . GLU C  1 100 ? 35.275 -2.586   -20.574  1.00 89.63  ? 101 GLU C OE1 1 
ATOM   2957  O  OE2 . GLU C  1 100 ? 33.421 -3.862   -20.718  1.00 86.93  ? 101 GLU C OE2 1 
ATOM   2958  N  N   . ASP C  1 101 ? 31.980 1.068    -23.483  1.00 66.72  ? 102 ASP C N   1 
ATOM   2959  C  CA  . ASP C  1 101 ? 32.278 1.746    -24.746  1.00 63.67  ? 102 ASP C CA  1 
ATOM   2960  C  C   . ASP C  1 101 ? 33.664 2.365    -24.803  1.00 66.01  ? 102 ASP C C   1 
ATOM   2961  O  O   . ASP C  1 101 ? 34.188 2.827    -23.801  1.00 69.08  ? 102 ASP C O   1 
ATOM   2962  C  CB  . ASP C  1 101 ? 31.255 2.830    -25.016  1.00 60.40  ? 102 ASP C CB  1 
ATOM   2963  C  CG  . ASP C  1 101 ? 31.284 3.287    -26.450  1.00 57.46  ? 102 ASP C CG  1 
ATOM   2964  O  OD1 . ASP C  1 101 ? 30.917 2.483    -27.342  1.00 55.57  ? 102 ASP C OD1 1 
ATOM   2965  O  OD2 . ASP C  1 101 ? 31.695 4.441    -26.687  1.00 57.31  ? 102 ASP C OD2 1 
ATOM   2966  N  N   . SER C  1 102 ? 34.229 2.385    -26.006  1.00 65.08  ? 103 SER C N   1 
ATOM   2967  C  CA  . SER C  1 102 ? 35.622 2.788    -26.239  1.00 68.02  ? 103 SER C CA  1 
ATOM   2968  C  C   . SER C  1 102 ? 35.792 4.092    -27.015  1.00 66.25  ? 103 SER C C   1 
ATOM   2969  O  O   . SER C  1 102 ? 36.893 4.638    -27.063  1.00 69.15  ? 103 SER C O   1 
ATOM   2970  C  CB  . SER C  1 102 ? 36.362 1.686    -27.000  1.00 70.00  ? 103 SER C CB  1 
ATOM   2971  O  OG  . SER C  1 102 ? 36.235 0.434    -26.349  1.00 72.52  ? 103 SER C OG  1 
ATOM   2972  N  N   . VAL C  1 103 ? 34.722 4.575    -27.639  1.00 62.25  ? 104 VAL C N   1 
ATOM   2973  C  CA  . VAL C  1 103 ? 34.771 5.831    -28.384  1.00 61.04  ? 104 VAL C CA  1 
ATOM   2974  C  C   . VAL C  1 103 ? 34.607 7.018    -27.444  1.00 61.98  ? 104 VAL C C   1 
ATOM   2975  O  O   . VAL C  1 103 ? 35.366 7.957    -27.525  1.00 63.99  ? 104 VAL C O   1 
ATOM   2976  C  CB  . VAL C  1 103 ? 33.681 5.901    -29.474  1.00 57.28  ? 104 VAL C CB  1 
ATOM   2977  C  CG1 . VAL C  1 103 ? 33.735 7.209    -30.218  1.00 56.92  ? 104 VAL C CG1 1 
ATOM   2978  C  CG2 . VAL C  1 103 ? 33.841 4.776    -30.443  1.00 57.17  ? 104 VAL C CG2 1 
ATOM   2979  N  N   . ILE C  1 104 ? 33.607 6.982    -26.568  1.00 61.16  ? 105 ILE C N   1 
ATOM   2980  C  CA  . ILE C  1 104 ? 33.397 8.074    -25.617  1.00 62.67  ? 105 ILE C CA  1 
ATOM   2981  C  C   . ILE C  1 104 ? 34.551 8.108    -24.647  1.00 67.03  ? 105 ILE C C   1 
ATOM   2982  O  O   . ILE C  1 104 ? 35.313 7.142    -24.531  1.00 68.69  ? 105 ILE C O   1 
ATOM   2983  C  CB  . ILE C  1 104 ? 32.080 7.963    -24.812  1.00 61.92  ? 105 ILE C CB  1 
ATOM   2984  C  CG1 . ILE C  1 104 ? 32.060 6.708    -23.937  1.00 63.56  ? 105 ILE C CG1 1 
ATOM   2985  C  CG2 . ILE C  1 104 ? 30.884 7.973    -25.734  1.00 58.35  ? 105 ILE C CG2 1 
ATOM   2986  C  CD1 . ILE C  1 104 ? 31.048 6.784    -22.795  1.00 64.54  ? 105 ILE C CD1 1 
ATOM   2987  N  N   . SER C  1 105 ? 34.697 9.234    -23.961  1.00 69.50  ? 106 SER C N   1 
ATOM   2988  C  CA  . SER C  1 105 ? 35.730 9.361    -22.919  1.00 74.43  ? 106 SER C CA  1 
ATOM   2989  C  C   . SER C  1 105 ? 35.371 10.422   -21.880  1.00 76.96  ? 106 SER C C   1 
ATOM   2990  O  O   . SER C  1 105 ? 34.585 11.353   -22.145  1.00 75.38  ? 106 SER C O   1 
ATOM   2991  C  CB  . SER C  1 105 ? 37.115 9.669    -23.528  1.00 76.67  ? 106 SER C CB  1 
ATOM   2992  O  OG  . SER C  1 105 ? 38.158 9.506    -22.575  1.00 81.60  ? 106 SER C OG  1 
ATOM   2993  N  N   . LEU C  1 106 ? 35.966 10.258   -20.696  1.00 81.44  ? 107 LEU C N   1 
ATOM   2994  C  CA  . LEU C  1 106 ? 35.827 11.230   -19.611  1.00 85.23  ? 107 LEU C CA  1 
ATOM   2995  C  C   . LEU C  1 106 ? 36.985 12.254   -19.577  1.00 89.02  ? 107 LEU C C   1 
ATOM   2996  O  O   . LEU C  1 106 ? 37.185 12.957   -18.584  1.00 93.53  ? 107 LEU C O   1 
ATOM   2997  C  CB  . LEU C  1 106 ? 35.710 10.485   -18.275  1.00 88.83  ? 107 LEU C CB  1 
ATOM   2998  C  CG  . LEU C  1 106 ? 34.517 9.523    -18.156  1.00 85.82  ? 107 LEU C CG  1 
ATOM   2999  C  CD1 . LEU C  1 106 ? 34.528 8.860    -16.784  1.00 90.64  ? 107 LEU C CD1 1 
ATOM   3000  C  CD2 . LEU C  1 106 ? 33.173 10.249   -18.419  1.00 82.56  ? 107 LEU C CD2 1 
ATOM   3001  N  N   . SER C  1 107 ? 37.735 12.330   -20.672  1.00 87.73  ? 108 SER C N   1 
ATOM   3002  C  CA  . SER C  1 107 ? 38.883 13.227   -20.786  1.00 91.42  ? 108 SER C CA  1 
ATOM   3003  C  C   . SER C  1 107 ? 39.291 13.440   -22.252  1.00 89.02  ? 108 SER C C   1 
ATOM   3004  O  O   . SER C  1 107 ? 39.308 12.508   -23.071  1.00 86.04  ? 108 SER C O   1 
ATOM   3005  C  CB  . SER C  1 107 ? 40.098 12.699   -19.986  1.00 96.89  ? 108 SER C CB  1 
ATOM   3006  O  OG  . SER C  1 107 ? 40.547 11.421   -20.432  1.00 95.91  ? 108 SER C OG  1 
ATOM   3007  N  N   . GLY C  1 108 ? 39.635 14.683   -22.565  1.00 91.02  ? 109 GLY C N   1 
ATOM   3008  C  CA  . GLY C  1 108 ? 40.236 15.039   -23.861  1.00 90.45  ? 109 GLY C CA  1 
ATOM   3009  C  C   . GLY C  1 108 ? 39.265 15.475   -24.946  1.00 86.17  ? 109 GLY C C   1 
ATOM   3010  O  O   . GLY C  1 108 ? 38.191 16.018   -24.665  1.00 84.76  ? 109 GLY C O   1 
ATOM   3011  N  N   . ASP C  1 109 ? 39.665 15.246   -26.195  1.00 84.91  ? 110 ASP C N   1 
ATOM   3012  C  CA  . ASP C  1 109 ? 38.868 15.619   -27.389  1.00 81.59  ? 110 ASP C CA  1 
ATOM   3013  C  C   . ASP C  1 109 ? 37.423 15.077   -27.350  1.00 76.76  ? 110 ASP C C   1 
ATOM   3014  O  O   . ASP C  1 109 ? 36.447 15.782   -27.672  1.00 74.93  ? 110 ASP C O   1 
ATOM   3015  C  CB  . ASP C  1 109 ? 39.585 15.067   -28.633  1.00 81.42  ? 110 ASP C CB  1 
ATOM   3016  C  CG  . ASP C  1 109 ? 39.329 15.883   -29.888  1.00 81.50  ? 110 ASP C CG  1 
ATOM   3017  O  OD1 . ASP C  1 109 ? 38.324 15.614   -30.606  1.00 77.87  ? 110 ASP C OD1 1 
ATOM   3018  O  OD2 . ASP C  1 109 ? 40.166 16.772   -30.179  1.00 85.74  ? 110 ASP C OD2 1 
ATOM   3019  N  N   . HIS C  1 110 ? 37.335 13.809   -26.940  1.00 75.15  ? 111 HIS C N   1 
ATOM   3020  C  CA  . HIS C  1 110 ? 36.090 13.049   -26.855  1.00 71.27  ? 111 HIS C CA  1 
ATOM   3021  C  C   . HIS C  1 110 ? 35.365 13.227   -25.507  1.00 72.18  ? 111 HIS C C   1 
ATOM   3022  O  O   . HIS C  1 110 ? 34.392 12.520   -25.223  1.00 69.83  ? 111 HIS C O   1 
ATOM   3023  C  CB  . HIS C  1 110 ? 36.399 11.563   -27.041  1.00 69.92  ? 111 HIS C CB  1 
ATOM   3024  C  CG  . HIS C  1 110 ? 36.864 11.195   -28.415  1.00 69.13  ? 111 HIS C CG  1 
ATOM   3025  N  ND1 . HIS C  1 110 ? 36.954 9.886    -28.843  1.00 67.92  ? 111 HIS C ND1 1 
ATOM   3026  C  CD2 . HIS C  1 110 ? 37.243 11.957   -29.466  1.00 70.04  ? 111 HIS C CD2 1 
ATOM   3027  C  CE1 . HIS C  1 110 ? 37.380 9.855    -30.094  1.00 67.92  ? 111 HIS C CE1 1 
ATOM   3028  N  NE2 . HIS C  1 110 ? 37.564 11.100   -30.496  1.00 69.44  ? 111 HIS C NE2 1 
ATOM   3029  N  N   . CYS C  1 111 ? 35.829 14.168   -24.684  1.00 76.02  ? 112 CYS C N   1 
ATOM   3030  C  CA  . CYS C  1 111 ? 35.295 14.339   -23.326  1.00 78.00  ? 112 CYS C CA  1 
ATOM   3031  C  C   . CYS C  1 111 ? 33.786 14.613   -23.342  1.00 75.75  ? 112 CYS C C   1 
ATOM   3032  O  O   . CYS C  1 111 ? 33.328 15.602   -23.922  1.00 75.67  ? 112 CYS C O   1 
ATOM   3033  C  CB  . CYS C  1 111 ? 36.011 15.461   -22.590  1.00 83.06  ? 112 CYS C CB  1 
ATOM   3034  S  SG  . CYS C  1 111 ? 35.593 15.500   -20.837  1.00 86.83  ? 112 CYS C SG  1 
ATOM   3035  N  N   . ILE C  1 112 ? 33.024 13.714   -22.727  1.00 74.46  ? 113 ILE C N   1 
ATOM   3036  C  CA  . ILE C  1 112 ? 31.553 13.851   -22.665  1.00 73.18  ? 113 ILE C CA  1 
ATOM   3037  C  C   . ILE C  1 112 ? 31.080 14.633   -21.433  1.00 77.49  ? 113 ILE C C   1 
ATOM   3038  O  O   . ILE C  1 112 ? 29.885 14.999   -21.336  1.00 77.63  ? 113 ILE C O   1 
ATOM   3039  C  CB  . ILE C  1 112 ? 30.811 12.472   -22.683  1.00 70.16  ? 113 ILE C CB  1 
ATOM   3040  C  CG1 . ILE C  1 112 ? 31.260 11.581   -21.511  1.00 72.35  ? 113 ILE C CG1 1 
ATOM   3041  C  CG2 . ILE C  1 112 ? 31.007 11.768   -24.021  1.00 66.28  ? 113 ILE C CG2 1 
ATOM   3042  C  CD1 . ILE C  1 112 ? 30.246 10.537   -21.167  1.00 71.02  ? 113 ILE C CD1 1 
ATOM   3043  N  N   . ILE C  1 113 ? 32.008 14.869   -20.494  1.00 81.45  ? 114 ILE C N   1 
ATOM   3044  C  CA  . ILE C  1 113 ? 31.678 15.549   -19.234  1.00 86.18  ? 114 ILE C CA  1 
ATOM   3045  C  C   . ILE C  1 113 ? 31.235 16.960   -19.521  1.00 87.89  ? 114 ILE C C   1 
ATOM   3046  O  O   . ILE C  1 113 ? 31.843 17.662   -20.318  1.00 87.60  ? 114 ILE C O   1 
ATOM   3047  C  CB  . ILE C  1 113 ? 32.858 15.581   -18.254  1.00 90.81  ? 114 ILE C CB  1 
ATOM   3048  C  CG1 . ILE C  1 113 ? 33.101 14.177   -17.667  1.00 90.82  ? 114 ILE C CG1 1 
ATOM   3049  C  CG2 . ILE C  1 113 ? 32.570 16.577   -17.140  1.00 96.34  ? 114 ILE C CG2 1 
ATOM   3050  C  CD1 . ILE C  1 113 ? 34.401 14.039   -16.856  1.00 95.65  ? 114 ILE C CD1 1 
ATOM   3051  N  N   . GLY C  1 114 ? 30.151 17.353   -18.885  1.00 90.26  ? 115 GLY C N   1 
ATOM   3052  C  CA  . GLY C  1 114 ? 29.562 18.659   -19.116  1.00 93.01  ? 115 GLY C CA  1 
ATOM   3053  C  C   . GLY C  1 114 ? 28.563 18.647   -20.258  1.00 89.37  ? 115 GLY C C   1 
ATOM   3054  O  O   . GLY C  1 114 ? 27.983 19.684   -20.613  1.00 91.56  ? 115 GLY C O   1 
ATOM   3055  N  N   . ARG C  1 115 ? 28.358 17.472   -20.838  1.00 84.38  ? 116 ARG C N   1 
ATOM   3056  C  CA  . ARG C  1 115 ? 27.396 17.323   -21.914  1.00 81.32  ? 116 ARG C CA  1 
ATOM   3057  C  C   . ARG C  1 115 ? 26.201 16.512   -21.431  1.00 80.90  ? 116 ARG C C   1 
ATOM   3058  O  O   . ARG C  1 115 ? 26.237 15.918   -20.355  1.00 82.37  ? 116 ARG C O   1 
ATOM   3059  C  CB  . ARG C  1 115 ? 28.053 16.668   -23.126  1.00 76.42  ? 116 ARG C CB  1 
ATOM   3060  C  CG  . ARG C  1 115 ? 29.285 17.415   -23.597  1.00 77.51  ? 116 ARG C CG  1 
ATOM   3061  C  CD  . ARG C  1 115 ? 29.862 16.846   -24.866  1.00 73.77  ? 116 ARG C CD  1 
ATOM   3062  N  NE  . ARG C  1 115 ? 31.154 17.456   -25.191  1.00 75.16  ? 116 ARG C NE  1 
ATOM   3063  C  CZ  . ARG C  1 115 ? 31.318 18.586   -25.867  1.00 77.02  ? 116 ARG C CZ  1 
ATOM   3064  N  NH1 . ARG C  1 115 ? 30.276 19.287   -26.317  1.00 77.81  ? 116 ARG C NH1 1 
ATOM   3065  N  NH2 . ARG C  1 115 ? 32.549 19.011   -26.100  1.00 79.12  ? 116 ARG C NH2 1 
ATOM   3066  N  N   . THR C  1 116 ? 25.155 16.481   -22.254  1.00 79.30  ? 117 THR C N   1 
ATOM   3067  C  CA  . THR C  1 116 ? 23.877 15.869   -21.890  1.00 79.72  ? 117 THR C CA  1 
ATOM   3068  C  C   . THR C  1 116 ? 23.726 14.412   -22.358  1.00 75.02  ? 117 THR C C   1 
ATOM   3069  O  O   . THR C  1 116 ? 23.927 14.109   -23.542  1.00 71.33  ? 117 THR C O   1 
ATOM   3070  C  CB  . THR C  1 116 ? 22.691 16.679   -22.480  1.00 81.91  ? 117 THR C CB  1 
ATOM   3071  O  OG1 . THR C  1 116 ? 22.659 17.985   -21.894  1.00 87.32  ? 117 THR C OG1 1 
ATOM   3072  C  CG2 . THR C  1 116 ? 21.358 15.978   -22.202  1.00 82.71  ? 117 THR C CG2 1 
ATOM   3073  N  N   . LEU C  1 117 ? 23.347 13.533   -21.424  1.00 75.92  ? 118 LEU C N   1 
ATOM   3074  C  CA  . LEU C  1 117 ? 22.871 12.166   -21.737  1.00 72.60  ? 118 LEU C CA  1 
ATOM   3075  C  C   . LEU C  1 117 ? 21.361 12.196   -22.003  1.00 73.69  ? 118 LEU C C   1 
ATOM   3076  O  O   . LEU C  1 117 ? 20.655 13.002   -21.437  1.00 78.38  ? 118 LEU C O   1 
ATOM   3077  C  CB  . LEU C  1 117 ? 23.174 11.210   -20.586  1.00 73.83  ? 118 LEU C CB  1 
ATOM   3078  C  CG  . LEU C  1 117 ? 22.863 9.736    -20.839  1.00 70.86  ? 118 LEU C CG  1 
ATOM   3079  C  CD1 . LEU C  1 117 ? 23.665 9.224    -22.019  1.00 66.31  ? 118 LEU C CD1 1 
ATOM   3080  C  CD2 . LEU C  1 117 ? 23.173 8.909    -19.614  1.00 73.20  ? 118 LEU C CD2 1 
ATOM   3081  N  N   . VAL C  1 118 ? 20.868 11.342   -22.881  1.00 70.25  ? 119 VAL C N   1 
ATOM   3082  C  CA  . VAL C  1 118 ? 19.469 11.427   -23.303  1.00 71.70  ? 119 VAL C CA  1 
ATOM   3083  C  C   . VAL C  1 118 ? 18.883 10.072   -23.671  1.00 69.47  ? 119 VAL C C   1 
ATOM   3084  O  O   . VAL C  1 118 ? 19.376 9.402    -24.583  1.00 65.56  ? 119 VAL C O   1 
ATOM   3085  C  CB  . VAL C  1 118 ? 19.307 12.328   -24.527  1.00 71.04  ? 119 VAL C CB  1 
ATOM   3086  C  CG1 . VAL C  1 118 ? 17.915 12.185   -25.104  1.00 72.50  ? 119 VAL C CG1 1 
ATOM   3087  C  CG2 . VAL C  1 118 ? 19.571 13.760   -24.161  1.00 74.88  ? 119 VAL C CG2 1 
ATOM   3088  N  N   . VAL C  1 119 ? 17.818 9.675    -22.979  1.00 72.67  ? 120 VAL C N   1 
ATOM   3089  C  CA  . VAL C  1 119 ? 17.114 8.433    -23.300  1.00 71.26  ? 120 VAL C CA  1 
ATOM   3090  C  C   . VAL C  1 119 ? 15.898 8.791    -24.149  1.00 72.71  ? 120 VAL C C   1 
ATOM   3091  O  O   . VAL C  1 119 ? 15.297 9.852    -23.964  1.00 76.71  ? 120 VAL C O   1 
ATOM   3092  C  CB  . VAL C  1 119 ? 16.703 7.669    -22.041  1.00 74.48  ? 120 VAL C CB  1 
ATOM   3093  C  CG1 . VAL C  1 119 ? 15.510 8.334    -21.379  1.00 80.73  ? 120 VAL C CG1 1 
ATOM   3094  C  CG2 . VAL C  1 119 ? 16.371 6.236    -22.390  1.00 72.54  ? 120 VAL C CG2 1 
ATOM   3095  N  N   . HIS C  1 120 ? 15.546 7.903    -25.076  1.00 70.19  ? 121 HIS C N   1 
ATOM   3096  C  CA  . HIS C  1 120 ? 14.652 8.255    -26.198  1.00 70.99  ? 121 HIS C CA  1 
ATOM   3097  C  C   . HIS C  1 120 ? 13.318 7.528    -26.259  1.00 73.64  ? 121 HIS C C   1 
ATOM   3098  O  O   . HIS C  1 120 ? 13.126 6.481    -25.649  1.00 73.71  ? 121 HIS C O   1 
ATOM   3099  C  CB  . HIS C  1 120 ? 15.384 8.063    -27.531  1.00 66.32  ? 121 HIS C CB  1 
ATOM   3100  C  CG  . HIS C  1 120 ? 16.156 9.262    -27.956  1.00 65.49  ? 121 HIS C CG  1 
ATOM   3101  N  ND1 . HIS C  1 120 ? 15.770 10.059   -29.010  1.00 66.85  ? 121 HIS C ND1 1 
ATOM   3102  C  CD2 . HIS C  1 120 ? 17.278 9.819    -27.450  1.00 64.50  ? 121 HIS C CD2 1 
ATOM   3103  C  CE1 . HIS C  1 120 ? 16.634 11.047   -29.150  1.00 66.49  ? 121 HIS C CE1 1 
ATOM   3104  N  NE2 . HIS C  1 120 ? 17.554 10.926   -28.211  1.00 65.21  ? 121 HIS C NE2 1 
ATOM   3105  N  N   . GLU C  1 121 ? 12.413 8.110    -27.041  1.00 76.25  ? 122 GLU C N   1 
ATOM   3106  C  CA  . GLU C  1 121 ? 11.051 7.589    -27.218  1.00 79.94  ? 122 GLU C CA  1 
ATOM   3107  C  C   . GLU C  1 121 ? 11.033 6.186    -27.824  1.00 76.77  ? 122 GLU C C   1 
ATOM   3108  O  O   . GLU C  1 121 ? 10.610 5.203    -27.172  1.00 77.96  ? 122 GLU C O   1 
ATOM   3109  C  CB  . GLU C  1 121 ? 10.242 8.529    -28.114  1.00 83.34  ? 122 GLU C CB  1 
ATOM   3110  C  CG  . GLU C  1 121 ? 8.836  8.024    -28.458  1.00 87.85  ? 122 GLU C CG  1 
ATOM   3111  C  CD  . GLU C  1 121 ? 8.129  8.865    -29.543  1.00 91.81  ? 122 GLU C CD  1 
ATOM   3112  O  OE1 . GLU C  1 121 ? 8.750  9.808    -30.093  1.00 90.59  ? 122 GLU C OE1 1 
ATOM   3113  O  OE2 . GLU C  1 121 ? 6.943  8.580    -29.854  1.00 96.22  ? 122 GLU C OE2 1 
ATOM   3114  N  N   . LYS C  1 122 ? 11.501 6.114    -29.076  1.00 73.30  ? 123 LYS C N   1 
ATOM   3115  C  CA  . LYS C  1 122 ? 11.585 4.856    -29.846  1.00 70.28  ? 123 LYS C CA  1 
ATOM   3116  C  C   . LYS C  1 122 ? 12.997 4.234    -29.754  1.00 65.18  ? 123 LYS C C   1 
ATOM   3117  O  O   . LYS C  1 122 ? 13.896 4.752    -29.060  1.00 64.05  ? 123 LYS C O   1 
ATOM   3118  C  CB  . LYS C  1 122 ? 11.246 5.105    -31.319  1.00 70.25  ? 123 LYS C CB  1 
ATOM   3119  C  CG  . LYS C  1 122 ? 9.979  5.905    -31.577  1.00 76.04  ? 123 LYS C CG  1 
ATOM   3120  C  CD  . LYS C  1 122 ? 9.772  6.135    -33.083  1.00 76.49  ? 123 LYS C CD  1 
ATOM   3121  C  CE  . LYS C  1 122 ? 8.635  7.125    -33.356  1.00 82.93  ? 123 LYS C CE  1 
ATOM   3122  N  NZ  . LYS C  1 122 ? 8.235  7.162    -34.798  1.00 84.43  ? 123 LYS C NZ  1 
ATOM   3123  N  N   . ALA C  1 123 ? 13.185 3.119    -30.449  1.00 62.72  ? 124 ALA C N   1 
ATOM   3124  C  CA  . ALA C  1 123 ? 14.490 2.472    -30.504  1.00 58.62  ? 124 ALA C CA  1 
ATOM   3125  C  C   . ALA C  1 123 ? 15.319 3.088    -31.600  1.00 56.05  ? 124 ALA C C   1 
ATOM   3126  O  O   . ALA C  1 123 ? 14.770 3.511    -32.619  1.00 56.82  ? 124 ALA C O   1 
ATOM   3127  C  CB  . ALA C  1 123 ? 14.341 1.017    -30.749  1.00 58.20  ? 124 ALA C CB  1 
ATOM   3128  N  N   . ASP C  1 124 ? 16.638 3.134    -31.365  1.00 53.58  ? 125 ASP C N   1 
ATOM   3129  C  CA  . ASP C  1 124 ? 17.650 3.621    -32.348  1.00 51.39  ? 125 ASP C CA  1 
ATOM   3130  C  C   . ASP C  1 124 ? 17.892 2.537    -33.412  1.00 50.02  ? 125 ASP C C   1 
ATOM   3131  O  O   . ASP C  1 124 ? 18.268 1.402    -33.084  1.00 49.24  ? 125 ASP C O   1 
ATOM   3132  C  CB  . ASP C  1 124 ? 18.977 3.992    -31.636  1.00 49.89  ? 125 ASP C CB  1 
ATOM   3133  C  CG  . ASP C  1 124 ? 20.035 4.593    -32.583  1.00 48.30  ? 125 ASP C CG  1 
ATOM   3134  O  OD1 . ASP C  1 124 ? 19.779 4.693    -33.802  1.00 48.21  ? 125 ASP C OD1 1 
ATOM   3135  O  OD2 . ASP C  1 124 ? 21.137 4.954    -32.097  1.00 47.37  ? 125 ASP C OD2 1 
ATOM   3136  N  N   . ASP C  1 125 ? 17.673 2.888    -34.679  1.00 50.27  ? 126 ASP C N   1 
ATOM   3137  C  CA  . ASP C  1 125 ? 17.783 1.918    -35.765  1.00 49.74  ? 126 ASP C CA  1 
ATOM   3138  C  C   . ASP C  1 125 ? 19.244 1.713    -36.175  1.00 47.84  ? 126 ASP C C   1 
ATOM   3139  O  O   . ASP C  1 125 ? 19.513 1.064    -37.173  1.00 47.96  ? 126 ASP C O   1 
ATOM   3140  C  CB  . ASP C  1 125 ? 16.913 2.310    -36.967  1.00 51.67  ? 126 ASP C CB  1 
ATOM   3141  C  CG  . ASP C  1 125 ? 17.481 3.460    -37.748  1.00 51.78  ? 126 ASP C CG  1 
ATOM   3142  O  OD1 . ASP C  1 125 ? 18.699 3.670    -37.680  1.00 50.12  ? 126 ASP C OD1 1 
ATOM   3143  O  OD2 . ASP C  1 125 ? 16.722 4.152    -38.448  1.00 53.89  ? 126 ASP C OD2 1 
ATOM   3144  N  N   . LEU C  1 126 ? 20.177 2.275    -35.406  1.00 46.72  ? 127 LEU C N   1 
ATOM   3145  C  CA  . LEU C  1 126 ? 21.630 2.095    -35.608  1.00 45.60  ? 127 LEU C CA  1 
ATOM   3146  C  C   . LEU C  1 126 ? 22.097 2.449    -37.020  1.00 46.06  ? 127 LEU C C   1 
ATOM   3147  O  O   . LEU C  1 126 ? 23.072 1.883    -37.523  1.00 46.21  ? 127 LEU C O   1 
ATOM   3148  C  CB  . LEU C  1 126 ? 22.072 0.669    -35.256  1.00 45.40  ? 127 LEU C CB  1 
ATOM   3149  C  CG  . LEU C  1 126 ? 21.583 0.116    -33.907  1.00 45.94  ? 127 LEU C CG  1 
ATOM   3150  C  CD1 . LEU C  1 126 ? 22.276 -1.224   -33.566  1.00 46.76  ? 127 LEU C CD1 1 
ATOM   3151  C  CD2 . LEU C  1 126 ? 21.767 1.098    -32.782  1.00 45.89  ? 127 LEU C CD2 1 
ATOM   3152  N  N   . GLY C  1 127 ? 21.390 3.380    -37.650  1.00 47.10  ? 128 GLY C N   1 
ATOM   3153  C  CA  . GLY C  1 127 ? 21.767 3.903    -38.959  1.00 48.19  ? 128 GLY C CA  1 
ATOM   3154  C  C   . GLY C  1 127 ? 21.393 3.050    -40.147  1.00 49.39  ? 128 GLY C C   1 
ATOM   3155  O  O   . GLY C  1 127 ? 21.580 3.457    -41.277  1.00 51.05  ? 128 GLY C O   1 
ATOM   3156  N  N   . LYS C  1 128 ? 20.834 1.879    -39.901  1.00 49.22  ? 129 LYS C N   1 
ATOM   3157  C  CA  . LYS C  1 128 ? 20.505 0.935    -40.979  1.00 50.90  ? 129 LYS C CA  1 
ATOM   3158  C  C   . LYS C  1 128 ? 19.091 1.110    -41.515  1.00 53.02  ? 129 LYS C C   1 
ATOM   3159  O  O   . LYS C  1 128 ? 18.522 0.178    -42.076  1.00 54.36  ? 129 LYS C O   1 
ATOM   3160  C  CB  . LYS C  1 128 ? 20.674 -0.508   -40.486  1.00 50.46  ? 129 LYS C CB  1 
ATOM   3161  C  CG  . LYS C  1 128 ? 22.023 -0.809   -39.836  1.00 49.57  ? 129 LYS C CG  1 
ATOM   3162  C  CD  . LYS C  1 128 ? 22.322 -2.313   -39.796  1.00 50.82  ? 129 LYS C CD  1 
ATOM   3163  C  CE  . LYS C  1 128 ? 23.619 -2.599   -39.018  1.00 50.76  ? 129 LYS C CE  1 
ATOM   3164  N  NZ  . LYS C  1 128 ? 24.141 -3.999   -39.242  1.00 52.92  ? 129 LYS C NZ  1 
ATOM   3165  N  N   . GLY C  1 129 ? 18.533 2.305    -41.339  1.00 53.86  ? 130 GLY C N   1 
ATOM   3166  C  CA  . GLY C  1 129 ? 17.105 2.561    -41.591  1.00 56.50  ? 130 GLY C CA  1 
ATOM   3167  C  C   . GLY C  1 129 ? 16.776 2.765    -43.061  1.00 59.66  ? 130 GLY C C   1 
ATOM   3168  O  O   . GLY C  1 129 ? 15.653 2.525    -43.511  1.00 62.35  ? 130 GLY C O   1 
ATOM   3169  N  N   . GLY C  1 130 ? 17.754 3.253    -43.811  1.00 59.80  ? 131 GLY C N   1 
ATOM   3170  C  CA  . GLY C  1 130 ? 17.571 3.492    -45.243  1.00 63.58  ? 131 GLY C CA  1 
ATOM   3171  C  C   . GLY C  1 130 ? 17.091 4.893    -45.616  1.00 66.72  ? 131 GLY C C   1 
ATOM   3172  O  O   . GLY C  1 130 ? 17.361 5.404    -46.710  1.00 69.61  ? 131 GLY C O   1 
ATOM   3173  N  N   . ASN C  1 131 ? 16.365 5.522    -44.703  1.00 66.79  ? 132 ASN C N   1 
ATOM   3174  C  CA  . ASN C  1 131 ? 15.909 6.885    -44.906  1.00 70.24  ? 132 ASN C CA  1 
ATOM   3175  C  C   . ASN C  1 131 ? 16.977 7.930    -44.526  1.00 68.81  ? 132 ASN C C   1 
ATOM   3176  O  O   . ASN C  1 131 ? 18.039 7.607    -43.973  1.00 64.81  ? 132 ASN C O   1 
ATOM   3177  C  CB  . ASN C  1 131 ? 14.565 7.131    -44.173  1.00 72.31  ? 132 ASN C CB  1 
ATOM   3178  C  CG  . ASN C  1 131 ? 14.725 7.357    -42.675  1.00 69.36  ? 132 ASN C CG  1 
ATOM   3179  O  OD1 . ASN C  1 131 ? 15.839 7.363    -42.140  1.00 65.70  ? 132 ASN C OD1 1 
ATOM   3180  N  ND2 . ASN C  1 131 ? 13.599 7.559    -41.991  1.00 71.85  ? 132 ASN C ND2 1 
ATOM   3181  N  N   . GLU C  1 132 ? 16.666 9.187    -44.836  1.00 72.70  ? 133 GLU C N   1 
ATOM   3182  C  CA  . GLU C  1 132 ? 17.559 10.314   -44.586  1.00 72.67  ? 133 GLU C CA  1 
ATOM   3183  C  C   . GLU C  1 132 ? 17.850 10.457   -43.099  1.00 69.06  ? 133 GLU C C   1 
ATOM   3184  O  O   . GLU C  1 132 ? 19.011 10.553   -42.682  1.00 66.13  ? 133 GLU C O   1 
ATOM   3185  C  CB  . GLU C  1 132 ? 16.918 11.607   -45.121  1.00 78.64  ? 133 GLU C CB  1 
ATOM   3186  C  CG  . GLU C  1 132 ? 17.574 12.930   -44.611  1.00 80.09  ? 133 GLU C CG  1 
ATOM   3187  C  CD  . GLU C  1 132 ? 18.893 13.312   -45.340  1.00 80.64  ? 133 GLU C CD  1 
ATOM   3188  O  OE1 . GLU C  1 132 ? 19.360 12.520   -46.216  1.00 80.14  ? 133 GLU C OE1 1 
ATOM   3189  O  OE2 . GLU C  1 132 ? 19.460 14.402   -45.014  1.00 81.71  ? 133 GLU C OE2 1 
ATOM   3190  N  N   . GLU C  1 133 ? 16.772 10.477   -42.321  1.00 69.89  ? 134 GLU C N   1 
ATOM   3191  C  CA  . GLU C  1 133 ? 16.830 10.776   -40.890  1.00 68.09  ? 134 GLU C CA  1 
ATOM   3192  C  C   . GLU C  1 133 ? 17.628 9.729    -40.103  1.00 62.77  ? 134 GLU C C   1 
ATOM   3193  O  O   . GLU C  1 133 ? 18.245 10.064   -39.085  1.00 60.91  ? 134 GLU C O   1 
ATOM   3194  C  CB  . GLU C  1 133 ? 15.400 10.929   -40.316  1.00 71.35  ? 134 GLU C CB  1 
ATOM   3195  C  CG  . GLU C  1 133 ? 15.306 11.643   -38.940  1.00 71.95  ? 134 GLU C CG  1 
ATOM   3196  C  CD  . GLU C  1 133 ? 15.670 13.138   -38.993  1.00 75.47  ? 134 GLU C CD  1 
ATOM   3197  O  OE1 . GLU C  1 133 ? 15.799 13.703   -40.112  1.00 78.42  ? 134 GLU C OE1 1 
ATOM   3198  O  OE2 . GLU C  1 133 ? 15.835 13.746   -37.909  1.00 75.52  ? 134 GLU C OE2 1 
ATOM   3199  N  N   . SER C  1 134 ? 17.623 8.481    -40.578  1.00 60.92  ? 135 SER C N   1 
ATOM   3200  C  CA  . SER C  1 134 ? 18.324 7.385    -39.897  1.00 56.85  ? 135 SER C CA  1 
ATOM   3201  C  C   . SER C  1 134 ? 19.816 7.634    -39.835  1.00 54.76  ? 135 SER C C   1 
ATOM   3202  O  O   . SER C  1 134 ? 20.502 7.162    -38.944  1.00 52.16  ? 135 SER C O   1 
ATOM   3203  C  CB  . SER C  1 134 ? 18.082 6.061    -40.596  1.00 56.34  ? 135 SER C CB  1 
ATOM   3204  O  OG  . SER C  1 134 ? 18.942 5.072    -40.085  1.00 53.08  ? 135 SER C OG  1 
ATOM   3205  N  N   . THR C  1 135 ? 20.308 8.379    -40.805  1.00 56.62  ? 136 THR C N   1 
ATOM   3206  C  CA  . THR C  1 135 ? 21.709 8.788    -40.843  1.00 55.81  ? 136 THR C CA  1 
ATOM   3207  C  C   . THR C  1 135 ? 22.072 9.907    -39.867  1.00 56.05  ? 136 THR C C   1 
ATOM   3208  O  O   . THR C  1 135 ? 23.247 10.220   -39.695  1.00 55.48  ? 136 THR C O   1 
ATOM   3209  C  CB  . THR C  1 135 ? 22.062 9.246    -42.247  1.00 58.55  ? 136 THR C CB  1 
ATOM   3210  O  OG1 . THR C  1 135 ? 22.265 8.091    -43.062  1.00 58.28  ? 136 THR C OG1 1 
ATOM   3211  C  CG2 . THR C  1 135 ? 23.317 10.094   -42.252  1.00 58.96  ? 136 THR C CG2 1 
ATOM   3212  N  N   . LYS C  1 136 ? 21.066 10.497   -39.228  1.00 57.57  ? 137 LYS C N   1 
ATOM   3213  C  CA  . LYS C  1 136 ? 21.261 11.622   -38.304  1.00 58.70  ? 137 LYS C CA  1 
ATOM   3214  C  C   . LYS C  1 136 ? 20.891 11.275   -36.849  1.00 57.13  ? 137 LYS C C   1 
ATOM   3215  O  O   . LYS C  1 136 ? 21.732 11.275   -35.946  1.00 55.43  ? 137 LYS C O   1 
ATOM   3216  C  CB  . LYS C  1 136 ? 20.399 12.808   -38.757  1.00 63.33  ? 137 LYS C CB  1 
ATOM   3217  C  CG  . LYS C  1 136 ? 20.894 13.560   -39.999  1.00 66.32  ? 137 LYS C CG  1 
ATOM   3218  C  CD  . LYS C  1 136 ? 19.922 14.746   -40.324  1.00 72.18  ? 137 LYS C CD  1 
ATOM   3219  C  CE  . LYS C  1 136 ? 20.570 15.867   -41.172  1.00 75.63  ? 137 LYS C CE  1 
ATOM   3220  N  NZ  . LYS C  1 136 ? 20.430 15.644   -42.643  1.00 77.95  ? 137 LYS C NZ  1 
ATOM   3221  N  N   . THR C  1 137 ? 19.609 10.998   -36.644  1.00 58.29  ? 138 THR C N   1 
ATOM   3222  C  CA  . THR C  1 137 ? 19.052 10.844   -35.308  1.00 58.40  ? 138 THR C CA  1 
ATOM   3223  C  C   . THR C  1 137 ? 18.859 9.409    -34.911  1.00 55.75  ? 138 THR C C   1 
ATOM   3224  O  O   . THR C  1 137 ? 18.642 9.121    -33.735  1.00 55.62  ? 138 THR C O   1 
ATOM   3225  C  CB  . THR C  1 137 ? 17.671 11.497   -35.222  1.00 62.77  ? 138 THR C CB  1 
ATOM   3226  O  OG1 . THR C  1 137 ? 16.724 10.722   -35.973  1.00 63.38  ? 138 THR C OG1 1 
ATOM   3227  C  CG2 . THR C  1 137 ? 17.715 12.923   -35.764  1.00 66.59  ? 138 THR C CG2 1 
ATOM   3228  N  N   . GLY C  1 138 ? 18.913 8.524    -35.904  1.00 54.43  ? 139 GLY C N   1 
ATOM   3229  C  CA  . GLY C  1 138 ? 18.682 7.084    -35.720  1.00 52.68  ? 139 GLY C CA  1 
ATOM   3230  C  C   . GLY C  1 138 ? 17.216 6.704    -35.723  1.00 54.78  ? 139 GLY C C   1 
ATOM   3231  O  O   . GLY C  1 138 ? 16.875 5.575    -35.399  1.00 54.00  ? 139 GLY C O   1 
ATOM   3232  N  N   . ASN C  1 139 ? 16.362 7.657    -36.081  1.00 58.20  ? 140 ASN C N   1 
ATOM   3233  C  CA  . ASN C  1 139 ? 14.905 7.497    -36.033  1.00 61.59  ? 140 ASN C CA  1 
ATOM   3234  C  C   . ASN C  1 139 ? 14.383 7.060    -34.673  1.00 62.06  ? 140 ASN C C   1 
ATOM   3235  O  O   . ASN C  1 139 ? 13.319 6.458    -34.595  1.00 64.17  ? 140 ASN C O   1 
ATOM   3236  C  CB  . ASN C  1 139 ? 14.420 6.534    -37.112  1.00 61.78  ? 140 ASN C CB  1 
ATOM   3237  C  CG  . ASN C  1 139 ? 14.357 7.176    -38.480  1.00 63.86  ? 140 ASN C CG  1 
ATOM   3238  O  OD1 . ASN C  1 139 ? 14.541 6.510    -39.479  1.00 63.48  ? 140 ASN C OD1 1 
ATOM   3239  N  ND2 . ASN C  1 139 ? 14.089 8.464    -38.532  1.00 66.63  ? 140 ASN C ND2 1 
ATOM   3240  N  N   . ALA C  1 140 ? 15.118 7.412    -33.615  1.00 60.81  ? 141 ALA C N   1 
ATOM   3241  C  CA  . ALA C  1 140 ? 14.797 7.008    -32.233  1.00 61.55  ? 141 ALA C CA  1 
ATOM   3242  C  C   . ALA C  1 140 ? 13.764 7.927    -31.542  1.00 66.47  ? 141 ALA C C   1 
ATOM   3243  O  O   . ALA C  1 140 ? 13.385 7.709    -30.373  1.00 68.03  ? 141 ALA C O   1 
ATOM   3244  C  CB  . ALA C  1 140 ? 16.061 6.958    -31.411  1.00 58.83  ? 141 ALA C CB  1 
ATOM   3245  N  N   . GLY C  1 141 ? 13.338 8.970    -32.257  1.00 69.38  ? 142 GLY C N   1 
ATOM   3246  C  CA  . GLY C  1 141 ? 12.198 9.772    -31.827  1.00 75.23  ? 142 GLY C CA  1 
ATOM   3247  C  C   . GLY C  1 141 ? 12.490 10.805   -30.750  1.00 77.48  ? 142 GLY C C   1 
ATOM   3248  O  O   . GLY C  1 141 ? 13.639 11.252   -30.590  1.00 74.81  ? 142 GLY C O   1 
ATOM   3249  N  N   . SER C  1 142 ? 11.436 11.172   -30.013  1.00 82.98  ? 143 SER C N   1 
ATOM   3250  C  CA  . SER C  1 142 ? 11.487 12.282   -29.045  1.00 86.88  ? 143 SER C CA  1 
ATOM   3251  C  C   . SER C  1 142 ? 12.377 11.980   -27.831  1.00 84.35  ? 143 SER C C   1 
ATOM   3252  O  O   . SER C  1 142 ? 12.828 10.830   -27.605  1.00 80.17  ? 143 SER C O   1 
ATOM   3253  C  CB  . SER C  1 142 ? 10.078 12.680   -28.562  1.00 94.35  ? 143 SER C CB  1 
ATOM   3254  O  OG  . SER C  1 142 ? 9.575  11.782   -27.586  1.00 95.36  ? 143 SER C OG  1 
ATOM   3255  N  N   . ARG C  1 143 ? 12.620 13.033   -27.057  1.00 87.46  ? 144 ARG C N   1 
ATOM   3256  C  CA  . ARG C  1 143 ? 13.499 12.948   -25.899  1.00 86.15  ? 144 ARG C CA  1 
ATOM   3257  C  C   . ARG C  1 143 ? 12.654 12.837   -24.634  1.00 91.47  ? 144 ARG C C   1 
ATOM   3258  O  O   . ARG C  1 143 ? 12.009 13.800   -24.210  1.00 97.72  ? 144 ARG C O   1 
ATOM   3259  C  CB  . ARG C  1 143 ? 14.429 14.163   -25.848  1.00 86.66  ? 144 ARG C CB  1 
ATOM   3260  C  CG  . ARG C  1 143 ? 15.321 14.254   -27.069  1.00 81.98  ? 144 ARG C CG  1 
ATOM   3261  C  CD  . ARG C  1 143 ? 16.117 15.531   -27.128  1.00 83.52  ? 144 ARG C CD  1 
ATOM   3262  N  NE  . ARG C  1 143 ? 16.803 15.662   -28.412  1.00 80.09  ? 144 ARG C NE  1 
ATOM   3263  C  CZ  . ARG C  1 143 ? 17.624 16.658   -28.735  1.00 80.92  ? 144 ARG C CZ  1 
ATOM   3264  N  NH1 . ARG C  1 143 ? 17.900 17.635   -27.867  1.00 84.92  ? 144 ARG C NH1 1 
ATOM   3265  N  NH2 . ARG C  1 143 ? 18.179 16.678   -29.936  1.00 78.68  ? 144 ARG C NH2 1 
ATOM   3266  N  N   . LEU C  1 144 ? 12.667 11.647   -24.045  1.00 89.54  ? 145 LEU C N   1 
ATOM   3267  C  CA  . LEU C  1 144 ? 11.840 11.353   -22.877  1.00 94.79  ? 145 LEU C CA  1 
ATOM   3268  C  C   . LEU C  1 144 ? 12.428 11.931   -21.597  1.00 97.48  ? 145 LEU C C   1 
ATOM   3269  O  O   . LEU C  1 144 ? 11.756 12.598   -20.832  1.00 104.26 ? 145 LEU C O   1 
ATOM   3270  C  CB  . LEU C  1 144 ? 11.669 9.835    -22.705  1.00 92.40  ? 145 LEU C CB  1 
ATOM   3271  C  CG  . LEU C  1 144 ? 10.839 9.102    -23.771  1.00 91.30  ? 145 LEU C CG  1 
ATOM   3272  C  CD1 . LEU C  1 144 ? 10.603 7.611    -23.383  1.00 90.10  ? 145 LEU C CD1 1 
ATOM   3273  C  CD2 . LEU C  1 144 ? 9.514  9.839    -24.026  1.00 97.61  ? 145 LEU C CD2 1 
ATOM   3274  N  N   . ALA C  1 145 ? 13.684 11.636   -21.359  1.00 92.95  ? 146 ALA C N   1 
ATOM   3275  C  CA  . ALA C  1 145 ? 14.345 12.091   -20.146  1.00 95.83  ? 146 ALA C CA  1 
ATOM   3276  C  C   . ALA C  1 145 ? 15.843 12.320   -20.418  1.00 91.01  ? 146 ALA C C   1 
ATOM   3277  O  O   . ALA C  1 145 ? 16.456 11.639   -21.250  1.00 85.36  ? 146 ALA C O   1 
ATOM   3278  C  CB  . ALA C  1 145 ? 14.146 11.084   -19.009  1.00 97.78  ? 146 ALA C CB  1 
ATOM   3279  N  N   . CYS C  1 146 ? 16.416 13.296   -19.727  1.00 93.92  ? 147 CYS C N   1 
ATOM   3280  C  CA  . CYS C  1 146 ? 17.801 13.669   -19.942  1.00 90.37  ? 147 CYS C CA  1 
ATOM   3281  C  C   . CYS C  1 146 ? 18.408 14.327   -18.716  1.00 94.86  ? 147 CYS C C   1 
ATOM   3282  O  O   . CYS C  1 146 ? 17.711 14.672   -17.758  1.00 101.15 ? 147 CYS C O   1 
ATOM   3283  C  CB  . CYS C  1 146 ? 17.917 14.621   -21.130  1.00 88.94  ? 147 CYS C CB  1 
ATOM   3284  S  SG  . CYS C  1 146 ? 17.102 16.199   -20.886  1.00 96.10  ? 147 CYS C SG  1 
ATOM   3285  N  N   . GLY C  1 147 ? 19.720 14.488   -18.750  1.00 92.29  ? 148 GLY C N   1 
ATOM   3286  C  CA  . GLY C  1 147 ? 20.434 15.101   -17.650  1.00 96.47  ? 148 GLY C CA  1 
ATOM   3287  C  C   . GLY C  1 147 ? 21.838 15.434   -18.048  1.00 93.51  ? 148 GLY C C   1 
ATOM   3288  O  O   . GLY C  1 147 ? 22.399 14.766   -18.911  1.00 88.05  ? 148 GLY C O   1 
ATOM   3289  N  N   . VAL C  1 148 ? 22.411 16.459   -17.417  1.00 97.76  ? 149 VAL C N   1 
ATOM   3290  C  CA  . VAL C  1 148 ? 23.806 16.868   -17.682  1.00 95.91  ? 149 VAL C CA  1 
ATOM   3291  C  C   . VAL C  1 148 ? 24.834 15.964   -16.972  1.00 94.88  ? 149 VAL C C   1 
ATOM   3292  O  O   . VAL C  1 148 ? 24.709 15.654   -15.800  1.00 98.69  ? 149 VAL C O   1 
ATOM   3293  C  CB  . VAL C  1 148 ? 24.049 18.318   -17.276  1.00 101.31 ? 149 VAL C CB  1 
ATOM   3294  C  CG1 . VAL C  1 148 ? 25.477 18.685   -17.551  1.00 100.02 ? 149 VAL C CG1 1 
ATOM   3295  C  CG2 . VAL C  1 148 ? 23.103 19.244   -18.030  1.00 102.92 ? 149 VAL C CG2 1 
ATOM   3296  N  N   . ILE C  1 149 ? 25.847 15.542   -17.709  1.00 90.35  ? 150 ILE C N   1 
ATOM   3297  C  CA  . ILE C  1 149 ? 26.809 14.592   -17.186  1.00 89.83  ? 150 ILE C CA  1 
ATOM   3298  C  C   . ILE C  1 149 ? 27.759 15.340   -16.301  1.00 94.72  ? 150 ILE C C   1 
ATOM   3299  O  O   . ILE C  1 149 ? 28.340 16.325   -16.738  1.00 95.47  ? 150 ILE C O   1 
ATOM   3300  C  CB  . ILE C  1 149 ? 27.612 13.889   -18.300  1.00 84.32  ? 150 ILE C CB  1 
ATOM   3301  C  CG1 . ILE C  1 149 ? 26.700 12.942   -19.096  1.00 79.96  ? 150 ILE C CG1 1 
ATOM   3302  C  CG2 . ILE C  1 149 ? 28.791 13.113   -17.696  1.00 85.00  ? 150 ILE C CG2 1 
ATOM   3303  C  CD1 . ILE C  1 149 ? 27.324 12.416   -20.382  1.00 74.87  ? 150 ILE C CD1 1 
ATOM   3304  N  N   . GLY C  1 150 ? 27.938 14.858   -15.073  1.00 98.70  ? 151 GLY C N   1 
ATOM   3305  C  CA  . GLY C  1 150 ? 28.750 15.562   -14.067  1.00 104.62 ? 151 GLY C CA  1 
ATOM   3306  C  C   . GLY C  1 150 ? 29.896 14.749   -13.479  1.00 105.85 ? 151 GLY C C   1 
ATOM   3307  O  O   . GLY C  1 150 ? 29.882 13.514   -13.479  1.00 103.66 ? 151 GLY C O   1 
ATOM   3308  N  N   . ILE C  1 151 ? 30.895 15.453   -12.966  1.00 110.01 ? 152 ILE C N   1 
ATOM   3309  C  CA  . ILE C  1 151 ? 32.028 14.793   -12.333  1.00 112.65 ? 152 ILE C CA  1 
ATOM   3310  C  C   . ILE C  1 151 ? 31.565 14.223   -11.022  1.00 117.70 ? 152 ILE C C   1 
ATOM   3311  O  O   . ILE C  1 151 ? 30.888 14.892   -10.257  1.00 122.34 ? 152 ILE C O   1 
ATOM   3312  C  CB  . ILE C  1 151 ? 33.214 15.751   -12.075  1.00 117.09 ? 152 ILE C CB  1 
ATOM   3313  C  CG1 . ILE C  1 151 ? 33.727 16.338   -13.394  1.00 112.77 ? 152 ILE C CG1 1 
ATOM   3314  C  CG2 . ILE C  1 151 ? 34.370 15.017   -11.363  1.00 120.52 ? 152 ILE C CG2 1 
ATOM   3315  C  CD1 . ILE C  1 151 ? 34.858 17.343   -13.224  1.00 117.18 ? 152 ILE C CD1 1 
ATOM   3316  N  N   . ALA C  1 152 ? 31.948 12.984   -10.766  1.00 117.61 ? 153 ALA C N   1 
ATOM   3317  C  CA  . ALA C  1 152 ? 31.507 12.262   -9.565   1.00 122.79 ? 153 ALA C CA  1 
ATOM   3318  C  C   . ALA C  1 152 ? 32.671 11.903   -8.623   1.00 128.97 ? 153 ALA C C   1 
ATOM   3319  O  O   . ALA C  1 152 ? 33.844 11.846   -9.058   1.00 128.00 ? 153 ALA C O   1 
ATOM   3320  C  CB  . ALA C  1 152 ? 30.769 11.001   -9.984   1.00 118.50 ? 153 ALA C CB  1 
ATOM   3321  N  N   . GLN C  1 153 ? 32.345 11.651   -7.350   1.00 135.71 ? 154 GLN C N   1 
ATOM   3322  C  CA  . GLN C  1 153 ? 33.381 11.290   -6.371   1.00 143.05 ? 154 GLN C CA  1 
ATOM   3323  C  C   . GLN C  1 153 ? 33.932 9.873    -6.602   1.00 141.63 ? 154 GLN C C   1 
ATOM   3324  O  O   . GLN C  1 153 ? 33.150 8.933    -6.780   1.00 138.96 ? 154 GLN C O   1 
ATOM   3325  C  CB  . GLN C  1 153 ? 32.867 11.417   -4.934   1.00 151.72 ? 154 GLN C CB  1 
ATOM   3326  C  CG  . GLN C  1 153 ? 33.967 11.113   -3.848   1.00 160.58 ? 154 GLN C CG  1 
ATOM   3327  C  CD  . GLN C  1 153 ? 33.514 11.365   -2.352   1.00 170.62 ? 154 GLN C CD  1 
ATOM   3328  O  OE1 . GLN C  1 153 ? 33.170 12.494   -1.959   1.00 174.06 ? 154 GLN C OE1 1 
ATOM   3329  N  NE2 . GLN C  1 153 ? 33.549 10.307   -1.531   1.00 175.53 ? 154 GLN C NE2 1 
ATOM   3330  O  OXT . GLN C  1 153 ? 35.150 9.635    -6.618   1.00 143.58 ? 154 GLN C OXT 1 
ATOM   3331  N  N   . ALA D  1 1   ? 34.332 31.596   -28.512  1.00 116.19 ? 2   ALA D N   1 
ATOM   3332  C  CA  . ALA D  1 1   ? 33.476 31.953   -27.342  1.00 116.85 ? 2   ALA D CA  1 
ATOM   3333  C  C   . ALA D  1 1   ? 32.929 30.692   -26.653  1.00 115.89 ? 2   ALA D C   1 
ATOM   3334  O  O   . ALA D  1 1   ? 31.876 30.184   -27.075  1.00 116.08 ? 2   ALA D O   1 
ATOM   3335  C  CB  . ALA D  1 1   ? 32.313 32.851   -27.798  1.00 118.06 ? 2   ALA D CB  1 
ATOM   3336  N  N   . THR D  1 2   ? 33.627 30.204   -25.605  1.00 115.16 ? 3   THR D N   1 
ATOM   3337  C  CA  . THR D  1 2   ? 33.208 29.008   -24.817  1.00 113.83 ? 3   THR D CA  1 
ATOM   3338  C  C   . THR D  1 2   ? 32.049 29.333   -23.859  1.00 114.74 ? 3   THR D C   1 
ATOM   3339  O  O   . THR D  1 2   ? 32.205 29.314   -22.631  1.00 114.57 ? 3   THR D O   1 
ATOM   3340  C  CB  . THR D  1 2   ? 34.372 28.387   -23.981  1.00 113.08 ? 3   THR D CB  1 
ATOM   3341  O  OG1 . THR D  1 2   ? 35.615 28.551   -24.674  1.00 112.44 ? 3   THR D OG1 1 
ATOM   3342  C  CG2 . THR D  1 2   ? 34.103 26.897   -23.675  1.00 111.18 ? 3   THR D CG2 1 
ATOM   3343  N  N   . LYS D  1 3   ? 30.885 29.610   -24.448  1.00 115.76 ? 4   LYS D N   1 
ATOM   3344  C  CA  . LYS D  1 3   ? 29.648 29.885   -23.713  1.00 116.88 ? 4   LYS D CA  1 
ATOM   3345  C  C   . LYS D  1 3   ? 29.170 28.616   -22.993  1.00 116.35 ? 4   LYS D C   1 
ATOM   3346  O  O   . LYS D  1 3   ? 29.187 27.515   -23.572  1.00 115.87 ? 4   LYS D O   1 
ATOM   3347  C  CB  . LYS D  1 3   ? 28.560 30.356   -24.680  1.00 117.74 ? 4   LYS D CB  1 
ATOM   3348  C  CG  . LYS D  1 3   ? 28.909 31.614   -25.479  1.00 119.32 ? 4   LYS D CG  1 
ATOM   3349  C  CD  . LYS D  1 3   ? 28.133 31.691   -26.808  1.00 120.82 ? 4   LYS D CD  1 
ATOM   3350  C  CE  . LYS D  1 3   ? 28.239 33.065   -27.514  1.00 122.86 ? 4   LYS D CE  1 
ATOM   3351  N  NZ  . LYS D  1 3   ? 27.267 34.098   -26.996  1.00 124.91 ? 4   LYS D NZ  1 
ATOM   3352  N  N   . ALA D  1 4   ? 28.761 28.766   -21.732  1.00 117.01 ? 5   ALA D N   1 
ATOM   3353  C  CA  . ALA D  1 4   ? 28.275 27.636   -20.930  1.00 116.23 ? 5   ALA D CA  1 
ATOM   3354  C  C   . ALA D  1 4   ? 26.888 27.946   -20.367  1.00 117.37 ? 5   ALA D C   1 
ATOM   3355  O  O   . ALA D  1 4   ? 26.251 28.959   -20.733  1.00 118.46 ? 5   ALA D O   1 
ATOM   3356  C  CB  . ALA D  1 4   ? 29.275 27.290   -19.799  1.00 115.56 ? 5   ALA D CB  1 
ATOM   3357  N  N   . VAL D  1 5   ? 26.414 27.045   -19.506  1.00 117.16 ? 6   VAL D N   1 
ATOM   3358  C  CA  . VAL D  1 5   ? 25.185 27.276   -18.739  1.00 118.38 ? 6   VAL D CA  1 
ATOM   3359  C  C   . VAL D  1 5   ? 25.120 26.388   -17.451  1.00 118.22 ? 6   VAL D C   1 
ATOM   3360  O  O   . VAL D  1 5   ? 25.790 25.330   -17.342  1.00 117.00 ? 6   VAL D O   1 
ATOM   3361  C  CB  . VAL D  1 5   ? 23.892 27.208   -19.654  1.00 118.76 ? 6   VAL D CB  1 
ATOM   3362  C  CG1 . VAL D  1 5   ? 23.754 25.843   -20.348  1.00 117.20 ? 6   VAL D CG1 1 
ATOM   3363  C  CG2 . VAL D  1 5   ? 22.646 27.583   -18.858  1.00 119.75 ? 6   VAL D CG2 1 
ATOM   3364  N  N   . CYS D  1 6   ? 24.383 26.898   -16.455  1.00 119.60 ? 7   CYS D N   1 
ATOM   3365  C  CA  . CYS D  1 6   ? 24.056 26.168   -15.227  1.00 119.45 ? 7   CYS D CA  1 
ATOM   3366  C  C   . CYS D  1 6   ? 22.588 26.426   -14.885  1.00 120.83 ? 7   CYS D C   1 
ATOM   3367  O  O   . CYS D  1 6   ? 22.069 27.551   -15.028  1.00 122.10 ? 7   CYS D O   1 
ATOM   3368  C  CB  . CYS D  1 6   ? 24.971 26.565   -14.053  1.00 119.92 ? 7   CYS D CB  1 
ATOM   3369  S  SG  . CYS D  1 6   ? 24.619 25.739   -12.447  1.00 119.44 ? 7   CYS D SG  1 
ATOM   3370  N  N   . VAL D  1 7   ? 21.925 25.336   -14.506  1.00 120.48 ? 8   VAL D N   1 
ATOM   3371  C  CA  . VAL D  1 7   ? 20.578 25.355   -13.966  1.00 121.77 ? 8   VAL D CA  1 
ATOM   3372  C  C   . VAL D  1 7   ? 20.800 24.894   -12.526  1.00 121.74 ? 8   VAL D C   1 
ATOM   3373  O  O   . VAL D  1 7   ? 21.526 23.922   -12.276  1.00 120.05 ? 8   VAL D O   1 
ATOM   3374  C  CB  . VAL D  1 7   ? 19.576 24.443   -14.792  1.00 121.60 ? 8   VAL D CB  1 
ATOM   3375  C  CG1 . VAL D  1 7   ? 18.292 24.160   -14.000  1.00 122.80 ? 8   VAL D CG1 1 
ATOM   3376  C  CG2 . VAL D  1 7   ? 19.239 25.071   -16.196  1.00 121.70 ? 8   VAL D CG2 1 
ATOM   3377  N  N   . LEU D  1 8   ? 20.200 25.632   -11.595  1.00 123.85 ? 9   LEU D N   1 
ATOM   3378  C  CA  . LEU D  1 8   ? 20.538 25.550   -10.182  1.00 124.65 ? 9   LEU D CA  1 
ATOM   3379  C  C   . LEU D  1 8   ? 19.296 25.330   -9.323   1.00 126.60 ? 9   LEU D C   1 
ATOM   3380  O  O   . LEU D  1 8   ? 19.079 26.029   -8.339   1.00 128.52 ? 9   LEU D O   1 
ATOM   3381  C  CB  . LEU D  1 8   ? 21.275 26.829   -9.758   1.00 125.75 ? 9   LEU D CB  1 
ATOM   3382  C  CG  . LEU D  1 8   ? 22.301 26.696   -8.630   1.00 125.16 ? 9   LEU D CG  1 
ATOM   3383  C  CD1 . LEU D  1 8   ? 23.472 27.660   -8.854   1.00 124.97 ? 9   LEU D CD1 1 
ATOM   3384  C  CD2 . LEU D  1 8   ? 21.675 26.903   -7.263   1.00 125.91 ? 9   LEU D CD2 1 
ATOM   3385  N  N   . LYS D  1 9   ? 18.476 24.352   -9.699   1.00 126.83 ? 10  LYS D N   1 
ATOM   3386  C  CA  . LYS D  1 9   ? 17.461 23.817   -8.786   1.00 128.45 ? 10  LYS D CA  1 
ATOM   3387  C  C   . LYS D  1 9   ? 18.245 23.133   -7.635   1.00 128.55 ? 10  LYS D C   1 
ATOM   3388  O  O   . LYS D  1 9   ? 19.464 23.305   -7.528   1.00 127.82 ? 10  LYS D O   1 
ATOM   3389  C  CB  . LYS D  1 9   ? 16.523 22.808   -9.485   1.00 127.93 ? 10  LYS D CB  1 
ATOM   3390  C  CG  . LYS D  1 9   ? 15.888 23.236   -10.829  1.00 128.74 ? 10  LYS D CG  1 
ATOM   3391  C  CD  . LYS D  1 9   ? 15.177 22.026   -11.495  1.00 128.41 ? 10  LYS D CD  1 
ATOM   3392  C  CE  . LYS D  1 9   ? 14.719 22.307   -12.933  1.00 128.57 ? 10  LYS D CE  1 
ATOM   3393  N  NZ  . LYS D  1 9   ? 15.864 22.549   -13.866  1.00 126.36 ? 10  LYS D NZ  1 
ATOM   3394  N  N   . GLY D  1 10  ? 17.576 22.367   -6.774   1.00 129.61 ? 11  GLY D N   1 
ATOM   3395  C  CA  . GLY D  1 10  ? 18.277 21.688   -5.689   1.00 129.73 ? 11  GLY D CA  1 
ATOM   3396  C  C   . GLY D  1 10  ? 17.351 20.934   -4.777   1.00 131.15 ? 11  GLY D C   1 
ATOM   3397  O  O   . GLY D  1 10  ? 17.155 19.740   -4.987   1.00 130.32 ? 11  GLY D O   1 
ATOM   3398  N  N   . ASP D  1 11  ? 16.780 21.617   -3.775   1.00 134.06 ? 12  ASP D N   1 
ATOM   3399  C  CA  . ASP D  1 11  ? 15.823 20.976   -2.833   1.00 135.77 ? 12  ASP D CA  1 
ATOM   3400  C  C   . ASP D  1 11  ? 14.652 21.901   -2.385   1.00 138.90 ? 12  ASP D C   1 
ATOM   3401  O  O   . ASP D  1 11  ? 14.123 21.769   -1.260   1.00 140.68 ? 12  ASP D O   1 
ATOM   3402  C  CB  . ASP D  1 11  ? 16.580 20.404   -1.608   1.00 135.75 ? 12  ASP D CB  1 
ATOM   3403  C  CG  . ASP D  1 11  ? 15.900 19.159   -1.006   1.00 135.36 ? 12  ASP D CG  1 
ATOM   3404  O  OD1 . ASP D  1 11  ? 15.766 18.130   -1.708   1.00 133.57 ? 12  ASP D OD1 1 
ATOM   3405  O  OD2 . ASP D  1 11  ? 15.521 19.209   0.182    1.00 136.75 ? 12  ASP D OD2 1 
ATOM   3406  N  N   . GLY D  1 12  ? 14.229 22.806   -3.277   1.00 140.02 ? 13  GLY D N   1 
ATOM   3407  C  CA  . GLY D  1 12  ? 13.154 23.770   -2.976   1.00 142.60 ? 13  GLY D CA  1 
ATOM   3408  C  C   . GLY D  1 12  ? 13.635 24.903   -2.062   1.00 144.67 ? 13  GLY D C   1 
ATOM   3409  O  O   . GLY D  1 12  ? 14.617 24.722   -1.311   1.00 144.22 ? 13  GLY D O   1 
ATOM   3410  N  N   . PRO D  1 13  ? 13.004 26.108   -2.161   1.00 146.93 ? 14  PRO D N   1 
ATOM   3411  C  CA  . PRO D  1 13  ? 12.088 26.624   -3.206   1.00 147.48 ? 14  PRO D CA  1 
ATOM   3412  C  C   . PRO D  1 13  ? 12.779 27.571   -4.230   1.00 147.01 ? 14  PRO D C   1 
ATOM   3413  O  O   . PRO D  1 13  ? 12.114 28.465   -4.789   1.00 148.60 ? 14  PRO D O   1 
ATOM   3414  C  CB  . PRO D  1 13  ? 11.041 27.390   -2.380   1.00 150.69 ? 14  PRO D CB  1 
ATOM   3415  C  CG  . PRO D  1 13  ? 11.767 27.828   -1.112   1.00 151.80 ? 14  PRO D CG  1 
ATOM   3416  C  CD  . PRO D  1 13  ? 13.069 27.050   -1.023   1.00 149.59 ? 14  PRO D CD  1 
ATOM   3417  N  N   . VAL D  1 14  ? 14.066 27.299   -4.520   1.00 144.67 ? 15  VAL D N   1 
ATOM   3418  C  CA  . VAL D  1 14  ? 15.047 28.317   -4.956   1.00 144.44 ? 15  VAL D CA  1 
ATOM   3419  C  C   . VAL D  1 14  ? 15.875 27.964   -6.234   1.00 141.87 ? 15  VAL D C   1 
ATOM   3420  O  O   . VAL D  1 14  ? 17.057 27.587   -6.136   1.00 139.94 ? 15  VAL D O   1 
ATOM   3421  C  CB  . VAL D  1 14  ? 16.005 28.591   -3.766   1.00 145.01 ? 15  VAL D CB  1 
ATOM   3422  C  CG1 . VAL D  1 14  ? 16.956 27.410   -3.570   1.00 141.88 ? 15  VAL D CG1 1 
ATOM   3423  C  CG2 . VAL D  1 14  ? 16.750 29.871   -3.959   1.00 146.31 ? 15  VAL D CG2 1 
ATOM   3424  N  N   . GLN D  1 15  ? 15.255 28.117   -7.418   1.00 141.71 ? 16  GLN D N   1 
ATOM   3425  C  CA  . GLN D  1 15  ? 15.912 27.808   -8.719   1.00 139.66 ? 16  GLN D CA  1 
ATOM   3426  C  C   . GLN D  1 15  ? 16.839 28.923   -9.148   1.00 139.96 ? 16  GLN D C   1 
ATOM   3427  O  O   . GLN D  1 15  ? 16.878 29.981   -8.502   1.00 142.21 ? 16  GLN D O   1 
ATOM   3428  C  CB  . GLN D  1 15  ? 14.916 27.600   -9.882   1.00 139.67 ? 16  GLN D CB  1 
ATOM   3429  C  CG  . GLN D  1 15  ? 13.945 26.467   -9.721   1.00 139.36 ? 16  GLN D CG  1 
ATOM   3430  C  CD  . GLN D  1 15  ? 12.618 26.960   -9.233   1.00 141.65 ? 16  GLN D CD  1 
ATOM   3431  O  OE1 . GLN D  1 15  ? 11.975 27.795   -9.884   1.00 142.02 ? 16  GLN D OE1 1 
ATOM   3432  N  NE2 . GLN D  1 15  ? 12.197 26.464   -8.069   1.00 142.49 ? 16  GLN D NE2 1 
ATOM   3433  N  N   . GLY D  1 16  ? 17.562 28.673   -10.250  1.00 137.83 ? 17  GLY D N   1 
ATOM   3434  C  CA  . GLY D  1 16  ? 18.446 29.666   -10.875  1.00 137.72 ? 17  GLY D CA  1 
ATOM   3435  C  C   . GLY D  1 16  ? 18.659 29.418   -12.353  1.00 135.93 ? 17  GLY D C   1 
ATOM   3436  O  O   . GLY D  1 16  ? 18.487 28.293   -12.828  1.00 134.11 ? 17  GLY D O   1 
ATOM   3437  N  N   . ILE D  1 17  ? 18.998 30.482   -13.079  1.00 136.63 ? 18  ILE D N   1 
ATOM   3438  C  CA  . ILE D  1 17  ? 19.355 30.381   -14.508  1.00 135.56 ? 18  ILE D CA  1 
ATOM   3439  C  C   . ILE D  1 17  ? 20.591 31.231   -14.837  1.00 135.30 ? 18  ILE D C   1 
ATOM   3440  O  O   . ILE D  1 17  ? 20.526 32.241   -15.586  1.00 136.79 ? 18  ILE D O   1 
ATOM   3441  C  CB  . ILE D  1 17  ? 18.129 30.649   -15.488  1.00 136.96 ? 18  ILE D CB  1 
ATOM   3442  C  CG1 . ILE D  1 17  ? 17.533 29.294   -15.954  1.00 136.04 ? 18  ILE D CG1 1 
ATOM   3443  C  CG2 . ILE D  1 17  ? 18.501 31.579   -16.723  1.00 136.65 ? 18  ILE D CG2 1 
ATOM   3444  C  CD1 . ILE D  1 17  ? 18.566 28.234   -16.484  1.00 133.74 ? 18  ILE D CD1 1 
ATOM   3445  N  N   . ILE D  1 18  ? 21.720 30.773   -14.279  1.00 133.12 ? 19  ILE D N   1 
ATOM   3446  C  CA  . ILE D  1 18  ? 23.038 31.368   -14.524  1.00 132.01 ? 19  ILE D CA  1 
ATOM   3447  C  C   . ILE D  1 18  ? 23.402 31.275   -16.028  1.00 129.96 ? 19  ILE D C   1 
ATOM   3448  O  O   . ILE D  1 18  ? 22.703 30.621   -16.825  1.00 129.30 ? 19  ILE D O   1 
ATOM   3449  C  CB  . ILE D  1 18  ? 24.137 30.676   -13.621  1.00 130.86 ? 19  ILE D CB  1 
ATOM   3450  C  CG1 . ILE D  1 18  ? 23.774 30.758   -12.138  1.00 132.11 ? 19  ILE D CG1 1 
ATOM   3451  C  CG2 . ILE D  1 18  ? 25.502 31.310   -13.799  1.00 131.03 ? 19  ILE D CG2 1 
ATOM   3452  C  CD1 . ILE D  1 18  ? 23.411 32.167   -11.681  1.00 135.67 ? 19  ILE D CD1 1 
ATOM   3453  N  N   . ASN D  1 19  ? 24.454 31.991   -16.413  1.00 128.90 ? 20  ASN D N   1 
ATOM   3454  C  CA  . ASN D  1 19  ? 25.162 31.747   -17.662  1.00 126.66 ? 20  ASN D CA  1 
ATOM   3455  C  C   . ASN D  1 19  ? 26.655 31.762   -17.424  1.00 125.54 ? 20  ASN D C   1 
ATOM   3456  O  O   . ASN D  1 19  ? 27.118 31.960   -16.304  1.00 125.58 ? 20  ASN D O   1 
ATOM   3457  C  CB  . ASN D  1 19  ? 24.813 32.802   -18.707  1.00 127.65 ? 20  ASN D CB  1 
ATOM   3458  C  CG  . ASN D  1 19  ? 23.547 32.497   -19.420  1.00 127.48 ? 20  ASN D CG  1 
ATOM   3459  O  OD1 . ASN D  1 19  ? 23.083 31.354   -19.438  1.00 125.32 ? 20  ASN D OD1 1 
ATOM   3460  N  ND2 . ASN D  1 19  ? 22.974 33.516   -20.041  1.00 129.41 ? 20  ASN D ND2 1 
ATOM   3461  N  N   . PHE D  1 20  ? 27.398 31.499   -18.486  1.00 124.19 ? 21  PHE D N   1 
ATOM   3462  C  CA  . PHE D  1 20  ? 28.812 31.774   -18.511  1.00 124.14 ? 21  PHE D CA  1 
ATOM   3463  C  C   . PHE D  1 20  ? 29.169 32.202   -19.934  1.00 123.92 ? 21  PHE D C   1 
ATOM   3464  O  O   . PHE D  1 20  ? 28.380 32.042   -20.877  1.00 123.34 ? 21  PHE D O   1 
ATOM   3465  C  CB  . PHE D  1 20  ? 29.631 30.552   -18.083  1.00 122.66 ? 21  PHE D CB  1 
ATOM   3466  C  CG  . PHE D  1 20  ? 29.400 30.108   -16.634  1.00 124.57 ? 21  PHE D CG  1 
ATOM   3467  C  CD1 . PHE D  1 20  ? 28.161 29.572   -16.216  1.00 125.23 ? 21  PHE D CD1 1 
ATOM   3468  C  CD2 . PHE D  1 20  ? 30.438 30.174   -15.690  1.00 126.23 ? 21  PHE D CD2 1 
ATOM   3469  C  CE1 . PHE D  1 20  ? 27.955 29.145   -14.881  1.00 125.46 ? 21  PHE D CE1 1 
ATOM   3470  C  CE2 . PHE D  1 20  ? 30.237 29.748   -14.345  1.00 126.34 ? 21  PHE D CE2 1 
ATOM   3471  C  CZ  . PHE D  1 20  ? 28.996 29.234   -13.948  1.00 125.82 ? 21  PHE D CZ  1 
ATOM   3472  N  N   . GLU D  1 21  ? 30.346 32.806   -20.049  1.00 124.48 ? 22  GLU D N   1 
ATOM   3473  C  CA  . GLU D  1 21  ? 30.989 33.111   -21.336  1.00 124.24 ? 22  GLU D CA  1 
ATOM   3474  C  C   . GLU D  1 21  ? 32.484 33.420   -21.045  1.00 124.52 ? 22  GLU D C   1 
ATOM   3475  O  O   . GLU D  1 21  ? 32.801 34.211   -20.139  1.00 126.20 ? 22  GLU D O   1 
ATOM   3476  C  CB  . GLU D  1 21  ? 30.276 34.260   -22.094  1.00 125.52 ? 22  GLU D CB  1 
ATOM   3477  C  CG  . GLU D  1 21  ? 30.835 34.506   -23.518  1.00 125.42 ? 22  GLU D CG  1 
ATOM   3478  C  CD  . GLU D  1 21  ? 29.902 35.320   -24.446  1.00 127.33 ? 22  GLU D CD  1 
ATOM   3479  O  OE1 . GLU D  1 21  ? 28.847 35.813   -23.976  1.00 129.10 ? 22  GLU D OE1 1 
ATOM   3480  O  OE2 . GLU D  1 21  ? 30.224 35.462   -25.659  1.00 126.33 ? 22  GLU D OE2 1 
ATOM   3481  N  N   . GLN D  1 22  ? 33.386 32.741   -21.761  1.00 123.04 ? 23  GLN D N   1 
ATOM   3482  C  CA  . GLN D  1 22  ? 34.829 32.953   -21.624  1.00 123.10 ? 23  GLN D CA  1 
ATOM   3483  C  C   . GLN D  1 22  ? 35.370 33.222   -23.013  1.00 123.56 ? 23  GLN D C   1 
ATOM   3484  O  O   . GLN D  1 22  ? 35.475 32.312   -23.834  1.00 122.30 ? 23  GLN D O   1 
ATOM   3485  C  CB  . GLN D  1 22  ? 35.526 31.743   -20.982  1.00 121.50 ? 23  GLN D CB  1 
ATOM   3486  C  CG  . GLN D  1 22  ? 37.059 31.873   -20.850  1.00 120.75 ? 23  GLN D CG  1 
ATOM   3487  C  CD  . GLN D  1 22  ? 37.685 30.980   -19.752  1.00 118.95 ? 23  GLN D CD  1 
ATOM   3488  O  OE1 . GLN D  1 22  ? 37.062 30.685   -18.735  1.00 118.23 ? 23  GLN D OE1 1 
ATOM   3489  N  NE2 . GLN D  1 22  ? 38.934 30.579   -19.956  1.00 117.54 ? 23  GLN D NE2 1 
ATOM   3490  N  N   . LYS D  1 23  ? 35.694 34.491   -23.267  1.00 125.97 ? 24  LYS D N   1 
ATOM   3491  C  CA  . LYS D  1 23  ? 36.129 34.972   -24.601  1.00 126.51 ? 24  LYS D CA  1 
ATOM   3492  C  C   . LYS D  1 23  ? 37.416 34.301   -25.083  1.00 124.95 ? 24  LYS D C   1 
ATOM   3493  O  O   . LYS D  1 23  ? 37.463 33.725   -26.174  1.00 123.86 ? 24  LYS D O   1 
ATOM   3494  C  CB  . LYS D  1 23  ? 36.318 36.512   -24.591  1.00 129.10 ? 24  LYS D CB  1 
ATOM   3495  C  CG  . LYS D  1 23  ? 35.000 37.344   -24.558  1.00 131.70 ? 24  LYS D CG  1 
ATOM   3496  C  CD  . LYS D  1 23  ? 35.251 38.812   -24.143  1.00 135.68 ? 24  LYS D CD  1 
ATOM   3497  C  CE  . LYS D  1 23  ? 34.066 39.731   -24.499  1.00 137.79 ? 24  LYS D CE  1 
ATOM   3498  N  NZ  . LYS D  1 23  ? 34.381 41.187   -24.303  1.00 140.64 ? 24  LYS D NZ  1 
ATOM   3499  N  N   . GLU D  1 24  ? 38.449 34.381   -24.259  1.00 124.96 ? 25  GLU D N   1 
ATOM   3500  C  CA  . GLU D  1 24  ? 39.738 33.825   -24.615  1.00 124.40 ? 25  GLU D CA  1 
ATOM   3501  C  C   . GLU D  1 24  ? 40.237 32.926   -23.486  1.00 123.50 ? 25  GLU D C   1 
ATOM   3502  O  O   . GLU D  1 24  ? 40.086 33.249   -22.312  1.00 124.01 ? 25  GLU D O   1 
ATOM   3503  C  CB  . GLU D  1 24  ? 40.742 34.950   -24.927  1.00 126.19 ? 25  GLU D CB  1 
ATOM   3504  C  CG  . GLU D  1 24  ? 40.195 36.122   -25.805  1.00 127.59 ? 25  GLU D CG  1 
ATOM   3505  C  CD  . GLU D  1 24  ? 39.956 35.751   -27.273  1.00 127.00 ? 25  GLU D CD  1 
ATOM   3506  O  OE1 . GLU D  1 24  ? 39.894 34.541   -27.603  1.00 125.96 ? 25  GLU D OE1 1 
ATOM   3507  O  OE2 . GLU D  1 24  ? 39.830 36.685   -28.100  1.00 127.33 ? 25  GLU D OE2 1 
ATOM   3508  N  N   . SER D  1 25  ? 40.833 31.798   -23.866  1.00 122.07 ? 26  SER D N   1 
ATOM   3509  C  CA  . SER D  1 25  ? 41.206 30.756   -22.921  1.00 121.36 ? 26  SER D CA  1 
ATOM   3510  C  C   . SER D  1 25  ? 41.849 31.331   -21.667  1.00 122.96 ? 26  SER D C   1 
ATOM   3511  O  O   . SER D  1 25  ? 41.528 30.905   -20.552  1.00 123.07 ? 26  SER D O   1 
ATOM   3512  C  CB  . SER D  1 25  ? 42.155 29.737   -23.575  1.00 120.59 ? 26  SER D CB  1 
ATOM   3513  O  OG  . SER D  1 25  ? 43.510 29.924   -23.176  1.00 121.35 ? 26  SER D OG  1 
ATOM   3514  N  N   . ASN D  1 26  ? 42.746 32.301   -21.864  1.00 124.57 ? 27  ASN D N   1 
ATOM   3515  C  CA  . ASN D  1 26  ? 43.535 32.917   -20.767  1.00 126.60 ? 27  ASN D CA  1 
ATOM   3516  C  C   . ASN D  1 26  ? 42.884 34.150   -20.089  1.00 128.50 ? 27  ASN D C   1 
ATOM   3517  O  O   . ASN D  1 26  ? 43.544 34.905   -19.353  1.00 130.32 ? 27  ASN D O   1 
ATOM   3518  C  CB  . ASN D  1 26  ? 44.970 33.235   -21.242  1.00 127.38 ? 27  ASN D CB  1 
ATOM   3519  C  CG  . ASN D  1 26  ? 45.036 34.362   -22.290  1.00 128.43 ? 27  ASN D CG  1 
ATOM   3520  O  OD1 . ASN D  1 26  ? 46.099 34.948   -22.481  1.00 130.31 ? 27  ASN D OD1 1 
ATOM   3521  N  ND2 . ASN D  1 26  ? 43.919 34.656   -22.970  1.00 126.74 ? 27  ASN D ND2 1 
ATOM   3522  N  N   . GLY D  1 27  ? 41.579 34.314   -20.300  1.00 128.24 ? 28  GLY D N   1 
ATOM   3523  C  CA  . GLY D  1 27  ? 40.889 35.552   -19.963  1.00 130.14 ? 28  GLY D CA  1 
ATOM   3524  C  C   . GLY D  1 27  ? 39.954 35.525   -18.766  1.00 130.93 ? 28  GLY D C   1 
ATOM   3525  O  O   . GLY D  1 27  ? 40.194 34.801   -17.792  1.00 130.46 ? 28  GLY D O   1 
ATOM   3526  N  N   . PRO D  1 28  ? 38.888 36.353   -18.828  1.00 132.44 ? 29  PRO D N   1 
ATOM   3527  C  CA  . PRO D  1 28  ? 37.887 36.479   -17.764  1.00 133.60 ? 29  PRO D CA  1 
ATOM   3528  C  C   . PRO D  1 28  ? 36.612 35.670   -18.047  1.00 132.11 ? 29  PRO D C   1 
ATOM   3529  O  O   . PRO D  1 28  ? 36.532 34.977   -19.068  1.00 130.43 ? 29  PRO D O   1 
ATOM   3530  C  CB  . PRO D  1 28  ? 37.575 37.985   -17.781  1.00 136.03 ? 29  PRO D CB  1 
ATOM   3531  C  CG  . PRO D  1 28  ? 37.733 38.388   -19.258  1.00 135.33 ? 29  PRO D CG  1 
ATOM   3532  C  CD  . PRO D  1 28  ? 38.635 37.336   -19.912  1.00 133.11 ? 29  PRO D CD  1 
ATOM   3533  N  N   . VAL D  1 29  ? 35.626 35.774   -17.156  1.00 133.22 ? 30  VAL D N   1 
ATOM   3534  C  CA  . VAL D  1 29  ? 34.366 35.038   -17.304  1.00 132.17 ? 30  VAL D CA  1 
ATOM   3535  C  C   . VAL D  1 29  ? 33.139 35.824   -16.845  1.00 133.95 ? 30  VAL D C   1 
ATOM   3536  O  O   . VAL D  1 29  ? 32.894 35.946   -15.633  1.00 134.78 ? 30  VAL D O   1 
ATOM   3537  C  CB  . VAL D  1 29  ? 34.354 33.707   -16.485  1.00 131.06 ? 30  VAL D CB  1 
ATOM   3538  C  CG1 . VAL D  1 29  ? 33.214 32.797   -16.996  1.00 129.49 ? 30  VAL D CG1 1 
ATOM   3539  C  CG2 . VAL D  1 29  ? 35.732 32.987   -16.509  1.00 130.13 ? 30  VAL D CG2 1 
ATOM   3540  N  N   . LYS D  1 30  ? 32.360 36.318   -17.813  1.00 134.46 ? 31  LYS D N   1 
ATOM   3541  C  CA  . LYS D  1 30  ? 31.005 36.861   -17.551  1.00 136.32 ? 31  LYS D CA  1 
ATOM   3542  C  C   . LYS D  1 30  ? 30.123 35.839   -16.775  1.00 136.08 ? 31  LYS D C   1 
ATOM   3543  O  O   . LYS D  1 30  ? 30.525 34.672   -16.626  1.00 134.62 ? 31  LYS D O   1 
ATOM   3544  C  CB  . LYS D  1 30  ? 30.324 37.265   -18.875  1.00 136.07 ? 31  LYS D CB  1 
ATOM   3545  C  CG  . LYS D  1 30  ? 30.377 38.760   -19.206  1.00 138.09 ? 31  LYS D CG  1 
ATOM   3546  C  CD  . LYS D  1 30  ? 29.608 39.085   -20.507  1.00 137.23 ? 31  LYS D CD  1 
ATOM   3547  C  CE  . LYS D  1 30  ? 28.677 40.310   -20.377  1.00 139.15 ? 31  LYS D CE  1 
ATOM   3548  N  NZ  . LYS D  1 30  ? 29.372 41.633   -20.270  1.00 140.20 ? 31  LYS D NZ  1 
ATOM   3549  N  N   . VAL D  1 31  ? 28.949 36.266   -16.279  1.00 138.03 ? 32  VAL D N   1 
ATOM   3550  C  CA  . VAL D  1 31  ? 28.008 35.369   -15.549  1.00 137.74 ? 32  VAL D CA  1 
ATOM   3551  C  C   . VAL D  1 31  ? 26.649 36.036   -15.281  1.00 140.15 ? 32  VAL D C   1 
ATOM   3552  O  O   . VAL D  1 31  ? 26.553 36.831   -14.361  1.00 142.38 ? 32  VAL D O   1 
ATOM   3553  C  CB  . VAL D  1 31  ? 28.557 34.936   -14.126  1.00 138.01 ? 32  VAL D CB  1 
ATOM   3554  C  CG1 . VAL D  1 31  ? 27.441 34.284   -13.309  1.00 137.85 ? 32  VAL D CG1 1 
ATOM   3555  C  CG2 . VAL D  1 31  ? 29.787 34.000   -14.196  1.00 135.62 ? 32  VAL D CG2 1 
ATOM   3556  N  N   . TRP D  1 32  ? 25.589 35.703   -16.021  1.00 140.41 ? 33  TRP D N   1 
ATOM   3557  C  CA  . TRP D  1 32  ? 24.288 36.395   -15.812  1.00 143.45 ? 33  TRP D CA  1 
ATOM   3558  C  C   . TRP D  1 32  ? 22.950 35.644   -16.035  1.00 143.31 ? 33  TRP D C   1 
ATOM   3559  O  O   . TRP D  1 32  ? 22.892 34.598   -16.695  1.00 141.46 ? 33  TRP D O   1 
ATOM   3560  C  CB  . TRP D  1 32  ? 24.250 37.656   -16.668  1.00 145.48 ? 33  TRP D CB  1 
ATOM   3561  C  CG  . TRP D  1 32  ? 24.022 37.419   -18.137  1.00 145.90 ? 33  TRP D CG  1 
ATOM   3562  C  CD1 . TRP D  1 32  ? 22.858 37.627   -18.835  1.00 147.73 ? 33  TRP D CD1 1 
ATOM   3563  C  CD2 . TRP D  1 32  ? 24.988 36.960   -19.095  1.00 146.50 ? 33  TRP D CD2 1 
ATOM   3564  N  NE1 . TRP D  1 32  ? 23.037 37.318   -20.167  1.00 147.21 ? 33  TRP D NE1 1 
ATOM   3565  C  CE2 . TRP D  1 32  ? 24.332 36.910   -20.359  1.00 146.58 ? 33  TRP D CE2 1 
ATOM   3566  C  CE3 . TRP D  1 32  ? 26.343 36.581   -19.013  1.00 145.79 ? 33  TRP D CE3 1 
ATOM   3567  C  CZ2 . TRP D  1 32  ? 24.986 36.500   -21.535  1.00 145.37 ? 33  TRP D CZ2 1 
ATOM   3568  C  CZ3 . TRP D  1 32  ? 26.995 36.170   -20.185  1.00 145.08 ? 33  TRP D CZ3 1 
ATOM   3569  C  CH2 . TRP D  1 32  ? 26.310 36.137   -21.431  1.00 144.69 ? 33  TRP D CH2 1 
ATOM   3570  N  N   . GLY D  1 33  ? 21.875 36.226   -15.484  1.00 145.95 ? 34  GLY D N   1 
ATOM   3571  C  CA  . GLY D  1 33  ? 20.482 35.778   -15.737  1.00 146.31 ? 34  GLY D CA  1 
ATOM   3572  C  C   . GLY D  1 33  ? 19.383 36.267   -14.766  1.00 149.03 ? 34  GLY D C   1 
ATOM   3573  O  O   . GLY D  1 33  ? 18.533 37.110   -15.142  1.00 150.78 ? 34  GLY D O   1 
ATOM   3574  N  N   . SER D  1 34  ? 19.410 35.702   -13.536  1.00 148.98 ? 35  SER D N   1 
ATOM   3575  C  CA  . SER D  1 34  ? 18.402 35.892   -12.437  1.00 150.92 ? 35  SER D CA  1 
ATOM   3576  C  C   . SER D  1 34  ? 18.530 34.745   -11.357  1.00 149.71 ? 35  SER D C   1 
ATOM   3577  O  O   . SER D  1 34  ? 19.461 33.910   -11.425  1.00 147.01 ? 35  SER D O   1 
ATOM   3578  C  CB  . SER D  1 34  ? 16.954 36.011   -12.998  1.00 151.97 ? 35  SER D CB  1 
ATOM   3579  O  OG  . SER D  1 34  ? 15.960 36.049   -11.983  1.00 152.82 ? 35  SER D OG  1 
ATOM   3580  N  N   . ILE D  1 35  ? 17.637 34.781   -10.348  1.00 151.72 ? 36  ILE D N   1 
ATOM   3581  C  CA  . ILE D  1 35  ? 17.363 33.674   -9.374   1.00 150.79 ? 36  ILE D CA  1 
ATOM   3582  C  C   . ILE D  1 35  ? 15.950 33.854   -8.739   1.00 153.61 ? 36  ILE D C   1 
ATOM   3583  O  O   . ILE D  1 35  ? 15.814 34.424   -7.635   1.00 155.90 ? 36  ILE D O   1 
ATOM   3584  C  CB  . ILE D  1 35  ? 18.429 33.527   -8.191   1.00 150.44 ? 36  ILE D CB  1 
ATOM   3585  C  CG1 . ILE D  1 35  ? 19.762 32.937   -8.662   1.00 147.22 ? 36  ILE D CG1 1 
ATOM   3586  C  CG2 . ILE D  1 35  ? 17.904 32.605   -7.058   1.00 149.54 ? 36  ILE D CG2 1 
ATOM   3587  C  CD1 . ILE D  1 35  ? 20.550 32.220   -7.537   1.00 145.47 ? 36  ILE D CD1 1 
ATOM   3588  N  N   . LYS D  1 36  ? 14.917 33.351   -9.424   1.00 153.66 ? 37  LYS D N   1 
ATOM   3589  C  CA  . LYS D  1 36  ? 13.547 33.323   -8.862   1.00 156.08 ? 37  LYS D CA  1 
ATOM   3590  C  C   . LYS D  1 36  ? 13.337 32.223   -7.774   1.00 155.87 ? 37  LYS D C   1 
ATOM   3591  O  O   . LYS D  1 36  ? 13.492 31.011   -8.025   1.00 152.94 ? 37  LYS D O   1 
ATOM   3592  C  CB  . LYS D  1 36  ? 12.491 33.211   -9.974   1.00 156.13 ? 37  LYS D CB  1 
ATOM   3593  C  CG  . LYS D  1 36  ? 12.301 31.816   -10.544  1.00 152.81 ? 37  LYS D CG  1 
ATOM   3594  C  CD  . LYS D  1 36  ? 11.634 31.851   -11.904  1.00 151.74 ? 37  LYS D CD  1 
ATOM   3595  C  CE  . LYS D  1 36  ? 11.530 30.461   -12.485  1.00 148.68 ? 37  LYS D CE  1 
ATOM   3596  N  NZ  . LYS D  1 36  ? 10.963 30.500   -13.841  1.00 148.29 ? 37  LYS D NZ  1 
ATOM   3597  N  N   . GLY D  1 37  ? 12.979 32.688   -6.572   1.00 159.19 ? 38  GLY D N   1 
ATOM   3598  C  CA  . GLY D  1 37  ? 12.804 31.847   -5.381   1.00 159.58 ? 38  GLY D CA  1 
ATOM   3599  C  C   . GLY D  1 37  ? 13.346 32.476   -4.094   1.00 162.20 ? 38  GLY D C   1 
ATOM   3600  O  O   . GLY D  1 37  ? 12.781 32.265   -3.007   1.00 163.63 ? 38  GLY D O   1 
ATOM   3601  N  N   . LEU D  1 38  ? 14.422 33.264   -4.218   1.00 163.23 ? 39  LEU D N   1 
ATOM   3602  C  CA  . LEU D  1 38  ? 15.201 33.742   -3.050   1.00 165.34 ? 39  LEU D CA  1 
ATOM   3603  C  C   . LEU D  1 38  ? 14.475 34.658   -2.061   1.00 169.44 ? 39  LEU D C   1 
ATOM   3604  O  O   . LEU D  1 38  ? 13.380 35.176   -2.342   1.00 171.30 ? 39  LEU D O   1 
ATOM   3605  C  CB  . LEU D  1 38  ? 16.499 34.424   -3.508   1.00 165.14 ? 39  LEU D CB  1 
ATOM   3606  C  CG  . LEU D  1 38  ? 17.661 33.445   -3.645   1.00 162.66 ? 39  LEU D CG  1 
ATOM   3607  C  CD1 . LEU D  1 38  ? 18.812 34.112   -4.367   1.00 163.62 ? 39  LEU D CD1 1 
ATOM   3608  C  CD2 . LEU D  1 38  ? 18.094 32.911   -2.269   1.00 162.71 ? 39  LEU D CD2 1 
ATOM   3609  N  N   . THR D  1 39  ? 15.129 34.850   -0.910   1.00 171.09 ? 40  THR D N   1 
ATOM   3610  C  CA  . THR D  1 39  ? 14.588 35.633   0.215    1.00 175.37 ? 40  THR D CA  1 
ATOM   3611  C  C   . THR D  1 39  ? 14.787 37.191   0.020    1.00 178.62 ? 40  THR D C   1 
ATOM   3612  O  O   . THR D  1 39  ? 14.385 37.789   -1.008   1.00 178.47 ? 40  THR D O   1 
ATOM   3613  C  CB  . THR D  1 39  ? 15.123 35.037   1.651    1.00 175.99 ? 40  THR D CB  1 
ATOM   3614  O  OG1 . THR D  1 39  ? 16.504 35.371   1.910    1.00 176.52 ? 40  THR D OG1 1 
ATOM   3615  C  CG2 . THR D  1 39  ? 14.947 33.488   1.741    1.00 172.29 ? 40  THR D CG2 1 
ATOM   3616  N  N   . GLU D  1 40  ? 15.352 37.835   1.038    1.00 181.58 ? 41  GLU D N   1 
ATOM   3617  C  CA  . GLU D  1 40  ? 15.969 39.151   0.906    1.00 184.25 ? 41  GLU D CA  1 
ATOM   3618  C  C   . GLU D  1 40  ? 17.357 39.087   1.614    1.00 184.29 ? 41  GLU D C   1 
ATOM   3619  O  O   . GLU D  1 40  ? 17.520 38.437   2.671    1.00 184.40 ? 41  GLU D O   1 
ATOM   3620  C  CB  . GLU D  1 40  ? 15.048 40.227   1.500    1.00 189.01 ? 41  GLU D CB  1 
ATOM   3621  C  CG  . GLU D  1 40  ? 15.519 41.664   1.290    1.00 192.09 ? 41  GLU D CG  1 
ATOM   3622  C  CD  . GLU D  1 40  ? 15.020 42.602   2.376    1.00 197.14 ? 41  GLU D CD  1 
ATOM   3623  O  OE1 . GLU D  1 40  ? 13.806 42.904   2.390    1.00 199.51 ? 41  GLU D OE1 1 
ATOM   3624  O  OE2 . GLU D  1 40  ? 15.846 43.034   3.212    1.00 198.38 ? 41  GLU D OE2 1 
ATOM   3625  N  N   . GLY D  1 41  ? 18.358 39.719   1.000    1.00 184.07 ? 42  GLY D N   1 
ATOM   3626  C  CA  . GLY D  1 41  ? 19.728 39.725   1.535    1.00 184.05 ? 42  GLY D CA  1 
ATOM   3627  C  C   . GLY D  1 41  ? 20.678 38.715   0.895    1.00 179.64 ? 42  GLY D C   1 
ATOM   3628  O  O   . GLY D  1 41  ? 20.425 38.168   -0.188   1.00 176.38 ? 42  GLY D O   1 
ATOM   3629  N  N   . LEU D  1 42  ? 21.771 38.451   1.600    1.00 179.75 ? 43  LEU D N   1 
ATOM   3630  C  CA  . LEU D  1 42  ? 22.869 37.638   1.073    1.00 176.20 ? 43  LEU D CA  1 
ATOM   3631  C  C   . LEU D  1 42  ? 22.571 36.128   1.136    1.00 172.67 ? 43  LEU D C   1 
ATOM   3632  O  O   . LEU D  1 42  ? 22.147 35.589   2.168    1.00 173.40 ? 43  LEU D O   1 
ATOM   3633  C  CB  . LEU D  1 42  ? 24.182 37.909   1.828    1.00 178.00 ? 43  LEU D CB  1 
ATOM   3634  C  CG  . LEU D  1 42  ? 24.307 39.061   2.837    1.00 183.56 ? 43  LEU D CG  1 
ATOM   3635  C  CD1 . LEU D  1 42  ? 23.723 38.680   4.234    1.00 185.30 ? 43  LEU D CD1 1 
ATOM   3636  C  CD2 . LEU D  1 42  ? 25.776 39.485   2.944    1.00 185.36 ? 43  LEU D CD2 1 
ATOM   3637  N  N   . HIS D  1 43  ? 22.811 35.462   0.009    1.00 168.91 ? 44  HIS D N   1 
ATOM   3638  C  CA  . HIS D  1 43  ? 22.793 33.996   -0.089   1.00 165.09 ? 44  HIS D CA  1 
ATOM   3639  C  C   . HIS D  1 43  ? 24.127 33.564   -0.770   1.00 161.91 ? 44  HIS D C   1 
ATOM   3640  O  O   . HIS D  1 43  ? 24.342 33.846   -1.972   1.00 160.36 ? 44  HIS D O   1 
ATOM   3641  C  CB  . HIS D  1 43  ? 21.544 33.514   -0.879   1.00 163.50 ? 44  HIS D CB  1 
ATOM   3642  C  CG  . HIS D  1 43  ? 20.240 33.666   -0.132   1.00 166.26 ? 44  HIS D CG  1 
ATOM   3643  N  ND1 . HIS D  1 43  ? 19.577 32.599   0.444    1.00 165.80 ? 44  HIS D ND1 1 
ATOM   3644  C  CD2 . HIS D  1 43  ? 19.471 34.756   0.114    1.00 169.61 ? 44  HIS D CD2 1 
ATOM   3645  C  CE1 . HIS D  1 43  ? 18.466 33.025   1.019    1.00 167.69 ? 44  HIS D CE1 1 
ATOM   3646  N  NE2 . HIS D  1 43  ? 18.380 34.331   0.836    1.00 170.47 ? 44  HIS D NE2 1 
ATOM   3647  N  N   . GLY D  1 44  ? 25.017 32.930   0.018    1.00 160.63 ? 45  GLY D N   1 
ATOM   3648  C  CA  . GLY D  1 44  ? 26.342 32.431   -0.446   1.00 157.69 ? 45  GLY D CA  1 
ATOM   3649  C  C   . GLY D  1 44  ? 26.312 31.618   -1.740   1.00 153.26 ? 45  GLY D C   1 
ATOM   3650  O  O   . GLY D  1 44  ? 25.300 30.986   -2.069   1.00 151.58 ? 45  GLY D O   1 
ATOM   3651  N  N   . PHE D  1 45  ? 27.430 31.609   -2.465   1.00 150.98 ? 46  PHE D N   1 
ATOM   3652  C  CA  . PHE D  1 45  ? 27.405 31.262   -3.889   1.00 147.51 ? 46  PHE D CA  1 
ATOM   3653  C  C   . PHE D  1 45  ? 28.744 30.742   -4.450   1.00 145.11 ? 46  PHE D C   1 
ATOM   3654  O  O   . PHE D  1 45  ? 29.596 31.538   -4.874   1.00 145.76 ? 46  PHE D O   1 
ATOM   3655  C  CB  . PHE D  1 45  ? 26.947 32.502   -4.669   1.00 148.55 ? 46  PHE D CB  1 
ATOM   3656  C  CG  . PHE D  1 45  ? 26.973 32.325   -6.135   1.00 146.44 ? 46  PHE D CG  1 
ATOM   3657  C  CD1 . PHE D  1 45  ? 26.443 31.184   -6.710   1.00 144.73 ? 46  PHE D CD1 1 
ATOM   3658  C  CD2 . PHE D  1 45  ? 27.528 33.290   -6.948   1.00 147.59 ? 46  PHE D CD2 1 
ATOM   3659  C  CE1 . PHE D  1 45  ? 26.466 31.006   -8.070   1.00 143.72 ? 46  PHE D CE1 1 
ATOM   3660  C  CE2 . PHE D  1 45  ? 27.555 33.124   -8.322   1.00 146.40 ? 46  PHE D CE2 1 
ATOM   3661  C  CZ  . PHE D  1 45  ? 27.020 31.983   -8.887   1.00 144.22 ? 46  PHE D CZ  1 
ATOM   3662  N  N   . HIS D  1 46  ? 28.906 29.410   -4.486   1.00 142.10 ? 47  HIS D N   1 
ATOM   3663  C  CA  . HIS D  1 46  ? 30.225 28.778   -4.786   1.00 140.08 ? 47  HIS D CA  1 
ATOM   3664  C  C   . HIS D  1 46  ? 30.240 27.633   -5.859   1.00 136.42 ? 47  HIS D C   1 
ATOM   3665  O  O   . HIS D  1 46  ? 29.269 27.425   -6.620   1.00 134.79 ? 47  HIS D O   1 
ATOM   3666  C  CB  . HIS D  1 46  ? 30.899 28.273   -3.471   1.00 141.16 ? 47  HIS D CB  1 
ATOM   3667  C  CG  . HIS D  1 46  ? 30.980 29.299   -2.385   1.00 143.58 ? 47  HIS D CG  1 
ATOM   3668  N  ND1 . HIS D  1 46  ? 29.920 29.580   -1.550   1.00 145.07 ? 47  HIS D ND1 1 
ATOM   3669  C  CD2 . HIS D  1 46  ? 31.998 30.094   -1.984   1.00 144.36 ? 47  HIS D CD2 1 
ATOM   3670  C  CE1 . HIS D  1 46  ? 30.280 30.515   -0.691   1.00 148.13 ? 47  HIS D CE1 1 
ATOM   3671  N  NE2 . HIS D  1 46  ? 31.537 30.845   -0.935   1.00 147.79 ? 47  HIS D NE2 1 
ATOM   3672  N  N   . VAL D  1 47  ? 31.394 26.950   -5.913   1.00 134.76 ? 48  VAL D N   1 
ATOM   3673  C  CA  . VAL D  1 47  ? 31.631 25.759   -6.722   1.00 131.72 ? 48  VAL D CA  1 
ATOM   3674  C  C   . VAL D  1 47  ? 32.226 24.657   -5.858   1.00 131.01 ? 48  VAL D C   1 
ATOM   3675  O  O   . VAL D  1 47  ? 33.115 24.912   -5.035   1.00 132.01 ? 48  VAL D O   1 
ATOM   3676  C  CB  . VAL D  1 47  ? 32.615 26.059   -7.881   1.00 131.00 ? 48  VAL D CB  1 
ATOM   3677  C  CG1 . VAL D  1 47  ? 33.532 24.863   -8.175   1.00 128.73 ? 48  VAL D CG1 1 
ATOM   3678  C  CG2 . VAL D  1 47  ? 31.833 26.486   -9.129   1.00 130.54 ? 48  VAL D CG2 1 
ATOM   3679  N  N   . HIS D  1 48  ? 31.730 23.438   -6.066   1.00 128.92 ? 49  HIS D N   1 
ATOM   3680  C  CA  . HIS D  1 48  ? 32.171 22.256   -5.308   1.00 128.47 ? 49  HIS D CA  1 
ATOM   3681  C  C   . HIS D  1 48  ? 32.833 21.185   -6.193   1.00 125.97 ? 49  HIS D C   1 
ATOM   3682  O  O   . HIS D  1 48  ? 32.644 21.163   -7.421   1.00 124.52 ? 49  HIS D O   1 
ATOM   3683  C  CB  . HIS D  1 48  ? 30.999 21.614   -4.551   1.00 128.79 ? 49  HIS D CB  1 
ATOM   3684  C  CG  . HIS D  1 48  ? 30.341 22.514   -3.546   1.00 131.68 ? 49  HIS D CG  1 
ATOM   3685  N  ND1 . HIS D  1 48  ? 30.596 22.433   -2.191   1.00 133.09 ? 49  HIS D ND1 1 
ATOM   3686  C  CD2 . HIS D  1 48  ? 29.406 23.485   -3.701   1.00 132.62 ? 49  HIS D CD2 1 
ATOM   3687  C  CE1 . HIS D  1 48  ? 29.861 23.330   -1.558   1.00 135.29 ? 49  HIS D CE1 1 
ATOM   3688  N  NE2 . HIS D  1 48  ? 29.132 23.981   -2.450   1.00 135.16 ? 49  HIS D NE2 1 
ATOM   3689  N  N   . GLU D  1 49  ? 33.555 20.276   -5.522   1.00 125.35 ? 50  GLU D N   1 
ATOM   3690  C  CA  . GLU D  1 49  ? 34.533 19.360   -6.134   1.00 123.64 ? 50  GLU D CA  1 
ATOM   3691  C  C   . GLU D  1 49  ? 33.903 18.264   -6.977   1.00 121.40 ? 50  GLU D C   1 
ATOM   3692  O  O   . GLU D  1 49  ? 34.615 17.609   -7.740   1.00 120.60 ? 50  GLU D O   1 
ATOM   3693  C  CB  . GLU D  1 49  ? 35.402 18.706   -5.041   1.00 124.85 ? 50  GLU D CB  1 
ATOM   3694  C  CG  . GLU D  1 49  ? 36.643 17.910   -5.534   1.00 124.58 ? 50  GLU D CG  1 
ATOM   3695  C  CD  . GLU D  1 49  ? 37.255 16.978   -4.463   1.00 125.25 ? 50  GLU D CD  1 
ATOM   3696  O  OE1 . GLU D  1 49  ? 37.007 17.182   -3.252   1.00 125.85 ? 50  GLU D OE1 1 
ATOM   3697  O  OE2 . GLU D  1 49  ? 37.986 16.031   -4.843   1.00 124.07 ? 50  GLU D OE2 1 
ATOM   3698  N  N   . PHE D  1 50  ? 32.591 18.047   -6.833   1.00 120.44 ? 51  PHE D N   1 
ATOM   3699  C  CA  . PHE D  1 50  ? 31.875 17.064   -7.654   1.00 118.47 ? 51  PHE D CA  1 
ATOM   3700  C  C   . PHE D  1 50  ? 30.513 17.542   -8.161   1.00 117.67 ? 51  PHE D C   1 
ATOM   3701  O  O   . PHE D  1 50  ? 29.932 18.496   -7.633   1.00 118.44 ? 51  PHE D O   1 
ATOM   3702  C  CB  . PHE D  1 50  ? 31.727 15.753   -6.889   1.00 118.49 ? 51  PHE D CB  1 
ATOM   3703  C  CG  . PHE D  1 50  ? 33.034 15.170   -6.461   1.00 119.71 ? 51  PHE D CG  1 
ATOM   3704  C  CD1 . PHE D  1 50  ? 34.053 14.966   -7.393   1.00 120.04 ? 51  PHE D CD1 1 
ATOM   3705  C  CD2 . PHE D  1 50  ? 33.266 14.842   -5.136   1.00 121.83 ? 51  PHE D CD2 1 
ATOM   3706  C  CE1 . PHE D  1 50  ? 35.286 14.441   -7.017   1.00 121.45 ? 51  PHE D CE1 1 
ATOM   3707  C  CE2 . PHE D  1 50  ? 34.501 14.309   -4.745   1.00 123.39 ? 51  PHE D CE2 1 
ATOM   3708  C  CZ  . PHE D  1 50  ? 35.513 14.101   -5.692   1.00 123.01 ? 51  PHE D CZ  1 
ATOM   3709  N  N   . GLY D  1 51  ? 30.052 16.876   -9.227   1.00 116.12 ? 52  GLY D N   1 
ATOM   3710  C  CA  . GLY D  1 51  ? 28.701 17.041   -9.821   1.00 115.33 ? 52  GLY D CA  1 
ATOM   3711  C  C   . GLY D  1 51  ? 27.950 15.729   -9.678   1.00 114.32 ? 52  GLY D C   1 
ATOM   3712  O  O   . GLY D  1 51  ? 28.115 14.822   -10.491  1.00 113.67 ? 52  GLY D O   1 
ATOM   3713  N  N   . ASP D  1 52  ? 27.122 15.645   -8.635   1.00 114.21 ? 53  ASP D N   1 
ATOM   3714  C  CA  . ASP D  1 52  ? 26.717 14.365   -8.044   1.00 113.17 ? 53  ASP D CA  1 
ATOM   3715  C  C   . ASP D  1 52  ? 25.329 14.531   -7.387   1.00 113.44 ? 53  ASP D C   1 
ATOM   3716  O  O   . ASP D  1 52  ? 25.198 14.545   -6.169   1.00 113.79 ? 53  ASP D O   1 
ATOM   3717  C  CB  . ASP D  1 52  ? 27.805 13.952   -7.018   1.00 113.41 ? 53  ASP D CB  1 
ATOM   3718  C  CG  . ASP D  1 52  ? 28.299 12.523   -7.189   1.00 111.33 ? 53  ASP D CG  1 
ATOM   3719  O  OD1 . ASP D  1 52  ? 27.460 11.629   -7.400   1.00 109.78 ? 53  ASP D OD1 1 
ATOM   3720  O  OD2 . ASP D  1 52  ? 29.528 12.300   -7.063   1.00 107.98 ? 53  ASP D OD2 1 
ATOM   3721  N  N   . ASN D  1 53  ? 24.296 14.667   -8.214   1.00 113.20 ? 54  ASN D N   1 
ATOM   3722  C  CA  . ASN D  1 53  ? 22.904 14.805   -7.728   1.00 114.39 ? 54  ASN D CA  1 
ATOM   3723  C  C   . ASN D  1 53  ? 22.243 13.458   -7.273   1.00 114.77 ? 54  ASN D C   1 
ATOM   3724  O  O   . ASN D  1 53  ? 20.991 13.341   -7.186   1.00 114.72 ? 54  ASN D O   1 
ATOM   3725  C  CB  . ASN D  1 53  ? 22.012 15.525   -8.779   1.00 114.56 ? 54  ASN D CB  1 
ATOM   3726  C  CG  . ASN D  1 53  ? 22.419 16.981   -9.022   1.00 114.36 ? 54  ASN D CG  1 
ATOM   3727  O  OD1 . ASN D  1 53  ? 23.519 17.270   -9.509   1.00 112.31 ? 54  ASN D OD1 1 
ATOM   3728  N  ND2 . ASN D  1 53  ? 21.509 17.901   -8.707   1.00 114.91 ? 54  ASN D ND2 1 
ATOM   3729  N  N   . THR D  1 54  ? 23.095 12.459   -6.995   1.00 114.91 ? 55  THR D N   1 
ATOM   3730  C  CA  . THR D  1 54  ? 22.690 11.228   -6.308   1.00 115.57 ? 55  THR D CA  1 
ATOM   3731  C  C   . THR D  1 54  ? 22.323 11.546   -4.860   1.00 117.38 ? 55  THR D C   1 
ATOM   3732  O  O   . THR D  1 54  ? 21.327 11.020   -4.352   1.00 118.02 ? 55  THR D O   1 
ATOM   3733  C  CB  . THR D  1 54  ? 23.797 10.111   -6.323   1.00 115.09 ? 55  THR D CB  1 
ATOM   3734  O  OG1 . THR D  1 54  ? 25.107 10.694   -6.413   1.00 114.17 ? 55  THR D OG1 1 
ATOM   3735  C  CG2 . THR D  1 54  ? 23.580 9.139    -7.489   1.00 114.34 ? 55  THR D CG2 1 
ATOM   3736  N  N   . ALA D  1 55  ? 23.136 12.386   -4.201   1.00 118.67 ? 56  ALA D N   1 
ATOM   3737  C  CA  . ALA D  1 55  ? 22.796 12.956   -2.874   1.00 120.65 ? 56  ALA D CA  1 
ATOM   3738  C  C   . ALA D  1 55  ? 22.531 14.481   -2.942   1.00 121.77 ? 56  ALA D C   1 
ATOM   3739  O  O   . ALA D  1 55  ? 22.656 15.209   -1.949   1.00 122.81 ? 56  ALA D O   1 
ATOM   3740  C  CB  . ALA D  1 55  ? 23.879 12.607   -1.825   1.00 121.29 ? 56  ALA D CB  1 
ATOM   3741  N  N   . GLY D  1 56  ? 22.112 14.927   -4.124   1.00 121.96 ? 57  GLY D N   1 
ATOM   3742  C  CA  . GLY D  1 56  ? 21.925 16.342   -4.435   1.00 123.17 ? 57  GLY D CA  1 
ATOM   3743  C  C   . GLY D  1 56  ? 23.145 17.232   -4.192   1.00 124.04 ? 57  GLY D C   1 
ATOM   3744  O  O   . GLY D  1 56  ? 24.312 16.856   -4.415   1.00 123.20 ? 57  GLY D O   1 
ATOM   3745  N  N   . CYS D  1 57  ? 22.835 18.432   -3.732   1.00 125.95 ? 58  CYS D N   1 
ATOM   3746  C  CA  . CYS D  1 57  ? 23.810 19.419   -3.345   1.00 127.36 ? 58  CYS D CA  1 
ATOM   3747  C  C   . CYS D  1 57  ? 24.922 18.790   -2.527   1.00 127.69 ? 58  CYS D C   1 
ATOM   3748  O  O   . CYS D  1 57  ? 26.095 18.966   -2.864   1.00 127.66 ? 58  CYS D O   1 
ATOM   3749  C  CB  . CYS D  1 57  ? 23.079 20.484   -2.534   1.00 129.51 ? 58  CYS D CB  1 
ATOM   3750  S  SG  . CYS D  1 57  ? 21.356 20.635   -3.096   1.00 131.11 ? 58  CYS D SG  1 
ATOM   3751  N  N   . THR D  1 58  ? 24.534 18.024   -1.497   1.00 128.49 ? 59  THR D N   1 
ATOM   3752  C  CA  . THR D  1 58  ? 25.456 17.472   -0.475   1.00 129.16 ? 59  THR D CA  1 
ATOM   3753  C  C   . THR D  1 58  ? 26.527 16.480   -0.996   1.00 128.22 ? 59  THR D C   1 
ATOM   3754  O  O   . THR D  1 58  ? 27.620 16.385   -0.422   1.00 128.79 ? 59  THR D O   1 
ATOM   3755  C  CB  . THR D  1 58  ? 24.663 16.814   0.721    1.00 130.04 ? 59  THR D CB  1 
ATOM   3756  O  OG1 . THR D  1 58  ? 25.466 16.859   1.897    1.00 131.63 ? 59  THR D OG1 1 
ATOM   3757  C  CG2 . THR D  1 58  ? 24.270 15.360   0.450    1.00 127.76 ? 59  THR D CG2 1 
ATOM   3758  N  N   . SER D  1 59  ? 26.222 15.757   -2.077   1.00 126.97 ? 60  SER D N   1 
ATOM   3759  C  CA  . SER D  1 59  ? 27.150 14.742   -2.614   1.00 126.12 ? 60  SER D CA  1 
ATOM   3760  C  C   . SER D  1 59  ? 28.333 15.355   -3.395   1.00 125.99 ? 60  SER D C   1 
ATOM   3761  O  O   . SER D  1 59  ? 29.432 14.782   -3.426   1.00 125.77 ? 60  SER D O   1 
ATOM   3762  C  CB  . SER D  1 59  ? 26.395 13.696   -3.454   1.00 124.86 ? 60  SER D CB  1 
ATOM   3763  O  OG  . SER D  1 59  ? 25.998 12.585   -2.654   1.00 125.06 ? 60  SER D OG  1 
ATOM   3764  N  N   . ALA D  1 60  ? 28.092 16.513   -4.015   1.00 126.38 ? 61  ALA D N   1 
ATOM   3765  C  CA  . ALA D  1 60  ? 29.154 17.356   -4.598   1.00 126.63 ? 61  ALA D CA  1 
ATOM   3766  C  C   . ALA D  1 60  ? 30.349 17.538   -3.627   1.00 128.17 ? 61  ALA D C   1 
ATOM   3767  O  O   . ALA D  1 60  ? 31.515 17.412   -4.017   1.00 127.71 ? 61  ALA D O   1 
ATOM   3768  C  CB  . ALA D  1 60  ? 28.562 18.725   -5.007   1.00 126.98 ? 61  ALA D CB  1 
ATOM   3769  N  N   . GLY D  1 61  ? 30.033 17.845   -2.368   1.00 130.19 ? 62  GLY D N   1 
ATOM   3770  C  CA  . GLY D  1 61  ? 30.997 17.804   -1.268   1.00 132.15 ? 62  GLY D CA  1 
ATOM   3771  C  C   . GLY D  1 61  ? 31.722 19.107   -0.958   1.00 134.30 ? 62  GLY D C   1 
ATOM   3772  O  O   . GLY D  1 61  ? 31.086 20.173   -0.845   1.00 135.08 ? 62  GLY D O   1 
ATOM   3773  N  N   . PRO D  1 62  ? 33.064 19.031   -0.807   1.00 135.58 ? 63  PRO D N   1 
ATOM   3774  C  CA  . PRO D  1 62  ? 33.840 20.199   -0.388   1.00 138.02 ? 63  PRO D CA  1 
ATOM   3775  C  C   . PRO D  1 62  ? 33.807 21.312   -1.422   1.00 138.14 ? 63  PRO D C   1 
ATOM   3776  O  O   . PRO D  1 62  ? 33.327 21.103   -2.537   1.00 135.97 ? 63  PRO D O   1 
ATOM   3777  C  CB  . PRO D  1 62  ? 35.266 19.648   -0.223   1.00 138.45 ? 63  PRO D CB  1 
ATOM   3778  C  CG  . PRO D  1 62  ? 35.325 18.486   -1.113   1.00 136.17 ? 63  PRO D CG  1 
ATOM   3779  C  CD  . PRO D  1 62  ? 33.939 17.892   -1.148   1.00 134.68 ? 63  PRO D CD  1 
ATOM   3780  N  N   . HIS D  1 63  ? 34.287 22.490   -1.024   1.00 141.18 ? 64  HIS D N   1 
ATOM   3781  C  CA  . HIS D  1 63  ? 34.332 23.664   -1.911   1.00 141.87 ? 64  HIS D CA  1 
ATOM   3782  C  C   . HIS D  1 63  ? 35.550 23.461   -2.835   1.00 140.73 ? 64  HIS D C   1 
ATOM   3783  O  O   . HIS D  1 63  ? 36.536 22.818   -2.443   1.00 141.09 ? 64  HIS D O   1 
ATOM   3784  C  CB  . HIS D  1 63  ? 34.354 25.003   -1.103   1.00 145.16 ? 64  HIS D CB  1 
ATOM   3785  C  CG  . HIS D  1 63  ? 32.988 25.484   -0.653   1.00 147.46 ? 64  HIS D CG  1 
ATOM   3786  N  ND1 . HIS D  1 63  ? 32.471 26.722   -0.993   1.00 149.06 ? 64  HIS D ND1 1 
ATOM   3787  C  CD2 . HIS D  1 63  ? 32.041 24.884   0.115    1.00 148.74 ? 64  HIS D CD2 1 
ATOM   3788  C  CE1 . HIS D  1 63  ? 31.269 26.857   -0.456   1.00 150.18 ? 64  HIS D CE1 1 
ATOM   3789  N  NE2 . HIS D  1 63  ? 30.982 25.755   0.215    1.00 149.76 ? 64  HIS D NE2 1 
ATOM   3790  N  N   . PHE D  1 64  ? 35.458 23.955   -4.071   1.00 139.35 ? 65  PHE D N   1 
ATOM   3791  C  CA  . PHE D  1 64  ? 36.392 23.526   -5.111   1.00 137.87 ? 65  PHE D CA  1 
ATOM   3792  C  C   . PHE D  1 64  ? 37.805 24.023   -4.872   1.00 138.98 ? 65  PHE D C   1 
ATOM   3793  O  O   . PHE D  1 64  ? 38.103 25.193   -5.116   1.00 140.02 ? 65  PHE D O   1 
ATOM   3794  C  CB  . PHE D  1 64  ? 35.915 23.958   -6.503   1.00 136.58 ? 65  PHE D CB  1 
ATOM   3795  C  CG  . PHE D  1 64  ? 36.888 23.599   -7.634   1.00 136.93 ? 65  PHE D CG  1 
ATOM   3796  C  CD1 . PHE D  1 64  ? 37.784 22.512   -7.523   1.00 136.93 ? 65  PHE D CD1 1 
ATOM   3797  C  CD2 . PHE D  1 64  ? 36.891 24.331   -8.823   1.00 137.29 ? 65  PHE D CD2 1 
ATOM   3798  C  CE1 . PHE D  1 64  ? 38.663 22.185   -8.571   1.00 135.40 ? 65  PHE D CE1 1 
ATOM   3799  C  CE2 . PHE D  1 64  ? 37.777 23.998   -9.873   1.00 136.02 ? 65  PHE D CE2 1 
ATOM   3800  C  CZ  . PHE D  1 64  ? 38.656 22.926   -9.739   1.00 134.89 ? 65  PHE D CZ  1 
ATOM   3801  N  N   . ASN D  1 65  ? 38.669 23.115   -4.424   1.00 138.78 ? 66  ASN D N   1 
ATOM   3802  C  CA  . ASN D  1 65  ? 40.064 23.449   -4.117   1.00 140.60 ? 66  ASN D CA  1 
ATOM   3803  C  C   . ASN D  1 65  ? 41.056 22.313   -4.465   1.00 139.69 ? 66  ASN D C   1 
ATOM   3804  O  O   . ASN D  1 65  ? 41.262 21.379   -3.674   1.00 139.96 ? 66  ASN D O   1 
ATOM   3805  C  CB  . ASN D  1 65  ? 40.212 23.868   -2.639   1.00 143.56 ? 66  ASN D CB  1 
ATOM   3806  C  CG  . ASN D  1 65  ? 41.644 24.315   -2.278   1.00 145.91 ? 66  ASN D CG  1 
ATOM   3807  O  OD1 . ASN D  1 65  ? 42.157 25.339   -2.784   1.00 146.11 ? 66  ASN D OD1 1 
ATOM   3808  N  ND2 . ASN D  1 65  ? 42.289 23.546   -1.392   1.00 145.49 ? 66  ASN D ND2 1 
ATOM   3809  N  N   . PRO D  1 66  ? 41.676 22.405   -5.655   1.00 138.56 ? 67  PRO D N   1 
ATOM   3810  C  CA  . PRO D  1 66  ? 42.680 21.474   -6.148   1.00 138.08 ? 67  PRO D CA  1 
ATOM   3811  C  C   . PRO D  1 66  ? 44.128 21.887   -5.880   1.00 140.29 ? 67  PRO D C   1 
ATOM   3812  O  O   . PRO D  1 66  ? 45.050 21.172   -6.282   1.00 140.03 ? 67  PRO D O   1 
ATOM   3813  C  CB  . PRO D  1 66  ? 42.425 21.484   -7.651   1.00 135.93 ? 67  PRO D CB  1 
ATOM   3814  C  CG  . PRO D  1 66  ? 42.033 22.885   -7.923   1.00 136.45 ? 67  PRO D CG  1 
ATOM   3815  C  CD  . PRO D  1 66  ? 41.317 23.386   -6.693   1.00 137.78 ? 67  PRO D CD  1 
ATOM   3816  N  N   . LEU D  1 67  ? 44.337 23.022   -5.224   1.00 142.78 ? 68  LEU D N   1 
ATOM   3817  C  CA  . LEU D  1 67  ? 45.701 23.435   -4.867   1.00 145.66 ? 68  LEU D CA  1 
ATOM   3818  C  C   . LEU D  1 67  ? 46.046 23.034   -3.407   1.00 148.12 ? 68  LEU D C   1 
ATOM   3819  O  O   . LEU D  1 67  ? 46.842 22.104   -3.192   1.00 148.81 ? 68  LEU D O   1 
ATOM   3820  C  CB  . LEU D  1 67  ? 45.926 24.943   -5.154   1.00 147.22 ? 68  LEU D CB  1 
ATOM   3821  C  CG  . LEU D  1 67  ? 46.425 25.340   -6.572   1.00 146.21 ? 68  LEU D CG  1 
ATOM   3822  C  CD1 . LEU D  1 67  ? 45.970 26.762   -6.965   1.00 146.77 ? 68  LEU D CD1 1 
ATOM   3823  C  CD2 . LEU D  1 67  ? 47.959 25.187   -6.725   1.00 146.65 ? 68  LEU D CD2 1 
ATOM   3824  N  N   . SER D  1 68  ? 45.429 23.716   -2.433   1.00 149.66 ? 69  SER D N   1 
ATOM   3825  C  CA  . SER D  1 68  ? 45.686 23.529   -0.976   1.00 152.41 ? 69  SER D CA  1 
ATOM   3826  C  C   . SER D  1 68  ? 45.260 24.773   -0.135   1.00 154.94 ? 69  SER D C   1 
ATOM   3827  O  O   . SER D  1 68  ? 45.884 25.078   0.898    1.00 158.25 ? 69  SER D O   1 
ATOM   3828  C  CB  . SER D  1 68  ? 47.178 23.208   -0.691   1.00 154.58 ? 69  SER D CB  1 
ATOM   3829  O  OG  . SER D  1 68  ? 47.525 21.862   -1.000   1.00 153.39 ? 69  SER D OG  1 
ATOM   3830  N  N   . ARG D  1 69  ? 44.191 25.463   -0.563   1.00 153.69 ? 70  ARG D N   1 
ATOM   3831  C  CA  . ARG D  1 69  ? 43.817 26.812   -0.058   1.00 155.77 ? 70  ARG D CA  1 
ATOM   3832  C  C   . ARG D  1 69  ? 42.804 26.791   1.107    1.00 156.80 ? 70  ARG D C   1 
ATOM   3833  O  O   . ARG D  1 69  ? 42.506 25.716   1.660    1.00 156.19 ? 70  ARG D O   1 
ATOM   3834  C  CB  . ARG D  1 69  ? 43.278 27.678   -1.222   1.00 153.90 ? 70  ARG D CB  1 
ATOM   3835  C  CG  . ARG D  1 69  ? 44.167 27.672   -2.490   1.00 152.64 ? 70  ARG D CG  1 
ATOM   3836  C  CD  . ARG D  1 69  ? 45.620 28.192   -2.192   1.00 155.56 ? 70  ARG D CD  1 
ATOM   3837  N  NE  . ARG D  1 69  ? 46.468 28.337   -3.393   1.00 153.48 ? 70  ARG D NE  1 
ATOM   3838  C  CZ  . ARG D  1 69  ? 47.681 27.805   -3.571   1.00 153.17 ? 70  ARG D CZ  1 
ATOM   3839  N  NH1 . ARG D  1 69  ? 48.268 27.060   -2.630   1.00 154.63 ? 70  ARG D NH1 1 
ATOM   3840  N  NH2 . ARG D  1 69  ? 48.319 28.023   -4.717   1.00 151.78 ? 70  ARG D NH2 1 
ATOM   3841  N  N   . LYS D  1 70  ? 42.324 27.986   1.493    1.00 158.51 ? 71  LYS D N   1 
ATOM   3842  C  CA  . LYS D  1 70  ? 41.221 28.160   2.469    1.00 159.20 ? 71  LYS D CA  1 
ATOM   3843  C  C   . LYS D  1 70  ? 40.263 29.251   2.005    1.00 158.55 ? 71  LYS D C   1 
ATOM   3844  O  O   . LYS D  1 70  ? 40.690 30.221   1.380    1.00 158.69 ? 71  LYS D O   1 
ATOM   3845  C  CB  . LYS D  1 70  ? 41.752 28.483   3.879    1.00 163.38 ? 71  LYS D CB  1 
ATOM   3846  C  CG  . LYS D  1 70  ? 42.094 27.219   4.713    1.00 163.90 ? 71  LYS D CG  1 
ATOM   3847  C  CD  . LYS D  1 70  ? 42.273 27.487   6.227    1.00 167.65 ? 71  LYS D CD  1 
ATOM   3848  C  CE  . LYS D  1 70  ? 42.290 26.186   7.039    1.00 166.75 ? 71  LYS D CE  1 
ATOM   3849  N  NZ  . LYS D  1 70  ? 42.174 26.419   8.499    1.00 169.68 ? 71  LYS D NZ  1 
ATOM   3850  N  N   . HIS D  1 71  ? 38.978 29.081   2.328    1.00 157.56 ? 72  HIS D N   1 
ATOM   3851  C  CA  . HIS D  1 71  ? 37.914 29.960   1.824    1.00 157.17 ? 72  HIS D CA  1 
ATOM   3852  C  C   . HIS D  1 71  ? 38.231 31.449   1.957    1.00 160.63 ? 72  HIS D C   1 
ATOM   3853  O  O   . HIS D  1 71  ? 38.951 31.871   2.873    1.00 164.14 ? 72  HIS D O   1 
ATOM   3854  C  CB  . HIS D  1 71  ? 36.575 29.697   2.534    1.00 157.00 ? 72  HIS D CB  1 
ATOM   3855  C  CG  . HIS D  1 71  ? 35.499 30.695   2.187    1.00 157.14 ? 72  HIS D CG  1 
ATOM   3856  N  ND1 . HIS D  1 71  ? 35.032 30.869   0.901    1.00 155.14 ? 72  HIS D ND1 1 
ATOM   3857  C  CD2 . HIS D  1 71  ? 34.813 31.579   2.951    1.00 159.23 ? 72  HIS D CD2 1 
ATOM   3858  C  CE1 . HIS D  1 71  ? 34.100 31.805   0.889    1.00 155.40 ? 72  HIS D CE1 1 
ATOM   3859  N  NE2 . HIS D  1 71  ? 33.950 32.254   2.120    1.00 157.99 ? 72  HIS D NE2 1 
ATOM   3860  N  N   . GLY D  1 72  ? 37.670 32.234   1.034    1.00 159.89 ? 73  GLY D N   1 
ATOM   3861  C  CA  . GLY D  1 72  ? 37.671 33.692   1.129    1.00 162.87 ? 73  GLY D CA  1 
ATOM   3862  C  C   . GLY D  1 72  ? 36.546 34.348   0.338    1.00 161.81 ? 73  GLY D C   1 
ATOM   3863  O  O   . GLY D  1 72  ? 35.478 33.754   0.122    1.00 159.14 ? 73  GLY D O   1 
ATOM   3864  N  N   . GLY D  1 73  ? 36.803 35.592   -0.075   1.00 163.86 ? 74  GLY D N   1 
ATOM   3865  C  CA  . GLY D  1 73  ? 35.907 36.361   -0.957   1.00 163.35 ? 74  GLY D CA  1 
ATOM   3866  C  C   . GLY D  1 73  ? 36.373 36.377   -2.411   1.00 160.76 ? 74  GLY D C   1 
ATOM   3867  O  O   . GLY D  1 73  ? 37.387 35.737   -2.759   1.00 159.09 ? 74  GLY D O   1 
ATOM   3868  N  N   . PRO D  1 74  ? 35.646 37.123   -3.273   1.00 160.52 ? 75  PRO D N   1 
ATOM   3869  C  CA  . PRO D  1 74  ? 35.932 37.062   -4.731   1.00 158.09 ? 75  PRO D CA  1 
ATOM   3870  C  C   . PRO D  1 74  ? 37.347 37.554   -5.113   1.00 159.21 ? 75  PRO D C   1 
ATOM   3871  O  O   . PRO D  1 74  ? 38.018 36.947   -5.969   1.00 156.59 ? 75  PRO D O   1 
ATOM   3872  C  CB  . PRO D  1 74  ? 34.822 37.938   -5.367   1.00 158.34 ? 75  PRO D CB  1 
ATOM   3873  C  CG  . PRO D  1 74  ? 34.309 38.811   -4.252   1.00 162.04 ? 75  PRO D CG  1 
ATOM   3874  C  CD  . PRO D  1 74  ? 34.593 38.105   -2.935   1.00 162.72 ? 75  PRO D CD  1 
ATOM   3875  N  N   . LYS D  1 75  ? 37.791 38.619   -4.440   1.00 163.08 ? 76  LYS D N   1 
ATOM   3876  C  CA  . LYS D  1 75  ? 39.017 39.342   -4.791   1.00 164.63 ? 76  LYS D CA  1 
ATOM   3877  C  C   . LYS D  1 75  ? 40.278 38.860   -4.009   1.00 165.54 ? 76  LYS D C   1 
ATOM   3878  O  O   . LYS D  1 75  ? 41.371 39.413   -4.160   1.00 167.19 ? 76  LYS D O   1 
ATOM   3879  C  CB  . LYS D  1 75  ? 38.760 40.840   -4.578   1.00 168.43 ? 76  LYS D CB  1 
ATOM   3880  C  CG  . LYS D  1 75  ? 37.488 41.364   -5.283   1.00 168.42 ? 76  LYS D CG  1 
ATOM   3881  C  CD  . LYS D  1 75  ? 36.683 42.364   -4.401   1.00 173.78 ? 76  LYS D CD  1 
ATOM   3882  C  CE  . LYS D  1 75  ? 37.234 43.833   -4.408   1.00 177.86 ? 76  LYS D CE  1 
ATOM   3883  N  NZ  . LYS D  1 75  ? 38.508 44.079   -3.622   1.00 180.19 ? 76  LYS D NZ  1 
ATOM   3884  N  N   . ASP D  1 76  ? 40.129 37.821   -3.193   1.00 164.36 ? 77  ASP D N   1 
ATOM   3885  C  CA  . ASP D  1 76  ? 41.251 37.263   -2.445   1.00 165.29 ? 77  ASP D CA  1 
ATOM   3886  C  C   . ASP D  1 76  ? 42.252 36.600   -3.364   1.00 162.97 ? 77  ASP D C   1 
ATOM   3887  O  O   . ASP D  1 76  ? 41.915 36.258   -4.496   1.00 159.88 ? 77  ASP D O   1 
ATOM   3888  C  CB  . ASP D  1 76  ? 40.758 36.195   -1.467   1.00 164.56 ? 77  ASP D CB  1 
ATOM   3889  C  CG  . ASP D  1 76  ? 39.976 36.771   -0.314   1.00 167.42 ? 77  ASP D CG  1 
ATOM   3890  O  OD1 . ASP D  1 76  ? 39.560 37.953   -0.375   1.00 169.30 ? 77  ASP D OD1 1 
ATOM   3891  O  OD2 . ASP D  1 76  ? 39.777 36.022   0.660    1.00 166.86 ? 77  ASP D OD2 1 
ATOM   3892  N  N   . GLU D  1 77  ? 43.479 36.415   -2.868   1.00 164.89 ? 78  GLU D N   1 
ATOM   3893  C  CA  . GLU D  1 77  ? 44.418 35.434   -3.448   1.00 162.87 ? 78  GLU D CA  1 
ATOM   3894  C  C   . GLU D  1 77  ? 44.253 34.097   -2.721   1.00 162.25 ? 78  GLU D C   1 
ATOM   3895  O  O   . GLU D  1 77  ? 44.115 33.048   -3.366   1.00 159.03 ? 78  GLU D O   1 
ATOM   3896  C  CB  . GLU D  1 77  ? 45.887 35.885   -3.357   1.00 165.43 ? 78  GLU D CB  1 
ATOM   3897  C  CG  . GLU D  1 77  ? 46.904 34.972   -4.135   1.00 162.10 ? 78  GLU D CG  1 
ATOM   3898  C  CD  . GLU D  1 77  ? 47.669 33.951   -3.266   1.00 160.43 ? 78  GLU D CD  1 
ATOM   3899  O  OE1 . GLU D  1 77  ? 47.072 33.016   -2.697   1.00 157.06 ? 78  GLU D OE1 1 
ATOM   3900  O  OE2 . GLU D  1 77  ? 48.898 34.073   -3.184   1.00 160.71 ? 78  GLU D OE2 1 
ATOM   3901  N  N   . GLU D  1 78  ? 44.286 34.130   -1.383   1.00 165.68 ? 79  GLU D N   1 
ATOM   3902  C  CA  . GLU D  1 78  ? 43.985 32.926   -0.588   1.00 165.18 ? 79  GLU D CA  1 
ATOM   3903  C  C   . GLU D  1 78  ? 42.468 32.719   -0.494   1.00 164.10 ? 79  GLU D C   1 
ATOM   3904  O  O   . GLU D  1 78  ? 41.778 33.261   0.394    1.00 166.48 ? 79  GLU D O   1 
ATOM   3905  C  CB  . GLU D  1 78  ? 44.611 32.965   0.809    1.00 168.91 ? 79  GLU D CB  1 
ATOM   3906  C  CG  . GLU D  1 78  ? 44.616 31.596   1.524    1.00 167.65 ? 79  GLU D CG  1 
ATOM   3907  C  CD  . GLU D  1 78  ? 45.653 30.609   0.955    1.00 165.83 ? 79  GLU D CD  1 
ATOM   3908  O  OE1 . GLU D  1 78  ? 46.215 30.845   -0.140   1.00 163.77 ? 79  GLU D OE1 1 
ATOM   3909  O  OE2 . GLU D  1 78  ? 45.915 29.583   1.616    1.00 165.72 ? 79  GLU D OE2 1 
ATOM   3910  N  N   . ARG D  1 79  ? 41.971 31.955   -1.467   1.00 160.82 ? 80  ARG D N   1 
ATOM   3911  C  CA  . ARG D  1 79  ? 40.577 31.501   -1.530   1.00 158.86 ? 80  ARG D CA  1 
ATOM   3912  C  C   . ARG D  1 79  ? 40.613 30.057   -2.064   1.00 155.27 ? 80  ARG D C   1 
ATOM   3913  O  O   . ARG D  1 79  ? 41.691 29.551   -2.440   1.00 154.69 ? 80  ARG D O   1 
ATOM   3914  C  CB  . ARG D  1 79  ? 39.689 32.435   -2.412   1.00 158.27 ? 80  ARG D CB  1 
ATOM   3915  C  CG  . ARG D  1 79  ? 40.378 33.099   -3.616   1.00 158.47 ? 80  ARG D CG  1 
ATOM   3916  C  CD  . ARG D  1 79  ? 39.379 33.742   -4.581   1.00 158.51 ? 80  ARG D CD  1 
ATOM   3917  N  NE  . ARG D  1 79  ? 38.841 32.779   -5.550   1.00 156.74 ? 80  ARG D NE  1 
ATOM   3918  C  CZ  . ARG D  1 79  ? 38.115 33.090   -6.634   1.00 156.54 ? 80  ARG D CZ  1 
ATOM   3919  N  NH1 . ARG D  1 79  ? 37.808 34.356   -6.924   1.00 158.92 ? 80  ARG D NH1 1 
ATOM   3920  N  NH2 . ARG D  1 79  ? 37.683 32.127   -7.444   1.00 153.53 ? 80  ARG D NH2 1 
ATOM   3921  N  N   . HIS D  1 80  ? 39.459 29.386   -2.069   1.00 152.78 ? 81  HIS D N   1 
ATOM   3922  C  CA  . HIS D  1 80  ? 39.333 28.156   -2.843   1.00 148.93 ? 81  HIS D CA  1 
ATOM   3923  C  C   . HIS D  1 80  ? 39.169 28.539   -4.301   1.00 146.84 ? 81  HIS D C   1 
ATOM   3924  O  O   . HIS D  1 80  ? 38.606 29.598   -4.627   1.00 147.37 ? 81  HIS D O   1 
ATOM   3925  C  CB  . HIS D  1 80  ? 38.169 27.283   -2.384   1.00 147.39 ? 81  HIS D CB  1 
ATOM   3926  C  CG  . HIS D  1 80  ? 38.287 26.839   -0.971   1.00 148.13 ? 81  HIS D CG  1 
ATOM   3927  N  ND1 . HIS D  1 80  ? 37.211 26.391   -0.241   1.00 147.91 ? 81  HIS D ND1 1 
ATOM   3928  C  CD2 . HIS D  1 80  ? 39.354 26.798   -0.143   1.00 149.60 ? 81  HIS D CD2 1 
ATOM   3929  C  CE1 . HIS D  1 80  ? 37.611 26.084   0.979    1.00 150.26 ? 81  HIS D CE1 1 
ATOM   3930  N  NE2 . HIS D  1 80  ? 38.907 26.325   1.065    1.00 151.20 ? 81  HIS D NE2 1 
ATOM   3931  N  N   . VAL D  1 81  ? 39.646 27.643   -5.158   1.00 144.45 ? 82  VAL D N   1 
ATOM   3932  C  CA  . VAL D  1 81  ? 39.805 27.886   -6.593   1.00 142.64 ? 82  VAL D CA  1 
ATOM   3933  C  C   . VAL D  1 81  ? 38.510 28.360   -7.345   1.00 141.36 ? 82  VAL D C   1 
ATOM   3934  O  O   . VAL D  1 81  ? 38.584 28.762   -8.520   1.00 140.39 ? 82  VAL D O   1 
ATOM   3935  C  CB  . VAL D  1 81  ? 40.531 26.645   -7.244   1.00 140.75 ? 82  VAL D CB  1 
ATOM   3936  C  CG1 . VAL D  1 81  ? 40.299 26.549   -8.750   1.00 138.37 ? 82  VAL D CG1 1 
ATOM   3937  C  CG2 . VAL D  1 81  ? 42.060 26.671   -6.894   1.00 141.89 ? 82  VAL D CG2 1 
ATOM   3938  N  N   . GLY D  1 82  ? 37.350 28.355   -6.675   1.00 141.44 ? 83  GLY D N   1 
ATOM   3939  C  CA  . GLY D  1 82  ? 36.162 29.021   -7.224   1.00 140.96 ? 83  GLY D CA  1 
ATOM   3940  C  C   . GLY D  1 82  ? 35.184 29.551   -6.194   1.00 142.71 ? 83  GLY D C   1 
ATOM   3941  O  O   . GLY D  1 82  ? 34.084 29.014   -6.082   1.00 141.96 ? 83  GLY D O   1 
ATOM   3942  N  N   . ASP D  1 83  ? 35.560 30.594   -5.447   1.00 145.44 ? 84  ASP D N   1 
ATOM   3943  C  CA  . ASP D  1 83  ? 34.647 31.217   -4.459   1.00 147.68 ? 84  ASP D CA  1 
ATOM   3944  C  C   . ASP D  1 83  ? 34.038 32.515   -4.988   1.00 148.97 ? 84  ASP D C   1 
ATOM   3945  O  O   . ASP D  1 83  ? 34.768 33.451   -5.286   1.00 150.40 ? 84  ASP D O   1 
ATOM   3946  C  CB  . ASP D  1 83  ? 35.378 31.486   -3.147   1.00 150.48 ? 84  ASP D CB  1 
ATOM   3947  C  CG  . ASP D  1 83  ? 35.656 30.215   -2.366   1.00 149.87 ? 84  ASP D CG  1 
ATOM   3948  O  OD1 . ASP D  1 83  ? 34.699 29.448   -2.101   1.00 148.02 ? 84  ASP D OD1 1 
ATOM   3949  O  OD2 . ASP D  1 83  ? 36.832 29.993   -2.001   1.00 150.55 ? 84  ASP D OD2 1 
ATOM   3950  N  N   . LEU D  1 84  ? 32.709 32.575   -5.098   1.00 148.81 ? 85  LEU D N   1 
ATOM   3951  C  CA  . LEU D  1 84  ? 32.048 33.674   -5.830   1.00 149.93 ? 85  LEU D CA  1 
ATOM   3952  C  C   . LEU D  1 84  ? 31.147 34.597   -4.973   1.00 153.15 ? 85  LEU D C   1 
ATOM   3953  O  O   . LEU D  1 84  ? 30.334 35.374   -5.520   1.00 153.86 ? 85  LEU D O   1 
ATOM   3954  C  CB  . LEU D  1 84  ? 31.273 33.128   -7.037   1.00 147.29 ? 85  LEU D CB  1 
ATOM   3955  C  CG  . LEU D  1 84  ? 31.979 32.043   -7.865   1.00 145.10 ? 85  LEU D CG  1 
ATOM   3956  C  CD1 . LEU D  1 84  ? 31.118 31.652   -9.067   1.00 143.21 ? 85  LEU D CD1 1 
ATOM   3957  C  CD2 . LEU D  1 84  ? 33.394 32.481   -8.313   1.00 145.80 ? 85  LEU D CD2 1 
ATOM   3958  N  N   . GLY D  1 85  ? 31.298 34.513   -3.644   1.00 155.19 ? 86  GLY D N   1 
ATOM   3959  C  CA  . GLY D  1 85  ? 30.907 35.609   -2.747   1.00 158.82 ? 86  GLY D CA  1 
ATOM   3960  C  C   . GLY D  1 85  ? 29.471 35.646   -2.259   1.00 159.70 ? 86  GLY D C   1 
ATOM   3961  O  O   . GLY D  1 85  ? 29.061 34.763   -1.498   1.00 159.01 ? 86  GLY D O   1 
ATOM   3962  N  N   . ASN D  1 86  ? 28.727 36.682   -2.678   1.00 161.36 ? 87  ASN D N   1 
ATOM   3963  C  CA  . ASN D  1 86  ? 27.357 36.958   -2.183   1.00 163.12 ? 87  ASN D CA  1 
ATOM   3964  C  C   . ASN D  1 86  ? 26.430 37.548   -3.233   1.00 163.22 ? 87  ASN D C   1 
ATOM   3965  O  O   . ASN D  1 86  ? 26.819 38.441   -3.979   1.00 163.64 ? 87  ASN D O   1 
ATOM   3966  C  CB  . ASN D  1 86  ? 27.394 37.945   -1.007   1.00 167.38 ? 87  ASN D CB  1 
ATOM   3967  C  CG  . ASN D  1 86  ? 27.310 37.263   0.340    1.00 168.25 ? 87  ASN D CG  1 
ATOM   3968  O  OD1 . ASN D  1 86  ? 26.513 36.348   0.533    1.00 166.62 ? 87  ASN D OD1 1 
ATOM   3969  N  ND2 . ASN D  1 86  ? 28.117 37.723   1.294    1.00 171.28 ? 87  ASN D ND2 1 
ATOM   3970  N  N   . VAL D  1 87  ? 25.193 37.063   -3.276   1.00 163.22 ? 88  VAL D N   1 
ATOM   3971  C  CA  . VAL D  1 87  ? 24.160 37.711   -4.102   1.00 164.63 ? 88  VAL D CA  1 
ATOM   3972  C  C   . VAL D  1 87  ? 22.927 38.066   -3.267   1.00 168.01 ? 88  VAL D C   1 
ATOM   3973  O  O   . VAL D  1 87  ? 22.222 37.191   -2.730   1.00 167.06 ? 88  VAL D O   1 
ATOM   3974  C  CB  . VAL D  1 87  ? 23.740 36.902   -5.376   1.00 161.20 ? 88  VAL D CB  1 
ATOM   3975  C  CG1 . VAL D  1 87  ? 24.012 37.736   -6.658   1.00 160.97 ? 88  VAL D CG1 1 
ATOM   3976  C  CG2 . VAL D  1 87  ? 24.409 35.511   -5.410   1.00 157.91 ? 88  VAL D CG2 1 
ATOM   3977  N  N   . THR D  1 88  ? 22.690 39.372   -3.161   1.00 172.21 ? 89  THR D N   1 
ATOM   3978  C  CA  . THR D  1 88  ? 21.550 39.884   -2.433   1.00 175.74 ? 89  THR D CA  1 
ATOM   3979  C  C   . THR D  1 88  ? 20.303 39.579   -3.242   1.00 175.07 ? 89  THR D C   1 
ATOM   3980  O  O   . THR D  1 88  ? 20.254 39.834   -4.465   1.00 174.00 ? 89  THR D O   1 
ATOM   3981  C  CB  . THR D  1 88  ? 21.645 41.410   -2.163   1.00 180.11 ? 89  THR D CB  1 
ATOM   3982  O  OG1 . THR D  1 88  ? 22.762 41.671   -1.307   1.00 182.01 ? 89  THR D OG1 1 
ATOM   3983  C  CG2 . THR D  1 88  ? 20.364 41.946   -1.498   1.00 183.07 ? 89  THR D CG2 1 
ATOM   3984  N  N   . ALA D  1 89  ? 19.323 38.992   -2.550   1.00 175.95 ? 90  ALA D N   1 
ATOM   3985  C  CA  . ALA D  1 89  ? 17.950 38.930   -3.033   1.00 176.34 ? 90  ALA D CA  1 
ATOM   3986  C  C   . ALA D  1 89  ? 17.301 40.321   -2.921   1.00 180.86 ? 90  ALA D C   1 
ATOM   3987  O  O   . ALA D  1 89  ? 17.482 41.054   -1.935   1.00 183.88 ? 90  ALA D O   1 
ATOM   3988  C  CB  . ALA D  1 89  ? 17.148 37.888   -2.251   1.00 175.40 ? 90  ALA D CB  1 
ATOM   3989  N  N   . ASP D  1 90  ? 16.573 40.680   -3.971   1.00 181.44 ? 91  ASP D N   1 
ATOM   3990  C  CA  . ASP D  1 90  ? 15.642 41.805   -3.939   1.00 185.90 ? 91  ASP D CA  1 
ATOM   3991  C  C   . ASP D  1 90  ? 14.432 41.498   -2.963   1.00 188.33 ? 91  ASP D C   1 
ATOM   3992  O  O   . ASP D  1 90  ? 14.356 40.417   -2.307   1.00 186.25 ? 91  ASP D O   1 
ATOM   3993  C  CB  . ASP D  1 90  ? 15.163 42.080   -5.397   1.00 184.99 ? 91  ASP D CB  1 
ATOM   3994  C  CG  . ASP D  1 90  ? 14.687 43.525   -5.640   1.00 188.90 ? 91  ASP D CG  1 
ATOM   3995  O  OD1 . ASP D  1 90  ? 14.707 44.347   -4.701   1.00 193.35 ? 91  ASP D OD1 1 
ATOM   3996  O  OD2 . ASP D  1 90  ? 14.283 43.833   -6.789   1.00 187.04 ? 91  ASP D OD2 1 
ATOM   3997  N  N   . LYS D  1 91  ? 13.528 42.480   -2.848   1.00 192.65 ? 92  LYS D N   1 
ATOM   3998  C  CA  . LYS D  1 91  ? 12.173 42.272   -2.299   1.00 194.92 ? 92  LYS D CA  1 
ATOM   3999  C  C   . LYS D  1 91  ? 11.465 41.038   -2.929   1.00 191.63 ? 92  LYS D C   1 
ATOM   4000  O  O   . LYS D  1 91  ? 11.135 40.059   -2.235   1.00 190.50 ? 92  LYS D O   1 
ATOM   4001  C  CB  . LYS D  1 91  ? 11.294 43.541   -2.507   1.00 199.35 ? 92  LYS D CB  1 
ATOM   4002  C  CG  . LYS D  1 91  ? 11.037 44.369   -1.241   1.00 204.37 ? 92  LYS D CG  1 
ATOM   4003  C  CD  . LYS D  1 91  ? 10.129 43.639   -0.202   1.00 204.96 ? 92  LYS D CD  1 
ATOM   4004  C  CE  . LYS D  1 91  ? 10.208 44.309   1.188    1.00 209.27 ? 92  LYS D CE  1 
ATOM   4005  N  NZ  . LYS D  1 91  ? 9.662  43.484   2.306    1.00 209.22 ? 92  LYS D NZ  1 
ATOM   4006  N  N   . ASP D  1 92  ? 11.256 41.108   -4.248   1.00 190.32 ? 93  ASP D N   1 
ATOM   4007  C  CA  . ASP D  1 92  ? 10.527 40.073   -5.013   1.00 187.72 ? 93  ASP D CA  1 
ATOM   4008  C  C   . ASP D  1 92  ? 11.354 38.781   -5.323   1.00 182.78 ? 93  ASP D C   1 
ATOM   4009  O  O   . ASP D  1 92  ? 10.943 37.964   -6.167   1.00 180.47 ? 93  ASP D O   1 
ATOM   4010  C  CB  . ASP D  1 92  ? 9.873  40.665   -6.309   1.00 188.90 ? 93  ASP D CB  1 
ATOM   4011  C  CG  . ASP D  1 92  ? 10.677 41.841   -6.946   1.00 191.36 ? 93  ASP D CG  1 
ATOM   4012  O  OD1 . ASP D  1 92  ? 10.872 42.891   -6.271   1.00 196.20 ? 93  ASP D OD1 1 
ATOM   4013  O  OD2 . ASP D  1 92  ? 11.072 41.725   -8.140   1.00 190.01 ? 93  ASP D OD2 1 
ATOM   4014  N  N   . GLY D  1 93  ? 12.495 38.594   -4.635   1.00 181.33 ? 94  GLY D N   1 
ATOM   4015  C  CA  . GLY D  1 93  ? 13.347 37.392   -4.786   1.00 176.86 ? 94  GLY D CA  1 
ATOM   4016  C  C   . GLY D  1 93  ? 14.013 37.224   -6.152   1.00 173.83 ? 94  GLY D C   1 
ATOM   4017  O  O   . GLY D  1 93  ? 14.425 36.115   -6.505   1.00 170.24 ? 94  GLY D O   1 
ATOM   4018  N  N   . VAL D  1 94  ? 14.141 38.342   -6.887   1.00 175.23 ? 95  VAL D N   1 
ATOM   4019  C  CA  . VAL D  1 94  ? 14.522 38.395   -8.330   1.00 173.10 ? 95  VAL D CA  1 
ATOM   4020  C  C   . VAL D  1 94  ? 15.969 38.943   -8.531   1.00 172.34 ? 95  VAL D C   1 
ATOM   4021  O  O   . VAL D  1 94  ? 16.199 39.964   -9.220   1.00 173.57 ? 95  VAL D O   1 
ATOM   4022  C  CB  . VAL D  1 94  ? 13.451 39.229   -9.157   1.00 175.48 ? 95  VAL D CB  1 
ATOM   4023  C  CG1 . VAL D  1 94  ? 13.978 39.694   -10.536  1.00 174.22 ? 95  VAL D CG1 1 
ATOM   4024  C  CG2 . VAL D  1 94  ? 12.157 38.419   -9.318   1.00 175.06 ? 95  VAL D CG2 1 
ATOM   4025  N  N   . ALA D  1 95  ? 16.927 38.204   -7.943   1.00 169.99 ? 96  ALA D N   1 
ATOM   4026  C  CA  . ALA D  1 95  ? 18.349 38.610   -7.811   1.00 169.32 ? 96  ALA D CA  1 
ATOM   4027  C  C   . ALA D  1 95  ? 19.178 38.596   -9.123   1.00 166.55 ? 96  ALA D C   1 
ATOM   4028  O  O   . ALA D  1 95  ? 19.703 37.539   -9.520   1.00 163.43 ? 96  ALA D O   1 
ATOM   4029  C  CB  . ALA D  1 95  ? 19.050 37.732   -6.728   1.00 167.85 ? 96  ALA D CB  1 
ATOM   4030  N  N   . ASP D  1 96  ? 19.313 39.775   -9.756   1.00 167.64 ? 97  ASP D N   1 
ATOM   4031  C  CA  . ASP D  1 96  ? 20.160 39.952   -10.959  1.00 165.20 ? 97  ASP D CA  1 
ATOM   4032  C  C   . ASP D  1 96  ? 21.651 39.610   -10.710  1.00 162.88 ? 97  ASP D C   1 
ATOM   4033  O  O   . ASP D  1 96  ? 22.191 39.768   -9.594   1.00 163.70 ? 97  ASP D O   1 
ATOM   4034  C  CB  . ASP D  1 96  ? 20.021 41.371   -11.558  1.00 167.83 ? 97  ASP D CB  1 
ATOM   4035  C  CG  . ASP D  1 96  ? 18.697 41.574   -12.301  1.00 168.50 ? 97  ASP D CG  1 
ATOM   4036  O  OD1 . ASP D  1 96  ? 18.744 41.824   -13.528  1.00 166.51 ? 97  ASP D OD1 1 
ATOM   4037  O  OD2 . ASP D  1 96  ? 17.620 41.480   -11.658  1.00 169.36 ? 97  ASP D OD2 1 
ATOM   4038  N  N   . VAL D  1 97  ? 22.280 39.103   -11.773  1.00 159.56 ? 98  VAL D N   1 
ATOM   4039  C  CA  . VAL D  1 97  ? 23.684 38.697   -11.753  1.00 157.20 ? 98  VAL D CA  1 
ATOM   4040  C  C   . VAL D  1 97  ? 24.409 39.401   -12.930  1.00 156.41 ? 98  VAL D C   1 
ATOM   4041  O  O   . VAL D  1 97  ? 23.859 39.518   -14.053  1.00 155.82 ? 98  VAL D O   1 
ATOM   4042  C  CB  . VAL D  1 97  ? 23.882 37.120   -11.826  1.00 153.89 ? 98  VAL D CB  1 
ATOM   4043  C  CG1 . VAL D  1 97  ? 24.913 36.636   -10.764  1.00 153.18 ? 98  VAL D CG1 1 
ATOM   4044  C  CG2 . VAL D  1 97  ? 22.547 36.356   -11.671  1.00 153.47 ? 98  VAL D CG2 1 
ATOM   4045  N  N   . SER D  1 98  ? 25.614 39.907   -12.626  1.00 156.05 ? 99  SER D N   1 
ATOM   4046  C  CA  . SER D  1 98  ? 26.575 40.423   -13.615  1.00 154.50 ? 99  SER D CA  1 
ATOM   4047  C  C   . SER D  1 98  ? 27.964 40.465   -12.928  1.00 154.22 ? 99  SER D C   1 
ATOM   4048  O  O   . SER D  1 98  ? 28.598 41.518   -12.792  1.00 156.39 ? 99  SER D O   1 
ATOM   4049  C  CB  . SER D  1 98  ? 26.126 41.787   -14.166  1.00 156.95 ? 99  SER D CB  1 
ATOM   4050  O  OG  . SER D  1 98  ? 26.327 41.845   -15.561  1.00 154.38 ? 99  SER D OG  1 
ATOM   4051  N  N   . ILE D  1 99  ? 28.398 39.281   -12.489  1.00 151.36 ? 100 ILE D N   1 
ATOM   4052  C  CA  . ILE D  1 99  ? 29.674 39.057   -11.782  1.00 150.95 ? 100 ILE D CA  1 
ATOM   4053  C  C   . ILE D  1 99  ? 30.812 38.697   -12.761  1.00 148.32 ? 100 ILE D C   1 
ATOM   4054  O  O   . ILE D  1 99  ? 30.541 38.239   -13.882  1.00 146.47 ? 100 ILE D O   1 
ATOM   4055  C  CB  . ILE D  1 99  ? 29.485 37.940   -10.703  1.00 150.17 ? 100 ILE D CB  1 
ATOM   4056  C  CG1 . ILE D  1 99  ? 28.494 38.441   -9.617   1.00 153.19 ? 100 ILE D CG1 1 
ATOM   4057  C  CG2 . ILE D  1 99  ? 30.842 37.473   -10.123  1.00 149.31 ? 100 ILE D CG2 1 
ATOM   4058  C  CD1 . ILE D  1 99  ? 28.021 37.392   -8.604   1.00 152.13 ? 100 ILE D CD1 1 
ATOM   4059  N  N   . GLU D  1 100 ? 32.068 38.922   -12.345  1.00 148.31 ? 101 GLU D N   1 
ATOM   4060  C  CA  . GLU D  1 100 ? 33.259 38.739   -13.222  1.00 146.27 ? 101 GLU D CA  1 
ATOM   4061  C  C   . GLU D  1 100 ? 34.474 38.147   -12.446  1.00 145.83 ? 101 GLU D C   1 
ATOM   4062  O  O   . GLU D  1 100 ? 34.696 38.496   -11.282  1.00 148.06 ? 101 GLU D O   1 
ATOM   4063  C  CB  . GLU D  1 100 ? 33.618 40.086   -13.884  1.00 147.90 ? 101 GLU D CB  1 
ATOM   4064  C  CG  . GLU D  1 100 ? 34.215 39.988   -15.289  1.00 145.61 ? 101 GLU D CG  1 
ATOM   4065  C  CD  . GLU D  1 100 ? 33.337 40.625   -16.385  1.00 145.48 ? 101 GLU D CD  1 
ATOM   4066  O  OE1 . GLU D  1 100 ? 33.913 41.166   -17.362  1.00 144.51 ? 101 GLU D OE1 1 
ATOM   4067  O  OE2 . GLU D  1 100 ? 32.082 40.568   -16.280  1.00 144.86 ? 101 GLU D OE2 1 
ATOM   4068  N  N   . ASP D  1 101 ? 35.252 37.258   -13.078  1.00 143.08 ? 102 ASP D N   1 
ATOM   4069  C  CA  . ASP D  1 101 ? 36.287 36.477   -12.353  1.00 142.35 ? 102 ASP D CA  1 
ATOM   4070  C  C   . ASP D  1 101 ? 37.479 36.022   -13.229  1.00 140.71 ? 102 ASP D C   1 
ATOM   4071  O  O   . ASP D  1 101 ? 37.350 35.821   -14.435  1.00 138.67 ? 102 ASP D O   1 
ATOM   4072  C  CB  . ASP D  1 101 ? 35.628 35.262   -11.653  1.00 140.77 ? 102 ASP D CB  1 
ATOM   4073  C  CG  . ASP D  1 101 ? 36.469 34.694   -10.491  1.00 141.11 ? 102 ASP D CG  1 
ATOM   4074  O  OD1 . ASP D  1 101 ? 36.124 34.954   -9.314   1.00 142.32 ? 102 ASP D OD1 1 
ATOM   4075  O  OD2 . ASP D  1 101 ? 37.462 33.972   -10.749  1.00 138.54 ? 102 ASP D OD2 1 
ATOM   4076  N  N   . SER D  1 102 ? 38.631 35.846   -12.571  1.00 141.86 ? 103 SER D N   1 
ATOM   4077  C  CA  . SER D  1 102 ? 39.946 35.561   -13.205  1.00 141.28 ? 103 SER D CA  1 
ATOM   4078  C  C   . SER D  1 102 ? 40.483 34.126   -13.039  1.00 139.38 ? 103 SER D C   1 
ATOM   4079  O  O   . SER D  1 102 ? 41.180 33.640   -13.941  1.00 138.00 ? 103 SER D O   1 
ATOM   4080  C  CB  . SER D  1 102 ? 41.035 36.507   -12.649  1.00 144.11 ? 103 SER D CB  1 
ATOM   4081  O  OG  . SER D  1 102 ? 40.999 37.785   -13.260  1.00 146.13 ? 103 SER D OG  1 
ATOM   4082  N  N   . VAL D  1 103 ? 40.195 33.469   -11.902  1.00 139.47 ? 104 VAL D N   1 
ATOM   4083  C  CA  . VAL D  1 103 ? 40.814 32.146   -11.572  1.00 138.01 ? 104 VAL D CA  1 
ATOM   4084  C  C   . VAL D  1 103 ? 39.959 30.909   -11.999  1.00 135.01 ? 104 VAL D C   1 
ATOM   4085  O  O   . VAL D  1 103 ? 40.509 29.819   -12.265  1.00 133.42 ? 104 VAL D O   1 
ATOM   4086  C  CB  . VAL D  1 103 ? 41.231 32.025   -10.068  1.00 140.10 ? 104 VAL D CB  1 
ATOM   4087  C  CG1 . VAL D  1 103 ? 42.572 31.261   -9.954   1.00 139.28 ? 104 VAL D CG1 1 
ATOM   4088  C  CG2 . VAL D  1 103 ? 41.335 33.418   -9.406   1.00 143.44 ? 104 VAL D CG2 1 
ATOM   4089  N  N   . ILE D  1 104 ? 38.634 31.075   -12.078  1.00 133.92 ? 105 ILE D N   1 
ATOM   4090  C  CA  . ILE D  1 104 ? 37.793 30.070   -12.741  1.00 131.05 ? 105 ILE D CA  1 
ATOM   4091  C  C   . ILE D  1 104 ? 38.032 30.038   -14.265  1.00 129.31 ? 105 ILE D C   1 
ATOM   4092  O  O   . ILE D  1 104 ? 37.939 31.070   -14.968  1.00 129.85 ? 105 ILE D O   1 
ATOM   4093  C  CB  . ILE D  1 104 ? 36.268 30.257   -12.478  1.00 130.98 ? 105 ILE D CB  1 
ATOM   4094  C  CG1 . ILE D  1 104 ? 35.793 31.675   -12.872  1.00 132.32 ? 105 ILE D CG1 1 
ATOM   4095  C  CG2 . ILE D  1 104 ? 35.946 29.901   -11.023  1.00 131.73 ? 105 ILE D CG2 1 
ATOM   4096  C  CD1 . ILE D  1 104 ? 34.438 31.710   -13.588  1.00 130.88 ? 105 ILE D CD1 1 
ATOM   4097  N  N   . SER D  1 105 ? 38.339 28.837   -14.756  1.00 127.03 ? 106 SER D N   1 
ATOM   4098  C  CA  . SER D  1 105 ? 38.460 28.572   -16.191  1.00 125.04 ? 106 SER D CA  1 
ATOM   4099  C  C   . SER D  1 105 ? 37.324 27.631   -16.681  1.00 122.72 ? 106 SER D C   1 
ATOM   4100  O  O   . SER D  1 105 ? 36.701 26.893   -15.900  1.00 122.15 ? 106 SER D O   1 
ATOM   4101  C  CB  . SER D  1 105 ? 39.853 27.971   -16.494  1.00 124.70 ? 106 SER D CB  1 
ATOM   4102  O  OG  . SER D  1 105 ? 40.209 28.104   -17.863  1.00 123.78 ? 106 SER D OG  1 
ATOM   4103  N  N   . LEU D  1 106 ? 37.047 27.703   -17.977  1.00 121.10 ? 107 LEU D N   1 
ATOM   4104  C  CA  . LEU D  1 106 ? 36.270 26.695   -18.661  1.00 119.01 ? 107 LEU D CA  1 
ATOM   4105  C  C   . LEU D  1 106 ? 37.272 25.915   -19.481  1.00 117.93 ? 107 LEU D C   1 
ATOM   4106  O  O   . LEU D  1 106 ? 37.126 25.812   -20.690  1.00 117.24 ? 107 LEU D O   1 
ATOM   4107  C  CB  . LEU D  1 106 ? 35.227 27.349   -19.573  1.00 118.91 ? 107 LEU D CB  1 
ATOM   4108  C  CG  . LEU D  1 106 ? 34.279 28.380   -18.943  1.00 120.01 ? 107 LEU D CG  1 
ATOM   4109  C  CD1 . LEU D  1 106 ? 33.098 28.657   -19.885  1.00 119.69 ? 107 LEU D CD1 1 
ATOM   4110  C  CD2 . LEU D  1 106 ? 33.774 27.969   -17.549  1.00 119.59 ? 107 LEU D CD2 1 
ATOM   4111  N  N   . SER D  1 107 ? 38.306 25.396   -18.818  1.00 118.10 ? 108 SER D N   1 
ATOM   4112  C  CA  . SER D  1 107 ? 39.390 24.653   -19.489  1.00 117.89 ? 108 SER D CA  1 
ATOM   4113  C  C   . SER D  1 107 ? 40.505 24.165   -18.533  1.00 118.85 ? 108 SER D C   1 
ATOM   4114  O  O   . SER D  1 107 ? 40.776 24.796   -17.491  1.00 119.85 ? 108 SER D O   1 
ATOM   4115  C  CB  . SER D  1 107 ? 40.020 25.501   -20.606  1.00 118.09 ? 108 SER D CB  1 
ATOM   4116  O  OG  . SER D  1 107 ? 40.107 26.857   -20.215  1.00 118.85 ? 108 SER D OG  1 
ATOM   4117  N  N   . GLY D  1 108 ? 41.146 23.052   -18.915  1.00 118.69 ? 109 GLY D N   1 
ATOM   4118  C  CA  . GLY D  1 108 ? 42.309 22.500   -18.195  1.00 119.85 ? 109 GLY D CA  1 
ATOM   4119  C  C   . GLY D  1 108 ? 41.953 22.032   -16.791  1.00 120.67 ? 109 GLY D C   1 
ATOM   4120  O  O   . GLY D  1 108 ? 40.757 21.872   -16.481  1.00 120.65 ? 109 GLY D O   1 
ATOM   4121  N  N   . ASP D  1 109 ? 42.976 21.808   -15.950  1.00 121.85 ? 110 ASP D N   1 
ATOM   4122  C  CA  . ASP D  1 109 ? 42.801 21.539   -14.493  1.00 122.63 ? 110 ASP D CA  1 
ATOM   4123  C  C   . ASP D  1 109 ? 41.588 22.269   -13.842  1.00 122.75 ? 110 ASP D C   1 
ATOM   4124  O  O   . ASP D  1 109 ? 40.699 21.643   -13.264  1.00 122.24 ? 110 ASP D O   1 
ATOM   4125  C  CB  . ASP D  1 109 ? 44.104 21.912   -13.739  1.00 124.55 ? 110 ASP D CB  1 
ATOM   4126  C  CG  . ASP D  1 109 ? 43.936 21.934   -12.203  1.00 125.37 ? 110 ASP D CG  1 
ATOM   4127  O  OD1 . ASP D  1 109 ? 44.120 20.860   -11.569  1.00 124.79 ? 110 ASP D OD1 1 
ATOM   4128  O  OD2 . ASP D  1 109 ? 43.645 23.028   -11.645  1.00 124.39 ? 110 ASP D OD2 1 
ATOM   4129  N  N   . HIS D  1 110 ? 41.551 23.589   -13.961  1.00 123.56 ? 111 HIS D N   1 
ATOM   4130  C  CA  . HIS D  1 110 ? 40.486 24.384   -13.363  1.00 124.25 ? 111 HIS D CA  1 
ATOM   4131  C  C   . HIS D  1 110 ? 39.096 24.050   -13.869  1.00 122.52 ? 111 HIS D C   1 
ATOM   4132  O  O   . HIS D  1 110 ? 38.118 24.500   -13.261  1.00 122.87 ? 111 HIS D O   1 
ATOM   4133  C  CB  . HIS D  1 110 ? 40.701 25.864   -13.678  1.00 125.90 ? 111 HIS D CB  1 
ATOM   4134  C  CG  . HIS D  1 110 ? 41.866 26.472   -12.972  1.00 129.42 ? 111 HIS D CG  1 
ATOM   4135  N  ND1 . HIS D  1 110 ? 41.742 27.580   -12.158  1.00 132.63 ? 111 HIS D ND1 1 
ATOM   4136  C  CD2 . HIS D  1 110 ? 43.177 26.133   -12.959  1.00 130.65 ? 111 HIS D CD2 1 
ATOM   4137  C  CE1 . HIS D  1 110 ? 42.928 27.894   -11.671  1.00 134.28 ? 111 HIS D CE1 1 
ATOM   4138  N  NE2 . HIS D  1 110 ? 43.814 27.031   -12.142  1.00 133.15 ? 111 HIS D NE2 1 
ATOM   4139  N  N   . CYS D  1 111 ? 38.996 23.324   -14.990  1.00 120.84 ? 112 CYS D N   1 
ATOM   4140  C  CA  . CYS D  1 111 ? 37.730 23.245   -15.710  1.00 119.78 ? 112 CYS D CA  1 
ATOM   4141  C  C   . CYS D  1 111 ? 36.605 23.125   -14.705  1.00 119.83 ? 112 CYS D C   1 
ATOM   4142  O  O   . CYS D  1 111 ? 36.426 22.065   -14.095  1.00 119.94 ? 112 CYS D O   1 
ATOM   4143  C  CB  . CYS D  1 111 ? 37.657 22.081   -16.701  1.00 118.38 ? 112 CYS D CB  1 
ATOM   4144  S  SG  . CYS D  1 111 ? 36.016 22.055   -17.570  1.00 118.33 ? 112 CYS D SG  1 
ATOM   4145  N  N   . ILE D  1 112 ? 35.871 24.219   -14.514  1.00 120.09 ? 113 ILE D N   1 
ATOM   4146  C  CA  . ILE D  1 112 ? 34.746 24.211   -13.602  1.00 120.26 ? 113 ILE D CA  1 
ATOM   4147  C  C   . ILE D  1 112 ? 33.592 23.391   -14.198  1.00 118.84 ? 113 ILE D C   1 
ATOM   4148  O  O   . ILE D  1 112 ? 32.728 22.913   -13.454  1.00 118.70 ? 113 ILE D O   1 
ATOM   4149  C  CB  . ILE D  1 112 ? 34.293 25.658   -13.221  1.00 121.97 ? 113 ILE D CB  1 
ATOM   4150  C  CG1 . ILE D  1 112 ? 33.522 26.350   -14.371  1.00 122.15 ? 113 ILE D CG1 1 
ATOM   4151  C  CG2 . ILE D  1 112 ? 35.510 26.487   -12.783  1.00 123.36 ? 113 ILE D CG2 1 
ATOM   4152  C  CD1 . ILE D  1 112 ? 32.566 27.474   -13.924  1.00 122.92 ? 113 ILE D CD1 1 
ATOM   4153  N  N   . ILE D  1 113 ? 33.593 23.214   -15.529  1.00 117.84 ? 114 ILE D N   1 
ATOM   4154  C  CA  . ILE D  1 113 ? 32.509 22.489   -16.226  1.00 116.76 ? 114 ILE D CA  1 
ATOM   4155  C  C   . ILE D  1 113 ? 32.499 20.991   -15.859  1.00 115.89 ? 114 ILE D C   1 
ATOM   4156  O  O   . ILE D  1 113 ? 33.544 20.314   -15.870  1.00 115.03 ? 114 ILE D O   1 
ATOM   4157  C  CB  . ILE D  1 113 ? 32.505 22.699   -17.787  1.00 116.19 ? 114 ILE D CB  1 
ATOM   4158  C  CG1 . ILE D  1 113 ? 32.480 24.185   -18.157  1.00 116.40 ? 114 ILE D CG1 1 
ATOM   4159  C  CG2 . ILE D  1 113 ? 31.280 22.037   -18.402  1.00 115.97 ? 114 ILE D CG2 1 
ATOM   4160  C  CD1 . ILE D  1 113 ? 31.549 24.520   -19.325  1.00 115.15 ? 114 ILE D CD1 1 
ATOM   4161  N  N   . GLY D  1 114 ? 31.301 20.508   -15.514  1.00 115.86 ? 115 GLY D N   1 
ATOM   4162  C  CA  . GLY D  1 114 ? 31.114 19.166   -14.939  1.00 115.67 ? 115 GLY D CA  1 
ATOM   4163  C  C   . GLY D  1 114 ? 31.000 19.089   -13.409  1.00 116.28 ? 115 GLY D C   1 
ATOM   4164  O  O   . GLY D  1 114 ? 30.590 18.046   -12.868  1.00 115.62 ? 115 GLY D O   1 
ATOM   4165  N  N   . ARG D  1 115 ? 31.362 20.184   -12.723  1.00 117.34 ? 116 ARG D N   1 
ATOM   4166  C  CA  . ARG D  1 115 ? 31.340 20.278   -11.252  1.00 118.22 ? 116 ARG D CA  1 
ATOM   4167  C  C   . ARG D  1 115 ? 30.102 21.058   -10.777  1.00 119.32 ? 116 ARG D C   1 
ATOM   4168  O  O   . ARG D  1 115 ? 29.249 21.440   -11.608  1.00 118.72 ? 116 ARG D O   1 
ATOM   4169  C  CB  . ARG D  1 115 ? 32.632 20.920   -10.753  1.00 118.91 ? 116 ARG D CB  1 
ATOM   4170  C  CG  . ARG D  1 115 ? 33.888 20.248   -11.282  1.00 118.03 ? 116 ARG D CG  1 
ATOM   4171  C  CD  . ARG D  1 115 ? 35.108 20.955   -10.743  1.00 119.58 ? 116 ARG D CD  1 
ATOM   4172  N  NE  . ARG D  1 115 ? 36.386 20.349   -11.139  1.00 119.87 ? 116 ARG D NE  1 
ATOM   4173  C  CZ  . ARG D  1 115 ? 36.922 19.245   -10.605  1.00 119.99 ? 116 ARG D CZ  1 
ATOM   4174  N  NH1 . ARG D  1 115 ? 36.292 18.558   -9.651   1.00 120.23 ? 116 ARG D NH1 1 
ATOM   4175  N  NH2 . ARG D  1 115 ? 38.103 18.810   -11.039  1.00 119.48 ? 116 ARG D NH2 1 
ATOM   4176  N  N   . THR D  1 116 ? 29.988 21.280   -9.459   1.00 120.86 ? 117 THR D N   1 
ATOM   4177  C  CA  . THR D  1 116 ? 28.721 21.786   -8.884   1.00 122.24 ? 117 THR D CA  1 
ATOM   4178  C  C   . THR D  1 116 ? 28.680 23.254   -8.358   1.00 124.66 ? 117 THR D C   1 
ATOM   4179  O  O   . THR D  1 116 ? 29.343 23.635   -7.366   1.00 125.28 ? 117 THR D O   1 
ATOM   4180  C  CB  . THR D  1 116 ? 28.167 20.833   -7.804   1.00 122.37 ? 117 THR D CB  1 
ATOM   4181  O  OG1 . THR D  1 116 ? 28.162 19.502   -8.311   1.00 120.08 ? 117 THR D OG1 1 
ATOM   4182  C  CG2 . THR D  1 116 ? 26.727 21.200   -7.434   1.00 123.49 ? 117 THR D CG2 1 
ATOM   4183  N  N   . LEU D  1 117 ? 27.847 24.042   -9.055   1.00 125.88 ? 118 LEU D N   1 
ATOM   4184  C  CA  . LEU D  1 117 ? 27.468 25.401   -8.659   1.00 128.39 ? 118 LEU D CA  1 
ATOM   4185  C  C   . LEU D  1 117 ? 26.308 25.322   -7.678   1.00 130.14 ? 118 LEU D C   1 
ATOM   4186  O  O   . LEU D  1 117 ? 25.290 24.676   -7.977   1.00 129.53 ? 118 LEU D O   1 
ATOM   4187  C  CB  . LEU D  1 117 ? 27.018 26.221   -9.869   1.00 128.19 ? 118 LEU D CB  1 
ATOM   4188  C  CG  . LEU D  1 117 ? 27.181 27.718   -9.637   1.00 130.23 ? 118 LEU D CG  1 
ATOM   4189  C  CD1 . LEU D  1 117 ? 28.693 28.088   -9.682   1.00 129.15 ? 118 LEU D CD1 1 
ATOM   4190  C  CD2 . LEU D  1 117 ? 26.329 28.518   -10.647  1.00 130.36 ? 118 LEU D CD2 1 
ATOM   4191  N  N   . VAL D  1 118 ? 26.462 25.989   -6.527   1.00 132.77 ? 119 VAL D N   1 
ATOM   4192  C  CA  . VAL D  1 118 ? 25.532 25.852   -5.392   1.00 134.26 ? 119 VAL D CA  1 
ATOM   4193  C  C   . VAL D  1 118 ? 25.410 27.159   -4.562   1.00 137.16 ? 119 VAL D C   1 
ATOM   4194  O  O   . VAL D  1 118 ? 26.299 27.484   -3.743   1.00 138.24 ? 119 VAL D O   1 
ATOM   4195  C  CB  . VAL D  1 118 ? 25.958 24.652   -4.470   1.00 133.83 ? 119 VAL D CB  1 
ATOM   4196  C  CG1 . VAL D  1 118 ? 25.126 24.612   -3.206   1.00 135.96 ? 119 VAL D CG1 1 
ATOM   4197  C  CG2 . VAL D  1 118 ? 25.835 23.308   -5.203   1.00 131.59 ? 119 VAL D CG2 1 
ATOM   4198  N  N   . VAL D  1 119 ? 24.317 27.904   -4.795   1.00 138.57 ? 120 VAL D N   1 
ATOM   4199  C  CA  . VAL D  1 119 ? 23.916 29.030   -3.911   1.00 141.72 ? 120 VAL D CA  1 
ATOM   4200  C  C   . VAL D  1 119 ? 23.444 28.450   -2.565   1.00 142.88 ? 120 VAL D C   1 
ATOM   4201  O  O   . VAL D  1 119 ? 22.845 27.360   -2.536   1.00 142.03 ? 120 VAL D O   1 
ATOM   4202  C  CB  . VAL D  1 119 ? 22.795 29.958   -4.537   1.00 142.87 ? 120 VAL D CB  1 
ATOM   4203  C  CG1 . VAL D  1 119 ? 21.494 29.181   -4.832   1.00 141.72 ? 120 VAL D CG1 1 
ATOM   4204  C  CG2 . VAL D  1 119 ? 22.501 31.145   -3.614   1.00 146.00 ? 120 VAL D CG2 1 
ATOM   4205  N  N   . HIS D  1 120 ? 23.703 29.153   -1.461   1.00 145.20 ? 121 HIS D N   1 
ATOM   4206  C  CA  . HIS D  1 120 ? 23.341 28.641   -0.123   1.00 146.45 ? 121 HIS D CA  1 
ATOM   4207  C  C   . HIS D  1 120 ? 22.072 29.292   0.485    1.00 149.01 ? 121 HIS D C   1 
ATOM   4208  O  O   . HIS D  1 120 ? 21.451 30.157   -0.155   1.00 150.22 ? 121 HIS D O   1 
ATOM   4209  C  CB  . HIS D  1 120 ? 24.524 28.804   0.806    1.00 147.75 ? 121 HIS D CB  1 
ATOM   4210  C  CG  . HIS D  1 120 ? 25.738 28.064   0.353    1.00 146.26 ? 121 HIS D CG  1 
ATOM   4211  N  ND1 . HIS D  1 120 ? 26.190 26.929   0.991    1.00 146.69 ? 121 HIS D ND1 1 
ATOM   4212  C  CD2 . HIS D  1 120 ? 26.596 28.289   -0.673   1.00 145.35 ? 121 HIS D CD2 1 
ATOM   4213  C  CE1 . HIS D  1 120 ? 27.286 26.495   0.389    1.00 145.02 ? 121 HIS D CE1 1 
ATOM   4214  N  NE2 . HIS D  1 120 ? 27.551 27.301   -0.627   1.00 144.31 ? 121 HIS D NE2 1 
ATOM   4215  N  N   . GLU D  1 121 ? 21.667 28.852   1.686    1.00 149.99 ? 122 GLU D N   1 
ATOM   4216  C  CA  . GLU D  1 121 ? 20.587 29.524   2.426    1.00 152.61 ? 122 GLU D CA  1 
ATOM   4217  C  C   . GLU D  1 121 ? 21.176 30.757   3.107    1.00 155.70 ? 122 GLU D C   1 
ATOM   4218  O  O   . GLU D  1 121 ? 20.726 31.895   2.889    1.00 157.63 ? 122 GLU D O   1 
ATOM   4219  C  CB  . GLU D  1 121 ? 19.940 28.594   3.474    1.00 153.02 ? 122 GLU D CB  1 
ATOM   4220  C  CG  . GLU D  1 121 ? 18.584 29.147   4.077    1.00 155.95 ? 122 GLU D CG  1 
ATOM   4221  C  CD  . GLU D  1 121 ? 18.495 29.154   5.639    1.00 158.75 ? 122 GLU D CD  1 
ATOM   4222  O  OE1 . GLU D  1 121 ? 19.538 29.181   6.337    1.00 159.77 ? 122 GLU D OE1 1 
ATOM   4223  O  OE2 . GLU D  1 121 ? 17.363 29.163   6.177    1.00 159.41 ? 122 GLU D OE2 1 
ATOM   4224  N  N   . LYS D  1 122 ? 22.201 30.519   3.921    1.00 155.99 ? 123 LYS D N   1 
ATOM   4225  C  CA  . LYS D  1 122 ? 22.778 31.581   4.716    1.00 159.26 ? 123 LYS D CA  1 
ATOM   4226  C  C   . LYS D  1 122 ? 23.753 32.407   3.879    1.00 158.84 ? 123 LYS D C   1 
ATOM   4227  O  O   . LYS D  1 122 ? 23.822 32.267   2.652    1.00 155.54 ? 123 LYS D O   1 
ATOM   4228  C  CB  . LYS D  1 122 ? 23.410 31.018   6.004    1.00 160.68 ? 123 LYS D CB  1 
ATOM   4229  C  CG  . LYS D  1 122 ? 22.398 30.280   6.915    1.00 161.92 ? 123 LYS D CG  1 
ATOM   4230  C  CD  . LYS D  1 122 ? 22.701 30.444   8.438    1.00 165.71 ? 123 LYS D CD  1 
ATOM   4231  C  CE  . LYS D  1 122 ? 21.424 30.318   9.296    1.00 167.23 ? 123 LYS D CE  1 
ATOM   4232  N  NZ  . LYS D  1 122 ? 21.522 31.034   10.595   1.00 170.90 ? 123 LYS D NZ  1 
ATOM   4233  N  N   . ALA D  1 123 ? 24.453 33.316   4.554    1.00 162.00 ? 124 ALA D N   1 
ATOM   4234  C  CA  . ALA D  1 123 ? 25.361 34.246   3.902    1.00 162.57 ? 124 ALA D CA  1 
ATOM   4235  C  C   . ALA D  1 123 ? 26.767 33.711   4.014    1.00 161.50 ? 124 ALA D C   1 
ATOM   4236  O  O   . ALA D  1 123 ? 27.188 33.243   5.069    1.00 162.43 ? 124 ALA D O   1 
ATOM   4237  C  CB  . ALA D  1 123 ? 25.278 35.637   4.548    1.00 166.98 ? 124 ALA D CB  1 
ATOM   4238  N  N   . ASP D  1 124 ? 27.483 33.758   2.901    1.00 159.58 ? 125 ASP D N   1 
ATOM   4239  C  CA  . ASP D  1 124 ? 28.934 33.674   2.929    1.00 159.57 ? 125 ASP D CA  1 
ATOM   4240  C  C   . ASP D  1 124 ? 29.446 34.903   3.719    1.00 163.93 ? 125 ASP D C   1 
ATOM   4241  O  O   . ASP D  1 124 ? 29.045 36.065   3.469    1.00 165.89 ? 125 ASP D O   1 
ATOM   4242  C  CB  . ASP D  1 124 ? 29.493 33.654   1.487    1.00 156.94 ? 125 ASP D CB  1 
ATOM   4243  C  CG  . ASP D  1 124 ? 30.990 33.298   1.414    1.00 156.18 ? 125 ASP D CG  1 
ATOM   4244  O  OD1 . ASP D  1 124 ? 31.502 32.637   2.351    1.00 155.85 ? 125 ASP D OD1 1 
ATOM   4245  O  OD2 . ASP D  1 124 ? 31.641 33.676   0.401    1.00 154.88 ? 125 ASP D OD2 1 
ATOM   4246  N  N   . ASP D  1 125 ? 30.308 34.644   4.695    1.00 165.47 ? 126 ASP D N   1 
ATOM   4247  C  CA  . ASP D  1 125 ? 30.948 35.728   5.435    1.00 169.82 ? 126 ASP D CA  1 
ATOM   4248  C  C   . ASP D  1 125 ? 32.066 36.406   4.620    1.00 170.23 ? 126 ASP D C   1 
ATOM   4249  O  O   . ASP D  1 125 ? 32.581 37.445   5.046    1.00 174.10 ? 126 ASP D O   1 
ATOM   4250  C  CB  . ASP D  1 125 ? 31.484 35.228   6.781    1.00 171.86 ? 126 ASP D CB  1 
ATOM   4251  C  CG  . ASP D  1 125 ? 32.461 34.052   6.644    1.00 168.96 ? 126 ASP D CG  1 
ATOM   4252  O  OD1 . ASP D  1 125 ? 33.364 34.058   5.780    1.00 164.62 ? 126 ASP D OD1 1 
ATOM   4253  O  OD2 . ASP D  1 125 ? 32.328 33.108   7.443    1.00 169.81 ? 126 ASP D OD2 1 
ATOM   4254  N  N   . LEU D  1 126 ? 32.414 35.814   3.463    1.00 166.63 ? 127 LEU D N   1 
ATOM   4255  C  CA  . LEU D  1 126 ? 33.506 36.251   2.542    1.00 165.94 ? 127 LEU D CA  1 
ATOM   4256  C  C   . LEU D  1 126 ? 34.910 35.876   3.097    1.00 167.06 ? 127 LEU D C   1 
ATOM   4257  O  O   . LEU D  1 126 ? 35.930 36.437   2.699    1.00 167.49 ? 127 LEU D O   1 
ATOM   4258  C  CB  . LEU D  1 126 ? 33.394 37.761   2.187    1.00 168.76 ? 127 LEU D CB  1 
ATOM   4259  C  CG  . LEU D  1 126 ? 32.040 38.404   1.774    1.00 168.46 ? 127 LEU D CG  1 
ATOM   4260  C  CD1 . LEU D  1 126 ? 31.846 39.786   2.417    1.00 171.92 ? 127 LEU D CD1 1 
ATOM   4261  C  CD2 . LEU D  1 126 ? 31.881 38.508   0.251    1.00 164.96 ? 127 LEU D CD2 1 
ATOM   4262  N  N   . GLY D  1 127 ? 34.939 34.898   4.002    1.00 167.49 ? 128 GLY D N   1 
ATOM   4263  C  CA  . GLY D  1 127 ? 36.135 34.555   4.761    1.00 169.81 ? 128 GLY D CA  1 
ATOM   4264  C  C   . GLY D  1 127 ? 36.108 35.259   6.104    1.00 175.40 ? 128 GLY D C   1 
ATOM   4265  O  O   . GLY D  1 127 ? 36.650 34.741   7.090    1.00 176.96 ? 128 GLY D O   1 
ATOM   4266  N  N   . LYS D  1 128 ? 35.407 36.404   6.141    1.00 178.87 ? 129 LYS D N   1 
ATOM   4267  C  CA  . LYS D  1 128 ? 35.524 37.464   7.191    1.00 184.91 ? 129 LYS D CA  1 
ATOM   4268  C  C   . LYS D  1 128 ? 34.568 37.319   8.425    1.00 187.77 ? 129 LYS D C   1 
ATOM   4269  O  O   . LYS D  1 128 ? 33.723 38.207   8.710    1.00 190.00 ? 129 LYS D O   1 
ATOM   4270  C  CB  . LYS D  1 128 ? 35.352 38.858   6.533    1.00 186.67 ? 129 LYS D CB  1 
ATOM   4271  C  CG  . LYS D  1 128 ? 36.592 39.395   5.807    1.00 187.22 ? 129 LYS D CG  1 
ATOM   4272  C  CD  . LYS D  1 128 ? 37.393 40.328   6.721    1.00 193.53 ? 129 LYS D CD  1 
ATOM   4273  C  CE  . LYS D  1 128 ? 38.780 40.644   6.152    1.00 194.33 ? 129 LYS D CE  1 
ATOM   4274  N  NZ  . LYS D  1 128 ? 39.704 39.448   6.142    1.00 191.61 ? 129 LYS D NZ  1 
ATOM   4275  N  N   . GLY D  1 129 ? 34.741 36.193   9.142    1.00 187.64 ? 130 GLY D N   1 
ATOM   4276  C  CA  . GLY D  1 129 ? 34.017 35.871   10.392   1.00 190.02 ? 130 GLY D CA  1 
ATOM   4277  C  C   . GLY D  1 129 ? 34.952 35.346   11.484   1.00 192.73 ? 130 GLY D C   1 
ATOM   4278  O  O   . GLY D  1 129 ? 36.186 35.495   11.391   1.00 193.46 ? 130 GLY D O   1 
ATOM   4279  N  N   . GLY D  1 130 ? 34.366 34.702   12.499   1.00 194.10 ? 131 GLY D N   1 
ATOM   4280  C  CA  . GLY D  1 130 ? 35.088 34.361   13.743   1.00 197.90 ? 131 GLY D CA  1 
ATOM   4281  C  C   . GLY D  1 130 ? 35.723 32.973   13.861   1.00 195.98 ? 131 GLY D C   1 
ATOM   4282  O  O   . GLY D  1 130 ? 36.936 32.848   14.100   1.00 197.57 ? 131 GLY D O   1 
ATOM   4283  N  N   . ASN D  1 131 ? 34.897 31.932   13.718   1.00 193.06 ? 132 ASN D N   1 
ATOM   4284  C  CA  . ASN D  1 131 ? 35.325 30.510   13.850   1.00 190.93 ? 132 ASN D CA  1 
ATOM   4285  C  C   . ASN D  1 131 ? 36.004 29.917   12.571   1.00 186.67 ? 132 ASN D C   1 
ATOM   4286  O  O   . ASN D  1 131 ? 36.162 30.620   11.552   1.00 185.51 ? 132 ASN D O   1 
ATOM   4287  C  CB  . ASN D  1 131 ? 34.113 29.640   14.290   1.00 189.50 ? 132 ASN D CB  1 
ATOM   4288  C  CG  . ASN D  1 131 ? 32.914 29.698   13.292   1.00 186.76 ? 132 ASN D CG  1 
ATOM   4289  O  OD1 . ASN D  1 131 ? 32.813 30.605   12.440   1.00 187.17 ? 132 ASN D OD1 1 
ATOM   4290  N  ND2 . ASN D  1 131 ? 32.004 28.726   13.413   1.00 184.40 ? 132 ASN D ND2 1 
ATOM   4291  N  N   . GLU D  1 132 ? 36.399 28.634   12.627   1.00 184.44 ? 133 GLU D N   1 
ATOM   4292  C  CA  . GLU D  1 132 ? 36.921 27.905   11.426   1.00 180.14 ? 133 GLU D CA  1 
ATOM   4293  C  C   . GLU D  1 132 ? 35.888 27.721   10.286   1.00 175.69 ? 133 GLU D C   1 
ATOM   4294  O  O   . GLU D  1 132 ? 36.278 27.460   9.136    1.00 172.53 ? 133 GLU D O   1 
ATOM   4295  C  CB  . GLU D  1 132 ? 37.530 26.517   11.784   1.00 179.11 ? 133 GLU D CB  1 
ATOM   4296  C  CG  . GLU D  1 132 ? 36.505 25.328   11.929   1.00 176.62 ? 133 GLU D CG  1 
ATOM   4297  C  CD  . GLU D  1 132 ? 35.708 24.967   10.634   1.00 171.44 ? 133 GLU D CD  1 
ATOM   4298  O  OE1 . GLU D  1 132 ? 36.304 24.833   9.541    1.00 168.67 ? 133 GLU D OE1 1 
ATOM   4299  O  OE2 . GLU D  1 132 ? 34.471 24.813   10.716   1.00 168.98 ? 133 GLU D OE2 1 
ATOM   4300  N  N   . GLU D  1 133 ? 34.591 27.822   10.607   1.00 175.28 ? 134 GLU D N   1 
ATOM   4301  C  CA  . GLU D  1 133 ? 33.521 27.641   9.613    1.00 171.51 ? 134 GLU D CA  1 
ATOM   4302  C  C   . GLU D  1 133 ? 33.413 28.830   8.620    1.00 170.94 ? 134 GLU D C   1 
ATOM   4303  O  O   . GLU D  1 133 ? 32.629 28.782   7.658    1.00 168.21 ? 134 GLU D O   1 
ATOM   4304  C  CB  . GLU D  1 133 ? 32.181 27.328   10.309   1.00 171.74 ? 134 GLU D CB  1 
ATOM   4305  C  CG  . GLU D  1 133 ? 31.034 26.868   9.381    1.00 168.53 ? 134 GLU D CG  1 
ATOM   4306  C  CD  . GLU D  1 133 ? 31.322 25.566   8.595    1.00 165.30 ? 134 GLU D CD  1 
ATOM   4307  O  OE1 . GLU D  1 133 ? 32.427 24.980   8.712    1.00 165.35 ? 134 GLU D OE1 1 
ATOM   4308  O  OE2 . GLU D  1 133 ? 30.414 25.128   7.847    1.00 162.75 ? 134 GLU D OE2 1 
ATOM   4309  N  N   . SER D  1 134 ? 34.206 29.881   8.844    1.00 173.40 ? 135 SER D N   1 
ATOM   4310  C  CA  . SER D  1 134 ? 34.532 30.821   7.769    1.00 172.39 ? 135 SER D CA  1 
ATOM   4311  C  C   . SER D  1 134 ? 35.582 30.219   6.824    1.00 169.47 ? 135 SER D C   1 
ATOM   4312  O  O   . SER D  1 134 ? 35.469 30.341   5.604    1.00 166.56 ? 135 SER D O   1 
ATOM   4313  C  CB  . SER D  1 134 ? 35.041 32.151   8.319    1.00 176.86 ? 135 SER D CB  1 
ATOM   4314  O  OG  . SER D  1 134 ? 35.192 33.092   7.267    1.00 175.37 ? 135 SER D OG  1 
ATOM   4315  N  N   . THR D  1 135 ? 36.589 29.555   7.403    1.00 170.22 ? 136 THR D N   1 
ATOM   4316  C  CA  . THR D  1 135 ? 37.702 28.937   6.642    1.00 168.13 ? 136 THR D CA  1 
ATOM   4317  C  C   . THR D  1 135 ? 37.393 27.523   6.047    1.00 164.10 ? 136 THR D C   1 
ATOM   4318  O  O   . THR D  1 135 ? 38.325 26.762   5.720    1.00 163.01 ? 136 THR D O   1 
ATOM   4319  C  CB  . THR D  1 135 ? 39.049 28.887   7.487    1.00 171.29 ? 136 THR D CB  1 
ATOM   4320  O  OG1 . THR D  1 135 ? 39.107 27.701   8.304    1.00 170.56 ? 136 THR D OG1 1 
ATOM   4321  C  CG2 . THR D  1 135 ? 39.235 30.161   8.350    1.00 175.61 ? 136 THR D CG2 1 
ATOM   4322  N  N   . LYS D  1 136 ? 36.101 27.189   5.906    1.00 162.00 ? 137 LYS D N   1 
ATOM   4323  C  CA  . LYS D  1 136 ? 35.657 25.958   5.219    1.00 157.89 ? 137 LYS D CA  1 
ATOM   4324  C  C   . LYS D  1 136 ? 34.349 26.156   4.432    1.00 155.72 ? 137 LYS D C   1 
ATOM   4325  O  O   . LYS D  1 136 ? 34.321 25.871   3.225    1.00 152.99 ? 137 LYS D O   1 
ATOM   4326  C  CB  . LYS D  1 136 ? 35.539 24.786   6.198    1.00 158.02 ? 137 LYS D CB  1 
ATOM   4327  C  CG  . LYS D  1 136 ? 36.874 24.088   6.473    1.00 158.12 ? 137 LYS D CG  1 
ATOM   4328  C  CD  . LYS D  1 136 ? 36.677 22.705   7.078    1.00 157.12 ? 137 LYS D CD  1 
ATOM   4329  C  CE  . LYS D  1 136 ? 37.948 21.871   7.006    1.00 156.75 ? 137 LYS D CE  1 
ATOM   4330  N  NZ  . LYS D  1 136 ? 39.082 22.536   7.684    1.00 159.99 ? 137 LYS D NZ  1 
ATOM   4331  N  N   . THR D  1 137 ? 33.281 26.630   5.084    1.00 157.12 ? 138 THR D N   1 
ATOM   4332  C  CA  . THR D  1 137 ? 32.082 27.074   4.334    1.00 156.09 ? 138 THR D CA  1 
ATOM   4333  C  C   . THR D  1 137 ? 32.007 28.596   4.109    1.00 157.99 ? 138 THR D C   1 
ATOM   4334  O  O   . THR D  1 137 ? 31.350 29.044   3.168    1.00 156.65 ? 138 THR D O   1 
ATOM   4335  C  CB  . THR D  1 137 ? 30.679 26.575   4.932    1.00 156.20 ? 138 THR D CB  1 
ATOM   4336  O  OG1 . THR D  1 137 ? 30.477 27.047   6.274    1.00 159.99 ? 138 THR D OG1 1 
ATOM   4337  C  CG2 . THR D  1 137 ? 30.529 25.041   4.867    1.00 154.09 ? 138 THR D CG2 1 
ATOM   4338  N  N   . GLY D  1 138 ? 32.671 29.390   4.945    1.00 161.39 ? 139 GLY D N   1 
ATOM   4339  C  CA  . GLY D  1 138 ? 32.416 30.829   4.949    1.00 164.14 ? 139 GLY D CA  1 
ATOM   4340  C  C   . GLY D  1 138 ? 31.073 31.100   5.611    1.00 165.87 ? 139 GLY D C   1 
ATOM   4341  O  O   . GLY D  1 138 ? 30.337 32.005   5.194    1.00 166.54 ? 139 GLY D O   1 
ATOM   4342  N  N   . ASN D  1 139 ? 30.767 30.295   6.638    1.00 166.74 ? 140 ASN D N   1 
ATOM   4343  C  CA  . ASN D  1 139 ? 29.499 30.337   7.398    1.00 168.40 ? 140 ASN D CA  1 
ATOM   4344  C  C   . ASN D  1 139 ? 28.220 30.522   6.549    1.00 166.82 ? 140 ASN D C   1 
ATOM   4345  O  O   . ASN D  1 139 ? 27.259 31.180   6.986    1.00 168.99 ? 140 ASN D O   1 
ATOM   4346  C  CB  . ASN D  1 139 ? 29.581 31.395   8.520    1.00 173.24 ? 140 ASN D CB  1 
ATOM   4347  C  CG  . ASN D  1 139 ? 30.524 30.982   9.653    1.00 175.69 ? 140 ASN D CG  1 
ATOM   4348  O  OD1 . ASN D  1 139 ? 31.430 31.736   10.041   1.00 178.66 ? 140 ASN D OD1 1 
ATOM   4349  N  ND2 . ASN D  1 139 ? 30.310 29.780   10.190   1.00 174.00 ? 140 ASN D ND2 1 
ATOM   4350  N  N   . ALA D  1 140 ? 28.211 29.907   5.357    1.00 163.23 ? 141 ALA D N   1 
ATOM   4351  C  CA  . ALA D  1 140 ? 27.069 29.976   4.428    1.00 161.36 ? 141 ALA D CA  1 
ATOM   4352  C  C   . ALA D  1 140 ? 25.883 29.044   4.838    1.00 160.36 ? 141 ALA D C   1 
ATOM   4353  O  O   . ALA D  1 140 ? 24.812 29.059   4.190    1.00 159.20 ? 141 ALA D O   1 
ATOM   4354  C  CB  . ALA D  1 140 ? 27.544 29.706   2.985    1.00 157.90 ? 141 ALA D CB  1 
ATOM   4355  N  N   . GLY D  1 141 ? 26.080 28.262   5.912    1.00 160.84 ? 142 GLY D N   1 
ATOM   4356  C  CA  . GLY D  1 141 ? 24.996 27.554   6.603    1.00 160.76 ? 142 GLY D CA  1 
ATOM   4357  C  C   . GLY D  1 141 ? 24.686 26.199   6.007    1.00 157.26 ? 142 GLY D C   1 
ATOM   4358  O  O   . GLY D  1 141 ? 25.249 25.187   6.413    1.00 155.97 ? 142 GLY D O   1 
ATOM   4359  N  N   . SER D  1 142 ? 23.760 26.195   5.051    1.00 155.95 ? 143 SER D N   1 
ATOM   4360  C  CA  . SER D  1 142 ? 23.409 24.999   4.267    1.00 152.73 ? 143 SER D CA  1 
ATOM   4361  C  C   . SER D  1 142 ? 23.043 25.392   2.816    1.00 150.83 ? 143 SER D C   1 
ATOM   4362  O  O   . SER D  1 142 ? 22.842 26.586   2.515    1.00 152.09 ? 143 SER D O   1 
ATOM   4363  C  CB  . SER D  1 142 ? 22.272 24.196   4.951    1.00 153.02 ? 143 SER D CB  1 
ATOM   4364  O  OG  . SER D  1 142 ? 21.175 25.017   5.346    1.00 155.35 ? 143 SER D OG  1 
ATOM   4365  N  N   . ARG D  1 143 ? 22.946 24.373   1.950    1.00 147.79 ? 144 ARG D N   1 
ATOM   4366  C  CA  . ARG D  1 143 ? 22.735 24.540   0.492    1.00 145.62 ? 144 ARG D CA  1 
ATOM   4367  C  C   . ARG D  1 143 ? 21.243 24.388   0.118    1.00 145.09 ? 144 ARG D C   1 
ATOM   4368  O  O   . ARG D  1 143 ? 20.671 23.291   0.167    1.00 143.66 ? 144 ARG D O   1 
ATOM   4369  C  CB  . ARG D  1 143 ? 23.602 23.538   -0.291   1.00 142.95 ? 144 ARG D CB  1 
ATOM   4370  C  CG  . ARG D  1 143 ? 24.894 23.102   0.455    1.00 143.38 ? 144 ARG D CG  1 
ATOM   4371  C  CD  . ARG D  1 143 ? 25.821 22.221   -0.397   1.00 141.22 ? 144 ARG D CD  1 
ATOM   4372  N  NE  . ARG D  1 143 ? 26.793 21.483   0.424    1.00 141.76 ? 144 ARG D NE  1 
ATOM   4373  C  CZ  . ARG D  1 143 ? 27.874 20.844   -0.039   1.00 140.56 ? 144 ARG D CZ  1 
ATOM   4374  N  NH1 . ARG D  1 143 ? 28.164 20.834   -1.342   1.00 138.53 ? 144 ARG D NH1 1 
ATOM   4375  N  NH2 . ARG D  1 143 ? 28.683 20.212   0.815    1.00 140.83 ? 144 ARG D NH2 1 
ATOM   4376  N  N   . LEU D  1 144 ? 20.617 25.512   -0.222   1.00 146.29 ? 145 LEU D N   1 
ATOM   4377  C  CA  . LEU D  1 144 ? 19.215 25.526   -0.598   1.00 146.57 ? 145 LEU D CA  1 
ATOM   4378  C  C   . LEU D  1 144 ? 19.100 24.683   -1.858   1.00 143.85 ? 145 LEU D C   1 
ATOM   4379  O  O   . LEU D  1 144 ? 18.522 23.578   -1.843   1.00 143.11 ? 145 LEU D O   1 
ATOM   4380  C  CB  . LEU D  1 144 ? 18.706 26.961   -0.886   1.00 148.83 ? 145 LEU D CB  1 
ATOM   4381  C  CG  . LEU D  1 144 ? 18.704 28.094   0.163    1.00 152.60 ? 145 LEU D CG  1 
ATOM   4382  C  CD1 . LEU D  1 144 ? 18.835 29.462   -0.520   1.00 154.16 ? 145 LEU D CD1 1 
ATOM   4383  C  CD2 . LEU D  1 144 ? 17.465 28.104   1.089    1.00 155.06 ? 145 LEU D CD2 1 
ATOM   4384  N  N   . ALA D  1 145 ? 19.695 25.204   -2.934   1.00 142.53 ? 146 ALA D N   1 
ATOM   4385  C  CA  . ALA D  1 145 ? 19.653 24.576   -4.253   1.00 139.79 ? 146 ALA D CA  1 
ATOM   4386  C  C   . ALA D  1 145 ? 21.059 24.076   -4.640   1.00 137.44 ? 146 ALA D C   1 
ATOM   4387  O  O   . ALA D  1 145 ? 22.018 24.224   -3.856   1.00 138.39 ? 146 ALA D O   1 
ATOM   4388  C  CB  . ALA D  1 145 ? 19.110 25.570   -5.295   1.00 140.41 ? 146 ALA D CB  1 
ATOM   4389  N  N   . CYS D  1 146 ? 21.170 23.470   -5.825   1.00 134.44 ? 147 CYS D N   1 
ATOM   4390  C  CA  . CYS D  1 146 ? 22.451 23.006   -6.373   1.00 132.04 ? 147 CYS D CA  1 
ATOM   4391  C  C   . CYS D  1 146 ? 22.322 22.965   -7.919   1.00 130.01 ? 147 CYS D C   1 
ATOM   4392  O  O   . CYS D  1 146 ? 21.264 23.296   -8.452   1.00 130.00 ? 147 CYS D O   1 
ATOM   4393  C  CB  . CYS D  1 146 ? 22.884 21.659   -5.723   1.00 130.96 ? 147 CYS D CB  1 
ATOM   4394  S  SG  . CYS D  1 146 ? 21.516 20.478   -5.154   1.00 131.98 ? 147 CYS D SG  1 
ATOM   4395  N  N   . GLY D  1 147 ? 23.387 22.615   -8.640   1.00 127.87 ? 148 GLY D N   1 
ATOM   4396  C  CA  . GLY D  1 147 ? 23.310 22.556   -10.108  1.00 126.12 ? 148 GLY D CA  1 
ATOM   4397  C  C   . GLY D  1 147 ? 24.632 22.195   -10.746  1.00 124.41 ? 148 GLY D C   1 
ATOM   4398  O  O   . GLY D  1 147 ? 25.678 22.679   -10.300  1.00 124.52 ? 148 GLY D O   1 
ATOM   4399  N  N   . VAL D  1 148 ? 24.588 21.354   -11.789  1.00 122.75 ? 149 VAL D N   1 
ATOM   4400  C  CA  . VAL D  1 148 ? 25.818 20.884   -12.486  1.00 121.20 ? 149 VAL D CA  1 
ATOM   4401  C  C   . VAL D  1 148 ? 26.196 21.824   -13.662  1.00 120.74 ? 149 VAL D C   1 
ATOM   4402  O  O   . VAL D  1 148 ? 25.306 22.350   -14.378  1.00 120.92 ? 149 VAL D O   1 
ATOM   4403  C  CB  . VAL D  1 148 ? 25.711 19.366   -12.960  1.00 120.05 ? 149 VAL D CB  1 
ATOM   4404  C  CG1 . VAL D  1 148 ? 26.999 18.904   -13.654  1.00 118.96 ? 149 VAL D CG1 1 
ATOM   4405  C  CG2 . VAL D  1 148 ? 25.398 18.420   -11.783  1.00 119.67 ? 149 VAL D CG2 1 
ATOM   4406  N  N   . ILE D  1 149 ? 27.508 22.036   -13.844  1.00 119.75 ? 150 ILE D N   1 
ATOM   4407  C  CA  . ILE D  1 149 ? 28.012 22.959   -14.879  1.00 119.53 ? 150 ILE D CA  1 
ATOM   4408  C  C   . ILE D  1 149 ? 28.150 22.272   -16.234  1.00 117.80 ? 150 ILE D C   1 
ATOM   4409  O  O   . ILE D  1 149 ? 28.960 21.343   -16.390  1.00 116.02 ? 150 ILE D O   1 
ATOM   4410  C  CB  . ILE D  1 149 ? 29.384 23.573   -14.518  1.00 120.10 ? 150 ILE D CB  1 
ATOM   4411  C  CG1 . ILE D  1 149 ? 29.339 24.259   -13.158  1.00 121.98 ? 150 ILE D CG1 1 
ATOM   4412  C  CG2 . ILE D  1 149 ? 29.803 24.613   -15.564  1.00 120.15 ? 150 ILE D CG2 1 
ATOM   4413  C  CD1 . ILE D  1 149 ? 30.710 24.639   -12.647  1.00 122.67 ? 150 ILE D CD1 1 
ATOM   4414  N  N   . GLY D  1 150 ? 27.367 22.766   -17.201  1.00 117.68 ? 151 GLY D N   1 
ATOM   4415  C  CA  . GLY D  1 150 ? 27.235 22.145   -18.525  1.00 116.92 ? 151 GLY D CA  1 
ATOM   4416  C  C   . GLY D  1 150 ? 27.393 23.113   -19.687  1.00 117.08 ? 151 GLY D C   1 
ATOM   4417  O  O   . GLY D  1 150 ? 27.129 24.312   -19.542  1.00 118.21 ? 151 GLY D O   1 
ATOM   4418  N  N   . ILE D  1 151 ? 27.800 22.575   -20.844  1.00 116.05 ? 152 ILE D N   1 
ATOM   4419  C  CA  . ILE D  1 151 ? 28.211 23.368   -22.017  1.00 115.96 ? 152 ILE D CA  1 
ATOM   4420  C  C   . ILE D  1 151 ? 27.043 23.713   -22.940  1.00 116.79 ? 152 ILE D C   1 
ATOM   4421  O  O   . ILE D  1 151 ? 26.266 22.836   -23.265  1.00 116.99 ? 152 ILE D O   1 
ATOM   4422  C  CB  . ILE D  1 151 ? 29.239 22.581   -22.856  1.00 115.00 ? 152 ILE D CB  1 
ATOM   4423  C  CG1 . ILE D  1 151 ? 30.501 22.276   -22.024  1.00 114.15 ? 152 ILE D CG1 1 
ATOM   4424  C  CG2 . ILE D  1 151 ? 29.572 23.349   -24.105  1.00 115.14 ? 152 ILE D CG2 1 
ATOM   4425  C  CD1 . ILE D  1 151 ? 31.570 21.444   -22.750  1.00 112.45 ? 152 ILE D CD1 1 
ATOM   4426  N  N   . ALA D  1 152 ? 26.935 24.974   -23.375  1.00 117.77 ? 153 ALA D N   1 
ATOM   4427  C  CA  . ALA D  1 152 ? 25.872 25.429   -24.320  1.00 118.83 ? 153 ALA D CA  1 
ATOM   4428  C  C   . ALA D  1 152 ? 26.460 25.906   -25.652  1.00 119.06 ? 153 ALA D C   1 
ATOM   4429  O  O   . ALA D  1 152 ? 27.687 25.887   -25.858  1.00 118.08 ? 153 ALA D O   1 
ATOM   4430  C  CB  . ALA D  1 152 ? 25.004 26.538   -23.697  1.00 120.01 ? 153 ALA D CB  1 
ATOM   4431  N  N   . GLN D  1 153 ? 25.588 26.336   -26.560  1.00 120.31 ? 154 GLN D N   1 
ATOM   4432  C  CA  . GLN D  1 153 ? 26.038 26.620   -27.927  1.00 120.93 ? 154 GLN D CA  1 
ATOM   4433  C  C   . GLN D  1 153 ? 26.744 27.964   -28.041  1.00 121.62 ? 154 GLN D C   1 
ATOM   4434  O  O   . GLN D  1 153 ? 26.110 28.977   -28.389  1.00 122.92 ? 154 GLN D O   1 
ATOM   4435  C  CB  . GLN D  1 153 ? 24.896 26.524   -28.947  1.00 122.16 ? 154 GLN D CB  1 
ATOM   4436  C  CG  . GLN D  1 153 ? 25.369 26.736   -30.399  1.00 121.92 ? 154 GLN D CG  1 
ATOM   4437  C  CD  . GLN D  1 153 ? 24.615 25.888   -31.391  1.00 122.17 ? 154 GLN D CD  1 
ATOM   4438  O  OE1 . GLN D  1 153 ? 23.679 25.176   -31.029  1.00 123.07 ? 154 GLN D OE1 1 
ATOM   4439  N  NE2 . GLN D  1 153 ? 25.022 25.949   -32.651  1.00 121.74 ? 154 GLN D NE2 1 
ATOM   4440  O  OXT . GLN D  1 153 ? 27.967 28.012   -27.799  1.00 120.93 ? 154 GLN D OXT 1 
ATOM   4441  N  N   . ALA E  1 1   ? 24.609 -16.146  -75.338  1.00 94.87  ? 2   ALA E N   1 
ATOM   4442  C  CA  . ALA E  1 1   ? 23.791 -15.490  -76.409  1.00 94.70  ? 2   ALA E CA  1 
ATOM   4443  C  C   . ALA E  1 1   ? 22.812 -14.432  -75.821  1.00 90.53  ? 2   ALA E C   1 
ATOM   4444  O  O   . ALA E  1 1   ? 21.658 -14.761  -75.479  1.00 90.13  ? 2   ALA E O   1 
ATOM   4445  C  CB  . ALA E  1 1   ? 23.023 -16.566  -77.232  1.00 97.89  ? 2   ALA E CB  1 
ATOM   4446  N  N   . THR E  1 2   ? 23.247 -13.161  -75.775  1.00 88.01  ? 3   THR E N   1 
ATOM   4447  C  CA  . THR E  1 2   ? 22.575 -12.096  -74.976  1.00 84.07  ? 3   THR E CA  1 
ATOM   4448  C  C   . THR E  1 2   ? 21.116 -11.976  -75.420  1.00 83.43  ? 3   THR E C   1 
ATOM   4449  O  O   . THR E  1 2   ? 20.809 -12.030  -76.616  1.00 85.25  ? 3   THR E O   1 
ATOM   4450  C  CB  . THR E  1 2   ? 23.257 -10.671  -75.102  1.00 82.86  ? 3   THR E CB  1 
ATOM   4451  O  OG1 . THR E  1 2   ? 24.647 -10.810  -75.439  1.00 85.19  ? 3   THR E OG1 1 
ATOM   4452  C  CG2 . THR E  1 2   ? 23.116 -9.837   -73.778  1.00 79.36  ? 3   THR E CG2 1 
ATOM   4453  N  N   . LYS E  1 3   ? 20.230 -11.813  -74.443  1.00 81.24  ? 4   LYS E N   1 
ATOM   4454  C  CA  . LYS E  1 3   ? 18.806 -11.617  -74.697  1.00 80.92  ? 4   LYS E CA  1 
ATOM   4455  C  C   . LYS E  1 3   ? 18.298 -10.411  -73.922  1.00 78.18  ? 4   LYS E C   1 
ATOM   4456  O  O   . LYS E  1 3   ? 18.768 -10.109  -72.831  1.00 76.58  ? 4   LYS E O   1 
ATOM   4457  C  CB  . LYS E  1 3   ? 18.006 -12.845  -74.278  1.00 82.22  ? 4   LYS E CB  1 
ATOM   4458  C  CG  . LYS E  1 3   ? 18.278 -14.104  -75.099  1.00 85.92  ? 4   LYS E CG  1 
ATOM   4459  C  CD  . LYS E  1 3   ? 17.247 -15.204  -74.794  1.00 87.80  ? 4   LYS E CD  1 
ATOM   4460  C  CE  . LYS E  1 3   ? 17.785 -16.606  -75.058  1.00 91.26  ? 4   LYS E CE  1 
ATOM   4461  N  NZ  . LYS E  1 3   ? 17.047 -17.625  -74.235  1.00 92.21  ? 4   LYS E NZ  1 
ATOM   4462  N  N   . ALA E  1 4   ? 17.327 -9.722   -74.501  1.00 78.31  ? 5   ALA E N   1 
ATOM   4463  C  CA  . ALA E  1 4   ? 16.630 -8.620   -73.828  1.00 76.57  ? 5   ALA E CA  1 
ATOM   4464  C  C   . ALA E  1 4   ? 15.105 -8.721   -74.083  1.00 77.63  ? 5   ALA E C   1 
ATOM   4465  O  O   . ALA E  1 4   ? 14.644 -9.472   -74.952  1.00 79.62  ? 5   ALA E O   1 
ATOM   4466  C  CB  . ALA E  1 4   ? 17.193 -7.246   -74.275  1.00 75.80  ? 5   ALA E CB  1 
ATOM   4467  N  N   . VAL E  1 5   ? 14.335 -7.994   -73.282  1.00 76.66  ? 6   VAL E N   1 
ATOM   4468  C  CA  . VAL E  1 5   ? 12.876 -7.980   -73.413  1.00 78.22  ? 6   VAL E CA  1 
ATOM   4469  C  C   . VAL E  1 5   ? 12.355 -6.613   -73.014  1.00 77.62  ? 6   VAL E C   1 
ATOM   4470  O  O   . VAL E  1 5   ? 13.022 -5.876   -72.294  1.00 75.90  ? 6   VAL E O   1 
ATOM   4471  C  CB  . VAL E  1 5   ? 12.174 -9.071   -72.541  1.00 78.93  ? 6   VAL E CB  1 
ATOM   4472  C  CG1 . VAL E  1 5   ? 12.101 -8.634   -71.079  1.00 77.61  ? 6   VAL E CG1 1 
ATOM   4473  C  CG2 . VAL E  1 5   ? 10.770 -9.368   -73.046  1.00 81.51  ? 6   VAL E CG2 1 
ATOM   4474  N  N   . CYS E  1 6   ? 11.165 -6.286   -73.501  1.00 79.59  ? 7   CYS E N   1 
ATOM   4475  C  CA  . CYS E  1 6   ? 10.524 -5.024   -73.189  1.00 80.06  ? 7   CYS E CA  1 
ATOM   4476  C  C   . CYS E  1 6   ? 9.009  -5.157   -73.217  1.00 82.85  ? 7   CYS E C   1 
ATOM   4477  O  O   . CYS E  1 6   ? 8.433  -5.613   -74.199  1.00 85.13  ? 7   CYS E O   1 
ATOM   4478  C  CB  . CYS E  1 6   ? 10.945 -3.944   -74.174  1.00 80.46  ? 7   CYS E CB  1 
ATOM   4479  S  SG  . CYS E  1 6   ? 9.997  -2.399   -73.965  1.00 81.90  ? 7   CYS E SG  1 
ATOM   4480  N  N   . VAL E  1 7   ? 8.365  -4.733   -72.134  1.00 83.26  ? 8   VAL E N   1 
ATOM   4481  C  CA  . VAL E  1 7   ? 6.894  -4.665   -72.065  1.00 86.30  ? 8   VAL E CA  1 
ATOM   4482  C  C   . VAL E  1 7   ? 6.424  -3.242   -72.439  1.00 87.96  ? 8   VAL E C   1 
ATOM   4483  O  O   . VAL E  1 7   ? 6.616  -2.267   -71.676  1.00 87.05  ? 8   VAL E O   1 
ATOM   4484  C  CB  . VAL E  1 7   ? 6.343  -5.081   -70.669  1.00 86.66  ? 8   VAL E CB  1 
ATOM   4485  C  CG1 . VAL E  1 7   ? 4.835  -4.818   -70.555  1.00 90.29  ? 8   VAL E CG1 1 
ATOM   4486  C  CG2 . VAL E  1 7   ? 6.639  -6.558   -70.398  1.00 85.86  ? 8   VAL E CG2 1 
ATOM   4487  N  N   . LEU E  1 8   ? 5.817  -3.163   -73.630  1.00 90.57  ? 9   LEU E N   1 
ATOM   4488  C  CA  . LEU E  1 8   ? 5.223  -1.929   -74.147  1.00 93.17  ? 9   LEU E CA  1 
ATOM   4489  C  C   . LEU E  1 8   ? 3.861  -1.658   -73.501  1.00 96.47  ? 9   LEU E C   1 
ATOM   4490  O  O   . LEU E  1 8   ? 2.972  -2.530   -73.511  1.00 98.67  ? 9   LEU E O   1 
ATOM   4491  C  CB  . LEU E  1 8   ? 5.048  -2.019   -75.658  1.00 95.30  ? 9   LEU E CB  1 
ATOM   4492  C  CG  . LEU E  1 8   ? 6.363  -1.977   -76.444  1.00 93.18  ? 9   LEU E CG  1 
ATOM   4493  C  CD1 . LEU E  1 8   ? 6.183  -2.524   -77.834  1.00 95.33  ? 9   LEU E CD1 1 
ATOM   4494  C  CD2 . LEU E  1 8   ? 6.932  -0.556   -76.501  1.00 92.72  ? 9   LEU E CD2 1 
ATOM   4495  N  N   . LYS E  1 9   ? 3.718  -0.466   -72.917  1.00 97.22  ? 10  LYS E N   1 
ATOM   4496  C  CA  . LYS E  1 9   ? 2.474  -0.049   -72.274  1.00 100.93 ? 10  LYS E CA  1 
ATOM   4497  C  C   . LYS E  1 9   ? 2.278  1.445    -72.431  1.00 103.36 ? 10  LYS E C   1 
ATOM   4498  O  O   . LYS E  1 9   ? 3.225  2.196    -72.664  1.00 101.62 ? 10  LYS E O   1 
ATOM   4499  C  CB  . LYS E  1 9   ? 2.464  -0.394   -70.781  1.00 99.84  ? 10  LYS E CB  1 
ATOM   4500  C  CG  . LYS E  1 9   ? 2.015  -1.828   -70.451  1.00 100.52 ? 10  LYS E CG  1 
ATOM   4501  C  CD  . LYS E  1 9   ? 1.406  -1.914   -69.022  1.00 102.44 ? 10  LYS E CD  1 
ATOM   4502  C  CE  . LYS E  1 9   ? 1.301  -3.371   -68.496  1.00 101.65 ? 10  LYS E CE  1 
ATOM   4503  N  NZ  . LYS E  1 9   ? 0.094  -4.069   -69.019  1.00 105.56 ? 10  LYS E NZ  1 
ATOM   4504  N  N   . GLY E  1 10  ? 1.033  1.877    -72.275  1.00 108.13 ? 11  GLY E N   1 
ATOM   4505  C  CA  . GLY E  1 10  ? 0.694  3.298    -72.420  1.00 111.51 ? 11  GLY E CA  1 
ATOM   4506  C  C   . GLY E  1 10  ? -0.666 3.719    -71.858  1.00 117.01 ? 11  GLY E C   1 
ATOM   4507  O  O   . GLY E  1 10  ? -1.425 2.898    -71.271  1.00 118.33 ? 11  GLY E O   1 
ATOM   4508  N  N   . ASP E  1 11  ? -0.978 5.003    -72.062  1.00 120.64 ? 12  ASP E N   1 
ATOM   4509  C  CA  . ASP E  1 11  ? -2.238 5.611    -71.560  1.00 126.64 ? 12  ASP E CA  1 
ATOM   4510  C  C   . ASP E  1 11  ? -3.536 4.985    -72.138  1.00 131.18 ? 12  ASP E C   1 
ATOM   4511  O  O   . ASP E  1 11  ? -4.566 4.881    -71.438  1.00 135.20 ? 12  ASP E O   1 
ATOM   4512  C  CB  . ASP E  1 11  ? -2.228 7.122    -71.821  1.00 130.06 ? 12  ASP E CB  1 
ATOM   4513  C  CG  . ASP E  1 11  ? -1.587 7.889    -70.687  1.00 129.14 ? 12  ASP E CG  1 
ATOM   4514  O  OD1 . ASP E  1 11  ? -1.961 7.648    -69.524  1.00 130.30 ? 12  ASP E OD1 1 
ATOM   4515  O  OD2 . ASP E  1 11  ? -0.704 8.720    -70.943  1.00 128.32 ? 12  ASP E OD2 1 
ATOM   4516  N  N   . GLY E  1 12  ? -3.458 4.549    -73.398  1.00 130.78 ? 13  GLY E N   1 
ATOM   4517  C  CA  . GLY E  1 12  ? -4.595 3.957    -74.095  1.00 135.15 ? 13  GLY E CA  1 
ATOM   4518  C  C   . GLY E  1 12  ? -4.484 2.441    -74.245  1.00 132.32 ? 13  GLY E C   1 
ATOM   4519  O  O   . GLY E  1 12  ? -3.728 1.777    -73.502  1.00 127.42 ? 13  GLY E O   1 
ATOM   4520  N  N   . PRO E  1 13  ? -5.211 1.879    -75.234  1.00 135.76 ? 14  PRO E N   1 
ATOM   4521  C  CA  . PRO E  1 13  ? -5.398 0.421    -75.379  1.00 134.97 ? 14  PRO E CA  1 
ATOM   4522  C  C   . PRO E  1 13  ? -4.185 -0.308   -75.954  1.00 129.50 ? 14  PRO E C   1 
ATOM   4523  O  O   . PRO E  1 13  ? -4.127 -1.545   -75.889  1.00 128.13 ? 14  PRO E O   1 
ATOM   4524  C  CB  . PRO E  1 13  ? -6.537 0.321    -76.391  1.00 141.44 ? 14  PRO E CB  1 
ATOM   4525  C  CG  . PRO E  1 13  ? -6.319 1.541    -77.303  1.00 142.95 ? 14  PRO E CG  1 
ATOM   4526  C  CD  . PRO E  1 13  ? -5.687 2.616    -76.429  1.00 140.35 ? 14  PRO E CD  1 
ATOM   4527  N  N   . VAL E  1 14  ? -3.247 0.458    -76.522  1.00 126.98 ? 15  VAL E N   1 
ATOM   4528  C  CA  . VAL E  1 14  ? -2.031 -0.102   -77.116  1.00 122.19 ? 15  VAL E CA  1 
ATOM   4529  C  C   . VAL E  1 14  ? -1.131 -0.725   -76.037  1.00 116.60 ? 15  VAL E C   1 
ATOM   4530  O  O   . VAL E  1 14  ? -0.713 -0.058   -75.062  1.00 114.34 ? 15  VAL E O   1 
ATOM   4531  C  CB  . VAL E  1 14  ? -1.201 0.957    -77.910  1.00 121.29 ? 15  VAL E CB  1 
ATOM   4532  C  CG1 . VAL E  1 14  ? -0.041 0.286    -78.651  1.00 117.36 ? 15  VAL E CG1 1 
ATOM   4533  C  CG2 . VAL E  1 14  ? -2.082 1.699    -78.900  1.00 127.27 ? 15  VAL E CG2 1 
ATOM   4534  N  N   . GLN E  1 15  ? -0.864 -2.015   -76.233  1.00 114.83 ? 16  GLN E N   1 
ATOM   4535  C  CA  . GLN E  1 15  ? 0.038  -2.769   -75.373  1.00 110.15 ? 16  GLN E CA  1 
ATOM   4536  C  C   . GLN E  1 15  ? 0.633  -3.977   -76.093  1.00 108.48 ? 16  GLN E C   1 
ATOM   4537  O  O   . GLN E  1 15  ? 0.109  -4.455   -77.100  1.00 111.47 ? 16  GLN E O   1 
ATOM   4538  C  CB  . GLN E  1 15  ? -0.659 -3.218   -74.081  1.00 111.17 ? 16  GLN E CB  1 
ATOM   4539  C  CG  . GLN E  1 15  ? -1.955 -3.999   -74.291  1.00 116.31 ? 16  GLN E CG  1 
ATOM   4540  C  CD  . GLN E  1 15  ? -2.492 -4.618   -73.003  1.00 117.60 ? 16  GLN E CD  1 
ATOM   4541  O  OE1 . GLN E  1 15  ? -3.212 -5.624   -73.044  1.00 120.73 ? 16  GLN E OE1 1 
ATOM   4542  N  NE2 . GLN E  1 15  ? -2.141 -4.023   -71.849  1.00 115.47 ? 16  GLN E NE2 1 
ATOM   4543  N  N   . GLY E  1 16  ? 1.748  -4.453   -75.550  1.00 104.10 ? 17  GLY E N   1 
ATOM   4544  C  CA  . GLY E  1 16  ? 2.483  -5.555   -76.152  1.00 102.59 ? 17  GLY E CA  1 
ATOM   4545  C  C   . GLY E  1 16  ? 3.800  -5.917   -75.467  1.00 97.85  ? 17  GLY E C   1 
ATOM   4546  O  O   . GLY E  1 16  ? 4.257  -5.236   -74.534  1.00 95.26  ? 17  GLY E O   1 
ATOM   4547  N  N   . ILE E  1 17  ? 4.394  -7.002   -75.972  1.00 97.15  ? 18  ILE E N   1 
ATOM   4548  C  CA  . ILE E  1 17  ? 5.678  -7.540   -75.518  1.00 93.35  ? 18  ILE E CA  1 
ATOM   4549  C  C   . ILE E  1 17  ? 6.603  -7.688   -76.722  1.00 92.95  ? 18  ILE E C   1 
ATOM   4550  O  O   . ILE E  1 17  ? 6.225  -8.297   -77.720  1.00 95.94  ? 18  ILE E O   1 
ATOM   4551  C  CB  . ILE E  1 17  ? 5.495  -8.945   -74.889  1.00 93.88  ? 18  ILE E CB  1 
ATOM   4552  C  CG1 . ILE E  1 17  ? 5.008  -8.834   -73.447  1.00 93.49  ? 18  ILE E CG1 1 
ATOM   4553  C  CG2 . ILE E  1 17  ? 6.789  -9.775   -74.963  1.00 91.57  ? 18  ILE E CG2 1 
ATOM   4554  C  CD1 . ILE E  1 17  ? 5.064  -10.151  -72.704  1.00 93.74  ? 18  ILE E CD1 1 
ATOM   4555  N  N   . ILE E  1 18  ? 7.817  -7.161   -76.619  1.00 89.95  ? 19  ILE E N   1 
ATOM   4556  C  CA  . ILE E  1 18  ? 8.837  -7.303   -77.682  1.00 89.75  ? 19  ILE E CA  1 
ATOM   4557  C  C   . ILE E  1 18  ? 10.135 -7.920   -77.161  1.00 87.00  ? 19  ILE E C   1 
ATOM   4558  O  O   . ILE E  1 18  ? 10.719 -7.452   -76.200  1.00 84.51  ? 19  ILE E O   1 
ATOM   4559  C  CB  . ILE E  1 18  ? 9.192  -5.939   -78.320  1.00 89.75  ? 19  ILE E CB  1 
ATOM   4560  C  CG1 . ILE E  1 18  ? 7.993  -5.374   -79.084  1.00 93.44  ? 19  ILE E CG1 1 
ATOM   4561  C  CG2 . ILE E  1 18  ? 10.385 -6.068   -79.256  1.00 89.51  ? 19  ILE E CG2 1 
ATOM   4562  C  CD1 . ILE E  1 18  ? 7.644  -6.156   -80.338  1.00 97.03  ? 19  ILE E CD1 1 
ATOM   4563  N  N   . ASN E  1 19  ? 10.601 -8.953   -77.832  1.00 88.22  ? 20  ASN E N   1 
ATOM   4564  C  CA  . ASN E  1 19  ? 11.846 -9.614   -77.471  1.00 86.62  ? 20  ASN E CA  1 
ATOM   4565  C  C   . ASN E  1 19  ? 13.039 -9.190   -78.324  1.00 86.54  ? 20  ASN E C   1 
ATOM   4566  O  O   . ASN E  1 19  ? 12.896 -8.843   -79.501  1.00 88.79  ? 20  ASN E O   1 
ATOM   4567  C  CB  . ASN E  1 19  ? 11.693 -11.113  -77.617  1.00 88.72  ? 20  ASN E CB  1 
ATOM   4568  C  CG  . ASN E  1 19  ? 10.658 -11.659  -76.714  1.00 89.43  ? 20  ASN E CG  1 
ATOM   4569  O  OD1 . ASN E  1 19  ? 9.547  -11.954  -77.147  1.00 92.58  ? 20  ASN E OD1 1 
ATOM   4570  N  ND2 . ASN E  1 19  ? 10.993 -11.785  -75.436  1.00 87.19  ? 20  ASN E ND2 1 
ATOM   4571  N  N   . PHE E  1 20  ? 14.219 -9.263   -77.715  1.00 84.46  ? 21  PHE E N   1 
ATOM   4572  C  CA  . PHE E  1 20  ? 15.488 -9.052   -78.411  1.00 84.66  ? 21  PHE E CA  1 
ATOM   4573  C  C   . PHE E  1 20  ? 16.393 -10.277  -78.227  1.00 85.24  ? 21  PHE E C   1 
ATOM   4574  O  O   . PHE E  1 20  ? 16.353 -10.962  -77.202  1.00 84.31  ? 21  PHE E O   1 
ATOM   4575  C  CB  . PHE E  1 20  ? 16.198 -7.811   -77.889  1.00 82.29  ? 21  PHE E CB  1 
ATOM   4576  C  CG  . PHE E  1 20  ? 15.416 -6.542   -78.059  1.00 82.27  ? 21  PHE E CG  1 
ATOM   4577  C  CD1 . PHE E  1 20  ? 14.384 -6.217   -77.183  1.00 81.39  ? 21  PHE E CD1 1 
ATOM   4578  C  CD2 . PHE E  1 20  ? 15.730 -5.656   -79.067  1.00 83.59  ? 21  PHE E CD2 1 
ATOM   4579  C  CE1 . PHE E  1 20  ? 13.677 -5.040   -77.320  1.00 81.76  ? 21  PHE E CE1 1 
ATOM   4580  C  CE2 . PHE E  1 20  ? 15.028 -4.475   -79.203  1.00 83.95  ? 21  PHE E CE2 1 
ATOM   4581  C  CZ  . PHE E  1 20  ? 14.002 -4.168   -78.327  1.00 83.18  ? 21  PHE E CZ  1 
ATOM   4582  N  N   . GLU E  1 21  ? 17.198 -10.557  -79.239  1.00 87.45  ? 22  GLU E N   1 
ATOM   4583  C  CA  . GLU E  1 21  ? 18.173 -11.636  -79.163  1.00 88.72  ? 22  GLU E CA  1 
ATOM   4584  C  C   . GLU E  1 21  ? 19.377 -11.417  -80.105  1.00 90.67  ? 22  GLU E C   1 
ATOM   4585  O  O   . GLU E  1 21  ? 19.265 -11.488  -81.346  1.00 93.58  ? 22  GLU E O   1 
ATOM   4586  C  CB  . GLU E  1 21  ? 17.521 -12.990  -79.444  1.00 91.46  ? 22  GLU E CB  1 
ATOM   4587  C  CG  . GLU E  1 21  ? 18.519 -14.165  -79.309  1.00 93.85  ? 22  GLU E CG  1 
ATOM   4588  C  CD  . GLU E  1 21  ? 17.846 -15.556  -79.297  1.00 97.07  ? 22  GLU E CD  1 
ATOM   4589  O  OE1 . GLU E  1 21  ? 16.686 -15.682  -79.747  1.00 98.67  ? 22  GLU E OE1 1 
ATOM   4590  O  OE2 . GLU E  1 21  ? 18.474 -16.534  -78.831  1.00 98.40  ? 22  GLU E OE2 1 
ATOM   4591  N  N   . GLN E  1 22  ? 20.528 -11.162  -79.487  1.00 89.40  ? 23  GLN E N   1 
ATOM   4592  C  CA  . GLN E  1 22  ? 21.791 -10.988  -80.198  1.00 91.45  ? 23  GLN E CA  1 
ATOM   4593  C  C   . GLN E  1 22  ? 22.650 -12.202  -79.880  1.00 93.26  ? 23  GLN E C   1 
ATOM   4594  O  O   . GLN E  1 22  ? 23.126 -12.366  -78.757  1.00 91.45  ? 23  GLN E O   1 
ATOM   4595  C  CB  . GLN E  1 22  ? 22.481 -9.701   -79.746  1.00 89.31  ? 23  GLN E CB  1 
ATOM   4596  C  CG  . GLN E  1 22  ? 23.716 -9.330   -80.546  1.00 91.72  ? 23  GLN E CG  1 
ATOM   4597  C  CD  . GLN E  1 22  ? 24.388 -8.062   -80.032  1.00 90.18  ? 23  GLN E CD  1 
ATOM   4598  O  OE1 . GLN E  1 22  ? 24.564 -7.877   -78.817  1.00 87.82  ? 23  GLN E OE1 1 
ATOM   4599  N  NE2 . GLN E  1 22  ? 24.779 -7.185   -80.954  1.00 92.14  ? 23  GLN E NE2 1 
ATOM   4600  N  N   . LYS E  1 23  ? 22.830 -13.067  -80.869  1.00 97.39  ? 24  LYS E N   1 
ATOM   4601  C  CA  . LYS E  1 23  ? 23.610 -14.303  -80.672  1.00 100.16 ? 24  LYS E CA  1 
ATOM   4602  C  C   . LYS E  1 23  ? 25.095 -14.050  -80.433  1.00 100.81 ? 24  LYS E C   1 
ATOM   4603  O  O   . LYS E  1 23  ? 25.730 -14.786  -79.673  1.00 101.43 ? 24  LYS E O   1 
ATOM   4604  C  CB  . LYS E  1 23  ? 23.476 -15.239  -81.874  1.00 105.17 ? 24  LYS E CB  1 
ATOM   4605  C  CG  . LYS E  1 23  ? 22.063 -15.787  -82.082  1.00 105.98 ? 24  LYS E CG  1 
ATOM   4606  C  CD  . LYS E  1 23  ? 22.090 -17.170  -82.755  1.00 111.37 ? 24  LYS E CD  1 
ATOM   4607  C  CE  . LYS E  1 23  ? 20.787 -17.448  -83.508  1.00 113.42 ? 24  LYS E CE  1 
ATOM   4608  N  NZ  . LYS E  1 23  ? 20.906 -18.645  -84.428  1.00 119.35 ? 24  LYS E NZ  1 
ATOM   4609  N  N   . GLU E  1 24  ? 25.637 -13.026  -81.100  1.00 101.30 ? 25  GLU E N   1 
ATOM   4610  C  CA  . GLU E  1 24  ? 27.068 -12.697  -81.007  1.00 102.76 ? 25  GLU E CA  1 
ATOM   4611  C  C   . GLU E  1 24  ? 27.324 -11.206  -80.886  1.00 100.44 ? 25  GLU E C   1 
ATOM   4612  O  O   . GLU E  1 24  ? 26.735 -10.399  -81.610  1.00 100.26 ? 25  GLU E O   1 
ATOM   4613  C  CB  . GLU E  1 24  ? 27.797 -13.253  -82.209  1.00 108.28 ? 25  GLU E CB  1 
ATOM   4614  C  CG  . GLU E  1 24  ? 27.496 -14.741  -82.353  1.00 111.50 ? 25  GLU E CG  1 
ATOM   4615  C  CD  . GLU E  1 24  ? 28.381 -15.461  -83.312  1.00 118.23 ? 25  GLU E CD  1 
ATOM   4616  O  OE1 . GLU E  1 24  ? 28.555 -14.970  -84.463  1.00 121.29 ? 25  GLU E OE1 1 
ATOM   4617  O  OE2 . GLU E  1 24  ? 28.879 -16.538  -82.906  1.00 120.78 ? 25  GLU E OE2 1 
ATOM   4618  N  N   . SER E  1 25  ? 28.219 -10.863  -79.967  1.00 99.30  ? 26  SER E N   1 
ATOM   4619  C  CA  . SER E  1 25  ? 28.488 -9.468   -79.584  1.00 97.30  ? 26  SER E CA  1 
ATOM   4620  C  C   . SER E  1 25  ? 28.655 -8.517   -80.776  1.00 99.38  ? 26  SER E C   1 
ATOM   4621  O  O   . SER E  1 25  ? 28.212 -7.357   -80.745  1.00 97.38  ? 26  SER E O   1 
ATOM   4622  C  CB  . SER E  1 25  ? 29.746 -9.402   -78.691  1.00 97.96  ? 26  SER E CB  1 
ATOM   4623  O  OG  . SER E  1 25  ? 30.816 -10.185  -79.217  1.00 102.93 ? 26  SER E OG  1 
ATOM   4624  N  N   . ASN E  1 26  ? 29.311 -9.028   -81.814  1.00 103.94 ? 27  ASN E N   1 
ATOM   4625  C  CA  . ASN E  1 26  ? 29.578 -8.269   -83.040  1.00 107.15 ? 27  ASN E CA  1 
ATOM   4626  C  C   . ASN E  1 26  ? 28.465 -8.395   -84.090  1.00 108.04 ? 27  ASN E C   1 
ATOM   4627  O  O   . ASN E  1 26  ? 28.547 -7.790   -85.170  1.00 111.02 ? 27  ASN E O   1 
ATOM   4628  C  CB  . ASN E  1 26  ? 30.920 -8.702   -83.660  1.00 112.43 ? 27  ASN E CB  1 
ATOM   4629  C  CG  . ASN E  1 26  ? 30.881 -10.131  -84.241  1.00 115.87 ? 27  ASN E CG  1 
ATOM   4630  O  OD1 . ASN E  1 26  ? 30.307 -11.063  -83.651  1.00 113.81 ? 27  ASN E OD1 1 
ATOM   4631  N  ND2 . ASN E  1 26  ? 31.504 -10.297  -85.397  1.00 121.06 ? 27  ASN E ND2 1 
ATOM   4632  N  N   . GLY E  1 27  ? 27.425 -9.164   -83.761  1.00 105.90 ? 28  GLY E N   1 
ATOM   4633  C  CA  . GLY E  1 27  ? 26.423 -9.592   -84.747  1.00 107.58 ? 28  GLY E CA  1 
ATOM   4634  C  C   . GLY E  1 27  ? 25.087 -8.853   -84.694  1.00 104.56 ? 28  GLY E C   1 
ATOM   4635  O  O   . GLY E  1 27  ? 24.907 -7.908   -83.909  1.00 101.16 ? 28  GLY E O   1 
ATOM   4636  N  N   . PRO E  1 28  ? 24.133 -9.278   -85.544  1.00 106.39 ? 29  PRO E N   1 
ATOM   4637  C  CA  . PRO E  1 28  ? 22.856 -8.586   -85.637  1.00 104.52 ? 29  PRO E CA  1 
ATOM   4638  C  C   . PRO E  1 28  ? 21.910 -9.006   -84.516  1.00 100.66 ? 29  PRO E C   1 
ATOM   4639  O  O   . PRO E  1 28  ? 22.066 -10.085  -83.907  1.00 100.20 ? 29  PRO E O   1 
ATOM   4640  C  CB  . PRO E  1 28  ? 22.307 -9.061   -86.987  1.00 108.96 ? 29  PRO E CB  1 
ATOM   4641  C  CG  . PRO E  1 28  ? 22.806 -10.470  -87.099  1.00 111.37 ? 29  PRO E CG  1 
ATOM   4642  C  CD  . PRO E  1 28  ? 24.170 -10.469  -86.419  1.00 110.74 ? 29  PRO E CD  1 
ATOM   4643  N  N   . VAL E  1 29  ? 20.929 -8.142   -84.277  1.00 98.41  ? 30  VAL E N   1 
ATOM   4644  C  CA  . VAL E  1 29  ? 19.942 -8.335   -83.220  1.00 95.02  ? 30  VAL E CA  1 
ATOM   4645  C  C   . VAL E  1 29  ? 18.585 -8.657   -83.823  1.00 96.60  ? 30  VAL E C   1 
ATOM   4646  O  O   . VAL E  1 29  ? 17.990 -7.824   -84.520  1.00 97.82  ? 30  VAL E O   1 
ATOM   4647  C  CB  . VAL E  1 29  ? 19.768 -7.064   -82.370  1.00 91.66  ? 30  VAL E CB  1 
ATOM   4648  C  CG1 . VAL E  1 29  ? 18.642 -7.271   -81.343  1.00 88.81  ? 30  VAL E CG1 1 
ATOM   4649  C  CG2 . VAL E  1 29  ? 21.097 -6.686   -81.699  1.00 90.21  ? 30  VAL E CG2 1 
ATOM   4650  N  N   . LYS E  1 30  ? 18.089 -9.856   -83.540  1.00 97.00  ? 31  LYS E N   1 
ATOM   4651  C  CA  . LYS E  1 30  ? 16.719 -10.198  -83.912  1.00 98.60  ? 31  LYS E CA  1 
ATOM   4652  C  C   . LYS E  1 30  ? 15.750 -9.552   -82.946  1.00 95.39  ? 31  LYS E C   1 
ATOM   4653  O  O   . LYS E  1 30  ? 15.930 -9.628   -81.742  1.00 92.57  ? 31  LYS E O   1 
ATOM   4654  C  CB  . LYS E  1 30  ? 16.508 -11.712  -83.941  1.00 100.84 ? 31  LYS E CB  1 
ATOM   4655  C  CG  . LYS E  1 30  ? 17.220 -12.356  -85.129  1.00 105.67 ? 31  LYS E CG  1 
ATOM   4656  C  CD  . LYS E  1 30  ? 16.729 -13.766  -85.412  1.00 109.56 ? 31  LYS E CD  1 
ATOM   4657  C  CE  . LYS E  1 30  ? 17.445 -14.360  -86.627  1.00 114.65 ? 31  LYS E CE  1 
ATOM   4658  N  NZ  . LYS E  1 30  ? 16.846 -15.700  -87.027  1.00 119.19 ? 31  LYS E NZ  1 
ATOM   4659  N  N   . VAL E  1 31  ? 14.730 -8.904   -83.484  1.00 96.63  ? 32  VAL E N   1 
ATOM   4660  C  CA  . VAL E  1 31  ? 13.699 -8.268   -82.672  1.00 94.67  ? 32  VAL E CA  1 
ATOM   4661  C  C   . VAL E  1 31  ? 12.372 -8.906   -83.034  1.00 97.47  ? 32  VAL E C   1 
ATOM   4662  O  O   . VAL E  1 31  ? 11.977 -8.895   -84.208  1.00 101.28 ? 32  VAL E O   1 
ATOM   4663  C  CB  . VAL E  1 31  ? 13.627 -6.756   -82.952  1.00 94.32  ? 32  VAL E CB  1 
ATOM   4664  C  CG1 . VAL E  1 31  ? 12.598 -6.085   -82.040  1.00 92.49  ? 32  VAL E CG1 1 
ATOM   4665  C  CG2 . VAL E  1 31  ? 15.009 -6.141   -82.808  1.00 92.73  ? 32  VAL E CG2 1 
ATOM   4666  N  N   . TRP E  1 32  ? 11.683 -9.477   -82.057  1.00 96.25  ? 33  TRP E N   1 
ATOM   4667  C  CA  . TRP E  1 32  ? 10.375 -10.057  -82.360  1.00 99.52  ? 33  TRP E CA  1 
ATOM   4668  C  C   . TRP E  1 32  ? 9.400  -10.006  -81.196  1.00 98.19  ? 33  TRP E C   1 
ATOM   4669  O  O   . TRP E  1 32  ? 9.788  -9.927   -80.038  1.00 95.19  ? 33  TRP E O   1 
ATOM   4670  C  CB  . TRP E  1 32  ? 10.515 -11.499  -82.858  1.00 102.40 ? 33  TRP E CB  1 
ATOM   4671  C  CG  . TRP E  1 32  ? 10.546 -12.519  -81.770  1.00 101.24 ? 33  TRP E CG  1 
ATOM   4672  C  CD1 . TRP E  1 32  ? 9.513  -13.313  -81.342  1.00 103.19 ? 33  TRP E CD1 1 
ATOM   4673  C  CD2 . TRP E  1 32  ? 11.669 -12.852  -80.964  1.00 98.58  ? 33  TRP E CD2 1 
ATOM   4674  N  NE1 . TRP E  1 32  ? 9.930  -14.127  -80.316  1.00 101.43 ? 33  TRP E NE1 1 
ATOM   4675  C  CE2 . TRP E  1 32  ? 11.252 -13.874  -80.062  1.00 98.77  ? 33  TRP E CE2 1 
ATOM   4676  C  CE3 . TRP E  1 32  ? 13.000 -12.391  -80.912  1.00 96.68  ? 33  TRP E CE3 1 
ATOM   4677  C  CZ2 . TRP E  1 32  ? 12.127 -14.452  -79.108  1.00 97.11  ? 33  TRP E CZ2 1 
ATOM   4678  C  CZ3 . TRP E  1 32  ? 13.882 -12.967  -79.957  1.00 94.94  ? 33  TRP E CZ3 1 
ATOM   4679  C  CH2 . TRP E  1 32  ? 13.430 -13.991  -79.070  1.00 95.12  ? 33  TRP E CH2 1 
ATOM   4680  N  N   . GLY E  1 33  ? 8.121  -10.083  -81.526  1.00 101.19 ? 34  GLY E N   1 
ATOM   4681  C  CA  . GLY E  1 33  ? 7.075  -10.062  -80.519  1.00 100.96 ? 34  GLY E CA  1 
ATOM   4682  C  C   . GLY E  1 33  ? 5.727  -9.705   -81.112  1.00 104.94 ? 34  GLY E C   1 
ATOM   4683  O  O   . GLY E  1 33  ? 5.528  -9.778   -82.336  1.00 108.43 ? 34  GLY E O   1 
ATOM   4684  N  N   . SER E  1 34  ? 4.804  -9.310   -80.240  1.00 104.83 ? 35  SER E N   1 
ATOM   4685  C  CA  . SER E  1 34  ? 3.450  -9.018   -80.655  1.00 109.03 ? 35  SER E CA  1 
ATOM   4686  C  C   . SER E  1 34  ? 2.879  -7.807   -79.932  1.00 108.27 ? 35  SER E C   1 
ATOM   4687  O  O   . SER E  1 34  ? 2.723  -7.839   -78.709  1.00 106.38 ? 35  SER E O   1 
ATOM   4688  C  CB  . SER E  1 34  ? 2.574  -10.241  -80.406  1.00 112.08 ? 35  SER E CB  1 
ATOM   4689  O  OG  . SER E  1 34  ? 1.324  -10.063  -81.035  1.00 117.32 ? 35  SER E OG  1 
ATOM   4690  N  N   . ILE E  1 35  ? 2.566  -6.758   -80.699  1.00 110.26 ? 36  ILE E N   1 
ATOM   4691  C  CA  . ILE E  1 35  ? 1.869  -5.572   -80.175  1.00 111.05 ? 36  ILE E CA  1 
ATOM   4692  C  C   . ILE E  1 35  ? 0.416  -5.577   -80.633  1.00 116.79 ? 36  ILE E C   1 
ATOM   4693  O  O   . ILE E  1 35  ? 0.132  -5.934   -81.774  1.00 120.20 ? 36  ILE E O   1 
ATOM   4694  C  CB  . ILE E  1 35  ? 2.483  -4.249   -80.673  1.00 110.14 ? 36  ILE E CB  1 
ATOM   4695  C  CG1 . ILE E  1 35  ? 3.978  -4.222   -80.425  1.00 105.44 ? 36  ILE E CG1 1 
ATOM   4696  C  CG2 . ILE E  1 35  ? 1.847  -3.035   -79.961  1.00 110.58 ? 36  ILE E CG2 1 
ATOM   4697  C  CD1 . ILE E  1 35  ? 4.619  -2.972   -80.982  1.00 105.33 ? 36  ILE E CD1 1 
ATOM   4698  N  N   . LYS E  1 36  ? -0.488 -5.139   -79.750  1.00 118.28 ? 37  LYS E N   1 
ATOM   4699  C  CA  . LYS E  1 36  ? -1.932 -5.104   -80.050  1.00 124.16 ? 37  LYS E CA  1 
ATOM   4700  C  C   . LYS E  1 36  ? -2.644 -3.819   -79.586  1.00 126.17 ? 37  LYS E C   1 
ATOM   4701  O  O   . LYS E  1 36  ? -2.074 -2.995   -78.852  1.00 122.76 ? 37  LYS E O   1 
ATOM   4702  C  CB  . LYS E  1 36  ? -2.631 -6.342   -79.473  1.00 125.94 ? 37  LYS E CB  1 
ATOM   4703  C  CG  . LYS E  1 36  ? -2.509 -6.512   -77.982  1.00 123.15 ? 37  LYS E CG  1 
ATOM   4704  C  CD  . LYS E  1 36  ? -3.614 -7.424   -77.471  1.00 127.58 ? 37  LYS E CD  1 
ATOM   4705  C  CE  . LYS E  1 36  ? -3.473 -7.727   -75.979  1.00 125.16 ? 37  LYS E CE  1 
ATOM   4706  N  NZ  . LYS E  1 36  ? -4.703 -8.381   -75.439  1.00 129.89 ? 37  LYS E NZ  1 
ATOM   4707  N  N   . GLY E  1 37  ? -3.894 -3.668   -80.042  1.00 132.25 ? 38  GLY E N   1 
ATOM   4708  C  CA  . GLY E  1 37  ? -4.693 -2.448   -79.809  1.00 135.69 ? 38  GLY E CA  1 
ATOM   4709  C  C   . GLY E  1 37  ? -4.338 -1.328   -80.776  1.00 136.63 ? 38  GLY E C   1 
ATOM   4710  O  O   . GLY E  1 37  ? -4.614 -0.151   -80.512  1.00 138.16 ? 38  GLY E O   1 
ATOM   4711  N  N   . LEU E  1 38  ? -3.703 -1.703   -81.889  1.00 136.06 ? 39  LEU E N   1 
ATOM   4712  C  CA  . LEU E  1 38  ? -3.132 -0.735   -82.852  1.00 136.59 ? 39  LEU E CA  1 
ATOM   4713  C  C   . LEU E  1 38  ? -4.116 -0.424   -83.970  1.00 143.50 ? 39  LEU E C   1 
ATOM   4714  O  O   . LEU E  1 38  ? -4.854 -1.318   -84.432  1.00 146.95 ? 39  LEU E O   1 
ATOM   4715  C  CB  . LEU E  1 38  ? -1.801 -1.239   -83.471  1.00 132.40 ? 39  LEU E CB  1 
ATOM   4716  C  CG  . LEU E  1 38  ? -0.520 -0.996   -82.665  1.00 125.86 ? 39  LEU E CG  1 
ATOM   4717  C  CD1 . LEU E  1 38  ? 0.598  -1.910   -83.190  1.00 122.51 ? 39  LEU E CD1 1 
ATOM   4718  C  CD2 . LEU E  1 38  ? -0.115 0.488    -82.700  1.00 125.68 ? 39  LEU E CD2 1 
ATOM   4719  N  N   . THR E  1 39  ? -4.109 0.852    -84.385  1.00 145.73 ? 40  THR E N   1 
ATOM   4720  C  CA  . THR E  1 39  ? -4.906 1.316    -85.535  1.00 152.56 ? 40  THR E CA  1 
ATOM   4721  C  C   . THR E  1 39  ? -4.341 0.626    -86.788  1.00 152.84 ? 40  THR E C   1 
ATOM   4722  O  O   . THR E  1 39  ? -3.121 0.562    -86.974  1.00 148.33 ? 40  THR E O   1 
ATOM   4723  C  CB  . THR E  1 39  ? -4.893 2.878    -85.716  1.00 154.97 ? 40  THR E CB  1 
ATOM   4724  O  OG1 . THR E  1 39  ? -4.047 3.235    -86.818  1.00 155.14 ? 40  THR E OG1 1 
ATOM   4725  C  CG2 . THR E  1 39  ? -4.445 3.633    -84.423  1.00 150.75 ? 40  THR E CG2 1 
ATOM   4726  N  N   . GLU E  1 40  ? -5.214 0.076    -87.627  1.00 158.69 ? 41  GLU E N   1 
ATOM   4727  C  CA  . GLU E  1 40  ? -4.756 -0.745   -88.765  1.00 159.59 ? 41  GLU E CA  1 
ATOM   4728  C  C   . GLU E  1 40  ? -3.764 0.051    -89.609  1.00 158.69 ? 41  GLU E C   1 
ATOM   4729  O  O   . GLU E  1 40  ? -3.960 1.256    -89.876  1.00 161.45 ? 41  GLU E O   1 
ATOM   4730  C  CB  . GLU E  1 40  ? -5.921 -1.213   -89.658  1.00 167.45 ? 41  GLU E CB  1 
ATOM   4731  C  CG  . GLU E  1 40  ? -5.454 -2.010   -90.916  1.00 169.56 ? 41  GLU E CG  1 
ATOM   4732  C  CD  . GLU E  1 40  ? -6.607 -2.358   -91.884  1.00 178.52 ? 41  GLU E CD  1 
ATOM   4733  O  OE1 . GLU E  1 40  ? -7.369 -1.420   -92.237  1.00 183.75 ? 41  GLU E OE1 1 
ATOM   4734  O  OE2 . GLU E  1 40  ? -6.739 -3.553   -92.291  1.00 180.12 ? 41  GLU E OE2 1 
ATOM   4735  N  N   . GLY E  1 41  ? -2.700 -0.637   -90.009  1.00 155.21 ? 42  GLY E N   1 
ATOM   4736  C  CA  . GLY E  1 41  ? -1.695 -0.056   -90.895  1.00 155.02 ? 42  GLY E CA  1 
ATOM   4737  C  C   . GLY E  1 41  ? -0.299 0.083    -90.272  1.00 147.93 ? 42  GLY E C   1 
ATOM   4738  O  O   . GLY E  1 41  ? 0.060  -0.572   -89.264  1.00 142.49 ? 42  GLY E O   1 
ATOM   4739  N  N   . LEU E  1 42  ? 0.485  0.964    -90.894  1.00 148.29 ? 43  LEU E N   1 
ATOM   4740  C  CA  . LEU E  1 42  ? 1.889  1.170    -90.512  1.00 142.56 ? 43  LEU E CA  1 
ATOM   4741  C  C   . LEU E  1 42  ? 2.027  2.007    -89.247  1.00 138.71 ? 43  LEU E C   1 
ATOM   4742  O  O   . LEU E  1 42  ? 1.260  2.960    -89.007  1.00 141.66 ? 43  LEU E O   1 
ATOM   4743  C  CB  . LEU E  1 42  ? 2.686  1.863    -91.630  1.00 144.96 ? 43  LEU E CB  1 
ATOM   4744  C  CG  . LEU E  1 42  ? 3.091  0.969    -92.820  1.00 147.33 ? 43  LEU E CG  1 
ATOM   4745  C  CD1 . LEU E  1 42  ? 2.323  1.326    -94.100  1.00 155.01 ? 43  LEU E CD1 1 
ATOM   4746  C  CD2 . LEU E  1 42  ? 4.600  1.086    -93.075  1.00 144.43 ? 43  LEU E CD2 1 
ATOM   4747  N  N   . HIS E  1 43  ? 3.026  1.647    -88.450  1.00 132.67 ? 44  HIS E N   1 
ATOM   4748  C  CA  . HIS E  1 43  ? 3.345  2.389    -87.233  1.00 128.83 ? 44  HIS E CA  1 
ATOM   4749  C  C   . HIS E  1 43  ? 4.844  2.535    -87.059  1.00 124.38 ? 44  HIS E C   1 
ATOM   4750  O  O   . HIS E  1 43  ? 5.603  1.558    -87.224  1.00 121.66 ? 44  HIS E O   1 
ATOM   4751  C  CB  . HIS E  1 43  ? 2.738  1.717    -85.994  1.00 126.11 ? 44  HIS E CB  1 
ATOM   4752  C  CG  . HIS E  1 43  ? 1.253  1.855    -85.913  1.00 130.68 ? 44  HIS E CG  1 
ATOM   4753  N  ND1 . HIS E  1 43  ? 0.638  2.997    -85.437  1.00 133.06 ? 44  HIS E ND1 1 
ATOM   4754  C  CD2 . HIS E  1 43  ? 0.260  1.007    -86.278  1.00 134.11 ? 44  HIS E CD2 1 
ATOM   4755  C  CE1 . HIS E  1 43  ? -0.675 2.836    -85.492  1.00 137.71 ? 44  HIS E CE1 1 
ATOM   4756  N  NE2 . HIS E  1 43  ? -0.929 1.639    -85.999  1.00 138.48 ? 44  HIS E NE2 1 
ATOM   4757  N  N   . GLY E  1 44  ? 5.238  3.766    -86.709  1.00 124.01 ? 45  GLY E N   1 
ATOM   4758  C  CA  . GLY E  1 44  ? 6.626  4.087    -86.367  1.00 120.27 ? 45  GLY E CA  1 
ATOM   4759  C  C   . GLY E  1 44  ? 7.097  3.305    -85.130  1.00 114.63 ? 45  GLY E C   1 
ATOM   4760  O  O   . GLY E  1 44  ? 6.305  3.021    -84.211  1.00 113.61 ? 45  GLY E O   1 
ATOM   4761  N  N   . PHE E  1 45  ? 8.385  2.952    -85.113  1.00 111.40 ? 46  PHE E N   1 
ATOM   4762  C  CA  . PHE E  1 45  ? 8.898  1.959    -84.166  1.00 106.53 ? 46  PHE E CA  1 
ATOM   4763  C  C   . PHE E  1 45  ? 10.359 2.197    -83.903  1.00 103.55 ? 46  PHE E C   1 
ATOM   4764  O  O   . PHE E  1 45  ? 11.212 1.770    -84.666  1.00 103.82 ? 46  PHE E O   1 
ATOM   4765  C  CB  . PHE E  1 45  ? 8.700  0.566    -84.748  1.00 107.04 ? 46  PHE E CB  1 
ATOM   4766  C  CG  . PHE E  1 45  ? 8.949  -0.533   -83.789  1.00 103.12 ? 46  PHE E CG  1 
ATOM   4767  C  CD1 . PHE E  1 45  ? 8.318  -0.546   -82.559  1.00 101.24 ? 46  PHE E CD1 1 
ATOM   4768  C  CD2 . PHE E  1 45  ? 9.786  -1.596   -84.139  1.00 102.09 ? 46  PHE E CD2 1 
ATOM   4769  C  CE1 . PHE E  1 45  ? 8.532  -1.599   -81.676  1.00 98.44  ? 46  PHE E CE1 1 
ATOM   4770  C  CE2 . PHE E  1 45  ? 10.009 -2.661   -83.265  1.00 99.20  ? 46  PHE E CE2 1 
ATOM   4771  C  CZ  . PHE E  1 45  ? 9.386  -2.669   -82.029  1.00 97.37  ? 46  PHE E CZ  1 
ATOM   4772  N  N   . HIS E  1 46  ? 10.642 2.892    -82.813  1.00 101.30 ? 47  HIS E N   1 
ATOM   4773  C  CA  . HIS E  1 46  ? 12.004 3.371    -82.534  1.00 99.39  ? 47  HIS E CA  1 
ATOM   4774  C  C   . HIS E  1 46  ? 12.486 3.152    -81.091  1.00 95.26  ? 47  HIS E C   1 
ATOM   4775  O  O   . HIS E  1 46  ? 11.687 3.102    -80.135  1.00 94.34  ? 47  HIS E O   1 
ATOM   4776  C  CB  . HIS E  1 46  ? 12.101 4.860    -82.841  1.00 102.15 ? 47  HIS E CB  1 
ATOM   4777  C  CG  . HIS E  1 46  ? 11.336 5.265    -84.054  1.00 106.91 ? 47  HIS E CG  1 
ATOM   4778  N  ND1 . HIS E  1 46  ? 10.091 5.861    -83.989  1.00 109.78 ? 47  HIS E ND1 1 
ATOM   4779  C  CD2 . HIS E  1 46  ? 11.617 5.120    -85.371  1.00 110.37 ? 47  HIS E CD2 1 
ATOM   4780  C  CE1 . HIS E  1 46  ? 9.654  6.102    -85.213  1.00 114.30 ? 47  HIS E CE1 1 
ATOM   4781  N  NE2 . HIS E  1 46  ? 10.556 5.655    -86.071  1.00 114.75 ? 47  HIS E NE2 1 
ATOM   4782  N  N   . VAL E  1 47  ? 13.806 3.032    -80.953  1.00 93.31  ? 48  VAL E N   1 
ATOM   4783  C  CA  . VAL E  1 47  ? 14.457 3.035    -79.645  1.00 89.94  ? 48  VAL E CA  1 
ATOM   4784  C  C   . VAL E  1 47  ? 14.874 4.449    -79.290  1.00 90.98  ? 48  VAL E C   1 
ATOM   4785  O  O   . VAL E  1 47  ? 15.688 5.057    -79.968  1.00 92.62  ? 48  VAL E O   1 
ATOM   4786  C  CB  . VAL E  1 47  ? 15.700 2.166    -79.614  1.00 87.91  ? 48  VAL E CB  1 
ATOM   4787  C  CG1 . VAL E  1 47  ? 16.473 2.395    -78.303  1.00 85.10  ? 48  VAL E CG1 1 
ATOM   4788  C  CG2 . VAL E  1 47  ? 15.318 0.686    -79.790  1.00 87.15  ? 48  VAL E CG2 1 
ATOM   4789  N  N   . HIS E  1 48  ? 14.301 4.962    -78.216  1.00 90.55  ? 49  HIS E N   1 
ATOM   4790  C  CA  . HIS E  1 48  ? 14.605 6.311    -77.756  1.00 92.08  ? 49  HIS E CA  1 
ATOM   4791  C  C   . HIS E  1 48  ? 15.723 6.318    -76.729  1.00 89.59  ? 49  HIS E C   1 
ATOM   4792  O  O   . HIS E  1 48  ? 16.035 5.295    -76.134  1.00 86.74  ? 49  HIS E O   1 
ATOM   4793  C  CB  . HIS E  1 48  ? 13.361 6.948    -77.160  1.00 93.74  ? 49  HIS E CB  1 
ATOM   4794  C  CG  . HIS E  1 48  ? 12.323 7.288    -78.181  1.00 97.46  ? 49  HIS E CG  1 
ATOM   4795  N  ND1 . HIS E  1 48  ? 11.856 8.576    -78.360  1.00 101.47 ? 49  HIS E ND1 1 
ATOM   4796  C  CD2 . HIS E  1 48  ? 11.665 6.516    -79.081  1.00 97.80  ? 49  HIS E CD2 1 
ATOM   4797  C  CE1 . HIS E  1 48  ? 10.937 8.577    -79.310  1.00 104.30 ? 49  HIS E CE1 1 
ATOM   4798  N  NE2 . HIS E  1 48  ? 10.800 7.338    -79.759  1.00 102.29 ? 49  HIS E NE2 1 
ATOM   4799  N  N   . GLU E  1 49  ? 16.286 7.494    -76.494  1.00 91.29  ? 50  GLU E N   1 
ATOM   4800  C  CA  . GLU E  1 49  ? 17.518 7.620    -75.698  1.00 89.93  ? 50  GLU E CA  1 
ATOM   4801  C  C   . GLU E  1 49  ? 17.397 7.116    -74.249  1.00 87.02  ? 50  GLU E C   1 
ATOM   4802  O  O   . GLU E  1 49  ? 18.163 6.269    -73.797  1.00 84.33  ? 50  GLU E O   1 
ATOM   4803  C  CB  . GLU E  1 49  ? 18.005 9.078    -75.688  1.00 93.26  ? 50  GLU E CB  1 
ATOM   4804  C  CG  . GLU E  1 49  ? 19.413 9.267    -75.105  1.00 92.61  ? 50  GLU E CG  1 
ATOM   4805  C  CD  . GLU E  1 49  ? 19.997 10.662   -75.349  1.00 96.64  ? 50  GLU E CD  1 
ATOM   4806  O  OE1 . GLU E  1 49  ? 19.456 11.454   -76.160  1.00 99.72  ? 50  GLU E OE1 1 
ATOM   4807  O  OE2 . GLU E  1 49  ? 21.021 10.974   -74.713  1.00 97.03  ? 50  GLU E OE2 1 
ATOM   4808  N  N   . PHE E  1 50  ? 16.426 7.649    -73.529  1.00 87.99  ? 51  PHE E N   1 
ATOM   4809  C  CA  . PHE E  1 50  ? 16.340 7.437    -72.089  1.00 86.29  ? 51  PHE E CA  1 
ATOM   4810  C  C   . PHE E  1 50  ? 15.346 6.351    -71.692  1.00 84.52  ? 51  PHE E C   1 
ATOM   4811  O  O   . PHE E  1 50  ? 14.237 6.242    -72.259  1.00 85.66  ? 51  PHE E O   1 
ATOM   4812  C  CB  . PHE E  1 50  ? 15.985 8.746    -71.389  1.00 88.95  ? 51  PHE E CB  1 
ATOM   4813  C  CG  . PHE E  1 50  ? 16.890 9.855    -71.739  1.00 91.47  ? 51  PHE E CG  1 
ATOM   4814  C  CD1 . PHE E  1 50  ? 18.244 9.754    -71.506  1.00 90.50  ? 51  PHE E CD1 1 
ATOM   4815  C  CD2 . PHE E  1 50  ? 16.396 11.003   -72.322  1.00 95.90  ? 51  PHE E CD2 1 
ATOM   4816  C  CE1 . PHE E  1 50  ? 19.104 10.781   -71.836  1.00 93.70  ? 51  PHE E CE1 1 
ATOM   4817  C  CE2 . PHE E  1 50  ? 17.252 12.059   -72.654  1.00 98.96  ? 51  PHE E CE2 1 
ATOM   4818  C  CZ  . PHE E  1 50  ? 18.612 11.947   -72.407  1.00 97.78  ? 51  PHE E CZ  1 
ATOM   4819  N  N   . GLY E  1 51  ? 15.761 5.560    -70.699  1.00 82.08  ? 52  GLY E N   1 
ATOM   4820  C  CA  . GLY E  1 51  ? 14.866 4.614    -70.004  1.00 80.79  ? 52  GLY E CA  1 
ATOM   4821  C  C   . GLY E  1 51  ? 14.073 5.279    -68.878  1.00 82.37  ? 52  GLY E C   1 
ATOM   4822  O  O   . GLY E  1 51  ? 13.854 4.676    -67.816  1.00 81.24  ? 52  GLY E O   1 
ATOM   4823  N  N   . ASP E  1 52  ? 13.613 6.508    -69.142  1.00 85.39  ? 53  ASP E N   1 
ATOM   4824  C  CA  . ASP E  1 52  ? 12.894 7.334    -68.174  1.00 87.84  ? 53  ASP E CA  1 
ATOM   4825  C  C   . ASP E  1 52  ? 11.383 7.310    -68.450  1.00 90.07  ? 53  ASP E C   1 
ATOM   4826  O  O   . ASP E  1 52  ? 10.926 7.655    -69.536  1.00 91.84  ? 53  ASP E O   1 
ATOM   4827  C  CB  . ASP E  1 52  ? 13.402 8.760    -68.252  1.00 90.67  ? 53  ASP E CB  1 
ATOM   4828  C  CG  . ASP E  1 52  ? 12.901 9.603    -67.123  1.00 93.57  ? 53  ASP E CG  1 
ATOM   4829  O  OD1 . ASP E  1 52  ? 11.766 9.340    -66.679  1.00 94.61  ? 53  ASP E OD1 1 
ATOM   4830  O  OD2 . ASP E  1 52  ? 13.640 10.516   -66.686  1.00 95.12  ? 53  ASP E OD2 1 
ATOM   4831  N  N   . ASN E  1 53  ? 10.615 6.872    -67.466  1.00 90.41  ? 54  ASN E N   1 
ATOM   4832  C  CA  . ASN E  1 53  ? 9.159  6.761    -67.607  1.00 92.93  ? 54  ASN E CA  1 
ATOM   4833  C  C   . ASN E  1 53  ? 8.450  7.646    -66.605  1.00 96.30  ? 54  ASN E C   1 
ATOM   4834  O  O   . ASN E  1 53  ? 7.259  7.504    -66.366  1.00 98.48  ? 54  ASN E O   1 
ATOM   4835  C  CB  . ASN E  1 53  ? 8.716  5.301    -67.412  1.00 90.99  ? 54  ASN E CB  1 
ATOM   4836  C  CG  . ASN E  1 53  ? 7.768  4.827    -68.500  1.00 92.51  ? 54  ASN E CG  1 
ATOM   4837  O  OD1 . ASN E  1 53  ? 8.170  4.725    -69.670  1.00 92.23  ? 54  ASN E OD1 1 
ATOM   4838  N  ND2 . ASN E  1 53  ? 6.514  4.519    -68.126  1.00 94.74  ? 54  ASN E ND2 1 
ATOM   4839  N  N   . THR E  1 54  ? 9.218  8.555    -66.022  1.00 97.05  ? 55  THR E N   1 
ATOM   4840  C  CA  . THR E  1 54  ? 8.738  9.496    -65.007  1.00 101.09 ? 55  THR E CA  1 
ATOM   4841  C  C   . THR E  1 54  ? 7.392  10.108   -65.382  1.00 105.89 ? 55  THR E C   1 
ATOM   4842  O  O   . THR E  1 54  ? 6.367  9.820    -64.746  1.00 107.84 ? 55  THR E O   1 
ATOM   4843  C  CB  . THR E  1 54  ? 9.779  10.650   -64.802  1.00 102.30 ? 55  THR E CB  1 
ATOM   4844  O  OG1 . THR E  1 54  ? 10.938 10.137   -64.153  1.00 99.13  ? 55  THR E OG1 1 
ATOM   4845  C  CG2 . THR E  1 54  ? 9.229  11.808   -63.973  1.00 107.54 ? 55  THR E CG2 1 
ATOM   4846  N  N   . ALA E  1 55  ? 7.428  10.939   -66.434  1.00 108.06 ? 56  ALA E N   1 
ATOM   4847  C  CA  . ALA E  1 55  ? 6.262  11.634   -66.991  1.00 112.96 ? 56  ALA E CA  1 
ATOM   4848  C  C   . ALA E  1 55  ? 5.764  10.908   -68.260  1.00 111.90 ? 56  ALA E C   1 
ATOM   4849  O  O   . ALA E  1 55  ? 5.575  11.536   -69.317  1.00 114.40 ? 56  ALA E O   1 
ATOM   4850  C  CB  . ALA E  1 55  ? 6.623  13.080   -67.301  1.00 116.60 ? 56  ALA E CB  1 
ATOM   4851  N  N   . GLY E  1 56  ? 5.581  9.583    -68.136  1.00 108.52 ? 57  GLY E N   1 
ATOM   4852  C  CA  . GLY E  1 56  ? 5.037  8.737    -69.206  1.00 107.81 ? 57  GLY E CA  1 
ATOM   4853  C  C   . GLY E  1 56  ? 6.067  8.414    -70.276  1.00 104.42 ? 57  GLY E C   1 
ATOM   4854  O  O   . GLY E  1 56  ? 7.264  8.318    -69.990  1.00 101.17 ? 57  GLY E O   1 
ATOM   4855  N  N   . CYS E  1 57  ? 5.595  8.253    -71.512  1.00 105.71 ? 58  CYS E N   1 
ATOM   4856  C  CA  . CYS E  1 57  ? 6.474  7.993    -72.651  1.00 103.37 ? 58  CYS E CA  1 
ATOM   4857  C  C   . CYS E  1 57  ? 7.277  9.219    -73.033  1.00 104.83 ? 58  CYS E C   1 
ATOM   4858  O  O   . CYS E  1 57  ? 8.347  9.076    -73.584  1.00 102.70 ? 58  CYS E O   1 
ATOM   4859  C  CB  . CYS E  1 57  ? 5.687  7.515    -73.884  1.00 105.21 ? 58  CYS E CB  1 
ATOM   4860  S  SG  . CYS E  1 57  ? 4.984  5.811    -73.808  1.00 103.71 ? 58  CYS E SG  1 
ATOM   4861  N  N   . THR E  1 58  ? 6.774  10.418   -72.748  1.00 109.20 ? 59  THR E N   1 
ATOM   4862  C  CA  . THR E  1 58  ? 7.453  11.682   -73.144  1.00 111.72 ? 59  THR E CA  1 
ATOM   4863  C  C   . THR E  1 58  ? 8.856  11.814   -72.567  1.00 108.57 ? 59  THR E C   1 
ATOM   4864  O  O   . THR E  1 58  ? 9.738  12.409   -73.179  1.00 109.08 ? 59  THR E O   1 
ATOM   4865  C  CB  . THR E  1 58  ? 6.676  12.951   -72.665  1.00 117.40 ? 59  THR E CB  1 
ATOM   4866  O  OG1 . THR E  1 58  ? 5.278  12.789   -72.906  1.00 120.87 ? 59  THR E OG1 1 
ATOM   4867  C  CG2 . THR E  1 58  ? 7.182  14.218   -73.381  1.00 120.93 ? 59  THR E CG2 1 
ATOM   4868  N  N   . SER E  1 59  ? 9.026  11.271   -71.364  1.00 105.93 ? 60  SER E N   1 
ATOM   4869  C  CA  . SER E  1 59  ? 10.298 11.329   -70.621  1.00 103.35 ? 60  SER E CA  1 
ATOM   4870  C  C   . SER E  1 59  ? 11.449 10.626   -71.334  1.00 99.57  ? 60  SER E C   1 
ATOM   4871  O  O   . SER E  1 59  ? 12.624 10.962   -71.111  1.00 98.62  ? 60  SER E O   1 
ATOM   4872  C  CB  . SER E  1 59  ? 10.112 10.713   -69.230  1.00 101.44 ? 60  SER E CB  1 
ATOM   4873  O  OG  . SER E  1 59  ? 8.922  11.217   -68.639  1.00 105.66 ? 60  SER E OG  1 
ATOM   4874  N  N   . ALA E  1 60  ? 11.094 9.651    -72.183  1.00 98.00  ? 61  ALA E N   1 
ATOM   4875  C  CA  . ALA E  1 60  ? 12.069 8.828    -72.936  1.00 94.90  ? 61  ALA E CA  1 
ATOM   4876  C  C   . ALA E  1 60  ? 12.976 9.687    -73.857  1.00 96.75  ? 61  ALA E C   1 
ATOM   4877  O  O   . ALA E  1 60  ? 13.997 9.208    -74.369  1.00 94.89  ? 61  ALA E O   1 
ATOM   4878  C  CB  . ALA E  1 60  ? 11.357 7.717    -73.747  1.00 93.85  ? 61  ALA E CB  1 
ATOM   4879  N  N   . GLY E  1 61  ? 12.596 10.944   -74.077  1.00 100.89 ? 62  GLY E N   1 
ATOM   4880  C  CA  . GLY E  1 61  ? 13.404 11.850   -74.874  1.00 103.34 ? 62  GLY E CA  1 
ATOM   4881  C  C   . GLY E  1 61  ? 13.346 11.476   -76.342  1.00 104.08 ? 62  GLY E C   1 
ATOM   4882  O  O   . GLY E  1 61  ? 12.451 10.752   -76.771  1.00 103.60 ? 62  GLY E O   1 
ATOM   4883  N  N   . PRO E  1 62  ? 14.327 11.946   -77.122  1.00 105.61 ? 63  PRO E N   1 
ATOM   4884  C  CA  . PRO E  1 62  ? 14.316 11.730   -78.563  1.00 107.25 ? 63  PRO E CA  1 
ATOM   4885  C  C   . PRO E  1 62  ? 14.802 10.350   -78.987  1.00 103.64 ? 63  PRO E C   1 
ATOM   4886  O  O   . PRO E  1 62  ? 15.119 9.486    -78.150  1.00 99.62  ? 63  PRO E O   1 
ATOM   4887  C  CB  . PRO E  1 62  ? 15.295 12.795   -79.061  1.00 110.43 ? 63  PRO E CB  1 
ATOM   4888  C  CG  . PRO E  1 62  ? 16.300 12.875   -77.984  1.00 108.11 ? 63  PRO E CG  1 
ATOM   4889  C  CD  . PRO E  1 62  ? 15.546 12.658   -76.693  1.00 106.07 ? 63  PRO E CD  1 
ATOM   4890  N  N   . HIS E  1 63  ? 14.854 10.173   -80.304  1.00 105.68 ? 64  HIS E N   1 
ATOM   4891  C  CA  . HIS E  1 63  ? 15.405 8.963    -80.935  1.00 103.44 ? 64  HIS E CA  1 
ATOM   4892  C  C   . HIS E  1 63  ? 16.846 8.742    -80.473  1.00 100.91 ? 64  HIS E C   1 
ATOM   4893  O  O   . HIS E  1 63  ? 17.653 9.691    -80.392  1.00 102.65 ? 64  HIS E O   1 
ATOM   4894  C  CB  . HIS E  1 63  ? 15.370 9.099    -82.479  1.00 107.34 ? 64  HIS E CB  1 
ATOM   4895  C  CG  . HIS E  1 63  ? 13.989 9.038    -83.074  1.00 109.65 ? 64  HIS E CG  1 
ATOM   4896  N  ND1 . HIS E  1 63  ? 13.733 8.456    -84.298  1.00 111.44 ? 64  HIS E ND1 1 
ATOM   4897  C  CD2 . HIS E  1 63  ? 12.789 9.457    -82.600  1.00 110.71 ? 64  HIS E CD2 1 
ATOM   4898  C  CE1 . HIS E  1 63  ? 12.441 8.531    -84.558  1.00 113.69 ? 64  HIS E CE1 1 
ATOM   4899  N  NE2 . HIS E  1 63  ? 11.846 9.137    -83.547  1.00 113.26 ? 64  HIS E NE2 1 
ATOM   4900  N  N   . PHE E  1 64  ? 17.164 7.493    -80.163  1.00 97.30  ? 65  PHE E N   1 
ATOM   4901  C  CA  . PHE E  1 64  ? 18.524 7.169    -79.735  1.00 95.51  ? 65  PHE E CA  1 
ATOM   4902  C  C   . PHE E  1 64  ? 19.513 7.433    -80.882  1.00 98.31  ? 65  PHE E C   1 
ATOM   4903  O  O   . PHE E  1 64  ? 19.467 6.786    -81.947  1.00 99.03  ? 65  PHE E O   1 
ATOM   4904  C  CB  . PHE E  1 64  ? 18.633 5.723    -79.234  1.00 91.77  ? 65  PHE E CB  1 
ATOM   4905  C  CG  . PHE E  1 64  ? 20.021 5.339    -78.752  1.00 90.02  ? 65  PHE E CG  1 
ATOM   4906  C  CD1 . PHE E  1 64  ? 20.780 6.203    -77.956  1.00 90.24  ? 65  PHE E CD1 1 
ATOM   4907  C  CD2 . PHE E  1 64  ? 20.552 4.088    -79.076  1.00 89.01  ? 65  PHE E CD2 1 
ATOM   4908  C  CE1 . PHE E  1 64  ? 22.045 5.823    -77.509  1.00 89.58  ? 65  PHE E CE1 1 
ATOM   4909  C  CE2 . PHE E  1 64  ? 21.822 3.699    -78.632  1.00 88.17  ? 65  PHE E CE2 1 
ATOM   4910  C  CZ  . PHE E  1 64  ? 22.566 4.560    -77.847  1.00 88.43  ? 65  PHE E CZ  1 
ATOM   4911  N  N   . ASN E  1 65  ? 20.407 8.388    -80.627  1.00 100.10 ? 66  ASN E N   1 
ATOM   4912  C  CA  . ASN E  1 65  ? 21.263 8.957    -81.670  1.00 104.11 ? 66  ASN E CA  1 
ATOM   4913  C  C   . ASN E  1 65  ? 22.705 9.362    -81.194  1.00 104.77 ? 66  ASN E C   1 
ATOM   4914  O  O   . ASN E  1 65  ? 23.070 10.565   -81.154  1.00 107.86 ? 66  ASN E O   1 
ATOM   4915  C  CB  . ASN E  1 65  ? 20.540 10.157   -82.273  1.00 108.20 ? 66  ASN E CB  1 
ATOM   4916  C  CG  . ASN E  1 65  ? 21.238 10.691   -83.511  1.00 112.99 ? 66  ASN E CG  1 
ATOM   4917  O  OD1 . ASN E  1 65  ? 22.140 10.034   -84.088  1.00 113.33 ? 66  ASN E OD1 1 
ATOM   4918  N  ND2 . ASN E  1 65  ? 20.826 11.891   -83.936  1.00 117.26 ? 66  ASN E ND2 1 
ATOM   4919  N  N   . PRO E  1 66  ? 23.531 8.351    -80.850  1.00 102.24 ? 67  PRO E N   1 
ATOM   4920  C  CA  . PRO E  1 66  ? 24.850 8.596    -80.285  1.00 102.80 ? 67  PRO E CA  1 
ATOM   4921  C  C   . PRO E  1 66  ? 25.886 9.011    -81.309  1.00 107.39 ? 67  PRO E C   1 
ATOM   4922  O  O   . PRO E  1 66  ? 26.895 9.623    -80.937  1.00 109.48 ? 67  PRO E O   1 
ATOM   4923  C  CB  . PRO E  1 66  ? 25.237 7.239    -79.713  1.00 99.07  ? 67  PRO E CB  1 
ATOM   4924  C  CG  . PRO E  1 66  ? 24.546 6.266    -80.565  1.00 98.29  ? 67  PRO E CG  1 
ATOM   4925  C  CD  . PRO E  1 66  ? 23.249 6.907    -80.957  1.00 99.29  ? 67  PRO E CD  1 
ATOM   4926  N  N   . LEU E  1 67  ? 25.647 8.671    -82.578  1.00 109.41 ? 68  LEU E N   1 
ATOM   4927  C  CA  . LEU E  1 67  ? 26.536 9.091    -83.671  1.00 114.34 ? 68  LEU E CA  1 
ATOM   4928  C  C   . LEU E  1 67  ? 26.099 10.411   -84.338  1.00 118.79 ? 68  LEU E C   1 
ATOM   4929  O  O   . LEU E  1 67  ? 26.606 10.777   -85.410  1.00 123.40 ? 68  LEU E O   1 
ATOM   4930  C  CB  . LEU E  1 67  ? 26.650 7.985    -84.716  1.00 115.08 ? 68  LEU E CB  1 
ATOM   4931  C  CG  . LEU E  1 67  ? 27.135 6.620    -84.191  1.00 111.79 ? 68  LEU E CG  1 
ATOM   4932  C  CD1 . LEU E  1 67  ? 27.438 5.678    -85.383  1.00 114.04 ? 68  LEU E CD1 1 
ATOM   4933  C  CD2 . LEU E  1 67  ? 28.345 6.763    -83.255  1.00 111.43 ? 68  LEU E CD2 1 
ATOM   4934  N  N   . SER E  1 68  ? 25.158 11.113   -83.697  1.00 117.84 ? 69  SER E N   1 
ATOM   4935  C  CA  . SER E  1 68  ? 24.801 12.503   -84.052  1.00 122.28 ? 69  SER E CA  1 
ATOM   4936  C  C   . SER E  1 68  ? 24.405 12.658   -85.521  1.00 126.36 ? 69  SER E C   1 
ATOM   4937  O  O   . SER E  1 68  ? 24.837 13.605   -86.199  1.00 131.55 ? 69  SER E O   1 
ATOM   4938  C  CB  . SER E  1 68  ? 25.967 13.461   -83.740  1.00 125.77 ? 69  SER E CB  1 
ATOM   4939  O  OG  . SER E  1 68  ? 26.554 13.197   -82.479  1.00 122.76 ? 69  SER E OG  1 
ATOM   4940  N  N   . ARG E  1 69  ? 23.585 11.718   -85.998  1.00 124.35 ? 70  ARG E N   1 
ATOM   4941  C  CA  . ARG E  1 69  ? 23.127 11.706   -87.396  1.00 128.55 ? 70  ARG E CA  1 
ATOM   4942  C  C   . ARG E  1 69  ? 21.683 12.195   -87.554  1.00 129.31 ? 70  ARG E C   1 
ATOM   4943  O  O   . ARG E  1 69  ? 21.002 12.539   -86.573  1.00 127.00 ? 70  ARG E O   1 
ATOM   4944  C  CB  . ARG E  1 69  ? 23.208 10.296   -88.012  1.00 126.95 ? 70  ARG E CB  1 
ATOM   4945  C  CG  . ARG E  1 69  ? 24.452 9.486    -87.713  1.00 128.33 ? 70  ARG E CG  1 
ATOM   4946  C  CD  . ARG E  1 69  ? 25.602 9.797    -88.668  1.00 137.38 ? 70  ARG E CD  1 
ATOM   4947  N  NE  . ARG E  1 69  ? 26.294 8.569    -89.079  1.00 140.76 ? 70  ARG E NE  1 
ATOM   4948  C  CZ  . ARG E  1 69  ? 26.156 7.949    -90.261  1.00 146.64 ? 70  ARG E CZ  1 
ATOM   4949  N  NH1 . ARG E  1 69  ? 25.360 8.421    -91.223  1.00 150.29 ? 70  ARG E NH1 1 
ATOM   4950  N  NH2 . ARG E  1 69  ? 26.846 6.834    -90.497  1.00 148.26 ? 70  ARG E NH2 1 
ATOM   4951  N  N   . LYS E  1 70  ? 21.239 12.232   -88.814  1.00 133.31 ? 71  LYS E N   1 
ATOM   4952  C  CA  . LYS E  1 70  ? 19.864 12.603   -89.167  1.00 135.09 ? 71  LYS E CA  1 
ATOM   4953  C  C   . LYS E  1 70  ? 18.969 11.372   -89.159  1.00 131.34 ? 71  LYS E C   1 
ATOM   4954  O  O   . LYS E  1 70  ? 19.462 10.233   -89.319  1.00 128.67 ? 71  LYS E O   1 
ATOM   4955  C  CB  . LYS E  1 70  ? 19.818 13.228   -90.564  1.00 141.89 ? 71  LYS E CB  1 
ATOM   4956  C  CG  . LYS E  1 70  ? 20.711 14.446   -90.741  1.00 146.98 ? 71  LYS E CG  1 
ATOM   4957  C  CD  . LYS E  1 70  ? 19.943 15.765   -90.467  1.00 150.61 ? 71  LYS E CD  1 
ATOM   4958  C  CE  . LYS E  1 70  ? 20.802 17.037   -90.755  1.00 156.52 ? 71  LYS E CE  1 
ATOM   4959  N  NZ  . LYS E  1 70  ? 20.062 18.306   -90.497  1.00 160.01 ? 71  LYS E NZ  1 
ATOM   4960  N  N   . HIS E  1 71  ? 17.658 11.616   -89.005  1.00 131.53 ? 72  HIS E N   1 
ATOM   4961  C  CA  . HIS E  1 71  ? 16.660 10.529   -89.033  1.00 129.00 ? 72  HIS E CA  1 
ATOM   4962  C  C   . HIS E  1 71  ? 16.654 9.795    -90.396  1.00 131.76 ? 72  HIS E C   1 
ATOM   4963  O  O   . HIS E  1 71  ? 16.977 10.354   -91.440  1.00 136.92 ? 72  HIS E O   1 
ATOM   4964  C  CB  . HIS E  1 71  ? 15.228 11.013   -88.671  1.00 129.74 ? 72  HIS E CB  1 
ATOM   4965  C  CG  . HIS E  1 71  ? 14.211 9.897    -88.594  1.00 127.47 ? 72  HIS E CG  1 
ATOM   4966  N  ND1 . HIS E  1 71  ? 14.202 8.951    -87.583  1.00 121.85 ? 72  HIS E ND1 1 
ATOM   4967  C  CD2 . HIS E  1 71  ? 13.198 9.550    -89.429  1.00 130.26 ? 72  HIS E CD2 1 
ATOM   4968  C  CE1 . HIS E  1 71  ? 13.223 8.082    -87.791  1.00 121.21 ? 72  HIS E CE1 1 
ATOM   4969  N  NE2 . HIS E  1 71  ? 12.595 8.425    -88.901  1.00 126.12 ? 72  HIS E NE2 1 
ATOM   4970  N  N   . GLY E  1 72  ? 16.292 8.525    -90.358  1.00 128.71 ? 73  GLY E N   1 
ATOM   4971  C  CA  . GLY E  1 72  ? 16.162 7.737    -91.563  1.00 131.54 ? 73  GLY E CA  1 
ATOM   4972  C  C   . GLY E  1 72  ? 15.478 6.381    -91.357  1.00 128.50 ? 73  GLY E C   1 
ATOM   4973  O  O   . GLY E  1 72  ? 14.980 6.026    -90.261  1.00 124.09 ? 73  GLY E O   1 
ATOM   4974  N  N   . GLY E  1 73  ? 15.436 5.630    -92.450  1.00 131.38 ? 74  GLY E N   1 
ATOM   4975  C  CA  . GLY E  1 73  ? 14.916 4.280    -92.433  1.00 129.54 ? 74  GLY E CA  1 
ATOM   4976  C  C   . GLY E  1 73  ? 16.025 3.375    -91.963  1.00 125.91 ? 74  GLY E C   1 
ATOM   4977  O  O   . GLY E  1 73  ? 17.192 3.767    -92.033  1.00 126.41 ? 74  GLY E O   1 
ATOM   4978  N  N   . PRO E  1 74  ? 15.675 2.157    -91.492  1.00 122.95 ? 75  PRO E N   1 
ATOM   4979  C  CA  . PRO E  1 74  ? 16.683 1.219    -90.950  1.00 119.73 ? 75  PRO E CA  1 
ATOM   4980  C  C   . PRO E  1 74  ? 17.747 0.746    -91.953  1.00 123.10 ? 75  PRO E C   1 
ATOM   4981  O  O   . PRO E  1 74  ? 18.923 0.568    -91.592  1.00 121.57 ? 75  PRO E O   1 
ATOM   4982  C  CB  . PRO E  1 74  ? 15.848 0.023    -90.483  1.00 117.24 ? 75  PRO E CB  1 
ATOM   4983  C  CG  . PRO E  1 74  ? 14.599 0.111    -91.220  1.00 120.77 ? 75  PRO E CG  1 
ATOM   4984  C  CD  . PRO E  1 74  ? 14.329 1.562    -91.476  1.00 123.08 ? 75  PRO E CD  1 
ATOM   4985  N  N   . LYS E  1 75  ? 17.323 0.570    -93.201  1.00 128.16 ? 76  LYS E N   1 
ATOM   4986  C  CA  . LYS E  1 75  ? 18.241 0.228    -94.287  1.00 132.51 ? 76  LYS E CA  1 
ATOM   4987  C  C   . LYS E  1 75  ? 19.146 1.393    -94.672  1.00 135.03 ? 76  LYS E C   1 
ATOM   4988  O  O   . LYS E  1 75  ? 20.267 1.175    -95.115  1.00 137.15 ? 76  LYS E O   1 
ATOM   4989  C  CB  . LYS E  1 75  ? 17.476 -0.185   -95.533  1.00 137.93 ? 76  LYS E CB  1 
ATOM   4990  C  CG  . LYS E  1 75  ? 16.362 -1.200   -95.303  1.00 137.11 ? 76  LYS E CG  1 
ATOM   4991  C  CD  . LYS E  1 75  ? 16.075 -1.966   -96.603  1.00 143.22 ? 76  LYS E CD  1 
ATOM   4992  C  CE  . LYS E  1 75  ? 14.799 -2.809   -96.513  1.00 143.22 ? 76  LYS E CE  1 
ATOM   4993  N  NZ  . LYS E  1 75  ? 14.365 -3.305   -97.850  1.00 149.88 ? 76  LYS E NZ  1 
ATOM   4994  N  N   . ASP E  1 76  ? 18.648 2.619    -94.527  1.00 135.42 ? 77  ASP E N   1 
ATOM   4995  C  CA  . ASP E  1 76  ? 19.465 3.799    -94.808  1.00 138.33 ? 77  ASP E CA  1 
ATOM   4996  C  C   . ASP E  1 76  ? 20.731 3.787    -93.959  1.00 135.28 ? 77  ASP E C   1 
ATOM   4997  O  O   . ASP E  1 76  ? 20.695 3.378    -92.782  1.00 129.90 ? 77  ASP E O   1 
ATOM   4998  C  CB  . ASP E  1 76  ? 18.682 5.096    -94.563  1.00 138.91 ? 77  ASP E CB  1 
ATOM   4999  C  CG  . ASP E  1 76  ? 17.623 5.342    -95.634  1.00 144.22 ? 77  ASP E CG  1 
ATOM   5000  O  OD1 . ASP E  1 76  ? 17.776 4.839    -96.781  1.00 148.90 ? 77  ASP E OD1 1 
ATOM   5001  O  OD2 . ASP E  1 76  ? 16.627 6.046    -95.335  1.00 144.55 ? 77  ASP E OD2 1 
ATOM   5002  N  N   . GLU E  1 77  ? 21.849 4.205    -94.561  1.00 139.14 ? 78  GLU E N   1 
ATOM   5003  C  CA  . GLU E  1 77  ? 23.099 4.358    -93.810  1.00 137.15 ? 78  GLU E CA  1 
ATOM   5004  C  C   . GLU E  1 77  ? 22.982 5.574    -92.895  1.00 134.93 ? 78  GLU E C   1 
ATOM   5005  O  O   . GLU E  1 77  ? 23.333 5.484    -91.718  1.00 130.43 ? 78  GLU E O   1 
ATOM   5006  C  CB  . GLU E  1 77  ? 24.316 4.528    -94.714  1.00 142.65 ? 78  GLU E CB  1 
ATOM   5007  C  CG  . GLU E  1 77  ? 25.511 5.163    -93.953  1.00 142.28 ? 78  GLU E CG  1 
ATOM   5008  C  CD  . GLU E  1 77  ? 26.843 5.056    -94.681  1.00 148.11 ? 78  GLU E CD  1 
ATOM   5009  O  OE1 . GLU E  1 77  ? 26.840 5.098    -95.942  1.00 153.93 ? 78  GLU E OE1 1 
ATOM   5010  O  OE2 . GLU E  1 77  ? 27.892 4.943    -93.977  1.00 146.83 ? 78  GLU E OE2 1 
ATOM   5011  N  N   . GLU E  1 78  ? 22.542 6.709    -93.460  1.00 138.73 ? 79  GLU E N   1 
ATOM   5012  C  CA  . GLU E  1 78  ? 22.256 7.919    -92.676  1.00 137.49 ? 79  GLU E CA  1 
ATOM   5013  C  C   . GLU E  1 78  ? 20.935 7.698    -91.919  1.00 133.20 ? 79  GLU E C   1 
ATOM   5014  O  O   . GLU E  1 78  ? 19.837 7.975    -92.424  1.00 135.34 ? 79  GLU E O   1 
ATOM   5015  C  CB  . GLU E  1 78  ? 22.214 9.186    -93.552  1.00 143.71 ? 79  GLU E CB  1 
ATOM   5016  C  CG  . GLU E  1 78  ? 22.052 10.522   -92.766  1.00 143.63 ? 79  GLU E CG  1 
ATOM   5017  C  CD  . GLU E  1 78  ? 23.352 11.023   -92.101  1.00 143.61 ? 79  GLU E CD  1 
ATOM   5018  O  OE1 . GLU E  1 78  ? 24.398 10.329   -92.227  1.00 143.65 ? 79  GLU E OE1 1 
ATOM   5019  O  OE2 . GLU E  1 78  ? 23.323 12.121   -91.464  1.00 143.84 ? 79  GLU E OE2 1 
ATOM   5020  N  N   . ARG E  1 79  ? 21.079 7.169    -90.705  1.00 127.59 ? 80  ARG E N   1 
ATOM   5021  C  CA  . ARG E  1 79  ? 19.966 6.929    -89.783  1.00 123.23 ? 80  ARG E CA  1 
ATOM   5022  C  C   . ARG E  1 79  ? 20.379 7.147    -88.326  1.00 118.73 ? 80  ARG E C   1 
ATOM   5023  O  O   . ARG E  1 79  ? 21.572 7.171    -87.994  1.00 118.26 ? 80  ARG E O   1 
ATOM   5024  C  CB  . ARG E  1 79  ? 19.471 5.492    -89.928  1.00 121.04 ? 80  ARG E CB  1 
ATOM   5025  C  CG  . ARG E  1 79  ? 20.549 4.443    -89.678  1.00 118.82 ? 80  ARG E CG  1 
ATOM   5026  C  CD  . ARG E  1 79  ? 19.973 3.030    -89.600  1.00 116.63 ? 80  ARG E CD  1 
ATOM   5027  N  NE  . ARG E  1 79  ? 19.495 2.678    -88.243  1.00 111.57 ? 80  ARG E NE  1 
ATOM   5028  C  CZ  . ARG E  1 79  ? 19.147 1.444    -87.843  1.00 108.76 ? 80  ARG E CZ  1 
ATOM   5029  N  NH1 . ARG E  1 79  ? 19.209 0.411    -88.690  1.00 110.66 ? 80  ARG E NH1 1 
ATOM   5030  N  NH2 . ARG E  1 79  ? 18.738 1.240    -86.592  1.00 104.53 ? 80  ARG E NH2 1 
ATOM   5031  N  N   . HIS E  1 80  ? 19.387 7.278    -87.454  1.00 115.91 ? 81  HIS E N   1 
ATOM   5032  C  CA  . HIS E  1 80  ? 19.652 7.211    -86.019  1.00 111.41 ? 81  HIS E CA  1 
ATOM   5033  C  C   . HIS E  1 80  ? 19.874 5.727    -85.669  1.00 107.69 ? 81  HIS E C   1 
ATOM   5034  O  O   . HIS E  1 80  ? 19.251 4.825    -86.283  1.00 107.79 ? 81  HIS E O   1 
ATOM   5035  C  CB  . HIS E  1 80  ? 18.486 7.753    -85.184  1.00 110.01 ? 81  HIS E CB  1 
ATOM   5036  C  CG  . HIS E  1 80  ? 18.158 9.197    -85.434  1.00 113.83 ? 81  HIS E CG  1 
ATOM   5037  N  ND1 . HIS E  1 80  ? 16.870 9.695    -85.334  1.00 114.93 ? 81  HIS E ND1 1 
ATOM   5038  C  CD2 . HIS E  1 80  ? 18.943 10.250   -85.761  1.00 117.16 ? 81  HIS E CD2 1 
ATOM   5039  C  CE1 . HIS E  1 80  ? 16.878 10.992   -85.587  1.00 119.04 ? 81  HIS E CE1 1 
ATOM   5040  N  NE2 . HIS E  1 80  ? 18.124 11.355   -85.851  1.00 120.49 ? 81  HIS E NE2 1 
ATOM   5041  N  N   . VAL E  1 81  ? 20.735 5.483    -84.674  1.00 104.65 ? 82  VAL E N   1 
ATOM   5042  C  CA  . VAL E  1 81  ? 20.978 4.103    -84.197  1.00 101.21 ? 82  VAL E CA  1 
ATOM   5043  C  C   . VAL E  1 81  ? 19.653 3.430    -83.830  1.00 98.74  ? 82  VAL E C   1 
ATOM   5044  O  O   . VAL E  1 81  ? 19.443 2.242    -84.133  1.00 97.93  ? 82  VAL E O   1 
ATOM   5045  C  CB  . VAL E  1 81  ? 21.949 4.048    -82.979  1.00 98.40  ? 82  VAL E CB  1 
ATOM   5046  C  CG1 . VAL E  1 81  ? 22.021 2.615    -82.395  1.00 94.74  ? 82  VAL E CG1 1 
ATOM   5047  C  CG2 . VAL E  1 81  ? 23.344 4.538    -83.393  1.00 101.38 ? 82  VAL E CG2 1 
ATOM   5048  N  N   . GLY E  1 82  ? 18.767 4.212    -83.200  1.00 98.03  ? 83  GLY E N   1 
ATOM   5049  C  CA  . GLY E  1 82  ? 17.479 3.706    -82.724  1.00 96.33  ? 83  GLY E CA  1 
ATOM   5050  C  C   . GLY E  1 82  ? 16.354 3.607    -83.760  1.00 99.34  ? 83  GLY E C   1 
ATOM   5051  O  O   . GLY E  1 82  ? 15.234 3.141    -83.442  1.00 98.41  ? 83  GLY E O   1 
ATOM   5052  N  N   . ASP E  1 83  ? 16.628 4.035    -84.997  1.00 103.19 ? 84  ASP E N   1 
ATOM   5053  C  CA  . ASP E  1 83  ? 15.586 4.058    -86.040  1.00 106.60 ? 84  ASP E CA  1 
ATOM   5054  C  C   . ASP E  1 83  ? 15.324 2.663    -86.566  1.00 106.54 ? 84  ASP E C   1 
ATOM   5055  O  O   . ASP E  1 83  ? 16.015 2.202    -87.471  1.00 108.66 ? 84  ASP E O   1 
ATOM   5056  C  CB  . ASP E  1 83  ? 15.998 4.966    -87.197  1.00 111.19 ? 84  ASP E CB  1 
ATOM   5057  C  CG  . ASP E  1 83  ? 15.871 6.405    -86.856  1.00 112.43 ? 84  ASP E CG  1 
ATOM   5058  O  OD1 . ASP E  1 83  ? 15.155 6.725    -85.883  1.00 110.24 ? 84  ASP E OD1 1 
ATOM   5059  O  OD2 . ASP E  1 83  ? 16.493 7.229    -87.547  1.00 116.00 ? 84  ASP E OD2 1 
ATOM   5060  N  N   . LEU E  1 84  ? 14.342 1.981    -85.988  1.00 104.65 ? 85  LEU E N   1 
ATOM   5061  C  CA  . LEU E  1 84  ? 13.989 0.618    -86.451  1.00 105.17 ? 85  LEU E CA  1 
ATOM   5062  C  C   . LEU E  1 84  ? 12.850 0.605    -87.487  1.00 109.54 ? 85  LEU E C   1 
ATOM   5063  O  O   . LEU E  1 84  ? 12.308 -0.478   -87.850  1.00 110.40 ? 85  LEU E O   1 
ATOM   5064  C  CB  . LEU E  1 84  ? 13.625 -0.289   -85.270  1.00 101.34 ? 85  LEU E CB  1 
ATOM   5065  C  CG  . LEU E  1 84  ? 14.822 -0.782   -84.459  1.00 97.66  ? 85  LEU E CG  1 
ATOM   5066  C  CD1 . LEU E  1 84  ? 14.347 -1.603   -83.269  1.00 94.22  ? 85  LEU E CD1 1 
ATOM   5067  C  CD2 . LEU E  1 84  ? 15.763 -1.588   -85.354  1.00 99.07  ? 85  LEU E CD2 1 
ATOM   5068  N  N   . GLY E  1 85  ? 12.485 1.807    -87.952  1.00 112.58 ? 86  GLY E N   1 
ATOM   5069  C  CA  . GLY E  1 85  ? 11.520 1.949    -89.046  1.00 117.50 ? 86  GLY E CA  1 
ATOM   5070  C  C   . GLY E  1 85  ? 10.068 1.751    -88.629  1.00 117.89 ? 86  GLY E C   1 
ATOM   5071  O  O   . GLY E  1 85  ? 9.597  2.390    -87.669  1.00 116.21 ? 86  GLY E O   1 
ATOM   5072  N  N   . ASN E  1 86  ? 9.360  0.884    -89.365  1.00 120.55 ? 87  ASN E N   1 
ATOM   5073  C  CA  . ASN E  1 86  ? 7.913  0.684    -89.167  1.00 122.14 ? 87  ASN E CA  1 
ATOM   5074  C  C   . ASN E  1 86  ? 7.530  -0.714   -88.763  1.00 120.51 ? 87  ASN E C   1 
ATOM   5075  O  O   . ASN E  1 86  ? 8.270  -1.676   -89.014  1.00 119.54 ? 87  ASN E O   1 
ATOM   5076  C  CB  . ASN E  1 86  ? 7.134  1.037    -90.431  1.00 128.27 ? 87  ASN E CB  1 
ATOM   5077  C  CG  . ASN E  1 86  ? 7.047  2.542    -90.650  1.00 131.08 ? 87  ASN E CG  1 
ATOM   5078  O  OD1 . ASN E  1 86  ? 6.640  3.300    -89.753  1.00 130.06 ? 87  ASN E OD1 1 
ATOM   5079  N  ND2 . ASN E  1 86  ? 7.441  2.987    -91.835  1.00 135.22 ? 87  ASN E ND2 1 
ATOM   5080  N  N   . VAL E  1 87  ? 6.374  -0.810   -88.112  1.00 120.75 ? 88  VAL E N   1 
ATOM   5081  C  CA  . VAL E  1 87  ? 5.742  -2.104   -87.828  1.00 120.75 ? 88  VAL E CA  1 
ATOM   5082  C  C   . VAL E  1 87  ? 4.342  -2.044   -88.410  1.00 126.19 ? 88  VAL E C   1 
ATOM   5083  O  O   . VAL E  1 87  ? 3.693  -0.981   -88.395  1.00 128.46 ? 88  VAL E O   1 
ATOM   5084  C  CB  . VAL E  1 87  ? 5.640  -2.428   -86.304  1.00 116.19 ? 88  VAL E CB  1 
ATOM   5085  C  CG1 . VAL E  1 87  ? 7.016  -2.732   -85.698  1.00 111.13 ? 88  VAL E CG1 1 
ATOM   5086  C  CG2 . VAL E  1 87  ? 4.946  -1.278   -85.557  1.00 116.28 ? 88  VAL E CG2 1 
ATOM   5087  N  N   . THR E  1 88  ? 3.872  -3.180   -88.919  1.00 128.88 ? 89  THR E N   1 
ATOM   5088  C  CA  . THR E  1 88  ? 2.577  -3.220   -89.610  1.00 134.88 ? 89  THR E CA  1 
ATOM   5089  C  C   . THR E  1 88  ? 1.474  -3.893   -88.777  1.00 135.29 ? 89  THR E C   1 
ATOM   5090  O  O   . THR E  1 88  ? 1.630  -5.034   -88.305  1.00 133.30 ? 89  THR E O   1 
ATOM   5091  C  CB  . THR E  1 88  ? 2.703  -3.892   -91.001  1.00 139.41 ? 89  THR E CB  1 
ATOM   5092  O  OG1 . THR E  1 88  ? 3.486  -3.042   -91.872  1.00 140.56 ? 89  THR E OG1 1 
ATOM   5093  C  CG2 . THR E  1 88  ? 1.299  -4.136   -91.614  1.00 145.92 ? 89  THR E CG2 1 
ATOM   5094  N  N   . ALA E  1 89  ? 0.358  -3.165   -88.637  1.00 138.57 ? 90  ALA E N   1 
ATOM   5095  C  CA  . ALA E  1 89  ? -0.830 -3.627   -87.898  1.00 140.25 ? 90  ALA E CA  1 
ATOM   5096  C  C   . ALA E  1 89  ? -1.992 -4.134   -88.829  1.00 147.42 ? 90  ALA E C   1 
ATOM   5097  O  O   . ALA E  1 89  ? -2.458 -3.414   -89.757  1.00 152.22 ? 90  ALA E O   1 
ATOM   5098  C  CB  . ALA E  1 89  ? -1.331 -2.497   -86.947  1.00 139.33 ? 90  ALA E CB  1 
ATOM   5099  N  N   . ASP E  1 90  ? -2.450 -5.366   -88.560  1.00 148.30 ? 91  ASP E N   1 
ATOM   5100  C  CA  . ASP E  1 90  ? -3.550 -5.974   -89.319  1.00 155.17 ? 91  ASP E CA  1 
ATOM   5101  C  C   . ASP E  1 90  ? -4.944 -5.605   -88.754  1.00 159.10 ? 91  ASP E C   1 
ATOM   5102  O  O   . ASP E  1 90  ? -5.071 -5.162   -87.597  1.00 156.05 ? 91  ASP E O   1 
ATOM   5103  C  CB  . ASP E  1 90  ? -3.358 -7.497   -89.441  1.00 155.33 ? 91  ASP E CB  1 
ATOM   5104  C  CG  . ASP E  1 90  ? -3.620 -8.269   -88.126  1.00 152.65 ? 91  ASP E CG  1 
ATOM   5105  O  OD1 . ASP E  1 90  ? -3.523 -9.512   -88.167  1.00 153.60 ? 91  ASP E OD1 1 
ATOM   5106  O  OD2 . ASP E  1 90  ? -3.921 -7.685   -87.060  1.00 150.13 ? 91  ASP E OD2 1 
ATOM   5107  N  N   . LYS E  1 91  ? -5.966 -5.772   -89.600  1.00 166.37 ? 92  LYS E N   1 
ATOM   5108  C  CA  . LYS E  1 91  ? -7.403 -5.500   -89.266  1.00 171.88 ? 92  LYS E CA  1 
ATOM   5109  C  C   . LYS E  1 91  ? -7.731 -5.397   -87.755  1.00 168.68 ? 92  LYS E C   1 
ATOM   5110  O  O   . LYS E  1 91  ? -8.102 -4.307   -87.252  1.00 168.89 ? 92  LYS E O   1 
ATOM   5111  C  CB  . LYS E  1 91  ? -8.357 -6.581   -89.851  1.00 178.76 ? 92  LYS E CB  1 
ATOM   5112  C  CG  . LYS E  1 91  ? -7.875 -7.374   -91.071  1.00 181.31 ? 92  LYS E CG  1 
ATOM   5113  C  CD  . LYS E  1 91  ? -7.834 -6.514   -92.334  1.00 185.60 ? 92  LYS E CD  1 
ATOM   5114  C  CE  . LYS E  1 91  ? -7.842 -7.382   -93.606  1.00 190.90 ? 92  LYS E CE  1 
ATOM   5115  N  NZ  . LYS E  1 91  ? -9.227 -7.721   -94.061  1.00 199.70 ? 92  LYS E NZ  1 
ATOM   5116  N  N   . ASP E  1 92  ? -7.571 -6.537   -87.052  1.00 166.02 ? 93  ASP E N   1 
ATOM   5117  C  CA  . ASP E  1 92  ? -8.003 -6.679   -85.639  1.00 164.20 ? 93  ASP E CA  1 
ATOM   5118  C  C   . ASP E  1 92  ? -7.026 -6.016   -84.650  1.00 156.76 ? 93  ASP E C   1 
ATOM   5119  O  O   . ASP E  1 92  ? -7.085 -6.285   -83.449  1.00 154.35 ? 93  ASP E O   1 
ATOM   5120  C  CB  . ASP E  1 92  ? -8.313 -8.158   -85.234  1.00 165.25 ? 93  ASP E CB  1 
ATOM   5121  C  CG  . ASP E  1 92  ? -8.026 -9.176   -86.347  1.00 167.88 ? 93  ASP E CG  1 
ATOM   5122  O  OD1 . ASP E  1 92  ? -6.833 -9.371   -86.693  1.00 163.46 ? 93  ASP E OD1 1 
ATOM   5123  O  OD2 . ASP E  1 92  ? -9.008 -9.790   -86.850  1.00 174.58 ? 93  ASP E OD2 1 
ATOM   5124  N  N   . GLY E  1 93  ? -6.143 -5.151   -85.164  1.00 153.84 ? 94  GLY E N   1 
ATOM   5125  C  CA  . GLY E  1 93  ? -5.291 -4.283   -84.338  1.00 147.82 ? 94  GLY E CA  1 
ATOM   5126  C  C   . GLY E  1 93  ? -3.877 -4.769   -84.109  1.00 141.18 ? 94  GLY E C   1 
ATOM   5127  O  O   . GLY E  1 93  ? -3.236 -4.431   -83.103  1.00 135.91 ? 94  GLY E O   1 
ATOM   5128  N  N   . VAL E  1 94  ? -3.374 -5.471   -85.130  1.00 142.32 ? 95  VAL E N   1 
ATOM   5129  C  CA  . VAL E  1 94  ? -1.944 -5.572   -85.398  1.00 137.53 ? 95  VAL E CA  1 
ATOM   5130  C  C   . VAL E  1 94  ? -1.369 -6.685   -84.590  1.00 133.51 ? 95  VAL E C   1 
ATOM   5131  O  O   . VAL E  1 94  ? -2.081 -7.644   -84.215  1.00 135.62 ? 95  VAL E O   1 
ATOM   5132  C  CB  . VAL E  1 94  ? -1.248 -4.232   -85.029  1.00 134.11 ? 95  VAL E CB  1 
ATOM   5133  N  N   . ALA E  1 95  ? -0.072 -6.582   -84.312  1.00 127.72 ? 96  ALA E N   1 
ATOM   5134  C  CA  . ALA E  1 95  ? 1.050  -6.235   -85.224  1.00 126.16 ? 96  ALA E CA  1 
ATOM   5135  C  C   . ALA E  1 95  ? 2.058  -7.303   -84.845  1.00 122.37 ? 96  ALA E C   1 
ATOM   5136  O  O   . ALA E  1 95  ? 2.626  -7.262   -83.738  1.00 117.83 ? 96  ALA E O   1 
ATOM   5137  C  CB  . ALA E  1 95  ? 1.655  -4.802   -84.968  1.00 123.08 ? 96  ALA E CB  1 
ATOM   5138  N  N   . ASP E  1 96  ? 2.248  -8.281   -85.723  1.00 124.77 ? 97  ASP E N   1 
ATOM   5139  C  CA  . ASP E  1 96  ? 3.200  -9.368   -85.452  1.00 122.31 ? 97  ASP E CA  1 
ATOM   5140  C  C   . ASP E  1 96  ? 4.627  -8.978   -85.869  1.00 119.41 ? 97  ASP E C   1 
ATOM   5141  O  O   . ASP E  1 96  ? 5.041  -9.222   -87.018  1.00 122.23 ? 97  ASP E O   1 
ATOM   5142  C  CB  . ASP E  1 96  ? 2.765  -10.663  -86.141  1.00 126.98 ? 97  ASP E CB  1 
ATOM   5143  C  CG  . ASP E  1 96  ? 1.679  -11.411  -85.348  1.00 129.37 ? 97  ASP E CG  1 
ATOM   5144  O  OD1 . ASP E  1 96  ? 1.875  -11.638  -84.127  1.00 125.79 ? 97  ASP E OD1 1 
ATOM   5145  O  OD2 . ASP E  1 96  ? 0.634  -11.783  -85.942  1.00 135.13 ? 97  ASP E OD2 1 
ATOM   5146  N  N   . VAL E  1 97  ? 5.365  -8.387   -84.916  1.00 114.29 ? 98  VAL E N   1 
ATOM   5147  C  CA  . VAL E  1 97  ? 6.702  -7.828   -85.173  1.00 111.47 ? 98  VAL E CA  1 
ATOM   5148  C  C   . VAL E  1 97  ? 7.737  -8.941   -85.432  1.00 111.08 ? 98  VAL E C   1 
ATOM   5149  O  O   . VAL E  1 97  ? 7.830  -9.939   -84.685  1.00 109.68 ? 98  VAL E O   1 
ATOM   5150  C  CB  . VAL E  1 97  ? 7.209  -6.946   -84.009  1.00 106.58 ? 98  VAL E CB  1 
ATOM   5151  C  CG1 . VAL E  1 97  ? 8.570  -6.342   -84.353  1.00 104.61 ? 98  VAL E CG1 1 
ATOM   5152  C  CG2 . VAL E  1 97  ? 6.205  -5.846   -83.699  1.00 107.66 ? 98  VAL E CG2 1 
ATOM   5153  N  N   . SER E  1 98  ? 8.491  -8.764   -86.517  1.00 112.88 ? 99  SER E N   1 
ATOM   5154  C  CA  . SER E  1 98  ? 9.659  -9.609   -86.810  1.00 112.72 ? 99  SER E CA  1 
ATOM   5155  C  C   . SER E  1 98  ? 10.689 -8.834   -87.637  1.00 113.23 ? 99  SER E C   1 
ATOM   5156  O  O   . SER E  1 98  ? 10.677 -8.860   -88.884  1.00 117.51 ? 99  SER E O   1 
ATOM   5157  C  CB  . SER E  1 98  ? 9.264  -10.890  -87.539  1.00 117.21 ? 99  SER E CB  1 
ATOM   5158  O  OG  . SER E  1 98  ? 10.437 -11.615  -87.903  1.00 117.49 ? 99  SER E OG  1 
ATOM   5159  N  N   . ILE E  1 99  ? 11.564 -8.132   -86.921  1.00 109.17 ? 100 ILE E N   1 
ATOM   5160  C  CA  . ILE E  1 99  ? 12.633 -7.349   -87.532  1.00 109.36 ? 100 ILE E CA  1 
ATOM   5161  C  C   . ILE E  1 99  ? 13.968 -8.051   -87.275  1.00 107.93 ? 100 ILE E C   1 
ATOM   5162  O  O   . ILE E  1 99  ? 14.084 -8.878   -86.365  1.00 105.79 ? 100 ILE E O   1 
ATOM   5163  C  CB  . ILE E  1 99  ? 12.649 -5.895   -86.983  1.00 106.66 ? 100 ILE E CB  1 
ATOM   5164  C  CG1 . ILE E  1 99  ? 11.354 -5.162   -87.379  1.00 109.10 ? 100 ILE E CG1 1 
ATOM   5165  C  CG2 . ILE E  1 99  ? 13.885 -5.129   -87.486  1.00 106.90 ? 100 ILE E CG2 1 
ATOM   5166  C  CD1 . ILE E  1 99  ? 11.463 -3.639   -87.273  1.00 108.48 ? 100 ILE E CD1 1 
ATOM   5167  N  N   . GLU E  1 100 ? 14.948 -7.757   -88.121  1.00 109.92 ? 101 GLU E N   1 
ATOM   5168  C  CA  . GLU E  1 100 ? 16.339 -8.116   -87.859  1.00 108.75 ? 101 GLU E CA  1 
ATOM   5169  C  C   . GLU E  1 100 ? 17.207 -6.906   -88.218  1.00 108.88 ? 101 GLU E C   1 
ATOM   5170  O  O   . GLU E  1 100 ? 17.120 -6.366   -89.325  1.00 112.51 ? 101 GLU E O   1 
ATOM   5171  C  CB  . GLU E  1 100 ? 16.747 -9.347   -88.656  1.00 112.63 ? 101 GLU E CB  1 
ATOM   5172  C  CG  . GLU E  1 100 ? 18.149 -9.842   -88.317  1.00 112.60 ? 101 GLU E CG  1 
ATOM   5173  C  CD  . GLU E  1 100 ? 18.493 -11.222  -88.928  1.00 117.32 ? 101 GLU E CD  1 
ATOM   5174  O  OE1 . GLU E  1 100 ? 19.560 -11.807  -88.574  1.00 117.06 ? 101 GLU E OE1 1 
ATOM   5175  O  OE2 . GLU E  1 100 ? 17.708 -11.728  -89.760  1.00 121.11 ? 101 GLU E OE2 1 
ATOM   5176  N  N   . ASP E  1 101 ? 18.021 -6.461   -87.264  1.00 105.41 ? 102 ASP E N   1 
ATOM   5177  C  CA  . ASP E  1 101 ? 18.784 -5.206   -87.420  1.00 105.40 ? 102 ASP E CA  1 
ATOM   5178  C  C   . ASP E  1 101 ? 20.258 -5.351   -86.987  1.00 104.52 ? 102 ASP E C   1 
ATOM   5179  O  O   . ASP E  1 101 ? 20.599 -6.110   -86.062  1.00 101.92 ? 102 ASP E O   1 
ATOM   5180  C  CB  . ASP E  1 101 ? 18.115 -4.051   -86.649  1.00 102.42 ? 102 ASP E CB  1 
ATOM   5181  C  CG  . ASP E  1 101 ? 18.630 -2.679   -87.076  1.00 103.71 ? 102 ASP E CG  1 
ATOM   5182  O  OD1 . ASP E  1 101 ? 18.345 -2.268   -88.215  1.00 107.48 ? 102 ASP E OD1 1 
ATOM   5183  O  OD2 . ASP E  1 101 ? 19.323 -2.009   -86.283  1.00 101.27 ? 102 ASP E OD2 1 
ATOM   5184  N  N   . SER E  1 102 ? 21.114 -4.588   -87.669  1.00 107.09 ? 103 SER E N   1 
ATOM   5185  C  CA  . SER E  1 102 ? 22.566 -4.653   -87.492  1.00 107.55 ? 103 SER E CA  1 
ATOM   5186  C  C   . SER E  1 102 ? 23.183 -3.390   -86.868  1.00 105.81 ? 103 SER E C   1 
ATOM   5187  O  O   . SER E  1 102 ? 24.341 -3.439   -86.440  1.00 105.79 ? 103 SER E O   1 
ATOM   5188  C  CB  . SER E  1 102 ? 23.226 -4.901   -88.845  1.00 112.99 ? 103 SER E CB  1 
ATOM   5189  O  OG  . SER E  1 102 ? 22.656 -6.030   -89.488  1.00 115.46 ? 103 SER E OG  1 
ATOM   5190  N  N   . VAL E  1 103 ? 22.441 -2.276   -86.828  1.00 104.91 ? 104 VAL E N   1 
ATOM   5191  C  CA  . VAL E  1 103 ? 22.957 -1.046   -86.217  1.00 103.77 ? 104 VAL E CA  1 
ATOM   5192  C  C   . VAL E  1 103 ? 22.798 -1.083   -84.695  1.00 99.12  ? 104 VAL E C   1 
ATOM   5193  O  O   . VAL E  1 103 ? 23.748 -0.777   -83.951  1.00 98.15  ? 104 VAL E O   1 
ATOM   5194  C  CB  . VAL E  1 103 ? 22.267 0.208    -86.756  1.00 105.51 ? 104 VAL E CB  1 
ATOM   5195  C  CG1 . VAL E  1 103 ? 22.829 1.469    -86.090  1.00 104.68 ? 104 VAL E CG1 1 
ATOM   5196  C  CG2 . VAL E  1 103 ? 22.458 0.287    -88.246  1.00 110.98 ? 104 VAL E CG2 1 
ATOM   5197  N  N   . ILE E  1 104 ? 21.603 -1.442   -84.226  1.00 96.73  ? 105 ILE E N   1 
ATOM   5198  C  CA  . ILE E  1 104 ? 21.375 -1.553   -82.778  1.00 92.52  ? 105 ILE E CA  1 
ATOM   5199  C  C   . ILE E  1 104 ? 22.223 -2.699   -82.213  1.00 91.35  ? 105 ILE E C   1 
ATOM   5200  O  O   . ILE E  1 104 ? 22.682 -3.588   -82.962  1.00 93.45  ? 105 ILE E O   1 
ATOM   5201  C  CB  . ILE E  1 104 ? 19.880 -1.784   -82.398  1.00 90.72  ? 105 ILE E CB  1 
ATOM   5202  C  CG1 . ILE E  1 104 ? 19.385 -3.137   -82.930  1.00 91.63  ? 105 ILE E CG1 1 
ATOM   5203  C  CG2 . ILE E  1 104 ? 19.019 -0.607   -82.875  1.00 92.13  ? 105 ILE E CG2 1 
ATOM   5204  C  CD1 . ILE E  1 104 ? 18.181 -3.647   -82.237  1.00 89.48  ? 105 ILE E CD1 1 
ATOM   5205  N  N   . SER E  1 105 ? 22.433 -2.658   -80.897  1.00 88.41  ? 106 SER E N   1 
ATOM   5206  C  CA  . SER E  1 105 ? 23.132 -3.734   -80.189  1.00 87.27  ? 106 SER E CA  1 
ATOM   5207  C  C   . SER E  1 105 ? 22.731 -3.835   -78.712  1.00 83.87  ? 106 SER E C   1 
ATOM   5208  O  O   . SER E  1 105 ? 22.294 -2.850   -78.062  1.00 82.29  ? 106 SER E O   1 
ATOM   5209  C  CB  . SER E  1 105 ? 24.651 -3.556   -80.292  1.00 89.08  ? 106 SER E CB  1 
ATOM   5210  O  OG  . SER E  1 105 ? 25.313 -4.717   -79.833  1.00 88.69  ? 106 SER E OG  1 
ATOM   5211  N  N   . LEU E  1 106 ? 22.910 -5.046   -78.191  1.00 83.11  ? 107 LEU E N   1 
ATOM   5212  C  CA  . LEU E  1 106 ? 22.706 -5.331   -76.764  1.00 80.39  ? 107 LEU E CA  1 
ATOM   5213  C  C   . LEU E  1 106 ? 24.017 -5.227   -75.953  1.00 80.22  ? 107 LEU E C   1 
ATOM   5214  O  O   . LEU E  1 106 ? 24.095 -5.736   -74.825  1.00 78.73  ? 107 LEU E O   1 
ATOM   5215  C  CB  . LEU E  1 106 ? 22.104 -6.729   -76.592  1.00 80.11  ? 107 LEU E CB  1 
ATOM   5216  C  CG  . LEU E  1 106 ? 20.777 -6.933   -77.302  1.00 80.50  ? 107 LEU E CG  1 
ATOM   5217  C  CD1 . LEU E  1 106 ? 20.283 -8.339   -76.998  1.00 80.81  ? 107 LEU E CD1 1 
ATOM   5218  C  CD2 . LEU E  1 106 ? 19.764 -5.861   -76.884  1.00 78.69  ? 107 LEU E CD2 1 
ATOM   5219  N  N   . SER E  1 107 ? 25.033 -4.575   -76.537  1.00 82.18  ? 108 SER E N   1 
ATOM   5220  C  CA  . SER E  1 107 ? 26.340 -4.394   -75.896  1.00 82.67  ? 108 SER E CA  1 
ATOM   5221  C  C   . SER E  1 107 ? 27.175 -3.270   -76.536  1.00 84.88  ? 108 SER E C   1 
ATOM   5222  O  O   . SER E  1 107 ? 27.200 -3.107   -77.749  1.00 87.18  ? 108 SER E O   1 
ATOM   5223  C  CB  . SER E  1 107 ? 27.129 -5.719   -75.891  1.00 84.16  ? 108 SER E CB  1 
ATOM   5224  O  OG  . SER E  1 107 ? 27.313 -6.247   -77.190  1.00 86.84  ? 108 SER E OG  1 
ATOM   5225  N  N   . GLY E  1 108 ? 27.837 -2.490   -75.692  1.00 84.70  ? 109 GLY E N   1 
ATOM   5226  C  CA  . GLY E  1 108 ? 28.788 -1.474   -76.136  1.00 87.53  ? 109 GLY E CA  1 
ATOM   5227  C  C   . GLY E  1 108 ? 28.255 -0.054   -76.363  1.00 87.80  ? 109 GLY E C   1 
ATOM   5228  O  O   . GLY E  1 108 ? 27.302 0.400    -75.729  1.00 85.45  ? 109 GLY E O   1 
ATOM   5229  N  N   . ASP E  1 109 ? 28.909 0.653    -77.280  1.00 91.25  ? 110 ASP E N   1 
ATOM   5230  C  CA  . ASP E  1 109 ? 28.563 2.044    -77.646  1.00 92.61  ? 110 ASP E CA  1 
ATOM   5231  C  C   . ASP E  1 109 ? 27.095 2.202    -78.060  1.00 90.93  ? 110 ASP E C   1 
ATOM   5232  O  O   . ASP E  1 109 ? 26.419 3.153    -77.684  1.00 89.96  ? 110 ASP E O   1 
ATOM   5233  C  CB  . ASP E  1 109 ? 29.446 2.501    -78.831  1.00 97.31  ? 110 ASP E CB  1 
ATOM   5234  C  CG  . ASP E  1 109 ? 29.659 4.038    -78.860  1.00 100.19 ? 110 ASP E CG  1 
ATOM   5235  O  OD1 . ASP E  1 109 ? 28.833 4.742    -79.517  1.00 100.86 ? 110 ASP E OD1 1 
ATOM   5236  O  OD2 . ASP E  1 109 ? 30.642 4.532    -78.218  1.00 101.83 ? 110 ASP E OD2 1 
ATOM   5237  N  N   . HIS E  1 110 ? 26.644 1.238    -78.860  1.00 90.96  ? 111 HIS E N   1 
ATOM   5238  C  CA  . HIS E  1 110 ? 25.276 1.170    -79.414  1.00 90.32  ? 111 HIS E CA  1 
ATOM   5239  C  C   . HIS E  1 110 ? 24.260 0.450    -78.482  1.00 86.63  ? 111 HIS E C   1 
ATOM   5240  O  O   . HIS E  1 110 ? 23.112 0.149    -78.887  1.00 86.07  ? 111 HIS E O   1 
ATOM   5241  C  CB  . HIS E  1 110 ? 25.312 0.409    -80.769  1.00 92.80  ? 111 HIS E CB  1 
ATOM   5242  C  CG  . HIS E  1 110 ? 26.039 1.135    -81.863  1.00 97.10  ? 111 HIS E CG  1 
ATOM   5243  N  ND1 . HIS E  1 110 ? 25.941 0.759    -83.188  1.00 100.07 ? 111 HIS E ND1 1 
ATOM   5244  C  CD2 . HIS E  1 110 ? 26.842 2.230    -81.837  1.00 99.21  ? 111 HIS E CD2 1 
ATOM   5245  C  CE1 . HIS E  1 110 ? 26.661 1.582    -83.930  1.00 103.82 ? 111 HIS E CE1 1 
ATOM   5246  N  NE2 . HIS E  1 110 ? 27.213 2.485    -83.135  1.00 103.63 ? 111 HIS E NE2 1 
ATOM   5247  N  N   . CYS E  1 111 ? 24.685 0.168    -77.250  1.00 84.43  ? 112 CYS E N   1 
ATOM   5248  C  CA  . CYS E  1 111 ? 23.872 -0.609   -76.326  1.00 81.39  ? 112 CYS E CA  1 
ATOM   5249  C  C   . CYS E  1 111 ? 22.526 0.065    -76.101  1.00 80.35  ? 112 CYS E C   1 
ATOM   5250  O  O   . CYS E  1 111 ? 22.457 1.208    -75.598  1.00 80.38  ? 112 CYS E O   1 
ATOM   5251  C  CB  . CYS E  1 111 ? 24.591 -0.776   -74.993  1.00 80.05  ? 112 CYS E CB  1 
ATOM   5252  S  SG  . CYS E  1 111 ? 23.777 -1.902   -73.850  1.00 76.94  ? 112 CYS E SG  1 
ATOM   5253  N  N   . ILE E  1 112 ? 21.465 -0.640   -76.493  1.00 79.81  ? 113 ILE E N   1 
ATOM   5254  C  CA  . ILE E  1 112 ? 20.085 -0.134   -76.310  1.00 79.49  ? 113 ILE E CA  1 
ATOM   5255  C  C   . ILE E  1 112 ? 19.461 -0.518   -74.955  1.00 77.20  ? 113 ILE E C   1 
ATOM   5256  O  O   . ILE E  1 112 ? 18.384 -0.001   -74.587  1.00 77.03  ? 113 ILE E O   1 
ATOM   5257  C  CB  . ILE E  1 112 ? 19.128 -0.606   -77.438  1.00 80.85  ? 113 ILE E CB  1 
ATOM   5258  C  CG1 . ILE E  1 112 ? 19.044 -2.147   -77.491  1.00 80.05  ? 113 ILE E CG1 1 
ATOM   5259  C  CG2 . ILE E  1 112 ? 19.567 -0.006   -78.767  1.00 83.79  ? 113 ILE E CG2 1 
ATOM   5260  C  CD1 . ILE E  1 112 ? 17.754 -2.674   -78.113  1.00 81.10  ? 113 ILE E CD1 1 
ATOM   5261  N  N   . ILE E  1 113 ? 20.132 -1.426   -74.233  1.00 75.81  ? 114 ILE E N   1 
ATOM   5262  C  CA  . ILE E  1 113 ? 19.643 -1.911   -72.939  1.00 73.80  ? 114 ILE E CA  1 
ATOM   5263  C  C   . ILE E  1 113 ? 19.609 -0.760   -71.936  1.00 73.38  ? 114 ILE E C   1 
ATOM   5264  O  O   . ILE E  1 113 ? 20.540 0.036    -71.827  1.00 73.83  ? 114 ILE E O   1 
ATOM   5265  C  CB  . ILE E  1 113 ? 20.493 -3.065   -72.380  1.00 73.02  ? 114 ILE E CB  1 
ATOM   5266  C  CG1 . ILE E  1 113 ? 20.246 -4.338   -73.190  1.00 73.83  ? 114 ILE E CG1 1 
ATOM   5267  C  CG2 . ILE E  1 113 ? 20.169 -3.320   -70.909  1.00 71.44  ? 114 ILE E CG2 1 
ATOM   5268  C  CD1 . ILE E  1 113 ? 21.219 -5.467   -72.868  1.00 74.23  ? 114 ILE E CD1 1 
ATOM   5269  N  N   . GLY E  1 114 ? 18.496 -0.671   -71.227  1.00 72.90  ? 115 GLY E N   1 
ATOM   5270  C  CA  . GLY E  1 114 ? 18.285 0.396    -70.268  1.00 73.07  ? 115 GLY E CA  1 
ATOM   5271  C  C   . GLY E  1 114 ? 17.685 1.611    -70.917  1.00 74.85  ? 115 GLY E C   1 
ATOM   5272  O  O   . GLY E  1 114 ? 17.522 2.638    -70.276  1.00 75.82  ? 115 GLY E O   1 
ATOM   5273  N  N   . ARG E  1 115 ? 17.354 1.495    -72.196  1.00 75.93  ? 116 ARG E N   1 
ATOM   5274  C  CA  . ARG E  1 115 ? 16.696 2.579    -72.916  1.00 78.35  ? 116 ARG E CA  1 
ATOM   5275  C  C   . ARG E  1 115 ? 15.258 2.192    -73.247  1.00 79.06  ? 116 ARG E C   1 
ATOM   5276  O  O   . ARG E  1 115 ? 14.856 1.040    -73.023  1.00 77.76  ? 116 ARG E O   1 
ATOM   5277  C  CB  . ARG E  1 115 ? 17.499 2.939    -74.175  1.00 79.86  ? 116 ARG E CB  1 
ATOM   5278  C  CG  . ARG E  1 115 ? 18.962 3.276    -73.867  1.00 79.68  ? 116 ARG E CG  1 
ATOM   5279  C  CD  . ARG E  1 115 ? 19.719 3.745    -75.084  1.00 81.89  ? 116 ARG E CD  1 
ATOM   5280  N  NE  . ARG E  1 115 ? 21.139 3.901    -74.798  1.00 81.80  ? 116 ARG E NE  1 
ATOM   5281  C  CZ  . ARG E  1 115 ? 21.699 4.986    -74.255  1.00 83.02  ? 116 ARG E CZ  1 
ATOM   5282  N  NH1 . ARG E  1 115 ? 20.984 6.062    -73.916  1.00 84.17  ? 116 ARG E NH1 1 
ATOM   5283  N  NH2 . ARG E  1 115 ? 23.008 4.995    -74.053  1.00 83.78  ? 116 ARG E NH2 1 
ATOM   5284  N  N   . THR E  1 116 ? 14.507 3.168    -73.773  1.00 81.54  ? 117 THR E N   1 
ATOM   5285  C  CA  . THR E  1 116 ? 13.076 3.008    -74.069  1.00 83.09  ? 117 THR E CA  1 
ATOM   5286  C  C   . THR E  1 116 ? 12.755 2.652    -75.545  1.00 84.80  ? 117 THR E C   1 
ATOM   5287  O  O   . THR E  1 116 ? 13.192 3.344    -76.475  1.00 86.50  ? 117 THR E O   1 
ATOM   5288  C  CB  . THR E  1 116 ? 12.283 4.282    -73.697  1.00 85.52  ? 117 THR E CB  1 
ATOM   5289  O  OG1 . THR E  1 116 ? 12.424 4.527    -72.301  1.00 84.29  ? 117 THR E OG1 1 
ATOM   5290  C  CG2 . THR E  1 116 ? 10.788 4.122    -74.019  1.00 87.80  ? 117 THR E CG2 1 
ATOM   5291  N  N   . LEU E  1 117 ? 11.970 1.575    -75.722  1.00 84.75  ? 118 LEU E N   1 
ATOM   5292  C  CA  . LEU E  1 117 ? 11.332 1.232    -77.005  1.00 86.95  ? 118 LEU E CA  1 
ATOM   5293  C  C   . LEU E  1 117 ? 9.990  1.956    -77.086  1.00 89.95  ? 118 LEU E C   1 
ATOM   5294  O  O   . LEU E  1 117 ? 9.315  2.141    -76.069  1.00 90.15  ? 118 LEU E O   1 
ATOM   5295  C  CB  . LEU E  1 117 ? 11.102 -0.281   -77.115  1.00 86.02  ? 118 LEU E CB  1 
ATOM   5296  C  CG  . LEU E  1 117 ? 10.561 -0.776   -78.458  1.00 88.51  ? 118 LEU E CG  1 
ATOM   5297  C  CD1 . LEU E  1 117 ? 11.531 -0.391   -79.555  1.00 89.51  ? 118 LEU E CD1 1 
ATOM   5298  C  CD2 . LEU E  1 117 ? 10.301 -2.285   -78.440  1.00 87.86  ? 118 LEU E CD2 1 
ATOM   5299  N  N   . VAL E  1 118 ? 9.593  2.361    -78.283  1.00 92.93  ? 119 VAL E N   1 
ATOM   5300  C  CA  . VAL E  1 118 ? 8.387  3.196    -78.439  1.00 96.61  ? 119 VAL E CA  1 
ATOM   5301  C  C   . VAL E  1 118 ? 7.629  2.930    -79.747  1.00 100.18 ? 119 VAL E C   1 
ATOM   5302  O  O   . VAL E  1 118 ? 8.171  3.081    -80.838  1.00 101.70 ? 119 VAL E O   1 
ATOM   5303  C  CB  . VAL E  1 118 ? 8.744  4.710    -78.396  1.00 98.25  ? 119 VAL E CB  1 
ATOM   5304  C  CG1 . VAL E  1 118 ? 7.562  5.565    -78.876  1.00 102.99 ? 119 VAL E CG1 1 
ATOM   5305  C  CG2 . VAL E  1 118 ? 9.195  5.131    -76.987  1.00 95.88  ? 119 VAL E CG2 1 
ATOM   5306  N  N   . VAL E  1 119 ? 6.368  2.548    -79.638  1.00 102.24 ? 120 VAL E N   1 
ATOM   5307  C  CA  . VAL E  1 119 ? 5.532  2.380    -80.817  1.00 106.38 ? 120 VAL E CA  1 
ATOM   5308  C  C   . VAL E  1 119 ? 4.738  3.683    -80.984  1.00 110.69 ? 120 VAL E C   1 
ATOM   5309  O  O   . VAL E  1 119 ? 4.415  4.372    -79.998  1.00 110.62 ? 120 VAL E O   1 
ATOM   5310  C  CB  . VAL E  1 119 ? 4.616  1.129    -80.722  1.00 107.04 ? 120 VAL E CB  1 
ATOM   5311  C  CG1 . VAL E  1 119 ? 3.445  1.377    -79.792  1.00 109.05 ? 120 VAL E CG1 1 
ATOM   5312  C  CG2 . VAL E  1 119 ? 4.093  0.742    -82.073  1.00 110.95 ? 120 VAL E CG2 1 
ATOM   5313  N  N   . HIS E  1 120 ? 4.441  4.017    -82.240  1.00 114.86 ? 121 HIS E N   1 
ATOM   5314  C  CA  . HIS E  1 120 ? 3.967  5.365    -82.598  1.00 119.29 ? 121 HIS E CA  1 
ATOM   5315  C  C   . HIS E  1 120 ? 2.569  5.456    -83.211  1.00 125.03 ? 121 HIS E C   1 
ATOM   5316  O  O   . HIS E  1 120 ? 2.031  4.468    -83.753  1.00 126.01 ? 121 HIS E O   1 
ATOM   5317  C  CB  . HIS E  1 120 ? 4.977  6.043    -83.530  1.00 119.98 ? 121 HIS E CB  1 
ATOM   5318  C  CG  . HIS E  1 120 ? 6.062  6.755    -82.793  1.00 116.82 ? 121 HIS E CG  1 
ATOM   5319  N  ND1 . HIS E  1 120 ? 6.128  8.134    -82.707  1.00 119.71 ? 121 HIS E ND1 1 
ATOM   5320  C  CD2 . HIS E  1 120 ? 7.090  6.278    -82.052  1.00 111.67 ? 121 HIS E CD2 1 
ATOM   5321  C  CE1 . HIS E  1 120 ? 7.175  8.478    -81.976  1.00 116.27 ? 121 HIS E CE1 1 
ATOM   5322  N  NE2 . HIS E  1 120 ? 7.767  7.371    -81.555  1.00 111.67 ? 121 HIS E NE2 1 
ATOM   5323  N  N   . GLU E  1 121 ? 2.021  6.679    -83.118  1.00 128.99 ? 122 GLU E N   1 
ATOM   5324  C  CA  . GLU E  1 121 ? 0.676  7.002    -83.602  1.00 135.29 ? 122 GLU E CA  1 
ATOM   5325  C  C   . GLU E  1 121 ? 0.541  6.727    -85.106  1.00 138.99 ? 122 GLU E C   1 
ATOM   5326  O  O   . GLU E  1 121 ? -0.253 5.858    -85.528  1.00 141.01 ? 122 GLU E O   1 
ATOM   5327  C  CB  . GLU E  1 121 ? 0.360  8.473    -83.324  1.00 139.10 ? 122 GLU E CB  1 
ATOM   5328  C  CG  . GLU E  1 121 ? -0.995 8.953    -83.910  1.00 146.92 ? 122 GLU E CG  1 
ATOM   5329  C  CD  . GLU E  1 121 ? -1.217 10.488   -83.820  1.00 152.10 ? 122 GLU E CD  1 
ATOM   5330  O  OE1 . GLU E  1 121 ? -0.245 11.235   -83.490  1.00 149.78 ? 122 GLU E OE1 1 
ATOM   5331  O  OE2 . GLU E  1 121 ? -2.372 10.940   -84.107  1.00 158.53 ? 122 GLU E OE2 1 
ATOM   5332  N  N   . LYS E  1 122 ? 1.330  7.480    -85.889  1.00 140.17 ? 123 LYS E N   1 
ATOM   5333  C  CA  . LYS E  1 122 ? 1.356  7.394    -87.364  1.00 144.07 ? 123 LYS E CA  1 
ATOM   5334  C  C   . LYS E  1 122 ? 2.518  6.524    -87.837  1.00 139.95 ? 123 LYS E C   1 
ATOM   5335  O  O   . LYS E  1 122 ? 3.328  6.032    -87.024  1.00 134.17 ? 123 LYS E O   1 
ATOM   5336  C  CB  . LYS E  1 122 ? 1.505  8.802    -88.002  1.00 148.80 ? 123 LYS E CB  1 
ATOM   5337  C  CG  . LYS E  1 122 ? 0.553  9.880    -87.468  1.00 153.41 ? 123 LYS E CG  1 
ATOM   5338  C  CD  . LYS E  1 122 ? 0.804  11.239   -88.143  1.00 158.48 ? 123 LYS E CD  1 
ATOM   5339  C  CE  . LYS E  1 122 ? -0.013 12.364   -87.466  1.00 162.80 ? 123 LYS E CE  1 
ATOM   5340  N  NZ  . LYS E  1 122 ? -0.010 13.625   -88.287  1.00 169.24 ? 123 LYS E NZ  1 
ATOM   5341  N  N   . ALA E  1 123 ? 2.607  6.370    -89.162  1.00 143.52 ? 124 ALA E N   1 
ATOM   5342  C  CA  . ALA E  1 123 ? 3.736  5.665    -89.793  1.00 140.89 ? 124 ALA E CA  1 
ATOM   5343  C  C   . ALA E  1 123 ? 4.981  6.573    -89.903  1.00 139.68 ? 124 ALA E C   1 
ATOM   5344  O  O   . ALA E  1 123 ? 4.888  7.805    -90.090  1.00 142.96 ? 124 ALA E O   1 
ATOM   5345  C  CB  . ALA E  1 123 ? 3.347  5.114    -91.161  1.00 145.58 ? 124 ALA E CB  1 
ATOM   5346  N  N   . ASP E  1 124 ? 6.144  5.944    -89.748  1.00 135.20 ? 125 ASP E N   1 
ATOM   5347  C  CA  . ASP E  1 124 ? 7.442  6.610    -89.938  1.00 134.37 ? 125 ASP E CA  1 
ATOM   5348  C  C   . ASP E  1 124 ? 7.736  6.778    -91.433  1.00 139.39 ? 125 ASP E C   1 
ATOM   5349  O  O   . ASP E  1 124 ? 7.846  5.774    -92.154  1.00 139.91 ? 125 ASP E O   1 
ATOM   5350  C  CB  . ASP E  1 124 ? 8.575  5.792    -89.269  1.00 128.27 ? 125 ASP E CB  1 
ATOM   5351  C  CG  . ASP E  1 124 ? 9.963  6.498    -89.334  1.00 127.53 ? 125 ASP E CG  1 
ATOM   5352  O  OD1 . ASP E  1 124 ? 10.059 7.628    -89.894  1.00 131.50 ? 125 ASP E OD1 1 
ATOM   5353  O  OD2 . ASP E  1 124 ? 10.961 5.914    -88.816  1.00 123.08 ? 125 ASP E OD2 1 
ATOM   5354  N  N   . ASP E  1 125 ? 7.903  8.037    -91.873  1.00 143.29 ? 126 ASP E N   1 
ATOM   5355  C  CA  . ASP E  1 125 ? 8.124  8.344    -93.305  1.00 149.04 ? 126 ASP E CA  1 
ATOM   5356  C  C   . ASP E  1 125 ? 9.561  8.016    -93.792  1.00 147.75 ? 126 ASP E C   1 
ATOM   5357  O  O   . ASP E  1 125 ? 9.942  8.324    -94.945  1.00 152.50 ? 126 ASP E O   1 
ATOM   5358  C  CB  . ASP E  1 125 ? 7.738  9.807    -93.634  1.00 154.53 ? 126 ASP E CB  1 
ATOM   5359  C  CG  . ASP E  1 125 ? 8.762  10.855   -93.101  1.00 153.14 ? 126 ASP E CG  1 
ATOM   5360  O  OD1 . ASP E  1 125 ? 9.963  10.546   -92.899  1.00 149.26 ? 126 ASP E OD1 1 
ATOM   5361  O  OD2 . ASP E  1 125 ? 8.358  12.025   -92.892  1.00 156.05 ? 126 ASP E OD2 1 
ATOM   5362  N  N   . LEU E  1 126 ? 10.350 7.416    -92.897  1.00 141.65 ? 127 LEU E N   1 
ATOM   5363  C  CA  . LEU E  1 126 ? 11.735 6.997    -93.192  1.00 140.12 ? 127 LEU E CA  1 
ATOM   5364  C  C   . LEU E  1 126 ? 12.617 8.156    -93.721  1.00 143.75 ? 127 LEU E C   1 
ATOM   5365  O  O   . LEU E  1 126 ? 13.523 7.949    -94.556  1.00 146.00 ? 127 LEU E O   1 
ATOM   5366  C  CB  . LEU E  1 126 ? 11.752 5.813    -94.171  1.00 141.76 ? 127 LEU E CB  1 
ATOM   5367  C  CG  . LEU E  1 126 ? 10.810 4.655    -93.826  1.00 139.67 ? 127 LEU E CG  1 
ATOM   5368  C  CD1 . LEU E  1 126 ? 11.113 3.467    -94.703  1.00 141.46 ? 127 LEU E CD1 1 
ATOM   5369  C  CD2 . LEU E  1 126 ? 10.908 4.263    -92.360  1.00 133.22 ? 127 LEU E CD2 1 
ATOM   5370  N  N   . GLY E  1 127 ? 12.335 9.372    -93.236  1.00 144.86 ? 128 GLY E N   1 
ATOM   5371  C  CA  . GLY E  1 127 ? 13.158 10.538   -93.546  1.00 148.09 ? 128 GLY E CA  1 
ATOM   5372  C  C   . GLY E  1 127 ? 12.959 11.100   -94.941  1.00 155.56 ? 128 GLY E C   1 
ATOM   5373  O  O   . GLY E  1 127 ? 13.553 12.127   -95.272  1.00 159.31 ? 128 GLY E O   1 
ATOM   5374  N  N   . LYS E  1 128 ? 12.103 10.464   -95.746  1.00 158.27 ? 129 LYS E N   1 
ATOM   5375  C  CA  . LYS E  1 128 ? 11.861 10.902   -97.138  1.00 166.02 ? 129 LYS E CA  1 
ATOM   5376  C  C   . LYS E  1 128 ? 10.674 11.865   -97.272  1.00 170.81 ? 129 LYS E C   1 
ATOM   5377  O  O   . LYS E  1 128 ? 10.057 11.949   -98.343  1.00 176.81 ? 129 LYS E O   1 
ATOM   5378  C  CB  . LYS E  1 128 ? 11.599 9.690    -98.036  1.00 167.49 ? 129 LYS E CB  1 
ATOM   5379  C  CG  . LYS E  1 128 ? 12.649 8.593    -97.924  1.00 163.54 ? 129 LYS E CG  1 
ATOM   5380  C  CD  . LYS E  1 128 ? 12.616 7.672    -99.153  1.00 168.01 ? 129 LYS E CD  1 
ATOM   5381  C  CE  . LYS E  1 128 ? 13.570 6.468    -99.007  1.00 164.46 ? 129 LYS E CE  1 
ATOM   5382  N  NZ  . LYS E  1 128 ? 13.826 5.750    -100.333 1.00 169.60 ? 129 LYS E NZ  1 
ATOM   5383  N  N   . GLY E  1 129 ? 10.371 12.583   -96.186  1.00 168.58 ? 130 GLY E N   1 
ATOM   5384  C  CA  . GLY E  1 129 ? 9.158  13.422   -96.078  1.00 172.56 ? 130 GLY E CA  1 
ATOM   5385  C  C   . GLY E  1 129 ? 9.291  14.777   -96.755  1.00 179.63 ? 130 GLY E C   1 
ATOM   5386  O  O   . GLY E  1 129 ? 8.288  15.354   -97.209  1.00 185.34 ? 130 GLY E O   1 
ATOM   5387  N  N   . GLY E  1 130 ? 10.528 15.281   -96.817  1.00 179.60 ? 131 GLY E N   1 
ATOM   5388  C  CA  . GLY E  1 130 ? 10.807 16.562   -97.466  1.00 186.79 ? 131 GLY E CA  1 
ATOM   5389  C  C   . GLY E  1 130 ? 10.763 17.750   -96.508  1.00 187.25 ? 131 GLY E C   1 
ATOM   5390  O  O   . GLY E  1 130 ? 11.476 18.753   -96.731  1.00 191.24 ? 131 GLY E O   1 
ATOM   5391  N  N   . ASN E  1 131 ? 9.928  17.651   -95.457  1.00 183.66 ? 132 ASN E N   1 
ATOM   5392  C  CA  . ASN E  1 131 ? 9.836  18.708   -94.440  1.00 183.91 ? 132 ASN E CA  1 
ATOM   5393  C  C   . ASN E  1 131 ? 10.985 18.622   -93.395  1.00 177.64 ? 132 ASN E C   1 
ATOM   5394  O  O   . ASN E  1 131 ? 11.795 17.653   -93.381  1.00 172.31 ? 132 ASN E O   1 
ATOM   5395  C  CB  . ASN E  1 131 ? 8.434  18.734   -93.774  1.00 183.97 ? 132 ASN E CB  1 
ATOM   5396  C  CG  . ASN E  1 131 ? 8.235  17.634   -92.689  1.00 175.93 ? 132 ASN E CG  1 
ATOM   5397  O  OD1 . ASN E  1 131 ? 9.115  16.785   -92.442  1.00 169.98 ? 132 ASN E OD1 1 
ATOM   5398  N  ND2 . ASN E  1 131 ? 7.058  17.665   -92.030  1.00 176.27 ? 132 ASN E ND2 1 
ATOM   5399  N  N   . GLU E  1 132 ? 11.034 19.648   -92.536  1.00 178.70 ? 133 GLU E N   1 
ATOM   5400  C  CA  . GLU E  1 132 ? 12.034 19.742   -91.456  1.00 173.83 ? 133 GLU E CA  1 
ATOM   5401  C  C   . GLU E  1 132 ? 11.930 18.542   -90.466  1.00 165.38 ? 133 GLU E C   1 
ATOM   5402  O  O   . GLU E  1 132 ? 12.941 17.852   -90.140  1.00 160.00 ? 133 GLU E O   1 
ATOM   5403  C  CB  . GLU E  1 132 ? 11.837 21.070   -90.683  1.00 177.43 ? 133 GLU E CB  1 
ATOM   5404  C  CG  . GLU E  1 132 ? 12.572 21.149   -89.305  1.00 172.66 ? 133 GLU E CG  1 
ATOM   5405  C  CD  . GLU E  1 132 ? 14.072 21.471   -89.423  1.00 173.29 ? 133 GLU E CD  1 
ATOM   5406  O  OE1 . GLU E  1 132 ? 14.595 21.593   -90.559  1.00 177.40 ? 133 GLU E OE1 1 
ATOM   5407  O  OE2 . GLU E  1 132 ? 14.727 21.591   -88.368  1.00 169.75 ? 133 GLU E OE2 1 
ATOM   5408  N  N   . GLU E  1 133 ? 10.695 18.326   -89.997  1.00 164.56 ? 134 GLU E N   1 
ATOM   5409  C  CA  . GLU E  1 133 ? 10.414 17.351   -88.946  1.00 157.62 ? 134 GLU E CA  1 
ATOM   5410  C  C   . GLU E  1 133 ? 10.711 15.896   -89.377  1.00 152.83 ? 134 GLU E C   1 
ATOM   5411  O  O   . GLU E  1 133 ? 11.040 15.053   -88.531  1.00 146.47 ? 134 GLU E O   1 
ATOM   5412  C  CB  . GLU E  1 133 ? 8.947  17.483   -88.478  1.00 159.34 ? 134 GLU E CB  1 
ATOM   5413  C  CG  . GLU E  1 133 ? 8.643  16.816   -87.109  1.00 153.35 ? 134 GLU E CG  1 
ATOM   5414  C  CD  . GLU E  1 133 ? 9.319  17.558   -85.917  1.00 152.22 ? 134 GLU E CD  1 
ATOM   5415  O  OE1 . GLU E  1 133 ? 9.837  18.701   -86.125  1.00 156.79 ? 134 GLU E OE1 1 
ATOM   5416  O  OE2 . GLU E  1 133 ? 9.339  17.001   -84.777  1.00 146.80 ? 134 GLU E OE2 1 
ATOM   5417  N  N   . SER E  1 134 ? 10.591 15.608   -90.675  1.00 156.21 ? 135 SER E N   1 
ATOM   5418  C  CA  . SER E  1 134 ? 10.849 14.255   -91.194  1.00 152.97 ? 135 SER E CA  1 
ATOM   5419  C  C   . SER E  1 134 ? 12.312 13.825   -91.027  1.00 149.00 ? 135 SER E C   1 
ATOM   5420  O  O   . SER E  1 134 ? 12.630 12.621   -90.966  1.00 144.58 ? 135 SER E O   1 
ATOM   5421  C  CB  . SER E  1 134 ? 10.524 14.159   -92.670  1.00 158.60 ? 135 SER E CB  1 
ATOM   5422  O  OG  . SER E  1 134 ? 10.968 12.901   -93.142  1.00 155.57 ? 135 SER E OG  1 
ATOM   5423  N  N   . THR E  1 135 ? 13.189 14.823   -90.977  1.00 151.10 ? 136 THR E N   1 
ATOM   5424  C  CA  . THR E  1 135 ? 14.615 14.620   -90.666  1.00 148.15 ? 136 THR E CA  1 
ATOM   5425  C  C   . THR E  1 135 ? 14.939 14.296   -89.171  1.00 141.83 ? 136 THR E C   1 
ATOM   5426  O  O   . THR E  1 135 ? 16.068 13.851   -88.818  1.00 138.51 ? 136 THR E O   1 
ATOM   5427  C  CB  . THR E  1 135 ? 15.412 15.875   -91.096  1.00 153.42 ? 136 THR E CB  1 
ATOM   5428  O  OG1 . THR E  1 135 ? 15.616 15.816   -92.510  1.00 158.62 ? 136 THR E OG1 1 
ATOM   5429  C  CG2 . THR E  1 135 ? 16.763 15.972   -90.395  1.00 150.35 ? 136 THR E CG2 1 
ATOM   5430  N  N   . LYS E  1 136 ? 13.946 14.493   -88.305  1.00 140.55 ? 137 LYS E N   1 
ATOM   5431  C  CA  . LYS E  1 136 ? 14.120 14.311   -86.859  1.00 135.27 ? 137 LYS E CA  1 
ATOM   5432  C  C   . LYS E  1 136 ? 13.322 13.087   -86.362  1.00 130.51 ? 137 LYS E C   1 
ATOM   5433  O  O   . LYS E  1 136 ? 13.900 12.060   -85.950  1.00 125.48 ? 137 LYS E O   1 
ATOM   5434  C  CB  . LYS E  1 136 ? 13.666 15.590   -86.122  1.00 138.08 ? 137 LYS E CB  1 
ATOM   5435  C  CG  . LYS E  1 136 ? 14.619 16.784   -86.254  1.00 142.18 ? 137 LYS E CG  1 
ATOM   5436  C  CD  . LYS E  1 136 ? 14.042 17.978   -85.481  1.00 145.76 ? 137 LYS E CD  1 
ATOM   5437  C  CE  . LYS E  1 136 ? 15.106 19.001   -85.073  1.00 147.81 ? 137 LYS E CE  1 
ATOM   5438  N  NZ  . LYS E  1 136 ? 15.306 20.019   -86.124  1.00 155.04 ? 137 LYS E NZ  1 
ATOM   5439  N  N   . THR E  1 137 ? 11.994 13.228   -86.417  1.00 132.61 ? 138 THR E N   1 
ATOM   5440  C  CA  . THR E  1 137 ? 11.061 12.298   -85.777  1.00 129.23 ? 138 THR E CA  1 
ATOM   5441  C  C   . THR E  1 137 ? 10.516 11.252   -86.780  1.00 129.77 ? 138 THR E C   1 
ATOM   5442  O  O   . THR E  1 137 ? 9.959  10.209   -86.398  1.00 126.72 ? 138 THR E O   1 
ATOM   5443  C  CB  . THR E  1 137 ? 9.883  13.088   -85.100  1.00 131.82 ? 138 THR E CB  1 
ATOM   5444  O  OG1 . THR E  1 137 ? 9.015  13.676   -86.107  1.00 138.11 ? 138 THR E OG1 1 
ATOM   5445  C  CG2 . THR E  1 137 ? 10.441 14.181   -84.177  1.00 132.12 ? 138 THR E CG2 1 
ATOM   5446  N  N   . GLY E  1 138 ? 10.664 11.550   -88.064  1.00 134.15 ? 139 GLY E N   1 
ATOM   5447  C  CA  . GLY E  1 138 ? 10.061 10.721   -89.108  1.00 136.25 ? 139 GLY E CA  1 
ATOM   5448  C  C   . GLY E  1 138 ? 8.576  11.001   -89.367  1.00 140.57 ? 139 GLY E C   1 
ATOM   5449  O  O   . GLY E  1 138 ? 7.890  10.242   -90.090  1.00 142.10 ? 139 GLY E O   1 
ATOM   5450  N  N   . ASN E  1 139 ? 8.080  12.094   -88.771  1.00 142.85 ? 140 ASN E N   1 
ATOM   5451  C  CA  . ASN E  1 139 ? 6.654  12.473   -88.840  1.00 147.37 ? 140 ASN E CA  1 
ATOM   5452  C  C   . ASN E  1 139 ? 5.683  11.339   -88.393  1.00 145.01 ? 140 ASN E C   1 
ATOM   5453  O  O   . ASN E  1 139 ? 4.484  11.303   -88.793  1.00 149.25 ? 140 ASN E O   1 
ATOM   5454  C  CB  . ASN E  1 139 ? 6.301  12.962   -90.256  1.00 154.37 ? 140 ASN E CB  1 
ATOM   5455  C  CG  . ASN E  1 139 ? 6.802  14.369   -90.539  1.00 158.71 ? 140 ASN E CG  1 
ATOM   5456  O  OD1 . ASN E  1 139 ? 7.146  14.686   -91.685  1.00 163.02 ? 140 ASN E OD1 1 
ATOM   5457  N  ND2 . ASN E  1 139 ? 6.841  15.225   -89.497  1.00 157.89 ? 140 ASN E ND2 1 
ATOM   5458  N  N   . ALA E  1 140 ? 6.190  10.447   -87.529  1.00 138.64 ? 141 ALA E N   1 
ATOM   5459  C  CA  . ALA E  1 140 ? 5.422  9.263    -87.086  1.00 136.00 ? 141 ALA E CA  1 
ATOM   5460  C  C   . ALA E  1 140 ? 4.443  9.600    -85.928  1.00 136.17 ? 141 ALA E C   1 
ATOM   5461  O  O   . ALA E  1 140 ? 3.701  8.705    -85.462  1.00 134.54 ? 141 ALA E O   1 
ATOM   5462  C  CB  . ALA E  1 140 ? 6.362  8.111    -86.698  1.00 129.65 ? 141 ALA E CB  1 
ATOM   5463  N  N   . GLY E  1 141 ? 4.462  10.867   -85.461  1.00 138.25 ? 142 GLY E N   1 
ATOM   5464  C  CA  . GLY E  1 141 ? 3.456  11.363   -84.522  1.00 140.17 ? 142 GLY E CA  1 
ATOM   5465  C  C   . GLY E  1 141 ? 3.665  10.958   -83.064  1.00 134.93 ? 142 GLY E C   1 
ATOM   5466  O  O   . GLY E  1 141 ? 4.787  10.624   -82.634  1.00 129.74 ? 142 GLY E O   1 
ATOM   5467  N  N   . SER E  1 142 ? 2.559  10.968   -82.313  1.00 136.71 ? 143 SER E N   1 
ATOM   5468  C  CA  . SER E  1 142 ? 2.587  10.792   -80.847  1.00 133.12 ? 143 SER E CA  1 
ATOM   5469  C  C   . SER E  1 142 ? 3.052  9.376    -80.420  1.00 126.93 ? 143 SER E C   1 
ATOM   5470  O  O   . SER E  1 142 ? 3.162  8.431    -81.250  1.00 125.68 ? 143 SER E O   1 
ATOM   5471  C  CB  . SER E  1 142 ? 1.206  11.117   -80.220  1.00 137.45 ? 143 SER E CB  1 
ATOM   5472  O  OG  . SER E  1 142 ? 0.248  10.067   -80.429  1.00 138.29 ? 143 SER E OG  1 
ATOM   5473  N  N   . ARG E  1 143 ? 3.297  9.257    -79.111  1.00 123.39 ? 144 ARG E N   1 
ATOM   5474  C  CA  . ARG E  1 143 ? 3.791  8.013    -78.512  1.00 117.76 ? 144 ARG E CA  1 
ATOM   5475  C  C   . ARG E  1 143 ? 2.685  7.225    -77.832  1.00 118.20 ? 144 ARG E C   1 
ATOM   5476  O  O   . ARG E  1 143 ? 2.262  7.566    -76.714  1.00 118.78 ? 144 ARG E O   1 
ATOM   5477  C  CB  . ARG E  1 143 ? 4.881  8.327    -77.501  1.00 113.89 ? 144 ARG E CB  1 
ATOM   5478  C  CG  . ARG E  1 143 ? 6.057  9.021    -78.158  1.00 113.73 ? 144 ARG E CG  1 
ATOM   5479  C  CD  . ARG E  1 143 ? 7.102  9.478    -77.160  1.00 110.99 ? 144 ARG E CD  1 
ATOM   5480  N  NE  . ARG E  1 143 ? 8.119  10.311   -77.813  1.00 111.79 ? 144 ARG E NE  1 
ATOM   5481  C  CZ  . ARG E  1 143 ? 9.182  10.817   -77.198  1.00 110.23 ? 144 ARG E CZ  1 
ATOM   5482  N  NH1 . ARG E  1 143 ? 9.391  10.572   -75.902  1.00 107.62 ? 144 ARG E NH1 1 
ATOM   5483  N  NH2 . ARG E  1 143 ? 10.042 11.565   -77.882  1.00 112.15 ? 144 ARG E NH2 1 
ATOM   5484  N  N   . LEU E  1 144 ? 2.246  6.159    -78.507  1.00 118.30 ? 145 LEU E N   1 
ATOM   5485  C  CA  . LEU E  1 144 ? 1.054  5.374    -78.081  1.00 120.10 ? 145 LEU E CA  1 
ATOM   5486  C  C   . LEU E  1 144 ? 1.327  4.466    -76.886  1.00 115.72 ? 145 LEU E C   1 
ATOM   5487  O  O   . LEU E  1 144 ? 0.560  4.420    -75.901  1.00 117.13 ? 145 LEU E O   1 
ATOM   5488  C  CB  . LEU E  1 144 ? 0.514  4.493    -79.230  1.00 122.24 ? 145 LEU E CB  1 
ATOM   5489  C  CG  . LEU E  1 144 ? -0.128 5.209    -80.443  1.00 128.11 ? 145 LEU E CG  1 
ATOM   5490  C  CD1 . LEU E  1 144 ? -0.779 4.216    -81.442  1.00 130.36 ? 145 LEU E CD1 1 
ATOM   5491  C  CD2 . LEU E  1 144 ? -1.145 6.258    -79.976  1.00 133.08 ? 145 LEU E CD2 1 
ATOM   5492  N  N   . ALA E  1 145 ? 2.408  3.715    -77.004  1.00 111.00 ? 146 ALA E N   1 
ATOM   5493  C  CA  . ALA E  1 145 ? 2.807  2.791    -75.945  1.00 107.06 ? 146 ALA E CA  1 
ATOM   5494  C  C   . ALA E  1 145 ? 4.342  2.656    -75.915  1.00 102.35 ? 146 ALA E C   1 
ATOM   5495  O  O   . ALA E  1 145 ? 5.008  2.722    -76.972  1.00 102.31 ? 146 ALA E O   1 
ATOM   5496  C  CB  . ALA E  1 145 ? 2.107  1.406    -76.134  1.00 107.44 ? 146 ALA E CB  1 
ATOM   5497  N  N   . CYS E  1 146 ? 4.905  2.485    -74.718  1.00 98.95  ? 147 CYS E N   1 
ATOM   5498  C  CA  . CYS E  1 146 ? 6.354  2.358    -74.591  1.00 94.80  ? 147 CYS E CA  1 
ATOM   5499  C  C   . CYS E  1 146 ? 6.729  1.537    -73.384  1.00 91.69  ? 147 CYS E C   1 
ATOM   5500  O  O   . CYS E  1 146 ? 5.889  1.221    -72.540  1.00 92.70  ? 147 CYS E O   1 
ATOM   5501  C  CB  . CYS E  1 146 ? 7.017  3.735    -74.515  1.00 95.09  ? 147 CYS E CB  1 
ATOM   5502  S  SG  . CYS E  1 146 ? 6.527  4.656    -73.086  1.00 96.17  ? 147 CYS E SG  1 
ATOM   5503  N  N   . GLY E  1 147 ? 8.009  1.192    -73.325  1.00 88.52  ? 148 GLY E N   1 
ATOM   5504  C  CA  . GLY E  1 147 ? 8.554  0.434    -72.206  1.00 85.70  ? 148 GLY E CA  1 
ATOM   5505  C  C   . GLY E  1 147 ? 10.070 0.480    -72.189  1.00 82.84  ? 148 GLY E C   1 
ATOM   5506  O  O   . GLY E  1 147 ? 10.694 0.626    -73.244  1.00 82.79  ? 148 GLY E O   1 
ATOM   5507  N  N   . VAL E  1 148 ? 10.654 0.343    -70.994  1.00 80.82  ? 149 VAL E N   1 
ATOM   5508  C  CA  . VAL E  1 148 ? 12.116 0.303    -70.848  1.00 78.31  ? 149 VAL E CA  1 
ATOM   5509  C  C   . VAL E  1 148 ? 12.663 -1.084   -71.194  1.00 76.61  ? 149 VAL E C   1 
ATOM   5510  O  O   . VAL E  1 148 ? 12.106 -2.116   -70.785  1.00 76.33  ? 149 VAL E O   1 
ATOM   5511  C  CB  . VAL E  1 148 ? 12.554 0.680    -69.444  1.00 77.36  ? 149 VAL E CB  1 
ATOM   5512  C  CG1 . VAL E  1 148 ? 14.060 0.622    -69.352  1.00 75.43  ? 149 VAL E CG1 1 
ATOM   5513  C  CG2 . VAL E  1 148 ? 12.058 2.087    -69.095  1.00 79.57  ? 149 VAL E CG2 1 
ATOM   5514  N  N   . ILE E  1 149 ? 13.750 -1.092   -71.959  1.00 75.96  ? 150 ILE E N   1 
ATOM   5515  C  CA  . ILE E  1 149 ? 14.341 -2.343   -72.453  1.00 75.30  ? 150 ILE E CA  1 
ATOM   5516  C  C   . ILE E  1 149 ? 15.200 -2.989   -71.377  1.00 73.40  ? 150 ILE E C   1 
ATOM   5517  O  O   . ILE E  1 149 ? 16.126 -2.365   -70.866  1.00 72.62  ? 150 ILE E O   1 
ATOM   5518  C  CB  . ILE E  1 149 ? 15.225 -2.133   -73.708  1.00 76.02  ? 150 ILE E CB  1 
ATOM   5519  C  CG1 . ILE E  1 149 ? 14.367 -1.733   -74.914  1.00 78.25  ? 150 ILE E CG1 1 
ATOM   5520  C  CG2 . ILE E  1 149 ? 16.026 -3.424   -74.025  1.00 75.35  ? 150 ILE E CG2 1 
ATOM   5521  C  CD1 . ILE E  1 149 ? 15.169 -1.296   -76.098  1.00 79.57  ? 150 ILE E CD1 1 
ATOM   5522  N  N   . GLY E  1 150 ? 14.908 -4.248   -71.066  1.00 73.12  ? 151 GLY E N   1 
ATOM   5523  C  CA  . GLY E  1 150 ? 15.513 -4.902   -69.917  1.00 71.91  ? 151 GLY E CA  1 
ATOM   5524  C  C   . GLY E  1 150 ? 16.194 -6.193   -70.241  1.00 71.86  ? 151 GLY E C   1 
ATOM   5525  O  O   . GLY E  1 150 ? 15.838 -6.856   -71.199  1.00 73.05  ? 151 GLY E O   1 
ATOM   5526  N  N   . ILE E  1 151 ? 17.170 -6.546   -69.416  1.00 71.07  ? 152 ILE E N   1 
ATOM   5527  C  CA  . ILE E  1 151 ? 17.934 -7.786   -69.593  1.00 71.61  ? 152 ILE E CA  1 
ATOM   5528  C  C   . ILE E  1 151 ? 17.036 -8.988   -69.286  1.00 72.57  ? 152 ILE E C   1 
ATOM   5529  O  O   . ILE E  1 151 ? 16.368 -9.024   -68.253  1.00 72.45  ? 152 ILE E O   1 
ATOM   5530  C  CB  . ILE E  1 151 ? 19.185 -7.847   -68.676  1.00 71.02  ? 152 ILE E CB  1 
ATOM   5531  C  CG1 . ILE E  1 151 ? 20.134 -6.686   -68.994  1.00 70.71  ? 152 ILE E CG1 1 
ATOM   5532  C  CG2 . ILE E  1 151 ? 19.895 -9.191   -68.819  1.00 71.92  ? 152 ILE E CG2 1 
ATOM   5533  C  CD1 . ILE E  1 151 ? 21.369 -6.655   -68.126  1.00 70.79  ? 152 ILE E CD1 1 
ATOM   5534  N  N   . ALA E  1 152 ? 17.045 -9.971   -70.179  1.00 74.02  ? 153 ALA E N   1 
ATOM   5535  C  CA  . ALA E  1 152 ? 16.162 -11.127  -70.072  1.00 75.54  ? 153 ALA E CA  1 
ATOM   5536  C  C   . ALA E  1 152 ? 16.934 -12.407  -69.865  1.00 76.93  ? 153 ALA E C   1 
ATOM   5537  O  O   . ALA E  1 152 ? 18.132 -12.490  -70.177  1.00 76.96  ? 153 ALA E O   1 
ATOM   5538  C  CB  . ALA E  1 152 ? 15.351 -11.249  -71.294  1.00 77.19  ? 153 ALA E CB  1 
ATOM   5539  N  N   . GLN E  1 153 ? 16.243 -13.417  -69.352  1.00 78.54  ? 154 GLN E N   1 
ATOM   5540  C  CA  . GLN E  1 153 ? 16.893 -14.712  -69.087  1.00 80.79  ? 154 GLN E CA  1 
ATOM   5541  C  C   . GLN E  1 153 ? 17.155 -15.497  -70.373  1.00 83.36  ? 154 GLN E C   1 
ATOM   5542  O  O   . GLN E  1 153 ? 16.257 -15.574  -71.236  1.00 84.69  ? 154 GLN E O   1 
ATOM   5543  C  CB  . GLN E  1 153 ? 16.064 -15.592  -68.144  1.00 82.47  ? 154 GLN E CB  1 
ATOM   5544  C  CG  . GLN E  1 153 ? 16.759 -16.953  -67.808  1.00 85.13  ? 154 GLN E CG  1 
ATOM   5545  C  CD  . GLN E  1 153 ? 15.999 -17.785  -66.738  1.00 87.34  ? 154 GLN E CD  1 
ATOM   5546  O  OE1 . GLN E  1 153 ? 15.841 -17.359  -65.583  1.00 86.39  ? 154 GLN E OE1 1 
ATOM   5547  N  NE2 . GLN E  1 153 ? 15.539 -18.977  -67.126  1.00 90.48  ? 154 GLN E NE2 1 
ATOM   5548  O  OXT . GLN E  1 153 ? 18.245 -16.082  -70.553  1.00 84.62  ? 154 GLN E OXT 1 
ATOM   5549  N  N   . ALA F  1 1   ? 28.924 12.293   -63.581  1.00 92.96  ? 2   ALA F N   1 
ATOM   5550  C  CA  . ALA F  1 1   ? 28.878 11.600   -64.910  1.00 93.00  ? 2   ALA F CA  1 
ATOM   5551  C  C   . ALA F  1 1   ? 27.539 10.829   -65.151  1.00 88.81  ? 2   ALA F C   1 
ATOM   5552  O  O   . ALA F  1 1   ? 26.595 11.382   -65.756  1.00 90.71  ? 2   ALA F O   1 
ATOM   5553  C  CB  . ALA F  1 1   ? 30.125 10.676   -65.102  1.00 92.59  ? 2   ALA F CB  1 
ATOM   5554  N  N   . THR F  1 2   ? 27.447 9.579    -64.684  1.00 83.50  ? 3   THR F N   1 
ATOM   5555  C  CA  . THR F  1 2   ? 26.312 8.697    -65.050  1.00 79.87  ? 3   THR F CA  1 
ATOM   5556  C  C   . THR F  1 2   ? 25.137 8.822    -64.079  1.00 76.75  ? 3   THR F C   1 
ATOM   5557  O  O   . THR F  1 2   ? 25.321 8.918    -62.862  1.00 74.99  ? 3   THR F O   1 
ATOM   5558  C  CB  . THR F  1 2   ? 26.718 7.191    -65.136  1.00 76.93  ? 3   THR F CB  1 
ATOM   5559  O  OG1 . THR F  1 2   ? 28.126 7.077    -65.380  1.00 79.42  ? 3   THR F OG1 1 
ATOM   5560  C  CG2 . THR F  1 2   ? 25.935 6.461    -66.254  1.00 76.26  ? 3   THR F CG2 1 
ATOM   5561  N  N   . LYS F  1 3   ? 23.934 8.815    -64.641  1.00 76.50  ? 4   LYS F N   1 
ATOM   5562  C  CA  . LYS F  1 3   ? 22.693 8.867    -63.859  1.00 74.13  ? 4   LYS F CA  1 
ATOM   5563  C  C   . LYS F  1 3   ? 21.744 7.805    -64.370  1.00 71.76  ? 4   LYS F C   1 
ATOM   5564  O  O   . LYS F  1 3   ? 21.776 7.446    -65.550  1.00 73.53  ? 4   LYS F O   1 
ATOM   5565  C  CB  . LYS F  1 3   ? 22.014 10.240   -63.978  1.00 77.82  ? 4   LYS F CB  1 
ATOM   5566  C  CG  . LYS F  1 3   ? 22.796 11.409   -63.356  1.00 81.02  ? 4   LYS F CG  1 
ATOM   5567  C  CD  . LYS F  1 3   ? 21.935 12.690   -63.308  1.00 84.80  ? 4   LYS F CD  1 
ATOM   5568  C  CE  . LYS F  1 3   ? 22.783 13.990   -63.305  1.00 89.87  ? 4   LYS F CE  1 
ATOM   5569  N  NZ  . LYS F  1 3   ? 22.018 15.198   -63.842  1.00 94.38  ? 4   LYS F NZ  1 
ATOM   5570  N  N   . ALA F  1 4   ? 20.908 7.299    -63.477  1.00 68.34  ? 5   ALA F N   1 
ATOM   5571  C  CA  . ALA F  1 4   ? 19.841 6.376    -63.858  1.00 66.71  ? 5   ALA F CA  1 
ATOM   5572  C  C   . ALA F  1 4   ? 18.594 6.706    -63.057  1.00 65.83  ? 5   ALA F C   1 
ATOM   5573  O  O   . ALA F  1 4   ? 18.660 7.462    -62.082  1.00 65.81  ? 5   ALA F O   1 
ATOM   5574  C  CB  . ALA F  1 4   ? 20.257 4.925    -63.634  1.00 63.38  ? 5   ALA F CB  1 
ATOM   5575  N  N   . VAL F  1 5   ? 17.460 6.153    -63.482  1.00 65.66  ? 6   VAL F N   1 
ATOM   5576  C  CA  . VAL F  1 5   ? 16.172 6.375    -62.797  1.00 65.26  ? 6   VAL F CA  1 
ATOM   5577  C  C   . VAL F  1 5   ? 15.288 5.156    -62.947  1.00 63.47  ? 6   VAL F C   1 
ATOM   5578  O  O   . VAL F  1 5   ? 15.480 4.363    -63.868  1.00 63.76  ? 6   VAL F O   1 
ATOM   5579  C  CB  . VAL F  1 5   ? 15.425 7.616    -63.349  1.00 69.66  ? 6   VAL F CB  1 
ATOM   5580  C  CG1 . VAL F  1 5   ? 14.792 7.316    -64.696  1.00 72.60  ? 6   VAL F CG1 1 
ATOM   5581  C  CG2 . VAL F  1 5   ? 14.366 8.075    -62.378  1.00 69.71  ? 6   VAL F CG2 1 
ATOM   5582  N  N   . CYS F  1 6   ? 14.334 5.006    -62.038  1.00 62.09  ? 7   CYS F N   1 
ATOM   5583  C  CA  . CYS F  1 6   ? 13.411 3.868    -62.079  1.00 61.14  ? 7   CYS F CA  1 
ATOM   5584  C  C   . CYS F  1 6   ? 12.070 4.214    -61.472  1.00 62.28  ? 7   CYS F C   1 
ATOM   5585  O  O   . CYS F  1 6   ? 12.009 4.671    -60.325  1.00 61.21  ? 7   CYS F O   1 
ATOM   5586  C  CB  . CYS F  1 6   ? 13.964 2.664    -61.320  1.00 57.29  ? 7   CYS F CB  1 
ATOM   5587  S  SG  . CYS F  1 6   ? 12.744 1.292    -61.090  1.00 55.59  ? 7   CYS F SG  1 
ATOM   5588  N  N   . VAL F  1 7   ? 11.001 3.966    -62.235  1.00 64.89  ? 8   VAL F N   1 
ATOM   5589  C  CA  . VAL F  1 7   ? 9.623  4.165    -61.762  1.00 66.38  ? 8   VAL F CA  1 
ATOM   5590  C  C   . VAL F  1 7   ? 9.054  2.855    -61.219  1.00 64.17  ? 8   VAL F C   1 
ATOM   5591  O  O   . VAL F  1 7   ? 8.743  1.918    -61.970  1.00 64.66  ? 8   VAL F O   1 
ATOM   5592  C  CB  . VAL F  1 7   ? 8.714  4.705    -62.869  1.00 71.35  ? 8   VAL F CB  1 
ATOM   5593  C  CG1 . VAL F  1 7   ? 7.244  4.721    -62.419  1.00 73.38  ? 8   VAL F CG1 1 
ATOM   5594  C  CG2 . VAL F  1 7   ? 9.165  6.099    -63.269  1.00 74.04  ? 8   VAL F CG2 1 
ATOM   5595  N  N   . LEU F  1 8   ? 8.933  2.815    -59.896  1.00 61.94  ? 9   LEU F N   1 
ATOM   5596  C  CA  . LEU F  1 8   ? 8.384  1.664    -59.181  1.00 60.05  ? 9   LEU F CA  1 
ATOM   5597  C  C   . LEU F  1 8   ? 6.866  1.666    -59.262  1.00 63.26  ? 9   LEU F C   1 
ATOM   5598  O  O   . LEU F  1 8   ? 6.223  2.655    -58.890  1.00 65.48  ? 9   LEU F O   1 
ATOM   5599  C  CB  . LEU F  1 8   ? 8.810  1.700    -57.712  1.00 56.97  ? 9   LEU F CB  1 
ATOM   5600  C  CG  . LEU F  1 8   ? 10.289 1.429    -57.449  1.00 53.67  ? 9   LEU F CG  1 
ATOM   5601  C  CD1 . LEU F  1 8   ? 10.690 1.917    -56.077  1.00 51.76  ? 9   LEU F CD1 1 
ATOM   5602  C  CD2 . LEU F  1 8   ? 10.574 -0.048   -57.615  1.00 51.84  ? 9   LEU F CD2 1 
ATOM   5603  N  N   . LYS F  1 9   ? 6.308  0.555    -59.743  1.00 64.02  ? 10  LYS F N   1 
ATOM   5604  C  CA  . LYS F  1 9   ? 4.846  0.371    -59.855  1.00 67.66  ? 10  LYS F CA  1 
ATOM   5605  C  C   . LYS F  1 9   ? 4.430  -1.069   -59.616  1.00 67.00  ? 10  LYS F C   1 
ATOM   5606  O  O   . LYS F  1 9   ? 5.231  -1.991   -59.742  1.00 64.75  ? 10  LYS F O   1 
ATOM   5607  C  CB  . LYS F  1 9   ? 4.349  0.754    -61.242  1.00 72.21  ? 10  LYS F CB  1 
ATOM   5608  C  CG  . LYS F  1 9   ? 4.074  2.245    -61.423  1.00 75.86  ? 10  LYS F CG  1 
ATOM   5609  C  CD  . LYS F  1 9   ? 3.010  2.495    -62.525  1.00 81.95  ? 10  LYS F CD  1 
ATOM   5610  C  CE  . LYS F  1 9   ? 2.963  3.965    -62.980  1.00 85.23  ? 10  LYS F CE  1 
ATOM   5611  N  NZ  . LYS F  1 9   ? 2.121  4.810    -62.069  1.00 87.10  ? 10  LYS F NZ  1 
ATOM   5612  N  N   . GLY F  1 10  ? 3.160  -1.271   -59.303  1.00 69.73  ? 11  GLY F N   1 
ATOM   5613  C  CA  . GLY F  1 10  ? 2.672  -2.618   -59.027  1.00 69.77  ? 11  GLY F CA  1 
ATOM   5614  C  C   . GLY F  1 10  ? 1.161  -2.793   -59.038  1.00 74.39  ? 11  GLY F C   1 
ATOM   5615  O  O   . GLY F  1 10  ? 0.405  -1.870   -59.315  1.00 77.92  ? 11  GLY F O   1 
ATOM   5616  N  N   . ASP F  1 11  ? 0.741  -4.001   -58.683  1.00 74.71  ? 12  ASP F N   1 
ATOM   5617  C  CA  . ASP F  1 11  ? -0.668 -4.384   -58.659  1.00 79.38  ? 12  ASP F CA  1 
ATOM   5618  C  C   . ASP F  1 11  ? -1.488 -3.568   -57.654  1.00 80.69  ? 12  ASP F C   1 
ATOM   5619  O  O   . ASP F  1 11  ? -2.654 -3.276   -57.897  1.00 85.79  ? 12  ASP F O   1 
ATOM   5620  C  CB  . ASP F  1 11  ? -0.817 -5.892   -58.353  1.00 79.24  ? 12  ASP F CB  1 
ATOM   5621  C  CG  . ASP F  1 11  ? -0.815 -6.745   -59.610  1.00 82.38  ? 12  ASP F CG  1 
ATOM   5622  O  OD1 . ASP F  1 11  ? -1.503 -6.354   -60.581  1.00 87.51  ? 12  ASP F OD1 1 
ATOM   5623  O  OD2 . ASP F  1 11  ? -0.139 -7.799   -59.637  1.00 80.83  ? 12  ASP F OD2 1 
ATOM   5624  N  N   . GLY F  1 12  ? -0.881 -3.208   -56.530  1.00 76.68  ? 13  GLY F N   1 
ATOM   5625  C  CA  . GLY F  1 12  ? -1.576 -2.500   -55.461  1.00 77.79  ? 13  GLY F CA  1 
ATOM   5626  C  C   . GLY F  1 12  ? -1.120 -1.058   -55.377  1.00 77.13  ? 13  GLY F C   1 
ATOM   5627  O  O   . GLY F  1 12  ? -0.565 -0.526   -56.354  1.00 77.07  ? 13  GLY F O   1 
ATOM   5628  N  N   . PRO F  1 13  ? -1.319 -0.428   -54.196  1.00 76.84  ? 14  PRO F N   1 
ATOM   5629  C  CA  . PRO F  1 13  ? -1.207 1.022    -54.025  1.00 78.03  ? 14  PRO F CA  1 
ATOM   5630  C  C   . PRO F  1 13  ? 0.208  1.529    -53.992  1.00 73.90  ? 14  PRO F C   1 
ATOM   5631  O  O   . PRO F  1 13  ? 0.441  2.735    -54.116  1.00 75.16  ? 14  PRO F O   1 
ATOM   5632  C  CB  . PRO F  1 13  ? -1.820 1.247    -52.656  1.00 79.06  ? 14  PRO F CB  1 
ATOM   5633  C  CG  . PRO F  1 13  ? -1.549 0.014    -51.905  1.00 75.56  ? 14  PRO F CG  1 
ATOM   5634  C  CD  . PRO F  1 13  ? -1.494 -1.108   -52.899  1.00 75.15  ? 14  PRO F CD  1 
ATOM   5635  N  N   . VAL F  1 14  ? 1.138  0.604    -53.800  1.00 69.54  ? 15  VAL F N   1 
ATOM   5636  C  CA  . VAL F  1 14  ? 2.549  0.943    -53.684  1.00 65.57  ? 15  VAL F CA  1 
ATOM   5637  C  C   . VAL F  1 14  ? 3.077  1.464    -55.011  1.00 66.17  ? 15  VAL F C   1 
ATOM   5638  O  O   . VAL F  1 14  ? 2.955  0.805    -56.058  1.00 66.89  ? 15  VAL F O   1 
ATOM   5639  C  CB  . VAL F  1 14  ? 3.406  -0.264   -53.237  1.00 61.27  ? 15  VAL F CB  1 
ATOM   5640  C  CG1 . VAL F  1 14  ? 4.839  0.182    -53.000  1.00 57.79  ? 15  VAL F CG1 1 
ATOM   5641  C  CG2 . VAL F  1 14  ? 2.814  -0.919   -51.986  1.00 61.03  ? 15  VAL F CG2 1 
ATOM   5642  N  N   . GLN F  1 15  ? 3.637  2.666    -54.948  1.00 66.32  ? 16  GLN F N   1 
ATOM   5643  C  CA  . GLN F  1 15  ? 4.278  3.283    -56.105  1.00 67.23  ? 16  GLN F CA  1 
ATOM   5644  C  C   . GLN F  1 15  ? 5.324  4.304    -55.687  1.00 65.88  ? 16  GLN F C   1 
ATOM   5645  O  O   . GLN F  1 15  ? 5.326  4.778    -54.549  1.00 65.55  ? 16  GLN F O   1 
ATOM   5646  C  CB  . GLN F  1 15  ? 3.239  3.919    -57.055  1.00 72.62  ? 16  GLN F CB  1 
ATOM   5647  C  CG  . GLN F  1 15  ? 2.249  4.900    -56.404  1.00 76.66  ? 16  GLN F CG  1 
ATOM   5648  C  CD  . GLN F  1 15  ? 1.359  5.645    -57.423  1.00 82.82  ? 16  GLN F CD  1 
ATOM   5649  O  OE1 . GLN F  1 15  ? 0.867  6.744    -57.137  1.00 86.63  ? 16  GLN F OE1 1 
ATOM   5650  N  NE2 . GLN F  1 15  ? 1.151  5.045    -58.606  1.00 83.96  ? 16  GLN F NE2 1 
ATOM   5651  N  N   . GLY F  1 16  ? 6.212  4.629    -56.619  1.00 65.60  ? 17  GLY F N   1 
ATOM   5652  C  CA  . GLY F  1 16  ? 7.273  5.583    -56.351  1.00 64.93  ? 17  GLY F CA  1 
ATOM   5653  C  C   . GLY F  1 16  ? 8.242  5.800    -57.499  1.00 64.99  ? 17  GLY F C   1 
ATOM   5654  O  O   . GLY F  1 16  ? 8.135  5.182    -58.565  1.00 65.39  ? 17  GLY F O   1 
ATOM   5655  N  N   . ILE F  1 17  ? 9.185  6.706    -57.254  1.00 64.98  ? 18  ILE F N   1 
ATOM   5656  C  CA  . ILE F  1 17  ? 10.278 7.031    -58.166  1.00 65.18  ? 18  ILE F CA  1 
ATOM   5657  C  C   . ILE F  1 17  ? 11.602 6.981    -57.425  1.00 62.22  ? 18  ILE F C   1 
ATOM   5658  O  O   . ILE F  1 17  ? 11.730 7.600    -56.374  1.00 62.63  ? 18  ILE F O   1 
ATOM   5659  C  CB  . ILE F  1 17  ? 10.132 8.458    -58.690  1.00 69.87  ? 18  ILE F CB  1 
ATOM   5660  C  CG1 . ILE F  1 17  ? 9.151  8.494    -59.862  1.00 73.59  ? 18  ILE F CG1 1 
ATOM   5661  C  CG2 . ILE F  1 17  ? 11.496 9.035    -59.097  1.00 70.09  ? 18  ILE F CG2 1 
ATOM   5662  C  CD1 . ILE F  1 17  ? 9.186  9.812    -60.629  1.00 78.61  ? 18  ILE F CD1 1 
ATOM   5663  N  N   . ILE F  1 18  ? 12.582 6.266    -57.970  1.00 60.02  ? 19  ILE F N   1 
ATOM   5664  C  CA  . ILE F  1 18  ? 13.909 6.180    -57.362  1.00 57.82  ? 19  ILE F CA  1 
ATOM   5665  C  C   . ILE F  1 18  ? 14.982 6.595    -58.348  1.00 59.22  ? 19  ILE F C   1 
ATOM   5666  O  O   . ILE F  1 18  ? 15.010 6.126    -59.475  1.00 59.76  ? 19  ILE F O   1 
ATOM   5667  C  CB  . ILE F  1 18  ? 14.225 4.757    -56.868  1.00 53.97  ? 19  ILE F CB  1 
ATOM   5668  C  CG1 . ILE F  1 18  ? 13.323 4.381    -55.694  1.00 52.87  ? 19  ILE F CG1 1 
ATOM   5669  C  CG2 . ILE F  1 18  ? 15.669 4.634    -56.442  1.00 52.34  ? 19  ILE F CG2 1 
ATOM   5670  C  CD1 . ILE F  1 18  ? 13.568 5.188    -54.434  1.00 53.38  ? 19  ILE F CD1 1 
ATOM   5671  N  N   . ASN F  1 19  ? 15.869 7.477    -57.902  1.00 60.38  ? 20  ASN F N   1 
ATOM   5672  C  CA  . ASN F  1 19  ? 17.000 7.951    -58.708  1.00 62.23  ? 20  ASN F CA  1 
ATOM   5673  C  C   . ASN F  1 19  ? 18.332 7.310    -58.357  1.00 60.07  ? 20  ASN F C   1 
ATOM   5674  O  O   . ASN F  1 19  ? 18.578 6.937    -57.212  1.00 58.05  ? 20  ASN F O   1 
ATOM   5675  C  CB  . ASN F  1 19  ? 17.173 9.445    -58.531  1.00 65.98  ? 20  ASN F CB  1 
ATOM   5676  C  CG  . ASN F  1 19  ? 15.999 10.191   -59.005  1.00 69.41  ? 20  ASN F CG  1 
ATOM   5677  O  OD1 . ASN F  1 19  ? 15.170 10.637   -58.199  1.00 70.57  ? 20  ASN F OD1 1 
ATOM   5678  N  ND2 . ASN F  1 19  ? 15.877 10.319   -60.332  1.00 71.60  ? 20  ASN F ND2 1 
ATOM   5679  N  N   . PHE F  1 20  ? 19.202 7.218    -59.353  1.00 61.13  ? 21  PHE F N   1 
ATOM   5680  C  CA  . PHE F  1 20  ? 20.574 6.750    -59.158  1.00 60.01  ? 21  PHE F CA  1 
ATOM   5681  C  C   . PHE F  1 20  ? 21.543 7.795    -59.690  1.00 63.76  ? 21  PHE F C   1 
ATOM   5682  O  O   . PHE F  1 20  ? 21.255 8.475    -60.686  1.00 66.89  ? 21  PHE F O   1 
ATOM   5683  C  CB  . PHE F  1 20  ? 20.815 5.429    -59.895  1.00 58.20  ? 21  PHE F CB  1 
ATOM   5684  C  CG  . PHE F  1 20  ? 19.953 4.290    -59.419  1.00 54.98  ? 21  PHE F CG  1 
ATOM   5685  C  CD1 . PHE F  1 20  ? 18.645 4.181    -59.841  1.00 55.35  ? 21  PHE F CD1 1 
ATOM   5686  C  CD2 . PHE F  1 20  ? 20.456 3.321    -58.568  1.00 52.09  ? 21  PHE F CD2 1 
ATOM   5687  C  CE1 . PHE F  1 20  ? 17.852 3.136    -59.411  1.00 52.91  ? 21  PHE F CE1 1 
ATOM   5688  C  CE2 . PHE F  1 20  ? 19.667 2.286    -58.135  1.00 49.53  ? 21  PHE F CE2 1 
ATOM   5689  C  CZ  . PHE F  1 20  ? 18.364 2.191    -58.558  1.00 50.09  ? 21  PHE F CZ  1 
ATOM   5690  N  N   . GLU F  1 21  ? 22.696 7.915    -59.038  1.00 64.04  ? 22  GLU F N   1 
ATOM   5691  C  CA  . GLU F  1 21  ? 23.753 8.821    -59.506  1.00 67.94  ? 22  GLU F CA  1 
ATOM   5692  C  C   . GLU F  1 21  ? 25.160 8.364    -59.105  1.00 67.71  ? 22  GLU F C   1 
ATOM   5693  O  O   . GLU F  1 21  ? 25.542 8.422    -57.945  1.00 67.10  ? 22  GLU F O   1 
ATOM   5694  C  CB  . GLU F  1 21  ? 23.514 10.253   -59.029  1.00 71.22  ? 22  GLU F CB  1 
ATOM   5695  C  CG  . GLU F  1 21  ? 24.583 11.224   -59.558  1.00 76.43  ? 22  GLU F CG  1 
ATOM   5696  C  CD  . GLU F  1 21  ? 24.260 12.702   -59.331  1.00 81.31  ? 22  GLU F CD  1 
ATOM   5697  O  OE1 . GLU F  1 21  ? 23.437 12.998   -58.432  1.00 80.90  ? 22  GLU F OE1 1 
ATOM   5698  O  OE2 . GLU F  1 21  ? 24.842 13.565   -60.040  1.00 85.65  ? 22  GLU F OE2 1 
ATOM   5699  N  N   . GLN F  1 22  ? 25.929 7.933    -60.094  1.00 68.83  ? 23  GLN F N   1 
ATOM   5700  C  CA  . GLN F  1 22  ? 27.315 7.533    -59.896  1.00 69.64  ? 23  GLN F CA  1 
ATOM   5701  C  C   . GLN F  1 22  ? 28.202 8.594    -60.528  1.00 74.76  ? 23  GLN F C   1 
ATOM   5702  O  O   . GLN F  1 22  ? 28.258 8.708    -61.757  1.00 76.81  ? 23  GLN F O   1 
ATOM   5703  C  CB  . GLN F  1 22  ? 27.566 6.179    -60.553  1.00 67.79  ? 23  GLN F CB  1 
ATOM   5704  C  CG  . GLN F  1 22  ? 28.925 5.543    -60.255  1.00 68.32  ? 23  GLN F CG  1 
ATOM   5705  C  CD  . GLN F  1 22  ? 29.083 4.168    -60.903  1.00 66.79  ? 23  GLN F CD  1 
ATOM   5706  O  OE1 . GLN F  1 22  ? 28.712 3.950    -62.060  1.00 67.56  ? 23  GLN F OE1 1 
ATOM   5707  N  NE2 . GLN F  1 22  ? 29.624 3.235    -60.148  1.00 65.21  ? 23  GLN F NE2 1 
ATOM   5708  N  N   . LYS F  1 23  ? 28.883 9.376    -59.691  1.00 77.28  ? 24  LYS F N   1 
ATOM   5709  C  CA  . LYS F  1 23  ? 29.754 10.470   -60.175  1.00 82.81  ? 24  LYS F CA  1 
ATOM   5710  C  C   . LYS F  1 23  ? 30.978 9.968    -60.927  1.00 84.76  ? 24  LYS F C   1 
ATOM   5711  O  O   . LYS F  1 23  ? 31.423 10.590   -61.882  1.00 88.87  ? 24  LYS F O   1 
ATOM   5712  C  CB  . LYS F  1 23  ? 30.241 11.360   -59.030  1.00 85.51  ? 24  LYS F CB  1 
ATOM   5713  C  CG  . LYS F  1 23  ? 29.124 12.128   -58.325  1.00 85.58  ? 24  LYS F CG  1 
ATOM   5714  C  CD  . LYS F  1 23  ? 29.622 13.455   -57.720  1.00 90.93  ? 24  LYS F CD  1 
ATOM   5715  C  CE  . LYS F  1 23  ? 28.721 13.906   -56.551  1.00 90.12  ? 24  LYS F CE  1 
ATOM   5716  N  NZ  . LYS F  1 23  ? 29.307 15.021   -55.766  1.00 95.18  ? 24  LYS F NZ  1 
ATOM   5717  N  N   . GLU F  1 24  ? 31.523 8.842    -60.484  1.00 82.33  ? 25  GLU F N   1 
ATOM   5718  C  CA  . GLU F  1 24  ? 32.726 8.278    -61.100  1.00 84.61  ? 25  GLU F CA  1 
ATOM   5719  C  C   . GLU F  1 24  ? 32.650 6.774    -61.304  1.00 80.91  ? 25  GLU F C   1 
ATOM   5720  O  O   . GLU F  1 24  ? 32.221 6.027    -60.435  1.00 77.16  ? 25  GLU F O   1 
ATOM   5721  C  CB  . GLU F  1 24  ? 33.935 8.640    -60.259  1.00 87.82  ? 25  GLU F CB  1 
ATOM   5722  C  CG  . GLU F  1 24  ? 33.996 10.130   -60.022  1.00 92.32  ? 25  GLU F CG  1 
ATOM   5723  C  CD  . GLU F  1 24  ? 35.317 10.563   -59.467  1.00 97.69  ? 25  GLU F CD  1 
ATOM   5724  O  OE1 . GLU F  1 24  ? 35.809 9.867    -58.542  1.00 96.60  ? 25  GLU F OE1 1 
ATOM   5725  O  OE2 . GLU F  1 24  ? 35.846 11.597   -59.952  1.00 103.26 ? 25  GLU F OE2 1 
ATOM   5726  N  N   . SER F  1 25  ? 33.090 6.338    -62.469  1.00 82.75  ? 26  SER F N   1 
ATOM   5727  C  CA  . SER F  1 25  ? 32.957 4.930    -62.895  1.00 80.49  ? 26  SER F CA  1 
ATOM   5728  C  C   . SER F  1 25  ? 33.382 3.890    -61.832  1.00 78.10  ? 26  SER F C   1 
ATOM   5729  O  O   . SER F  1 25  ? 32.791 2.806    -61.701  1.00 74.59  ? 26  SER F O   1 
ATOM   5730  C  CB  . SER F  1 25  ? 33.762 4.697    -64.197  1.00 84.46  ? 26  SER F CB  1 
ATOM   5731  O  OG  . SER F  1 25  ? 35.066 5.289    -64.138  1.00 89.51  ? 26  SER F OG  1 
ATOM   5732  N  N   . ASN F  1 26  ? 34.436 4.231    -61.104  1.00 80.66  ? 27  ASN F N   1 
ATOM   5733  C  CA  . ASN F  1 26  ? 34.994 3.371    -60.056  1.00 79.52  ? 27  ASN F CA  1 
ATOM   5734  C  C   . ASN F  1 26  ? 34.340 3.612    -58.666  1.00 76.36  ? 27  ASN F C   1 
ATOM   5735  O  O   . ASN F  1 26  ? 34.653 2.950    -57.680  1.00 75.30  ? 27  ASN F O   1 
ATOM   5736  C  CB  . ASN F  1 26  ? 36.542 3.574    -59.999  1.00 84.72  ? 27  ASN F CB  1 
ATOM   5737  C  CG  . ASN F  1 26  ? 36.983 4.996    -59.439  1.00 88.17  ? 27  ASN F CG  1 
ATOM   5738  O  OD1 . ASN F  1 26  ? 36.446 6.053    -59.812  1.00 88.86  ? 27  ASN F OD1 1 
ATOM   5739  N  ND2 . ASN F  1 26  ? 37.968 4.986    -58.552  1.00 90.39  ? 27  ASN F ND2 1 
ATOM   5740  N  N   . GLY F  1 27  ? 33.422 4.558    -58.598  1.00 75.32  ? 28  GLY F N   1 
ATOM   5741  C  CA  . GLY F  1 27  ? 32.991 5.099    -57.308  1.00 74.10  ? 28  GLY F CA  1 
ATOM   5742  C  C   . GLY F  1 27  ? 31.628 4.622    -56.854  1.00 69.15  ? 28  GLY F C   1 
ATOM   5743  O  O   . GLY F  1 27  ? 31.009 3.798    -57.535  1.00 66.67  ? 28  GLY F O   1 
ATOM   5744  N  N   . PRO F  1 28  ? 31.146 5.166    -55.714  1.00 68.10  ? 29  PRO F N   1 
ATOM   5745  C  CA  . PRO F  1 28  ? 29.902 4.734    -55.148  1.00 63.98  ? 29  PRO F CA  1 
ATOM   5746  C  C   . PRO F  1 28  ? 28.697 5.358    -55.850  1.00 63.27  ? 29  PRO F C   1 
ATOM   5747  O  O   . PRO F  1 28  ? 28.815 6.404    -56.500  1.00 66.33  ? 29  PRO F O   1 
ATOM   5748  C  CB  . PRO F  1 28  ? 29.996 5.239    -53.714  1.00 64.58  ? 29  PRO F CB  1 
ATOM   5749  C  CG  . PRO F  1 28  ? 30.719 6.490    -53.829  1.00 69.09  ? 29  PRO F CG  1 
ATOM   5750  C  CD  . PRO F  1 28  ? 31.704 6.298    -54.952  1.00 71.59  ? 29  PRO F CD  1 
ATOM   5751  N  N   . VAL F  1 29  ? 27.550 4.698    -55.698  1.00 59.58  ? 30  VAL F N   1 
ATOM   5752  C  CA  . VAL F  1 29  ? 26.299 5.102    -56.318  1.00 58.70  ? 30  VAL F CA  1 
ATOM   5753  C  C   . VAL F  1 29  ? 25.355 5.628    -55.264  1.00 57.72  ? 30  VAL F C   1 
ATOM   5754  O  O   . VAL F  1 29  ? 24.979 4.896    -54.370  1.00 55.27  ? 30  VAL F O   1 
ATOM   5755  C  CB  . VAL F  1 29  ? 25.606 3.904    -56.977  1.00 55.88  ? 30  VAL F CB  1 
ATOM   5756  C  CG1 . VAL F  1 29  ? 24.272 4.321    -57.526  1.00 55.53  ? 30  VAL F CG1 1 
ATOM   5757  C  CG2 . VAL F  1 29  ? 26.487 3.305    -58.060  1.00 57.30  ? 30  VAL F CG2 1 
ATOM   5758  N  N   . LYS F  1 30  ? 24.972 6.891    -55.359  1.00 60.24  ? 31  LYS F N   1 
ATOM   5759  C  CA  . LYS F  1 30  ? 23.912 7.430    -54.503  1.00 59.76  ? 31  LYS F CA  1 
ATOM   5760  C  C   . LYS F  1 30  ? 22.558 7.020    -55.035  1.00 57.60  ? 31  LYS F C   1 
ATOM   5761  O  O   . LYS F  1 30  ? 22.290 7.126    -56.220  1.00 58.66  ? 31  LYS F O   1 
ATOM   5762  C  CB  . LYS F  1 30  ? 23.988 8.944    -54.415  1.00 63.99  ? 31  LYS F CB  1 
ATOM   5763  C  CG  . LYS F  1 30  ? 25.187 9.409    -53.614  1.00 67.00  ? 31  LYS F CG  1 
ATOM   5764  C  CD  . LYS F  1 30  ? 25.097 10.878   -53.202  1.00 71.80  ? 31  LYS F CD  1 
ATOM   5765  C  CE  . LYS F  1 30  ? 26.307 11.264   -52.354  1.00 74.78  ? 31  LYS F CE  1 
ATOM   5766  N  NZ  . LYS F  1 30  ? 26.165 12.609   -51.761  1.00 79.70  ? 31  LYS F NZ  1 
ATOM   5767  N  N   . VAL F  1 31  ? 21.715 6.524    -54.148  1.00 55.15  ? 32  VAL F N   1 
ATOM   5768  C  CA  . VAL F  1 31  ? 20.372 6.085    -54.507  1.00 53.63  ? 32  VAL F CA  1 
ATOM   5769  C  C   . VAL F  1 31  ? 19.374 6.863    -53.691  1.00 54.80  ? 32  VAL F C   1 
ATOM   5770  O  O   . VAL F  1 31  ? 19.408 6.801    -52.469  1.00 54.39  ? 32  VAL F O   1 
ATOM   5771  C  CB  . VAL F  1 31  ? 20.147 4.615    -54.175  1.00 50.00  ? 32  VAL F CB  1 
ATOM   5772  C  CG1 . VAL F  1 31  ? 18.795 4.176    -54.658  1.00 48.97  ? 32  VAL F CG1 1 
ATOM   5773  C  CG2 . VAL F  1 31  ? 21.207 3.781    -54.792  1.00 49.59  ? 32  VAL F CG2 1 
ATOM   5774  N  N   . TRP F  1 32  ? 18.485 7.603    -54.340  1.00 56.95  ? 33  TRP F N   1 
ATOM   5775  C  CA  . TRP F  1 32  ? 17.513 8.401    -53.590  1.00 58.77  ? 33  TRP F CA  1 
ATOM   5776  C  C   . TRP F  1 32  ? 16.187 8.554    -54.303  1.00 59.81  ? 33  TRP F C   1 
ATOM   5777  O  O   . TRP F  1 32  ? 16.096 8.441    -55.518  1.00 60.56  ? 33  TRP F O   1 
ATOM   5778  C  CB  . TRP F  1 32  ? 18.096 9.792    -53.225  1.00 62.79  ? 33  TRP F CB  1 
ATOM   5779  C  CG  . TRP F  1 32  ? 17.916 10.859   -54.282  1.00 66.82  ? 33  TRP F CG  1 
ATOM   5780  C  CD1 . TRP F  1 32  ? 16.967 11.840   -54.305  1.00 70.48  ? 33  TRP F CD1 1 
ATOM   5781  C  CD2 . TRP F  1 32  ? 18.698 11.032   -55.463  1.00 68.09  ? 33  TRP F CD2 1 
ATOM   5782  N  NE1 . TRP F  1 32  ? 17.109 12.609   -55.436  1.00 73.60  ? 33  TRP F NE1 1 
ATOM   5783  C  CE2 . TRP F  1 32  ? 18.169 12.137   -56.158  1.00 72.32  ? 33  TRP F CE2 1 
ATOM   5784  C  CE3 . TRP F  1 32  ? 19.793 10.355   -56.003  1.00 66.89  ? 33  TRP F CE3 1 
ATOM   5785  C  CZ2 . TRP F  1 32  ? 18.699 12.586   -57.363  1.00 75.34  ? 33  TRP F CZ2 1 
ATOM   5786  C  CZ3 . TRP F  1 32  ? 20.327 10.799   -57.206  1.00 69.75  ? 33  TRP F CZ3 1 
ATOM   5787  C  CH2 . TRP F  1 32  ? 19.778 11.906   -57.875  1.00 73.89  ? 33  TRP F CH2 1 
ATOM   5788  N  N   . GLY F  1 33  ? 15.164 8.847    -53.520  1.00 60.56  ? 34  GLY F N   1 
ATOM   5789  C  CA  . GLY F  1 33  ? 13.843 9.063    -54.064  1.00 62.47  ? 34  GLY F CA  1 
ATOM   5790  C  C   . GLY F  1 33  ? 12.777 8.930    -53.004  1.00 62.38  ? 34  GLY F C   1 
ATOM   5791  O  O   . GLY F  1 33  ? 13.075 9.017    -51.794  1.00 61.84  ? 34  GLY F O   1 
ATOM   5792  N  N   . SER F  1 34  ? 11.540 8.721    -53.468  1.00 63.25  ? 35  SER F N   1 
ATOM   5793  C  CA  . SER F  1 34  ? 10.390 8.626    -52.582  1.00 63.92  ? 35  SER F CA  1 
ATOM   5794  C  C   . SER F  1 34  ? 9.403  7.561    -53.016  1.00 62.66  ? 35  SER F C   1 
ATOM   5795  O  O   . SER F  1 34  ? 8.847  7.650    -54.093  1.00 64.63  ? 35  SER F O   1 
ATOM   5796  C  CB  . SER F  1 34  ? 9.678  9.971    -52.512  1.00 69.01  ? 35  SER F CB  1 
ATOM   5797  O  OG  . SER F  1 34  ? 8.704  9.975    -51.478  1.00 70.20  ? 35  SER F OG  1 
ATOM   5798  N  N   . ILE F  1 35  ? 9.195  6.555    -52.165  1.00 59.99  ? 36  ILE F N   1 
ATOM   5799  C  CA  . ILE F  1 35  ? 8.166  5.514    -52.376  1.00 59.34  ? 36  ILE F CA  1 
ATOM   5800  C  C   . ILE F  1 35  ? 7.009  5.723    -51.414  1.00 61.47  ? 36  ILE F C   1 
ATOM   5801  O  O   . ILE F  1 35  ? 7.218  6.064    -50.247  1.00 61.29  ? 36  ILE F O   1 
ATOM   5802  C  CB  . ILE F  1 35  ? 8.685  4.091    -52.104  1.00 55.18  ? 36  ILE F CB  1 
ATOM   5803  C  CG1 . ILE F  1 35  ? 9.943  3.807    -52.903  1.00 53.34  ? 36  ILE F CG1 1 
ATOM   5804  C  CG2 . ILE F  1 35  ? 7.643  3.058    -52.459  1.00 55.04  ? 36  ILE F CG2 1 
ATOM   5805  C  CD1 . ILE F  1 35  ? 10.505 2.441    -52.605  1.00 50.03  ? 36  ILE F CD1 1 
ATOM   5806  N  N   . LYS F  1 36  ? 5.793  5.490    -51.901  1.00 63.83  ? 37  LYS F N   1 
ATOM   5807  C  CA  . LYS F  1 36  ? 4.586  5.690    -51.094  1.00 66.69  ? 37  LYS F CA  1 
ATOM   5808  C  C   . LYS F  1 36  ? 3.546  4.576    -51.239  1.00 66.82  ? 37  LYS F C   1 
ATOM   5809  O  O   . LYS F  1 36  ? 3.641  3.728    -52.123  1.00 65.39  ? 37  LYS F O   1 
ATOM   5810  C  CB  . LYS F  1 36  ? 3.945  7.052    -51.399  1.00 71.88  ? 37  LYS F CB  1 
ATOM   5811  C  CG  . LYS F  1 36  ? 3.520  7.269    -52.834  1.00 74.66  ? 37  LYS F CG  1 
ATOM   5812  C  CD  . LYS F  1 36  ? 2.473  8.384    -52.912  1.00 81.03  ? 37  LYS F CD  1 
ATOM   5813  C  CE  . LYS F  1 36  ? 2.112  8.736    -54.356  1.00 84.48  ? 37  LYS F CE  1 
ATOM   5814  N  NZ  . LYS F  1 36  ? 0.921  9.630    -54.415  1.00 90.66  ? 37  LYS F NZ  1 
ATOM   5815  N  N   . GLY F  1 37  ? 2.555  4.603    -50.349  1.00 69.05  ? 38  GLY F N   1 
ATOM   5816  C  CA  . GLY F  1 37  ? 1.543  3.555    -50.249  1.00 69.78  ? 38  GLY F CA  1 
ATOM   5817  C  C   . GLY F  1 37  ? 2.027  2.358    -49.445  1.00 65.80  ? 38  GLY F C   1 
ATOM   5818  O  O   . GLY F  1 37  ? 1.454  1.263    -49.519  1.00 65.60  ? 38  GLY F O   1 
ATOM   5819  N  N   . LEU F  1 38  ? 3.083  2.572    -48.668  1.00 63.05  ? 39  LEU F N   1 
ATOM   5820  C  CA  . LEU F  1 38  ? 3.767  1.478    -47.977  1.00 59.33  ? 39  LEU F CA  1 
ATOM   5821  C  C   . LEU F  1 38  ? 3.205  1.273    -46.574  1.00 60.16  ? 39  LEU F C   1 
ATOM   5822  O  O   . LEU F  1 38  ? 2.838  2.231    -45.903  1.00 62.61  ? 39  LEU F O   1 
ATOM   5823  C  CB  . LEU F  1 38  ? 5.291  1.725    -47.923  1.00 56.11  ? 39  LEU F CB  1 
ATOM   5824  C  CG  . LEU F  1 38  ? 6.110  1.301    -49.137  1.00 53.63  ? 39  LEU F CG  1 
ATOM   5825  C  CD1 . LEU F  1 38  ? 7.453  1.945    -49.138  1.00 51.99  ? 39  LEU F CD1 1 
ATOM   5826  C  CD2 . LEU F  1 38  ? 6.246  -0.190   -49.135  1.00 51.40  ? 39  LEU F CD2 1 
ATOM   5827  N  N   . THR F  1 39  ? 3.154  0.013    -46.151  1.00 58.36  ? 40  THR F N   1 
ATOM   5828  C  CA  . THR F  1 39  ? 2.798  -0.335   -44.779  1.00 58.95  ? 40  THR F CA  1 
ATOM   5829  C  C   . THR F  1 39  ? 3.897  0.191    -43.843  1.00 57.15  ? 40  THR F C   1 
ATOM   5830  O  O   . THR F  1 39  ? 5.074  0.018    -44.109  1.00 54.09  ? 40  THR F O   1 
ATOM   5831  C  CB  . THR F  1 39  ? 2.606  -1.881   -44.569  1.00 57.77  ? 40  THR F CB  1 
ATOM   5832  O  OG1 . THR F  1 39  ? 3.722  -2.431   -43.857  1.00 54.79  ? 40  THR F OG1 1 
ATOM   5833  C  CG2 . THR F  1 39  ? 2.422  -2.629   -45.905  1.00 57.54  ? 40  THR F CG2 1 
ATOM   5834  N  N   . GLU F  1 40  ? 3.511  0.824    -42.742  1.00 59.69  ? 41  GLU F N   1 
ATOM   5835  C  CA  . GLU F  1 40  ? 4.483  1.484    -41.853  1.00 59.11  ? 41  GLU F CA  1 
ATOM   5836  C  C   . GLU F  1 40  ? 5.554  0.521    -41.400  1.00 55.45  ? 41  GLU F C   1 
ATOM   5837  O  O   . GLU F  1 40  ? 5.260  -0.599   -41.011  1.00 54.58  ? 41  GLU F O   1 
ATOM   5838  C  CB  . GLU F  1 40  ? 3.828  2.083    -40.598  1.00 62.80  ? 41  GLU F CB  1 
ATOM   5839  C  CG  . GLU F  1 40  ? 4.853  2.714    -39.618  1.00 62.94  ? 41  GLU F CG  1 
ATOM   5840  C  CD  . GLU F  1 40  ? 4.238  3.186    -38.301  1.00 67.20  ? 41  GLU F CD  1 
ATOM   5841  O  OE1 . GLU F  1 40  ? 3.512  2.407    -37.641  1.00 67.92  ? 41  GLU F OE1 1 
ATOM   5842  O  OE2 . GLU F  1 40  ? 4.505  4.343    -37.910  1.00 69.82  ? 41  GLU F OE2 1 
ATOM   5843  N  N   . GLY F  1 41  ? 6.795  0.986    -41.441  1.00 53.83  ? 42  GLY F N   1 
ATOM   5844  C  CA  . GLY F  1 41  ? 7.931  0.211    -40.952  1.00 51.12  ? 42  GLY F CA  1 
ATOM   5845  C  C   . GLY F  1 41  ? 8.952  -0.126   -42.027  1.00 48.25  ? 42  GLY F C   1 
ATOM   5846  O  O   . GLY F  1 41  ? 9.023  0.542    -43.065  1.00 48.43  ? 42  GLY F O   1 
ATOM   5847  N  N   . LEU F  1 42  ? 9.737  -1.174   -41.769  1.00 45.96  ? 43  LEU F N   1 
ATOM   5848  C  CA  . LEU F  1 42  ? 10.845 -1.568   -42.651  1.00 43.51  ? 43  LEU F CA  1 
ATOM   5849  C  C   . LEU F  1 42  ? 10.360 -2.329   -43.860  1.00 42.63  ? 43  LEU F C   1 
ATOM   5850  O  O   . LEU F  1 42  ? 9.393  -3.080   -43.777  1.00 43.43  ? 43  LEU F O   1 
ATOM   5851  C  CB  . LEU F  1 42  ? 11.869 -2.432   -41.911  1.00 42.10  ? 43  LEU F CB  1 
ATOM   5852  C  CG  . LEU F  1 42  ? 12.829 -1.682   -40.976  1.00 42.77  ? 43  LEU F CG  1 
ATOM   5853  C  CD1 . LEU F  1 42  ? 12.579 -1.982   -39.495  1.00 44.32  ? 43  LEU F CD1 1 
ATOM   5854  C  CD2 . LEU F  1 42  ? 14.246 -2.032   -41.305  1.00 41.40  ? 43  LEU F CD2 1 
ATOM   5855  N  N   . HIS F  1 43  ? 11.040 -2.129   -44.981  1.00 41.57  ? 44  HIS F N   1 
ATOM   5856  C  CA  . HIS F  1 43  ? 10.751 -2.872   -46.211  1.00 41.09  ? 44  HIS F CA  1 
ATOM   5857  C  C   . HIS F  1 43  ? 12.019 -3.273   -46.936  1.00 39.32  ? 44  HIS F C   1 
ATOM   5858  O  O   . HIS F  1 43  ? 12.936 -2.478   -47.082  1.00 39.14  ? 44  HIS F O   1 
ATOM   5859  C  CB  . HIS F  1 43  ? 9.857  -2.063   -47.160  1.00 42.88  ? 44  HIS F CB  1 
ATOM   5860  C  CG  . HIS F  1 43  ? 8.442  -1.946   -46.693  1.00 45.01  ? 44  HIS F CG  1 
ATOM   5861  N  ND1 . HIS F  1 43  ? 7.508  -2.936   -46.890  1.00 45.85  ? 44  HIS F ND1 1 
ATOM   5862  C  CD2 . HIS F  1 43  ? 7.809  -0.961   -46.019  1.00 47.21  ? 44  HIS F CD2 1 
ATOM   5863  C  CE1 . HIS F  1 43  ? 6.357  -2.561   -46.367  1.00 48.44  ? 44  HIS F CE1 1 
ATOM   5864  N  NE2 . HIS F  1 43  ? 6.514  -1.368   -45.831  1.00 49.28  ? 44  HIS F NE2 1 
ATOM   5865  N  N   . GLY F  1 44  ? 12.049 -4.515   -47.398  1.00 38.56  ? 45  GLY F N   1 
ATOM   5866  C  CA  . GLY F  1 44  ? 13.155 -5.013   -48.200  1.00 37.62  ? 45  GLY F CA  1 
ATOM   5867  C  C   . GLY F  1 44  ? 13.295 -4.246   -49.497  1.00 38.08  ? 45  GLY F C   1 
ATOM   5868  O  O   . GLY F  1 44  ? 12.317 -3.783   -50.039  1.00 39.64  ? 45  GLY F O   1 
ATOM   5869  N  N   . PHE F  1 45  ? 14.505 -4.130   -50.011  1.00 37.41  ? 46  PHE F N   1 
ATOM   5870  C  CA  . PHE F  1 45  ? 14.756 -3.237   -51.122  1.00 38.24  ? 46  PHE F CA  1 
ATOM   5871  C  C   . PHE F  1 45  ? 15.931 -3.712   -51.913  1.00 38.04  ? 46  PHE F C   1 
ATOM   5872  O  O   . PHE F  1 45  ? 17.054 -3.454   -51.530  1.00 37.81  ? 46  PHE F O   1 
ATOM   5873  C  CB  . PHE F  1 45  ? 15.052 -1.865   -50.560  1.00 38.94  ? 46  PHE F CB  1 
ATOM   5874  C  CG  . PHE F  1 45  ? 15.121 -0.771   -51.581  1.00 40.36  ? 46  PHE F CG  1 
ATOM   5875  C  CD1 . PHE F  1 45  ? 14.094 -0.571   -52.475  1.00 41.77  ? 46  PHE F CD1 1 
ATOM   5876  C  CD2 . PHE F  1 45  ? 16.182 0.115    -51.587  1.00 41.05  ? 46  PHE F CD2 1 
ATOM   5877  C  CE1 . PHE F  1 45  ? 14.140 0.460    -53.387  1.00 43.68  ? 46  PHE F CE1 1 
ATOM   5878  C  CE2 . PHE F  1 45  ? 16.237 1.152    -52.490  1.00 43.01  ? 46  PHE F CE2 1 
ATOM   5879  C  CZ  . PHE F  1 45  ? 15.213 1.324    -53.395  1.00 44.41  ? 46  PHE F CZ  1 
ATOM   5880  N  N   . HIS F  1 46  ? 15.681 -4.394   -53.026  1.00 38.66  ? 47  HIS F N   1 
ATOM   5881  C  CA  . HIS F  1 46  ? 16.744 -5.069   -53.768  1.00 38.79  ? 47  HIS F CA  1 
ATOM   5882  C  C   . HIS F  1 46  ? 16.717 -4.852   -55.274  1.00 40.39  ? 47  HIS F C   1 
ATOM   5883  O  O   . HIS F  1 46  ? 15.677 -4.604   -55.835  1.00 41.63  ? 47  HIS F O   1 
ATOM   5884  C  CB  . HIS F  1 46  ? 16.672 -6.562   -53.492  1.00 38.50  ? 47  HIS F CB  1 
ATOM   5885  C  CG  . HIS F  1 46  ? 16.377 -6.899   -52.070  1.00 37.22  ? 47  HIS F CG  1 
ATOM   5886  N  ND1 . HIS F  1 46  ? 15.150 -7.343   -51.658  1.00 37.63  ? 47  HIS F ND1 1 
ATOM   5887  C  CD2 . HIS F  1 46  ? 17.144 -6.853   -50.960  1.00 36.92  ? 47  HIS F CD2 1 
ATOM   5888  C  CE1 . HIS F  1 46  ? 15.173 -7.568   -50.360  1.00 36.93  ? 47  HIS F CE1 1 
ATOM   5889  N  NE2 . HIS F  1 46  ? 16.374 -7.280   -49.910  1.00 36.32  ? 47  HIS F NE2 1 
ATOM   5890  N  N   . VAL F  1 47  ? 17.881 -4.955   -55.912  1.00 40.92  ? 48  VAL F N   1 
ATOM   5891  C  CA  . VAL F  1 47  ? 17.981 -4.991   -57.365  1.00 42.67  ? 48  VAL F CA  1 
ATOM   5892  C  C   . VAL F  1 47  ? 17.974 -6.425   -57.820  1.00 43.53  ? 48  VAL F C   1 
ATOM   5893  O  O   . VAL F  1 47  ? 18.866 -7.182   -57.468  1.00 43.27  ? 48  VAL F O   1 
ATOM   5894  C  CB  . VAL F  1 47  ? 19.272 -4.386   -57.850  1.00 43.40  ? 48  VAL F CB  1 
ATOM   5895  C  CG1 . VAL F  1 47  ? 19.462 -4.664   -59.311  1.00 45.57  ? 48  VAL F CG1 1 
ATOM   5896  C  CG2 . VAL F  1 47  ? 19.258 -2.924   -57.609  1.00 43.82  ? 48  VAL F CG2 1 
ATOM   5897  N  N   . HIS F  1 48  ? 16.971 -6.798   -58.606  1.00 45.12  ? 49  HIS F N   1 
ATOM   5898  C  CA  . HIS F  1 48  ? 16.849 -8.170   -59.121  1.00 46.82  ? 49  HIS F CA  1 
ATOM   5899  C  C   . HIS F  1 48  ? 17.494 -8.332   -60.491  1.00 49.30  ? 49  HIS F C   1 
ATOM   5900  O  O   . HIS F  1 48  ? 17.736 -7.349   -61.187  1.00 50.15  ? 49  HIS F O   1 
ATOM   5901  C  CB  . HIS F  1 48  ? 15.386 -8.590   -59.205  1.00 47.91  ? 49  HIS F CB  1 
ATOM   5902  C  CG  . HIS F  1 48  ? 14.748 -8.826   -57.876  1.00 46.13  ? 49  HIS F CG  1 
ATOM   5903  N  ND1 . HIS F  1 48  ? 14.144 -10.017  -57.536  1.00 46.89  ? 49  HIS F ND1 1 
ATOM   5904  C  CD2 . HIS F  1 48  ? 14.626 -8.022   -56.798  1.00 43.85  ? 49  HIS F CD2 1 
ATOM   5905  C  CE1 . HIS F  1 48  ? 13.673 -9.934   -56.308  1.00 45.26  ? 49  HIS F CE1 1 
ATOM   5906  N  NE2 . HIS F  1 48  ? 13.945 -8.731   -55.841  1.00 43.52  ? 49  HIS F NE2 1 
ATOM   5907  N  N   . GLU F  1 49  ? 17.733 -9.583   -60.881  1.00 50.97  ? 50  GLU F N   1 
ATOM   5908  C  CA  . GLU F  1 49  ? 18.562 -9.892   -62.052  1.00 53.61  ? 50  GLU F CA  1 
ATOM   5909  C  C   . GLU F  1 49  ? 18.009 -9.341   -63.353  1.00 56.10  ? 50  GLU F C   1 
ATOM   5910  O  O   . GLU F  1 49  ? 18.723 -8.642   -64.061  1.00 57.13  ? 50  GLU F O   1 
ATOM   5911  C  CB  . GLU F  1 49  ? 18.766 -11.395  -62.198  1.00 55.76  ? 50  GLU F CB  1 
ATOM   5912  C  CG  . GLU F  1 49  ? 19.792 -11.783  -63.250  1.00 58.69  ? 50  GLU F CG  1 
ATOM   5913  C  CD  . GLU F  1 49  ? 20.129 -13.263  -63.231  1.00 61.06  ? 50  GLU F CD  1 
ATOM   5914  O  OE1 . GLU F  1 49  ? 19.788 -13.968  -62.248  1.00 59.54  ? 50  GLU F OE1 1 
ATOM   5915  O  OE2 . GLU F  1 49  ? 20.735 -13.719  -64.226  1.00 64.64  ? 50  GLU F OE2 1 
ATOM   5916  N  N   . PHE F  1 50  ? 16.749 -9.645   -63.660  1.00 57.51  ? 51  PHE F N   1 
ATOM   5917  C  CA  . PHE F  1 50  ? 16.182 -9.354   -64.980  1.00 60.84  ? 51  PHE F CA  1 
ATOM   5918  C  C   . PHE F  1 50  ? 15.290 -8.128   -65.039  1.00 60.63  ? 51  PHE F C   1 
ATOM   5919  O  O   . PHE F  1 50  ? 14.459 -7.906   -64.153  1.00 58.84  ? 51  PHE F O   1 
ATOM   5920  C  CB  . PHE F  1 50  ? 15.383 -10.542  -65.455  1.00 63.89  ? 51  PHE F CB  1 
ATOM   5921  C  CG  . PHE F  1 50  ? 16.149 -11.816  -65.429  1.00 65.16  ? 51  PHE F CG  1 
ATOM   5922  C  CD1 . PHE F  1 50  ? 17.319 -11.931  -66.153  1.00 66.91  ? 51  PHE F CD1 1 
ATOM   5923  C  CD2 . PHE F  1 50  ? 15.702 -12.915  -64.693  1.00 65.40  ? 51  PHE F CD2 1 
ATOM   5924  C  CE1 . PHE F  1 50  ? 18.047 -13.124  -66.138  1.00 68.81  ? 51  PHE F CE1 1 
ATOM   5925  C  CE2 . PHE F  1 50  ? 16.419 -14.107  -64.672  1.00 66.97  ? 51  PHE F CE2 1 
ATOM   5926  C  CZ  . PHE F  1 50  ? 17.596 -14.210  -65.389  1.00 68.72  ? 51  PHE F CZ  1 
ATOM   5927  N  N   . GLY F  1 51  ? 15.455 -7.354   -66.113  1.00 62.94  ? 52  GLY F N   1 
ATOM   5928  C  CA  . GLY F  1 51  ? 14.546 -6.244   -66.447  1.00 64.17  ? 52  GLY F CA  1 
ATOM   5929  C  C   . GLY F  1 51  ? 13.278 -6.726   -67.168  1.00 67.79  ? 52  GLY F C   1 
ATOM   5930  O  O   . GLY F  1 51  ? 12.765 -6.095   -68.096  1.00 70.97  ? 52  GLY F O   1 
ATOM   5931  N  N   . ASP F  1 52  ? 12.747 -7.844   -66.713  1.00 67.71  ? 53  ASP F N   1 
ATOM   5932  C  CA  . ASP F  1 52  ? 11.620 -8.474   -67.353  1.00 71.59  ? 53  ASP F CA  1 
ATOM   5933  C  C   . ASP F  1 52  ? 10.370 -8.152   -66.540  1.00 70.93  ? 53  ASP F C   1 
ATOM   5934  O  O   . ASP F  1 52  ? 10.287 -8.469   -65.348  1.00 67.87  ? 53  ASP F O   1 
ATOM   5935  C  CB  . ASP F  1 52  ? 11.883 -9.986   -67.397  1.00 72.94  ? 53  ASP F CB  1 
ATOM   5936  C  CG  . ASP F  1 52  ? 10.879 -10.747  -68.231  1.00 78.22  ? 53  ASP F CG  1 
ATOM   5937  O  OD1 . ASP F  1 52  ? 9.692  -10.326  -68.261  1.00 80.12  ? 53  ASP F OD1 1 
ATOM   5938  O  OD2 . ASP F  1 52  ? 11.280 -11.782  -68.832  1.00 80.79  ? 53  ASP F OD2 1 
ATOM   5939  N  N   . ASN F  1 53  ? 9.396  -7.523   -67.187  1.00 74.19  ? 54  ASN F N   1 
ATOM   5940  C  CA  . ASN F  1 53  ? 8.124  -7.204   -66.534  1.00 74.63  ? 54  ASN F CA  1 
ATOM   5941  C  C   . ASN F  1 53  ? 6.934  -7.950   -67.160  1.00 79.51  ? 54  ASN F C   1 
ATOM   5942  O  O   . ASN F  1 53  ? 5.767  -7.624   -66.893  1.00 81.10  ? 54  ASN F O   1 
ATOM   5943  C  CB  . ASN F  1 53  ? 7.882  -5.694   -66.569  1.00 74.64  ? 54  ASN F CB  1 
ATOM   5944  C  CG  . ASN F  1 53  ? 7.492  -5.131   -65.201  1.00 71.86  ? 54  ASN F CG  1 
ATOM   5945  O  OD1 . ASN F  1 53  ? 8.304  -5.141   -64.266  1.00 68.14  ? 54  ASN F OD1 1 
ATOM   5946  N  ND2 . ASN F  1 53  ? 6.256  -4.637   -65.078  1.00 74.14  ? 54  ASN F ND2 1 
ATOM   5947  N  N   . THR F  1 54  ? 7.256  -8.961   -67.968  1.00 82.08  ? 55  THR F N   1 
ATOM   5948  C  CA  . THR F  1 54  ? 6.279  -9.768   -68.702  1.00 87.74  ? 55  THR F CA  1 
ATOM   5949  C  C   . THR F  1 54  ? 5.090  -10.165  -67.832  1.00 88.46  ? 55  THR F C   1 
ATOM   5950  O  O   . THR F  1 54  ? 3.965  -9.678   -68.036  1.00 91.55  ? 55  THR F O   1 
ATOM   5951  C  CB  . THR F  1 54  ? 6.960  -11.057  -69.240  1.00 89.56  ? 55  THR F CB  1 
ATOM   5952  O  OG1 . THR F  1 54  ? 7.847  -10.709  -70.310  1.00 90.89  ? 55  THR F OG1 1 
ATOM   5953  C  CG2 . THR F  1 54  ? 5.942  -12.099  -69.726  1.00 95.52  ? 55  THR F CG2 1 
ATOM   5954  N  N   . ALA F  1 55  ? 5.378  -11.032  -66.854  1.00 85.72  ? 56  ALA F N   1 
ATOM   5955  C  CA  . ALA F  1 55  ? 4.399  -11.537  -65.885  1.00 86.04  ? 56  ALA F CA  1 
ATOM   5956  C  C   . ALA F  1 55  ? 4.493  -10.769  -64.551  1.00 80.79  ? 56  ALA F C   1 
ATOM   5957  O  O   . ALA F  1 55  ? 4.526  -11.388  -63.472  1.00 78.52  ? 56  ALA F O   1 
ATOM   5958  C  CB  . ALA F  1 55  ? 4.603  -13.053  -65.651  1.00 86.98  ? 56  ALA F CB  1 
ATOM   5959  N  N   . GLY F  1 56  ? 4.536  -9.435   -64.639  1.00 79.29  ? 57  GLY F N   1 
ATOM   5960  C  CA  . GLY F  1 56  ? 4.549  -8.574   -63.463  1.00 75.28  ? 57  GLY F CA  1 
ATOM   5961  C  C   . GLY F  1 56  ? 5.919  -8.445   -62.866  1.00 70.10  ? 57  GLY F C   1 
ATOM   5962  O  O   . GLY F  1 56  ? 6.896  -8.469   -63.594  1.00 69.87  ? 57  GLY F O   1 
ATOM   5963  N  N   . CYS F  1 57  ? 5.987  -8.305   -61.543  1.00 66.56  ? 58  CYS F N   1 
ATOM   5964  C  CA  . CYS F  1 57  ? 7.269  -8.254   -60.827  1.00 61.96  ? 58  CYS F CA  1 
ATOM   5965  C  C   . CYS F  1 57  ? 7.935  -9.620   -60.705  1.00 61.50  ? 58  CYS F C   1 
ATOM   5966  O  O   . CYS F  1 57  ? 9.161  -9.670   -60.536  1.00 59.01  ? 58  CYS F O   1 
ATOM   5967  C  CB  . CYS F  1 57  ? 7.118  -7.699   -59.415  1.00 58.95  ? 58  CYS F CB  1 
ATOM   5968  S  SG  . CYS F  1 57  ? 6.789  -5.948   -59.269  1.00 58.81  ? 58  CYS F SG  1 
ATOM   5969  N  N   . THR F  1 58  ? 7.156  -10.711  -60.772  1.00 64.30  ? 59  THR F N   1 
ATOM   5970  C  CA  . THR F  1 58  ? 7.711  -12.079  -60.632  1.00 64.53  ? 59  THR F CA  1 
ATOM   5971  C  C   . THR F  1 58  ? 8.748  -12.416  -61.695  1.00 65.49  ? 59  THR F C   1 
ATOM   5972  O  O   . THR F  1 58  ? 9.685  -13.165  -61.440  1.00 64.41  ? 59  THR F O   1 
ATOM   5973  C  CB  . THR F  1 58  ? 6.634  -13.140  -60.719  1.00 68.65  ? 59  THR F CB  1 
ATOM   5974  O  OG1 . THR F  1 58  ? 5.506  -12.727  -59.949  1.00 69.01  ? 59  THR F OG1 1 
ATOM   5975  C  CG2 . THR F  1 58  ? 7.159  -14.481  -60.200  1.00 68.56  ? 59  THR F CG2 1 
ATOM   5976  N  N   . SER F  1 59  ? 8.562  -11.846  -62.881  1.00 68.03  ? 60  SER F N   1 
ATOM   5977  C  CA  . SER F  1 59  ? 9.443  -12.067  -64.034  1.00 69.86  ? 60  SER F CA  1 
ATOM   5978  C  C   . SER F  1 59  ? 10.861 -11.578  -63.816  1.00 66.22  ? 60  SER F C   1 
ATOM   5979  O  O   . SER F  1 59  ? 11.772 -12.027  -64.507  1.00 67.52  ? 60  SER F O   1 
ATOM   5980  C  CB  . SER F  1 59  ? 8.888  -11.363  -65.277  1.00 73.39  ? 60  SER F CB  1 
ATOM   5981  O  OG  . SER F  1 59  ? 7.506  -11.610  -65.435  1.00 77.53  ? 60  SER F OG  1 
ATOM   5982  N  N   . ALA F  1 60  ? 11.033 -10.641  -62.882  1.00 62.40  ? 61  ALA F N   1 
ATOM   5983  C  CA  . ALA F  1 60  ? 12.343 -10.037  -62.562  1.00 59.08  ? 61  ALA F CA  1 
ATOM   5984  C  C   . ALA F  1 60  ? 13.361 -11.042  -62.061  1.00 57.80  ? 61  ALA F C   1 
ATOM   5985  O  O   . ALA F  1 60  ? 14.545 -10.746  -62.046  1.00 56.28  ? 61  ALA F O   1 
ATOM   5986  C  CB  . ALA F  1 60  ? 12.180 -8.927   -61.545  1.00 55.85  ? 61  ALA F CB  1 
ATOM   5987  N  N   . GLY F  1 61  ? 12.891 -12.219  -61.656  1.00 58.95  ? 62  GLY F N   1 
ATOM   5988  C  CA  . GLY F  1 61  ? 13.764 -13.308  -61.230  1.00 58.85  ? 62  GLY F CA  1 
ATOM   5989  C  C   . GLY F  1 61  ? 14.281 -13.050  -59.842  1.00 55.09  ? 62  GLY F C   1 
ATOM   5990  O  O   . GLY F  1 61  ? 13.676 -12.279  -59.110  1.00 53.14  ? 62  GLY F O   1 
ATOM   5991  N  N   . PRO F  1 62  ? 15.417 -13.661  -59.476  1.00 54.52  ? 63  PRO F N   1 
ATOM   5992  C  CA  . PRO F  1 62  ? 15.989 -13.518  -58.151  1.00 51.54  ? 63  PRO F CA  1 
ATOM   5993  C  C   . PRO F  1 62  ? 16.879 -12.275  -57.962  1.00 49.04  ? 63  PRO F C   1 
ATOM   5994  O  O   . PRO F  1 62  ? 17.060 -11.469  -58.889  1.00 49.44  ? 63  PRO F O   1 
ATOM   5995  C  CB  . PRO F  1 62  ? 16.852 -14.767  -58.037  1.00 53.18  ? 63  PRO F CB  1 
ATOM   5996  C  CG  . PRO F  1 62  ? 17.363 -14.941  -59.387  1.00 55.86  ? 63  PRO F CG  1 
ATOM   5997  C  CD  . PRO F  1 62  ? 16.256 -14.523  -60.314  1.00 57.34  ? 63  PRO F CD  1 
ATOM   5998  N  N   . HIS F  1 63  ? 17.427 -12.155  -56.751  1.00 46.77  ? 64  HIS F N   1 
ATOM   5999  C  CA  . HIS F  1 63  ? 18.327 -11.075  -56.393  1.00 44.81  ? 64  HIS F CA  1 
ATOM   6000  C  C   . HIS F  1 63  ? 19.506 -11.072  -57.318  1.00 46.18  ? 64  HIS F C   1 
ATOM   6001  O  O   . HIS F  1 63  ? 20.083 -12.118  -57.556  1.00 48.02  ? 64  HIS F O   1 
ATOM   6002  C  CB  . HIS F  1 63  ? 18.840 -11.276  -54.978  1.00 43.37  ? 64  HIS F CB  1 
ATOM   6003  C  CG  . HIS F  1 63  ? 17.823 -11.002  -53.923  1.00 41.75  ? 64  HIS F CG  1 
ATOM   6004  N  ND1 . HIS F  1 63  ? 18.155 -10.466  -52.698  1.00 39.88  ? 64  HIS F ND1 1 
ATOM   6005  C  CD2 . HIS F  1 63  ? 16.483 -11.188  -53.907  1.00 42.05  ? 64  HIS F CD2 1 
ATOM   6006  C  CE1 . HIS F  1 63  ? 17.058 -10.335  -51.973  1.00 39.42  ? 64  HIS F CE1 1 
ATOM   6007  N  NE2 . HIS F  1 63  ? 16.032 -10.768  -52.682  1.00 40.55  ? 64  HIS F NE2 1 
ATOM   6008  N  N   . PHE F  1 64  ? 19.890 -9.899   -57.811  1.00 45.81  ? 65  PHE F N   1 
ATOM   6009  C  CA  . PHE F  1 64  ? 21.034 -9.794   -58.734  1.00 47.70  ? 65  PHE F CA  1 
ATOM   6010  C  C   . PHE F  1 64  ? 22.314 -10.264  -58.079  1.00 47.82  ? 65  PHE F C   1 
ATOM   6011  O  O   . PHE F  1 64  ? 22.802 -9.624   -57.153  1.00 46.16  ? 65  PHE F O   1 
ATOM   6012  C  CB  . PHE F  1 64  ? 21.222 -8.363   -59.231  1.00 47.57  ? 65  PHE F CB  1 
ATOM   6013  C  CG  . PHE F  1 64  ? 22.380 -8.188   -60.198  1.00 49.67  ? 65  PHE F CG  1 
ATOM   6014  C  CD1 . PHE F  1 64  ? 22.624 -9.109   -61.203  1.00 52.41  ? 65  PHE F CD1 1 
ATOM   6015  C  CD2 . PHE F  1 64  ? 23.181 -7.059   -60.136  1.00 49.75  ? 65  PHE F CD2 1 
ATOM   6016  C  CE1 . PHE F  1 64  ? 23.657 -8.913   -62.093  1.00 55.09  ? 65  PHE F CE1 1 
ATOM   6017  C  CE2 . PHE F  1 64  ? 24.216 -6.864   -61.030  1.00 52.25  ? 65  PHE F CE2 1 
ATOM   6018  C  CZ  . PHE F  1 64  ? 24.455 -7.788   -62.002  1.00 54.89  ? 65  PHE F CZ  1 
ATOM   6019  N  N   . ASN F  1 65  ? 22.868 -11.361  -58.590  1.00 50.33  ? 66  ASN F N   1 
ATOM   6020  C  CA  . ASN F  1 65  ? 23.931 -12.101  -57.893  1.00 51.27  ? 66  ASN F CA  1 
ATOM   6021  C  C   . ASN F  1 65  ? 25.010 -12.692  -58.821  1.00 54.89  ? 66  ASN F C   1 
ATOM   6022  O  O   . ASN F  1 65  ? 25.134 -13.920  -58.933  1.00 57.17  ? 66  ASN F O   1 
ATOM   6023  C  CB  . ASN F  1 65  ? 23.293 -13.212  -57.065  1.00 50.95  ? 66  ASN F CB  1 
ATOM   6024  C  CG  . ASN F  1 65  ? 24.287 -13.923  -56.177  1.00 51.88  ? 66  ASN F CG  1 
ATOM   6025  O  OD1 . ASN F  1 65  ? 25.411 -13.475  -56.017  1.00 52.54  ? 66  ASN F OD1 1 
ATOM   6026  N  ND2 . ASN F  1 65  ? 23.873 -15.030  -55.588  1.00 52.64  ? 66  ASN F ND2 1 
ATOM   6027  N  N   . PRO F  1 66  ? 25.807 -11.818  -59.481  1.00 55.83  ? 67  PRO F N   1 
ATOM   6028  C  CA  . PRO F  1 66  ? 26.762 -12.267  -60.500  1.00 59.55  ? 67  PRO F CA  1 
ATOM   6029  C  C   . PRO F  1 66  ? 28.003 -12.919  -59.917  1.00 61.64  ? 67  PRO F C   1 
ATOM   6030  O  O   . PRO F  1 66  ? 28.652 -13.692  -60.612  1.00 65.57  ? 67  PRO F O   1 
ATOM   6031  C  CB  . PRO F  1 66  ? 27.139 -10.973  -61.222  1.00 59.64  ? 67  PRO F CB  1 
ATOM   6032  C  CG  . PRO F  1 66  ? 26.979 -9.929   -60.205  1.00 56.44  ? 67  PRO F CG  1 
ATOM   6033  C  CD  . PRO F  1 66  ? 25.837 -10.353  -59.326  1.00 53.83  ? 67  PRO F CD  1 
ATOM   6034  N  N   . LEU F  1 67  ? 28.334 -12.605  -58.664  1.00 59.76  ? 68  LEU F N   1 
ATOM   6035  C  CA  . LEU F  1 67  ? 29.494 -13.216  -57.987  1.00 61.82  ? 68  LEU F CA  1 
ATOM   6036  C  C   . LEU F  1 67  ? 29.111 -14.472  -57.179  1.00 61.92  ? 68  LEU F C   1 
ATOM   6037  O  O   . LEU F  1 67  ? 29.887 -14.957  -56.363  1.00 63.20  ? 68  LEU F O   1 
ATOM   6038  C  CB  . LEU F  1 67  ? 30.192 -12.185  -57.097  1.00 60.67  ? 68  LEU F CB  1 
ATOM   6039  C  CG  . LEU F  1 67  ? 30.698 -10.912  -57.791  1.00 61.15  ? 68  LEU F CG  1 
ATOM   6040  C  CD1 . LEU F  1 67  ? 31.577 -10.101  -56.834  1.00 61.21  ? 68  LEU F CD1 1 
ATOM   6041  C  CD2 . LEU F  1 67  ? 31.437 -11.223  -59.079  1.00 64.93  ? 68  LEU F CD2 1 
ATOM   6042  N  N   . SER F  1 68  ? 27.899 -14.969  -57.414  1.00 60.99  ? 69  SER F N   1 
ATOM   6043  C  CA  . SER F  1 68  ? 27.439 -16.276  -56.924  1.00 62.23  ? 69  SER F CA  1 
ATOM   6044  C  C   . SER F  1 68  ? 27.567 -16.452  -55.417  1.00 60.79  ? 69  SER F C   1 
ATOM   6045  O  O   . SER F  1 68  ? 27.979 -17.511  -54.944  1.00 63.28  ? 69  SER F O   1 
ATOM   6046  C  CB  . SER F  1 68  ? 28.195 -17.405  -57.637  1.00 67.34  ? 69  SER F CB  1 
ATOM   6047  O  OG  . SER F  1 68  ? 28.265 -17.204  -59.047  1.00 69.55  ? 69  SER F OG  1 
ATOM   6048  N  N   . ARG F  1 69  ? 27.186 -15.424  -54.671  1.00 57.23  ? 70  ARG F N   1 
ATOM   6049  C  CA  . ARG F  1 69  ? 27.307 -15.444  -53.210  1.00 56.28  ? 70  ARG F CA  1 
ATOM   6050  C  C   . ARG F  1 69  ? 25.955 -15.624  -52.520  1.00 53.65  ? 70  ARG F C   1 
ATOM   6051  O  O   . ARG F  1 69  ? 24.926 -15.765  -53.177  1.00 53.08  ? 70  ARG F O   1 
ATOM   6052  C  CB  . ARG F  1 69  ? 28.048 -14.198  -52.725  1.00 55.19  ? 70  ARG F CB  1 
ATOM   6053  C  CG  . ARG F  1 69  ? 29.528 -14.189  -53.223  1.00 60.76  ? 70  ARG F CG  1 
ATOM   6054  C  CD  . ARG F  1 69  ? 30.539 -13.540  -52.244  1.00 64.01  ? 70  ARG F CD  1 
ATOM   6055  N  NE  . ARG F  1 69  ? 31.599 -12.779  -52.931  1.00 68.67  ? 70  ARG F NE  1 
ATOM   6056  C  CZ  . ARG F  1 69  ? 32.453 -11.921  -52.345  1.00 71.85  ? 70  ARG F CZ  1 
ATOM   6057  N  NH1 . ARG F  1 69  ? 32.425 -11.693  -51.025  1.00 71.04  ? 70  ARG F NH1 1 
ATOM   6058  N  NH2 . ARG F  1 69  ? 33.366 -11.281  -53.089  1.00 75.02  ? 70  ARG F NH2 1 
ATOM   6059  N  N   . LYS F  1 70  ? 25.984 -15.658  -51.195  1.00 52.72  ? 71  LYS F N   1 
ATOM   6060  C  CA  . LYS F  1 70  ? 24.786 -15.802  -50.369  1.00 50.77  ? 71  LYS F CA  1 
ATOM   6061  C  C   . LYS F  1 70  ? 24.190 -14.449  -50.057  1.00 47.37  ? 71  LYS F C   1 
ATOM   6062  O  O   . LYS F  1 70  ? 24.882 -13.444  -50.125  1.00 46.64  ? 71  LYS F O   1 
ATOM   6063  C  CB  . LYS F  1 70  ? 25.135 -16.467  -49.036  1.00 52.16  ? 71  LYS F CB  1 
ATOM   6064  C  CG  . LYS F  1 70  ? 25.813 -17.835  -49.143  1.00 56.53  ? 71  LYS F CG  1 
ATOM   6065  C  CD  . LYS F  1 70  ? 24.800 -18.975  -49.060  1.00 57.84  ? 71  LYS F CD  1 
ATOM   6066  C  CE  . LYS F  1 70  ? 25.464 -20.354  -49.104  1.00 62.55  ? 71  LYS F CE  1 
ATOM   6067  N  NZ  . LYS F  1 70  ? 24.437 -21.440  -49.059  1.00 64.03  ? 71  LYS F NZ  1 
ATOM   6068  N  N   . HIS F  1 71  ? 22.909 -14.437  -49.682  1.00 45.82  ? 72  HIS F N   1 
ATOM   6069  C  CA  . HIS F  1 71  ? 22.203 -13.187  -49.332  1.00 43.13  ? 72  HIS F CA  1 
ATOM   6070  C  C   . HIS F  1 71  ? 22.802 -12.556  -48.078  1.00 42.47  ? 72  HIS F C   1 
ATOM   6071  O  O   . HIS F  1 71  ? 23.370 -13.252  -47.224  1.00 43.75  ? 72  HIS F O   1 
ATOM   6072  C  CB  . HIS F  1 71  ? 20.696 -13.399  -49.122  1.00 42.18  ? 72  HIS F CB  1 
ATOM   6073  C  CG  . HIS F  1 71  ? 19.940 -12.133  -48.846  1.00 40.00  ? 72  HIS F CG  1 
ATOM   6074  N  ND1 . HIS F  1 71  ? 19.725 -11.166  -49.804  1.00 39.05  ? 72  HIS F ND1 1 
ATOM   6075  C  CD2 . HIS F  1 71  ? 19.346 -11.681  -47.715  1.00 38.84  ? 72  HIS F CD2 1 
ATOM   6076  C  CE1 . HIS F  1 71  ? 19.041 -10.170  -49.268  1.00 37.81  ? 72  HIS F CE1 1 
ATOM   6077  N  NE2 . HIS F  1 71  ? 18.794 -10.459  -48.005  1.00 37.27  ? 72  HIS F NE2 1 
ATOM   6078  N  N   . GLY F  1 72  ? 22.677 -11.232  -47.991  1.00 40.82  ? 73  GLY F N   1 
ATOM   6079  C  CA  . GLY F  1 72  ? 23.160 -10.494  -46.835  1.00 40.65  ? 73  GLY F CA  1 
ATOM   6080  C  C   . GLY F  1 72  ? 22.719 -9.055   -46.801  1.00 39.17  ? 73  GLY F C   1 
ATOM   6081  O  O   . GLY F  1 72  ? 21.967 -8.612   -47.651  1.00 38.31  ? 73  GLY F O   1 
ATOM   6082  N  N   . GLY F  1 73  ? 23.180 -8.346   -45.784  1.00 39.64  ? 74  GLY F N   1 
ATOM   6083  C  CA  . GLY F  1 73  ? 22.931 -6.913   -45.637  1.00 39.26  ? 74  GLY F CA  1 
ATOM   6084  C  C   . GLY F  1 73  ? 23.927 -6.137   -46.452  1.00 40.15  ? 74  GLY F C   1 
ATOM   6085  O  O   . GLY F  1 73  ? 24.952 -6.661   -46.779  1.00 41.78  ? 74  GLY F O   1 
ATOM   6086  N  N   . PRO F  1 74  ? 23.639 -4.886   -46.788  1.00 40.00  ? 75  PRO F N   1 
ATOM   6087  C  CA  . PRO F  1 74  ? 24.508 -4.160   -47.712  1.00 41.37  ? 75  PRO F CA  1 
ATOM   6088  C  C   . PRO F  1 74  ? 25.918 -3.956   -47.180  1.00 43.73  ? 75  PRO F C   1 
ATOM   6089  O  O   . PRO F  1 74  ? 26.875 -4.014   -47.929  1.00 45.24  ? 75  PRO F O   1 
ATOM   6090  C  CB  . PRO F  1 74  ? 23.796 -2.822   -47.890  1.00 41.28  ? 75  PRO F CB  1 
ATOM   6091  C  CG  . PRO F  1 74  ? 22.889 -2.715   -46.738  1.00 40.73  ? 75  PRO F CG  1 
ATOM   6092  C  CD  . PRO F  1 74  ? 22.499 -4.083   -46.351  1.00 39.37  ? 75  PRO F CD  1 
ATOM   6093  N  N   . LYS F  1 75  ? 26.034 -3.735   -45.882  1.00 44.62  ? 76  LYS F N   1 
ATOM   6094  C  CA  . LYS F  1 75  ? 27.331 -3.566   -45.243  1.00 47.35  ? 76  LYS F CA  1 
ATOM   6095  C  C   . LYS F  1 75  ? 28.091 -4.862   -45.194  1.00 48.18  ? 76  LYS F C   1 
ATOM   6096  O  O   . LYS F  1 75  ? 29.297 -4.848   -45.144  1.00 50.87  ? 76  LYS F O   1 
ATOM   6097  C  CB  . LYS F  1 75  ? 27.180 -3.089   -43.807  1.00 48.58  ? 76  LYS F CB  1 
ATOM   6098  C  CG  . LYS F  1 75  ? 26.266 -1.893   -43.611  1.00 48.69  ? 76  LYS F CG  1 
ATOM   6099  C  CD  . LYS F  1 75  ? 26.641 -1.152   -42.315  1.00 51.63  ? 76  LYS F CD  1 
ATOM   6100  C  CE  . LYS F  1 75  ? 25.598 -0.103   -41.911  1.00 51.83  ? 76  LYS F CE  1 
ATOM   6101  N  NZ  . LYS F  1 75  ? 25.783 0.365    -40.487  1.00 54.36  ? 76  LYS F NZ  1 
ATOM   6102  N  N   . ASP F  1 76  ? 27.384 -5.986   -45.148  1.00 46.58  ? 77  ASP F N   1 
ATOM   6103  C  CA  . ASP F  1 76  ? 28.029 -7.305   -45.152  1.00 47.82  ? 77  ASP F CA  1 
ATOM   6104  C  C   . ASP F  1 76  ? 28.904 -7.443   -46.403  1.00 49.22  ? 77  ASP F C   1 
ATOM   6105  O  O   . ASP F  1 76  ? 28.561 -6.942   -47.472  1.00 48.21  ? 77  ASP F O   1 
ATOM   6106  C  CB  . ASP F  1 76  ? 26.991 -8.452   -45.066  1.00 45.99  ? 77  ASP F CB  1 
ATOM   6107  C  CG  . ASP F  1 76  ? 26.362 -8.592   -43.677  1.00 45.84  ? 77  ASP F CG  1 
ATOM   6108  O  OD1 . ASP F  1 76  ? 27.037 -8.243   -42.697  1.00 48.12  ? 77  ASP F OD1 1 
ATOM   6109  O  OD2 . ASP F  1 76  ? 25.208 -9.073   -43.542  1.00 44.34  ? 77  ASP F OD2 1 
ATOM   6110  N  N   . GLU F  1 77  ? 30.055 -8.090   -46.258  1.00 52.16  ? 78  GLU F N   1 
ATOM   6111  C  CA  . GLU F  1 77  ? 30.882 -8.430   -47.411  1.00 54.02  ? 78  GLU F CA  1 
ATOM   6112  C  C   . GLU F  1 77  ? 30.251 -9.567   -48.197  1.00 52.82  ? 78  GLU F C   1 
ATOM   6113  O  O   . GLU F  1 77  ? 30.108 -9.465   -49.411  1.00 52.45  ? 78  GLU F O   1 
ATOM   6114  C  CB  . GLU F  1 77  ? 32.286 -8.847   -47.003  1.00 58.21  ? 78  GLU F CB  1 
ATOM   6115  C  CG  . GLU F  1 77  ? 33.003 -9.623   -48.129  1.00 60.98  ? 78  GLU F CG  1 
ATOM   6116  C  CD  . GLU F  1 77  ? 34.510 -9.735   -47.962  1.00 66.30  ? 78  GLU F CD  1 
ATOM   6117  O  OE1 . GLU F  1 77  ? 34.994 -9.906   -46.802  1.00 68.26  ? 78  GLU F OE1 1 
ATOM   6118  O  OE2 . GLU F  1 77  ? 35.189 -9.676   -49.025  1.00 68.54  ? 78  GLU F OE2 1 
ATOM   6119  N  N   . GLU F  1 78  ? 29.905 -10.651  -47.501  1.00 52.71  ? 79  GLU F N   1 
ATOM   6120  C  CA  . GLU F  1 78  ? 29.116 -11.742  -48.099  1.00 51.86  ? 79  GLU F CA  1 
ATOM   6121  C  C   . GLU F  1 78  ? 27.663 -11.281  -48.319  1.00 48.36  ? 79  GLU F C   1 
ATOM   6122  O  O   . GLU F  1 78  ? 26.797 -11.444  -47.447  1.00 46.80  ? 79  GLU F O   1 
ATOM   6123  C  CB  . GLU F  1 78  ? 29.154 -13.012  -47.237  1.00 53.46  ? 79  GLU F CB  1 
ATOM   6124  C  CG  . GLU F  1 78  ? 28.481 -14.256  -47.866  1.00 53.65  ? 79  GLU F CG  1 
ATOM   6125  C  CD  . GLU F  1 78  ? 29.290 -14.892  -48.978  1.00 56.78  ? 79  GLU F CD  1 
ATOM   6126  O  OE1 . GLU F  1 78  ? 30.368 -14.362  -49.293  1.00 58.88  ? 79  GLU F OE1 1 
ATOM   6127  O  OE2 . GLU F  1 78  ? 28.861 -15.925  -49.544  1.00 57.65  ? 79  GLU F OE2 1 
ATOM   6128  N  N   . ARG F  1 79  ? 27.434 -10.696  -49.495  1.00 47.47  ? 80  ARG F N   1 
ATOM   6129  C  CA  . ARG F  1 79  ? 26.121 -10.247  -49.939  1.00 44.87  ? 80  ARG F CA  1 
ATOM   6130  C  C   . ARG F  1 79  ? 25.903 -10.483  -51.424  1.00 45.31  ? 80  ARG F C   1 
ATOM   6131  O  O   . ARG F  1 79  ? 26.832 -10.757  -52.158  1.00 47.54  ? 80  ARG F O   1 
ATOM   6132  C  CB  . ARG F  1 79  ? 25.970 -8.764   -49.663  1.00 43.63  ? 80  ARG F CB  1 
ATOM   6133  C  CG  . ARG F  1 79  ? 27.034 -7.896   -50.303  1.00 45.18  ? 80  ARG F CG  1 
ATOM   6134  C  CD  . ARG F  1 79  ? 26.718 -6.409   -50.177  1.00 44.39  ? 80  ARG F CD  1 
ATOM   6135  N  NE  . ARG F  1 79  ? 25.845 -5.928   -51.247  1.00 43.32  ? 80  ARG F NE  1 
ATOM   6136  C  CZ  . ARG F  1 79  ? 25.599 -4.643   -51.508  1.00 43.34  ? 80  ARG F CZ  1 
ATOM   6137  N  NH1 . ARG F  1 79  ? 26.149 -3.679   -50.779  1.00 44.33  ? 80  ARG F NH1 1 
ATOM   6138  N  NH2 . ARG F  1 79  ? 24.799 -4.307   -52.511  1.00 42.98  ? 80  ARG F NH2 1 
ATOM   6139  N  N   . HIS F  1 80  ? 24.662 -10.372  -51.868  1.00 43.78  ? 81  HIS F N   1 
ATOM   6140  C  CA  . HIS F  1 80  ? 24.373 -10.288  -53.300  1.00 44.39  ? 81  HIS F CA  1 
ATOM   6141  C  C   . HIS F  1 80  ? 24.693 -8.871   -53.752  1.00 44.14  ? 81  HIS F C   1 
ATOM   6142  O  O   . HIS F  1 80  ? 24.518 -7.930   -52.992  1.00 42.99  ? 81  HIS F O   1 
ATOM   6143  C  CB  . HIS F  1 80  ? 22.905 -10.573  -53.620  1.00 43.33  ? 81  HIS F CB  1 
ATOM   6144  C  CG  . HIS F  1 80  ? 22.439 -11.947  -53.242  1.00 43.94  ? 81  HIS F CG  1 
ATOM   6145  N  ND1 . HIS F  1 80  ? 21.155 -12.206  -52.808  1.00 42.66  ? 81  HIS F ND1 1 
ATOM   6146  C  CD2 . HIS F  1 80  ? 23.083 -13.136  -53.235  1.00 46.05  ? 81  HIS F CD2 1 
ATOM   6147  C  CE1 . HIS F  1 80  ? 21.033 -13.495  -52.555  1.00 44.14  ? 81  HIS F CE1 1 
ATOM   6148  N  NE2 . HIS F  1 80  ? 22.187 -14.081  -52.803  1.00 46.08  ? 81  HIS F NE2 1 
ATOM   6149  N  N   . VAL F  1 81  ? 25.158 -8.718   -54.986  1.00 45.73  ? 82  VAL F N   1 
ATOM   6150  C  CA  . VAL F  1 81  ? 25.447 -7.401   -55.536  1.00 45.93  ? 82  VAL F CA  1 
ATOM   6151  C  C   . VAL F  1 81  ? 24.219 -6.509   -55.442  1.00 43.94  ? 82  VAL F C   1 
ATOM   6152  O  O   . VAL F  1 81  ? 24.320 -5.323   -55.171  1.00 43.68  ? 82  VAL F O   1 
ATOM   6153  C  CB  . VAL F  1 81  ? 25.888 -7.478   -57.003  1.00 48.30  ? 82  VAL F CB  1 
ATOM   6154  C  CG1 . VAL F  1 81  ? 26.033 -6.078   -57.595  1.00 48.71  ? 82  VAL F CG1 1 
ATOM   6155  C  CG2 . VAL F  1 81  ? 27.187 -8.221   -57.110  1.00 50.96  ? 82  VAL F CG2 1 
ATOM   6156  N  N   . GLY F  1 82  ? 23.051 -7.091   -55.654  1.00 43.13  ? 83  GLY F N   1 
ATOM   6157  C  CA  . GLY F  1 82  ? 21.796 -6.328   -55.623  1.00 42.02  ? 83  GLY F CA  1 
ATOM   6158  C  C   . GLY F  1 82  ? 21.151 -6.094   -54.266  1.00 40.22  ? 83  GLY F C   1 
ATOM   6159  O  O   . GLY F  1 82  ? 20.107 -5.447   -54.192  1.00 39.46  ? 83  GLY F O   1 
ATOM   6160  N  N   . ASP F  1 83  ? 21.766 -6.614   -53.198  1.00 39.91  ? 84  ASP F N   1 
ATOM   6161  C  CA  . ASP F  1 83  ? 21.212 -6.514   -51.840  1.00 38.40  ? 84  ASP F CA  1 
ATOM   6162  C  C   . ASP F  1 83  ? 21.428 -5.130   -51.273  1.00 38.33  ? 84  ASP F C   1 
ATOM   6163  O  O   . ASP F  1 83  ? 22.455 -4.869   -50.692  1.00 39.10  ? 84  ASP F O   1 
ATOM   6164  C  CB  . ASP F  1 83  ? 21.845 -7.541   -50.916  1.00 38.40  ? 84  ASP F CB  1 
ATOM   6165  C  CG  . ASP F  1 83  ? 21.354 -8.940   -51.175  1.00 38.58  ? 84  ASP F CG  1 
ATOM   6166  O  OD1 . ASP F  1 83  ? 20.365 -9.157   -51.894  1.00 38.07  ? 84  ASP F OD1 1 
ATOM   6167  O  OD2 . ASP F  1 83  ? 21.961 -9.869   -50.640  1.00 39.71  ? 84  ASP F OD2 1 
ATOM   6168  N  N   . LEU F  1 84  ? 20.461 -4.245   -51.460  1.00 38.08  ? 85  LEU F N   1 
ATOM   6169  C  CA  . LEU F  1 84  ? 20.537 -2.890   -50.922  1.00 38.60  ? 85  LEU F CA  1 
ATOM   6170  C  C   . LEU F  1 84  ? 19.884 -2.760   -49.541  1.00 38.05  ? 85  LEU F C   1 
ATOM   6171  O  O   . LEU F  1 84  ? 19.741 -1.666   -49.009  1.00 38.81  ? 85  LEU F O   1 
ATOM   6172  C  CB  . LEU F  1 84  ? 19.917 -1.899   -51.902  1.00 39.51  ? 85  LEU F CB  1 
ATOM   6173  C  CG  . LEU F  1 84  ? 20.772 -1.585   -53.121  1.00 40.71  ? 85  LEU F CG  1 
ATOM   6174  C  CD1 . LEU F  1 84  ? 20.030 -0.648   -54.051  1.00 41.84  ? 85  LEU F CD1 1 
ATOM   6175  C  CD2 . LEU F  1 84  ? 22.068 -0.974   -52.692  1.00 41.78  ? 85  LEU F CD2 1 
ATOM   6176  N  N   . GLY F  1 85  ? 19.491 -3.879   -48.954  1.00 37.17  ? 86  GLY F N   1 
ATOM   6177  C  CA  . GLY F  1 85  ? 18.979 -3.876   -47.589  1.00 36.97  ? 86  GLY F CA  1 
ATOM   6178  C  C   . GLY F  1 85  ? 17.539 -3.398   -47.462  1.00 36.97  ? 86  GLY F C   1 
ATOM   6179  O  O   . GLY F  1 85  ? 16.664 -3.846   -48.202  1.00 36.78  ? 86  GLY F O   1 
ATOM   6180  N  N   . ASN F  1 86  ? 17.297 -2.488   -46.514  1.00 37.72  ? 87  ASN F N   1 
ATOM   6181  C  CA  . ASN F  1 86  ? 15.941 -2.037   -46.174  1.00 38.01  ? 87  ASN F CA  1 
ATOM   6182  C  C   . ASN F  1 86  ? 15.688 -0.582   -46.439  1.00 39.44  ? 87  ASN F C   1 
ATOM   6183  O  O   . ASN F  1 86  ? 16.597 0.206    -46.512  1.00 40.26  ? 87  ASN F O   1 
ATOM   6184  C  CB  . ASN F  1 86  ? 15.647 -2.307   -44.706  1.00 38.21  ? 87  ASN F CB  1 
ATOM   6185  C  CG  . ASN F  1 86  ? 15.384 -3.767   -44.434  1.00 37.36  ? 87  ASN F CG  1 
ATOM   6186  O  OD1 . ASN F  1 86  ? 14.570 -4.397   -45.098  1.00 37.38  ? 87  ASN F OD1 1 
ATOM   6187  N  ND2 . ASN F  1 86  ? 16.065 -4.313   -43.450  1.00 37.54  ? 87  ASN F ND2 1 
ATOM   6188  N  N   . VAL F  1 87  ? 14.419 -0.252   -46.606  1.00 40.46  ? 88  VAL F N   1 
ATOM   6189  C  CA  . VAL F  1 87  ? 13.940 1.146    -46.647  1.00 42.89  ? 88  VAL F CA  1 
ATOM   6190  C  C   . VAL F  1 87  ? 12.847 1.326    -45.595  1.00 44.17  ? 88  VAL F C   1 
ATOM   6191  O  O   . VAL F  1 87  ? 12.038 0.418    -45.366  1.00 43.57  ? 88  VAL F O   1 
ATOM   6192  C  CB  . VAL F  1 87  ? 13.350 1.562    -48.035  1.00 43.74  ? 88  VAL F CB  1 
ATOM   6193  C  CG1 . VAL F  1 87  ? 14.429 1.616    -49.093  1.00 43.16  ? 88  VAL F CG1 1 
ATOM   6194  C  CG2 . VAL F  1 87  ? 12.246 0.618    -48.457  1.00 43.32  ? 88  VAL F CG2 1 
ATOM   6195  N  N   . THR F  1 88  ? 12.815 2.487    -44.959  1.00 46.45  ? 89  THR F N   1 
ATOM   6196  C  CA  . THR F  1 88  ? 11.890 2.704    -43.835  1.00 48.39  ? 89  THR F CA  1 
ATOM   6197  C  C   . THR F  1 88  ? 10.691 3.605    -44.171  1.00 51.30  ? 89  THR F C   1 
ATOM   6198  O  O   . THR F  1 88  ? 10.853 4.744    -44.644  1.00 53.42  ? 89  THR F O   1 
ATOM   6199  C  CB  . THR F  1 88  ? 12.616 3.287    -42.605  1.00 49.86  ? 89  THR F CB  1 
ATOM   6200  O  OG1 . THR F  1 88  ? 13.510 2.310    -42.053  1.00 47.84  ? 89  THR F OG1 1 
ATOM   6201  C  CG2 . THR F  1 88  ? 11.614 3.700    -41.524  1.00 52.51  ? 89  THR F CG2 1 
ATOM   6202  N  N   . ALA F  1 89  ? 9.494  3.087    -43.887  1.00 51.86  ? 90  ALA F N   1 
ATOM   6203  C  CA  . ALA F  1 89  ? 8.236  3.772    -44.191  1.00 55.01  ? 90  ALA F CA  1 
ATOM   6204  C  C   . ALA F  1 89  ? 7.615  4.398    -42.945  1.00 58.20  ? 90  ALA F C   1 
ATOM   6205  O  O   . ALA F  1 89  ? 7.436  3.710    -41.926  1.00 57.71  ? 90  ALA F O   1 
ATOM   6206  C  CB  . ALA F  1 89  ? 7.253  2.799    -44.804  1.00 54.43  ? 90  ALA F CB  1 
ATOM   6207  N  N   . ASP F  1 90  ? 7.260  5.688    -43.045  1.00 61.86  ? 91  ASP F N   1 
ATOM   6208  C  CA  . ASP F  1 90  ? 6.644  6.434    -41.927  1.00 65.66  ? 91  ASP F CA  1 
ATOM   6209  C  C   . ASP F  1 90  ? 5.111  6.390    -41.934  1.00 68.61  ? 91  ASP F C   1 
ATOM   6210  O  O   . ASP F  1 90  ? 4.488  6.104    -42.951  1.00 68.59  ? 91  ASP F O   1 
ATOM   6211  C  CB  . ASP F  1 90  ? 7.138  7.882    -41.885  1.00 68.86  ? 91  ASP F CB  1 
ATOM   6212  C  CG  . ASP F  1 90  ? 6.585  8.738    -43.012  1.00 71.75  ? 91  ASP F CG  1 
ATOM   6213  O  OD1 . ASP F  1 90  ? 6.873  9.955    -43.006  1.00 75.41  ? 91  ASP F OD1 1 
ATOM   6214  O  OD2 . ASP F  1 90  ? 5.873  8.223    -43.900  1.00 70.90  ? 91  ASP F OD2 1 
ATOM   6215  N  N   . LYS F  1 91  ? 4.529  6.668    -40.773  1.00 71.66  ? 92  LYS F N   1 
ATOM   6216  C  CA  . LYS F  1 91  ? 3.063  6.643    -40.537  1.00 75.30  ? 92  LYS F CA  1 
ATOM   6217  C  C   . LYS F  1 91  ? 2.197  6.649    -41.798  1.00 76.45  ? 92  LYS F C   1 
ATOM   6218  O  O   . LYS F  1 91  ? 1.465  5.681    -42.075  1.00 75.58  ? 92  LYS F O   1 
ATOM   6219  C  CB  . LYS F  1 91  ? 2.600  7.836    -39.663  1.00 80.92  ? 92  LYS F CB  1 
ATOM   6220  C  CG  . LYS F  1 91  ? 3.620  8.475    -38.723  1.00 81.85  ? 92  LYS F CG  1 
ATOM   6221  C  CD  . LYS F  1 91  ? 3.978  7.557    -37.541  1.00 80.14  ? 92  LYS F CD  1 
ATOM   6222  C  CE  . LYS F  1 91  ? 4.603  8.331    -36.353  1.00 82.99  ? 92  LYS F CE  1 
ATOM   6223  N  NZ  . LYS F  1 91  ? 3.601  8.848    -35.348  1.00 88.64  ? 92  LYS F NZ  1 
ATOM   6224  N  N   . ASP F  1 92  ? 2.292  7.754    -42.544  1.00 78.79  ? 93  ASP F N   1 
ATOM   6225  C  CA  . ASP F  1 92  ? 1.411  8.018    -43.692  1.00 81.41  ? 93  ASP F CA  1 
ATOM   6226  C  C   . ASP F  1 92  ? 1.862  7.287    -44.958  1.00 77.49  ? 93  ASP F C   1 
ATOM   6227  O  O   . ASP F  1 92  ? 1.460  7.644    -46.067  1.00 79.54  ? 93  ASP F O   1 
ATOM   6228  C  CB  . ASP F  1 92  ? 1.213  9.526    -43.949  1.00 86.63  ? 93  ASP F CB  1 
ATOM   6229  C  CG  . ASP F  1 92  ? 2.043  10.405   -43.022  1.00 88.13  ? 93  ASP F CG  1 
ATOM   6230  O  OD1 . ASP F  1 92  ? 3.283  10.432   -43.195  1.00 85.03  ? 93  ASP F OD1 1 
ATOM   6231  O  OD2 . ASP F  1 92  ? 1.449  11.068   -42.127  1.00 92.80  ? 93  ASP F OD2 1 
ATOM   6232  N  N   . GLY F  1 93  ? 2.685  6.256    -44.777  1.00 72.47  ? 94  GLY F N   1 
ATOM   6233  C  CA  . GLY F  1 93  ? 3.014  5.300    -45.842  1.00 68.90  ? 94  GLY F CA  1 
ATOM   6234  C  C   . GLY F  1 93  ? 4.170  5.699    -46.753  1.00 66.88  ? 94  GLY F C   1 
ATOM   6235  O  O   . GLY F  1 93  ? 4.472  4.991    -47.714  1.00 64.38  ? 94  GLY F O   1 
ATOM   6236  N  N   . VAL F  1 94  ? 4.803  6.840    -46.457  1.00 68.39  ? 95  VAL F N   1 
ATOM   6237  C  CA  . VAL F  1 94  ? 5.897  7.394    -47.262  1.00 67.10  ? 95  VAL F CA  1 
ATOM   6238  C  C   . VAL F  1 94  ? 7.267  6.919    -46.776  1.00 63.40  ? 95  VAL F C   1 
ATOM   6239  O  O   . VAL F  1 94  ? 7.582  6.973    -45.580  1.00 63.17  ? 95  VAL F O   1 
ATOM   6240  C  CB  . VAL F  1 94  ? 5.885  8.939    -47.223  1.00 71.53  ? 95  VAL F CB  1 
ATOM   6241  C  CG1 . VAL F  1 94  ? 7.266  9.523    -47.622  1.00 69.84  ? 95  VAL F CG1 1 
ATOM   6242  C  CG2 . VAL F  1 94  ? 4.756  9.473    -48.101  1.00 75.18  ? 95  VAL F CG2 1 
ATOM   6243  N  N   . ALA F  1 95  ? 8.092  6.495    -47.728  1.00 60.79  ? 96  ALA F N   1 
ATOM   6244  C  CA  . ALA F  1 95  ? 9.447  6.055    -47.426  1.00 57.42  ? 96  ALA F CA  1 
ATOM   6245  C  C   . ALA F  1 95  ? 10.396 6.961    -48.187  1.00 58.42  ? 96  ALA F C   1 
ATOM   6246  O  O   . ALA F  1 95  ? 10.465 6.896    -49.416  1.00 58.17  ? 96  ALA F O   1 
ATOM   6247  C  CB  . ALA F  1 95  ? 9.640  4.630    -47.838  1.00 53.69  ? 96  ALA F CB  1 
ATOM   6248  N  N   . ASP F  1 96  ? 11.087 7.840    -47.463  1.00 60.04  ? 97  ASP F N   1 
ATOM   6249  C  CA  . ASP F  1 96  ? 12.012 8.793    -48.100  1.00 61.86  ? 97  ASP F CA  1 
ATOM   6250  C  C   . ASP F  1 96  ? 13.378 8.174    -48.251  1.00 58.80  ? 97  ASP F C   1 
ATOM   6251  O  O   . ASP F  1 96  ? 14.201 8.276    -47.352  1.00 58.95  ? 97  ASP F O   1 
ATOM   6252  C  CB  . ASP F  1 96  ? 12.094 10.101   -47.307  1.00 66.16  ? 97  ASP F CB  1 
ATOM   6253  C  CG  . ASP F  1 96  ? 10.931 11.048   -47.625  1.00 71.25  ? 97  ASP F CG  1 
ATOM   6254  O  OD1 . ASP F  1 96  ? 10.671 11.259   -48.846  1.00 72.31  ? 97  ASP F OD1 1 
ATOM   6255  O  OD2 . ASP F  1 96  ? 10.283 11.575   -46.666  1.00 74.45  ? 97  ASP F OD2 1 
ATOM   6256  N  N   . VAL F  1 97  ? 13.607 7.525    -49.393  1.00 56.64  ? 98  VAL F N   1 
ATOM   6257  C  CA  . VAL F  1 97  ? 14.816 6.716    -49.607  1.00 53.67  ? 98  VAL F CA  1 
ATOM   6258  C  C   . VAL F  1 97  ? 16.051 7.577    -49.783  1.00 55.52  ? 98  VAL F C   1 
ATOM   6259  O  O   . VAL F  1 97  ? 16.027 8.524    -50.578  1.00 58.33  ? 98  VAL F O   1 
ATOM   6260  C  CB  . VAL F  1 97  ? 14.700 5.846    -50.866  1.00 51.74  ? 98  VAL F CB  1 
ATOM   6261  C  CG1 . VAL F  1 97  ? 15.952 5.015    -51.057  1.00 49.40  ? 98  VAL F CG1 1 
ATOM   6262  C  CG2 . VAL F  1 97  ? 13.505 4.947    -50.775  1.00 50.62  ? 98  VAL F CG2 1 
ATOM   6263  N  N   . SER F  1 98  ? 17.113 7.244    -49.040  1.00 54.45  ? 99  SER F N   1 
ATOM   6264  C  CA  . SER F  1 98  ? 18.442 7.866    -49.222  1.00 56.29  ? 99  SER F CA  1 
ATOM   6265  C  C   . SER F  1 98  ? 19.540 6.907    -48.822  1.00 54.08  ? 99  SER F C   1 
ATOM   6266  O  O   . SER F  1 98  ? 19.985 6.895    -47.685  1.00 54.66  ? 99  SER F O   1 
ATOM   6267  C  CB  . SER F  1 98  ? 18.597 9.164    -48.416  1.00 60.44  ? 99  SER F CB  1 
ATOM   6268  O  OG  . SER F  1 98  ? 19.937 9.660    -48.485  1.00 62.03  ? 99  SER F OG  1 
ATOM   6269  N  N   . ILE F  1 99  ? 19.970 6.102    -49.775  1.00 52.13  ? 100 ILE F N   1 
ATOM   6270  C  CA  . ILE F  1 99  ? 21.024 5.133    -49.565  1.00 50.34  ? 100 ILE F CA  1 
ATOM   6271  C  C   . ILE F  1 99  ? 22.254 5.576    -50.322  1.00 52.35  ? 100 ILE F C   1 
ATOM   6272  O  O   . ILE F  1 99  ? 22.154 6.330    -51.270  1.00 54.48  ? 100 ILE F O   1 
ATOM   6273  C  CB  . ILE F  1 99  ? 20.589 3.767    -50.074  1.00 47.13  ? 100 ILE F CB  1 
ATOM   6274  C  CG1 . ILE F  1 99  ? 19.451 3.226    -49.224  1.00 45.55  ? 100 ILE F CG1 1 
ATOM   6275  C  CG2 . ILE F  1 99  ? 21.726 2.794    -50.028  1.00 46.35  ? 100 ILE F CG2 1 
ATOM   6276  C  CD1 . ILE F  1 99  ? 19.242 1.739    -49.374  1.00 42.89  ? 100 ILE F CD1 1 
ATOM   6277  N  N   . GLU F  1 100 ? 23.419 5.120    -49.888  1.00 52.50  ? 101 GLU F N   1 
ATOM   6278  C  CA  . GLU F  1 100 ? 24.651 5.245    -50.669  1.00 54.31  ? 101 GLU F CA  1 
ATOM   6279  C  C   . GLU F  1 100 ? 25.364 3.886    -50.653  1.00 52.33  ? 101 GLU F C   1 
ATOM   6280  O  O   . GLU F  1 100 ? 25.590 3.317    -49.589  1.00 51.64  ? 101 GLU F O   1 
ATOM   6281  C  CB  . GLU F  1 100 ? 25.541 6.358    -50.103  1.00 58.26  ? 101 GLU F CB  1 
ATOM   6282  C  CG  . GLU F  1 100 ? 26.793 6.652    -50.946  1.00 61.54  ? 101 GLU F CG  1 
ATOM   6283  C  CD  . GLU F  1 100 ? 27.569 7.922    -50.508  1.00 66.82  ? 101 GLU F CD  1 
ATOM   6284  O  OE1 . GLU F  1 100 ? 28.536 8.302    -51.219  1.00 69.52  ? 101 GLU F OE1 1 
ATOM   6285  O  OE2 . GLU F  1 100 ? 27.227 8.539    -49.466  1.00 68.22  ? 101 GLU F OE2 1 
ATOM   6286  N  N   . ASP F  1 101 ? 25.687 3.357    -51.830  1.00 51.89  ? 102 ASP F N   1 
ATOM   6287  C  CA  . ASP F  1 101 ? 26.228 2.003    -51.932  1.00 50.46  ? 102 ASP F CA  1 
ATOM   6288  C  C   . ASP F  1 101 ? 27.413 1.865    -52.893  1.00 52.57  ? 102 ASP F C   1 
ATOM   6289  O  O   . ASP F  1 101 ? 27.476 2.536    -53.903  1.00 54.17  ? 102 ASP F O   1 
ATOM   6290  C  CB  . ASP F  1 101 ? 25.143 1.029    -52.355  1.00 47.47  ? 102 ASP F CB  1 
ATOM   6291  C  CG  . ASP F  1 101 ? 25.539 -0.413   -52.111  1.00 46.07  ? 102 ASP F CG  1 
ATOM   6292  O  OD1 . ASP F  1 101 ? 25.637 -0.821   -50.941  1.00 45.29  ? 102 ASP F OD1 1 
ATOM   6293  O  OD2 . ASP F  1 101 ? 25.770 -1.145   -53.082  1.00 45.98  ? 102 ASP F OD2 1 
ATOM   6294  N  N   . SER F  1 102 ? 28.330 0.957    -52.562  1.00 52.95  ? 103 SER F N   1 
ATOM   6295  C  CA  . SER F  1 102 ? 29.607 0.794    -53.265  1.00 55.60  ? 103 SER F CA  1 
ATOM   6296  C  C   . SER F  1 102 ? 29.750 -0.503   -54.037  1.00 54.69  ? 103 SER F C   1 
ATOM   6297  O  O   . SER F  1 102 ? 30.673 -0.648   -54.816  1.00 57.12  ? 103 SER F O   1 
ATOM   6298  C  CB  . SER F  1 102 ? 30.751 0.855    -52.261  1.00 58.06  ? 103 SER F CB  1 
ATOM   6299  O  OG  . SER F  1 102 ? 30.675 2.020    -51.472  1.00 59.82  ? 103 SER F OG  1 
ATOM   6300  N  N   . VAL F  1 103 ? 28.862 -1.459   -53.800  1.00 51.83  ? 104 VAL F N   1 
ATOM   6301  C  CA  . VAL F  1 103 ? 28.888 -2.735   -54.522  1.00 51.37  ? 104 VAL F CA  1 
ATOM   6302  C  C   . VAL F  1 103 ? 28.172 -2.649   -55.856  1.00 51.21  ? 104 VAL F C   1 
ATOM   6303  O  O   . VAL F  1 103 ? 28.688 -3.133   -56.850  1.00 53.10  ? 104 VAL F O   1 
ATOM   6304  C  CB  . VAL F  1 103 ? 28.225 -3.862   -53.743  1.00 48.96  ? 104 VAL F CB  1 
ATOM   6305  C  CG1 . VAL F  1 103 ? 28.293 -5.158   -54.518  1.00 49.27  ? 104 VAL F CG1 1 
ATOM   6306  C  CG2 . VAL F  1 103 ? 28.897 -4.038   -52.414  1.00 50.00  ? 104 VAL F CG2 1 
ATOM   6307  N  N   . ILE F  1 104 ? 26.979 -2.055   -55.881  1.00 49.50  ? 105 ILE F N   1 
ATOM   6308  C  CA  . ILE F  1 104 ? 26.266 -1.848   -57.148  1.00 49.68  ? 105 ILE F CA  1 
ATOM   6309  C  C   . ILE F  1 104 ? 27.009 -0.851   -58.019  1.00 52.66  ? 105 ILE F C   1 
ATOM   6310  O  O   . ILE F  1 104 ? 27.807 -0.055   -57.527  1.00 54.18  ? 105 ILE F O   1 
ATOM   6311  C  CB  . ILE F  1 104 ? 24.817 -1.333   -56.966  1.00 47.90  ? 105 ILE F CB  1 
ATOM   6312  C  CG1 . ILE F  1 104 ? 24.784 0.050    -56.298  1.00 48.52  ? 105 ILE F CG1 1 
ATOM   6313  C  CG2 . ILE F  1 104 ? 24.004 -2.337   -56.196  1.00 45.39  ? 105 ILE F CG2 1 
ATOM   6314  C  CD1 . ILE F  1 104 ? 23.500 0.785    -56.510  1.00 47.87  ? 105 ILE F CD1 1 
ATOM   6315  N  N   . SER F  1 105 ? 26.734 -0.879   -59.314  1.00 53.94  ? 106 SER F N   1 
ATOM   6316  C  CA  . SER F  1 105 ? 27.305 0.116    -60.218  1.00 57.15  ? 106 SER F CA  1 
ATOM   6317  C  C   . SER F  1 105 ? 26.434 0.382    -61.442  1.00 58.15  ? 106 SER F C   1 
ATOM   6318  O  O   . SER F  1 105 ? 25.622 -0.466   -61.853  1.00 56.96  ? 106 SER F O   1 
ATOM   6319  C  CB  . SER F  1 105 ? 28.691 -0.303   -60.670  1.00 59.85  ? 106 SER F CB  1 
ATOM   6320  O  OG  . SER F  1 105 ? 29.328 0.761    -61.350  1.00 63.15  ? 106 SER F OG  1 
ATOM   6321  N  N   . LEU F  1 106 ? 26.618 1.574    -62.017  1.00 60.68  ? 107 LEU F N   1 
ATOM   6322  C  CA  . LEU F  1 106 ? 25.948 1.951    -63.266  1.00 62.47  ? 107 LEU F CA  1 
ATOM   6323  C  C   . LEU F  1 106 ? 26.803 1.656    -64.507  1.00 65.67  ? 107 LEU F C   1 
ATOM   6324  O  O   . LEU F  1 106 ? 26.525 2.175    -65.590  1.00 68.22  ? 107 LEU F O   1 
ATOM   6325  C  CB  . LEU F  1 106 ? 25.562 3.434    -63.226  1.00 63.97  ? 107 LEU F CB  1 
ATOM   6326  C  CG  . LEU F  1 106 ? 24.626 3.829    -62.081  1.00 61.22  ? 107 LEU F CG  1 
ATOM   6327  C  CD1 . LEU F  1 106 ? 24.269 5.310    -62.196  1.00 63.80  ? 107 LEU F CD1 1 
ATOM   6328  C  CD2 . LEU F  1 106 ? 23.374 2.967    -62.074  1.00 58.40  ? 107 LEU F CD2 1 
ATOM   6329  N  N   . SER F  1 107 ? 27.832 0.823    -64.335  1.00 65.95  ? 108 SER F N   1 
ATOM   6330  C  CA  . SER F  1 107 ? 28.753 0.460    -65.417  1.00 69.32  ? 108 SER F CA  1 
ATOM   6331  C  C   . SER F  1 107 ? 29.551 -0.798   -65.100  1.00 69.05  ? 108 SER F C   1 
ATOM   6332  O  O   . SER F  1 107 ? 29.992 -1.008   -63.973  1.00 67.45  ? 108 SER F O   1 
ATOM   6333  C  CB  . SER F  1 107 ? 29.719 1.616    -65.745  1.00 73.00  ? 108 SER F CB  1 
ATOM   6334  O  OG  . SER F  1 107 ? 30.477 2.040    -64.619  1.00 72.55  ? 108 SER F OG  1 
ATOM   6335  N  N   . GLY F  1 108 ? 29.721 -1.639   -66.110  1.00 71.23  ? 109 GLY F N   1 
ATOM   6336  C  CA  . GLY F  1 108 ? 30.601 -2.811   -66.010  1.00 72.43  ? 109 GLY F CA  1 
ATOM   6337  C  C   . GLY F  1 108 ? 29.968 -4.110   -65.534  1.00 69.92  ? 109 GLY F C   1 
ATOM   6338  O  O   . GLY F  1 108 ? 28.776 -4.348   -65.737  1.00 68.18  ? 109 GLY F O   1 
ATOM   6339  N  N   . ASP F  1 109 ? 30.794 -4.960   -64.924  1.00 70.36  ? 110 ASP F N   1 
ATOM   6340  C  CA  . ASP F  1 109 ? 30.378 -6.295   -64.443  1.00 68.91  ? 110 ASP F CA  1 
ATOM   6341  C  C   . ASP F  1 109 ? 29.138 -6.238   -63.514  1.00 64.33  ? 110 ASP F C   1 
ATOM   6342  O  O   . ASP F  1 109 ? 28.217 -7.064   -63.588  1.00 62.80  ? 110 ASP F O   1 
ATOM   6343  C  CB  . ASP F  1 109 ? 31.557 -6.924   -63.683  1.00 70.31  ? 110 ASP F CB  1 
ATOM   6344  C  CG  . ASP F  1 109 ? 31.563 -8.442   -63.733  1.00 71.88  ? 110 ASP F CG  1 
ATOM   6345  O  OD1 . ASP F  1 109 ? 30.985 -9.092   -62.808  1.00 69.27  ? 110 ASP F OD1 1 
ATOM   6346  O  OD2 . ASP F  1 109 ? 32.179 -8.974   -64.690  1.00 76.03  ? 110 ASP F OD2 1 
ATOM   6347  N  N   . HIS F  1 110 ? 29.161 -5.243   -62.635  1.00 62.43  ? 111 HIS F N   1 
ATOM   6348  C  CA  . HIS F  1 110 ? 28.136 -5.017   -61.618  1.00 58.70  ? 111 HIS F CA  1 
ATOM   6349  C  C   . HIS F  1 110 ? 27.006 -4.118   -62.129  1.00 57.76  ? 111 HIS F C   1 
ATOM   6350  O  O   . HIS F  1 110 ? 26.191 -3.650   -61.341  1.00 55.29  ? 111 HIS F O   1 
ATOM   6351  C  CB  . HIS F  1 110 ? 28.785 -4.332   -60.393  1.00 57.94  ? 111 HIS F CB  1 
ATOM   6352  C  CG  . HIS F  1 110 ? 29.756 -5.195   -59.632  1.00 58.77  ? 111 HIS F CG  1 
ATOM   6353  N  ND1 . HIS F  1 110 ? 30.248 -4.844   -58.391  1.00 57.97  ? 111 HIS F ND1 1 
ATOM   6354  C  CD2 . HIS F  1 110 ? 30.309 -6.395   -59.928  1.00 60.69  ? 111 HIS F CD2 1 
ATOM   6355  C  CE1 . HIS F  1 110 ? 31.060 -5.790   -57.957  1.00 59.34  ? 111 HIS F CE1 1 
ATOM   6356  N  NE2 . HIS F  1 110 ? 31.117 -6.741   -58.871  1.00 61.15  ? 111 HIS F NE2 1 
ATOM   6357  N  N   . CYS F  1 111 ? 26.968 -3.862   -63.435  1.00 60.20  ? 112 CYS F N   1 
ATOM   6358  C  CA  . CYS F  1 111 ? 26.010 -2.909   -64.009  1.00 60.23  ? 112 CYS F CA  1 
ATOM   6359  C  C   . CYS F  1 111 ? 24.571 -3.319   -63.736  1.00 57.79  ? 112 CYS F C   1 
ATOM   6360  O  O   . CYS F  1 111 ? 24.121 -4.374   -64.191  1.00 58.05  ? 112 CYS F O   1 
ATOM   6361  C  CB  . CYS F  1 111 ? 26.213 -2.773   -65.512  1.00 63.94  ? 112 CYS F CB  1 
ATOM   6362  S  SG  . CYS F  1 111 ? 25.286 -1.418   -66.264  1.00 65.22  ? 112 CYS F SG  1 
ATOM   6363  N  N   . ILE F  1 112 ? 23.863 -2.469   -62.990  1.00 55.85  ? 113 ILE F N   1 
ATOM   6364  C  CA  . ILE F  1 112 ? 22.449 -2.713   -62.631  1.00 53.98  ? 113 ILE F CA  1 
ATOM   6365  C  C   . ILE F  1 112 ? 21.445 -2.156   -63.655  1.00 55.79  ? 113 ILE F C   1 
ATOM   6366  O  O   . ILE F  1 112 ? 20.247 -2.432   -63.579  1.00 54.98  ? 113 ILE F O   1 
ATOM   6367  C  CB  . ILE F  1 112 ? 22.091 -2.125   -61.230  1.00 51.42  ? 113 ILE F CB  1 
ATOM   6368  C  CG1 . ILE F  1 112 ? 22.300 -0.602   -61.175  1.00 52.33  ? 113 ILE F CG1 1 
ATOM   6369  C  CG2 . ILE F  1 112 ? 22.905 -2.816   -60.136  1.00 49.79  ? 113 ILE F CG2 1 
ATOM   6370  C  CD1 . ILE F  1 112 ? 21.456 0.077    -60.104  1.00 50.72  ? 113 ILE F CD1 1 
ATOM   6371  N  N   . ILE F  1 113 ? 21.948 -1.352   -64.591  1.00 58.59  ? 114 ILE F N   1 
ATOM   6372  C  CA  . ILE F  1 113 ? 21.112 -0.736   -65.618  1.00 60.78  ? 114 ILE F CA  1 
ATOM   6373  C  C   . ILE F  1 113 ? 20.532 -1.821   -66.502  1.00 62.07  ? 114 ILE F C   1 
ATOM   6374  O  O   . ILE F  1 113 ? 21.225 -2.731   -66.947  1.00 62.98  ? 114 ILE F O   1 
ATOM   6375  C  CB  . ILE F  1 113 ? 21.885 0.279    -66.480  1.00 63.97  ? 114 ILE F CB  1 
ATOM   6376  C  CG1 . ILE F  1 113 ? 22.157 1.561    -65.663  1.00 63.63  ? 114 ILE F CG1 1 
ATOM   6377  C  CG2 . ILE F  1 113 ? 21.116 0.589    -67.735  1.00 67.00  ? 114 ILE F CG2 1 
ATOM   6378  C  CD1 . ILE F  1 113 ? 23.100 2.578    -66.349  1.00 67.34  ? 114 ILE F CD1 1 
ATOM   6379  N  N   . GLY F  1 114 ? 19.237 -1.711   -66.737  1.00 62.66  ? 115 GLY F N   1 
ATOM   6380  C  CA  . GLY F  1 114 ? 18.514 -2.682   -67.536  1.00 64.46  ? 115 GLY F CA  1 
ATOM   6381  C  C   . GLY F  1 114 ? 18.009 -3.820   -66.694  1.00 62.00  ? 115 GLY F C   1 
ATOM   6382  O  O   . GLY F  1 114 ? 17.472 -4.788   -67.207  1.00 63.55  ? 115 GLY F O   1 
ATOM   6383  N  N   . ARG F  1 115 ? 18.177 -3.696   -65.390  1.00 58.67  ? 116 ARG F N   1 
ATOM   6384  C  CA  . ARG F  1 115 ? 17.634 -4.669   -64.454  1.00 56.62  ? 116 ARG F CA  1 
ATOM   6385  C  C   . ARG F  1 115 ? 16.531 -4.035   -63.591  1.00 55.00  ? 116 ARG F C   1 
ATOM   6386  O  O   . ARG F  1 115 ? 16.309 -2.823   -63.611  1.00 55.30  ? 116 ARG F O   1 
ATOM   6387  C  CB  . ARG F  1 115 ? 18.755 -5.236   -63.581  1.00 54.48  ? 116 ARG F CB  1 
ATOM   6388  C  CG  . ARG F  1 115 ? 19.909 -5.804   -64.394  1.00 56.64  ? 116 ARG F CG  1 
ATOM   6389  C  CD  . ARG F  1 115 ? 20.977 -6.459   -63.522  1.00 55.19  ? 116 ARG F CD  1 
ATOM   6390  N  NE  . ARG F  1 115 ? 22.159 -6.825   -64.304  1.00 57.50  ? 116 ARG F NE  1 
ATOM   6391  C  CZ  . ARG F  1 115 ? 22.295 -7.945   -65.010  1.00 59.80  ? 116 ARG F CZ  1 
ATOM   6392  N  NH1 . ARG F  1 115 ? 21.333 -8.860   -65.052  1.00 60.11  ? 116 ARG F NH1 1 
ATOM   6393  N  NH2 . ARG F  1 115 ? 23.418 -8.149   -65.683  1.00 62.62  ? 116 ARG F NH2 1 
ATOM   6394  N  N   . THR F  1 116 ? 15.858 -4.876   -62.822  1.00 53.61  ? 117 THR F N   1 
ATOM   6395  C  CA  . THR F  1 116 ? 14.686 -4.460   -62.043  1.00 52.73  ? 117 THR F CA  1 
ATOM   6396  C  C   . THR F  1 116 ? 14.990 -4.123   -60.562  1.00 49.59  ? 117 THR F C   1 
ATOM   6397  O  O   . THR F  1 116 ? 15.619 -4.904   -59.842  1.00 47.94  ? 117 THR F O   1 
ATOM   6398  C  CB  . THR F  1 116 ? 13.589 -5.562   -62.062  1.00 53.75  ? 117 THR F CB  1 
ATOM   6399  O  OG1 . THR F  1 116 ? 13.142 -5.787   -63.400  1.00 57.00  ? 117 THR F OG1 1 
ATOM   6400  C  CG2 . THR F  1 116 ? 12.396 -5.158   -61.202  1.00 53.04  ? 117 THR F CG2 1 
ATOM   6401  N  N   . LEU F  1 117 ? 14.516 -2.965   -60.120  1.00 49.39  ? 118 LEU F N   1 
ATOM   6402  C  CA  . LEU F  1 117 ? 14.497 -2.609   -58.699  1.00 47.04  ? 118 LEU F CA  1 
ATOM   6403  C  C   . LEU F  1 117 ? 13.195 -3.112   -58.134  1.00 46.94  ? 118 LEU F C   1 
ATOM   6404  O  O   . LEU F  1 117 ? 12.237 -3.168   -58.855  1.00 49.45  ? 118 LEU F O   1 
ATOM   6405  C  CB  . LEU F  1 117 ? 14.581 -1.098   -58.524  1.00 47.74  ? 118 LEU F CB  1 
ATOM   6406  C  CG  . LEU F  1 117 ? 14.682 -0.587   -57.089  1.00 45.80  ? 118 LEU F CG  1 
ATOM   6407  C  CD1 . LEU F  1 117 ? 15.878 -1.189   -56.432  1.00 43.94  ? 118 LEU F CD1 1 
ATOM   6408  C  CD2 . LEU F  1 117 ? 14.785 0.924    -57.030  1.00 47.18  ? 118 LEU F CD2 1 
ATOM   6409  N  N   . VAL F  1 118 ? 13.150 -3.475   -56.861  1.00 44.84  ? 119 VAL F N   1 
ATOM   6410  C  CA  . VAL F  1 118 ? 11.955 -4.104   -56.270  1.00 44.99  ? 119 VAL F CA  1 
ATOM   6411  C  C   . VAL F  1 118 ? 11.811 -3.773   -54.795  1.00 43.54  ? 119 VAL F C   1 
ATOM   6412  O  O   . VAL F  1 118 ? 12.713 -4.046   -54.019  1.00 42.00  ? 119 VAL F O   1 
ATOM   6413  C  CB  . VAL F  1 118 ? 12.020 -5.634   -56.396  1.00 44.78  ? 119 VAL F CB  1 
ATOM   6414  C  CG1 . VAL F  1 118 ? 10.960 -6.295   -55.586  1.00 45.08  ? 119 VAL F CG1 1 
ATOM   6415  C  CG2 . VAL F  1 118 ? 11.873 -6.040   -57.807  1.00 47.26  ? 119 VAL F CG2 1 
ATOM   6416  N  N   . VAL F  1 119 ? 10.683 -3.199   -54.396  1.00 44.70  ? 120 VAL F N   1 
ATOM   6417  C  CA  . VAL F  1 119 ? 10.405 -2.947   -52.975  1.00 43.75  ? 120 VAL F CA  1 
ATOM   6418  C  C   . VAL F  1 119 ? 9.495  -4.042   -52.462  1.00 44.11  ? 120 VAL F C   1 
ATOM   6419  O  O   . VAL F  1 119 ? 8.654  -4.532   -53.184  1.00 46.09  ? 120 VAL F O   1 
ATOM   6420  C  CB  . VAL F  1 119 ? 9.775  -1.582   -52.753  1.00 45.47  ? 120 VAL F CB  1 
ATOM   6421  C  CG1 . VAL F  1 119 ? 8.361  -1.568   -53.232  1.00 48.69  ? 120 VAL F CG1 1 
ATOM   6422  C  CG2 . VAL F  1 119 ? 9.834  -1.213   -51.307  1.00 44.66  ? 120 VAL F CG2 1 
ATOM   6423  N  N   . HIS F  1 120 ? 9.649  -4.419   -51.209  1.00 42.89  ? 121 HIS F N   1 
ATOM   6424  C  CA  . HIS F  1 120 ? 9.114  -5.698   -50.712  1.00 43.14  ? 121 HIS F CA  1 
ATOM   6425  C  C   . HIS F  1 120 ? 8.095  -5.633   -49.593  1.00 44.23  ? 121 HIS F C   1 
ATOM   6426  O  O   . HIS F  1 120 ? 8.016  -4.648   -48.873  1.00 44.34  ? 121 HIS F O   1 
ATOM   6427  C  CB  . HIS F  1 120 ? 10.261 -6.562   -50.223  1.00 41.26  ? 121 HIS F CB  1 
ATOM   6428  C  CG  . HIS F  1 120 ? 10.871 -7.397   -51.293  1.00 41.00  ? 121 HIS F CG  1 
ATOM   6429  N  ND1 . HIS F  1 120 ? 10.689 -8.757   -51.360  1.00 42.15  ? 121 HIS F ND1 1 
ATOM   6430  C  CD2 . HIS F  1 120 ? 11.631 -7.065   -52.356  1.00 40.70  ? 121 HIS F CD2 1 
ATOM   6431  C  CE1 . HIS F  1 120 ? 11.326 -9.233   -52.414  1.00 42.38  ? 121 HIS F CE1 1 
ATOM   6432  N  NE2 . HIS F  1 120 ? 11.898 -8.223   -53.040  1.00 41.52  ? 121 HIS F NE2 1 
ATOM   6433  N  N   . GLU F  1 121 ? 7.349  -6.724   -49.441  1.00 45.47  ? 122 GLU F N   1 
ATOM   6434  C  CA  . GLU F  1 121 ? 6.239  -6.812   -48.488  1.00 47.30  ? 122 GLU F CA  1 
ATOM   6435  C  C   . GLU F  1 121 ? 6.719  -6.587   -47.055  1.00 45.94  ? 122 GLU F C   1 
ATOM   6436  O  O   . GLU F  1 121 ? 6.305  -5.636   -46.384  1.00 46.75  ? 122 GLU F O   1 
ATOM   6437  C  CB  . GLU F  1 121 ? 5.549  -8.179   -48.610  1.00 49.10  ? 122 GLU F CB  1 
ATOM   6438  C  CG  . GLU F  1 121 ? 4.438  -8.456   -47.573  1.00 51.45  ? 122 GLU F CG  1 
ATOM   6439  C  CD  . GLU F  1 121 ? 3.945  -9.910   -47.576  1.00 53.64  ? 122 GLU F CD  1 
ATOM   6440  O  OE1 . GLU F  1 121 ? 4.533  -10.764  -48.276  1.00 53.19  ? 122 GLU F OE1 1 
ATOM   6441  O  OE2 . GLU F  1 121 ? 2.972  -10.209  -46.858  1.00 56.03  ? 122 GLU F OE2 1 
ATOM   6442  N  N   . LYS F  1 122 ? 7.585  -7.489   -46.600  1.00 44.41  ? 123 LYS F N   1 
ATOM   6443  C  CA  . LYS F  1 122 ? 8.122  -7.484   -45.233  1.00 43.43  ? 123 LYS F CA  1 
ATOM   6444  C  C   . LYS F  1 122 ? 9.508  -6.868   -45.240  1.00 41.37  ? 123 LYS F C   1 
ATOM   6445  O  O   . LYS F  1 122 ? 10.017 -6.487   -46.298  1.00 40.82  ? 123 LYS F O   1 
ATOM   6446  C  CB  . LYS F  1 122 ? 8.235  -8.910   -44.670  1.00 43.65  ? 123 LYS F CB  1 
ATOM   6447  C  CG  . LYS F  1 122 ? 6.989  -9.772   -44.778  1.00 46.40  ? 123 LYS F CG  1 
ATOM   6448  C  CD  . LYS F  1 122 ? 7.221  -11.176  -44.223  1.00 47.09  ? 123 LYS F CD  1 
ATOM   6449  C  CE  . LYS F  1 122 ? 6.031  -12.117  -44.518  1.00 50.37  ? 123 LYS F CE  1 
ATOM   6450  N  NZ  . LYS F  1 122 ? 6.081  -13.411  -43.746  1.00 51.71  ? 123 LYS F NZ  1 
ATOM   6451  N  N   . ALA F  1 123 ? 10.127 -6.800   -44.062  1.00 40.68  ? 124 ALA F N   1 
ATOM   6452  C  CA  . ALA F  1 123 ? 11.498 -6.303   -43.931  1.00 39.05  ? 124 ALA F CA  1 
ATOM   6453  C  C   . ALA F  1 123 ? 12.508 -7.390   -44.270  1.00 38.00  ? 124 ALA F C   1 
ATOM   6454  O  O   . ALA F  1 123 ? 12.277 -8.560   -44.003  1.00 38.36  ? 124 ALA F O   1 
ATOM   6455  C  CB  . ALA F  1 123 ? 11.736 -5.794   -42.539  1.00 39.47  ? 124 ALA F CB  1 
ATOM   6456  N  N   . ASP F  1 124 ? 13.627 -6.985   -44.864  1.00 37.15  ? 125 ASP F N   1 
ATOM   6457  C  CA  . ASP F  1 124 ? 14.765 -7.875   -45.155  1.00 36.61  ? 125 ASP F CA  1 
ATOM   6458  C  C   . ASP F  1 124 ? 15.545 -8.145   -43.866  1.00 36.87  ? 125 ASP F C   1 
ATOM   6459  O  O   . ASP F  1 124 ? 16.013 -7.212   -43.222  1.00 37.01  ? 125 ASP F O   1 
ATOM   6460  C  CB  . ASP F  1 124 ? 15.687 -7.231   -46.210  1.00 36.06  ? 125 ASP F CB  1 
ATOM   6461  C  CG  . ASP F  1 124 ? 16.862 -8.134   -46.635  1.00 36.10  ? 125 ASP F CG  1 
ATOM   6462  O  OD1 . ASP F  1 124 ? 17.001 -9.223   -46.059  1.00 36.60  ? 125 ASP F OD1 1 
ATOM   6463  O  OD2 . ASP F  1 124 ? 17.666 -7.754   -47.530  1.00 35.80  ? 125 ASP F OD2 1 
ATOM   6464  N  N   . ASP F  1 125 ? 15.692 -9.418   -43.494  1.00 37.42  ? 126 ASP F N   1 
ATOM   6465  C  CA  . ASP F  1 125 ? 16.368 -9.789   -42.232  1.00 38.13  ? 126 ASP F CA  1 
ATOM   6466  C  C   . ASP F  1 125 ? 17.903 -9.764   -42.358  1.00 38.18  ? 126 ASP F C   1 
ATOM   6467  O  O   . ASP F  1 125 ? 18.620 -10.189  -41.458  1.00 39.17  ? 126 ASP F O   1 
ATOM   6468  C  CB  . ASP F  1 125 ? 15.888 -11.153  -41.718  1.00 39.25  ? 126 ASP F CB  1 
ATOM   6469  C  CG  . ASP F  1 125 ? 16.464 -12.301  -42.488  1.00 39.70  ? 126 ASP F CG  1 
ATOM   6470  O  OD1 . ASP F  1 125 ? 17.541 -12.150  -43.100  1.00 39.41  ? 126 ASP F OD1 1 
ATOM   6471  O  OD2 . ASP F  1 125 ? 15.838 -13.372  -42.461  1.00 40.75  ? 126 ASP F OD2 1 
ATOM   6472  N  N   . LEU F  1 126 ? 18.388 -9.271   -43.489  1.00 37.41  ? 127 LEU F N   1 
ATOM   6473  C  CA  . LEU F  1 126 ? 19.812 -9.092   -43.744  1.00 37.83  ? 127 LEU F CA  1 
ATOM   6474  C  C   . LEU F  1 126 ? 20.606 -10.371  -43.565  1.00 39.23  ? 127 LEU F C   1 
ATOM   6475  O  O   . LEU F  1 126 ? 21.798 -10.318  -43.259  1.00 40.62  ? 127 LEU F O   1 
ATOM   6476  C  CB  . LEU F  1 126 ? 20.401 -7.987   -42.869  1.00 38.37  ? 127 LEU F CB  1 
ATOM   6477  C  CG  . LEU F  1 126 ? 19.650 -6.652   -42.871  1.00 37.98  ? 127 LEU F CG  1 
ATOM   6478  C  CD1 . LEU F  1 126 ? 20.439 -5.541   -42.154  1.00 39.45  ? 127 LEU F CD1 1 
ATOM   6479  C  CD2 . LEU F  1 126 ? 19.318 -6.220   -44.276  1.00 37.05  ? 127 LEU F CD2 1 
ATOM   6480  N  N   . GLY F  1 127 ? 19.958 -11.512  -43.788  1.00 39.54  ? 128 GLY F N   1 
ATOM   6481  C  CA  . GLY F  1 127 ? 20.633 -12.811  -43.778  1.00 41.30  ? 128 GLY F CA  1 
ATOM   6482  C  C   . GLY F  1 127 ? 20.862 -13.421  -42.422  1.00 42.78  ? 128 GLY F C   1 
ATOM   6483  O  O   . GLY F  1 127 ? 21.375 -14.516  -42.318  1.00 44.63  ? 128 GLY F O   1 
ATOM   6484  N  N   . LYS F  1 128 ? 20.470 -12.711  -41.380  1.00 42.42  ? 129 LYS F N   1 
ATOM   6485  C  CA  . LYS F  1 128 ? 20.705 -13.158  -40.008  1.00 44.32  ? 129 LYS F CA  1 
ATOM   6486  C  C   . LYS F  1 128 ? 19.503 -13.900  -39.432  1.00 44.79  ? 129 LYS F C   1 
ATOM   6487  O  O   . LYS F  1 128 ? 19.322 -13.954  -38.215  1.00 45.77  ? 129 LYS F O   1 
ATOM   6488  C  CB  . LYS F  1 128 ? 21.027 -11.967  -39.100  1.00 44.52  ? 129 LYS F CB  1 
ATOM   6489  C  CG  . LYS F  1 128 ? 22.145 -11.037  -39.584  1.00 44.68  ? 129 LYS F CG  1 
ATOM   6490  C  CD  . LYS F  1 128 ? 22.712 -10.155  -38.451  1.00 46.43  ? 129 LYS F CD  1 
ATOM   6491  C  CE  . LYS F  1 128 ? 23.700 -9.125   -38.990  1.00 46.98  ? 129 LYS F CE  1 
ATOM   6492  N  NZ  . LYS F  1 128 ? 24.509 -8.531   -37.885  1.00 49.60  ? 129 LYS F NZ  1 
ATOM   6493  N  N   . GLY F  1 129 ? 18.703 -14.485  -40.314  1.00 44.49  ? 130 GLY F N   1 
ATOM   6494  C  CA  . GLY F  1 129 ? 17.422 -15.100  -39.948  1.00 45.15  ? 130 GLY F CA  1 
ATOM   6495  C  C   . GLY F  1 129 ? 17.547 -16.488  -39.366  1.00 47.80  ? 130 GLY F C   1 
ATOM   6496  O  O   . GLY F  1 129 ? 16.706 -16.906  -38.579  1.00 48.95  ? 130 GLY F O   1 
ATOM   6497  N  N   . GLY F  1 130 ? 18.595 -17.203  -39.762  1.00 49.13  ? 131 GLY F N   1 
ATOM   6498  C  CA  . GLY F  1 130 ? 18.866 -18.529  -39.245  1.00 52.46  ? 131 GLY F CA  1 
ATOM   6499  C  C   . GLY F  1 130 ? 18.272 -19.634  -40.086  1.00 54.14  ? 131 GLY F C   1 
ATOM   6500  O  O   . GLY F  1 130 ? 18.819 -20.736  -40.125  1.00 57.29  ? 131 GLY F O   1 
ATOM   6501  N  N   . ASN F  1 131 ? 17.153 -19.359  -40.751  1.00 52.76  ? 132 ASN F N   1 
ATOM   6502  C  CA  . ASN F  1 131 ? 16.515 -20.343  -41.622  1.00 54.69  ? 132 ASN F CA  1 
ATOM   6503  C  C   . ASN F  1 131 ? 17.109 -20.383  -43.029  1.00 54.40  ? 132 ASN F C   1 
ATOM   6504  O  O   . ASN F  1 131 ? 17.935 -19.560  -43.391  1.00 52.36  ? 132 ASN F O   1 
ATOM   6505  C  CB  . ASN F  1 131 ? 15.012 -20.107  -41.703  1.00 54.32  ? 132 ASN F CB  1 
ATOM   6506  C  CG  . ASN F  1 131 ? 14.641 -18.978  -42.613  1.00 51.51  ? 132 ASN F CG  1 
ATOM   6507  O  OD1 . ASN F  1 131 ? 15.496 -18.313  -43.195  1.00 49.61  ? 132 ASN F OD1 1 
ATOM   6508  N  ND2 . ASN F  1 131 ? 13.345 -18.754  -42.747  1.00 51.81  ? 132 ASN F ND2 1 
ATOM   6509  N  N   . GLU F  1 132 ? 16.674 -21.356  -43.816  1.00 56.96  ? 133 GLU F N   1 
ATOM   6510  C  CA  . GLU F  1 132 ? 17.202 -21.578  -45.162  1.00 57.69  ? 133 GLU F CA  1 
ATOM   6511  C  C   . GLU F  1 132 ? 16.982 -20.378  -46.036  1.00 54.36  ? 133 GLU F C   1 
ATOM   6512  O  O   . GLU F  1 132 ? 17.897 -19.881  -46.692  1.00 53.21  ? 133 GLU F O   1 
ATOM   6513  C  CB  . GLU F  1 132 ? 16.537 -22.816  -45.787  1.00 61.65  ? 133 GLU F CB  1 
ATOM   6514  C  CG  . GLU F  1 132 ? 16.712 -22.972  -47.319  1.00 63.22  ? 133 GLU F CG  1 
ATOM   6515  C  CD  . GLU F  1 132 ? 18.096 -23.547  -47.774  1.00 66.09  ? 133 GLU F CD  1 
ATOM   6516  O  OE1 . GLU F  1 132 ? 18.986 -23.853  -46.918  1.00 67.21  ? 133 GLU F OE1 1 
ATOM   6517  O  OE2 . GLU F  1 132 ? 18.301 -23.681  -49.017  1.00 67.20  ? 133 GLU F OE2 1 
ATOM   6518  N  N   . GLU F  1 133 ? 15.745 -19.924  -46.026  1.00 53.28  ? 134 GLU F N   1 
ATOM   6519  C  CA  . GLU F  1 133 ? 15.288 -18.879  -46.931  1.00 51.09  ? 134 GLU F CA  1 
ATOM   6520  C  C   . GLU F  1 133 ? 15.971 -17.521  -46.666  1.00 47.61  ? 134 GLU F C   1 
ATOM   6521  O  O   . GLU F  1 133 ? 16.146 -16.715  -47.575  1.00 46.11  ? 134 GLU F O   1 
ATOM   6522  C  CB  . GLU F  1 133 ? 13.758 -18.758  -46.849  1.00 51.53  ? 134 GLU F CB  1 
ATOM   6523  C  CG  . GLU F  1 133 ? 13.087 -18.008  -48.018  1.00 51.08  ? 134 GLU F CG  1 
ATOM   6524  C  CD  . GLU F  1 133 ? 13.111 -18.769  -49.351  1.00 54.02  ? 134 GLU F CD  1 
ATOM   6525  O  OE1 . GLU F  1 133 ? 13.419 -19.979  -49.353  1.00 57.10  ? 134 GLU F OE1 1 
ATOM   6526  O  OE2 . GLU F  1 133 ? 12.835 -18.147  -50.406  1.00 53.41  ? 134 GLU F OE2 1 
ATOM   6527  N  N   . SER F  1 134 ? 16.380 -17.276  -45.431  1.00 46.77  ? 135 SER F N   1 
ATOM   6528  C  CA  . SER F  1 134 ? 17.025 -16.012  -45.092  1.00 44.25  ? 135 SER F CA  1 
ATOM   6529  C  C   . SER F  1 134 ? 18.305 -15.815  -45.857  1.00 44.08  ? 135 SER F C   1 
ATOM   6530  O  O   . SER F  1 134 ? 18.689 -14.693  -46.134  1.00 42.27  ? 135 SER F O   1 
ATOM   6531  C  CB  . SER F  1 134 ? 17.326 -15.935  -43.608  1.00 44.38  ? 135 SER F CB  1 
ATOM   6532  O  OG  . SER F  1 134 ? 18.159 -14.823  -43.345  1.00 42.66  ? 135 SER F OG  1 
ATOM   6533  N  N   . THR F  1 135 ? 18.959 -16.924  -46.179  1.00 46.49  ? 136 THR F N   1 
ATOM   6534  C  CA  . THR F  1 135 ? 20.188 -16.938  -46.967  1.00 47.19  ? 136 THR F CA  1 
ATOM   6535  C  C   . THR F  1 135 ? 19.983 -16.614  -48.449  1.00 46.93  ? 136 THR F C   1 
ATOM   6536  O  O   . THR F  1 135 ? 20.936 -16.392  -49.173  1.00 47.46  ? 136 THR F O   1 
ATOM   6537  C  CB  . THR F  1 135 ? 20.836 -18.298  -46.815  1.00 50.43  ? 136 THR F CB  1 
ATOM   6538  O  OG1 . THR F  1 135 ? 21.512 -18.314  -45.559  1.00 50.98  ? 136 THR F OG1 1 
ATOM   6539  C  CG2 . THR F  1 135 ? 21.798 -18.597  -47.947  1.00 52.23  ? 136 THR F CG2 1 
ATOM   6540  N  N   . LYS F  1 136 ? 18.734 -16.576  -48.889  1.00 46.65  ? 137 LYS F N   1 
ATOM   6541  C  CA  . LYS F  1 136 ? 18.392 -16.381  -50.300  1.00 46.96  ? 137 LYS F CA  1 
ATOM   6542  C  C   . LYS F  1 136 ? 17.637 -15.080  -50.554  1.00 44.45  ? 137 LYS F C   1 
ATOM   6543  O  O   . LYS F  1 136 ? 18.100 -14.196  -51.255  1.00 43.45  ? 137 LYS F O   1 
ATOM   6544  C  CB  . LYS F  1 136 ? 17.502 -17.537  -50.778  1.00 49.85  ? 137 LYS F CB  1 
ATOM   6545  C  CG  . LYS F  1 136 ? 18.195 -18.882  -50.995  1.00 53.58  ? 137 LYS F CG  1 
ATOM   6546  C  CD  . LYS F  1 136 ? 17.168 -19.941  -51.488  1.00 57.13  ? 137 LYS F CD  1 
ATOM   6547  C  CE  . LYS F  1 136 ? 17.829 -21.123  -52.250  1.00 61.22  ? 137 LYS F CE  1 
ATOM   6548  N  NZ  . LYS F  1 136 ? 18.235 -22.255  -51.349  1.00 63.80  ? 137 LYS F NZ  1 
ATOM   6549  N  N   . THR F  1 137 ? 16.451 -14.986  -49.979  1.00 43.97  ? 138 THR F N   1 
ATOM   6550  C  CA  . THR F  1 137 ? 15.532 -13.879  -50.248  1.00 42.69  ? 138 THR F CA  1 
ATOM   6551  C  C   . THR F  1 137 ? 15.528 -12.810  -49.161  1.00 40.45  ? 138 THR F C   1 
ATOM   6552  O  O   . THR F  1 137 ? 15.019 -11.722  -49.369  1.00 39.35  ? 138 THR F O   1 
ATOM   6553  C  CB  . THR F  1 137 ? 14.066 -14.394  -50.425  1.00 44.42  ? 138 THR F CB  1 
ATOM   6554  O  OG1 . THR F  1 137 ? 13.511 -14.802  -49.176  1.00 44.70  ? 138 THR F OG1 1 
ATOM   6555  C  CG2 . THR F  1 137 ? 14.002 -15.575  -51.367  1.00 47.41  ? 138 THR F CG2 1 
ATOM   6556  N  N   . GLY F  1 138 ? 16.088 -13.155  -48.006  1.00 40.33  ? 139 GLY F N   1 
ATOM   6557  C  CA  . GLY F  1 138 ? 16.095 -12.297  -46.827  1.00 39.06  ? 139 GLY F CA  1 
ATOM   6558  C  C   . GLY F  1 138 ? 14.815 -12.372  -46.007  1.00 39.38  ? 139 GLY F C   1 
ATOM   6559  O  O   . GLY F  1 138 ? 14.629 -11.624  -45.063  1.00 38.68  ? 139 GLY F O   1 
ATOM   6560  N  N   . ASN F  1 139 ? 13.944 -13.302  -46.360  1.00 41.02  ? 140 ASN F N   1 
ATOM   6561  C  CA  . ASN F  1 139 ? 12.622 -13.434  -45.754  1.00 42.11  ? 140 ASN F CA  1 
ATOM   6562  C  C   . ASN F  1 139 ? 11.787 -12.168  -45.845  1.00 41.45  ? 140 ASN F C   1 
ATOM   6563  O  O   . ASN F  1 139 ? 10.899 -11.958  -45.031  1.00 42.17  ? 140 ASN F O   1 
ATOM   6564  C  CB  . ASN F  1 139 ? 12.730 -13.895  -44.302  1.00 42.64  ? 140 ASN F CB  1 
ATOM   6565  C  CG  . ASN F  1 139 ? 12.988 -15.365  -44.187  1.00 44.62  ? 140 ASN F CG  1 
ATOM   6566  O  OD1 . ASN F  1 139 ? 13.625 -15.824  -43.244  1.00 45.23  ? 140 ASN F OD1 1 
ATOM   6567  N  ND2 . ASN F  1 139 ? 12.493 -16.123  -45.147  1.00 46.05  ? 140 ASN F ND2 1 
ATOM   6568  N  N   . ALA F  1 140 ? 12.049 -11.351  -46.864  1.00 40.56  ? 141 ALA F N   1 
ATOM   6569  C  CA  . ALA F  1 140 ? 11.399 -10.043  -47.012  1.00 40.14  ? 141 ALA F CA  1 
ATOM   6570  C  C   . ALA F  1 140 ? 10.066 -10.119  -47.727  1.00 41.98  ? 141 ALA F C   1 
ATOM   6571  O  O   . ALA F  1 140 ? 9.403  -9.102   -47.910  1.00 42.29  ? 141 ALA F O   1 
ATOM   6572  C  CB  . ALA F  1 140 ? 12.292 -9.101   -47.742  1.00 38.95  ? 141 ALA F CB  1 
ATOM   6573  N  N   . GLY F  1 141 ? 9.684  -11.316  -48.150  1.00 43.73  ? 142 GLY F N   1 
ATOM   6574  C  CA  . GLY F  1 141 ? 8.317  -11.572  -48.615  1.00 46.35  ? 142 GLY F CA  1 
ATOM   6575  C  C   . GLY F  1 141 ? 8.027  -11.152  -50.038  1.00 47.27  ? 142 GLY F C   1 
ATOM   6576  O  O   . GLY F  1 141 ? 8.934  -11.013  -50.846  1.00 46.14  ? 142 GLY F O   1 
ATOM   6577  N  N   . SER F  1 142 ? 6.745  -10.951  -50.324  1.00 49.74  ? 143 SER F N   1 
ATOM   6578  C  CA  . SER F  1 142 ? 6.267  -10.739  -51.696  1.00 51.79  ? 143 SER F CA  1 
ATOM   6579  C  C   . SER F  1 142 ? 6.741  -9.416   -52.284  1.00 50.27  ? 143 SER F C   1 
ATOM   6580  O  O   . SER F  1 142 ? 7.290  -8.572   -51.574  1.00 48.06  ? 143 SER F O   1 
ATOM   6581  C  CB  . SER F  1 142 ? 4.742  -10.797  -51.759  1.00 55.35  ? 143 SER F CB  1 
ATOM   6582  O  OG  . SER F  1 142 ? 4.174  -9.607   -51.243  1.00 55.45  ? 143 SER F OG  1 
ATOM   6583  N  N   . ARG F  1 143 ? 6.513  -9.260   -53.586  1.00 51.92  ? 144 ARG F N   1 
ATOM   6584  C  CA  . ARG F  1 143 ? 6.975  -8.094   -54.331  1.00 51.25  ? 144 ARG F CA  1 
ATOM   6585  C  C   . ARG F  1 143 ? 5.832  -7.100   -54.515  1.00 53.62  ? 144 ARG F C   1 
ATOM   6586  O  O   . ARG F  1 143 ? 4.909  -7.317   -55.295  1.00 57.17  ? 144 ARG F O   1 
ATOM   6587  C  CB  . ARG F  1 143 ? 7.564  -8.525   -55.678  1.00 52.15  ? 144 ARG F CB  1 
ATOM   6588  C  CG  . ARG F  1 143 ? 8.749  -9.432   -55.521  1.00 50.52  ? 144 ARG F CG  1 
ATOM   6589  C  CD  . ARG F  1 143 ? 9.245  -10.024  -56.819  1.00 52.23  ? 144 ARG F CD  1 
ATOM   6590  N  NE  . ARG F  1 143 ? 10.276 -11.044  -56.576  1.00 51.11  ? 144 ARG F NE  1 
ATOM   6591  C  CZ  . ARG F  1 143 ? 10.952 -11.670  -57.532  1.00 52.60  ? 144 ARG F CZ  1 
ATOM   6592  N  NH1 . ARG F  1 143 ? 10.726 -11.411  -58.818  1.00 55.23  ? 144 ARG F NH1 1 
ATOM   6593  N  NH2 . ARG F  1 143 ? 11.862 -12.564  -57.206  1.00 52.50  ? 144 ARG F NH2 1 
ATOM   6594  N  N   . LEU F  1 144 ? 5.893  -5.997   -53.794  1.00 52.32  ? 145 LEU F N   1 
ATOM   6595  C  CA  . LEU F  1 144 ? 4.800  -5.037   -53.800  1.00 55.05  ? 145 LEU F CA  1 
ATOM   6596  C  C   . LEU F  1 144 ? 4.780  -4.185   -55.051  1.00 56.89  ? 145 LEU F C   1 
ATOM   6597  O  O   . LEU F  1 144 ? 3.750  -4.072   -55.721  1.00 60.58  ? 145 LEU F O   1 
ATOM   6598  C  CB  . LEU F  1 144 ? 4.891  -4.117   -52.587  1.00 53.84  ? 145 LEU F CB  1 
ATOM   6599  C  CG  . LEU F  1 144 ? 4.604  -4.769   -51.233  1.00 53.31  ? 145 LEU F CG  1 
ATOM   6600  C  CD1 . LEU F  1 144 ? 4.557  -3.697   -50.120  1.00 52.89  ? 145 LEU F CD1 1 
ATOM   6601  C  CD2 . LEU F  1 144 ? 3.304  -5.604   -51.264  1.00 56.36  ? 145 LEU F CD2 1 
ATOM   6602  N  N   . ALA F  1 145 ? 5.920  -3.571   -55.341  1.00 54.72  ? 146 ALA F N   1 
ATOM   6603  C  CA  . ALA F  1 145 ? 6.052  -2.669   -56.479  1.00 56.44  ? 146 ALA F CA  1 
ATOM   6604  C  C   . ALA F  1 145 ? 7.467  -2.741   -57.066  1.00 54.31  ? 146 ALA F C   1 
ATOM   6605  O  O   . ALA F  1 145 ? 8.445  -2.891   -56.338  1.00 51.49  ? 146 ALA F O   1 
ATOM   6606  C  CB  . ALA F  1 145 ? 5.718  -1.262   -56.062  1.00 57.46  ? 146 ALA F CB  1 
ATOM   6607  N  N   . CYS F  1 146 ? 7.567  -2.644   -58.387  1.00 56.17  ? 147 CYS F N   1 
ATOM   6608  C  CA  . CYS F  1 146 ? 8.840  -2.764   -59.066  1.00 54.78  ? 147 CYS F CA  1 
ATOM   6609  C  C   . CYS F  1 146 ? 8.898  -1.970   -60.355  1.00 57.61  ? 147 CYS F C   1 
ATOM   6610  O  O   . CYS F  1 146 ? 7.902  -1.438   -60.826  1.00 60.87  ? 147 CYS F O   1 
ATOM   6611  C  CB  . CYS F  1 146 ? 9.162  -4.228   -59.355  1.00 54.26  ? 147 CYS F CB  1 
ATOM   6612  S  SG  . CYS F  1 146 ? 8.093  -5.028   -60.493  1.00 57.88  ? 147 CYS F SG  1 
ATOM   6613  N  N   . GLY F  1 147 ? 10.096 -1.881   -60.911  1.00 56.86  ? 148 GLY F N   1 
ATOM   6614  C  CA  . GLY F  1 147 ? 10.301 -1.183   -62.164  1.00 59.65  ? 148 GLY F CA  1 
ATOM   6615  C  C   . GLY F  1 147 ? 11.668 -1.469   -62.731  1.00 58.65  ? 148 GLY F C   1 
ATOM   6616  O  O   . GLY F  1 147 ? 12.587 -1.780   -61.977  1.00 55.74  ? 148 GLY F O   1 
ATOM   6617  N  N   . VAL F  1 148 ? 11.796 -1.350   -64.054  1.00 61.54  ? 149 VAL F N   1 
ATOM   6618  C  CA  . VAL F  1 148 ? 13.084 -1.531   -64.737  1.00 61.34  ? 149 VAL F CA  1 
ATOM   6619  C  C   . VAL F  1 148 ? 13.957 -0.269   -64.621  1.00 60.97  ? 149 VAL F C   1 
ATOM   6620  O  O   . VAL F  1 148 ? 13.480 0.855    -64.801  1.00 62.76  ? 149 VAL F O   1 
ATOM   6621  C  CB  . VAL F  1 148 ? 12.897 -1.894   -66.212  1.00 65.01  ? 149 VAL F CB  1 
ATOM   6622  C  CG1 . VAL F  1 148 ? 14.223 -2.071   -66.866  1.00 65.28  ? 149 VAL F CG1 1 
ATOM   6623  C  CG2 . VAL F  1 148 ? 12.116 -3.158   -66.343  1.00 65.95  ? 149 VAL F CG2 1 
ATOM   6624  N  N   . ILE F  1 149 ? 15.235 -0.478   -64.310  1.00 59.01  ? 150 ILE F N   1 
ATOM   6625  C  CA  . ILE F  1 149 ? 16.166 0.623    -64.100  1.00 58.97  ? 150 ILE F CA  1 
ATOM   6626  C  C   . ILE F  1 149 ? 16.637 1.130    -65.449  1.00 62.42  ? 150 ILE F C   1 
ATOM   6627  O  O   . ILE F  1 149 ? 17.121 0.356    -66.279  1.00 63.37  ? 150 ILE F O   1 
ATOM   6628  C  CB  . ILE F  1 149 ? 17.397 0.209    -63.284  1.00 56.33  ? 150 ILE F CB  1 
ATOM   6629  C  CG1 . ILE F  1 149 ? 17.011 -0.112   -61.846  1.00 53.30  ? 150 ILE F CG1 1 
ATOM   6630  C  CG2 . ILE F  1 149 ? 18.433 1.336    -63.273  1.00 57.18  ? 150 ILE F CG2 1 
ATOM   6631  C  CD1 . ILE F  1 149 ? 18.132 -0.761   -61.061  1.00 50.98  ? 150 ILE F CD1 1 
ATOM   6632  N  N   . GLY F  1 150 ? 16.499 2.440    -65.649  1.00 64.62  ? 151 GLY F N   1 
ATOM   6633  C  CA  . GLY F  1 150 ? 16.750 3.055    -66.947  1.00 68.53  ? 151 GLY F CA  1 
ATOM   6634  C  C   . GLY F  1 150 ? 17.727 4.204    -66.916  1.00 69.73  ? 151 GLY F C   1 
ATOM   6635  O  O   . GLY F  1 150 ? 17.886 4.872    -65.889  1.00 68.30  ? 151 GLY F O   1 
ATOM   6636  N  N   . ILE F  1 151 ? 18.373 4.424    -68.064  1.00 72.89  ? 152 ILE F N   1 
ATOM   6637  C  CA  . ILE F  1 151 ? 19.364 5.478    -68.211  1.00 74.91  ? 152 ILE F CA  1 
ATOM   6638  C  C   . ILE F  1 151 ? 18.619 6.800    -68.182  1.00 77.60  ? 152 ILE F C   1 
ATOM   6639  O  O   . ILE F  1 151 ? 17.585 6.943    -68.847  1.00 80.02  ? 152 ILE F O   1 
ATOM   6640  C  CB  . ILE F  1 151 ? 20.173 5.368    -69.512  1.00 78.19  ? 152 ILE F CB  1 
ATOM   6641  C  CG1 . ILE F  1 151 ? 20.944 4.056    -69.570  1.00 76.21  ? 152 ILE F CG1 1 
ATOM   6642  C  CG2 . ILE F  1 151 ? 21.162 6.539    -69.598  1.00 80.76  ? 152 ILE F CG2 1 
ATOM   6643  C  CD1 . ILE F  1 151 ? 21.711 3.860    -70.832  1.00 79.83  ? 152 ILE F CD1 1 
ATOM   6644  N  N   . ALA F  1 152 ? 19.142 7.746    -67.400  1.00 77.68  ? 153 ALA F N   1 
ATOM   6645  C  CA  . ALA F  1 152 ? 18.499 9.040    -67.191  1.00 80.39  ? 153 ALA F CA  1 
ATOM   6646  C  C   . ALA F  1 152 ? 19.358 10.181   -67.704  1.00 84.66  ? 153 ALA F C   1 
ATOM   6647  O  O   . ALA F  1 152 ? 20.580 10.034   -67.880  1.00 84.55  ? 153 ALA F O   1 
ATOM   6648  C  CB  . ALA F  1 152 ? 18.202 9.232    -65.734  1.00 77.67  ? 153 ALA F CB  1 
ATOM   6649  N  N   . GLN F  1 153 ? 18.705 11.322   -67.934  1.00 88.79  ? 154 GLN F N   1 
ATOM   6650  C  CA  . GLN F  1 153 ? 19.406 12.521   -68.422  1.00 93.98  ? 154 GLN F CA  1 
ATOM   6651  C  C   . GLN F  1 153 ? 20.201 13.188   -67.308  1.00 93.58  ? 154 GLN F C   1 
ATOM   6652  O  O   . GLN F  1 153 ? 19.648 13.398   -66.229  1.00 91.88  ? 154 GLN F O   1 
ATOM   6653  C  CB  . GLN F  1 153 ? 18.452 13.565   -69.027  1.00 99.21  ? 154 GLN F CB  1 
ATOM   6654  C  CG  . GLN F  1 153 ? 19.208 14.796   -69.620  1.00 105.10 ? 154 GLN F CG  1 
ATOM   6655  C  CD  . GLN F  1 153 ? 18.314 15.780   -70.368  1.00 111.13 ? 154 GLN F CD  1 
ATOM   6656  O  OE1 . GLN F  1 153 ? 17.705 15.420   -71.388  1.00 112.91 ? 154 GLN F OE1 1 
ATOM   6657  N  NE2 . GLN F  1 153 ? 18.254 17.039   -69.881  1.00 114.55 ? 154 GLN F NE2 1 
ATOM   6658  O  OXT . GLN F  1 153 ? 21.373 13.544   -67.486  1.00 95.54  ? 154 GLN F OXT 1 
ATOM   6659  N  N   . ALA G  1 1   ? 24.881 -61.930  -72.198  1.00 101.24 ? 2   ALA G N   1 
ATOM   6660  C  CA  . ALA G  1 1   ? 23.725 -61.037  -71.828  1.00 98.74  ? 2   ALA G CA  1 
ATOM   6661  C  C   . ALA G  1 1   ? 23.443 -61.019  -70.297  1.00 93.35  ? 2   ALA G C   1 
ATOM   6662  O  O   . ALA G  1 1   ? 22.703 -61.926  -69.835  1.00 93.01  ? 2   ALA G O   1 
ATOM   6663  C  CB  . ALA G  1 1   ? 22.446 -61.499  -72.605  1.00 101.24 ? 2   ALA G CB  1 
ATOM   6664  N  N   . THR G  1 2   ? 23.997 -60.057  -69.503  1.00 89.22  ? 3   THR G N   1 
ATOM   6665  C  CA  . THR G  1 2   ? 23.536 -59.963  -68.096  1.00 84.43  ? 3   THR G CA  1 
ATOM   6666  C  C   . THR G  1 2   ? 22.176 -59.246  -68.048  1.00 83.34  ? 3   THR G C   1 
ATOM   6667  O  O   . THR G  1 2   ? 21.957 -58.231  -68.714  1.00 84.64  ? 3   THR G O   1 
ATOM   6668  C  CB  . THR G  1 2   ? 24.504 -59.272  -67.078  1.00 81.59  ? 3   THR G CB  1 
ATOM   6669  O  OG1 . THR G  1 2   ? 25.841 -59.305  -67.555  1.00 83.81  ? 3   THR G OG1 1 
ATOM   6670  C  CG2 . THR G  1 2   ? 24.426 -59.976  -65.696  1.00 78.09  ? 3   THR G CG2 1 
ATOM   6671  N  N   . LYS G  1 3   ? 21.264 -59.814  -67.276  1.00 81.37  ? 4   LYS G N   1 
ATOM   6672  C  CA  . LYS G  1 3   ? 19.951 -59.236  -67.086  1.00 80.74  ? 4   LYS G CA  1 
ATOM   6673  C  C   . LYS G  1 3   ? 19.652 -59.237  -65.616  1.00 77.01  ? 4   LYS G C   1 
ATOM   6674  O  O   . LYS G  1 3   ? 20.132 -60.105  -64.898  1.00 75.87  ? 4   LYS G O   1 
ATOM   6675  C  CB  . LYS G  1 3   ? 18.871 -60.051  -67.815  1.00 83.88  ? 4   LYS G CB  1 
ATOM   6676  C  CG  . LYS G  1 3   ? 18.956 -59.998  -69.358  1.00 88.67  ? 4   LYS G CG  1 
ATOM   6677  C  CD  . LYS G  1 3   ? 17.688 -60.597  -70.030  1.00 92.16  ? 4   LYS G CD  1 
ATOM   6678  C  CE  . LYS G  1 3   ? 17.964 -61.102  -71.465  1.00 96.91  ? 4   LYS G CE  1 
ATOM   6679  N  NZ  . LYS G  1 3   ? 17.000 -62.146  -71.925  1.00 99.93  ? 4   LYS G NZ  1 
ATOM   6680  N  N   . ALA G  1 4   ? 18.857 -58.265  -65.178  1.00 75.69  ? 5   ALA G N   1 
ATOM   6681  C  CA  . ALA G  1 4   ? 18.332 -58.230  -63.814  1.00 72.65  ? 5   ALA G CA  1 
ATOM   6682  C  C   . ALA G  1 4   ? 16.868 -57.796  -63.836  1.00 73.50  ? 5   ALA G C   1 
ATOM   6683  O  O   . ALA G  1 4   ? 16.357 -57.346  -64.862  1.00 76.13  ? 5   ALA G O   1 
ATOM   6684  C  CB  . ALA G  1 4   ? 19.165 -57.298  -62.954  1.00 69.90  ? 5   ALA G CB  1 
ATOM   6685  N  N   . VAL G  1 5   ? 16.195 -57.961  -62.706  1.00 71.74  ? 6   VAL G N   1 
ATOM   6686  C  CA  . VAL G  1 5   ? 14.794 -57.546  -62.564  1.00 72.86  ? 6   VAL G CA  1 
ATOM   6687  C  C   . VAL G  1 5   ? 14.489 -57.172  -61.136  1.00 70.22  ? 6   VAL G C   1 
ATOM   6688  O  O   . VAL G  1 5   ? 15.185 -57.605  -60.225  1.00 67.94  ? 6   VAL G O   1 
ATOM   6689  C  CB  . VAL G  1 5   ? 13.813 -58.657  -62.956  1.00 75.74  ? 6   VAL G CB  1 
ATOM   6690  C  CG1 . VAL G  1 5   ? 13.722 -59.707  -61.855  1.00 74.57  ? 6   VAL G CG1 1 
ATOM   6691  C  CG2 . VAL G  1 5   ? 12.424 -58.083  -63.233  1.00 78.31  ? 6   VAL G CG2 1 
ATOM   6692  N  N   . CYS G  1 6   ? 13.451 -56.361  -60.953  1.00 71.10  ? 7   CYS G N   1 
ATOM   6693  C  CA  . CYS G  1 6   ? 13.050 -55.892  -59.623  1.00 69.38  ? 7   CYS G CA  1 
ATOM   6694  C  C   . CYS G  1 6   ? 11.561 -55.604  -59.523  1.00 71.72  ? 7   CYS G C   1 
ATOM   6695  O  O   . CYS G  1 6   ? 11.025 -54.805  -60.289  1.00 73.81  ? 7   CYS G O   1 
ATOM   6696  C  CB  . CYS G  1 6   ? 13.805 -54.616  -59.241  1.00 67.34  ? 7   CYS G CB  1 
ATOM   6697  S  SG  . CYS G  1 6   ? 13.188 -53.844  -57.715  1.00 65.95  ? 7   CYS G SG  1 
ATOM   6698  N  N   . VAL G  1 7   ? 10.919 -56.239  -58.549  1.00 71.67  ? 8   VAL G N   1 
ATOM   6699  C  CA  . VAL G  1 7   ? 9.512  -56.006  -58.273  1.00 74.17  ? 8   VAL G CA  1 
ATOM   6700  C  C   . VAL G  1 7   ? 9.366  -54.940  -57.202  1.00 72.78  ? 8   VAL G C   1 
ATOM   6701  O  O   . VAL G  1 7   ? 9.626  -55.189  -56.015  1.00 70.79  ? 8   VAL G O   1 
ATOM   6702  C  CB  . VAL G  1 7   ? 8.805  -57.288  -57.809  1.00 75.81  ? 8   VAL G CB  1 
ATOM   6703  C  CG1 . VAL G  1 7   ? 7.378  -56.997  -57.298  1.00 78.55  ? 8   VAL G CG1 1 
ATOM   6704  C  CG2 . VAL G  1 7   ? 8.791  -58.275  -58.939  1.00 78.20  ? 8   VAL G CG2 1 
ATOM   6705  N  N   . LEU G  1 8   ? 8.928  -53.758  -57.630  1.00 74.17  ? 9   LEU G N   1 
ATOM   6706  C  CA  . LEU G  1 8   ? 8.652  -52.633  -56.728  1.00 73.56  ? 9   LEU G CA  1 
ATOM   6707  C  C   . LEU G  1 8   ? 7.325  -52.816  -55.989  1.00 76.03  ? 9   LEU G C   1 
ATOM   6708  O  O   . LEU G  1 8   ? 6.290  -53.043  -56.615  1.00 79.75  ? 9   LEU G O   1 
ATOM   6709  C  CB  . LEU G  1 8   ? 8.622  -51.330  -57.512  1.00 74.70  ? 9   LEU G CB  1 
ATOM   6710  C  CG  . LEU G  1 8   ? 9.995  -50.896  -58.050  1.00 72.52  ? 9   LEU G CG  1 
ATOM   6711  C  CD1 . LEU G  1 8   ? 9.856  -49.890  -59.192  1.00 74.69  ? 9   LEU G CD1 1 
ATOM   6712  C  CD2 . LEU G  1 8   ? 10.880 -50.329  -56.932  1.00 69.36  ? 9   LEU G CD2 1 
ATOM   6713  N  N   . LYS G  1 9   ? 7.378  -52.736  -54.660  1.00 74.45  ? 10  LYS G N   1 
ATOM   6714  C  CA  . LYS G  1 9   ? 6.195  -52.848  -53.803  1.00 77.03  ? 10  LYS G CA  1 
ATOM   6715  C  C   . LYS G  1 9   ? 6.295  -51.956  -52.564  1.00 75.78  ? 10  LYS G C   1 
ATOM   6716  O  O   . LYS G  1 9   ? 7.376  -51.538  -52.153  1.00 72.76  ? 10  LYS G O   1 
ATOM   6717  C  CB  . LYS G  1 9   ? 5.978  -54.295  -53.355  1.00 77.54  ? 10  LYS G CB  1 
ATOM   6718  C  CG  . LYS G  1 9   ? 5.233  -55.177  -54.369  1.00 81.44  ? 10  LYS G CG  1 
ATOM   6719  C  CD  . LYS G  1 9   ? 4.467  -56.326  -53.648  1.00 84.13  ? 10  LYS G CD  1 
ATOM   6720  C  CE  . LYS G  1 9   ? 3.966  -57.425  -54.615  1.00 87.06  ? 10  LYS G CE  1 
ATOM   6721  N  NZ  . LYS G  1 9   ? 2.636  -57.089  -55.278  1.00 91.98  ? 10  LYS G NZ  1 
ATOM   6722  N  N   . GLY G  1 10  ? 5.153  -51.676  -51.958  1.00 78.75  ? 11  GLY G N   1 
ATOM   6723  C  CA  . GLY G  1 10  ? 5.143  -50.817  -50.785  1.00 78.38  ? 11  GLY G CA  1 
ATOM   6724  C  C   . GLY G  1 10  ? 3.885  -50.863  -49.940  1.00 82.09  ? 11  GLY G C   1 
ATOM   6725  O  O   . GLY G  1 10  ? 2.980  -51.667  -50.189  1.00 85.19  ? 11  GLY G O   1 
ATOM   6726  N  N   . ASP G  1 11  ? 3.854  -49.986  -48.934  1.00 82.12  ? 12  ASP G N   1 
ATOM   6727  C  CA  . ASP G  1 11  ? 2.734  -49.899  -47.987  1.00 85.87  ? 12  ASP G CA  1 
ATOM   6728  C  C   . ASP G  1 11  ? 1.407  -49.486  -48.640  1.00 90.83  ? 12  ASP G C   1 
ATOM   6729  O  O   . ASP G  1 11  ? 0.329  -49.963  -48.234  1.00 94.72  ? 12  ASP G O   1 
ATOM   6730  C  CB  . ASP G  1 11  ? 3.073  -48.934  -46.835  1.00 85.02  ? 12  ASP G CB  1 
ATOM   6731  C  CG  . ASP G  1 11  ? 3.707  -49.643  -45.644  1.00 83.28  ? 12  ASP G CG  1 
ATOM   6732  O  OD1 . ASP G  1 11  ? 3.128  -50.660  -45.199  1.00 85.68  ? 12  ASP G OD1 1 
ATOM   6733  O  OD2 . ASP G  1 11  ? 4.768  -49.191  -45.144  1.00 80.62  ? 12  ASP G OD2 1 
ATOM   6734  N  N   . GLY G  1 12  ? 1.508  -48.620  -49.651  1.00 90.91  ? 13  GLY G N   1 
ATOM   6735  C  CA  . GLY G  1 12  ? 0.342  -48.074  -50.343  1.00 95.71  ? 13  GLY G CA  1 
ATOM   6736  C  C   . GLY G  1 12  ? 0.174  -48.649  -51.738  1.00 96.84  ? 13  GLY G C   1 
ATOM   6737  O  O   . GLY G  1 12  ? 0.760  -49.684  -52.055  1.00 94.35  ? 13  GLY G O   1 
ATOM   6738  N  N   . PRO G  1 13  ? -0.590 -47.945  -52.598  1.00 100.82 ? 14  PRO G N   1 
ATOM   6739  C  CA  . PRO G  1 13  ? -1.060 -48.467  -53.884  1.00 103.68 ? 14  PRO G CA  1 
ATOM   6740  C  C   . PRO G  1 13  ? 0.036  -48.562  -54.926  1.00 100.21 ? 14  PRO G C   1 
ATOM   6741  O  O   . PRO G  1 13  ? -0.155 -49.243  -55.940  1.00 102.02 ? 14  PRO G O   1 
ATOM   6742  C  CB  . PRO G  1 13  ? -2.085 -47.419  -54.333  1.00 108.99 ? 14  PRO G CB  1 
ATOM   6743  C  CG  . PRO G  1 13  ? -1.545 -46.127  -53.781  1.00 106.73 ? 14  PRO G CG  1 
ATOM   6744  C  CD  . PRO G  1 13  ? -0.790 -46.482  -52.505  1.00 102.28 ? 14  PRO G CD  1 
ATOM   6745  N  N   . VAL G  1 14  ? 1.158  -47.877  -54.685  1.00 95.81  ? 15  VAL G N   1 
ATOM   6746  C  CA  . VAL G  1 14  ? 2.256  -47.840  -55.653  1.00 92.77  ? 15  VAL G CA  1 
ATOM   6747  C  C   . VAL G  1 14  ? 2.880  -49.226  -55.800  1.00 90.08  ? 15  VAL G C   1 
ATOM   6748  O  O   . VAL G  1 14  ? 3.269  -49.859  -54.809  1.00 87.44  ? 15  VAL G O   1 
ATOM   6749  C  CB  . VAL G  1 14  ? 3.344  -46.809  -55.274  1.00 89.14  ? 15  VAL G CB  1 
ATOM   6750  C  CG1 . VAL G  1 14  ? 4.404  -46.713  -56.403  1.00 86.92  ? 15  VAL G CG1 1 
ATOM   6751  C  CG2 . VAL G  1 14  ? 2.706  -45.439  -54.987  1.00 91.89  ? 15  VAL G CG2 1 
ATOM   6752  N  N   . GLN G  1 15  ? 2.925  -49.692  -57.042  1.00 91.23  ? 16  GLN G N   1 
ATOM   6753  C  CA  . GLN G  1 15  ? 3.567  -50.952  -57.363  1.00 89.37  ? 16  GLN G CA  1 
ATOM   6754  C  C   . GLN G  1 15  ? 3.998  -50.991  -58.833  1.00 90.07  ? 16  GLN G C   1 
ATOM   6755  O  O   . GLN G  1 15  ? 3.532  -50.199  -59.663  1.00 92.95  ? 16  GLN G O   1 
ATOM   6756  C  CB  . GLN G  1 15  ? 2.662  -52.147  -57.009  1.00 92.07  ? 16  GLN G CB  1 
ATOM   6757  C  CG  . GLN G  1 15  ? 1.265  -52.086  -57.602  1.00 98.30  ? 16  GLN G CG  1 
ATOM   6758  C  CD  . GLN G  1 15  ? 0.505  -53.384  -57.420  1.00 101.82 ? 16  GLN G CD  1 
ATOM   6759  O  OE1 . GLN G  1 15  ? -0.378 -53.706  -58.227  1.00 107.01 ? 16  GLN G OE1 1 
ATOM   6760  N  NE2 . GLN G  1 15  ? 0.850  -54.153  -56.366  1.00 99.13  ? 16  GLN G NE2 1 
ATOM   6761  N  N   . GLY G  1 16  ? 4.909  -51.916  -59.130  1.00 87.57  ? 17  GLY G N   1 
ATOM   6762  C  CA  . GLY G  1 16  ? 5.429  -52.063  -60.480  1.00 88.23  ? 17  GLY G CA  1 
ATOM   6763  C  C   . GLY G  1 16  ? 6.513  -53.110  -60.633  1.00 85.31  ? 17  GLY G C   1 
ATOM   6764  O  O   . GLY G  1 16  ? 6.908  -53.758  -59.659  1.00 82.56  ? 17  GLY G O   1 
ATOM   6765  N  N   . ILE G  1 17  ? 6.971  -53.259  -61.877  1.00 86.32  ? 18  ILE G N   1 
ATOM   6766  C  CA  . ILE G  1 17  ? 8.070  -54.147  -62.258  1.00 84.23  ? 18  ILE G CA  1 
ATOM   6767  C  C   . ILE G  1 17  ? 9.071  -53.370  -63.089  1.00 83.34  ? 18  ILE G C   1 
ATOM   6768  O  O   . ILE G  1 17  ? 8.682  -52.712  -64.046  1.00 86.49  ? 18  ILE G O   1 
ATOM   6769  C  CB  . ILE G  1 17  ? 7.558  -55.311  -63.131  1.00 87.92  ? 18  ILE G CB  1 
ATOM   6770  C  CG1 . ILE G  1 17  ? 6.947  -56.417  -62.264  1.00 88.31  ? 18  ILE G CG1 1 
ATOM   6771  C  CG2 . ILE G  1 17  ? 8.688  -55.871  -64.046  1.00 87.23  ? 18  ILE G CG2 1 
ATOM   6772  C  CD1 . ILE G  1 17  ? 6.645  -57.703  -63.031  1.00 91.55  ? 18  ILE G CD1 1 
ATOM   6773  N  N   . ILE G  1 18  ? 10.352 -53.459  -62.744  1.00 79.73  ? 19  ILE G N   1 
ATOM   6774  C  CA  . ILE G  1 18  ? 11.415 -52.789  -63.522  1.00 79.34  ? 19  ILE G CA  1 
ATOM   6775  C  C   . ILE G  1 18  ? 12.509 -53.745  -63.967  1.00 78.40  ? 19  ILE G C   1 
ATOM   6776  O  O   . ILE G  1 18  ? 13.081 -54.455  -63.142  1.00 75.89  ? 19  ILE G O   1 
ATOM   6777  C  CB  . ILE G  1 18  ? 12.113 -51.667  -62.722  1.00 76.41  ? 19  ILE G CB  1 
ATOM   6778  C  CG1 . ILE G  1 18  ? 11.146 -50.523  -62.452  1.00 78.01  ? 19  ILE G CG1 1 
ATOM   6779  C  CG2 . ILE G  1 18  ? 13.317 -51.115  -63.511  1.00 76.16  ? 19  ILE G CG2 1 
ATOM   6780  C  CD1 . ILE G  1 18  ? 10.770 -49.747  -63.724  1.00 82.05  ? 19  ILE G CD1 1 
ATOM   6781  N  N   . ASN G  1 19  ? 12.823 -53.724  -65.260  1.00 80.88  ? 20  ASN G N   1 
ATOM   6782  C  CA  . ASN G  1 19  ? 13.852 -54.595  -65.827  1.00 80.91  ? 20  ASN G CA  1 
ATOM   6783  C  C   . ASN G  1 19  ? 15.173 -53.888  -66.052  1.00 79.68  ? 20  ASN G C   1 
ATOM   6784  O  O   . ASN G  1 19  ? 15.208 -52.679  -66.301  1.00 80.30  ? 20  ASN G O   1 
ATOM   6785  C  CB  . ASN G  1 19  ? 13.400 -55.163  -67.166  1.00 85.26  ? 20  ASN G CB  1 
ATOM   6786  C  CG  . ASN G  1 19  ? 12.160 -55.998  -67.049  1.00 87.50  ? 20  ASN G CG  1 
ATOM   6787  O  OD1 . ASN G  1 19  ? 11.057 -55.524  -67.360  1.00 90.63  ? 20  ASN G OD1 1 
ATOM   6788  N  ND2 . ASN G  1 19  ? 12.313 -57.241  -66.576  1.00 86.34  ? 20  ASN G ND2 1 
ATOM   6789  N  N   . PHE G  1 20  ? 16.246 -54.680  -65.984  1.00 78.50  ? 21  PHE G N   1 
ATOM   6790  C  CA  . PHE G  1 20  ? 17.614 -54.237  -66.296  1.00 77.96  ? 21  PHE G CA  1 
ATOM   6791  C  C   . PHE G  1 20  ? 18.225 -55.140  -67.357  1.00 80.45  ? 21  PHE G C   1 
ATOM   6792  O  O   . PHE G  1 20  ? 17.940 -56.329  -67.414  1.00 81.09  ? 21  PHE G O   1 
ATOM   6793  C  CB  . PHE G  1 20  ? 18.510 -54.260  -65.054  1.00 74.26  ? 21  PHE G CB  1 
ATOM   6794  C  CG  . PHE G  1 20  ? 18.028 -53.367  -63.933  1.00 72.05  ? 21  PHE G CG  1 
ATOM   6795  C  CD1 . PHE G  1 20  ? 16.998 -53.775  -63.090  1.00 70.87  ? 21  PHE G CD1 1 
ATOM   6796  C  CD2 . PHE G  1 20  ? 18.615 -52.113  -63.719  1.00 71.32  ? 21  PHE G CD2 1 
ATOM   6797  C  CE1 . PHE G  1 20  ? 16.567 -52.959  -62.074  1.00 69.12  ? 21  PHE G CE1 1 
ATOM   6798  C  CE2 . PHE G  1 20  ? 18.190 -51.293  -62.697  1.00 69.30  ? 21  PHE G CE2 1 
ATOM   6799  C  CZ  . PHE G  1 20  ? 17.168 -51.715  -61.874  1.00 68.45  ? 21  PHE G CZ  1 
ATOM   6800  N  N   . GLU G  1 21  ? 19.057 -54.556  -68.206  1.00 82.39  ? 22  GLU G N   1 
ATOM   6801  C  CA  . GLU G  1 21  ? 19.771 -55.313  -69.231  1.00 85.22  ? 22  GLU G CA  1 
ATOM   6802  C  C   . GLU G  1 21  ? 21.079 -54.643  -69.687  1.00 86.20  ? 22  GLU G C   1 
ATOM   6803  O  O   . GLU G  1 21  ? 21.091 -53.640  -70.397  1.00 88.33  ? 22  GLU G O   1 
ATOM   6804  C  CB  . GLU G  1 21  ? 18.882 -55.583  -70.445  1.00 89.41  ? 22  GLU G CB  1 
ATOM   6805  C  CG  . GLU G  1 21  ? 19.602 -56.441  -71.508  1.00 93.34  ? 22  GLU G CG  1 
ATOM   6806  C  CD  . GLU G  1 21  ? 18.661 -57.003  -72.587  1.00 98.16  ? 22  GLU G CD  1 
ATOM   6807  O  OE1 . GLU G  1 21  ? 17.532 -56.446  -72.740  1.00 99.50  ? 22  GLU G OE1 1 
ATOM   6808  O  OE2 . GLU G  1 21  ? 19.055 -57.998  -73.270  1.00 100.67 ? 22  GLU G OE2 1 
ATOM   6809  N  N   . GLN G  1 22  ? 22.180 -55.251  -69.294  1.00 85.17  ? 23  GLN G N   1 
ATOM   6810  C  CA  . GLN G  1 22  ? 23.507 -54.798  -69.673  1.00 86.77  ? 23  GLN G CA  1 
ATOM   6811  C  C   . GLN G  1 22  ? 24.109 -55.788  -70.687  1.00 90.43  ? 23  GLN G C   1 
ATOM   6812  O  O   . GLN G  1 22  ? 24.503 -56.909  -70.338  1.00 89.84  ? 23  GLN G O   1 
ATOM   6813  C  CB  . GLN G  1 22  ? 24.398 -54.708  -68.427  1.00 83.64  ? 23  GLN G CB  1 
ATOM   6814  C  CG  . GLN G  1 22  ? 25.784 -54.064  -68.660  1.00 85.24  ? 23  GLN G CG  1 
ATOM   6815  C  CD  . GLN G  1 22  ? 26.664 -54.018  -67.395  1.00 82.58  ? 23  GLN G CD  1 
ATOM   6816  O  OE1 . GLN G  1 22  ? 26.750 -54.980  -66.636  1.00 80.97  ? 23  GLN G OE1 1 
ATOM   6817  N  NE2 . GLN G  1 22  ? 27.323 -52.902  -67.182  1.00 83.01  ? 23  GLN G NE2 1 
ATOM   6818  N  N   . LYS G  1 23  ? 24.188 -55.377  -71.944  1.00 94.61  ? 24  LYS G N   1 
ATOM   6819  C  CA  . LYS G  1 23  ? 24.664 -56.286  -73.007  1.00 98.70  ? 24  LYS G CA  1 
ATOM   6820  C  C   . LYS G  1 23  ? 26.114 -56.647  -72.845  1.00 99.08  ? 24  LYS G C   1 
ATOM   6821  O  O   . LYS G  1 23  ? 26.517 -57.744  -73.175  1.00 100.96 ? 24  LYS G O   1 
ATOM   6822  C  CB  . LYS G  1 23  ? 24.467 -55.671  -74.397  1.00 103.55 ? 24  LYS G CB  1 
ATOM   6823  C  CG  . LYS G  1 23  ? 22.989 -55.474  -74.784  1.00 104.77 ? 24  LYS G CG  1 
ATOM   6824  C  CD  . LYS G  1 23  ? 22.787 -55.525  -76.304  1.00 110.70 ? 24  LYS G CD  1 
ATOM   6825  C  CE  . LYS G  1 23  ? 21.517 -54.780  -76.731  1.00 112.30 ? 24  LYS G CE  1 
ATOM   6826  N  NZ  . LYS G  1 23  ? 21.461 -54.622  -78.205  1.00 118.28 ? 24  LYS G NZ  1 
ATOM   6827  N  N   . GLU G  1 24  ? 26.895 -55.700  -72.354  1.00 98.04  ? 25  GLU G N   1 
ATOM   6828  C  CA  . GLU G  1 24  ? 28.341 -55.895  -72.213  1.00 99.52  ? 25  GLU G CA  1 
ATOM   6829  C  C   . GLU G  1 24  ? 28.894 -55.367  -70.889  1.00 95.90  ? 25  GLU G C   1 
ATOM   6830  O  O   . GLU G  1 24  ? 28.571 -54.266  -70.446  1.00 94.24  ? 25  GLU G O   1 
ATOM   6831  C  CB  . GLU G  1 24  ? 29.066 -55.247  -73.394  1.00 104.58 ? 25  GLU G CB  1 
ATOM   6832  C  CG  . GLU G  1 24  ? 28.496 -55.755  -74.724  1.00 108.88 ? 25  GLU G CG  1 
ATOM   6833  C  CD  . GLU G  1 24  ? 29.347 -55.400  -75.923  1.00 115.32 ? 25  GLU G CD  1 
ATOM   6834  O  OE1 . GLU G  1 24  ? 29.796 -54.223  -76.025  1.00 116.85 ? 25  GLU G OE1 1 
ATOM   6835  O  OE2 . GLU G  1 24  ? 29.558 -56.307  -76.767  1.00 119.25 ? 25  GLU G OE2 1 
ATOM   6836  N  N   . SER G  1 25  ? 29.755 -56.161  -70.281  1.00 95.34  ? 26  SER G N   1 
ATOM   6837  C  CA  . SER G  1 25  ? 30.270 -55.875  -68.944  1.00 92.41  ? 26  SER G CA  1 
ATOM   6838  C  C   . SER G  1 25  ? 30.746 -54.423  -68.753  1.00 92.77  ? 26  SER G C   1 
ATOM   6839  O  O   . SER G  1 25  ? 30.547 -53.820  -67.691  1.00 89.59  ? 26  SER G O   1 
ATOM   6840  C  CB  . SER G  1 25  ? 31.419 -56.844  -68.620  1.00 93.88  ? 26  SER G CB  1 
ATOM   6841  O  OG  . SER G  1 25  ? 32.334 -56.982  -69.713  1.00 99.44  ? 26  SER G OG  1 
ATOM   6842  N  N   . ASN G  1 26  ? 31.380 -53.882  -69.789  1.00 97.14  ? 27  ASN G N   1 
ATOM   6843  C  CA  . ASN G  1 26  ? 31.923 -52.511  -69.772  1.00 98.62  ? 27  ASN G CA  1 
ATOM   6844  C  C   . ASN G  1 26  ? 30.926 -51.454  -70.287  1.00 98.55  ? 27  ASN G C   1 
ATOM   6845  O  O   . ASN G  1 26  ? 31.255 -50.256  -70.338  1.00 100.06 ? 27  ASN G O   1 
ATOM   6846  C  CB  . ASN G  1 26  ? 33.196 -52.437  -70.629  1.00 104.09 ? 27  ASN G CB  1 
ATOM   6847  C  CG  . ASN G  1 26  ? 32.894 -52.579  -72.140  1.00 108.25 ? 27  ASN G CG  1 
ATOM   6848  O  OD1 . ASN G  1 26  ? 32.043 -53.393  -72.572  1.00 107.30 ? 27  ASN G OD1 1 
ATOM   6849  N  ND2 . ASN G  1 26  ? 33.572 -51.765  -72.937  1.00 112.60 ? 27  ASN G ND2 1 
ATOM   6850  N  N   . GLY G  1 27  ? 29.721 -51.894  -70.655  1.00 97.17  ? 28  GLY G N   1 
ATOM   6851  C  CA  . GLY G  1 27  ? 28.769 -51.054  -71.385  1.00 98.12  ? 28  GLY G CA  1 
ATOM   6852  C  C   . GLY G  1 27  ? 27.617 -50.528  -70.559  1.00 94.09  ? 28  GLY G C   1 
ATOM   6853  O  O   . GLY G  1 27  ? 27.538 -50.770  -69.368  1.00 90.45  ? 28  GLY G O   1 
ATOM   6854  N  N   . PRO G  1 28  ? 26.704 -49.795  -71.193  1.00 95.32  ? 29  PRO G N   1 
ATOM   6855  C  CA  . PRO G  1 28  ? 25.609 -49.169  -70.473  1.00 92.31  ? 29  PRO G CA  1 
ATOM   6856  C  C   . PRO G  1 28  ? 24.490 -50.147  -70.127  1.00 89.72  ? 29  PRO G C   1 
ATOM   6857  O  O   . PRO G  1 28  ? 24.355 -51.203  -70.750  1.00 91.11  ? 29  PRO G O   1 
ATOM   6858  C  CB  . PRO G  1 28  ? 25.112 -48.123  -71.471  1.00 95.78  ? 29  PRO G CB  1 
ATOM   6859  C  CG  . PRO G  1 28  ? 25.331 -48.755  -72.794  1.00 99.77  ? 29  PRO G CG  1 
ATOM   6860  C  CD  . PRO G  1 28  ? 26.590 -49.582  -72.645  1.00 100.09 ? 29  PRO G CD  1 
ATOM   6861  N  N   . VAL G  1 29  ? 23.689 -49.764  -69.142  1.00 86.41  ? 30  VAL G N   1 
ATOM   6862  C  CA  . VAL G  1 29  ? 22.573 -50.575  -68.663  1.00 84.10  ? 30  VAL G CA  1 
ATOM   6863  C  C   . VAL G  1 29  ? 21.230 -49.960  -69.048  1.00 85.18  ? 30  VAL G C   1 
ATOM   6864  O  O   . VAL G  1 29  ? 20.893 -48.859  -68.609  1.00 84.50  ? 30  VAL G O   1 
ATOM   6865  C  CB  . VAL G  1 29  ? 22.583 -50.683  -67.139  1.00 79.79  ? 30  VAL G CB  1 
ATOM   6866  C  CG1 . VAL G  1 29  ? 21.386 -51.518  -66.662  1.00 77.83  ? 30  VAL G CG1 1 
ATOM   6867  C  CG2 . VAL G  1 29  ? 23.895 -51.261  -66.669  1.00 78.96  ? 30  VAL G CG2 1 
ATOM   6868  N  N   . LYS G  1 30  ? 20.461 -50.670  -69.861  1.00 87.30  ? 31  LYS G N   1 
ATOM   6869  C  CA  . LYS G  1 30  ? 19.100 -50.237  -70.162  1.00 88.77  ? 31  LYS G CA  1 
ATOM   6870  C  C   . LYS G  1 30  ? 18.199 -50.592  -69.007  1.00 85.46  ? 31  LYS G C   1 
ATOM   6871  O  O   . LYS G  1 30  ? 18.252 -51.691  -68.493  1.00 83.85  ? 31  LYS G O   1 
ATOM   6872  C  CB  . LYS G  1 30  ? 18.574 -50.867  -71.450  1.00 93.02  ? 31  LYS G CB  1 
ATOM   6873  C  CG  . LYS G  1 30  ? 19.255 -50.281  -72.693  1.00 97.65  ? 31  LYS G CG  1 
ATOM   6874  C  CD  . LYS G  1 30  ? 18.520 -50.610  -73.995  1.00 102.94 ? 31  LYS G CD  1 
ATOM   6875  C  CE  . LYS G  1 30  ? 19.250 -49.990  -75.197  1.00 107.28 ? 31  LYS G CE  1 
ATOM   6876  N  NZ  . LYS G  1 30  ? 18.496 -50.193  -76.476  1.00 112.90 ? 31  LYS G NZ  1 
ATOM   6877  N  N   . VAL G  1 31  ? 17.385 -49.640  -68.590  1.00 85.06  ? 32  VAL G N   1 
ATOM   6878  C  CA  . VAL G  1 31  ? 16.438 -49.852  -67.511  1.00 82.67  ? 32  VAL G CA  1 
ATOM   6879  C  C   . VAL G  1 31  ? 15.060 -49.594  -68.072  1.00 85.87  ? 32  VAL G C   1 
ATOM   6880  O  O   . VAL G  1 31  ? 14.798 -48.526  -68.614  1.00 88.50  ? 32  VAL G O   1 
ATOM   6881  C  CB  . VAL G  1 31  ? 16.687 -48.879  -66.347  1.00 79.74  ? 32  VAL G CB  1 
ATOM   6882  C  CG1 . VAL G  1 31  ? 15.755 -49.189  -65.186  1.00 77.43  ? 32  VAL G CG1 1 
ATOM   6883  C  CG2 . VAL G  1 31  ? 18.110 -48.948  -65.900  1.00 77.84  ? 32  VAL G CG2 1 
ATOM   6884  N  N   . TRP G  1 32  ? 14.162 -50.553  -67.966  1.00 86.39  ? 33  TRP G N   1 
ATOM   6885  C  CA  . TRP G  1 32  ? 12.805 -50.295  -68.445  1.00 89.98  ? 33  TRP G CA  1 
ATOM   6886  C  C   . TRP G  1 32  ? 11.762 -51.104  -67.701  1.00 89.58  ? 33  TRP G C   1 
ATOM   6887  O  O   . TRP G  1 32  ? 12.072 -52.132  -67.066  1.00 87.29  ? 33  TRP G O   1 
ATOM   6888  C  CB  . TRP G  1 32  ? 12.694 -50.569  -69.946  1.00 94.72  ? 33  TRP G CB  1 
ATOM   6889  C  CG  . TRP G  1 32  ? 12.414 -52.014  -70.286  1.00 96.26  ? 33  TRP G CG  1 
ATOM   6890  C  CD1 . TRP G  1 32  ? 11.193 -52.574  -70.603  1.00 99.72  ? 33  TRP G CD1 1 
ATOM   6891  C  CD2 . TRP G  1 32  ? 13.370 -53.080  -70.335  1.00 94.80  ? 33  TRP G CD2 1 
ATOM   6892  N  NE1 . TRP G  1 32  ? 11.338 -53.928  -70.843  1.00 100.14 ? 33  TRP G NE1 1 
ATOM   6893  C  CE2 . TRP G  1 32  ? 12.659 -54.267  -70.692  1.00 97.24  ? 33  TRP G CE2 1 
ATOM   6894  C  CE3 . TRP G  1 32  ? 14.754 -53.156  -70.101  1.00 92.25  ? 33  TRP G CE3 1 
ATOM   6895  C  CZ2 . TRP G  1 32  ? 13.293 -55.516  -70.836  1.00 97.23  ? 33  TRP G CZ2 1 
ATOM   6896  C  CZ3 . TRP G  1 32  ? 15.387 -54.404  -70.235  1.00 92.32  ? 33  TRP G CZ3 1 
ATOM   6897  C  CH2 . TRP G  1 32  ? 14.650 -55.568  -70.607  1.00 94.69  ? 33  TRP G CH2 1 
ATOM   6898  N  N   . GLY G  1 33  ? 10.519 -50.633  -67.798  1.00 92.34  ? 34  GLY G N   1 
ATOM   6899  C  CA  . GLY G  1 33  ? 9.396  -51.294  -67.138  1.00 92.83  ? 34  GLY G CA  1 
ATOM   6900  C  C   . GLY G  1 33  ? 8.237  -50.354  -66.935  1.00 95.13  ? 34  GLY G C   1 
ATOM   6901  O  O   . GLY G  1 33  ? 8.166  -49.322  -67.571  1.00 97.44  ? 34  GLY G O   1 
ATOM   6902  N  N   . SER G  1 34  ? 7.341  -50.719  -66.027  1.00 94.99  ? 35  SER G N   1 
ATOM   6903  C  CA  . SER G  1 34  ? 6.115  -49.963  -65.804  1.00 98.02  ? 35  SER G CA  1 
ATOM   6904  C  C   . SER G  1 34  ? 5.719  -49.899  -64.332  1.00 95.56  ? 35  SER G C   1 
ATOM   6905  O  O   . SER G  1 34  ? 5.404  -50.925  -63.712  1.00 94.95  ? 35  SER G O   1 
ATOM   6906  C  CB  . SER G  1 34  ? 4.977  -50.591  -66.607  1.00 103.50 ? 35  SER G CB  1 
ATOM   6907  O  OG  . SER G  1 34  ? 3.865  -49.726  -66.624  1.00 107.58 ? 35  SER G OG  1 
ATOM   6908  N  N   . ILE G  1 35  ? 5.720  -48.689  -63.780  1.00 94.59  ? 36  ILE G N   1 
ATOM   6909  C  CA  . ILE G  1 35  ? 5.230  -48.466  -62.408  1.00 93.29  ? 36  ILE G CA  1 
ATOM   6910  C  C   . ILE G  1 35  ? 3.852  -47.811  -62.431  1.00 98.06  ? 36  ILE G C   1 
ATOM   6911  O  O   . ILE G  1 35  ? 3.573  -46.954  -63.275  1.00 101.12 ? 36  ILE G O   1 
ATOM   6912  C  CB  . ILE G  1 35  ? 6.151  -47.544  -61.581  1.00 89.28  ? 36  ILE G CB  1 
ATOM   6913  C  CG1 . ILE G  1 35  ? 7.601  -48.024  -61.648  1.00 85.34  ? 36  ILE G CG1 1 
ATOM   6914  C  CG2 . ILE G  1 35  ? 5.664  -47.470  -60.103  1.00 87.57  ? 36  ILE G CG2 1 
ATOM   6915  C  CD1 . ILE G  1 35  ? 8.584  -47.063  -60.975  1.00 82.34  ? 36  ILE G CD1 1 
ATOM   6916  N  N   . LYS G  1 36  ? 3.005  -48.199  -61.485  1.00 98.94  ? 37  LYS G N   1 
ATOM   6917  C  CA  . LYS G  1 36  ? 1.646  -47.659  -61.423  1.00 104.00 ? 37  LYS G CA  1 
ATOM   6918  C  C   . LYS G  1 36  ? 1.194  -47.319  -59.997  1.00 103.14 ? 37  LYS G C   1 
ATOM   6919  O  O   . LYS G  1 36  ? 1.862  -47.680  -59.018  1.00 98.76  ? 37  LYS G O   1 
ATOM   6920  C  CB  . LYS G  1 36  ? 0.647  -48.618  -62.101  1.00 108.94 ? 37  LYS G CB  1 
ATOM   6921  C  CG  . LYS G  1 36  ? 0.569  -50.010  -61.511  1.00 107.87 ? 37  LYS G CG  1 
ATOM   6922  C  CD  . LYS G  1 36  ? -0.755 -50.663  -61.891  1.00 114.48 ? 37  LYS G CD  1 
ATOM   6923  C  CE  . LYS G  1 36  ? -0.820 -52.125  -61.434  1.00 114.07 ? 37  LYS G CE  1 
ATOM   6924  N  NZ  . LYS G  1 36  ? -2.192 -52.706  -61.591  1.00 120.49 ? 37  LYS G NZ  1 
ATOM   6925  N  N   . GLY G  1 37  ? 0.054  -46.627  -59.911  1.00 107.84 ? 38  GLY G N   1 
ATOM   6926  C  CA  . GLY G  1 37  ? -0.498 -46.117  -58.638  1.00 108.23 ? 38  GLY G CA  1 
ATOM   6927  C  C   . GLY G  1 37  ? 0.150  -44.804  -58.212  1.00 105.81 ? 38  GLY G C   1 
ATOM   6928  O  O   . GLY G  1 37  ? 0.011  -44.377  -57.056  1.00 104.93 ? 38  GLY G O   1 
ATOM   6929  N  N   . LEU G  1 38  ? 0.842  -44.165  -59.159  1.00 105.07 ? 39  LEU G N   1 
ATOM   6930  C  CA  . LEU G  1 38  ? 1.673  -42.997  -58.868  1.00 102.59 ? 39  LEU G CA  1 
ATOM   6931  C  C   . LEU G  1 38  ? 0.874  -41.716  -59.019  1.00 107.15 ? 39  LEU G C   1 
ATOM   6932  O  O   . LEU G  1 38  ? 0.017  -41.613  -59.907  1.00 112.03 ? 39  LEU G O   1 
ATOM   6933  C  CB  . LEU G  1 38  ? 2.917  -42.941  -59.783  1.00 99.82  ? 39  LEU G CB  1 
ATOM   6934  C  CG  . LEU G  1 38  ? 4.151  -43.743  -59.329  1.00 94.11  ? 39  LEU G CG  1 
ATOM   6935  C  CD1 . LEU G  1 38  ? 5.139  -43.913  -60.472  1.00 92.78  ? 39  LEU G CD1 1 
ATOM   6936  C  CD2 . LEU G  1 38  ? 4.858  -43.101  -58.152  1.00 90.59  ? 39  LEU G CD2 1 
ATOM   6937  N  N   . THR G  1 39  ? 1.176  -40.744  -58.151  1.00 105.80 ? 40  THR G N   1 
ATOM   6938  C  CA  . THR G  1 39  ? 0.615  -39.378  -58.257  1.00 109.83 ? 40  THR G CA  1 
ATOM   6939  C  C   . THR G  1 39  ? 1.138  -38.727  -59.570  1.00 110.82 ? 40  THR G C   1 
ATOM   6940  O  O   . THR G  1 39  ? 2.326  -38.855  -59.919  1.00 106.91 ? 40  THR G O   1 
ATOM   6941  C  CB  . THR G  1 39  ? 0.947  -38.477  -56.994  1.00 108.09 ? 40  THR G CB  1 
ATOM   6942  O  OG1 . THR G  1 39  ? 1.978  -37.513  -57.300  1.00 106.51 ? 40  THR G OG1 1 
ATOM   6943  C  CG2 . THR G  1 39  ? 1.354  -39.330  -55.778  1.00 103.78 ? 40  THR G CG2 1 
ATOM   6944  N  N   . GLU G  1 40  ? 0.254  -38.065  -60.310  1.00 116.39 ? 41  GLU G N   1 
ATOM   6945  C  CA  . GLU G  1 40  ? 0.646  -37.554  -61.619  1.00 118.30 ? 41  GLU G CA  1 
ATOM   6946  C  C   . GLU G  1 40  ? 1.864  -36.642  -61.494  1.00 115.02 ? 41  GLU G C   1 
ATOM   6947  O  O   . GLU G  1 40  ? 1.937  -35.805  -60.589  1.00 114.51 ? 41  GLU G O   1 
ATOM   6948  C  CB  . GLU G  1 40  ? -0.490 -36.783  -62.312  1.00 125.56 ? 41  GLU G CB  1 
ATOM   6949  C  CG  . GLU G  1 40  ? -0.057 -36.160  -63.703  1.00 128.27 ? 41  GLU G CG  1 
ATOM   6950  C  CD  . GLU G  1 40  ? -1.122 -35.248  -64.382  1.00 136.22 ? 41  GLU G CD  1 
ATOM   6951  O  OE1 . GLU G  1 40  ? -1.717 -34.356  -63.693  1.00 138.59 ? 41  GLU G OE1 1 
ATOM   6952  O  OE2 . GLU G  1 40  ? -1.325 -35.417  -65.622  1.00 139.56 ? 41  GLU G OE2 1 
ATOM   6953  N  N   . GLY G  1 41  ? 2.808  -36.808  -62.416  1.00 113.31 ? 42  GLY G N   1 
ATOM   6954  C  CA  . GLY G  1 41  ? 3.967  -35.919  -62.509  1.00 111.32 ? 42  GLY G CA  1 
ATOM   6955  C  C   . GLY G  1 41  ? 5.280  -36.622  -62.282  1.00 105.71 ? 42  GLY G C   1 
ATOM   6956  O  O   . GLY G  1 41  ? 5.370  -37.847  -62.455  1.00 103.85 ? 42  GLY G O   1 
ATOM   6957  N  N   . LEU G  1 42  ? 6.298  -35.847  -61.899  1.00 103.45 ? 43  LEU G N   1 
ATOM   6958  C  CA  . LEU G  1 42  ? 7.664  -36.379  -61.717  1.00 98.66  ? 43  LEU G CA  1 
ATOM   6959  C  C   . LEU G  1 42  ? 7.839  -37.137  -60.393  1.00 94.47  ? 43  LEU G C   1 
ATOM   6960  O  O   . LEU G  1 42  ? 7.242  -36.779  -59.371  1.00 94.89  ? 43  LEU G O   1 
ATOM   6961  C  CB  . LEU G  1 42  ? 8.713  -35.273  -61.804  1.00 98.43  ? 43  LEU G CB  1 
ATOM   6962  C  CG  . LEU G  1 42  ? 9.025  -34.766  -63.216  1.00 101.53 ? 43  LEU G CG  1 
ATOM   6963  C  CD1 . LEU G  1 42  ? 8.508  -33.342  -63.403  1.00 106.17 ? 43  LEU G CD1 1 
ATOM   6964  C  CD2 . LEU G  1 42  ? 10.515 -34.820  -63.501  1.00 99.24  ? 43  LEU G CD2 1 
ATOM   6965  N  N   . HIS G  1 43  ? 8.653  -38.193  -60.436  1.00 90.88  ? 44  HIS G N   1 
ATOM   6966  C  CA  . HIS G  1 43  ? 9.004  -38.962  -59.242  1.00 86.86  ? 44  HIS G CA  1 
ATOM   6967  C  C   . HIS G  1 43  ? 10.478 -39.342  -59.227  1.00 83.35  ? 44  HIS G C   1 
ATOM   6968  O  O   . HIS G  1 43  ? 11.032 -39.793  -60.240  1.00 83.29  ? 44  HIS G O   1 
ATOM   6969  C  CB  . HIS G  1 43  ? 8.157  -40.219  -59.130  1.00 86.67  ? 44  HIS G CB  1 
ATOM   6970  C  CG  . HIS G  1 43  ? 6.725  -39.946  -58.773  1.00 90.18  ? 44  HIS G CG  1 
ATOM   6971  N  ND1 . HIS G  1 43  ? 6.306  -39.709  -57.479  1.00 89.96  ? 44  HIS G ND1 1 
ATOM   6972  C  CD2 . HIS G  1 43  ? 5.613  -39.868  -59.544  1.00 94.58  ? 44  HIS G CD2 1 
ATOM   6973  C  CE1 . HIS G  1 43  ? 4.999  -39.506  -57.466  1.00 93.75  ? 44  HIS G CE1 1 
ATOM   6974  N  NE2 . HIS G  1 43  ? 4.555  -39.593  -58.706  1.00 96.72  ? 44  HIS G NE2 1 
ATOM   6975  N  N   . GLY G  1 44  ? 11.097 -39.146  -58.062  1.00 80.79  ? 45  GLY G N   1 
ATOM   6976  C  CA  . GLY G  1 44  ? 12.490 -39.521  -57.834  1.00 77.66  ? 45  GLY G CA  1 
ATOM   6977  C  C   . GLY G  1 44  ? 12.653 -41.023  -57.973  1.00 75.47  ? 45  GLY G C   1 
ATOM   6978  O  O   . GLY G  1 44  ? 11.728 -41.803  -57.664  1.00 75.57  ? 45  GLY G O   1 
ATOM   6979  N  N   . PHE G  1 45  ? 13.830 -41.433  -58.433  1.00 73.96  ? 46  PHE G N   1 
ATOM   6980  C  CA  . PHE G  1 45  ? 14.040 -42.817  -58.858  1.00 72.56  ? 46  PHE G CA  1 
ATOM   6981  C  C   . PHE G  1 45  ? 15.499 -43.198  -58.698  1.00 70.36  ? 46  PHE G C   1 
ATOM   6982  O  O   . PHE G  1 45  ? 16.336 -42.838  -59.549  1.00 71.33  ? 46  PHE G O   1 
ATOM   6983  C  CB  . PHE G  1 45  ? 13.630 -42.945  -60.321  1.00 75.28  ? 46  PHE G CB  1 
ATOM   6984  C  CG  . PHE G  1 45  ? 13.544 -44.357  -60.822  1.00 74.70  ? 46  PHE G CG  1 
ATOM   6985  C  CD1 . PHE G  1 45  ? 12.781 -45.312  -60.146  1.00 73.64  ? 46  PHE G CD1 1 
ATOM   6986  C  CD2 . PHE G  1 45  ? 14.176 -44.715  -62.014  1.00 75.70  ? 46  PHE G CD2 1 
ATOM   6987  C  CE1 . PHE G  1 45  ? 12.671 -46.605  -60.639  1.00 73.69  ? 46  PHE G CE1 1 
ATOM   6988  C  CE2 . PHE G  1 45  ? 14.074 -46.005  -62.509  1.00 75.77  ? 46  PHE G CE2 1 
ATOM   6989  C  CZ  . PHE G  1 45  ? 13.323 -46.956  -61.820  1.00 74.81  ? 46  PHE G CZ  1 
ATOM   6990  N  N   . HIS G  1 46  ? 15.796 -43.917  -57.608  1.00 67.72  ? 47  HIS G N   1 
ATOM   6991  C  CA  . HIS G  1 46  ? 17.184 -44.190  -57.231  1.00 65.90  ? 47  HIS G CA  1 
ATOM   6992  C  C   . HIS G  1 46  ? 17.461 -45.602  -56.755  1.00 63.69  ? 47  HIS G C   1 
ATOM   6993  O  O   . HIS G  1 46  ? 16.595 -46.290  -56.239  1.00 63.09  ? 47  HIS G O   1 
ATOM   6994  C  CB  . HIS G  1 46  ? 17.613 -43.231  -56.133  1.00 65.57  ? 47  HIS G CB  1 
ATOM   6995  C  CG  . HIS G  1 46  ? 17.079 -41.840  -56.300  1.00 67.74  ? 47  HIS G CG  1 
ATOM   6996  N  ND1 . HIS G  1 46  ? 16.020 -41.356  -55.557  1.00 68.35  ? 47  HIS G ND1 1 
ATOM   6997  C  CD2 . HIS G  1 46  ? 17.449 -40.836  -57.131  1.00 70.22  ? 47  HIS G CD2 1 
ATOM   6998  C  CE1 . HIS G  1 46  ? 15.771 -40.109  -55.910  1.00 70.78  ? 47  HIS G CE1 1 
ATOM   6999  N  NE2 . HIS G  1 46  ? 16.622 -39.770  -56.865  1.00 71.98  ? 47  HIS G NE2 1 
ATOM   7000  N  N   . VAL G  1 47  ? 18.703 -46.014  -56.947  1.00 63.10  ? 48  VAL G N   1 
ATOM   7001  C  CA  . VAL G  1 47  ? 19.202 -47.268  -56.402  1.00 61.31  ? 48  VAL G CA  1 
ATOM   7002  C  C   . VAL G  1 47  ? 19.858 -46.970  -55.071  1.00 60.11  ? 48  VAL G C   1 
ATOM   7003  O  O   . VAL G  1 47  ? 20.849 -46.254  -55.008  1.00 60.72  ? 48  VAL G O   1 
ATOM   7004  C  CB  . VAL G  1 47  ? 20.272 -47.930  -57.323  1.00 61.80  ? 48  VAL G CB  1 
ATOM   7005  C  CG1 . VAL G  1 47  ? 20.976 -49.104  -56.612  1.00 59.95  ? 48  VAL G CG1 1 
ATOM   7006  C  CG2 . VAL G  1 47  ? 19.638 -48.389  -58.646  1.00 63.40  ? 48  VAL G CG2 1 
ATOM   7007  N  N   . HIS G  1 48  ? 19.313 -47.551  -54.017  1.00 58.93  ? 49  HIS G N   1 
ATOM   7008  C  CA  . HIS G  1 48  ? 19.857 -47.389  -52.674  1.00 58.19  ? 49  HIS G CA  1 
ATOM   7009  C  C   . HIS G  1 48  ? 20.865 -48.481  -52.325  1.00 57.28  ? 49  HIS G C   1 
ATOM   7010  O  O   . HIS G  1 48  ? 20.921 -49.517  -52.976  1.00 57.26  ? 49  HIS G O   1 
ATOM   7011  C  CB  . HIS G  1 48  ? 18.723 -47.387  -51.647  1.00 57.99  ? 49  HIS G CB  1 
ATOM   7012  C  CG  . HIS G  1 48  ? 17.883 -46.152  -51.692  1.00 59.32  ? 49  HIS G CG  1 
ATOM   7013  N  ND1 . HIS G  1 48  ? 17.713 -45.323  -50.602  1.00 59.68  ? 49  HIS G ND1 1 
ATOM   7014  C  CD2 . HIS G  1 48  ? 17.182 -45.598  -52.705  1.00 60.44  ? 49  HIS G CD2 1 
ATOM   7015  C  CE1 . HIS G  1 48  ? 16.929 -44.318  -50.942  1.00 61.19  ? 49  HIS G CE1 1 
ATOM   7016  N  NE2 . HIS G  1 48  ? 16.589 -44.464  -52.209  1.00 61.83  ? 49  HIS G NE2 1 
ATOM   7017  N  N   . GLU G  1 49  ? 21.625 -48.255  -51.260  1.00 57.17  ? 50  GLU G N   1 
ATOM   7018  C  CA  . GLU G  1 49  ? 22.777 -49.102  -50.908  1.00 56.95  ? 50  GLU G CA  1 
ATOM   7019  C  C   . GLU G  1 49  ? 22.419 -50.558  -50.586  1.00 55.78  ? 50  GLU G C   1 
ATOM   7020  O  O   . GLU G  1 49  ? 22.950 -51.487  -51.195  1.00 55.62  ? 50  GLU G O   1 
ATOM   7021  C  CB  . GLU G  1 49  ? 23.540 -48.494  -49.728  1.00 57.66  ? 50  GLU G CB  1 
ATOM   7022  C  CG  . GLU G  1 49  ? 24.878 -49.143  -49.458  1.00 58.29  ? 50  GLU G CG  1 
ATOM   7023  C  CD  . GLU G  1 49  ? 25.737 -48.364  -48.460  1.00 59.75  ? 50  GLU G CD  1 
ATOM   7024  O  OE1 . GLU G  1 49  ? 25.448 -47.194  -48.166  1.00 60.04  ? 50  GLU G OE1 1 
ATOM   7025  O  OE2 . GLU G  1 49  ? 26.724 -48.934  -47.960  1.00 60.94  ? 50  GLU G OE2 1 
ATOM   7026  N  N   . PHE G  1 50  ? 21.494 -50.744  -49.653  1.00 55.20  ? 51  PHE G N   1 
ATOM   7027  C  CA  . PHE G  1 50  ? 21.213 -52.068  -49.108  1.00 54.58  ? 51  PHE G CA  1 
ATOM   7028  C  C   . PHE G  1 50  ? 19.964 -52.753  -49.637  1.00 54.43  ? 51  PHE G C   1 
ATOM   7029  O  O   . PHE G  1 50  ? 18.915 -52.144  -49.752  1.00 54.75  ? 51  PHE G O   1 
ATOM   7030  C  CB  . PHE G  1 50  ? 21.088 -51.988  -47.599  1.00 54.68  ? 51  PHE G CB  1 
ATOM   7031  C  CG  . PHE G  1 50  ? 22.248 -51.326  -46.941  1.00 55.43  ? 51  PHE G CG  1 
ATOM   7032  C  CD1 . PHE G  1 50  ? 23.513 -51.834  -47.089  1.00 55.98  ? 51  PHE G CD1 1 
ATOM   7033  C  CD2 . PHE G  1 50  ? 22.073 -50.193  -46.175  1.00 56.44  ? 51  PHE G CD2 1 
ATOM   7034  C  CE1 . PHE G  1 50  ? 24.591 -51.221  -46.485  1.00 57.52  ? 51  PHE G CE1 1 
ATOM   7035  C  CE2 . PHE G  1 50  ? 23.140 -49.571  -45.572  1.00 57.61  ? 51  PHE G CE2 1 
ATOM   7036  C  CZ  . PHE G  1 50  ? 24.402 -50.084  -45.723  1.00 58.26  ? 51  PHE G CZ  1 
ATOM   7037  N  N   . GLY G  1 51  ? 20.099 -54.048  -49.916  1.00 54.48  ? 52  GLY G N   1 
ATOM   7038  C  CA  . GLY G  1 51  ? 18.980 -54.927  -50.283  1.00 54.82  ? 52  GLY G CA  1 
ATOM   7039  C  C   . GLY G  1 51  ? 18.222 -55.423  -49.065  1.00 54.92  ? 52  GLY G C   1 
ATOM   7040  O  O   . GLY G  1 51  ? 17.773 -56.562  -49.005  1.00 55.31  ? 52  GLY G O   1 
ATOM   7041  N  N   . ASP G  1 52  ? 18.055 -54.532  -48.103  1.00 54.94  ? 53  ASP G N   1 
ATOM   7042  C  CA  . ASP G  1 52  ? 17.452 -54.860  -46.827  1.00 55.41  ? 53  ASP G CA  1 
ATOM   7043  C  C   . ASP G  1 52  ? 16.015 -54.350  -46.823  1.00 56.41  ? 53  ASP G C   1 
ATOM   7044  O  O   . ASP G  1 52  ? 15.756 -53.168  -47.001  1.00 56.57  ? 53  ASP G O   1 
ATOM   7045  C  CB  . ASP G  1 52  ? 18.269 -54.205  -45.710  1.00 55.38  ? 53  ASP G CB  1 
ATOM   7046  C  CG  . ASP G  1 52  ? 17.874 -54.681  -44.335  1.00 56.32  ? 53  ASP G CG  1 
ATOM   7047  O  OD1 . ASP G  1 52  ? 16.680 -54.965  -44.115  1.00 57.41  ? 53  ASP G OD1 1 
ATOM   7048  O  OD2 . ASP G  1 52  ? 18.757 -54.752  -43.464  1.00 56.37  ? 53  ASP G OD2 1 
ATOM   7049  N  N   . ASN G  1 53  ? 15.080 -55.255  -46.625  1.00 57.48  ? 54  ASN G N   1 
ATOM   7050  C  CA  . ASN G  1 53  ? 13.667 -54.895  -46.571  1.00 59.21  ? 54  ASN G CA  1 
ATOM   7051  C  C   . ASN G  1 53  ? 13.050 -55.199  -45.197  1.00 60.47  ? 54  ASN G C   1 
ATOM   7052  O  O   . ASN G  1 53  ? 11.828 -55.256  -45.055  1.00 62.24  ? 54  ASN G O   1 
ATOM   7053  C  CB  . ASN G  1 53  ? 12.919 -55.670  -47.649  1.00 60.44  ? 54  ASN G CB  1 
ATOM   7054  C  CG  . ASN G  1 53  ? 12.021 -54.799  -48.474  1.00 62.00  ? 54  ASN G CG  1 
ATOM   7055  O  OD1 . ASN G  1 53  ? 12.494 -53.905  -49.195  1.00 61.63  ? 54  ASN G OD1 1 
ATOM   7056  N  ND2 . ASN G  1 53  ? 10.713 -55.069  -48.409  1.00 64.47  ? 54  ASN G ND2 1 
ATOM   7057  N  N   . THR G  1 54  ? 13.917 -55.418  -44.209  1.00 59.73  ? 55  THR G N   1 
ATOM   7058  C  CA  . THR G  1 54  ? 13.539 -55.790  -42.848  1.00 61.24  ? 55  THR G CA  1 
ATOM   7059  C  C   . THR G  1 54  ? 12.404 -54.928  -42.332  1.00 63.26  ? 55  THR G C   1 
ATOM   7060  O  O   . THR G  1 54  ? 11.306 -55.425  -42.075  1.00 65.29  ? 55  THR G O   1 
ATOM   7061  C  CB  . THR G  1 54  ? 14.759 -55.630  -41.907  1.00 60.60  ? 55  THR G CB  1 
ATOM   7062  O  OG1 . THR G  1 54  ? 15.727 -56.631  -42.212  1.00 59.69  ? 55  THR G OG1 1 
ATOM   7063  C  CG2 . THR G  1 54  ? 14.367 -55.725  -40.421  1.00 62.68  ? 55  THR G CG2 1 
ATOM   7064  N  N   . ALA G  1 55  ? 12.694 -53.630  -42.191  1.00 62.99  ? 56  ALA G N   1 
ATOM   7065  C  CA  . ALA G  1 55  ? 11.742 -52.617  -41.708  1.00 64.95  ? 56  ALA G CA  1 
ATOM   7066  C  C   . ALA G  1 55  ? 11.215 -51.775  -42.880  1.00 64.89  ? 56  ALA G C   1 
ATOM   7067  O  O   . ALA G  1 55  ? 11.205 -50.555  -42.843  1.00 65.45  ? 56  ALA G O   1 
ATOM   7068  C  CB  . ALA G  1 55  ? 12.398 -51.726  -40.624  1.00 65.16  ? 56  ALA G CB  1 
ATOM   7069  N  N   . GLY G  1 56  ? 10.787 -52.453  -43.929  1.00 64.81  ? 57  GLY G N   1 
ATOM   7070  C  CA  . GLY G  1 56  ? 10.180 -51.810  -45.081  1.00 65.44  ? 57  GLY G CA  1 
ATOM   7071  C  C   . GLY G  1 56  ? 11.213 -51.260  -46.023  1.00 63.24  ? 57  GLY G C   1 
ATOM   7072  O  O   . GLY G  1 56  ? 12.297 -51.790  -46.132  1.00 61.48  ? 57  GLY G O   1 
ATOM   7073  N  N   . CYS G  1 57  ? 10.867 -50.188  -46.711  1.00 63.97  ? 58  CYS G N   1 
ATOM   7074  C  CA  . CYS G  1 57  ? 11.800 -49.505  -47.602  1.00 62.44  ? 58  CYS G CA  1 
ATOM   7075  C  C   . CYS G  1 57  ? 12.876 -48.727  -46.853  1.00 61.31  ? 58  CYS G C   1 
ATOM   7076  O  O   . CYS G  1 57  ? 13.939 -48.467  -47.409  1.00 60.06  ? 58  CYS G O   1 
ATOM   7077  C  CB  . CYS G  1 57  ? 11.049 -48.553  -48.541  1.00 64.18  ? 58  CYS G CB  1 
ATOM   7078  S  SG  . CYS G  1 57  ? 9.963  -49.406  -49.794  1.00 66.56  ? 58  CYS G SG  1 
ATOM   7079  N  N   . THR G  1 58  ? 12.597 -48.328  -45.613  1.00 62.33  ? 59  THR G N   1 
ATOM   7080  C  CA  . THR G  1 58  ? 13.539 -47.509  -44.834  1.00 62.02  ? 59  THR G CA  1 
ATOM   7081  C  C   . THR G  1 58  ? 14.875 -48.207  -44.643  1.00 60.27  ? 59  THR G C   1 
ATOM   7082  O  O   . THR G  1 58  ? 15.928 -47.550  -44.620  1.00 59.84  ? 59  THR G O   1 
ATOM   7083  C  CB  . THR G  1 58  ? 12.997 -47.195  -43.439  1.00 63.78  ? 59  THR G CB  1 
ATOM   7084  O  OG1 . THR G  1 58  ? 11.623 -46.837  -43.539  1.00 66.07  ? 59  THR G OG1 1 
ATOM   7085  C  CG2 . THR G  1 58  ? 13.798 -46.060  -42.794  1.00 64.22  ? 59  THR G CG2 1 
ATOM   7086  N  N   . SER G  1 59  ? 14.813 -49.536  -44.511  1.00 59.66  ? 60  SER G N   1 
ATOM   7087  C  CA  . SER G  1 59  ? 15.995 -50.386  -44.267  1.00 58.40  ? 60  SER G CA  1 
ATOM   7088  C  C   . SER G  1 59  ? 17.042 -50.331  -45.386  1.00 57.07  ? 60  SER G C   1 
ATOM   7089  O  O   . SER G  1 59  ? 18.215 -50.607  -45.152  1.00 56.55  ? 60  SER G O   1 
ATOM   7090  C  CB  . SER G  1 59  ? 15.551 -51.833  -44.081  1.00 58.42  ? 60  SER G CB  1 
ATOM   7091  O  OG  . SER G  1 59  ? 14.424 -51.893  -43.231  1.00 60.44  ? 60  SER G OG  1 
ATOM   7092  N  N   . ALA G  1 60  ? 16.601 -49.973  -46.592  1.00 57.09  ? 61  ALA G N   1 
ATOM   7093  C  CA  . ALA G  1 60  ? 17.464 -49.879  -47.788  1.00 56.30  ? 61  ALA G CA  1 
ATOM   7094  C  C   . ALA G  1 60  ? 18.594 -48.879  -47.654  1.00 56.27  ? 61  ALA G C   1 
ATOM   7095  O  O   . ALA G  1 60  ? 19.508 -48.870  -48.473  1.00 55.86  ? 61  ALA G O   1 
ATOM   7096  C  CB  . ALA G  1 60  ? 16.630 -49.513  -49.018  1.00 57.03  ? 61  ALA G CB  1 
ATOM   7097  N  N   . GLY G  1 61  ? 18.494 -48.012  -46.651  1.00 57.11  ? 62  GLY G N   1 
ATOM   7098  C  CA  . GLY G  1 61  ? 19.542 -47.049  -46.366  1.00 57.93  ? 62  GLY G CA  1 
ATOM   7099  C  C   . GLY G  1 61  ? 19.569 -45.943  -47.401  1.00 58.68  ? 62  GLY G C   1 
ATOM   7100  O  O   . GLY G  1 61  ? 18.578 -45.716  -48.088  1.00 58.95  ? 62  GLY G O   1 
ATOM   7101  N  N   . PRO G  1 62  ? 20.715 -45.261  -47.542  1.00 59.42  ? 63  PRO G N   1 
ATOM   7102  C  CA  . PRO G  1 62  ? 20.805 -44.104  -48.406  1.00 60.65  ? 63  PRO G CA  1 
ATOM   7103  C  C   . PRO G  1 62  ? 21.062 -44.440  -49.846  1.00 60.37  ? 63  PRO G C   1 
ATOM   7104  O  O   . PRO G  1 62  ? 21.144 -45.596  -50.196  1.00 59.36  ? 63  PRO G O   1 
ATOM   7105  C  CB  . PRO G  1 62  ? 22.023 -43.383  -47.859  1.00 62.10  ? 63  PRO G CB  1 
ATOM   7106  C  CG  . PRO G  1 62  ? 22.894 -44.452  -47.413  1.00 61.24  ? 63  PRO G CG  1 
ATOM   7107  C  CD  . PRO G  1 62  ? 21.997 -45.520  -46.872  1.00 59.75  ? 63  PRO G CD  1 
ATOM   7108  N  N   . HIS G  1 63  ? 21.195 -43.407  -50.663  1.00 61.84  ? 64  HIS G N   1 
ATOM   7109  C  CA  . HIS G  1 63  ? 21.516 -43.543  -52.074  1.00 62.25  ? 64  HIS G CA  1 
ATOM   7110  C  C   . HIS G  1 63  ? 22.829 -44.296  -52.245  1.00 61.91  ? 64  HIS G C   1 
ATOM   7111  O  O   . HIS G  1 63  ? 23.790 -44.030  -51.532  1.00 62.58  ? 64  HIS G O   1 
ATOM   7112  C  CB  . HIS G  1 63  ? 21.655 -42.153  -52.713  1.00 64.62  ? 64  HIS G CB  1 
ATOM   7113  C  CG  . HIS G  1 63  ? 20.353 -41.423  -52.892  1.00 65.25  ? 64  HIS G CG  1 
ATOM   7114  N  ND1 . HIS G  1 63  ? 20.122 -40.565  -53.945  1.00 66.96  ? 64  HIS G ND1 1 
ATOM   7115  C  CD2 . HIS G  1 63  ? 19.215 -41.433  -52.161  1.00 64.66  ? 64  HIS G CD2 1 
ATOM   7116  C  CE1 . HIS G  1 63  ? 18.905 -40.070  -53.848  1.00 67.72  ? 64  HIS G CE1 1 
ATOM   7117  N  NE2 . HIS G  1 63  ? 18.335 -40.575  -52.771  1.00 66.28  ? 64  HIS G NE2 1 
ATOM   7118  N  N   . PHE G  1 64  ? 22.863 -45.236  -53.191  1.00 61.36  ? 65  PHE G N   1 
ATOM   7119  C  CA  . PHE G  1 64  ? 24.064 -46.035  -53.420  1.00 61.50  ? 65  PHE G CA  1 
ATOM   7120  C  C   . PHE G  1 64  ? 25.175 -45.117  -53.870  1.00 63.69  ? 65  PHE G C   1 
ATOM   7121  O  O   . PHE G  1 64  ? 25.073 -44.490  -54.913  1.00 64.87  ? 65  PHE G O   1 
ATOM   7122  C  CB  . PHE G  1 64  ? 23.820 -47.152  -54.438  1.00 61.05  ? 65  PHE G CB  1 
ATOM   7123  C  CG  . PHE G  1 64  ? 25.036 -48.012  -54.717  1.00 61.36  ? 65  PHE G CG  1 
ATOM   7124  C  CD1 . PHE G  1 64  ? 25.865 -48.434  -53.701  1.00 61.15  ? 65  PHE G CD1 1 
ATOM   7125  C  CD2 . PHE G  1 64  ? 25.316 -48.427  -56.004  1.00 62.67  ? 65  PHE G CD2 1 
ATOM   7126  C  CE1 . PHE G  1 64  ? 26.950 -49.225  -53.969  1.00 62.39  ? 65  PHE G CE1 1 
ATOM   7127  C  CE2 . PHE G  1 64  ? 26.396 -49.223  -56.275  1.00 63.66  ? 65  PHE G CE2 1 
ATOM   7128  C  CZ  . PHE G  1 64  ? 27.215 -49.621  -55.261  1.00 63.59  ? 65  PHE G CZ  1 
ATOM   7129  N  N   . ASN G  1 65  ? 26.226 -45.055  -53.062  1.00 64.57  ? 66  ASN G N   1 
ATOM   7130  C  CA  . ASN G  1 65  ? 27.265 -44.048  -53.211  1.00 67.48  ? 66  ASN G CA  1 
ATOM   7131  C  C   . ASN G  1 65  ? 28.677 -44.554  -52.839  1.00 68.99  ? 66  ASN G C   1 
ATOM   7132  O  O   . ASN G  1 65  ? 29.266 -44.112  -51.858  1.00 70.31  ? 66  ASN G O   1 
ATOM   7133  C  CB  . ASN G  1 65  ? 26.880 -42.835  -52.363  1.00 68.08  ? 66  ASN G CB  1 
ATOM   7134  C  CG  . ASN G  1 65  ? 27.805 -41.639  -52.571  1.00 71.52  ? 66  ASN G CG  1 
ATOM   7135  O  OD1 . ASN G  1 65  ? 28.652 -41.615  -53.478  1.00 73.78  ? 66  ASN G OD1 1 
ATOM   7136  N  ND2 . ASN G  1 65  ? 27.641 -40.632  -51.726  1.00 72.51  ? 66  ASN G ND2 1 
ATOM   7137  N  N   . PRO G  1 66  ? 29.238 -45.468  -53.641  1.00 69.33  ? 67  PRO G N   1 
ATOM   7138  C  CA  . PRO G  1 66  ? 30.522 -46.059  -53.324  1.00 71.06  ? 67  PRO G CA  1 
ATOM   7139  C  C   . PRO G  1 66  ? 31.710 -45.145  -53.592  1.00 75.11  ? 67  PRO G C   1 
ATOM   7140  O  O   . PRO G  1 66  ? 32.761 -45.323  -52.976  1.00 77.37  ? 67  PRO G O   1 
ATOM   7141  C  CB  . PRO G  1 66  ? 30.577 -47.268  -54.250  1.00 70.47  ? 67  PRO G CB  1 
ATOM   7142  C  CG  . PRO G  1 66  ? 29.781 -46.876  -55.411  1.00 70.16  ? 67  PRO G CG  1 
ATOM   7143  C  CD  . PRO G  1 66  ? 28.692 -45.999  -54.898  1.00 68.71  ? 67  PRO G CD  1 
ATOM   7144  N  N   . LEU G  1 67  ? 31.552 -44.182  -54.498  1.00 76.59  ? 68  LEU G N   1 
ATOM   7145  C  CA  . LEU G  1 67  ? 32.634 -43.222  -54.807  1.00 80.83  ? 68  LEU G CA  1 
ATOM   7146  C  C   . LEU G  1 67  ? 32.561 -41.949  -53.947  1.00 82.06  ? 68  LEU G C   1 
ATOM   7147  O  O   . LEU G  1 67  ? 33.251 -40.955  -54.225  1.00 85.66  ? 68  LEU G O   1 
ATOM   7148  C  CB  . LEU G  1 67  ? 32.629 -42.855  -56.295  1.00 82.64  ? 68  LEU G CB  1 
ATOM   7149  C  CG  . LEU G  1 67  ? 32.779 -44.041  -57.264  1.00 82.53  ? 68  LEU G CG  1 
ATOM   7150  C  CD1 . LEU G  1 67  ? 32.977 -43.507  -58.704  1.00 85.42  ? 68  LEU G CD1 1 
ATOM   7151  C  CD2 . LEU G  1 67  ? 33.902 -45.041  -56.839  1.00 83.56  ? 68  LEU G CD2 1 
ATOM   7152  N  N   . SER G  1 68  ? 31.718 -41.994  -52.912  1.00 79.37  ? 69  SER G N   1 
ATOM   7153  C  CA  . SER G  1 68  ? 31.683 -40.975  -51.854  1.00 80.56  ? 69  SER G CA  1 
ATOM   7154  C  C   . SER G  1 68  ? 31.486 -39.575  -52.415  1.00 82.64  ? 69  SER G C   1 
ATOM   7155  O  O   . SER G  1 68  ? 32.175 -38.639  -52.029  1.00 85.94  ? 69  SER G O   1 
ATOM   7156  C  CB  . SER G  1 68  ? 32.973 -41.025  -51.009  1.00 83.74  ? 69  SER G CB  1 
ATOM   7157  O  OG  . SER G  1 68  ? 33.327 -42.355  -50.649  1.00 82.72  ? 69  SER G OG  1 
ATOM   7158  N  N   . ARG G  1 69  ? 30.539 -39.442  -53.328  1.00 81.10  ? 70  ARG G N   1 
ATOM   7159  C  CA  . ARG G  1 69  ? 30.248 -38.150  -53.945  1.00 83.63  ? 70  ARG G CA  1 
ATOM   7160  C  C   . ARG G  1 69  ? 28.959 -37.515  -53.408  1.00 81.84  ? 70  ARG G C   1 
ATOM   7161  O  O   . ARG G  1 69  ? 28.271 -38.068  -52.550  1.00 78.97  ? 70  ARG G O   1 
ATOM   7162  C  CB  . ARG G  1 69  ? 30.140 -38.302  -55.471  1.00 84.31  ? 70  ARG G CB  1 
ATOM   7163  C  CG  . ARG G  1 69  ? 31.441 -38.177  -56.259  1.00 90.06  ? 70  ARG G CG  1 
ATOM   7164  C  CD  . ARG G  1 69  ? 31.259 -38.786  -57.651  1.00 91.82  ? 70  ARG G CD  1 
ATOM   7165  N  NE  . ARG G  1 69  ? 32.494 -38.825  -58.442  1.00 97.82  ? 70  ARG G NE  1 
ATOM   7166  C  CZ  . ARG G  1 69  ? 32.710 -39.616  -59.502  1.00 99.06  ? 70  ARG G CZ  1 
ATOM   7167  N  NH1 . ARG G  1 69  ? 31.789 -40.482  -59.927  1.00 96.00  ? 70  ARG G NH1 1 
ATOM   7168  N  NH2 . ARG G  1 69  ? 33.867 -39.543  -60.149  1.00 103.39 ? 70  ARG G NH2 1 
ATOM   7169  N  N   . LYS G  1 70  ? 28.654 -36.332  -53.936  1.00 84.10  ? 71  LYS G N   1 
ATOM   7170  C  CA  . LYS G  1 70  ? 27.411 -35.603  -53.623  1.00 83.30  ? 71  LYS G CA  1 
ATOM   7171  C  C   . LYS G  1 70  ? 26.274 -36.002  -54.560  1.00 81.10  ? 71  LYS G C   1 
ATOM   7172  O  O   . LYS G  1 70  ? 26.522 -36.461  -55.679  1.00 81.28  ? 71  LYS G O   1 
ATOM   7173  C  CB  . LYS G  1 70  ? 27.637 -34.090  -53.779  1.00 87.44  ? 71  LYS G CB  1 
ATOM   7174  C  CG  . LYS G  1 70  ? 28.795 -33.502  -52.941  1.00 90.82  ? 71  LYS G CG  1 
ATOM   7175  C  CD  . LYS G  1 70  ? 28.287 -32.959  -51.612  1.00 90.91  ? 71  LYS G CD  1 
ATOM   7176  C  CE  . LYS G  1 70  ? 29.367 -32.287  -50.802  1.00 94.78  ? 71  LYS G CE  1 
ATOM   7177  N  NZ  . LYS G  1 70  ? 28.776 -31.779  -49.519  1.00 94.66  ? 71  LYS G NZ  1 
ATOM   7178  N  N   . HIS G  1 71  ? 25.036 -35.780  -54.119  1.00 79.55  ? 72  HIS G N   1 
ATOM   7179  C  CA  . HIS G  1 71  ? 23.856 -36.106  -54.938  1.00 78.20  ? 72  HIS G CA  1 
ATOM   7180  C  C   . HIS G  1 71  ? 23.831 -35.278  -56.209  1.00 81.11  ? 72  HIS G C   1 
ATOM   7181  O  O   . HIS G  1 71  ? 24.399 -34.185  -56.261  1.00 84.23  ? 72  HIS G O   1 
ATOM   7182  C  CB  . HIS G  1 71  ? 22.541 -35.893  -54.192  1.00 76.93  ? 72  HIS G CB  1 
ATOM   7183  C  CG  . HIS G  1 71  ? 21.332 -36.278  -54.988  1.00 76.13  ? 72  HIS G CG  1 
ATOM   7184  N  ND1 . HIS G  1 71  ? 21.026 -37.586  -55.293  1.00 73.72  ? 72  HIS G ND1 1 
ATOM   7185  C  CD2 . HIS G  1 71  ? 20.358 -35.527  -55.558  1.00 77.87  ? 72  HIS G CD2 1 
ATOM   7186  C  CE1 . HIS G  1 71  ? 19.910 -37.628  -56.003  1.00 73.92  ? 72  HIS G CE1 1 
ATOM   7187  N  NE2 . HIS G  1 71  ? 19.483 -36.391  -56.178  1.00 76.19  ? 72  HIS G NE2 1 
ATOM   7188  N  N   . GLY G  1 72  ? 23.200 -35.824  -57.242  1.00 80.41  ? 73  GLY G N   1 
ATOM   7189  C  CA  . GLY G  1 72  ? 23.061 -35.118  -58.508  1.00 83.39  ? 73  GLY G CA  1 
ATOM   7190  C  C   . GLY G  1 72  ? 22.113 -35.790  -59.486  1.00 82.69  ? 73  GLY G C   1 
ATOM   7191  O  O   . GLY G  1 72  ? 21.478 -36.805  -59.173  1.00 79.90  ? 73  GLY G O   1 
ATOM   7192  N  N   . GLY G  1 73  ? 22.000 -35.185  -60.667  1.00 85.77  ? 74  GLY G N   1 
ATOM   7193  C  CA  . GLY G  1 73  ? 21.210 -35.735  -61.768  1.00 86.14  ? 74  GLY G CA  1 
ATOM   7194  C  C   . GLY G  1 73  ? 22.042 -36.759  -62.519  1.00 85.86  ? 74  GLY G C   1 
ATOM   7195  O  O   . GLY G  1 73  ? 23.277 -36.739  -62.444  1.00 86.64  ? 74  GLY G O   1 
ATOM   7196  N  N   . PRO G  1 74  ? 21.382 -37.672  -63.251  1.00 85.33  ? 75  PRO G N   1 
ATOM   7197  C  CA  . PRO G  1 74  ? 22.122 -38.778  -63.868  1.00 84.85  ? 75  PRO G CA  1 
ATOM   7198  C  C   . PRO G  1 74  ? 23.151 -38.306  -64.870  1.00 88.43  ? 75  PRO G C   1 
ATOM   7199  O  O   . PRO G  1 74  ? 24.239 -38.879  -64.953  1.00 88.52  ? 75  PRO G O   1 
ATOM   7200  C  CB  . PRO G  1 74  ? 21.029 -39.599  -64.555  1.00 84.49  ? 75  PRO G CB  1 
ATOM   7201  C  CG  . PRO G  1 74  ? 19.891 -38.696  -64.684  1.00 86.28  ? 75  PRO G CG  1 
ATOM   7202  C  CD  . PRO G  1 74  ? 19.945 -37.736  -63.551  1.00 85.52  ? 75  PRO G CD  1 
ATOM   7203  N  N   . LYS G  1 75  ? 22.815 -37.251  -65.598  1.00 91.96  ? 76  LYS G N   1 
ATOM   7204  C  CA  . LYS G  1 75  ? 23.747 -36.666  -66.567  1.00 96.25  ? 76  LYS G CA  1 
ATOM   7205  C  C   . LYS G  1 75  ? 24.919 -35.966  -65.891  1.00 97.09  ? 76  LYS G C   1 
ATOM   7206  O  O   . LYS G  1 75  ? 26.009 -35.866  -66.474  1.00 99.97  ? 76  LYS G O   1 
ATOM   7207  C  CB  . LYS G  1 75  ? 23.060 -35.650  -67.468  1.00 100.20 ? 76  LYS G CB  1 
ATOM   7208  C  CG  . LYS G  1 75  ? 21.762 -36.116  -68.078  1.00 100.63 ? 76  LYS G CG  1 
ATOM   7209  C  CD  . LYS G  1 75  ? 21.477 -35.311  -69.336  1.00 106.05 ? 76  LYS G CD  1 
ATOM   7210  C  CE  . LYS G  1 75  ? 20.042 -35.506  -69.835  1.00 107.02 ? 76  LYS G CE  1 
ATOM   7211  N  NZ  . LYS G  1 75  ? 19.629 -34.451  -70.825  1.00 112.23 ? 76  LYS G NZ  1 
ATOM   7212  N  N   . ASP G  1 76  ? 24.689 -35.455  -64.683  1.00 95.20  ? 77  ASP G N   1 
ATOM   7213  C  CA  . ASP G  1 76  ? 25.766 -34.812  -63.918  1.00 96.28  ? 77  ASP G CA  1 
ATOM   7214  C  C   . ASP G  1 76  ? 26.919 -35.793  -63.679  1.00 95.24  ? 77  ASP G C   1 
ATOM   7215  O  O   . ASP G  1 76  ? 26.693 -37.007  -63.435  1.00 91.78  ? 77  ASP G O   1 
ATOM   7216  C  CB  . ASP G  1 76  ? 25.249 -34.256  -62.579  1.00 94.24  ? 77  ASP G CB  1 
ATOM   7217  C  CG  . ASP G  1 76  ? 24.340 -33.049  -62.761  1.00 96.72  ? 77  ASP G CG  1 
ATOM   7218  O  OD1 . ASP G  1 76  ? 24.503 -32.333  -63.787  1.00 101.04 ? 77  ASP G OD1 1 
ATOM   7219  O  OD2 . ASP G  1 76  ? 23.463 -32.817  -61.885  1.00 95.08  ? 77  ASP G OD2 1 
ATOM   7220  N  N   . GLU G  1 77  ? 28.146 -35.274  -63.781  1.00 98.56  ? 78  GLU G N   1 
ATOM   7221  C  CA  . GLU G  1 77  ? 29.316 -36.074  -63.427  1.00 98.29  ? 78  GLU G CA  1 
ATOM   7222  C  C   . GLU G  1 77  ? 29.354 -36.269  -61.903  1.00 95.02  ? 78  GLU G C   1 
ATOM   7223  O  O   . GLU G  1 77  ? 29.483 -37.398  -61.412  1.00 92.11  ? 78  GLU G O   1 
ATOM   7224  C  CB  . GLU G  1 77  ? 30.625 -35.441  -63.891  1.00 103.43 ? 78  GLU G CB  1 
ATOM   7225  C  CG  . GLU G  1 77  ? 31.849 -36.020  -63.128  1.00 103.90 ? 78  GLU G CG  1 
ATOM   7226  C  CD  . GLU G  1 77  ? 33.179 -35.695  -63.765  1.00 110.07 ? 78  GLU G CD  1 
ATOM   7227  O  OE1 . GLU G  1 77  ? 33.313 -34.585  -64.350  1.00 114.29 ? 78  GLU G OE1 1 
ATOM   7228  O  OE2 . GLU G  1 77  ? 34.095 -36.556  -63.669  1.00 110.79 ? 78  GLU G OE2 1 
ATOM   7229  N  N   . GLU G  1 78  ? 29.266 -35.161  -61.170  1.00 95.91  ? 79  GLU G N   1 
ATOM   7230  C  CA  . GLU G  1 78  ? 29.165 -35.218  -59.713  1.00 93.32  ? 79  GLU G CA  1 
ATOM   7231  C  C   . GLU G  1 78  ? 27.762 -35.743  -59.328  1.00 89.11  ? 79  GLU G C   1 
ATOM   7232  O  O   . GLU G  1 78  ? 26.805 -34.957  -59.138  1.00 89.13  ? 79  GLU G O   1 
ATOM   7233  C  CB  . GLU G  1 78  ? 29.450 -33.848  -59.063  1.00 96.21  ? 79  GLU G CB  1 
ATOM   7234  C  CG  . GLU G  1 78  ? 29.496 -33.862  -57.510  1.00 94.37  ? 79  GLU G CG  1 
ATOM   7235  C  CD  . GLU G  1 78  ? 30.783 -34.490  -56.930  1.00 95.43  ? 79  GLU G CD  1 
ATOM   7236  O  OE1 . GLU G  1 78  ? 31.675 -34.928  -57.713  1.00 97.60  ? 79  GLU G OE1 1 
ATOM   7237  O  OE2 . GLU G  1 78  ? 30.899 -34.556  -55.674  1.00 94.21  ? 79  GLU G OE2 1 
ATOM   7238  N  N   . ARG G  1 79  ? 27.661 -37.073  -59.226  1.00 85.85  ? 80  ARG G N   1 
ATOM   7239  C  CA  . ARG G  1 79  ? 26.423 -37.753  -58.824  1.00 81.95  ? 80  ARG G CA  1 
ATOM   7240  C  C   . ARG G  1 79  ? 26.730 -38.961  -57.961  1.00 78.99  ? 80  ARG G C   1 
ATOM   7241  O  O   . ARG G  1 79  ? 27.879 -39.418  -57.903  1.00 79.84  ? 80  ARG G O   1 
ATOM   7242  C  CB  . ARG G  1 79  ? 25.655 -38.219  -60.061  1.00 81.85  ? 80  ARG G CB  1 
ATOM   7243  C  CG  . ARG G  1 79  ? 26.471 -39.118  -60.997  1.00 82.61  ? 80  ARG G CG  1 
ATOM   7244  C  CD  . ARG G  1 79  ? 25.610 -39.731  -62.091  1.00 82.49  ? 80  ARG G CD  1 
ATOM   7245  N  NE  . ARG G  1 79  ? 24.940 -40.966  -61.655  1.00 79.02  ? 80  ARG G NE  1 
ATOM   7246  C  CZ  . ARG G  1 79  ? 24.316 -41.824  -62.470  1.00 78.62  ? 80  ARG G CZ  1 
ATOM   7247  N  NH1 . ARG G  1 79  ? 24.259 -41.600  -63.781  1.00 81.36  ? 80  ARG G NH1 1 
ATOM   7248  N  NH2 . ARG G  1 79  ? 23.740 -42.919  -61.974  1.00 75.95  ? 80  ARG G NH2 1 
ATOM   7249  N  N   . HIS G  1 80  ? 25.696 -39.482  -57.302  1.00 75.95  ? 81  HIS G N   1 
ATOM   7250  C  CA  . HIS G  1 80  ? 25.783 -40.807  -56.685  1.00 73.07  ? 81  HIS G CA  1 
ATOM   7251  C  C   . HIS G  1 80  ? 25.658 -41.855  -57.792  1.00 72.58  ? 81  HIS G C   1 
ATOM   7252  O  O   . HIS G  1 80  ? 24.931 -41.644  -58.786  1.00 73.35  ? 81  HIS G O   1 
ATOM   7253  C  CB  . HIS G  1 80  ? 24.668 -41.046  -55.668  1.00 70.40  ? 81  HIS G CB  1 
ATOM   7254  C  CG  . HIS G  1 80  ? 24.673 -40.094  -54.516  1.00 70.89  ? 81  HIS G CG  1 
ATOM   7255  N  ND1 . HIS G  1 80  ? 23.518 -39.711  -53.867  1.00 69.81  ? 81  HIS G ND1 1 
ATOM   7256  C  CD2 . HIS G  1 80  ? 25.690 -39.460  -53.885  1.00 72.64  ? 81  HIS G CD2 1 
ATOM   7257  C  CE1 . HIS G  1 80  ? 23.825 -38.884  -52.885  1.00 71.06  ? 81  HIS G CE1 1 
ATOM   7258  N  NE2 . HIS G  1 80  ? 25.136 -38.710  -52.878  1.00 72.75  ? 81  HIS G NE2 1 
ATOM   7259  N  N   . VAL G  1 81  ? 26.346 -42.984  -57.615  1.00 71.55  ? 82  VAL G N   1 
ATOM   7260  C  CA  . VAL G  1 81  ? 26.247 -44.090  -58.578  1.00 71.07  ? 82  VAL G CA  1 
ATOM   7261  C  C   . VAL G  1 81  ? 24.792 -44.508  -58.787  1.00 69.04  ? 82  VAL G C   1 
ATOM   7262  O  O   . VAL G  1 81  ? 24.380 -44.790  -59.892  1.00 69.86  ? 82  VAL G O   1 
ATOM   7263  C  CB  . VAL G  1 81  ? 27.071 -45.310  -58.141  1.00 70.14  ? 82  VAL G CB  1 
ATOM   7264  C  CG1 . VAL G  1 81  ? 26.801 -46.468  -59.077  1.00 69.69  ? 82  VAL G CG1 1 
ATOM   7265  C  CG2 . VAL G  1 81  ? 28.569 -44.978  -58.113  1.00 72.90  ? 82  VAL G CG2 1 
ATOM   7266  N  N   . GLY G  1 82  ? 24.018 -44.505  -57.712  1.00 67.03  ? 83  GLY G N   1 
ATOM   7267  C  CA  . GLY G  1 82  ? 22.615 -44.909  -57.750  1.00 65.71  ? 83  GLY G CA  1 
ATOM   7268  C  C   . GLY G  1 82  ? 21.610 -43.846  -58.155  1.00 67.08  ? 83  GLY G C   1 
ATOM   7269  O  O   . GLY G  1 82  ? 20.411 -44.112  -58.150  1.00 66.38  ? 83  GLY G O   1 
ATOM   7270  N  N   . ASP G  1 83  ? 22.086 -42.642  -58.487  1.00 69.35  ? 84  ASP G N   1 
ATOM   7271  C  CA  . ASP G  1 83  ? 21.200 -41.525  -58.847  1.00 71.00  ? 84  ASP G CA  1 
ATOM   7272  C  C   . ASP G  1 83  ? 20.727 -41.683  -60.276  1.00 72.90  ? 84  ASP G C   1 
ATOM   7273  O  O   . ASP G  1 83  ? 21.410 -41.242  -61.193  1.00 75.37  ? 84  ASP G O   1 
ATOM   7274  C  CB  . ASP G  1 83  ? 21.910 -40.170  -58.706  1.00 73.02  ? 84  ASP G CB  1 
ATOM   7275  C  CG  . ASP G  1 83  ? 22.052 -39.728  -57.280  1.00 71.76  ? 84  ASP G CG  1 
ATOM   7276  O  OD1 . ASP G  1 83  ? 21.344 -40.257  -56.405  1.00 69.26  ? 84  ASP G OD1 1 
ATOM   7277  O  OD2 . ASP G  1 83  ? 22.871 -38.824  -57.029  1.00 73.69  ? 84  ASP G OD2 1 
ATOM   7278  N  N   . LEU G  1 84  ? 19.561 -42.303  -60.459  1.00 72.33  ? 85  LEU G N   1 
ATOM   7279  C  CA  . LEU G  1 84  ? 18.962 -42.462  -61.797  1.00 74.58  ? 85  LEU G CA  1 
ATOM   7280  C  C   . LEU G  1 84  ? 17.956 -41.364  -62.157  1.00 77.10  ? 85  LEU G C   1 
ATOM   7281  O  O   . LEU G  1 84  ? 17.266 -41.453  -63.178  1.00 79.34  ? 85  LEU G O   1 
ATOM   7282  C  CB  . LEU G  1 84  ? 18.293 -43.827  -61.924  1.00 73.33  ? 85  LEU G CB  1 
ATOM   7283  C  CG  . LEU G  1 84  ? 19.289 -44.967  -62.100  1.00 72.02  ? 85  LEU G CG  1 
ATOM   7284  C  CD1 . LEU G  1 84  ? 18.531 -46.291  -62.166  1.00 71.08  ? 85  LEU G CD1 1 
ATOM   7285  C  CD2 . LEU G  1 84  ? 20.149 -44.746  -63.335  1.00 74.37  ? 85  LEU G CD2 1 
ATOM   7286  N  N   . GLY G  1 85  ? 17.879 -40.334  -61.321  1.00 77.16  ? 86  GLY G N   1 
ATOM   7287  C  CA  . GLY G  1 85  ? 17.076 -39.151  -61.622  1.00 79.96  ? 86  GLY G CA  1 
ATOM   7288  C  C   . GLY G  1 85  ? 15.581 -39.374  -61.408  1.00 80.23  ? 86  GLY G C   1 
ATOM   7289  O  O   . GLY G  1 85  ? 15.164 -39.923  -60.377  1.00 78.01  ? 86  GLY G O   1 
ATOM   7290  N  N   . ASN G  1 86  ? 14.780 -38.954  -62.391  1.00 83.41  ? 87  ASN G N   1 
ATOM   7291  C  CA  . ASN G  1 86  ? 13.319 -38.955  -62.273  1.00 84.67  ? 87  ASN G CA  1 
ATOM   7292  C  C   . ASN G  1 86  ? 12.621 -39.900  -63.224  1.00 86.08  ? 87  ASN G C   1 
ATOM   7293  O  O   . ASN G  1 86  ? 13.155 -40.262  -64.272  1.00 87.11  ? 87  ASN G O   1 
ATOM   7294  C  CB  . ASN G  1 86  ? 12.755 -37.555  -62.511  1.00 88.15  ? 87  ASN G CB  1 
ATOM   7295  C  CG  . ASN G  1 86  ? 12.956 -36.641  -61.334  1.00 87.38  ? 87  ASN G CG  1 
ATOM   7296  O  OD1 . ASN G  1 86  ? 12.556 -36.954  -60.213  1.00 85.60  ? 87  ASN G OD1 1 
ATOM   7297  N  ND2 . ASN G  1 86  ? 13.576 -35.494  -61.580  1.00 89.48  ? 87  ASN G ND2 1 
ATOM   7298  N  N   . VAL G  1 87  ? 11.413 -40.287  -62.830  1.00 86.65  ? 88  VAL G N   1 
ATOM   7299  C  CA  . VAL G  1 87  ? 10.482 -40.992  -63.709  1.00 89.39  ? 88  VAL G CA  1 
ATOM   7300  C  C   . VAL G  1 87  ? 9.182  -40.200  -63.760  1.00 93.31  ? 88  VAL G C   1 
ATOM   7301  O  O   . VAL G  1 87  ? 8.744  -39.656  -62.738  1.00 92.74  ? 88  VAL G O   1 
ATOM   7302  C  CB  . VAL G  1 87  ? 10.165 -42.429  -63.226  1.00 87.08  ? 88  VAL G CB  1 
ATOM   7303  C  CG1 . VAL G  1 87  ? 11.400 -43.308  -63.348  1.00 84.06  ? 88  VAL G CG1 1 
ATOM   7304  C  CG2 . VAL G  1 87  ? 9.625  -42.408  -61.808  1.00 85.30  ? 88  VAL G CG2 1 
ATOM   7305  N  N   . THR G  1 88  ? 8.552  -40.177  -64.939  1.00 97.61  ? 89  THR G N   1 
ATOM   7306  C  CA  . THR G  1 88  ? 7.329  -39.384  -65.161  1.00 102.20 ? 89  THR G CA  1 
ATOM   7307  C  C   . THR G  1 88  ? 6.028  -40.214  -65.198  1.00 104.56 ? 89  THR G C   1 
ATOM   7308  O  O   . THR G  1 88  ? 5.890  -41.178  -65.963  1.00 105.58 ? 89  THR G O   1 
ATOM   7309  C  CB  . THR G  1 88  ? 7.442  -38.549  -66.438  1.00 106.39 ? 89  THR G CB  1 
ATOM   7310  O  OG1 . THR G  1 88  ? 8.480  -37.578  -66.261  1.00 105.12 ? 89  THR G OG1 1 
ATOM   7311  C  CG2 . THR G  1 88  ? 6.114  -37.843  -66.739  1.00 111.83 ? 89  THR G CG2 1 
ATOM   7312  N  N   . ALA G  1 89  ? 5.082  -39.801  -64.361  1.00 105.84 ? 90  ALA G N   1 
ATOM   7313  C  CA  . ALA G  1 89  ? 3.783  -40.473  -64.224  1.00 108.82 ? 90  ALA G CA  1 
ATOM   7314  C  C   . ALA G  1 89  ? 2.668  -39.698  -64.951  1.00 115.38 ? 90  ALA G C   1 
ATOM   7315  O  O   . ALA G  1 89  ? 2.504  -38.474  -64.769  1.00 117.30 ? 90  ALA G O   1 
ATOM   7316  C  CB  . ALA G  1 89  ? 3.419  -40.655  -62.736  1.00 106.40 ? 90  ALA G CB  1 
ATOM   7317  N  N   . ASP G  1 90  ? 1.901  -40.418  -65.769  1.00 119.26 ? 91  ASP G N   1 
ATOM   7318  C  CA  . ASP G  1 90  ? 0.788  -39.813  -66.530  1.00 126.18 ? 91  ASP G CA  1 
ATOM   7319  C  C   . ASP G  1 90  ? -0.544 -39.874  -65.757  1.00 129.37 ? 91  ASP G C   1 
ATOM   7320  O  O   . ASP G  1 90  ? -0.675 -40.643  -64.786  1.00 126.45 ? 91  ASP G O   1 
ATOM   7321  C  CB  . ASP G  1 90  ? 0.662  -40.441  -67.944  1.00 129.83 ? 91  ASP G CB  1 
ATOM   7322  C  CG  . ASP G  1 90  ? 0.097  -41.894  -67.939  1.00 130.52 ? 91  ASP G CG  1 
ATOM   7323  O  OD1 . ASP G  1 90  ? -0.027 -42.459  -69.059  1.00 133.97 ? 91  ASP G OD1 1 
ATOM   7324  O  OD2 . ASP G  1 90  ? -0.226 -42.467  -66.857  1.00 128.02 ? 91  ASP G OD2 1 
ATOM   7325  N  N   . LYS G  1 91  ? -1.490 -39.036  -66.204  1.00 135.61 ? 92  LYS G N   1 
ATOM   7326  C  CA  . LYS G  1 91  ? -2.869 -38.911  -65.630  1.00 140.43 ? 92  LYS G CA  1 
ATOM   7327  C  C   . LYS G  1 91  ? -3.335 -40.071  -64.753  1.00 138.87 ? 92  LYS G C   1 
ATOM   7328  O  O   . LYS G  1 91  ? -3.574 -39.891  -63.543  1.00 137.24 ? 92  LYS G O   1 
ATOM   7329  C  CB  . LYS G  1 91  ? -3.953 -38.748  -66.730  1.00 148.73 ? 92  LYS G CB  1 
ATOM   7330  C  CG  . LYS G  1 91  ? -3.505 -38.169  -68.085  1.00 151.58 ? 92  LYS G CG  1 
ATOM   7331  C  CD  . LYS G  1 91  ? -3.154 -36.673  -67.989  1.00 152.14 ? 92  LYS G CD  1 
ATOM   7332  C  CE  . LYS G  1 91  ? -3.233 -35.980  -69.363  1.00 157.64 ? 92  LYS G CE  1 
ATOM   7333  N  NZ  . LYS G  1 91  ? -4.596 -35.480  -69.730  1.00 166.17 ? 92  LYS G NZ  1 
ATOM   7334  N  N   . ASP G  1 92  ? -3.458 -41.252  -65.386  1.00 139.72 ? 93  ASP G N   1 
ATOM   7335  C  CA  . ASP G  1 92  ? -4.033 -42.469  -64.742  1.00 139.72 ? 93  ASP G CA  1 
ATOM   7336  C  C   . ASP G  1 92  ? -2.995 -43.221  -63.854  1.00 132.05 ? 93  ASP G C   1 
ATOM   7337  O  O   . ASP G  1 92  ? -3.164 -44.410  -63.523  1.00 131.32 ? 93  ASP G O   1 
ATOM   7338  C  CB  . ASP G  1 92  ? -4.718 -43.425  -65.764  1.00 144.86 ? 93  ASP G CB  1 
ATOM   7339  C  CG  . ASP G  1 92  ? -4.550 -42.971  -67.227  1.00 148.77 ? 93  ASP G CG  1 
ATOM   7340  O  OD1 . ASP G  1 92  ? -3.387 -42.932  -67.732  1.00 144.80 ? 93  ASP G OD1 1 
ATOM   7341  O  OD2 . ASP G  1 92  ? -5.588 -42.652  -67.861  1.00 155.97 ? 93  ASP G OD2 1 
ATOM   7342  N  N   . GLY G  1 93  ? -1.924 -42.511  -63.479  1.00 126.93 ? 94  GLY G N   1 
ATOM   7343  C  CA  . GLY G  1 93  ? -0.989 -42.969  -62.446  1.00 120.04 ? 94  GLY G CA  1 
ATOM   7344  C  C   . GLY G  1 93  ? 0.122  -43.875  -62.956  1.00 115.80 ? 94  GLY G C   1 
ATOM   7345  O  O   . GLY G  1 93  ? 0.888  -44.429  -62.159  1.00 110.46 ? 94  GLY G O   1 
ATOM   7346  N  N   . VAL G  1 94  ? 0.214  -44.014  -64.282  1.00 118.87 ? 95  VAL G N   1 
ATOM   7347  C  CA  . VAL G  1 94  ? 1.105  -44.999  -64.931  1.00 116.46 ? 95  VAL G CA  1 
ATOM   7348  C  C   . VAL G  1 94  ? 2.427  -44.379  -65.487  1.00 113.20 ? 95  VAL G C   1 
ATOM   7349  O  O   . VAL G  1 94  ? 2.419  -43.514  -66.383  1.00 116.31 ? 95  VAL G O   1 
ATOM   7350  C  CB  . VAL G  1 94  ? 0.320  -45.787  -66.062  1.00 122.30 ? 95  VAL G CB  1 
ATOM   7351  C  CG1 . VAL G  1 94  ? 1.265  -46.712  -66.899  1.00 119.80 ? 95  VAL G CG1 1 
ATOM   7352  C  CG2 . VAL G  1 94  ? -0.888 -46.571  -65.450  1.00 124.94 ? 95  VAL G CG2 1 
ATOM   7353  N  N   . ALA G  1 95  ? 3.559  -44.869  -64.985  1.00 107.04 ? 96  ALA G N   1 
ATOM   7354  C  CA  . ALA G  1 95  ? 4.865  -44.300  -65.342  1.00 104.00 ? 96  ALA G CA  1 
ATOM   7355  C  C   . ALA G  1 95  ? 5.605  -45.331  -66.200  1.00 103.05 ? 96  ALA G C   1 
ATOM   7356  O  O   . ALA G  1 95  ? 6.079  -46.364  -65.701  1.00 99.70  ? 96  ALA G O   1 
ATOM   7357  C  CB  . ALA G  1 95  ? 5.684  -43.921  -64.096  1.00 98.69  ? 96  ALA G CB  1 
ATOM   7358  N  N   . ASP G  1 96  ? 5.665  -45.068  -67.496  1.00 106.48 ? 97  ASP G N   1 
ATOM   7359  C  CA  . ASP G  1 96  ? 6.309  -45.991  -68.419  1.00 106.69 ? 97  ASP G CA  1 
ATOM   7360  C  C   . ASP G  1 96  ? 7.808  -45.735  -68.469  1.00 102.87 ? 97  ASP G C   1 
ATOM   7361  O  O   . ASP G  1 96  ? 8.297  -44.965  -69.290  1.00 104.95 ? 97  ASP G O   1 
ATOM   7362  C  CB  . ASP G  1 96  ? 5.666  -45.917  -69.811  1.00 112.96 ? 97  ASP G CB  1 
ATOM   7363  C  CG  . ASP G  1 96  ? 4.349  -46.727  -69.894  1.00 117.56 ? 97  ASP G CG  1 
ATOM   7364  O  OD1 . ASP G  1 96  ? 4.325  -47.909  -69.447  1.00 115.76 ? 97  ASP G OD1 1 
ATOM   7365  O  OD2 . ASP G  1 96  ? 3.334  -46.187  -70.412  1.00 123.27 ? 97  ASP G OD2 1 
ATOM   7366  N  N   . VAL G  1 97  ? 8.536  -46.416  -67.596  1.00 97.90  ? 98  VAL G N   1 
ATOM   7367  C  CA  . VAL G  1 97  ? 9.968  -46.188  -67.456  1.00 94.40  ? 98  VAL G CA  1 
ATOM   7368  C  C   . VAL G  1 97  ? 10.802 -46.662  -68.647  1.00 95.74  ? 98  VAL G C   1 
ATOM   7369  O  O   . VAL G  1 97  ? 10.689 -47.798  -69.097  1.00 96.64  ? 98  VAL G O   1 
ATOM   7370  C  CB  . VAL G  1 97  ? 10.530 -46.893  -66.214  1.00 89.48  ? 98  VAL G CB  1 
ATOM   7371  C  CG1 . VAL G  1 97  ? 12.027 -46.527  -66.039  1.00 86.48  ? 98  VAL G CG1 1 
ATOM   7372  C  CG2 . VAL G  1 97  ? 9.710  -46.537  -64.961  1.00 88.51  ? 98  VAL G CG2 1 
ATOM   7373  N  N   . SER G  1 98  ? 11.664 -45.783  -69.132  1.00 96.25  ? 99  SER G N   1 
ATOM   7374  C  CA  . SER G  1 98  ? 12.658 -46.160  -70.147  1.00 97.51  ? 99  SER G CA  1 
ATOM   7375  C  C   . SER G  1 98  ? 13.926 -45.302  -70.072  1.00 96.10  ? 99  SER G C   1 
ATOM   7376  O  O   . SER G  1 98  ? 14.057 -44.279  -70.742  1.00 99.04  ? 99  SER G O   1 
ATOM   7377  C  CB  . SER G  1 98  ? 12.086 -46.068  -71.556  1.00 103.24 ? 99  SER G CB  1 
ATOM   7378  O  OG  . SER G  1 98  ? 13.122 -46.311  -72.509  1.00 104.28 ? 99  SER G OG  1 
ATOM   7379  N  N   . ILE G  1 99  ? 14.853 -45.737  -69.240  1.00 92.01  ? 100 ILE G N   1 
ATOM   7380  C  CA  . ILE G  1 99  ? 16.101 -45.030  -69.014  1.00 90.62  ? 100 ILE G CA  1 
ATOM   7381  C  C   . ILE G  1 99  ? 17.216 -45.814  -69.656  1.00 90.93  ? 100 ILE G C   1 
ATOM   7382  O  O   . ILE G  1 99  ? 17.075 -46.986  -69.936  1.00 91.21  ? 100 ILE G O   1 
ATOM   7383  C  CB  . ILE G  1 99  ? 16.368 -44.845  -67.486  1.00 86.23  ? 100 ILE G CB  1 
ATOM   7384  C  CG1 . ILE G  1 99  ? 15.310 -43.901  -66.868  1.00 86.66  ? 100 ILE G CG1 1 
ATOM   7385  C  CG2 . ILE G  1 99  ? 17.767 -44.298  -67.233  1.00 85.15  ? 100 ILE G CG2 1 
ATOM   7386  C  CD1 . ILE G  1 99  ? 15.725 -43.254  -65.529  1.00 83.50  ? 100 ILE G CD1 1 
ATOM   7387  N  N   . GLU G  1 100 ? 18.315 -45.143  -69.935  1.00 91.79  ? 101 GLU G N   1 
ATOM   7388  C  CA  . GLU G  1 100 ? 19.560 -45.818  -70.290  1.00 91.86  ? 101 GLU G CA  1 
ATOM   7389  C  C   . GLU G  1 100 ? 20.713 -45.116  -69.564  1.00 90.23  ? 101 GLU G C   1 
ATOM   7390  O  O   . GLU G  1 100 ? 20.903 -43.904  -69.715  1.00 92.11  ? 101 GLU G O   1 
ATOM   7391  C  CB  . GLU G  1 100 ? 19.781 -45.789  -71.797  1.00 96.69  ? 101 GLU G CB  1 
ATOM   7392  C  CG  . GLU G  1 100 ? 21.018 -46.558  -72.253  1.00 97.95  ? 101 GLU G CG  1 
ATOM   7393  C  CD  . GLU G  1 100 ? 21.136 -46.725  -73.784  1.00 103.76 ? 101 GLU G CD  1 
ATOM   7394  O  OE1 . GLU G  1 100 ? 22.063 -47.445  -74.235  1.00 104.78 ? 101 GLU G OE1 1 
ATOM   7395  O  OE2 . GLU G  1 100 ? 20.310 -46.158  -74.544  1.00 107.21 ? 101 GLU G OE2 1 
ATOM   7396  N  N   . ASP G  1 101 ? 21.482 -45.871  -68.780  1.00 87.25  ? 102 ASP G N   1 
ATOM   7397  C  CA  . ASP G  1 101 ? 22.500 -45.272  -67.908  1.00 85.63  ? 102 ASP G CA  1 
ATOM   7398  C  C   . ASP G  1 101 ? 23.846 -45.971  -67.963  1.00 85.80  ? 102 ASP G C   1 
ATOM   7399  O  O   . ASP G  1 101 ? 23.919 -47.186  -68.118  1.00 85.13  ? 102 ASP G O   1 
ATOM   7400  C  CB  . ASP G  1 101 ? 22.025 -45.258  -66.465  1.00 81.64  ? 102 ASP G CB  1 
ATOM   7401  C  CG  . ASP G  1 101 ? 22.869 -44.342  -65.586  1.00 80.77  ? 102 ASP G CG  1 
ATOM   7402  O  OD1 . ASP G  1 101 ? 22.783 -43.113  -65.785  1.00 82.55  ? 102 ASP G OD1 1 
ATOM   7403  O  OD2 . ASP G  1 101 ? 23.627 -44.841  -64.715  1.00 78.48  ? 102 ASP G OD2 1 
ATOM   7404  N  N   . SER G  1 102 ? 24.901 -45.177  -67.791  1.00 87.05  ? 103 SER G N   1 
ATOM   7405  C  CA  . SER G  1 102 ? 26.284 -45.630  -67.958  1.00 88.47  ? 103 SER G CA  1 
ATOM   7406  C  C   . SER G  1 102 ? 27.107 -45.678  -66.675  1.00 86.04  ? 103 SER G C   1 
ATOM   7407  O  O   . SER G  1 102 ? 28.206 -46.243  -66.684  1.00 87.11  ? 103 SER G O   1 
ATOM   7408  C  CB  . SER G  1 102 ? 27.000 -44.725  -68.944  1.00 93.06  ? 103 SER G CB  1 
ATOM   7409  O  OG  . SER G  1 102 ? 26.263 -44.646  -70.155  1.00 95.93  ? 103 SER G OG  1 
ATOM   7410  N  N   . VAL G  1 103 ? 26.595 -45.091  -65.590  1.00 83.34  ? 104 VAL G N   1 
ATOM   7411  C  CA  . VAL G  1 103 ? 27.283 -45.142  -64.281  1.00 81.28  ? 104 VAL G CA  1 
ATOM   7412  C  C   . VAL G  1 103 ? 26.977 -46.439  -63.521  1.00 77.93  ? 104 VAL G C   1 
ATOM   7413  O  O   . VAL G  1 103 ? 27.893 -47.105  -62.993  1.00 77.58  ? 104 VAL G O   1 
ATOM   7414  C  CB  . VAL G  1 103 ? 26.919 -43.950  -63.373  1.00 80.20  ? 104 VAL G CB  1 
ATOM   7415  C  CG1 . VAL G  1 103 ? 27.683 -44.033  -62.060  1.00 78.49  ? 104 VAL G CG1 1 
ATOM   7416  C  CG2 . VAL G  1 103 ? 27.241 -42.638  -64.061  1.00 84.14  ? 104 VAL G CG2 1 
ATOM   7417  N  N   . ILE G  1 104 ? 25.696 -46.796  -63.457  1.00 75.84  ? 105 ILE G N   1 
ATOM   7418  C  CA  . ILE G  1 104 ? 25.320 -48.059  -62.818  1.00 73.05  ? 105 ILE G CA  1 
ATOM   7419  C  C   . ILE G  1 104 ? 25.849 -49.237  -63.625  1.00 74.43  ? 105 ILE G C   1 
ATOM   7420  O  O   . ILE G  1 104 ? 26.184 -49.109  -64.813  1.00 77.33  ? 105 ILE G O   1 
ATOM   7421  C  CB  . ILE G  1 104 ? 23.787 -48.240  -62.623  1.00 71.22  ? 105 ILE G CB  1 
ATOM   7422  C  CG1 . ILE G  1 104 ? 23.051 -48.326  -63.952  1.00 73.47  ? 105 ILE G CG1 1 
ATOM   7423  C  CG2 . ILE G  1 104 ? 23.226 -47.119  -61.788  1.00 70.14  ? 105 ILE G CG2 1 
ATOM   7424  C  CD1 . ILE G  1 104 ? 21.687 -48.945  -63.815  1.00 71.87  ? 105 ILE G CD1 1 
ATOM   7425  N  N   . SER G  1 105 ? 25.919 -50.388  -62.968  1.00 72.66  ? 106 SER G N   1 
ATOM   7426  C  CA  . SER G  1 105 ? 26.315 -51.630  -63.643  1.00 73.92  ? 106 SER G CA  1 
ATOM   7427  C  C   . SER G  1 105 ? 25.749 -52.862  -62.956  1.00 71.51  ? 106 SER G C   1 
ATOM   7428  O  O   . SER G  1 105 ? 25.432 -52.850  -61.761  1.00 68.86  ? 106 SER G O   1 
ATOM   7429  C  CB  . SER G  1 105 ? 27.847 -51.745  -63.732  1.00 76.02  ? 106 SER G CB  1 
ATOM   7430  O  OG  . SER G  1 105 ? 28.231 -52.818  -64.573  1.00 77.78  ? 106 SER G OG  1 
ATOM   7431  N  N   . LEU G  1 106 ? 25.646 -53.926  -63.740  1.00 72.84  ? 107 LEU G N   1 
ATOM   7432  C  CA  . LEU G  1 106 ? 25.251 -55.249  -63.242  1.00 71.44  ? 107 LEU G CA  1 
ATOM   7433  C  C   . LEU G  1 106 ? 26.464 -56.156  -62.925  1.00 71.96  ? 107 LEU G C   1 
ATOM   7434  O  O   . LEU G  1 106 ? 26.331 -57.365  -62.790  1.00 71.67  ? 107 LEU G O   1 
ATOM   7435  C  CB  . LEU G  1 106 ? 24.335 -55.925  -64.264  1.00 73.01  ? 107 LEU G CB  1 
ATOM   7436  C  CG  . LEU G  1 106 ? 23.064 -55.158  -64.623  1.00 72.74  ? 107 LEU G CG  1 
ATOM   7437  C  CD1 . LEU G  1 106 ? 22.253 -55.977  -65.602  1.00 75.09  ? 107 LEU G CD1 1 
ATOM   7438  C  CD2 . LEU G  1 106 ? 22.256 -54.844  -63.397  1.00 69.52  ? 107 LEU G CD2 1 
ATOM   7439  N  N   . SER G  1 107 ? 27.637 -55.547  -62.797  1.00 73.12  ? 108 SER G N   1 
ATOM   7440  C  CA  . SER G  1 107 ? 28.862 -56.267  -62.485  1.00 74.20  ? 108 SER G CA  1 
ATOM   7441  C  C   . SER G  1 107 ? 29.963 -55.332  -61.975  1.00 75.03  ? 108 SER G C   1 
ATOM   7442  O  O   . SER G  1 107 ? 30.132 -54.218  -62.484  1.00 76.30  ? 108 SER G O   1 
ATOM   7443  C  CB  . SER G  1 107 ? 29.358 -57.024  -63.715  1.00 77.55  ? 108 SER G CB  1 
ATOM   7444  O  OG  . SER G  1 107 ? 29.520 -56.160  -64.819  1.00 79.93  ? 108 SER G OG  1 
ATOM   7445  N  N   . GLY G  1 108 ? 30.689 -55.804  -60.957  1.00 74.69  ? 109 GLY G N   1 
ATOM   7446  C  CA  . GLY G  1 108 ? 31.897 -55.129  -60.427  1.00 76.43  ? 109 GLY G CA  1 
ATOM   7447  C  C   . GLY G  1 108 ? 31.726 -54.197  -59.224  1.00 74.45  ? 109 GLY G C   1 
ATOM   7448  O  O   . GLY G  1 108 ? 30.843 -54.369  -58.375  1.00 71.35  ? 109 GLY G O   1 
ATOM   7449  N  N   . ASP G  1 109 ? 32.592 -53.188  -59.169  1.00 76.80  ? 110 ASP G N   1 
ATOM   7450  C  CA  . ASP G  1 109 ? 32.538 -52.115  -58.126  1.00 75.81  ? 110 ASP G CA  1 
ATOM   7451  C  C   . ASP G  1 109 ? 31.145 -51.408  -57.995  1.00 72.57  ? 110 ASP G C   1 
ATOM   7452  O  O   . ASP G  1 109 ? 30.614 -51.173  -56.910  1.00 69.83  ? 110 ASP G O   1 
ATOM   7453  C  CB  . ASP G  1 109 ? 33.607 -51.034  -58.458  1.00 79.61  ? 110 ASP G CB  1 
ATOM   7454  C  CG  . ASP G  1 109 ? 34.135 -50.314  -57.213  1.00 80.31  ? 110 ASP G CG  1 
ATOM   7455  O  OD1 . ASP G  1 109 ? 33.561 -49.267  -56.806  1.00 78.87  ? 110 ASP G OD1 1 
ATOM   7456  O  OD2 . ASP G  1 109 ? 35.137 -50.817  -56.651  1.00 82.64  ? 110 ASP G OD2 1 
ATOM   7457  N  N   . HIS G  1 110 ? 30.594 -51.073  -59.155  1.00 73.17  ? 111 HIS G N   1 
ATOM   7458  C  CA  . HIS G  1 110 ? 29.330 -50.358  -59.294  1.00 71.41  ? 111 HIS G CA  1 
ATOM   7459  C  C   . HIS G  1 110 ? 28.121 -51.307  -59.284  1.00 68.92  ? 111 HIS G C   1 
ATOM   7460  O  O   . HIS G  1 110 ? 26.990 -50.876  -59.557  1.00 67.96  ? 111 HIS G O   1 
ATOM   7461  C  CB  . HIS G  1 110 ? 29.332 -49.565  -60.626  1.00 74.02  ? 111 HIS G CB  1 
ATOM   7462  C  CG  . HIS G  1 110 ? 30.305 -48.419  -60.661  1.00 77.09  ? 111 HIS G CG  1 
ATOM   7463  N  ND1 . HIS G  1 110 ? 30.280 -47.450  -61.648  1.00 79.60  ? 111 HIS G ND1 1 
ATOM   7464  C  CD2 . HIS G  1 110 ? 31.324 -48.077  -59.825  1.00 78.31  ? 111 HIS G CD2 1 
ATOM   7465  C  CE1 . HIS G  1 110 ? 31.246 -46.568  -61.423  1.00 82.06  ? 111 HIS G CE1 1 
ATOM   7466  N  NE2 . HIS G  1 110 ? 31.893 -46.923  -60.321  1.00 81.51  ? 111 HIS G NE2 1 
ATOM   7467  N  N   . CYS G  1 111 ? 28.354 -52.588  -58.989  1.00 68.21  ? 112 CYS G N   1 
ATOM   7468  C  CA  . CYS G  1 111 ? 27.316 -53.620  -59.105  1.00 66.54  ? 112 CYS G CA  1 
ATOM   7469  C  C   . CYS G  1 111 ? 26.111 -53.276  -58.264  1.00 63.90  ? 112 CYS G C   1 
ATOM   7470  O  O   . CYS G  1 111 ? 26.224 -53.198  -57.046  1.00 62.49  ? 112 CYS G O   1 
ATOM   7471  C  CB  . CYS G  1 111 ? 27.874 -54.978  -58.655  1.00 66.61  ? 112 CYS G CB  1 
ATOM   7472  S  SG  . CYS G  1 111 ? 26.790 -56.405  -58.783  1.00 65.70  ? 112 CYS G SG  1 
ATOM   7473  N  N   . ILE G  1 112 ? 24.971 -53.061  -58.918  1.00 63.71  ? 113 ILE G N   1 
ATOM   7474  C  CA  . ILE G  1 112 ? 23.709 -52.726  -58.219  1.00 62.01  ? 113 ILE G CA  1 
ATOM   7475  C  C   . ILE G  1 112 ? 22.882 -53.959  -57.820  1.00 60.82  ? 113 ILE G C   1 
ATOM   7476  O  O   . ILE G  1 112 ? 21.875 -53.861  -57.113  1.00 59.54  ? 113 ILE G O   1 
ATOM   7477  C  CB  . ILE G  1 112 ? 22.804 -51.773  -59.052  1.00 62.99  ? 113 ILE G CB  1 
ATOM   7478  C  CG1 . ILE G  1 112 ? 22.380 -52.413  -60.376  1.00 64.67  ? 113 ILE G CG1 1 
ATOM   7479  C  CG2 . ILE G  1 112 ? 23.512 -50.445  -59.302  1.00 64.27  ? 113 ILE G CG2 1 
ATOM   7480  C  CD1 . ILE G  1 112 ? 21.053 -51.853  -60.924  1.00 65.41  ? 113 ILE G CD1 1 
ATOM   7481  N  N   . ILE G  1 113 ? 23.308 -55.116  -58.298  1.00 61.65  ? 114 ILE G N   1 
ATOM   7482  C  CA  . ILE G  1 113 ? 22.611 -56.356  -58.002  1.00 61.10  ? 114 ILE G CA  1 
ATOM   7483  C  C   . ILE G  1 113 ? 22.706 -56.673  -56.518  1.00 59.20  ? 114 ILE G C   1 
ATOM   7484  O  O   . ILE G  1 113 ? 23.781 -56.621  -55.925  1.00 58.81  ? 114 ILE G O   1 
ATOM   7485  C  CB  . ILE G  1 113 ? 23.153 -57.546  -58.833  1.00 62.74  ? 114 ILE G CB  1 
ATOM   7486  C  CG1 . ILE G  1 113 ? 22.713 -57.389  -60.294  1.00 64.87  ? 114 ILE G CG1 1 
ATOM   7487  C  CG2 . ILE G  1 113 ? 22.649 -58.880  -58.269  1.00 62.13  ? 114 ILE G CG2 1 
ATOM   7488  C  CD1 . ILE G  1 113 ? 23.374 -58.349  -61.232  1.00 67.42  ? 114 ILE G CD1 1 
ATOM   7489  N  N   . GLY G  1 114 ? 21.560 -57.012  -55.942  1.00 58.34  ? 115 GLY G N   1 
ATOM   7490  C  CA  . GLY G  1 114 ? 21.475 -57.311  -54.527  1.00 57.07  ? 115 GLY G CA  1 
ATOM   7491  C  C   . GLY G  1 114 ? 21.181 -56.075  -53.717  1.00 56.05  ? 115 GLY G C   1 
ATOM   7492  O  O   . GLY G  1 114 ? 21.121 -56.137  -52.493  1.00 55.21  ? 115 GLY G O   1 
ATOM   7493  N  N   . ARG G  1 115 ? 20.992 -54.951  -54.398  1.00 56.51  ? 116 ARG G N   1 
ATOM   7494  C  CA  . ARG G  1 115 ? 20.654 -53.685  -53.732  1.00 56.14  ? 116 ARG G CA  1 
ATOM   7495  C  C   . ARG G  1 115 ? 19.205 -53.286  -54.053  1.00 56.64  ? 116 ARG G C   1 
ATOM   7496  O  O   . ARG G  1 115 ? 18.546 -53.931  -54.875  1.00 57.58  ? 116 ARG G O   1 
ATOM   7497  C  CB  . ARG G  1 115 ? 21.635 -52.579  -54.132  1.00 56.67  ? 116 ARG G CB  1 
ATOM   7498  C  CG  . ARG G  1 115 ? 23.067 -52.948  -53.876  1.00 56.95  ? 116 ARG G CG  1 
ATOM   7499  C  CD  . ARG G  1 115 ? 24.022 -51.829  -54.182  1.00 58.19  ? 116 ARG G CD  1 
ATOM   7500  N  NE  . ARG G  1 115 ? 25.417 -52.281  -54.125  1.00 59.05  ? 116 ARG G NE  1 
ATOM   7501  C  CZ  . ARG G  1 115 ? 26.154 -52.373  -53.016  1.00 59.05  ? 116 ARG G CZ  1 
ATOM   7502  N  NH1 . ARG G  1 115 ? 25.654 -52.037  -51.829  1.00 58.10  ? 116 ARG G NH1 1 
ATOM   7503  N  NH2 . ARG G  1 115 ? 27.406 -52.800  -53.090  1.00 60.67  ? 116 ARG G NH2 1 
ATOM   7504  N  N   . THR G  1 116 ? 18.717 -52.235  -53.396  1.00 56.37  ? 117 THR G N   1 
ATOM   7505  C  CA  . THR G  1 116 ? 17.308 -51.846  -53.490  1.00 57.18  ? 117 THR G CA  1 
ATOM   7506  C  C   . THR G  1 116 ? 17.041 -50.690  -54.449  1.00 58.54  ? 117 THR G C   1 
ATOM   7507  O  O   . THR G  1 116 ? 17.680 -49.655  -54.380  1.00 58.63  ? 117 THR G O   1 
ATOM   7508  C  CB  . THR G  1 116 ? 16.745 -51.425  -52.132  1.00 56.80  ? 117 THR G CB  1 
ATOM   7509  O  OG1 . THR G  1 116 ? 16.701 -52.541  -51.237  1.00 55.93  ? 117 THR G OG1 1 
ATOM   7510  C  CG2 . THR G  1 116 ? 15.345 -50.930  -52.292  1.00 58.28  ? 117 THR G CG2 1 
ATOM   7511  N  N   . LEU G  1 117 ? 16.073 -50.889  -55.340  1.00 60.17  ? 118 LEU G N   1 
ATOM   7512  C  CA  . LEU G  1 117 ? 15.540 -49.825  -56.201  1.00 61.83  ? 118 LEU G CA  1 
ATOM   7513  C  C   . LEU G  1 117 ? 14.393 -49.203  -55.450  1.00 62.43  ? 118 LEU G C   1 
ATOM   7514  O  O   . LEU G  1 117 ? 13.680 -49.907  -54.736  1.00 62.35  ? 118 LEU G O   1 
ATOM   7515  C  CB  . LEU G  1 117 ? 15.022 -50.387  -57.535  1.00 63.75  ? 118 LEU G CB  1 
ATOM   7516  C  CG  . LEU G  1 117 ? 14.545 -49.367  -58.565  1.00 65.88  ? 118 LEU G CG  1 
ATOM   7517  C  CD1 . LEU G  1 117 ? 15.686 -48.433  -58.915  1.00 65.81  ? 118 LEU G CD1 1 
ATOM   7518  C  CD2 . LEU G  1 117 ? 14.005 -50.054  -59.813  1.00 68.11  ? 118 LEU G CD2 1 
ATOM   7519  N  N   . VAL G  1 118 ? 14.205 -47.896  -55.639  1.00 63.59  ? 119 VAL G N   1 
ATOM   7520  C  CA  . VAL G  1 118 ? 13.232 -47.108  -54.859  1.00 64.48  ? 119 VAL G CA  1 
ATOM   7521  C  C   . VAL G  1 118 ? 12.604 -45.962  -55.652  1.00 66.98  ? 119 VAL G C   1 
ATOM   7522  O  O   . VAL G  1 118 ? 13.300 -45.083  -56.163  1.00 67.40  ? 119 VAL G O   1 
ATOM   7523  C  CB  . VAL G  1 118 ? 13.892 -46.489  -53.614  1.00 62.96  ? 119 VAL G CB  1 
ATOM   7524  C  CG1 . VAL G  1 118 ? 12.955 -45.517  -52.942  1.00 64.60  ? 119 VAL G CG1 1 
ATOM   7525  C  CG2 . VAL G  1 118 ? 14.314 -47.558  -52.640  1.00 61.12  ? 119 VAL G CG2 1 
ATOM   7526  N  N   . VAL G  1 119 ? 11.281 -45.980  -55.742  1.00 69.22  ? 120 VAL G N   1 
ATOM   7527  C  CA  . VAL G  1 119 ? 10.541 -44.888  -56.363  1.00 72.27  ? 120 VAL G CA  1 
ATOM   7528  C  C   . VAL G  1 119 ? 9.999  -43.992  -55.256  1.00 73.01  ? 120 VAL G C   1 
ATOM   7529  O  O   . VAL G  1 119 ? 9.614  -44.476  -54.178  1.00 72.23  ? 120 VAL G O   1 
ATOM   7530  C  CB  . VAL G  1 119 ? 9.382  -45.392  -57.262  1.00 75.41  ? 120 VAL G CB  1 
ATOM   7531  C  CG1 . VAL G  1 119 ? 8.205  -45.939  -56.424  1.00 76.76  ? 120 VAL G CG1 1 
ATOM   7532  C  CG2 . VAL G  1 119 ? 8.914  -44.268  -58.200  1.00 78.68  ? 120 VAL G CG2 1 
ATOM   7533  N  N   . HIS G  1 120 ? 9.947  -42.690  -55.539  1.00 74.96  ? 121 HIS G N   1 
ATOM   7534  C  CA  . HIS G  1 120 ? 9.801  -41.667  -54.484  1.00 75.47  ? 121 HIS G CA  1 
ATOM   7535  C  C   . HIS G  1 120 ? 8.557  -40.796  -54.527  1.00 79.28  ? 121 HIS G C   1 
ATOM   7536  O  O   . HIS G  1 120 ? 7.923  -40.642  -55.565  1.00 81.92  ? 121 HIS G O   1 
ATOM   7537  C  CB  . HIS G  1 120 ? 11.010 -40.756  -54.491  1.00 74.41  ? 121 HIS G CB  1 
ATOM   7538  C  CG  . HIS G  1 120 ? 12.134 -41.266  -53.655  1.00 71.00  ? 121 HIS G CG  1 
ATOM   7539  N  ND1 . HIS G  1 120 ? 12.478 -40.703  -52.445  1.00 70.76  ? 121 HIS G ND1 1 
ATOM   7540  C  CD2 . HIS G  1 120 ? 12.978 -42.304  -53.843  1.00 68.55  ? 121 HIS G CD2 1 
ATOM   7541  C  CE1 . HIS G  1 120 ? 13.499 -41.363  -51.930  1.00 68.15  ? 121 HIS G CE1 1 
ATOM   7542  N  NE2 . HIS G  1 120 ? 13.813 -42.347  -52.753  1.00 66.89  ? 121 HIS G NE2 1 
ATOM   7543  N  N   . GLU G  1 121 ? 8.256  -40.210  -53.371  1.00 79.85  ? 122 GLU G N   1 
ATOM   7544  C  CA  . GLU G  1 121 ? 7.064  -39.382  -53.171  1.00 83.85  ? 122 GLU G CA  1 
ATOM   7545  C  C   . GLU G  1 121 ? 7.040  -38.183  -54.134  1.00 86.57  ? 122 GLU G C   1 
ATOM   7546  O  O   . GLU G  1 121 ? 6.150  -38.064  -54.989  1.00 89.86  ? 122 GLU G O   1 
ATOM   7547  C  CB  . GLU G  1 121 ? 7.007  -38.877  -51.715  1.00 83.87  ? 122 GLU G CB  1 
ATOM   7548  C  CG  . GLU G  1 121 ? 5.836  -37.909  -51.408  1.00 88.47  ? 122 GLU G CG  1 
ATOM   7549  C  CD  . GLU G  1 121 ? 5.899  -37.316  -50.004  1.00 89.09  ? 122 GLU G CD  1 
ATOM   7550  O  OE1 . GLU G  1 121 ? 6.920  -37.541  -49.306  1.00 85.90  ? 122 GLU G OE1 1 
ATOM   7551  O  OE2 . GLU G  1 121 ? 4.923  -36.628  -49.605  1.00 92.80  ? 122 GLU G OE2 1 
ATOM   7552  N  N   . LYS G  1 122 ? 8.018  -37.301  -53.966  1.00 85.57  ? 123 LYS G N   1 
ATOM   7553  C  CA  . LYS G  1 122 ? 8.128  -36.087  -54.765  1.00 88.26  ? 123 LYS G CA  1 
ATOM   7554  C  C   . LYS G  1 122 ? 9.119  -36.311  -55.890  1.00 86.82  ? 123 LYS G C   1 
ATOM   7555  O  O   . LYS G  1 122 ? 9.664  -37.405  -56.024  1.00 84.03  ? 123 LYS G O   1 
ATOM   7556  C  CB  . LYS G  1 122 ? 8.618  -34.914  -53.900  1.00 88.84  ? 123 LYS G CB  1 
ATOM   7557  C  CG  . LYS G  1 122 ? 7.855  -34.699  -52.591  1.00 90.24  ? 123 LYS G CG  1 
ATOM   7558  C  CD  . LYS G  1 122 ? 8.454  -33.524  -51.785  1.00 91.17  ? 123 LYS G CD  1 
ATOM   7559  C  CE  . LYS G  1 122 ? 7.845  -33.424  -50.367  1.00 92.11  ? 123 LYS G CE  1 
ATOM   7560  N  NZ  . LYS G  1 122 ? 8.197  -32.161  -49.653  1.00 93.95  ? 123 LYS G NZ  1 
ATOM   7561  N  N   . ALA G  1 123 ? 9.358  -35.265  -56.680  1.00 89.12  ? 124 ALA G N   1 
ATOM   7562  C  CA  . ALA G  1 123 ? 10.365 -35.299  -57.746  1.00 88.38  ? 124 ALA G CA  1 
ATOM   7563  C  C   . ALA G  1 123 ? 11.752 -34.983  -57.202  1.00 86.08  ? 124 ALA G C   1 
ATOM   7564  O  O   . ALA G  1 123 ? 11.905 -34.204  -56.260  1.00 86.24  ? 124 ALA G O   1 
ATOM   7565  C  CB  . ALA G  1 123 ? 10.020 -34.341  -58.846  1.00 92.49  ? 124 ALA G CB  1 
ATOM   7566  N  N   . ASP G  1 124 ? 12.754 -35.613  -57.810  1.00 84.30  ? 125 ASP G N   1 
ATOM   7567  C  CA  . ASP G  1 124 ? 14.170 -35.381  -57.490  1.00 82.71  ? 125 ASP G CA  1 
ATOM   7568  C  C   . ASP G  1 124 ? 14.617 -34.065  -58.146  1.00 85.89  ? 125 ASP G C   1 
ATOM   7569  O  O   . ASP G  1 124 ? 14.564 -33.918  -59.368  1.00 87.98  ? 125 ASP G O   1 
ATOM   7570  C  CB  . ASP G  1 124 ? 15.038 -36.568  -57.977  1.00 80.11  ? 125 ASP G CB  1 
ATOM   7571  C  CG  . ASP G  1 124 ? 16.527 -36.465  -57.547  1.00 78.74  ? 125 ASP G CG  1 
ATOM   7572  O  OD1 . ASP G  1 124 ? 16.909 -35.517  -56.842  1.00 79.59  ? 125 ASP G OD1 1 
ATOM   7573  O  OD2 . ASP G  1 124 ? 17.342 -37.335  -57.926  1.00 77.01  ? 125 ASP G OD2 1 
ATOM   7574  N  N   . ASP G  1 125 ? 15.093 -33.128  -57.330  1.00 86.56  ? 126 ASP G N   1 
ATOM   7575  C  CA  . ASP G  1 125 ? 15.522 -31.799  -57.820  1.00 90.05  ? 126 ASP G CA  1 
ATOM   7576  C  C   . ASP G  1 125 ? 16.885 -31.807  -58.504  1.00 90.15  ? 126 ASP G C   1 
ATOM   7577  O  O   . ASP G  1 125 ? 17.397 -30.743  -58.861  1.00 93.14  ? 126 ASP G O   1 
ATOM   7578  C  CB  . ASP G  1 125 ? 15.487 -30.725  -56.693  1.00 91.52  ? 126 ASP G CB  1 
ATOM   7579  C  CG  . ASP G  1 125 ? 16.684 -30.803  -55.689  1.00 89.44  ? 126 ASP G CG  1 
ATOM   7580  O  OD1 . ASP G  1 125 ? 17.786 -31.277  -56.054  1.00 88.08  ? 126 ASP G OD1 1 
ATOM   7581  O  OD2 . ASP G  1 125 ? 16.511 -30.349  -54.527  1.00 89.06  ? 126 ASP G OD2 1 
ATOM   7582  N  N   . LEU G  1 126 ? 17.455 -33.005  -58.653  1.00 87.21  ? 127 LEU G N   1 
ATOM   7583  C  CA  . LEU G  1 126 ? 18.729 -33.245  -59.337  1.00 87.36  ? 127 LEU G CA  1 
ATOM   7584  C  C   . LEU G  1 126 ? 19.893 -32.487  -58.721  1.00 88.44  ? 127 LEU G C   1 
ATOM   7585  O  O   . LEU G  1 126 ? 20.856 -32.150  -59.426  1.00 90.76  ? 127 LEU G O   1 
ATOM   7586  C  CB  . LEU G  1 126 ? 18.608 -32.948  -60.846  1.00 90.45  ? 127 LEU G CB  1 
ATOM   7587  C  CG  . LEU G  1 126 ? 17.406 -33.610  -61.559  1.00 90.51  ? 127 LEU G CG  1 
ATOM   7588  C  CD1 . LEU G  1 126 ? 17.514 -33.448  -63.088  1.00 94.01  ? 127 LEU G CD1 1 
ATOM   7589  C  CD2 . LEU G  1 126 ? 17.258 -35.085  -61.194  1.00 86.75  ? 127 LEU G CD2 1 
ATOM   7590  N  N   . GLY G  1 127 ? 19.803 -32.224  -57.415  1.00 87.34  ? 128 GLY G N   1 
ATOM   7591  C  CA  . GLY G  1 127 ? 20.874 -31.536  -56.681  1.00 88.65  ? 128 GLY G CA  1 
ATOM   7592  C  C   . GLY G  1 127 ? 20.934 -30.016  -56.823  1.00 93.03  ? 128 GLY G C   1 
ATOM   7593  O  O   . GLY G  1 127 ? 21.763 -29.369  -56.173  1.00 94.59  ? 128 GLY G O   1 
ATOM   7594  N  N   . LYS G  1 128 ? 20.062 -29.443  -57.666  1.00 95.36  ? 129 LYS G N   1 
ATOM   7595  C  CA  . LYS G  1 128 ? 20.069 -27.997  -57.975  1.00 99.86  ? 129 LYS G CA  1 
ATOM   7596  C  C   . LYS G  1 128 ? 19.126 -27.224  -57.035  1.00 100.97 ? 129 LYS G C   1 
ATOM   7597  O  O   . LYS G  1 128 ? 18.664 -26.119  -57.364  1.00 104.77 ? 129 LYS G O   1 
ATOM   7598  C  CB  . LYS G  1 128 ? 19.650 -27.751  -59.436  1.00 102.46 ? 129 LYS G CB  1 
ATOM   7599  C  CG  . LYS G  1 128 ? 20.442 -28.538  -60.471  1.00 102.26 ? 129 LYS G CG  1 
ATOM   7600  C  CD  . LYS G  1 128 ? 20.354 -27.910  -61.873  1.00 106.92 ? 129 LYS G CD  1 
ATOM   7601  C  CE  . LYS G  1 128 ? 21.027 -28.816  -62.938  1.00 106.80 ? 129 LYS G CE  1 
ATOM   7602  N  NZ  . LYS G  1 128 ? 21.312 -28.141  -64.250  1.00 111.56 ? 129 LYS G NZ  1 
ATOM   7603  N  N   . GLY G  1 129 ? 18.847 -27.801  -55.863  1.00 98.04  ? 130 GLY G N   1 
ATOM   7604  C  CA  . GLY G  1 129 ? 17.826 -27.273  -54.946  1.00 98.70  ? 130 GLY G CA  1 
ATOM   7605  C  C   . GLY G  1 129 ? 18.290 -26.089  -54.133  1.00 101.62 ? 130 GLY G C   1 
ATOM   7606  O  O   . GLY G  1 129 ? 17.467 -25.282  -53.722  1.00 103.90 ? 130 GLY G O   1 
ATOM   7607  N  N   . GLY G  1 130 ? 19.604 -26.003  -53.892  1.00 101.91 ? 131 GLY G N   1 
ATOM   7608  C  CA  . GLY G  1 130 ? 20.210 -24.885  -53.152  1.00 105.42 ? 131 GLY G CA  1 
ATOM   7609  C  C   . GLY G  1 130 ? 20.291 -25.117  -51.649  1.00 104.11 ? 131 GLY G C   1 
ATOM   7610  O  O   . GLY G  1 130 ? 21.166 -24.554  -50.975  1.00 106.39 ? 131 GLY G O   1 
ATOM   7611  N  N   . ASN G  1 131 ? 19.389 -25.941  -51.114  1.00 100.94 ? 132 ASN G N   1 
ATOM   7612  C  CA  . ASN G  1 131 ? 19.446 -26.309  -49.691  1.00 99.64  ? 132 ASN G CA  1 
ATOM   7613  C  C   . ASN G  1 131 ? 20.444 -27.458  -49.382  1.00 96.43  ? 132 ASN G C   1 
ATOM   7614  O  O   . ASN G  1 131 ? 21.013 -28.087  -50.284  1.00 94.71  ? 132 ASN G O   1 
ATOM   7615  C  CB  . ASN G  1 131 ? 18.034 -26.604  -49.140  1.00 98.48  ? 132 ASN G CB  1 
ATOM   7616  C  CG  . ASN G  1 131 ? 17.520 -27.965  -49.516  1.00 94.45  ? 132 ASN G CG  1 
ATOM   7617  O  OD1 . ASN G  1 131 ? 18.168 -28.730  -50.227  1.00 92.23  ? 132 ASN G OD1 1 
ATOM   7618  N  ND2 . ASN G  1 131 ? 16.334 -28.281  -49.031  1.00 94.13  ? 132 ASN G ND2 1 
ATOM   7619  N  N   . GLU G  1 132 ? 20.643 -27.716  -48.096  1.00 95.86  ? 133 GLU G N   1 
ATOM   7620  C  CA  . GLU G  1 132 ? 21.541 -28.775  -47.641  1.00 93.29  ? 133 GLU G CA  1 
ATOM   7621  C  C   . GLU G  1 132 ? 21.095 -30.157  -48.140  1.00 88.91  ? 133 GLU G C   1 
ATOM   7622  O  O   . GLU G  1 132 ? 21.886 -30.935  -48.665  1.00 87.02  ? 133 GLU G O   1 
ATOM   7623  C  CB  . GLU G  1 132 ? 21.548 -28.784  -46.116  1.00 94.02  ? 133 GLU G CB  1 
ATOM   7624  C  CG  . GLU G  1 132 ? 22.145 -30.058  -45.491  1.00 91.69  ? 133 GLU G CG  1 
ATOM   7625  C  CD  . GLU G  1 132 ? 23.677 -30.088  -45.512  1.00 93.44  ? 133 GLU G CD  1 
ATOM   7626  O  OE1 . GLU G  1 132 ? 24.268 -29.149  -46.091  1.00 96.65  ? 133 GLU G OE1 1 
ATOM   7627  O  OE2 . GLU G  1 132 ? 24.285 -31.042  -44.948  1.00 91.76  ? 133 GLU G OE2 1 
ATOM   7628  N  N   . GLU G  1 133 ? 19.811 -30.444  -47.940  1.00 87.64  ? 134 GLU G N   1 
ATOM   7629  C  CA  . GLU G  1 133 ? 19.242 -31.759  -48.208  1.00 83.98  ? 134 GLU G CA  1 
ATOM   7630  C  C   . GLU G  1 133 ? 19.299 -32.120  -49.700  1.00 82.88  ? 134 GLU G C   1 
ATOM   7631  O  O   . GLU G  1 133 ? 19.435 -33.293  -50.044  1.00 80.11  ? 134 GLU G O   1 
ATOM   7632  C  CB  . GLU G  1 133 ? 17.790 -31.833  -47.672  1.00 84.01  ? 134 GLU G CB  1 
ATOM   7633  C  CG  . GLU G  1 133 ? 17.219 -33.267  -47.507  1.00 80.83  ? 134 GLU G CG  1 
ATOM   7634  C  CD  . GLU G  1 133 ? 17.893 -34.066  -46.380  1.00 79.49  ? 134 GLU G CD  1 
ATOM   7635  O  OE1 . GLU G  1 133 ? 18.715 -33.511  -45.617  1.00 81.34  ? 134 GLU G OE1 1 
ATOM   7636  O  OE2 . GLU G  1 133 ? 17.604 -35.263  -46.259  1.00 76.85  ? 134 GLU G OE2 1 
ATOM   7637  N  N   . SER G  1 134 ? 19.209 -31.123  -50.579  1.00 85.47  ? 135 SER G N   1 
ATOM   7638  C  CA  . SER G  1 134 ? 19.219 -31.370  -52.036  1.00 85.26  ? 135 SER G CA  1 
ATOM   7639  C  C   . SER G  1 134 ? 20.523 -32.018  -52.471  1.00 84.00  ? 135 SER G C   1 
ATOM   7640  O  O   . SER G  1 134 ? 20.572 -32.743  -53.454  1.00 82.73  ? 135 SER G O   1 
ATOM   7641  C  CB  . SER G  1 134 ? 19.027 -30.075  -52.830  1.00 89.08  ? 135 SER G CB  1 
ATOM   7642  O  OG  . SER G  1 134 ? 19.230 -30.290  -54.225  1.00 89.08  ? 135 SER G OG  1 
ATOM   7643  N  N   . THR G  1 135 ? 21.574 -31.740  -51.724  1.00 84.79  ? 136 THR G N   1 
ATOM   7644  C  CA  . THR G  1 135 ? 22.864 -32.352  -51.955  1.00 84.35  ? 136 THR G CA  1 
ATOM   7645  C  C   . THR G  1 135 ? 22.959 -33.811  -51.487  1.00 80.88  ? 136 THR G C   1 
ATOM   7646  O  O   . THR G  1 135 ? 23.964 -34.496  -51.753  1.00 80.49  ? 136 THR G O   1 
ATOM   7647  C  CB  . THR G  1 135 ? 23.938 -31.547  -51.253  1.00 87.20  ? 136 THR G CB  1 
ATOM   7648  O  OG1 . THR G  1 135 ? 24.251 -30.418  -52.068  1.00 91.01  ? 136 THR G OG1 1 
ATOM   7649  C  CG2 . THR G  1 135 ? 25.197 -32.355  -51.022  1.00 86.48  ? 136 THR G CG2 1 
ATOM   7650  N  N   . LYS G  1 136 ? 21.922 -34.294  -50.808  1.00 78.86  ? 137 LYS G N   1 
ATOM   7651  C  CA  . LYS G  1 136 ? 21.906 -35.659  -50.265  1.00 75.67  ? 137 LYS G CA  1 
ATOM   7652  C  C   . LYS G  1 136 ? 20.824 -36.526  -50.900  1.00 73.30  ? 137 LYS G C   1 
ATOM   7653  O  O   . LYS G  1 136 ? 21.103 -37.485  -51.617  1.00 71.75  ? 137 LYS G O   1 
ATOM   7654  C  CB  . LYS G  1 136 ? 21.668 -35.607  -48.752  1.00 75.71  ? 137 LYS G CB  1 
ATOM   7655  C  CG  . LYS G  1 136 ? 22.878 -35.121  -47.906  1.00 78.07  ? 137 LYS G CG  1 
ATOM   7656  C  CD  . LYS G  1 136 ? 22.504 -35.141  -46.406  1.00 78.45  ? 137 LYS G CD  1 
ATOM   7657  C  CE  . LYS G  1 136 ? 23.720 -35.242  -45.498  1.00 79.53  ? 137 LYS G CE  1 
ATOM   7658  N  NZ  . LYS G  1 136 ? 24.271 -33.912  -45.225  1.00 83.54  ? 137 LYS G NZ  1 
ATOM   7659  N  N   . THR G  1 137 ? 19.582 -36.172  -50.632  1.00 73.56  ? 138 THR G N   1 
ATOM   7660  C  CA  . THR G  1 137 ? 18.448 -37.001  -51.019  1.00 72.07  ? 138 THR G CA  1 
ATOM   7661  C  C   . THR G  1 137 ? 17.789 -36.524  -52.311  1.00 73.61  ? 138 THR G C   1 
ATOM   7662  O  O   . THR G  1 137 ? 16.995 -37.257  -52.910  1.00 72.84  ? 138 THR G O   1 
ATOM   7663  C  CB  . THR G  1 137 ? 17.391 -37.009  -49.914  1.00 72.11  ? 138 THR G CB  1 
ATOM   7664  O  OG1 . THR G  1 137 ? 16.733 -35.728  -49.844  1.00 74.98  ? 138 THR G OG1 1 
ATOM   7665  C  CG2 . THR G  1 137 ? 18.044 -37.336  -48.598  1.00 71.46  ? 138 THR G CG2 1 
ATOM   7666  N  N   . GLY G  1 138 ? 18.116 -35.302  -52.728  1.00 76.16  ? 139 GLY G N   1 
ATOM   7667  C  CA  . GLY G  1 138 ? 17.486 -34.687  -53.886  1.00 78.41  ? 139 GLY G CA  1 
ATOM   7668  C  C   . GLY G  1 138 ? 16.137 -34.064  -53.563  1.00 80.23  ? 139 GLY G C   1 
ATOM   7669  O  O   . GLY G  1 138 ? 15.388 -33.673  -54.469  1.00 82.29  ? 139 GLY G O   1 
ATOM   7670  N  N   . ASN G  1 139 ? 15.814 -33.978  -52.275  1.00 79.90  ? 140 ASN G N   1 
ATOM   7671  C  CA  . ASN G  1 139 ? 14.506 -33.467  -51.808  1.00 81.93  ? 140 ASN G CA  1 
ATOM   7672  C  C   . ASN G  1 139 ? 13.288 -34.185  -52.394  1.00 81.83  ? 140 ASN G C   1 
ATOM   7673  O  O   . ASN G  1 139 ? 12.186 -33.620  -52.463  1.00 84.46  ? 140 ASN G O   1 
ATOM   7674  C  CB  . ASN G  1 139 ? 14.397 -31.951  -52.062  1.00 85.84  ? 140 ASN G CB  1 
ATOM   7675  C  CG  . ASN G  1 139 ? 15.178 -31.125  -51.041  1.00 86.84  ? 140 ASN G CG  1 
ATOM   7676  O  OD1 . ASN G  1 139 ? 15.722 -30.072  -51.384  1.00 89.44  ? 140 ASN G OD1 1 
ATOM   7677  N  ND2 . ASN G  1 139 ? 15.238 -31.600  -49.782  1.00 84.90  ? 140 ASN G ND2 1 
ATOM   7678  N  N   . ALA G  1 140 ? 13.496 -35.441  -52.785  1.00 79.24  ? 141 ALA G N   1 
ATOM   7679  C  CA  . ALA G  1 140 ? 12.476 -36.237  -53.484  1.00 79.32  ? 141 ALA G CA  1 
ATOM   7680  C  C   . ALA G  1 140 ? 11.491 -36.908  -52.513  1.00 78.77  ? 141 ALA G C   1 
ATOM   7681  O  O   . ALA G  1 140 ? 10.538 -37.570  -52.933  1.00 79.30  ? 141 ALA G O   1 
ATOM   7682  C  CB  . ALA G  1 140 ? 13.141 -37.270  -54.383  1.00 77.19  ? 141 ALA G CB  1 
ATOM   7683  N  N   . GLY G  1 141 ? 11.722 -36.726  -51.221  1.00 78.12  ? 142 GLY G N   1 
ATOM   7684  C  CA  . GLY G  1 141 ? 10.730 -37.092  -50.230  1.00 78.80  ? 142 GLY G CA  1 
ATOM   7685  C  C   . GLY G  1 141 ? 10.711 -38.564  -49.889  1.00 76.24  ? 142 GLY G C   1 
ATOM   7686  O  O   . GLY G  1 141 ? 11.702 -39.270  -50.102  1.00 73.45  ? 142 GLY G O   1 
ATOM   7687  N  N   . SER G  1 142 ? 9.561  -39.016  -49.370  1.00 77.56  ? 143 SER G N   1 
ATOM   7688  C  CA  . SER G  1 142 ? 9.410  -40.365  -48.785  1.00 75.72  ? 143 SER G CA  1 
ATOM   7689  C  C   . SER G  1 142 ? 9.492  -41.485  -49.818  1.00 74.11  ? 143 SER G C   1 
ATOM   7690  O  O   . SER G  1 142 ? 9.456  -41.255  -51.037  1.00 74.89  ? 143 SER G O   1 
ATOM   7691  C  CB  . SER G  1 142 ? 8.084  -40.488  -48.019  1.00 78.37  ? 143 SER G CB  1 
ATOM   7692  O  OG  . SER G  1 142 ? 6.975  -40.590  -48.903  1.00 81.03  ? 143 SER G OG  1 
ATOM   7693  N  N   . ARG G  1 143 ? 9.586  -42.706  -49.308  1.00 72.20  ? 144 ARG G N   1 
ATOM   7694  C  CA  . ARG G  1 143 ? 9.760  -43.883  -50.155  1.00 70.76  ? 144 ARG G CA  1 
ATOM   7695  C  C   . ARG G  1 143 ? 8.431  -44.606  -50.346  1.00 72.86  ? 144 ARG G C   1 
ATOM   7696  O  O   . ARG G  1 143 ? 7.928  -45.255  -49.424  1.00 73.24  ? 144 ARG G O   1 
ATOM   7697  C  CB  . ARG G  1 143 ? 10.804 -44.812  -49.544  1.00 67.71  ? 144 ARG G CB  1 
ATOM   7698  C  CG  . ARG G  1 143 ? 12.157 -44.149  -49.433  1.00 66.15  ? 144 ARG G CG  1 
ATOM   7699  C  CD  . ARG G  1 143 ? 13.137 -44.992  -48.668  1.00 64.02  ? 144 ARG G CD  1 
ATOM   7700  N  NE  . ARG G  1 143 ? 14.367 -44.260  -48.408  1.00 63.22  ? 144 ARG G NE  1 
ATOM   7701  C  CZ  . ARG G  1 143 ? 15.445 -44.782  -47.827  1.00 61.86  ? 144 ARG G CZ  1 
ATOM   7702  N  NH1 . ARG G  1 143 ? 15.469 -46.051  -47.421  1.00 60.68  ? 144 ARG G NH1 1 
ATOM   7703  N  NH2 . ARG G  1 143 ? 16.515 -44.011  -47.646  1.00 62.45  ? 144 ARG G NH2 1 
ATOM   7704  N  N   . LEU G  1 144 ? 7.873  -44.480  -51.547  1.00 74.70  ? 145 LEU G N   1 
ATOM   7705  C  CA  . LEU G  1 144 ? 6.525  -44.993  -51.841  1.00 77.91  ? 145 LEU G CA  1 
ATOM   7706  C  C   . LEU G  1 144 ? 6.485  -46.499  -52.046  1.00 76.94  ? 145 LEU G C   1 
ATOM   7707  O  O   . LEU G  1 144 ? 5.627  -47.196  -51.484  1.00 78.63  ? 145 LEU G O   1 
ATOM   7708  C  CB  . LEU G  1 144 ? 5.954  -44.322  -53.100  1.00 80.95  ? 145 LEU G CB  1 
ATOM   7709  C  CG  . LEU G  1 144 ? 5.620  -42.827  -53.014  1.00 83.36  ? 145 LEU G CG  1 
ATOM   7710  C  CD1 . LEU G  1 144 ? 4.928  -42.302  -54.284  1.00 86.72  ? 145 LEU G CD1 1 
ATOM   7711  C  CD2 . LEU G  1 144 ? 4.766  -42.587  -51.768  1.00 85.35  ? 145 LEU G CD2 1 
ATOM   7712  N  N   . ALA G  1 145 ? 7.394  -46.974  -52.892  1.00 74.75  ? 146 ALA G N   1 
ATOM   7713  C  CA  . ALA G  1 145 ? 7.502  -48.394  -53.216  1.00 73.91  ? 146 ALA G CA  1 
ATOM   7714  C  C   . ALA G  1 145 ? 8.951  -48.746  -53.535  1.00 70.55  ? 146 ALA G C   1 
ATOM   7715  O  O   . ALA G  1 145 ? 9.702  -47.935  -54.083  1.00 70.02  ? 146 ALA G O   1 
ATOM   7716  C  CB  . ALA G  1 145 ? 6.607  -48.735  -54.389  1.00 77.03  ? 146 ALA G CB  1 
ATOM   7717  N  N   . CYS G  1 146 ? 9.344  -49.960  -53.185  1.00 68.83  ? 147 CYS G N   1 
ATOM   7718  C  CA  . CYS G  1 146 ? 10.715 -50.405  -53.421  1.00 65.95  ? 147 CYS G CA  1 
ATOM   7719  C  C   . CYS G  1 146 ? 10.822 -51.917  -53.544  1.00 65.58  ? 147 CYS G C   1 
ATOM   7720  O  O   . CYS G  1 146 ? 9.887  -52.660  -53.233  1.00 67.26  ? 147 CYS G O   1 
ATOM   7721  C  CB  . CYS G  1 146 ? 11.609 -49.943  -52.292  1.00 63.63  ? 147 CYS G CB  1 
ATOM   7722  S  SG  . CYS G  1 146 ? 11.196 -50.745  -50.759  1.00 63.31  ? 147 CYS G SG  1 
ATOM   7723  N  N   . GLY G  1 147 ? 11.981 -52.368  -53.996  1.00 63.87  ? 148 GLY G N   1 
ATOM   7724  C  CA  . GLY G  1 147 ? 12.224 -53.803  -54.155  1.00 63.65  ? 148 GLY G CA  1 
ATOM   7725  C  C   . GLY G  1 147 ? 13.695 -54.110  -54.325  1.00 61.51  ? 148 GLY G C   1 
ATOM   7726  O  O   . GLY G  1 147 ? 14.460 -53.262  -54.784  1.00 60.89  ? 148 GLY G O   1 
ATOM   7727  N  N   . VAL G  1 148 ? 14.091 -55.319  -53.942  1.00 60.69  ? 149 VAL G N   1 
ATOM   7728  C  CA  . VAL G  1 148 ? 15.481 -55.739  -54.097  1.00 59.20  ? 149 VAL G CA  1 
ATOM   7729  C  C   . VAL G  1 148 ? 15.751 -56.157  -55.544  1.00 60.36  ? 149 VAL G C   1 
ATOM   7730  O  O   . VAL G  1 148 ? 14.959 -56.878  -56.154  1.00 61.99  ? 149 VAL G O   1 
ATOM   7731  C  CB  . VAL G  1 148 ? 15.840 -56.905  -53.149  1.00 58.39  ? 149 VAL G CB  1 
ATOM   7732  C  CG1 . VAL G  1 148 ? 17.273 -57.335  -53.346  1.00 57.33  ? 149 VAL G CG1 1 
ATOM   7733  C  CG2 . VAL G  1 148 ? 15.635 -56.506  -51.713  1.00 57.72  ? 149 VAL G CG2 1 
ATOM   7734  N  N   . ILE G  1 149 ? 16.883 -55.704  -56.076  1.00 59.89  ? 150 ILE G N   1 
ATOM   7735  C  CA  . ILE G  1 149 ? 17.273 -55.977  -57.466  1.00 61.33  ? 150 ILE G CA  1 
ATOM   7736  C  C   . ILE G  1 149 ? 17.885 -57.355  -57.584  1.00 61.47  ? 150 ILE G C   1 
ATOM   7737  O  O   . ILE G  1 149 ? 18.887 -57.668  -56.933  1.00 60.17  ? 150 ILE G O   1 
ATOM   7738  C  CB  . ILE G  1 149 ? 18.319 -54.980  -57.995  1.00 61.26  ? 150 ILE G CB  1 
ATOM   7739  C  CG1 . ILE G  1 149 ? 17.706 -53.588  -58.138  1.00 61.76  ? 150 ILE G CG1 1 
ATOM   7740  C  CG2 . ILE G  1 149 ? 18.852 -55.446  -59.330  1.00 62.90  ? 150 ILE G CG2 1 
ATOM   7741  C  CD1 . ILE G  1 149 ? 18.725 -52.517  -58.447  1.00 61.77  ? 150 ILE G CD1 1 
ATOM   7742  N  N   . GLY G  1 150 ? 17.295 -58.163  -58.453  1.00 63.49  ? 151 GLY G N   1 
ATOM   7743  C  CA  . GLY G  1 150 ? 17.640 -59.583  -58.540  1.00 64.26  ? 151 GLY G CA  1 
ATOM   7744  C  C   . GLY G  1 150 ? 18.124 -60.027  -59.913  1.00 66.38  ? 151 GLY G C   1 
ATOM   7745  O  O   . GLY G  1 150 ? 17.815 -59.397  -60.941  1.00 67.97  ? 151 GLY G O   1 
ATOM   7746  N  N   . ILE G  1 151 ? 18.892 -61.119  -59.919  1.00 66.71  ? 152 ILE G N   1 
ATOM   7747  C  CA  . ILE G  1 151 ? 19.406 -61.692  -61.154  1.00 68.96  ? 152 ILE G CA  1 
ATOM   7748  C  C   . ILE G  1 151 ? 18.245 -62.355  -61.879  1.00 71.63  ? 152 ILE G C   1 
ATOM   7749  O  O   . ILE G  1 151 ? 17.474 -63.110  -61.259  1.00 71.73  ? 152 ILE G O   1 
ATOM   7750  C  CB  . ILE G  1 151 ? 20.506 -62.730  -60.914  1.00 69.02  ? 152 ILE G CB  1 
ATOM   7751  C  CG1 . ILE G  1 151 ? 21.699 -62.101  -60.212  1.00 67.10  ? 152 ILE G CG1 1 
ATOM   7752  C  CG2 . ILE G  1 151 ? 20.985 -63.302  -62.238  1.00 71.91  ? 152 ILE G CG2 1 
ATOM   7753  C  CD1 . ILE G  1 151 ? 22.829 -63.069  -59.973  1.00 67.77  ? 152 ILE G CD1 1 
ATOM   7754  N  N   . ALA G  1 152 ? 18.138 -62.049  -63.178  1.00 74.08  ? 153 ALA G N   1 
ATOM   7755  C  CA  . ALA G  1 152 ? 17.028 -62.486  -64.015  1.00 77.33  ? 153 ALA G CA  1 
ATOM   7756  C  C   . ALA G  1 152 ? 17.501 -63.424  -65.113  1.00 80.53  ? 153 ALA G C   1 
ATOM   7757  O  O   . ALA G  1 152 ? 18.688 -63.414  -65.470  1.00 80.29  ? 153 ALA G O   1 
ATOM   7758  C  CB  . ALA G  1 152 ? 16.344 -61.281  -64.625  1.00 78.39  ? 153 ALA G CB  1 
ATOM   7759  N  N   . GLN G  1 153 ? 16.561 -64.221  -65.645  1.00 83.85  ? 154 GLN G N   1 
ATOM   7760  C  CA  . GLN G  1 153 ? 16.874 -65.170  -66.738  1.00 87.82  ? 154 GLN G CA  1 
ATOM   7761  C  C   . GLN G  1 153 ? 17.068 -64.462  -68.081  1.00 90.49  ? 154 GLN G C   1 
ATOM   7762  O  O   . GLN G  1 153 ? 16.216 -63.661  -68.466  1.00 91.68  ? 154 GLN G O   1 
ATOM   7763  C  CB  . GLN G  1 153 ? 15.789 -66.250  -66.906  1.00 91.16  ? 154 GLN G CB  1 
ATOM   7764  C  CG  . GLN G  1 153 ? 16.159 -67.329  -67.990  1.00 95.43  ? 154 GLN G CG  1 
ATOM   7765  C  CD  . GLN G  1 153 ? 15.143 -68.458  -68.085  1.00 99.01  ? 154 GLN G CD  1 
ATOM   7766  O  OE1 . GLN G  1 153 ? 14.972 -69.248  -67.154  1.00 98.15  ? 154 GLN G OE1 1 
ATOM   7767  N  NE2 . GLN G  1 153 ? 14.455 -68.529  -69.213  1.00 103.40 ? 154 GLN G NE2 1 
ATOM   7768  O  OXT . GLN G  1 153 ? 18.044 -64.684  -68.810  1.00 91.95  ? 154 GLN G OXT 1 
ATOM   7769  N  N   . ALA H  1 1   ? 33.290 -59.372  -41.965  1.00 63.50  ? 2   ALA H N   1 
ATOM   7770  C  CA  . ALA H  1 1   ? 33.000 -58.750  -43.283  1.00 63.40  ? 2   ALA H CA  1 
ATOM   7771  C  C   . ALA H  1 1   ? 31.524 -58.999  -43.804  1.00 60.06  ? 2   ALA H C   1 
ATOM   7772  O  O   . ALA H  1 1   ? 30.544 -58.652  -43.123  1.00 58.95  ? 2   ALA H O   1 
ATOM   7773  C  CB  . ALA H  1 1   ? 34.088 -59.160  -44.324  1.00 64.54  ? 2   ALA H CB  1 
ATOM   7774  N  N   . THR H  1 2   ? 31.368 -59.631  -44.966  1.00 59.04  ? 3   THR H N   1 
ATOM   7775  C  CA  . THR H  1 2   ? 30.155 -59.473  -45.812  1.00 56.79  ? 3   THR H CA  1 
ATOM   7776  C  C   . THR H  1 2   ? 28.904 -60.004  -45.120  1.00 53.94  ? 3   THR H C   1 
ATOM   7777  O  O   . THR H  1 2   ? 28.951 -61.031  -44.454  1.00 52.79  ? 3   THR H O   1 
ATOM   7778  C  CB  . THR H  1 2   ? 30.286 -60.213  -47.170  1.00 56.22  ? 3   THR H CB  1 
ATOM   7779  O  OG1 . THR H  1 2   ? 31.676 -60.360  -47.518  1.00 58.93  ? 3   THR H OG1 1 
ATOM   7780  C  CG2 . THR H  1 2   ? 29.508 -59.472  -48.291  1.00 56.08  ? 3   THR H CG2 1 
ATOM   7781  N  N   . LYS H  1 3   ? 27.793 -59.294  -45.274  1.00 53.26  ? 4   LYS H N   1 
ATOM   7782  C  CA  . LYS H  1 3   ? 26.518 -59.709  -44.703  1.00 51.10  ? 4   LYS H CA  1 
ATOM   7783  C  C   . LYS H  1 3   ? 25.446 -59.619  -45.745  1.00 50.07  ? 4   LYS H C   1 
ATOM   7784  O  O   . LYS H  1 3   ? 25.514 -58.794  -46.620  1.00 51.69  ? 4   LYS H O   1 
ATOM   7785  C  CB  . LYS H  1 3   ? 26.127 -58.819  -43.528  1.00 52.43  ? 4   LYS H CB  1 
ATOM   7786  C  CG  . LYS H  1 3   ? 27.029 -58.940  -42.282  1.00 54.12  ? 4   LYS H CG  1 
ATOM   7787  C  CD  . LYS H  1 3   ? 26.415 -58.210  -41.055  1.00 55.43  ? 4   LYS H CD  1 
ATOM   7788  C  CE  . LYS H  1 3   ? 27.480 -57.774  -40.038  1.00 58.08  ? 4   LYS H CE  1 
ATOM   7789  N  NZ  . LYS H  1 3   ? 27.017 -56.644  -39.203  1.00 59.91  ? 4   LYS H NZ  1 
ATOM   7790  N  N   . ALA H  1 4   ? 24.457 -60.485  -45.659  1.00 48.04  ? 5   ALA H N   1 
ATOM   7791  C  CA  . ALA H  1 4   ? 23.285 -60.415  -46.529  1.00 47.63  ? 5   ALA H CA  1 
ATOM   7792  C  C   . ALA H  1 4   ? 22.037 -60.738  -45.715  1.00 46.68  ? 5   ALA H C   1 
ATOM   7793  O  O   . ALA H  1 4   ? 22.128 -61.278  -44.607  1.00 45.99  ? 5   ALA H O   1 
ATOM   7794  C  CB  . ALA H  1 4   ? 23.408 -61.368  -47.688  1.00 46.71  ? 5   ALA H CB  1 
ATOM   7795  N  N   . VAL H  1 5   ? 20.876 -60.397  -46.271  1.00 47.13  ? 6   VAL H N   1 
ATOM   7796  C  CA  . VAL H  1 5   ? 19.580 -60.622  -45.612  1.00 46.82  ? 6   VAL H CA  1 
ATOM   7797  C  C   . VAL H  1 5   ? 18.484 -60.878  -46.638  1.00 46.98  ? 6   VAL H C   1 
ATOM   7798  O  O   . VAL H  1 5   ? 18.591 -60.478  -47.793  1.00 47.92  ? 6   VAL H O   1 
ATOM   7799  C  CB  . VAL H  1 5   ? 19.144 -59.427  -44.761  1.00 48.82  ? 6   VAL H CB  1 
ATOM   7800  C  CG1 . VAL H  1 5   ? 18.584 -58.338  -45.631  1.00 51.38  ? 6   VAL H CG1 1 
ATOM   7801  C  CG2 . VAL H  1 5   ? 18.091 -59.836  -43.776  1.00 48.84  ? 6   VAL H CG2 1 
ATOM   7802  N  N   . CYS H  1 6   ? 17.436 -61.563  -46.214  1.00 46.51  ? 7   CYS H N   1 
ATOM   7803  C  CA  . CYS H  1 6   ? 16.350 -61.915  -47.112  1.00 47.21  ? 7   CYS H CA  1 
ATOM   7804  C  C   . CYS H  1 6   ? 15.049 -62.029  -46.375  1.00 48.30  ? 7   CYS H C   1 
ATOM   7805  O  O   . CYS H  1 6   ? 14.963 -62.789  -45.400  1.00 47.20  ? 7   CYS H O   1 
ATOM   7806  C  CB  . CYS H  1 6   ? 16.593 -63.261  -47.766  1.00 45.53  ? 7   CYS H CB  1 
ATOM   7807  S  SG  . CYS H  1 6   ? 15.124 -63.838  -48.619  1.00 46.50  ? 7   CYS H SG  1 
ATOM   7808  N  N   . VAL H  1 7   ? 14.041 -61.296  -46.861  1.00 50.90  ? 8   VAL H N   1 
ATOM   7809  C  CA  . VAL H  1 7   ? 12.678 -61.348  -46.302  1.00 52.56  ? 8   VAL H CA  1 
ATOM   7810  C  C   . VAL H  1 7   ? 11.798 -62.347  -47.056  1.00 52.74  ? 8   VAL H C   1 
ATOM   7811  O  O   . VAL H  1 7   ? 11.385 -62.096  -48.185  1.00 54.33  ? 8   VAL H O   1 
ATOM   7812  C  CB  . VAL H  1 7   ? 12.010 -59.977  -46.307  1.00 55.86  ? 8   VAL H CB  1 
ATOM   7813  C  CG1 . VAL H  1 7   ? 10.551 -60.104  -45.891  1.00 58.30  ? 8   VAL H CG1 1 
ATOM   7814  C  CG2 . VAL H  1 7   ? 12.746 -59.050  -45.382  1.00 55.93  ? 8   VAL H CG2 1 
ATOM   7815  N  N   . LEU H  1 8   ? 11.527 -63.476  -46.409  1.00 51.41  ? 9   LEU H N   1 
ATOM   7816  C  CA  . LEU H  1 8   ? 10.717 -64.546  -46.979  1.00 51.71  ? 9   LEU H CA  1 
ATOM   7817  C  C   . LEU H  1 8   ? 9.260  -64.196  -46.856  1.00 55.01  ? 9   LEU H C   1 
ATOM   7818  O  O   . LEU H  1 8   ? 8.798  -63.906  -45.758  1.00 56.08  ? 9   LEU H O   1 
ATOM   7819  C  CB  . LEU H  1 8   ? 10.978 -65.881  -46.256  1.00 49.46  ? 9   LEU H CB  1 
ATOM   7820  C  CG  . LEU H  1 8   ? 12.337 -66.546  -46.514  1.00 46.34  ? 9   LEU H CG  1 
ATOM   7821  C  CD1 . LEU H  1 8   ? 12.625 -67.560  -45.455  1.00 44.51  ? 9   LEU H CD1 1 
ATOM   7822  C  CD2 . LEU H  1 8   ? 12.382 -67.192  -47.882  1.00 46.23  ? 9   LEU H CD2 1 
ATOM   7823  N  N   . LYS H  1 9   ? 8.556  -64.241  -47.987  1.00 57.14  ? 10  LYS H N   1 
ATOM   7824  C  CA  . LYS H  1 9   ? 7.108  -63.961  -48.057  1.00 61.35  ? 10  LYS H CA  1 
ATOM   7825  C  C   . LYS H  1 9   ? 6.408  -64.806  -49.111  1.00 62.80  ? 10  LYS H C   1 
ATOM   7826  O  O   . LYS H  1 9   ? 7.039  -65.282  -50.055  1.00 61.48  ? 10  LYS H O   1 
ATOM   7827  C  CB  . LYS H  1 9   ? 6.842  -62.478  -48.393  1.00 64.59  ? 10  LYS H CB  1 
ATOM   7828  C  CG  . LYS H  1 9   ? 6.868  -61.532  -47.180  1.00 65.88  ? 10  LYS H CG  1 
ATOM   7829  C  CD  . LYS H  1 9   ? 6.004  -60.290  -47.402  1.00 70.81  ? 10  LYS H CD  1 
ATOM   7830  C  CE  . LYS H  1 9   ? 6.289  -59.188  -46.365  1.00 71.43  ? 10  LYS H CE  1 
ATOM   7831  N  NZ  . LYS H  1 9   ? 5.568  -59.419  -45.067  1.00 72.59  ? 10  LYS H NZ  1 
ATOM   7832  N  N   . GLY H  1 10  ? 5.096  -64.947  -48.985  1.00 66.21  ? 11  GLY H N   1 
ATOM   7833  C  CA  . GLY H  1 10  ? 4.357  -65.743  -49.955  1.00 68.33  ? 11  GLY H CA  1 
ATOM   7834  C  C   . GLY H  1 10  ? 2.859  -65.529  -49.964  1.00 73.67  ? 11  GLY H C   1 
ATOM   7835  O  O   . GLY H  1 10  ? 2.335  -64.663  -49.245  1.00 76.06  ? 11  GLY H O   1 
ATOM   7836  N  N   . ASP H  1 11  ? 2.177  -66.349  -50.776  1.00 75.84  ? 12  ASP H N   1 
ATOM   7837  C  CA  . ASP H  1 11  ? 0.713  -66.286  -50.945  1.00 81.43  ? 12  ASP H CA  1 
ATOM   7838  C  C   . ASP H  1 11  ? -0.068 -66.600  -49.677  1.00 82.69  ? 12  ASP H C   1 
ATOM   7839  O  O   . ASP H  1 11  ? -1.124 -66.026  -49.457  1.00 87.64  ? 12  ASP H O   1 
ATOM   7840  C  CB  . ASP H  1 11  ? 0.246  -67.230  -52.057  1.00 83.40  ? 12  ASP H CB  1 
ATOM   7841  C  CG  . ASP H  1 11  ? 0.215  -66.563  -53.418  1.00 86.72  ? 12  ASP H CG  1 
ATOM   7842  O  OD1 . ASP H  1 11  ? -0.398 -65.478  -53.547  1.00 91.46  ? 12  ASP H OD1 1 
ATOM   7843  O  OD2 . ASP H  1 11  ? 0.782  -67.133  -54.369  1.00 85.70  ? 12  ASP H OD2 1 
ATOM   7844  N  N   . GLY H  1 12  ? 0.463  -67.494  -48.850  1.00 78.78  ? 13  GLY H N   1 
ATOM   7845  C  CA  . GLY H  1 12  ? -0.201 -67.909  -47.613  1.00 79.98  ? 13  GLY H CA  1 
ATOM   7846  C  C   . GLY H  1 12  ? 0.463  -67.347  -46.373  1.00 77.40  ? 13  GLY H C   1 
ATOM   7847  O  O   . GLY H  1 12  ? 1.177  -66.363  -46.467  1.00 76.00  ? 13  GLY H O   1 
ATOM   7848  N  N   . PRO H  1 13  ? 0.257  -67.994  -45.208  1.00 77.15  ? 14  PRO H N   1 
ATOM   7849  C  CA  . PRO H  1 13  ? 0.643  -67.477  -43.891  1.00 76.31  ? 14  PRO H CA  1 
ATOM   7850  C  C   . PRO H  1 13  ? 2.149  -67.536  -43.599  1.00 70.93  ? 14  PRO H C   1 
ATOM   7851  O  O   . PRO H  1 13  ? 2.627  -66.882  -42.658  1.00 70.19  ? 14  PRO H O   1 
ATOM   7852  C  CB  . PRO H  1 13  ? -0.102 -68.410  -42.923  1.00 78.27  ? 14  PRO H CB  1 
ATOM   7853  C  CG  . PRO H  1 13  ? -0.121 -69.710  -43.617  1.00 76.84  ? 14  PRO H CG  1 
ATOM   7854  C  CD  . PRO H  1 13  ? -0.149 -69.408  -45.115  1.00 77.32  ? 14  PRO H CD  1 
ATOM   7855  N  N   . VAL H  1 14  ? 2.873  -68.320  -44.399  1.00 67.66  ? 15  VAL H N   1 
ATOM   7856  C  CA  . VAL H  1 14  ? 4.304  -68.522  -44.199  1.00 62.78  ? 15  VAL H CA  1 
ATOM   7857  C  C   . VAL H  1 14  ? 5.051  -67.230  -44.488  1.00 61.84  ? 15  VAL H C   1 
ATOM   7858  O  O   . VAL H  1 14  ? 4.937  -66.648  -45.583  1.00 62.87  ? 15  VAL H O   1 
ATOM   7859  C  CB  . VAL H  1 14  ? 4.876  -69.634  -45.081  1.00 60.05  ? 15  VAL H CB  1 
ATOM   7860  C  CG1 . VAL H  1 14  ? 6.305  -69.879  -44.720  1.00 55.85  ? 15  VAL H CG1 1 
ATOM   7861  C  CG2 . VAL H  1 14  ? 4.095  -70.906  -44.894  1.00 61.64  ? 15  VAL H CG2 1 
ATOM   7862  N  N   . GLN H  1 15  ? 5.795  -66.784  -43.479  1.00 60.25  ? 16  GLN H N   1 
ATOM   7863  C  CA  . GLN H  1 15  ? 6.663  -65.613  -43.595  1.00 59.24  ? 16  GLN H CA  1 
ATOM   7864  C  C   . GLN H  1 15  ? 7.794  -65.640  -42.592  1.00 56.44  ? 16  GLN H C   1 
ATOM   7865  O  O   . GLN H  1 15  ? 7.728  -66.320  -41.579  1.00 56.09  ? 16  GLN H O   1 
ATOM   7866  C  CB  . GLN H  1 15  ? 5.875  -64.318  -43.435  1.00 63.17  ? 16  GLN H CB  1 
ATOM   7867  C  CG  . GLN H  1 15  ? 5.040  -64.221  -42.171  1.00 66.31  ? 16  GLN H CG  1 
ATOM   7868  C  CD  . GLN H  1 15  ? 4.432  -62.822  -41.962  1.00 70.72  ? 16  GLN H CD  1 
ATOM   7869  O  OE1 . GLN H  1 15  ? 4.115  -62.447  -40.838  1.00 72.99  ? 16  GLN H OE1 1 
ATOM   7870  N  NE2 . GLN H  1 15  ? 4.255  -62.058  -43.050  1.00 72.09  ? 16  GLN H NE2 1 
ATOM   7871  N  N   . GLY H  1 16  ? 8.836  -64.884  -42.899  1.00 54.92  ? 17  GLY H N   1 
ATOM   7872  C  CA  . GLY H  1 16  ? 10.026 -64.861  -42.061  1.00 52.71  ? 17  GLY H CA  1 
ATOM   7873  C  C   . GLY H  1 16  ? 11.133 -63.973  -42.565  1.00 51.38  ? 17  GLY H C   1 
ATOM   7874  O  O   . GLY H  1 16  ? 11.028 -63.380  -43.636  1.00 51.93  ? 17  GLY H O   1 
ATOM   7875  N  N   . ILE H  1 17  ? 12.189 -63.908  -41.759  1.00 50.00  ? 18  ILE H N   1 
ATOM   7876  C  CA  . ILE H  1 17  ? 13.431 -63.179  -42.064  1.00 49.08  ? 18  ILE H CA  1 
ATOM   7877  C  C   . ILE H  1 17  ? 14.646 -64.096  -41.889  1.00 46.51  ? 18  ILE H C   1 
ATOM   7878  O  O   . ILE H  1 17  ? 14.764 -64.759  -40.856  1.00 46.42  ? 18  ILE H O   1 
ATOM   7879  C  CB  . ILE H  1 17  ? 13.629 -61.997  -41.102  1.00 51.01  ? 18  ILE H CB  1 
ATOM   7880  C  CG1 . ILE H  1 17  ? 12.804 -60.788  -41.546  1.00 54.03  ? 18  ILE H CG1 1 
ATOM   7881  C  CG2 . ILE H  1 17  ? 15.095 -61.610  -41.018  1.00 49.78  ? 18  ILE H CG2 1 
ATOM   7882  C  CD1 . ILE H  1 17  ? 13.171 -59.479  -40.818  1.00 55.98  ? 18  ILE H CD1 1 
ATOM   7883  N  N   . ILE H  1 18  ? 15.539 -64.141  -42.878  1.00 45.00  ? 19  ILE H N   1 
ATOM   7884  C  CA  . ILE H  1 18  ? 16.740 -64.975  -42.783  1.00 43.08  ? 19  ILE H CA  1 
ATOM   7885  C  C   . ILE H  1 18  ? 17.974 -64.136  -43.051  1.00 43.18  ? 19  ILE H C   1 
ATOM   7886  O  O   . ILE H  1 18  ? 18.028 -63.420  -44.043  1.00 43.75  ? 19  ILE H O   1 
ATOM   7887  C  CB  . ILE H  1 18  ? 16.722 -66.146  -43.778  1.00 41.59  ? 19  ILE H CB  1 
ATOM   7888  C  CG1 . ILE H  1 18  ? 15.654 -67.162  -43.418  1.00 41.68  ? 19  ILE H CG1 1 
ATOM   7889  C  CG2 . ILE H  1 18  ? 18.030 -66.867  -43.770  1.00 40.32  ? 19  ILE H CG2 1 
ATOM   7890  C  CD1 . ILE H  1 18  ? 15.926 -67.916  -42.168  1.00 41.60  ? 19  ILE H CD1 1 
ATOM   7891  N  N   . ASN H  1 19  ? 18.960 -64.245  -42.157  1.00 43.14  ? 20  ASN H N   1 
ATOM   7892  C  CA  . ASN H  1 19  ? 20.238 -63.519  -42.262  1.00 43.71  ? 20  ASN H CA  1 
ATOM   7893  C  C   . ASN H  1 19  ? 21.395 -64.372  -42.768  1.00 42.63  ? 20  ASN H C   1 
ATOM   7894  O  O   . ASN H  1 19  ? 21.449 -65.573  -42.500  1.00 41.72  ? 20  ASN H O   1 
ATOM   7895  C  CB  . ASN H  1 19  ? 20.659 -62.982  -40.895  1.00 45.17  ? 20  ASN H CB  1 
ATOM   7896  C  CG  . ASN H  1 19  ? 19.691 -61.998  -40.333  1.00 46.92  ? 20  ASN H CG  1 
ATOM   7897  O  OD1 . ASN H  1 19  ? 18.900 -62.335  -39.448  1.00 47.55  ? 20  ASN H OD1 1 
ATOM   7898  N  ND2 . ASN H  1 19  ? 19.738 -60.761  -40.838  1.00 48.22  ? 20  ASN H ND2 1 
ATOM   7899  N  N   . PHE H  1 20  ? 22.332 -63.728  -43.459  1.00 43.24  ? 21  PHE H N   1 
ATOM   7900  C  CA  . PHE H  1 20  ? 23.553 -64.380  -43.913  1.00 42.92  ? 21  PHE H CA  1 
ATOM   7901  C  C   . PHE H  1 20  ? 24.732 -63.616  -43.401  1.00 44.72  ? 21  PHE H C   1 
ATOM   7902  O  O   . PHE H  1 20  ? 24.643 -62.403  -43.272  1.00 46.26  ? 21  PHE H O   1 
ATOM   7903  C  CB  . PHE H  1 20  ? 23.611 -64.413  -45.429  1.00 42.73  ? 21  PHE H CB  1 
ATOM   7904  C  CG  . PHE H  1 20  ? 22.501 -65.213  -46.060  1.00 41.57  ? 21  PHE H CG  1 
ATOM   7905  C  CD1 . PHE H  1 20  ? 21.249 -64.665  -46.229  1.00 41.82  ? 21  PHE H CD1 1 
ATOM   7906  C  CD2 . PHE H  1 20  ? 22.711 -66.524  -46.485  1.00 40.46  ? 21  PHE H CD2 1 
ATOM   7907  C  CE1 . PHE H  1 20  ? 20.234 -65.404  -46.801  1.00 41.03  ? 21  PHE H CE1 1 
ATOM   7908  C  CE2 . PHE H  1 20  ? 21.698 -67.259  -47.049  1.00 39.37  ? 21  PHE H CE2 1 
ATOM   7909  C  CZ  . PHE H  1 20  ? 20.465 -66.698  -47.211  1.00 39.92  ? 21  PHE H CZ  1 
ATOM   7910  N  N   . GLU H  1 21  ? 25.828 -64.317  -43.104  1.00 45.11  ? 22  GLU H N   1 
ATOM   7911  C  CA  . GLU H  1 21  ? 27.074 -63.668  -42.684  1.00 47.36  ? 22  GLU H CA  1 
ATOM   7912  C  C   . GLU H  1 21  ? 28.303 -64.490  -43.018  1.00 48.00  ? 22  GLU H C   1 
ATOM   7913  O  O   . GLU H  1 21  ? 28.542 -65.530  -42.452  1.00 47.84  ? 22  GLU H O   1 
ATOM   7914  C  CB  . GLU H  1 21  ? 27.056 -63.331  -41.188  1.00 48.70  ? 22  GLU H CB  1 
ATOM   7915  C  CG  . GLU H  1 21  ? 28.326 -62.604  -40.725  1.00 52.06  ? 22  GLU H CG  1 
ATOM   7916  C  CD  . GLU H  1 21  ? 28.236 -62.011  -39.343  1.00 54.28  ? 22  GLU H CD  1 
ATOM   7917  O  OE1 . GLU H  1 21  ? 27.357 -62.441  -38.569  1.00 53.79  ? 22  GLU H OE1 1 
ATOM   7918  O  OE2 . GLU H  1 21  ? 29.064 -61.124  -39.029  1.00 56.92  ? 22  GLU H OE2 1 
ATOM   7919  N  N   . GLN H  1 22  ? 29.098 -63.985  -43.935  1.00 49.39  ? 23  GLN H N   1 
ATOM   7920  C  CA  . GLN H  1 22  ? 30.351 -64.615  -44.313  1.00 51.11  ? 23  GLN H CA  1 
ATOM   7921  C  C   . GLN H  1 22  ? 31.505 -63.765  -43.799  1.00 54.38  ? 23  GLN H C   1 
ATOM   7922  O  O   . GLN H  1 22  ? 31.751 -62.679  -44.313  1.00 55.89  ? 23  GLN H O   1 
ATOM   7923  C  CB  . GLN H  1 22  ? 30.420 -64.760  -45.842  1.00 50.92  ? 23  GLN H CB  1 
ATOM   7924  C  CG  . GLN H  1 22  ? 31.595 -65.569  -46.357  1.00 52.50  ? 23  GLN H CG  1 
ATOM   7925  C  CD  . GLN H  1 22  ? 31.603 -65.696  -47.845  1.00 52.78  ? 23  GLN H CD  1 
ATOM   7926  O  OE1 . GLN H  1 22  ? 31.330 -64.743  -48.563  1.00 53.49  ? 23  GLN H OE1 1 
ATOM   7927  N  NE2 . GLN H  1 22  ? 31.938 -66.877  -48.327  1.00 53.04  ? 23  GLN H NE2 1 
ATOM   7928  N  N   . LYS H  1 23  ? 32.217 -64.244  -42.786  1.00 55.98  ? 24  LYS H N   1 
ATOM   7929  C  CA  . LYS H  1 23  ? 33.303 -63.454  -42.203  1.00 59.64  ? 24  LYS H CA  1 
ATOM   7930  C  C   . LYS H  1 23  ? 34.478 -63.280  -43.153  1.00 62.26  ? 24  LYS H C   1 
ATOM   7931  O  O   . LYS H  1 23  ? 35.134 -62.237  -43.166  1.00 65.18  ? 24  LYS H O   1 
ATOM   7932  C  CB  . LYS H  1 23  ? 33.814 -64.065  -40.914  1.00 61.40  ? 24  LYS H CB  1 
ATOM   7933  C  CG  . LYS H  1 23  ? 32.783 -64.072  -39.792  1.00 60.41  ? 24  LYS H CG  1 
ATOM   7934  C  CD  . LYS H  1 23  ? 33.455 -64.044  -38.401  1.00 63.98  ? 24  LYS H CD  1 
ATOM   7935  C  CE  . LYS H  1 23  ? 32.556 -64.674  -37.315  1.00 62.81  ? 24  LYS H CE  1 
ATOM   7936  N  NZ  . LYS H  1 23  ? 33.297 -64.968  -36.050  1.00 66.26  ? 24  LYS H NZ  1 
ATOM   7937  N  N   . GLU H  1 24  ? 34.754 -64.299  -43.950  1.00 61.80  ? 25  GLU H N   1 
ATOM   7938  C  CA  . GLU H  1 24  ? 35.904 -64.246  -44.855  1.00 64.90  ? 25  GLU H CA  1 
ATOM   7939  C  C   . GLU H  1 24  ? 35.586 -64.788  -46.239  1.00 63.43  ? 25  GLU H C   1 
ATOM   7940  O  O   . GLU H  1 24  ? 34.932 -65.816  -46.370  1.00 61.07  ? 25  GLU H O   1 
ATOM   7941  C  CB  . GLU H  1 24  ? 37.074 -65.002  -44.241  1.00 68.16  ? 25  GLU H CB  1 
ATOM   7942  C  CG  . GLU H  1 24  ? 37.416 -64.471  -42.845  1.00 70.61  ? 25  GLU H CG  1 
ATOM   7943  C  CD  . GLU H  1 24  ? 38.760 -64.958  -42.325  1.00 75.68  ? 25  GLU H CD  1 
ATOM   7944  O  OE1 . GLU H  1 24  ? 39.035 -66.176  -42.473  1.00 76.20  ? 25  GLU H OE1 1 
ATOM   7945  O  OE2 . GLU H  1 24  ? 39.516 -64.126  -41.763  1.00 79.33  ? 25  GLU H OE2 1 
ATOM   7946  N  N   . SER H  1 25  ? 36.064 -64.088  -47.265  1.00 65.48  ? 26  SER H N   1 
ATOM   7947  C  CA  . SER H  1 25  ? 35.698 -64.361  -48.673  1.00 64.75  ? 26  SER H CA  1 
ATOM   7948  C  C   . SER H  1 25  ? 35.810 -65.845  -49.050  1.00 64.18  ? 26  SER H C   1 
ATOM   7949  O  O   . SER H  1 25  ? 34.972 -66.390  -49.777  1.00 61.78  ? 26  SER H O   1 
ATOM   7950  C  CB  . SER H  1 25  ? 36.566 -63.511  -49.603  1.00 68.49  ? 26  SER H CB  1 
ATOM   7951  O  OG  . SER H  1 25  ? 37.914 -63.537  -49.181  1.00 73.03  ? 26  SER H OG  1 
ATOM   7952  N  N   . ASN H  1 26  ? 36.849 -66.486  -48.527  1.00 66.75  ? 27  ASN H N   1 
ATOM   7953  C  CA  . ASN H  1 26  ? 37.114 -67.904  -48.786  1.00 67.10  ? 27  ASN H CA  1 
ATOM   7954  C  C   . ASN H  1 26  ? 36.390 -68.863  -47.807  1.00 64.16  ? 27  ASN H C   1 
ATOM   7955  O  O   . ASN H  1 26  ? 36.526 -70.080  -47.907  1.00 64.46  ? 27  ASN H O   1 
ATOM   7956  C  CB  . ASN H  1 26  ? 38.641 -68.159  -48.749  1.00 72.08  ? 27  ASN H CB  1 
ATOM   7957  C  CG  . ASN H  1 26  ? 39.242 -68.055  -47.319  1.00 74.01  ? 27  ASN H CG  1 
ATOM   7958  O  OD1 . ASN H  1 26  ? 38.977 -67.093  -46.566  1.00 73.27  ? 27  ASN H OD1 1 
ATOM   7959  N  ND2 . ASN H  1 26  ? 40.059 -69.050  -46.953  1.00 76.40  ? 27  ASN H ND2 1 
ATOM   7960  N  N   . GLY H  1 27  ? 35.639 -68.308  -46.861  1.00 61.85  ? 28  GLY H N   1 
ATOM   7961  C  CA  . GLY H  1 27  ? 35.184 -69.061  -45.679  1.00 60.26  ? 28  GLY H CA  1 
ATOM   7962  C  C   . GLY H  1 27  ? 33.724 -69.432  -45.720  1.00 56.05  ? 28  GLY H C   1 
ATOM   7963  O  O   . GLY H  1 27  ? 33.062 -69.157  -46.717  1.00 54.54  ? 28  GLY H O   1 
ATOM   7964  N  N   . PRO H  1 28  ? 33.214 -70.042  -44.633  1.00 54.64  ? 29  PRO H N   1 
ATOM   7965  C  CA  . PRO H  1 28  ? 31.858 -70.524  -44.591  1.00 51.31  ? 29  PRO H CA  1 
ATOM   7966  C  C   . PRO H  1 28  ? 30.889 -69.419  -44.276  1.00 49.52  ? 29  PRO H C   1 
ATOM   7967  O  O   . PRO H  1 28  ? 31.285 -68.404  -43.717  1.00 50.95  ? 29  PRO H O   1 
ATOM   7968  C  CB  . PRO H  1 28  ? 31.882 -71.514  -43.439  1.00 51.67  ? 29  PRO H CB  1 
ATOM   7969  C  CG  . PRO H  1 28  ? 32.829 -70.939  -42.504  1.00 54.50  ? 29  PRO H CG  1 
ATOM   7970  C  CD  . PRO H  1 28  ? 33.883 -70.252  -43.343  1.00 56.95  ? 29  PRO H CD  1 
ATOM   7971  N  N   . VAL H  1 29  ? 29.628 -69.646  -44.630  1.00 46.82  ? 30  VAL H N   1 
ATOM   7972  C  CA  . VAL H  1 29  ? 28.556 -68.678  -44.469  1.00 45.23  ? 30  VAL H CA  1 
ATOM   7973  C  C   . VAL H  1 29  ? 27.597 -69.137  -43.407  1.00 43.86  ? 30  VAL H C   1 
ATOM   7974  O  O   . VAL H  1 29  ? 26.976 -70.173  -43.552  1.00 42.73  ? 30  VAL H O   1 
ATOM   7975  C  CB  . VAL H  1 29  ? 27.741 -68.551  -45.764  1.00 43.93  ? 30  VAL H CB  1 
ATOM   7976  C  CG1 . VAL H  1 29  ? 26.574 -67.610  -45.550  1.00 42.78  ? 30  VAL H CG1 1 
ATOM   7977  C  CG2 . VAL H  1 29  ? 28.632 -68.123  -46.931  1.00 45.56  ? 30  VAL H CG2 1 
ATOM   7978  N  N   . LYS H  1 30  ? 27.465 -68.371  -42.340  1.00 44.55  ? 31  LYS H N   1 
ATOM   7979  C  CA  . LYS H  1 30  ? 26.443 -68.654  -41.325  1.00 43.75  ? 31  LYS H CA  1 
ATOM   7980  C  C   . LYS H  1 30  ? 25.107 -68.139  -41.783  1.00 42.08  ? 31  LYS H C   1 
ATOM   7981  O  O   . LYS H  1 30  ? 24.995 -67.015  -42.225  1.00 42.60  ? 31  LYS H O   1 
ATOM   7982  C  CB  . LYS H  1 30  ? 26.786 -68.025  -39.983  1.00 45.72  ? 31  LYS H CB  1 
ATOM   7983  C  CG  . LYS H  1 30  ? 27.959 -68.710  -39.302  1.00 48.27  ? 31  LYS H CG  1 
ATOM   7984  C  CD  . LYS H  1 30  ? 28.103 -68.326  -37.831  1.00 51.02  ? 31  LYS H CD  1 
ATOM   7985  C  CE  . LYS H  1 30  ? 29.276 -69.074  -37.183  1.00 53.66  ? 31  LYS H CE  1 
ATOM   7986  N  NZ  . LYS H  1 30  ? 29.384 -68.859  -35.710  1.00 56.49  ? 31  LYS H NZ  1 
ATOM   7987  N  N   . VAL H  1 31  ? 24.096 -68.978  -41.678  1.00 40.83  ? 32  VAL H N   1 
ATOM   7988  C  CA  . VAL H  1 31  ? 22.734 -68.625  -42.075  1.00 39.93  ? 32  VAL H CA  1 
ATOM   7989  C  C   . VAL H  1 31  ? 21.831 -68.747  -40.867  1.00 40.36  ? 32  VAL H C   1 
ATOM   7990  O  O   . VAL H  1 31  ? 21.762 -69.805  -40.259  1.00 40.62  ? 32  VAL H O   1 
ATOM   7991  C  CB  . VAL H  1 31  ? 22.202 -69.569  -43.161  1.00 38.61  ? 32  VAL H CB  1 
ATOM   7992  C  CG1 . VAL H  1 31  ? 20.821 -69.123  -43.627  1.00 38.01  ? 32  VAL H CG1 1 
ATOM   7993  C  CG2 . VAL H  1 31  ? 23.181 -69.639  -44.318  1.00 38.91  ? 32  VAL H CG2 1 
ATOM   7994  N  N   . TRP H  1 32  ? 21.151 -67.682  -40.486  1.00 41.06  ? 33  TRP H N   1 
ATOM   7995  C  CA  . TRP H  1 32  ? 20.279 -67.783  -39.328  1.00 42.03  ? 33  TRP H CA  1 
ATOM   7996  C  C   . TRP H  1 32  ? 19.108 -66.851  -39.430  1.00 42.67  ? 33  TRP H C   1 
ATOM   7997  O  O   . TRP H  1 32  ? 19.130 -65.882  -40.167  1.00 42.99  ? 33  TRP H O   1 
ATOM   7998  C  CB  . TRP H  1 32  ? 21.055 -67.539  -38.029  1.00 43.88  ? 33  TRP H CB  1 
ATOM   7999  C  CG  . TRP H  1 32  ? 21.177 -66.095  -37.658  1.00 45.64  ? 33  TRP H CG  1 
ATOM   8000  C  CD1 . TRP H  1 32  ? 20.418 -65.414  -36.746  1.00 47.58  ? 33  TRP H CD1 1 
ATOM   8001  C  CD2 . TRP H  1 32  ? 22.104 -65.147  -38.191  1.00 45.94  ? 33  TRP H CD2 1 
ATOM   8002  N  NE1 . TRP H  1 32  ? 20.812 -64.102  -36.683  1.00 48.77  ? 33  TRP H NE1 1 
ATOM   8003  C  CE2 . TRP H  1 32  ? 21.841 -63.909  -37.565  1.00 47.90  ? 33  TRP H CE2 1 
ATOM   8004  C  CE3 . TRP H  1 32  ? 23.133 -65.224  -39.127  1.00 45.53  ? 33  TRP H CE3 1 
ATOM   8005  C  CZ2 . TRP H  1 32  ? 22.573 -62.759  -37.844  1.00 49.41  ? 33  TRP H CZ2 1 
ATOM   8006  C  CZ3 . TRP H  1 32  ? 23.854 -64.080  -39.412  1.00 47.05  ? 33  TRP H CZ3 1 
ATOM   8007  C  CH2 . TRP H  1 32  ? 23.575 -62.864  -38.770  1.00 48.88  ? 33  TRP H CH2 1 
ATOM   8008  N  N   . GLY H  1 33  ? 18.073 -67.166  -38.676  1.00 43.48  ? 34  GLY H N   1 
ATOM   8009  C  CA  . GLY H  1 33  ? 16.860 -66.358  -38.655  1.00 44.85  ? 34  GLY H CA  1 
ATOM   8010  C  C   . GLY H  1 33  ? 15.661 -67.123  -38.132  1.00 45.66  ? 34  GLY H C   1 
ATOM   8011  O  O   . GLY H  1 33  ? 15.809 -68.177  -37.521  1.00 45.68  ? 34  GLY H O   1 
ATOM   8012  N  N   . SER H  1 34  ? 14.469 -66.594  -38.384  1.00 46.90  ? 35  SER H N   1 
ATOM   8013  C  CA  . SER H  1 34  ? 13.239 -67.194  -37.873  1.00 48.41  ? 35  SER H CA  1 
ATOM   8014  C  C   . SER H  1 34  ? 12.096 -67.154  -38.885  1.00 48.91  ? 35  SER H C   1 
ATOM   8015  O  O   . SER H  1 34  ? 11.669 -66.076  -39.291  1.00 50.19  ? 35  SER H O   1 
ATOM   8016  C  CB  . SER H  1 34  ? 12.810 -66.486  -36.604  1.00 51.24  ? 35  SER H CB  1 
ATOM   8017  O  OG  . SER H  1 34  ? 11.770 -67.207  -35.984  1.00 53.06  ? 35  SER H OG  1 
ATOM   8018  N  N   . ILE H  1 35  ? 11.631 -68.339  -39.302  1.00 48.30  ? 36  ILE H N   1 
ATOM   8019  C  CA  . ILE H  1 35  ? 10.475 -68.477  -40.201  1.00 49.29  ? 36  ILE H CA  1 
ATOM   8020  C  C   . ILE H  1 35  ? 9.300  -68.975  -39.393  1.00 51.95  ? 36  ILE H C   1 
ATOM   8021  O  O   . ILE H  1 35  ? 9.474  -69.800  -38.491  1.00 51.82  ? 36  ILE H O   1 
ATOM   8022  C  CB  . ILE H  1 35  ? 10.699 -69.486  -41.337  1.00 47.29  ? 36  ILE H CB  1 
ATOM   8023  C  CG1 . ILE H  1 35  ? 11.965 -69.162  -42.119  1.00 45.22  ? 36  ILE H CG1 1 
ATOM   8024  C  CG2 . ILE H  1 35  ? 9.527  -69.478  -42.292  1.00 48.77  ? 36  ILE H CG2 1 
ATOM   8025  C  CD1 . ILE H  1 35  ? 12.273 -70.158  -43.203  1.00 43.93  ? 36  ILE H CD1 1 
ATOM   8026  N  N   . LYS H  1 36  ? 8.109  -68.464  -39.721  1.00 54.72  ? 37  LYS H N   1 
ATOM   8027  C  CA  . LYS H  1 36  ? 6.870  -68.827  -39.016  1.00 57.95  ? 37  LYS H CA  1 
ATOM   8028  C  C   . LYS H  1 36  ? 5.649  -69.023  -39.930  1.00 60.13  ? 37  LYS H C   1 
ATOM   8029  O  O   . LYS H  1 36  ? 5.670  -68.678  -41.109  1.00 59.63  ? 37  LYS H O   1 
ATOM   8030  C  CB  . LYS H  1 36  ? 6.540  -67.795  -37.944  1.00 60.88  ? 37  LYS H CB  1 
ATOM   8031  C  CG  . LYS H  1 36  ? 6.321  -66.383  -38.452  1.00 62.60  ? 37  LYS H CG  1 
ATOM   8032  C  CD  . LYS H  1 36  ? 5.513  -65.576  -37.425  1.00 67.27  ? 37  LYS H CD  1 
ATOM   8033  C  CE  . LYS H  1 36  ? 5.369  -64.107  -37.821  1.00 69.19  ? 37  LYS H CE  1 
ATOM   8034  N  NZ  . LYS H  1 36  ? 4.376  -63.407  -36.949  1.00 73.97  ? 37  LYS H NZ  1 
ATOM   8035  N  N   . GLY H  1 37  ? 4.586  -69.589  -39.367  1.00 63.12  ? 38  GLY H N   1 
ATOM   8036  C  CA  . GLY H  1 37  ? 3.399  -69.993  -40.142  1.00 65.76  ? 38  GLY H CA  1 
ATOM   8037  C  C   . GLY H  1 37  ? 3.563  -71.346  -40.842  1.00 63.91  ? 38  GLY H C   1 
ATOM   8038  O  O   . GLY H  1 37  ? 2.813  -71.672  -41.783  1.00 65.26  ? 38  GLY H O   1 
ATOM   8039  N  N   . LEU H  1 38  ? 4.546  -72.129  -40.360  1.00 61.05  ? 39  LEU H N   1 
ATOM   8040  C  CA  . LEU H  1 38  ? 4.979  -73.394  -40.992  1.00 58.74  ? 39  LEU H CA  1 
ATOM   8041  C  C   . LEU H  1 38  ? 4.295  -74.606  -40.380  1.00 60.60  ? 39  LEU H C   1 
ATOM   8042  O  O   . LEU H  1 38  ? 4.100  -74.681  -39.158  1.00 61.96  ? 39  LEU H O   1 
ATOM   8043  C  CB  . LEU H  1 38  ? 6.510  -73.585  -40.892  1.00 54.68  ? 39  LEU H CB  1 
ATOM   8044  C  CG  . LEU H  1 38  ? 7.361  -72.888  -41.952  1.00 52.03  ? 39  LEU H CG  1 
ATOM   8045  C  CD1 . LEU H  1 38  ? 8.790  -72.847  -41.537  1.00 48.96  ? 39  LEU H CD1 1 
ATOM   8046  C  CD2 . LEU H  1 38  ? 7.208  -73.586  -43.290  1.00 51.78  ? 39  LEU H CD2 1 
ATOM   8047  N  N   . THR H  1 39  ? 3.946  -75.551  -41.252  1.00 60.80  ? 40  THR H N   1 
ATOM   8048  C  CA  . THR H  1 39  ? 3.355  -76.818  -40.824  1.00 62.67  ? 40  THR H CA  1 
ATOM   8049  C  C   . THR H  1 39  ? 4.410  -77.559  -39.990  1.00 60.23  ? 40  THR H C   1 
ATOM   8050  O  O   . THR H  1 39  ? 5.576  -77.613  -40.369  1.00 56.72  ? 40  THR H O   1 
ATOM   8051  C  CB  . THR H  1 39  ? 2.863  -77.685  -42.035  1.00 63.40  ? 40  THR H CB  1 
ATOM   8052  O  OG1 . THR H  1 39  ? 3.803  -78.729  -42.321  1.00 60.89  ? 40  THR H OG1 1 
ATOM   8053  C  CG2 . THR H  1 39  ? 2.675  -76.855  -43.290  1.00 63.50  ? 40  THR H CG2 1 
ATOM   8054  N  N   . GLU H  1 40  ? 4.007  -78.122  -38.856  1.00 62.56  ? 41  GLU H N   1 
ATOM   8055  C  CA  . GLU H  1 40  ? 4.981  -78.750  -37.959  1.00 61.14  ? 41  GLU H CA  1 
ATOM   8056  C  C   . GLU H  1 40  ? 5.824  -79.794  -38.677  1.00 58.37  ? 41  GLU H C   1 
ATOM   8057  O  O   . GLU H  1 40  ? 5.314  -80.599  -39.435  1.00 59.13  ? 41  GLU H O   1 
ATOM   8058  C  CB  . GLU H  1 40  ? 4.326  -79.413  -36.736  1.00 64.80  ? 41  GLU H CB  1 
ATOM   8059  C  CG  . GLU H  1 40  ? 5.386  -80.101  -35.811  1.00 63.92  ? 41  GLU H CG  1 
ATOM   8060  C  CD  . GLU H  1 40  ? 4.818  -80.887  -34.666  1.00 68.11  ? 41  GLU H CD  1 
ATOM   8061  O  OE1 . GLU H  1 40  ? 3.961  -81.732  -34.923  1.00 70.50  ? 41  GLU H OE1 1 
ATOM   8062  O  OE2 . GLU H  1 40  ? 5.263  -80.718  -33.516  1.00 68.98  ? 41  GLU H OE2 1 
ATOM   8063  N  N   . GLY H  1 41  ? 7.122  -79.774  -38.417  1.00 55.67  ? 42  GLY H N   1 
ATOM   8064  C  CA  . GLY H  1 41  ? 8.035  -80.779  -38.948  1.00 53.62  ? 42  GLY H CA  1 
ATOM   8065  C  C   . GLY H  1 41  ? 9.085  -80.215  -39.887  1.00 50.38  ? 42  GLY H C   1 
ATOM   8066  O  O   . GLY H  1 41  ? 9.388  -79.035  -39.846  1.00 49.46  ? 42  GLY H O   1 
ATOM   8067  N  N   . LEU H  1 42  ? 9.633  -81.072  -40.741  1.00 49.04  ? 43  LEU H N   1 
ATOM   8068  C  CA  . LEU H  1 42  ? 10.734 -80.699  -41.638  1.00 46.32  ? 43  LEU H CA  1 
ATOM   8069  C  C   . LEU H  1 42  ? 10.254 -79.930  -42.845  1.00 46.01  ? 43  LEU H C   1 
ATOM   8070  O  O   . LEU H  1 42  ? 9.181  -80.184  -43.347  1.00 47.98  ? 43  LEU H O   1 
ATOM   8071  C  CB  . LEU H  1 42  ? 11.505 -81.936  -42.112  1.00 45.70  ? 43  LEU H CB  1 
ATOM   8072  C  CG  . LEU H  1 42  ? 12.483 -82.550  -41.113  1.00 45.42  ? 43  LEU H CG  1 
ATOM   8073  C  CD1 . LEU H  1 42  ? 11.991 -83.923  -40.603  1.00 47.85  ? 43  LEU H CD1 1 
ATOM   8074  C  CD2 . LEU H  1 42  ? 13.829 -82.668  -41.757  1.00 43.68  ? 43  LEU H CD2 1 
ATOM   8075  N  N   . HIS H  1 43  ? 11.076 -79.005  -43.315  1.00 44.10  ? 44  HIS H N   1 
ATOM   8076  C  CA  . HIS H  1 43  ? 10.803 -78.275  -44.543  1.00 44.06  ? 44  HIS H CA  1 
ATOM   8077  C  C   . HIS H  1 43  ? 12.049 -78.085  -45.391  1.00 42.05  ? 44  HIS H C   1 
ATOM   8078  O  O   . HIS H  1 43  ? 13.112 -77.788  -44.894  1.00 40.76  ? 44  HIS H O   1 
ATOM   8079  C  CB  . HIS H  1 43  ? 10.188 -76.922  -44.234  1.00 44.92  ? 44  HIS H CB  1 
ATOM   8080  C  CG  . HIS H  1 43  ? 8.786  -77.004  -43.736  1.00 47.60  ? 44  HIS H CG  1 
ATOM   8081  N  ND1 . HIS H  1 43  ? 7.708  -77.098  -44.584  1.00 50.02  ? 44  HIS H ND1 1 
ATOM   8082  C  CD2 . HIS H  1 43  ? 8.283  -77.007  -42.480  1.00 49.13  ? 44  HIS H CD2 1 
ATOM   8083  C  CE1 . HIS H  1 43  ? 6.597  -77.154  -43.868  1.00 52.93  ? 44  HIS H CE1 1 
ATOM   8084  N  NE2 . HIS H  1 43  ? 6.920  -77.100  -42.588  1.00 52.29  ? 44  HIS H NE2 1 
ATOM   8085  N  N   . GLY H  1 44  ? 11.895 -78.272  -46.687  1.00 42.40  ? 45  GLY H N   1 
ATOM   8086  C  CA  . GLY H  1 44  ? 12.967 -78.056  -47.632  1.00 41.24  ? 45  GLY H CA  1 
ATOM   8087  C  C   . GLY H  1 44  ? 13.347 -76.613  -47.625  1.00 40.47  ? 45  GLY H C   1 
ATOM   8088  O  O   . GLY H  1 44  ? 12.536 -75.769  -47.327  1.00 41.39  ? 45  GLY H O   1 
ATOM   8089  N  N   . PHE H  1 45  ? 14.594 -76.336  -47.957  1.00 39.36  ? 46  PHE H N   1 
ATOM   8090  C  CA  . PHE H  1 45  ? 15.156 -75.003  -47.776  1.00 38.75  ? 46  PHE H CA  1 
ATOM   8091  C  C   . PHE H  1 45  ? 16.307 -74.779  -48.724  1.00 38.29  ? 46  PHE H C   1 
ATOM   8092  O  O   . PHE H  1 45  ? 17.414 -75.199  -48.442  1.00 37.62  ? 46  PHE H O   1 
ATOM   8093  C  CB  . PHE H  1 45  ? 15.646 -74.884  -46.328  1.00 38.08  ? 46  PHE H CB  1 
ATOM   8094  C  CG  . PHE H  1 45  ? 16.033 -73.489  -45.909  1.00 37.85  ? 46  PHE H CG  1 
ATOM   8095  C  CD1 . PHE H  1 45  ? 15.173 -72.430  -46.106  1.00 38.90  ? 46  PHE H CD1 1 
ATOM   8096  C  CD2 . PHE H  1 45  ? 17.240 -73.249  -45.272  1.00 37.11  ? 46  PHE H CD2 1 
ATOM   8097  C  CE1 . PHE H  1 45  ? 15.521 -71.163  -45.709  1.00 39.03  ? 46  PHE H CE1 1 
ATOM   8098  C  CE2 . PHE H  1 45  ? 17.591 -71.986  -44.875  1.00 37.34  ? 46  PHE H CE2 1 
ATOM   8099  C  CZ  . PHE H  1 45  ? 16.732 -70.941  -45.092  1.00 38.38  ? 46  PHE H CZ  1 
ATOM   8100  N  N   . HIS H  1 46  ? 16.055 -74.106  -49.837  1.00 39.19  ? 47  HIS H N   1 
ATOM   8101  C  CA  . HIS H  1 46  ? 17.060 -73.993  -50.890  1.00 39.52  ? 47  HIS H CA  1 
ATOM   8102  C  C   . HIS H  1 46  ? 17.217 -72.591  -51.477  1.00 40.40  ? 47  HIS H C   1 
ATOM   8103  O  O   . HIS H  1 46  ? 16.278 -71.795  -51.469  1.00 41.33  ? 47  HIS H O   1 
ATOM   8104  C  CB  . HIS H  1 46  ? 16.712 -74.943  -52.013  1.00 40.72  ? 47  HIS H CB  1 
ATOM   8105  C  CG  . HIS H  1 46  ? 16.204 -76.259  -51.542  1.00 40.42  ? 47  HIS H CG  1 
ATOM   8106  N  ND1 . HIS H  1 46  ? 14.873 -76.593  -51.581  1.00 41.76  ? 47  HIS H ND1 1 
ATOM   8107  C  CD2 . HIS H  1 46  ? 16.839 -77.326  -51.010  1.00 40.22  ? 47  HIS H CD2 1 
ATOM   8108  C  CE1 . HIS H  1 46  ? 14.706 -77.813  -51.103  1.00 41.67  ? 47  HIS H CE1 1 
ATOM   8109  N  NE2 . HIS H  1 46  ? 15.885 -78.279  -50.741  1.00 40.66  ? 47  HIS H NE2 1 
ATOM   8110  N  N   . VAL H  1 47  ? 18.416 -72.314  -51.992  1.00 40.45  ? 48  VAL H N   1 
ATOM   8111  C  CA  . VAL H  1 47  ? 18.670 -71.105  -52.766  1.00 41.68  ? 48  VAL H CA  1 
ATOM   8112  C  C   . VAL H  1 47  ? 18.444 -71.413  -54.219  1.00 43.75  ? 48  VAL H C   1 
ATOM   8113  O  O   . VAL H  1 47  ? 19.142 -72.259  -54.765  1.00 44.15  ? 48  VAL H O   1 
ATOM   8114  C  CB  . VAL H  1 47  ? 20.106 -70.633  -52.638  1.00 41.39  ? 48  VAL H CB  1 
ATOM   8115  C  CG1 . VAL H  1 47  ? 20.400 -69.559  -53.654  1.00 43.14  ? 48  VAL H CG1 1 
ATOM   8116  C  CG2 . VAL H  1 47  ? 20.348 -70.122  -51.257  1.00 40.38  ? 48  VAL H CG2 1 
ATOM   8117  N  N   . HIS H  1 48  ? 17.477 -70.734  -54.841  1.00 45.54  ? 49  HIS H N   1 
ATOM   8118  C  CA  . HIS H  1 48  ? 17.164 -70.926  -56.271  1.00 48.23  ? 49  HIS H CA  1 
ATOM   8119  C  C   . HIS H  1 48  ? 17.908 -69.935  -57.160  1.00 50.19  ? 49  HIS H C   1 
ATOM   8120  O  O   . HIS H  1 48  ? 18.436 -68.935  -56.686  1.00 49.84  ? 49  HIS H O   1 
ATOM   8121  C  CB  . HIS H  1 48  ? 15.687 -70.798  -56.523  1.00 49.86  ? 49  HIS H CB  1 
ATOM   8122  C  CG  . HIS H  1 48  ? 14.887 -71.930  -55.971  1.00 49.18  ? 49  HIS H CG  1 
ATOM   8123  N  ND1 . HIS H  1 48  ? 14.030 -72.682  -56.746  1.00 51.34  ? 49  HIS H ND1 1 
ATOM   8124  C  CD2 . HIS H  1 48  ? 14.789 -72.422  -54.715  1.00 46.63  ? 49  HIS H CD2 1 
ATOM   8125  C  CE1 . HIS H  1 48  ? 13.436 -73.586  -55.989  1.00 50.19  ? 49  HIS H CE1 1 
ATOM   8126  N  NE2 . HIS H  1 48  ? 13.879 -73.449  -54.753  1.00 47.44  ? 49  HIS H NE2 1 
ATOM   8127  N  N   . GLU H  1 49  ? 17.945 -70.224  -58.456  1.00 52.81  ? 50  GLU H N   1 
ATOM   8128  C  CA  . GLU H  1 49  ? 18.849 -69.534  -59.399  1.00 54.91  ? 50  GLU H CA  1 
ATOM   8129  C  C   . GLU H  1 49  ? 18.570 -68.066  -59.535  1.00 56.26  ? 50  GLU H C   1 
ATOM   8130  O  O   . GLU H  1 49  ? 19.475 -67.264  -59.398  1.00 56.03  ? 50  GLU H O   1 
ATOM   8131  C  CB  . GLU H  1 49  ? 18.778 -70.181  -60.790  1.00 58.22  ? 50  GLU H CB  1 
ATOM   8132  C  CG  . GLU H  1 49  ? 19.825 -69.678  -61.778  1.00 60.79  ? 50  GLU H CG  1 
ATOM   8133  C  CD  . GLU H  1 49  ? 19.892 -70.499  -63.057  1.00 63.87  ? 50  GLU H CD  1 
ATOM   8134  O  OE1 . GLU H  1 49  ? 19.336 -71.608  -63.111  1.00 63.28  ? 50  GLU H OE1 1 
ATOM   8135  O  OE2 . GLU H  1 49  ? 20.504 -70.021  -64.025  1.00 67.27  ? 50  GLU H OE2 1 
ATOM   8136  N  N   . PHE H  1 50  ? 17.311 -67.732  -59.804  1.00 58.06  ? 51  PHE H N   1 
ATOM   8137  C  CA  . PHE H  1 50  ? 16.927 -66.354  -60.166  1.00 60.71  ? 51  PHE H CA  1 
ATOM   8138  C  C   . PHE H  1 50  ? 16.293 -65.517  -59.054  1.00 59.46  ? 51  PHE H C   1 
ATOM   8139  O  O   . PHE H  1 50  ? 15.420 -65.989  -58.318  1.00 58.04  ? 51  PHE H O   1 
ATOM   8140  C  CB  . PHE H  1 50  ? 15.975 -66.367  -61.356  1.00 64.70  ? 51  PHE H CB  1 
ATOM   8141  C  CG  . PHE H  1 50  ? 16.502 -67.127  -62.526  1.00 66.94  ? 51  PHE H CG  1 
ATOM   8142  C  CD1 . PHE H  1 50  ? 17.722 -66.775  -63.114  1.00 67.99  ? 51  PHE H CD1 1 
ATOM   8143  C  CD2 . PHE H  1 50  ? 15.791 -68.214  -63.034  1.00 68.44  ? 51  PHE H CD2 1 
ATOM   8144  C  CE1 . PHE H  1 50  ? 18.219 -67.487  -64.190  1.00 70.54  ? 51  PHE H CE1 1 
ATOM   8145  C  CE2 . PHE H  1 50  ? 16.283 -68.942  -64.114  1.00 70.65  ? 51  PHE H CE2 1 
ATOM   8146  C  CZ  . PHE H  1 50  ? 17.500 -68.578  -64.694  1.00 71.81  ? 51  PHE H CZ  1 
ATOM   8147  N  N   . GLY H  1 51  ? 16.728 -64.258  -58.966  1.00 60.37  ? 52  GLY H N   1 
ATOM   8148  C  CA  . GLY H  1 51  ? 16.107 -63.281  -58.083  1.00 60.30  ? 52  GLY H CA  1 
ATOM   8149  C  C   . GLY H  1 51  ? 14.899 -62.641  -58.740  1.00 64.18  ? 52  GLY H C   1 
ATOM   8150  O  O   . GLY H  1 51  ? 14.709 -61.432  -58.663  1.00 66.06  ? 52  GLY H O   1 
ATOM   8151  N  N   . ASP H  1 52  ? 14.070 -63.473  -59.369  1.00 65.70  ? 53  ASP H N   1 
ATOM   8152  C  CA  . ASP H  1 52  ? 12.892 -63.038  -60.119  1.00 69.93  ? 53  ASP H CA  1 
ATOM   8153  C  C   . ASP H  1 52  ? 11.646 -63.356  -59.303  1.00 69.43  ? 53  ASP H C   1 
ATOM   8154  O  O   . ASP H  1 52  ? 11.413 -64.490  -58.932  1.00 67.33  ? 53  ASP H O   1 
ATOM   8155  C  CB  . ASP H  1 52  ? 12.862 -63.762  -61.476  1.00 72.74  ? 53  ASP H CB  1 
ATOM   8156  C  CG  . ASP H  1 52  ? 11.832 -63.202  -62.425  1.00 78.19  ? 53  ASP H CG  1 
ATOM   8157  O  OD1 . ASP H  1 52  ? 10.753 -62.784  -61.958  1.00 79.67  ? 53  ASP H OD1 1 
ATOM   8158  O  OD2 . ASP H  1 52  ? 12.103 -63.192  -63.645  1.00 81.49  ? 53  ASP H OD2 1 
ATOM   8159  N  N   . ASN H  1 53  ? 10.856 -62.339  -59.020  1.00 71.89  ? 54  ASN H N   1 
ATOM   8160  C  CA  . ASN H  1 53  ? 9.602  -62.525  -58.286  1.00 72.67  ? 54  ASN H CA  1 
ATOM   8161  C  C   . ASN H  1 53  ? 8.365  -62.122  -59.103  1.00 78.13  ? 54  ASN H C   1 
ATOM   8162  O  O   . ASN H  1 53  ? 7.266  -61.957  -58.558  1.00 79.68  ? 54  ASN H O   1 
ATOM   8163  C  CB  . ASN H  1 53  ? 9.641  -61.728  -56.990  1.00 71.10  ? 54  ASN H CB  1 
ATOM   8164  C  CG  . ASN H  1 53  ? 9.205  -62.554  -55.796  1.00 68.66  ? 54  ASN H CG  1 
ATOM   8165  O  OD1 . ASN H  1 53  ? 9.887  -63.515  -55.430  1.00 65.47  ? 54  ASN H OD1 1 
ATOM   8166  N  ND2 . ASN H  1 53  ? 8.073  -62.194  -55.185  1.00 70.72  ? 54  ASN H ND2 1 
ATOM   8167  N  N   . THR H  1 54  ? 8.576  -61.971  -60.411  1.00 81.23  ? 55  THR H N   1 
ATOM   8168  C  CA  . THR H  1 54  ? 7.558  -61.545  -61.371  1.00 87.31  ? 55  THR H CA  1 
ATOM   8169  C  C   . THR H  1 54  ? 6.244  -62.270  -61.145  1.00 89.12  ? 55  THR H C   1 
ATOM   8170  O  O   . THR H  1 54  ? 5.250  -61.671  -60.757  1.00 92.00  ? 55  THR H O   1 
ATOM   8171  C  CB  . THR H  1 54  ? 8.049  -61.819  -62.826  1.00 89.94  ? 55  THR H CB  1 
ATOM   8172  O  OG1 . THR H  1 54  ? 9.117  -60.930  -63.142  1.00 89.83  ? 55  THR H OG1 1 
ATOM   8173  C  CG2 . THR H  1 54  ? 6.930  -61.666  -63.864  1.00 96.74  ? 55  THR H CG2 1 
ATOM   8174  N  N   . ALA H  1 55  ? 6.268  -63.573  -61.391  1.00 87.71  ? 56  ALA H N   1 
ATOM   8175  C  CA  . ALA H  1 55  ? 5.099  -64.432  -61.246  1.00 89.55  ? 56  ALA H CA  1 
ATOM   8176  C  C   . ALA H  1 55  ? 5.178  -65.228  -59.943  1.00 84.53  ? 56  ALA H C   1 
ATOM   8177  O  O   . ALA H  1 55  ? 4.960  -66.439  -59.927  1.00 83.58  ? 56  ALA H O   1 
ATOM   8178  C  CB  . ALA H  1 55  ? 4.982  -65.375  -62.456  1.00 92.14  ? 56  ALA H CB  1 
ATOM   8179  N  N   . GLY H  1 56  ? 5.488  -64.528  -58.854  1.00 81.83  ? 57  GLY H N   1 
ATOM   8180  C  CA  . GLY H  1 56  ? 5.554  -65.125  -57.518  1.00 77.59  ? 57  GLY H CA  1 
ATOM   8181  C  C   . GLY H  1 56  ? 6.878  -65.827  -57.281  1.00 72.38  ? 57  GLY H C   1 
ATOM   8182  O  O   . GLY H  1 56  ? 7.912  -65.415  -57.825  1.00 71.38  ? 57  GLY H O   1 
ATOM   8183  N  N   . CYS H  1 57  ? 6.833  -66.901  -56.479  1.00 69.50  ? 58  CYS H N   1 
ATOM   8184  C  CA  . CYS H  1 57  ? 8.018  -67.748  -56.212  1.00 64.76  ? 58  CYS H CA  1 
ATOM   8185  C  C   . CYS H  1 57  ? 8.420  -68.606  -57.411  1.00 65.30  ? 58  CYS H C   1 
ATOM   8186  O  O   . CYS H  1 57  ? 9.582  -68.961  -57.552  1.00 62.57  ? 58  CYS H O   1 
ATOM   8187  C  CB  . CYS H  1 57  ? 7.782  -68.652  -54.999  1.00 62.07  ? 58  CYS H CB  1 
ATOM   8188  S  SG  . CYS H  1 57  ? 7.736  -67.794  -53.410  1.00 60.60  ? 58  CYS H SG  1 
ATOM   8189  N  N   . THR H  1 58  ? 7.455  -68.930  -58.265  1.00 69.27  ? 59  THR H N   1 
ATOM   8190  C  CA  . THR H  1 58  ? 7.699  -69.811  -59.398  1.00 70.69  ? 59  THR H CA  1 
ATOM   8191  C  C   . THR H  1 58  ? 8.738  -69.252  -60.338  1.00 71.15  ? 59  THR H C   1 
ATOM   8192  O  O   . THR H  1 58  ? 9.453  -70.004  -60.987  1.00 70.72  ? 59  THR H O   1 
ATOM   8193  C  CB  . THR H  1 58  ? 6.443  -70.054  -60.223  1.00 75.96  ? 59  THR H CB  1 
ATOM   8194  O  OG1 . THR H  1 58  ? 5.336  -70.281  -59.346  1.00 76.69  ? 59  THR H OG1 1 
ATOM   8195  C  CG2 . THR H  1 58  ? 6.639  -71.280  -61.144  1.00 76.96  ? 59  THR H CG2 1 
ATOM   8196  N  N   . SER H  1 59  ? 8.799  -67.931  -60.422  1.00 72.58  ? 60  SER H N   1 
ATOM   8197  C  CA  . SER H  1 59  ? 9.753  -67.228  -61.307  1.00 73.77  ? 60  SER H CA  1 
ATOM   8198  C  C   . SER H  1 59  ? 11.229 -67.422  -60.937  1.00 69.44  ? 60  SER H C   1 
ATOM   8199  O  O   . SER H  1 59  ? 12.119 -67.224  -61.766  1.00 70.34  ? 60  SER H O   1 
ATOM   8200  C  CB  . SER H  1 59  ? 9.447  -65.735  -61.280  1.00 76.18  ? 60  SER H CB  1 
ATOM   8201  O  OG  . SER H  1 59  ? 8.042  -65.510  -61.334  1.00 80.35  ? 60  SER H OG  1 
ATOM   8202  N  N   . ALA H  1 60  ? 11.463 -67.801  -59.682  1.00 65.28  ? 61  ALA H N   1 
ATOM   8203  C  CA  . ALA H  1 60  ? 12.809 -68.030  -59.144  1.00 61.40  ? 61  ALA H CA  1 
ATOM   8204  C  C   . ALA H  1 60  ? 13.595 -69.111  -59.882  1.00 61.18  ? 61  ALA H C   1 
ATOM   8205  O  O   . ALA H  1 60  ? 14.829 -69.187  -59.768  1.00 59.16  ? 61  ALA H O   1 
ATOM   8206  C  CB  . ALA H  1 60  ? 12.710 -68.389  -57.671  1.00 57.79  ? 61  ALA H CB  1 
ATOM   8207  N  N   . GLY H  1 61  ? 12.868 -69.959  -60.611  1.00 63.54  ? 62  GLY H N   1 
ATOM   8208  C  CA  . GLY H  1 61  ? 13.461 -71.042  -61.385  1.00 64.00  ? 62  GLY H CA  1 
ATOM   8209  C  C   . GLY H  1 61  ? 13.864 -72.203  -60.499  1.00 60.40  ? 62  GLY H C   1 
ATOM   8210  O  O   . GLY H  1 61  ? 13.316 -72.378  -59.410  1.00 58.16  ? 62  GLY H O   1 
ATOM   8211  N  N   . PRO H  1 62  ? 14.835 -73.003  -60.964  1.00 60.20  ? 63  PRO H N   1 
ATOM   8212  C  CA  . PRO H  1 62  ? 15.250 -74.189  -60.246  1.00 57.55  ? 63  PRO H CA  1 
ATOM   8213  C  C   . PRO H  1 62  ? 16.292 -73.914  -59.166  1.00 54.07  ? 63  PRO H C   1 
ATOM   8214  O  O   . PRO H  1 62  ? 16.644 -72.761  -58.911  1.00 53.47  ? 63  PRO H O   1 
ATOM   8215  C  CB  . PRO H  1 62  ? 15.868 -75.038  -61.345  1.00 59.70  ? 63  PRO H CB  1 
ATOM   8216  C  CG  . PRO H  1 62  ? 16.482 -74.054  -62.244  1.00 61.77  ? 63  PRO H CG  1 
ATOM   8217  C  CD  . PRO H  1 62  ? 15.573 -72.867  -62.235  1.00 63.03  ? 63  PRO H CD  1 
ATOM   8218  N  N   . HIS H  1 63  ? 16.741 -74.991  -58.526  1.00 52.09  ? 64  HIS H N   1 
ATOM   8219  C  CA  . HIS H  1 63  ? 17.792 -74.936  -57.512  1.00 49.25  ? 64  HIS H CA  1 
ATOM   8220  C  C   . HIS H  1 63  ? 19.045 -74.350  -58.120  1.00 50.00  ? 64  HIS H C   1 
ATOM   8221  O  O   . HIS H  1 63  ? 19.419 -74.708  -59.225  1.00 52.39  ? 64  HIS H O   1 
ATOM   8222  C  CB  . HIS H  1 63  ? 18.101 -76.337  -57.001  1.00 48.18  ? 64  HIS H CB  1 
ATOM   8223  C  CG  . HIS H  1 63  ? 17.037 -76.913  -56.125  1.00 46.98  ? 64  HIS H CG  1 
ATOM   8224  N  ND1 . HIS H  1 63  ? 17.317 -77.785  -55.094  1.00 45.14  ? 64  HIS H ND1 1 
ATOM   8225  C  CD2 . HIS H  1 63  ? 15.691 -76.757  -56.131  1.00 47.84  ? 64  HIS H CD2 1 
ATOM   8226  C  CE1 . HIS H  1 63  ? 16.191 -78.135  -54.496  1.00 44.98  ? 64  HIS H CE1 1 
ATOM   8227  N  NE2 . HIS H  1 63  ? 15.190 -77.526  -55.104  1.00 46.56  ? 64  HIS H NE2 1 
ATOM   8228  N  N   . PHE H  1 64  ? 19.697 -73.455  -57.403  1.00 48.45  ? 65  PHE H N   1 
ATOM   8229  C  CA  . PHE H  1 64  ? 20.909 -72.822  -57.917  1.00 49.76  ? 65  PHE H CA  1 
ATOM   8230  C  C   . PHE H  1 64  ? 21.987 -73.887  -58.113  1.00 50.21  ? 65  PHE H C   1 
ATOM   8231  O  O   . PHE H  1 64  ? 22.418 -74.527  -57.156  1.00 48.25  ? 65  PHE H O   1 
ATOM   8232  C  CB  . PHE H  1 64  ? 21.395 -71.715  -56.971  1.00 48.37  ? 65  PHE H CB  1 
ATOM   8233  C  CG  . PHE H  1 64  ? 22.658 -71.006  -57.424  1.00 49.67  ? 65  PHE H CG  1 
ATOM   8234  C  CD1 . PHE H  1 64  ? 22.837 -70.631  -58.740  1.00 52.68  ? 65  PHE H CD1 1 
ATOM   8235  C  CD2 . PHE H  1 64  ? 23.647 -70.682  -56.504  1.00 48.69  ? 65  PHE H CD2 1 
ATOM   8236  C  CE1 . PHE H  1 64  ? 23.977 -69.971  -59.134  1.00 54.70  ? 65  PHE H CE1 1 
ATOM   8237  C  CE2 . PHE H  1 64  ? 24.784 -70.019  -56.894  1.00 50.67  ? 65  PHE H CE2 1 
ATOM   8238  C  CZ  . PHE H  1 64  ? 24.949 -69.662  -58.212  1.00 53.67  ? 65  PHE H CZ  1 
ATOM   8239  N  N   . ASN H  1 65  ? 22.430 -74.049  -59.355  1.00 53.17  ? 66  ASN H N   1 
ATOM   8240  C  CA  . ASN H  1 65  ? 23.259 -75.182  -59.732  1.00 54.47  ? 66  ASN H CA  1 
ATOM   8241  C  C   . ASN H  1 65  ? 24.278 -74.858  -60.829  1.00 57.85  ? 66  ASN H C   1 
ATOM   8242  O  O   . ASN H  1 65  ? 24.183 -75.372  -61.926  1.00 60.83  ? 66  ASN H O   1 
ATOM   8243  C  CB  . ASN H  1 65  ? 22.325 -76.309  -60.183  1.00 55.27  ? 66  ASN H CB  1 
ATOM   8244  C  CG  . ASN H  1 65  ? 23.050 -77.585  -60.479  1.00 56.65  ? 66  ASN H CG  1 
ATOM   8245  O  OD1 . ASN H  1 65  ? 24.240 -77.712  -60.210  1.00 57.04  ? 66  ASN H OD1 1 
ATOM   8246  N  ND2 . ASN H  1 65  ? 22.338 -78.543  -61.052  1.00 58.13  ? 66  ASN H ND2 1 
ATOM   8247  N  N   . PRO H  1 66  ? 25.274 -74.021  -60.531  1.00 57.97  ? 67  PRO H N   1 
ATOM   8248  C  CA  . PRO H  1 66  ? 26.252 -73.564  -61.516  1.00 61.61  ? 67  PRO H CA  1 
ATOM   8249  C  C   . PRO H  1 66  ? 27.307 -74.584  -61.899  1.00 64.06  ? 67  PRO H C   1 
ATOM   8250  O  O   . PRO H  1 66  ? 27.913 -74.457  -62.962  1.00 67.98  ? 67  PRO H O   1 
ATOM   8251  C  CB  . PRO H  1 66  ? 26.940 -72.408  -60.811  1.00 60.64  ? 67  PRO H CB  1 
ATOM   8252  C  CG  . PRO H  1 66  ? 26.871 -72.745  -59.410  1.00 57.19  ? 67  PRO H CG  1 
ATOM   8253  C  CD  . PRO H  1 66  ? 25.567 -73.476  -59.206  1.00 55.28  ? 67  PRO H CD  1 
ATOM   8254  N  N   . LEU H  1 67  ? 27.537 -75.574  -61.036  1.00 62.36  ? 68  LEU H N   1 
ATOM   8255  C  CA  . LEU H  1 67  ? 28.479 -76.675  -61.332  1.00 64.69  ? 68  LEU H CA  1 
ATOM   8256  C  C   . LEU H  1 67  ? 27.803 -77.897  -61.994  1.00 65.83  ? 68  LEU H C   1 
ATOM   8257  O  O   . LEU H  1 67  ? 28.424 -78.951  -62.150  1.00 67.58  ? 68  LEU H O   1 
ATOM   8258  C  CB  . LEU H  1 67  ? 29.223 -77.088  -60.057  1.00 62.96  ? 68  LEU H CB  1 
ATOM   8259  C  CG  . LEU H  1 67  ? 30.014 -75.974  -59.357  1.00 62.48  ? 68  LEU H CG  1 
ATOM   8260  C  CD1 . LEU H  1 67  ? 30.909 -76.561  -58.258  1.00 62.04  ? 68  LEU H CD1 1 
ATOM   8261  C  CD2 . LEU H  1 67  ? 30.829 -75.153  -60.363  1.00 66.21  ? 68  LEU H CD2 1 
ATOM   8262  N  N   . SER H  1 68  ? 26.531 -77.733  -62.380  1.00 65.27  ? 69  SER H N   1 
ATOM   8263  C  CA  . SER H  1 68  ? 25.777 -78.701  -63.216  1.00 67.15  ? 69  SER H CA  1 
ATOM   8264  C  C   . SER H  1 68  ? 25.666 -80.103  -62.613  1.00 65.96  ? 69  SER H C   1 
ATOM   8265  O  O   . SER H  1 68  ? 25.794 -81.096  -63.321  1.00 68.70  ? 69  SER H O   1 
ATOM   8266  C  CB  . SER H  1 68  ? 26.400 -78.792  -64.624  1.00 72.23  ? 69  SER H CB  1 
ATOM   8267  O  OG  . SER H  1 68  ? 26.657 -77.511  -65.182  1.00 74.07  ? 69  SER H OG  1 
ATOM   8268  N  N   . ARG H  1 69  ? 25.420 -80.171  -61.309  1.00 62.22  ? 70  ARG H N   1 
ATOM   8269  C  CA  . ARG H  1 69  ? 25.397 -81.443  -60.588  1.00 61.35  ? 70  ARG H CA  1 
ATOM   8270  C  C   . ARG H  1 69  ? 23.968 -81.878  -60.273  1.00 59.39  ? 70  ARG H C   1 
ATOM   8271  O  O   . ARG H  1 69  ? 23.009 -81.205  -60.634  1.00 59.05  ? 70  ARG H O   1 
ATOM   8272  C  CB  . ARG H  1 69  ? 26.230 -81.336  -59.303  1.00 59.40  ? 70  ARG H CB  1 
ATOM   8273  C  CG  . ARG H  1 69  ? 27.736 -81.567  -59.466  1.00 63.22  ? 70  ARG H CG  1 
ATOM   8274  C  CD  . ARG H  1 69  ? 28.496 -80.829  -58.349  1.00 63.48  ? 70  ARG H CD  1 
ATOM   8275  N  NE  . ARG H  1 69  ? 29.841 -81.352  -58.080  1.00 68.24  ? 70  ARG H NE  1 
ATOM   8276  C  CZ  . ARG H  1 69  ? 30.706 -80.817  -57.208  1.00 70.24  ? 70  ARG H CZ  1 
ATOM   8277  N  NH1 . ARG H  1 69  ? 30.376 -79.726  -56.513  1.00 68.67  ? 70  ARG H NH1 1 
ATOM   8278  N  NH2 . ARG H  1 69  ? 31.914 -81.369  -57.019  1.00 73.51  ? 70  ARG H NH2 1 
ATOM   8279  N  N   . LYS H  1 70  ? 23.853 -83.023  -59.605  1.00 58.72  ? 71  LYS H N   1 
ATOM   8280  C  CA  . LYS H  1 70  ? 22.570 -83.602  -59.168  1.00 57.28  ? 71  LYS H CA  1 
ATOM   8281  C  C   . LYS H  1 70  ? 22.196 -83.150  -57.776  1.00 53.57  ? 71  LYS H C   1 
ATOM   8282  O  O   . LYS H  1 70  ? 23.065 -82.817  -56.981  1.00 52.24  ? 71  LYS H O   1 
ATOM   8283  C  CB  . LYS H  1 70  ? 22.662 -85.128  -59.119  1.00 58.91  ? 71  LYS H CB  1 
ATOM   8284  C  CG  . LYS H  1 70  ? 23.078 -85.811  -60.427  1.00 63.37  ? 71  LYS H CG  1 
ATOM   8285  C  CD  . LYS H  1 70  ? 21.876 -86.239  -61.259  1.00 65.29  ? 71  LYS H CD  1 
ATOM   8286  C  CE  . LYS H  1 70  ? 22.279 -86.998  -62.506  1.00 69.95  ? 71  LYS H CE  1 
ATOM   8287  N  NZ  . LYS H  1 70  ? 21.082 -87.426  -63.262  1.00 71.90  ? 71  LYS H NZ  1 
ATOM   8288  N  N   . HIS H  1 71  ? 20.907 -83.194  -57.460  1.00 52.35  ? 72  HIS H N   1 
ATOM   8289  C  CA  . HIS H  1 71  ? 20.421 -82.735  -56.146  1.00 49.43  ? 72  HIS H CA  1 
ATOM   8290  C  C   . HIS H  1 71  ? 20.993 -83.588  -55.057  1.00 48.43  ? 72  HIS H C   1 
ATOM   8291  O  O   . HIS H  1 71  ? 21.336 -84.723  -55.288  1.00 50.07  ? 72  HIS H O   1 
ATOM   8292  C  CB  . HIS H  1 71  ? 18.883 -82.737  -56.050  1.00 49.25  ? 72  HIS H CB  1 
ATOM   8293  C  CG  . HIS H  1 71  ? 18.338 -82.215  -54.743  1.00 46.68  ? 72  HIS H CG  1 
ATOM   8294  N  ND1 . HIS H  1 71  ? 18.377 -80.885  -54.388  1.00 44.99  ? 72  HIS H ND1 1 
ATOM   8295  C  CD2 . HIS H  1 71  ? 17.717 -82.853  -53.723  1.00 45.68  ? 72  HIS H CD2 1 
ATOM   8296  C  CE1 . HIS H  1 71  ? 17.830 -80.734  -53.197  1.00 43.30  ? 72  HIS H CE1 1 
ATOM   8297  N  NE2 . HIS H  1 71  ? 17.417 -81.911  -52.774  1.00 43.33  ? 72  HIS H NE2 1 
ATOM   8298  N  N   . GLY H  1 72  ? 21.107 -83.010  -53.871  1.00 46.26  ? 73  GLY H N   1 
ATOM   8299  C  CA  . GLY H  1 72  ? 21.580 -83.730  -52.700  1.00 45.70  ? 73  GLY H CA  1 
ATOM   8300  C  C   . GLY H  1 72  ? 21.423 -82.977  -51.392  1.00 43.49  ? 73  GLY H C   1 
ATOM   8301  O  O   . GLY H  1 72  ? 20.898 -81.875  -51.343  1.00 42.36  ? 73  GLY H O   1 
ATOM   8302  N  N   . GLY H  1 73  ? 21.881 -83.601  -50.323  1.00 43.48  ? 74  GLY H N   1 
ATOM   8303  C  CA  . GLY H  1 73  ? 21.898 -82.986  -49.007  1.00 42.17  ? 74  GLY H CA  1 
ATOM   8304  C  C   . GLY H  1 73  ? 23.104 -82.083  -48.875  1.00 42.13  ? 74  GLY H C   1 
ATOM   8305  O  O   . GLY H  1 73  ? 24.065 -82.215  -49.613  1.00 43.66  ? 74  GLY H O   1 
ATOM   8306  N  N   . PRO H  1 74  ? 23.074 -81.149  -47.930  1.00 41.02  ? 75  PRO H N   1 
ATOM   8307  C  CA  . PRO H  1 74  ? 24.153 -80.172  -47.864  1.00 41.27  ? 75  PRO H CA  1 
ATOM   8308  C  C   . PRO H  1 74  ? 25.496 -80.797  -47.558  1.00 43.21  ? 75  PRO H C   1 
ATOM   8309  O  O   . PRO H  1 74  ? 26.505 -80.354  -48.088  1.00 44.50  ? 75  PRO H O   1 
ATOM   8310  C  CB  . PRO H  1 74  ? 23.726 -79.253  -46.727  1.00 40.05  ? 75  PRO H CB  1 
ATOM   8311  C  CG  . PRO H  1 74  ? 22.739 -80.020  -45.958  1.00 39.85  ? 75  PRO H CG  1 
ATOM   8312  C  CD  . PRO H  1 74  ? 22.060 -80.931  -46.895  1.00 39.96  ? 75  PRO H CD  1 
ATOM   8313  N  N   . LYS H  1 75  ? 25.499 -81.825  -46.716  1.00 44.02  ? 76  LYS H N   1 
ATOM   8314  C  CA  . LYS H  1 75  ? 26.723 -82.546  -46.391  1.00 46.40  ? 76  LYS H CA  1 
ATOM   8315  C  C   . LYS H  1 75  ? 27.231 -83.359  -47.558  1.00 48.10  ? 76  LYS H C   1 
ATOM   8316  O  O   . LYS H  1 75  ? 28.408 -83.641  -47.628  1.00 50.49  ? 76  LYS H O   1 
ATOM   8317  C  CB  . LYS H  1 75  ? 26.514 -83.508  -45.243  1.00 47.30  ? 76  LYS H CB  1 
ATOM   8318  C  CG  . LYS H  1 75  ? 25.834 -82.935  -44.038  1.00 46.63  ? 76  LYS H CG  1 
ATOM   8319  C  CD  . LYS H  1 75  ? 26.196 -83.770  -42.793  1.00 48.95  ? 76  LYS H CD  1 
ATOM   8320  C  CE  . LYS H  1 75  ? 25.325 -83.433  -41.593  1.00 48.48  ? 76  LYS H CE  1 
ATOM   8321  N  NZ  . LYS H  1 75  ? 25.436 -84.533  -40.580  1.00 50.61  ? 76  LYS H NZ  1 
ATOM   8322  N  N   . ASP H  1 76  ? 26.335 -83.784  -48.440  1.00 47.53  ? 77  ASP H N   1 
ATOM   8323  C  CA  . ASP H  1 76  ? 26.725 -84.539  -49.636  1.00 49.59  ? 77  ASP H CA  1 
ATOM   8324  C  C   . ASP H  1 76  ? 27.646 -83.695  -50.514  1.00 50.62  ? 77  ASP H C   1 
ATOM   8325  O  O   . ASP H  1 76  ? 27.469 -82.481  -50.611  1.00 48.99  ? 77  ASP H O   1 
ATOM   8326  C  CB  . ASP H  1 76  ? 25.501 -84.998  -50.452  1.00 48.89  ? 77  ASP H CB  1 
ATOM   8327  C  CG  . ASP H  1 76  ? 24.722 -86.128  -49.784  1.00 49.01  ? 77  ASP H CG  1 
ATOM   8328  O  OD1 . ASP H  1 76  ? 25.315 -86.875  -48.995  1.00 50.75  ? 77  ASP H OD1 1 
ATOM   8329  O  OD2 . ASP H  1 76  ? 23.513 -86.286  -50.052  1.00 48.28  ? 77  ASP H OD2 1 
ATOM   8330  N  N   . GLU H  1 77  ? 28.650 -84.348  -51.107  1.00 53.71  ? 78  GLU H N   1 
ATOM   8331  C  CA  . GLU H  1 77  ? 29.551 -83.690  -52.046  1.00 55.53  ? 78  GLU H CA  1 
ATOM   8332  C  C   . GLU H  1 77  ? 28.812 -83.460  -53.340  1.00 55.12  ? 78  GLU H C   1 
ATOM   8333  O  O   . GLU H  1 77  ? 28.850 -82.361  -53.875  1.00 54.82  ? 78  GLU H O   1 
ATOM   8334  C  CB  . GLU H  1 77  ? 30.818 -84.500  -52.324  1.00 59.59  ? 78  GLU H CB  1 
ATOM   8335  C  CG  . GLU H  1 77  ? 31.510 -84.046  -53.611  1.00 62.61  ? 78  GLU H CG  1 
ATOM   8336  C  CD  . GLU H  1 77  ? 32.937 -84.555  -53.764  1.00 67.72  ? 78  GLU H CD  1 
ATOM   8337  O  OE1 . GLU H  1 77  ? 33.199 -85.709  -53.338  1.00 69.46  ? 78  GLU H OE1 1 
ATOM   8338  O  OE2 . GLU H  1 77  ? 33.779 -83.798  -54.339  1.00 70.00  ? 78  GLU H OE2 1 
ATOM   8339  N  N   . GLU H  1 78  ? 28.177 -84.505  -53.861  1.00 55.67  ? 79  GLU H N   1 
ATOM   8340  C  CA  . GLU H  1 78  ? 27.297 -84.369  -55.034  1.00 55.59  ? 79  GLU H CA  1 
ATOM   8341  C  C   . GLU H  1 78  ? 25.983 -83.682  -54.637  1.00 52.28  ? 79  GLU H C   1 
ATOM   8342  O  O   . GLU H  1 78  ? 25.003 -84.329  -54.284  1.00 51.26  ? 79  GLU H O   1 
ATOM   8343  C  CB  . GLU H  1 78  ? 27.019 -85.724  -55.690  1.00 57.85  ? 79  GLU H CB  1 
ATOM   8344  C  CG  . GLU H  1 78  ? 26.217 -85.660  -57.003  1.00 58.77  ? 79  GLU H CG  1 
ATOM   8345  C  CD  . GLU H  1 78  ? 27.039 -85.187  -58.192  1.00 61.82  ? 79  GLU H CD  1 
ATOM   8346  O  OE1 . GLU H  1 78  ? 28.233 -84.874  -58.026  1.00 63.38  ? 79  GLU H OE1 1 
ATOM   8347  O  OE2 . GLU H  1 78  ? 26.496 -85.130  -59.305  1.00 63.09  ? 79  GLU H OE2 1 
ATOM   8348  N  N   . ARG H  1 79  ? 25.999 -82.355  -54.698  1.00 51.06  ? 80  ARG H N   1 
ATOM   8349  C  CA  . ARG H  1 79  ? 24.852 -81.509  -54.375  1.00 48.48  ? 80  ARG H CA  1 
ATOM   8350  C  C   . ARG H  1 79  ? 24.793 -80.284  -55.279  1.00 48.89  ? 80  ARG H C   1 
ATOM   8351  O  O   . ARG H  1 79  ? 25.785 -79.920  -55.919  1.00 50.75  ? 80  ARG H O   1 
ATOM   8352  C  CB  . ARG H  1 79  ? 24.947 -81.005  -52.931  1.00 46.36  ? 80  ARG H CB  1 
ATOM   8353  C  CG  . ARG H  1 79  ? 26.218 -80.228  -52.626  1.00 46.86  ? 80  ARG H CG  1 
ATOM   8354  C  CD  . ARG H  1 79  ? 26.187 -79.571  -51.263  1.00 45.13  ? 80  ARG H CD  1 
ATOM   8355  N  NE  . ARG H  1 79  ? 25.566 -78.256  -51.299  1.00 43.65  ? 80  ARG H NE  1 
ATOM   8356  C  CZ  . ARG H  1 79  ? 25.598 -77.370  -50.306  1.00 42.51  ? 80  ARG H CZ  1 
ATOM   8357  N  NH1 . ARG H  1 79  ? 26.230 -77.633  -49.173  1.00 42.54  ? 80  ARG H NH1 1 
ATOM   8358  N  NH2 . ARG H  1 79  ? 24.985 -76.195  -50.449  1.00 41.90  ? 80  ARG H NH2 1 
ATOM   8359  N  N   . HIS H  1 80  ? 23.630 -79.633  -55.305  1.00 47.50  ? 81  HIS H N   1 
ATOM   8360  C  CA  . HIS H  1 80  ? 23.512 -78.328  -55.943  1.00 47.72  ? 81  HIS H CA  1 
ATOM   8361  C  C   . HIS H  1 80  ? 24.144 -77.320  -55.017  1.00 46.34  ? 81  HIS H C   1 
ATOM   8362  O  O   . HIS H  1 80  ? 24.061 -77.479  -53.815  1.00 44.83  ? 81  HIS H O   1 
ATOM   8363  C  CB  . HIS H  1 80  ? 22.057 -77.931  -56.172  1.00 47.10  ? 81  HIS H CB  1 
ATOM   8364  C  CG  . HIS H  1 80  ? 21.312 -78.822  -57.116  1.00 48.77  ? 81  HIS H CG  1 
ATOM   8365  N  ND1 . HIS H  1 80  ? 19.961 -79.067  -56.995  1.00 48.21  ? 81  HIS H ND1 1 
ATOM   8366  C  CD2 . HIS H  1 80  ? 21.723 -79.506  -58.210  1.00 51.34  ? 81  HIS H CD2 1 
ATOM   8367  C  CE1 . HIS H  1 80  ? 19.575 -79.871  -57.972  1.00 50.55  ? 81  HIS H CE1 1 
ATOM   8368  N  NE2 . HIS H  1 80  ? 20.627 -80.158  -58.719  1.00 52.36  ? 81  HIS H NE2 1 
ATOM   8369  N  N   . VAL H  1 81  ? 24.755 -76.278  -55.559  1.00 47.39  ? 82  VAL H N   1 
ATOM   8370  C  CA  . VAL H  1 81  ? 25.317 -75.211  -54.726  1.00 46.41  ? 82  VAL H CA  1 
ATOM   8371  C  C   . VAL H  1 81  ? 24.266 -74.653  -53.778  1.00 43.86  ? 82  VAL H C   1 
ATOM   8372  O  O   . VAL H  1 81  ? 24.555 -74.366  -52.632  1.00 42.61  ? 82  VAL H O   1 
ATOM   8373  C  CB  . VAL H  1 81  ? 25.898 -74.070  -55.561  1.00 48.28  ? 82  VAL H CB  1 
ATOM   8374  C  CG1 . VAL H  1 81  ? 26.293 -72.918  -54.683  1.00 47.26  ? 82  VAL H CG1 1 
ATOM   8375  C  CG2 . VAL H  1 81  ? 27.104 -74.557  -56.340  1.00 51.26  ? 82  VAL H CG2 1 
ATOM   8376  N  N   . GLY H  1 82  ? 23.040 -74.541  -54.253  1.00 43.63  ? 83  GLY H N   1 
ATOM   8377  C  CA  . GLY H  1 82  ? 21.954 -73.984  -53.455  1.00 42.12  ? 83  GLY H CA  1 
ATOM   8378  C  C   . GLY H  1 82  ? 21.221 -74.918  -52.522  1.00 40.65  ? 83  GLY H C   1 
ATOM   8379  O  O   . GLY H  1 82  ? 20.265 -74.509  -51.881  1.00 39.72  ? 83  GLY H O   1 
ATOM   8380  N  N   . ASP H  1 83  ? 21.649 -76.168  -52.454  1.00 40.87  ? 84  ASP H N   1 
ATOM   8381  C  CA  . ASP H  1 83  ? 20.977 -77.168  -51.627  1.00 40.01  ? 84  ASP H CA  1 
ATOM   8382  C  C   . ASP H  1 83  ? 21.383 -77.035  -50.170  1.00 38.90  ? 84  ASP H C   1 
ATOM   8383  O  O   . ASP H  1 83  ? 22.354 -77.628  -49.750  1.00 39.29  ? 84  ASP H O   1 
ATOM   8384  C  CB  . ASP H  1 83  ? 21.314 -78.587  -52.091  1.00 41.04  ? 84  ASP H CB  1 
ATOM   8385  C  CG  . ASP H  1 83  ? 20.640 -78.970  -53.391  1.00 42.38  ? 84  ASP H CG  1 
ATOM   8386  O  OD1 . ASP H  1 83  ? 19.666 -78.330  -53.816  1.00 42.37  ? 84  ASP H OD1 1 
ATOM   8387  O  OD2 . ASP H  1 83  ? 21.082 -79.943  -54.015  1.00 43.93  ? 84  ASP H OD2 1 
ATOM   8388  N  N   . LEU H  1 84  ? 20.618 -76.269  -49.397  1.00 38.15  ? 85  LEU H N   1 
ATOM   8389  C  CA  . LEU H  1 84  ? 20.865 -76.077  -47.952  1.00 37.31  ? 85  LEU H CA  1 
ATOM   8390  C  C   . LEU H  1 84  ? 20.079 -77.050  -47.074  1.00 37.11  ? 85  LEU H C   1 
ATOM   8391  O  O   . LEU H  1 84  ? 20.044 -76.907  -45.859  1.00 36.81  ? 85  LEU H O   1 
ATOM   8392  C  CB  . LEU H  1 84  ? 20.548 -74.638  -47.539  1.00 36.94  ? 85  LEU H CB  1 
ATOM   8393  C  CG  . LEU H  1 84  ? 21.577 -73.606  -47.993  1.00 37.21  ? 85  LEU H CG  1 
ATOM   8394  C  CD1 . LEU H  1 84  ? 21.159 -72.218  -47.603  1.00 37.05  ? 85  LEU H CD1 1 
ATOM   8395  C  CD2 . LEU H  1 84  ? 22.921 -73.933  -47.422  1.00 37.58  ? 85  LEU H CD2 1 
ATOM   8396  N  N   . GLY H  1 85  ? 19.449 -78.037  -47.696  1.00 37.62  ? 86  GLY H N   1 
ATOM   8397  C  CA  . GLY H  1 85  ? 18.807 -79.109  -46.958  1.00 37.98  ? 86  GLY H CA  1 
ATOM   8398  C  C   . GLY H  1 85  ? 17.479 -78.711  -46.326  1.00 37.99  ? 86  GLY H C   1 
ATOM   8399  O  O   . GLY H  1 85  ? 16.637 -78.108  -46.981  1.00 38.40  ? 86  GLY H O   1 
ATOM   8400  N  N   . ASN H  1 86  ? 17.279 -79.062  -45.057  1.00 38.06  ? 87  ASN H N   1 
ATOM   8401  C  CA  . ASN H  1 86  ? 15.990 -78.871  -44.391  1.00 38.45  ? 87  ASN H CA  1 
ATOM   8402  C  C   . ASN H  1 86  ? 16.038 -77.876  -43.262  1.00 38.40  ? 87  ASN H C   1 
ATOM   8403  O  O   . ASN H  1 86  ? 17.097 -77.587  -42.731  1.00 38.20  ? 87  ASN H O   1 
ATOM   8404  C  CB  . ASN H  1 86  ? 15.495 -80.190  -43.822  1.00 39.50  ? 87  ASN H CB  1 
ATOM   8405  C  CG  . ASN H  1 86  ? 14.908 -81.056  -44.842  1.00 40.19  ? 87  ASN H CG  1 
ATOM   8406  O  OD1 . ASN H  1 86  ? 14.094 -80.617  -45.615  1.00 40.91  ? 87  ASN H OD1 1 
ATOM   8407  N  ND2 . ASN H  1 86  ? 15.303 -82.305  -44.859  1.00 41.14  ? 87  ASN H ND2 1 
ATOM   8408  N  N   . VAL H  1 87  ? 14.875 -77.358  -42.901  1.00 39.22  ? 88  VAL H N   1 
ATOM   8409  C  CA  . VAL H  1 87  ? 14.693 -76.575  -41.678  1.00 40.00  ? 88  VAL H CA  1 
ATOM   8410  C  C   . VAL H  1 87  ? 13.562 -77.190  -40.898  1.00 41.67  ? 88  VAL H C   1 
ATOM   8411  O  O   . VAL H  1 87  ? 12.625 -77.669  -41.482  1.00 42.50  ? 88  VAL H O   1 
ATOM   8412  C  CB  . VAL H  1 87  ? 14.354 -75.095  -41.969  1.00 40.09  ? 88  VAL H CB  1 
ATOM   8413  C  CG1 . VAL H  1 87  ? 15.531 -74.376  -42.623  1.00 38.69  ? 88  VAL H CG1 1 
ATOM   8414  C  CG2 . VAL H  1 87  ? 13.147 -74.982  -42.854  1.00 41.11  ? 88  VAL H CG2 1 
ATOM   8415  N  N   . THR H  1 88  ? 13.642 -77.164  -39.582  1.00 42.91  ? 89  THR H N   1 
ATOM   8416  C  CA  . THR H  1 88  ? 12.656 -77.843  -38.720  1.00 45.23  ? 89  THR H CA  1 
ATOM   8417  C  C   . THR H  1 88  ? 11.696 -76.913  -37.981  1.00 47.15  ? 89  THR H C   1 
ATOM   8418  O  O   . THR H  1 88  ? 12.104 -76.018  -37.269  1.00 47.49  ? 89  THR H O   1 
ATOM   8419  C  CB  . THR H  1 88  ? 13.340 -78.734  -37.682  1.00 46.09  ? 89  THR H CB  1 
ATOM   8420  O  OG1 . THR H  1 88  ? 13.938 -79.853  -38.343  1.00 45.25  ? 89  THR H OG1 1 
ATOM   8421  C  CG2 . THR H  1 88  ? 12.351 -79.245  -36.683  1.00 48.89  ? 89  THR H CG2 1 
ATOM   8422  N  N   . ALA H  1 89  ? 10.409 -77.164  -38.135  1.00 48.96  ? 90  ALA H N   1 
ATOM   8423  C  CA  . ALA H  1 89  ? 9.375  -76.318  -37.566  1.00 51.40  ? 90  ALA H CA  1 
ATOM   8424  C  C   . ALA H  1 89  ? 8.741  -76.964  -36.338  1.00 54.39  ? 90  ALA H C   1 
ATOM   8425  O  O   . ALA H  1 89  ? 8.348  -78.118  -36.381  1.00 55.44  ? 90  ALA H O   1 
ATOM   8426  C  CB  . ALA H  1 89  ? 8.328  -76.039  -38.614  1.00 52.26  ? 90  ALA H CB  1 
ATOM   8427  N  N   . ASP H  1 90  ? 8.628  -76.206  -35.253  1.00 56.32  ? 91  ASP H N   1 
ATOM   8428  C  CA  . ASP H  1 90  ? 8.043  -76.707  -33.993  1.00 59.81  ? 91  ASP H CA  1 
ATOM   8429  C  C   . ASP H  1 90  ? 6.539  -76.445  -33.885  1.00 63.36  ? 91  ASP H C   1 
ATOM   8430  O  O   . ASP H  1 90  ? 5.990  -75.612  -34.614  1.00 63.42  ? 91  ASP H O   1 
ATOM   8431  C  CB  . ASP H  1 90  ? 8.775  -76.133  -32.766  1.00 60.77  ? 91  ASP H CB  1 
ATOM   8432  C  CG  . ASP H  1 90  ? 8.504  -74.633  -32.528  1.00 61.97  ? 91  ASP H CG  1 
ATOM   8433  O  OD1 . ASP H  1 90  ? 9.010  -74.114  -31.501  1.00 63.46  ? 91  ASP H OD1 1 
ATOM   8434  O  OD2 . ASP H  1 90  ? 7.811  -73.971  -33.345  1.00 61.82  ? 91  ASP H OD2 1 
ATOM   8435  N  N   . LYS H  1 91  ? 5.898  -77.169  -32.966  1.00 66.74  ? 92  LYS H N   1 
ATOM   8436  C  CA  . LYS H  1 91  ? 4.431  -77.095  -32.703  1.00 71.13  ? 92  LYS H CA  1 
ATOM   8437  C  C   . LYS H  1 91  ? 3.718  -75.841  -33.225  1.00 72.09  ? 92  LYS H C   1 
ATOM   8438  O  O   . LYS H  1 91  ? 2.851  -75.921  -34.115  1.00 73.06  ? 92  LYS H O   1 
ATOM   8439  C  CB  . LYS H  1 91  ? 4.102  -77.180  -31.202  1.00 75.39  ? 92  LYS H CB  1 
ATOM   8440  C  CG  . LYS H  1 91  ? 5.126  -77.859  -30.287  1.00 75.34  ? 92  LYS H CG  1 
ATOM   8441  C  CD  . LYS H  1 91  ? 5.171  -79.382  -30.496  1.00 75.54  ? 92  LYS H CD  1 
ATOM   8442  C  CE  . LYS H  1 91  ? 5.763  -80.130  -29.299  1.00 77.25  ? 92  LYS H CE  1 
ATOM   8443  N  NZ  . LYS H  1 91  ? 4.744  -80.512  -28.284  1.00 82.81  ? 92  LYS H NZ  1 
ATOM   8444  N  N   . ASP H  1 92  ? 4.088  -74.690  -32.667  1.00 72.21  ? 93  ASP H N   1 
ATOM   8445  C  CA  . ASP H  1 92  ? 3.388  -73.431  -32.947  1.00 74.07  ? 93  ASP H CA  1 
ATOM   8446  C  C   . ASP H  1 92  ? 3.839  -72.796  -34.267  1.00 70.53  ? 93  ASP H C   1 
ATOM   8447  O  O   . ASP H  1 92  ? 3.597  -71.614  -34.511  1.00 71.60  ? 93  ASP H O   1 
ATOM   8448  C  CB  . ASP H  1 92  ? 3.464  -72.439  -31.773  1.00 76.72  ? 93  ASP H CB  1 
ATOM   8449  C  CG  . ASP H  1 92  ? 4.300  -72.944  -30.613  1.00 77.13  ? 93  ASP H CG  1 
ATOM   8450  O  OD1 . ASP H  1 92  ? 5.530  -73.126  -30.802  1.00 73.66  ? 93  ASP H OD1 1 
ATOM   8451  O  OD2 . ASP H  1 92  ? 3.731  -73.130  -29.509  1.00 81.24  ? 93  ASP H OD2 1 
ATOM   8452  N  N   . GLY H  1 93  ? 4.453  -73.597  -35.133  1.00 66.95  ? 94  GLY H N   1 
ATOM   8453  C  CA  . GLY H  1 93  ? 4.701  -73.217  -36.525  1.00 64.20  ? 94  GLY H CA  1 
ATOM   8454  C  C   . GLY H  1 93  ? 6.005  -72.493  -36.747  1.00 60.59  ? 94  GLY H C   1 
ATOM   8455  O  O   . GLY H  1 93  ? 6.259  -72.044  -37.857  1.00 58.73  ? 94  GLY H O   1 
ATOM   8456  N  N   . VAL H  1 94  ? 6.840  -72.399  -35.708  1.00 59.72  ? 95  VAL H N   1 
ATOM   8457  C  CA  . VAL H  1 94  ? 8.039  -71.549  -35.753  1.00 57.30  ? 95  VAL H CA  1 
ATOM   8458  C  C   . VAL H  1 94  ? 9.322  -72.345  -35.976  1.00 53.97  ? 95  VAL H C   1 
ATOM   8459  O  O   . VAL H  1 94  ? 9.615  -73.283  -35.250  1.00 53.86  ? 95  VAL H O   1 
ATOM   8460  C  CB  . VAL H  1 94  ? 8.202  -70.651  -34.472  1.00 59.71  ? 95  VAL H CB  1 
ATOM   8461  C  CG1 . VAL H  1 94  ? 7.467  -69.303  -34.637  1.00 61.80  ? 95  VAL H CG1 1 
ATOM   8462  C  CG2 . VAL H  1 94  ? 7.752  -71.370  -33.192  1.00 62.46  ? 95  VAL H CG2 1 
ATOM   8463  N  N   . ALA H  1 95  ? 10.100 -71.928  -36.970  1.00 51.64  ? 96  ALA H N   1 
ATOM   8464  C  CA  . ALA H  1 95  ? 11.300 -72.653  -37.364  1.00 48.82  ? 96  ALA H CA  1 
ATOM   8465  C  C   . ALA H  1 95  ? 12.476 -71.763  -37.102  1.00 47.79  ? 96  ALA H C   1 
ATOM   8466  O  O   . ALA H  1 95  ? 12.703 -70.812  -37.846  1.00 46.91  ? 96  ALA H O   1 
ATOM   8467  C  CB  . ALA H  1 95  ? 11.263 -73.018  -38.826  1.00 47.06  ? 96  ALA H CB  1 
ATOM   8468  N  N   . ASP H  1 96  ? 13.218 -72.071  -36.043  1.00 48.28  ? 97  ASP H N   1 
ATOM   8469  C  CA  . ASP H  1 96  ? 14.373 -71.263  -35.656  1.00 47.99  ? 97  ASP H CA  1 
ATOM   8470  C  C   . ASP H  1 96  ? 15.617 -71.689  -36.414  1.00 45.49  ? 97  ASP H C   1 
ATOM   8471  O  O   . ASP H  1 96  ? 16.364 -72.532  -35.959  1.00 45.64  ? 97  ASP H O   1 
ATOM   8472  C  CB  . ASP H  1 96  ? 14.592 -71.328  -34.143  1.00 50.56  ? 97  ASP H CB  1 
ATOM   8473  C  CG  . ASP H  1 96  ? 13.658 -70.386  -33.381  1.00 53.94  ? 97  ASP H CG  1 
ATOM   8474  O  OD1 . ASP H  1 96  ? 13.520 -69.201  -33.787  1.00 54.08  ? 97  ASP H OD1 1 
ATOM   8475  O  OD2 . ASP H  1 96  ? 13.058 -70.827  -32.379  1.00 56.78  ? 97  ASP H OD2 1 
ATOM   8476  N  N   . VAL H  1 97  ? 15.831 -71.085  -37.575  1.00 43.77  ? 98  VAL H N   1 
ATOM   8477  C  CA  . VAL H  1 97  ? 16.884 -71.517  -38.488  1.00 41.80  ? 98  VAL H CA  1 
ATOM   8478  C  C   . VAL H  1 97  ? 18.266 -71.186  -37.961  1.00 42.09  ? 98  VAL H C   1 
ATOM   8479  O  O   . VAL H  1 97  ? 18.515 -70.060  -37.528  1.00 43.18  ? 98  VAL H O   1 
ATOM   8480  C  CB  . VAL H  1 97  ? 16.756 -70.840  -39.861  1.00 40.66  ? 98  VAL H CB  1 
ATOM   8481  C  CG1 . VAL H  1 97  ? 17.830 -71.352  -40.796  1.00 39.18  ? 98  VAL H CG1 1 
ATOM   8482  C  CG2 . VAL H  1 97  ? 15.384 -71.057  -40.460  1.00 41.17  ? 98  VAL H CG2 1 
ATOM   8483  N  N   . SER H  1 98  ? 19.162 -72.169  -37.998  1.00 41.72  ? 99  SER H N   1 
ATOM   8484  C  CA  . SER H  1 98  ? 20.591 -71.959  -37.692  1.00 42.33  ? 99  SER H CA  1 
ATOM   8485  C  C   . SER H  1 98  ? 21.432 -72.983  -38.423  1.00 41.48  ? 99  SER H C   1 
ATOM   8486  O  O   . SER H  1 98  ? 21.689 -74.062  -37.910  1.00 42.25  ? 99  SER H O   1 
ATOM   8487  C  CB  . SER H  1 98  ? 20.873 -72.032  -36.190  1.00 44.70  ? 99  SER H CB  1 
ATOM   8488  O  OG  . SER H  1 98  ? 22.251 -71.899  -35.922  1.00 45.47  ? 99  SER H OG  1 
ATOM   8489  N  N   . ILE H  1 99  ? 21.831 -72.626  -39.637  1.00 40.30  ? 100 ILE H N   1 
ATOM   8490  C  CA  . ILE H  1 99  ? 22.661 -73.462  -40.496  1.00 39.81  ? 100 ILE H CA  1 
ATOM   8491  C  C   . ILE H  1 99  ? 24.017 -72.820  -40.631  1.00 40.79  ? 100 ILE H C   1 
ATOM   8492  O  O   . ILE H  1 99  ? 24.154 -71.635  -40.385  1.00 41.52  ? 100 ILE H O   1 
ATOM   8493  C  CB  . ILE H  1 99  ? 22.047 -73.603  -41.886  1.00 38.26  ? 100 ILE H CB  1 
ATOM   8494  C  CG1 . ILE H  1 99  ? 20.738 -74.385  -41.776  1.00 37.94  ? 100 ILE H CG1 1 
ATOM   8495  C  CG2 . ILE H  1 99  ? 23.009 -74.258  -42.831  1.00 38.32  ? 100 ILE H CG2 1 
ATOM   8496  C  CD1 . ILE H  1 99  ? 20.266 -74.986  -43.064  1.00 37.20  ? 100 ILE H CD1 1 
ATOM   8497  N  N   . GLU H  1 100 ? 25.026 -73.623  -40.958  1.00 41.54  ? 101 GLU H N   1 
ATOM   8498  C  CA  . GLU H  1 100 ? 26.350 -73.129  -41.344  1.00 42.72  ? 101 GLU H CA  1 
ATOM   8499  C  C   . GLU H  1 100 ? 26.794 -73.939  -42.545  1.00 42.48  ? 101 GLU H C   1 
ATOM   8500  O  O   . GLU H  1 100 ? 26.814 -75.167  -42.495  1.00 42.77  ? 101 GLU H O   1 
ATOM   8501  C  CB  . GLU H  1 100 ? 27.358 -73.246  -40.189  1.00 45.23  ? 101 GLU H CB  1 
ATOM   8502  C  CG  . GLU H  1 100 ? 28.709 -72.610  -40.478  1.00 47.67  ? 101 GLU H CG  1 
ATOM   8503  C  CD  . GLU H  1 100 ? 29.603 -72.497  -39.254  1.00 51.04  ? 101 GLU H CD  1 
ATOM   8504  O  OE1 . GLU H  1 100 ? 30.671 -71.850  -39.369  1.00 52.98  ? 101 GLU H OE1 1 
ATOM   8505  O  OE2 . GLU H  1 100 ? 29.243 -73.041  -38.190  1.00 51.72  ? 101 GLU H OE2 1 
ATOM   8506  N  N   . ASP H  1 101 ? 27.136 -73.248  -43.629  1.00 42.41  ? 102 ASP H N   1 
ATOM   8507  C  CA  . ASP H  1 101 ? 27.430 -73.918  -44.905  1.00 42.54  ? 102 ASP H CA  1 
ATOM   8508  C  C   . ASP H  1 101 ? 28.671 -73.381  -45.605  1.00 44.39  ? 102 ASP H C   1 
ATOM   8509  O  O   . ASP H  1 101 ? 28.986 -72.201  -45.499  1.00 44.85  ? 102 ASP H O   1 
ATOM   8510  C  CB  . ASP H  1 101 ? 26.244 -73.805  -45.853  1.00 40.69  ? 102 ASP H CB  1 
ATOM   8511  C  CG  . ASP H  1 101 ? 26.337 -74.751  -47.001  1.00 40.79  ? 102 ASP H CG  1 
ATOM   8512  O  OD1 . ASP H  1 101 ? 26.263 -75.960  -46.750  1.00 40.90  ? 102 ASP H OD1 1 
ATOM   8513  O  OD2 . ASP H  1 101 ? 26.487 -74.294  -48.144  1.00 41.00  ? 102 ASP H OD2 1 
ATOM   8514  N  N   . SER H  1 102 ? 29.354 -74.272  -46.325  1.00 45.77  ? 103 SER H N   1 
ATOM   8515  C  CA  . SER H  1 102 ? 30.642 -73.981  -46.957  1.00 48.31  ? 103 SER H CA  1 
ATOM   8516  C  C   . SER H  1 102 ? 30.622 -73.964  -48.473  1.00 48.58  ? 103 SER H C   1 
ATOM   8517  O  O   . SER H  1 102 ? 31.574 -73.498  -49.087  1.00 50.91  ? 103 SER H O   1 
ATOM   8518  C  CB  . SER H  1 102 ? 31.660 -75.012  -46.512  1.00 50.84  ? 103 SER H CB  1 
ATOM   8519  O  OG  . SER H  1 102 ? 31.670 -75.087  -45.108  1.00 51.39  ? 103 SER H OG  1 
ATOM   8520  N  N   . VAL H  1 103 ? 29.559 -74.482  -49.079  1.00 46.79  ? 104 VAL H N   1 
ATOM   8521  C  CA  . VAL H  1 103 ? 29.435 -74.483  -50.536  1.00 47.50  ? 104 VAL H CA  1 
ATOM   8522  C  C   . VAL H  1 103 ? 28.905 -73.148  -51.046  1.00 46.97  ? 104 VAL H C   1 
ATOM   8523  O  O   . VAL H  1 103 ? 29.460 -72.601  -51.993  1.00 49.08  ? 104 VAL H O   1 
ATOM   8524  C  CB  . VAL H  1 103 ? 28.497 -75.577  -51.055  1.00 46.50  ? 104 VAL H CB  1 
ATOM   8525  C  CG1 . VAL H  1 103 ? 28.423 -75.520  -52.562  1.00 47.74  ? 104 VAL H CG1 1 
ATOM   8526  C  CG2 . VAL H  1 103 ? 28.966 -76.939  -50.630  1.00 47.76  ? 104 VAL H CG2 1 
ATOM   8527  N  N   . ILE H  1 104 ? 27.837 -72.625  -50.439  1.00 44.68  ? 105 ILE H N   1 
ATOM   8528  C  CA  . ILE H  1 104 ? 27.324 -71.307  -50.822  1.00 44.27  ? 105 ILE H CA  1 
ATOM   8529  C  C   . ILE H  1 104 ? 28.315 -70.207  -50.485  1.00 45.77  ? 105 ILE H C   1 
ATOM   8530  O  O   . ILE H  1 104 ? 29.188 -70.372  -49.659  1.00 46.56  ? 105 ILE H O   1 
ATOM   8531  C  CB  . ILE H  1 104 ? 25.985 -70.963  -50.146  1.00 42.18  ? 105 ILE H CB  1 
ATOM   8532  C  CG1 . ILE H  1 104 ? 26.116 -70.845  -48.629  1.00 41.60  ? 105 ILE H CG1 1 
ATOM   8533  C  CG2 . ILE H  1 104 ? 24.959 -72.001  -50.456  1.00 41.09  ? 105 ILE H CG2 1 
ATOM   8534  C  CD1 . ILE H  1 104 ? 24.962 -70.093  -47.969  1.00 40.00  ? 105 ILE H CD1 1 
ATOM   8535  N  N   . SER H  1 105 ? 28.172 -69.066  -51.125  1.00 46.71  ? 106 SER H N   1 
ATOM   8536  C  CA  . SER H  1 105 ? 29.013 -67.909  -50.811  1.00 48.41  ? 106 SER H CA  1 
ATOM   8537  C  C   . SER H  1 105 ? 28.339 -66.569  -51.104  1.00 48.44  ? 106 SER H C   1 
ATOM   8538  O  O   . SER H  1 105 ? 27.424 -66.461  -51.917  1.00 48.08  ? 106 SER H O   1 
ATOM   8539  C  CB  . SER H  1 105 ? 30.339 -67.984  -51.568  1.00 51.40  ? 106 SER H CB  1 
ATOM   8540  O  OG  . SER H  1 105 ? 31.217 -66.974  -51.119  1.00 53.11  ? 106 SER H OG  1 
ATOM   8541  N  N   . LEU H  1 106 ? 28.812 -65.540  -50.426  1.00 49.31  ? 107 LEU H N   1 
ATOM   8542  C  CA  . LEU H  1 106 ? 28.343 -64.184  -50.676  1.00 50.11  ? 107 LEU H CA  1 
ATOM   8543  C  C   . LEU H  1 106 ? 29.257 -63.430  -51.654  1.00 53.19  ? 107 LEU H C   1 
ATOM   8544  O  O   . LEU H  1 106 ? 29.163 -62.220  -51.792  1.00 54.56  ? 107 LEU H O   1 
ATOM   8545  C  CB  . LEU H  1 106 ? 28.229 -63.428  -49.353  1.00 49.72  ? 107 LEU H CB  1 
ATOM   8546  C  CG  . LEU H  1 106 ? 27.277 -64.029  -48.333  1.00 46.94  ? 107 LEU H CG  1 
ATOM   8547  C  CD1 . LEU H  1 106 ? 27.254 -63.156  -47.118  1.00 47.50  ? 107 LEU H CD1 1 
ATOM   8548  C  CD2 . LEU H  1 106 ? 25.899 -64.169  -48.901  1.00 45.31  ? 107 LEU H CD2 1 
ATOM   8549  N  N   . SER H  1 107 ? 30.125 -64.158  -52.348  1.00 54.74  ? 108 SER H N   1 
ATOM   8550  C  CA  . SER H  1 107 ? 31.064 -63.569  -53.316  1.00 58.10  ? 108 SER H CA  1 
ATOM   8551  C  C   . SER H  1 107 ? 31.589 -64.606  -54.320  1.00 59.57  ? 108 SER H C   1 
ATOM   8552  O  O   . SER H  1 107 ? 31.877 -65.757  -53.969  1.00 58.74  ? 108 SER H O   1 
ATOM   8553  C  CB  . SER H  1 107 ? 32.253 -62.916  -52.601  1.00 60.29  ? 108 SER H CB  1 
ATOM   8554  O  OG  . SER H  1 107 ? 32.940 -63.840  -51.763  1.00 59.91  ? 108 SER H OG  1 
ATOM   8555  N  N   . GLY H  1 108 ? 31.697 -64.190  -55.576  1.00 62.23  ? 109 GLY H N   1 
ATOM   8556  C  CA  . GLY H  1 108 ? 32.321 -65.010  -56.624  1.00 64.67  ? 109 GLY H CA  1 
ATOM   8557  C  C   . GLY H  1 108 ? 31.402 -65.930  -57.413  1.00 63.56  ? 109 GLY H C   1 
ATOM   8558  O  O   . GLY H  1 108 ? 30.198 -65.668  -57.567  1.00 61.78  ? 109 GLY H O   1 
ATOM   8559  N  N   . ASP H  1 109 ? 31.994 -67.006  -57.930  1.00 65.10  ? 110 ASP H N   1 
ATOM   8560  C  CA  . ASP H  1 109 ? 31.284 -67.989  -58.777  1.00 65.05  ? 110 ASP H CA  1 
ATOM   8561  C  C   . ASP H  1 109 ? 29.987 -68.532  -58.123  1.00 60.78  ? 110 ASP H C   1 
ATOM   8562  O  O   . ASP H  1 109 ? 28.926 -68.663  -58.748  1.00 59.90  ? 110 ASP H O   1 
ATOM   8563  C  CB  . ASP H  1 109 ? 32.228 -69.163  -59.067  1.00 67.27  ? 110 ASP H CB  1 
ATOM   8564  C  CG  . ASP H  1 109 ? 31.946 -69.848  -60.398  1.00 69.91  ? 110 ASP H CG  1 
ATOM   8565  O  OD1 . ASP H  1 109 ? 31.146 -70.817  -60.416  1.00 67.97  ? 110 ASP H OD1 1 
ATOM   8566  O  OD2 . ASP H  1 109 ? 32.558 -69.430  -61.412  1.00 74.22  ? 110 ASP H OD2 1 
ATOM   8567  N  N   . HIS H  1 110 ? 30.112 -68.827  -56.839  1.00 58.35  ? 111 HIS H N   1 
ATOM   8568  C  CA  . HIS H  1 110 ? 29.037 -69.379  -56.025  1.00 54.79  ? 111 HIS H CA  1 
ATOM   8569  C  C   . HIS H  1 110 ? 28.149 -68.304  -55.401  1.00 52.86  ? 111 HIS H C   1 
ATOM   8570  O  O   . HIS H  1 110 ? 27.328 -68.629  -54.554  1.00 50.21  ? 111 HIS H O   1 
ATOM   8571  C  CB  . HIS H  1 110 ? 29.651 -70.210  -54.890  1.00 53.75  ? 111 HIS H CB  1 
ATOM   8572  C  CG  . HIS H  1 110 ? 30.348 -71.456  -55.347  1.00 55.54  ? 111 HIS H CG  1 
ATOM   8573  N  ND1 . HIS H  1 110 ? 30.739 -72.450  -54.475  1.00 54.79  ? 111 HIS H ND1 1 
ATOM   8574  C  CD2 . HIS H  1 110 ? 30.715 -71.873  -56.580  1.00 58.34  ? 111 HIS H CD2 1 
ATOM   8575  C  CE1 . HIS H  1 110 ? 31.325 -73.422  -55.148  1.00 57.05  ? 111 HIS H CE1 1 
ATOM   8576  N  NE2 . HIS H  1 110 ? 31.325 -73.096  -56.427  1.00 59.46  ? 111 HIS H NE2 1 
ATOM   8577  N  N   . CYS H  1 111 ? 28.310 -67.042  -55.813  1.00 54.53  ? 112 CYS H N   1 
ATOM   8578  C  CA  . CYS H  1 111 ? 27.614 -65.908  -55.181  1.00 53.29  ? 112 CYS H CA  1 
ATOM   8579  C  C   . CYS H  1 111 ? 26.102 -66.081  -55.215  1.00 51.37  ? 112 CYS H C   1 
ATOM   8580  O  O   . CYS H  1 111 ? 25.505 -66.162  -56.290  1.00 52.59  ? 112 CYS H O   1 
ATOM   8581  C  CB  . CYS H  1 111 ? 28.000 -64.592  -55.860  1.00 56.23  ? 112 CYS H CB  1 
ATOM   8582  S  SG  . CYS H  1 111 ? 27.462 -63.052  -54.989  1.00 55.99  ? 112 CYS H SG  1 
ATOM   8583  N  N   . ILE H  1 112 ? 25.494 -66.162  -54.038  1.00 48.78  ? 113 ILE H N   1 
ATOM   8584  C  CA  . ILE H  1 112 ? 24.039 -66.328  -53.927  1.00 47.52  ? 113 ILE H CA  1 
ATOM   8585  C  C   . ILE H  1 112 ? 23.284 -64.997  -53.827  1.00 48.27  ? 113 ILE H C   1 
ATOM   8586  O  O   . ILE H  1 112 ? 22.050 -64.964  -53.816  1.00 47.86  ? 113 ILE H O   1 
ATOM   8587  C  CB  . ILE H  1 112 ? 23.619 -67.184  -52.704  1.00 44.97  ? 113 ILE H CB  1 
ATOM   8588  C  CG1 . ILE H  1 112 ? 24.085 -66.558  -51.398  1.00 44.20  ? 113 ILE H CG1 1 
ATOM   8589  C  CG2 . ILE H  1 112 ? 24.145 -68.582  -52.822  1.00 44.57  ? 113 ILE H CG2 1 
ATOM   8590  C  CD1 . ILE H  1 112 ? 23.269 -66.998  -50.227  1.00 42.23  ? 113 ILE H CD1 1 
ATOM   8591  N  N   . ILE H  1 113 ? 24.028 -63.902  -53.724  1.00 49.72  ? 114 ILE H N   1 
ATOM   8592  C  CA  . ILE H  1 113 ? 23.428 -62.569  -53.636  1.00 50.76  ? 114 ILE H CA  1 
ATOM   8593  C  C   . ILE H  1 113 ? 22.743 -62.191  -54.944  1.00 52.91  ? 114 ILE H C   1 
ATOM   8594  O  O   . ILE H  1 113 ? 23.302 -62.334  -56.029  1.00 54.57  ? 114 ILE H O   1 
ATOM   8595  C  CB  . ILE H  1 113 ? 24.460 -61.491  -53.277  1.00 52.19  ? 114 ILE H CB  1 
ATOM   8596  C  CG1 . ILE H  1 113 ? 24.884 -61.638  -51.816  1.00 50.54  ? 114 ILE H CG1 1 
ATOM   8597  C  CG2 . ILE H  1 113 ? 23.871 -60.114  -53.488  1.00 54.09  ? 114 ILE H CG2 1 
ATOM   8598  C  CD1 . ILE H  1 113 ? 26.055 -60.790  -51.445  1.00 52.57  ? 114 ILE H CD1 1 
ATOM   8599  N  N   . GLY H  1 114 ? 21.519 -61.701  -54.817  1.00 53.22  ? 115 GLY H N   1 
ATOM   8600  C  CA  . GLY H  1 114 ? 20.700 -61.369  -55.968  1.00 55.76  ? 115 GLY H CA  1 
ATOM   8601  C  C   . GLY H  1 114 ? 19.862 -62.546  -56.429  1.00 55.13  ? 115 GLY H C   1 
ATOM   8602  O  O   . GLY H  1 114 ? 19.153 -62.451  -57.426  1.00 57.59  ? 115 GLY H O   1 
ATOM   8603  N  N   . ARG H  1 115 ? 19.940 -63.663  -55.712  1.00 52.32  ? 116 ARG H N   1 
ATOM   8604  C  CA  . ARG H  1 115 ? 19.155 -64.851  -56.048  1.00 51.79  ? 116 ARG H CA  1 
ATOM   8605  C  C   . ARG H  1 115 ? 18.118 -65.070  -54.987  1.00 50.09  ? 116 ARG H C   1 
ATOM   8606  O  O   . ARG H  1 115 ? 18.137 -64.415  -53.971  1.00 49.30  ? 116 ARG H O   1 
ATOM   8607  C  CB  . ARG H  1 115 ? 20.055 -66.074  -56.197  1.00 50.51  ? 116 ARG H CB  1 
ATOM   8608  C  CG  . ARG H  1 115 ? 21.163 -65.870  -57.223  1.00 52.81  ? 116 ARG H CG  1 
ATOM   8609  C  CD  . ARG H  1 115 ? 22.012 -67.107  -57.450  1.00 52.38  ? 116 ARG H CD  1 
ATOM   8610  N  NE  . ARG H  1 115 ? 23.187 -66.828  -58.276  1.00 54.37  ? 116 ARG H NE  1 
ATOM   8611  C  CZ  . ARG H  1 115 ? 23.183 -66.790  -59.604  1.00 57.47  ? 116 ARG H CZ  1 
ATOM   8612  N  NH1 . ARG H  1 115 ? 22.080 -67.024  -60.306  1.00 58.76  ? 116 ARG H NH1 1 
ATOM   8613  N  NH2 . ARG H  1 115 ? 24.296 -66.515  -60.244  1.00 60.15  ? 116 ARG H NH2 1 
ATOM   8614  N  N   . THR H  1 116 ? 17.215 -65.998  -55.230  1.00 50.06  ? 117 THR H N   1 
ATOM   8615  C  CA  . THR H  1 116 ? 16.066 -66.228  -54.353  1.00 49.34  ? 117 THR H CA  1 
ATOM   8616  C  C   . THR H  1 116 ? 16.270 -67.366  -53.345  1.00 46.63  ? 117 THR H C   1 
ATOM   8617  O  O   . THR H  1 116 ? 16.701 -68.458  -53.707  1.00 46.09  ? 117 THR H O   1 
ATOM   8618  C  CB  . THR H  1 116 ? 14.808 -66.553  -55.182  1.00 51.66  ? 117 THR H CB  1 
ATOM   8619  O  OG1 . THR H  1 116 ? 14.483 -65.441  -56.020  1.00 54.49  ? 117 THR H OG1 1 
ATOM   8620  C  CG2 . THR H  1 116 ? 13.629 -66.875  -54.278  1.00 51.24  ? 117 THR H CG2 1 
ATOM   8621  N  N   . LEU H  1 117 ? 15.950 -67.099  -52.082  1.00 45.49  ? 118 LEU H N   1 
ATOM   8622  C  CA  . LEU H  1 117 ? 15.843 -68.136  -51.047  1.00 43.49  ? 118 LEU H CA  1 
ATOM   8623  C  C   . LEU H  1 117 ? 14.409 -68.624  -51.014  1.00 44.49  ? 118 LEU H C   1 
ATOM   8624  O  O   . LEU H  1 117 ? 13.503 -67.840  -51.258  1.00 46.75  ? 118 LEU H O   1 
ATOM   8625  C  CB  . LEU H  1 117 ? 16.207 -67.573  -49.681  1.00 42.42  ? 118 LEU H CB  1 
ATOM   8626  C  CG  . LEU H  1 117 ? 16.246 -68.579  -48.530  1.00 40.66  ? 118 LEU H CG  1 
ATOM   8627  C  CD1 . LEU H  1 117 ? 17.266 -69.645  -48.813  1.00 39.50  ? 118 LEU H CD1 1 
ATOM   8628  C  CD2 . LEU H  1 117 ? 16.565 -67.901  -47.213  1.00 40.20  ? 118 LEU H CD2 1 
ATOM   8629  N  N   . VAL H  1 118 ? 14.199 -69.903  -50.708  1.00 43.42  ? 119 VAL H N   1 
ATOM   8630  C  CA  . VAL H  1 118 ? 12.866 -70.512  -50.807  1.00 44.79  ? 119 VAL H CA  1 
ATOM   8631  C  C   . VAL H  1 118 ? 12.638 -71.591  -49.760  1.00 43.55  ? 119 VAL H C   1 
ATOM   8632  O  O   . VAL H  1 118 ? 13.415 -72.522  -49.655  1.00 42.18  ? 119 VAL H O   1 
ATOM   8633  C  CB  . VAL H  1 118 ? 12.654 -71.153  -52.189  1.00 46.19  ? 119 VAL H CB  1 
ATOM   8634  C  CG1 . VAL H  1 118 ? 11.405 -71.991  -52.181  1.00 47.83  ? 119 VAL H CG1 1 
ATOM   8635  C  CG2 . VAL H  1 118 ? 12.570 -70.104  -53.270  1.00 48.37  ? 119 VAL H CG2 1 
ATOM   8636  N  N   . VAL H  1 119 ? 11.572 -71.451  -48.986  1.00 44.67  ? 120 VAL H N   1 
ATOM   8637  C  CA  . VAL H  1 119 ? 11.171 -72.473  -48.023  1.00 44.33  ? 120 VAL H CA  1 
ATOM   8638  C  C   . VAL H  1 119 ? 10.048 -73.272  -48.654  1.00 46.36  ? 120 VAL H C   1 
ATOM   8639  O  O   . VAL H  1 119 ? 9.287  -72.746  -49.445  1.00 48.64  ? 120 VAL H O   1 
ATOM   8640  C  CB  . VAL H  1 119 ? 10.746 -71.873  -46.651  1.00 44.80  ? 120 VAL H CB  1 
ATOM   8641  C  CG1 . VAL H  1 119 ? 9.392  -71.228  -46.718  1.00 47.96  ? 120 VAL H CG1 1 
ATOM   8642  C  CG2 . VAL H  1 119 ? 10.726 -72.925  -45.585  1.00 44.25  ? 120 VAL H CG2 1 
ATOM   8643  N  N   . HIS H  1 120 ? 9.954  -74.547  -48.308  1.00 46.12  ? 121 HIS H N   1 
ATOM   8644  C  CA  . HIS H  1 120 ? 9.143  -75.501  -49.072  1.00 47.99  ? 121 HIS H CA  1 
ATOM   8645  C  C   . HIS H  1 120 ? 8.029  -76.214  -48.320  1.00 49.84  ? 121 HIS H C   1 
ATOM   8646  O  O   . HIS H  1 120 ? 8.022  -76.295  -47.095  1.00 49.18  ? 121 HIS H O   1 
ATOM   8647  C  CB  . HIS H  1 120 ? 10.050 -76.557  -49.692  1.00 46.69  ? 121 HIS H CB  1 
ATOM   8648  C  CG  . HIS H  1 120 ? 10.597 -76.159  -51.015  1.00 46.57  ? 121 HIS H CG  1 
ATOM   8649  N  ND1 . HIS H  1 120 ? 10.185 -76.738  -52.192  1.00 48.91  ? 121 HIS H ND1 1 
ATOM   8650  C  CD2 . HIS H  1 120 ? 11.501 -75.219  -51.356  1.00 45.41  ? 121 HIS H CD2 1 
ATOM   8651  C  CE1 . HIS H  1 120 ? 10.821 -76.178  -53.203  1.00 48.97  ? 121 HIS H CE1 1 
ATOM   8652  N  NE2 . HIS H  1 120 ? 11.626 -75.253  -52.721  1.00 46.93  ? 121 HIS H NE2 1 
ATOM   8653  N  N   . GLU H  1 121 ? 7.103  -76.757  -49.105  1.00 52.46  ? 122 GLU H N   1 
ATOM   8654  C  CA  . GLU H  1 121 ? 5.908  -77.419  -48.599  1.00 55.19  ? 122 GLU H CA  1 
ATOM   8655  C  C   . GLU H  1 121 ? 6.248  -78.614  -47.730  1.00 53.96  ? 122 GLU H C   1 
ATOM   8656  O  O   . GLU H  1 121 ? 5.922  -78.655  -46.550  1.00 54.22  ? 122 GLU H O   1 
ATOM   8657  C  CB  . GLU H  1 121 ? 5.015  -77.861  -49.776  1.00 58.42  ? 122 GLU H CB  1 
ATOM   8658  C  CG  . GLU H  1 121 ? 3.751  -78.662  -49.362  1.00 62.02  ? 122 GLU H CG  1 
ATOM   8659  C  CD  . GLU H  1 121 ? 2.967  -79.228  -50.537  1.00 65.64  ? 122 GLU H CD  1 
ATOM   8660  O  OE1 . GLU H  1 121 ? 3.430  -79.127  -51.693  1.00 65.35  ? 122 GLU H OE1 1 
ATOM   8661  O  OE2 . GLU H  1 121 ? 1.882  -79.786  -50.288  1.00 68.89  ? 122 GLU H OE2 1 
ATOM   8662  N  N   . LYS H  1 122 ? 6.876  -79.597  -48.360  1.00 53.14  ? 123 LYS H N   1 
ATOM   8663  C  CA  . LYS H  1 122 ? 7.253  -80.852  -47.711  1.00 52.43  ? 123 LYS H CA  1 
ATOM   8664  C  C   . LYS H  1 122 ? 8.727  -80.805  -47.342  1.00 49.17  ? 123 LYS H C   1 
ATOM   8665  O  O   . LYS H  1 122 ? 9.414  -79.827  -47.630  1.00 47.64  ? 123 LYS H O   1 
ATOM   8666  C  CB  . LYS H  1 122 ? 7.037  -82.048  -48.652  1.00 53.96  ? 123 LYS H CB  1 
ATOM   8667  C  CG  . LYS H  1 122 ? 5.684  -82.142  -49.307  1.00 57.94  ? 123 LYS H CG  1 
ATOM   8668  C  CD  . LYS H  1 122 ? 5.593  -83.353  -50.264  1.00 59.95  ? 123 LYS H CD  1 
ATOM   8669  C  CE  . LYS H  1 122 ? 4.294  -83.352  -51.125  1.00 64.19  ? 123 LYS H CE  1 
ATOM   8670  N  NZ  . LYS H  1 122 ? 4.057  -84.638  -51.859  1.00 66.33  ? 123 LYS H NZ  1 
ATOM   8671  N  N   . ALA H  1 123 ? 9.210  -81.894  -46.749  1.00 48.55  ? 124 ALA H N   1 
ATOM   8672  C  CA  . ALA H  1 123 ? 10.620 -82.060  -46.422  1.00 46.04  ? 124 ALA H CA  1 
ATOM   8673  C  C   . ALA H  1 123 ? 11.466 -82.488  -47.624  1.00 45.31  ? 124 ALA H C   1 
ATOM   8674  O  O   . ALA H  1 123 ? 11.022 -83.240  -48.460  1.00 46.77  ? 124 ALA H O   1 
ATOM   8675  C  CB  . ALA H  1 123 ? 10.760 -83.071  -45.317  1.00 46.41  ? 124 ALA H CB  1 
ATOM   8676  N  N   . ASP H  1 124 ? 12.698 -81.998  -47.685  1.00 43.55  ? 125 ASP H N   1 
ATOM   8677  C  CA  . ASP H  1 124 ? 13.675 -82.374  -48.719  1.00 43.25  ? 125 ASP H CA  1 
ATOM   8678  C  C   . ASP H  1 124 ? 14.237 -83.746  -48.379  1.00 43.71  ? 125 ASP H C   1 
ATOM   8679  O  O   . ASP H  1 124 ? 14.790 -83.934  -47.306  1.00 43.13  ? 125 ASP H O   1 
ATOM   8680  C  CB  . ASP H  1 124 ? 14.812 -81.326  -48.799  1.00 41.52  ? 125 ASP H CB  1 
ATOM   8681  C  CG  . ASP H  1 124 ? 15.835 -81.616  -49.908  1.00 41.76  ? 125 ASP H CG  1 
ATOM   8682  O  OD1 . ASP H  1 124 ? 15.724 -82.651  -50.591  1.00 43.18  ? 125 ASP H OD1 1 
ATOM   8683  O  OD2 . ASP H  1 124 ? 16.771 -80.807  -50.099  1.00 40.78  ? 125 ASP H OD2 1 
ATOM   8684  N  N   . ASP H  1 125 ? 14.103 -84.701  -49.295  1.00 45.20  ? 126 ASP H N   1 
ATOM   8685  C  CA  . ASP H  1 125 ? 14.559 -86.077  -49.051  1.00 46.07  ? 126 ASP H CA  1 
ATOM   8686  C  C   . ASP H  1 125 ? 16.073 -86.229  -49.225  1.00 45.41  ? 126 ASP H C   1 
ATOM   8687  O  O   . ASP H  1 125 ? 16.593 -87.327  -49.164  1.00 46.57  ? 126 ASP H O   1 
ATOM   8688  C  CB  . ASP H  1 125 ? 13.775 -87.099  -49.912  1.00 48.45  ? 126 ASP H CB  1 
ATOM   8689  C  CG  . ASP H  1 125 ? 14.203 -87.123  -51.379  1.00 49.27  ? 126 ASP H CG  1 
ATOM   8690  O  OD1 . ASP H  1 125 ? 15.356 -86.747  -51.669  1.00 48.33  ? 126 ASP H OD1 1 
ATOM   8691  O  OD2 . ASP H  1 125 ? 13.394 -87.546  -52.247  1.00 50.93  ? 126 ASP H OD2 1 
ATOM   8692  N  N   . LEU H  1 126 ? 16.767 -85.117  -49.440  1.00 43.96  ? 127 LEU H N   1 
ATOM   8693  C  CA  . LEU H  1 126 ? 18.222 -85.086  -49.567  1.00 43.71  ? 127 LEU H CA  1 
ATOM   8694  C  C   . LEU H  1 126 ? 18.752 -86.009  -50.659  1.00 45.62  ? 127 LEU H C   1 
ATOM   8695  O  O   . LEU H  1 126 ? 19.874 -86.522  -50.564  1.00 46.52  ? 127 LEU H O   1 
ATOM   8696  C  CB  . LEU H  1 126 ? 18.895 -85.411  -48.234  1.00 43.40  ? 127 LEU H CB  1 
ATOM   8697  C  CG  . LEU H  1 126 ? 18.365 -84.644  -47.021  1.00 42.20  ? 127 LEU H CG  1 
ATOM   8698  C  CD1 . LEU H  1 126 ? 19.223 -84.874  -45.792  1.00 42.73  ? 127 LEU H CD1 1 
ATOM   8699  C  CD2 . LEU H  1 126 ? 18.275 -83.187  -47.331  1.00 40.86  ? 127 LEU H CD2 1 
ATOM   8700  N  N   . GLY H  1 127 ? 17.946 -86.208  -51.699  1.00 46.80  ? 128 GLY H N   1 
ATOM   8701  C  CA  . GLY H  1 127 ? 18.355 -86.980  -52.876  1.00 49.01  ? 128 GLY H CA  1 
ATOM   8702  C  C   . GLY H  1 127 ? 18.329 -88.492  -52.721  1.00 50.95  ? 128 GLY H C   1 
ATOM   8703  O  O   . GLY H  1 127 ? 18.608 -89.200  -53.678  1.00 53.12  ? 128 GLY H O   1 
ATOM   8704  N  N   . LYS H  1 128 ? 17.981 -88.985  -51.530  1.00 50.51  ? 129 LYS H N   1 
ATOM   8705  C  CA  . LYS H  1 128 ? 17.953 -90.429  -51.230  1.00 52.49  ? 129 LYS H CA  1 
ATOM   8706  C  C   . LYS H  1 128 ? 16.568 -91.052  -51.435  1.00 53.89  ? 129 LYS H C   1 
ATOM   8707  O  O   . LYS H  1 128 ? 16.226 -92.065  -50.831  1.00 55.03  ? 129 LYS H O   1 
ATOM   8708  C  CB  . LYS H  1 128 ? 18.381 -90.680  -49.788  1.00 51.92  ? 129 LYS H CB  1 
ATOM   8709  C  CG  . LYS H  1 128 ? 19.677 -90.018  -49.373  1.00 51.17  ? 129 LYS H CG  1 
ATOM   8710  C  CD  . LYS H  1 128 ? 20.272 -90.665  -48.110  1.00 52.31  ? 129 LYS H CD  1 
ATOM   8711  C  CE  . LYS H  1 128 ? 21.502 -89.875  -47.595  1.00 51.96  ? 129 LYS H CE  1 
ATOM   8712  N  NZ  . LYS H  1 128 ? 22.298 -90.621  -46.558  1.00 53.80  ? 129 LYS H NZ  1 
ATOM   8713  N  N   . GLY H  1 129 ? 15.780 -90.439  -52.304  1.00 54.18  ? 130 GLY H N   1 
ATOM   8714  C  CA  . GLY H  1 129 ? 14.390 -90.822  -52.513  1.00 55.77  ? 130 GLY H CA  1 
ATOM   8715  C  C   . GLY H  1 129 ? 14.215 -92.048  -53.394  1.00 58.92  ? 130 GLY H C   1 
ATOM   8716  O  O   . GLY H  1 129 ? 13.260 -92.799  -53.236  1.00 60.68  ? 130 GLY H O   1 
ATOM   8717  N  N   . GLY H  1 130 ? 15.125 -92.236  -54.346  1.00 59.94  ? 131 GLY H N   1 
ATOM   8718  C  CA  . GLY H  1 130 ? 15.060 -93.373  -55.261  1.00 63.43  ? 131 GLY H CA  1 
ATOM   8719  C  C   . GLY H  1 130 ? 14.360 -93.089  -56.573  1.00 65.55  ? 131 GLY H C   1 
ATOM   8720  O  O   . GLY H  1 130 ? 14.676 -93.701  -57.580  1.00 68.46  ? 131 GLY H O   1 
ATOM   8721  N  N   . ASN H  1 131 ? 13.420 -92.153  -56.571  1.00 64.76  ? 132 ASN H N   1 
ATOM   8722  C  CA  . ASN H  1 131 ? 12.730 -91.748  -57.800  1.00 67.12  ? 132 ASN H CA  1 
ATOM   8723  C  C   . ASN H  1 131 ? 13.518 -90.708  -58.619  1.00 66.31  ? 132 ASN H C   1 
ATOM   8724  O  O   . ASN H  1 131 ? 14.554 -90.189  -58.199  1.00 63.51  ? 132 ASN H O   1 
ATOM   8725  C  CB  . ASN H  1 131 ? 11.290 -91.277  -57.498  1.00 67.47  ? 132 ASN H CB  1 
ATOM   8726  C  CG  . ASN H  1 131 ? 11.230 -89.876  -56.960  1.00 64.60  ? 132 ASN H CG  1 
ATOM   8727  O  OD1 . ASN H  1 131 ? 12.257 -89.209  -56.780  1.00 62.11  ? 132 ASN H OD1 1 
ATOM   8728  N  ND2 . ASN H  1 131 ? 10.017 -89.406  -56.704  1.00 65.61  ? 132 ASN H ND2 1 
ATOM   8729  N  N   . GLU H  1 132 ? 12.997 -90.422  -59.800  1.00 69.17  ? 133 GLU H N   1 
ATOM   8730  C  CA  . GLU H  1 132 ? 13.604 -89.460  -60.722  1.00 69.60  ? 133 GLU H CA  1 
ATOM   8731  C  C   . GLU H  1 132 ? 13.698 -88.046  -60.132  1.00 66.08  ? 133 GLU H C   1 
ATOM   8732  O  O   . GLU H  1 132 ? 14.732 -87.382  -60.202  1.00 64.29  ? 133 GLU H O   1 
ATOM   8733  C  CB  . GLU H  1 132 ? 12.769 -89.401  -62.021  1.00 73.99  ? 133 GLU H CB  1 
ATOM   8734  C  CG  . GLU H  1 132 ? 13.074 -88.174  -62.945  1.00 75.24  ? 133 GLU H CG  1 
ATOM   8735  C  CD  . GLU H  1 132 ? 14.325 -88.348  -63.830  1.00 77.24  ? 133 GLU H CD  1 
ATOM   8736  O  OE1 . GLU H  1 132 ? 15.008 -89.400  -63.747  1.00 77.93  ? 133 GLU H OE1 1 
ATOM   8737  O  OE2 . GLU H  1 132 ? 14.616 -87.418  -64.618  1.00 78.32  ? 133 GLU H OE2 1 
ATOM   8738  N  N   . GLU H  1 133 ? 12.565 -87.599  -59.598  1.00 65.55  ? 134 GLU H N   1 
ATOM   8739  C  CA  . GLU H  1 133 ? 12.393 -86.233  -59.113  1.00 63.08  ? 134 GLU H CA  1 
ATOM   8740  C  C   . GLU H  1 133 ? 13.308 -85.949  -57.912  1.00 58.95  ? 134 GLU H C   1 
ATOM   8741  O  O   . GLU H  1 133 ? 13.776 -84.825  -57.752  1.00 57.10  ? 134 GLU H O   1 
ATOM   8742  C  CB  . GLU H  1 133 ? 10.901 -85.966  -58.766  1.00 64.20  ? 134 GLU H CB  1 
ATOM   8743  C  CG  . GLU H  1 133 ? 10.513 -84.467  -58.631  1.00 63.35  ? 134 GLU H CG  1 
ATOM   8744  C  CD  . GLU H  1 133 ? 10.543 -83.697  -59.957  1.00 66.21  ? 134 GLU H CD  1 
ATOM   8745  O  OE1 . GLU H  1 133 ? 10.719 -84.323  -61.034  1.00 69.52  ? 134 GLU H OE1 1 
ATOM   8746  O  OE2 . GLU H  1 133 ? 10.382 -82.458  -59.923  1.00 65.45  ? 134 GLU H OE2 1 
ATOM   8747  N  N   . SER H  1 134 ? 13.582 -86.960  -57.087  1.00 57.96  ? 135 SER H N   1 
ATOM   8748  C  CA  . SER H  1 134 ? 14.400 -86.766  -55.886  1.00 54.72  ? 135 SER H CA  1 
ATOM   8749  C  C   . SER H  1 134 ? 15.794 -86.267  -56.238  1.00 53.78  ? 135 SER H C   1 
ATOM   8750  O  O   . SER H  1 134 ? 16.439 -85.593  -55.458  1.00 51.37  ? 135 SER H O   1 
ATOM   8751  C  CB  . SER H  1 134 ? 14.508 -88.051  -55.091  1.00 54.84  ? 135 SER H CB  1 
ATOM   8752  O  OG  . SER H  1 134 ? 15.448 -87.893  -54.064  1.00 52.29  ? 135 SER H OG  1 
ATOM   8753  N  N   . THR H  1 135 ? 16.245 -86.623  -57.428  1.00 56.26  ? 136 THR H N   1 
ATOM   8754  C  CA  . THR H  1 135 ? 17.529 -86.194  -57.953  1.00 56.24  ? 136 THR H CA  1 
ATOM   8755  C  C   . THR H  1 135 ? 17.517 -84.764  -58.445  1.00 55.84  ? 136 THR H C   1 
ATOM   8756  O  O   . THR H  1 135 ? 18.560 -84.233  -58.770  1.00 56.06  ? 136 THR H O   1 
ATOM   8757  C  CB  . THR H  1 135 ? 17.933 -87.095  -59.091  1.00 59.55  ? 136 THR H CB  1 
ATOM   8758  O  OG1 . THR H  1 135 ? 18.475 -88.282  -58.535  1.00 59.85  ? 136 THR H OG1 1 
ATOM   8759  C  CG2 . THR H  1 135 ? 18.959 -86.464  -59.956  1.00 60.72  ? 136 THR H CG2 1 
ATOM   8760  N  N   . LYS H  1 136 ? 16.351 -84.137  -58.492  1.00 55.91  ? 137 LYS H N   1 
ATOM   8761  C  CA  . LYS H  1 136 ? 16.215 -82.757  -58.995  1.00 56.10  ? 137 LYS H CA  1 
ATOM   8762  C  C   . LYS H  1 136 ? 15.758 -81.768  -57.909  1.00 53.21  ? 137 LYS H C   1 
ATOM   8763  O  O   . LYS H  1 136 ? 16.476 -80.853  -57.538  1.00 51.39  ? 137 LYS H O   1 
ATOM   8764  C  CB  . LYS H  1 136 ? 15.195 -82.716  -60.139  1.00 59.60  ? 137 LYS H CB  1 
ATOM   8765  C  CG  . LYS H  1 136 ? 15.659 -83.292  -61.472  1.00 63.40  ? 137 LYS H CG  1 
ATOM   8766  C  CD  . LYS H  1 136 ? 14.510 -83.193  -62.522  1.00 67.63  ? 137 LYS H CD  1 
ATOM   8767  C  CE  . LYS H  1 136 ? 15.010 -83.239  -63.980  1.00 71.40  ? 137 LYS H CE  1 
ATOM   8768  N  NZ  . LYS H  1 136 ? 15.114 -84.636  -64.513  1.00 74.13  ? 137 LYS H NZ  1 
ATOM   8769  N  N   . THR H  1 137 ? 14.548 -81.974  -57.417  1.00 53.18  ? 138 THR H N   1 
ATOM   8770  C  CA  . THR H  1 137 ? 13.905 -81.042  -56.526  1.00 51.56  ? 138 THR H CA  1 
ATOM   8771  C  C   . THR H  1 137 ? 13.995 -81.471  -55.076  1.00 49.22  ? 138 THR H C   1 
ATOM   8772  O  O   . THR H  1 137 ? 13.741 -80.661  -54.174  1.00 47.81  ? 138 THR H O   1 
ATOM   8773  C  CB  . THR H  1 137 ? 12.433 -80.897  -56.891  1.00 54.06  ? 138 THR H CB  1 
ATOM   8774  O  OG1 . THR H  1 137 ? 11.719 -82.107  -56.576  1.00 55.12  ? 138 THR H OG1 1 
ATOM   8775  C  CG2 . THR H  1 137 ? 12.312 -80.601  -58.364  1.00 57.39  ? 138 THR H CG2 1 
ATOM   8776  N  N   . GLY H  1 138 ? 14.343 -82.734  -54.851  1.00 49.24  ? 139 GLY H N   1 
ATOM   8777  C  CA  . GLY H  1 138 ? 14.372 -83.305  -53.510  1.00 47.73  ? 139 GLY H CA  1 
ATOM   8778  C  C   . GLY H  1 138 ? 13.004 -83.748  -53.016  1.00 48.86  ? 139 GLY H C   1 
ATOM   8779  O  O   . GLY H  1 138 ? 12.845 -84.073  -51.840  1.00 47.98  ? 139 GLY H O   1 
ATOM   8780  N  N   . ASN H  1 139 ? 12.020 -83.770  -53.916  1.00 51.37  ? 140 ASN H N   1 
ATOM   8781  C  CA  . ASN H  1 139 ? 10.624 -84.116  -53.585  1.00 53.29  ? 140 ASN H CA  1 
ATOM   8782  C  C   . ASN H  1 139 ? 10.035 -83.274  -52.448  1.00 52.18  ? 140 ASN H C   1 
ATOM   8783  O  O   . ASN H  1 139 ? 9.113  -83.706  -51.760  1.00 53.30  ? 140 ASN H O   1 
ATOM   8784  C  CB  . ASN H  1 139 ? 10.493 -85.613  -53.252  1.00 54.45  ? 140 ASN H CB  1 
ATOM   8785  C  CG  . ASN H  1 139 ? 10.470 -86.491  -54.481  1.00 56.91  ? 140 ASN H CG  1 
ATOM   8786  O  OD1 . ASN H  1 139 ? 10.916 -87.626  -54.421  1.00 57.47  ? 140 ASN H OD1 1 
ATOM   8787  N  ND2 . ASN H  1 139 ? 9.941  -85.982  -55.589  1.00 58.65  ? 140 ASN H ND2 1 
ATOM   8788  N  N   . ALA H  1 140 ? 10.566 -82.064  -52.276  1.00 50.41  ? 141 ALA H N   1 
ATOM   8789  C  CA  . ALA H  1 140 ? 10.193 -81.171  -51.159  1.00 49.31  ? 141 ALA H CA  1 
ATOM   8790  C  C   . ALA H  1 140 ? 8.935  -80.348  -51.433  1.00 51.51  ? 141 ALA H C   1 
ATOM   8791  O  O   . ALA H  1 140 ? 8.495  -79.565  -50.583  1.00 51.16  ? 141 ALA H O   1 
ATOM   8792  C  CB  . ALA H  1 140 ? 11.325 -80.255  -50.834  1.00 46.73  ? 141 ALA H CB  1 
ATOM   8793  N  N   . GLY H  1 141 ? 8.381  -80.513  -52.630  1.00 54.11  ? 142 GLY H N   1 
ATOM   8794  C  CA  . GLY H  1 141 ? 7.061  -79.985  -52.949  1.00 57.32  ? 142 GLY H CA  1 
ATOM   8795  C  C   . GLY H  1 141 ? 7.017  -78.512  -53.314  1.00 57.60  ? 142 GLY H C   1 
ATOM   8796  O  O   . GLY H  1 141 ? 8.023  -77.932  -53.735  1.00 55.73  ? 142 GLY H O   1 
ATOM   8797  N  N   . SER H  1 142 ? 5.833  -77.921  -53.142  1.00 60.34  ? 143 SER H N   1 
ATOM   8798  C  CA  . SER H  1 142 ? 5.548  -76.556  -53.605  1.00 61.78  ? 143 SER H CA  1 
ATOM   8799  C  C   . SER H  1 142 ? 6.315  -75.503  -52.819  1.00 58.80  ? 143 SER H C   1 
ATOM   8800  O  O   . SER H  1 142 ? 6.880  -75.791  -51.760  1.00 56.15  ? 143 SER H O   1 
ATOM   8801  C  CB  . SER H  1 142 ? 4.052  -76.244  -53.509  1.00 65.95  ? 143 SER H CB  1 
ATOM   8802  O  OG  . SER H  1 142 ? 3.664  -75.989  -52.165  1.00 65.45  ? 143 SER H OG  1 
ATOM   8803  N  N   . ARG H  1 143 ? 6.290  -74.278  -53.335  1.00 59.80  ? 144 ARG H N   1 
ATOM   8804  C  CA  . ARG H  1 143 ? 7.036  -73.155  -52.760  1.00 57.48  ? 144 ARG H CA  1 
ATOM   8805  C  C   . ARG H  1 143 ? 6.130  -72.274  -51.886  1.00 59.17  ? 144 ARG H C   1 
ATOM   8806  O  O   . ARG H  1 143 ? 5.321  -71.482  -52.396  1.00 62.65  ? 144 ARG H O   1 
ATOM   8807  C  CB  . ARG H  1 143 ? 7.666  -72.343  -53.880  1.00 57.85  ? 144 ARG H CB  1 
ATOM   8808  C  CG  . ARG H  1 143 ? 8.617  -73.155  -54.691  1.00 56.63  ? 144 ARG H CG  1 
ATOM   8809  C  CD  . ARG H  1 143 ? 9.126  -72.420  -55.900  1.00 58.24  ? 144 ARG H CD  1 
ATOM   8810  N  NE  . ARG H  1 143 ? 9.932  -73.291  -56.761  1.00 57.73  ? 144 ARG H NE  1 
ATOM   8811  C  CZ  . ARG H  1 143 ? 10.599 -72.888  -57.839  1.00 58.97  ? 144 ARG H CZ  1 
ATOM   8812  N  NH1 . ARG H  1 143 ? 10.574 -71.621  -58.226  1.00 60.87  ? 144 ARG H NH1 1 
ATOM   8813  N  NH2 . ARG H  1 143 ? 11.299 -73.756  -58.540  1.00 59.35  ? 144 ARG H NH2 1 
ATOM   8814  N  N   . LEU H  1 144 ? 6.281  -72.405  -50.571  1.00 57.12  ? 145 LEU H N   1 
ATOM   8815  C  CA  . LEU H  1 144 ? 5.398  -71.738  -49.626  1.00 59.09  ? 145 LEU H CA  1 
ATOM   8816  C  C   . LEU H  1 144 ? 5.719  -70.259  -49.547  1.00 59.23  ? 145 LEU H C   1 
ATOM   8817  O  O   . LEU H  1 144 ? 4.831  -69.415  -49.685  1.00 62.89  ? 145 LEU H O   1 
ATOM   8818  C  CB  . LEU H  1 144 ? 5.502  -72.346  -48.229  1.00 57.48  ? 145 LEU H CB  1 
ATOM   8819  C  CG  . LEU H  1 144 ? 4.958  -73.760  -48.063  1.00 58.42  ? 145 LEU H CG  1 
ATOM   8820  C  CD1 . LEU H  1 144 ? 4.974  -74.196  -46.576  1.00 57.34  ? 145 LEU H CD1 1 
ATOM   8821  C  CD2 . LEU H  1 144 ? 3.557  -73.875  -48.676  1.00 62.86  ? 145 LEU H CD2 1 
ATOM   8822  N  N   . ALA H  1 145 ? 6.980  -69.940  -49.310  1.00 55.78  ? 146 ALA H N   1 
ATOM   8823  C  CA  . ALA H  1 145 ? 7.386  -68.558  -49.142  1.00 55.84  ? 146 ALA H CA  1 
ATOM   8824  C  C   . ALA H  1 145 ? 8.785  -68.384  -49.678  1.00 53.13  ? 146 ALA H C   1 
ATOM   8825  O  O   . ALA H  1 145 ? 9.588  -69.298  -49.613  1.00 50.71  ? 146 ALA H O   1 
ATOM   8826  C  CB  . ALA H  1 145 ? 7.310  -68.154  -47.674  1.00 55.45  ? 146 ALA H CB  1 
ATOM   8827  N  N   . CYS H  1 146 ? 9.066  -67.206  -50.222  1.00 54.14  ? 147 CYS H N   1 
ATOM   8828  C  CA  . CYS H  1 146 ? 10.376 -66.917  -50.788  1.00 52.12  ? 147 CYS H CA  1 
ATOM   8829  C  C   . CYS H  1 146 ? 10.711 -65.447  -50.759  1.00 53.13  ? 147 CYS H C   1 
ATOM   8830  O  O   . CYS H  1 146 ? 9.869  -64.621  -50.454  1.00 55.69  ? 147 CYS H O   1 
ATOM   8831  C  CB  . CYS H  1 146 ? 10.455 -67.428  -52.217  1.00 53.05  ? 147 CYS H CB  1 
ATOM   8832  S  SG  . CYS H  1 146 ? 9.400  -66.629  -53.375  1.00 56.97  ? 147 CYS H SG  1 
ATOM   8833  N  N   . GLY H  1 147 ? 11.959 -65.136  -51.066  1.00 51.63  ? 148 GLY H N   1 
ATOM   8834  C  CA  . GLY H  1 147 ? 12.412 -63.756  -51.119  1.00 52.81  ? 148 GLY H CA  1 
ATOM   8835  C  C   . GLY H  1 147 ? 13.758 -63.637  -51.783  1.00 51.66  ? 148 GLY H C   1 
ATOM   8836  O  O   . GLY H  1 147 ? 14.537 -64.573  -51.754  1.00 49.45  ? 148 GLY H O   1 
ATOM   8837  N  N   . VAL H  1 148 ? 14.027 -62.484  -52.382  1.00 53.59  ? 149 VAL H N   1 
ATOM   8838  C  CA  . VAL H  1 148 ? 15.310 -62.233  -53.027  1.00 53.12  ? 149 VAL H CA  1 
ATOM   8839  C  C   . VAL H  1 148 ? 16.385 -61.898  -51.995  1.00 51.15  ? 149 VAL H C   1 
ATOM   8840  O  O   . VAL H  1 148 ? 16.158 -61.112  -51.085  1.00 51.53  ? 149 VAL H O   1 
ATOM   8841  C  CB  . VAL H  1 148 ? 15.204 -61.094  -54.046  1.00 56.44  ? 149 VAL H CB  1 
ATOM   8842  C  CG1 . VAL H  1 148 ? 16.546 -60.839  -54.692  1.00 56.56  ? 149 VAL H CG1 1 
ATOM   8843  C  CG2 . VAL H  1 148 ? 14.182 -61.426  -55.087  1.00 58.91  ? 149 VAL H CG2 1 
ATOM   8844  N  N   . ILE H  1 149 ? 17.564 -62.489  -52.153  1.00 49.62  ? 150 ILE H N   1 
ATOM   8845  C  CA  . ILE H  1 149 ? 18.677 -62.292  -51.209  1.00 48.26  ? 150 ILE H CA  1 
ATOM   8846  C  C   . ILE H  1 149 ? 19.409 -60.976  -51.474  1.00 50.16  ? 150 ILE H C   1 
ATOM   8847  O  O   . ILE H  1 149 ? 19.920 -60.747  -52.577  1.00 51.65  ? 150 ILE H O   1 
ATOM   8848  C  CB  . ILE H  1 149 ? 19.716 -63.431  -51.283  1.00 46.48  ? 150 ILE H CB  1 
ATOM   8849  C  CG1 . ILE H  1 149 ? 19.115 -64.737  -50.758  1.00 44.62  ? 150 ILE H CG1 1 
ATOM   8850  C  CG2 . ILE H  1 149 ? 20.964 -63.065  -50.484  1.00 45.89  ? 150 ILE H CG2 1 
ATOM   8851  C  CD1 . ILE H  1 149 ? 19.993 -65.932  -51.015  1.00 43.49  ? 150 ILE H CD1 1 
ATOM   8852  N  N   . GLY H  1 150 ? 19.490 -60.135  -50.446  1.00 50.34  ? 151 GLY H N   1 
ATOM   8853  C  CA  . GLY H  1 150 ? 19.975 -58.769  -50.614  1.00 52.63  ? 151 GLY H CA  1 
ATOM   8854  C  C   . GLY H  1 150 ? 21.137 -58.408  -49.727  1.00 52.23  ? 151 GLY H C   1 
ATOM   8855  O  O   . GLY H  1 150 ? 21.331 -59.007  -48.671  1.00 50.56  ? 151 GLY H O   1 
ATOM   8856  N  N   . ILE H  1 151 ? 21.922 -57.433  -50.178  1.00 54.28  ? 152 ILE H N   1 
ATOM   8857  C  CA  . ILE H  1 151 ? 23.107 -56.988  -49.446  1.00 54.64  ? 152 ILE H CA  1 
ATOM   8858  C  C   . ILE H  1 151 ? 22.619 -56.256  -48.224  1.00 55.06  ? 152 ILE H C   1 
ATOM   8859  O  O   . ILE H  1 151 ? 21.713 -55.464  -48.312  1.00 56.66  ? 152 ILE H O   1 
ATOM   8860  C  CB  . ILE H  1 151 ? 24.028 -56.068  -50.285  1.00 57.32  ? 152 ILE H CB  1 
ATOM   8861  C  CG1 . ILE H  1 151 ? 24.568 -56.819  -51.508  1.00 57.48  ? 152 ILE H CG1 1 
ATOM   8862  C  CG2 . ILE H  1 151 ? 25.180 -55.557  -49.446  1.00 58.05  ? 152 ILE H CG2 1 
ATOM   8863  C  CD1 . ILE H  1 151 ? 25.460 -56.002  -52.403  1.00 60.59  ? 152 ILE H CD1 1 
ATOM   8864  N  N   . ALA H  1 152 ? 23.210 -56.555  -47.078  1.00 54.26  ? 153 ALA H N   1 
ATOM   8865  C  CA  . ALA H  1 152 ? 22.793 -55.971  -45.801  1.00 54.94  ? 153 ALA H CA  1 
ATOM   8866  C  C   . ALA H  1 152 ? 23.896 -55.129  -45.162  1.00 56.98  ? 153 ALA H C   1 
ATOM   8867  O  O   . ALA H  1 152 ? 25.081 -55.264  -45.484  1.00 57.34  ? 153 ALA H O   1 
ATOM   8868  C  CB  . ALA H  1 152 ? 22.368 -57.067  -44.851  1.00 52.84  ? 153 ALA H CB  1 
ATOM   8869  N  N   . GLN H  1 153 ? 23.509 -54.274  -44.228  1.00 58.73  ? 154 GLN H N   1 
ATOM   8870  C  CA  . GLN H  1 153 ? 24.490 -53.433  -43.530  1.00 61.34  ? 154 GLN H CA  1 
ATOM   8871  C  C   . GLN H  1 153 ? 25.307 -54.233  -42.507  1.00 60.55  ? 154 GLN H C   1 
ATOM   8872  O  O   . GLN H  1 153 ? 24.738 -54.973  -41.700  1.00 59.14  ? 154 GLN H O   1 
ATOM   8873  C  CB  . GLN H  1 153 ? 23.816 -52.241  -42.831  1.00 63.99  ? 154 GLN H CB  1 
ATOM   8874  C  CG  . GLN H  1 153 ? 24.835 -51.260  -42.171  1.00 67.12  ? 154 GLN H CG  1 
ATOM   8875  C  CD  . GLN H  1 153 ? 24.206 -50.006  -41.582  1.00 70.23  ? 154 GLN H CD  1 
ATOM   8876  O  OE1 . GLN H  1 153 ? 23.650 -49.180  -42.292  1.00 71.96  ? 154 GLN H OE1 1 
ATOM   8877  N  NE2 . GLN H  1 153 ? 24.306 -49.860  -40.277  1.00 71.36  ? 154 GLN H NE2 1 
ATOM   8878  O  OXT . GLN H  1 153 ? 26.541 -54.138  -42.451  1.00 61.76  ? 154 GLN H OXT 1 
ATOM   8879  N  N   . ALA I  1 1   ? 28.888 -127.596 -55.360  1.00 73.75  ? 2   ALA I N   1 
ATOM   8880  C  CA  . ALA I  1 1   ? 28.293 -127.697 -56.739  1.00 70.90  ? 2   ALA I CA  1 
ATOM   8881  C  C   . ALA I  1 1   ? 27.376 -126.501 -57.049  1.00 66.62  ? 2   ALA I C   1 
ATOM   8882  O  O   . ALA I  1 1   ? 26.746 -125.926 -56.126  1.00 66.13  ? 2   ALA I O   1 
ATOM   8883  C  CB  . ALA I  1 1   ? 27.515 -129.042 -56.924  1.00 71.80  ? 2   ALA I CB  1 
ATOM   8884  N  N   . THR I  1 2   ? 27.308 -126.129 -58.341  1.00 63.69  ? 3   THR I N   1 
ATOM   8885  C  CA  . THR I  1 2   ? 26.346 -125.101 -58.792  1.00 59.57  ? 3   THR I CA  1 
ATOM   8886  C  C   . THR I  1 2   ? 24.972 -125.735 -58.951  1.00 58.08  ? 3   THR I C   1 
ATOM   8887  O  O   . THR I  1 2   ? 24.833 -126.838 -59.480  1.00 58.89  ? 3   THR I O   1 
ATOM   8888  C  CB  . THR I  1 2   ? 26.717 -124.389 -60.139  1.00 57.78  ? 3   THR I CB  1 
ATOM   8889  O  OG1 . THR I  1 2   ? 28.121 -124.483 -60.379  1.00 60.43  ? 3   THR I OG1 1 
ATOM   8890  C  CG2 . THR I  1 2   ? 26.302 -122.882 -60.127  1.00 54.89  ? 3   THR I CG2 1 
ATOM   8891  N  N   . LYS I  1 3   ? 23.971 -125.014 -58.466  1.00 56.29  ? 4   LYS I N   1 
ATOM   8892  C  CA  . LYS I  1 3   ? 22.579 -125.405 -58.584  1.00 55.17  ? 4   LYS I CA  1 
ATOM   8893  C  C   . LYS I  1 3   ? 21.769 -124.234 -59.137  1.00 52.01  ? 4   LYS I C   1 
ATOM   8894  O  O   . LYS I  1 3   ? 22.134 -123.076 -58.954  1.00 51.17  ? 4   LYS I O   1 
ATOM   8895  C  CB  . LYS I  1 3   ? 22.017 -125.846 -57.228  1.00 57.25  ? 4   LYS I CB  1 
ATOM   8896  C  CG  . LYS I  1 3   ? 22.628 -127.127 -56.651  1.00 61.02  ? 4   LYS I CG  1 
ATOM   8897  C  CD  . LYS I  1 3   ? 21.825 -127.621 -55.435  1.00 63.49  ? 4   LYS I CD  1 
ATOM   8898  C  CE  . LYS I  1 3   ? 22.662 -128.470 -54.472  1.00 67.66  ? 4   LYS I CE  1 
ATOM   8899  N  NZ  . LYS I  1 3   ? 22.058 -128.464 -53.085  1.00 69.59  ? 4   LYS I NZ  1 
ATOM   8900  N  N   . ALA I  1 4   ? 20.694 -124.559 -59.846  1.00 50.61  ? 5   ALA I N   1 
ATOM   8901  C  CA  . ALA I  1 4   ? 19.734 -123.565 -60.292  1.00 48.31  ? 5   ALA I CA  1 
ATOM   8902  C  C   . ALA I  1 4   ? 18.341 -124.126 -60.161  1.00 48.30  ? 5   ALA I C   1 
ATOM   8903  O  O   . ALA I  1 4   ? 18.187 -125.317 -59.948  1.00 49.96  ? 5   ALA I O   1 
ATOM   8904  C  CB  . ALA I  1 4   ? 20.013 -123.149 -61.716  1.00 46.63  ? 5   ALA I CB  1 
ATOM   8905  N  N   . VAL I  1 5   ? 17.341 -123.252 -60.264  1.00 46.98  ? 6   VAL I N   1 
ATOM   8906  C  CA  . VAL I  1 5   ? 15.928 -123.638 -60.186  1.00 47.30  ? 6   VAL I CA  1 
ATOM   8907  C  C   . VAL I  1 5   ? 15.060 -122.703 -60.997  1.00 45.40  ? 6   VAL I C   1 
ATOM   8908  O  O   . VAL I  1 5   ? 15.423 -121.568 -61.232  1.00 44.20  ? 6   VAL I O   1 
ATOM   8909  C  CB  . VAL I  1 5   ? 15.410 -123.627 -58.752  1.00 49.25  ? 6   VAL I CB  1 
ATOM   8910  C  CG1 . VAL I  1 5   ? 15.135 -122.229 -58.325  1.00 49.08  ? 6   VAL I CG1 1 
ATOM   8911  C  CG2 . VAL I  1 5   ? 14.152 -124.437 -58.633  1.00 50.68  ? 6   VAL I CG2 1 
ATOM   8912  N  N   . CYS I  1 6   ? 13.908 -123.195 -61.422  1.00 45.67  ? 7   CYS I N   1 
ATOM   8913  C  CA  . CYS I  1 6   ? 12.984 -122.412 -62.244  1.00 44.72  ? 7   CYS I CA  1 
ATOM   8914  C  C   . CYS I  1 6   ? 11.520 -122.787 -62.010  1.00 46.13  ? 7   CYS I C   1 
ATOM   8915  O  O   . CYS I  1 6   ? 11.146 -123.948 -62.151  1.00 47.24  ? 7   CYS I O   1 
ATOM   8916  C  CB  . CYS I  1 6   ? 13.286 -122.594 -63.727  1.00 43.37  ? 7   CYS I CB  1 
ATOM   8917  S  SG  . CYS I  1 6   ? 12.058 -121.810 -64.796  1.00 42.30  ? 7   CYS I SG  1 
ATOM   8918  N  N   . VAL I  1 7   ? 10.697 -121.791 -61.682  1.00 46.45  ? 8   VAL I N   1 
ATOM   8919  C  CA  . VAL I  1 7   ? 9.261  -121.994 -61.502  1.00 48.02  ? 8   VAL I CA  1 
ATOM   8920  C  C   . VAL I  1 7   ? 8.504  -121.692 -62.801  1.00 47.27  ? 8   VAL I C   1 
ATOM   8921  O  O   . VAL I  1 7   ? 8.358  -120.531 -63.216  1.00 46.41  ? 8   VAL I O   1 
ATOM   8922  C  CB  . VAL I  1 7   ? 8.720  -121.124 -60.369  1.00 49.64  ? 8   VAL I CB  1 
ATOM   8923  C  CG1 . VAL I  1 7   ? 7.209  -121.173 -60.326  1.00 51.65  ? 8   VAL I CG1 1 
ATOM   8924  C  CG2 . VAL I  1 7   ? 9.316  -121.557 -59.043  1.00 51.10  ? 8   VAL I CG2 1 
ATOM   8925  N  N   . LEU I  1 8   ? 8.031  -122.756 -63.441  1.00 47.76  ? 9   LEU I N   1 
ATOM   8926  C  CA  . LEU I  1 8   ? 7.276  -122.645 -64.688  1.00 47.39  ? 9   LEU I CA  1 
ATOM   8927  C  C   . LEU I  1 8   ? 5.844  -122.227 -64.412  1.00 49.30  ? 9   LEU I C   1 
ATOM   8928  O  O   . LEU I  1 8   ? 5.164  -122.846 -63.617  1.00 51.52  ? 9   LEU I O   1 
ATOM   8929  C  CB  . LEU I  1 8   ? 7.283  -123.979 -65.427  1.00 47.70  ? 9   LEU I CB  1 
ATOM   8930  C  CG  . LEU I  1 8   ? 8.630  -124.368 -66.047  1.00 46.11  ? 9   LEU I CG  1 
ATOM   8931  C  CD1 . LEU I  1 8   ? 8.674  -125.833 -66.379  1.00 47.13  ? 9   LEU I CD1 1 
ATOM   8932  C  CD2 . LEU I  1 8   ? 8.916  -123.551 -67.289  1.00 44.56  ? 9   LEU I CD2 1 
ATOM   8933  N  N   . LYS I  1 9   ? 5.394  -121.166 -65.068  1.00 49.00  ? 10  LYS I N   1 
ATOM   8934  C  CA  . LYS I  1 9   ? 4.007  -120.671 -64.927  1.00 51.35  ? 10  LYS I CA  1 
ATOM   8935  C  C   . LYS I  1 9   ? 3.496  -120.064 -66.215  1.00 51.10  ? 10  LYS I C   1 
ATOM   8936  O  O   . LYS I  1 9   ? 4.268  -119.674 -67.080  1.00 49.39  ? 10  LYS I O   1 
ATOM   8937  C  CB  . LYS I  1 9   ? 3.897  -119.598 -63.848  1.00 52.51  ? 10  LYS I CB  1 
ATOM   8938  C  CG  . LYS I  1 9   ? 3.729  -120.131 -62.421  1.00 55.07  ? 10  LYS I CG  1 
ATOM   8939  C  CD  . LYS I  1 9   ? 3.016  -119.090 -61.508  1.00 57.82  ? 10  LYS I CD  1 
ATOM   8940  C  CE  . LYS I  1 9   ? 3.155  -119.416 -60.010  1.00 59.54  ? 10  LYS I CE  1 
ATOM   8941  N  NZ  . LYS I  1 9   ? 2.154  -120.427 -59.572  1.00 62.45  ? 10  LYS I NZ  1 
ATOM   8942  N  N   . GLY I  1 10  ? 2.186  -119.954 -66.329  1.00 53.52  ? 11  GLY I N   1 
ATOM   8943  C  CA  . GLY I  1 10  ? 1.597  -119.438 -67.562  1.00 54.02  ? 11  GLY I CA  1 
ATOM   8944  C  C   . GLY I  1 10  ? 0.137  -119.023 -67.472  1.00 57.40  ? 11  GLY I C   1 
ATOM   8945  O  O   . GLY I  1 10  ? -0.475 -119.061 -66.397  1.00 59.64  ? 11  GLY I O   1 
ATOM   8946  N  N   . ASP I  1 11  ? -0.412 -118.616 -68.619  1.00 58.15  ? 12  ASP I N   1 
ATOM   8947  C  CA  . ASP I  1 11  ? -1.790 -118.103 -68.705  1.00 61.58  ? 12  ASP I CA  1 
ATOM   8948  C  C   . ASP I  1 11  ? -2.837 -119.147 -68.335  1.00 64.22  ? 12  ASP I C   1 
ATOM   8949  O  O   . ASP I  1 11  ? -3.884 -118.814 -67.787  1.00 67.60  ? 12  ASP I O   1 
ATOM   8950  C  CB  . ASP I  1 11  ? -2.078 -117.549 -70.104  1.00 61.92  ? 12  ASP I CB  1 
ATOM   8951  C  CG  . ASP I  1 11  ? -1.782 -116.064 -70.206  1.00 62.37  ? 12  ASP I CG  1 
ATOM   8952  O  OD1 . ASP I  1 11  ? -2.177 -115.322 -69.285  1.00 64.62  ? 12  ASP I OD1 1 
ATOM   8953  O  OD2 . ASP I  1 11  ? -1.149 -115.630 -71.193  1.00 61.47  ? 12  ASP I OD2 1 
ATOM   8954  N  N   . GLY I  1 12  ? -2.537 -120.406 -68.626  1.00 63.14  ? 13  GLY I N   1 
ATOM   8955  C  CA  . GLY I  1 12  ? -3.467 -121.505 -68.374  1.00 65.83  ? 13  GLY I CA  1 
ATOM   8956  C  C   . GLY I  1 12  ? -3.053 -122.401 -67.222  1.00 65.74  ? 13  GLY I C   1 
ATOM   8957  O  O   . GLY I  1 12  ? -2.256 -121.989 -66.377  1.00 64.25  ? 13  GLY I O   1 
ATOM   8958  N  N   . PRO I  1 13  ? -3.562 -123.651 -67.208  1.00 67.64  ? 14  PRO I N   1 
ATOM   8959  C  CA  . PRO I  1 13  ? -3.416 -124.553 -66.074  1.00 68.88  ? 14  PRO I CA  1 
ATOM   8960  C  C   . PRO I  1 13  ? -2.028 -125.133 -65.924  1.00 65.75  ? 14  PRO I C   1 
ATOM   8961  O  O   . PRO I  1 13  ? -1.727 -125.673 -64.870  1.00 66.67  ? 14  PRO I O   1 
ATOM   8962  C  CB  . PRO I  1 13  ? -4.403 -125.678 -66.399  1.00 72.15  ? 14  PRO I CB  1 
ATOM   8963  C  CG  . PRO I  1 13  ? -4.376 -125.768 -67.882  1.00 70.65  ? 14  PRO I CG  1 
ATOM   8964  C  CD  . PRO I  1 13  ? -4.074 -124.368 -68.394  1.00 68.51  ? 14  PRO I CD  1 
ATOM   8965  N  N   . VAL I  1 14  ? -1.208 -125.032 -66.969  1.00 62.64  ? 15  VAL I N   1 
ATOM   8966  C  CA  . VAL I  1 14  ? 0.132  -125.611 -66.959  1.00 60.03  ? 15  VAL I CA  1 
ATOM   8967  C  C   . VAL I  1 14  ? 1.017  -124.884 -65.941  1.00 58.43  ? 15  VAL I C   1 
ATOM   8968  O  O   . VAL I  1 14  ? 1.119  -123.652 -65.959  1.00 57.35  ? 15  VAL I O   1 
ATOM   8969  C  CB  . VAL I  1 14  ? 0.798  -125.566 -68.350  1.00 57.54  ? 15  VAL I CB  1 
ATOM   8970  C  CG1 . VAL I  1 14  ? 2.132  -126.298 -68.313  1.00 55.61  ? 15  VAL I CG1 1 
ATOM   8971  C  CG2 . VAL I  1 14  ? -0.112 -126.177 -69.401  1.00 59.42  ? 15  VAL I CG2 1 
ATOM   8972  N  N   . GLN I  1 15  ? 1.604  -125.655 -65.031  1.00 58.64  ? 16  GLN I N   1 
ATOM   8973  C  CA  . GLN I  1 15  ? 2.544  -125.125 -64.061  1.00 57.39  ? 16  GLN I CA  1 
ATOM   8974  C  C   . GLN I  1 15  ? 3.445  -126.233 -63.530  1.00 57.42  ? 16  GLN I C   1 
ATOM   8975  O  O   . GLN I  1 15  ? 3.127  -127.403 -63.620  1.00 59.14  ? 16  GLN I O   1 
ATOM   8976  C  CB  . GLN I  1 15  ? 1.829  -124.400 -62.913  1.00 59.69  ? 16  GLN I CB  1 
ATOM   8977  C  CG  . GLN I  1 15  ? 0.761  -125.207 -62.202  1.00 64.11  ? 16  GLN I CG  1 
ATOM   8978  C  CD  . GLN I  1 15  ? 0.270  -124.557 -60.902  1.00 67.12  ? 16  GLN I CD  1 
ATOM   8979  O  OE1 . GLN I  1 15  ? -0.171 -125.248 -59.975  1.00 70.62  ? 16  GLN I OE1 1 
ATOM   8980  N  NE2 . GLN I  1 15  ? 0.354  -123.233 -60.827  1.00 65.99  ? 16  GLN I NE2 1 
ATOM   8981  N  N   . GLY I  1 16  ? 4.584  -125.831 -62.981  1.00 55.87  ? 17  GLY I N   1 
ATOM   8982  C  CA  . GLY I  1 16  ? 5.587  -126.759 -62.461  1.00 55.94  ? 17  GLY I CA  1 
ATOM   8983  C  C   . GLY I  1 16  ? 6.871  -126.119 -61.929  1.00 54.05  ? 17  GLY I C   1 
ATOM   8984  O  O   . GLY I  1 16  ? 7.099  -124.911 -62.023  1.00 52.21  ? 17  GLY I O   1 
ATOM   8985  N  N   . ILE I  1 17  ? 7.717  -126.969 -61.376  1.00 54.79  ? 18  ILE I N   1 
ATOM   8986  C  CA  . ILE I  1 17  ? 9.015  -126.581 -60.841  1.00 53.56  ? 18  ILE I CA  1 
ATOM   8987  C  C   . ILE I  1 17  ? 10.086 -127.458 -61.439  1.00 52.88  ? 18  ILE I C   1 
ATOM   8988  O  O   . ILE I  1 17  ? 9.959  -128.650 -61.394  1.00 55.11  ? 18  ILE I O   1 
ATOM   8989  C  CB  . ILE I  1 17  ? 9.069  -126.820 -59.334  1.00 56.27  ? 18  ILE I CB  1 
ATOM   8990  C  CG1 . ILE I  1 17  ? 8.422  -125.658 -58.572  1.00 56.94  ? 18  ILE I CG1 1 
ATOM   8991  C  CG2 . ILE I  1 17  ? 10.516 -127.057 -58.891  1.00 55.97  ? 18  ILE I CG2 1 
ATOM   8992  C  CD1 . ILE I  1 17  ? 8.705  -125.679 -57.061  1.00 59.48  ? 18  ILE I CD1 1 
ATOM   8993  N  N   . ILE I  1 18  ? 11.147 -126.877 -61.977  1.00 50.64  ? 19  ILE I N   1 
ATOM   8994  C  CA  . ILE I  1 18  ? 12.257 -127.656 -62.565  1.00 50.50  ? 19  ILE I CA  1 
ATOM   8995  C  C   . ILE I  1 18  ? 13.599 -127.285 -61.941  1.00 50.22  ? 19  ILE I C   1 
ATOM   8996  O  O   . ILE I  1 18  ? 13.953 -126.116 -61.878  1.00 48.83  ? 19  ILE I O   1 
ATOM   8997  C  CB  . ILE I  1 18  ? 12.383 -127.433 -64.081  1.00 48.58  ? 19  ILE I CB  1 
ATOM   8998  C  CG1 . ILE I  1 18  ? 11.182 -128.007 -64.817  1.00 49.44  ? 19  ILE I CG1 1 
ATOM   8999  C  CG2 . ILE I  1 18  ? 13.643 -128.092 -64.610  1.00 48.72  ? 19  ILE I CG2 1 
ATOM   9000  C  CD1 . ILE I  1 18  ? 11.108 -129.518 -64.789  1.00 52.13  ? 19  ILE I CD1 1 
ATOM   9001  N  N   . ASN I  1 19  ? 14.353 -128.279 -61.504  1.00 52.07  ? 20  ASN I N   1 
ATOM   9002  C  CA  . ASN I  1 19  ? 15.656 -128.055 -60.890  1.00 52.44  ? 20  ASN I CA  1 
ATOM   9003  C  C   . ASN I  1 19  ? 16.816 -128.324 -61.827  1.00 52.13  ? 20  ASN I C   1 
ATOM   9004  O  O   . ASN I  1 19  ? 16.728 -129.167 -62.720  1.00 52.82  ? 20  ASN I O   1 
ATOM   9005  C  CB  . ASN I  1 19  ? 15.822 -128.964 -59.704  1.00 55.62  ? 20  ASN I CB  1 
ATOM   9006  C  CG  . ASN I  1 19  ? 14.841 -128.680 -58.652  1.00 56.90  ? 20  ASN I CG  1 
ATOM   9007  O  OD1 . ASN I  1 19  ? 13.854 -129.401 -58.503  1.00 58.95  ? 20  ASN I OD1 1 
ATOM   9008  N  ND2 . ASN I  1 19  ? 15.080 -127.610 -57.902  1.00 56.20  ? 20  ASN I ND2 1 
ATOM   9009  N  N   . PHE I  1 20  ? 17.921 -127.624 -61.589  1.00 51.60  ? 21  PHE I N   1 
ATOM   9010  C  CA  . PHE I  1 20  ? 19.174 -127.854 -62.308  1.00 51.77  ? 21  PHE I CA  1 
ATOM   9011  C  C   . PHE I  1 20  ? 20.275 -128.131 -61.310  1.00 54.03  ? 21  PHE I C   1 
ATOM   9012  O  O   . PHE I  1 20  ? 20.257 -127.598 -60.205  1.00 54.45  ? 21  PHE I O   1 
ATOM   9013  C  CB  . PHE I  1 20  ? 19.552 -126.644 -63.141  1.00 49.44  ? 21  PHE I CB  1 
ATOM   9014  C  CG  . PHE I  1 20  ? 18.541 -126.291 -64.204  1.00 47.51  ? 21  PHE I CG  1 
ATOM   9015  C  CD1 . PHE I  1 20  ? 17.389 -125.588 -63.882  1.00 46.29  ? 21  PHE I CD1 1 
ATOM   9016  C  CD2 . PHE I  1 20  ? 18.761 -126.627 -65.525  1.00 47.23  ? 21  PHE I CD2 1 
ATOM   9017  C  CE1 . PHE I  1 20  ? 16.481 -125.249 -64.849  1.00 44.85  ? 21  PHE I CE1 1 
ATOM   9018  C  CE2 . PHE I  1 20  ? 17.852 -126.290 -66.489  1.00 45.73  ? 21  PHE I CE2 1 
ATOM   9019  C  CZ  . PHE I  1 20  ? 16.709 -125.603 -66.151  1.00 44.68  ? 21  PHE I CZ  1 
ATOM   9020  N  N   . GLU I  1 21  ? 21.222 -128.978 -61.697  1.00 56.06  ? 22  GLU I N   1 
ATOM   9021  C  CA  . GLU I  1 21  ? 22.397 -129.271 -60.866  1.00 58.72  ? 22  GLU I CA  1 
ATOM   9022  C  C   . GLU I  1 21  ? 23.629 -129.700 -61.682  1.00 60.23  ? 22  GLU I C   1 
ATOM   9023  O  O   . GLU I  1 21  ? 23.661 -130.771 -62.278  1.00 62.01  ? 22  GLU I O   1 
ATOM   9024  C  CB  . GLU I  1 21  ? 22.083 -130.323 -59.810  1.00 61.78  ? 22  GLU I CB  1 
ATOM   9025  C  CG  . GLU I  1 21  ? 23.299 -130.605 -58.893  1.00 65.50  ? 22  GLU I CG  1 
ATOM   9026  C  CD  . GLU I  1 21  ? 22.970 -131.432 -57.633  1.00 69.35  ? 22  GLU I CD  1 
ATOM   9027  O  OE1 . GLU I  1 21  ? 21.932 -132.147 -57.627  1.00 70.28  ? 22  GLU I OE1 1 
ATOM   9028  O  OE2 . GLU I  1 21  ? 23.761 -131.360 -56.650  1.00 71.55  ? 22  GLU I OE2 1 
ATOM   9029  N  N   . GLN I  1 22  ? 24.636 -128.837 -61.693  1.00 59.96  ? 23  GLN I N   1 
ATOM   9030  C  CA  . GLN I  1 22  ? 25.891 -129.087 -62.388  1.00 61.93  ? 23  GLN I CA  1 
ATOM   9031  C  C   . GLN I  1 22  ? 26.963 -129.302 -61.326  1.00 65.21  ? 23  GLN I C   1 
ATOM   9032  O  O   . GLN I  1 22  ? 27.381 -128.357 -60.647  1.00 64.73  ? 23  GLN I O   1 
ATOM   9033  C  CB  . GLN I  1 22  ? 26.254 -127.897 -63.297  1.00 59.64  ? 23  GLN I CB  1 
ATOM   9034  C  CG  . GLN I  1 22  ? 27.453 -128.129 -64.208  1.00 61.77  ? 23  GLN I CG  1 
ATOM   9035  C  CD  . GLN I  1 22  ? 27.794 -126.925 -65.056  1.00 60.09  ? 23  GLN I CD  1 
ATOM   9036  O  OE1 . GLN I  1 22  ? 27.769 -125.801 -64.582  1.00 58.71  ? 23  GLN I OE1 1 
ATOM   9037  N  NE2 . GLN I  1 22  ? 28.126 -127.156 -66.311  1.00 61.04  ? 23  GLN I NE2 1 
ATOM   9038  N  N   . LYS I  1 23  ? 27.409 -130.547 -61.177  1.00 68.92  ? 24  LYS I N   1 
ATOM   9039  C  CA  . LYS I  1 23  ? 28.399 -130.862 -60.141  1.00 72.61  ? 24  LYS I CA  1 
ATOM   9040  C  C   . LYS I  1 23  ? 29.736 -130.220 -60.409  1.00 73.60  ? 24  LYS I C   1 
ATOM   9041  O  O   . LYS I  1 23  ? 30.417 -129.830 -59.471  1.00 75.34  ? 24  LYS I O   1 
ATOM   9042  C  CB  . LYS I  1 23  ? 28.599 -132.371 -59.987  1.00 76.93  ? 24  LYS I CB  1 
ATOM   9043  C  CG  . LYS I  1 23  ? 27.363 -133.092 -59.458  1.00 77.36  ? 24  LYS I CG  1 
ATOM   9044  C  CD  . LYS I  1 23  ? 27.737 -134.350 -58.672  1.00 82.71  ? 24  LYS I CD  1 
ATOM   9045  C  CE  . LYS I  1 23  ? 26.599 -135.378 -58.688  1.00 83.83  ? 24  LYS I CE  1 
ATOM   9046  N  NZ  . LYS I  1 23  ? 27.041 -136.733 -58.226  1.00 89.40  ? 24  LYS I NZ  1 
ATOM   9047  N  N   . GLU I  1 24  ? 30.116 -130.132 -61.680  1.00 73.24  ? 25  GLU I N   1 
ATOM   9048  C  CA  . GLU I  1 24  ? 31.441 -129.603 -62.056  1.00 75.14  ? 25  GLU I CA  1 
ATOM   9049  C  C   . GLU I  1 24  ? 31.392 -128.692 -63.260  1.00 72.40  ? 25  GLU I C   1 
ATOM   9050  O  O   . GLU I  1 24  ? 30.733 -128.999 -64.243  1.00 71.12  ? 25  GLU I O   1 
ATOM   9051  C  CB  . GLU I  1 24  ? 32.402 -130.752 -62.323  1.00 80.14  ? 25  GLU I CB  1 
ATOM   9052  C  CG  . GLU I  1 24  ? 32.452 -131.707 -61.140  1.00 83.69  ? 25  GLU I CG  1 
ATOM   9053  C  CD  . GLU I  1 24  ? 33.594 -132.676 -61.215  1.00 90.10  ? 25  GLU I CD  1 
ATOM   9054  O  OE1 . GLU I  1 24  ? 33.806 -133.277 -62.323  1.00 91.90  ? 25  GLU I OE1 1 
ATOM   9055  O  OE2 . GLU I  1 24  ? 34.260 -132.834 -60.146  1.00 93.58  ? 25  GLU I OE2 1 
ATOM   9056  N  N   . SER I  1 25  ? 32.120 -127.586 -63.173  1.00 72.20  ? 26  SER I N   1 
ATOM   9057  C  CA  . SER I  1 25  ? 32.055 -126.498 -64.166  1.00 69.98  ? 26  SER I CA  1 
ATOM   9058  C  C   . SER I  1 25  ? 32.165 -126.955 -65.622  1.00 70.84  ? 26  SER I C   1 
ATOM   9059  O  O   . SER I  1 25  ? 31.515 -126.394 -66.517  1.00 68.21  ? 26  SER I O   1 
ATOM   9060  C  CB  . SER I  1 25  ? 33.149 -125.470 -63.884  1.00 71.43  ? 26  SER I CB  1 
ATOM   9061  O  OG  . SER I  1 25  ? 34.384 -126.100 -63.617  1.00 76.48  ? 26  SER I OG  1 
ATOM   9062  N  N   . ASN I  1 26  ? 32.992 -127.974 -65.837  1.00 74.95  ? 27  ASN I N   1 
ATOM   9063  C  CA  . ASN I  1 26  ? 33.203 -128.572 -67.166  1.00 76.88  ? 27  ASN I CA  1 
ATOM   9064  C  C   . ASN I  1 26  ? 32.257 -129.765 -67.489  1.00 76.56  ? 27  ASN I C   1 
ATOM   9065  O  O   . ASN I  1 26  ? 32.327 -130.374 -68.557  1.00 78.27  ? 27  ASN I O   1 
ATOM   9066  C  CB  . ASN I  1 26  ? 34.665 -129.013 -67.308  1.00 82.16  ? 27  ASN I CB  1 
ATOM   9067  C  CG  . ASN I  1 26  ? 35.007 -130.192 -66.425  1.00 85.70  ? 27  ASN I CG  1 
ATOM   9068  O  OD1 . ASN I  1 26  ? 34.607 -130.256 -65.255  1.00 84.48  ? 27  ASN I OD1 1 
ATOM   9069  N  ND2 . ASN I  1 26  ? 35.756 -131.133 -66.976  1.00 90.26  ? 27  ASN I ND2 1 
ATOM   9070  N  N   . GLY I  1 27  ? 31.353 -130.072 -66.569  1.00 74.61  ? 28  GLY I N   1 
ATOM   9071  C  CA  . GLY I  1 27  ? 30.579 -131.308 -66.629  1.00 75.22  ? 28  GLY I CA  1 
ATOM   9072  C  C   . GLY I  1 27  ? 29.134 -131.142 -67.020  1.00 71.17  ? 28  GLY I C   1 
ATOM   9073  O  O   . GLY I  1 27  ? 28.692 -130.052 -67.311  1.00 67.86  ? 28  GLY I O   1 
ATOM   9074  N  N   . PRO I  1 28  ? 28.381 -132.242 -67.016  1.00 71.97  ? 29  PRO I N   1 
ATOM   9075  C  CA  . PRO I  1 28  ? 27.009 -132.219 -67.472  1.00 68.98  ? 29  PRO I CA  1 
ATOM   9076  C  C   . PRO I  1 28  ? 26.068 -131.685 -66.395  1.00 65.97  ? 29  PRO I C   1 
ATOM   9077  O  O   . PRO I  1 28  ? 26.408 -131.710 -65.189  1.00 66.90  ? 29  PRO I O   1 
ATOM   9078  C  CB  . PRO I  1 28  ? 26.712 -133.701 -67.744  1.00 72.01  ? 29  PRO I CB  1 
ATOM   9079  C  CG  . PRO I  1 28  ? 27.482 -134.400 -66.705  1.00 75.45  ? 29  PRO I CG  1 
ATOM   9080  C  CD  . PRO I  1 28  ? 28.742 -133.570 -66.499  1.00 76.20  ? 29  PRO I CD  1 
ATOM   9081  N  N   . VAL I  1 29  ? 24.898 -131.234 -66.859  1.00 62.62  ? 30  VAL I N   1 
ATOM   9082  C  CA  . VAL I  1 29  ? 23.876 -130.638 -66.013  1.00 59.81  ? 30  VAL I CA  1 
ATOM   9083  C  C   . VAL I  1 29  ? 22.689 -131.583 -65.907  1.00 60.11  ? 30  VAL I C   1 
ATOM   9084  O  O   . VAL I  1 29  ? 22.067 -131.903 -66.910  1.00 59.76  ? 30  VAL I O   1 
ATOM   9085  C  CB  . VAL I  1 29  ? 23.374 -129.300 -66.603  1.00 56.28  ? 30  VAL I CB  1 
ATOM   9086  C  CG1 . VAL I  1 29  ? 22.261 -128.726 -65.737  1.00 53.84  ? 30  VAL I CG1 1 
ATOM   9087  C  CG2 . VAL I  1 29  ? 24.520 -128.314 -66.767  1.00 55.98  ? 30  VAL I CG2 1 
ATOM   9088  N  N   . LYS I  1 30  ? 22.384 -132.033 -64.698  1.00 61.29  ? 31  LYS I N   1 
ATOM   9089  C  CA  . LYS I  1 30  ? 21.166 -132.803 -64.460  1.00 61.85  ? 31  LYS I CA  1 
ATOM   9090  C  C   . LYS I  1 30  ? 19.990 -131.872 -64.352  1.00 58.49  ? 31  LYS I C   1 
ATOM   9091  O  O   . LYS I  1 30  ? 20.047 -130.899 -63.635  1.00 57.23  ? 31  LYS I O   1 
ATOM   9092  C  CB  . LYS I  1 30  ? 21.275 -133.648 -63.194  1.00 65.11  ? 31  LYS I CB  1 
ATOM   9093  C  CG  . LYS I  1 30  ? 22.230 -134.825 -63.381  1.00 69.73  ? 31  LYS I CG  1 
ATOM   9094  C  CD  . LYS I  1 30  ? 22.083 -135.890 -62.303  1.00 74.10  ? 31  LYS I CD  1 
ATOM   9095  C  CE  . LYS I  1 30  ? 23.049 -137.071 -62.568  1.00 78.63  ? 31  LYS I CE  1 
ATOM   9096  N  NZ  . LYS I  1 30  ? 22.851 -138.228 -61.629  1.00 83.33  ? 31  LYS I NZ  1 
ATOM   9097  N  N   . VAL I  1 31  ? 18.924 -132.179 -65.069  1.00 57.74  ? 32  VAL I N   1 
ATOM   9098  C  CA  . VAL I  1 31  ? 17.711 -131.379 -65.034  1.00 55.26  ? 32  VAL I CA  1 
ATOM   9099  C  C   . VAL I  1 31  ? 16.564 -132.263 -64.579  1.00 57.10  ? 32  VAL I C   1 
ATOM   9100  O  O   . VAL I  1 31  ? 16.267 -133.279 -65.220  1.00 59.01  ? 32  VAL I O   1 
ATOM   9101  C  CB  . VAL I  1 31  ? 17.372 -130.832 -66.416  1.00 53.11  ? 32  VAL I CB  1 
ATOM   9102  C  CG1 . VAL I  1 31  ? 16.160 -129.897 -66.344  1.00 50.62  ? 32  VAL I CG1 1 
ATOM   9103  C  CG2 . VAL I  1 31  ? 18.575 -130.126 -66.997  1.00 52.35  ? 32  VAL I CG2 1 
ATOM   9104  N  N   . TRP I  1 32  ? 15.914 -131.899 -63.480  1.00 57.11  ? 33  TRP I N   1 
ATOM   9105  C  CA  . TRP I  1 32  ? 14.787 -132.710 -62.986  1.00 59.34  ? 33  TRP I CA  1 
ATOM   9106  C  C   . TRP I  1 32  ? 13.721 -131.907 -62.264  1.00 58.46  ? 33  TRP I C   1 
ATOM   9107  O  O   . TRP I  1 32  ? 13.971 -130.813 -61.757  1.00 57.06  ? 33  TRP I O   1 
ATOM   9108  C  CB  . TRP I  1 32  ? 15.275 -133.820 -62.064  1.00 63.15  ? 33  TRP I CB  1 
ATOM   9109  C  CG  . TRP I  1 32  ? 15.426 -133.416 -60.623  1.00 64.28  ? 33  TRP I CG  1 
ATOM   9110  C  CD1 . TRP I  1 32  ? 14.562 -133.681 -59.603  1.00 66.75  ? 33  TRP I CD1 1 
ATOM   9111  C  CD2 . TRP I  1 32  ? 16.519 -132.696 -60.044  1.00 63.52  ? 33  TRP I CD2 1 
ATOM   9112  N  NE1 . TRP I  1 32  ? 15.043 -133.161 -58.420  1.00 67.15  ? 33  TRP I NE1 1 
ATOM   9113  C  CE2 . TRP I  1 32  ? 16.245 -132.557 -58.664  1.00 65.24  ? 33  TRP I CE2 1 
ATOM   9114  C  CE3 . TRP I  1 32  ? 17.707 -132.157 -60.558  1.00 62.19  ? 33  TRP I CE3 1 
ATOM   9115  C  CZ2 . TRP I  1 32  ? 17.106 -131.911 -57.796  1.00 65.69  ? 33  TRP I CZ2 1 
ATOM   9116  C  CZ3 . TRP I  1 32  ? 18.569 -131.510 -59.692  1.00 62.56  ? 33  TRP I CZ3 1 
ATOM   9117  C  CH2 . TRP I  1 32  ? 18.263 -131.391 -58.323  1.00 64.25  ? 33  TRP I CH2 1 
ATOM   9118  N  N   . GLY I  1 33  ? 12.527 -132.469 -62.214  1.00 59.93  ? 34  GLY I N   1 
ATOM   9119  C  CA  . GLY I  1 33  ? 11.411 -131.817 -61.559  1.00 59.85  ? 34  GLY I CA  1 
ATOM   9120  C  C   . GLY I  1 33  ? 10.096 -132.394 -62.010  1.00 61.34  ? 34  GLY I C   1 
ATOM   9121  O  O   . GLY I  1 33  ? 10.053 -133.482 -62.564  1.00 63.27  ? 34  GLY I O   1 
ATOM   9122  N  N   . SER I  1 34  ? 9.021  -131.643 -61.791  1.00 60.96  ? 35  SER I N   1 
ATOM   9123  C  CA  . SER I  1 34  ? 7.665  -132.092 -62.109  1.00 62.68  ? 35  SER I CA  1 
ATOM   9124  C  C   . SER I  1 34  ? 6.785  -130.970 -62.671  1.00 60.54  ? 35  SER I C   1 
ATOM   9125  O  O   . SER I  1 34  ? 6.531  -129.974 -62.002  1.00 59.99  ? 35  SER I O   1 
ATOM   9126  C  CB  . SER I  1 34  ? 7.026  -132.682 -60.853  1.00 66.66  ? 35  SER I CB  1 
ATOM   9127  O  OG  . SER I  1 34  ? 5.832  -133.364 -61.170  1.00 69.38  ? 35  SER I OG  1 
ATOM   9128  N  N   . ILE I  1 35  ? 6.338  -131.140 -63.911  1.00 59.88  ? 36  ILE I N   1 
ATOM   9129  C  CA  . ILE I  1 35  ? 5.369  -130.225 -64.539  1.00 58.82  ? 36  ILE I CA  1 
ATOM   9130  C  C   . ILE I  1 35  ? 3.998  -130.882 -64.599  1.00 62.03  ? 36  ILE I C   1 
ATOM   9131  O  O   . ILE I  1 35  ? 3.898  -132.074 -64.840  1.00 64.19  ? 36  ILE I O   1 
ATOM   9132  C  CB  . ILE I  1 35  ? 5.740  -129.868 -65.984  1.00 56.17  ? 36  ILE I CB  1 
ATOM   9133  C  CG1 . ILE I  1 35  ? 7.156  -129.336 -66.058  1.00 53.69  ? 36  ILE I CG1 1 
ATOM   9134  C  CG2 . ILE I  1 35  ? 4.773  -128.838 -66.544  1.00 55.13  ? 36  ILE I CG2 1 
ATOM   9135  C  CD1 . ILE I  1 35  ? 7.558  -129.034 -67.456  1.00 52.00  ? 36  ILE I CD1 1 
ATOM   9136  N  N   . LYS I  1 36  ? 2.944  -130.098 -64.394  1.00 62.83  ? 37  LYS I N   1 
ATOM   9137  C  CA  . LYS I  1 36  ? 1.568  -130.621 -64.395  1.00 66.23  ? 37  LYS I CA  1 
ATOM   9138  C  C   . LYS I  1 36  ? 0.562  -129.711 -65.117  1.00 65.79  ? 37  LYS I C   1 
ATOM   9139  O  O   . LYS I  1 36  ? 0.864  -128.568 -65.460  1.00 63.07  ? 37  LYS I O   1 
ATOM   9140  C  CB  . LYS I  1 36  ? 1.094  -130.911 -62.966  1.00 69.72  ? 37  LYS I CB  1 
ATOM   9141  C  CG  . LYS I  1 36  ? 1.086  -129.719 -62.034  1.00 69.36  ? 37  LYS I CG  1 
ATOM   9142  C  CD  . LYS I  1 36  ? 0.144  -129.973 -60.860  1.00 74.31  ? 37  LYS I CD  1 
ATOM   9143  C  CE  . LYS I  1 36  ? 0.200  -128.859 -59.815  1.00 74.47  ? 37  LYS I CE  1 
ATOM   9144  N  NZ  . LYS I  1 36  ? -0.899 -129.002 -58.824  1.00 79.32  ? 37  LYS I NZ  1 
ATOM   9145  N  N   . GLY I  1 37  ? -0.631 -130.249 -65.344  1.00 68.94  ? 38  GLY I N   1 
ATOM   9146  C  CA  . GLY I  1 37  ? -1.663 -129.587 -66.138  1.00 69.43  ? 38  GLY I CA  1 
ATOM   9147  C  C   . GLY I  1 37  ? -1.475 -129.771 -67.634  1.00 67.79  ? 38  GLY I C   1 
ATOM   9148  O  O   . GLY I  1 37  ? -2.101 -129.068 -68.435  1.00 67.51  ? 38  GLY I O   1 
ATOM   9149  N  N   . LEU I  1 38  ? -0.630 -130.737 -68.006  1.00 67.16  ? 39  LEU I N   1 
ATOM   9150  C  CA  . LEU I  1 38  ? -0.190 -130.935 -69.404  1.00 65.48  ? 39  LEU I CA  1 
ATOM   9151  C  C   . LEU I  1 38  ? -1.079 -131.909 -70.165  1.00 68.44  ? 39  LEU I C   1 
ATOM   9152  O  O   . LEU I  1 38  ? -1.550 -132.892 -69.602  1.00 71.60  ? 39  LEU I O   1 
ATOM   9153  C  CB  . LEU I  1 38  ? 1.261  -131.438 -69.455  1.00 63.50  ? 39  LEU I CB  1 
ATOM   9154  C  CG  . LEU I  1 38  ? 2.369  -130.377 -69.376  1.00 59.69  ? 39  LEU I CG  1 
ATOM   9155  C  CD1 . LEU I  1 38  ? 3.722  -130.994 -69.057  1.00 58.68  ? 39  LEU I CD1 1 
ATOM   9156  C  CD2 . LEU I  1 38  ? 2.442  -129.604 -70.674  1.00 57.80  ? 39  LEU I CD2 1 
ATOM   9157  N  N   . THR I  1 39  ? -1.298 -131.621 -71.444  1.00 67.73  ? 40  THR I N   1 
ATOM   9158  C  CA  . THR I  1 39  ? -2.067 -132.508 -72.322  1.00 70.59  ? 40  THR I CA  1 
ATOM   9159  C  C   . THR I  1 39  ? -1.264 -133.779 -72.503  1.00 71.13  ? 40  THR I C   1 
ATOM   9160  O  O   . THR I  1 39  ? -0.062 -133.716 -72.682  1.00 68.53  ? 40  THR I O   1 
ATOM   9161  C  CB  . THR I  1 39  ? -2.363 -131.890 -73.719  1.00 69.96  ? 40  THR I CB  1 
ATOM   9162  O  OG1 . THR I  1 39  ? -1.496 -132.471 -74.690  1.00 69.26  ? 40  THR I OG1 1 
ATOM   9163  C  CG2 . THR I  1 39  ? -2.202 -130.346 -73.739  1.00 67.37  ? 40  THR I CG2 1 
ATOM   9164  N  N   . GLU I  1 40  ? -1.923 -134.931 -72.432  1.00 75.07  ? 41  GLU I N   1 
ATOM   9165  C  CA  . GLU I  1 40  ? -1.205 -136.213 -72.426  1.00 76.55  ? 41  GLU I CA  1 
ATOM   9166  C  C   . GLU I  1 40  ? -0.322 -136.345 -73.649  1.00 74.70  ? 41  GLU I C   1 
ATOM   9167  O  O   . GLU I  1 40  ? -0.747 -136.088 -74.768  1.00 74.72  ? 41  GLU I O   1 
ATOM   9168  C  CB  . GLU I  1 40  ? -2.152 -137.424 -72.365  1.00 81.64  ? 41  GLU I CB  1 
ATOM   9169  C  CG  . GLU I  1 40  ? -1.397 -138.805 -72.407  1.00 84.11  ? 41  GLU I CG  1 
ATOM   9170  C  CD  . GLU I  1 40  ? -2.323 -140.041 -72.445  1.00 89.92  ? 41  GLU I CD  1 
ATOM   9171  O  OE1 . GLU I  1 40  ? -3.289 -140.047 -73.272  1.00 91.62  ? 41  GLU I OE1 1 
ATOM   9172  O  OE2 . GLU I  1 40  ? -2.054 -141.005 -71.663  1.00 92.37  ? 41  GLU I OE2 1 
ATOM   9173  N  N   . GLY I  1 41  ? 0.907  -136.775 -73.418  1.00 73.67  ? 42  GLY I N   1 
ATOM   9174  C  CA  . GLY I  1 41  ? 1.844  -137.033 -74.500  1.00 72.79  ? 42  GLY I CA  1 
ATOM   9175  C  C   . GLY I  1 41  ? 3.103  -136.179 -74.443  1.00 68.88  ? 42  GLY I C   1 
ATOM   9176  O  O   . GLY I  1 41  ? 3.496  -135.666 -73.391  1.00 67.03  ? 42  GLY I O   1 
ATOM   9177  N  N   . LEU I  1 42  ? 3.749  -136.069 -75.595  1.00 67.94  ? 43  LEU I N   1 
ATOM   9178  C  CA  . LEU I  1 42  ? 5.036  -135.398 -75.705  1.00 65.03  ? 43  LEU I CA  1 
ATOM   9179  C  C   . LEU I  1 42  ? 4.855  -133.896 -75.699  1.00 62.00  ? 43  LEU I C   1 
ATOM   9180  O  O   . LEU I  1 42  ? 3.850  -133.384 -76.189  1.00 62.40  ? 43  LEU I O   1 
ATOM   9181  C  CB  . LEU I  1 42  ? 5.799  -135.825 -76.975  1.00 65.83  ? 43  LEU I CB  1 
ATOM   9182  C  CG  . LEU I  1 42  ? 6.498  -137.190 -76.926  1.00 68.41  ? 43  LEU I CG  1 
ATOM   9183  C  CD1 . LEU I  1 42  ? 5.802  -138.188 -77.840  1.00 72.19  ? 43  LEU I CD1 1 
ATOM   9184  C  CD2 . LEU I  1 42  ? 7.954  -137.058 -77.327  1.00 67.54  ? 43  LEU I CD2 1 
ATOM   9185  N  N   . HIS I  1 43  ? 5.835  -133.203 -75.126  1.00 59.48  ? 44  HIS I N   1 
ATOM   9186  C  CA  . HIS I  1 43  ? 5.870  -131.739 -75.139  1.00 56.74  ? 44  HIS I CA  1 
ATOM   9187  C  C   . HIS I  1 43  ? 7.280  -131.223 -75.349  1.00 54.77  ? 44  HIS I C   1 
ATOM   9188  O  O   . HIS I  1 43  ? 8.234  -131.727 -74.752  1.00 54.79  ? 44  HIS I O   1 
ATOM   9189  C  CB  . HIS I  1 43  ? 5.302  -131.163 -73.845  1.00 55.93  ? 44  HIS I CB  1 
ATOM   9190  C  CG  . HIS I  1 43  ? 3.822  -131.310 -73.734  1.00 57.96  ? 44  HIS I CG  1 
ATOM   9191  N  ND1 . HIS I  1 43  ? 2.938  -130.445 -74.344  1.00 58.11  ? 44  HIS I ND1 1 
ATOM   9192  C  CD2 . HIS I  1 43  ? 3.065  -132.244 -73.114  1.00 60.70  ? 44  HIS I CD2 1 
ATOM   9193  C  CE1 . HIS I  1 43  ? 1.698  -130.828 -74.086  1.00 60.58  ? 44  HIS I CE1 1 
ATOM   9194  N  NE2 . HIS I  1 43  ? 1.748  -131.919 -73.343  1.00 62.26  ? 44  HIS I NE2 1 
ATOM   9195  N  N   . GLY I  1 44  ? 7.395  -130.219 -76.211  1.00 53.43  ? 45  GLY I N   1 
ATOM   9196  C  CA  . GLY I  1 44  ? 8.665  -129.556 -76.468  1.00 51.84  ? 45  GLY I CA  1 
ATOM   9197  C  C   . GLY I  1 44  ? 9.153  -128.897 -75.207  1.00 49.93  ? 45  GLY I C   1 
ATOM   9198  O  O   . GLY I  1 44  ? 8.353  -128.478 -74.387  1.00 49.66  ? 45  GLY I O   1 
ATOM   9199  N  N   . PHE I  1 45  ? 10.464 -128.789 -75.059  1.00 49.18  ? 46  PHE I N   1 
ATOM   9200  C  CA  . PHE I  1 45  ? 11.059 -128.359 -73.798  1.00 47.83  ? 46  PHE I CA  1 
ATOM   9201  C  C   . PHE I  1 45  ? 12.402 -127.694 -74.025  1.00 46.92  ? 46  PHE I C   1 
ATOM   9202  O  O   . PHE I  1 45  ? 13.401 -128.387 -74.157  1.00 48.08  ? 46  PHE I O   1 
ATOM   9203  C  CB  . PHE I  1 45  ? 11.237 -129.585 -72.918  1.00 49.26  ? 46  PHE I CB  1 
ATOM   9204  C  CG  . PHE I  1 45  ? 11.619 -129.284 -71.496  1.00 48.45  ? 46  PHE I CG  1 
ATOM   9205  C  CD1 . PHE I  1 45  ? 10.887 -128.399 -70.738  1.00 47.37  ? 46  PHE I CD1 1 
ATOM   9206  C  CD2 . PHE I  1 45  ? 12.678 -129.938 -70.901  1.00 49.29  ? 46  PHE I CD2 1 
ATOM   9207  C  CE1 . PHE I  1 45  ? 11.226 -128.155 -69.432  1.00 47.09  ? 46  PHE I CE1 1 
ATOM   9208  C  CE2 . PHE I  1 45  ? 13.009 -129.700 -69.596  1.00 49.02  ? 46  PHE I CE2 1 
ATOM   9209  C  CZ  . PHE I  1 45  ? 12.287 -128.809 -68.862  1.00 47.98  ? 46  PHE I CZ  1 
ATOM   9210  N  N   . HIS I  1 46  ? 12.432 -126.363 -74.050  1.00 45.32  ? 47  HIS I N   1 
ATOM   9211  C  CA  . HIS I  1 46  ? 13.633 -125.633 -74.459  1.00 44.86  ? 47  HIS I CA  1 
ATOM   9212  C  C   . HIS I  1 46  ? 14.011 -124.457 -73.576  1.00 43.42  ? 47  HIS I C   1 
ATOM   9213  O  O   . HIS I  1 46  ? 13.169 -123.846 -72.942  1.00 42.85  ? 47  HIS I O   1 
ATOM   9214  C  CB  . HIS I  1 46  ? 13.439 -125.114 -75.865  1.00 45.40  ? 47  HIS I CB  1 
ATOM   9215  C  CG  . HIS I  1 46  ? 12.748 -126.080 -76.771  1.00 46.86  ? 47  HIS I CG  1 
ATOM   9216  N  ND1 . HIS I  1 46  ? 11.431 -125.942 -77.137  1.00 47.23  ? 47  HIS I ND1 1 
ATOM   9217  C  CD2 . HIS I  1 46  ? 13.190 -127.197 -77.389  1.00 49.08  ? 47  HIS I CD2 1 
ATOM   9218  C  CE1 . HIS I  1 46  ? 11.092 -126.919 -77.954  1.00 49.00  ? 47  HIS I CE1 1 
ATOM   9219  N  NE2 . HIS I  1 46  ? 12.141 -127.698 -78.119  1.00 50.15  ? 47  HIS I NE2 1 
ATOM   9220  N  N   . VAL I  1 47  ? 15.295 -124.136 -73.555  1.00 43.42  ? 48  VAL I N   1 
ATOM   9221  C  CA  . VAL I  1 47  ? 15.776 -122.919 -72.913  1.00 42.34  ? 48  VAL I CA  1 
ATOM   9222  C  C   . VAL I  1 47  ? 15.837 -121.819 -73.951  1.00 42.53  ? 48  VAL I C   1 
ATOM   9223  O  O   . VAL I  1 47  ? 16.551 -121.933 -74.951  1.00 43.73  ? 48  VAL I O   1 
ATOM   9224  C  CB  . VAL I  1 47  ? 17.183 -123.101 -72.336  1.00 42.79  ? 48  VAL I CB  1 
ATOM   9225  C  CG1 . VAL I  1 47  ? 17.758 -121.776 -71.888  1.00 42.05  ? 48  VAL I CG1 1 
ATOM   9226  C  CG2 . VAL I  1 47  ? 17.159 -124.058 -71.178  1.00 43.19  ? 48  VAL I CG2 1 
ATOM   9227  N  N   . HIS I  1 48  ? 15.091 -120.752 -73.712  1.00 41.85  ? 49  HIS I N   1 
ATOM   9228  C  CA  . HIS I  1 48  ? 15.066 -119.607 -74.628  1.00 42.57  ? 49  HIS I CA  1 
ATOM   9229  C  C   . HIS I  1 48  ? 16.036 -118.512 -74.231  1.00 42.54  ? 49  HIS I C   1 
ATOM   9230  O  O   . HIS I  1 48  ? 16.489 -118.474 -73.110  1.00 41.95  ? 49  HIS I O   1 
ATOM   9231  C  CB  . HIS I  1 48  ? 13.664 -119.019 -74.708  1.00 42.54  ? 49  HIS I CB  1 
ATOM   9232  C  CG  . HIS I  1 48  ? 12.688 -119.882 -75.441  1.00 43.15  ? 49  HIS I CG  1 
ATOM   9233  N  ND1 . HIS I  1 48  ? 11.989 -119.447 -76.548  1.00 44.20  ? 49  HIS I ND1 1 
ATOM   9234  C  CD2 . HIS I  1 48  ? 12.306 -121.161 -75.230  1.00 42.87  ? 49  HIS I CD2 1 
ATOM   9235  C  CE1 . HIS I  1 48  ? 11.202 -120.416 -76.972  1.00 44.73  ? 49  HIS I CE1 1 
ATOM   9236  N  NE2 . HIS I  1 48  ? 11.377 -121.465 -76.191  1.00 44.05  ? 49  HIS I NE2 1 
ATOM   9237  N  N   . GLU I  1 49  ? 16.316 -117.601 -75.157  1.00 43.74  ? 50  GLU I N   1 
ATOM   9238  C  CA  . GLU I  1 49  ? 17.428 -116.649 -75.013  1.00 44.46  ? 50  GLU I CA  1 
ATOM   9239  C  C   . GLU I  1 49  ? 17.293 -115.720 -73.831  1.00 43.52  ? 50  GLU I C   1 
ATOM   9240  O  O   . GLU I  1 49  ? 18.208 -115.604 -73.031  1.00 43.30  ? 50  GLU I O   1 
ATOM   9241  C  CB  . GLU I  1 49  ? 17.613 -115.817 -76.279  1.00 46.44  ? 50  GLU I CB  1 
ATOM   9242  C  CG  . GLU I  1 49  ? 18.886 -114.984 -76.276  1.00 47.74  ? 50  GLU I CG  1 
ATOM   9243  C  CD  . GLU I  1 49  ? 19.220 -114.379 -77.622  1.00 50.56  ? 50  GLU I CD  1 
ATOM   9244  O  OE1 . GLU I  1 49  ? 18.627 -114.771 -78.650  1.00 51.20  ? 50  GLU I OE1 1 
ATOM   9245  O  OE2 . GLU I  1 49  ? 20.100 -113.493 -77.656  1.00 52.41  ? 50  GLU I OE2 1 
ATOM   9246  N  N   . PHE I  1 50  ? 16.152 -115.060 -73.732  1.00 43.41  ? 51  PHE I N   1 
ATOM   9247  C  CA  . PHE I  1 50  ? 15.963 -113.982 -72.764  1.00 43.32  ? 51  PHE I CA  1 
ATOM   9248  C  C   . PHE I  1 50  ? 15.170 -114.362 -71.504  1.00 42.19  ? 51  PHE I C   1 
ATOM   9249  O  O   . PHE I  1 50  ? 14.166 -115.067 -71.558  1.00 41.78  ? 51  PHE I O   1 
ATOM   9250  C  CB  . PHE I  1 50  ? 15.286 -112.800 -73.447  1.00 44.72  ? 51  PHE I CB  1 
ATOM   9251  C  CG  . PHE I  1 50  ? 15.981 -112.352 -74.685  1.00 46.55  ? 51  PHE I CG  1 
ATOM   9252  C  CD1 . PHE I  1 50  ? 17.290 -111.929 -74.638  1.00 47.50  ? 51  PHE I CD1 1 
ATOM   9253  C  CD2 . PHE I  1 50  ? 15.327 -112.342 -75.894  1.00 48.14  ? 51  PHE I CD2 1 
ATOM   9254  C  CE1 . PHE I  1 50  ? 17.939 -111.512 -75.772  1.00 49.86  ? 51  PHE I CE1 1 
ATOM   9255  C  CE2 . PHE I  1 50  ? 15.973 -111.925 -77.031  1.00 50.32  ? 51  PHE I CE2 1 
ATOM   9256  C  CZ  . PHE I  1 50  ? 17.283 -111.509 -76.969  1.00 51.20  ? 51  PHE I CZ  1 
ATOM   9257  N  N   . GLY I  1 51  ? 15.632 -113.863 -70.363  1.00 42.12  ? 52  GLY I N   1 
ATOM   9258  C  CA  . GLY I  1 51  ? 14.879 -113.923 -69.108  1.00 41.68  ? 52  GLY I CA  1 
ATOM   9259  C  C   . GLY I  1 51  ? 13.861 -112.785 -68.986  1.00 42.65  ? 52  GLY I C   1 
ATOM   9260  O  O   . GLY I  1 51  ? 13.672 -112.196 -67.937  1.00 43.08  ? 52  GLY I O   1 
ATOM   9261  N  N   . ASP I  1 52  ? 13.182 -112.496 -70.076  1.00 43.35  ? 53  ASP I N   1 
ATOM   9262  C  CA  . ASP I  1 52  ? 12.248 -111.404 -70.137  1.00 44.88  ? 53  ASP I CA  1 
ATOM   9263  C  C   . ASP I  1 52  ? 10.837 -111.946 -70.092  1.00 45.12  ? 53  ASP I C   1 
ATOM   9264  O  O   . ASP I  1 52  ? 10.445 -112.727 -70.942  1.00 44.81  ? 53  ASP I O   1 
ATOM   9265  C  CB  . ASP I  1 52  ? 12.459 -110.664 -71.445  1.00 46.43  ? 53  ASP I CB  1 
ATOM   9266  C  CG  . ASP I  1 52  ? 11.696 -109.371 -71.513  1.00 48.81  ? 53  ASP I CG  1 
ATOM   9267  O  OD1 . ASP I  1 52  ? 10.591 -109.322 -70.935  1.00 49.44  ? 53  ASP I OD1 1 
ATOM   9268  O  OD2 . ASP I  1 52  ? 12.202 -108.411 -72.150  1.00 50.32  ? 53  ASP I OD2 1 
ATOM   9269  N  N   . ASN I  1 53  ? 10.075 -111.529 -69.094  1.00 46.11  ? 54  ASN I N   1 
ATOM   9270  C  CA  . ASN I  1 53  ? 8.689  -111.981 -68.918  1.00 46.92  ? 54  ASN I CA  1 
ATOM   9271  C  C   . ASN I  1 53  ? 7.689  -110.839 -69.057  1.00 49.21  ? 54  ASN I C   1 
ATOM   9272  O  O   . ASN I  1 53  ? 6.523  -110.978 -68.724  1.00 50.33  ? 54  ASN I O   1 
ATOM   9273  C  CB  . ASN I  1 53  ? 8.529  -112.648 -67.556  1.00 46.61  ? 54  ASN I CB  1 
ATOM   9274  C  CG  . ASN I  1 53  ? 7.799  -113.951 -67.643  1.00 46.62  ? 54  ASN I CG  1 
ATOM   9275  O  OD1 . ASN I  1 53  ? 8.295  -114.915 -68.242  1.00 45.74  ? 54  ASN I OD1 1 
ATOM   9276  N  ND2 . ASN I  1 53  ? 6.615  -114.003 -67.045  1.00 48.21  ? 54  ASN I ND2 1 
ATOM   9277  N  N   . THR I  1 54  ? 8.180  -109.719 -69.563  1.00 50.19  ? 55  THR I N   1 
ATOM   9278  C  CA  . THR I  1 54  ? 7.412  -108.496 -69.740  1.00 53.23  ? 55  THR I CA  1 
ATOM   9279  C  C   . THR I  1 54  ? 6.020  -108.778 -70.300  1.00 54.94  ? 55  THR I C   1 
ATOM   9280  O  O   . THR I  1 54  ? 5.007  -108.585 -69.624  1.00 56.74  ? 55  THR I O   1 
ATOM   9281  C  CB  . THR I  1 54  ? 8.161  -107.537 -70.717  1.00 54.31  ? 55  THR I CB  1 
ATOM   9282  O  OG1 . THR I  1 54  ? 9.346  -107.058 -70.093  1.00 53.90  ? 55  THR I OG1 1 
ATOM   9283  C  CG2 . THR I  1 54  ? 7.299  -106.351 -71.150  1.00 57.92  ? 55  THR I CG2 1 
ATOM   9284  N  N   . ALA I  1 55  ? 5.991  -109.237 -71.549  1.00 54.70  ? 56  ALA I N   1 
ATOM   9285  C  CA  . ALA I  1 55  ? 4.762  -109.545 -72.269  1.00 56.21  ? 56  ALA I CA  1 
ATOM   9286  C  C   . ALA I  1 55  ? 4.544  -111.046 -72.284  1.00 54.14  ? 56  ALA I C   1 
ATOM   9287  O  O   . ALA I  1 55  ? 4.289  -111.629 -73.310  1.00 54.20  ? 56  ALA I O   1 
ATOM   9288  C  CB  . ALA I  1 55  ? 4.845  -108.995 -73.683  1.00 57.79  ? 56  ALA I CB  1 
ATOM   9289  N  N   . GLY I  1 56  ? 4.659  -111.662 -71.120  1.00 52.87  ? 57  GLY I N   1 
ATOM   9290  C  CA  . GLY I  1 56  ? 4.398  -113.097 -70.954  1.00 51.66  ? 57  GLY I CA  1 
ATOM   9291  C  C   . GLY I  1 56  ? 5.574  -113.977 -71.349  1.00 49.04  ? 57  GLY I C   1 
ATOM   9292  O  O   . GLY I  1 56  ? 6.718  -113.583 -71.195  1.00 48.01  ? 57  GLY I O   1 
ATOM   9293  N  N   . CYS I  1 57  ? 5.291  -115.180 -71.838  1.00 48.45  ? 58  CYS I N   1 
ATOM   9294  C  CA  . CYS I  1 57  ? 6.332  -116.073 -72.343  1.00 46.44  ? 58  CYS I CA  1 
ATOM   9295  C  C   . CYS I  1 57  ? 6.889  -115.639 -73.699  1.00 46.69  ? 58  CYS I C   1 
ATOM   9296  O  O   . CYS I  1 57  ? 7.997  -116.006 -74.051  1.00 45.54  ? 58  CYS I O   1 
ATOM   9297  C  CB  . CYS I  1 57  ? 5.799  -117.484 -72.486  1.00 46.39  ? 58  CYS I CB  1 
ATOM   9298  S  SG  . CYS I  1 57  ? 5.443  -118.310 -70.973  1.00 46.24  ? 58  CYS I SG  1 
ATOM   9299  N  N   . THR I  1 58  ? 6.117  -114.881 -74.469  1.00 48.67  ? 59  THR I N   1 
ATOM   9300  C  CA  . THR I  1 58  ? 6.549  -114.432 -75.799  1.00 49.61  ? 59  THR I CA  1 
ATOM   9301  C  C   . THR I  1 58  ? 7.801  -113.583 -75.758  1.00 49.21  ? 59  THR I C   1 
ATOM   9302  O  O   . THR I  1 58  ? 8.563  -113.579 -76.703  1.00 49.65  ? 59  THR I O   1 
ATOM   9303  C  CB  . THR I  1 58  ? 5.497  -113.578 -76.491  1.00 52.35  ? 59  THR I CB  1 
ATOM   9304  O  OG1 . THR I  1 58  ? 4.220  -114.185 -76.322  1.00 53.38  ? 59  THR I OG1 1 
ATOM   9305  C  CG2 . THR I  1 58  ? 5.810  -113.434 -77.970  1.00 53.67  ? 59  THR I CG2 1 
ATOM   9306  N  N   . SER I  1 59  ? 7.985  -112.841 -74.673  1.00 48.96  ? 60  SER I N   1 
ATOM   9307  C  CA  . SER I  1 59  ? 9.141  -111.954 -74.486  1.00 48.89  ? 60  SER I CA  1 
ATOM   9308  C  C   . SER I  1 59  ? 10.468 -112.677 -74.382  1.00 46.96  ? 60  SER I C   1 
ATOM   9309  O  O   . SER I  1 59  ? 11.512 -112.096 -74.649  1.00 47.45  ? 60  SER I O   1 
ATOM   9310  C  CB  . SER I  1 59  ? 8.936  -111.130 -73.229  1.00 49.32  ? 60  SER I CB  1 
ATOM   9311  O  OG  . SER I  1 59  ? 7.606  -110.611 -73.223  1.00 51.83  ? 60  SER I OG  1 
ATOM   9312  N  N   . ALA I  1 60  ? 10.416 -113.948 -74.007  1.00 45.42  ? 61  ALA I N   1 
ATOM   9313  C  CA  . ALA I  1 60  ? 11.605 -114.794 -73.874  1.00 43.98  ? 61  ALA I CA  1 
ATOM   9314  C  C   . ALA I  1 60  ? 12.413 -114.916 -75.151  1.00 44.72  ? 61  ALA I C   1 
ATOM   9315  O  O   . ALA I  1 60  ? 13.551 -115.344 -75.125  1.00 44.29  ? 61  ALA I O   1 
ATOM   9316  C  CB  . ALA I  1 60  ? 11.211 -116.177 -73.409  1.00 42.97  ? 61  ALA I CB  1 
ATOM   9317  N  N   . GLY I  1 61  ? 11.813 -114.574 -76.276  1.00 46.42  ? 62  GLY I N   1 
ATOM   9318  C  CA  . GLY I  1 61  ? 12.501 -114.622 -77.561  1.00 47.84  ? 62  GLY I CA  1 
ATOM   9319  C  C   . GLY I  1 61  ? 12.647 -116.052 -78.058  1.00 47.44  ? 62  GLY I C   1 
ATOM   9320  O  O   . GLY I  1 61  ? 11.917 -116.936 -77.616  1.00 46.48  ? 62  GLY I O   1 
ATOM   9321  N  N   . PRO I  1 62  ? 13.600 -116.293 -78.971  1.00 48.58  ? 63  PRO I N   1 
ATOM   9322  C  CA  . PRO I  1 62  ? 13.768 -117.594 -79.589  1.00 48.86  ? 63  PRO I CA  1 
ATOM   9323  C  C   . PRO I  1 62  ? 14.579 -118.559 -78.755  1.00 47.48  ? 63  PRO I C   1 
ATOM   9324  O  O   . PRO I  1 62  ? 14.991 -118.224 -77.650  1.00 46.26  ? 63  PRO I O   1 
ATOM   9325  C  CB  . PRO I  1 62  ? 14.539 -117.255 -80.852  1.00 51.37  ? 63  PRO I CB  1 
ATOM   9326  C  CG  . PRO I  1 62  ? 15.385 -116.126 -80.458  1.00 51.59  ? 63  PRO I CG  1 
ATOM   9327  C  CD  . PRO I  1 62  ? 14.583 -115.326 -79.485  1.00 50.26  ? 63  PRO I CD  1 
ATOM   9328  N  N   . HIS I  1 63  ? 14.808 -119.745 -79.307  1.00 48.18  ? 64  HIS I N   1 
ATOM   9329  C  CA  . HIS I  1 63  ? 15.636 -120.780 -78.676  1.00 47.63  ? 64  HIS I CA  1 
ATOM   9330  C  C   . HIS I  1 63  ? 17.037 -120.266 -78.406  1.00 47.87  ? 64  HIS I C   1 
ATOM   9331  O  O   . HIS I  1 63  ? 17.636 -119.661 -79.276  1.00 49.73  ? 64  HIS I O   1 
ATOM   9332  C  CB  . HIS I  1 63  ? 15.741 -121.987 -79.604  1.00 49.43  ? 64  HIS I CB  1 
ATOM   9333  C  CG  . HIS I  1 63  ? 14.486 -122.785 -79.712  1.00 49.04  ? 64  HIS I CG  1 
ATOM   9334  N  ND1 . HIS I  1 63  ? 14.490 -124.147 -79.887  1.00 49.81  ? 64  HIS I ND1 1 
ATOM   9335  C  CD2 . HIS I  1 63  ? 13.190 -122.414 -79.673  1.00 48.51  ? 64  HIS I CD2 1 
ATOM   9336  C  CE1 . HIS I  1 63  ? 13.248 -124.583 -79.949  1.00 49.96  ? 64  HIS I CE1 1 
ATOM   9337  N  NE2 . HIS I  1 63  ? 12.440 -123.551 -79.824  1.00 49.00  ? 64  HIS I NE2 1 
ATOM   9338  N  N   . PHE I  1 64  ? 17.574 -120.526 -77.225  1.00 46.51  ? 65  PHE I N   1 
ATOM   9339  C  CA  . PHE I  1 64  ? 18.910 -120.038 -76.899  1.00 47.22  ? 65  PHE I CA  1 
ATOM   9340  C  C   . PHE I  1 64  ? 19.925 -120.643 -77.860  1.00 49.65  ? 65  PHE I C   1 
ATOM   9341  O  O   . PHE I  1 64  ? 20.097 -121.839 -77.897  1.00 50.16  ? 65  PHE I O   1 
ATOM   9342  C  CB  . PHE I  1 64  ? 19.264 -120.358 -75.445  1.00 45.93  ? 65  PHE I CB  1 
ATOM   9343  C  CG  . PHE I  1 64  ? 20.636 -119.894 -75.017  1.00 46.56  ? 65  PHE I CG  1 
ATOM   9344  C  CD1 . PHE I  1 64  ? 21.120 -118.664 -75.383  1.00 47.62  ? 65  PHE I CD1 1 
ATOM   9345  C  CD2 . PHE I  1 64  ? 21.434 -120.693 -74.217  1.00 47.16  ? 65  PHE I CD2 1 
ATOM   9346  C  CE1 . PHE I  1 64  ? 22.392 -118.242 -74.983  1.00 49.08  ? 65  PHE I CE1 1 
ATOM   9347  C  CE2 . PHE I  1 64  ? 22.698 -120.278 -73.813  1.00 48.43  ? 65  PHE I CE2 1 
ATOM   9348  C  CZ  . PHE I  1 64  ? 23.172 -119.048 -74.197  1.00 49.34  ? 65  PHE I CZ  1 
ATOM   9349  N  N   . ASN I  1 65  ? 20.604 -119.803 -78.628  1.00 51.62  ? 66  ASN I N   1 
ATOM   9350  C  CA  . ASN I  1 65  ? 21.415 -120.259 -79.759  1.00 54.76  ? 66  ASN I CA  1 
ATOM   9351  C  C   . ASN I  1 65  ? 22.673 -119.408 -80.009  1.00 57.10  ? 66  ASN I C   1 
ATOM   9352  O  O   . ASN I  1 65  ? 22.786 -118.745 -81.038  1.00 59.37  ? 66  ASN I O   1 
ATOM   9353  C  CB  . ASN I  1 65  ? 20.528 -120.264 -81.009  1.00 55.97  ? 66  ASN I CB  1 
ATOM   9354  C  CG  . ASN I  1 65  ? 21.220 -120.844 -82.223  1.00 59.44  ? 66  ASN I CG  1 
ATOM   9355  O  OD1 . ASN I  1 65  ? 22.317 -121.406 -82.124  1.00 61.10  ? 66  ASN I OD1 1 
ATOM   9356  N  ND2 . ASN I  1 65  ? 20.577 -120.714 -83.385  1.00 61.00  ? 66  ASN I ND2 1 
ATOM   9357  N  N   . PRO I  1 66  ? 23.639 -119.441 -79.079  1.00 57.05  ? 67  PRO I N   1 
ATOM   9358  C  CA  . PRO I  1 66  ? 24.826 -118.590 -79.155  1.00 59.38  ? 67  PRO I CA  1 
ATOM   9359  C  C   . PRO I  1 66  ? 25.872 -119.024 -80.188  1.00 63.56  ? 67  PRO I C   1 
ATOM   9360  O  O   . PRO I  1 66  ? 26.697 -118.212 -80.620  1.00 66.48  ? 67  PRO I O   1 
ATOM   9361  C  CB  . PRO I  1 66  ? 25.418 -118.714 -77.760  1.00 57.99  ? 67  PRO I CB  1 
ATOM   9362  C  CG  . PRO I  1 66  ? 25.028 -120.052 -77.316  1.00 56.59  ? 67  PRO I CG  1 
ATOM   9363  C  CD  . PRO I  1 66  ? 23.683 -120.313 -77.899  1.00 55.26  ? 67  PRO I CD  1 
ATOM   9364  N  N   . LEU I  1 67  ? 25.841 -120.291 -80.572  1.00 64.40  ? 68  LEU I N   1 
ATOM   9365  C  CA  . LEU I  1 67  ? 26.740 -120.798 -81.610  1.00 68.66  ? 68  LEU I CA  1 
ATOM   9366  C  C   . LEU I  1 67  ? 26.125 -120.721 -83.021  1.00 70.47  ? 68  LEU I C   1 
ATOM   9367  O  O   . LEU I  1 67  ? 26.656 -121.267 -83.983  1.00 74.13  ? 68  LEU I O   1 
ATOM   9368  C  CB  . LEU I  1 67  ? 27.167 -122.233 -81.262  1.00 69.54  ? 68  LEU I CB  1 
ATOM   9369  C  CG  . LEU I  1 67  ? 27.866 -122.414 -79.901  1.00 68.65  ? 68  LEU I CG  1 
ATOM   9370  C  CD1 . LEU I  1 67  ? 28.420 -123.837 -79.767  1.00 70.67  ? 68  LEU I CD1 1 
ATOM   9371  C  CD2 . LEU I  1 67  ? 28.964 -121.355 -79.660  1.00 70.33  ? 68  LEU I CD2 1 
ATOM   9372  N  N   . SER I  1 68  ? 24.989 -120.047 -83.133  1.00 68.37  ? 69  SER I N   1 
ATOM   9373  C  CA  . SER I  1 68  ? 24.379 -119.726 -84.434  1.00 70.41  ? 69  SER I CA  1 
ATOM   9374  C  C   . SER I  1 68  ? 24.101 -120.965 -85.300  1.00 72.07  ? 69  SER I C   1 
ATOM   9375  O  O   . SER I  1 68  ? 24.357 -120.960 -86.499  1.00 75.84  ? 69  SER I O   1 
ATOM   9376  C  CB  . SER I  1 68  ? 25.264 -118.733 -85.211  1.00 74.45  ? 69  SER I CB  1 
ATOM   9377  O  OG  . SER I  1 68  ? 25.721 -117.674 -84.391  1.00 73.79  ? 69  SER I OG  1 
ATOM   9378  N  N   . ARG I  1 69  ? 23.553 -122.008 -84.691  1.00 69.64  ? 70  ARG I N   1 
ATOM   9379  C  CA  . ARG I  1 69  ? 23.267 -123.242 -85.411  1.00 71.59  ? 70  ARG I CA  1 
ATOM   9380  C  C   . ARG I  1 69  ? 21.773 -123.389 -85.713  1.00 69.62  ? 70  ARG I C   1 
ATOM   9381  O  O   . ARG I  1 69  ? 20.952 -122.510 -85.399  1.00 67.03  ? 70  ARG I O   1 
ATOM   9382  C  CB  . ARG I  1 69  ? 23.736 -124.463 -84.618  1.00 71.33  ? 70  ARG I CB  1 
ATOM   9383  C  CG  . ARG I  1 69  ? 25.080 -124.343 -83.930  1.00 74.27  ? 70  ARG I CG  1 
ATOM   9384  C  CD  . ARG I  1 69  ? 26.229 -124.362 -84.910  1.00 82.08  ? 70  ARG I CD  1 
ATOM   9385  N  NE  . ARG I  1 69  ? 27.394 -125.053 -84.352  1.00 86.54  ? 70  ARG I NE  1 
ATOM   9386  C  CZ  . ARG I  1 69  ? 27.592 -126.375 -84.393  1.00 91.15  ? 70  ARG I CZ  1 
ATOM   9387  N  NH1 . ARG I  1 69  ? 26.713 -127.199 -84.968  1.00 91.40  ? 70  ARG I NH1 1 
ATOM   9388  N  NH2 . ARG I  1 69  ? 28.694 -126.889 -83.855  1.00 95.09  ? 70  ARG I NH2 1 
ATOM   9389  N  N   . LYS I  1 70  ? 21.449 -124.518 -86.343  1.00 71.34  ? 71  LYS I N   1 
ATOM   9390  C  CA  . LYS I  1 70  ? 20.066 -124.904 -86.671  1.00 70.17  ? 71  LYS I CA  1 
ATOM   9391  C  C   . LYS I  1 70  ? 19.444 -125.732 -85.555  1.00 66.88  ? 71  LYS I C   1 
ATOM   9392  O  O   . LYS I  1 70  ? 20.172 -126.358 -84.774  1.00 66.41  ? 71  LYS I O   1 
ATOM   9393  C  CB  . LYS I  1 70  ? 20.038 -125.755 -87.953  1.00 74.28  ? 71  LYS I CB  1 
ATOM   9394  C  CG  . LYS I  1 70  ? 20.677 -125.104 -89.197  1.00 78.69  ? 71  LYS I CG  1 
ATOM   9395  C  CD  . LYS I  1 70  ? 19.639 -124.377 -90.051  1.00 79.42  ? 71  LYS I CD  1 
ATOM   9396  C  CE  . LYS I  1 70  ? 20.223 -123.824 -91.330  1.00 84.25  ? 71  LYS I CE  1 
ATOM   9397  N  NZ  . LYS I  1 70  ? 19.141 -123.179 -92.128  1.00 84.94  ? 71  LYS I NZ  1 
ATOM   9398  N  N   . HIS I  1 71  ? 18.107 -125.755 -85.516  1.00 64.99  ? 72  HIS I N   1 
ATOM   9399  C  CA  . HIS I  1 71  ? 17.370 -126.512 -84.492  1.00 62.51  ? 72  HIS I CA  1 
ATOM   9400  C  C   . HIS I  1 71  ? 17.629 -127.998 -84.641  1.00 64.50  ? 72  HIS I C   1 
ATOM   9401  O  O   . HIS I  1 71  ? 17.906 -128.482 -85.733  1.00 67.79  ? 72  HIS I O   1 
ATOM   9402  C  CB  . HIS I  1 71  ? 15.848 -126.254 -84.533  1.00 61.00  ? 72  HIS I CB  1 
ATOM   9403  C  CG  . HIS I  1 71  ? 15.075 -126.949 -83.440  1.00 58.75  ? 72  HIS I CG  1 
ATOM   9404  N  ND1 . HIS I  1 71  ? 15.141 -126.573 -82.116  1.00 55.84  ? 72  HIS I ND1 1 
ATOM   9405  C  CD2 . HIS I  1 71  ? 14.223 -128.000 -83.484  1.00 59.21  ? 72  HIS I CD2 1 
ATOM   9406  C  CE1 . HIS I  1 71  ? 14.371 -127.365 -81.394  1.00 54.82  ? 72  HIS I CE1 1 
ATOM   9407  N  NE2 . HIS I  1 71  ? 13.797 -128.235 -82.201  1.00 56.51  ? 72  HIS I NE2 1 
ATOM   9408  N  N   . GLY I  1 72  ? 17.545 -128.703 -83.521  1.00 62.84  ? 73  GLY I N   1 
ATOM   9409  C  CA  . GLY I  1 72  ? 17.712 -130.141 -83.506  1.00 64.94  ? 73  GLY I CA  1 
ATOM   9410  C  C   . GLY I  1 72  ? 17.324 -130.798 -82.191  1.00 63.15  ? 73  GLY I C   1 
ATOM   9411  O  O   . GLY I  1 72  ? 16.851 -130.139 -81.248  1.00 60.18  ? 73  GLY I O   1 
ATOM   9412  N  N   . GLY I  1 73  ? 17.524 -132.116 -82.138  1.00 65.52  ? 74  GLY I N   1 
ATOM   9413  C  CA  . GLY I  1 73  ? 17.313 -132.908 -80.918  1.00 64.79  ? 74  GLY I CA  1 
ATOM   9414  C  C   . GLY I  1 73  ? 18.529 -132.815 -80.008  1.00 64.63  ? 74  GLY I C   1 
ATOM   9415  O  O   . GLY I  1 73  ? 19.616 -132.481 -80.453  1.00 66.23  ? 74  GLY I O   1 
ATOM   9416  N  N   . PRO I  1 74  ? 18.366 -133.103 -78.718  1.00 63.36  ? 75  PRO I N   1 
ATOM   9417  C  CA  . PRO I  1 74  ? 19.469 -132.873 -77.791  1.00 63.15  ? 75  PRO I CA  1 
ATOM   9418  C  C   . PRO I  1 74  ? 20.688 -133.728 -78.090  1.00 67.03  ? 75  PRO I C   1 
ATOM   9419  O  O   . PRO I  1 74  ? 21.819 -133.275 -77.914  1.00 67.69  ? 75  PRO I O   1 
ATOM   9420  C  CB  . PRO I  1 74  ? 18.870 -133.241 -76.432  1.00 61.76  ? 75  PRO I CB  1 
ATOM   9421  C  CG  . PRO I  1 74  ? 17.704 -134.067 -76.732  1.00 62.65  ? 75  PRO I CG  1 
ATOM   9422  C  CD  . PRO I  1 74  ? 17.176 -133.623 -78.038  1.00 62.48  ? 75  PRO I CD  1 
ATOM   9423  N  N   . LYS I  1 75  ? 20.447 -134.948 -78.549  1.00 70.11  ? 76  LYS I N   1 
ATOM   9424  C  CA  . LYS I  1 75  ? 21.521 -135.851 -78.937  1.00 74.52  ? 76  LYS I CA  1 
ATOM   9425  C  C   . LYS I  1 75  ? 22.213 -135.416 -80.215  1.00 76.38  ? 76  LYS I C   1 
ATOM   9426  O  O   . LYS I  1 75  ? 23.393 -135.706 -80.394  1.00 79.61  ? 76  LYS I O   1 
ATOM   9427  C  CB  . LYS I  1 75  ? 20.994 -137.250 -79.172  1.00 77.79  ? 76  LYS I CB  1 
ATOM   9428  C  CG  . LYS I  1 75  ? 20.125 -137.803 -78.068  1.00 77.16  ? 76  LYS I CG  1 
ATOM   9429  C  CD  . LYS I  1 75  ? 20.153 -139.338 -78.109  1.00 82.06  ? 76  LYS I CD  1 
ATOM   9430  C  CE  . LYS I  1 75  ? 19.077 -139.969 -77.227  1.00 81.87  ? 76  LYS I CE  1 
ATOM   9431  N  NZ  . LYS I  1 75  ? 18.874 -141.427 -77.546  1.00 86.51  ? 76  LYS I NZ  1 
ATOM   9432  N  N   . ASP I  1 76  ? 21.479 -134.747 -81.104  1.00 74.94  ? 77  ASP I N   1 
ATOM   9433  C  CA  . ASP I  1 76  ? 22.057 -134.203 -82.348  1.00 76.95  ? 77  ASP I CA  1 
ATOM   9434  C  C   . ASP I  1 76  ? 23.211 -133.240 -82.037  1.00 76.62  ? 77  ASP I C   1 
ATOM   9435  O  O   . ASP I  1 76  ? 23.156 -132.476 -81.061  1.00 73.20  ? 77  ASP I O   1 
ATOM   9436  C  CB  . ASP I  1 76  ? 20.992 -133.488 -83.207  1.00 75.14  ? 77  ASP I CB  1 
ATOM   9437  C  CG  . ASP I  1 76  ? 19.981 -134.457 -83.829  1.00 76.89  ? 77  ASP I CG  1 
ATOM   9438  O  OD1 . ASP I  1 76  ? 20.329 -135.631 -84.017  1.00 80.85  ? 77  ASP I OD1 1 
ATOM   9439  O  OD2 . ASP I  1 76  ? 18.834 -134.066 -84.133  1.00 75.03  ? 77  ASP I OD2 1 
ATOM   9440  N  N   . GLU I  1 77  ? 24.274 -133.311 -82.840  1.00 80.59  ? 78  GLU I N   1 
ATOM   9441  C  CA  . GLU I  1 77  ? 25.385 -132.366 -82.708  1.00 80.89  ? 78  GLU I CA  1 
ATOM   9442  C  C   . GLU I  1 77  ? 24.962 -131.012 -83.235  1.00 78.43  ? 78  GLU I C   1 
ATOM   9443  O  O   . GLU I  1 77  ? 25.213 -130.006 -82.586  1.00 76.03  ? 78  GLU I O   1 
ATOM   9444  C  CB  . GLU I  1 77  ? 26.617 -132.807 -83.477  1.00 86.50  ? 78  GLU I CB  1 
ATOM   9445  C  CG  . GLU I  1 77  ? 27.581 -131.625 -83.744  1.00 87.85  ? 78  GLU I CG  1 
ATOM   9446  C  CD  . GLU I  1 77  ? 28.994 -132.052 -84.182  1.00 94.40  ? 78  GLU I CD  1 
ATOM   9447  O  OE1 . GLU I  1 77  ? 29.116 -133.118 -84.844  1.00 98.58  ? 78  GLU I OE1 1 
ATOM   9448  O  OE2 . GLU I  1 77  ? 29.979 -131.311 -83.868  1.00 95.32  ? 78  GLU I OE2 1 
ATOM   9449  N  N   . GLU I  1 78  ? 24.363 -130.994 -84.427  1.00 79.56  ? 79  GLU I N   1 
ATOM   9450  C  CA  . GLU I  1 78  ? 23.732 -129.782 -84.964  1.00 77.52  ? 79  GLU I CA  1 
ATOM   9451  C  C   . GLU I  1 78  ? 22.402 -129.500 -84.224  1.00 72.77  ? 79  GLU I C   1 
ATOM   9452  O  O   . GLU I  1 78  ? 21.327 -129.962 -84.626  1.00 72.35  ? 79  GLU I O   1 
ATOM   9453  C  CB  . GLU I  1 78  ? 23.512 -129.876 -86.481  1.00 80.92  ? 79  GLU I CB  1 
ATOM   9454  C  CG  . GLU I  1 78  ? 23.020 -128.562 -87.155  1.00 79.99  ? 79  GLU I CG  1 
ATOM   9455  C  CD  . GLU I  1 78  ? 24.122 -127.477 -87.350  1.00 81.82  ? 79  GLU I CD  1 
ATOM   9456  O  OE1 . GLU I  1 78  ? 25.305 -127.724 -87.012  1.00 84.06  ? 79  GLU I OE1 1 
ATOM   9457  O  OE2 . GLU I  1 78  ? 23.806 -126.363 -87.848  1.00 81.16  ? 79  GLU I OE2 1 
ATOM   9458  N  N   . ARG I  1 79  ? 22.517 -128.741 -83.130  1.00 69.55  ? 80  ARG I N   1 
ATOM   9459  C  CA  . ARG I  1 79  ? 21.389 -128.318 -82.298  1.00 65.21  ? 80  ARG I CA  1 
ATOM   9460  C  C   . ARG I  1 79  ? 21.607 -126.912 -81.752  1.00 62.90  ? 80  ARG I C   1 
ATOM   9461  O  O   . ARG I  1 79  ? 22.722 -126.395 -81.777  1.00 64.37  ? 80  ARG I O   1 
ATOM   9462  C  CB  . ARG I  1 79  ? 21.224 -129.257 -81.113  1.00 63.94  ? 80  ARG I CB  1 
ATOM   9463  C  CG  . ARG I  1 79  ? 22.461 -129.370 -80.244  1.00 64.67  ? 80  ARG I CG  1 
ATOM   9464  C  CD  . ARG I  1 79  ? 22.191 -130.144 -78.965  1.00 63.63  ? 80  ARG I CD  1 
ATOM   9465  N  NE  . ARG I  1 79  ? 21.661 -129.295 -77.895  1.00 59.97  ? 80  ARG I NE  1 
ATOM   9466  C  CZ  . ARG I  1 79  ? 21.559 -129.660 -76.617  1.00 58.81  ? 80  ARG I CZ  1 
ATOM   9467  N  NH1 . ARG I  1 79  ? 21.950 -130.872 -76.220  1.00 60.96  ? 80  ARG I NH1 1 
ATOM   9468  N  NH2 . ARG I  1 79  ? 21.058 -128.810 -75.724  1.00 56.00  ? 80  ARG I NH2 1 
ATOM   9469  N  N   . HIS I  1 80  ? 20.538 -126.302 -81.247  1.00 59.74  ? 81  HIS I N   1 
ATOM   9470  C  CA  . HIS I  1 80  ? 20.657 -125.084 -80.453  1.00 57.25  ? 81  HIS I CA  1 
ATOM   9471  C  C   . HIS I  1 80  ? 21.140 -125.483 -79.062  1.00 56.03  ? 81  HIS I C   1 
ATOM   9472  O  O   . HIS I  1 80  ? 20.778 -126.550 -78.555  1.00 55.95  ? 81  HIS I O   1 
ATOM   9473  C  CB  . HIS I  1 80  ? 19.319 -124.365 -80.312  1.00 54.72  ? 81  HIS I CB  1 
ATOM   9474  C  CG  . HIS I  1 80  ? 18.725 -123.896 -81.602  1.00 55.95  ? 81  HIS I CG  1 
ATOM   9475  N  ND1 . HIS I  1 80  ? 17.366 -123.824 -81.809  1.00 54.72  ? 81  HIS I ND1 1 
ATOM   9476  C  CD2 . HIS I  1 80  ? 19.303 -123.451 -82.743  1.00 58.72  ? 81  HIS I CD2 1 
ATOM   9477  C  CE1 . HIS I  1 80  ? 17.132 -123.359 -83.025  1.00 56.73  ? 81  HIS I CE1 1 
ATOM   9478  N  NE2 . HIS I  1 80  ? 18.291 -123.129 -83.615  1.00 59.11  ? 81  HIS I NE2 1 
ATOM   9479  N  N   . VAL I  1 81  ? 21.934 -124.622 -78.431  1.00 55.42  ? 82  VAL I N   1 
ATOM   9480  C  CA  . VAL I  1 81  ? 22.395 -124.878 -77.067  1.00 54.29  ? 82  VAL I CA  1 
ATOM   9481  C  C   . VAL I  1 81  ? 21.198 -125.153 -76.172  1.00 51.60  ? 82  VAL I C   1 
ATOM   9482  O  O   . VAL I  1 81  ? 21.235 -126.046 -75.354  1.00 51.74  ? 82  VAL I O   1 
ATOM   9483  C  CB  . VAL I  1 81  ? 23.210 -123.708 -76.496  1.00 53.89  ? 82  VAL I CB  1 
ATOM   9484  C  CG1 . VAL I  1 81  ? 23.510 -123.918 -75.019  1.00 52.55  ? 82  VAL I CG1 1 
ATOM   9485  C  CG2 . VAL I  1 81  ? 24.487 -123.547 -77.272  1.00 57.30  ? 82  VAL I CG2 1 
ATOM   9486  N  N   . GLY I  1 82  ? 20.118 -124.412 -76.363  1.00 49.80  ? 83  GLY I N   1 
ATOM   9487  C  CA  . GLY I  1 82  ? 18.927 -124.542 -75.522  1.00 47.81  ? 83  GLY I CA  1 
ATOM   9488  C  C   . GLY I  1 82  ? 17.956 -125.659 -75.871  1.00 48.34  ? 83  GLY I C   1 
ATOM   9489  O  O   . GLY I  1 82  ? 16.924 -125.805 -75.217  1.00 47.01  ? 83  GLY I O   1 
ATOM   9490  N  N   . ASP I  1 83  ? 18.269 -126.444 -76.900  1.00 50.59  ? 84  ASP I N   1 
ATOM   9491  C  CA  . ASP I  1 83  ? 17.374 -127.508 -77.356  1.00 51.42  ? 84  ASP I CA  1 
ATOM   9492  C  C   . ASP I  1 83  ? 17.487 -128.713 -76.459  1.00 52.20  ? 84  ASP I C   1 
ATOM   9493  O  O   . ASP I  1 83  ? 18.349 -129.548 -76.671  1.00 54.51  ? 84  ASP I O   1 
ATOM   9494  C  CB  . ASP I  1 83  ? 17.701 -127.926 -78.787  1.00 53.91  ? 84  ASP I CB  1 
ATOM   9495  C  CG  . ASP I  1 83  ? 17.264 -126.904 -79.807  1.00 53.63  ? 84  ASP I CG  1 
ATOM   9496  O  OD1 . ASP I  1 83  ? 16.444 -126.027 -79.486  1.00 51.30  ? 84  ASP I OD1 1 
ATOM   9497  O  OD2 . ASP I  1 83  ? 17.738 -126.960 -80.955  1.00 56.14  ? 84  ASP I OD2 1 
ATOM   9498  N  N   . LEU I  1 84  ? 16.615 -128.796 -75.458  1.00 50.79  ? 85  LEU I N   1 
ATOM   9499  C  CA  . LEU I  1 84  ? 16.579 -129.945 -74.537  1.00 51.85  ? 85  LEU I CA  1 
ATOM   9500  C  C   . LEU I  1 84  ? 15.574 -131.011 -74.951  1.00 53.39  ? 85  LEU I C   1 
ATOM   9501  O  O   . LEU I  1 84  ? 15.315 -131.943 -74.198  1.00 54.58  ? 85  LEU I O   1 
ATOM   9502  C  CB  . LEU I  1 84  ? 16.277 -129.487 -73.105  1.00 50.18  ? 85  LEU I CB  1 
ATOM   9503  C  CG  . LEU I  1 84  ? 17.460 -128.819 -72.392  1.00 49.46  ? 85  LEU I CG  1 
ATOM   9504  C  CD1 . LEU I  1 84  ? 17.059 -128.357 -71.003  1.00 47.92  ? 85  LEU I CD1 1 
ATOM   9505  C  CD2 . LEU I  1 84  ? 18.646 -129.753 -72.309  1.00 51.71  ? 85  LEU I CD2 1 
ATOM   9506  N  N   . GLY I  1 85  ? 14.996 -130.866 -76.139  1.00 53.81  ? 86  GLY I N   1 
ATOM   9507  C  CA  . GLY I  1 85  ? 14.130 -131.898 -76.713  1.00 55.76  ? 86  GLY I CA  1 
ATOM   9508  C  C   . GLY I  1 85  ? 12.721 -131.956 -76.144  1.00 55.00  ? 86  GLY I C   1 
ATOM   9509  O  O   . GLY I  1 85  ? 12.034 -130.940 -76.057  1.00 53.21  ? 86  GLY I O   1 
ATOM   9510  N  N   . ASN I  1 86  ? 12.284 -133.153 -75.763  1.00 56.90  ? 87  ASN I N   1 
ATOM   9511  C  CA  . ASN I  1 86  ? 10.909 -133.356 -75.297  1.00 56.99  ? 87  ASN I CA  1 
ATOM   9512  C  C   . ASN I  1 86  ? 10.775 -133.812 -73.851  1.00 57.40  ? 87  ASN I C   1 
ATOM   9513  O  O   . ASN I  1 86  ? 11.708 -134.359 -73.267  1.00 58.37  ? 87  ASN I O   1 
ATOM   9514  C  CB  . ASN I  1 86  ? 10.206 -134.386 -76.170  1.00 59.73  ? 87  ASN I CB  1 
ATOM   9515  C  CG  . ASN I  1 86  ? 9.811  -133.837 -77.521  1.00 59.69  ? 87  ASN I CG  1 
ATOM   9516  O  OD1 . ASN I  1 86  ? 9.149  -132.795 -77.618  1.00 58.20  ? 87  ASN I OD1 1 
ATOM   9517  N  ND2 . ASN I  1 86  ? 10.196 -134.550 -78.581  1.00 62.09  ? 87  ASN I ND2 1 
ATOM   9518  N  N   . VAL I  1 87  ? 9.598  -133.560 -73.284  1.00 57.08  ? 88  VAL I N   1 
ATOM   9519  C  CA  . VAL I  1 87  ? 9.215  -134.103 -71.982  1.00 58.40  ? 88  VAL I CA  1 
ATOM   9520  C  C   . VAL I  1 87  ? 7.894  -134.799 -72.154  1.00 60.79  ? 88  VAL I C   1 
ATOM   9521  O  O   . VAL I  1 87  ? 7.035  -134.310 -72.887  1.00 60.25  ? 88  VAL I O   1 
ATOM   9522  C  CB  . VAL I  1 87  ? 9.027  -133.019 -70.903  1.00 56.28  ? 88  VAL I CB  1 
ATOM   9523  C  CG1 . VAL I  1 87  ? 10.347 -132.371 -70.550  1.00 54.38  ? 88  VAL I CG1 1 
ATOM   9524  C  CG2 . VAL I  1 87  ? 8.014  -131.973 -71.349  1.00 54.89  ? 88  VAL I CG2 1 
ATOM   9525  N  N   . THR I  1 88  ? 7.718  -135.918 -71.456  1.00 63.83  ? 89  THR I N   1 
ATOM   9526  C  CA  . THR I  1 88  ? 6.524  -136.778 -71.644  1.00 66.97  ? 89  THR I CA  1 
ATOM   9527  C  C   . THR I  1 88  ? 5.494  -136.683 -70.509  1.00 68.10  ? 89  THR I C   1 
ATOM   9528  O  O   . THR I  1 88  ? 5.817  -136.877 -69.329  1.00 68.89  ? 89  THR I O   1 
ATOM   9529  C  CB  . THR I  1 88  ? 6.916  -138.266 -71.848  1.00 70.63  ? 89  THR I CB  1 
ATOM   9530  O  OG1 . THR I  1 88  ? 7.589  -138.424 -73.110  1.00 70.43  ? 89  THR I OG1 1 
ATOM   9531  C  CG2 . THR I  1 88  ? 5.678  -139.151 -71.836  1.00 74.24  ? 89  THR I CG2 1 
ATOM   9532  N  N   . ALA I  1 89  ? 4.249  -136.405 -70.888  1.00 68.66  ? 90  ALA I N   1 
ATOM   9533  C  CA  . ALA I  1 89  ? 3.152  -136.218 -69.922  1.00 70.23  ? 90  ALA I CA  1 
ATOM   9534  C  C   . ALA I  1 89  ? 2.228  -137.431 -69.852  1.00 74.78  ? 90  ALA I C   1 
ATOM   9535  O  O   . ALA I  1 89  ? 1.737  -137.897 -70.874  1.00 76.24  ? 90  ALA I O   1 
ATOM   9536  C  CB  . ALA I  1 89  ? 2.344  -134.990 -70.280  1.00 68.32  ? 90  ALA I CB  1 
ATOM   9537  N  N   . ASP I  1 90  ? 1.975  -137.919 -68.642  1.00 77.40  ? 91  ASP I N   1 
ATOM   9538  C  CA  . ASP I  1 90  ? 1.116  -139.098 -68.446  1.00 82.41  ? 91  ASP I CA  1 
ATOM   9539  C  C   . ASP I  1 90  ? -0.364 -138.716 -68.278  1.00 84.33  ? 91  ASP I C   1 
ATOM   9540  O  O   . ASP I  1 90  ? -0.681 -137.550 -67.997  1.00 82.07  ? 91  ASP I O   1 
ATOM   9541  C  CB  . ASP I  1 90  ? 1.624  -139.974 -67.276  1.00 85.30  ? 91  ASP I CB  1 
ATOM   9542  C  CG  . ASP I  1 90  ? 1.407  -139.343 -65.891  1.00 85.50  ? 91  ASP I CG  1 
ATOM   9543  O  OD1 . ASP I  1 90  ? 1.786  -140.012 -64.903  1.00 88.36  ? 91  ASP I OD1 1 
ATOM   9544  O  OD2 . ASP I  1 90  ? 0.873  -138.209 -65.772  1.00 83.23  ? 91  ASP I OD2 1 
ATOM   9545  N  N   . LYS I  1 91  ? -1.240 -139.711 -68.469  1.00 88.83  ? 92  LYS I N   1 
ATOM   9546  C  CA  . LYS I  1 91  ? -2.732 -139.592 -68.335  1.00 91.94  ? 92  LYS I CA  1 
ATOM   9547  C  C   . LYS I  1 91  ? -3.241 -138.372 -67.567  1.00 90.54  ? 92  LYS I C   1 
ATOM   9548  O  O   . LYS I  1 91  ? -3.922 -137.518 -68.130  1.00 89.30  ? 92  LYS I O   1 
ATOM   9549  C  CB  . LYS I  1 91  ? -3.363 -140.818 -67.623  1.00 98.09  ? 92  LYS I CB  1 
ATOM   9550  C  CG  . LYS I  1 91  ? -2.602 -142.154 -67.672  1.00 100.87 ? 92  LYS I CG  1 
ATOM   9551  C  CD  . LYS I  1 91  ? -2.599 -142.773 -69.091  1.00 101.66 ? 92  LYS I CD  1 
ATOM   9552  C  CE  . LYS I  1 91  ? -2.312 -144.286 -69.069  1.00 106.22 ? 92  LYS I CE  1 
ATOM   9553  N  NZ  . LYS I  1 91  ? -3.556 -145.118 -68.911  1.00 112.44 ? 92  LYS I NZ  1 
ATOM   9554  N  N   . ASP I  1 92  ? -2.904 -138.312 -66.273  1.00 91.22  ? 93  ASP I N   1 
ATOM   9555  C  CA  . ASP I  1 92  ? -3.437 -137.275 -65.352  1.00 91.12  ? 93  ASP I CA  1 
ATOM   9556  C  C   . ASP I  1 92  ? -2.711 -135.921 -65.507  1.00 85.66  ? 93  ASP I C   1 
ATOM   9557  O  O   . ASP I  1 92  ? -2.819 -135.045 -64.648  1.00 85.32  ? 93  ASP I O   1 
ATOM   9558  C  CB  . ASP I  1 92  ? -3.504 -137.743 -63.859  1.00 94.86  ? 93  ASP I CB  1 
ATOM   9559  C  CG  . ASP I  1 92  ? -2.936 -139.131 -63.628  1.00 98.14  ? 93  ASP I CG  1 
ATOM   9560  O  OD1 . ASP I  1 92  ? -1.701 -139.317 -63.796  1.00 95.67  ? 93  ASP I OD1 1 
ATOM   9561  O  OD2 . ASP I  1 92  ? -3.735 -140.029 -63.269  1.00 103.47 ? 93  ASP I OD2 1 
ATOM   9562  N  N   . GLY I  1 93  ? -1.984 -135.757 -66.611  1.00 81.96  ? 94  GLY I N   1 
ATOM   9563  C  CA  . GLY I  1 93  ? -1.414 -134.473 -66.983  1.00 77.14  ? 94  GLY I CA  1 
ATOM   9564  C  C   . GLY I  1 93  ? -0.055 -134.192 -66.385  1.00 74.31  ? 94  GLY I C   1 
ATOM   9565  O  O   . GLY I  1 93  ? 0.487  -133.104 -66.603  1.00 70.62  ? 94  GLY I O   1 
ATOM   9566  N  N   . VAL I  1 94  ? 0.487  -135.149 -65.619  1.00 76.42  ? 95  VAL I N   1 
ATOM   9567  C  CA  . VAL I  1 94  ? 1.810  -134.993 -64.998  1.00 74.26  ? 95  VAL I CA  1 
ATOM   9568  C  C   . VAL I  1 94  ? 2.956  -135.368 -65.968  1.00 72.12  ? 95  VAL I C   1 
ATOM   9569  O  O   . VAL I  1 94  ? 2.823  -136.273 -66.805  1.00 73.84  ? 95  VAL I O   1 
ATOM   9570  C  CB  . VAL I  1 94  ? 1.897  -135.792 -63.683  1.00 77.96  ? 95  VAL I CB  1 
ATOM   9571  C  CG1 . VAL I  1 94  ? 3.360  -135.822 -63.105  1.00 75.73  ? 95  VAL I CG1 1 
ATOM   9572  C  CG2 . VAL I  1 94  ? 0.894  -135.207 -62.691  1.00 79.99  ? 95  VAL I CG2 1 
ATOM   9573  N  N   . ALA I  1 95  ? 4.057  -134.621 -65.876  1.00 68.54  ? 96  ALA I N   1 
ATOM   9574  C  CA  . ALA I  1 95  ? 5.265  -134.928 -66.621  1.00 66.69  ? 96  ALA I CA  1 
ATOM   9575  C  C   . ALA I  1 95  ? 6.419  -134.958 -65.638  1.00 66.33  ? 96  ALA I C   1 
ATOM   9576  O  O   . ALA I  1 95  ? 6.841  -133.915 -65.160  1.00 63.96  ? 96  ALA I O   1 
ATOM   9577  C  CB  . ALA I  1 95  ? 5.499  -133.891 -67.695  1.00 62.95  ? 96  ALA I CB  1 
ATOM   9578  N  N   . ASP I  1 96  ? 6.907  -136.152 -65.319  1.00 69.12  ? 97  ASP I N   1 
ATOM   9579  C  CA  . ASP I  1 96  ? 8.022  -136.295 -64.377  1.00 69.71  ? 97  ASP I CA  1 
ATOM   9580  C  C   . ASP I  1 96  ? 9.357  -136.155 -65.109  1.00 67.39  ? 97  ASP I C   1 
ATOM   9581  O  O   . ASP I  1 96  ? 9.913  -137.129 -65.599  1.00 69.43  ? 97  ASP I O   1 
ATOM   9582  C  CB  . ASP I  1 96  ? 7.940  -137.621 -63.608  1.00 74.57  ? 97  ASP I CB  1 
ATOM   9583  C  CG  . ASP I  1 96  ? 6.972  -137.550 -62.425  1.00 77.73  ? 97  ASP I CG  1 
ATOM   9584  O  OD1 . ASP I  1 96  ? 7.084  -136.606 -61.600  1.00 76.29  ? 97  ASP I OD1 1 
ATOM   9585  O  OD2 . ASP I  1 96  ? 6.092  -138.437 -62.320  1.00 81.99  ? 97  ASP I OD2 1 
ATOM   9586  N  N   . VAL I  1 97  ? 9.863  -134.927 -65.164  1.00 63.68  ? 98  VAL I N   1 
ATOM   9587  C  CA  . VAL I  1 97  ? 11.059 -134.606 -65.935  1.00 61.46  ? 98  VAL I CA  1 
ATOM   9588  C  C   . VAL I  1 97  ? 12.316 -135.167 -65.291  1.00 63.18  ? 98  VAL I C   1 
ATOM   9589  O  O   . VAL I  1 97  ? 12.548 -134.987 -64.096  1.00 63.94  ? 98  VAL I O   1 
ATOM   9590  C  CB  . VAL I  1 97  ? 11.276 -133.096 -66.063  1.00 57.66  ? 98  VAL I CB  1 
ATOM   9591  C  CG1 . VAL I  1 97  ? 12.493 -132.822 -66.907  1.00 56.08  ? 98  VAL I CG1 1 
ATOM   9592  C  CG2 . VAL I  1 97  ? 10.072 -132.438 -66.659  1.00 56.60  ? 98  VAL I CG2 1 
ATOM   9593  N  N   . SER I  1 98  ? 13.127 -135.849 -66.095  1.00 64.35  ? 99  SER I N   1 
ATOM   9594  C  CA  . SER I  1 98  ? 14.476 -136.301 -65.674  1.00 65.97  ? 99  SER I CA  1 
ATOM   9595  C  C   . SER I  1 98  ? 15.418 -136.401 -66.855  1.00 65.58  ? 99  SER I C   1 
ATOM   9596  O  O   . SER I  1 98  ? 15.554 -137.453 -67.461  1.00 68.31  ? 99  SER I O   1 
ATOM   9597  C  CB  . SER I  1 98  ? 14.440 -137.646 -64.959  1.00 70.49  ? 99  SER I CB  1 
ATOM   9598  O  OG  . SER I  1 98  ? 15.768 -138.094 -64.727  1.00 71.95  ? 99  SER I OG  1 
ATOM   9599  N  N   . ILE I  1 99  ? 16.046 -135.276 -67.171  1.00 62.61  ? 100 ILE I N   1 
ATOM   9600  C  CA  . ILE I  1 99  ? 16.967 -135.171 -68.292  1.00 62.30  ? 100 ILE I CA  1 
ATOM   9601  C  C   . ILE I  1 99  ? 18.371 -135.025 -67.741  1.00 63.12  ? 100 ILE I C   1 
ATOM   9602  O  O   . ILE I  1 99  ? 18.549 -134.601 -66.605  1.00 62.82  ? 100 ILE I O   1 
ATOM   9603  C  CB  . ILE I  1 99  ? 16.619 -133.946 -69.197  1.00 58.70  ? 100 ILE I CB  1 
ATOM   9604  C  CG1 . ILE I  1 99  ? 15.269 -134.169 -69.895  1.00 58.45  ? 100 ILE I CG1 1 
ATOM   9605  C  CG2 . ILE I  1 99  ? 17.703 -133.701 -70.229  1.00 58.82  ? 100 ILE I CG2 1 
ATOM   9606  C  CD1 . ILE I  1 99  ? 15.046 -133.341 -71.133  1.00 56.25  ? 100 ILE I CD1 1 
ATOM   9607  N  N   . GLU I  1 100 ? 19.359 -135.413 -68.541  1.00 64.81  ? 101 GLU I N   1 
ATOM   9608  C  CA  . GLU I  1 100 ? 20.759 -135.089 -68.267  1.00 65.49  ? 101 GLU I CA  1 
ATOM   9609  C  C   . GLU I  1 100 ? 21.394 -134.594 -69.561  1.00 64.81  ? 101 GLU I C   1 
ATOM   9610  O  O   . GLU I  1 100 ? 21.322 -135.264 -70.579  1.00 66.67  ? 101 GLU I O   1 
ATOM   9611  C  CB  . GLU I  1 100 ? 21.503 -136.304 -67.718  1.00 70.01  ? 101 GLU I CB  1 
ATOM   9612  C  CG  . GLU I  1 100 ? 22.950 -135.991 -67.265  1.00 71.81  ? 101 GLU I CG  1 
ATOM   9613  C  CD  . GLU I  1 100 ? 23.619 -137.110 -66.429  1.00 76.98  ? 101 GLU I CD  1 
ATOM   9614  O  OE1 . GLU I  1 100 ? 24.735 -136.876 -65.902  1.00 78.05  ? 101 GLU I OE1 1 
ATOM   9615  O  OE2 . GLU I  1 100 ? 23.038 -138.217 -66.294  1.00 79.88  ? 101 GLU I OE2 1 
ATOM   9616  N  N   . ASP I  1 101 ? 22.001 -133.415 -69.529  1.00 62.72  ? 102 ASP I N   1 
ATOM   9617  C  CA  . ASP I  1 101 ? 22.500 -132.789 -70.756  1.00 62.15  ? 102 ASP I CA  1 
ATOM   9618  C  C   . ASP I  1 101 ? 23.904 -132.207 -70.608  1.00 63.04  ? 102 ASP I C   1 
ATOM   9619  O  O   . ASP I  1 101 ? 24.291 -131.756 -69.530  1.00 62.38  ? 102 ASP I O   1 
ATOM   9620  C  CB  . ASP I  1 101 ? 21.541 -131.705 -71.225  1.00 58.48  ? 102 ASP I CB  1 
ATOM   9621  C  CG  . ASP I  1 101 ? 21.813 -131.288 -72.641  1.00 58.54  ? 102 ASP I CG  1 
ATOM   9622  O  OD1 . ASP I  1 101 ? 21.601 -132.123 -73.537  1.00 60.38  ? 102 ASP I OD1 1 
ATOM   9623  O  OD2 . ASP I  1 101 ? 22.265 -130.146 -72.865  1.00 57.08  ? 102 ASP I OD2 1 
ATOM   9624  N  N   . SER I  1 102 ? 24.643 -132.212 -71.714  1.00 64.83  ? 103 SER I N   1 
ATOM   9625  C  CA  . SER I  1 102 ? 26.058 -131.817 -71.736  1.00 66.85  ? 103 SER I CA  1 
ATOM   9626  C  C   . SER I  1 102 ? 26.368 -130.561 -72.544  1.00 65.37  ? 103 SER I C   1 
ATOM   9627  O  O   . SER I  1 102 ? 27.486 -130.050 -72.458  1.00 66.88  ? 103 SER I O   1 
ATOM   9628  C  CB  . SER I  1 102 ? 26.898 -132.948 -72.320  1.00 71.63  ? 103 SER I CB  1 
ATOM   9629  O  OG  . SER I  1 102 ? 26.638 -134.169 -71.640  1.00 73.96  ? 103 SER I OG  1 
ATOM   9630  N  N   . VAL I  1 103 ? 25.410 -130.079 -73.338  1.00 63.01  ? 104 VAL I N   1 
ATOM   9631  C  CA  . VAL I  1 103 ? 25.594 -128.831 -74.096  1.00 61.80  ? 104 VAL I CA  1 
ATOM   9632  C  C   . VAL I  1 103 ? 25.309 -127.612 -73.222  1.00 58.64  ? 104 VAL I C   1 
ATOM   9633  O  O   . VAL I  1 103 ? 26.118 -126.684 -73.196  1.00 59.06  ? 104 VAL I O   1 
ATOM   9634  C  CB  . VAL I  1 103 ? 24.706 -128.763 -75.350  1.00 61.13  ? 104 VAL I CB  1 
ATOM   9635  C  CG1 . VAL I  1 103 ? 24.974 -127.479 -76.116  1.00 60.48  ? 104 VAL I CG1 1 
ATOM   9636  C  CG2 . VAL I  1 103 ? 24.963 -129.942 -76.242  1.00 64.92  ? 104 VAL I CG2 1 
ATOM   9637  N  N   . ILE I  1 104 ? 24.172 -127.616 -72.515  1.00 55.99  ? 105 ILE I N   1 
ATOM   9638  C  CA  . ILE I  1 104 ? 23.821 -126.507 -71.615  1.00 53.19  ? 105 ILE I CA  1 
ATOM   9639  C  C   . ILE I  1 104 ? 24.802 -126.439 -70.457  1.00 54.23  ? 105 ILE I C   1 
ATOM   9640  O  O   . ILE I  1 104 ? 25.493 -127.415 -70.156  1.00 56.65  ? 105 ILE I O   1 
ATOM   9641  C  CB  . ILE I  1 104 ? 22.385 -126.610 -71.033  1.00 50.87  ? 105 ILE I CB  1 
ATOM   9642  C  CG1 . ILE I  1 104 ? 22.213 -127.833 -70.129  1.00 52.04  ? 105 ILE I CG1 1 
ATOM   9643  C  CG2 . ILE I  1 104 ? 21.357 -126.651 -72.151  1.00 50.08  ? 105 ILE I CG2 1 
ATOM   9644  C  CD1 . ILE I  1 104 ? 21.032 -127.744 -69.199  1.00 49.93  ? 105 ILE I CD1 1 
ATOM   9645  N  N   . SER I  1 105 ? 24.869 -125.280 -69.814  1.00 52.73  ? 106 SER I N   1 
ATOM   9646  C  CA  . SER I  1 105 ? 25.714 -125.124 -68.625  1.00 53.66  ? 106 SER I CA  1 
ATOM   9647  C  C   . SER I  1 105 ? 25.230 -124.031 -67.708  1.00 51.41  ? 106 SER I C   1 
ATOM   9648  O  O   . SER I  1 105 ? 24.550 -123.099 -68.141  1.00 49.50  ? 106 SER I O   1 
ATOM   9649  C  CB  . SER I  1 105 ? 27.162 -124.831 -69.006  1.00 56.27  ? 106 SER I CB  1 
ATOM   9650  O  OG  . SER I  1 105 ? 28.006 -124.916 -67.864  1.00 57.51  ? 106 SER I OG  1 
ATOM   9651  N  N   . LEU I  1 106 ? 25.597 -124.168 -66.436  1.00 52.08  ? 107 LEU I N   1 
ATOM   9652  C  CA  . LEU I  1 106 ? 25.292 -123.178 -65.409  1.00 50.66  ? 107 LEU I CA  1 
ATOM   9653  C  C   . LEU I  1 106 ? 26.455 -122.216 -65.209  1.00 51.87  ? 107 LEU I C   1 
ATOM   9654  O  O   . LEU I  1 106 ? 26.528 -121.558 -64.182  1.00 51.81  ? 107 LEU I O   1 
ATOM   9655  C  CB  . LEU I  1 106 ? 24.959 -123.859 -64.081  1.00 51.14  ? 107 LEU I CB  1 
ATOM   9656  C  CG  . LEU I  1 106 ? 23.753 -124.793 -64.097  1.00 50.31  ? 107 LEU I CG  1 
ATOM   9657  C  CD1 . LEU I  1 106 ? 23.491 -125.322 -62.716  1.00 51.50  ? 107 LEU I CD1 1 
ATOM   9658  C  CD2 . LEU I  1 106 ? 22.515 -124.119 -64.608  1.00 47.52  ? 107 LEU I CD2 1 
ATOM   9659  N  N   . SER I  1 107 ? 27.363 -122.143 -66.186  1.00 53.50  ? 108 SER I N   1 
ATOM   9660  C  CA  . SER I  1 107 ? 28.528 -121.240 -66.138  1.00 54.93  ? 108 SER I CA  1 
ATOM   9661  C  C   . SER I  1 107 ? 29.192 -121.054 -67.507  1.00 56.45  ? 108 SER I C   1 
ATOM   9662  O  O   . SER I  1 107 ? 29.323 -122.000 -68.283  1.00 57.67  ? 108 SER I O   1 
ATOM   9663  C  CB  . SER I  1 107 ? 29.566 -121.744 -65.131  1.00 57.46  ? 108 SER I CB  1 
ATOM   9664  O  OG  . SER I  1 107 ? 29.984 -123.058 -65.425  1.00 59.56  ? 108 SER I OG  1 
ATOM   9665  N  N   . GLY I  1 108 ? 29.592 -119.817 -67.793  1.00 56.83  ? 109 GLY I N   1 
ATOM   9666  C  CA  . GLY I  1 108 ? 30.353 -119.484 -69.002  1.00 59.10  ? 109 GLY I CA  1 
ATOM   9667  C  C   . GLY I  1 108 ? 29.564 -119.087 -70.249  1.00 57.98  ? 109 GLY I C   1 
ATOM   9668  O  O   . GLY I  1 108 ? 28.482 -118.522 -70.184  1.00 55.38  ? 109 GLY I O   1 
ATOM   9669  N  N   . ASP I  1 109 ? 30.142 -119.374 -71.405  1.00 60.56  ? 110 ASP I N   1 
ATOM   9670  C  CA  . ASP I  1 109 ? 29.545 -119.022 -72.712  1.00 60.49  ? 110 ASP I CA  1 
ATOM   9671  C  C   . ASP I  1 109 ? 28.126 -119.562 -72.901  1.00 57.35  ? 110 ASP I C   1 
ATOM   9672  O  O   . ASP I  1 109 ? 27.251 -118.895 -73.448  1.00 55.54  ? 110 ASP I O   1 
ATOM   9673  C  CB  . ASP I  1 109 ? 30.422 -119.580 -73.850  1.00 64.40  ? 110 ASP I CB  1 
ATOM   9674  C  CG  . ASP I  1 109 ? 30.321 -118.741 -75.137  1.00 66.14  ? 110 ASP I CG  1 
ATOM   9675  O  OD1 . ASP I  1 109 ? 29.461 -119.048 -76.008  1.00 65.22  ? 110 ASP I OD1 1 
ATOM   9676  O  OD2 . ASP I  1 109 ? 31.101 -117.756 -75.253  1.00 68.51  ? 110 ASP I OD2 1 
ATOM   9677  N  N   . HIS I  1 110 ? 27.953 -120.802 -72.458  1.00 57.06  ? 111 HIS I N   1 
ATOM   9678  C  CA  . HIS I  1 110 ? 26.706 -121.552 -72.569  1.00 55.01  ? 111 HIS I CA  1 
ATOM   9679  C  C   . HIS I  1 110 ? 25.781 -121.325 -71.363  1.00 52.08  ? 111 HIS I C   1 
ATOM   9680  O  O   . HIS I  1 110 ? 24.778 -122.029 -71.200  1.00 50.73  ? 111 HIS I O   1 
ATOM   9681  C  CB  . HIS I  1 110 ? 27.020 -123.060 -72.674  1.00 56.85  ? 111 HIS I CB  1 
ATOM   9682  C  CG  . HIS I  1 110 ? 27.685 -123.472 -73.961  1.00 60.17  ? 111 HIS I CG  1 
ATOM   9683  N  ND1 . HIS I  1 110 ? 27.815 -124.795 -74.343  1.00 62.13  ? 111 HIS I ND1 1 
ATOM   9684  C  CD2 . HIS I  1 110 ? 28.244 -122.739 -74.959  1.00 62.17  ? 111 HIS I CD2 1 
ATOM   9685  C  CE1 . HIS I  1 110 ? 28.431 -124.858 -75.512  1.00 65.06  ? 111 HIS I CE1 1 
ATOM   9686  N  NE2 . HIS I  1 110 ? 28.704 -123.625 -75.909  1.00 65.33  ? 111 HIS I NE2 1 
ATOM   9687  N  N   . CYS I  1 111 ? 26.112 -120.352 -70.520  1.00 51.53  ? 112 CYS I N   1 
ATOM   9688  C  CA  . CYS I  1 111 ? 25.377 -120.134 -69.265  1.00 49.40  ? 112 CYS I CA  1 
ATOM   9689  C  C   . CYS I  1 111 ? 23.905 -119.868 -69.526  1.00 46.98  ? 112 CYS I C   1 
ATOM   9690  O  O   . CYS I  1 111 ? 23.562 -118.885 -70.176  1.00 46.39  ? 112 CYS I O   1 
ATOM   9691  C  CB  . CYS I  1 111 ? 25.975 -118.970 -68.475  1.00 49.73  ? 112 CYS I CB  1 
ATOM   9692  S  SG  . CYS I  1 111 ? 25.335 -118.767 -66.812  1.00 47.94  ? 112 CYS I SG  1 
ATOM   9693  N  N   . ILE I  1 112 ? 23.058 -120.763 -69.023  1.00 45.92  ? 113 ILE I N   1 
ATOM   9694  C  CA  . ILE I  1 112 ? 21.605 -120.636 -69.163  1.00 44.23  ? 113 ILE I CA  1 
ATOM   9695  C  C   . ILE I  1 112 ? 20.948 -119.820 -68.022  1.00 43.12  ? 113 ILE I C   1 
ATOM   9696  O  O   . ILE I  1 112 ? 19.761 -119.454 -68.099  1.00 42.01  ? 113 ILE I O   1 
ATOM   9697  C  CB  . ILE I  1 112 ? 20.905 -122.020 -69.272  1.00 44.24  ? 113 ILE I CB  1 
ATOM   9698  C  CG1 . ILE I  1 112 ? 21.137 -122.870 -68.019  1.00 44.74  ? 113 ILE I CG1 1 
ATOM   9699  C  CG2 . ILE I  1 112 ? 21.367 -122.745 -70.516  1.00 45.65  ? 113 ILE I CG2 1 
ATOM   9700  C  CD1 . ILE I  1 112 ? 20.081 -123.923 -67.797  1.00 44.69  ? 113 ILE I CD1 1 
ATOM   9701  N  N   . ILE I  1 113 ? 21.717 -119.543 -66.969  1.00 43.72  ? 114 ILE I N   1 
ATOM   9702  C  CA  . ILE I  1 113 ? 21.204 -118.817 -65.802  1.00 42.90  ? 114 ILE I CA  1 
ATOM   9703  C  C   . ILE I  1 113 ? 20.850 -117.407 -66.199  1.00 42.32  ? 114 ILE I C   1 
ATOM   9704  O  O   . ILE I  1 113 ? 21.643 -116.726 -66.852  1.00 42.95  ? 114 ILE I O   1 
ATOM   9705  C  CB  . ILE I  1 113 ? 22.219 -118.759 -64.658  1.00 44.04  ? 114 ILE I CB  1 
ATOM   9706  C  CG1 . ILE I  1 113 ? 22.304 -120.122 -63.984  1.00 44.98  ? 114 ILE I CG1 1 
ATOM   9707  C  CG2 . ILE I  1 113 ? 21.833 -117.710 -63.647  1.00 43.65  ? 114 ILE I CG2 1 
ATOM   9708  C  CD1 . ILE I  1 113 ? 23.403 -120.216 -62.978  1.00 46.98  ? 114 ILE I CD1 1 
ATOM   9709  N  N   . GLY I  1 114 ? 19.653 -116.985 -65.796  1.00 41.51  ? 115 GLY I N   1 
ATOM   9710  C  CA  . GLY I  1 114 ? 19.116 -115.670 -66.142  1.00 41.33  ? 115 GLY I CA  1 
ATOM   9711  C  C   . GLY I  1 114 ? 18.327 -115.702 -67.434  1.00 40.84  ? 115 GLY I C   1 
ATOM   9712  O  O   . GLY I  1 114 ? 17.873 -114.662 -67.915  1.00 41.04  ? 115 GLY I O   1 
ATOM   9713  N  N   . ARG I  1 115 ? 18.178 -116.897 -67.999  1.00 40.53  ? 116 ARG I N   1 
ATOM   9714  C  CA  . ARG I  1 115 ? 17.398 -117.089 -69.211  1.00 40.54  ? 116 ARG I CA  1 
ATOM   9715  C  C   . ARG I  1 115 ? 16.131 -117.883 -68.922  1.00 39.99  ? 116 ARG I C   1 
ATOM   9716  O  O   . ARG I  1 115 ? 15.979 -118.430 -67.843  1.00 39.93  ? 116 ARG I O   1 
ATOM   9717  C  CB  . ARG I  1 115 ? 18.241 -117.789 -70.274  1.00 41.20  ? 116 ARG I CB  1 
ATOM   9718  C  CG  . ARG I  1 115 ? 19.539 -117.059 -70.572  1.00 42.35  ? 116 ARG I CG  1 
ATOM   9719  C  CD  . ARG I  1 115 ? 20.283 -117.663 -71.716  1.00 43.70  ? 116 ARG I CD  1 
ATOM   9720  N  NE  . ARG I  1 115 ? 21.611 -117.079 -71.851  1.00 45.04  ? 116 ARG I NE  1 
ATOM   9721  C  CZ  . ARG I  1 115 ? 21.895 -115.972 -72.524  1.00 46.12  ? 116 ARG I CZ  1 
ATOM   9722  N  NH1 . ARG I  1 115 ? 20.941 -115.281 -73.133  1.00 45.92  ? 116 ARG I NH1 1 
ATOM   9723  N  NH2 . ARG I  1 115 ? 23.157 -115.558 -72.592  1.00 48.16  ? 116 ARG I NH2 1 
ATOM   9724  N  N   . THR I  1 116 ? 15.233 -117.943 -69.899  1.00 40.02  ? 117 THR I N   1 
ATOM   9725  C  CA  . THR I  1 116 ? 13.907 -118.540 -69.720  1.00 39.92  ? 117 THR I CA  1 
ATOM   9726  C  C   . THR I  1 116 ? 13.794 -120.009 -70.169  1.00 40.24  ? 117 THR I C   1 
ATOM   9727  O  O   . THR I  1 116 ? 14.160 -120.368 -71.292  1.00 40.73  ? 117 THR I O   1 
ATOM   9728  C  CB  . THR I  1 116 ? 12.850 -117.753 -70.492  1.00 40.25  ? 117 THR I CB  1 
ATOM   9729  O  OG1 . THR I  1 116 ? 12.767 -116.429 -69.978  1.00 40.26  ? 117 THR I OG1 1 
ATOM   9730  C  CG2 . THR I  1 116 ? 11.513 -118.407 -70.353  1.00 40.69  ? 117 THR I CG2 1 
ATOM   9731  N  N   . LEU I  1 117 ? 13.262 -120.848 -69.282  1.00 40.44  ? 118 LEU I N   1 
ATOM   9732  C  CA  . LEU I  1 117 ? 12.866 -122.223 -69.618  1.00 40.98  ? 118 LEU I CA  1 
ATOM   9733  C  C   . LEU I  1 117 ? 11.427 -122.198 -70.101  1.00 41.36  ? 118 LEU I C   1 
ATOM   9734  O  O   . LEU I  1 117 ? 10.638 -121.402 -69.605  1.00 41.68  ? 118 LEU I O   1 
ATOM   9735  C  CB  . LEU I  1 117 ? 12.975 -123.128 -68.393  1.00 41.53  ? 118 LEU I CB  1 
ATOM   9736  C  CG  . LEU I  1 117 ? 12.722 -124.609 -68.640  1.00 42.60  ? 118 LEU I CG  1 
ATOM   9737  C  CD1 . LEU I  1 117 ? 13.710 -125.148 -69.649  1.00 42.99  ? 118 LEU I CD1 1 
ATOM   9738  C  CD2 . LEU I  1 117 ? 12.824 -125.400 -67.351  1.00 43.61  ? 118 LEU I CD2 1 
ATOM   9739  N  N   . VAL I  1 118 ? 11.076 -123.064 -71.049  1.00 41.88  ? 119 VAL I N   1 
ATOM   9740  C  CA  . VAL I  1 118 ? 9.760  -123.003 -71.695  1.00 42.58  ? 119 VAL I CA  1 
ATOM   9741  C  C   . VAL I  1 118 ? 9.222  -124.360 -72.095  1.00 43.87  ? 119 VAL I C   1 
ATOM   9742  O  O   . VAL I  1 118 ? 9.843  -125.053 -72.868  1.00 44.41  ? 119 VAL I O   1 
ATOM   9743  C  CB  . VAL I  1 118 ? 9.805  -122.150 -72.965  1.00 42.44  ? 119 VAL I CB  1 
ATOM   9744  C  CG1 . VAL I  1 118 ? 8.546  -122.317 -73.756  1.00 43.72  ? 119 VAL I CG1 1 
ATOM   9745  C  CG2 . VAL I  1 118 ? 10.005 -120.700 -72.622  1.00 41.96  ? 119 VAL I CG2 1 
ATOM   9746  N  N   . VAL I  1 119 ? 8.053  -124.722 -71.576  1.00 44.98  ? 120 VAL I N   1 
ATOM   9747  C  CA  . VAL I  1 119 ? 7.396  -125.964 -71.947  1.00 46.60  ? 120 VAL I CA  1 
ATOM   9748  C  C   . VAL I  1 119 ? 6.349  -125.617 -72.978  1.00 47.46  ? 120 VAL I C   1 
ATOM   9749  O  O   . VAL I  1 119 ? 5.755  -124.555 -72.914  1.00 47.28  ? 120 VAL I O   1 
ATOM   9750  C  CB  . VAL I  1 119 ? 6.775  -126.676 -70.738  1.00 47.93  ? 120 VAL I CB  1 
ATOM   9751  C  CG1 . VAL I  1 119 ? 5.533  -125.971 -70.281  1.00 49.01  ? 120 VAL I CG1 1 
ATOM   9752  C  CG2 . VAL I  1 119 ? 6.481  -128.115 -71.074  1.00 49.97  ? 120 VAL I CG2 1 
ATOM   9753  N  N   . HIS I  1 120 ? 6.119  -126.523 -73.920  1.00 48.95  ? 121 HIS I N   1 
ATOM   9754  C  CA  . HIS I  1 120 ? 5.402  -126.199 -75.169  1.00 49.94  ? 121 HIS I CA  1 
ATOM   9755  C  C   . HIS I  1 120 ? 4.091  -126.939 -75.418  1.00 52.33  ? 121 HIS I C   1 
ATOM   9756  O  O   . HIS I  1 120 ? 3.821  -127.991 -74.825  1.00 53.48  ? 121 HIS I O   1 
ATOM   9757  C  CB  . HIS I  1 120 ? 6.331  -126.423 -76.363  1.00 49.89  ? 121 HIS I CB  1 
ATOM   9758  C  CG  . HIS I  1 120 ? 7.164  -125.234 -76.689  1.00 48.15  ? 121 HIS I CG  1 
ATOM   9759  N  ND1 . HIS I  1 120 ? 6.923  -124.436 -77.785  1.00 48.94  ? 121 HIS I ND1 1 
ATOM   9760  C  CD2 . HIS I  1 120 ? 8.211  -124.682 -76.040  1.00 46.38  ? 121 HIS I CD2 1 
ATOM   9761  C  CE1 . HIS I  1 120 ? 7.807  -123.457 -77.814  1.00 47.66  ? 121 HIS I CE1 1 
ATOM   9762  N  NE2 . HIS I  1 120 ? 8.591  -123.577 -76.760  1.00 46.23  ? 121 HIS I NE2 1 
ATOM   9763  N  N   . GLU I  1 121 ? 3.313  -126.382 -76.347  1.00 53.39  ? 122 GLU I N   1 
ATOM   9764  C  CA  . GLU I  1 121 ? 1.986  -126.907 -76.724  1.00 56.04  ? 122 GLU I CA  1 
ATOM   9765  C  C   . GLU I  1 121 ? 2.064  -128.325 -77.282  1.00 57.61  ? 122 GLU I C   1 
ATOM   9766  O  O   . GLU I  1 121 ? 1.516  -129.262 -76.694  1.00 59.14  ? 122 GLU I O   1 
ATOM   9767  C  CB  . GLU I  1 121 ? 1.321  -125.979 -77.759  1.00 56.98  ? 122 GLU I CB  1 
ATOM   9768  C  CG  . GLU I  1 121 ? -0.034 -126.476 -78.294  1.00 60.21  ? 122 GLU I CG  1 
ATOM   9769  C  CD  . GLU I  1 121 ? -0.564 -125.675 -79.478  1.00 61.94  ? 122 GLU I CD  1 
ATOM   9770  O  OE1 . GLU I  1 121 ? 0.178  -124.839 -80.028  1.00 60.76  ? 122 GLU I OE1 1 
ATOM   9771  O  OE2 . GLU I  1 121 ? -1.723 -125.896 -79.876  1.00 64.54  ? 122 GLU I OE2 1 
ATOM   9772  N  N   . LYS I  1 122 ? 2.746  -128.446 -78.424  1.00 57.66  ? 123 LYS I N   1 
ATOM   9773  C  CA  . LYS I  1 122 ? 2.917  -129.712 -79.150  1.00 59.55  ? 123 LYS I CA  1 
ATOM   9774  C  C   . LYS I  1 122 ? 4.270  -130.339 -78.825  1.00 58.51  ? 123 LYS I C   1 
ATOM   9775  O  O   . LYS I  1 122 ? 5.038  -129.802 -78.030  1.00 56.46  ? 123 LYS I O   1 
ATOM   9776  C  CB  . LYS I  1 122 ? 2.830  -129.497 -80.677  1.00 60.87  ? 123 LYS I CB  1 
ATOM   9777  C  CG  . LYS I  1 122 ? 1.627  -128.703 -81.167  1.00 62.38  ? 123 LYS I CG  1 
ATOM   9778  C  CD  . LYS I  1 122 ? 1.663  -128.510 -82.679  1.00 64.18  ? 123 LYS I CD  1 
ATOM   9779  C  CE  . LYS I  1 122 ? 0.585  -127.529 -83.149  1.00 65.66  ? 123 LYS I CE  1 
ATOM   9780  N  NZ  . LYS I  1 122 ? 0.446  -127.585 -84.639  1.00 68.22  ? 123 LYS I NZ  1 
ATOM   9781  N  N   . ALA I  1 123 ? 4.556  -131.476 -79.451  1.00 60.33  ? 124 ALA I N   1 
ATOM   9782  C  CA  . ALA I  1 123 ? 5.857  -132.117 -79.316  1.00 59.90  ? 124 ALA I CA  1 
ATOM   9783  C  C   . ALA I  1 123 ? 6.881  -131.513 -80.285  1.00 59.14  ? 124 ALA I C   1 
ATOM   9784  O  O   . ALA I  1 123 ? 6.545  -131.090 -81.393  1.00 59.77  ? 124 ALA I O   1 
ATOM   9785  C  CB  . ALA I  1 123 ? 5.729  -133.595 -79.542  1.00 62.85  ? 124 ALA I CB  1 
ATOM   9786  N  N   . ASP I  1 124 ? 8.132  -131.478 -79.833  1.00 58.06  ? 125 ASP I N   1 
ATOM   9787  C  CA  . ASP I  1 124 ? 9.280  -131.050 -80.639  1.00 57.96  ? 125 ASP I CA  1 
ATOM   9788  C  C   . ASP I  1 124 ? 9.680  -132.168 -81.611  1.00 61.06  ? 125 ASP I C   1 
ATOM   9789  O  O   . ASP I  1 124 ? 10.029 -133.272 -81.193  1.00 62.45  ? 125 ASP I O   1 
ATOM   9790  C  CB  . ASP I  1 124 ? 10.470 -130.696 -79.729  1.00 56.04  ? 125 ASP I CB  1 
ATOM   9791  C  CG  . ASP I  1 124 ? 11.667 -130.144 -80.498  1.00 56.36  ? 125 ASP I CG  1 
ATOM   9792  O  OD1 . ASP I  1 124 ? 11.571 -129.963 -81.729  1.00 57.81  ? 125 ASP I OD1 1 
ATOM   9793  O  OD2 . ASP I  1 124 ? 12.720 -129.881 -79.868  1.00 55.35  ? 125 ASP I OD2 1 
ATOM   9794  N  N   . ASP I  1 125 ? 9.651  -131.874 -82.911  1.00 62.53  ? 126 ASP I N   1 
ATOM   9795  C  CA  . ASP I  1 125 ? 9.950  -132.885 -83.945  1.00 65.77  ? 126 ASP I CA  1 
ATOM   9796  C  C   . ASP I  1 125 ? 11.453 -133.136 -84.119  1.00 66.68  ? 126 ASP I C   1 
ATOM   9797  O  O   . ASP I  1 125 ? 11.875 -133.794 -85.057  1.00 69.71  ? 126 ASP I O   1 
ATOM   9798  C  CB  . ASP I  1 125 ? 9.292  -132.518 -85.289  1.00 67.53  ? 126 ASP I CB  1 
ATOM   9799  C  CG  . ASP I  1 125 ? 10.008 -131.407 -86.030  1.00 67.19  ? 126 ASP I CG  1 
ATOM   9800  O  OD1 . ASP I  1 125 ? 11.235 -131.232 -85.868  1.00 66.68  ? 126 ASP I OD1 1 
ATOM   9801  O  OD2 . ASP I  1 125 ? 9.323  -130.721 -86.817  1.00 67.58  ? 126 ASP I OD2 1 
ATOM   9802  N  N   . LEU I  1 126 ? 12.252 -132.569 -83.225  1.00 64.38  ? 127 LEU I N   1 
ATOM   9803  C  CA  . LEU I  1 126 ? 13.705 -132.742 -83.200  1.00 65.27  ? 127 LEU I CA  1 
ATOM   9804  C  C   . LEU I  1 126 ? 14.389 -132.406 -84.526  1.00 67.65  ? 127 LEU I C   1 
ATOM   9805  O  O   . LEU I  1 126 ? 15.432 -132.964 -84.858  1.00 70.29  ? 127 LEU I O   1 
ATOM   9806  C  CB  . LEU I  1 126 ? 14.071 -134.150 -82.753  1.00 67.38  ? 127 LEU I CB  1 
ATOM   9807  C  CG  . LEU I  1 126 ? 13.366 -134.634 -81.493  1.00 66.11  ? 127 LEU I CG  1 
ATOM   9808  C  CD1 . LEU I  1 126 ? 13.983 -135.927 -81.014  1.00 69.02  ? 127 LEU I CD1 1 
ATOM   9809  C  CD2 . LEU I  1 126 ? 13.435 -133.605 -80.417  1.00 62.70  ? 127 LEU I CD2 1 
ATOM   9810  N  N   . GLY I  1 127 ? 13.802 -131.474 -85.272  1.00 67.29  ? 128 GLY I N   1 
ATOM   9811  C  CA  . GLY I  1 127 ? 14.392 -130.969 -86.517  1.00 69.61  ? 128 GLY I CA  1 
ATOM   9812  C  C   . GLY I  1 127 ? 14.185 -131.844 -87.739  1.00 73.68  ? 128 GLY I C   1 
ATOM   9813  O  O   . GLY I  1 127 ? 14.547 -131.440 -88.845  1.00 76.10  ? 128 GLY I O   1 
ATOM   9814  N  N   . LYS I  1 128 ? 13.587 -133.026 -87.549  1.00 74.83  ? 129 LYS I N   1 
ATOM   9815  C  CA  . LYS I  1 128 ? 13.421 -134.023 -88.633  1.00 79.05  ? 129 LYS I CA  1 
ATOM   9816  C  C   . LYS I  1 128 ? 12.089 -133.860 -89.366  1.00 79.71  ? 129 LYS I C   1 
ATOM   9817  O  O   . LYS I  1 128 ? 11.563 -134.813 -89.958  1.00 82.50  ? 129 LYS I O   1 
ATOM   9818  C  CB  . LYS I  1 128 ? 13.505 -135.441 -88.072  1.00 80.58  ? 129 LYS I CB  1 
ATOM   9819  C  CG  . LYS I  1 128 ? 14.743 -135.715 -87.238  1.00 80.69  ? 129 LYS I CG  1 
ATOM   9820  C  CD  . LYS I  1 128 ? 15.035 -137.230 -87.110  1.00 84.58  ? 129 LYS I CD  1 
ATOM   9821  C  CE  . LYS I  1 128 ? 16.209 -137.511 -86.114  1.00 84.71  ? 129 LYS I CE  1 
ATOM   9822  N  NZ  . LYS I  1 128 ? 16.801 -138.901 -86.227  1.00 89.26  ? 129 LYS I NZ  1 
ATOM   9823  N  N   . GLY I  1 129 ? 11.553 -132.640 -89.320  1.00 77.35  ? 130 GLY I N   1 
ATOM   9824  C  CA  . GLY I  1 129 ? 10.194 -132.354 -89.795  1.00 77.61  ? 130 GLY I CA  1 
ATOM   9825  C  C   . GLY I  1 129 ? 10.101 -132.169 -91.288  1.00 81.14  ? 130 GLY I C   1 
ATOM   9826  O  O   . GLY I  1 129 ? 9.059  -132.402 -91.879  1.00 82.90  ? 130 GLY I O   1 
ATOM   9827  N  N   . GLY I  1 130 ? 11.188 -131.724 -91.897  1.00 82.59  ? 131 GLY I N   1 
ATOM   9828  C  CA  . GLY I  1 130 ? 11.235 -131.571 -93.349  1.00 86.86  ? 131 GLY I CA  1 
ATOM   9829  C  C   . GLY I  1 130 ? 10.827 -130.194 -93.830  1.00 86.54  ? 131 GLY I C   1 
ATOM   9830  O  O   . GLY I  1 130 ? 11.283 -129.736 -94.884  1.00 89.80  ? 131 GLY I O   1 
ATOM   9831  N  N   . ASN I  1 131 ? 9.968  -129.525 -93.067  1.00 83.19  ? 132 ASN I N   1 
ATOM   9832  C  CA  . ASN I  1 131 ? 9.575  -128.147 -93.401  1.00 82.98  ? 132 ASN I CA  1 
ATOM   9833  C  C   . ASN I  1 131 ? 10.579 -127.076 -92.900  1.00 80.82  ? 132 ASN I C   1 
ATOM   9834  O  O   . ASN I  1 131 ? 11.560 -127.378 -92.198  1.00 79.04  ? 132 ASN I O   1 
ATOM   9835  C  CB  . ASN I  1 131 ? 8.142  -127.850 -92.916  1.00 81.10  ? 132 ASN I CB  1 
ATOM   9836  C  CG  . ASN I  1 131 ? 8.072  -127.525 -91.451  1.00 76.74  ? 132 ASN I CG  1 
ATOM   9837  O  OD1 . ASN I  1 131 ? 9.074  -127.536 -90.729  1.00 74.79  ? 132 ASN I OD1 1 
ATOM   9838  N  ND2 . ASN I  1 131 ? 6.874  -127.221 -90.996  1.00 75.85  ? 132 ASN I ND2 1 
ATOM   9839  N  N   . GLU I  1 132 ? 10.313 -125.832 -93.281  1.00 81.26  ? 133 GLU I N   1 
ATOM   9840  C  CA  . GLU I  1 132 ? 11.170 -124.706 -92.922  1.00 80.01  ? 133 GLU I CA  1 
ATOM   9841  C  C   . GLU I  1 132 ? 11.230 -124.522 -91.432  1.00 75.24  ? 133 GLU I C   1 
ATOM   9842  O  O   . GLU I  1 132 ? 12.308 -124.403 -90.852  1.00 73.83  ? 133 GLU I O   1 
ATOM   9843  C  CB  . GLU I  1 132 ? 10.640 -123.418 -93.567  1.00 81.84  ? 133 GLU I CB  1 
ATOM   9844  C  CG  . GLU I  1 132 ? 11.166 -122.072 -92.962  1.00 80.48  ? 133 GLU I CG  1 
ATOM   9845  C  CD  . GLU I  1 132 ? 12.506 -121.609 -93.486  1.00 83.43  ? 133 GLU I CD  1 
ATOM   9846  O  OE1 . GLU I  1 132 ? 13.166 -122.405 -94.185  1.00 86.67  ? 133 GLU I OE1 1 
ATOM   9847  O  OE2 . GLU I  1 132 ? 12.904 -120.446 -93.193  1.00 82.69  ? 133 GLU I OE2 1 
ATOM   9848  N  N   . GLU I  1 133 ? 10.047 -124.499 -90.834  1.00 73.25  ? 134 GLU I N   1 
ATOM   9849  C  CA  . GLU I  1 133 ? 9.884  -124.165 -89.417  1.00 69.25  ? 134 GLU I CA  1 
ATOM   9850  C  C   . GLU I  1 133 ? 10.509 -125.199 -88.474  1.00 67.07  ? 134 GLU I C   1 
ATOM   9851  O  O   . GLU I  1 133 ? 10.955 -124.844 -87.389  1.00 64.30  ? 134 GLU I O   1 
ATOM   9852  C  CB  . GLU I  1 133 ? 8.390  -123.979 -89.085  1.00 68.59  ? 134 GLU I CB  1 
ATOM   9853  C  CG  . GLU I  1 133 ? 8.092  -123.224 -87.745  1.00 65.43  ? 134 GLU I CG  1 
ATOM   9854  C  CD  . GLU I  1 133 ? 8.426  -121.717 -87.775  1.00 65.77  ? 134 GLU I CD  1 
ATOM   9855  O  OE1 . GLU I  1 133 ? 8.709  -121.185 -88.893  1.00 68.90  ? 134 GLU I OE1 1 
ATOM   9856  O  OE2 . GLU I  1 133 ? 8.396  -121.073 -86.681  1.00 62.94  ? 134 GLU I OE2 1 
ATOM   9857  N  N   . SER I  1 134 ? 10.562 -126.459 -88.893  1.00 68.72  ? 135 SER I N   1 
ATOM   9858  C  CA  . SER I  1 134 ? 11.160 -127.520 -88.072  1.00 67.56  ? 135 SER I CA  1 
ATOM   9859  C  C   . SER I  1 134 ? 12.634 -127.249 -87.793  1.00 67.16  ? 135 SER I C   1 
ATOM   9860  O  O   . SER I  1 134 ? 13.165 -127.667 -86.768  1.00 65.37  ? 135 SER I O   1 
ATOM   9861  C  CB  . SER I  1 134 ? 11.040 -128.886 -88.750  1.00 70.58  ? 135 SER I CB  1 
ATOM   9862  O  OG  . SER I  1 134 ? 11.804 -129.882 -88.061  1.00 69.95  ? 135 SER I OG  1 
ATOM   9863  N  N   . THR I  1 135 ? 13.285 -126.559 -88.718  1.00 69.26  ? 136 THR I N   1 
ATOM   9864  C  CA  . THR I  1 135 ? 14.670 -126.141 -88.554  1.00 69.51  ? 136 THR I CA  1 
ATOM   9865  C  C   . THR I  1 135 ? 14.882 -125.011 -87.545  1.00 66.49  ? 136 THR I C   1 
ATOM   9866  O  O   . THR I  1 135 ? 16.014 -124.707 -87.168  1.00 66.44  ? 136 THR I O   1 
ATOM   9867  C  CB  . THR I  1 135 ? 15.202 -125.712 -89.896  1.00 73.27  ? 136 THR I CB  1 
ATOM   9868  O  OG1 . THR I  1 135 ? 15.543 -126.885 -90.610  1.00 76.80  ? 136 THR I OG1 1 
ATOM   9869  C  CG2 . THR I  1 135 ? 16.417 -124.859 -89.779  1.00 73.72  ? 136 THR I CG2 1 
ATOM   9870  N  N   . LYS I  1 136 ? 13.793 -124.406 -87.090  1.00 64.40  ? 137 LYS I N   1 
ATOM   9871  C  CA  . LYS I  1 136 ? 13.853 -123.262 -86.186  1.00 61.83  ? 137 LYS I CA  1 
ATOM   9872  C  C   . LYS I  1 136 ? 13.263 -123.602 -84.810  1.00 58.41  ? 137 LYS I C   1 
ATOM   9873  O  O   . LYS I  1 136 ? 13.955 -123.628 -83.797  1.00 56.54  ? 137 LYS I O   1 
ATOM   9874  C  CB  . LYS I  1 136 ? 13.080 -122.079 -86.802  1.00 62.82  ? 137 LYS I CB  1 
ATOM   9875  C  CG  . LYS I  1 136 ? 13.771 -121.362 -87.964  1.00 66.42  ? 137 LYS I CG  1 
ATOM   9876  C  CD  . LYS I  1 136 ? 12.899 -120.194 -88.468  1.00 67.84  ? 137 LYS I CD  1 
ATOM   9877  C  CE  . LYS I  1 136 ? 13.687 -119.124 -89.226  1.00 70.54  ? 137 LYS I CE  1 
ATOM   9878  N  NZ  . LYS I  1 136 ? 13.771 -119.389 -90.682  1.00 74.95  ? 137 LYS I NZ  1 
ATOM   9879  N  N   . THR I  1 137 ? 11.964 -123.845 -84.794  1.00 58.05  ? 138 THR I N   1 
ATOM   9880  C  CA  . THR I  1 137 ? 11.196 -123.957 -83.554  1.00 55.55  ? 138 THR I CA  1 
ATOM   9881  C  C   . THR I  1 137 ? 10.943 -125.398 -83.154  1.00 55.53  ? 138 THR I C   1 
ATOM   9882  O  O   . THR I  1 137 ? 10.523 -125.677 -82.026  1.00 53.85  ? 138 THR I O   1 
ATOM   9883  C  CB  . THR I  1 137 ? 9.822  -123.264 -83.691  1.00 55.74  ? 138 THR I CB  1 
ATOM   9884  O  OG1 . THR I  1 137 ? 8.952  -124.040 -84.528  1.00 57.72  ? 138 THR I OG1 1 
ATOM   9885  C  CG2 . THR I  1 137 ? 9.988  -121.867 -84.288  1.00 56.89  ? 138 THR I CG2 1 
ATOM   9886  N  N   . GLY I  1 138 ? 11.178 -126.304 -84.094  1.00 57.90  ? 139 GLY I N   1 
ATOM   9887  C  CA  . GLY I  1 138 ? 10.890 -127.720 -83.900  1.00 58.75  ? 139 GLY I CA  1 
ATOM   9888  C  C   . GLY I  1 138 ? 9.429  -128.074 -84.137  1.00 59.62  ? 139 GLY I C   1 
ATOM   9889  O  O   . GLY I  1 138 ? 9.015  -129.204 -83.869  1.00 60.44  ? 139 GLY I O   1 
ATOM   9890  N  N   . ASN I  1 139 ? 8.652  -127.111 -84.639  1.00 59.88  ? 140 ASN I N   1 
ATOM   9891  C  CA  . ASN I  1 139 ? 7.192  -127.251 -84.819  1.00 60.94  ? 140 ASN I CA  1 
ATOM   9892  C  C   . ASN I  1 139 ? 6.420  -127.610 -83.549  1.00 59.50  ? 140 ASN I C   1 
ATOM   9893  O  O   . ASN I  1 139 ? 5.335  -128.191 -83.625  1.00 60.95  ? 140 ASN I O   1 
ATOM   9894  C  CB  . ASN I  1 139 ? 6.884  -128.271 -85.920  1.00 64.14  ? 140 ASN I CB  1 
ATOM   9895  C  CG  . ASN I  1 139 ? 7.060  -127.702 -87.309  1.00 66.39  ? 140 ASN I CG  1 
ATOM   9896  O  OD1 . ASN I  1 139 ? 7.471  -128.416 -88.212  1.00 69.04  ? 140 ASN I OD1 1 
ATOM   9897  N  ND2 . ASN I  1 139 ? 6.742  -126.420 -87.493  1.00 65.70  ? 140 ASN I ND2 1 
ATOM   9898  N  N   . ALA I  1 140 ? 6.982  -127.239 -82.393  1.00 57.09  ? 141 ALA I N   1 
ATOM   9899  C  CA  . ALA I  1 140 ? 6.457  -127.631 -81.064  1.00 55.81  ? 141 ALA I CA  1 
ATOM   9900  C  C   . ALA I  1 140 ? 5.370  -126.689 -80.556  1.00 55.15  ? 141 ALA I C   1 
ATOM   9901  O  O   . ALA I  1 140 ? 4.842  -126.854 -79.459  1.00 54.33  ? 141 ALA I O   1 
ATOM   9902  C  CB  . ALA I  1 140 ? 7.580  -127.699 -80.062  1.00 53.93  ? 141 ALA I CB  1 
ATOM   9903  N  N   . GLY I  1 141 ? 5.062  -125.681 -81.356  1.00 55.80  ? 142 GLY I N   1 
ATOM   9904  C  CA  . GLY I  1 141 ? 3.869  -124.884 -81.133  1.00 56.41  ? 142 GLY I CA  1 
ATOM   9905  C  C   . GLY I  1 141 ? 3.999  -123.858 -80.026  1.00 54.53  ? 142 GLY I C   1 
ATOM   9906  O  O   . GLY I  1 141 ? 5.113  -123.491 -79.628  1.00 52.70  ? 142 GLY I O   1 
ATOM   9907  N  N   . SER I  1 142 ? 2.844  -123.408 -79.525  1.00 55.34  ? 143 SER I N   1 
ATOM   9908  C  CA  . SER I  1 142 ? 2.761  -122.248 -78.621  1.00 54.23  ? 143 SER I CA  1 
ATOM   9909  C  C   . SER I  1 142 ? 3.435  -122.514 -77.276  1.00 52.23  ? 143 SER I C   1 
ATOM   9910  O  O   . SER I  1 142 ? 3.836  -123.660 -76.964  1.00 51.90  ? 143 SER I O   1 
ATOM   9911  C  CB  . SER I  1 142 ? 1.309  -121.826 -78.389  1.00 56.19  ? 143 SER I CB  1 
ATOM   9912  O  OG  . SER I  1 142 ? 0.657  -122.707 -77.506  1.00 56.74  ? 143 SER I OG  1 
ATOM   9913  N  N   . ARG I  1 143 ? 3.562  -121.444 -76.490  1.00 51.18  ? 144 ARG I N   1 
ATOM   9914  C  CA  . ARG I  1 143 ? 4.257  -121.496 -75.203  1.00 49.33  ? 144 ARG I CA  1 
ATOM   9915  C  C   . ARG I  1 143 ? 3.266  -121.563 -74.065  1.00 50.21  ? 144 ARG I C   1 
ATOM   9916  O  O   . ARG I  1 143 ? 2.646  -120.559 -73.736  1.00 51.16  ? 144 ARG I O   1 
ATOM   9917  C  CB  . ARG I  1 143 ? 5.170  -120.286 -75.053  1.00 47.97  ? 144 ARG I CB  1 
ATOM   9918  C  CG  . ARG I  1 143 ? 6.250  -120.253 -76.123  1.00 47.56  ? 144 ARG I CG  1 
ATOM   9919  C  CD  . ARG I  1 143 ? 7.052  -118.975 -76.101  1.00 47.08  ? 144 ARG I CD  1 
ATOM   9920  N  NE  . ARG I  1 143 ? 7.938  -118.881 -77.256  1.00 47.22  ? 144 ARG I NE  1 
ATOM   9921  C  CZ  . ARG I  1 143 ? 8.817  -117.908 -77.446  1.00 47.26  ? 144 ARG I CZ  1 
ATOM   9922  N  NH1 . ARG I  1 143 ? 8.946  -116.920 -76.562  1.00 46.90  ? 144 ARG I NH1 1 
ATOM   9923  N  NH2 . ARG I  1 143 ? 9.576  -117.929 -78.525  1.00 48.49  ? 144 ARG I NH2 1 
ATOM   9924  N  N   . LEU I  1 144 ? 3.137  -122.747 -73.469  1.00 50.45  ? 145 LEU I N   1 
ATOM   9925  C  CA  . LEU I  1 144 ? 2.121  -123.005 -72.450  1.00 52.12  ? 145 LEU I CA  1 
ATOM   9926  C  C   . LEU I  1 144 ? 2.475  -122.397 -71.110  1.00 51.28  ? 145 LEU I C   1 
ATOM   9927  O  O   . LEU I  1 144 ? 1.671  -121.697 -70.495  1.00 52.76  ? 145 LEU I O   1 
ATOM   9928  C  CB  . LEU I  1 144 ? 1.919  -124.509 -72.259  1.00 53.32  ? 145 LEU I CB  1 
ATOM   9929  C  CG  . LEU I  1 144 ? 1.276  -125.265 -73.418  1.00 55.10  ? 145 LEU I CG  1 
ATOM   9930  C  CD1 . LEU I  1 144 ? 0.978  -126.720 -73.018  1.00 56.68  ? 145 LEU I CD1 1 
ATOM   9931  C  CD2 . LEU I  1 144 ? 0.009  -124.542 -73.881  1.00 57.06  ? 145 LEU I CD2 1 
ATOM   9932  N  N   . ALA I  1 145 ? 3.682  -122.696 -70.653  1.00 49.47  ? 146 ALA I N   1 
ATOM   9933  C  CA  . ALA I  1 145 ? 4.175  -122.212 -69.355  1.00 48.88  ? 146 ALA I CA  1 
ATOM   9934  C  C   . ALA I  1 145 ? 5.693  -121.989 -69.386  1.00 46.56  ? 146 ALA I C   1 
ATOM   9935  O  O   . ALA I  1 145 ? 6.417  -122.727 -70.046  1.00 46.02  ? 146 ALA I O   1 
ATOM   9936  C  CB  . ALA I  1 145 ? 3.805  -123.192 -68.247  1.00 50.30  ? 146 ALA I CB  1 
ATOM   9937  N  N   . CYS I  1 146 ? 6.162  -120.973 -68.672  1.00 45.68  ? 147 CYS I N   1 
ATOM   9938  C  CA  . CYS I  1 146 ? 7.566  -120.636 -68.677  1.00 43.81  ? 147 CYS I CA  1 
ATOM   9939  C  C   . CYS I  1 146 ? 7.985  -119.967 -67.390  1.00 43.79  ? 147 CYS I C   1 
ATOM   9940  O  O   . CYS I  1 146 ? 7.177  -119.615 -66.553  1.00 45.15  ? 147 CYS I O   1 
ATOM   9941  C  CB  . CYS I  1 146 ? 7.880  -119.731 -69.857  1.00 43.15  ? 147 CYS I CB  1 
ATOM   9942  S  SG  . CYS I  1 146 ? 7.076  -118.131 -69.797  1.00 43.94  ? 147 CYS I SG  1 
ATOM   9943  N  N   . GLY I  1 147 ? 9.283  -119.811 -67.235  1.00 42.76  ? 148 GLY I N   1 
ATOM   9944  C  CA  . GLY I  1 147 ? 9.844  -119.145 -66.061  1.00 42.81  ? 148 GLY I CA  1 
ATOM   9945  C  C   . GLY I  1 147 ? 11.315 -118.807 -66.248  1.00 41.58  ? 148 GLY I C   1 
ATOM   9946  O  O   . GLY I  1 147 ? 12.009 -119.463 -67.017  1.00 41.00  ? 148 GLY I O   1 
ATOM   9947  N  N   . VAL I  1 148 ? 11.788 -117.784 -65.544  1.00 41.55  ? 149 VAL I N   1 
ATOM   9948  C  CA  . VAL I  1 148 ? 13.198 -117.396 -65.598  1.00 40.71  ? 149 VAL I CA  1 
ATOM   9949  C  C   . VAL I  1 148 ? 14.047 -118.292 -64.706  1.00 40.81  ? 149 VAL I C   1 
ATOM   9950  O  O   . VAL I  1 148 ? 13.678 -118.574 -63.572  1.00 41.61  ? 149 VAL I O   1 
ATOM   9951  C  CB  . VAL I  1 148 ? 13.391 -115.948 -65.176  1.00 41.00  ? 149 VAL I CB  1 
ATOM   9952  C  CG1 . VAL I  1 148 ? 14.817 -115.579 -65.240  1.00 40.68  ? 149 VAL I CG1 1 
ATOM   9953  C  CG2 . VAL I  1 148 ? 12.615 -115.046 -66.077  1.00 41.51  ? 149 VAL I CG2 1 
ATOM   9954  N  N   . ILE I  1 149 ? 15.182 -118.738 -65.237  1.00 40.48  ? 150 ILE I N   1 
ATOM   9955  C  CA  . ILE I  1 149 ? 16.068 -119.677 -64.545  1.00 41.05  ? 150 ILE I CA  1 
ATOM   9956  C  C   . ILE I  1 149 ? 16.905 -118.926 -63.541  1.00 41.42  ? 150 ILE I C   1 
ATOM   9957  O  O   . ILE I  1 149 ? 17.611 -118.007 -63.896  1.00 41.21  ? 150 ILE I O   1 
ATOM   9958  C  CB  . ILE I  1 149 ? 17.025 -120.419 -65.524  1.00 41.12  ? 150 ILE I CB  1 
ATOM   9959  C  CG1 . ILE I  1 149 ? 16.253 -121.404 -66.400  1.00 41.03  ? 150 ILE I CG1 1 
ATOM   9960  C  CG2 . ILE I  1 149 ? 18.106 -121.166 -64.766  1.00 42.12  ? 150 ILE I CG2 1 
ATOM   9961  C  CD1 . ILE I  1 149 ? 17.074 -121.981 -67.495  1.00 41.29  ? 150 ILE I CD1 1 
ATOM   9962  N  N   . GLY I  1 150 ? 16.854 -119.355 -62.292  1.00 42.45  ? 151 GLY I N   1 
ATOM   9963  C  CA  . GLY I  1 150 ? 17.492 -118.625 -61.202  1.00 43.36  ? 151 GLY I CA  1 
ATOM   9964  C  C   . GLY I  1 150 ? 18.487 -119.429 -60.380  1.00 44.63  ? 151 GLY I C   1 
ATOM   9965  O  O   . GLY I  1 150 ? 18.414 -120.649 -60.309  1.00 45.35  ? 151 GLY I O   1 
ATOM   9966  N  N   . ILE I  1 151 ? 19.411 -118.725 -59.742  1.00 45.28  ? 152 ILE I N   1 
ATOM   9967  C  CA  . ILE I  1 151 ? 20.426 -119.353 -58.915  1.00 46.88  ? 152 ILE I CA  1 
ATOM   9968  C  C   . ILE I  1 151 ? 19.763 -119.879 -57.668  1.00 48.38  ? 152 ILE I C   1 
ATOM   9969  O  O   . ILE I  1 151 ? 19.021 -119.173 -57.035  1.00 48.83  ? 152 ILE I O   1 
ATOM   9970  C  CB  . ILE I  1 151 ? 21.542 -118.364 -58.513  1.00 47.62  ? 152 ILE I CB  1 
ATOM   9971  C  CG1 . ILE I  1 151 ? 22.275 -117.854 -59.744  1.00 46.79  ? 152 ILE I CG1 1 
ATOM   9972  C  CG2 . ILE I  1 151 ? 22.551 -119.013 -57.599  1.00 49.65  ? 152 ILE I CG2 1 
ATOM   9973  C  CD1 . ILE I  1 151 ? 23.393 -116.908 -59.405  1.00 47.93  ? 152 ILE I CD1 1 
ATOM   9974  N  N   . ALA I  1 152 ? 20.059 -121.117 -57.310  1.00 49.97  ? 153 ALA I N   1 
ATOM   9975  C  CA  . ALA I  1 152 ? 19.428 -121.792 -56.174  1.00 52.03  ? 153 ALA I CA  1 
ATOM   9976  C  C   . ALA I  1 152 ? 20.421 -122.137 -55.084  1.00 54.65  ? 153 ALA I C   1 
ATOM   9977  O  O   . ALA I  1 152 ? 21.623 -122.187 -55.323  1.00 54.85  ? 153 ALA I O   1 
ATOM   9978  C  CB  . ALA I  1 152 ? 18.761 -123.044 -56.644  1.00 52.42  ? 153 ALA I CB  1 
ATOM   9979  N  N   . GLN I  1 153 ? 19.907 -122.385 -53.886  1.00 57.03  ? 154 GLN I N   1 
ATOM   9980  C  CA  . GLN I  1 153 ? 20.769 -122.710 -52.744  1.00 60.39  ? 154 GLN I CA  1 
ATOM   9981  C  C   . GLN I  1 153 ? 21.242 -124.152 -52.844  1.00 62.33  ? 154 GLN I C   1 
ATOM   9982  O  O   . GLN I  1 153 ? 20.449 -125.033 -53.175  1.00 62.48  ? 154 GLN I O   1 
ATOM   9983  C  CB  . GLN I  1 153 ? 20.067 -122.510 -51.391  1.00 63.00  ? 154 GLN I CB  1 
ATOM   9984  C  CG  . GLN I  1 153 ? 20.990 -122.772 -50.167  1.00 66.60  ? 154 GLN I CG  1 
ATOM   9985  C  CD  . GLN I  1 153 ? 20.354 -122.450 -48.823  1.00 69.58  ? 154 GLN I CD  1 
ATOM   9986  O  OE1 . GLN I  1 153 ? 20.079 -121.304 -48.526  1.00 69.12  ? 154 GLN I OE1 1 
ATOM   9987  N  NE2 . GLN I  1 153 ? 20.145 -123.467 -47.996  1.00 73.05  ? 154 GLN I NE2 1 
ATOM   9988  O  OXT . GLN I  1 153 ? 22.413 -124.469 -52.577  1.00 64.21  ? 154 GLN I OXT 1 
ATOM   9989  N  N   . ALA J  1 1   ? 26.895 -102.450 -72.728  1.00 69.72  ? 2   ALA J N   1 
ATOM   9990  C  CA  . ALA J  1 1   ? 26.361 -103.413 -73.748  1.00 69.97  ? 2   ALA J CA  1 
ATOM   9991  C  C   . ALA J  1 1   ? 25.615 -104.626 -73.109  1.00 65.39  ? 2   ALA J C   1 
ATOM   9992  O  O   . ALA J  1 1   ? 25.261 -105.587 -73.807  1.00 66.27  ? 2   ALA J O   1 
ATOM   9993  C  CB  . ALA J  1 1   ? 27.501 -103.884 -74.719  1.00 74.30  ? 2   ALA J CB  1 
ATOM   9994  N  N   . THR J  1 2   ? 25.415 -104.593 -71.790  1.00 60.97  ? 3   THR J N   1 
ATOM   9995  C  CA  . THR J  1 2   ? 24.524 -105.550 -71.109  1.00 56.73  ? 3   THR J CA  1 
ATOM   9996  C  C   . THR J  1 2   ? 23.240 -104.907 -70.586  1.00 53.75  ? 3   THR J C   1 
ATOM   9997  O  O   . THR J  1 2   ? 23.251 -103.796 -70.060  1.00 53.52  ? 3   THR J O   1 
ATOM   9998  C  CB  . THR J  1 2   ? 25.223 -106.270 -69.913  1.00 55.26  ? 3   THR J CB  1 
ATOM   9999  O  OG1 . THR J  1 2   ? 26.644 -106.208 -70.060  1.00 58.69  ? 3   THR J OG1 1 
ATOM   10000 C  CG2 . THR J  1 2   ? 24.778 -107.749 -69.807  1.00 53.33  ? 3   THR J CG2 1 
ATOM   10001 N  N   . LYS J  1 3   ? 22.137 -105.633 -70.733  1.00 51.87  ? 4   LYS J N   1 
ATOM   10002 C  CA  . LYS J  1 3   ? 20.836 -105.221 -70.210  1.00 49.36  ? 4   LYS J CA  1 
ATOM   10003 C  C   . LYS J  1 3   ? 20.195 -106.387 -69.472  1.00 46.60  ? 4   LYS J C   1 
ATOM   10004 O  O   . LYS J  1 3   ? 20.437 -107.541 -69.813  1.00 47.18  ? 4   LYS J O   1 
ATOM   10005 C  CB  . LYS J  1 3   ? 19.906 -104.781 -71.338  1.00 50.95  ? 4   LYS J CB  1 
ATOM   10006 C  CG  . LYS J  1 3   ? 20.320 -103.498 -72.072  1.00 54.28  ? 4   LYS J CG  1 
ATOM   10007 C  CD  . LYS J  1 3   ? 19.205 -103.003 -73.016  1.00 55.79  ? 4   LYS J CD  1 
ATOM   10008 C  CE  . LYS J  1 3   ? 19.740 -102.177 -74.180  1.00 60.04  ? 4   LYS J CE  1 
ATOM   10009 N  NZ  . LYS J  1 3   ? 18.793 -102.202 -75.338  1.00 61.75  ? 4   LYS J NZ  1 
ATOM   10010 N  N   . ALA J  1 4   ? 19.394 -106.074 -68.457  1.00 44.06  ? 5   ALA J N   1 
ATOM   10011 C  CA  . ALA J  1 4   ? 18.615 -107.073 -67.746  1.00 41.86  ? 5   ALA J CA  1 
ATOM   10012 C  C   . ALA J  1 4   ? 17.241 -106.514 -67.497  1.00 40.65  ? 5   ALA J C   1 
ATOM   10013 O  O   . ALA J  1 4   ? 17.024 -105.340 -67.729  1.00 41.36  ? 5   ALA J O   1 
ATOM   10014 C  CB  . ALA J  1 4   ? 19.281 -107.438 -66.457  1.00 40.47  ? 5   ALA J CB  1 
ATOM   10015 N  N   . VAL J  1 5   ? 16.312 -107.365 -67.071  1.00 39.38  ? 6   VAL J N   1 
ATOM   10016 C  CA  . VAL J  1 5   ? 14.954 -106.942 -66.739  1.00 38.58  ? 6   VAL J CA  1 
ATOM   10017 C  C   . VAL J  1 5   ? 14.387 -107.856 -65.697  1.00 37.07  ? 6   VAL J C   1 
ATOM   10018 O  O   . VAL J  1 5   ? 14.846 -108.969 -65.567  1.00 37.17  ? 6   VAL J O   1 
ATOM   10019 C  CB  . VAL J  1 5   ? 14.036 -106.966 -67.966  1.00 40.38  ? 6   VAL J CB  1 
ATOM   10020 C  CG1 . VAL J  1 5   ? 13.623 -108.382 -68.287  1.00 41.24  ? 6   VAL J CG1 1 
ATOM   10021 C  CG2 . VAL J  1 5   ? 12.813 -106.111 -67.744  1.00 40.36  ? 6   VAL J CG2 1 
ATOM   10022 N  N   . CYS J  1 6   ? 13.384 -107.384 -64.964  1.00 36.34  ? 7   CYS J N   1 
ATOM   10023 C  CA  . CYS J  1 6   ? 12.714 -108.180 -63.923  1.00 35.54  ? 7   CYS J CA  1 
ATOM   10024 C  C   . CYS J  1 6   ? 11.261 -107.797 -63.711  1.00 35.88  ? 7   CYS J C   1 
ATOM   10025 O  O   . CYS J  1 6   ? 10.963 -106.636 -63.466  1.00 35.71  ? 7   CYS J O   1 
ATOM   10026 C  CB  . CYS J  1 6   ? 13.408 -108.014 -62.594  1.00 34.24  ? 7   CYS J CB  1 
ATOM   10027 S  SG  . CYS J  1 6   ? 12.491 -108.787 -61.257  1.00 33.24  ? 7   CYS J SG  1 
ATOM   10028 N  N   . VAL J  1 7   ? 10.373 -108.789 -63.784  1.00 36.82  ? 8   VAL J N   1 
ATOM   10029 C  CA  . VAL J  1 7   ? 8.931  -108.609 -63.537  1.00 37.57  ? 8   VAL J CA  1 
ATOM   10030 C  C   . VAL J  1 7   ? 8.558  -108.913 -62.088  1.00 36.88  ? 8   VAL J C   1 
ATOM   10031 O  O   . VAL J  1 7   ? 8.473  -110.071 -61.676  1.00 37.06  ? 8   VAL J O   1 
ATOM   10032 C  CB  . VAL J  1 7   ? 8.080  -109.487 -64.459  1.00 39.42  ? 8   VAL J CB  1 
ATOM   10033 C  CG1 . VAL J  1 7   ? 6.642  -109.439 -64.052  1.00 40.71  ? 8   VAL J CG1 1 
ATOM   10034 C  CG2 . VAL J  1 7   ? 8.237  -109.026 -65.887  1.00 40.60  ? 8   VAL J CG2 1 
ATOM   10035 N  N   . LEU J  1 8   ? 8.326  -107.847 -61.333  1.00 36.24  ? 9   LEU J N   1 
ATOM   10036 C  CA  . LEU J  1 8   ? 7.962  -107.946 -59.936  1.00 35.92  ? 9   LEU J CA  1 
ATOM   10037 C  C   . LEU J  1 8   ? 6.509  -108.369 -59.806  1.00 37.74  ? 9   LEU J C   1 
ATOM   10038 O  O   . LEU J  1 8   ? 5.641  -107.777 -60.416  1.00 39.10  ? 9   LEU J O   1 
ATOM   10039 C  CB  . LEU J  1 8   ? 8.182  -106.599 -59.248  1.00 35.07  ? 9   LEU J CB  1 
ATOM   10040 C  CG  . LEU J  1 8   ? 9.642  -106.194 -59.044  1.00 33.59  ? 9   LEU J CG  1 
ATOM   10041 C  CD1 . LEU J  1 8   ? 9.762  -104.723 -58.783  1.00 33.23  ? 9   LEU J CD1 1 
ATOM   10042 C  CD2 . LEU J  1 8   ? 10.266 -106.976 -57.895  1.00 33.03  ? 9   LEU J CD2 1 
ATOM   10043 N  N   . LYS J  1 9   ? 6.252  -109.407 -59.023  1.00 38.40  ? 10  LYS J N   1 
ATOM   10044 C  CA  . LYS J  1 9   ? 4.886  -109.895 -58.762  1.00 40.78  ? 10  LYS J CA  1 
ATOM   10045 C  C   . LYS J  1 9   ? 4.768  -110.482 -57.376  1.00 41.29  ? 10  LYS J C   1 
ATOM   10046 O  O   . LYS J  1 9   ? 5.759  -110.865 -56.790  1.00 40.33  ? 10  LYS J O   1 
ATOM   10047 C  CB  . LYS J  1 9   ? 4.486  -110.977 -59.760  1.00 42.60  ? 10  LYS J CB  1 
ATOM   10048 C  CG  . LYS J  1 9   ? 3.925  -110.449 -61.077  1.00 44.14  ? 10  LYS J CG  1 
ATOM   10049 C  CD  . LYS J  1 9   ? 2.992  -111.476 -61.739  1.00 47.30  ? 10  LYS J CD  1 
ATOM   10050 C  CE  . LYS J  1 9   ? 2.680  -111.155 -63.209  1.00 48.38  ? 10  LYS J CE  1 
ATOM   10051 N  NZ  . LYS J  1 9   ? 1.569  -110.156 -63.353  1.00 50.00  ? 10  LYS J NZ  1 
ATOM   10052 N  N   . GLY J  1 10  ? 3.550  -110.586 -56.863  1.00 43.52  ? 11  GLY J N   1 
ATOM   10053 C  CA  . GLY J  1 10  ? 3.346  -111.121 -55.519  1.00 44.67  ? 11  GLY J CA  1 
ATOM   10054 C  C   . GLY J  1 10  ? 1.940  -111.544 -55.187  1.00 48.08  ? 11  GLY J C   1 
ATOM   10055 O  O   . GLY J  1 10  ? 1.058  -111.522 -56.032  1.00 49.78  ? 11  GLY J O   1 
ATOM   10056 N  N   . ASP J  1 11  ? 1.743  -111.925 -53.933  1.00 49.52  ? 12  ASP J N   1 
ATOM   10057 C  CA  . ASP J  1 11  ? 0.442  -112.408 -53.444  1.00 53.48  ? 12  ASP J CA  1 
ATOM   10058 C  C   . ASP J  1 11  ? -0.659 -111.365 -53.469  1.00 54.89  ? 12  ASP J C   1 
ATOM   10059 O  O   . ASP J  1 11  ? -1.826 -111.699 -53.657  1.00 58.47  ? 12  ASP J O   1 
ATOM   10060 C  CB  . ASP J  1 11  ? 0.555  -112.948 -52.014  1.00 55.02  ? 12  ASP J CB  1 
ATOM   10061 C  CG  . ASP J  1 11  ? 0.872  -114.448 -51.972  1.00 57.20  ? 12  ASP J CG  1 
ATOM   10062 O  OD1 . ASP J  1 11  ? 0.181  -115.212 -52.709  1.00 59.96  ? 12  ASP J OD1 1 
ATOM   10063 O  OD2 . ASP J  1 11  ? 1.804  -114.859 -51.205  1.00 56.87  ? 12  ASP J OD2 1 
ATOM   10064 N  N   . GLY J  1 12  ? -0.288 -110.107 -53.275  1.00 52.67  ? 13  GLY J N   1 
ATOM   10065 C  CA  . GLY J  1 12  ? -1.244 -108.996 -53.240  1.00 53.90  ? 13  GLY J CA  1 
ATOM   10066 C  C   . GLY J  1 12  ? -1.134 -108.093 -54.443  1.00 52.34  ? 13  GLY J C   1 
ATOM   10067 O  O   . GLY J  1 12  ? -0.608 -108.498 -55.461  1.00 51.18  ? 13  GLY J O   1 
ATOM   10068 N  N   . PRO J  1 13  ? -1.608 -106.849 -54.330  1.00 52.83  ? 14  PRO J N   1 
ATOM   10069 C  CA  . PRO J  1 13  ? -1.825 -105.967 -55.475  1.00 52.93  ? 14  PRO J CA  1 
ATOM   10070 C  C   . PRO J  1 13  ? -0.572 -105.375 -56.052  1.00 49.55  ? 14  PRO J C   1 
ATOM   10071 O  O   . PRO J  1 13  ? -0.607 -104.818 -57.141  1.00 49.54  ? 14  PRO J O   1 
ATOM   10072 C  CB  . PRO J  1 13  ? -2.652 -104.852 -54.880  1.00 54.98  ? 14  PRO J CB  1 
ATOM   10073 C  CG  . PRO J  1 13  ? -2.200 -104.767 -53.481  1.00 53.78  ? 14  PRO J CG  1 
ATOM   10074 C  CD  . PRO J  1 13  ? -1.784 -106.134 -53.066  1.00 53.35  ? 14  PRO J CD  1 
ATOM   10075 N  N   . VAL J  1 14  ? 0.522  -105.487 -55.309  1.00 47.16  ? 15  VAL J N   1 
ATOM   10076 C  CA  . VAL J  1 14  ? 1.790  -104.903 -55.714  1.00 44.09  ? 15  VAL J CA  1 
ATOM   10077 C  C   . VAL J  1 14  ? 2.343  -105.632 -56.922  1.00 43.12  ? 15  VAL J C   1 
ATOM   10078 O  O   . VAL J  1 14  ? 2.475  -106.854 -56.925  1.00 43.25  ? 15  VAL J O   1 
ATOM   10079 C  CB  . VAL J  1 14  ? 2.811  -104.931 -54.599  1.00 42.10  ? 15  VAL J CB  1 
ATOM   10080 C  CG1 . VAL J  1 14  ? 4.044  -104.194 -55.055  1.00 39.77  ? 15  VAL J CG1 1 
ATOM   10081 C  CG2 . VAL J  1 14  ? 2.236  -104.297 -53.335  1.00 43.55  ? 15  VAL J CG2 1 
ATOM   10082 N  N   . GLN J  1 15  ? 2.622  -104.872 -57.965  1.00 42.55  ? 16  GLN J N   1 
ATOM   10083 C  CA  . GLN J  1 15  ? 3.237  -105.410 -59.159  1.00 41.93  ? 16  GLN J CA  1 
ATOM   10084 C  C   . GLN J  1 15  ? 3.950  -104.320 -59.954  1.00 41.01  ? 16  GLN J C   1 
ATOM   10085 O  O   . GLN J  1 15  ? 3.658  -103.142 -59.808  1.00 41.61  ? 16  GLN J O   1 
ATOM   10086 C  CB  . GLN J  1 15  ? 2.208  -106.143 -60.038  1.00 44.49  ? 16  GLN J CB  1 
ATOM   10087 C  CG  . GLN J  1 15  ? 0.975  -105.346 -60.404  1.00 47.41  ? 16  GLN J CG  1 
ATOM   10088 C  CD  . GLN J  1 15  ? 0.106  -106.037 -61.461  1.00 50.33  ? 16  GLN J CD  1 
ATOM   10089 O  OE1 . GLN J  1 15  ? -0.635 -105.390 -62.185  1.00 52.83  ? 16  GLN J OE1 1 
ATOM   10090 N  NE2 . GLN J  1 15  ? 0.204  -107.346 -61.547  1.00 50.36  ? 16  GLN J NE2 1 
ATOM   10091 N  N   . GLY J  1 16  ? 4.883  -104.739 -60.803  1.00 40.04  ? 17  GLY J N   1 
ATOM   10092 C  CA  . GLY J  1 16  ? 5.691  -103.822 -61.595  1.00 39.56  ? 17  GLY J CA  1 
ATOM   10093 C  C   . GLY J  1 16  ? 6.760  -104.468 -62.467  1.00 38.70  ? 17  GLY J C   1 
ATOM   10094 O  O   . GLY J  1 16  ? 6.979  -105.672 -62.428  1.00 38.19  ? 17  GLY J O   1 
ATOM   10095 N  N   . ILE J  1 17  ? 7.425  -103.630 -63.249  1.00 38.87  ? 18  ILE J N   1 
ATOM   10096 C  CA  . ILE J  1 17  ? 8.509  -104.030 -64.135  1.00 38.56  ? 18  ILE J CA  1 
ATOM   10097 C  C   . ILE J  1 17  ? 9.708  -103.156 -63.866  1.00 37.74  ? 18  ILE J C   1 
ATOM   10098 O  O   . ILE J  1 17  ? 9.561  -101.948 -63.841  1.00 38.80  ? 18  ILE J O   1 
ATOM   10099 C  CB  . ILE J  1 17  ? 8.134  -103.790 -65.584  1.00 40.85  ? 18  ILE J CB  1 
ATOM   10100 C  CG1 . ILE J  1 17  ? 7.299  -104.937 -66.126  1.00 42.15  ? 18  ILE J CG1 1 
ATOM   10101 C  CG2 . ILE J  1 17  ? 9.377  -103.620 -66.436  1.00 41.09  ? 18  ILE J CG2 1 
ATOM   10102 C  CD1 . ILE J  1 17  ? 7.145  -104.902 -67.642  1.00 44.54  ? 18  ILE J CD1 1 
ATOM   10103 N  N   . ILE J  1 18  ? 10.884 -103.748 -63.671  1.00 36.51  ? 19  ILE J N   1 
ATOM   10104 C  CA  . ILE J  1 18  ? 12.113 -102.980 -63.418  1.00 36.15  ? 19  ILE J CA  1 
ATOM   10105 C  C   . ILE J  1 18  ? 13.192 -103.370 -64.409  1.00 36.92  ? 19  ILE J C   1 
ATOM   10106 O  O   . ILE J  1 18  ? 13.455 -104.551 -64.591  1.00 36.66  ? 19  ILE J O   1 
ATOM   10107 C  CB  . ILE J  1 18  ? 12.665 -103.209 -62.004  1.00 34.43  ? 19  ILE J CB  1 
ATOM   10108 C  CG1 . ILE J  1 18  ? 11.753 -102.588 -60.951  1.00 34.28  ? 19  ILE J CG1 1 
ATOM   10109 C  CG2 . ILE J  1 18  ? 14.025 -102.612 -61.863  1.00 34.66  ? 19  ILE J CG2 1 
ATOM   10110 C  CD1 . ILE J  1 18  ? 11.680 -101.074 -60.977  1.00 35.51  ? 19  ILE J CD1 1 
ATOM   10111 N  N   . ASN J  1 19  ? 13.811 -102.366 -65.034  1.00 38.35  ? 20  ASN J N   1 
ATOM   10112 C  CA  . ASN J  1 19  ? 14.893 -102.563 -66.001  1.00 39.67  ? 20  ASN J CA  1 
ATOM   10113 C  C   . ASN J  1 19  ? 16.280 -102.318 -65.417  1.00 39.52  ? 20  ASN J C   1 
ATOM   10114 O  O   . ASN J  1 19  ? 16.445 -101.533 -64.504  1.00 39.18  ? 20  ASN J O   1 
ATOM   10115 C  CB  . ASN J  1 19  ? 14.718 -101.637 -67.196  1.00 42.23  ? 20  ASN J CB  1 
ATOM   10116 C  CG  . ASN J  1 19  ? 13.473 -101.910 -67.944  1.00 43.23  ? 20  ASN J CG  1 
ATOM   10117 O  OD1 . ASN J  1 19  ? 12.520 -101.155 -67.844  1.00 44.24  ? 20  ASN J OD1 1 
ATOM   10118 N  ND2 . ASN J  1 19  ? 13.449 -103.001 -68.693  1.00 43.57  ? 20  ASN J ND2 1 
ATOM   10119 N  N   . PHE J  1 20  ? 17.275 -102.998 -65.979  1.00 40.39  ? 21  PHE J N   1 
ATOM   10120 C  CA  . PHE J  1 20  ? 18.684 -102.786 -65.660  1.00 40.95  ? 21  PHE J CA  1 
ATOM   10121 C  C   . PHE J  1 20  ? 19.480 -102.543 -66.935  1.00 43.84  ? 21  PHE J C   1 
ATOM   10122 O  O   . PHE J  1 20  ? 19.184 -103.127 -67.981  1.00 44.91  ? 21  PHE J O   1 
ATOM   10123 C  CB  . PHE J  1 20  ? 19.263 -104.003 -64.970  1.00 39.69  ? 21  PHE J CB  1 
ATOM   10124 C  CG  . PHE J  1 20  ? 18.606 -104.332 -63.665  1.00 37.34  ? 21  PHE J CG  1 
ATOM   10125 C  CD1 . PHE J  1 20  ? 17.427 -105.021 -63.635  1.00 36.40  ? 21  PHE J CD1 1 
ATOM   10126 C  CD2 . PHE J  1 20  ? 19.182 -103.971 -62.468  1.00 36.66  ? 21  PHE J CD2 1 
ATOM   10127 C  CE1 . PHE J  1 20  ? 16.826 -105.333 -62.439  1.00 34.73  ? 21  PHE J CE1 1 
ATOM   10128 C  CE2 . PHE J  1 20  ? 18.590 -104.285 -61.278  1.00 34.80  ? 21  PHE J CE2 1 
ATOM   10129 C  CZ  . PHE J  1 20  ? 17.410 -104.961 -61.264  1.00 34.04  ? 21  PHE J CZ  1 
ATOM   10130 N  N   . GLU J  1 21  ? 20.491 -101.683 -66.846  1.00 45.61  ? 22  GLU J N   1 
ATOM   10131 C  CA  . GLU J  1 21  ? 21.371 -101.395 -67.989  1.00 48.94  ? 22  GLU J CA  1 
ATOM   10132 C  C   . GLU J  1 21  ? 22.765 -100.979 -67.546  1.00 50.49  ? 22  GLU J C   1 
ATOM   10133 O  O   . GLU J  1 21  ? 22.964 -99.918  -66.986  1.00 51.09  ? 22  GLU J O   1 
ATOM   10134 C  CB  . GLU J  1 21  ? 20.779 -100.320 -68.905  1.00 51.22  ? 22  GLU J CB  1 
ATOM   10135 C  CG  . GLU J  1 21  ? 21.650 -100.042 -70.117  1.00 55.55  ? 22  GLU J CG  1 
ATOM   10136 C  CD  . GLU J  1 21  ? 20.989 -99.196  -71.179  1.00 58.70  ? 22  GLU J CD  1 
ATOM   10137 O  OE1 . GLU J  1 21  ? 20.041 -98.446  -70.859  1.00 58.30  ? 22  GLU J OE1 1 
ATOM   10138 O  OE2 . GLU J  1 21  ? 21.444 -99.274  -72.343  1.00 61.93  ? 22  GLU J OE2 1 
ATOM   10139 N  N   . GLN J  1 22  ? 23.724 -101.839 -67.824  1.00 51.61  ? 23  GLN J N   1 
ATOM   10140 C  CA  . GLN J  1 22  ? 25.120 -101.577 -67.546  1.00 54.01  ? 23  GLN J CA  1 
ATOM   10141 C  C   . GLN J  1 22  ? 25.841 -101.380 -68.878  1.00 58.22  ? 23  GLN J C   1 
ATOM   10142 O  O   . GLN J  1 22  ? 26.031 -102.322 -69.638  1.00 59.04  ? 23  GLN J O   1 
ATOM   10143 C  CB  . GLN J  1 22  ? 25.729 -102.746 -66.775  1.00 52.78  ? 23  GLN J CB  1 
ATOM   10144 C  CG  . GLN J  1 22  ? 27.139 -102.512 -66.243  1.00 55.02  ? 23  GLN J CG  1 
ATOM   10145 C  CD  . GLN J  1 22  ? 27.681 -103.703 -65.458  1.00 54.13  ? 23  GLN J CD  1 
ATOM   10146 O  OE1 . GLN J  1 22  ? 27.544 -104.861 -65.871  1.00 53.82  ? 23  GLN J OE1 1 
ATOM   10147 N  NE2 . GLN J  1 22  ? 28.312 -103.417 -64.319  1.00 54.27  ? 23  GLN J NE2 1 
ATOM   10148 N  N   . LYS J  1 23  ? 26.237 -100.145 -69.162  1.00 61.28  ? 24  LYS J N   1 
ATOM   10149 C  CA  . LYS J  1 23  ? 26.866 -99.836  -70.431  1.00 65.76  ? 24  LYS J CA  1 
ATOM   10150 C  C   . LYS J  1 23  ? 28.222 -100.474 -70.535  1.00 68.20  ? 24  LYS J C   1 
ATOM   10151 O  O   . LYS J  1 23  ? 28.594 -100.906 -71.604  1.00 71.09  ? 24  LYS J O   1 
ATOM   10152 C  CB  . LYS J  1 23  ? 26.999 -98.331  -70.636  1.00 69.09  ? 24  LYS J CB  1 
ATOM   10153 C  CG  . LYS J  1 23  ? 25.644 -97.591  -70.781  1.00 68.14  ? 24  LYS J CG  1 
ATOM   10154 C  CD  . LYS J  1 23  ? 25.772 -96.314  -71.642  1.00 73.15  ? 24  LYS J CD  1 
ATOM   10155 C  CE  . LYS J  1 23  ? 24.694 -95.287  -71.304  1.00 72.27  ? 24  LYS J CE  1 
ATOM   10156 N  NZ  . LYS J  1 23  ? 24.968 -93.948  -71.918  1.00 77.31  ? 24  LYS J NZ  1 
ATOM   10157 N  N   . GLU J  1 24  ? 28.965 -100.522 -69.438  1.00 67.65  ? 25  GLU J N   1 
ATOM   10158 C  CA  . GLU J  1 24  ? 30.340 -101.051 -69.478  1.00 70.87  ? 25  GLU J CA  1 
ATOM   10159 C  C   . GLU J  1 24  ? 30.632 -101.960 -68.318  1.00 68.33  ? 25  GLU J C   1 
ATOM   10160 O  O   . GLU J  1 24  ? 30.287 -101.632 -67.189  1.00 65.97  ? 25  GLU J O   1 
ATOM   10161 C  CB  . GLU J  1 24  ? 31.346 -99.908  -69.479  1.00 75.40  ? 25  GLU J CB  1 
ATOM   10162 C  CG  . GLU J  1 24  ? 31.079 -98.943  -70.619  1.00 79.02  ? 25  GLU J CG  1 
ATOM   10163 C  CD  . GLU J  1 24  ? 32.217 -97.961  -70.859  1.00 85.38  ? 25  GLU J CD  1 
ATOM   10164 O  OE1 . GLU J  1 24  ? 32.704 -97.355  -69.864  1.00 85.94  ? 25  GLU J OE1 1 
ATOM   10165 O  OE2 . GLU J  1 24  ? 32.601 -97.793  -72.051  1.00 89.99  ? 25  GLU J OE2 1 
ATOM   10166 N  N   . SER J  1 25  ? 31.294 -103.079 -68.595  1.00 69.49  ? 26  SER J N   1 
ATOM   10167 C  CA  . SER J  1 25  ? 31.502 -104.167 -67.611  1.00 67.53  ? 26  SER J CA  1 
ATOM   10168 C  C   . SER J  1 25  ? 32.040 -103.714 -66.243  1.00 67.21  ? 26  SER J C   1 
ATOM   10169 O  O   . SER J  1 25  ? 31.696 -104.247 -65.198  1.00 64.28  ? 26  SER J O   1 
ATOM   10170 C  CB  . SER J  1 25  ? 32.452 -105.203 -68.208  1.00 70.84  ? 26  SER J CB  1 
ATOM   10171 O  OG  . SER J  1 25  ? 33.525 -104.563 -68.874  1.00 76.45  ? 26  SER J OG  1 
ATOM   10172 N  N   . ASN J  1 26  ? 32.901 -102.720 -66.272  1.00 70.89  ? 27  ASN J N   1 
ATOM   10173 C  CA  . ASN J  1 26  ? 33.494 -102.165 -65.065  1.00 71.54  ? 27  ASN J CA  1 
ATOM   10174 C  C   . ASN J  1 26  ? 32.656 -101.026 -64.451  1.00 69.17  ? 27  ASN J C   1 
ATOM   10175 O  O   . ASN J  1 26  ? 33.006 -100.501 -63.396  1.00 69.56  ? 27  ASN J O   1 
ATOM   10176 C  CB  . ASN J  1 26  ? 34.941 -101.685 -65.383  1.00 77.48  ? 27  ASN J CB  1 
ATOM   10177 C  CG  . ASN J  1 26  ? 35.004 -100.458 -66.374  1.00 80.88  ? 27  ASN J CG  1 
ATOM   10178 O  OD1 . ASN J  1 26  ? 34.305 -100.396 -67.414  1.00 80.17  ? 27  ASN J OD1 1 
ATOM   10179 N  ND2 . ASN J  1 26  ? 35.867 -99.492  -66.040  1.00 84.56  ? 27  ASN J ND2 1 
ATOM   10180 N  N   . GLY J  1 27  ? 31.555 -100.660 -65.106  1.00 67.14  ? 28  GLY J N   1 
ATOM   10181 C  CA  . GLY J  1 27  ? 30.846 -99.397  -64.839  1.00 66.26  ? 28  GLY J CA  1 
ATOM   10182 C  C   . GLY J  1 27  ? 29.562 -99.548  -64.043  1.00 61.31  ? 28  GLY J C   1 
ATOM   10183 O  O   . GLY J  1 27  ? 29.203 -100.668 -63.642  1.00 58.45  ? 28  GLY J O   1 
ATOM   10184 N  N   . PRO J  1 28  ? 28.857 -98.415  -63.818  1.00 60.60  ? 29  PRO J N   1 
ATOM   10185 C  CA  . PRO J  1 28  ? 27.676 -98.426  -62.983  1.00 56.51  ? 29  PRO J CA  1 
ATOM   10186 C  C   . PRO J  1 28  ? 26.470 -98.980  -63.724  1.00 54.02  ? 29  PRO J C   1 
ATOM   10187 O  O   . PRO J  1 28  ? 26.456 -99.013  -64.960  1.00 55.77  ? 29  PRO J O   1 
ATOM   10188 C  CB  . PRO J  1 28  ? 27.477 -96.949  -62.657  1.00 57.80  ? 29  PRO J CB  1 
ATOM   10189 C  CG  . PRO J  1 28  ? 27.935 -96.259  -63.875  1.00 61.78  ? 29  PRO J CG  1 
ATOM   10190 C  CD  . PRO J  1 28  ? 29.068 -97.084  -64.423  1.00 64.12  ? 29  PRO J CD  1 
ATOM   10191 N  N   . VAL J  1 29  ? 25.477 -99.404  -62.948  1.00 50.31  ? 30  VAL J N   1 
ATOM   10192 C  CA  . VAL J  1 29  ? 24.245 -99.984  -63.465  1.00 47.88  ? 30  VAL J CA  1 
ATOM   10193 C  C   . VAL J  1 29  ? 23.078 -99.045  -63.240  1.00 46.71  ? 30  VAL J C   1 
ATOM   10194 O  O   . VAL J  1 29  ? 22.750 -98.747  -62.113  1.00 45.26  ? 30  VAL J O   1 
ATOM   10195 C  CB  . VAL J  1 29  ? 23.916 -101.291 -62.723  1.00 45.07  ? 30  VAL J CB  1 
ATOM   10196 C  CG1 . VAL J  1 29  ? 22.592 -101.851 -63.198  1.00 42.93  ? 30  VAL J CG1 1 
ATOM   10197 C  CG2 . VAL J  1 29  ? 25.052 -102.291 -62.883  1.00 46.43  ? 30  VAL J CG2 1 
ATOM   10198 N  N   . LYS J  1 30  ? 22.451 -98.581  -64.310  1.00 47.83  ? 31  LYS J N   1 
ATOM   10199 C  CA  . LYS J  1 30  ? 21.209 -97.816  -64.190  1.00 47.03  ? 31  LYS J CA  1 
ATOM   10200 C  C   . LYS J  1 30  ? 20.039 -98.749  -63.960  1.00 43.92  ? 31  LYS J C   1 
ATOM   10201 O  O   . LYS J  1 30  ? 19.877 -99.728  -64.665  1.00 43.64  ? 31  LYS J O   1 
ATOM   10202 C  CB  . LYS J  1 30  ? 20.945 -96.965  -65.425  1.00 49.94  ? 31  LYS J CB  1 
ATOM   10203 C  CG  . LYS J  1 30  ? 21.901 -95.806  -65.528  1.00 53.94  ? 31  LYS J CG  1 
ATOM   10204 C  CD  . LYS J  1 30  ? 21.443 -94.745  -66.533  1.00 57.65  ? 31  LYS J CD  1 
ATOM   10205 C  CE  . LYS J  1 30  ? 22.446 -93.566  -66.586  1.00 61.74  ? 31  LYS J CE  1 
ATOM   10206 N  NZ  . LYS J  1 30  ? 21.984 -92.439  -67.443  1.00 65.42  ? 31  LYS J NZ  1 
ATOM   10207 N  N   . VAL J  1 31  ? 19.226 -98.431  -62.964  1.00 42.12  ? 32  VAL J N   1 
ATOM   10208 C  CA  . VAL J  1 31  ? 18.059 -99.227  -62.626  1.00 39.77  ? 32  VAL J CA  1 
ATOM   10209 C  C   . VAL J  1 31  ? 16.849 -98.346  -62.757  1.00 40.26  ? 32  VAL J C   1 
ATOM   10210 O  O   . VAL J  1 31  ? 16.793 -97.314  -62.128  1.00 41.09  ? 32  VAL J O   1 
ATOM   10211 C  CB  . VAL J  1 31  ? 18.129 -99.738  -61.191  1.00 37.63  ? 32  VAL J CB  1 
ATOM   10212 C  CG1 . VAL J  1 31  ? 16.966 -100.655 -60.880  1.00 35.52  ? 32  VAL J CG1 1 
ATOM   10213 C  CG2 . VAL J  1 31  ? 19.424 -100.457 -60.988  1.00 38.13  ? 32  VAL J CG2 1 
ATOM   10214 N  N   . TRP J  1 32  ? 15.894 -98.726  -63.592  1.00 40.44  ? 33  TRP J N   1 
ATOM   10215 C  CA  . TRP J  1 32  ? 14.688 -97.924  -63.757  1.00 41.44  ? 33  TRP J CA  1 
ATOM   10216 C  C   . TRP J  1 32  ? 13.454 -98.736  -64.126  1.00 40.79  ? 33  TRP J C   1 
ATOM   10217 O  O   . TRP J  1 32  ? 13.543 -99.828  -64.655  1.00 40.41  ? 33  TRP J O   1 
ATOM   10218 C  CB  . TRP J  1 32  ? 14.906 -96.812  -64.789  1.00 44.64  ? 33  TRP J CB  1 
ATOM   10219 C  CG  . TRP J  1 32  ? 14.630 -97.209  -66.202  1.00 46.37  ? 33  TRP J CG  1 
ATOM   10220 C  CD1 . TRP J  1 32  ? 13.498 -96.947  -66.923  1.00 48.13  ? 33  TRP J CD1 1 
ATOM   10221 C  CD2 . TRP J  1 32  ? 15.503 -97.922  -67.073  1.00 47.02  ? 33  TRP J CD2 1 
ATOM   10222 N  NE1 . TRP J  1 32  ? 13.614 -97.462  -68.187  1.00 49.43  ? 33  TRP J NE1 1 
ATOM   10223 C  CE2 . TRP J  1 32  ? 14.837 -98.069  -68.302  1.00 48.97  ? 33  TRP J CE2 1 
ATOM   10224 C  CE3 . TRP J  1 32  ? 16.781 -98.462  -66.932  1.00 46.83  ? 33  TRP J CE3 1 
ATOM   10225 C  CZ2 . TRP J  1 32  ? 15.411 -98.735  -69.385  1.00 50.72  ? 33  TRP J CZ2 1 
ATOM   10226 C  CZ3 . TRP J  1 32  ? 17.346 -99.125  -68.007  1.00 48.44  ? 33  TRP J CZ3 1 
ATOM   10227 C  CH2 . TRP J  1 32  ? 16.664 -99.255  -69.218  1.00 50.21  ? 33  TRP J CH2 1 
ATOM   10228 N  N   . GLY J  1 33  ? 12.294 -98.169  -63.843  1.00 41.22  ? 34  GLY J N   1 
ATOM   10229 C  CA  . GLY J  1 33  ? 11.031 -98.811  -64.140  1.00 41.14  ? 34  GLY J CA  1 
ATOM   10230 C  C   . GLY J  1 33  ? 9.909  -98.223  -63.327  1.00 41.35  ? 34  GLY J C   1 
ATOM   10231 O  O   . GLY J  1 33  ? 10.045 -97.142  -62.782  1.00 42.11  ? 34  GLY J O   1 
ATOM   10232 N  N   . SER J  1 34  ? 8.806  -98.953  -63.229  1.00 41.13  ? 35  SER J N   1 
ATOM   10233 C  CA  . SER J  1 34  ? 7.612  -98.479  -62.535  1.00 41.90  ? 35  SER J CA  1 
ATOM   10234 C  C   . SER J  1 34  ? 6.929  -99.581  -61.735  1.00 40.60  ? 35  SER J C   1 
ATOM   10235 O  O   . SER J  1 34  ? 6.506  -100.568 -62.296  1.00 40.89  ? 35  SER J O   1 
ATOM   10236 C  CB  . SER J  1 34  ? 6.637  -97.900  -63.555  1.00 44.86  ? 35  SER J CB  1 
ATOM   10237 O  OG  . SER J  1 34  ? 5.571  -97.234  -62.920  1.00 46.31  ? 35  SER J OG  1 
ATOM   10238 N  N   . ILE J  1 35  ? 6.844  -99.417  -60.420  1.00 39.68  ? 36  ILE J N   1 
ATOM   10239 C  CA  . ILE J  1 35  ? 6.111  -100.351 -59.555  1.00 39.18  ? 36  ILE J CA  1 
ATOM   10240 C  C   . ILE J  1 35  ? 4.842  -99.699  -59.106  1.00 41.15  ? 36  ILE J C   1 
ATOM   10241 O  O   . ILE J  1 35  ? 4.850  -98.514  -58.847  1.00 42.07  ? 36  ILE J O   1 
ATOM   10242 C  CB  . ILE J  1 35  ? 6.887  -100.712 -58.282  1.00 37.27  ? 36  ILE J CB  1 
ATOM   10243 C  CG1 . ILE J  1 35  ? 8.269  -101.237 -58.633  1.00 35.69  ? 36  ILE J CG1 1 
ATOM   10244 C  CG2 . ILE J  1 35  ? 6.118  -101.729 -57.447  1.00 36.95  ? 36  ILE J CG2 1 
ATOM   10245 C  CD1 . ILE J  1 35  ? 9.065  -101.531 -57.443  1.00 34.58  ? 36  ILE J CD1 1 
ATOM   10246 N  N   . LYS J  1 36  ? 3.767  -100.475 -58.994  1.00 42.31  ? 37  LYS J N   1 
ATOM   10247 C  CA  . LYS J  1 36  ? 2.455  -99.946  -58.584  1.00 44.84  ? 37  LYS J CA  1 
ATOM   10248 C  C   . LYS J  1 36  ? 1.713  -100.812 -57.581  1.00 45.16  ? 37  LYS J C   1 
ATOM   10249 O  O   . LYS J  1 36  ? 2.088  -101.947 -57.347  1.00 43.96  ? 37  LYS J O   1 
ATOM   10250 C  CB  . LYS J  1 36  ? 1.566  -99.672  -59.799  1.00 47.63  ? 37  LYS J CB  1 
ATOM   10251 C  CG  . LYS J  1 36  ? 1.272  -100.861 -60.675  1.00 48.23  ? 37  LYS J CG  1 
ATOM   10252 C  CD  . LYS J  1 36  ? 0.015  -100.599 -61.525  1.00 52.23  ? 37  LYS J CD  1 
ATOM   10253 C  CE  . LYS J  1 36  ? -0.242 -101.714 -62.545  1.00 53.08  ? 37  LYS J CE  1 
ATOM   10254 N  NZ  . LYS J  1 36  ? -1.564 -101.575 -63.193  1.00 56.76  ? 37  LYS J NZ  1 
ATOM   10255 N  N   . GLY J  1 37  ? 0.655  -100.260 -56.998  1.00 47.42  ? 38  GLY J N   1 
ATOM   10256 C  CA  . GLY J  1 37  ? -0.103 -100.937 -55.946  1.00 48.65  ? 38  GLY J CA  1 
ATOM   10257 C  C   . GLY J  1 37  ? 0.542  -100.790 -54.589  1.00 47.08  ? 38  GLY J C   1 
ATOM   10258 O  O   . GLY J  1 37  ? 0.268  -101.540 -53.660  1.00 47.43  ? 38  GLY J O   1 
ATOM   10259 N  N   . LEU J  1 38  ? 1.400  -99.795  -54.477  1.00 45.80  ? 39  LEU J N   1 
ATOM   10260 C  CA  . LEU J  1 38  ? 2.199  -99.597  -53.271  1.00 44.44  ? 39  LEU J CA  1 
ATOM   10261 C  C   . LEU J  1 38  ? 1.558  -98.603  -52.294  1.00 46.38  ? 39  LEU J C   1 
ATOM   10262 O  O   . LEU J  1 38  ? 0.971  -97.606  -52.698  1.00 48.06  ? 39  LEU J O   1 
ATOM   10263 C  CB  . LEU J  1 38  ? 3.621  -99.122  -53.635  1.00 42.19  ? 39  LEU J CB  1 
ATOM   10264 C  CG  . LEU J  1 38  ? 4.651  -100.190 -54.034  1.00 39.58  ? 39  LEU J CG  1 
ATOM   10265 C  CD1 . LEU J  1 38  ? 5.800  -99.598  -54.782  1.00 38.21  ? 39  LEU J CD1 1 
ATOM   10266 C  CD2 . LEU J  1 38  ? 5.142  -100.933 -52.810  1.00 38.67  ? 39  LEU J CD2 1 
ATOM   10267 N  N   . THR J  1 39  ? 1.700  -98.894  -51.005  1.00 46.24  ? 40  THR J N   1 
ATOM   10268 C  CA  . THR J  1 39  ? 1.235  -98.013  -49.947  1.00 48.12  ? 40  THR J CA  1 
ATOM   10269 C  C   . THR J  1 39  ? 2.069  -96.743  -50.011  1.00 47.41  ? 40  THR J C   1 
ATOM   10270 O  O   . THR J  1 39  ? 3.273  -96.821  -50.151  1.00 45.20  ? 40  THR J O   1 
ATOM   10271 C  CB  . THR J  1 39  ? 1.383  -98.652  -48.549  1.00 48.31  ? 40  THR J CB  1 
ATOM   10272 O  OG1 . THR J  1 39  ? 2.527  -98.107  -47.885  1.00 47.09  ? 40  THR J OG1 1 
ATOM   10273 C  CG2 . THR J  1 39  ? 1.525  -100.184 -48.619  1.00 47.41  ? 40  THR J CG2 1 
ATOM   10274 N  N   . GLU J  1 40  ? 1.442  -95.576  -49.911  1.00 49.94  ? 41  GLU J N   1 
ATOM   10275 C  CA  . GLU J  1 40  ? 2.145  -94.295  -50.126  1.00 49.91  ? 41  GLU J CA  1 
ATOM   10276 C  C   . GLU J  1 40  ? 3.331  -94.176  -49.205  1.00 48.14  ? 41  GLU J C   1 
ATOM   10277 O  O   . GLU J  1 40  ? 3.234  -94.472  -48.023  1.00 48.50  ? 41  GLU J O   1 
ATOM   10278 C  CB  . GLU J  1 40  ? 1.235  -93.081  -49.896  1.00 53.55  ? 41  GLU J CB  1 
ATOM   10279 C  CG  . GLU J  1 40  ? 1.966  -91.711  -50.049  1.00 54.42  ? 41  GLU J CG  1 
ATOM   10280 C  CD  . GLU J  1 40  ? 1.113  -90.470  -49.680  1.00 58.70  ? 41  GLU J CD  1 
ATOM   10281 O  OE1 . GLU J  1 40  ? 0.419  -90.474  -48.635  1.00 60.39  ? 41  GLU J OE1 1 
ATOM   10282 O  OE2 . GLU J  1 40  ? 1.153  -89.467  -50.425  1.00 60.14  ? 41  GLU J OE2 1 
ATOM   10283 N  N   . GLY J  1 41  ? 4.445  -93.732  -49.760  1.00 46.69  ? 42  GLY J N   1 
ATOM   10284 C  CA  . GLY J  1 41  ? 5.645  -93.456  -48.981  1.00 45.63  ? 42  GLY J CA  1 
ATOM   10285 C  C   . GLY J  1 41  ? 6.838  -94.283  -49.399  1.00 42.97  ? 42  GLY J C   1 
ATOM   10286 O  O   . GLY J  1 41  ? 6.893  -94.781  -50.530  1.00 42.02  ? 42  GLY J O   1 
ATOM   10287 N  N   . LEU J  1 42  ? 7.796  -94.421  -48.482  1.00 42.11  ? 43  LEU J N   1 
ATOM   10288 C  CA  . LEU J  1 42  ? 9.052  -95.120  -48.765  1.00 39.98  ? 43  LEU J CA  1 
ATOM   10289 C  C   . LEU J  1 42  ? 8.896  -96.632  -48.706  1.00 38.61  ? 43  LEU J C   1 
ATOM   10290 O  O   . LEU J  1 42  ? 8.162  -97.154  -47.874  1.00 39.39  ? 43  LEU J O   1 
ATOM   10291 C  CB  . LEU J  1 42  ? 10.146 -94.701  -47.778  1.00 40.22  ? 43  LEU J CB  1 
ATOM   10292 C  CG  . LEU J  1 42  ? 10.795 -93.347  -48.041  1.00 41.16  ? 43  LEU J CG  1 
ATOM   10293 C  CD1 . LEU J  1 42  ? 10.414 -92.337  -46.972  1.00 43.60  ? 43  LEU J CD1 1 
ATOM   10294 C  CD2 . LEU J  1 42  ? 12.269 -93.514  -48.096  1.00 40.48  ? 43  LEU J CD2 1 
ATOM   10295 N  N   . HIS J  1 43  ? 9.626  -97.327  -49.572  1.00 36.96  ? 44  HIS J N   1 
ATOM   10296 C  CA  . HIS J  1 43  ? 9.676  -98.790  -49.557  1.00 35.89  ? 44  HIS J CA  1 
ATOM   10297 C  C   . HIS J  1 43  ? 11.095 -99.325  -49.756  1.00 34.50  ? 44  HIS J C   1 
ATOM   10298 O  O   . HIS J  1 43  ? 11.836 -98.837  -50.594  1.00 34.11  ? 44  HIS J O   1 
ATOM   10299 C  CB  . HIS J  1 43  ? 8.752  -99.368  -50.625  1.00 35.84  ? 44  HIS J CB  1 
ATOM   10300 C  CG  . HIS J  1 43  ? 7.300  -99.211  -50.309  1.00 37.43  ? 44  HIS J CG  1 
ATOM   10301 N  ND1 . HIS J  1 43  ? 6.626  -100.075 -49.476  1.00 38.37  ? 44  HIS J ND1 1 
ATOM   10302 C  CD2 . HIS J  1 43  ? 6.398  -98.292  -50.714  1.00 38.81  ? 44  HIS J CD2 1 
ATOM   10303 C  CE1 . HIS J  1 43  ? 5.370  -99.691  -49.378  1.00 40.35  ? 44  HIS J CE1 1 
ATOM   10304 N  NE2 . HIS J  1 43  ? 5.207  -98.613  -50.121  1.00 40.63  ? 44  HIS J NE2 1 
ATOM   10305 N  N   . GLY J  1 44  ? 11.450 -100.327 -48.961  1.00 34.18  ? 45  GLY J N   1 
ATOM   10306 C  CA  . GLY J  1 44  ? 12.718 -101.014 -49.079  1.00 33.38  ? 45  GLY J CA  1 
ATOM   10307 C  C   . GLY J  1 44  ? 12.809 -101.699 -50.415  1.00 32.41  ? 45  GLY J C   1 
ATOM   10308 O  O   . GLY J  1 44  ? 11.810 -102.118 -50.962  1.00 32.55  ? 45  GLY J O   1 
ATOM   10309 N  N   . PHE J  1 45  ? 14.020 -101.818 -50.937  1.00 32.05  ? 46  PHE J N   1 
ATOM   10310 C  CA  . PHE J  1 45  ? 14.230 -102.239 -52.320  1.00 31.48  ? 46  PHE J CA  1 
ATOM   10311 C  C   . PHE J  1 45  ? 15.592 -102.868 -52.449  1.00 31.46  ? 46  PHE J C   1 
ATOM   10312 O  O   . PHE J  1 45  ? 16.582 -102.155 -52.524  1.00 31.97  ? 46  PHE J O   1 
ATOM   10313 C  CB  . PHE J  1 45  ? 14.144 -101.019 -53.223  1.00 31.81  ? 46  PHE J CB  1 
ATOM   10314 C  CG  . PHE J  1 45  ? 14.081 -101.323 -54.690  1.00 31.51  ? 46  PHE J CG  1 
ATOM   10315 C  CD1 . PHE J  1 45  ? 13.165 -102.202 -55.203  1.00 31.19  ? 46  PHE J CD1 1 
ATOM   10316 C  CD2 . PHE J  1 45  ? 14.901 -100.655 -55.563  1.00 32.24  ? 46  PHE J CD2 1 
ATOM   10317 C  CE1 . PHE J  1 45  ? 13.095 -102.443 -56.552  1.00 31.36  ? 46  PHE J CE1 1 
ATOM   10318 C  CE2 . PHE J  1 45  ? 14.831 -100.893 -56.911  1.00 32.61  ? 46  PHE J CE2 1 
ATOM   10319 C  CZ  . PHE J  1 45  ? 13.923 -101.797 -57.403  1.00 32.12  ? 46  PHE J CZ  1 
ATOM   10320 N  N   . HIS J  1 46  ? 15.632 -104.201 -52.471  1.00 31.30  ? 47  HIS J N   1 
ATOM   10321 C  CA  . HIS J  1 46  ? 16.886 -104.944 -52.430  1.00 31.68  ? 47  HIS J CA  1 
ATOM   10322 C  C   . HIS J  1 46  ? 16.996 -106.108 -53.397  1.00 31.66  ? 47  HIS J C   1 
ATOM   10323 O  O   . HIS J  1 46  ? 16.007 -106.693 -53.768  1.00 31.64  ? 47  HIS J O   1 
ATOM   10324 C  CB  . HIS J  1 46  ? 17.092 -105.475 -51.030  1.00 32.40  ? 47  HIS J CB  1 
ATOM   10325 C  CG  . HIS J  1 46  ? 16.706 -104.510 -49.966  1.00 32.47  ? 47  HIS J CG  1 
ATOM   10326 N  ND1 . HIS J  1 46  ? 15.572 -104.662 -49.214  1.00 32.83  ? 47  HIS J ND1 1 
ATOM   10327 C  CD2 . HIS J  1 46  ? 17.301 -103.381 -49.524  1.00 33.47  ? 47  HIS J CD2 1 
ATOM   10328 C  CE1 . HIS J  1 46  ? 15.491 -103.677 -48.342  1.00 33.54  ? 47  HIS J CE1 1 
ATOM   10329 N  NE2 . HIS J  1 46  ? 16.530 -102.884 -48.510  1.00 33.75  ? 47  HIS J NE2 1 
ATOM   10330 N  N   . VAL J  1 47  ? 18.224 -106.437 -53.786  1.00 32.29  ? 48  VAL J N   1 
ATOM   10331 C  CA  . VAL J  1 47  ? 18.509 -107.655 -54.531  1.00 32.68  ? 48  VAL J CA  1 
ATOM   10332 C  C   . VAL J  1 47  ? 18.849 -108.756 -53.555  1.00 33.76  ? 48  VAL J C   1 
ATOM   10333 O  O   . VAL J  1 47  ? 19.825 -108.639 -52.828  1.00 34.72  ? 48  VAL J O   1 
ATOM   10334 C  CB  . VAL J  1 47  ? 19.694 -107.479 -55.460  1.00 33.23  ? 48  VAL J CB  1 
ATOM   10335 C  CG1 . VAL J  1 47  ? 20.089 -108.797 -56.056  1.00 34.04  ? 48  VAL J CG1 1 
ATOM   10336 C  CG2 . VAL J  1 47  ? 19.343 -106.527 -56.527  1.00 33.02  ? 48  VAL J CG2 1 
ATOM   10337 N  N   . HIS J  1 48  ? 18.050 -109.821 -53.542  1.00 34.04  ? 49  HIS J N   1 
ATOM   10338 C  CA  . HIS J  1 48  ? 18.280 -110.969 -52.652  1.00 35.69  ? 49  HIS J CA  1 
ATOM   10339 C  C   . HIS J  1 48  ? 19.070 -112.070 -53.339  1.00 37.06  ? 49  HIS J C   1 
ATOM   10340 O  O   . HIS J  1 48  ? 19.145 -112.108 -54.571  1.00 36.77  ? 49  HIS J O   1 
ATOM   10341 C  CB  . HIS J  1 48  ? 16.965 -111.553 -52.165  1.00 36.03  ? 49  HIS J CB  1 
ATOM   10342 C  CG  . HIS J  1 48  ? 16.238 -110.677 -51.197  1.00 35.51  ? 49  HIS J CG  1 
ATOM   10343 N  ND1 . HIS J  1 48  ? 15.873 -111.103 -49.940  1.00 36.86  ? 49  HIS J ND1 1 
ATOM   10344 C  CD2 . HIS J  1 48  ? 15.812 -109.399 -51.299  1.00 33.87  ? 49  HIS J CD2 1 
ATOM   10345 C  CE1 . HIS J  1 48  ? 15.247 -110.128 -49.312  1.00 36.16  ? 49  HIS J CE1 1 
ATOM   10346 N  NE2 . HIS J  1 48  ? 15.195 -109.085 -50.116  1.00 34.44  ? 49  HIS J NE2 1 
ATOM   10347 N  N   . GLU J  1 49  ? 19.622 -112.979 -52.529  1.00 38.97  ? 50  GLU J N   1 
ATOM   10348 C  CA  . GLU J  1 49  ? 20.640 -113.940 -52.979  1.00 40.77  ? 50  GLU J CA  1 
ATOM   10349 C  C   . GLU J  1 49  ? 20.159 -114.878 -54.065  1.00 40.99  ? 50  GLU J C   1 
ATOM   10350 O  O   . GLU J  1 49  ? 20.791 -114.985 -55.091  1.00 41.26  ? 50  GLU J O   1 
ATOM   10351 C  CB  . GLU J  1 49  ? 21.178 -114.761 -51.802  1.00 43.34  ? 50  GLU J CB  1 
ATOM   10352 C  CG  . GLU J  1 49  ? 22.389 -115.621 -52.163  1.00 45.84  ? 50  GLU J CG  1 
ATOM   10353 C  CD  . GLU J  1 49  ? 23.076 -116.231 -50.969  1.00 48.62  ? 50  GLU J CD  1 
ATOM   10354 O  OE1 . GLU J  1 49  ? 22.773 -115.815 -49.835  1.00 48.27  ? 50  GLU J OE1 1 
ATOM   10355 O  OE2 . GLU J  1 49  ? 23.929 -117.123 -51.182  1.00 51.32  ? 50  GLU J OE2 1 
ATOM   10356 N  N   . PHE J  1 50  ? 19.042 -115.550 -53.834  1.00 41.31  ? 51  PHE J N   1 
ATOM   10357 C  CA  . PHE J  1 50  ? 18.601 -116.631 -54.704  1.00 42.39  ? 51  PHE J CA  1 
ATOM   10358 C  C   . PHE J  1 50  ? 17.486 -116.244 -55.656  1.00 40.92  ? 51  PHE J C   1 
ATOM   10359 O  O   . PHE J  1 50  ? 16.553 -115.542 -55.281  1.00 39.66  ? 51  PHE J O   1 
ATOM   10360 C  CB  . PHE J  1 50  ? 18.140 -117.805 -53.861  1.00 44.78  ? 51  PHE J CB  1 
ATOM   10361 C  CG  . PHE J  1 50  ? 19.165 -118.268 -52.872  1.00 47.09  ? 51  PHE J CG  1 
ATOM   10362 C  CD1 . PHE J  1 50  ? 20.403 -118.686 -53.293  1.00 48.54  ? 51  PHE J CD1 1 
ATOM   10363 C  CD2 . PHE J  1 50  ? 18.888 -118.288 -51.516  1.00 48.43  ? 51  PHE J CD2 1 
ATOM   10364 C  CE1 . PHE J  1 50  ? 21.342 -119.108 -52.388  1.00 51.15  ? 51  PHE J CE1 1 
ATOM   10365 C  CE2 . PHE J  1 50  ? 19.831 -118.709 -50.610  1.00 50.74  ? 51  PHE J CE2 1 
ATOM   10366 C  CZ  . PHE J  1 50  ? 21.053 -119.119 -51.045  1.00 52.15  ? 51  PHE J CZ  1 
ATOM   10367 N  N   . GLY J  1 51  ? 17.590 -116.730 -56.892  1.00 41.53  ? 52  GLY J N   1 
ATOM   10368 C  CA  . GLY J  1 51  ? 16.501 -116.665 -57.882  1.00 40.94  ? 52  GLY J CA  1 
ATOM   10369 C  C   . GLY J  1 51  ? 15.481 -117.800 -57.707  1.00 42.77  ? 52  GLY J C   1 
ATOM   10370 O  O   . GLY J  1 51  ? 15.001 -118.391 -58.662  1.00 43.72  ? 52  GLY J O   1 
ATOM   10371 N  N   . ASP J  1 52  ? 15.134 -118.091 -56.466  1.00 43.62  ? 53  ASP J N   1 
ATOM   10372 C  CA  . ASP J  1 52  ? 14.246 -119.180 -56.135  1.00 45.91  ? 53  ASP J CA  1 
ATOM   10373 C  C   . ASP J  1 52  ? 12.895 -118.595 -55.780  1.00 45.30  ? 53  ASP J C   1 
ATOM   10374 O  O   . ASP J  1 52  ? 12.776 -117.767 -54.879  1.00 44.05  ? 53  ASP J O   1 
ATOM   10375 C  CB  . ASP J  1 52  ? 14.816 -119.937 -54.944  1.00 48.27  ? 53  ASP J CB  1 
ATOM   10376 C  CG  . ASP J  1 52  ? 14.078 -121.239 -54.654  1.00 51.72  ? 53  ASP J CG  1 
ATOM   10377 O  OD1 . ASP J  1 52  ? 12.871 -121.295 -54.926  1.00 52.13  ? 53  ASP J OD1 1 
ATOM   10378 O  OD2 . ASP J  1 52  ? 14.697 -122.199 -54.127  1.00 54.26  ? 53  ASP J OD2 1 
ATOM   10379 N  N   . ASN J  1 53  ? 11.876 -119.026 -56.507  1.00 46.54  ? 54  ASN J N   1 
ATOM   10380 C  CA  . ASN J  1 53  ? 10.491 -118.574 -56.280  1.00 46.65  ? 54  ASN J CA  1 
ATOM   10381 C  C   . ASN J  1 53  ? 9.580  -119.715 -55.858  1.00 49.88  ? 54  ASN J C   1 
ATOM   10382 O  O   . ASN J  1 53  ? 8.371  -119.582 -55.898  1.00 50.60  ? 54  ASN J O   1 
ATOM   10383 C  CB  . ASN J  1 53  ? 9.934  -117.945 -57.563  1.00 45.60  ? 54  ASN J CB  1 
ATOM   10384 C  CG  . ASN J  1 53  ? 9.257  -116.607 -57.324  1.00 44.24  ? 54  ASN J CG  1 
ATOM   10385 O  OD1 . ASN J  1 53  ? 9.922  -115.620 -56.930  1.00 42.70  ? 54  ASN J OD1 1 
ATOM   10386 N  ND2 . ASN J  1 53  ? 7.945  -116.544 -57.598  1.00 45.21  ? 54  ASN J ND2 1 
ATOM   10387 N  N   . THR J  1 54  ? 10.195 -120.834 -55.481  1.00 52.18  ? 55  THR J N   1 
ATOM   10388 C  CA  . THR J  1 54  ? 9.515  -122.060 -55.090  1.00 56.16  ? 55  THR J CA  1 
ATOM   10389 C  C   . THR J  1 54  ? 8.375  -121.773 -54.135  1.00 57.44  ? 55  THR J C   1 
ATOM   10390 O  O   . THR J  1 54  ? 7.203  -121.966 -54.490  1.00 59.20  ? 55  THR J O   1 
ATOM   10391 C  CB  . THR J  1 54  ? 10.514 -123.017 -54.414  1.00 58.38  ? 55  THR J CB  1 
ATOM   10392 O  OG1 . THR J  1 54  ? 11.417 -123.505 -55.412  1.00 58.32  ? 55  THR J OG1 1 
ATOM   10393 C  CG2 . THR J  1 54  ? 9.807  -124.187 -53.680  1.00 63.14  ? 55  THR J CG2 1 
ATOM   10394 N  N   . ALA J  1 55  ? 8.725  -121.305 -52.936  1.00 56.81  ? 56  ALA J N   1 
ATOM   10395 C  CA  . ALA J  1 55  ? 7.752  -120.981 -51.891  1.00 58.25  ? 56  ALA J CA  1 
ATOM   10396 C  C   . ALA J  1 55  ? 7.503  -119.463 -51.817  1.00 54.83  ? 56  ALA J C   1 
ATOM   10397 O  O   . ALA J  1 55  ? 7.479  -118.859 -50.750  1.00 54.59  ? 56  ALA J O   1 
ATOM   10398 C  CB  . ALA J  1 55  ? 8.213  -121.536 -50.547  1.00 60.63  ? 56  ALA J CB  1 
ATOM   10399 N  N   . GLY J  1 56  ? 7.290  -118.861 -52.975  1.00 52.62  ? 57  GLY J N   1 
ATOM   10400 C  CA  . GLY J  1 56  ? 6.987  -117.448 -53.062  1.00 49.86  ? 57  GLY J CA  1 
ATOM   10401 C  C   . GLY J  1 56  ? 8.236  -116.614 -53.015  1.00 46.58  ? 57  GLY J C   1 
ATOM   10402 O  O   . GLY J  1 56  ? 9.277  -117.043 -53.462  1.00 46.06  ? 57  GLY J O   1 
ATOM   10403 N  N   . CYS J  1 57  ? 8.117  -115.404 -52.491  1.00 44.95  ? 58  CYS J N   1 
ATOM   10404 C  CA  . CYS J  1 57  ? 9.263  -114.501 -52.327  1.00 42.24  ? 58  CYS J CA  1 
ATOM   10405 C  C   . CYS J  1 57  ? 10.197 -114.974 -51.216  1.00 43.06  ? 58  CYS J C   1 
ATOM   10406 O  O   . CYS J  1 57  ? 11.367 -114.642 -51.216  1.00 41.61  ? 58  CYS J O   1 
ATOM   10407 C  CB  . CYS J  1 57  ? 8.813  -113.069 -52.006  1.00 40.62  ? 58  CYS J CB  1 
ATOM   10408 S  SG  . CYS J  1 57  ? 8.109  -112.140 -53.297  1.00 39.08  ? 58  CYS J SG  1 
ATOM   10409 N  N   . THR J  1 58  ? 9.668  -115.721 -50.256  1.00 45.84  ? 59  THR J N   1 
ATOM   10410 C  CA  . THR J  1 58  ? 10.454 -116.158 -49.092  1.00 47.45  ? 59  THR J CA  1 
ATOM   10411 C  C   . THR J  1 58  ? 11.642 -117.007 -49.482  1.00 47.82  ? 59  THR J C   1 
ATOM   10412 O  O   . THR J  1 58  ? 12.658 -117.001 -48.803  1.00 48.18  ? 59  THR J O   1 
ATOM   10413 C  CB  . THR J  1 58  ? 9.616  -116.998 -48.096  1.00 51.26  ? 59  THR J CB  1 
ATOM   10414 O  OG1 . THR J  1 58  ? 8.335  -116.376 -47.904  1.00 51.67  ? 59  THR J OG1 1 
ATOM   10415 C  CG2 . THR J  1 58  ? 10.348 -117.149 -46.739  1.00 52.77  ? 59  THR J CG2 1 
ATOM   10416 N  N   . SER J  1 59  ? 11.486 -117.750 -50.566  1.00 48.26  ? 60  SER J N   1 
ATOM   10417 C  CA  . SER J  1 59  ? 12.529 -118.639 -51.089  1.00 49.16  ? 60  SER J CA  1 
ATOM   10418 C  C   . SER J  1 59  ? 13.779 -117.903 -51.571  1.00 46.58  ? 60  SER J C   1 
ATOM   10419 O  O   . SER J  1 59  ? 14.855 -118.484 -51.631  1.00 47.66  ? 60  SER J O   1 
ATOM   10420 C  CB  . SER J  1 59  ? 11.980 -119.456 -52.262  1.00 50.20  ? 60  SER J CB  1 
ATOM   10421 O  OG  . SER J  1 59  ? 10.689 -119.984 -51.991  1.00 53.02  ? 60  SER J OG  1 
ATOM   10422 N  N   . ALA J  1 60  ? 13.626 -116.627 -51.908  1.00 43.79  ? 61  ALA J N   1 
ATOM   10423 C  CA  . ALA J  1 60  ? 14.732 -115.777 -52.376  1.00 41.62  ? 61  ALA J CA  1 
ATOM   10424 C  C   . ALA J  1 60  ? 15.879 -115.629 -51.375  1.00 42.16  ? 61  ALA J C   1 
ATOM   10425 O  O   . ALA J  1 60  ? 16.952 -115.171 -51.723  1.00 41.36  ? 61  ALA J O   1 
ATOM   10426 C  CB  . ALA J  1 60  ? 14.205 -114.392 -52.735  1.00 39.18  ? 61  ALA J CB  1 
ATOM   10427 N  N   . GLY J  1 61  ? 15.641 -115.979 -50.125  1.00 43.96  ? 62  GLY J N   1 
ATOM   10428 C  CA  . GLY J  1 61  ? 16.683 -115.943 -49.115  1.00 45.20  ? 62  GLY J CA  1 
ATOM   10429 C  C   . GLY J  1 61  ? 16.975 -114.523 -48.702  1.00 43.26  ? 62  GLY J C   1 
ATOM   10430 O  O   . GLY J  1 61  ? 16.163 -113.650 -48.905  1.00 41.54  ? 62  GLY J O   1 
ATOM   10431 N  N   . PRO J  1 62  ? 18.140 -114.283 -48.116  1.00 44.02  ? 63  PRO J N   1 
ATOM   10432 C  CA  . PRO J  1 62  ? 18.476 -112.987 -47.570  1.00 42.85  ? 63  PRO J CA  1 
ATOM   10433 C  C   . PRO J  1 62  ? 19.025 -112.040 -48.603  1.00 40.67  ? 63  PRO J C   1 
ATOM   10434 O  O   . PRO J  1 62  ? 19.088 -112.380 -49.780  1.00 39.91  ? 63  PRO J O   1 
ATOM   10435 C  CB  . PRO J  1 62  ? 19.580 -113.322 -46.577  1.00 45.43  ? 63  PRO J CB  1 
ATOM   10436 C  CG  . PRO J  1 62  ? 20.272 -114.443 -47.193  1.00 46.90  ? 63  PRO J CG  1 
ATOM   10437 C  CD  . PRO J  1 62  ? 19.215 -115.255 -47.890  1.00 46.67  ? 63  PRO J CD  1 
ATOM   10438 N  N   . HIS J  1 63  ? 19.413 -110.856 -48.132  1.00 40.07  ? 64  HIS J N   1 
ATOM   10439 C  CA  . HIS J  1 63  ? 20.024 -109.816 -48.962  1.00 38.68  ? 64  HIS J CA  1 
ATOM   10440 C  C   . HIS J  1 63  ? 21.294 -110.337 -49.602  1.00 39.71  ? 64  HIS J C   1 
ATOM   10441 O  O   . HIS J  1 63  ? 22.103 -110.951 -48.926  1.00 41.90  ? 64  HIS J O   1 
ATOM   10442 C  CB  . HIS J  1 63  ? 20.387 -108.598 -48.121  1.00 38.81  ? 64  HIS J CB  1 
ATOM   10443 C  CG  . HIS J  1 63  ? 19.218 -107.796 -47.688  1.00 37.52  ? 64  HIS J CG  1 
ATOM   10444 N  ND1 . HIS J  1 63  ? 19.276 -106.429 -47.548  1.00 36.85  ? 64  HIS J ND1 1 
ATOM   10445 C  CD2 . HIS J  1 63  ? 17.958 -108.162 -47.355  1.00 37.38  ? 64  HIS J CD2 1 
ATOM   10446 C  CE1 . HIS J  1 63  ? 18.097 -105.987 -47.139  1.00 36.54  ? 64  HIS J CE1 1 
ATOM   10447 N  NE2 . HIS J  1 63  ? 17.279 -107.018 -47.019  1.00 36.71  ? 64  HIS J NE2 1 
ATOM   10448 N  N   . PHE J  1 64  ? 21.480 -110.074 -50.893  1.00 38.58  ? 65  PHE J N   1 
ATOM   10449 C  CA  . PHE J  1 64  ? 22.652 -110.573 -51.607  1.00 39.91  ? 65  PHE J CA  1 
ATOM   10450 C  C   . PHE J  1 64  ? 23.873 -109.972 -50.986  1.00 41.41  ? 65  PHE J C   1 
ATOM   10451 O  O   . PHE J  1 64  ? 24.038 -108.768 -50.992  1.00 40.64  ? 65  PHE J O   1 
ATOM   10452 C  CB  . PHE J  1 64  ? 22.575 -110.246 -53.094  1.00 38.83  ? 65  PHE J CB  1 
ATOM   10453 C  CG  . PHE J  1 64  ? 23.747 -110.729 -53.896  1.00 40.30  ? 65  PHE J CG  1 
ATOM   10454 C  CD1 . PHE J  1 64  ? 24.285 -111.974 -53.698  1.00 42.39  ? 65  PHE J CD1 1 
ATOM   10455 C  CD2 . PHE J  1 64  ? 24.284 -109.935 -54.887  1.00 40.60  ? 65  PHE J CD2 1 
ATOM   10456 C  CE1 . PHE J  1 64  ? 25.360 -112.407 -54.455  1.00 44.68  ? 65  PHE J CE1 1 
ATOM   10457 C  CE2 . PHE J  1 64  ? 25.350 -110.364 -55.652  1.00 42.77  ? 65  PHE J CE2 1 
ATOM   10458 C  CZ  . PHE J  1 64  ? 25.888 -111.604 -55.435  1.00 44.74  ? 65  PHE J CZ  1 
ATOM   10459 N  N   . ASN J  1 65  ? 24.730 -110.825 -50.446  1.00 44.06  ? 66  ASN J N   1 
ATOM   10460 C  CA  . ASN J  1 65  ? 25.838 -110.386 -49.595  1.00 46.37  ? 66  ASN J CA  1 
ATOM   10461 C  C   . ASN J  1 65  ? 27.112 -111.230 -49.718  1.00 49.49  ? 66  ASN J C   1 
ATOM   10462 O  O   . ASN J  1 65  ? 27.480 -111.918 -48.779  1.00 51.94  ? 66  ASN J O   1 
ATOM   10463 C  CB  . ASN J  1 65  ? 25.347 -110.396 -48.144  1.00 46.87  ? 66  ASN J CB  1 
ATOM   10464 C  CG  . ASN J  1 65  ? 26.340 -109.818 -47.187  1.00 49.14  ? 66  ASN J CG  1 
ATOM   10465 O  OD1 . ASN J  1 65  ? 27.349 -109.227 -47.589  1.00 50.47  ? 66  ASN J OD1 1 
ATOM   10466 N  ND2 . ASN J  1 65  ? 26.058 -109.963 -45.904  1.00 50.26  ? 66  ASN J ND2 1 
ATOM   10467 N  N   . PRO J  1 66  ? 27.800 -111.167 -50.869  1.00 49.97  ? 67  PRO J N   1 
ATOM   10468 C  CA  . PRO J  1 66  ? 28.928 -112.044 -51.141  1.00 53.21  ? 67  PRO J CA  1 
ATOM   10469 C  C   . PRO J  1 66  ? 30.186 -111.628 -50.436  1.00 56.42  ? 67  PRO J C   1 
ATOM   10470 O  O   . PRO J  1 66  ? 31.040 -112.459 -50.221  1.00 59.87  ? 67  PRO J O   1 
ATOM   10471 C  CB  . PRO J  1 66  ? 29.112 -111.920 -52.654  1.00 52.65  ? 67  PRO J CB  1 
ATOM   10472 C  CG  . PRO J  1 66  ? 28.617 -110.590 -52.973  1.00 50.13  ? 67  PRO J CG  1 
ATOM   10473 C  CD  . PRO J  1 66  ? 27.502 -110.302 -52.016  1.00 47.95  ? 67  PRO J CD  1 
ATOM   10474 N  N   . LEU J  1 67  ? 30.298 -110.348 -50.089  1.00 55.93  ? 68  LEU J N   1 
ATOM   10475 C  CA  . LEU J  1 67  ? 31.465 -109.823 -49.362  1.00 59.08  ? 68  LEU J CA  1 
ATOM   10476 C  C   . LEU J  1 67  ? 31.247 -109.856 -47.847  1.00 59.85  ? 68  LEU J C   1 
ATOM   10477 O  O   . LEU J  1 67  ? 31.977 -109.228 -47.097  1.00 62.17  ? 68  LEU J O   1 
ATOM   10478 C  CB  . LEU J  1 67  ? 31.803 -108.399 -49.822  1.00 58.78  ? 68  LEU J CB  1 
ATOM   10479 C  CG  . LEU J  1 67  ? 32.109 -108.220 -51.310  1.00 58.86  ? 68  LEU J CG  1 
ATOM   10480 C  CD1 . LEU J  1 67  ? 32.647 -106.823 -51.574  1.00 59.84  ? 68  LEU J CD1 1 
ATOM   10481 C  CD2 . LEU J  1 67  ? 33.094 -109.283 -51.816  1.00 62.10  ? 68  LEU J CD2 1 
ATOM   10482 N  N   . SER J  1 68  ? 30.226 -110.577 -47.405  1.00 58.38  ? 69  SER J N   1 
ATOM   10483 C  CA  . SER J  1 68  ? 30.017 -110.901 -45.990  1.00 59.92  ? 69  SER J CA  1 
ATOM   10484 C  C   . SER J  1 68  ? 30.051 -109.675 -45.084  1.00 60.00  ? 69  SER J C   1 
ATOM   10485 O  O   . SER J  1 68  ? 30.704 -109.693 -44.040  1.00 63.14  ? 69  SER J O   1 
ATOM   10486 C  CB  . SER J  1 68  ? 31.059 -111.911 -45.518  1.00 64.55  ? 69  SER J CB  1 
ATOM   10487 O  OG  . SER J  1 68  ? 31.198 -112.998 -46.435  1.00 65.37  ? 69  SER J OG  1 
ATOM   10488 N  N   . ARG J  1 69  ? 29.338 -108.618 -45.482  1.00 56.92  ? 70  ARG J N   1 
ATOM   10489 C  CA  . ARG J  1 69  ? 29.257 -107.374 -44.699  1.00 56.85  ? 70  ARG J CA  1 
ATOM   10490 C  C   . ARG J  1 69  ? 27.916 -107.177 -44.007  1.00 54.53  ? 70  ARG J C   1 
ATOM   10491 O  O   . ARG J  1 69  ? 27.028 -108.007 -44.094  1.00 53.14  ? 70  ARG J O   1 
ATOM   10492 C  CB  . ARG J  1 69  ? 29.571 -106.194 -45.586  1.00 55.95  ? 70  ARG J CB  1 
ATOM   10493 C  CG  . ARG J  1 69  ? 30.930 -106.335 -46.169  1.00 58.88  ? 70  ARG J CG  1 
ATOM   10494 C  CD  . ARG J  1 69  ? 31.609 -105.021 -46.342  1.00 61.05  ? 70  ARG J CD  1 
ATOM   10495 N  NE  . ARG J  1 69  ? 32.259 -104.931 -47.641  1.00 62.94  ? 70  ARG J NE  1 
ATOM   10496 C  CZ  . ARG J  1 69  ? 33.001 -103.905 -48.037  1.00 66.68  ? 70  ARG J CZ  1 
ATOM   10497 N  NH1 . ARG J  1 69  ? 33.211 -102.854 -47.229  1.00 68.53  ? 70  ARG J NH1 1 
ATOM   10498 N  NH2 . ARG J  1 69  ? 33.540 -103.932 -49.250  1.00 68.23  ? 70  ARG J NH2 1 
ATOM   10499 N  N   . LYS J  1 70  ? 27.803 -106.080 -43.284  1.00 54.68  ? 71  LYS J N   1 
ATOM   10500 C  CA  . LYS J  1 70  ? 26.580 -105.726 -42.578  1.00 53.05  ? 71  LYS J CA  1 
ATOM   10501 C  C   . LYS J  1 70  ? 25.662 -104.915 -43.473  1.00 49.61  ? 71  LYS J C   1 
ATOM   10502 O  O   . LYS J  1 70  ? 26.129 -104.310 -44.440  1.00 48.97  ? 71  LYS J O   1 
ATOM   10503 C  CB  . LYS J  1 70  ? 26.927 -104.870 -41.368  1.00 55.42  ? 71  LYS J CB  1 
ATOM   10504 C  CG  . LYS J  1 70  ? 27.887 -105.504 -40.380  1.00 59.63  ? 71  LYS J CG  1 
ATOM   10505 C  CD  . LYS J  1 70  ? 27.140 -106.194 -39.262  1.00 60.84  ? 71  LYS J CD  1 
ATOM   10506 C  CE  . LYS J  1 70  ? 28.070 -106.737 -38.198  1.00 65.59  ? 71  LYS J CE  1 
ATOM   10507 N  NZ  . LYS J  1 70  ? 27.281 -107.392 -37.101  1.00 66.87  ? 71  LYS J NZ  1 
ATOM   10508 N  N   . HIS J  1 71  ? 24.373 -104.862 -43.127  1.00 47.84  ? 72  HIS J N   1 
ATOM   10509 C  CA  . HIS J  1 71  ? 23.383 -104.072 -43.901  1.00 45.07  ? 72  HIS J CA  1 
ATOM   10510 C  C   . HIS J  1 71  ? 23.681 -102.584 -43.856  1.00 45.14  ? 72  HIS J C   1 
ATOM   10511 O  O   . HIS J  1 71  ? 24.276 -102.094 -42.914  1.00 47.18  ? 72  HIS J O   1 
ATOM   10512 C  CB  . HIS J  1 71  ? 21.934 -104.325 -43.430  1.00 43.95  ? 72  HIS J CB  1 
ATOM   10513 C  CG  . HIS J  1 71  ? 20.887 -103.634 -44.258  1.00 41.35  ? 72  HIS J CG  1 
ATOM   10514 N  ND1 . HIS J  1 71  ? 20.577 -104.014 -45.545  1.00 39.36  ? 72  HIS J ND1 1 
ATOM   10515 C  CD2 . HIS J  1 71  ? 20.081 -102.587 -43.971  1.00 40.69  ? 72  HIS J CD2 1 
ATOM   10516 C  CE1 . HIS J  1 71  ? 19.636 -103.217 -46.019  1.00 37.90  ? 72  HIS J CE1 1 
ATOM   10517 N  NE2 . HIS J  1 71  ? 19.316 -102.344 -45.082  1.00 38.36  ? 72  HIS J NE2 1 
ATOM   10518 N  N   . GLY J  1 72  ? 23.270 -101.886 -44.901  1.00 43.24  ? 73  GLY J N   1 
ATOM   10519 C  CA  . GLY J  1 72  ? 23.445 -100.449 -44.967  1.00 43.86  ? 73  GLY J CA  1 
ATOM   10520 C  C   . GLY J  1 72  ? 22.724 -99.783  -46.114  1.00 41.93  ? 73  GLY J C   1 
ATOM   10521 O  O   . GLY J  1 72  ? 22.024 -100.431 -46.874  1.00 40.26  ? 73  GLY J O   1 
ATOM   10522 N  N   . GLY J  1 73  ? 22.889 -98.474  -46.222  1.00 42.78  ? 74  GLY J N   1 
ATOM   10523 C  CA  . GLY J  1 73  ? 22.316 -97.704  -47.325  1.00 41.88  ? 74  GLY J CA  1 
ATOM   10524 C  C   . GLY J  1 73  ? 23.193 -97.830  -48.544  1.00 42.32  ? 74  GLY J C   1 
ATOM   10525 O  O   . GLY J  1 73  ? 24.322 -98.198  -48.425  1.00 44.25  ? 74  GLY J O   1 
ATOM   10526 N  N   . PRO J  1 74  ? 22.688 -97.531  -49.733  1.00 41.40  ? 75  PRO J N   1 
ATOM   10527 C  CA  . PRO J  1 74  ? 23.477 -97.751  -50.934  1.00 42.13  ? 75  PRO J CA  1 
ATOM   10528 C  C   . PRO J  1 74  ? 24.723 -96.882  -50.993  1.00 45.18  ? 75  PRO J C   1 
ATOM   10529 O  O   . PRO J  1 74  ? 25.760 -97.318  -51.476  1.00 46.77  ? 75  PRO J O   1 
ATOM   10530 C  CB  . PRO J  1 74  ? 22.516 -97.384  -52.066  1.00 40.96  ? 75  PRO J CB  1 
ATOM   10531 C  CG  . PRO J  1 74  ? 21.492 -96.555  -51.446  1.00 40.74  ? 75  PRO J CG  1 
ATOM   10532 C  CD  . PRO J  1 74  ? 21.363 -96.993  -50.037  1.00 40.29  ? 75  PRO J CD  1 
ATOM   10533 N  N   . LYS J  1 75  ? 24.624 -95.664  -50.493  1.00 46.60  ? 76  LYS J N   1 
ATOM   10534 C  CA  . LYS J  1 75  ? 25.776 -94.769  -50.455  1.00 50.07  ? 76  LYS J CA  1 
ATOM   10535 C  C   . LYS J  1 75  ? 26.808 -95.229  -49.439  1.00 51.71  ? 76  LYS J C   1 
ATOM   10536 O  O   . LYS J  1 75  ? 27.986 -94.966  -49.602  1.00 54.71  ? 76  LYS J O   1 
ATOM   10537 C  CB  . LYS J  1 75  ? 25.363 -93.345  -50.088  1.00 51.66  ? 76  LYS J CB  1 
ATOM   10538 C  CG  . LYS J  1 75  ? 24.203 -92.779  -50.873  1.00 50.94  ? 76  LYS J CG  1 
ATOM   10539 C  CD  . LYS J  1 75  ? 24.242 -91.265  -50.845  1.00 53.96  ? 76  LYS J CD  1 
ATOM   10540 C  CE  . LYS J  1 75  ? 22.942 -90.657  -51.390  1.00 53.41  ? 76  LYS J CE  1 
ATOM   10541 N  NZ  . LYS J  1 75  ? 22.822 -89.193  -50.987  1.00 56.35  ? 76  LYS J NZ  1 
ATOM   10542 N  N   . ASP J  1 76  ? 26.360 -95.883  -48.373  1.00 50.33  ? 77  ASP J N   1 
ATOM   10543 C  CA  . ASP J  1 76  ? 27.268 -96.400  -47.352  1.00 52.20  ? 77  ASP J CA  1 
ATOM   10544 C  C   . ASP J  1 76  ? 28.266 -97.359  -47.996  1.00 53.19  ? 77  ASP J C   1 
ATOM   10545 O  O   . ASP J  1 76  ? 27.915 -98.096  -48.910  1.00 51.19  ? 77  ASP J O   1 
ATOM   10546 C  CB  . ASP J  1 76  ? 26.506 -97.107  -46.215  1.00 50.62  ? 77  ASP J CB  1 
ATOM   10547 C  CG  . ASP J  1 76  ? 25.759 -96.138  -45.310  1.00 50.93  ? 77  ASP J CG  1 
ATOM   10548 O  OD1 . ASP J  1 76  ? 26.195 -94.976  -45.234  1.00 53.39  ? 77  ASP J OD1 1 
ATOM   10549 O  OD2 . ASP J  1 76  ? 24.741 -96.531  -44.672  1.00 49.41  ? 77  ASP J OD2 1 
ATOM   10550 N  N   . GLU J  1 77  ? 29.518 -97.309  -47.537  1.00 56.74  ? 78  GLU J N   1 
ATOM   10551 C  CA  . GLU J  1 77  ? 30.541 -98.260  -47.972  1.00 58.29  ? 78  GLU J CA  1 
ATOM   10552 C  C   . GLU J  1 77  ? 30.289 -99.614  -47.340  1.00 56.88  ? 78  GLU J C   1 
ATOM   10553 O  O   . GLU J  1 77  ? 30.350 -100.618 -48.033  1.00 56.05  ? 78  GLU J O   1 
ATOM   10554 C  CB  . GLU J  1 77  ? 31.944 -97.816  -47.592  1.00 63.04  ? 78  GLU J CB  1 
ATOM   10555 C  CG  . GLU J  1 77  ? 32.953 -99.002  -47.618  1.00 65.60  ? 78  GLU J CG  1 
ATOM   10556 C  CD  . GLU J  1 77  ? 34.446 -98.587  -47.592  1.00 71.47  ? 78  GLU J CD  1 
ATOM   10557 O  OE1 . GLU J  1 77  ? 34.813 -97.596  -46.892  1.00 74.01  ? 78  GLU J OE1 1 
ATOM   10558 O  OE2 . GLU J  1 77  ? 35.259 -99.282  -48.265  1.00 73.42  ? 78  GLU J OE2 1 
ATOM   10559 N  N   . GLU J  1 78  ? 30.060 -99.634  -46.025  1.00 57.16  ? 79  GLU J N   1 
ATOM   10560 C  CA  . GLU J  1 78  ? 29.620 -100.849 -45.322  1.00 56.04  ? 79  GLU J CA  1 
ATOM   10561 C  C   . GLU J  1 78  ? 28.147 -101.129 -45.647  1.00 52.04  ? 79  GLU J C   1 
ATOM   10562 O  O   . GLU J  1 78  ? 27.245 -100.663 -44.952  1.00 50.90  ? 79  GLU J O   1 
ATOM   10563 C  CB  . GLU J  1 78  ? 29.835 -100.736 -43.803  1.00 58.26  ? 79  GLU J CB  1 
ATOM   10564 C  CG  . GLU J  1 78  ? 29.557 -102.024 -43.006  1.00 58.25  ? 79  GLU J CG  1 
ATOM   10565 C  CD  . GLU J  1 78  ? 30.659 -103.082 -43.131  1.00 61.13  ? 79  GLU J CD  1 
ATOM   10566 O  OE1 . GLU J  1 78  ? 31.658 -102.844 -43.833  1.00 63.33  ? 79  GLU J OE1 1 
ATOM   10567 O  OE2 . GLU J  1 78  ? 30.531 -104.174 -42.532  1.00 61.66  ? 79  GLU J OE2 1 
ATOM   10568 N  N   . ARG J  1 79  ? 27.939 -101.886 -46.725  1.00 50.32  ? 80  ARG J N   1 
ATOM   10569 C  CA  . ARG J  1 79  ? 26.621 -102.309 -47.196  1.00 46.93  ? 80  ARG J CA  1 
ATOM   10570 C  C   . ARG J  1 79  ? 26.648 -103.702 -47.796  1.00 46.34  ? 80  ARG J C   1 
ATOM   10571 O  O   . ARG J  1 79  ? 27.693 -104.217 -48.133  1.00 48.32  ? 80  ARG J O   1 
ATOM   10572 C  CB  . ARG J  1 79  ? 26.120 -101.364 -48.278  1.00 45.43  ? 80  ARG J CB  1 
ATOM   10573 C  CG  . ARG J  1 79  ? 27.034 -101.244 -49.481  1.00 46.61  ? 80  ARG J CG  1 
ATOM   10574 C  CD  . ARG J  1 79  ? 26.405 -100.459 -50.633  1.00 45.31  ? 80  ARG J CD  1 
ATOM   10575 N  NE  . ARG J  1 79  ? 25.591 -101.308 -51.504  1.00 43.08  ? 80  ARG J NE  1 
ATOM   10576 C  CZ  . ARG J  1 79  ? 25.101 -100.944 -52.688  1.00 42.09  ? 80  ARG J CZ  1 
ATOM   10577 N  NH1 . ARG J  1 79  ? 25.342 -99.741  -53.175  1.00 43.31  ? 80  ARG J NH1 1 
ATOM   10578 N  NH2 . ARG J  1 79  ? 24.375 -101.792 -53.396  1.00 40.44  ? 80  ARG J NH2 1 
ATOM   10579 N  N   . HIS J  1 80  ? 25.478 -104.304 -47.946  1.00 44.08  ? 81  HIS J N   1 
ATOM   10580 C  CA  . HIS J  1 80  ? 25.356 -105.528 -48.723  1.00 43.38  ? 81  HIS J CA  1 
ATOM   10581 C  C   . HIS J  1 80  ? 25.436 -105.136 -50.190  1.00 42.55  ? 81  HIS J C   1 
ATOM   10582 O  O   . HIS J  1 80  ? 25.012 -104.055 -50.576  1.00 41.68  ? 81  HIS J O   1 
ATOM   10583 C  CB  . HIS J  1 80  ? 24.023 -106.235 -48.473  1.00 41.56  ? 81  HIS J CB  1 
ATOM   10584 C  CG  . HIS J  1 80  ? 23.808 -106.683 -47.059  1.00 42.62  ? 81  HIS J CG  1 
ATOM   10585 N  ND1 . HIS J  1 80  ? 22.559 -106.738 -46.470  1.00 41.31  ? 81  HIS J ND1 1 
ATOM   10586 C  CD2 . HIS J  1 80  ? 24.681 -107.121 -46.124  1.00 45.31  ? 81  HIS J CD2 1 
ATOM   10587 C  CE1 . HIS J  1 80  ? 22.676 -107.192 -45.235  1.00 43.22  ? 81  HIS J CE1 1 
ATOM   10588 N  NE2 . HIS J  1 80  ? 23.953 -107.420 -44.996  1.00 45.62  ? 81  HIS J NE2 1 
ATOM   10589 N  N   . VAL J  1 81  ? 25.973 -106.011 -51.020  1.00 43.24  ? 82  VAL J N   1 
ATOM   10590 C  CA  . VAL J  1 81  ? 26.018 -105.743 -52.463  1.00 42.62  ? 82  VAL J CA  1 
ATOM   10591 C  C   . VAL J  1 81  ? 24.631 -105.427 -52.969  1.00 39.73  ? 82  VAL J C   1 
ATOM   10592 O  O   . VAL J  1 81  ? 24.446 -104.523 -53.754  1.00 39.22  ? 82  VAL J O   1 
ATOM   10593 C  CB  . VAL J  1 81  ? 26.625 -106.932 -53.251  1.00 43.82  ? 82  VAL J CB  1 
ATOM   10594 C  CG1 . VAL J  1 81  ? 26.467 -106.752 -54.751  1.00 42.92  ? 82  VAL J CG1 1 
ATOM   10595 C  CG2 . VAL J  1 81  ? 28.092 -107.089 -52.875  1.00 47.30  ? 82  VAL J CG2 1 
ATOM   10596 N  N   . GLY J  1 82  ? 23.652 -106.161 -52.474  1.00 38.48  ? 83  GLY J N   1 
ATOM   10597 C  CA  . GLY J  1 82  ? 22.261 -106.040 -52.944  1.00 36.51  ? 83  GLY J CA  1 
ATOM   10598 C  C   . GLY J  1 82  ? 21.414 -104.935 -52.335  1.00 35.50  ? 83  GLY J C   1 
ATOM   10599 O  O   . GLY J  1 82  ? 20.249 -104.793 -52.692  1.00 34.05  ? 83  GLY J O   1 
ATOM   10600 N  N   . ASP J  1 83  ? 22.000 -104.151 -51.430  1.00 36.58  ? 84  ASP J N   1 
ATOM   10601 C  CA  . ASP J  1 83  ? 21.278 -103.085 -50.728  1.00 35.90  ? 84  ASP J CA  1 
ATOM   10602 C  C   . ASP J  1 83  ? 21.113 -101.871 -51.600  1.00 35.70  ? 84  ASP J C   1 
ATOM   10603 O  O   . ASP J  1 83  ? 21.966 -101.001 -51.593  1.00 37.25  ? 84  ASP J O   1 
ATOM   10604 C  CB  . ASP J  1 83  ? 22.011 -102.679 -49.451  1.00 37.41  ? 84  ASP J CB  1 
ATOM   10605 C  CG  . ASP J  1 83  ? 21.881 -103.709 -48.340  1.00 37.72  ? 84  ASP J CG  1 
ATOM   10606 O  OD1 . ASP J  1 83  ? 21.033 -104.623 -48.403  1.00 36.42  ? 84  ASP J OD1 1 
ATOM   10607 O  OD2 . ASP J  1 83  ? 22.641 -103.615 -47.370  1.00 39.66  ? 84  ASP J OD2 1 
ATOM   10608 N  N   . LEU J  1 84  ? 20.014 -101.815 -52.342  1.00 34.39  ? 85  LEU J N   1 
ATOM   10609 C  CA  . LEU J  1 84  ? 19.721 -100.674 -53.221  1.00 34.70  ? 85  LEU J CA  1 
ATOM   10610 C  C   . LEU J  1 84  ? 18.914 -99.568  -52.533  1.00 34.86  ? 85  LEU J C   1 
ATOM   10611 O  O   . LEU J  1 84  ? 18.529 -98.585  -53.170  1.00 35.28  ? 85  LEU J O   1 
ATOM   10612 C  CB  . LEU J  1 84  ? 19.017 -101.136 -54.500  1.00 33.79  ? 85  LEU J CB  1 
ATOM   10613 C  CG  . LEU J  1 84  ? 19.918 -101.805 -55.526  1.00 34.13  ? 85  LEU J CG  1 
ATOM   10614 C  CD1 . LEU J  1 84  ? 19.134 -102.263 -56.694  1.00 33.42  ? 85  LEU J CD1 1 
ATOM   10615 C  CD2 . LEU J  1 84  ? 20.968 -100.858 -55.994  1.00 35.95  ? 85  LEU J CD2 1 
ATOM   10616 N  N   . GLY J  1 85  ? 18.686 -99.718  -51.231  1.00 34.89  ? 86  GLY J N   1 
ATOM   10617 C  CA  . GLY J  1 85  ? 18.053 -98.671  -50.435  1.00 35.40  ? 86  GLY J CA  1 
ATOM   10618 C  C   . GLY J  1 85  ? 16.557 -98.632  -50.599  1.00 34.53  ? 86  GLY J C   1 
ATOM   10619 O  O   . GLY J  1 85  ? 15.928 -99.674  -50.533  1.00 33.80  ? 86  GLY J O   1 
ATOM   10620 N  N   . ASN J  1 86  ? 15.995 -97.439  -50.814  1.00 35.12  ? 87  ASN J N   1 
ATOM   10621 C  CA  . ASN J  1 86  ? 14.538 -97.237  -50.849  1.00 34.83  ? 87  ASN J CA  1 
ATOM   10622 C  C   . ASN J  1 86  ? 14.000 -96.800  -52.201  1.00 34.98  ? 87  ASN J C   1 
ATOM   10623 O  O   . ASN J  1 86  ? 14.723 -96.265  -53.023  1.00 35.70  ? 87  ASN J O   1 
ATOM   10624 C  CB  . ASN J  1 86  ? 14.118 -96.198  -49.818  1.00 36.09  ? 87  ASN J CB  1 
ATOM   10625 C  CG  . ASN J  1 86  ? 14.112 -96.730  -48.433  1.00 36.09  ? 87  ASN J CG  1 
ATOM   10626 O  OD1 . ASN J  1 86  ? 13.513 -97.742  -48.155  1.00 35.78  ? 87  ASN J OD1 1 
ATOM   10627 N  ND2 . ASN J  1 86  ? 14.766 -96.038  -47.545  1.00 37.62  ? 87  ASN J ND2 1 
ATOM   10628 N  N   . VAL J  1 87  ? 12.716 -97.046  -52.414  1.00 34.86  ? 88  VAL J N   1 
ATOM   10629 C  CA  . VAL J  1 87  ? 11.974 -96.480  -53.545  1.00 35.81  ? 88  VAL J CA  1 
ATOM   10630 C  C   . VAL J  1 87  ? 10.760 -95.753  -52.998  1.00 37.21  ? 88  VAL J C   1 
ATOM   10631 O  O   . VAL J  1 87  ? 10.186 -96.180  -51.995  1.00 37.09  ? 88  VAL J O   1 
ATOM   10632 C  CB  . VAL J  1 87  ? 11.489 -97.545  -54.526  1.00 34.96  ? 88  VAL J CB  1 
ATOM   10633 C  CG1 . VAL J  1 87  ? 12.659 -98.182  -55.239  1.00 34.13  ? 88  VAL J CG1 1 
ATOM   10634 C  CG2 . VAL J  1 87  ? 10.664 -98.587  -53.816  1.00 34.43  ? 88  VAL J CG2 1 
ATOM   10635 N  N   . THR J  1 88  ? 10.376 -94.653  -53.639  1.00 39.00  ? 89  THR J N   1 
ATOM   10636 C  CA  . THR J  1 88  ? 9.293  -93.783  -53.124  1.00 40.99  ? 89  THR J CA  1 
ATOM   10637 C  C   . THR J  1 88  ? 7.981  -93.901  -53.915  1.00 42.04  ? 89  THR J C   1 
ATOM   10638 O  O   . THR J  1 88  ? 7.960  -93.737  -55.136  1.00 42.66  ? 89  THR J O   1 
ATOM   10639 C  CB  . THR J  1 88  ? 9.724  -92.300  -53.068  1.00 43.00  ? 89  THR J CB  1 
ATOM   10640 O  OG1 . THR J  1 88  ? 10.718 -92.149  -52.065  1.00 42.76  ? 89  THR J OG1 1 
ATOM   10641 C  CG2 . THR J  1 88  ? 8.574  -91.403  -52.706  1.00 45.40  ? 89  THR J CG2 1 
ATOM   10642 N  N   . ALA J  1 89  ? 6.894  -94.167  -53.189  1.00 42.63  ? 90  ALA J N   1 
ATOM   10643 C  CA  . ALA J  1 89  ? 5.569  -94.367  -53.771  1.00 44.05  ? 90  ALA J CA  1 
ATOM   10644 C  C   . ALA J  1 89  ? 4.654  -93.158  -53.574  1.00 47.21  ? 90  ALA J C   1 
ATOM   10645 O  O   . ALA J  1 89  ? 4.479  -92.694  -52.458  1.00 48.26  ? 90  ALA J O   1 
ATOM   10646 C  CB  . ALA J  1 89  ? 4.942  -95.567  -53.159  1.00 43.25  ? 90  ALA J CB  1 
ATOM   10647 N  N   . ASP J  1 90  ? 4.058  -92.661  -54.655  1.00 49.20  ? 91  ASP J N   1 
ATOM   10648 C  CA  . ASP J  1 90  ? 3.192  -91.471  -54.596  1.00 52.62  ? 91  ASP J CA  1 
ATOM   10649 C  C   . ASP J  1 90  ? 1.723  -91.836  -54.346  1.00 54.55  ? 91  ASP J C   1 
ATOM   10650 O  O   . ASP J  1 90  ? 1.329  -92.979  -54.537  1.00 53.47  ? 91  ASP J O   1 
ATOM   10651 C  CB  . ASP J  1 90  ? 3.359  -90.587  -55.856  1.00 54.61  ? 91  ASP J CB  1 
ATOM   10652 C  CG  . ASP J  1 90  ? 2.788  -91.218  -57.121  1.00 55.17  ? 91  ASP J CG  1 
ATOM   10653 O  OD1 . ASP J  1 90  ? 2.852  -90.558  -58.176  1.00 57.36  ? 91  ASP J OD1 1 
ATOM   10654 O  OD2 . ASP J  1 90  ? 2.273  -92.354  -57.073  1.00 53.97  ? 91  ASP J OD2 1 
ATOM   10655 N  N   . LYS J  1 91  ? 0.946  -90.835  -53.911  1.00 57.84  ? 92  LYS J N   1 
ATOM   10656 C  CA  . LYS J  1 91  ? -0.499 -90.937  -53.583  1.00 60.66  ? 92  LYS J CA  1 
ATOM   10657 C  C   . LYS J  1 91  ? -1.193 -92.162  -54.156  1.00 60.33  ? 92  LYS J C   1 
ATOM   10658 O  O   . LYS J  1 91  ? -1.676 -93.011  -53.402  1.00 59.95  ? 92  LYS J O   1 
ATOM   10659 C  CB  . LYS J  1 91  ? -1.300 -89.708  -54.077  1.00 65.14  ? 92  LYS J CB  1 
ATOM   10660 C  CG  . LYS J  1 91  ? -0.562 -88.387  -54.258  1.00 66.62  ? 92  LYS J CG  1 
ATOM   10661 C  CD  . LYS J  1 91  ? -0.164 -87.759  -52.916  1.00 67.12  ? 92  LYS J CD  1 
ATOM   10662 C  CE  . LYS J  1 91  ? 0.118  -86.237  -53.026  1.00 70.00  ? 92  LYS J CE  1 
ATOM   10663 N  NZ  . LYS J  1 91  ? -1.103 -85.393  -52.833  1.00 74.85  ? 92  LYS J NZ  1 
ATOM   10664 N  N   . ASP J  1 92  ? -1.248 -92.226  -55.492  1.00 60.80  ? 93  ASP J N   1 
ATOM   10665 C  CA  . ASP J  1 92  ? -2.029 -93.248  -56.214  1.00 61.55  ? 93  ASP J CA  1 
ATOM   10666 C  C   . ASP J  1 92  ? -1.284 -94.587  -56.312  1.00 57.82  ? 93  ASP J C   1 
ATOM   10667 O  O   . ASP J  1 92  ? -1.638 -95.460  -57.117  1.00 58.21  ? 93  ASP J O   1 
ATOM   10668 C  CB  . ASP J  1 92  ? -2.537 -92.765  -57.597  1.00 64.47  ? 93  ASP J CB  1 
ATOM   10669 C  CG  . ASP J  1 92  ? -2.088 -91.368  -57.933  1.00 66.34  ? 93  ASP J CG  1 
ATOM   10670 O  OD1 . ASP J  1 92  ? -0.864 -91.194  -58.164  1.00 64.26  ? 93  ASP J OD1 1 
ATOM   10671 O  OD2 . ASP J  1 92  ? -2.960 -90.463  -57.971  1.00 70.19  ? 93  ASP J OD2 1 
ATOM   10672 N  N   . GLY J  1 93  ? -0.274 -94.753  -55.465  1.00 54.73  ? 94  GLY J N   1 
ATOM   10673 C  CA  . GLY J  1 93  ? 0.361  -96.046  -55.259  1.00 51.56  ? 94  GLY J CA  1 
ATOM   10674 C  C   . GLY J  1 93  ? 1.495  -96.358  -56.199  1.00 49.03  ? 94  GLY J C   1 
ATOM   10675 O  O   . GLY J  1 93  ? 2.055  -97.427  -56.102  1.00 46.85  ? 94  GLY J O   1 
ATOM   10676 N  N   . VAL J  1 94  ? 1.819  -95.459  -57.124  1.00 49.54  ? 95  VAL J N   1 
ATOM   10677 C  CA  . VAL J  1 94  ? 2.898  -95.701  -58.076  1.00 47.47  ? 95  VAL J CA  1 
ATOM   10678 C  C   . VAL J  1 94  ? 4.234  -95.354  -57.425  1.00 45.52  ? 95  VAL J C   1 
ATOM   10679 O  O   . VAL J  1 94  ? 4.303  -94.579  -56.481  1.00 45.99  ? 95  VAL J O   1 
ATOM   10680 C  CB  . VAL J  1 94  ? 2.682  -94.909  -59.399  1.00 49.88  ? 95  VAL J CB  1 
ATOM   10681 C  CG1 . VAL J  1 94  ? 3.867  -95.045  -60.347  1.00 47.58  ? 95  VAL J CG1 1 
ATOM   10682 C  CG2 . VAL J  1 94  ? 1.416  -95.384  -60.085  1.00 51.98  ? 95  VAL J CG2 1 
ATOM   10683 N  N   . ALA J  1 95  ? 5.282  -95.999  -57.900  1.00 43.86  ? 96  ALA J N   1 
ATOM   10684 C  CA  . ALA J  1 95  ? 6.641  -95.641  -57.544  1.00 42.39  ? 96  ALA J CA  1 
ATOM   10685 C  C   . ALA J  1 95  ? 7.456  -95.611  -58.811  1.00 42.36  ? 96  ALA J C   1 
ATOM   10686 O  O   . ALA J  1 95  ? 7.696  -96.645  -59.396  1.00 41.21  ? 96  ALA J O   1 
ATOM   10687 C  CB  . ALA J  1 95  ? 7.208  -96.648  -56.596  1.00 39.97  ? 96  ALA J CB  1 
ATOM   10688 N  N   . ASP J  1 96  ? 7.849  -94.426  -59.253  1.00 44.11  ? 97  ASP J N   1 
ATOM   10689 C  CA  . ASP J  1 96  ? 8.622  -94.294  -60.488  1.00 44.99  ? 97  ASP J CA  1 
ATOM   10690 C  C   . ASP J  1 96  ? 10.107 -94.437  -60.196  1.00 43.44  ? 97  ASP J C   1 
ATOM   10691 O  O   . ASP J  1 96  ? 10.783 -93.459  -59.917  1.00 44.82  ? 97  ASP J O   1 
ATOM   10692 C  CB  . ASP J  1 96  ? 8.344  -92.950  -61.179  1.00 48.56  ? 97  ASP J CB  1 
ATOM   10693 C  CG  . ASP J  1 96  ? 7.100  -92.979  -62.066  1.00 51.40  ? 97  ASP J CG  1 
ATOM   10694 O  OD1 . ASP J  1 96  ? 7.010  -93.913  -62.909  1.00 50.92  ? 97  ASP J OD1 1 
ATOM   10695 O  OD2 . ASP J  1 96  ? 6.238  -92.048  -61.938  1.00 54.36  ? 97  ASP J OD2 1 
ATOM   10696 N  N   . VAL J  1 97  ? 10.610 -95.662  -60.278  1.00 41.18  ? 98  VAL J N   1 
ATOM   10697 C  CA  . VAL J  1 97  ? 11.975 -95.980  -59.867  1.00 39.66  ? 98  VAL J CA  1 
ATOM   10698 C  C   . VAL J  1 97  ? 12.972 -95.398  -60.842  1.00 41.38  ? 98  VAL J C   1 
ATOM   10699 O  O   . VAL J  1 97  ? 12.799 -95.510  -62.041  1.00 42.66  ? 98  VAL J O   1 
ATOM   10700 C  CB  . VAL J  1 97  ? 12.217 -97.500  -59.778  1.00 37.41  ? 98  VAL J CB  1 
ATOM   10701 C  CG1 . VAL J  1 97  ? 13.589 -97.778  -59.320  1.00 36.53  ? 98  VAL J CG1 1 
ATOM   10702 C  CG2 . VAL J  1 97  ? 11.262 -98.147  -58.820  1.00 36.46  ? 98  VAL J CG2 1 
ATOM   10703 N  N   . SER J  1 98  ? 14.002 -94.752  -60.309  1.00 42.03  ? 99  SER J N   1 
ATOM   10704 C  CA  . SER J  1 98  ? 15.176 -94.311  -61.085  1.00 43.91  ? 99  SER J CA  1 
ATOM   10705 C  C   . SER J  1 98  ? 16.413 -94.209  -60.189  1.00 43.59  ? 99  SER J C   1 
ATOM   10706 O  O   . SER J  1 98  ? 16.726 -93.162  -59.631  1.00 45.12  ? 99  SER J O   1 
ATOM   10707 C  CB  . SER J  1 98  ? 14.930 -92.976  -61.777  1.00 47.32  ? 99  SER J CB  1 
ATOM   10708 O  OG  . SER J  1 98  ? 16.112 -92.545  -62.422  1.00 49.15  ? 99  SER J OG  1 
ATOM   10709 N  N   . ILE J  1 99  ? 17.105 -95.327  -60.066  1.00 41.98  ? 100 ILE J N   1 
ATOM   10710 C  CA  . ILE J  1 99  ? 18.317 -95.434  -59.274  1.00 41.82  ? 100 ILE J CA  1 
ATOM   10711 C  C   . ILE J  1 99  ? 19.507 -95.599  -60.202  1.00 43.60  ? 100 ILE J C   1 
ATOM   10712 O  O   . ILE J  1 99  ? 19.340 -96.042  -61.333  1.00 44.26  ? 100 ILE J O   1 
ATOM   10713 C  CB  . ILE J  1 99  ? 18.240 -96.644  -58.353  1.00 39.06  ? 100 ILE J CB  1 
ATOM   10714 C  CG1 . ILE J  1 99  ? 17.138 -96.441  -57.323  1.00 37.88  ? 100 ILE J CG1 1 
ATOM   10715 C  CG2 . ILE J  1 99  ? 19.549 -96.865  -57.675  1.00 39.60  ? 100 ILE J CG2 1 
ATOM   10716 C  CD1 . ILE J  1 99  ? 17.251 -97.321  -56.128  1.00 36.22  ? 100 ILE J CD1 1 
ATOM   10717 N  N   . GLU J  1 100 ? 20.693 -95.207  -59.739  1.00 45.06  ? 101 GLU J N   1 
ATOM   10718 C  CA  . GLU J  1 100 ? 21.957 -95.518  -60.416  1.00 46.86  ? 101 GLU J CA  1 
ATOM   10719 C  C   . GLU J  1 100 ? 22.960 -95.991  -59.382  1.00 46.52  ? 101 GLU J C   1 
ATOM   10720 O  O   . GLU J  1 100 ? 23.227 -95.287  -58.427  1.00 47.37  ? 101 GLU J O   1 
ATOM   10721 C  CB  . GLU J  1 100 ? 22.503 -94.303  -61.157  1.00 50.71  ? 101 GLU J CB  1 
ATOM   10722 C  CG  . GLU J  1 100 ? 23.746 -94.617  -62.016  1.00 53.84  ? 101 GLU J CG  1 
ATOM   10723 C  CD  . GLU J  1 100 ? 24.140 -93.494  -63.014  1.00 58.72  ? 101 GLU J CD  1 
ATOM   10724 O  OE1 . GLU J  1 100 ? 25.047 -93.735  -63.859  1.00 60.84  ? 101 GLU J OE1 1 
ATOM   10725 O  OE2 . GLU J  1 100 ? 23.546 -92.378  -62.963  1.00 60.20  ? 101 GLU J OE2 1 
ATOM   10726 N  N   . ASP J  1 101 ? 23.514 -97.181  -59.567  1.00 45.78  ? 102 ASP J N   1 
ATOM   10727 C  CA  . ASP J  1 101 ? 24.343 -97.807  -58.530  1.00 45.45  ? 102 ASP J CA  1 
ATOM   10728 C  C   . ASP J  1 101 ? 25.625 -98.419  -59.083  1.00 47.57  ? 102 ASP J C   1 
ATOM   10729 O  O   . ASP J  1 101 ? 25.673 -98.882  -60.218  1.00 48.07  ? 102 ASP J O   1 
ATOM   10730 C  CB  . ASP J  1 101 ? 23.546 -98.882  -57.805  1.00 42.35  ? 102 ASP J CB  1 
ATOM   10731 C  CG  . ASP J  1 101 ? 24.167 -99.289  -56.491  1.00 42.10  ? 102 ASP J CG  1 
ATOM   10732 O  OD1 . ASP J  1 101 ? 24.179 -98.469  -55.578  1.00 42.39  ? 102 ASP J OD1 1 
ATOM   10733 O  OD2 . ASP J  1 101 ? 24.620 -100.437 -56.349  1.00 41.86  ? 102 ASP J OD2 1 
ATOM   10734 N  N   . SER J  1 102 ? 26.656 -98.428  -58.248  1.00 49.17  ? 103 SER J N   1 
ATOM   10735 C  CA  . SER J  1 102 ? 28.010 -98.838  -58.637  1.00 52.02  ? 103 SER J CA  1 
ATOM   10736 C  C   . SER J  1 102 ? 28.526 -100.093 -57.980  1.00 51.36  ? 103 SER J C   1 
ATOM   10737 O  O   . SER J  1 102 ? 29.539 -100.613 -58.402  1.00 53.77  ? 103 SER J O   1 
ATOM   10738 C  CB  . SER J  1 102 ? 28.982 -97.724  -58.304  1.00 55.63  ? 103 SER J CB  1 
ATOM   10739 O  OG  . SER J  1 102 ? 28.524 -96.505  -58.855  1.00 57.09  ? 103 SER J OG  1 
ATOM   10740 N  N   . VAL J  1 103 ? 27.848 -100.567 -56.946  1.00 48.75  ? 104 VAL J N   1 
ATOM   10741 C  CA  . VAL J  1 103 ? 28.223 -101.805 -56.277  1.00 48.38  ? 104 VAL J CA  1 
ATOM   10742 C  C   . VAL J  1 103 ? 27.664 -103.020 -57.001  1.00 46.69  ? 104 VAL J C   1 
ATOM   10743 O  O   . VAL J  1 103 ? 28.379 -103.976 -57.218  1.00 48.22  ? 104 VAL J O   1 
ATOM   10744 C  CB  . VAL J  1 103 ? 27.736 -101.854 -54.830  1.00 46.85  ? 104 VAL J CB  1 
ATOM   10745 C  CG1 . VAL J  1 103 ? 28.171 -103.140 -54.184  1.00 47.17  ? 104 VAL J CG1 1 
ATOM   10746 C  CG2 . VAL J  1 103 ? 28.264 -100.679 -54.039  1.00 49.07  ? 104 VAL J CG2 1 
ATOM   10747 N  N   . ILE J  1 104 ? 26.388 -103.001 -57.357  1.00 44.04  ? 105 ILE J N   1 
ATOM   10748 C  CA  . ILE J  1 104 ? 25.806 -104.121 -58.092  1.00 42.73  ? 105 ILE J CA  1 
ATOM   10749 C  C   . ILE J  1 104 ? 26.408 -104.195 -59.474  1.00 44.68  ? 105 ILE J C   1 
ATOM   10750 O  O   . ILE J  1 104 ? 26.951 -103.220 -59.967  1.00 46.59  ? 105 ILE J O   1 
ATOM   10751 C  CB  . ILE J  1 104 ? 24.264 -104.043 -58.229  1.00 40.03  ? 105 ILE J CB  1 
ATOM   10752 C  CG1 . ILE J  1 104 ? 23.835 -102.811 -59.037  1.00 40.47  ? 105 ILE J CG1 1 
ATOM   10753 C  CG2 . ILE J  1 104 ? 23.617 -104.055 -56.882  1.00 38.27  ? 105 ILE J CG2 1 
ATOM   10754 C  CD1 . ILE J  1 104 ? 22.418 -102.881 -59.601  1.00 38.23  ? 105 ILE J CD1 1 
ATOM   10755 N  N   . SER J  1 105 ? 26.297 -105.355 -60.104  1.00 44.66  ? 106 SER J N   1 
ATOM   10756 C  CA  . SER J  1 105 ? 26.752 -105.524 -61.494  1.00 46.79  ? 106 SER J CA  1 
ATOM   10757 C  C   . SER J  1 105 ? 26.002 -106.620 -62.249  1.00 45.72  ? 106 SER J C   1 
ATOM   10758 O  O   . SER J  1 105 ? 25.479 -107.565 -61.649  1.00 44.19  ? 106 SER J O   1 
ATOM   10759 C  CB  . SER J  1 105 ? 28.256 -105.823 -61.557  1.00 50.18  ? 106 SER J CB  1 
ATOM   10760 O  OG  . SER J  1 105 ? 28.760 -105.762 -62.892  1.00 52.44  ? 106 SER J OG  1 
ATOM   10761 N  N   . LEU J  1 106 ? 25.982 -106.480 -63.575  1.00 46.90  ? 107 LEU J N   1 
ATOM   10762 C  CA  . LEU J  1 106 ? 25.398 -107.474 -64.456  1.00 46.57  ? 107 LEU J CA  1 
ATOM   10763 C  C   . LEU J  1 106 ? 26.454 -108.456 -64.966  1.00 49.27  ? 107 LEU J C   1 
ATOM   10764 O  O   . LEU J  1 106 ? 26.215 -109.173 -65.933  1.00 50.09  ? 107 LEU J O   1 
ATOM   10765 C  CB  . LEU J  1 106 ? 24.708 -106.783 -65.629  1.00 46.83  ? 107 LEU J CB  1 
ATOM   10766 C  CG  . LEU J  1 106 ? 23.596 -105.817 -65.247  1.00 44.45  ? 107 LEU J CG  1 
ATOM   10767 C  CD1 . LEU J  1 106 ? 22.950 -105.259 -66.488  1.00 45.43  ? 107 LEU J CD1 1 
ATOM   10768 C  CD2 . LEU J  1 106 ? 22.584 -106.523 -64.384  1.00 41.59  ? 107 LEU J CD2 1 
ATOM   10769 N  N   . SER J  1 107 ? 27.616 -108.492 -64.310  1.00 51.08  ? 108 SER J N   1 
ATOM   10770 C  CA  . SER J  1 107 ? 28.713 -109.398 -64.681  1.00 53.95  ? 108 SER J CA  1 
ATOM   10771 C  C   . SER J  1 107 ? 29.714 -109.590 -63.548  1.00 55.21  ? 108 SER J C   1 
ATOM   10772 O  O   . SER J  1 107 ? 30.035 -108.665 -62.825  1.00 55.18  ? 108 SER J O   1 
ATOM   10773 C  CB  . SER J  1 107 ? 29.440 -108.891 -65.932  1.00 57.18  ? 108 SER J CB  1 
ATOM   10774 O  OG  . SER J  1 107 ? 29.934 -107.572 -65.759  1.00 58.12  ? 108 SER J OG  1 
ATOM   10775 N  N   . GLY J  1 108 ? 30.187 -110.813 -63.396  1.00 56.77  ? 109 GLY J N   1 
ATOM   10776 C  CA  . GLY J  1 108 ? 31.279 -111.116 -62.474  1.00 59.22  ? 109 GLY J CA  1 
ATOM   10777 C  C   . GLY J  1 108 ? 30.884 -111.489 -61.059  1.00 57.44  ? 109 GLY J C   1 
ATOM   10778 O  O   . GLY J  1 108 ? 29.810 -112.030 -60.829  1.00 54.93  ? 109 GLY J O   1 
ATOM   10779 N  N   . ASP J  1 109 ? 31.790 -111.233 -60.119  1.00 59.41  ? 110 ASP J N   1 
ATOM   10780 C  CA  . ASP J  1 109 ? 31.616 -111.590 -58.690  1.00 58.71  ? 110 ASP J CA  1 
ATOM   10781 C  C   . ASP J  1 109 ? 30.319 -111.062 -58.076  1.00 54.56  ? 110 ASP J C   1 
ATOM   10782 O  O   . ASP J  1 109 ? 29.634 -111.743 -57.313  1.00 52.88  ? 110 ASP J O   1 
ATOM   10783 C  CB  . ASP J  1 109 ? 32.792 -111.019 -57.897  1.00 61.73  ? 110 ASP J CB  1 
ATOM   10784 C  CG  . ASP J  1 109 ? 33.089 -111.801 -56.641  1.00 63.52  ? 110 ASP J CG  1 
ATOM   10785 O  OD1 . ASP J  1 109 ? 32.458 -111.511 -55.591  1.00 61.48  ? 110 ASP J OD1 1 
ATOM   10786 O  OD2 . ASP J  1 109 ? 33.977 -112.689 -56.711  1.00 67.26  ? 110 ASP J OD2 1 
ATOM   10787 N  N   . HIS J  1 110 ? 30.012 -109.826 -58.441  1.00 53.27  ? 111 HIS J N   1 
ATOM   10788 C  CA  . HIS J  1 110 ? 28.827 -109.087 -57.986  1.00 49.88  ? 111 HIS J CA  1 
ATOM   10789 C  C   . HIS J  1 110 ? 27.579 -109.316 -58.866  1.00 47.33  ? 111 HIS J C   1 
ATOM   10790 O  O   . HIS J  1 110 ? 26.582 -108.623 -58.714  1.00 44.93  ? 111 HIS J O   1 
ATOM   10791 C  CB  . HIS J  1 110 ? 29.162 -107.583 -57.996  1.00 50.40  ? 111 HIS J CB  1 
ATOM   10792 C  CG  . HIS J  1 110 ? 30.192 -107.171 -56.990  1.00 52.78  ? 111 HIS J CG  1 
ATOM   10793 N  ND1 . HIS J  1 110 ? 30.446 -105.848 -56.690  1.00 53.33  ? 111 HIS J ND1 1 
ATOM   10794 C  CD2 . HIS J  1 110 ? 31.013 -107.902 -56.200  1.00 55.11  ? 111 HIS J CD2 1 
ATOM   10795 C  CE1 . HIS J  1 110 ? 31.378 -105.781 -55.756  1.00 55.79  ? 111 HIS J CE1 1 
ATOM   10796 N  NE2 . HIS J  1 110 ? 31.736 -107.014 -55.438  1.00 57.11  ? 111 HIS J NE2 1 
ATOM   10797 N  N   . CYS J  1 111 ? 27.648 -110.271 -59.790  1.00 48.27  ? 112 CYS J N   1 
ATOM   10798 C  CA  . CYS J  1 111 ? 26.589 -110.484 -60.792  1.00 46.57  ? 112 CYS J CA  1 
ATOM   10799 C  C   . CYS J  1 111 ? 25.252 -110.733 -60.119  1.00 43.74  ? 112 CYS J C   1 
ATOM   10800 O  O   . CYS J  1 111 ? 25.113 -111.708 -59.387  1.00 43.83  ? 112 CYS J O   1 
ATOM   10801 C  CB  . CYS J  1 111 ? 26.928 -111.671 -61.706  1.00 48.48  ? 112 CYS J CB  1 
ATOM   10802 S  SG  . CYS J  1 111 ? 25.803 -111.936 -63.072  1.00 47.06  ? 112 CYS J SG  1 
ATOM   10803 N  N   . ILE J  1 112 ? 24.290 -109.842 -60.359  1.00 41.63  ? 113 ILE J N   1 
ATOM   10804 C  CA  . ILE J  1 112 ? 22.940 -109.970 -59.802  1.00 39.36  ? 113 ILE J CA  1 
ATOM   10805 C  C   . ILE J  1 112 ? 21.986 -110.753 -60.705  1.00 39.04  ? 113 ILE J C   1 
ATOM   10806 O  O   . ILE J  1 112 ? 20.867 -111.074 -60.319  1.00 37.77  ? 113 ILE J O   1 
ATOM   10807 C  CB  . ILE J  1 112 ? 22.303 -108.611 -59.515  1.00 37.80  ? 113 ILE J CB  1 
ATOM   10808 C  CG1 . ILE J  1 112 ? 22.174 -107.772 -60.781  1.00 38.07  ? 113 ILE J CG1 1 
ATOM   10809 C  CG2 . ILE J  1 112 ? 23.121 -107.856 -58.510  1.00 38.49  ? 113 ILE J CG2 1 
ATOM   10810 C  CD1 . ILE J  1 112 ? 21.124 -106.721 -60.687  1.00 36.70  ? 113 ILE J CD1 1 
ATOM   10811 N  N   . ILE J  1 113 ? 22.431 -111.061 -61.917  1.00 40.59  ? 114 ILE J N   1 
ATOM   10812 C  CA  . ILE J  1 113 ? 21.607 -111.805 -62.872  1.00 40.51  ? 114 ILE J CA  1 
ATOM   10813 C  C   . ILE J  1 113 ? 21.362 -113.215 -62.374  1.00 40.84  ? 114 ILE J C   1 
ATOM   10814 O  O   . ILE J  1 113 ? 22.276 -113.906 -61.946  1.00 42.25  ? 114 ILE J O   1 
ATOM   10815 C  CB  . ILE J  1 113 ? 22.237 -111.857 -64.278  1.00 42.44  ? 114 ILE J CB  1 
ATOM   10816 C  CG1 . ILE J  1 113 ? 22.158 -110.479 -64.940  1.00 42.35  ? 114 ILE J CG1 1 
ATOM   10817 C  CG2 . ILE J  1 113 ? 21.522 -112.894 -65.127  1.00 42.92  ? 114 ILE J CG2 1 
ATOM   10818 C  CD1 . ILE J  1 113 ? 22.910 -110.359 -66.206  1.00 45.06  ? 114 ILE J CD1 1 
ATOM   10819 N  N   . GLY J  1 114 ? 20.110 -113.629 -62.436  1.00 40.02  ? 115 GLY J N   1 
ATOM   10820 C  CA  . GLY J  1 114 ? 19.698 -114.931 -61.927  1.00 40.83  ? 115 GLY J CA  1 
ATOM   10821 C  C   . GLY J  1 114 ? 19.306 -114.884 -60.455  1.00 39.78  ? 115 GLY J C   1 
ATOM   10822 O  O   . GLY J  1 114 ? 18.961 -115.901 -59.848  1.00 40.63  ? 115 GLY J O   1 
ATOM   10823 N  N   . ARG J  1 115 ? 19.347 -113.696 -59.881  1.00 38.20  ? 116 ARG J N   1 
ATOM   10824 C  CA  . ARG J  1 115 ? 18.945 -113.522 -58.505  1.00 37.59  ? 116 ARG J CA  1 
ATOM   10825 C  C   . ARG J  1 115 ? 17.643 -112.734 -58.438  1.00 36.04  ? 116 ARG J C   1 
ATOM   10826 O  O   . ARG J  1 115 ? 17.170 -112.239 -59.459  1.00 35.57  ? 116 ARG J O   1 
ATOM   10827 C  CB  . ARG J  1 115 ? 20.046 -112.826 -57.724  1.00 37.64  ? 116 ARG J CB  1 
ATOM   10828 C  CG  . ARG J  1 115 ? 21.368 -113.546 -57.820  1.00 39.83  ? 116 ARG J CG  1 
ATOM   10829 C  CD  . ARG J  1 115 ? 22.432 -112.935 -56.936  1.00 40.57  ? 116 ARG J CD  1 
ATOM   10830 N  NE  . ARG J  1 115 ? 23.748 -113.519 -57.191  1.00 42.76  ? 116 ARG J NE  1 
ATOM   10831 C  CZ  . ARG J  1 115 ? 24.207 -114.639 -56.647  1.00 44.79  ? 116 ARG J CZ  1 
ATOM   10832 N  NH1 . ARG J  1 115 ? 23.478 -115.340 -55.787  1.00 44.88  ? 116 ARG J NH1 1 
ATOM   10833 N  NH2 . ARG J  1 115 ? 25.418 -115.060 -56.964  1.00 47.58  ? 116 ARG J NH2 1 
ATOM   10834 N  N   . THR J  1 116 ? 17.074 -112.631 -57.237  1.00 35.54  ? 117 THR J N   1 
ATOM   10835 C  CA  . THR J  1 116 ? 15.754 -112.050 -57.042  1.00 34.51  ? 117 THR J CA  1 
ATOM   10836 C  C   . THR J  1 116 ? 15.786 -110.596 -56.595  1.00 33.29  ? 117 THR J C   1 
ATOM   10837 O  O   . THR J  1 116 ? 16.505 -110.264 -55.671  1.00 33.48  ? 117 THR J O   1 
ATOM   10838 C  CB  . THR J  1 116 ? 14.985 -112.838 -56.001  1.00 35.32  ? 117 THR J CB  1 
ATOM   10839 O  OG1 . THR J  1 116 ? 14.740 -114.153 -56.493  1.00 36.56  ? 117 THR J OG1 1 
ATOM   10840 C  CG2 . THR J  1 116 ? 13.678 -112.165 -55.708  1.00 34.89  ? 117 THR J CG2 1 
ATOM   10841 N  N   . LEU J  1 117 ? 15.009 -109.745 -57.265  1.00 32.57  ? 118 LEU J N   1 
ATOM   10842 C  CA  . LEU J  1 117 ? 14.733 -108.370 -56.826  1.00 31.67  ? 118 LEU J CA  1 
ATOM   10843 C  C   . LEU J  1 117 ? 13.512 -108.398 -55.937  1.00 31.70  ? 118 LEU J C   1 
ATOM   10844 O  O   . LEU J  1 117 ? 12.651 -109.217 -56.130  1.00 32.69  ? 118 LEU J O   1 
ATOM   10845 C  CB  . LEU J  1 117 ? 14.471 -107.463 -58.024  1.00 31.47  ? 118 LEU J CB  1 
ATOM   10846 C  CG  . LEU J  1 117 ? 14.276 -105.994 -57.715  1.00 30.94  ? 118 LEU J CG  1 
ATOM   10847 C  CD1 . LEU J  1 117 ? 15.495 -105.462 -57.008  1.00 31.13  ? 118 LEU J CD1 1 
ATOM   10848 C  CD2 . LEU J  1 117 ? 14.016 -105.212 -58.974  1.00 31.32  ? 118 LEU J CD2 1 
ATOM   10849 N  N   . VAL J  1 118 ? 13.426 -107.514 -54.959  1.00 31.28  ? 119 VAL J N   1 
ATOM   10850 C  CA  . VAL J  1 118 ? 12.344 -107.569 -53.967  1.00 31.74  ? 119 VAL J CA  1 
ATOM   10851 C  C   . VAL J  1 118 ? 11.954 -106.190 -53.433  1.00 31.55  ? 119 VAL J C   1 
ATOM   10852 O  O   . VAL J  1 118 ? 12.772 -105.482 -52.890  1.00 31.45  ? 119 VAL J O   1 
ATOM   10853 C  CB  . VAL J  1 118 ? 12.733 -108.439 -52.767  1.00 32.42  ? 119 VAL J CB  1 
ATOM   10854 C  CG1 . VAL J  1 118 ? 11.745 -108.293 -51.655  1.00 33.32  ? 119 VAL J CG1 1 
ATOM   10855 C  CG2 . VAL J  1 118 ? 12.810 -109.861 -53.168  1.00 33.42  ? 119 VAL J CG2 1 
ATOM   10856 N  N   . VAL J  1 119 ? 10.691 -105.818 -53.579  1.00 32.12  ? 120 VAL J N   1 
ATOM   10857 C  CA  . VAL J  1 119 ? 10.181 -104.575 -53.018  1.00 32.29  ? 120 VAL J CA  1 
ATOM   10858 C  C   . VAL J  1 119 ? 9.491  -104.923 -51.714  1.00 33.40  ? 120 VAL J C   1 
ATOM   10859 O  O   . VAL J  1 119 ? 8.918  -105.995 -51.587  1.00 34.28  ? 120 VAL J O   1 
ATOM   10860 C  CB  . VAL J  1 119 ? 9.231  -103.859 -53.977  1.00 32.76  ? 120 VAL J CB  1 
ATOM   10861 C  CG1 . VAL J  1 119 ? 7.918  -104.570 -54.054  1.00 34.33  ? 120 VAL J CG1 1 
ATOM   10862 C  CG2 . VAL J  1 119 ? 9.034  -102.430 -53.539  1.00 33.21  ? 120 VAL J CG2 1 
ATOM   10863 N  N   . HIS J  1 120 ? 9.545  -104.015 -50.748  1.00 33.85  ? 121 HIS J N   1 
ATOM   10864 C  CA  . HIS J  1 120 ? 9.230  -104.336 -49.344  1.00 35.01  ? 121 HIS J CA  1 
ATOM   10865 C  C   . HIS J  1 120 ? 8.082  -103.568 -48.711  1.00 36.49  ? 121 HIS J C   1 
ATOM   10866 O  O   . HIS J  1 120 ? 7.683  -102.503 -49.170  1.00 36.46  ? 121 HIS J O   1 
ATOM   10867 C  CB  . HIS J  1 120 ? 10.464 -104.114 -48.482  1.00 34.81  ? 121 HIS J CB  1 
ATOM   10868 C  CG  . HIS J  1 120 ? 11.362 -105.296 -48.410  1.00 34.32  ? 121 HIS J CG  1 
ATOM   10869 N  ND1 . HIS J  1 120 ? 11.483 -106.066 -47.278  1.00 35.86  ? 121 HIS J ND1 1 
ATOM   10870 C  CD2 . HIS J  1 120 ? 12.173 -105.851 -49.333  1.00 33.28  ? 121 HIS J CD2 1 
ATOM   10871 C  CE1 . HIS J  1 120 ? 12.334 -107.047 -47.505  1.00 35.67  ? 121 HIS J CE1 1 
ATOM   10872 N  NE2 . HIS J  1 120 ? 12.764 -106.939 -48.745  1.00 34.25  ? 121 HIS J NE2 1 
ATOM   10873 N  N   . GLU J  1 121 ? 7.588  -104.134 -47.613  1.00 38.24  ? 122 GLU J N   1 
ATOM   10874 C  CA  . GLU J  1 121 ? 6.419  -103.619 -46.884  1.00 40.34  ? 122 GLU J CA  1 
ATOM   10875 C  C   . GLU J  1 121 ? 6.663  -102.205 -46.391  1.00 40.39  ? 122 GLU J C   1 
ATOM   10876 O  O   . GLU J  1 121 ? 5.999  -101.270 -46.832  1.00 40.82  ? 122 GLU J O   1 
ATOM   10877 C  CB  . GLU J  1 121 ? 6.078  -104.541 -45.702  1.00 42.37  ? 122 GLU J CB  1 
ATOM   10878 C  CG  . GLU J  1 121 ? 4.955  -104.045 -44.800  1.00 45.22  ? 122 GLU J CG  1 
ATOM   10879 C  CD  . GLU J  1 121 ? 4.778  -104.866 -43.519  1.00 48.16  ? 122 GLU J CD  1 
ATOM   10880 O  OE1 . GLU J  1 121 ? 5.670  -105.691 -43.195  1.00 47.87  ? 122 GLU J OE1 1 
ATOM   10881 O  OE2 . GLU J  1 121 ? 3.736  -104.685 -42.829  1.00 50.86  ? 122 GLU J OE2 1 
ATOM   10882 N  N   . LYS J  1 122 ? 7.626  -102.078 -45.478  1.00 40.35  ? 123 LYS J N   1 
ATOM   10883 C  CA  . LYS J  1 122 ? 7.991  -100.810 -44.831  1.00 40.72  ? 123 LYS J CA  1 
ATOM   10884 C  C   . LYS J  1 122 ? 9.207  -100.211 -45.519  1.00 38.93  ? 123 LYS J C   1 
ATOM   10885 O  O   . LYS J  1 122 ? 9.725  -100.777 -46.473  1.00 37.55  ? 123 LYS J O   1 
ATOM   10886 C  CB  . LYS J  1 122 ? 8.343  -101.024 -43.356  1.00 42.22  ? 123 LYS J CB  1 
ATOM   10887 C  CG  . LYS J  1 122 ? 7.336  -101.838 -42.540  1.00 44.81  ? 123 LYS J CG  1 
ATOM   10888 C  CD  . LYS J  1 122 ? 7.814  -102.036 -41.082  1.00 46.78  ? 123 LYS J CD  1 
ATOM   10889 C  CE  . LYS J  1 122 ? 6.937  -103.004 -40.300  1.00 49.51  ? 123 LYS J CE  1 
ATOM   10890 N  NZ  . LYS J  1 122 ? 7.214  -102.965 -38.836  1.00 51.85  ? 123 LYS J NZ  1 
ATOM   10891 N  N   . ALA J  1 123 ? 9.665  -99.070  -45.017  1.00 39.39  ? 124 ALA J N   1 
ATOM   10892 C  CA  . ALA J  1 123 ? 10.862 -98.410  -45.533  1.00 38.18  ? 124 ALA J CA  1 
ATOM   10893 C  C   . ALA J  1 123 ? 12.123 -98.995  -44.912  1.00 37.91  ? 124 ALA J C   1 
ATOM   10894 O  O   . ALA J  1 123 ? 12.109 -99.389  -43.751  1.00 38.90  ? 124 ALA J O   1 
ATOM   10895 C  CB  . ALA J  1 123 ? 10.786 -96.929  -45.256  1.00 39.40  ? 124 ALA J CB  1 
ATOM   10896 N  N   . ASP J  1 124 ? 13.196 -99.049  -45.708  1.00 36.93  ? 125 ASP J N   1 
ATOM   10897 C  CA  . ASP J  1 124 ? 14.534 -99.502  -45.271  1.00 37.09  ? 125 ASP J CA  1 
ATOM   10898 C  C   . ASP J  1 124 ? 15.185 -98.395  -44.456  1.00 38.56  ? 125 ASP J C   1 
ATOM   10899 O  O   . ASP J  1 124 ? 15.366 -97.301  -44.957  1.00 38.78  ? 125 ASP J O   1 
ATOM   10900 C  CB  . ASP J  1 124 ? 15.417 -99.872  -46.486  1.00 35.81  ? 125 ASP J CB  1 
ATOM   10901 C  CG  . ASP J  1 124 ? 16.809 -100.411 -46.100  1.00 36.45  ? 125 ASP J CG  1 
ATOM   10902 O  OD1 . ASP J  1 124 ? 17.096 -100.541 -44.897  1.00 37.71  ? 125 ASP J OD1 1 
ATOM   10903 O  OD2 . ASP J  1 124 ? 17.632 -100.701 -47.010  1.00 35.70  ? 125 ASP J OD2 1 
ATOM   10904 N  N   . ASP J  1 125 ? 15.543 -98.687  -43.205  1.00 39.98  ? 126 ASP J N   1 
ATOM   10905 C  CA  . ASP J  1 125 ? 16.122 -97.679  -42.299  1.00 41.74  ? 126 ASP J CA  1 
ATOM   10906 C  C   . ASP J  1 125 ? 17.603 -97.404  -42.572  1.00 42.27  ? 126 ASP J C   1 
ATOM   10907 O  O   . ASP J  1 125 ? 18.238 -96.667  -41.826  1.00 44.04  ? 126 ASP J O   1 
ATOM   10908 C  CB  . ASP J  1 125 ? 15.887 -98.043  -40.820  1.00 43.54  ? 126 ASP J CB  1 
ATOM   10909 C  CG  . ASP J  1 125 ? 16.767 -99.172  -40.322  1.00 44.12  ? 126 ASP J CG  1 
ATOM   10910 O  OD1 . ASP J  1 125 ? 17.875 -99.363  -40.842  1.00 43.98  ? 126 ASP J OD1 1 
ATOM   10911 O  OD2 . ASP J  1 125 ? 16.367 -99.860  -39.364  1.00 45.12  ? 126 ASP J OD2 1 
ATOM   10912 N  N   . LEU J  1 126 ? 18.132 -98.011  -43.640  1.00 40.94  ? 127 LEU J N   1 
ATOM   10913 C  CA  . LEU J  1 126 ? 19.522 -97.845  -44.094  1.00 41.50  ? 127 LEU J CA  1 
ATOM   10914 C  C   . LEU J  1 126 ? 20.562 -98.179  -43.028  1.00 43.56  ? 127 LEU J C   1 
ATOM   10915 O  O   . LEU J  1 126 ? 21.653 -97.618  -43.023  1.00 45.37  ? 127 LEU J O   1 
ATOM   10916 C  CB  . LEU J  1 126 ? 19.751 -96.441  -44.643  1.00 42.15  ? 127 LEU J CB  1 
ATOM   10917 C  CG  . LEU J  1 126 ? 18.728 -95.959  -45.664  1.00 40.83  ? 127 LEU J CG  1 
ATOM   10918 C  CD1 . LEU J  1 126 ? 19.203 -94.665  -46.297  1.00 42.60  ? 127 LEU J CD1 1 
ATOM   10919 C  CD2 . LEU J  1 126 ? 18.478 -96.983  -46.723  1.00 38.93  ? 127 LEU J CD2 1 
ATOM   10920 N  N   . GLY J  1 127 ? 20.215 -99.101  -42.138  1.00 43.86  ? 128 GLY J N   1 
ATOM   10921 C  CA  . GLY J  1 127 ? 21.124 -99.597  -41.117  1.00 46.13  ? 128 GLY J CA  1 
ATOM   10922 C  C   . GLY J  1 127 ? 21.284 -98.723  -39.903  1.00 48.56  ? 128 GLY J C   1 
ATOM   10923 O  O   . GLY J  1 127 ? 21.944 -99.115  -38.955  1.00 50.75  ? 128 GLY J O   1 
ATOM   10924 N  N   . LYS J  1 128 ? 20.665 -97.547  -39.921  1.00 48.52  ? 129 LYS J N   1 
ATOM   10925 C  CA  . LYS J  1 128 ? 20.817 -96.552  -38.846  1.00 51.08  ? 129 LYS J CA  1 
ATOM   10926 C  C   . LYS J  1 128 ? 19.744 -96.710  -37.762  1.00 51.81  ? 129 LYS J C   1 
ATOM   10927 O  O   . LYS J  1 128 ? 19.415 -95.748  -37.047  1.00 53.33  ? 129 LYS J O   1 
ATOM   10928 C  CB  . LYS J  1 128 ? 20.764 -95.123  -39.400  1.00 51.20  ? 129 LYS J CB  1 
ATOM   10929 C  CG  . LYS J  1 128 ? 21.698 -94.851  -40.549  1.00 51.17  ? 129 LYS J CG  1 
ATOM   10930 C  CD  . LYS J  1 128 ? 21.939 -93.355  -40.747  1.00 53.32  ? 129 LYS J CD  1 
ATOM   10931 C  CE  . LYS J  1 128 ? 22.761 -93.077  -42.028  1.00 53.68  ? 129 LYS J CE  1 
ATOM   10932 N  NZ  . LYS J  1 128 ? 23.306 -91.666  -42.068  1.00 56.50  ? 129 LYS J NZ  1 
ATOM   10933 N  N   . GLY J  1 129 ? 19.217 -97.925  -37.631  1.00 51.04  ? 130 GLY J N   1 
ATOM   10934 C  CA  . GLY J  1 129 ? 18.070 -98.190  -36.762  1.00 51.84  ? 130 GLY J CA  1 
ATOM   10935 C  C   . GLY J  1 129 ? 18.419 -98.378  -35.298  1.00 54.98  ? 130 GLY J C   1 
ATOM   10936 O  O   . GLY J  1 129 ? 17.591 -98.165  -34.417  1.00 56.50  ? 130 GLY J O   1 
ATOM   10937 N  N   . GLY J  1 130 ? 19.635 -98.820  -35.034  1.00 56.29  ? 131 GLY J N   1 
ATOM   10938 C  CA  . GLY J  1 130 ? 20.088 -98.994  -33.664  1.00 60.01  ? 131 GLY J CA  1 
ATOM   10939 C  C   . GLY J  1 130 ? 19.812 -100.363 -33.062  1.00 61.38  ? 131 GLY J C   1 
ATOM   10940 O  O   . GLY J  1 130 ? 20.520 -100.831 -32.161  1.00 64.47  ? 131 GLY J O   1 
ATOM   10941 N  N   . ASN J  1 131 ? 18.781 -101.026 -33.555  1.00 59.59  ? 132 ASN J N   1 
ATOM   10942 C  CA  . ASN J  1 131 ? 18.505 -102.405 -33.135  1.00 60.99  ? 132 ASN J CA  1 
ATOM   10943 C  C   . ASN J  1 131 ? 19.293 -103.464 -33.924  1.00 59.89  ? 132 ASN J C   1 
ATOM   10944 O  O   . ASN J  1 131 ? 19.971 -103.185 -34.912  1.00 57.63  ? 132 ASN J O   1 
ATOM   10945 C  CB  . ASN J  1 131 ? 16.997 -102.703 -33.187  1.00 60.28  ? 132 ASN J CB  1 
ATOM   10946 C  CG  . ASN J  1 131 ? 16.518 -103.022 -34.566  1.00 56.87  ? 132 ASN J CG  1 
ATOM   10947 O  OD1 . ASN J  1 131 ? 17.305 -103.019 -35.525  1.00 54.77  ? 132 ASN J OD1 1 
ATOM   10948 N  ND2 . ASN J  1 131 ? 15.211 -103.298 -34.690  1.00 56.72  ? 132 ASN J ND2 1 
ATOM   10949 N  N   . GLU J  1 132 ? 19.175 -104.693 -33.462  1.00 61.93  ? 133 GLU J N   1 
ATOM   10950 C  CA  . GLU J  1 132 ? 19.888 -105.822 -34.050  1.00 62.01  ? 133 GLU J CA  1 
ATOM   10951 C  C   . GLU J  1 132 ? 19.523 -106.008 -35.514  1.00 58.06  ? 133 GLU J C   1 
ATOM   10952 O  O   . GLU J  1 132 ? 20.398 -106.131 -36.379  1.00 56.62  ? 133 GLU J O   1 
ATOM   10953 C  CB  . GLU J  1 132 ? 19.569 -107.110 -33.253  1.00 65.37  ? 133 GLU J CB  1 
ATOM   10954 C  CG  . GLU J  1 132 ? 19.948 -108.446 -33.964  1.00 65.85  ? 133 GLU J CG  1 
ATOM   10955 C  CD  . GLU J  1 132 ? 21.433 -108.828 -33.876  1.00 68.33  ? 133 GLU J CD  1 
ATOM   10956 O  OE1 . GLU J  1 132 ? 22.242 -108.076 -33.274  1.00 70.09  ? 133 GLU J OE1 1 
ATOM   10957 O  OE2 . GLU J  1 132 ? 21.780 -109.901 -34.427  1.00 68.58  ? 133 GLU J OE2 1 
ATOM   10958 N  N   . GLU J  1 133 ? 18.216 -106.048 -35.751  1.00 56.64  ? 134 GLU J N   1 
ATOM   10959 C  CA  . GLU J  1 133 ? 17.646 -106.399 -37.049  1.00 53.54  ? 134 GLU J CA  1 
ATOM   10960 C  C   . GLU J  1 133 ? 17.967 -105.367 -38.123  1.00 50.31  ? 134 GLU J C   1 
ATOM   10961 O  O   . GLU J  1 133 ? 18.034 -105.715 -39.286  1.00 48.21  ? 134 GLU J O   1 
ATOM   10962 C  CB  . GLU J  1 133 ? 16.116 -106.577 -36.927  1.00 53.72  ? 134 GLU J CB  1 
ATOM   10963 C  CG  . GLU J  1 133 ? 15.428 -107.323 -38.096  1.00 51.94  ? 134 GLU J CG  1 
ATOM   10964 C  CD  . GLU J  1 133 ? 15.755 -108.832 -38.148  1.00 53.97  ? 134 GLU J CD  1 
ATOM   10965 O  OE1 . GLU J  1 133 ? 16.388 -109.368 -37.195  1.00 57.20  ? 134 GLU J OE1 1 
ATOM   10966 O  OE2 . GLU J  1 133 ? 15.378 -109.482 -39.156  1.00 52.36  ? 134 GLU J OE2 1 
ATOM   10967 N  N   . SER J  1 134 ? 18.160 -104.105 -37.738  1.00 50.38  ? 135 SER J N   1 
ATOM   10968 C  CA  . SER J  1 134 ? 18.452 -103.035 -38.708  1.00 48.03  ? 135 SER J CA  1 
ATOM   10969 C  C   . SER J  1 134 ? 19.753 -103.286 -39.446  1.00 47.73  ? 135 SER J C   1 
ATOM   10970 O  O   . SER J  1 134 ? 19.925 -102.853 -40.579  1.00 45.55  ? 135 SER J O   1 
ATOM   10971 C  CB  . SER J  1 134 ? 18.542 -101.687 -38.025  1.00 49.11  ? 135 SER J CB  1 
ATOM   10972 O  OG  . SER J  1 134 ? 19.058 -100.732 -38.934  1.00 47.45  ? 135 SER J OG  1 
ATOM   10973 N  N   . THR J  1 135 ? 20.666 -103.982 -38.762  1.00 50.38  ? 136 THR J N   1 
ATOM   10974 C  CA  . THR J  1 135 ? 21.971 -104.404 -39.294  1.00 50.77  ? 136 THR J CA  1 
ATOM   10975 C  C   . THR J  1 135 ? 21.872 -105.555 -40.295  1.00 49.40  ? 136 THR J C   1 
ATOM   10976 O  O   . THR J  1 135 ? 22.827 -105.843 -40.995  1.00 49.64  ? 136 THR J O   1 
ATOM   10977 C  CB  . THR J  1 135 ? 22.887 -104.788 -38.124  1.00 54.33  ? 136 THR J CB  1 
ATOM   10978 O  OG1 . THR J  1 135 ? 23.409 -103.582 -37.564  1.00 55.61  ? 136 THR J OG1 1 
ATOM   10979 C  CG2 . THR J  1 135 ? 24.011 -105.676 -38.550  1.00 55.62  ? 136 THR J CG2 1 
ATOM   10980 N  N   . LYS J  1 136 ? 20.706 -106.180 -40.388  1.00 48.44  ? 137 LYS J N   1 
ATOM   10981 C  CA  . LYS J  1 136 ? 20.485 -107.327 -41.270  1.00 47.54  ? 137 LYS J CA  1 
ATOM   10982 C  C   . LYS J  1 136 ? 19.507 -107.020 -42.417  1.00 44.40  ? 137 LYS J C   1 
ATOM   10983 O  O   . LYS J  1 136 ? 19.869 -107.012 -43.597  1.00 42.79  ? 137 LYS J O   1 
ATOM   10984 C  CB  . LYS J  1 136 ? 19.927 -108.494 -40.461  1.00 49.75  ? 137 LYS J CB  1 
ATOM   10985 C  CG  . LYS J  1 136 ? 20.923 -109.188 -39.543  1.00 53.65  ? 137 LYS J CG  1 
ATOM   10986 C  CD  . LYS J  1 136 ? 20.224 -110.350 -38.784  1.00 56.60  ? 137 LYS J CD  1 
ATOM   10987 C  CE  . LYS J  1 136 ? 21.210 -111.428 -38.264  1.00 60.14  ? 137 LYS J CE  1 
ATOM   10988 N  NZ  . LYS J  1 136 ? 21.707 -111.130 -36.879  1.00 63.47  ? 137 LYS J NZ  1 
ATOM   10989 N  N   . THR J  1 137 ? 18.261 -106.767 -42.050  1.00 43.88  ? 138 THR J N   1 
ATOM   10990 C  CA  . THR J  1 137 ? 17.183 -106.638 -43.011  1.00 41.71  ? 138 THR J CA  1 
ATOM   10991 C  C   . THR J  1 137 ? 16.852 -105.192 -43.330  1.00 40.31  ? 138 THR J C   1 
ATOM   10992 O  O   . THR J  1 137 ? 16.162 -104.915 -44.305  1.00 38.66  ? 138 THR J O   1 
ATOM   10993 C  CB  . THR J  1 137 ? 15.916 -107.293 -42.483  1.00 42.72  ? 138 THR J CB  1 
ATOM   10994 O  OG1 . THR J  1 137 ? 15.400 -106.529 -41.396  1.00 43.85  ? 138 THR J OG1 1 
ATOM   10995 C  CG2 . THR J  1 137 ? 16.207 -108.662 -41.987  1.00 45.28  ? 138 THR J CG2 1 
ATOM   10996 N  N   . GLY J  1 138 ? 17.333 -104.272 -42.501  1.00 41.39  ? 139 GLY J N   1 
ATOM   10997 C  CA  . GLY J  1 138 ? 16.994 -102.849 -42.614  1.00 40.63  ? 139 GLY J CA  1 
ATOM   10998 C  C   . GLY J  1 138 ? 15.660 -102.490 -41.974  1.00 41.11  ? 139 GLY J C   1 
ATOM   10999 O  O   . GLY J  1 138 ? 15.202 -101.372 -42.099  1.00 40.72  ? 139 GLY J O   1 
ATOM   11000 N  N   . ASN J  1 139 ? 15.058 -103.440 -41.266  1.00 42.49  ? 140 ASN J N   1 
ATOM   11001 C  CA  . ASN J  1 139 ? 13.729 -103.289 -40.664  1.00 43.59  ? 140 ASN J CA  1 
ATOM   11002 C  C   . ASN J  1 139 ? 12.664 -102.908 -41.677  1.00 41.98  ? 140 ASN J C   1 
ATOM   11003 O  O   . ASN J  1 139 ? 11.671 -102.312 -41.325  1.00 42.86  ? 140 ASN J O   1 
ATOM   11004 C  CB  . ASN J  1 139 ? 13.752 -102.274 -39.506  1.00 45.51  ? 140 ASN J CB  1 
ATOM   11005 C  CG  . ASN J  1 139 ? 14.271 -102.863 -38.189  1.00 48.03  ? 140 ASN J CG  1 
ATOM   11006 O  OD1 . ASN J  1 139 ? 14.841 -102.135 -37.375  1.00 49.39  ? 140 ASN J OD1 1 
ATOM   11007 N  ND2 . ASN J  1 139 ? 14.050 -104.163 -37.967  1.00 48.66  ? 140 ASN J ND2 1 
ATOM   11008 N  N   . ALA J  1 140 ? 12.869 -103.289 -42.929  1.00 40.13  ? 141 ALA J N   1 
ATOM   11009 C  CA  . ALA J  1 140 ? 11.975 -102.911 -44.030  1.00 38.82  ? 141 ALA J CA  1 
ATOM   11010 C  C   . ALA J  1 140 ? 10.784 -103.832 -44.183  1.00 39.49  ? 141 ALA J C   1 
ATOM   11011 O  O   . ALA J  1 140 ? 9.977  -103.637 -45.082  1.00 38.72  ? 141 ALA J O   1 
ATOM   11012 C  CB  . ALA J  1 140 ? 12.725 -102.881 -45.320  1.00 36.96  ? 141 ALA J CB  1 
ATOM   11013 N  N   . GLY J  1 141 ? 10.697 -104.850 -43.333  1.00 41.27  ? 142 GLY J N   1 
ATOM   11014 C  CA  . GLY J  1 141 ? 9.477  -105.651 -43.202  1.00 42.89  ? 142 GLY J CA  1 
ATOM   11015 C  C   . GLY J  1 141 ? 9.270  -106.697 -44.275  1.00 42.14  ? 142 GLY J C   1 
ATOM   11016 O  O   . GLY J  1 141 ? 10.214 -107.109 -44.924  1.00 40.77  ? 142 GLY J O   1 
ATOM   11017 N  N   . SER J  1 142 ? 8.020  -107.112 -44.452  1.00 43.49  ? 143 SER J N   1 
ATOM   11018 C  CA  . SER J  1 142 ? 7.677  -108.266 -45.291  1.00 43.77  ? 143 SER J CA  1 
ATOM   11019 C  C   . SER J  1 142 ? 7.930  -108.023 -46.765  1.00 41.33  ? 143 SER J C   1 
ATOM   11020 O  O   . SER J  1 142 ? 8.202  -106.897 -47.177  1.00 39.78  ? 143 SER J O   1 
ATOM   11021 C  CB  . SER J  1 142 ? 6.213  -108.681 -45.089  1.00 46.48  ? 143 SER J CB  1 
ATOM   11022 O  OG  . SER J  1 142 ? 5.308  -107.818 -45.754  1.00 46.11  ? 143 SER J OG  1 
ATOM   11023 N  N   . ARG J  1 143 ? 7.830  -109.092 -47.553  1.00 41.38  ? 144 ARG J N   1 
ATOM   11024 C  CA  . ARG J  1 143 ? 8.107  -109.040 -48.990  1.00 39.46  ? 144 ARG J CA  1 
ATOM   11025 C  C   . ARG J  1 143 ? 6.834  -108.970 -49.815  1.00 40.09  ? 144 ARG J C   1 
ATOM   11026 O  O   . ARG J  1 143 ? 6.139  -109.950 -49.994  1.00 41.92  ? 144 ARG J O   1 
ATOM   11027 C  CB  . ARG J  1 143 ? 8.935  -110.250 -49.397  1.00 39.52  ? 144 ARG J CB  1 
ATOM   11028 C  CG  . ARG J  1 143 ? 10.275 -110.307 -48.676  1.00 39.26  ? 144 ARG J CG  1 
ATOM   11029 C  CD  . ARG J  1 143 ? 11.037 -111.593 -48.928  1.00 40.04  ? 144 ARG J CD  1 
ATOM   11030 N  NE  . ARG J  1 143 ? 12.213 -111.693 -48.076  1.00 40.20  ? 144 ARG J NE  1 
ATOM   11031 C  CZ  . ARG J  1 143 ? 13.104 -112.672 -48.145  1.00 41.35  ? 144 ARG J CZ  1 
ATOM   11032 N  NH1 . ARG J  1 143 ? 12.970 -113.655 -49.026  1.00 42.08  ? 144 ARG J NH1 1 
ATOM   11033 N  NH2 . ARG J  1 143 ? 14.141 -112.671 -47.325  1.00 42.60  ? 144 ARG J NH2 1 
ATOM   11034 N  N   . LEU J  1 144 ? 6.549  -107.795 -50.336  1.00 39.09  ? 145 LEU J N   1 
ATOM   11035 C  CA  . LEU J  1 144 ? 5.287  -107.546 -51.009  1.00 40.32  ? 145 LEU J CA  1 
ATOM   11036 C  C   . LEU J  1 144 ? 5.257  -108.166 -52.379  1.00 39.91  ? 145 LEU J C   1 
ATOM   11037 O  O   . LEU J  1 144 ? 4.310  -108.858 -52.718  1.00 41.92  ? 145 LEU J O   1 
ATOM   11038 C  CB  . LEU J  1 144 ? 5.021  -106.047 -51.141  1.00 39.87  ? 145 LEU J CB  1 
ATOM   11039 C  CG  . LEU J  1 144 ? 4.731  -105.289 -49.855  1.00 40.96  ? 145 LEU J CG  1 
ATOM   11040 C  CD1 . LEU J  1 144 ? 4.314  -103.856 -50.195  1.00 41.01  ? 145 LEU J CD1 1 
ATOM   11041 C  CD2 . LEU J  1 144 ? 3.678  -105.986 -49.023  1.00 43.72  ? 145 LEU J CD2 1 
ATOM   11042 N  N   . ALA J  1 145 ? 6.276  -107.879 -53.173  1.00 37.76  ? 146 ALA J N   1 
ATOM   11043 C  CA  . ALA J  1 145 ? 6.346  -108.362 -54.545  1.00 37.60  ? 146 ALA J CA  1 
ATOM   11044 C  C   . ALA J  1 145 ? 7.779  -108.597 -54.934  1.00 35.93  ? 146 ALA J C   1 
ATOM   11045 O  O   . ALA J  1 145 ? 8.637  -107.858 -54.515  1.00 34.99  ? 146 ALA J O   1 
ATOM   11046 C  CB  . ALA J  1 145 ? 5.726  -107.359 -55.495  1.00 37.76  ? 146 ALA J CB  1 
ATOM   11047 N  N   . CYS J  1 146 ? 8.031  -109.608 -55.758  1.00 36.14  ? 147 CYS J N   1 
ATOM   11048 C  CA  . CYS J  1 146 ? 9.385  -109.943 -56.175  1.00 34.88  ? 147 CYS J CA  1 
ATOM   11049 C  C   . CYS J  1 146 ? 9.425  -110.643 -57.508  1.00 35.44  ? 147 CYS J C   1 
ATOM   11050 O  O   . CYS J  1 146 ? 8.416  -111.061 -58.017  1.00 37.03  ? 147 CYS J O   1 
ATOM   11051 C  CB  . CYS J  1 146 ? 10.030 -110.836 -55.140  1.00 35.33  ? 147 CYS J CB  1 
ATOM   11052 S  SG  . CYS J  1 146 ? 9.252  -112.409 -54.939  1.00 37.20  ? 147 CYS J SG  1 
ATOM   11053 N  N   . GLY J  1 147 ? 10.611 -110.773 -58.070  1.00 34.76  ? 148 GLY J N   1 
ATOM   11054 C  CA  . GLY J  1 147 ? 10.783 -111.427 -59.360  1.00 35.53  ? 148 GLY J CA  1 
ATOM   11055 C  C   . GLY J  1 147 ? 12.225 -111.730 -59.642  1.00 35.11  ? 148 GLY J C   1 
ATOM   11056 O  O   . GLY J  1 147 ? 13.088 -111.028 -59.155  1.00 34.20  ? 148 GLY J O   1 
ATOM   11057 N  N   . VAL J  1 148 ? 12.485 -112.774 -60.425  1.00 36.25  ? 149 VAL J N   1 
ATOM   11058 C  CA  . VAL J  1 148 ? 13.863 -113.177 -60.767  1.00 36.35  ? 149 VAL J CA  1 
ATOM   11059 C  C   . VAL J  1 148 ? 14.440 -112.306 -61.865  1.00 35.90  ? 149 VAL J C   1 
ATOM   11060 O  O   . VAL J  1 148 ? 13.765 -112.007 -62.834  1.00 36.24  ? 149 VAL J O   1 
ATOM   11061 C  CB  . VAL J  1 148 ? 13.938 -114.624 -61.216  1.00 38.04  ? 149 VAL J CB  1 
ATOM   11062 C  CG1 . VAL J  1 148 ? 15.347 -114.969 -61.567  1.00 38.50  ? 149 VAL J CG1 1 
ATOM   11063 C  CG2 . VAL J  1 148 ? 13.430 -115.521 -60.123  1.00 39.10  ? 149 VAL J CG2 1 
ATOM   11064 N  N   . ILE J  1 149 ? 15.686 -111.888 -61.690  1.00 35.64  ? 150 ILE J N   1 
ATOM   11065 C  CA  . ILE J  1 149 ? 16.325 -110.939 -62.607  1.00 35.82  ? 150 ILE J CA  1 
ATOM   11066 C  C   . ILE J  1 149 ? 16.832 -111.682 -63.812  1.00 37.33  ? 150 ILE J C   1 
ATOM   11067 O  O   . ILE J  1 149 ? 17.565 -112.640 -63.674  1.00 38.34  ? 150 ILE J O   1 
ATOM   11068 C  CB  . ILE J  1 149 ? 17.515 -110.193 -61.959  1.00 35.49  ? 150 ILE J CB  1 
ATOM   11069 C  CG1 . ILE J  1 149 ? 17.033 -109.220 -60.885  1.00 34.06  ? 150 ILE J CG1 1 
ATOM   11070 C  CG2 . ILE J  1 149 ? 18.286 -109.436 -63.014  1.00 36.30  ? 150 ILE J CG2 1 
ATOM   11071 C  CD1 . ILE J  1 149 ? 18.133 -108.672 -60.065  1.00 33.98  ? 150 ILE J CD1 1 
ATOM   11072 N  N   . GLY J  1 150 ? 16.453 -111.231 -64.995  1.00 37.99  ? 151 GLY J N   1 
ATOM   11073 C  CA  . GLY J  1 150 ? 16.726 -111.984 -66.215  1.00 39.90  ? 151 GLY J CA  1 
ATOM   11074 C  C   . GLY J  1 150 ? 17.440 -111.205 -67.281  1.00 40.97  ? 151 GLY J C   1 
ATOM   11075 O  O   . GLY J  1 150 ? 17.358 -109.991 -67.312  1.00 40.65  ? 151 GLY J O   1 
ATOM   11076 N  N   . ILE J  1 151 ? 18.128 -111.919 -68.160  1.00 42.77  ? 152 ILE J N   1 
ATOM   11077 C  CA  . ILE J  1 151 ? 18.860 -111.291 -69.243  1.00 44.61  ? 152 ILE J CA  1 
ATOM   11078 C  C   . ILE J  1 151 ? 17.888 -110.776 -70.270  1.00 45.50  ? 152 ILE J C   1 
ATOM   11079 O  O   . ILE J  1 151 ? 17.015 -111.498 -70.681  1.00 46.14  ? 152 ILE J O   1 
ATOM   11080 C  CB  . ILE J  1 151 ? 19.783 -112.262 -69.943  1.00 46.89  ? 152 ILE J CB  1 
ATOM   11081 C  CG1 . ILE J  1 151 ? 20.844 -112.772 -68.972  1.00 46.92  ? 152 ILE J CG1 1 
ATOM   11082 C  CG2 . ILE J  1 151 ? 20.452 -111.585 -71.104  1.00 49.15  ? 152 ILE J CG2 1 
ATOM   11083 C  CD1 . ILE J  1 151 ? 21.828 -113.771 -69.583  1.00 49.62  ? 152 ILE J CD1 1 
ATOM   11084 N  N   . ALA J  1 152 ? 18.056 -109.532 -70.699  1.00 46.25  ? 153 ALA J N   1 
ATOM   11085 C  CA  . ALA J  1 152 ? 17.110 -108.863 -71.603  1.00 47.30  ? 153 ALA J CA  1 
ATOM   11086 C  C   . ALA J  1 152 ? 17.755 -108.476 -72.934  1.00 50.51  ? 153 ALA J C   1 
ATOM   11087 O  O   . ALA J  1 152 ? 18.977 -108.372 -73.046  1.00 51.62  ? 153 ALA J O   1 
ATOM   11088 C  CB  . ALA J  1 152 ? 16.553 -107.640 -70.940  1.00 46.13  ? 153 ALA J CB  1 
ATOM   11089 N  N   . GLN J  1 153 ? 16.918 -108.240 -73.940  1.00 52.44  ? 154 GLN J N   1 
ATOM   11090 C  CA  . GLN J  1 153 ? 17.407 -107.920 -75.289  1.00 56.14  ? 154 GLN J CA  1 
ATOM   11091 C  C   . GLN J  1 153 ? 17.931 -106.501 -75.363  1.00 57.33  ? 154 GLN J C   1 
ATOM   11092 O  O   . GLN J  1 153 ? 17.280 -105.585 -74.873  1.00 56.32  ? 154 GLN J O   1 
ATOM   11093 C  CB  . GLN J  1 153 ? 16.320 -108.118 -76.359  1.00 58.21  ? 154 GLN J CB  1 
ATOM   11094 C  CG  . GLN J  1 153 ? 16.839 -107.871 -77.798  1.00 62.53  ? 154 GLN J CG  1 
ATOM   11095 C  CD  . GLN J  1 153 ? 15.802 -108.172 -78.891  1.00 65.12  ? 154 GLN J CD  1 
ATOM   11096 O  OE1 . GLN J  1 153 ? 15.361 -109.303 -79.046  1.00 65.18  ? 154 GLN J OE1 1 
ATOM   11097 N  NE2 . GLN J  1 153 ? 15.427 -107.152 -79.662  1.00 67.62  ? 154 GLN J NE2 1 
ATOM   11098 O  OXT . GLN J  1 153 ? 18.991 -106.252 -75.936  1.00 59.79  ? 154 GLN J OXT 1 
ATOM   11099 N  N   . ALA K  1 1   ? 38.767 -80.164  -9.402   1.00 91.03  ? 2   ALA K N   1 
ATOM   11100 C  CA  . ALA K  1 1   ? 38.199 -80.742  -8.136   1.00 90.13  ? 2   ALA K CA  1 
ATOM   11101 C  C   . ALA K  1 1   ? 37.164 -81.887  -8.415   1.00 85.30  ? 2   ALA K C   1 
ATOM   11102 O  O   . ALA K  1 1   ? 35.994 -81.608  -8.727   1.00 83.83  ? 2   ALA K O   1 
ATOM   11103 C  CB  . ALA K  1 1   ? 37.581 -79.592  -7.264   1.00 92.45  ? 2   ALA K CB  1 
ATOM   11104 N  N   . THR K  1 2   ? 37.576 -83.160  -8.296   1.00 83.22  ? 3   THR K N   1 
ATOM   11105 C  CA  . THR K  1 2   ? 36.673 -84.272  -8.697   1.00 79.21  ? 3   THR K CA  1 
ATOM   11106 C  C   . THR K  1 2   ? 35.549 -84.421  -7.683   1.00 78.04  ? 3   THR K C   1 
ATOM   11107 O  O   . THR K  1 2   ? 35.773 -84.356  -6.473   1.00 79.88  ? 3   THR K O   1 
ATOM   11108 C  CB  . THR K  1 2   ? 37.371 -85.666  -8.866   1.00 78.52  ? 3   THR K CB  1 
ATOM   11109 O  OG1 . THR K  1 2   ? 38.764 -85.483  -9.124   1.00 81.52  ? 3   THR K OG1 1 
ATOM   11110 C  CG2 . THR K  1 2   ? 36.723 -86.492  -10.019  1.00 75.20  ? 3   THR K CG2 1 
ATOM   11111 N  N   . LYS K  1 3   ? 34.341 -84.608  -8.203   1.00 75.43  ? 4   LYS K N   1 
ATOM   11112 C  CA  . LYS K  1 3   ? 33.160 -84.852  -7.387   1.00 74.51  ? 4   LYS K CA  1 
ATOM   11113 C  C   . LYS K  1 3   ? 32.398 -86.065  -7.915   1.00 71.59  ? 4   LYS K C   1 
ATOM   11114 O  O   . LYS K  1 3   ? 32.397 -86.357  -9.115   1.00 70.18  ? 4   LYS K O   1 
ATOM   11115 C  CB  . LYS K  1 3   ? 32.230 -83.637  -7.382   1.00 75.33  ? 4   LYS K CB  1 
ATOM   11116 C  CG  . LYS K  1 3   ? 32.805 -82.381  -6.720   1.00 79.08  ? 4   LYS K CG  1 
ATOM   11117 C  CD  . LYS K  1 3   ? 31.721 -81.303  -6.537   1.00 80.49  ? 4   LYS K CD  1 
ATOM   11118 C  CE  . LYS K  1 3   ? 32.302 -79.882  -6.484   1.00 84.12  ? 4   LYS K CE  1 
ATOM   11119 N  NZ  . LYS K  1 3   ? 31.295 -78.846  -6.894   1.00 84.88  ? 4   LYS K NZ  1 
ATOM   11120 N  N   . ALA K  1 4   ? 31.762 -86.776  -6.994   1.00 71.20  ? 5   ALA K N   1 
ATOM   11121 C  CA  . ALA K  1 4   ? 30.867 -87.875  -7.344   1.00 69.12  ? 5   ALA K CA  1 
ATOM   11122 C  C   . ALA K  1 4   ? 29.616 -87.808  -6.483   1.00 69.22  ? 5   ALA K C   1 
ATOM   11123 O  O   . ALA K  1 4   ? 29.579 -87.072  -5.498   1.00 71.07  ? 5   ALA K O   1 
ATOM   11124 C  CB  . ALA K  1 4   ? 31.560 -89.218  -7.163   1.00 68.99  ? 5   ALA K CB  1 
ATOM   11125 N  N   . VAL K  1 5   ? 28.591 -88.559  -6.877   1.00 67.75  ? 6   VAL K N   1 
ATOM   11126 C  CA  . VAL K  1 5   ? 27.320 -88.625  -6.133   1.00 68.19  ? 6   VAL K CA  1 
ATOM   11127 C  C   . VAL K  1 5   ? 26.675 -89.990  -6.307   1.00 67.16  ? 6   VAL K C   1 
ATOM   11128 O  O   . VAL K  1 5   ? 26.956 -90.700  -7.275   1.00 66.04  ? 6   VAL K O   1 
ATOM   11129 C  CB  . VAL K  1 5   ? 26.315 -87.526  -6.563   1.00 68.52  ? 6   VAL K CB  1 
ATOM   11130 C  CG1 . VAL K  1 5   ? 25.627 -87.890  -7.852   1.00 67.48  ? 6   VAL K CG1 1 
ATOM   11131 C  CG2 . VAL K  1 5   ? 25.277 -87.314  -5.504   1.00 70.11  ? 6   VAL K CG2 1 
ATOM   11132 N  N   . CYS K  1 6   ? 25.837 -90.363  -5.349   1.00 68.14  ? 7   CYS K N   1 
ATOM   11133 C  CA  . CYS K  1 6   ? 25.155 -91.662  -5.372   1.00 68.11  ? 7   CYS K CA  1 
ATOM   11134 C  C   . CYS K  1 6   ? 23.800 -91.618  -4.683   1.00 69.44  ? 7   CYS K C   1 
ATOM   11135 O  O   . CYS K  1 6   ? 23.708 -91.252  -3.506   1.00 71.02  ? 7   CYS K O   1 
ATOM   11136 C  CB  . CYS K  1 6   ? 25.996 -92.757  -4.693   1.00 68.88  ? 7   CYS K CB  1 
ATOM   11137 S  SG  . CYS K  1 6   ? 25.123 -94.381  -4.442   1.00 69.37  ? 7   CYS K SG  1 
ATOM   11138 N  N   . VAL K  1 7   ? 22.766 -92.028  -5.421   1.00 69.18  ? 8   VAL K N   1 
ATOM   11139 C  CA  . VAL K  1 7   ? 21.413 -92.129  -4.886   1.00 70.74  ? 8   VAL K CA  1 
ATOM   11140 C  C   . VAL K  1 7   ? 21.174 -93.554  -4.392   1.00 71.60  ? 8   VAL K C   1 
ATOM   11141 O  O   . VAL K  1 7   ? 21.062 -94.507  -5.178   1.00 70.90  ? 8   VAL K O   1 
ATOM   11142 C  CB  . VAL K  1 7   ? 20.343 -91.719  -5.928   1.00 70.87  ? 8   VAL K CB  1 
ATOM   11143 C  CG1 . VAL K  1 7   ? 18.915 -91.997  -5.411   1.00 72.99  ? 8   VAL K CG1 1 
ATOM   11144 C  CG2 . VAL K  1 7   ? 20.504 -90.237  -6.296   1.00 70.72  ? 8   VAL K CG2 1 
ATOM   11145 N  N   . LEU K  1 8   ? 21.120 -93.674  -3.067   1.00 73.42  ? 9   LEU K N   1 
ATOM   11146 C  CA  . LEU K  1 8   ? 20.844 -94.944  -2.400   1.00 75.05  ? 9   LEU K CA  1 
ATOM   11147 C  C   . LEU K  1 8   ? 19.343 -95.238  -2.423   1.00 76.71  ? 9   LEU K C   1 
ATOM   11148 O  O   . LEU K  1 8   ? 18.541 -94.392  -2.018   1.00 78.03  ? 9   LEU K O   1 
ATOM   11149 C  CB  . LEU K  1 8   ? 21.335 -94.901  -0.952   1.00 76.80  ? 9   LEU K CB  1 
ATOM   11150 C  CG  . LEU K  1 8   ? 22.852 -94.908  -0.801   1.00 76.03  ? 9   LEU K CG  1 
ATOM   11151 C  CD1 . LEU K  1 8   ? 23.225 -94.426  0.571    1.00 78.15  ? 9   LEU K CD1 1 
ATOM   11152 C  CD2 . LEU K  1 8   ? 23.422 -96.291  -1.072   1.00 76.15  ? 9   LEU K CD2 1 
ATOM   11153 N  N   . LYS K  1 9   ? 18.975 -96.426  -2.907   1.00 77.15  ? 10  LYS K N   1 
ATOM   11154 C  CA  . LYS K  1 9   ? 17.570 -96.867  -2.950   1.00 79.33  ? 10  LYS K CA  1 
ATOM   11155 C  C   . LYS K  1 9   ? 17.481 -98.367  -2.769   1.00 81.14  ? 10  LYS K C   1 
ATOM   11156 O  O   . LYS K  1 9   ? 18.456 -99.092  -3.000   1.00 80.57  ? 10  LYS K O   1 
ATOM   11157 C  CB  . LYS K  1 9   ? 16.913 -96.516  -4.287   1.00 78.64  ? 10  LYS K CB  1 
ATOM   11158 C  CG  . LYS K  1 9   ? 16.360 -95.111  -4.382   1.00 79.13  ? 10  LYS K CG  1 
ATOM   11159 C  CD  . LYS K  1 9   ? 15.229 -95.026  -5.421   1.00 80.57  ? 10  LYS K CD  1 
ATOM   11160 C  CE  . LYS K  1 9   ? 14.888 -93.548  -5.792   1.00 80.50  ? 10  LYS K CE  1 
ATOM   11161 N  NZ  . LYS K  1 9   ? 14.011 -92.833  -4.785   1.00 83.10  ? 10  LYS K NZ  1 
ATOM   11162 N  N   . GLY K  1 10  ? 16.299 -98.842  -2.397   1.00 83.98  ? 11  GLY K N   1 
ATOM   11163 C  CA  . GLY K  1 10  ? 16.109 -100.275 -2.174   1.00 86.45  ? 11  GLY K CA  1 
ATOM   11164 C  C   . GLY K  1 10  ? 14.673 -100.739 -2.127   1.00 89.84  ? 11  GLY K C   1 
ATOM   11165 O  O   . GLY K  1 10  ? 13.744 -99.952  -2.332   1.00 90.43  ? 11  GLY K O   1 
ATOM   11166 N  N   . ASP K  1 11  ? 14.504 -102.028 -1.833   1.00 92.65  ? 12  ASP K N   1 
ATOM   11167 C  CA  . ASP K  1 11  ? 13.174 -102.674 -1.780   1.00 96.61  ? 12  ASP K CA  1 
ATOM   11168 C  C   . ASP K  1 11  ? 12.252 -102.093 -0.707   1.00 99.06  ? 12  ASP K C   1 
ATOM   11169 O  O   . ASP K  1 11  ? 11.033 -102.011 -0.903   1.00 101.57 ? 12  ASP K O   1 
ATOM   11170 C  CB  . ASP K  1 11  ? 13.307 -104.192 -1.573   1.00 99.57  ? 12  ASP K CB  1 
ATOM   11171 C  CG  . ASP K  1 11  ? 13.371 -104.952 -2.885   1.00 99.94  ? 12  ASP K CG  1 
ATOM   11172 O  OD1 . ASP K  1 11  ? 12.548 -104.666 -3.779   1.00 100.65 ? 12  ASP K OD1 1 
ATOM   11173 O  OD2 . ASP K  1 11  ? 14.240 -105.834 -3.035   1.00 100.60 ? 12  ASP K OD2 1 
ATOM   11174 N  N   . GLY K  1 12  ? 12.848 -101.677 0.411    1.00 98.75  ? 13  GLY K N   1 
ATOM   11175 C  CA  . GLY K  1 12  ? 12.097 -101.142 1.553    1.00 101.48 ? 13  GLY K CA  1 
ATOM   11176 C  C   . GLY K  1 12  ? 12.230 -99.632  1.711    1.00 99.44  ? 13  GLY K C   1 
ATOM   11177 O  O   . GLY K  1 12  ? 12.602 -98.924  0.757    1.00 96.14  ? 13  GLY K O   1 
ATOM   11178 N  N   . PRO K  1 13  ? 11.958 -99.131  2.929    1.00 101.76 ? 14  PRO K N   1 
ATOM   11179 C  CA  . PRO K  1 13  ? 11.821 -97.691  3.173    1.00 101.35 ? 14  PRO K CA  1 
ATOM   11180 C  C   . PRO K  1 13  ? 13.152 -96.930  3.161    1.00 97.81  ? 14  PRO K C   1 
ATOM   11181 O  O   . PRO K  1 13  ? 13.154 -95.691  3.066    1.00 96.96  ? 14  PRO K O   1 
ATOM   11182 C  CB  . PRO K  1 13  ? 11.218 -97.646  4.579    1.00 105.88 ? 14  PRO K CB  1 
ATOM   11183 C  CG  . PRO K  1 13  ? 11.811 -98.860  5.265    1.00 106.89 ? 14  PRO K CG  1 
ATOM   11184 C  CD  . PRO K  1 13  ? 12.036 -99.898  4.188    1.00 104.95 ? 14  PRO K CD  1 
ATOM   11185 N  N   . VAL K  1 14  ? 14.258 -97.672  3.264    1.00 96.30  ? 15  VAL K N   1 
ATOM   11186 C  CA  . VAL K  1 14  ? 15.590 -97.076  3.332    1.00 93.55  ? 15  VAL K CA  1 
ATOM   11187 C  C   . VAL K  1 14  ? 15.937 -96.400  2.009    1.00 89.77  ? 15  VAL K C   1 
ATOM   11188 O  O   . VAL K  1 14  ? 15.914 -97.040  0.944    1.00 88.21  ? 15  VAL K O   1 
ATOM   11189 C  CB  . VAL K  1 14  ? 16.695 -98.106  3.652    1.00 93.33  ? 15  VAL K CB  1 
ATOM   11190 C  CG1 . VAL K  1 14  ? 18.026 -97.388  3.843    1.00 91.28  ? 15  VAL K CG1 1 
ATOM   11191 C  CG2 . VAL K  1 14  ? 16.346 -98.913  4.898    1.00 97.63  ? 15  VAL K CG2 1 
ATOM   11192 N  N   . GLN K  1 15  ? 16.233 -95.102  2.098    1.00 88.74  ? 16  GLN K N   1 
ATOM   11193 C  CA  . GLN K  1 15  ? 16.662 -94.312  0.952    1.00 85.58  ? 16  GLN K CA  1 
ATOM   11194 C  C   . GLN K  1 15  ? 17.477 -93.099  1.386    1.00 85.05  ? 16  GLN K C   1 
ATOM   11195 O  O   . GLN K  1 15  ? 17.414 -92.660  2.540    1.00 87.52  ? 16  GLN K O   1 
ATOM   11196 C  CB  . GLN K  1 15  ? 15.470 -93.869  0.100    1.00 86.07  ? 16  GLN K CB  1 
ATOM   11197 C  CG  . GLN K  1 15  ? 14.375 -93.142  0.857    1.00 89.82  ? 16  GLN K CG  1 
ATOM   11198 C  CD  . GLN K  1 15  ? 13.313 -92.539  -0.071   1.00 91.04  ? 16  GLN K CD  1 
ATOM   11199 O  OE1 . GLN K  1 15  ? 12.654 -91.537  0.279    1.00 93.66  ? 16  GLN K OE1 1 
ATOM   11200 N  NE2 . GLN K  1 15  ? 13.140 -93.144  -1.260   1.00 89.35  ? 16  GLN K NE2 1 
ATOM   11201 N  N   . GLY K  1 16  ? 18.248 -92.568  0.440    1.00 82.27  ? 17  GLY K N   1 
ATOM   11202 C  CA  . GLY K  1 16  ? 19.144 -91.449  0.710    1.00 81.81  ? 17  GLY K CA  1 
ATOM   11203 C  C   . GLY K  1 16  ? 20.016 -91.020  -0.461   1.00 78.78  ? 17  GLY K C   1 
ATOM   11204 O  O   . GLY K  1 16  ? 20.009 -91.632  -1.543   1.00 76.60  ? 17  GLY K O   1 
ATOM   11205 N  N   . ILE K  1 17  ? 20.764 -89.945  -0.205   1.00 78.98  ? 18  ILE K N   1 
ATOM   11206 C  CA  . ILE K  1 17  ? 21.722 -89.355  -1.137   1.00 76.81  ? 18  ILE K CA  1 
ATOM   11207 C  C   . ILE K  1 17  ? 23.078 -89.160  -0.468   1.00 77.17  ? 18  ILE K C   1 
ATOM   11208 O  O   . ILE K  1 17  ? 23.170 -88.510  0.564    1.00 79.69  ? 18  ILE K O   1 
ATOM   11209 C  CB  . ILE K  1 17  ? 21.270 -87.954  -1.570   1.00 77.65  ? 18  ILE K CB  1 
ATOM   11210 C  CG1 . ILE K  1 17  ? 20.235 -88.034  -2.694   1.00 77.06  ? 18  ILE K CG1 1 
ATOM   11211 C  CG2 . ILE K  1 17  ? 22.470 -87.111  -2.012   1.00 76.84  ? 18  ILE K CG2 1 
ATOM   11212 C  CD1 . ILE K  1 17  ? 19.971 -86.652  -3.365   1.00 77.85  ? 18  ILE K CD1 1 
ATOM   11213 N  N   . ILE K  1 18  ? 24.132 -89.680  -1.086   1.00 75.30  ? 19  ILE K N   1 
ATOM   11214 C  CA  . ILE K  1 18  ? 25.493 -89.536  -0.554   1.00 76.11  ? 19  ILE K CA  1 
ATOM   11215 C  C   . ILE K  1 18  ? 26.425 -88.874  -1.567   1.00 74.66  ? 19  ILE K C   1 
ATOM   11216 O  O   . ILE K  1 18  ? 26.519 -89.320  -2.708   1.00 72.58  ? 19  ILE K O   1 
ATOM   11217 C  CB  . ILE K  1 18  ? 26.116 -90.903  -0.173   1.00 76.24  ? 19  ILE K CB  1 
ATOM   11218 C  CG1 . ILE K  1 18  ? 25.382 -91.515  1.004    1.00 78.52  ? 19  ILE K CG1 1 
ATOM   11219 C  CG2 . ILE K  1 18  ? 27.583 -90.739  0.212    1.00 77.30  ? 19  ILE K CG2 1 
ATOM   11220 C  CD1 . ILE K  1 18  ? 25.587 -90.749  2.270    1.00 81.83  ? 19  ILE K CD1 1 
ATOM   11221 N  N   . ASN K  1 19  ? 27.135 -87.842  -1.123   1.00 76.34  ? 20  ASN K N   1 
ATOM   11222 C  CA  . ASN K  1 19  ? 28.099 -87.113  -1.955   1.00 75.79  ? 20  ASN K CA  1 
ATOM   11223 C  C   . ASN K  1 19  ? 29.553 -87.505  -1.700   1.00 76.63  ? 20  ASN K C   1 
ATOM   11224 O  O   . ASN K  1 19  ? 29.921 -87.903  -0.595   1.00 78.79  ? 20  ASN K O   1 
ATOM   11225 C  CB  . ASN K  1 19  ? 27.977 -85.616  -1.713   1.00 77.91  ? 20  ASN K CB  1 
ATOM   11226 C  CG  . ASN K  1 19  ? 26.611 -85.071  -2.083   1.00 77.93  ? 20  ASN K CG  1 
ATOM   11227 O  OD1 . ASN K  1 19  ? 25.759 -84.836  -1.215   1.00 79.97  ? 20  ASN K OD1 1 
ATOM   11228 N  ND2 . ASN K  1 19  ? 26.392 -84.867  -3.380   1.00 76.02  ? 20  ASN K ND2 1 
ATOM   11229 N  N   . PHE K  1 20  ? 30.368 -87.383  -2.744   1.00 75.47  ? 21  PHE K N   1 
ATOM   11230 C  CA  . PHE K  1 20  ? 31.816 -87.594  -2.667   1.00 76.54  ? 21  PHE K CA  1 
ATOM   11231 C  C   . PHE K  1 20  ? 32.510 -86.363  -3.204   1.00 77.63  ? 21  PHE K C   1 
ATOM   11232 O  O   . PHE K  1 20  ? 32.005 -85.696  -4.114   1.00 76.50  ? 21  PHE K O   1 
ATOM   11233 C  CB  . PHE K  1 20  ? 32.256 -88.788  -3.493   1.00 74.69  ? 21  PHE K CB  1 
ATOM   11234 C  CG  . PHE K  1 20  ? 31.658 -90.073  -3.053   1.00 74.23  ? 21  PHE K CG  1 
ATOM   11235 C  CD1 . PHE K  1 20  ? 30.354 -90.413  -3.420   1.00 72.50  ? 21  PHE K CD1 1 
ATOM   11236 C  CD2 . PHE K  1 20  ? 32.385 -90.955  -2.281   1.00 76.02  ? 21  PHE K CD2 1 
ATOM   11237 C  CE1 . PHE K  1 20  ? 29.783 -91.609  -3.011   1.00 72.44  ? 21  PHE K CE1 1 
ATOM   11238 C  CE2 . PHE K  1 20  ? 31.828 -92.159  -1.873   1.00 76.06  ? 21  PHE K CE2 1 
ATOM   11239 C  CZ  . PHE K  1 20  ? 30.523 -92.489  -2.241   1.00 74.34  ? 21  PHE K CZ  1 
ATOM   11240 N  N   . GLU K  1 21  ? 33.662 -86.049  -2.621   1.00 80.53  ? 22  GLU K N   1 
ATOM   11241 C  CA  . GLU K  1 21  ? 34.501 -84.913  -3.074   1.00 82.24  ? 22  GLU K CA  1 
ATOM   11242 C  C   . GLU K  1 21  ? 35.999 -85.098  -2.741   1.00 84.95  ? 22  GLU K C   1 
ATOM   11243 O  O   . GLU K  1 21  ? 36.427 -85.071  -1.573   1.00 87.97  ? 22  GLU K O   1 
ATOM   11244 C  CB  . GLU K  1 21  ? 34.009 -83.582  -2.514   1.00 84.42  ? 22  GLU K CB  1 
ATOM   11245 C  CG  . GLU K  1 21  ? 34.836 -82.414  -3.029   1.00 87.04  ? 22  GLU K CG  1 
ATOM   11246 C  CD  . GLU K  1 21  ? 34.221 -81.057  -2.717   1.00 90.04  ? 22  GLU K CD  1 
ATOM   11247 O  OE1 . GLU K  1 21  ? 33.374 -80.987  -1.790   1.00 91.22  ? 22  GLU K OE1 1 
ATOM   11248 O  OE2 . GLU K  1 21  ? 34.591 -80.055  -3.393   1.00 91.47  ? 22  GLU K OE2 1 
ATOM   11249 N  N   . GLN K  1 22  ? 36.779 -85.300  -3.795   1.00 84.25  ? 23  GLN K N   1 
ATOM   11250 C  CA  . GLN K  1 22  ? 38.227 -85.466  -3.699   1.00 87.09  ? 23  GLN K CA  1 
ATOM   11251 C  C   . GLN K  1 22  ? 38.869 -84.236  -4.321   1.00 89.08  ? 23  GLN K C   1 
ATOM   11252 O  O   . GLN K  1 22  ? 38.868 -84.065  -5.547   1.00 87.29  ? 23  GLN K O   1 
ATOM   11253 C  CB  . GLN K  1 22  ? 38.675 -86.725  -4.443   1.00 85.51  ? 23  GLN K CB  1 
ATOM   11254 C  CG  . GLN K  1 22  ? 40.127 -87.095  -4.266   1.00 88.79  ? 23  GLN K CG  1 
ATOM   11255 C  CD  . GLN K  1 22  ? 40.512 -88.365  -5.051   1.00 87.72  ? 23  GLN K CD  1 
ATOM   11256 O  OE1 . GLN K  1 22  ? 40.149 -88.526  -6.216   1.00 85.10  ? 23  GLN K OE1 1 
ATOM   11257 N  NE2 . GLN K  1 22  ? 41.259 -89.260  -4.411   1.00 90.36  ? 23  GLN K NE2 1 
ATOM   11258 N  N   . LYS K  1 23  ? 39.414 -83.372  -3.466   1.00 93.30  ? 24  LYS K N   1 
ATOM   11259 C  CA  . LYS K  1 23  ? 40.011 -82.103  -3.920   1.00 95.98  ? 24  LYS K CA  1 
ATOM   11260 C  C   . LYS K  1 23  ? 41.251 -82.338  -4.780   1.00 97.10  ? 24  LYS K C   1 
ATOM   11261 O  O   . LYS K  1 23  ? 41.508 -81.581  -5.722   1.00 97.67  ? 24  LYS K O   1 
ATOM   11262 C  CB  . LYS K  1 23  ? 40.385 -81.194  -2.743   1.00 100.80 ? 24  LYS K CB  1 
ATOM   11263 C  CG  . LYS K  1 23  ? 39.183 -80.699  -1.949   1.00 101.05 ? 24  LYS K CG  1 
ATOM   11264 C  CD  . LYS K  1 23  ? 39.447 -79.321  -1.307   1.00 106.42 ? 24  LYS K CD  1 
ATOM   11265 C  CE  . LYS K  1 23  ? 38.558 -79.095  -0.060   1.00 107.95 ? 24  LYS K CE  1 
ATOM   11266 N  NZ  . LYS K  1 23  ? 39.004 -77.921  0.753    1.00 113.77 ? 24  LYS K NZ  1 
ATOM   11267 N  N   . GLU K  1 24  ? 42.025 -83.371  -4.444   1.00 98.06  ? 25  GLU K N   1 
ATOM   11268 C  CA  . GLU K  1 24  ? 43.286 -83.636  -5.142   1.00 100.10 ? 25  GLU K CA  1 
ATOM   11269 C  C   . GLU K  1 24  ? 43.498 -85.095  -5.403   1.00 98.37  ? 25  GLU K C   1 
ATOM   11270 O  O   . GLU K  1 24  ? 43.290 -85.925  -4.538   1.00 98.37  ? 25  GLU K O   1 
ATOM   11271 C  CB  . GLU K  1 24  ? 44.458 -83.075  -4.346   1.00 105.99 ? 25  GLU K CB  1 
ATOM   11272 C  CG  . GLU K  1 24  ? 44.232 -81.594  -4.042   1.00 108.67 ? 25  GLU K CG  1 
ATOM   11273 C  CD  . GLU K  1 24  ? 45.439 -80.898  -3.542   1.00 115.53 ? 25  GLU K CD  1 
ATOM   11274 O  OE1 . GLU K  1 24  ? 46.120 -81.461  -2.631   1.00 119.00 ? 25  GLU K OE1 1 
ATOM   11275 O  OE2 . GLU K  1 24  ? 45.668 -79.775  -4.066   1.00 117.77 ? 25  GLU K OE2 1 
ATOM   11276 N  N   . SER K  1 25  ? 43.945 -85.385  -6.612   1.00 97.60  ? 26  SER K N   1 
ATOM   11277 C  CA  . SER K  1 25  ? 44.058 -86.761  -7.113   1.00 96.23  ? 26  SER K CA  1 
ATOM   11278 C  C   . SER K  1 25  ? 44.719 -87.733  -6.148   1.00 99.03  ? 26  SER K C   1 
ATOM   11279 O  O   . SER K  1 25  ? 44.307 -88.899  -6.045   1.00 97.26  ? 26  SER K O   1 
ATOM   11280 C  CB  . SER K  1 25  ? 44.829 -86.777  -8.446   1.00 97.12  ? 26  SER K CB  1 
ATOM   11281 O  OG  . SER K  1 25  ? 45.997 -85.971  -8.387   1.00 102.11 ? 26  SER K OG  1 
ATOM   11282 N  N   . ASN K  1 26  ? 45.752 -87.234  -5.465   1.00 104.03 ? 27  ASN K N   1 
ATOM   11283 C  CA  . ASN K  1 26  ? 46.542 -88.022  -4.490   1.00 108.04 ? 27  ASN K CA  1 
ATOM   11284 C  C   . ASN K  1 26  ? 45.979 -87.962  -3.062   1.00 108.72 ? 27  ASN K C   1 
ATOM   11285 O  O   . ASN K  1 26  ? 46.522 -88.592  -2.156   1.00 112.27 ? 27  ASN K O   1 
ATOM   11286 C  CB  . ASN K  1 26  ? 48.000 -87.554  -4.486   1.00 113.69 ? 27  ASN K CB  1 
ATOM   11287 C  CG  . ASN K  1 26  ? 48.167 -86.137  -3.923   1.00 116.54 ? 27  ASN K CG  1 
ATOM   11288 O  OD1 . ASN K  1 26  ? 47.389 -85.210  -4.226   1.00 113.59 ? 27  ASN K OD1 1 
ATOM   11289 N  ND2 . ASN K  1 26  ? 49.185 -85.970  -3.094   1.00 122.32 ? 27  ASN K ND2 1 
ATOM   11290 N  N   . GLY K  1 27  ? 44.882 -87.221  -2.880   1.00 105.72 ? 28  GLY K N   1 
ATOM   11291 C  CA  . GLY K  1 27  ? 44.400 -86.833  -1.545   1.00 107.15 ? 28  GLY K CA  1 
ATOM   11292 C  C   . GLY K  1 27  ? 43.185 -87.607  -1.052   1.00 103.76 ? 28  GLY K C   1 
ATOM   11293 O  O   . GLY K  1 27  ? 42.715 -88.548  -1.714   1.00 100.33 ? 28  GLY K O   1 
ATOM   11294 N  N   . PRO K  1 28  ? 42.664 -87.215  0.125    1.00 105.14 ? 29  PRO K N   1 
ATOM   11295 C  CA  . PRO K  1 28  ? 41.565 -87.959  0.732    1.00 102.72 ? 29  PRO K CA  1 
ATOM   11296 C  C   . PRO K  1 28  ? 40.240 -87.562  0.113    1.00 97.88  ? 29  PRO K C   1 
ATOM   11297 O  O   . PRO K  1 28  ? 40.128 -86.465  -0.493   1.00 97.18  ? 29  PRO K O   1 
ATOM   11298 C  CB  . PRO K  1 28  ? 41.621 -87.521  2.199    1.00 107.04 ? 29  PRO K CB  1 
ATOM   11299 C  CG  . PRO K  1 28  ? 42.088 -86.088  2.125    1.00 109.44 ? 29  PRO K CG  1 
ATOM   11300 C  CD  . PRO K  1 28  ? 43.040 -86.031  0.929    1.00 109.34 ? 29  PRO K CD  1 
ATOM   11301 N  N   . VAL K  1 29  ? 39.253 -88.446  0.296    1.00 95.16  ? 30  VAL K N   1 
ATOM   11302 C  CA  . VAL K  1 29  ? 37.891 -88.259  -0.224   1.00 90.78  ? 30  VAL K CA  1 
ATOM   11303 C  C   . VAL K  1 29  ? 36.899 -87.973  0.889    1.00 91.35  ? 30  VAL K C   1 
ATOM   11304 O  O   . VAL K  1 29  ? 36.666 -88.819  1.737    1.00 92.39  ? 30  VAL K O   1 
ATOM   11305 C  CB  . VAL K  1 29  ? 37.400 -89.518  -0.934   1.00 87.43  ? 30  VAL K CB  1 
ATOM   11306 C  CG1 . VAL K  1 29  ? 35.961 -89.306  -1.416   1.00 83.54  ? 30  VAL K CG1 1 
ATOM   11307 C  CG2 . VAL K  1 29  ? 38.359 -89.890  -2.070   1.00 87.10  ? 30  VAL K CG2 1 
ATOM   11308 N  N   . LYS K  1 30  ? 36.308 -86.785  0.878    1.00 91.18  ? 31  LYS K N   1 
ATOM   11309 C  CA  . LYS K  1 30  ? 35.220 -86.494  1.809    1.00 91.87  ? 31  LYS K CA  1 
ATOM   11310 C  C   . LYS K  1 30  ? 33.937 -87.147  1.336    1.00 87.87  ? 31  LYS K C   1 
ATOM   11311 O  O   . LYS K  1 30  ? 33.573 -87.041  0.178    1.00 84.98  ? 31  LYS K O   1 
ATOM   11312 C  CB  . LYS K  1 30  ? 35.011 -84.991  1.986    1.00 93.86  ? 31  LYS K CB  1 
ATOM   11313 C  CG  . LYS K  1 30  ? 36.157 -84.341  2.774    1.00 99.46  ? 31  LYS K CG  1 
ATOM   11314 C  CD  . LYS K  1 30  ? 35.820 -82.945  3.297    1.00 102.95 ? 31  LYS K CD  1 
ATOM   11315 C  CE  . LYS K  1 30  ? 37.000 -82.380  4.103    1.00 108.45 ? 31  LYS K CE  1 
ATOM   11316 N  NZ  . LYS K  1 30  ? 36.680 -81.102  4.775    1.00 112.78 ? 31  LYS K NZ  1 
ATOM   11317 N  N   . VAL K  1 31  ? 33.265 -87.839  2.239    1.00 88.45  ? 32  VAL K N   1 
ATOM   11318 C  CA  . VAL K  1 31  ? 32.010 -88.494  1.929    1.00 85.57  ? 32  VAL K CA  1 
ATOM   11319 C  C   . VAL K  1 31  ? 30.939 -87.943  2.842    1.00 87.22  ? 32  VAL K C   1 
ATOM   11320 O  O   . VAL K  1 31  ? 31.054 -88.043  4.055    1.00 90.67  ? 32  VAL K O   1 
ATOM   11321 C  CB  . VAL K  1 31  ? 32.103 -89.996  2.162    1.00 85.36  ? 32  VAL K CB  1 
ATOM   11322 C  CG1 . VAL K  1 31  ? 30.812 -90.664  1.722    1.00 82.54  ? 32  VAL K CG1 1 
ATOM   11323 C  CG2 . VAL K  1 31  ? 33.298 -90.568  1.414    1.00 85.06  ? 32  VAL K CG2 1 
ATOM   11324 N  N   . TRP K  1 32  ? 29.894 -87.361  2.279    1.00 85.47  ? 33  TRP K N   1 
ATOM   11325 C  CA  . TRP K  1 32  ? 28.835 -86.823  3.126    1.00 87.63  ? 33  TRP K CA  1 
ATOM   11326 C  C   . TRP K  1 32  ? 27.463 -86.901  2.486    1.00 85.33  ? 33  TRP K C   1 
ATOM   11327 O  O   . TRP K  1 32  ? 27.327 -86.997  1.270    1.00 82.54  ? 33  TRP K O   1 
ATOM   11328 C  CB  . TRP K  1 32  ? 29.147 -85.376  3.554    1.00 90.83  ? 33  TRP K CB  1 
ATOM   11329 C  CG  . TRP K  1 32  ? 28.697 -84.324  2.592    1.00 89.78  ? 33  TRP K CG  1 
ATOM   11330 C  CD1 . TRP K  1 32  ? 27.569 -83.540  2.680    1.00 90.98  ? 33  TRP K CD1 1 
ATOM   11331 C  CD2 . TRP K  1 32  ? 29.367 -83.934  1.391    1.00 87.89  ? 33  TRP K CD2 1 
ATOM   11332 N  NE1 . TRP K  1 32  ? 27.508 -82.683  1.605    1.00 89.79  ? 33  TRP K NE1 1 
ATOM   11333 C  CE2 . TRP K  1 32  ? 28.597 -82.905  0.798    1.00 87.99  ? 33  TRP K CE2 1 
ATOM   11334 C  CE3 . TRP K  1 32  ? 30.544 -84.354  0.755    1.00 86.76  ? 33  TRP K CE3 1 
ATOM   11335 C  CZ2 . TRP K  1 32  ? 28.974 -82.292  -0.402   1.00 86.99  ? 33  TRP K CZ2 1 
ATOM   11336 C  CZ3 . TRP K  1 32  ? 30.913 -83.746  -0.442   1.00 85.59  ? 33  TRP K CZ3 1 
ATOM   11337 C  CH2 . TRP K  1 32  ? 30.135 -82.730  -1.005   1.00 85.64  ? 33  TRP K CH2 1 
ATOM   11338 N  N   . GLY K  1 33  ? 26.445 -86.848  3.332    1.00 87.26  ? 34  GLY K N   1 
ATOM   11339 C  CA  . GLY K  1 33  ? 25.062 -86.885  2.868    1.00 86.11  ? 34  GLY K CA  1 
ATOM   11340 C  C   . GLY K  1 33  ? 24.114 -87.306  3.978    1.00 88.59  ? 34  GLY K C   1 
ATOM   11341 O  O   . GLY K  1 33  ? 24.476 -87.275  5.159    1.00 91.83  ? 34  GLY K O   1 
ATOM   11342 N  N   . SER K  1 34  ? 22.910 -87.714  3.587    1.00 87.54  ? 35  SER K N   1 
ATOM   11343 C  CA  . SER K  1 34  ? 21.861 -88.056  4.537    1.00 90.13  ? 35  SER K CA  1 
ATOM   11344 C  C   . SER K  1 34  ? 21.055 -89.273  4.105    1.00 88.47  ? 35  SER K C   1 
ATOM   11345 O  O   . SER K  1 34  ? 20.344 -89.233  3.102    1.00 86.77  ? 35  SER K O   1 
ATOM   11346 C  CB  . SER K  1 34  ? 20.929 -86.854  4.712    1.00 92.68  ? 35  SER K CB  1 
ATOM   11347 O  OG  . SER K  1 34  ? 20.055 -87.052  5.803    1.00 96.34  ? 35  SER K OG  1 
ATOM   11348 N  N   . ILE K  1 35  ? 21.155 -90.349  4.872    1.00 89.66  ? 36  ILE K N   1 
ATOM   11349 C  CA  . ILE K  1 35  ? 20.319 -91.546  4.640    1.00 89.33  ? 36  ILE K CA  1 
ATOM   11350 C  C   . ILE K  1 35  ? 19.188 -91.618  5.661    1.00 93.21  ? 36  ILE K C   1 
ATOM   11351 O  O   . ILE K  1 35  ? 19.400 -91.311  6.844    1.00 96.42  ? 36  ILE K O   1 
ATOM   11352 C  CB  . ILE K  1 35  ? 21.102 -92.854  4.786    1.00 88.75  ? 36  ILE K CB  1 
ATOM   11353 C  CG1 . ILE K  1 35  ? 22.350 -92.834  3.908    1.00 85.85  ? 36  ILE K CG1 1 
ATOM   11354 C  CG2 . ILE K  1 35  ? 20.210 -94.053  4.431    1.00 88.26  ? 36  ILE K CG2 1 
ATOM   11355 C  CD1 . ILE K  1 35  ? 23.215 -94.075  4.072    1.00 86.10  ? 36  ILE K CD1 1 
ATOM   11356 N  N   . LYS K  1 36  ? 18.005 -92.051  5.214    1.00 93.31  ? 37  LYS K N   1 
ATOM   11357 C  CA  . LYS K  1 36  ? 16.832 -92.130  6.097    1.00 97.24  ? 37  LYS K CA  1 
ATOM   11358 C  C   . LYS K  1 36  ? 16.037 -93.439  5.960    1.00 97.79  ? 37  LYS K C   1 
ATOM   11359 O  O   . LYS K  1 36  ? 16.283 -94.240  5.054    1.00 95.04  ? 37  LYS K O   1 
ATOM   11360 C  CB  . LYS K  1 36  ? 15.921 -90.905  5.906    1.00 98.69  ? 37  LYS K CB  1 
ATOM   11361 C  CG  . LYS K  1 36  ? 15.377 -90.718  4.512    1.00 96.36  ? 37  LYS K CG  1 
ATOM   11362 C  CD  . LYS K  1 36  ? 14.125 -89.830  4.548    1.00 99.89  ? 37  LYS K CD  1 
ATOM   11363 C  CE  . LYS K  1 36  ? 13.617 -89.495  3.136    1.00 98.02  ? 37  LYS K CE  1 
ATOM   11364 N  NZ  . LYS K  1 36  ? 12.267 -88.891  3.152    1.00 101.52 ? 37  LYS K NZ  1 
ATOM   11365 N  N   . GLY K  1 37  ? 15.101 -93.640  6.892    1.00 101.84 ? 38  GLY K N   1 
ATOM   11366 C  CA  . GLY K  1 37  ? 14.307 -94.875  6.973    1.00 103.61 ? 38  GLY K CA  1 
ATOM   11367 C  C   . GLY K  1 37  ? 15.057 -96.001  7.668    1.00 104.54 ? 38  GLY K C   1 
ATOM   11368 O  O   . GLY K  1 37  ? 14.692 -97.177  7.572    1.00 105.40 ? 38  GLY K O   1 
ATOM   11369 N  N   . LEU K  1 38  ? 16.106 -95.627  8.389    1.00 104.90 ? 39  LEU K N   1 
ATOM   11370 C  CA  . LEU K  1 38  ? 17.027 -96.597  8.993    1.00 105.90 ? 39  LEU K CA  1 
ATOM   11371 C  C   . LEU K  1 38  ? 16.613 -96.970  10.414   1.00 111.11 ? 39  LEU K C   1 
ATOM   11372 O  O   . LEU K  1 38  ? 16.205 -96.115  11.213   1.00 113.79 ? 39  LEU K O   1 
ATOM   11373 C  CB  . LEU K  1 38  ? 18.481 -96.052  9.010    1.00 104.00 ? 39  LEU K CB  1 
ATOM   11374 C  CG  . LEU K  1 38  ? 19.328 -96.240  7.743    1.00 99.30  ? 39  LEU K CG  1 
ATOM   11375 C  CD1 . LEU K  1 38  ? 20.547 -95.307  7.756    1.00 97.73  ? 39  LEU K CD1 1 
ATOM   11376 C  CD2 . LEU K  1 38  ? 19.753 -97.695  7.590    1.00 99.36  ? 39  LEU K CD2 1 
ATOM   11377 N  N   . THR K  1 39  ? 16.787 -98.248  10.735   1.00 112.84 ? 40  THR K N   1 
ATOM   11378 C  CA  . THR K  1 39  ? 16.605 -98.732  12.114   1.00 118.21 ? 40  THR K CA  1 
ATOM   11379 C  C   . THR K  1 39  ? 17.633 -98.033  13.043   1.00 119.74 ? 40  THR K C   1 
ATOM   11380 O  O   . THR K  1 39  ? 18.830 -97.966  12.733   1.00 117.42 ? 40  THR K O   1 
ATOM   11381 C  CB  . THR K  1 39  ? 16.755 -100.298 12.230   1.00 120.07 ? 40  THR K CB  1 
ATOM   11382 O  OG1 . THR K  1 39  ? 18.018 -100.645 12.832   1.00 121.39 ? 40  THR K OG1 1 
ATOM   11383 C  CG2 . THR K  1 39  ? 16.620 -100.987 10.856   1.00 116.33 ? 40  THR K CG2 1 
ATOM   11384 N  N   . GLU K  1 40  ? 17.180 -97.531  14.185   1.00 124.29 ? 41  GLU K N   1 
ATOM   11385 C  CA  . GLU K  1 40  ? 18.076 -96.744  15.057   1.00 126.42 ? 41  GLU K CA  1 
ATOM   11386 C  C   . GLU K  1 40  ? 19.355 -97.538  15.357   1.00 126.92 ? 41  GLU K C   1 
ATOM   11387 O  O   . GLU K  1 40  ? 19.325 -98.762  15.621   1.00 128.79 ? 41  GLU K O   1 
ATOM   11388 C  CB  . GLU K  1 40  ? 17.398 -96.318  16.385   1.00 132.51 ? 41  GLU K CB  1 
ATOM   11389 C  CG  . GLU K  1 40  ? 18.332 -95.522  17.344   1.00 135.70 ? 41  GLU K CG  1 
ATOM   11390 C  CD  . GLU K  1 40  ? 17.710 -95.234  18.734   1.00 143.02 ? 41  GLU K CD  1 
ATOM   11391 O  OE1 . GLU K  1 40  ? 17.151 -96.179  19.371   1.00 146.62 ? 41  GLU K OE1 1 
ATOM   11392 O  OE2 . GLU K  1 40  ? 17.812 -94.065  19.202   1.00 144.96 ? 41  GLU K OE2 1 
ATOM   11393 N  N   . GLY K  1 41  ? 20.471 -96.821  15.298   1.00 125.52 ? 42  GLY K N   1 
ATOM   11394 C  CA  . GLY K  1 41  ? 21.757 -97.387  15.690   1.00 127.01 ? 42  GLY K CA  1 
ATOM   11395 C  C   . GLY K  1 41  ? 22.763 -97.464  14.564   1.00 122.20 ? 42  GLY K C   1 
ATOM   11396 O  O   . GLY K  1 41  ? 22.668 -96.721  13.559   1.00 117.77 ? 42  GLY K O   1 
ATOM   11397 N  N   . LEU K  1 42  ? 23.740 -98.353  14.748   1.00 123.51 ? 43  LEU K N   1 
ATOM   11398 C  CA  . LEU K  1 42  ? 24.844 -98.494  13.790   1.00 120.04 ? 43  LEU K CA  1 
ATOM   11399 C  C   . LEU K  1 42  ? 24.439 -99.293  12.549   1.00 116.06 ? 43  LEU K C   1 
ATOM   11400 O  O   . LEU K  1 42  ? 23.658 -100.266 12.638   1.00 117.53 ? 43  LEU K O   1 
ATOM   11401 C  CB  . LEU K  1 42  ? 26.073 -99.158  14.424   1.00 123.68 ? 43  LEU K CB  1 
ATOM   11402 C  CG  . LEU K  1 42  ? 26.911 -98.246  15.352   1.00 127.03 ? 43  LEU K CG  1 
ATOM   11403 C  CD1 . LEU K  1 42  ? 26.787 -98.665  16.834   1.00 133.85 ? 43  LEU K CD1 1 
ATOM   11404 C  CD2 . LEU K  1 42  ? 28.381 -98.231  14.935   1.00 126.44 ? 43  LEU K CD2 1 
ATOM   11405 N  N   . HIS K  1 43  ? 24.985 -98.864  11.399   1.00 111.44 ? 44  HIS K N   1 
ATOM   11406 C  CA  . HIS K  1 43  ? 24.796 -99.567  10.125   1.00 107.67 ? 44  HIS K CA  1 
ATOM   11407 C  C   . HIS K  1 43  ? 26.094 -99.666  9.324    1.00 105.45 ? 44  HIS K C   1 
ATOM   11408 O  O   . HIS K  1 43  ? 26.845 -98.679  9.188    1.00 104.05 ? 44  HIS K O   1 
ATOM   11409 C  CB  . HIS K  1 43  ? 23.716 -98.897  9.292    1.00 103.96 ? 44  HIS K CB  1 
ATOM   11410 C  CG  . HIS K  1 43  ? 22.342 -99.084  9.848    1.00 106.27 ? 44  HIS K CG  1 
ATOM   11411 N  ND1 . HIS K  1 43  ? 21.609 -100.239 9.653    1.00 107.50 ? 44  HIS K ND1 1 
ATOM   11412 C  CD2 . HIS K  1 43  ? 21.572 -98.269  10.609   1.00 108.23 ? 44  HIS K CD2 1 
ATOM   11413 C  CE1 . HIS K  1 43  ? 20.436 -100.117 10.251   1.00 109.92 ? 44  HIS K CE1 1 
ATOM   11414 N  NE2 . HIS K  1 43  ? 20.395 -98.937  10.848   1.00 110.55 ? 44  HIS K NE2 1 
ATOM   11415 N  N   . GLY K  1 44  ? 26.333 -100.876 8.804    1.00 105.53 ? 45  GLY K N   1 
ATOM   11416 C  CA  . GLY K  1 44  ? 27.458 -101.144 7.910    1.00 103.79 ? 45  GLY K CA  1 
ATOM   11417 C  C   . GLY K  1 44  ? 27.337 -100.314 6.630    1.00 98.73  ? 45  GLY K C   1 
ATOM   11418 O  O   . GLY K  1 44  ? 26.214 -100.024 6.161    1.00 96.67  ? 45  GLY K O   1 
ATOM   11419 N  N   . PHE K  1 45  ? 28.480 -99.921  6.067    1.00 97.17  ? 46  PHE K N   1 
ATOM   11420 C  CA  . PHE K  1 45  ? 28.505 -98.906  5.024    1.00 92.86  ? 46  PHE K CA  1 
ATOM   11421 C  C   . PHE K  1 45  ? 29.717 -99.120  4.160    1.00 91.87  ? 46  PHE K C   1 
ATOM   11422 O  O   . PHE K  1 45  ? 30.827 -98.712  4.522    1.00 93.45  ? 46  PHE K O   1 
ATOM   11423 C  CB  . PHE K  1 45  ? 28.555 -97.522  5.680    1.00 93.22  ? 46  PHE K CB  1 
ATOM   11424 C  CG  . PHE K  1 45  ? 28.344 -96.381  4.735    1.00 89.47  ? 46  PHE K CG  1 
ATOM   11425 C  CD1 . PHE K  1 45  ? 27.256 -96.362  3.885    1.00 86.64  ? 46  PHE K CD1 1 
ATOM   11426 C  CD2 . PHE K  1 45  ? 29.221 -95.300  4.728    1.00 89.38  ? 46  PHE K CD2 1 
ATOM   11427 C  CE1 . PHE K  1 45  ? 27.058 -95.295  3.030    1.00 83.97  ? 46  PHE K CE1 1 
ATOM   11428 C  CE2 . PHE K  1 45  ? 29.023 -94.232  3.882    1.00 86.62  ? 46  PHE K CE2 1 
ATOM   11429 C  CZ  . PHE K  1 45  ? 27.942 -94.225  3.029    1.00 83.98  ? 46  PHE K CZ  1 
ATOM   11430 N  N   . HIS K  1 46  ? 29.508 -99.762  3.017    1.00 89.68  ? 47  HIS K N   1 
ATOM   11431 C  CA  . HIS K  1 46  ? 30.635 -100.181 2.171    1.00 89.52  ? 47  HIS K CA  1 
ATOM   11432 C  C   . HIS K  1 46  ? 30.461 -99.928  0.666    1.00 85.75  ? 47  HIS K C   1 
ATOM   11433 O  O   . HIS K  1 46  ? 29.338 -99.880  0.140    1.00 83.74  ? 47  HIS K O   1 
ATOM   11434 C  CB  . HIS K  1 46  ? 30.906 -101.666 2.374    1.00 92.77  ? 47  HIS K CB  1 
ATOM   11435 C  CG  . HIS K  1 46  ? 30.745 -102.122 3.794    1.00 96.84  ? 47  HIS K CG  1 
ATOM   11436 N  ND1 . HIS K  1 46  ? 29.613 -102.772 4.248    1.00 98.06  ? 47  HIS K ND1 1 
ATOM   11437 C  CD2 . HIS K  1 46  ? 31.568 -102.014 4.862    1.00 100.83 ? 47  HIS K CD2 1 
ATOM   11438 C  CE1 . HIS K  1 46  ? 29.755 -103.067 5.526    1.00 102.12 ? 47  HIS K CE1 1 
ATOM   11439 N  NE2 . HIS K  1 46  ? 30.931 -102.617 5.924    1.00 103.99 ? 47  HIS K NE2 1 
ATOM   11440 N  N   . VAL K  1 47  ? 31.599 -99.774  -0.013   1.00 85.42  ? 48  VAL K N   1 
ATOM   11441 C  CA  . VAL K  1 47  ? 31.646 -99.716  -1.474   1.00 82.54  ? 48  VAL K CA  1 
ATOM   11442 C  C   . VAL K  1 47  ? 31.888 -101.113 -1.999   1.00 84.25  ? 48  VAL K C   1 
ATOM   11443 O  O   . VAL K  1 47  ? 32.928 -101.700 -1.739   1.00 87.18  ? 48  VAL K O   1 
ATOM   11444 C  CB  . VAL K  1 47  ? 32.787 -98.816  -1.990   1.00 81.70  ? 48  VAL K CB  1 
ATOM   11445 C  CG1 . VAL K  1 47  ? 32.970 -98.998  -3.485   1.00 79.61  ? 48  VAL K CG1 1 
ATOM   11446 C  CG2 . VAL K  1 47  ? 32.518 -97.345  -1.633   1.00 80.35  ? 48  VAL K CG2 1 
ATOM   11447 N  N   . HIS K  1 48  ? 30.924 -101.630 -2.745   1.00 83.02  ? 49  HIS K N   1 
ATOM   11448 C  CA  . HIS K  1 48  ? 31.037 -102.953 -3.358   1.00 85.09  ? 49  HIS K CA  1 
ATOM   11449 C  C   . HIS K  1 48  ? 31.613 -102.891 -4.765   1.00 83.85  ? 49  HIS K C   1 
ATOM   11450 O  O   . HIS K  1 48  ? 31.636 -101.839 -5.404   1.00 80.96  ? 49  HIS K O   1 
ATOM   11451 C  CB  . HIS K  1 48  ? 29.687 -103.644 -3.403   1.00 85.30  ? 49  HIS K CB  1 
ATOM   11452 C  CG  . HIS K  1 48  ? 29.189 -104.045 -2.054   1.00 88.10  ? 49  HIS K CG  1 
ATOM   11453 N  ND1 . HIS K  1 48  ? 28.847 -105.350 -1.744   1.00 91.57  ? 49  HIS K ND1 1 
ATOM   11454 C  CD2 . HIS K  1 48  ? 28.977 -103.314 -0.926   1.00 87.73  ? 49  HIS K CD2 1 
ATOM   11455 C  CE1 . HIS K  1 48  ? 28.429 -105.399 -0.488   1.00 93.33  ? 49  HIS K CE1 1 
ATOM   11456 N  NE2 . HIS K  1 48  ? 28.491 -104.178 0.026    1.00 91.22  ? 49  HIS K NE2 1 
ATOM   11457 N  N   . GLU K  1 49  ? 32.053 -104.050 -5.251   1.00 86.63  ? 50  GLU K N   1 
ATOM   11458 C  CA  . GLU K  1 49  ? 32.857 -104.136 -6.492   1.00 86.52  ? 50  GLU K CA  1 
ATOM   11459 C  C   . GLU K  1 49  ? 32.138 -103.622 -7.737   1.00 83.15  ? 50  GLU K C   1 
ATOM   11460 O  O   . GLU K  1 49  ? 32.642 -102.758 -8.441   1.00 81.13  ? 50  GLU K O   1 
ATOM   11461 C  CB  . GLU K  1 49  ? 33.313 -105.580 -6.734   1.00 90.81  ? 50  GLU K CB  1 
ATOM   11462 C  CG  . GLU K  1 49  ? 34.345 -105.712 -7.857   1.00 91.87  ? 50  GLU K CG  1 
ATOM   11463 C  CD  . GLU K  1 49  ? 35.019 -107.098 -7.931   1.00 97.05  ? 50  GLU K CD  1 
ATOM   11464 O  OE1 . GLU K  1 49  ? 34.906 -107.905 -6.981   1.00 99.86  ? 50  GLU K OE1 1 
ATOM   11465 O  OE2 . GLU K  1 49  ? 35.672 -107.376 -8.960   1.00 98.49  ? 50  GLU K OE2 1 
ATOM   11466 N  N   . PHE K  1 50  ? 30.947 -104.154 -7.984   1.00 83.06  ? 51  PHE K N   1 
ATOM   11467 C  CA  . PHE K  1 50  ? 30.222 -103.909 -9.239   1.00 81.11  ? 51  PHE K CA  1 
ATOM   11468 C  C   . PHE K  1 50  ? 29.112 -102.843 -9.162   1.00 77.88  ? 51  PHE K C   1 
ATOM   11469 O  O   . PHE K  1 50  ? 28.326 -102.788 -8.214   1.00 77.82  ? 51  PHE K O   1 
ATOM   11470 C  CB  . PHE K  1 50  ? 29.630 -105.221 -9.758   1.00 83.73  ? 51  PHE K CB  1 
ATOM   11471 C  CG  . PHE K  1 50  ? 30.631 -106.322 -9.853   1.00 87.78  ? 51  PHE K CG  1 
ATOM   11472 C  CD1 . PHE K  1 50  ? 31.762 -106.173 -10.654  1.00 88.27  ? 51  PHE K CD1 1 
ATOM   11473 C  CD2 . PHE K  1 50  ? 30.454 -107.510 -9.146   1.00 91.75  ? 51  PHE K CD2 1 
ATOM   11474 C  CE1 . PHE K  1 50  ? 32.706 -107.193 -10.755  1.00 92.68  ? 51  PHE K CE1 1 
ATOM   11475 C  CE2 . PHE K  1 50  ? 31.391 -108.534 -9.240   1.00 96.06  ? 51  PHE K CE2 1 
ATOM   11476 C  CZ  . PHE K  1 50  ? 32.524 -108.375 -10.049  1.00 96.53  ? 51  PHE K CZ  1 
ATOM   11477 N  N   . GLY K  1 51  ? 29.049 -102.015 -10.196  1.00 75.73  ? 52  GLY K N   1 
ATOM   11478 C  CA  . GLY K  1 51  ? 27.920 -101.091 -10.405  1.00 73.36  ? 52  GLY K CA  1 
ATOM   11479 C  C   . GLY K  1 51  ? 26.739 -101.766 -11.101  1.00 74.26  ? 52  GLY K C   1 
ATOM   11480 O  O   . GLY K  1 51  ? 26.092 -101.199 -11.991  1.00 72.92  ? 52  GLY K O   1 
ATOM   11481 N  N   . ASP K  1 52  ? 26.471 -103.001 -10.691  1.00 77.01  ? 53  ASP K N   1 
ATOM   11482 C  CA  . ASP K  1 52  ? 25.451 -103.847 -11.311  1.00 78.87  ? 53  ASP K CA  1 
ATOM   11483 C  C   . ASP K  1 52  ? 24.211 -103.876 -10.412  1.00 79.30  ? 53  ASP K C   1 
ATOM   11484 O  O   . ASP K  1 52  ? 24.283 -104.252 -9.236   1.00 80.36  ? 53  ASP K O   1 
ATOM   11485 C  CB  . ASP K  1 52  ? 25.992 -105.267 -11.492  1.00 82.44  ? 53  ASP K CB  1 
ATOM   11486 C  CG  . ASP K  1 52  ? 25.099 -106.125 -12.346  1.00 84.99  ? 53  ASP K CG  1 
ATOM   11487 O  OD1 . ASP K  1 52  ? 23.861 -105.914 -12.280  1.00 84.79  ? 53  ASP K OD1 1 
ATOM   11488 O  OD2 . ASP K  1 52  ? 25.646 -107.004 -13.068  1.00 87.50  ? 53  ASP K OD2 1 
ATOM   11489 N  N   . ASN K  1 53  ? 23.084 -103.447 -10.971  1.00 78.78  ? 54  ASN K N   1 
ATOM   11490 C  CA  . ASN K  1 53  ? 21.834 -103.379 -10.222  1.00 79.49  ? 54  ASN K CA  1 
ATOM   11491 C  C   . ASN K  1 53  ? 20.788 -104.288 -10.843  1.00 82.25  ? 54  ASN K C   1 
ATOM   11492 O  O   . ASN K  1 53  ? 19.597 -104.207 -10.519  1.00 83.18  ? 54  ASN K O   1 
ATOM   11493 C  CB  . ASN K  1 53  ? 21.326 -101.930 -10.171  1.00 77.00  ? 54  ASN K CB  1 
ATOM   11494 C  CG  . ASN K  1 53  ? 20.932 -101.510 -8.786   1.00 77.15  ? 54  ASN K CG  1 
ATOM   11495 O  OD1 . ASN K  1 53  ? 21.774 -101.446 -7.882   1.00 77.15  ? 54  ASN K OD1 1 
ATOM   11496 N  ND2 . ASN K  1 53  ? 19.649 -101.216 -8.604   1.00 78.03  ? 54  ASN K ND2 1 
ATOM   11497 N  N   . THR K  1 54  ? 21.250 -105.152 -11.735  1.00 83.95  ? 55  THR K N   1 
ATOM   11498 C  CA  . THR K  1 54  ? 20.386 -106.082 -12.467  1.00 87.56  ? 55  THR K CA  1 
ATOM   11499 C  C   . THR K  1 54  ? 19.339 -106.757 -11.585  1.00 90.46  ? 55  THR K C   1 
ATOM   11500 O  O   . THR K  1 54  ? 18.126 -106.516 -11.735  1.00 91.17  ? 55  THR K O   1 
ATOM   11501 C  CB  . THR K  1 54  ? 21.253 -107.177 -13.125  1.00 90.19  ? 55  THR K CB  1 
ATOM   11502 O  OG1 . THR K  1 54  ? 21.997 -106.576 -14.191  1.00 88.46  ? 55  THR K OG1 1 
ATOM   11503 C  CG2 . THR K  1 54  ? 20.402 -108.367 -13.657  1.00 94.96  ? 55  THR K CG2 1 
ATOM   11504 N  N   . ALA K  1 55  ? 19.843 -107.589 -10.669  1.00 92.29  ? 56  ALA K N   1 
ATOM   11505 C  CA  . ALA K  1 55  ? 19.026 -108.320 -9.705   1.00 95.51  ? 56  ALA K CA  1 
ATOM   11506 C  C   . ALA K  1 55  ? 19.067 -107.622 -8.306   1.00 93.65  ? 56  ALA K C   1 
ATOM   11507 O  O   . ALA K  1 55  ? 19.280 -108.250 -7.259   1.00 95.78  ? 56  ALA K O   1 
ATOM   11508 C  CB  . ALA K  1 55  ? 19.480 -109.788 -9.641   1.00 99.79  ? 56  ALA K CB  1 
ATOM   11509 N  N   . GLY K  1 56  ? 18.850 -106.306 -8.309   1.00 90.13  ? 57  GLY K N   1 
ATOM   11510 C  CA  . GLY K  1 56  ? 18.779 -105.517 -7.077   1.00 88.59  ? 57  GLY K CA  1 
ATOM   11511 C  C   . GLY K  1 56  ? 20.156 -105.160 -6.555   1.00 86.51  ? 57  GLY K C   1 
ATOM   11512 O  O   . GLY K  1 56  ? 21.086 -104.967 -7.343   1.00 84.84  ? 57  GLY K O   1 
ATOM   11513 N  N   . CYS K  1 57  ? 20.278 -105.074 -5.229   1.00 87.07  ? 58  CYS K N   1 
ATOM   11514 C  CA  . CYS K  1 57  ? 21.561 -104.809 -4.574   1.00 85.85  ? 58  CYS K CA  1 
ATOM   11515 C  C   . CYS K  1 57  ? 22.486 -105.993 -4.603   1.00 88.30  ? 58  CYS K C   1 
ATOM   11516 O  O   . CYS K  1 57  ? 23.688 -105.810 -4.569   1.00 87.49  ? 58  CYS K O   1 
ATOM   11517 C  CB  . CYS K  1 57  ? 21.349 -104.383 -3.129   1.00 86.52  ? 58  CYS K CB  1 
ATOM   11518 S  SG  . CYS K  1 57  ? 20.566 -102.748 -2.982   1.00 84.23  ? 58  CYS K SG  1 
ATOM   11519 N  N   . THR K  1 58  ? 21.922 -107.198 -4.678   1.00 91.98  ? 59  THR K N   1 
ATOM   11520 C  CA  . THR K  1 58  ? 22.707 -108.456 -4.655   1.00 95.60  ? 59  THR K CA  1 
ATOM   11521 C  C   . THR K  1 58  ? 23.735 -108.511 -5.780   1.00 94.55  ? 59  THR K C   1 
ATOM   11522 O  O   . THR K  1 58  ? 24.839 -109.043 -5.595   1.00 96.47  ? 59  THR K O   1 
ATOM   11523 C  CB  . THR K  1 58  ? 21.820 -109.756 -4.794   1.00 100.10 ? 59  THR K CB  1 
ATOM   11524 O  OG1 . THR K  1 58  ? 20.660 -109.671 -3.965   1.00 101.44 ? 59  THR K OG1 1 
ATOM   11525 C  CG2 . THR K  1 58  ? 22.602 -111.012 -4.396   1.00 104.53 ? 59  THR K CG2 1 
ATOM   11526 N  N   . SER K  1 59  ? 23.362 -107.957 -6.932   1.00 92.05  ? 60  SER K N   1 
ATOM   11527 C  CA  . SER K  1 59  ? 24.215 -107.937 -8.129   1.00 91.21  ? 60  SER K CA  1 
ATOM   11528 C  C   . SER K  1 59  ? 25.539 -107.166 -7.948   1.00 88.75  ? 60  SER K C   1 
ATOM   11529 O  O   . SER K  1 59  ? 26.521 -107.390 -8.673   1.00 89.28  ? 60  SER K O   1 
ATOM   11530 C  CB  . SER K  1 59  ? 23.445 -107.297 -9.282   1.00 89.10  ? 60  SER K CB  1 
ATOM   11531 O  OG  . SER K  1 59  ? 22.102 -107.746 -9.315   1.00 91.53  ? 60  SER K OG  1 
ATOM   11532 N  N   . ALA K  1 60  ? 25.554 -106.262 -6.975   1.00 86.62  ? 61  ALA K N   1 
ATOM   11533 C  CA  . ALA K  1 60  ? 26.733 -105.455 -6.675   1.00 84.82  ? 61  ALA K CA  1 
ATOM   11534 C  C   . ALA K  1 60  ? 27.950 -106.282 -6.296   1.00 87.89  ? 61  ALA K C   1 
ATOM   11535 O  O   . ALA K  1 60  ? 29.055 -105.750 -6.265   1.00 87.20  ? 61  ALA K O   1 
ATOM   11536 C  CB  . ALA K  1 60  ? 26.430 -104.461 -5.557   1.00 83.09  ? 61  ALA K CB  1 
ATOM   11537 N  N   . GLY K  1 61  ? 27.746 -107.557 -5.964   1.00 91.86  ? 62  GLY K N   1 
ATOM   11538 C  CA  . GLY K  1 61  ? 28.845 -108.452 -5.590   1.00 95.74  ? 62  GLY K CA  1 
ATOM   11539 C  C   . GLY K  1 61  ? 29.418 -108.127 -4.206   1.00 96.57  ? 62  GLY K C   1 
ATOM   11540 O  O   . GLY K  1 61  ? 28.778 -107.467 -3.386   1.00 94.89  ? 62  GLY K O   1 
ATOM   11541 N  N   . PRO K  1 62  ? 30.651 -108.565 -3.950   1.00 99.47  ? 63  PRO K N   1 
ATOM   11542 C  CA  . PRO K  1 62  ? 31.244 -108.381 -2.648   1.00 101.34 ? 63  PRO K CA  1 
ATOM   11543 C  C   . PRO K  1 62  ? 31.835 -107.002 -2.438   1.00 98.07  ? 63  PRO K C   1 
ATOM   11544 O  O   . PRO K  1 62  ? 31.753 -106.136 -3.315   1.00 94.05  ? 63  PRO K O   1 
ATOM   11545 C  CB  . PRO K  1 62  ? 32.361 -109.423 -2.647   1.00 106.35 ? 63  PRO K CB  1 
ATOM   11546 C  CG  . PRO K  1 62  ? 32.807 -109.447 -4.048   1.00 105.21 ? 63  PRO K CG  1 
ATOM   11547 C  CD  . PRO K  1 62  ? 31.580 -109.226 -4.881   1.00 101.74 ? 63  PRO K CD  1 
ATOM   11548 N  N   . HIS K  1 63  ? 32.428 -106.834 -1.260   1.00 100.28 ? 64  HIS K N   1 
ATOM   11549 C  CA  . HIS K  1 63  ? 33.138 -105.618 -0.890   1.00 98.56  ? 64  HIS K CA  1 
ATOM   11550 C  C   . HIS K  1 63  ? 34.257 -105.346 -1.899   1.00 97.88  ? 64  HIS K C   1 
ATOM   11551 O  O   . HIS K  1 63  ? 34.971 -106.285 -2.312   1.00 101.18 ? 64  HIS K O   1 
ATOM   11552 C  CB  . HIS K  1 63  ? 33.763 -105.777 0.501    1.00 102.84 ? 64  HIS K CB  1 
ATOM   11553 C  CG  . HIS K  1 63  ? 32.772 -105.760 1.627    1.00 103.42 ? 64  HIS K CG  1 
ATOM   11554 N  ND1 . HIS K  1 63  ? 33.069 -105.235 2.873    1.00 105.21 ? 64  HIS K ND1 1 
ATOM   11555 C  CD2 . HIS K  1 63  ? 31.493 -106.201 1.698    1.00 102.75 ? 64  HIS K CD2 1 
ATOM   11556 C  CE1 . HIS K  1 63  ? 32.016 -105.363 3.662    1.00 105.78 ? 64  HIS K CE1 1 
ATOM   11557 N  NE2 . HIS K  1 63  ? 31.050 -105.953 2.977    1.00 104.29 ? 64  HIS K NE2 1 
ATOM   11558 N  N   . PHE K  1 64  ? 34.415 -104.078 -2.284   1.00 94.11  ? 65  PHE K N   1 
ATOM   11559 C  CA  . PHE K  1 64  ? 35.443 -103.706 -3.256   1.00 93.60  ? 65  PHE K CA  1 
ATOM   11560 C  C   . PHE K  1 64  ? 36.828 -103.960 -2.651   1.00 97.96  ? 65  PHE K C   1 
ATOM   11561 O  O   . PHE K  1 64  ? 37.208 -103.348 -1.634   1.00 98.71  ? 65  PHE K O   1 
ATOM   11562 C  CB  . PHE K  1 64  ? 35.281 -102.251 -3.712   1.00 89.36  ? 65  PHE K CB  1 
ATOM   11563 C  CG  . PHE K  1 64  ? 36.311 -101.801 -4.731   1.00 88.87  ? 65  PHE K CG  1 
ATOM   11564 C  CD1 . PHE K  1 64  ? 36.667 -102.615 -5.805   1.00 90.05  ? 65  PHE K CD1 1 
ATOM   11565 C  CD2 . PHE K  1 64  ? 36.910 -100.534 -4.623   1.00 87.94  ? 65  PHE K CD2 1 
ATOM   11566 C  CE1 . PHE K  1 64  ? 37.629 -102.179 -6.741   1.00 90.38  ? 65  PHE K CE1 1 
ATOM   11567 C  CE2 . PHE K  1 64  ? 37.858 -100.087 -5.559   1.00 87.97  ? 65  PHE K CE2 1 
ATOM   11568 C  CZ  . PHE K  1 64  ? 38.217 -100.908 -6.614   1.00 89.18  ? 65  PHE K CZ  1 
ATOM   11569 N  N   . ASN K  1 65  ? 37.559 -104.880 -3.296   1.00 101.09 ? 66  ASN K N   1 
ATOM   11570 C  CA  . ASN K  1 65  ? 38.780 -105.454 -2.725   1.00 106.66 ? 66  ASN K CA  1 
ATOM   11571 C  C   . ASN K  1 65  ? 39.878 -105.776 -3.765   1.00 108.84 ? 66  ASN K C   1 
ATOM   11572 O  O   . ASN K  1 65  ? 40.221 -106.953 -4.003   1.00 112.95 ? 66  ASN K O   1 
ATOM   11573 C  CB  . ASN K  1 65  ? 38.407 -106.719 -1.931   1.00 110.70 ? 66  ASN K CB  1 
ATOM   11574 C  CG  . ASN K  1 65  ? 39.592 -107.294 -1.154   1.00 117.12 ? 66  ASN K CG  1 
ATOM   11575 O  OD1 . ASN K  1 65  ? 40.655 -106.638 -1.020   1.00 118.51 ? 66  ASN K OD1 1 
ATOM   11576 N  ND2 . ASN K  1 65  ? 39.417 -108.520 -0.633   1.00 121.52 ? 66  ASN K ND2 1 
ATOM   11577 N  N   . PRO K  1 66  ? 40.453 -104.726 -4.370   1.00 106.59 ? 67  PRO K N   1 
ATOM   11578 C  CA  . PRO K  1 66  ? 41.415 -104.938 -5.451   1.00 108.52 ? 67  PRO K CA  1 
ATOM   11579 C  C   . PRO K  1 66  ? 42.794 -105.372 -4.969   1.00 114.81 ? 67  PRO K C   1 
ATOM   11580 O  O   . PRO K  1 66  ? 43.532 -106.001 -5.723   1.00 118.32 ? 67  PRO K O   1 
ATOM   11581 C  CB  . PRO K  1 66  ? 41.504 -103.561 -6.101   1.00 104.28 ? 67  PRO K CB  1 
ATOM   11582 C  CG  . PRO K  1 66  ? 41.212 -102.613 -4.995   1.00 102.49 ? 67  PRO K CG  1 
ATOM   11583 C  CD  . PRO K  1 66  ? 40.222 -103.297 -4.104   1.00 102.54 ? 67  PRO K CD  1 
ATOM   11584 N  N   . LEU K  1 67  ? 43.136 -105.035 -3.726   1.00 116.90 ? 68  LEU K N   1 
ATOM   11585 C  CA  . LEU K  1 67  ? 44.429 -105.441 -3.146   1.00 123.41 ? 68  LEU K CA  1 
ATOM   11586 C  C   . LEU K  1 67  ? 44.352 -106.815 -2.425   1.00 128.57 ? 68  LEU K C   1 
ATOM   11587 O  O   . LEU K  1 67  ? 45.266 -107.183 -1.665   1.00 134.43 ? 68  LEU K O   1 
ATOM   11588 C  CB  . LEU K  1 67  ? 44.949 -104.341 -2.200   1.00 123.94 ? 68  LEU K CB  1 
ATOM   11589 C  CG  . LEU K  1 67  ? 45.160 -102.955 -2.836   1.00 120.02 ? 68  LEU K CG  1 
ATOM   11590 C  CD1 . LEU K  1 67  ? 45.886 -101.991 -1.890   1.00 122.13 ? 68  LEU K CD1 1 
ATOM   11591 C  CD2 . LEU K  1 67  ? 45.918 -103.078 -4.166   1.00 120.82 ? 68  LEU K CD2 1 
ATOM   11592 N  N   . SER K  1 68  ? 43.241 -107.539 -2.639   1.00 126.70 ? 69  SER K N   1 
ATOM   11593 C  CA  . SER K  1 68  ? 43.078 -108.940 -2.193   1.00 131.69 ? 69  SER K CA  1 
ATOM   11594 C  C   . SER K  1 68  ? 43.335 -109.140 -0.692   1.00 136.02 ? 69  SER K C   1 
ATOM   11595 O  O   . SER K  1 68  ? 44.022 -110.077 -0.291   1.00 142.66 ? 69  SER K O   1 
ATOM   11596 C  CB  . SER K  1 68  ? 44.014 -109.856 -3.001   1.00 136.98 ? 69  SER K CB  1 
ATOM   11597 O  OG  . SER K  1 68  ? 43.981 -109.558 -4.387   1.00 133.80 ? 69  SER K OG  1 
ATOM   11598 N  N   . ARG K  1 69  ? 42.798 -108.243 0.127    1.00 132.80 ? 70  ARG K N   1 
ATOM   11599 C  CA  . ARG K  1 69  ? 43.013 -108.289 1.579    1.00 137.08 ? 70  ARG K CA  1 
ATOM   11600 C  C   . ARG K  1 69  ? 41.761 -108.835 2.319    1.00 136.42 ? 70  ARG K C   1 
ATOM   11601 O  O   . ARG K  1 69  ? 40.749 -109.205 1.706    1.00 133.05 ? 70  ARG K O   1 
ATOM   11602 C  CB  . ARG K  1 69  ? 43.442 -106.899 2.118    1.00 135.37 ? 70  ARG K CB  1 
ATOM   11603 N  N   . LYS K  1 70  ? 41.872 -108.903 3.642    1.00 140.38 ? 71  LYS K N   1 
ATOM   11604 C  CA  . LYS K  1 70  ? 40.773 -109.294 4.533    1.00 140.48 ? 71  LYS K CA  1 
ATOM   11605 C  C   . LYS K  1 70  ? 39.929 -108.076 4.967    1.00 134.92 ? 71  LYS K C   1 
ATOM   11606 O  O   . LYS K  1 70  ? 40.405 -106.917 4.955    1.00 132.53 ? 71  LYS K O   1 
ATOM   11607 C  CB  . LYS K  1 70  ? 41.348 -109.943 5.796    1.00 148.34 ? 71  LYS K CB  1 
ATOM   11608 C  CG  . LYS K  1 70  ? 42.278 -111.141 5.550    1.00 155.56 ? 71  LYS K CG  1 
ATOM   11609 C  CD  . LYS K  1 70  ? 41.509 -112.462 5.634    1.00 158.64 ? 71  LYS K CD  1 
ATOM   11610 C  CE  . LYS K  1 70  ? 42.418 -113.669 5.522    1.00 166.55 ? 71  LYS K CE  1 
ATOM   11611 N  NZ  . LYS K  1 70  ? 41.582 -114.894 5.635    1.00 169.37 ? 71  LYS K NZ  1 
ATOM   11612 N  N   . HIS K  1 71  ? 38.695 -108.355 5.393    1.00 133.37 ? 72  HIS K N   1 
ATOM   11613 C  CA  . HIS K  1 71  ? 37.790 -107.302 5.857    1.00 128.92 ? 72  HIS K CA  1 
ATOM   11614 C  C   . HIS K  1 71  ? 38.360 -106.618 7.100    1.00 132.13 ? 72  HIS K C   1 
ATOM   11615 O  O   . HIS K  1 71  ? 39.088 -107.231 7.892    1.00 138.50 ? 72  HIS K O   1 
ATOM   11616 C  CB  . HIS K  1 71  ? 36.368 -107.834 6.148    1.00 127.79 ? 72  HIS K CB  1 
ATOM   11617 C  CG  . HIS K  1 71  ? 35.387 -106.760 6.533    1.00 123.63 ? 72  HIS K CG  1 
ATOM   11618 N  ND1 . HIS K  1 71  ? 34.933 -105.799 5.646    1.00 117.50 ? 72  HIS K ND1 1 
ATOM   11619 C  CD2 . HIS K  1 71  ? 34.801 -106.471 7.719    1.00 125.07 ? 72  HIS K CD2 1 
ATOM   11620 C  CE1 . HIS K  1 71  ? 34.106 -104.973 6.268    1.00 115.26 ? 72  HIS K CE1 1 
ATOM   11621 N  NE2 . HIS K  1 71  ? 34.005 -105.362 7.526    1.00 119.61 ? 72  HIS K NE2 1 
ATOM   11622 N  N   . GLY K  1 72  ? 38.018 -105.340 7.251    1.00 128.11 ? 73  GLY K N   1 
ATOM   11623 C  CA  . GLY K  1 72  ? 38.398 -104.572 8.423    1.00 130.89 ? 73  GLY K CA  1 
ATOM   11624 C  C   . GLY K  1 72  ? 37.656 -103.247 8.568    1.00 126.38 ? 73  GLY K C   1 
ATOM   11625 O  O   . GLY K  1 72  ? 36.739 -102.907 7.791    1.00 120.75 ? 73  GLY K O   1 
ATOM   11626 N  N   . GLY K  1 73  ? 38.045 -102.517 9.615    1.00 129.54 ? 74  GLY K N   1 
ATOM   11627 C  CA  . GLY K  1 73  ? 37.533 -101.170 9.875    1.00 126.54 ? 74  GLY K CA  1 
ATOM   11628 C  C   . GLY K  1 73  ? 38.309 -100.204 9.016    1.00 123.76 ? 74  GLY K C   1 
ATOM   11629 O  O   . GLY K  1 73  ? 39.383 -100.536 8.542    1.00 125.75 ? 74  GLY K O   1 
ATOM   11630 N  N   . PRO K  1 74  ? 37.771 -99.010  8.797    1.00 119.91 ? 75  PRO K N   1 
ATOM   11631 C  CA  . PRO K  1 74  ? 38.433 -98.062  7.881    1.00 117.47 ? 75  PRO K CA  1 
ATOM   11632 C  C   . PRO K  1 74  ? 39.820 -97.586  8.364    1.00 122.41 ? 75  PRO K C   1 
ATOM   11633 O  O   . PRO K  1 74  ? 40.754 -97.379  7.549    1.00 122.15 ? 75  PRO K O   1 
ATOM   11634 C  CB  . PRO K  1 74  ? 37.453 -96.868  7.824    1.00 113.60 ? 75  PRO K CB  1 
ATOM   11635 C  CG  . PRO K  1 74  ? 36.619 -96.989  9.057    1.00 115.97 ? 75  PRO K CG  1 
ATOM   11636 C  CD  . PRO K  1 74  ? 36.531 -98.465  9.366    1.00 118.30 ? 75  PRO K CD  1 
ATOM   11637 N  N   . LYS K  1 75  ? 39.947 -97.427  9.680    1.00 127.34 ? 76  LYS K N   1 
ATOM   11638 C  CA  . LYS K  1 75  ? 41.239 -97.065  10.284   1.00 133.18 ? 76  LYS K CA  1 
ATOM   11639 C  C   . LYS K  1 75  ? 42.265 -98.201  10.208   1.00 137.43 ? 76  LYS K C   1 
ATOM   11640 O  O   . LYS K  1 75  ? 43.471 -97.947  10.141   1.00 141.00 ? 76  LYS K O   1 
ATOM   11641 C  CB  . LYS K  1 75  ? 41.077 -96.703  11.751   1.00 138.10 ? 76  LYS K CB  1 
ATOM   11642 C  CG  . LYS K  1 75  ? 39.965 -95.720  12.027   1.00 135.59 ? 76  LYS K CG  1 
ATOM   11643 C  CD  . LYS K  1 75  ? 40.260 -94.987  13.338   1.00 141.80 ? 76  LYS K CD  1 
ATOM   11644 C  CE  . LYS K  1 75  ? 39.057 -94.172  13.851   1.00 140.38 ? 76  LYS K CE  1 
ATOM   11645 N  NZ  . LYS K  1 75  ? 39.262 -93.722  15.284   1.00 147.05 ? 76  LYS K NZ  1 
ATOM   11646 N  N   . ASP K  1 76  ? 41.779 -99.445  10.234   1.00 137.65 ? 77  ASP K N   1 
ATOM   11647 C  CA  . ASP K  1 76  ? 42.644 -100.627 10.078   1.00 141.88 ? 77  ASP K CA  1 
ATOM   11648 C  C   . ASP K  1 76  ? 43.426 -100.582 8.753    1.00 139.73 ? 77  ASP K C   1 
ATOM   11649 O  O   . ASP K  1 76  ? 42.891 -100.220 7.689    1.00 133.48 ? 77  ASP K O   1 
ATOM   11650 C  CB  . ASP K  1 76  ? 41.838 -101.949 10.168   1.00 141.89 ? 77  ASP K CB  1 
ATOM   11651 C  CG  . ASP K  1 76  ? 41.316 -102.249 11.599   1.00 146.36 ? 77  ASP K CG  1 
ATOM   11652 O  OD1 . ASP K  1 76  ? 41.982 -101.876 12.597   1.00 152.15 ? 77  ASP K OD1 1 
ATOM   11653 O  OD2 . ASP K  1 76  ? 40.241 -102.870 11.737   1.00 144.78 ? 77  ASP K OD2 1 
ATOM   11654 N  N   . GLU K  1 77  ? 44.706 -100.928 8.832    1.00 145.47 ? 78  GLU K N   1 
ATOM   11655 C  CA  . GLU K  1 77  ? 45.518 -101.014 7.629    1.00 144.63 ? 78  GLU K CA  1 
ATOM   11656 C  C   . GLU K  1 77  ? 45.029 -102.208 6.828    1.00 142.38 ? 78  GLU K C   1 
ATOM   11657 O  O   . GLU K  1 77  ? 44.779 -102.062 5.629    1.00 137.38 ? 78  GLU K O   1 
ATOM   11658 C  CB  . GLU K  1 77  ? 47.011 -101.160 7.929    1.00 152.14 ? 78  GLU K CB  1 
ATOM   11659 C  CG  . GLU K  1 77  ? 47.804 -101.724 6.709    1.00 153.01 ? 78  GLU K CG  1 
ATOM   11660 C  CD  . GLU K  1 77  ? 49.343 -101.579 6.804    1.00 160.66 ? 78  GLU K CD  1 
ATOM   11661 O  OE1 . GLU K  1 77  ? 49.916 -101.697 7.934    1.00 167.51 ? 78  GLU K OE1 1 
ATOM   11662 O  OE2 . GLU K  1 77  ? 49.975 -101.374 5.724    1.00 159.71 ? 78  GLU K OE2 1 
ATOM   11663 N  N   . GLU K  1 78  ? 44.934 -103.376 7.484    1.00 146.65 ? 79  GLU K N   1 
ATOM   11664 C  CA  . GLU K  1 78  ? 44.376 -104.586 6.857    1.00 145.40 ? 79  GLU K CA  1 
ATOM   11665 C  C   . GLU K  1 78  ? 42.855 -104.429 6.708    1.00 139.05 ? 79  GLU K C   1 
ATOM   11666 O  O   . GLU K  1 78  ? 42.075 -104.802 7.601    1.00 140.26 ? 79  GLU K O   1 
ATOM   11667 C  CB  . GLU K  1 78  ? 44.727 -105.863 7.641    1.00 152.74 ? 79  GLU K CB  1 
ATOM   11668 C  CG  . GLU K  1 78  ? 44.267 -107.200 6.957    1.00 152.78 ? 79  GLU K CG  1 
ATOM   11669 C  CD  . GLU K  1 78  ? 45.175 -107.667 5.786    1.00 154.49 ? 79  GLU K CD  1 
ATOM   11670 O  OE1 . GLU K  1 78  ? 46.165 -106.956 5.451    1.00 155.62 ? 79  GLU K OE1 1 
ATOM   11671 O  OE2 . GLU K  1 78  ? 44.909 -108.762 5.206    1.00 155.08 ? 79  GLU K OE2 1 
ATOM   11672 N  N   . ARG K  1 79  ? 42.458 -103.853 5.572    1.00 132.72 ? 80  ARG K N   1 
ATOM   11673 C  CA  . ARG K  1 79  ? 41.045 -103.628 5.234    1.00 126.50 ? 80  ARG K CA  1 
ATOM   11674 C  C   . ARG K  1 79  ? 40.811 -103.867 3.735    1.00 122.15 ? 80  ARG K C   1 
ATOM   11675 O  O   . ARG K  1 79  ? 41.764 -103.983 2.959    1.00 123.30 ? 80  ARG K O   1 
ATOM   11676 C  CB  . ARG K  1 79  ? 40.619 -102.198 5.620    1.00 123.04 ? 80  ARG K CB  1 
ATOM   11677 C  CG  . ARG K  1 79  ? 41.472 -101.102 4.982    1.00 121.56 ? 80  ARG K CG  1 
ATOM   11678 C  CD  . ARG K  1 79  ? 40.893 -99.709  5.197    1.00 118.06 ? 80  ARG K CD  1 
ATOM   11679 N  NE  . ARG K  1 79  ? 39.882 -99.358  4.192    1.00 111.71 ? 80  ARG K NE  1 
ATOM   11680 C  CZ  . ARG K  1 79  ? 39.376 -98.135  4.018    1.00 108.11 ? 80  ARG K CZ  1 
ATOM   11681 N  NH1 . ARG K  1 79  ? 39.773 -97.127  4.777    1.00 110.10 ? 80  ARG K NH1 1 
ATOM   11682 N  NH2 . ARG K  1 79  ? 38.462 -97.912  3.075    1.00 103.18 ? 80  ARG K NH2 1 
ATOM   11683 N  N   . HIS K  1 80  ? 39.540 -103.961 3.347    1.00 117.65 ? 81  HIS K N   1 
ATOM   11684 C  CA  . HIS K  1 80  ? 39.161 -103.850 1.941    1.00 112.74 ? 81  HIS K CA  1 
ATOM   11685 C  C   . HIS K  1 80  ? 39.178 -102.358 1.577    1.00 108.56 ? 81  HIS K C   1 
ATOM   11686 O  O   . HIS K  1 80  ? 38.884 -101.489 2.430    1.00 107.92 ? 81  HIS K O   1 
ATOM   11687 C  CB  . HIS K  1 80  ? 37.759 -104.397 1.689    1.00 109.88 ? 81  HIS K CB  1 
ATOM   11688 C  CG  . HIS K  1 80  ? 37.596 -105.853 2.021    1.00 114.06 ? 81  HIS K CG  1 
ATOM   11689 N  ND1 . HIS K  1 80  ? 36.407 -106.390 2.478    1.00 113.66 ? 81  HIS K ND1 1 
ATOM   11690 C  CD2 . HIS K  1 80  ? 38.464 -106.887 1.943    1.00 118.98 ? 81  HIS K CD2 1 
ATOM   11691 C  CE1 . HIS K  1 80  ? 36.547 -107.692 2.651    1.00 118.20 ? 81  HIS K CE1 1 
ATOM   11692 N  NE2 . HIS K  1 80  ? 37.787 -108.021 2.336    1.00 121.54 ? 81  HIS K NE2 1 
ATOM   11693 N  N   . VAL K  1 81  ? 39.516 -102.065 0.317    1.00 106.00 ? 82  VAL K N   1 
ATOM   11694 C  CA  . VAL K  1 81  ? 39.515 -100.675 -0.176   1.00 102.08 ? 82  VAL K CA  1 
ATOM   11695 C  C   . VAL K  1 81  ? 38.146 -100.035 0.053    1.00 97.84  ? 82  VAL K C   1 
ATOM   11696 O  O   . VAL K  1 81  ? 38.046 -98.856  0.425    1.00 96.48  ? 82  VAL K O   1 
ATOM   11697 C  CB  . VAL K  1 81  ? 39.884 -100.574 -1.681   1.00 99.93  ? 82  VAL K CB  1 
ATOM   11698 C  CG1 . VAL K  1 81  ? 39.725 -99.134  -2.182   1.00 95.92  ? 82  VAL K CG1 1 
ATOM   11699 C  CG2 . VAL K  1 81  ? 41.316 -101.018 -1.925   1.00 104.59 ? 82  VAL K CG2 1 
ATOM   11700 N  N   . GLY K  1 82  ? 37.096 -100.833 -0.147   1.00 96.44  ? 83  GLY K N   1 
ATOM   11701 C  CA  . GLY K  1 82  ? 35.709 -100.359 0.002    1.00 93.07  ? 83  GLY K CA  1 
ATOM   11702 C  C   . GLY K  1 82  ? 35.111 -100.354 1.412    1.00 94.99  ? 83  GLY K C   1 
ATOM   11703 O  O   . GLY K  1 82  ? 33.943 -99.975  1.584    1.00 92.66  ? 83  GLY K O   1 
ATOM   11704 N  N   . ASP K  1 83  ? 35.893 -100.764 2.416    1.00 99.62  ? 84  ASP K N   1 
ATOM   11705 C  CA  . ASP K  1 83  ? 35.407 -100.827 3.806    1.00 102.06 ? 84  ASP K CA  1 
ATOM   11706 C  C   . ASP K  1 83  ? 35.391 -99.446  4.452    1.00 101.55 ? 84  ASP K C   1 
ATOM   11707 O  O   . ASP K  1 83  ? 36.388 -98.992  5.013    1.00 104.64 ? 84  ASP K O   1 
ATOM   11708 C  CB  . ASP K  1 83  ? 36.278 -101.759 4.635    1.00 107.78 ? 84  ASP K CB  1 
ATOM   11709 C  CG  . ASP K  1 83  ? 36.042 -103.201 4.312    1.00 109.04 ? 84  ASP K CG  1 
ATOM   11710 O  OD1 . ASP K  1 83  ? 35.011 -103.520 3.685    1.00 105.42 ? 84  ASP K OD1 1 
ATOM   11711 O  OD2 . ASP K  1 83  ? 36.903 -104.012 4.692    1.00 114.04 ? 84  ASP K OD2 1 
ATOM   11712 N  N   . LEU K  1 84  ? 34.253 -98.775  4.358    1.00 98.27  ? 85  LEU K N   1 
ATOM   11713 C  CA  . LEU K  1 84  ? 34.100 -97.438  4.956    1.00 98.20  ? 85  LEU K CA  1 
ATOM   11714 C  C   . LEU K  1 84  ? 33.538 -97.481  6.386    1.00 101.53 ? 85  LEU K C   1 
ATOM   11715 O  O   . LEU K  1 84  ? 33.262 -96.414  6.987    1.00 101.88 ? 85  LEU K O   1 
ATOM   11716 C  CB  . LEU K  1 84  ? 33.230 -96.539  4.063    1.00 93.46  ? 85  LEU K CB  1 
ATOM   11717 C  CG  . LEU K  1 84  ? 33.965 -96.003  2.833    1.00 90.84  ? 85  LEU K CG  1 
ATOM   11718 C  CD1 . LEU K  1 84  ? 33.014 -95.201  1.959    1.00 86.61  ? 85  LEU K CD1 1 
ATOM   11719 C  CD2 . LEU K  1 84  ? 35.168 -95.151  3.266    1.00 93.22  ? 85  LEU K CD2 1 
ATOM   11720 N  N   . GLY K  1 85  ? 33.386 -98.703  6.924    1.00 104.32 ? 86  GLY K N   1 
ATOM   11721 C  CA  . GLY K  1 85  ? 32.984 -98.903  8.327    1.00 108.33 ? 86  GLY K CA  1 
ATOM   11722 C  C   . GLY K  1 85  ? 31.492 -98.735  8.581    1.00 106.73 ? 86  GLY K C   1 
ATOM   11723 O  O   . GLY K  1 85  ? 30.671 -99.315  7.863    1.00 104.18 ? 86  GLY K O   1 
ATOM   11724 N  N   . ASN K  1 86  ? 31.138 -97.922  9.583    1.00 108.64 ? 87  ASN K N   1 
ATOM   11725 C  CA  . ASN K  1 86  ? 29.731 -97.752  9.990    1.00 108.04 ? 87  ASN K CA  1 
ATOM   11726 C  C   . ASN K  1 86  ? 29.179 -96.354  9.827    1.00 105.71 ? 87  ASN K C   1 
ATOM   11727 O  O   . ASN K  1 86  ? 29.924 -95.377  9.795    1.00 105.77 ? 87  ASN K O   1 
ATOM   11728 C  CB  . ASN K  1 86  ? 29.553 -98.152  11.451   1.00 113.47 ? 87  ASN K CB  1 
ATOM   11729 C  CG  . ASN K  1 86  ? 29.560 -99.673  11.654   1.00 116.12 ? 87  ASN K CG  1 
ATOM   11730 O  OD1 . ASN K  1 86  ? 28.775 -100.408 11.037   1.00 114.18 ? 87  ASN K OD1 1 
ATOM   11731 N  ND2 . ASN K  1 86  ? 30.448 -100.147 12.534   1.00 121.27 ? 87  ASN K ND2 1 
ATOM   11732 N  N   . VAL K  1 87  ? 27.856 -96.286  9.724    1.00 104.29 ? 88  VAL K N   1 
ATOM   11733 C  CA  . VAL K  1 87  ? 27.117 -95.025  9.792    1.00 103.52 ? 88  VAL K CA  1 
ATOM   11734 C  C   . VAL K  1 87  ? 26.094 -95.147  10.908   1.00 107.06 ? 88  VAL K C   1 
ATOM   11735 O  O   . VAL K  1 87  ? 25.508 -96.207  11.113   1.00 107.98 ? 88  VAL K O   1 
ATOM   11736 C  CB  . VAL K  1 87  ? 26.373 -94.678  8.473    1.00 98.60  ? 88  VAL K CB  1 
ATOM   11737 C  CG1 . VAL K  1 87  ? 27.354 -94.359  7.342    1.00 95.43  ? 88  VAL K CG1 1 
ATOM   11738 C  CG2 . VAL K  1 87  ? 25.457 -95.797  8.075    1.00 97.62  ? 88  VAL K CG2 1 
ATOM   11739 N  N   . THR K  1 88  ? 25.869 -94.047  11.619   1.00 109.50 ? 89  THR K N   1 
ATOM   11740 C  CA  . THR K  1 88  ? 24.968 -94.046  12.798   1.00 113.81 ? 89  THR K CA  1 
ATOM   11741 C  C   . THR K  1 88  ? 23.589 -93.375  12.546   1.00 112.78 ? 89  THR K C   1 
ATOM   11742 O  O   . THR K  1 88  ? 23.478 -92.203  12.115   1.00 111.29 ? 89  THR K O   1 
ATOM   11743 C  CB  . THR K  1 88  ? 25.647 -93.390  14.044   1.00 118.91 ? 89  THR K CB  1 
ATOM   11744 O  OG1 . THR K  1 88  ? 26.705 -94.231  14.517   1.00 121.46 ? 89  THR K OG1 1 
ATOM   11745 C  CG2 . THR K  1 88  ? 24.659 -93.224  15.180   1.00 123.42 ? 89  THR K CG2 1 
ATOM   11746 N  N   . ALA K  1 89  ? 22.543 -94.129  12.861   1.00 114.09 ? 90  ALA K N   1 
ATOM   11747 C  CA  . ALA K  1 89  ? 21.178 -93.671  12.670   1.00 113.94 ? 90  ALA K CA  1 
ATOM   11748 C  C   . ALA K  1 89  ? 20.539 -93.248  13.987   1.00 119.42 ? 90  ALA K C   1 
ATOM   11749 O  O   . ALA K  1 89  ? 20.549 -94.010  14.964   1.00 123.17 ? 90  ALA K O   1 
ATOM   11750 C  CB  . ALA K  1 89  ? 20.352 -94.761  12.021   1.00 112.17 ? 90  ALA K CB  1 
ATOM   11751 N  N   . ASP K  1 90  ? 19.958 -92.043  13.983   1.00 120.15 ? 91  ASP K N   1 
ATOM   11752 C  CA  . ASP K  1 90  ? 19.268 -91.487  15.165   1.00 125.79 ? 91  ASP K CA  1 
ATOM   11753 C  C   . ASP K  1 90  ? 17.767 -91.874  15.226   1.00 127.41 ? 91  ASP K C   1 
ATOM   11754 O  O   . ASP K  1 90  ? 17.157 -92.255  14.197   1.00 123.80 ? 91  ASP K O   1 
ATOM   11755 C  CB  . ASP K  1 90  ? 19.459 -89.951  15.272   1.00 127.03 ? 91  ASP K CB  1 
ATOM   11756 C  CG  . ASP K  1 90  ? 18.614 -89.149  14.253   1.00 124.46 ? 91  ASP K CG  1 
ATOM   11757 O  OD1 . ASP K  1 90  ? 18.677 -87.903  14.295   1.00 126.21 ? 91  ASP K OD1 1 
ATOM   11758 O  OD2 . ASP K  1 90  ? 17.886 -89.728  13.419   1.00 121.34 ? 91  ASP K OD2 1 
ATOM   11759 N  N   . LYS K  1 91  ? 17.210 -91.770  16.442   1.00 133.18 ? 92  LYS K N   1 
ATOM   11760 C  CA  . LYS K  1 91  ? 15.781 -92.068  16.757   1.00 136.27 ? 92  LYS K CA  1 
ATOM   11761 C  C   . LYS K  1 91  ? 14.844 -92.138  15.545   1.00 132.58 ? 92  LYS K C   1 
ATOM   11762 O  O   . LYS K  1 91  ? 14.292 -93.197  15.239   1.00 131.86 ? 92  LYS K O   1 
ATOM   11763 C  CB  . LYS K  1 91  ? 15.161 -91.013  17.712   1.00 142.11 ? 92  LYS K CB  1 
ATOM   11764 C  CG  . LYS K  1 91  ? 16.112 -90.226  18.637   1.00 145.85 ? 92  LYS K CG  1 
ATOM   11765 C  CD  . LYS K  1 91  ? 16.696 -91.110  19.763   1.00 150.00 ? 92  LYS K CD  1 
ATOM   11766 C  CE  . LYS K  1 91  ? 17.195 -90.286  20.970   1.00 155.84 ? 92  LYS K CE  1 
ATOM   11767 N  NZ  . LYS K  1 91  ? 16.147 -90.082  22.038   1.00 162.68 ? 92  LYS K NZ  1 
ATOM   11768 N  N   . ASP K  1 92  ? 14.676 -90.996  14.869   1.00 130.75 ? 93  ASP K N   1 
ATOM   11769 C  CA  . ASP K  1 92  ? 13.689 -90.860  13.783   1.00 128.48 ? 93  ASP K CA  1 
ATOM   11770 C  C   . ASP K  1 92  ? 14.217 -91.461  12.459   1.00 122.17 ? 93  ASP K C   1 
ATOM   11771 O  O   . ASP K  1 92  ? 13.688 -91.170  11.378   1.00 119.81 ? 93  ASP K O   1 
ATOM   11772 C  CB  . ASP K  1 92  ? 13.176 -89.398  13.624   1.00 130.13 ? 93  ASP K CB  1 
ATOM   11773 C  CG  . ASP K  1 92  ? 13.859 -88.419  14.586   1.00 133.98 ? 93  ASP K CG  1 
ATOM   11774 O  OD1 . ASP K  1 92  ? 15.099 -88.182  14.434   1.00 131.69 ? 93  ASP K OD1 1 
ATOM   11775 O  OD2 . ASP K  1 92  ? 13.151 -87.911  15.498   1.00 139.49 ? 93  ASP K OD2 1 
ATOM   11776 N  N   . GLY K  1 93  ? 15.249 -92.300  12.553   1.00 120.16 ? 94  GLY K N   1 
ATOM   11777 C  CA  . GLY K  1 93  ? 15.718 -93.104  11.417   1.00 115.25 ? 94  GLY K CA  1 
ATOM   11778 C  C   . GLY K  1 93  ? 16.771 -92.455  10.506   1.00 110.88 ? 94  GLY K C   1 
ATOM   11779 O  O   . GLY K  1 93  ? 17.176 -93.043  9.494    1.00 106.64 ? 94  GLY K O   1 
ATOM   11780 N  N   . VAL K  1 94  ? 17.207 -91.242  10.873   1.00 112.78 ? 95  VAL K N   1 
ATOM   11781 C  CA  . VAL K  1 94  ? 18.052 -90.355  10.034   1.00 109.36 ? 95  VAL K CA  1 
ATOM   11782 C  C   . VAL K  1 94  ? 19.510 -90.621  10.347   1.00 108.51 ? 95  VAL K C   1 
ATOM   11783 O  O   . VAL K  1 94  ? 19.910 -90.672  11.519   1.00 112.50 ? 95  VAL K O   1 
ATOM   11784 C  CB  . VAL K  1 94  ? 17.735 -88.801  10.288   1.00 112.24 ? 95  VAL K CB  1 
ATOM   11785 C  CG1 . VAL K  1 94  ? 19.005 -87.976  10.666   1.00 112.37 ? 95  VAL K CG1 1 
ATOM   11786 C  CG2 . VAL K  1 94  ? 16.989 -88.168  9.100    1.00 110.16 ? 95  VAL K CG2 1 
ATOM   11787 N  N   . ALA K  1 95  ? 20.308 -90.805  9.304    1.00 103.68 ? 96  ALA K N   1 
ATOM   11788 C  CA  . ALA K  1 95  ? 21.743 -91.021  9.491    1.00 103.12 ? 96  ALA K CA  1 
ATOM   11789 C  C   . ALA K  1 95  ? 22.469 -89.908  8.746    1.00 100.89 ? 96  ALA K C   1 
ATOM   11790 O  O   . ALA K  1 95  ? 22.525 -89.911  7.510    1.00 97.02  ? 96  ALA K O   1 
ATOM   11791 C  CB  . ALA K  1 95  ? 22.176 -92.415  8.988    1.00 100.52 ? 96  ALA K CB  1 
ATOM   11792 N  N   . ASP K  1 96  ? 22.986 -88.938  9.496    1.00 103.89 ? 97  ASP K N   1 
ATOM   11793 C  CA  . ASP K  1 96  ? 23.682 -87.802  8.894    1.00 102.85 ? 97  ASP K CA  1 
ATOM   11794 C  C   . ASP K  1 96  ? 25.135 -88.178  8.689    1.00 101.54 ? 97  ASP K C   1 
ATOM   11795 O  O   . ASP K  1 96  ? 25.964 -87.999  9.581    1.00 104.99 ? 97  ASP K O   1 
ATOM   11796 C  CB  . ASP K  1 96  ? 23.546 -86.533  9.744    1.00 107.42 ? 97  ASP K CB  1 
ATOM   11797 C  CG  . ASP K  1 96  ? 22.221 -85.799  9.489    1.00 108.68 ? 97  ASP K CG  1 
ATOM   11798 O  OD1 . ASP K  1 96  ? 21.879 -85.562  8.297    1.00 105.17 ? 97  ASP K OD1 1 
ATOM   11799 O  OD2 . ASP K  1 96  ? 21.527 -85.461  10.487   1.00 113.53 ? 97  ASP K OD2 1 
ATOM   11800 N  N   . VAL K  1 97  ? 25.421 -88.700  7.499    1.00 97.11  ? 98  VAL K N   1 
ATOM   11801 C  CA  . VAL K  1 97  ? 26.755 -89.209  7.166    1.00 95.90  ? 98  VAL K CA  1 
ATOM   11802 C  C   . VAL K  1 97  ? 27.773 -88.080  6.980    1.00 96.63  ? 98  VAL K C   1 
ATOM   11803 O  O   . VAL K  1 97  ? 27.496 -87.070  6.303    1.00 95.34  ? 98  VAL K O   1 
ATOM   11804 C  CB  . VAL K  1 97  ? 26.756 -90.068  5.879    1.00 91.53  ? 98  VAL K CB  1 
ATOM   11805 C  CG1 . VAL K  1 97  ? 28.159 -90.662  5.622    1.00 90.89  ? 98  VAL K CG1 1 
ATOM   11806 C  CG2 . VAL K  1 97  ? 25.715 -91.196  5.969    1.00 91.16  ? 98  VAL K CG2 1 
ATOM   11807 N  N   . SER K  1 98  ? 28.931 -88.266  7.617    1.00 99.20  ? 99  SER K N   1 
ATOM   11808 C  CA  . SER K  1 98  ? 30.101 -87.387  7.432    1.00 100.51 ? 99  SER K CA  1 
ATOM   11809 C  C   . SER K  1 98  ? 31.414 -88.132  7.726    1.00 102.13 ? 99  SER K C   1 
ATOM   11810 O  O   . SER K  1 98  ? 31.954 -88.106  8.834    1.00 106.57 ? 99  SER K O   1 
ATOM   11811 C  CB  . SER K  1 98  ? 30.018 -86.113  8.288    1.00 104.87 ? 99  SER K CB  1 
ATOM   11812 O  OG  . SER K  1 98  ? 31.194 -85.310  8.141    1.00 106.30 ? 99  SER K OG  1 
ATOM   11813 N  N   . ILE K  1 99  ? 31.918 -88.794  6.698    1.00 98.88  ? 100 ILE K N   1 
ATOM   11814 C  CA  . ILE K  1 99  ? 33.152 -89.544  6.781    1.00 100.19 ? 100 ILE K CA  1 
ATOM   11815 C  C   . ILE K  1 99  ? 34.216 -88.768  6.024    1.00 100.03 ? 100 ILE K C   1 
ATOM   11816 O  O   . ILE K  1 99  ? 33.917 -87.901  5.214    1.00 97.98  ? 100 ILE K O   1 
ATOM   11817 C  CB  . ILE K  1 99  ? 32.957 -90.968  6.184    1.00 97.34  ? 100 ILE K CB  1 
ATOM   11818 C  CG1 . ILE K  1 99  ? 32.001 -91.773  7.075    1.00 98.75  ? 100 ILE K CG1 1 
ATOM   11819 C  CG2 . ILE K  1 99  ? 34.268 -91.698  6.028    1.00 98.87  ? 100 ILE K CG2 1 
ATOM   11820 C  CD1 . ILE K  1 99  ? 32.088 -93.300  6.879    1.00 98.17  ? 100 ILE K CD1 1 
ATOM   11821 N  N   . GLU K  1 100 ? 35.469 -89.052  6.334    1.00 103.12 ? 101 GLU K N   1 
ATOM   11822 C  CA  . GLU K  1 100 ? 36.604 -88.647  5.495    1.00 102.95 ? 101 GLU K CA  1 
ATOM   11823 C  C   . GLU K  1 100 ? 37.591 -89.828  5.407    1.00 104.19 ? 101 GLU K C   1 
ATOM   11824 O  O   . GLU K  1 100 ? 38.016 -90.370  6.430    1.00 108.33 ? 101 GLU K O   1 
ATOM   11825 C  CB  . GLU K  1 100 ? 37.285 -87.418  6.067    1.00 107.12 ? 101 GLU K CB  1 
ATOM   11826 C  CG  . GLU K  1 100 ? 38.386 -86.879  5.170    1.00 107.88 ? 101 GLU K CG  1 
ATOM   11827 C  CD  . GLU K  1 100 ? 38.905 -85.507  5.604    1.00 112.66 ? 101 GLU K CD  1 
ATOM   11828 O  OE1 . GLU K  1 100 ? 39.709 -84.905  4.836    1.00 112.79 ? 101 GLU K OE1 1 
ATOM   11829 O  OE2 . GLU K  1 100 ? 38.510 -85.039  6.708    1.00 116.12 ? 101 GLU K OE2 1 
ATOM   11830 N  N   . ASP K  1 101 ? 37.935 -90.239  4.191    1.00 101.19 ? 102 ASP K N   1 
ATOM   11831 C  CA  . ASP K  1 101 ? 38.721 -91.467  3.986    1.00 102.19 ? 102 ASP K CA  1 
ATOM   11832 C  C   . ASP K  1 101 ? 39.859 -91.287  2.978    1.00 102.33 ? 102 ASP K C   1 
ATOM   11833 O  O   . ASP K  1 101 ? 39.765 -90.518  2.016    1.00 99.66  ? 102 ASP K O   1 
ATOM   11834 C  CB  . ASP K  1 101 ? 37.810 -92.624  3.539    1.00 98.74  ? 102 ASP K CB  1 
ATOM   11835 C  CG  . ASP K  1 101 ? 38.493 -93.978  3.654    1.00 101.02 ? 102 ASP K CG  1 
ATOM   11836 O  OD1 . ASP K  1 101 ? 38.757 -94.422  4.798    1.00 105.07 ? 102 ASP K OD1 1 
ATOM   11837 O  OD2 . ASP K  1 101 ? 38.770 -94.599  2.605    1.00 99.07  ? 102 ASP K OD2 1 
ATOM   11838 N  N   . SER K  1 102 ? 40.922 -92.042  3.195    1.00 105.96 ? 103 SER K N   1 
ATOM   11839 C  CA  . SER K  1 102 ? 42.146 -91.919  2.403    1.00 107.42 ? 103 SER K CA  1 
ATOM   11840 C  C   . SER K  1 102 ? 42.461 -93.129  1.535    1.00 106.29 ? 103 SER K C   1 
ATOM   11841 O  O   . SER K  1 102 ? 43.291 -93.030  0.652    1.00 106.82 ? 103 SER K O   1 
ATOM   11842 C  CB  . SER K  1 102 ? 43.313 -91.654  3.342    1.00 113.76 ? 103 SER K CB  1 
ATOM   11843 O  OG  . SER K  1 102 ? 43.003 -90.535  4.164    1.00 115.45 ? 103 SER K OG  1 
ATOM   11844 N  N   . VAL K  1 103 ? 41.817 -94.264  1.786    1.00 105.45 ? 104 VAL K N   1 
ATOM   11845 C  CA  . VAL K  1 103 ? 42.055 -95.477  0.982    1.00 105.11 ? 104 VAL K CA  1 
ATOM   11846 C  C   . VAL K  1 103 ? 41.266 -95.426  -0.337   1.00 99.78  ? 104 VAL K C   1 
ATOM   11847 O  O   . VAL K  1 103 ? 41.818 -95.684  -1.419   1.00 99.43  ? 104 VAL K O   1 
ATOM   11848 C  CB  . VAL K  1 103 ? 41.684 -96.786  1.738    1.00 106.99 ? 104 VAL K CB  1 
ATOM   11849 C  CG1 . VAL K  1 103 ? 41.949 -98.016  0.862    1.00 106.99 ? 104 VAL K CG1 1 
ATOM   11850 C  CG2 . VAL K  1 103 ? 42.463 -96.893  3.037    1.00 113.17 ? 104 VAL K CG2 1 
ATOM   11851 N  N   . ILE K  1 104 ? 39.974 -95.103  -0.246   1.00 96.09  ? 105 ILE K N   1 
ATOM   11852 C  CA  . ILE K  1 104 ? 39.157 -94.969  -1.451   1.00 91.26  ? 105 ILE K CA  1 
ATOM   11853 C  C   . ILE K  1 104 ? 39.644 -93.774  -2.277   1.00 90.20  ? 105 ILE K C   1 
ATOM   11854 O  O   . ILE K  1 104 ? 40.308 -92.855  -1.742   1.00 92.46  ? 105 ILE K O   1 
ATOM   11855 C  CB  . ILE K  1 104 ? 37.646 -94.782  -1.143   1.00 88.17  ? 105 ILE K CB  1 
ATOM   11856 C  CG1 . ILE K  1 104 ? 37.382 -93.447  -0.416   1.00 88.36  ? 105 ILE K CG1 1 
ATOM   11857 C  CG2 . ILE K  1 104 ? 37.126 -95.989  -0.358   1.00 89.35  ? 105 ILE K CG2 1 
ATOM   11858 C  CD1 . ILE K  1 104 ? 35.939 -92.983  -0.511   1.00 84.80  ? 105 ILE K CD1 1 
ATOM   11859 N  N   . SER K  1 105 ? 39.297 -93.797  -3.569   1.00 87.10  ? 106 SER K N   1 
ATOM   11860 C  CA  . SER K  1 105 ? 39.601 -92.689  -4.480   1.00 85.92  ? 106 SER K CA  1 
ATOM   11861 C  C   . SER K  1 105 ? 38.634 -92.564  -5.657   1.00 81.89  ? 106 SER K C   1 
ATOM   11862 O  O   . SER K  1 105 ? 38.031 -93.539  -6.123   1.00 80.27  ? 106 SER K O   1 
ATOM   11863 C  CB  . SER K  1 105 ? 41.021 -92.810  -5.028   1.00 88.84  ? 106 SER K CB  1 
ATOM   11864 O  OG  . SER K  1 105 ? 41.414 -91.599  -5.663   1.00 88.40  ? 106 SER K OG  1 
ATOM   11865 N  N   . LEU K  1 106 ? 38.524 -91.337  -6.148   1.00 80.76  ? 107 LEU K N   1 
ATOM   11866 C  CA  . LEU K  1 106 ? 37.716 -91.048  -7.324   1.00 77.56  ? 107 LEU K CA  1 
ATOM   11867 C  C   . LEU K  1 106 ? 38.552 -91.088  -8.610   1.00 78.03  ? 107 LEU K C   1 
ATOM   11868 O  O   . LEU K  1 106 ? 38.147 -90.530  -9.628   1.00 76.35  ? 107 LEU K O   1 
ATOM   11869 C  CB  . LEU K  1 106 ? 37.055 -89.679  -7.165   1.00 76.56  ? 107 LEU K CB  1 
ATOM   11870 C  CG  . LEU K  1 106 ? 36.161 -89.537  -5.937   1.00 76.11  ? 107 LEU K CG  1 
ATOM   11871 C  CD1 . LEU K  1 106 ? 35.521 -88.154  -5.943   1.00 75.84  ? 107 LEU K CD1 1 
ATOM   11872 C  CD2 . LEU K  1 106 ? 35.117 -90.631  -5.895   1.00 73.92  ? 107 LEU K CD2 1 
ATOM   11873 N  N   . SER K  1 107 ? 39.717 -91.736  -8.553   1.00 80.87  ? 108 SER K N   1 
ATOM   11874 C  CA  . SER K  1 107 ? 40.623 -91.854  -9.710   1.00 82.01  ? 108 SER K CA  1 
ATOM   11875 C  C   . SER K  1 107 ? 41.683 -92.951  -9.522   1.00 85.29  ? 108 SER K C   1 
ATOM   11876 O  O   . SER K  1 107 ? 42.243 -93.129  -8.434   1.00 87.95  ? 108 SER K O   1 
ATOM   11877 C  CB  . SER K  1 107 ? 41.306 -90.501  -10.014  1.00 83.32  ? 108 SER K CB  1 
ATOM   11878 O  OG  . SER K  1 107 ? 41.974 -89.964  -8.887   1.00 86.08  ? 108 SER K OG  1 
ATOM   11879 N  N   . GLY K  1 108 ? 41.940 -93.690  -10.592  1.00 85.62  ? 109 GLY K N   1 
ATOM   11880 C  CA  . GLY K  1 108 ? 43.034 -94.671  -10.620  1.00 89.64  ? 109 GLY K CA  1 
ATOM   11881 C  C   . GLY K  1 108 ? 42.698 -96.107  -10.235  1.00 90.45  ? 109 GLY K C   1 
ATOM   11882 O  O   . GLY K  1 108 ? 41.581 -96.582  -10.437  1.00 87.74  ? 109 GLY K O   1 
ATOM   11883 N  N   . ASP K  1 109 ? 43.691 -96.803  -9.685   1.00 94.89  ? 110 ASP K N   1 
ATOM   11884 C  CA  . ASP K  1 109 ? 43.551 -98.218  -9.238   1.00 96.96  ? 110 ASP K CA  1 
ATOM   11885 C  C   . ASP K  1 109 ? 42.381 -98.443  -8.270   1.00 94.38  ? 110 ASP K C   1 
ATOM   11886 O  O   . ASP K  1 109 ? 41.618 -99.416  -8.388   1.00 93.19  ? 110 ASP K O   1 
ATOM   11887 C  CB  . ASP K  1 109 ? 44.853 -98.685  -8.531   1.00 102.86 ? 110 ASP K CB  1 
ATOM   11888 C  CG  . ASP K  1 109 ? 45.063 -100.222 -8.620   1.00 106.70 ? 110 ASP K CG  1 
ATOM   11889 O  OD1 . ASP K  1 109 ? 44.619 -100.964 -7.700   1.00 107.32 ? 110 ASP K OD1 1 
ATOM   11890 O  OD2 . ASP K  1 109 ? 45.658 -100.682 -9.638   1.00 109.18 ? 110 ASP K OD2 1 
ATOM   11891 N  N   . HIS K  1 110 ? 42.293 -97.515  -7.311   1.00 93.81  ? 111 HIS K N   1 
ATOM   11892 C  CA  . HIS K  1 110 ? 41.305 -97.523  -6.222   1.00 92.33  ? 111 HIS K CA  1 
ATOM   11893 C  C   . HIS K  1 110 ? 39.975 -96.872  -6.618   1.00 87.43  ? 111 HIS K C   1 
ATOM   11894 O  O   . HIS K  1 110 ? 39.110 -96.669  -5.746   1.00 86.18  ? 111 HIS K O   1 
ATOM   11895 C  CB  . HIS K  1 110 ? 41.881 -96.766  -4.993   1.00 94.81  ? 111 HIS K CB  1 
ATOM   11896 C  CG  . HIS K  1 110 ? 43.015 -97.477  -4.310   1.00 100.51 ? 111 HIS K CG  1 
ATOM   11897 N  ND1 . HIS K  1 110 ? 43.484 -97.107  -3.060   1.00 103.60 ? 111 HIS K ND1 1 
ATOM   11898 C  CD2 . HIS K  1 110 ? 43.760 -98.548  -4.693   1.00 103.92 ? 111 HIS K CD2 1 
ATOM   11899 C  CE1 . HIS K  1 110 ? 44.467 -97.918  -2.705   1.00 108.60 ? 111 HIS K CE1 1 
ATOM   11900 N  NE2 . HIS K  1 110 ? 44.652 -98.802  -3.675   1.00 109.19 ? 111 HIS K NE2 1 
ATOM   11901 N  N   . CYS K  1 111 ? 39.819 -96.535  -7.906   1.00 85.11  ? 112 CYS K N   1 
ATOM   11902 C  CA  . CYS K  1 111 ? 38.681 -95.747  -8.378   1.00 80.96  ? 112 CYS K CA  1 
ATOM   11903 C  C   . CYS K  1 111 ? 37.370 -96.452  -8.052   1.00 79.13  ? 112 CYS K C   1 
ATOM   11904 O  O   . CYS K  1 111 ? 37.135 -97.574  -8.519   1.00 79.41  ? 112 CYS K O   1 
ATOM   11905 C  CB  . CYS K  1 111 ? 38.777 -95.511  -9.873   1.00 79.76  ? 112 CYS K CB  1 
ATOM   11906 S  SG  . CYS K  1 111 ? 37.567 -94.335  -10.520  1.00 76.13  ? 112 CYS K SG  1 
ATOM   11907 N  N   . ILE K  1 112 ? 36.546 -95.795  -7.222   1.00 77.60  ? 113 ILE K N   1 
ATOM   11908 C  CA  . ILE K  1 112 ? 35.240 -96.337  -6.802   1.00 76.18  ? 113 ILE K CA  1 
ATOM   11909 C  C   . ILE K  1 112 ? 34.108 -95.923  -7.742   1.00 73.15  ? 113 ILE K C   1 
ATOM   11910 O  O   . ILE K  1 112 ? 32.987 -96.430  -7.627   1.00 72.21  ? 113 ILE K O   1 
ATOM   11911 C  CB  . ILE K  1 112 ? 34.858 -95.915  -5.360   1.00 76.84  ? 113 ILE K CB  1 
ATOM   11912 C  CG1 . ILE K  1 112 ? 34.781 -94.378  -5.221   1.00 75.75  ? 113 ILE K CG1 1 
ATOM   11913 C  CG2 . ILE K  1 112 ? 35.833 -96.523  -4.354   1.00 80.52  ? 113 ILE K CG2 1 
ATOM   11914 C  CD1 . ILE K  1 112 ? 33.888 -93.897  -4.069   1.00 75.79  ? 113 ILE K CD1 1 
ATOM   11915 N  N   . ILE K  1 113 ? 34.397 -94.988  -8.651   1.00 72.00  ? 114 ILE K N   1 
ATOM   11916 C  CA  . ILE K  1 113 ? 33.395 -94.485  -9.580   1.00 69.46  ? 114 ILE K CA  1 
ATOM   11917 C  C   . ILE K  1 113 ? 32.967 -95.597  -10.503  1.00 69.13  ? 114 ILE K C   1 
ATOM   11918 O  O   . ILE K  1 113 ? 33.791 -96.324  -11.027  1.00 70.47  ? 114 ILE K O   1 
ATOM   11919 C  CB  . ILE K  1 113 ? 33.907 -93.310  -10.413  1.00 69.01  ? 114 ILE K CB  1 
ATOM   11920 C  CG1 . ILE K  1 113 ? 33.995 -92.052  -9.554   1.00 69.36  ? 114 ILE K CG1 1 
ATOM   11921 C  CG2 . ILE K  1 113 ? 32.977 -93.055  -11.587  1.00 67.25  ? 114 ILE K CG2 1 
ATOM   11922 C  CD1 . ILE K  1 113 ? 34.696 -90.881  -10.248  1.00 70.05  ? 114 ILE K CD1 1 
ATOM   11923 N  N   . GLY K  1 114 ? 31.661 -95.717  -10.681  1.00 67.82  ? 115 GLY K N   1 
ATOM   11924 C  CA  . GLY K  1 114 ? 31.073 -96.778  -11.494  1.00 68.15  ? 115 GLY K CA  1 
ATOM   11925 C  C   . GLY K  1 114 ? 30.788 -98.037  -10.694  1.00 69.68  ? 115 GLY K C   1 
ATOM   11926 O  O   . GLY K  1 114 ? 30.327 -99.045  -11.242  1.00 70.46  ? 115 GLY K O   1 
ATOM   11927 N  N   . ARG K  1 115 ? 31.064 -97.977  -9.393   1.00 70.51  ? 116 ARG K N   1 
ATOM   11928 C  CA  . ARG K  1 115 ? 30.803 -99.093  -8.487   1.00 72.47  ? 116 ARG K CA  1 
ATOM   11929 C  C   . ARG K  1 115 ? 29.663 -98.722  -7.520   1.00 71.83  ? 116 ARG K C   1 
ATOM   11930 O  O   . ARG K  1 115 ? 29.218 -97.563  -7.449   1.00 70.05  ? 116 ARG K O   1 
ATOM   11931 C  CB  . ARG K  1 115 ? 32.069 -99.465  -7.717   1.00 74.85  ? 116 ARG K CB  1 
ATOM   11932 C  CG  . ARG K  1 115 ? 33.252 -99.739  -8.612   1.00 76.12  ? 116 ARG K CG  1 
ATOM   11933 C  CD  . ARG K  1 115 ? 34.469 -100.197 -7.844   1.00 79.44  ? 116 ARG K CD  1 
ATOM   11934 N  NE  . ARG K  1 115 ? 35.645 -100.297 -8.707   1.00 80.72  ? 116 ARG K NE  1 
ATOM   11935 C  CZ  . ARG K  1 115 ? 35.953 -101.347 -9.480   1.00 82.75  ? 116 ARG K CZ  1 
ATOM   11936 N  NH1 . ARG K  1 115 ? 35.183 -102.438 -9.524   1.00 83.70  ? 116 ARG K NH1 1 
ATOM   11937 N  NH2 . ARG K  1 115 ? 37.057 -101.308 -10.217  1.00 84.58  ? 116 ARG K NH2 1 
ATOM   11938 N  N   . THR K  1 116 ? 29.205 -99.721  -6.773   1.00 73.62  ? 117 THR K N   1 
ATOM   11939 C  CA  . THR K  1 116 ? 28.025 -99.584  -5.928   1.00 73.46  ? 117 THR K CA  1 
ATOM   11940 C  C   . THR K  1 116 ? 28.357 -99.242  -4.465   1.00 74.82  ? 117 THR K C   1 
ATOM   11941 O  O   . THR K  1 116 ? 29.167 -99.894  -3.820   1.00 77.31  ? 117 THR K O   1 
ATOM   11942 C  CB  . THR K  1 116 ? 27.180 -100.877 -5.966   1.00 75.20  ? 117 THR K CB  1 
ATOM   11943 O  OG1 . THR K  1 116 ? 26.716 -101.112 -7.309   1.00 74.17  ? 117 THR K OG1 1 
ATOM   11944 C  CG2 . THR K  1 116 ? 25.989 -100.765 -5.008   1.00 75.73  ? 117 THR K CG2 1 
ATOM   11945 N  N   . LEU K  1 117 ? 27.699 -98.218  -3.943   1.00 73.91  ? 118 LEU K N   1 
ATOM   11946 C  CA  . LEU K  1 117 ? 27.679 -97.944  -2.498   1.00 75.52  ? 118 LEU K CA  1 
ATOM   11947 C  C   . LEU K  1 117 ? 26.512 -98.731  -1.878   1.00 77.03  ? 118 LEU K C   1 
ATOM   11948 O  O   . LEU K  1 117 ? 25.484 -98.942  -2.529   1.00 76.36  ? 118 LEU K O   1 
ATOM   11949 C  CB  . LEU K  1 117 ? 27.488 -96.449  -2.243   1.00 74.30  ? 118 LEU K CB  1 
ATOM   11950 C  CG  . LEU K  1 117 ? 27.558 -96.017  -0.777   1.00 76.34  ? 118 LEU K CG  1 
ATOM   11951 C  CD1 . LEU K  1 117 ? 28.897 -96.414  -0.193   1.00 78.51  ? 118 LEU K CD1 1 
ATOM   11952 C  CD2 . LEU K  1 117 ? 27.309 -94.512  -0.626   1.00 75.45  ? 118 LEU K CD2 1 
ATOM   11953 N  N   . VAL K  1 118 ? 26.658 -99.150  -0.626   1.00 79.62  ? 119 VAL K N   1 
ATOM   11954 C  CA  . VAL K  1 118 ? 25.663 -100.029 0.009    1.00 81.76  ? 119 VAL K CA  1 
ATOM   11955 C  C   . VAL K  1 118 ? 25.556 -99.774  1.513    1.00 84.32  ? 119 VAL K C   1 
ATOM   11956 O  O   . VAL K  1 118 ? 26.555 -99.875  2.246    1.00 86.39  ? 119 VAL K O   1 
ATOM   11957 C  CB  . VAL K  1 118 ? 26.013 -101.539 -0.218   1.00 83.79  ? 119 VAL K CB  1 
ATOM   11958 C  CG1 . VAL K  1 118 ? 25.164 -102.431 0.664    1.00 86.96  ? 119 VAL K CG1 1 
ATOM   11959 C  CG2 . VAL K  1 118 ? 25.834 -101.922 -1.679   1.00 82.02  ? 119 VAL K CG2 1 
ATOM   11960 N  N   . VAL K  1 119 ? 24.341 -99.466  1.965    1.00 84.77  ? 120 VAL K N   1 
ATOM   11961 C  CA  . VAL K  1 119 ? 24.058 -99.358  3.395    1.00 87.81  ? 120 VAL K CA  1 
ATOM   11962 C  C   . VAL K  1 119 ? 23.426 -100.671 3.862    1.00 90.84  ? 120 VAL K C   1 
ATOM   11963 O  O   . VAL K  1 119 ? 22.693 -101.327 3.107    1.00 90.30  ? 120 VAL K O   1 
ATOM   11964 C  CB  . VAL K  1 119 ? 23.160 -98.144  3.715    1.00 87.31  ? 120 VAL K CB  1 
ATOM   11965 C  CG1 . VAL K  1 119 ? 21.722 -98.407  3.327    1.00 87.47  ? 120 VAL K CG1 1 
ATOM   11966 C  CG2 . VAL K  1 119 ? 23.251 -97.801  5.178    1.00 90.68  ? 120 VAL K CG2 1 
ATOM   11967 N  N   . HIS K  1 120 ? 23.720 -101.050 5.103    1.00 94.51  ? 121 HIS K N   1 
ATOM   11968 C  CA  . HIS K  1 120 ? 23.462 -102.421 5.571    1.00 98.24  ? 121 HIS K CA  1 
ATOM   11969 C  C   . HIS K  1 120 ? 22.447 -102.589 6.712    1.00 101.97 ? 121 HIS K C   1 
ATOM   11970 O  O   . HIS K  1 120 ? 22.138 -101.638 7.457    1.00 102.44 ? 121 HIS K O   1 
ATOM   11971 C  CB  . HIS K  1 120 ? 24.776 -103.088 5.964    1.00 100.53 ? 121 HIS K CB  1 
ATOM   11972 C  CG  . HIS K  1 120 ? 25.454 -103.747 4.819    1.00 98.81  ? 121 HIS K CG  1 
ATOM   11973 N  ND1 . HIS K  1 120 ? 25.511 -105.117 4.678    1.00 101.82 ? 121 HIS K ND1 1 
ATOM   11974 C  CD2 . HIS K  1 120 ? 26.061 -103.225 3.731    1.00 95.13  ? 121 HIS K CD2 1 
ATOM   11975 C  CE1 . HIS K  1 120 ? 26.157 -105.413 3.565    1.00 99.99  ? 121 HIS K CE1 1 
ATOM   11976 N  NE2 . HIS K  1 120 ? 26.490 -104.282 2.967    1.00 96.10  ? 121 HIS K NE2 1 
ATOM   11977 N  N   . GLU K  1 121 ? 21.959 -103.832 6.837    1.00 104.90 ? 122 GLU K N   1 
ATOM   11978 C  CA  . GLU K  1 121 ? 20.962 -104.206 7.850    1.00 108.96 ? 122 GLU K CA  1 
ATOM   11979 C  C   . GLU K  1 121 ? 21.488 -103.964 9.264    1.00 112.47 ? 122 GLU K C   1 
ATOM   11980 O  O   . GLU K  1 121 ? 20.979 -103.100 9.986    1.00 113.24 ? 122 GLU K O   1 
ATOM   11981 C  CB  . GLU K  1 121 ? 20.582 -105.680 7.690    1.00 112.03 ? 122 GLU K CB  1 
ATOM   11982 C  CG  . GLU K  1 121 ? 19.616 -106.227 8.774    1.00 117.39 ? 122 GLU K CG  1 
ATOM   11983 C  CD  . GLU K  1 121 ? 19.382 -107.790 8.698    1.00 121.85 ? 122 GLU K CD  1 
ATOM   11984 O  OE1 . GLU K  1 121 ? 20.104 -108.484 7.920    1.00 120.94 ? 122 GLU K OE1 1 
ATOM   11985 O  OE2 . GLU K  1 121 ? 18.473 -108.322 9.422    1.00 126.06 ? 122 GLU K OE2 1 
ATOM   11986 N  N   . LYS K  1 122 ? 22.523 -104.724 9.625    1.00 115.06 ? 123 LYS K N   1 
ATOM   11987 C  CA  . LYS K  1 122 ? 23.152 -104.653 10.956   1.00 119.29 ? 123 LYS K CA  1 
ATOM   11988 C  C   . LYS K  1 122 ? 24.380 -103.740 10.916   1.00 117.28 ? 123 LYS K C   1 
ATOM   11989 O  O   . LYS K  1 122 ? 24.703 -103.156 9.862    1.00 112.70 ? 123 LYS K O   1 
ATOM   11990 C  CB  . LYS K  1 122 ? 23.578 -106.051 11.444   1.00 124.21 ? 123 LYS K CB  1 
ATOM   11991 C  CG  . LYS K  1 122 ? 22.498 -107.126 11.345   1.00 126.84 ? 123 LYS K CG  1 
ATOM   11992 C  CD  . LYS K  1 122 ? 23.040 -108.500 11.809   1.00 132.61 ? 123 LYS K CD  1 
ATOM   11993 C  CE  . LYS K  1 122 ? 22.066 -109.667 11.488   1.00 135.03 ? 123 LYS K CE  1 
ATOM   11994 N  NZ  . LYS K  1 122 ? 22.463 -110.956 12.141   1.00 141.23 ? 123 LYS K NZ  1 
ATOM   11995 N  N   . ALA K  1 123 ? 25.057 -103.638 12.063   1.00 121.14 ? 124 ALA K N   1 
ATOM   11996 C  CA  . ALA K  1 123 ? 26.314 -102.897 12.151   1.00 120.48 ? 124 ALA K CA  1 
ATOM   11997 C  C   . ALA K  1 123 ? 27.508 -103.768 11.702   1.00 121.33 ? 124 ALA K C   1 
ATOM   11998 O  O   . ALA K  1 123 ? 27.518 -104.997 11.863   1.00 124.37 ? 124 ALA K O   1 
ATOM   11999 C  CB  . ALA K  1 123 ? 26.519 -102.336 13.552   1.00 124.79 ? 124 ALA K CB  1 
ATOM   12000 N  N   . ASP K  1 124 ? 28.491 -103.101 11.103   1.00 118.74 ? 125 ASP K N   1 
ATOM   12001 C  CA  . ASP K  1 124 ? 29.759 -103.725 10.722   1.00 120.08 ? 125 ASP K CA  1 
ATOM   12002 C  C   . ASP K  1 124 ? 30.656 -103.880 11.974   1.00 126.14 ? 125 ASP K C   1 
ATOM   12003 O  O   . ASP K  1 124 ? 31.019 -102.889 12.626   1.00 126.93 ? 125 ASP K O   1 
ATOM   12004 C  CB  . ASP K  1 124 ? 30.472 -102.869 9.651    1.00 115.50 ? 125 ASP K CB  1 
ATOM   12005 C  CG  . ASP K  1 124 ? 31.760 -103.529 9.089    1.00 116.83 ? 125 ASP K CG  1 
ATOM   12006 O  OD1 . ASP K  1 124 ? 32.086 -104.678 9.474    1.00 121.20 ? 125 ASP K OD1 1 
ATOM   12007 O  OD2 . ASP K  1 124 ? 32.452 -102.886 8.255    1.00 113.70 ? 125 ASP K OD2 1 
ATOM   12008 N  N   . ASP K  1 125 ? 31.039 -105.126 12.275   1.00 130.72 ? 126 ASP K N   1 
ATOM   12009 C  CA  . ASP K  1 125 ? 31.849 -105.440 13.473   1.00 137.18 ? 126 ASP K CA  1 
ATOM   12010 C  C   . ASP K  1 125 ? 33.322 -105.101 13.292   1.00 138.20 ? 126 ASP K C   1 
ATOM   12011 O  O   . ASP K  1 125 ? 34.135 -105.430 14.153   1.00 144.04 ? 126 ASP K O   1 
ATOM   12012 C  CB  . ASP K  1 125 ? 31.685 -106.921 13.888   1.00 142.45 ? 126 ASP K CB  1 
ATOM   12013 C  CG  . ASP K  1 125 ? 32.431 -107.926 12.946   1.00 142.91 ? 126 ASP K CG  1 
ATOM   12014 O  OD1 . ASP K  1 125 ? 33.456 -107.557 12.295   1.00 140.97 ? 126 ASP K OD1 1 
ATOM   12015 O  OD2 . ASP K  1 125 ? 31.976 -109.109 12.876   1.00 145.02 ? 126 ASP K OD2 1 
ATOM   12016 N  N   . LEU K  1 126 ? 33.646 -104.479 12.156   1.00 132.92 ? 127 LEU K N   1 
ATOM   12017 C  CA  . LEU K  1 126 ? 35.005 -104.023 11.820   1.00 133.51 ? 127 LEU K CA  1 
ATOM   12018 C  C   . LEU K  1 126 ? 36.053 -105.153 11.875   1.00 138.95 ? 127 LEU K C   1 
ATOM   12019 O  O   . LEU K  1 126 ? 37.234 -104.903 12.220   1.00 142.72 ? 127 LEU K O   1 
ATOM   12020 C  CB  . LEU K  1 126 ? 35.438 -102.855 12.719   1.00 135.36 ? 127 LEU K CB  1 
ATOM   12021 C  CG  . LEU K  1 126 ? 34.432 -101.706 12.816   1.00 131.52 ? 127 LEU K CG  1 
ATOM   12022 C  CD1 . LEU K  1 126 ? 35.050 -100.487 13.523   1.00 133.81 ? 127 LEU K CD1 1 
ATOM   12023 C  CD2 . LEU K  1 126 ? 33.928 -101.310 11.433   1.00 124.53 ? 127 LEU K CD2 1 
ATOM   12024 N  N   . GLY K  1 127 ? 35.617 -106.379 11.538   1.00 139.76 ? 128 GLY K N   1 
ATOM   12025 C  CA  . GLY K  1 127 ? 36.520 -107.529 11.427   1.00 144.76 ? 128 GLY K CA  1 
ATOM   12026 C  C   . GLY K  1 127 ? 36.927 -108.153 12.754   1.00 152.85 ? 128 GLY K C   1 
ATOM   12027 O  O   . GLY K  1 127 ? 37.595 -109.200 12.765   1.00 158.01 ? 128 GLY K O   1 
ATOM   12028 N  N   . LYS K  1 128 ? 36.515 -107.535 13.873   1.00 154.47 ? 129 LYS K N   1 
ATOM   12029 C  CA  . LYS K  1 128 ? 36.901 -107.996 15.234   1.00 162.61 ? 129 LYS K CA  1 
ATOM   12030 C  C   . LYS K  1 128 ? 35.879 -109.009 15.819   1.00 165.65 ? 129 LYS K C   1 
ATOM   12031 O  O   . LYS K  1 128 ? 35.762 -109.176 17.047   1.00 171.25 ? 129 LYS K O   1 
ATOM   12032 C  CB  . LYS K  1 128 ? 37.039 -106.806 16.198   1.00 163.73 ? 129 LYS K CB  1 
ATOM   12033 C  CG  . LYS K  1 128 ? 37.929 -105.685 15.693   1.00 161.20 ? 129 LYS K CG  1 
ATOM   12034 C  CD  . LYS K  1 128 ? 38.399 -104.781 16.840   1.00 165.86 ? 129 LYS K CD  1 
ATOM   12035 C  CE  . LYS K  1 128 ? 39.148 -103.541 16.300   1.00 163.07 ? 129 LYS K CE  1 
ATOM   12036 N  NZ  . LYS K  1 128 ? 39.936 -102.849 17.364   1.00 169.08 ? 129 LYS K NZ  1 
ATOM   12037 N  N   . GLY K  1 129 ? 35.160 -109.689 14.927   1.00 162.34 ? 130 GLY K N   1 
ATOM   12038 C  CA  . GLY K  1 129 ? 34.049 -110.556 15.303   1.00 164.23 ? 130 GLY K CA  1 
ATOM   12039 C  C   . GLY K  1 129 ? 34.490 -111.909 15.808   1.00 172.23 ? 130 GLY K C   1 
ATOM   12040 O  O   . GLY K  1 129 ? 33.777 -112.529 16.605   1.00 176.41 ? 130 GLY K O   1 
ATOM   12041 N  N   . GLY K  1 130 ? 35.651 -112.377 15.340   1.00 174.78 ? 131 GLY K N   1 
ATOM   12042 C  CA  . GLY K  1 130 ? 36.207 -113.668 15.779   1.00 183.31 ? 131 GLY K CA  1 
ATOM   12043 C  C   . GLY K  1 130 ? 35.767 -114.854 14.915   1.00 183.71 ? 131 GLY K C   1 
ATOM   12044 O  O   . GLY K  1 130 ? 36.498 -115.863 14.799   1.00 189.75 ? 131 GLY K O   1 
ATOM   12045 N  N   . ASN K  1 131 ? 34.576 -114.753 14.315   1.00 177.97 ? 132 ASN K N   1 
ATOM   12046 C  CA  . ASN K  1 131 ? 34.089 -115.804 13.411   1.00 178.01 ? 132 ASN K CA  1 
ATOM   12047 C  C   . ASN K  1 131 ? 34.679 -115.660 11.980   1.00 173.32 ? 132 ASN K C   1 
ATOM   12048 O  O   . ASN K  1 131 ? 35.369 -114.666 11.652   1.00 169.13 ? 132 ASN K O   1 
ATOM   12049 C  CB  . ASN K  1 131 ? 32.539 -115.865 13.404   1.00 175.04 ? 132 ASN K CB  1 
ATOM   12050 C  CG  . ASN K  1 131 ? 31.883 -114.765 12.538   1.00 165.84 ? 132 ASN K CG  1 
ATOM   12051 O  OD1 . ASN K  1 131 ? 32.554 -113.901 11.944   1.00 161.13 ? 132 ASN K OD1 1 
ATOM   12052 N  ND2 . ASN K  1 131 ? 30.554 -114.813 12.464   1.00 163.75 ? 132 ASN K ND2 1 
ATOM   12053 N  N   . GLU K  1 132 ? 34.385 -116.661 11.150   1.00 174.35 ? 133 GLU K N   1 
ATOM   12054 C  CA  . GLU K  1 132 ? 34.838 -116.696 9.750    1.00 170.95 ? 133 GLU K CA  1 
ATOM   12055 C  C   . GLU K  1 132 ? 34.310 -115.491 8.926    1.00 161.49 ? 133 GLU K C   1 
ATOM   12056 O  O   . GLU K  1 132 ? 35.066 -114.796 8.190    1.00 157.58 ? 133 GLU K O   1 
ATOM   12057 C  CB  . GLU K  1 132 ? 34.359 -118.011 9.091    1.00 174.33 ? 133 GLU K CB  1 
ATOM   12058 C  CG  . GLU K  1 132 ? 34.456 -118.037 7.534    1.00 170.43 ? 133 GLU K CG  1 
ATOM   12059 C  CD  . GLU K  1 132 ? 35.879 -118.315 7.003    1.00 174.09 ? 133 GLU K CD  1 
ATOM   12060 O  OE1 . GLU K  1 132 ? 36.842 -118.419 7.825    1.00 179.56 ? 133 GLU K OE1 1 
ATOM   12061 O  OE2 . GLU K  1 132 ? 36.010 -118.434 5.749    1.00 171.52 ? 133 GLU K OE2 1 
ATOM   12062 N  N   . GLU K  1 133 ? 32.997 -115.286 9.047    1.00 158.17 ? 134 GLU K N   1 
ATOM   12063 C  CA  . GLU K  1 133 ? 32.280 -114.315 8.233    1.00 150.01 ? 134 GLU K CA  1 
ATOM   12064 C  C   . GLU K  1 133 ? 32.692 -112.876 8.539    1.00 145.52 ? 134 GLU K C   1 
ATOM   12065 O  O   . GLU K  1 133 ? 32.613 -112.023 7.661    1.00 139.32 ? 134 GLU K O   1 
ATOM   12066 C  CB  . GLU K  1 133 ? 30.763 -114.488 8.420    1.00 148.98 ? 134 GLU K CB  1 
ATOM   12067 C  CG  . GLU K  1 133 ? 29.892 -113.814 7.316    1.00 142.01 ? 134 GLU K CG  1 
ATOM   12068 C  CD  . GLU K  1 133 ? 29.985 -114.497 5.912    1.00 141.58 ? 134 GLU K CD  1 
ATOM   12069 O  OE1 . GLU K  1 133 ? 30.593 -115.608 5.811    1.00 147.32 ? 134 GLU K OE1 1 
ATOM   12070 O  OE2 . GLU K  1 133 ? 29.438 -113.918 4.921    1.00 135.66 ? 134 GLU K OE2 1 
ATOM   12071 N  N   . SER K  1 134 ? 33.130 -112.614 9.770    1.00 149.13 ? 135 SER K N   1 
ATOM   12072 C  CA  . SER K  1 134 ? 33.553 -111.259 10.167   1.00 146.09 ? 135 SER K CA  1 
ATOM   12073 C  C   . SER K  1 134 ? 34.774 -110.791 9.405    1.00 144.30 ? 135 SER K C   1 
ATOM   12074 O  O   . SER K  1 134 ? 35.014 -109.588 9.267    1.00 140.22 ? 135 SER K O   1 
ATOM   12075 C  CB  . SER K  1 134 ? 33.904 -111.188 11.643   1.00 151.80 ? 135 SER K CB  1 
ATOM   12076 O  OG  . SER K  1 134 ? 34.516 -109.929 11.898   1.00 149.37 ? 135 SER K OG  1 
ATOM   12077 N  N   . THR K  1 135 ? 35.555 -111.756 8.948    1.00 148.10 ? 136 THR K N   1 
ATOM   12078 C  CA  . THR K  1 135 ? 36.710 -111.491 8.084    1.00 147.37 ? 136 THR K CA  1 
ATOM   12079 C  C   . THR K  1 135 ? 36.366 -111.148 6.614    1.00 140.80 ? 136 THR K C   1 
ATOM   12080 O  O   . THR K  1 135 ? 37.227 -110.692 5.846    1.00 139.15 ? 136 THR K O   1 
ATOM   12081 C  CB  . THR K  1 135 ? 37.672 -112.717 8.113    1.00 154.84 ? 136 THR K CB  1 
ATOM   12082 O  OG1 . THR K  1 135 ? 38.449 -112.681 9.323    1.00 160.94 ? 136 THR K OG1 1 
ATOM   12083 C  CG2 . THR K  1 135 ? 38.622 -112.754 6.890    1.00 153.75 ? 136 THR K CG2 1 
ATOM   12084 N  N   . LYS K  1 136 ? 35.111 -111.349 6.240    1.00 137.64 ? 137 LYS K N   1 
ATOM   12085 C  CA  . LYS K  1 136 ? 34.655 -111.130 4.859    1.00 132.12 ? 137 LYS K CA  1 
ATOM   12086 C  C   . LYS K  1 136 ? 33.674 -109.938 4.748    1.00 125.48 ? 137 LYS K C   1 
ATOM   12087 O  O   . LYS K  1 136 ? 33.962 -108.906 4.118    1.00 120.74 ? 137 LYS K O   1 
ATOM   12088 C  CB  . LYS K  1 136 ? 33.970 -112.405 4.345    1.00 134.43 ? 137 LYS K CB  1 
ATOM   12089 C  CG  . LYS K  1 136 ? 34.915 -113.558 4.021    1.00 140.52 ? 137 LYS K CG  1 
ATOM   12090 C  CD  . LYS K  1 136 ? 34.089 -114.753 3.509    1.00 143.28 ? 137 LYS K CD  1 
ATOM   12091 C  CE  . LYS K  1 136 ? 34.909 -115.730 2.653    1.00 147.33 ? 137 LYS K CE  1 
ATOM   12092 N  NZ  . LYS K  1 136 ? 35.583 -116.779 3.476    1.00 155.86 ? 137 LYS K NZ  1 
ATOM   12093 N  N   . THR K  1 137 ? 32.511 -110.113 5.372    1.00 125.62 ? 138 THR K N   1 
ATOM   12094 C  CA  . THR K  1 137 ? 31.386 -109.200 5.219    1.00 120.32 ? 138 THR K CA  1 
ATOM   12095 C  C   . THR K  1 137 ? 31.300 -108.196 6.371    1.00 120.05 ? 138 THR K C   1 
ATOM   12096 O  O   . THR K  1 137 ? 30.613 -107.179 6.264    1.00 115.87 ? 138 THR K O   1 
ATOM   12097 C  CB  . THR K  1 137 ? 30.054 -110.000 5.126    1.00 121.07 ? 138 THR K CB  1 
ATOM   12098 O  OG1 . THR K  1 137 ? 29.703 -110.542 6.416    1.00 125.97 ? 138 THR K OG1 1 
ATOM   12099 C  CG2 . THR K  1 137 ? 30.189 -111.136 4.109    1.00 122.82 ? 138 THR K CG2 1 
ATOM   12100 N  N   . GLY K  1 138 ? 31.979 -108.498 7.473    1.00 125.14 ? 139 GLY K N   1 
ATOM   12101 C  CA  . GLY K  1 138 ? 31.858 -107.708 8.703    1.00 126.39 ? 139 GLY K CA  1 
ATOM   12102 C  C   . GLY K  1 138 ? 30.627 -108.053 9.548    1.00 128.44 ? 139 GLY K C   1 
ATOM   12103 O  O   . GLY K  1 138 ? 30.282 -107.325 10.507   1.00 128.91 ? 139 GLY K O   1 
ATOM   12104 N  N   . ASN K  1 139 ? 29.954 -109.159 9.184    1.00 129.92 ? 140 ASN K N   1 
ATOM   12105 C  CA  . ASN K  1 139 ? 28.694 -109.595 9.838    1.00 132.07 ? 140 ASN K CA  1 
ATOM   12106 C  C   . ASN K  1 139 ? 27.594 -108.506 9.880    1.00 127.78 ? 140 ASN K C   1 
ATOM   12107 O  O   . ASN K  1 139 ? 26.696 -108.546 10.748   1.00 130.05 ? 140 ASN K O   1 
ATOM   12108 C  CB  . ASN K  1 139 ? 28.982 -110.121 11.262   1.00 139.00 ? 140 ASN K CB  1 
ATOM   12109 C  CG  . ASN K  1 139 ? 29.566 -111.547 11.263   1.00 144.59 ? 140 ASN K CG  1 
ATOM   12110 O  OD1 . ASN K  1 139 ? 30.372 -111.884 12.144   1.00 150.15 ? 140 ASN K OD1 1 
ATOM   12111 N  ND2 . ASN K  1 139 ? 29.166 -112.377 10.285   1.00 143.26 ? 140 ASN K ND2 1 
ATOM   12112 N  N   . ALA K  1 140 ? 27.657 -107.565 8.924    1.00 121.99 ? 141 ALA K N   1 
ATOM   12113 C  CA  . ALA K  1 140 ? 26.756 -106.390 8.900    1.00 117.88 ? 141 ALA K CA  1 
ATOM   12114 C  C   . ALA K  1 140 ? 25.397 -106.710 8.252    1.00 116.01 ? 141 ALA K C   1 
ATOM   12115 O  O   . ALA K  1 140 ? 24.517 -105.845 8.165    1.00 113.04 ? 141 ALA K O   1 
ATOM   12116 C  CB  . ALA K  1 140 ? 27.426 -105.220 8.200    1.00 113.16 ? 141 ALA K CB  1 
ATOM   12117 N  N   . GLY K  1 141 ? 25.244 -107.950 7.786    1.00 118.12 ? 142 GLY K N   1 
ATOM   12118 C  CA  . GLY K  1 141 ? 23.943 -108.452 7.369    1.00 118.19 ? 142 GLY K CA  1 
ATOM   12119 C  C   . GLY K  1 141 ? 23.513 -108.024 5.978    1.00 113.13 ? 142 GLY K C   1 
ATOM   12120 O  O   . GLY K  1 141 ? 24.350 -107.691 5.131    1.00 110.03 ? 142 GLY K O   1 
ATOM   12121 N  N   . SER K  1 142 ? 22.194 -108.040 5.760    1.00 112.83 ? 143 SER K N   1 
ATOM   12122 C  CA  . SER K  1 142 ? 21.591 -107.868 4.421    1.00 109.28 ? 143 SER K CA  1 
ATOM   12123 C  C   . SER K  1 142 ? 21.789 -106.469 3.869    1.00 104.08 ? 143 SER K C   1 
ATOM   12124 O  O   . SER K  1 142 ? 22.215 -105.535 4.600    1.00 103.25 ? 143 SER K O   1 
ATOM   12125 C  CB  . SER K  1 142 ? 20.082 -108.200 4.439    1.00 111.13 ? 143 SER K CB  1 
ATOM   12126 O  OG  . SER K  1 142 ? 19.309 -107.183 5.087    1.00 110.35 ? 143 SER K OG  1 
ATOM   12127 N  N   . ARG K  1 143 ? 21.454 -106.331 2.584    1.00 100.90 ? 144 ARG K N   1 
ATOM   12128 C  CA  . ARG K  1 143 ? 21.618 -105.050 1.891    1.00 96.23  ? 144 ARG K CA  1 
ATOM   12129 C  C   . ARG K  1 143 ? 20.293 -104.285 1.806    1.00 95.10  ? 144 ARG K C   1 
ATOM   12130 O  O   . ARG K  1 143 ? 19.391 -104.650 1.041    1.00 95.36  ? 144 ARG K O   1 
ATOM   12131 C  CB  . ARG K  1 143 ? 22.199 -105.290 0.510    1.00 93.94  ? 144 ARG K CB  1 
ATOM   12132 C  CG  . ARG K  1 143 ? 23.552 -105.961 0.583    1.00 95.49  ? 144 ARG K CG  1 
ATOM   12133 C  CD  . ARG K  1 143 ? 24.081 -106.357 -0.777   1.00 94.30  ? 144 ARG K CD  1 
ATOM   12134 N  NE  . ARG K  1 143 ? 25.298 -107.162 -0.657   1.00 96.69  ? 144 ARG K NE  1 
ATOM   12135 C  CZ  . ARG K  1 143 ? 26.009 -107.614 -1.689   1.00 96.75  ? 144 ARG K CZ  1 
ATOM   12136 N  NH1 . ARG K  1 143 ? 25.644 -107.339 -2.941   1.00 94.30  ? 144 ARG K NH1 1 
ATOM   12137 N  NH2 . ARG K  1 143 ? 27.096 -108.346 -1.469   1.00 100.10 ? 144 ARG K NH2 1 
ATOM   12138 N  N   . LEU K  1 144 ? 20.186 -103.228 2.602    1.00 94.44  ? 145 LEU K N   1 
ATOM   12139 C  CA  . LEU K  1 144 ? 18.930 -102.492 2.724    1.00 94.53  ? 145 LEU K CA  1 
ATOM   12140 C  C   . LEU K  1 144 ? 18.673 -101.585 1.520    1.00 90.76  ? 145 LEU K C   1 
ATOM   12141 O  O   . LEU K  1 144 ? 17.590 -101.608 0.915    1.00 91.09  ? 145 LEU K O   1 
ATOM   12142 C  CB  . LEU K  1 144 ? 18.923 -101.645 4.023    1.00 96.08  ? 145 LEU K CB  1 
ATOM   12143 C  CG  . LEU K  1 144 ? 18.886 -102.396 5.376    1.00 100.68 ? 145 LEU K CG  1 
ATOM   12144 C  CD1 . LEU K  1 144 ? 18.755 -101.415 6.571    1.00 101.90 ? 145 LEU K CD1 1 
ATOM   12145 C  CD2 . LEU K  1 144 ? 17.763 -103.486 5.382    1.00 103.80 ? 145 LEU K CD2 1 
ATOM   12146 N  N   . ALA K  1 145 ? 19.669 -100.765 1.211    1.00 87.77  ? 146 ALA K N   1 
ATOM   12147 C  CA  . ALA K  1 145 ? 19.559 -99.802  0.131    1.00 84.58  ? 146 ALA K CA  1 
ATOM   12148 C  C   . ALA K  1 145 ? 20.924 -99.600  -0.512   1.00 82.01  ? 146 ALA K C   1 
ATOM   12149 O  O   . ALA K  1 145 ? 21.961 -99.674  0.154    1.00 82.74  ? 146 ALA K O   1 
ATOM   12150 C  CB  . ALA K  1 145 ? 18.987 -98.469  0.649    1.00 84.40  ? 146 ALA K CB  1 
ATOM   12151 N  N   . CYS K  1 146 ? 20.914 -99.367  -1.817   1.00 79.56  ? 147 CYS K N   1 
ATOM   12152 C  CA  . CYS K  1 146 ? 22.146 -99.194  -2.563   1.00 77.40  ? 147 CYS K CA  1 
ATOM   12153 C  C   . CYS K  1 146 ? 21.959 -98.320  -3.804   1.00 74.90  ? 147 CYS K C   1 
ATOM   12154 O  O   . CYS K  1 146 ? 20.838 -97.988  -4.208   1.00 74.86  ? 147 CYS K O   1 
ATOM   12155 C  CB  . CYS K  1 146 ? 22.732 -100.566 -2.961   1.00 78.56  ? 147 CYS K CB  1 
ATOM   12156 S  SG  . CYS K  1 146 ? 21.741 -101.541 -4.159   1.00 79.15  ? 147 CYS K SG  1 
ATOM   12157 N  N   . GLY K  1 147 ? 23.089 -97.962  -4.400   1.00 73.29  ? 148 GLY K N   1 
ATOM   12158 C  CA  . GLY K  1 147 ? 23.097 -97.186  -5.629   1.00 71.26  ? 148 GLY K CA  1 
ATOM   12159 C  C   . GLY K  1 147 ? 24.464 -97.199  -6.292   1.00 70.05  ? 148 GLY K C   1 
ATOM   12160 O  O   . GLY K  1 147 ? 25.476 -97.384  -5.626   1.00 70.69  ? 148 GLY K O   1 
ATOM   12161 N  N   . VAL K  1 148 ? 24.486 -96.996  -7.606   1.00 68.73  ? 149 VAL K N   1 
ATOM   12162 C  CA  . VAL K  1 148 ? 25.744 -96.901  -8.353   1.00 67.74  ? 149 VAL K CA  1 
ATOM   12163 C  C   . VAL K  1 148 ? 26.355 -95.503  -8.230   1.00 66.61  ? 149 VAL K C   1 
ATOM   12164 O  O   . VAL K  1 148 ? 25.660 -94.486  -8.356   1.00 65.91  ? 149 VAL K O   1 
ATOM   12165 C  CB  . VAL K  1 148 ? 25.544 -97.216  -9.825   1.00 67.34  ? 149 VAL K CB  1 
ATOM   12166 C  CG1 . VAL K  1 148 ? 26.842 -97.064  -10.557  1.00 66.78  ? 149 VAL K CG1 1 
ATOM   12167 C  CG2 . VAL K  1 148 ? 25.021 -98.631  -9.983   1.00 69.13  ? 149 VAL K CG2 1 
ATOM   12168 N  N   . ILE K  1 149 ? 27.659 -95.462  -7.984   1.00 66.94  ? 150 ILE K N   1 
ATOM   12169 C  CA  . ILE K  1 149 ? 28.367 -94.199  -7.744   1.00 66.60  ? 150 ILE K CA  1 
ATOM   12170 C  C   . ILE K  1 149 ? 28.653 -93.514  -9.060   1.00 65.50  ? 150 ILE K C   1 
ATOM   12171 O  O   . ILE K  1 149 ? 29.267 -94.106  -9.950   1.00 65.61  ? 150 ILE K O   1 
ATOM   12172 C  CB  . ILE K  1 149 ? 29.703 -94.415  -7.036   1.00 67.97  ? 150 ILE K CB  1 
ATOM   12173 C  CG1 . ILE K  1 149 ? 29.470 -94.877  -5.606   1.00 69.68  ? 150 ILE K CG1 1 
ATOM   12174 C  CG2 . ILE K  1 149 ? 30.495 -93.128  -7.044   1.00 67.91  ? 150 ILE K CG2 1 
ATOM   12175 C  CD1 . ILE K  1 149 ? 30.721 -95.349  -4.933   1.00 71.79  ? 150 ILE K CD1 1 
ATOM   12176 N  N   . GLY K  1 150 ? 28.230 -92.262  -9.180   1.00 64.95  ? 151 GLY K N   1 
ATOM   12177 C  CA  . GLY K  1 150 ? 28.288 -91.565  -10.464  1.00 64.29  ? 151 GLY K CA  1 
ATOM   12178 C  C   . GLY K  1 150 ? 29.059 -90.271  -10.432  1.00 64.64  ? 151 GLY K C   1 
ATOM   12179 O  O   . GLY K  1 150 ? 29.183 -89.650  -9.382   1.00 65.52  ? 151 GLY K O   1 
ATOM   12180 N  N   . ILE K  1 151 ? 29.570 -89.866  -11.593  1.00 64.44  ? 152 ILE K N   1 
ATOM   12181 C  CA  . ILE K  1 151 ? 30.313 -88.612  -11.717  1.00 65.23  ? 152 ILE K CA  1 
ATOM   12182 C  C   . ILE K  1 151 ? 29.353 -87.434  -11.600  1.00 65.64  ? 152 ILE K C   1 
ATOM   12183 O  O   . ILE K  1 151 ? 28.315 -87.386  -12.267  1.00 65.25  ? 152 ILE K O   1 
ATOM   12184 C  CB  . ILE K  1 151 ? 31.049 -88.495  -13.058  1.00 65.46  ? 152 ILE K CB  1 
ATOM   12185 C  CG1 . ILE K  1 151 ? 32.070 -89.628  -13.225  1.00 65.77  ? 152 ILE K CG1 1 
ATOM   12186 C  CG2 . ILE K  1 151 ? 31.746 -87.131  -13.162  1.00 66.65  ? 152 ILE K CG2 1 
ATOM   12187 C  CD1 . ILE K  1 151 ? 32.848 -89.587  -14.545  1.00 66.38  ? 152 ILE K CD1 1 
ATOM   12188 N  N   . ALA K  1 152 ? 29.716 -86.473  -10.763  1.00 67.03  ? 153 ALA K N   1 
ATOM   12189 C  CA  . ALA K  1 152 ? 28.837 -85.345  -10.456  1.00 68.10  ? 153 ALA K CA  1 
ATOM   12190 C  C   . ALA K  1 152 ? 29.412 -84.024  -10.929  1.00 69.83  ? 153 ALA K C   1 
ATOM   12191 O  O   . ALA K  1 152 ? 30.616 -83.889  -11.143  1.00 70.38  ? 153 ALA K O   1 
ATOM   12192 C  CB  . ALA K  1 152 ? 28.601 -85.290  -8.979   1.00 69.25  ? 153 ALA K CB  1 
ATOM   12193 N  N   . GLN K  1 153 ? 28.544 -83.033  -11.066  1.00 71.26  ? 154 GLN K N   1 
ATOM   12194 C  CA  . GLN K  1 153 ? 28.988 -81.706  -11.522  1.00 73.88  ? 154 GLN K CA  1 
ATOM   12195 C  C   . GLN K  1 153 ? 29.747 -80.959  -10.414  1.00 76.31  ? 154 GLN K C   1 
ATOM   12196 O  O   . GLN K  1 153 ? 29.272 -80.929  -9.263   1.00 77.10  ? 154 GLN K O   1 
ATOM   12197 C  CB  . GLN K  1 153 ? 27.815 -80.833  -12.006  1.00 75.40  ? 154 GLN K CB  1 
ATOM   12198 C  CG  . GLN K  1 153 ? 28.265 -79.464  -12.551  1.00 78.33  ? 154 GLN K CG  1 
ATOM   12199 C  CD  . GLN K  1 153 ? 27.127 -78.687  -13.136  1.00 80.35  ? 154 GLN K CD  1 
ATOM   12200 O  OE1 . GLN K  1 153 ? 26.534 -79.105  -14.121  1.00 79.56  ? 154 GLN K OE1 1 
ATOM   12201 N  NE2 . GLN K  1 153 ? 26.805 -77.551  -12.533  1.00 83.46  ? 154 GLN K NE2 1 
ATOM   12202 O  OXT . GLN K  1 153 ? 30.820 -80.360  -10.655  1.00 77.93  ? 154 GLN K OXT 1 
ATOM   12203 N  N   . ALA L  1 1   ? 37.759 -108.307 -21.977  1.00 93.37  ? 2   ALA L N   1 
ATOM   12204 C  CA  . ALA L  1 1   ? 38.372 -107.482 -20.892  1.00 93.36  ? 2   ALA L CA  1 
ATOM   12205 C  C   . ALA L  1 1   ? 37.310 -106.759 -20.037  1.00 89.02  ? 2   ALA L C   1 
ATOM   12206 O  O   . ALA L  1 1   ? 36.827 -107.331 -19.036  1.00 90.78  ? 2   ALA L O   1 
ATOM   12207 C  CB  . ALA L  1 1   ? 39.402 -106.470 -21.470  1.00 92.84  ? 2   ALA L CB  1 
ATOM   12208 N  N   . THR L  1 2   ? 36.958 -105.520 -20.432  1.00 83.88  ? 3   THR L N   1 
ATOM   12209 C  CA  . THR L  1 2   ? 36.073 -104.629 -19.635  1.00 79.59  ? 3   THR L CA  1 
ATOM   12210 C  C   . THR L  1 2   ? 34.600 -104.746 -20.023  1.00 76.13  ? 3   THR L C   1 
ATOM   12211 O  O   . THR L  1 2   ? 34.248 -104.793 -21.209  1.00 74.51  ? 3   THR L O   1 
ATOM   12212 C  CB  . THR L  1 2   ? 36.448 -103.122 -19.757  1.00 76.74  ? 3   THR L CB  1 
ATOM   12213 O  OG1 . THR L  1 2   ? 37.810 -102.970 -20.167  1.00 79.71  ? 3   THR L OG1 1 
ATOM   12214 C  CG2 . THR L  1 2   ? 36.222 -102.403 -18.433  1.00 75.66  ? 3   THR L CG2 1 
ATOM   12215 N  N   . LYS L  1 3   ? 33.750 -104.782 -19.000  1.00 75.42  ? 4   LYS L N   1 
ATOM   12216 C  CA  . LYS L  1 3   ? 32.285 -104.836 -19.169  1.00 72.75  ? 4   LYS L CA  1 
ATOM   12217 C  C   . LYS L  1 3   ? 31.623 -103.779 -18.294  1.00 69.93  ? 4   LYS L C   1 
ATOM   12218 O  O   . LYS L  1 3   ? 32.134 -103.426 -17.219  1.00 71.30  ? 4   LYS L O   1 
ATOM   12219 C  CB  . LYS L  1 3   ? 31.727 -106.218 -18.784  1.00 75.99  ? 4   LYS L CB  1 
ATOM   12220 C  CG  . LYS L  1 3   ? 32.171 -107.379 -19.695  1.00 79.46  ? 4   LYS L CG  1 
ATOM   12221 C  CD  . LYS L  1 3   ? 31.369 -108.656 -19.402  1.00 82.66  ? 4   LYS L CD  1 
ATOM   12222 C  CE  . LYS L  1 3   ? 32.130 -109.938 -19.798  1.00 87.81  ? 4   LYS L CE  1 
ATOM   12223 N  NZ  . LYS L  1 3   ? 31.659 -111.151 -19.043  1.00 91.72  ? 4   LYS L NZ  1 
ATOM   12224 N  N   . ALA L  1 4   ? 30.498 -103.261 -18.762  1.00 66.42  ? 5   ALA L N   1 
ATOM   12225 C  CA  . ALA L  1 4   ? 29.699 -102.341 -17.959  1.00 64.40  ? 5   ALA L CA  1 
ATOM   12226 C  C   . ALA L  1 4   ? 28.240 -102.688 -18.143  1.00 63.37  ? 5   ALA L C   1 
ATOM   12227 O  O   . ALA L  1 4   ? 27.898 -103.455 -19.046  1.00 63.68  ? 5   ALA L O   1 
ATOM   12228 C  CB  . ALA L  1 4   ? 29.960 -100.894 -18.347  1.00 61.36  ? 5   ALA L CB  1 
ATOM   12229 N  N   . VAL L  1 5   ? 27.393 -102.136 -17.274  1.00 62.69  ? 6   VAL L N   1 
ATOM   12230 C  CA  . VAL L  1 5   ? 25.933 -102.355 -17.337  1.00 62.12  ? 6   VAL L CA  1 
ATOM   12231 C  C   . VAL L  1 5   ? 25.177 -101.158 -16.798  1.00 60.21  ? 6   VAL L C   1 
ATOM   12232 O  O   . VAL L  1 5   ? 25.716 -100.386 -16.010  1.00 60.38  ? 6   VAL L O   1 
ATOM   12233 C  CB  . VAL L  1 5   ? 25.491 -103.582 -16.530  1.00 65.79  ? 6   VAL L CB  1 
ATOM   12234 C  CG1 . VAL L  1 5   ? 25.475 -103.266 -15.026  1.00 67.82  ? 6   VAL L CG1 1 
ATOM   12235 C  CG2 . VAL L  1 5   ? 24.120 -104.033 -16.996  1.00 65.82  ? 6   VAL L CG2 1 
ATOM   12236 N  N   . CYS L  1 6   ? 23.933 -101.005 -17.233  1.00 58.98  ? 7   CYS L N   1 
ATOM   12237 C  CA  . CYS L  1 6   ? 23.109 -99.871  -16.816  1.00 57.89  ? 7   CYS L CA  1 
ATOM   12238 C  C   . CYS L  1 6   ? 21.633 -100.217 -16.781  1.00 58.88  ? 7   CYS L C   1 
ATOM   12239 O  O   . CYS L  1 6   ? 21.064 -100.666 -17.784  1.00 58.26  ? 7   CYS L O   1 
ATOM   12240 C  CB  . CYS L  1 6   ? 23.290 -98.675  -17.755  1.00 54.68  ? 7   CYS L CB  1 
ATOM   12241 S  SG  . CYS L  1 6   ? 22.164 -97.296  -17.376  1.00 53.41  ? 7   CYS L SG  1 
ATOM   12242 N  N   . VAL L  1 7   ? 21.009 -99.969  -15.635  1.00 60.72  ? 8   VAL L N   1 
ATOM   12243 C  CA  . VAL L  1 7   ? 19.574 -100.171 -15.488  1.00 62.12  ? 8   VAL L CA  1 
ATOM   12244 C  C   . VAL L  1 7   ? 18.841 -98.854  -15.740  1.00 60.29  ? 8   VAL L C   1 
ATOM   12245 O  O   . VAL L  1 7   ? 18.891 -97.931  -14.921  1.00 60.50  ? 8   VAL L O   1 
ATOM   12246 C  CB  . VAL L  1 7   ? 19.219 -100.721 -14.098  1.00 66.07  ? 8   VAL L CB  1 
ATOM   12247 C  CG1 . VAL L  1 7   ? 17.710 -100.741 -13.879  1.00 68.00  ? 8   VAL L CG1 1 
ATOM   12248 C  CG2 . VAL L  1 7   ? 19.783 -102.117 -13.931  1.00 68.46  ? 8   VAL L CG2 1 
ATOM   12249 N  N   . LEU L  1 8   ? 18.164 -98.794  -16.886  1.00 58.74  ? 9   LEU L N   1 
ATOM   12250 C  CA  . LEU L  1 8   ? 17.353 -97.640  -17.285  1.00 57.41  ? 9   LEU L CA  1 
ATOM   12251 C  C   . LEU L  1 8   ? 16.008 -97.636  -16.559  1.00 60.32  ? 9   LEU L C   1 
ATOM   12252 O  O   . LEU L  1 8   ? 15.292 -98.637  -16.576  1.00 62.65  ? 9   LEU L O   1 
ATOM   12253 C  CB  . LEU L  1 8   ? 17.110 -97.662  -18.802  1.00 55.20  ? 9   LEU L CB  1 
ATOM   12254 C  CG  . LEU L  1 8   ? 18.334 -97.382  -19.681  1.00 52.24  ? 9   LEU L CG  1 
ATOM   12255 C  CD1 . LEU L  1 8   ? 18.074 -97.814  -21.096  1.00 50.86  ? 9   LEU L CD1 1 
ATOM   12256 C  CD2 . LEU L  1 8   ? 18.714 -95.925  -19.649  1.00 50.61  ? 9   LEU L CD2 1 
ATOM   12257 N  N   . LYS L  1 9   ? 15.682 -96.520  -15.916  1.00 60.81  ? 10  LYS L N   1 
ATOM   12258 C  CA  . LYS L  1 9   ? 14.412 -96.369  -15.193  1.00 64.20  ? 10  LYS L CA  1 
ATOM   12259 C  C   . LYS L  1 9   ? 13.946 -94.937  -15.227  1.00 63.81  ? 10  LYS L C   1 
ATOM   12260 O  O   . LYS L  1 9   ? 14.730 -94.041  -15.457  1.00 61.78  ? 10  LYS L O   1 
ATOM   12261 C  CB  . LYS L  1 9   ? 14.553 -96.784  -13.723  1.00 67.76  ? 10  LYS L CB  1 
ATOM   12262 C  CG  . LYS L  1 9   ? 14.392 -98.285  -13.445  1.00 70.70  ? 10  LYS L CG  1 
ATOM   12263 C  CD  . LYS L  1 9   ? 13.901 -98.534  -12.005  1.00 75.66  ? 10  LYS L CD  1 
ATOM   12264 C  CE  . LYS L  1 9   ? 14.044 -100.005 -11.574  1.00 78.40  ? 10  LYS L CE  1 
ATOM   12265 N  NZ  . LYS L  1 9   ? 12.893 -100.866 -12.040  1.00 80.62  ? 10  LYS L NZ  1 
ATOM   12266 N  N   . GLY L  1 10  ? 12.671 -94.716  -14.959  1.00 66.59  ? 11  GLY L N   1 
ATOM   12267 C  CA  . GLY L  1 10  ? 12.133 -93.361  -15.011  1.00 67.00  ? 11  GLY L CA  1 
ATOM   12268 C  C   . GLY L  1 10  ? 10.773 -93.183  -14.377  1.00 71.59  ? 11  GLY L C   1 
ATOM   12269 O  O   . GLY L  1 10  ? 10.218 -94.121  -13.796  1.00 74.83  ? 11  GLY L O   1 
ATOM   12270 N  N   . ASP L  1 11  ? 10.221 -91.978  -14.520  1.00 72.36  ? 12  ASP L N   1 
ATOM   12271 C  CA  . ASP L  1 11  ? 8.919  -91.619  -13.918  1.00 77.11  ? 12  ASP L CA  1 
ATOM   12272 C  C   . ASP L  1 11  ? 7.753  -92.429  -14.456  1.00 78.96  ? 12  ASP L C   1 
ATOM   12273 O  O   . ASP L  1 11  ? 6.818  -92.723  -13.731  1.00 83.63  ? 12  ASP L O   1 
ATOM   12274 C  CB  . ASP L  1 11  ? 8.624  -90.122  -14.092  1.00 77.66  ? 12  ASP L CB  1 
ATOM   12275 C  CG  . ASP L  1 11  ? 9.141  -89.286  -12.927  1.00 80.03  ? 12  ASP L CG  1 
ATOM   12276 O  OD1 . ASP L  1 11  ? 8.850  -89.649  -11.761  1.00 84.31  ? 12  ASP L OD1 1 
ATOM   12277 O  OD2 . ASP L  1 11  ? 9.828  -88.264  -13.172  1.00 78.62  ? 12  ASP L OD2 1 
ATOM   12278 N  N   . GLY L  1 12  ? 7.830  -92.794  -15.724  1.00 75.83  ? 13  GLY L N   1 
ATOM   12279 C  CA  . GLY L  1 12  ? 6.755  -93.521  -16.390  1.00 77.66  ? 13  GLY L CA  1 
ATOM   12280 C  C   . GLY L  1 12  ? 7.096  -94.974  -16.655  1.00 76.81  ? 13  GLY L C   1 
ATOM   12281 O  O   . GLY L  1 12  ? 7.972  -95.537  -15.986  1.00 76.09  ? 13  GLY L O   1 
ATOM   12282 N  N   . PRO L  1 13  ? 6.410  -95.582  -17.644  1.00 77.19  ? 14  PRO L N   1 
ATOM   12283 C  CA  . PRO L  1 13  ? 6.439  -97.025  -17.854  1.00 78.11  ? 14  PRO L CA  1 
ATOM   12284 C  C   . PRO L  1 13  ? 7.712  -97.510  -18.498  1.00 73.83  ? 14  PRO L C   1 
ATOM   12285 O  O   . PRO L  1 13  ? 7.971  -98.711  -18.476  1.00 74.82  ? 14  PRO L O   1 
ATOM   12286 C  CB  . PRO L  1 13  ? 5.273  -97.255  -18.819  1.00 80.26  ? 14  PRO L CB  1 
ATOM   12287 C  CG  . PRO L  1 13  ? 5.210  -96.006  -19.631  1.00 77.52  ? 14  PRO L CG  1 
ATOM   12288 C  CD  . PRO L  1 13  ? 5.707  -94.889  -18.743  1.00 76.60  ? 14  PRO L CD  1 
ATOM   12289 N  N   . VAL L  1 14  ? 8.482  -96.584  -19.073  1.00 69.76  ? 15  VAL L N   1 
ATOM   12290 C  CA  . VAL L  1 14  ? 9.715  -96.923  -19.789  1.00 65.70  ? 15  VAL L CA  1 
ATOM   12291 C  C   . VAL L  1 14  ? 10.767 -97.459  -18.828  1.00 65.41  ? 15  VAL L C   1 
ATOM   12292 O  O   . VAL L  1 14  ? 11.096 -96.821  -17.827  1.00 65.78  ? 15  VAL L O   1 
ATOM   12293 C  CB  . VAL L  1 14  ? 10.297 -95.718  -20.542  1.00 61.97  ? 15  VAL L CB  1 
ATOM   12294 C  CG1 . VAL L  1 14  ? 11.502 -96.159  -21.374  1.00 58.50  ? 15  VAL L CG1 1 
ATOM   12295 C  CG2 . VAL L  1 14  ? 9.230  -95.071  -21.428  1.00 62.67  ? 15  VAL L CG2 1 
ATOM   12296 N  N   . GLN L  1 15  ? 11.251 -98.656  -19.125  1.00 65.27  ? 16  GLN L N   1 
ATOM   12297 C  CA  . GLN L  1 15  ? 12.308 -99.274  -18.351  1.00 65.40  ? 16  GLN L CA  1 
ATOM   12298 C  C   . GLN L  1 15  ? 13.058 -100.310 -19.177  1.00 64.27  ? 16  GLN L C   1 
ATOM   12299 O  O   . GLN L  1 15  ? 12.568 -100.789 -20.201  1.00 64.38  ? 16  GLN L O   1 
ATOM   12300 C  CB  . GLN L  1 15  ? 11.768 -99.900  -17.056  1.00 69.93  ? 16  GLN L CB  1 
ATOM   12301 C  CG  . GLN L  1 15  ? 10.627 -100.874 -17.225  1.00 74.02  ? 16  GLN L CG  1 
ATOM   12302 C  CD  . GLN L  1 15  ? 10.329 -101.657 -15.960  1.00 79.06  ? 16  GLN L CD  1 
ATOM   12303 O  OE1 . GLN L  1 15  ? 9.842  -102.776 -16.036  1.00 82.66  ? 16  GLN L OE1 1 
ATOM   12304 N  NE2 . GLN L  1 15  ? 10.633 -101.085 -14.794  1.00 79.67  ? 16  GLN L NE2 1 
ATOM   12305 N  N   . GLY L  1 16  ? 14.262 -100.640 -18.718  1.00 63.55  ? 17  GLY L N   1 
ATOM   12306 C  CA  . GLY L  1 16  ? 15.113 -101.582 -19.424  1.00 62.89  ? 17  GLY L CA  1 
ATOM   12307 C  C   . GLY L  1 16  ? 16.473 -101.800 -18.813  1.00 62.37  ? 17  GLY L C   1 
ATOM   12308 O  O   . GLY L  1 16  ? 16.827 -101.189 -17.821  1.00 62.32  ? 17  GLY L O   1 
ATOM   12309 N  N   . ILE L  1 17  ? 17.221 -102.693 -19.438  1.00 62.45  ? 18  ILE L N   1 
ATOM   12310 C  CA  . ILE L  1 17  ? 18.596 -103.006 -19.077  1.00 62.41  ? 18  ILE L CA  1 
ATOM   12311 C  C   . ILE L  1 17  ? 19.465 -102.937 -20.327  1.00 60.00  ? 18  ILE L C   1 
ATOM   12312 O  O   . ILE L  1 17  ? 19.124 -103.533 -21.355  1.00 60.45  ? 18  ILE L O   1 
ATOM   12313 C  CB  . ILE L  1 17  ? 18.711 -104.441 -18.532  1.00 66.58  ? 18  ILE L CB  1 
ATOM   12314 C  CG1 . ILE L  1 17  ? 18.334 -104.498 -17.050  1.00 69.50  ? 18  ILE L CG1 1 
ATOM   12315 C  CG2 . ILE L  1 17  ? 20.130 -105.006 -18.739  1.00 66.76  ? 18  ILE L CG2 1 
ATOM   12316 C  CD1 . ILE L  1 17  ? 18.740 -105.829 -16.346  1.00 73.76  ? 18  ILE L CD1 1 
ATOM   12317 N  N   . ILE L  1 18  ? 20.599 -102.240 -20.233  1.00 58.07  ? 19  ILE L N   1 
ATOM   12318 C  CA  . ILE L  1 18  ? 21.566 -102.154 -21.352  1.00 56.28  ? 19  ILE L CA  1 
ATOM   12319 C  C   . ILE L  1 18  ? 22.964 -102.568 -20.919  1.00 57.36  ? 19  ILE L C   1 
ATOM   12320 O  O   . ILE L  1 18  ? 23.472 -102.106 -19.906  1.00 57.68  ? 19  ILE L O   1 
ATOM   12321 C  CB  . ILE L  1 18  ? 21.654 -100.729 -21.941  1.00 52.88  ? 19  ILE L CB  1 
ATOM   12322 C  CG1 . ILE L  1 18  ? 20.329 -100.333 -22.614  1.00 52.00  ? 19  ILE L CG1 1 
ATOM   12323 C  CG2 . ILE L  1 18  ? 22.788 -100.641 -22.944  1.00 51.60  ? 19  ILE L CG2 1 
ATOM   12324 C  CD1 . ILE L  1 18  ? 20.011 -101.096 -23.873  1.00 52.57  ? 19  ILE L CD1 1 
ATOM   12325 N  N   . ASN L  1 19  ? 23.574 -103.436 -21.709  1.00 58.57  ? 20  ASN L N   1 
ATOM   12326 C  CA  . ASN L  1 19  ? 24.932 -103.919 -21.450  1.00 60.50  ? 20  ASN L CA  1 
ATOM   12327 C  C   . ASN L  1 19  ? 26.000 -103.251 -22.323  1.00 58.74  ? 20  ASN L C   1 
ATOM   12328 O  O   . ASN L  1 19  ? 25.733 -102.845 -23.443  1.00 57.08  ? 20  ASN L O   1 
ATOM   12329 C  CB  . ASN L  1 19  ? 25.016 -105.427 -21.684  1.00 64.18  ? 20  ASN L CB  1 
ATOM   12330 C  CG  . ASN L  1 19  ? 24.136 -106.217 -20.745  1.00 67.02  ? 20  ASN L CG  1 
ATOM   12331 O  OD1 . ASN L  1 19  ? 23.083 -106.707 -21.134  1.00 68.09  ? 20  ASN L OD1 1 
ATOM   12332 N  ND2 . ASN L  1 19  ? 24.572 -106.358 -19.504  1.00 68.78  ? 20  ASN L ND2 1 
ATOM   12333 N  N   . PHE L  1 20  ? 27.210 -103.155 -21.797  1.00 59.70  ? 21  PHE L N   1 
ATOM   12334 C  CA  . PHE L  1 20  ? 28.352 -102.680 -22.555  1.00 59.03  ? 21  PHE L CA  1 
ATOM   12335 C  C   . PHE L  1 20  ? 29.466 -103.706 -22.472  1.00 62.84  ? 21  PHE L C   1 
ATOM   12336 O  O   . PHE L  1 20  ? 29.642 -104.370 -21.436  1.00 65.60  ? 21  PHE L O   1 
ATOM   12337 C  CB  . PHE L  1 20  ? 28.869 -101.375 -21.980  1.00 57.35  ? 21  PHE L CB  1 
ATOM   12338 C  CG  . PHE L  1 20  ? 27.889 -100.260 -22.035  1.00 54.19  ? 21  PHE L CG  1 
ATOM   12339 C  CD1 . PHE L  1 20  ? 26.889 -100.158 -21.089  1.00 54.22  ? 21  PHE L CD1 1 
ATOM   12340 C  CD2 . PHE L  1 20  ? 27.978 -99.290  -23.008  1.00 51.82  ? 21  PHE L CD2 1 
ATOM   12341 C  CE1 . PHE L  1 20  ? 25.979 -99.103  -21.125  1.00 51.82  ? 21  PHE L CE1 1 
ATOM   12342 C  CE2 . PHE L  1 20  ? 27.073 -98.243  -23.052  1.00 49.34  ? 21  PHE L CE2 1 
ATOM   12343 C  CZ  . PHE L  1 20  ? 26.073 -98.152  -22.110  1.00 49.45  ? 21  PHE L CZ  1 
ATOM   12344 N  N   . GLU L  1 21  ? 30.239 -103.817 -23.547  1.00 63.47  ? 22  GLU L N   1 
ATOM   12345 C  CA  . GLU L  1 21  ? 31.398 -104.722 -23.569  1.00 67.55  ? 22  GLU L CA  1 
ATOM   12346 C  C   . GLU L  1 21  ? 32.492 -104.278 -24.531  1.00 67.86  ? 22  GLU L C   1 
ATOM   12347 O  O   . GLU L  1 21  ? 32.341 -104.347 -25.748  1.00 67.40  ? 22  GLU L O   1 
ATOM   12348 C  CB  . GLU L  1 21  ? 30.985 -106.162 -23.912  1.00 70.79  ? 22  GLU L CB  1 
ATOM   12349 C  CG  . GLU L  1 21  ? 32.168 -107.150 -23.891  1.00 76.08  ? 22  GLU L CG  1 
ATOM   12350 C  CD  . GLU L  1 21  ? 31.753 -108.615 -23.909  1.00 80.46  ? 22  GLU L CD  1 
ATOM   12351 O  OE1 . GLU L  1 21  ? 30.619 -108.917 -24.328  1.00 79.77  ? 22  GLU L OE1 1 
ATOM   12352 O  OE2 . GLU L  1 21  ? 32.576 -109.466 -23.505  1.00 84.99  ? 22  GLU L OE2 1 
ATOM   12353 N  N   . GLN L  1 22  ? 33.612 -103.861 -23.959  1.00 69.24  ? 23  GLN L N   1 
ATOM   12354 C  CA  . GLN L  1 22  ? 34.778 -103.443 -24.729  1.00 70.50  ? 23  GLN L CA  1 
ATOM   12355 C  C   . GLN L  1 22  ? 35.852 -104.512 -24.569  1.00 75.73  ? 23  GLN L C   1 
ATOM   12356 O  O   . GLN L  1 22  ? 36.433 -104.657 -23.499  1.00 77.92  ? 23  GLN L O   1 
ATOM   12357 C  CB  . GLN L  1 22  ? 35.274 -102.077 -24.222  1.00 68.70  ? 23  GLN L CB  1 
ATOM   12358 C  CG  . GLN L  1 22  ? 36.377 -101.442 -25.063  1.00 69.78  ? 23  GLN L CG  1 
ATOM   12359 C  CD  . GLN L  1 22  ? 36.832 -100.089 -24.526  1.00 68.60  ? 23  GLN L CD  1 
ATOM   12360 O  OE1 . GLN L  1 22  ? 37.030 -99.909  -23.313  1.00 69.39  ? 23  GLN L OE1 1 
ATOM   12361 N  NE2 . GLN L  1 22  ? 37.014 -99.130  -25.437  1.00 67.30  ? 23  GLN L NE2 1 
ATOM   12362 N  N   . LYS L  1 23  ? 36.105 -105.273 -25.622  1.00 78.24  ? 24  LYS L N   1 
ATOM   12363 C  CA  . LYS L  1 23  ? 37.089 -106.356 -25.535  1.00 83.99  ? 24  LYS L CA  1 
ATOM   12364 C  C   . LYS L  1 23  ? 38.504 -105.827 -25.346  1.00 86.35  ? 24  LYS L C   1 
ATOM   12365 O  O   . LYS L  1 23  ? 39.304 -106.430 -24.644  1.00 90.65  ? 24  LYS L O   1 
ATOM   12366 C  CB  . LYS L  1 23  ? 37.057 -107.250 -26.774  1.00 86.75  ? 24  LYS L CB  1 
ATOM   12367 C  CG  . LYS L  1 23  ? 35.746 -108.014 -26.940  1.00 86.25  ? 24  LYS L CG  1 
ATOM   12368 C  CD  . LYS L  1 23  ? 35.950 -109.321 -27.715  1.00 91.59  ? 24  LYS L CD  1 
ATOM   12369 C  CE  . LYS L  1 23  ? 34.653 -109.778 -28.403  1.00 90.43  ? 24  LYS L CE  1 
ATOM   12370 N  NZ  . LYS L  1 23  ? 34.889 -110.898 -29.366  1.00 95.46  ? 24  LYS L NZ  1 
ATOM   12371 N  N   . GLU L  1 24  ? 38.816 -104.706 -25.977  1.00 84.17  ? 25  GLU L N   1 
ATOM   12372 C  CA  . GLU L  1 24  ? 40.182 -104.166 -25.931  1.00 87.14  ? 25  GLU L CA  1 
ATOM   12373 C  C   . GLU L  1 24  ? 40.203 -102.657 -25.700  1.00 83.57  ? 25  GLU L C   1 
ATOM   12374 O  O   . GLU L  1 24  ? 39.423 -101.911 -26.284  1.00 79.66  ? 25  GLU L O   1 
ATOM   12375 C  CB  . GLU L  1 24  ? 40.928 -104.528 -27.217  1.00 90.68  ? 25  GLU L CB  1 
ATOM   12376 C  CG  . GLU L  1 24  ? 40.905 -106.027 -27.471  1.00 95.13  ? 25  GLU L CG  1 
ATOM   12377 C  CD  . GLU L  1 24  ? 41.891 -106.464 -28.528  1.00 100.91 ? 25  GLU L CD  1 
ATOM   12378 O  OE1 . GLU L  1 24  ? 41.921 -105.810 -29.600  1.00 99.92  ? 25  GLU L OE1 1 
ATOM   12379 O  OE2 . GLU L  1 24  ? 42.625 -107.459 -28.285  1.00 106.68 ? 25  GLU L OE2 1 
ATOM   12380 N  N   . SER L  1 25  ? 41.113 -102.215 -24.850  1.00 85.63  ? 26  SER L N   1 
ATOM   12381 C  CA  . SER L  1 25  ? 41.163 -100.810 -24.397  1.00 83.27  ? 26  SER L CA  1 
ATOM   12382 C  C   . SER L  1 25  ? 41.115 -99.770  -25.528  1.00 81.09  ? 26  SER L C   1 
ATOM   12383 O  O   . SER L  1 25  ? 40.518 -98.692  -25.403  1.00 77.37  ? 26  SER L O   1 
ATOM   12384 C  CB  . SER L  1 25  ? 42.430 -100.590 -23.554  1.00 87.61  ? 26  SER L CB  1 
ATOM   12385 O  OG  . SER L  1 25  ? 43.563 -101.198 -24.166  1.00 93.29  ? 26  SER L OG  1 
ATOM   12386 N  N   . ASN L  1 26  ? 41.768 -100.105 -26.629  1.00 83.96  ? 27  ASN L N   1 
ATOM   12387 C  CA  . ASN L  1 26  ? 41.817 -99.230  -27.799  1.00 82.84  ? 27  ASN L CA  1 
ATOM   12388 C  C   . ASN L  1 26  ? 40.654 -99.461  -28.781  1.00 79.36  ? 27  ASN L C   1 
ATOM   12389 O  O   . ASN L  1 26  ? 40.538 -98.769  -29.783  1.00 78.27  ? 27  ASN L O   1 
ATOM   12390 C  CB  . ASN L  1 26  ? 43.171 -99.421  -28.513  1.00 88.41  ? 27  ASN L CB  1 
ATOM   12391 C  CG  . ASN L  1 26  ? 43.328 -100.819 -29.163  1.00 91.83  ? 27  ASN L CG  1 
ATOM   12392 O  OD1 . ASN L  1 26  ? 43.041 -101.851 -28.543  1.00 92.50  ? 27  ASN L OD1 1 
ATOM   12393 N  ND2 . ASN L  1 26  ? 43.795 -100.844 -30.411  1.00 94.11  ? 27  ASN L ND2 1 
ATOM   12394 N  N   . GLY L  1 27  ? 39.787 -100.419 -28.471  1.00 78.05  ? 28  GLY L N   1 
ATOM   12395 C  CA  . GLY L  1 27  ? 38.832 -100.965 -29.443  1.00 76.38  ? 28  GLY L CA  1 
ATOM   12396 C  C   . GLY L  1 27  ? 37.397 -100.510 -29.253  1.00 71.14  ? 28  GLY L C   1 
ATOM   12397 O  O   . GLY L  1 27  ? 37.106 -99.723  -28.340  1.00 68.57  ? 28  GLY L O   1 
ATOM   12398 N  N   . PRO L  1 28  ? 36.487 -101.028 -30.109  1.00 69.92  ? 29  PRO L N   1 
ATOM   12399 C  CA  . PRO L  1 28  ? 35.106 -100.581 -30.089  1.00 65.42  ? 29  PRO L CA  1 
ATOM   12400 C  C   . PRO L  1 28  ? 34.324 -101.217 -28.944  1.00 64.47  ? 29  PRO L C   1 
ATOM   12401 O  O   . PRO L  1 28  ? 34.722 -102.264 -28.414  1.00 67.56  ? 29  PRO L O   1 
ATOM   12402 C  CB  . PRO L  1 28  ? 34.569 -101.072 -31.437  1.00 65.78  ? 29  PRO L CB  1 
ATOM   12403 C  CG  . PRO L  1 28  ? 35.295 -102.360 -31.665  1.00 70.37  ? 29  PRO L CG  1 
ATOM   12404 C  CD  . PRO L  1 28  ? 36.674 -102.154 -31.055  1.00 73.23  ? 29  PRO L CD  1 
ATOM   12405 N  N   . VAL L  1 29  ? 33.217 -100.572 -28.593  1.00 60.64  ? 30  VAL L N   1 
ATOM   12406 C  CA  . VAL L  1 29  ? 32.354 -100.985 -27.497  1.00 59.52  ? 30  VAL L CA  1 
ATOM   12407 C  C   . VAL L  1 29  ? 31.027 -101.485 -28.029  1.00 58.22  ? 30  VAL L C   1 
ATOM   12408 O  O   . VAL L  1 29  ? 30.271 -100.722 -28.627  1.00 55.66  ? 30  VAL L O   1 
ATOM   12409 C  CB  . VAL L  1 29  ? 32.024 -99.809  -26.594  1.00 56.80  ? 30  VAL L CB  1 
ATOM   12410 C  CG1 . VAL L  1 29  ? 31.047 -100.245 -25.546  1.00 56.08  ? 30  VAL L CG1 1 
ATOM   12411 C  CG2 . VAL L  1 29  ? 33.295 -99.228  -25.988  1.00 58.41  ? 30  VAL L CG2 1 
ATOM   12412 N  N   . LYS L  1 30  ? 30.734 -102.762 -27.813  1.00 60.64  ? 31  LYS L N   1 
ATOM   12413 C  CA  . LYS L  1 30  ? 29.417 -103.324 -28.158  1.00 59.95  ? 31  LYS L CA  1 
ATOM   12414 C  C   . LYS L  1 30  ? 28.418 -102.928 -27.102  1.00 57.67  ? 31  LYS L C   1 
ATOM   12415 O  O   . LYS L  1 30  ? 28.680 -103.069 -25.909  1.00 58.72  ? 31  LYS L O   1 
ATOM   12416 C  CB  . LYS L  1 30  ? 29.462 -104.842 -28.289  1.00 63.92  ? 31  LYS L CB  1 
ATOM   12417 C  CG  . LYS L  1 30  ? 30.210 -105.284 -29.528  1.00 66.86  ? 31  LYS L CG  1 
ATOM   12418 C  CD  . LYS L  1 30  ? 29.960 -106.736 -29.865  1.00 71.50  ? 31  LYS L CD  1 
ATOM   12419 C  CE  . LYS L  1 30  ? 30.720 -107.130 -31.136  1.00 74.57  ? 31  LYS L CE  1 
ATOM   12420 N  NZ  . LYS L  1 30  ? 30.440 -108.532 -31.569  1.00 79.35  ? 31  LYS L NZ  1 
ATOM   12421 N  N   . VAL L  1 31  ? 27.284 -102.410 -27.551  1.00 55.16  ? 32  VAL L N   1 
ATOM   12422 C  CA  . VAL L  1 31  ? 26.206 -101.984 -26.659  1.00 53.51  ? 32  VAL L CA  1 
ATOM   12423 C  C   . VAL L  1 31  ? 24.973 -102.801 -26.995  1.00 54.59  ? 32  VAL L C   1 
ATOM   12424 O  O   . VAL L  1 31  ? 24.524 -102.796 -28.141  1.00 54.40  ? 32  VAL L O   1 
ATOM   12425 C  CB  . VAL L  1 31  ? 25.857 -100.508 -26.844  1.00 50.08  ? 32  VAL L CB  1 
ATOM   12426 C  CG1 . VAL L  1 31  ? 24.858 -100.092 -25.806  1.00 48.89  ? 32  VAL L CG1 1 
ATOM   12427 C  CG2 . VAL L  1 31  ? 27.091 -99.667  -26.766  1.00 49.85  ? 32  VAL L CG2 1 
ATOM   12428 N  N   . TRP L  1 32  ? 24.431 -103.526 -26.024  1.00 56.40  ? 33  TRP L N   1 
ATOM   12429 C  CA  . TRP L  1 32  ? 23.236 -104.318 -26.289  1.00 57.99  ? 33  TRP L CA  1 
ATOM   12430 C  C   . TRP L  1 32  ? 22.348 -104.451 -25.074  1.00 58.76  ? 33  TRP L C   1 
ATOM   12431 O  O   . TRP L  1 32  ? 22.785 -104.276 -23.944  1.00 59.16  ? 33  TRP L O   1 
ATOM   12432 C  CB  . TRP L  1 32  ? 23.607 -105.695 -26.859  1.00 61.74  ? 33  TRP L CB  1 
ATOM   12433 C  CG  . TRP L  1 32  ? 23.888 -106.745 -25.839  1.00 65.33  ? 33  TRP L CG  1 
ATOM   12434 C  CD1 . TRP L  1 32  ? 23.037 -107.729 -25.420  1.00 68.72  ? 33  TRP L CD1 1 
ATOM   12435 C  CD2 . TRP L  1 32  ? 25.096 -106.929 -25.117  1.00 66.60  ? 33  TRP L CD2 1 
ATOM   12436 N  NE1 . TRP L  1 32  ? 23.639 -108.508 -24.473  1.00 71.60  ? 33  TRP L NE1 1 
ATOM   12437 C  CE2 . TRP L  1 32  ? 24.911 -108.039 -24.270  1.00 70.63  ? 33  TRP L CE2 1 
ATOM   12438 C  CE3 . TRP L  1 32  ? 26.315 -106.258 -25.090  1.00 65.63  ? 33  TRP L CE3 1 
ATOM   12439 C  CZ2 . TRP L  1 32  ? 25.915 -108.503 -23.407  1.00 73.49  ? 33  TRP L CZ2 1 
ATOM   12440 C  CZ3 . TRP L  1 32  ? 27.306 -106.706 -24.230  1.00 68.42  ? 33  TRP L CZ3 1 
ATOM   12441 C  CH2 . TRP L  1 32  ? 27.103 -107.824 -23.402  1.00 72.20  ? 33  TRP L CH2 1 
ATOM   12442 N  N   . GLY L  1 33  ? 21.088 -104.757 -25.330  1.00 59.52  ? 34  GLY L N   1 
ATOM   12443 C  CA  . GLY L  1 33  ? 20.124 -104.971 -24.266  1.00 61.03  ? 34  GLY L CA  1 
ATOM   12444 C  C   . GLY L  1 33  ? 18.710 -104.832 -24.764  1.00 61.17  ? 34  GLY L C   1 
ATOM   12445 O  O   . GLY L  1 33  ? 18.463 -104.861 -25.974  1.00 60.91  ? 34  GLY L O   1 
ATOM   12446 N  N   . SER L  1 34  ? 17.782 -104.660 -23.829  1.00 62.04  ? 35  SER L N   1 
ATOM   12447 C  CA  . SER L  1 34  ? 16.360 -104.568 -24.165  1.00 62.92  ? 35  SER L CA  1 
ATOM   12448 C  C   . SER L  1 34  ? 15.631 -103.501 -23.344  1.00 61.68  ? 35  SER L C   1 
ATOM   12449 O  O   . SER L  1 34  ? 15.557 -103.596 -22.123  1.00 63.22  ? 35  SER L O   1 
ATOM   12450 C  CB  . SER L  1 34  ? 15.699 -105.930 -23.961  1.00 67.62  ? 35  SER L CB  1 
ATOM   12451 O  OG  . SER L  1 34  ? 14.396 -105.947 -24.529  1.00 69.17  ? 35  SER L OG  1 
ATOM   12452 N  N   . ILE L  1 35  ? 15.103 -102.485 -24.026  1.00 59.41  ? 36  ILE L N   1 
ATOM   12453 C  CA  . ILE L  1 35  ? 14.266 -101.459 -23.382  1.00 59.02  ? 36  ILE L CA  1 
ATOM   12454 C  C   . ILE L  1 35  ? 12.817 -101.681 -23.747  1.00 61.56  ? 36  ILE L C   1 
ATOM   12455 O  O   . ILE L  1 35  ? 12.519 -102.053 -24.888  1.00 61.92  ? 36  ILE L O   1 
ATOM   12456 C  CB  . ILE L  1 35  ? 14.609 -100.045 -23.842  1.00 55.33  ? 36  ILE L CB  1 
ATOM   12457 C  CG1 . ILE L  1 35  ? 16.098 -99.772  -23.657  1.00 53.27  ? 36  ILE L CG1 1 
ATOM   12458 C  CG2 . ILE L  1 35  ? 13.775 -99.037  -23.080  1.00 55.35  ? 36  ILE L CG2 1 
ATOM   12459 C  CD1 . ILE L  1 35  ? 16.517 -98.426  -24.178  1.00 50.41  ? 36  ILE L CD1 1 
ATOM   12460 N  N   . LYS L  1 36  ? 11.920 -101.440 -22.794  1.00 63.73  ? 37  LYS L N   1 
ATOM   12461 C  CA  . LYS L  1 36  ? 10.483 -101.634 -23.026  1.00 66.87  ? 37  LYS L CA  1 
ATOM   12462 C  C   . LYS L  1 36  ? 9.591  -100.515 -22.472  1.00 67.22  ? 37  LYS L C   1 
ATOM   12463 O  O   . LYS L  1 36  ? 10.036 -99.659  -21.723  1.00 65.66  ? 37  LYS L O   1 
ATOM   12464 C  CB  . LYS L  1 36  ? 10.033 -103.002 -22.489  1.00 71.59  ? 37  LYS L CB  1 
ATOM   12465 C  CG  . LYS L  1 36  ? 10.249 -103.231 -21.011  1.00 73.61  ? 37  LYS L CG  1 
ATOM   12466 C  CD  . LYS L  1 36  ? 9.331  -104.355 -20.513  1.00 79.61  ? 37  LYS L CD  1 
ATOM   12467 C  CE  . LYS L  1 36  ? 9.618  -104.724 -19.060  1.00 82.25  ? 37  LYS L CE  1 
ATOM   12468 N  NZ  . LYS L  1 36  ? 8.583  -105.641 -18.479  1.00 88.12  ? 37  LYS L NZ  1 
ATOM   12469 N  N   . GLY L  1 37  ? 8.324  -100.544 -22.860  1.00 69.89  ? 38  GLY L N   1 
ATOM   12470 C  CA  . GLY L  1 37  ? 7.361  -99.505  -22.495  1.00 71.14  ? 38  GLY L CA  1 
ATOM   12471 C  C   . GLY L  1 37  ? 7.438  -98.310  -23.426  1.00 67.94  ? 38  GLY L C   1 
ATOM   12472 O  O   . GLY L  1 37  ? 6.916  -97.232  -23.132  1.00 68.26  ? 38  GLY L O   1 
ATOM   12473 N  N   . LEU L  1 38  ? 8.079  -98.510  -24.569  1.00 65.33  ? 39  LEU L N   1 
ATOM   12474 C  CA  . LEU L  1 38  ? 8.397  -97.408  -25.482  1.00 62.11  ? 39  LEU L CA  1 
ATOM   12475 C  C   . LEU L  1 38  ? 7.313  -97.199  -26.528  1.00 63.51  ? 39  LEU L C   1 
ATOM   12476 O  O   . LEU L  1 38  ? 6.741  -98.155  -27.037  1.00 65.81  ? 39  LEU L O   1 
ATOM   12477 C  CB  . LEU L  1 38  ? 9.759  -97.649  -26.179  1.00 58.69  ? 39  LEU L CB  1 
ATOM   12478 C  CG  . LEU L  1 38  ? 11.030 -97.243  -25.415  1.00 55.85  ? 39  LEU L CG  1 
ATOM   12479 C  CD1 . LEU L  1 38  ? 12.240 -97.914  -25.991  1.00 53.85  ? 39  LEU L CD1 1 
ATOM   12480 C  CD2 . LEU L  1 38  ? 11.201 -95.737  -25.433  1.00 53.85  ? 39  LEU L CD2 1 
ATOM   12481 N  N   . THR L  1 39  ? 7.071  -95.934  -26.858  1.00 62.38  ? 40  THR L N   1 
ATOM   12482 C  CA  . THR L  1 39  ? 6.156  -95.571  -27.943  1.00 63.70  ? 40  THR L CA  1 
ATOM   12483 C  C   . THR L  1 39  ? 6.753  -96.082  -29.264  1.00 61.80  ? 40  THR L C   1 
ATOM   12484 O  O   . THR L  1 39  ? 7.948  -95.926  -29.509  1.00 58.43  ? 40  THR L O   1 
ATOM   12485 C  CB  . THR L  1 39  ? 5.902  -94.036  -28.028  1.00 62.98  ? 40  THR L CB  1 
ATOM   12486 O  OG1 . THR L  1 39  ? 6.636  -93.489  -29.123  1.00 60.05  ? 40  THR L OG1 1 
ATOM   12487 C  CG2 . THR L  1 39  ? 6.303  -93.307  -26.733  1.00 62.48  ? 40  THR L CG2 1 
ATOM   12488 N  N   . GLU L  1 40  ? 5.930  -96.705  -30.106  1.00 64.50  ? 41  GLU L N   1 
ATOM   12489 C  CA  . GLU L  1 40  ? 6.441  -97.366  -31.321  1.00 63.58  ? 41  GLU L CA  1 
ATOM   12490 C  C   . GLU L  1 40  ? 7.232  -96.397  -32.159  1.00 59.94  ? 41  GLU L C   1 
ATOM   12491 O  O   . GLU L  1 40  ? 6.820  -95.270  -32.370  1.00 59.59  ? 41  GLU L O   1 
ATOM   12492 C  CB  . GLU L  1 40  ? 5.321  -97.959  -32.188  1.00 67.57  ? 41  GLU L CB  1 
ATOM   12493 C  CG  . GLU L  1 40  ? 5.833  -98.594  -33.512  1.00 67.41  ? 41  GLU L CG  1 
ATOM   12494 C  CD  . GLU L  1 40  ? 4.718  -99.070  -34.464  1.00 71.94  ? 41  GLU L CD  1 
ATOM   12495 O  OE1 . GLU L  1 40  ? 3.772  -98.297  -34.726  1.00 73.32  ? 41  GLU L OE1 1 
ATOM   12496 O  OE2 . GLU L  1 40  ? 4.802  -100.216 -34.972  1.00 73.94  ? 41  GLU L OE2 1 
ATOM   12497 N  N   . GLY L  1 41  ? 8.371  -96.855  -32.644  1.00 57.75  ? 42  GLY L N   1 
ATOM   12498 C  CA  . GLY L  1 41  ? 9.178  -96.070  -33.566  1.00 55.08  ? 42  GLY L CA  1 
ATOM   12499 C  C   . GLY L  1 41  ? 10.549 -95.736  -33.017  1.00 51.92  ? 42  GLY L C   1 
ATOM   12500 O  O   . GLY L  1 41  ? 11.031 -96.399  -32.084  1.00 51.73  ? 42  GLY L O   1 
ATOM   12501 N  N   . LEU L  1 42  ? 11.162 -94.694  -33.597  1.00 49.67  ? 43  LEU L N   1 
ATOM   12502 C  CA  . LEU L  1 42  ? 12.532 -94.298  -33.264  1.00 46.90  ? 43  LEU L CA  1 
ATOM   12503 C  C   . LEU L  1 42  ? 12.596 -93.566  -31.939  1.00 46.23  ? 43  LEU L C   1 
ATOM   12504 O  O   . LEU L  1 42  ? 11.679 -92.836  -31.586  1.00 47.50  ? 43  LEU L O   1 
ATOM   12505 C  CB  . LEU L  1 42  ? 13.135 -93.415  -34.361  1.00 45.47  ? 43  LEU L CB  1 
ATOM   12506 C  CG  . LEU L  1 42  ? 13.607 -94.152  -35.608  1.00 45.70  ? 43  LEU L CG  1 
ATOM   12507 C  CD1 . LEU L  1 42  ? 12.719 -93.816  -36.807  1.00 47.39  ? 43  LEU L CD1 1 
ATOM   12508 C  CD2 . LEU L  1 42  ? 15.045 -93.810  -35.899  1.00 44.00  ? 43  LEU L CD2 1 
ATOM   12509 N  N   . HIS L  1 43  ? 13.692 -93.762  -31.216  1.00 44.79  ? 44  HIS L N   1 
ATOM   12510 C  CA  . HIS L  1 43  ? 13.956 -93.015  -29.991  1.00 44.26  ? 44  HIS L CA  1 
ATOM   12511 C  C   . HIS L  1 43  ? 15.403 -92.615  -29.879  1.00 42.25  ? 44  HIS L C   1 
ATOM   12512 O  O   . HIS L  1 43  ? 16.293 -93.400  -30.143  1.00 41.84  ? 44  HIS L O   1 
ATOM   12513 C  CB  . HIS L  1 43  ? 13.563 -93.837  -28.773  1.00 45.83  ? 44  HIS L CB  1 
ATOM   12514 C  CG  . HIS L  1 43  ? 12.088 -93.968  -28.604  1.00 48.39  ? 44  HIS L CG  1 
ATOM   12515 N  ND1 . HIS L  1 43  ? 11.320 -92.982  -28.027  1.00 49.74  ? 44  HIS L ND1 1 
ATOM   12516 C  CD2 . HIS L  1 43  ? 11.231 -94.952  -28.968  1.00 50.57  ? 44  HIS L CD2 1 
ATOM   12517 C  CE1 . HIS L  1 43  ? 10.054 -93.362  -28.025  1.00 52.58  ? 44  HIS L CE1 1 
ATOM   12518 N  NE2 . HIS L  1 43  ? 9.974  -94.554  -28.591  1.00 53.06  ? 44  HIS L NE2 1 
ATOM   12519 N  N   . GLY L  1 44  ? 15.630 -91.383  -29.467  1.00 41.70  ? 45  GLY L N   1 
ATOM   12520 C  CA  . GLY L  1 44  ? 16.982 -90.890  -29.207  1.00 40.55  ? 45  GLY L CA  1 
ATOM   12521 C  C   . GLY L  1 44  ? 17.645 -91.652  -28.078  1.00 40.56  ? 45  GLY L C   1 
ATOM   12522 O  O   . GLY L  1 44  ? 16.983 -92.088  -27.149  1.00 41.83  ? 45  GLY L O   1 
ATOM   12523 N  N   . PHE L  1 45  ? 18.962 -91.775  -28.142  1.00 39.72  ? 46  PHE L N   1 
ATOM   12524 C  CA  . PHE L  1 45  ? 19.685 -92.677  -27.261  1.00 40.09  ? 46  PHE L CA  1 
ATOM   12525 C  C   . PHE L  1 45  ? 21.097 -92.184  -27.049  1.00 39.70  ? 46  PHE L C   1 
ATOM   12526 O  O   . PHE L  1 45  ? 21.940 -92.391  -27.899  1.00 39.41  ? 46  PHE L O   1 
ATOM   12527 C  CB  . PHE L  1 45  ? 19.712 -94.047  -27.903  1.00 40.52  ? 46  PHE L CB  1 
ATOM   12528 C  CG  . PHE L  1 45  ? 20.211 -95.143  -27.012  1.00 41.56  ? 46  PHE L CG  1 
ATOM   12529 C  CD1 . PHE L  1 45  ? 19.683 -95.337  -25.756  1.00 42.81  ? 46  PHE L CD1 1 
ATOM   12530 C  CD2 . PHE L  1 45  ? 21.159 -96.030  -27.460  1.00 42.05  ? 46  PHE L CD2 1 
ATOM   12531 C  CE1 . PHE L  1 45  ? 20.123 -96.372  -24.949  1.00 44.23  ? 46  PHE L CE1 1 
ATOM   12532 C  CE2 . PHE L  1 45  ? 21.596 -97.061  -26.665  1.00 43.62  ? 46  PHE L CE2 1 
ATOM   12533 C  CZ  . PHE L  1 45  ? 21.076 -97.232  -25.406  1.00 44.71  ? 46  PHE L CZ  1 
ATOM   12534 N  N   . HIS L  1 46  ? 21.351 -91.528  -25.921  1.00 40.16  ? 47  HIS L N   1 
ATOM   12535 C  CA  . HIS L  1 46  ? 22.618 -90.848  -25.691  1.00 40.20  ? 47  HIS L CA  1 
ATOM   12536 C  C   . HIS L  1 46  ? 23.209 -91.070  -24.307  1.00 41.39  ? 47  HIS L C   1 
ATOM   12537 O  O   . HIS L  1 46  ? 22.500 -91.346  -23.357  1.00 42.30  ? 47  HIS L O   1 
ATOM   12538 C  CB  . HIS L  1 46  ? 22.436 -89.357  -25.902  1.00 40.22  ? 47  HIS L CB  1 
ATOM   12539 C  CG  . HIS L  1 46  ? 21.549 -89.011  -27.050  1.00 39.34  ? 47  HIS L CG  1 
ATOM   12540 N  ND1 . HIS L  1 46  ? 20.260 -88.573  -26.887  1.00 39.85  ? 47  HIS L ND1 1 
ATOM   12541 C  CD2 . HIS L  1 46  ? 21.768 -89.035  -28.380  1.00 39.22  ? 47  HIS L CD2 1 
ATOM   12542 C  CE1 . HIS L  1 46  ? 19.721 -88.335  -28.064  1.00 39.56  ? 47  HIS L CE1 1 
ATOM   12543 N  NE2 . HIS L  1 46  ? 20.616 -88.607  -28.988  1.00 39.06  ? 47  HIS L NE2 1 
ATOM   12544 N  N   . VAL L  1 47  ? 24.529 -90.950  -24.217  1.00 41.90  ? 48  VAL L N   1 
ATOM   12545 C  CA  . VAL L  1 47  ? 25.238 -90.950  -22.942  1.00 43.29  ? 48  VAL L CA  1 
ATOM   12546 C  C   . VAL L  1 47  ? 25.426 -89.526  -22.517  1.00 44.17  ? 48  VAL L C   1 
ATOM   12547 O  O   . VAL L  1 47  ? 26.081 -88.769  -23.222  1.00 44.23  ? 48  VAL L O   1 
ATOM   12548 C  CB  . VAL L  1 47  ? 26.627 -91.553  -23.060  1.00 44.01  ? 48  VAL L CB  1 
ATOM   12549 C  CG1 . VAL L  1 47  ? 27.395 -91.311  -21.799  1.00 45.85  ? 48  VAL L CG1 1 
ATOM   12550 C  CG2 . VAL L  1 47  ? 26.550 -93.025  -23.338  1.00 44.30  ? 48  VAL L CG2 1 
ATOM   12551 N  N   . HIS L  1 48  ? 24.856 -89.158  -21.373  1.00 45.44  ? 49  HIS L N   1 
ATOM   12552 C  CA  . HIS L  1 48  ? 24.954 -87.784  -20.840  1.00 47.01  ? 49  HIS L CA  1 
ATOM   12553 C  C   . HIS L  1 48  ? 26.104 -87.622  -19.870  1.00 49.07  ? 49  HIS L C   1 
ATOM   12554 O  O   . HIS L  1 48  ? 26.606 -88.603  -19.340  1.00 49.71  ? 49  HIS L O   1 
ATOM   12555 C  CB  . HIS L  1 48  ? 23.666 -87.391  -20.148  1.00 47.83  ? 49  HIS L CB  1 
ATOM   12556 C  CG  . HIS L  1 48  ? 22.534 -87.165  -21.090  1.00 46.54  ? 49  HIS L CG  1 
ATOM   12557 N  ND1 . HIS L  1 48  ? 21.839 -85.977  -21.142  1.00 47.77  ? 49  HIS L ND1 1 
ATOM   12558 C  CD2 . HIS L  1 48  ? 21.996 -87.958  -22.040  1.00 44.45  ? 49  HIS L CD2 1 
ATOM   12559 C  CE1 . HIS L  1 48  ? 20.915 -86.052  -22.077  1.00 46.51  ? 49  HIS L CE1 1 
ATOM   12560 N  NE2 . HIS L  1 48  ? 20.989 -87.247  -22.635  1.00 44.57  ? 49  HIS L NE2 1 
ATOM   12561 N  N   . GLU L  1 49  ? 26.495 -86.377  -19.616  1.00 50.78  ? 50  GLU L N   1 
ATOM   12562 C  CA  . GLU L  1 49  ? 27.758 -86.076  -18.893  1.00 53.20  ? 50  GLU L CA  1 
ATOM   12563 C  C   . GLU L  1 49  ? 27.836 -86.642  -17.471  1.00 54.89  ? 50  GLU L C   1 
ATOM   12564 O  O   . GLU L  1 49  ? 28.784 -87.348  -17.121  1.00 55.51  ? 50  GLU L O   1 
ATOM   12565 C  CB  . GLU L  1 49  ? 28.003 -84.560  -18.837  1.00 55.44  ? 50  GLU L CB  1 
ATOM   12566 C  CG  . GLU L  1 49  ? 29.383 -84.165  -18.329  1.00 58.09  ? 50  GLU L CG  1 
ATOM   12567 C  CD  . GLU L  1 49  ? 29.694 -82.697  -18.531  1.00 60.41  ? 50  GLU L CD  1 
ATOM   12568 O  OE1 . GLU L  1 49  ? 28.962 -82.002  -19.264  1.00 59.21  ? 50  GLU L OE1 1 
ATOM   12569 O  OE2 . GLU L  1 49  ? 30.690 -82.235  -17.945  1.00 63.71  ? 50  GLU L OE2 1 
ATOM   12570 N  N   . PHE L  1 50  ? 26.825 -86.338  -16.667  1.00 55.89  ? 51  PHE L N   1 
ATOM   12571 C  CA  . PHE L  1 50  ? 26.861 -86.645  -15.236  1.00 58.33  ? 51  PHE L CA  1 
ATOM   12572 C  C   . PHE L  1 50  ? 26.064 -87.880  -14.818  1.00 57.68  ? 51  PHE L C   1 
ATOM   12573 O  O   . PHE L  1 50  ? 24.930 -88.089  -15.273  1.00 56.13  ? 51  PHE L O   1 
ATOM   12574 C  CB  . PHE L  1 50  ? 26.340 -85.454  -14.461  1.00 60.93  ? 51  PHE L CB  1 
ATOM   12575 C  CG  . PHE L  1 50  ? 27.032 -84.172  -14.805  1.00 62.47  ? 51  PHE L CG  1 
ATOM   12576 C  CD1 . PHE L  1 50  ? 28.391 -84.050  -14.641  1.00 64.12  ? 51  PHE L CD1 1 
ATOM   12577 C  CD2 . PHE L  1 50  ? 26.323 -83.080  -15.271  1.00 63.08  ? 51  PHE L CD2 1 
ATOM   12578 C  CE1 . PHE L  1 50  ? 29.032 -82.864  -14.936  1.00 66.22  ? 51  PHE L CE1 1 
ATOM   12579 C  CE2 . PHE L  1 50  ? 26.963 -81.894  -15.568  1.00 64.91  ? 51  PHE L CE2 1 
ATOM   12580 C  CZ  . PHE L  1 50  ? 28.312 -81.787  -15.399  1.00 66.50  ? 51  PHE L CZ  1 
ATOM   12581 N  N   . GLY L  1 51  ? 26.669 -88.673  -13.929  1.00 59.31  ? 52  GLY L N   1 
ATOM   12582 C  CA  . GLY L  1 51  ? 25.997 -89.798  -13.261  1.00 59.82  ? 52  GLY L CA  1 
ATOM   12583 C  C   . GLY L  1 51  ? 25.182 -89.341  -12.054  1.00 62.57  ? 52  GLY L C   1 
ATOM   12584 O  O   . GLY L  1 51  ? 25.170 -89.990  -11.004  1.00 64.68  ? 52  GLY L O   1 
ATOM   12585 N  N   . ASP L  1 52  ? 24.487 -88.219  -12.223  1.00 62.82  ? 53  ASP L N   1 
ATOM   12586 C  CA  . ASP L  1 52  ? 23.736 -87.578  -11.160  1.00 65.89  ? 53  ASP L CA  1 
ATOM   12587 C  C   . ASP L  1 52  ? 22.274 -87.862  -11.379  1.00 65.33  ? 53  ASP L C   1 
ATOM   12588 O  O   . ASP L  1 52  ? 21.733 -87.529  -12.428  1.00 63.18  ? 53  ASP L O   1 
ATOM   12589 C  CB  . ASP L  1 52  ? 23.980 -86.072  -11.207  1.00 67.48  ? 53  ASP L CB  1 
ATOM   12590 C  CG  . ASP L  1 52  ? 23.446 -85.359  -9.997   1.00 71.79  ? 53  ASP L CG  1 
ATOM   12591 O  OD1 . ASP L  1 52  ? 22.404 -85.808  -9.476   1.00 73.07  ? 53  ASP L OD1 1 
ATOM   12592 O  OD2 . ASP L  1 52  ? 24.065 -84.346  -9.578   1.00 74.38  ? 53  ASP L OD2 1 
ATOM   12593 N  N   . ASN L  1 53  ? 21.641 -88.479  -10.387  1.00 67.83  ? 54  ASN L N   1 
ATOM   12594 C  CA  . ASN L  1 53  ? 20.199 -88.817  -10.451  1.00 68.31  ? 54  ASN L CA  1 
ATOM   12595 C  C   . ASN L  1 53  ? 19.375 -88.103  -9.374   1.00 72.27  ? 54  ASN L C   1 
ATOM   12596 O  O   . ASN L  1 53  ? 18.217 -88.444  -9.141   1.00 73.49  ? 54  ASN L O   1 
ATOM   12597 C  CB  . ASN L  1 53  ? 20.013 -90.336  -10.330  1.00 68.05  ? 54  ASN L CB  1 
ATOM   12598 C  CG  . ASN L  1 53  ? 19.115 -90.904  -11.411  1.00 66.05  ? 54  ASN L CG  1 
ATOM   12599 O  OD1 . ASN L  1 53  ? 19.467 -90.904  -12.605  1.00 63.16  ? 54  ASN L OD1 1 
ATOM   12600 N  ND2 . ASN L  1 53  ? 17.958 -91.407  -11.002  1.00 68.09  ? 54  ASN L ND2 1 
ATOM   12601 N  N   . THR L  1 54  ? 20.009 -87.111  -8.750   1.00 74.46  ? 55  THR L N   1 
ATOM   12602 C  CA  . THR L  1 54  ? 19.445 -86.309  -7.674   1.00 79.15  ? 55  THR L CA  1 
ATOM   12603 C  C   . THR L  1 54  ? 18.008 -85.886  -7.969   1.00 80.33  ? 55  THR L C   1 
ATOM   12604 O  O   . THR L  1 54  ? 17.060 -86.320  -7.300   1.00 83.07  ? 55  THR L O   1 
ATOM   12605 C  CB  . THR L  1 54  ? 20.301 -85.035  -7.468   1.00 80.81  ? 55  THR L CB  1 
ATOM   12606 O  OG1 . THR L  1 54  ? 21.555 -85.410  -6.888   1.00 81.44  ? 55  THR L OG1 1 
ATOM   12607 C  CG2 . THR L  1 54  ? 19.598 -84.014  -6.586   1.00 85.96  ? 55  THR L CG2 1 
ATOM   12608 N  N   . ALA L  1 55  ? 17.858 -85.033  -8.978   1.00 78.60  ? 56  ALA L N   1 
ATOM   12609 C  CA  . ALA L  1 55  ? 16.551 -84.529  -9.396   1.00 79.68  ? 56  ALA L CA  1 
ATOM   12610 C  C   . ALA L  1 55  ? 16.083 -85.270  -10.665  1.00 75.54  ? 56  ALA L C   1 
ATOM   12611 O  O   . ALA L  1 55  ? 15.652 -84.651  -11.660  1.00 74.24  ? 56  ALA L O   1 
ATOM   12612 C  CB  . ALA L  1 55  ? 16.624 -83.009  -9.624   1.00 81.36  ? 56  ALA L CB  1 
ATOM   12613 N  N   . GLY L  1 56  ? 16.172 -86.601  -10.621  1.00 73.87  ? 57  GLY L N   1 
ATOM   12614 C  CA  . GLY L  1 56  ? 15.690 -87.456  -11.709  1.00 70.71  ? 57  GLY L CA  1 
ATOM   12615 C  C   . GLY L  1 56  ? 16.693 -87.591  -12.833  1.00 66.22  ? 57  GLY L C   1 
ATOM   12616 O  O   . GLY L  1 56  ? 17.896 -87.580  -12.592  1.00 65.49  ? 57  GLY L O   1 
ATOM   12617 N  N   . CYS L  1 57  ? 16.186 -87.721  -14.060  1.00 63.70  ? 58  CYS L N   1 
ATOM   12618 C  CA  . CYS L  1 57  ? 17.033 -87.753  -15.255  1.00 59.75  ? 58  CYS L CA  1 
ATOM   12619 C  C   . CYS L  1 57  ? 17.609 -86.385  -15.602  1.00 59.58  ? 58  CYS L C   1 
ATOM   12620 O  O   . CYS L  1 57  ? 18.682 -86.315  -16.168  1.00 57.51  ? 58  CYS L O   1 
ATOM   12621 C  CB  . CYS L  1 57  ? 16.266 -88.280  -16.471  1.00 57.62  ? 58  CYS L CB  1 
ATOM   12622 S  SG  . CYS L  1 57  ? 15.903 -90.049  -16.509  1.00 57.35  ? 58  CYS L SG  1 
ATOM   12623 N  N   . THR L  1 58  ? 16.910 -85.309  -15.249  1.00 62.41  ? 59  THR L N   1 
ATOM   12624 C  CA  . THR L  1 58  ? 17.341 -83.931  -15.584  1.00 63.12  ? 59  THR L CA  1 
ATOM   12625 C  C   . THR L  1 58  ? 18.719 -83.594  -15.038  1.00 63.54  ? 59  THR L C   1 
ATOM   12626 O  O   . THR L  1 58  ? 19.438 -82.813  -15.631  1.00 63.03  ? 59  THR L O   1 
ATOM   12627 C  CB  . THR L  1 58  ? 16.393 -82.851  -15.009  1.00 67.33  ? 59  THR L CB  1 
ATOM   12628 O  OG1 . THR L  1 58  ? 15.026 -83.252  -15.182  1.00 68.26  ? 59  THR L OG1 1 
ATOM   12629 C  CG2 . THR L  1 58  ? 16.650 -81.492  -15.679  1.00 67.75  ? 59  THR L CG2 1 
ATOM   12630 N  N   . SER L  1 59  ? 19.054 -84.175  -13.893  1.00 65.06  ? 60  SER L N   1 
ATOM   12631 C  CA  . SER L  1 59  ? 20.333 -83.950  -13.225  1.00 66.28  ? 60  SER L CA  1 
ATOM   12632 C  C   . SER L  1 59  ? 21.541 -84.434  -14.028  1.00 63.12  ? 60  SER L C   1 
ATOM   12633 O  O   . SER L  1 59  ? 22.665 -83.961  -13.812  1.00 64.15  ? 60  SER L O   1 
ATOM   12634 C  CB  . SER L  1 59  ? 20.346 -84.665  -11.874  1.00 68.67  ? 60  SER L CB  1 
ATOM   12635 O  OG  . SER L  1 59  ? 19.140 -84.456  -11.169  1.00 72.12  ? 60  SER L OG  1 
ATOM   12636 N  N   . ALA L  1 60  ? 21.305 -85.381  -14.938  1.00 59.81  ? 61  ALA L N   1 
ATOM   12637 C  CA  . ALA L  1 60  ? 22.364 -85.961  -15.781  1.00 56.97  ? 61  ALA L CA  1 
ATOM   12638 C  C   . ALA L  1 60  ? 23.075 -84.931  -16.667  1.00 56.34  ? 61  ALA L C   1 
ATOM   12639 O  O   . ALA L  1 60  ? 24.147 -85.201  -17.201  1.00 55.03  ? 61  ALA L O   1 
ATOM   12640 C  CB  . ALA L  1 60  ? 21.786 -87.073  -16.638  1.00 54.25  ? 61  ALA L CB  1 
ATOM   12641 N  N   . GLY L  1 61  ? 22.465 -83.764  -16.834  1.00 57.64  ? 62  GLY L N   1 
ATOM   12642 C  CA  . GLY L  1 61  ? 23.059 -82.700  -17.606  1.00 57.95  ? 62  GLY L CA  1 
ATOM   12643 C  C   . GLY L  1 61  ? 22.961 -82.976  -19.090  1.00 54.87  ? 62  GLY L C   1 
ATOM   12644 O  O   . GLY L  1 61  ? 22.096 -83.724  -19.518  1.00 52.95  ? 62  GLY L O   1 
ATOM   12645 N  N   . PRO L  1 62  ? 23.847 -82.359  -19.887  1.00 54.77  ? 63  PRO L N   1 
ATOM   12646 C  CA  . PRO L  1 62  ? 23.773 -82.455  -21.325  1.00 52.43  ? 63  PRO L CA  1 
ATOM   12647 C  C   . PRO L  1 62  ? 24.499 -83.655  -21.861  1.00 49.99  ? 63  PRO L C   1 
ATOM   12648 O  O   . PRO L  1 62  ? 25.040 -84.452  -21.100  1.00 49.99  ? 63  PRO L O   1 
ATOM   12649 C  CB  . PRO L  1 62  ? 24.501 -81.196  -21.783  1.00 54.43  ? 63  PRO L CB  1 
ATOM   12650 C  CG  . PRO L  1 62  ? 25.535 -81.007  -20.767  1.00 56.70  ? 63  PRO L CG  1 
ATOM   12651 C  CD  . PRO L  1 62  ? 24.925 -81.442  -19.473  1.00 57.53  ? 63  PRO L CD  1 
ATOM   12652 N  N   . HIS L  1 63  ? 24.495 -83.755  -23.185  1.00 48.34  ? 64  HIS L N   1 
ATOM   12653 C  CA  . HIS L  1 63  ? 25.162 -84.832  -23.912  1.00 46.51  ? 64  HIS L CA  1 
ATOM   12654 C  C   . HIS L  1 63  ? 26.636 -84.844  -23.563  1.00 47.61  ? 64  HIS L C   1 
ATOM   12655 O  O   . HIS L  1 63  ? 27.269 -83.803  -23.516  1.00 49.52  ? 64  HIS L O   1 
ATOM   12656 C  CB  . HIS L  1 63  ? 25.002 -84.636  -25.433  1.00 45.50  ? 64  HIS L CB  1 
ATOM   12657 C  CG  . HIS L  1 63  ? 23.620 -84.898  -25.957  1.00 43.96  ? 64  HIS L CG  1 
ATOM   12658 N  ND1 . HIS L  1 63  ? 23.395 -85.414  -27.216  1.00 42.29  ? 64  HIS L ND1 1 
ATOM   12659 C  CD2 . HIS L  1 63  ? 22.399 -84.707  -25.403  1.00 44.28  ? 64  HIS L CD2 1 
ATOM   12660 C  CE1 . HIS L  1 63  ? 22.094 -85.539  -27.409  1.00 42.00  ? 64  HIS L CE1 1 
ATOM   12661 N  NE2 . HIS L  1 63  ? 21.469 -85.111  -26.327  1.00 43.14  ? 64  HIS L NE2 1 
ATOM   12662 N  N   . PHE L  1 64  ? 27.181 -86.023  -23.331  1.00 46.93  ? 65  PHE L N   1 
ATOM   12663 C  CA  . PHE L  1 64  ? 28.587 -86.129  -22.977  1.00 48.74  ? 65  PHE L CA  1 
ATOM   12664 C  C   . PHE L  1 64  ? 29.436 -85.640  -24.127  1.00 49.13  ? 65  PHE L C   1 
ATOM   12665 O  O   . PHE L  1 64  ? 29.424 -86.229  -25.196  1.00 47.53  ? 65  PHE L O   1 
ATOM   12666 C  CB  . PHE L  1 64  ? 28.961 -87.570  -22.598  1.00 48.46  ? 65  PHE L CB  1 
ATOM   12667 C  CG  . PHE L  1 64  ? 30.423 -87.761  -22.197  1.00 50.55  ? 65  PHE L CG  1 
ATOM   12668 C  CD1 . PHE L  1 64  ? 31.080 -86.843  -21.375  1.00 53.14  ? 65  PHE L CD1 1 
ATOM   12669 C  CD2 . PHE L  1 64  ? 31.124 -88.884  -22.608  1.00 50.71  ? 65  PHE L CD2 1 
ATOM   12670 C  CE1 . PHE L  1 64  ? 32.413 -87.039  -21.002  1.00 55.70  ? 65  PHE L CE1 1 
ATOM   12671 C  CE2 . PHE L  1 64  ? 32.462 -89.077  -22.236  1.00 53.33  ? 65  PHE L CE2 1 
ATOM   12672 C  CZ  . PHE L  1 64  ? 33.099 -88.156  -21.432  1.00 55.67  ? 65  PHE L CZ  1 
ATOM   12673 N  N   . ASN L  1 65  ? 30.184 -84.569  -23.880  1.00 51.75  ? 66  ASN L N   1 
ATOM   12674 C  CA  . ASN L  1 65  ? 30.858 -83.834  -24.943  1.00 52.98  ? 66  ASN L CA  1 
ATOM   12675 C  C   . ASN L  1 65  ? 32.182 -83.240  -24.501  1.00 56.51  ? 66  ASN L C   1 
ATOM   12676 O  O   . ASN L  1 65  ? 32.295 -82.027  -24.368  1.00 58.91  ? 66  ASN L O   1 
ATOM   12677 C  CB  . ASN L  1 65  ? 29.941 -82.711  -25.414  1.00 52.95  ? 66  ASN L CB  1 
ATOM   12678 C  CG  . ASN L  1 65  ? 30.485 -81.979  -26.623  1.00 54.10  ? 66  ASN L CG  1 
ATOM   12679 O  OD1 . ASN L  1 65  ? 31.464 -82.397  -27.217  1.00 54.83  ? 66  ASN L OD1 1 
ATOM   12680 N  ND2 . ASN L  1 65  ? 29.842 -80.886  -26.993  1.00 54.96  ? 66  ASN L ND2 1 
ATOM   12681 N  N   . PRO L  1 66  ? 33.194 -84.088  -24.274  1.00 57.43  ? 67  PRO L N   1 
ATOM   12682 C  CA  . PRO L  1 66  ? 34.496 -83.633  -23.780  1.00 61.20  ? 67  PRO L CA  1 
ATOM   12683 C  C   . PRO L  1 66  ? 35.368 -82.960  -24.836  1.00 63.62  ? 67  PRO L C   1 
ATOM   12684 O  O   . PRO L  1 66  ? 36.241 -82.178  -24.484  1.00 67.51  ? 67  PRO L O   1 
ATOM   12685 C  CB  . PRO L  1 66  ? 35.158 -84.925  -23.313  1.00 61.33  ? 67  PRO L CB  1 
ATOM   12686 C  CG  . PRO L  1 66  ? 34.584 -85.966  -24.179  1.00 58.25  ? 67  PRO L CG  1 
ATOM   12687 C  CD  . PRO L  1 66  ? 33.166 -85.544  -24.470  1.00 55.48  ? 67  PRO L CD  1 
ATOM   12688 N  N   . LEU L  1 67  ? 35.137 -83.269  -26.111  1.00 61.98  ? 68  LEU L N   1 
ATOM   12689 C  CA  . LEU L  1 67  ? 35.898 -82.666  -27.215  1.00 64.25  ? 68  LEU L CA  1 
ATOM   12690 C  C   . LEU L  1 67  ? 35.214 -81.414  -27.764  1.00 64.39  ? 68  LEU L C   1 
ATOM   12691 O  O   . LEU L  1 67  ? 35.569 -80.920  -28.835  1.00 65.87  ? 68  LEU L O   1 
ATOM   12692 C  CB  . LEU L  1 67  ? 36.141 -83.693  -28.333  1.00 63.14  ? 68  LEU L CB  1 
ATOM   12693 C  CG  . LEU L  1 67  ? 36.898 -84.972  -27.931  1.00 63.72  ? 68  LEU L CG  1 
ATOM   12694 C  CD1 . LEU L  1 67  ? 37.258 -85.791  -29.170  1.00 63.73  ? 68  LEU L CD1 1 
ATOM   12695 C  CD2 . LEU L  1 67  ? 38.150 -84.657  -27.094  1.00 67.75  ? 68  LEU L CD2 1 
ATOM   12696 N  N   . SER L  1 68  ? 34.229 -80.918  -27.022  1.00 63.36  ? 69  SER L N   1 
ATOM   12697 C  CA  . SER L  1 68  ? 33.601 -79.597  -27.260  1.00 64.67  ? 69  SER L CA  1 
ATOM   12698 C  C   . SER L  1 68  ? 33.093 -79.416  -28.682  1.00 63.38  ? 69  SER L C   1 
ATOM   12699 O  O   . SER L  1 68  ? 33.312 -78.361  -29.280  1.00 65.89  ? 69  SER L O   1 
ATOM   12700 C  CB  . SER L  1 68  ? 34.576 -78.465  -26.928  1.00 69.72  ? 69  SER L CB  1 
ATOM   12701 O  OG  . SER L  1 68  ? 35.210 -78.670  -25.679  1.00 71.65  ? 69  SER L OG  1 
ATOM   12702 N  N   . ARG L  1 69  ? 32.414 -80.449  -29.201  1.00 59.82  ? 70  ARG L N   1 
ATOM   12703 C  CA  . ARG L  1 69  ? 31.884 -80.460  -30.579  1.00 58.66  ? 70  ARG L CA  1 
ATOM   12704 C  C   . ARG L  1 69  ? 30.376 -80.251  -30.632  1.00 56.17  ? 70  ARG L C   1 
ATOM   12705 O  O   . ARG L  1 69  ? 29.715 -80.145  -29.610  1.00 55.49  ? 70  ARG L O   1 
ATOM   12706 C  CB  . ARG L  1 69  ? 32.275 -81.755  -31.301  1.00 57.11  ? 70  ARG L CB  1 
ATOM   12707 C  CG  . ARG L  1 69  ? 33.708 -81.711  -31.810  1.00 61.72  ? 70  ARG L CG  1 
ATOM   12708 C  CD  . ARG L  1 69  ? 34.236 -83.048  -32.343  1.00 62.47  ? 70  ARG L CD  1 
ATOM   12709 N  NE  . ARG L  1 69  ? 35.702 -83.134  -32.247  1.00 67.38  ? 70  ARG L NE  1 
ATOM   12710 C  CZ  . ARG L  1 69  ? 36.471 -84.003  -32.907  1.00 69.91  ? 70  ARG L CZ  1 
ATOM   12711 N  NH1 . ARG L  1 69  ? 35.947 -84.883  -33.762  1.00 68.16  ? 70  ARG L NH1 1 
ATOM   12712 N  NH2 . ARG L  1 69  ? 37.790 -83.988  -32.718  1.00 74.18  ? 70  ARG L NH2 1 
ATOM   12713 N  N   . LYS L  1 70  ? 29.855 -80.176  -31.848  1.00 55.44  ? 71  LYS L N   1 
ATOM   12714 C  CA  . LYS L  1 70  ? 28.420 -80.049  -32.103  1.00 53.53  ? 71  LYS L CA  1 
ATOM   12715 C  C   . LYS L  1 70  ? 27.729 -81.420  -32.130  1.00 50.11  ? 71  LYS L C   1 
ATOM   12716 O  O   . LYS L  1 70  ? 28.361 -82.458  -32.366  1.00 49.21  ? 71  LYS L O   1 
ATOM   12717 C  CB  . LYS L  1 70  ? 28.188 -79.379  -33.457  1.00 54.80  ? 71  LYS L CB  1 
ATOM   12718 C  CG  . LYS L  1 70  ? 28.851 -78.015  -33.626  1.00 59.26  ? 71  LYS L CG  1 
ATOM   12719 C  CD  . LYS L  1 70  ? 27.899 -76.870  -33.267  1.00 60.92  ? 71  LYS L CD  1 
ATOM   12720 C  CE  . LYS L  1 70  ? 28.497 -75.488  -33.514  1.00 65.48  ? 71  LYS L CE  1 
ATOM   12721 N  NZ  . LYS L  1 70  ? 27.499 -74.421  -33.147  1.00 67.03  ? 71  LYS L NZ  1 
ATOM   12722 N  N   . HIS L  1 71  ? 26.419 -81.426  -31.915  1.00 48.64  ? 72  HIS L N   1 
ATOM   12723 C  CA  . HIS L  1 71  ? 25.645 -82.676  -31.943  1.00 45.90  ? 72  HIS L CA  1 
ATOM   12724 C  C   . HIS L  1 71  ? 25.666 -83.302  -33.330  1.00 45.07  ? 72  HIS L C   1 
ATOM   12725 O  O   . HIS L  1 71  ? 25.812 -82.612  -34.335  1.00 46.39  ? 72  HIS L O   1 
ATOM   12726 C  CB  . HIS L  1 71  ? 24.192 -82.461  -31.500  1.00 45.24  ? 72  HIS L CB  1 
ATOM   12727 C  CG  . HIS L  1 71  ? 23.394 -83.725  -31.427  1.00 43.03  ? 72  HIS L CG  1 
ATOM   12728 N  ND1 . HIS L  1 71  ? 23.604 -84.693  -30.468  1.00 41.94  ? 72  HIS L ND1 1 
ATOM   12729 C  CD2 . HIS L  1 71  ? 22.388 -84.181  -32.207  1.00 42.07  ? 72  HIS L CD2 1 
ATOM   12730 C  CE1 . HIS L  1 71  ? 22.761 -85.692  -30.665  1.00 40.61  ? 72  HIS L CE1 1 
ATOM   12731 N  NE2 . HIS L  1 71  ? 22.013 -85.406  -31.711  1.00 40.39  ? 72  HIS L NE2 1 
ATOM   12732 N  N   . GLY L  1 72  ? 25.525 -84.619  -33.372  1.00 43.34  ? 73  GLY L N   1 
ATOM   12733 C  CA  . GLY L  1 72  ? 25.474 -85.338  -34.638  1.00 42.95  ? 73  GLY L CA  1 
ATOM   12734 C  C   . GLY L  1 72  ? 25.109 -86.796  -34.502  1.00 41.42  ? 73  GLY L C   1 
ATOM   12735 O  O   . GLY L  1 72  ? 24.842 -87.284  -33.415  1.00 40.72  ? 73  GLY L O   1 
ATOM   12736 N  N   . GLY L  1 73  ? 25.082 -87.484  -35.628  1.00 41.56  ? 74  GLY L N   1 
ATOM   12737 C  CA  . GLY L  1 73  ? 24.765 -88.905  -35.655  1.00 40.95  ? 74  GLY L CA  1 
ATOM   12738 C  C   . GLY L  1 73  ? 26.008 -89.660  -35.323  1.00 41.66  ? 74  GLY L C   1 
ATOM   12739 O  O   . GLY L  1 73  ? 27.063 -89.112  -35.440  1.00 43.17  ? 74  GLY L O   1 
ATOM   12740 N  N   . PRO L  1 74  ? 25.897 -90.921  -34.909  1.00 41.51  ? 75  PRO L N   1 
ATOM   12741 C  CA  . PRO L  1 74  ? 27.075 -91.667  -34.463  1.00 42.74  ? 75  PRO L CA  1 
ATOM   12742 C  C   . PRO L  1 74  ? 28.110 -91.869  -35.551  1.00 44.67  ? 75  PRO L C   1 
ATOM   12743 O  O   . PRO L  1 74  ? 29.290 -91.845  -35.278  1.00 46.15  ? 75  PRO L O   1 
ATOM   12744 C  CB  . PRO L  1 74  ? 26.497 -93.017  -34.008  1.00 42.54  ? 75  PRO L CB  1 
ATOM   12745 C  CG  . PRO L  1 74  ? 25.195 -93.125  -34.663  1.00 41.96  ? 75  PRO L CG  1 
ATOM   12746 C  CD  . PRO L  1 74  ? 24.676 -91.730  -34.832  1.00 40.87  ? 75  PRO L CD  1 
ATOM   12747 N  N   . LYS L  1 75  ? 27.652 -92.062  -36.775  1.00 45.21  ? 76  LYS L N   1 
ATOM   12748 C  CA  . LYS L  1 75  ? 28.549 -92.217  -37.912  1.00 47.69  ? 76  LYS L CA  1 
ATOM   12749 C  C   . LYS L  1 75  ? 29.240 -90.918  -38.275  1.00 48.60  ? 76  LYS L C   1 
ATOM   12750 O  O   . LYS L  1 75  ? 30.331 -90.920  -38.811  1.00 51.06  ? 76  LYS L O   1 
ATOM   12751 C  CB  . LYS L  1 75  ? 27.793 -92.690  -39.148  1.00 48.40  ? 76  LYS L CB  1 
ATOM   12752 C  CG  . LYS L  1 75  ? 26.884 -93.882  -38.944  1.00 48.40  ? 76  LYS L CG  1 
ATOM   12753 C  CD  . LYS L  1 75  ? 26.675 -94.603  -40.284  1.00 50.76  ? 76  LYS L CD  1 
ATOM   12754 C  CE  . LYS L  1 75  ? 25.561 -95.658  -40.222  1.00 50.89  ? 76  LYS L CE  1 
ATOM   12755 N  NZ  . LYS L  1 75  ? 25.110 -96.087  -41.611  1.00 52.77  ? 76  LYS L NZ  1 
ATOM   12756 N  N   . ASP L  1 76  ? 28.578 -89.800  -38.018  1.00 47.33  ? 77  ASP L N   1 
ATOM   12757 C  CA  . ASP L  1 76  ? 29.166 -88.480  -38.272  1.00 48.58  ? 77  ASP L CA  1 
ATOM   12758 C  C   . ASP L  1 76  ? 30.488 -88.347  -37.489  1.00 50.16  ? 77  ASP L C   1 
ATOM   12759 O  O   . ASP L  1 76  ? 30.625 -88.835  -36.376  1.00 49.30  ? 77  ASP L O   1 
ATOM   12760 C  CB  . ASP L  1 76  ? 28.182 -87.341  -37.900  1.00 47.02  ? 77  ASP L CB  1 
ATOM   12761 C  CG  . ASP L  1 76  ? 27.021 -87.219  -38.867  1.00 46.54  ? 77  ASP L CG  1 
ATOM   12762 O  OD1 . ASP L  1 76  ? 27.192 -87.567  -40.043  1.00 48.21  ? 77  ASP L OD1 1 
ATOM   12763 O  OD2 . ASP L  1 76  ? 25.935 -86.764  -38.462  1.00 45.29  ? 77  ASP L OD2 1 
ATOM   12764 N  N   . GLU L  1 77  ? 31.474 -87.712  -38.098  1.00 52.98  ? 78  GLU L N   1 
ATOM   12765 C  CA  . GLU L  1 77  ? 32.702 -87.378  -37.389  1.00 55.00  ? 78  GLU L CA  1 
ATOM   12766 C  C   . GLU L  1 77  ? 32.429 -86.245  -36.408  1.00 54.14  ? 78  GLU L C   1 
ATOM   12767 O  O   . GLU L  1 77  ? 32.782 -86.350  -35.250  1.00 54.05  ? 78  GLU L O   1 
ATOM   12768 C  CB  . GLU L  1 77  ? 33.813 -86.953  -38.343  1.00 58.94  ? 78  GLU L CB  1 
ATOM   12769 C  CG  . GLU L  1 77  ? 34.950 -86.177  -37.626  1.00 62.04  ? 78  GLU L CG  1 
ATOM   12770 C  CD  . GLU L  1 77  ? 36.282 -86.079  -38.407  1.00 67.34  ? 78  GLU L CD  1 
ATOM   12771 O  OE1 . GLU L  1 77  ? 36.285 -85.939  -39.666  1.00 69.09  ? 78  GLU L OE1 1 
ATOM   12772 O  OE2 . GLU L  1 77  ? 37.342 -86.128  -37.729  1.00 69.78  ? 78  GLU L OE2 1 
ATOM   12773 N  N   . GLU L  1 78  ? 31.829 -85.157  -36.884  1.00 54.03  ? 79  GLU L N   1 
ATOM   12774 C  CA  . GLU L  1 78  ? 31.409 -84.068  -36.008  1.00 53.51  ? 79  GLU L CA  1 
ATOM   12775 C  C   . GLU L  1 78  ? 30.208 -84.523  -35.193  1.00 50.26  ? 79  GLU L C   1 
ATOM   12776 O  O   . GLU L  1 78  ? 29.068 -84.335  -35.600  1.00 48.95  ? 79  GLU L O   1 
ATOM   12777 C  CB  . GLU L  1 78  ? 31.075 -82.804  -36.806  1.00 55.06  ? 79  GLU L CB  1 
ATOM   12778 C  CG  . GLU L  1 78  ? 30.739 -81.556  -35.934  1.00 55.80  ? 79  GLU L CG  1 
ATOM   12779 C  CD  . GLU L  1 78  ? 31.957 -80.897  -35.269  1.00 59.03  ? 79  GLU L CD  1 
ATOM   12780 O  OE1 . GLU L  1 78  ? 33.079 -81.375  -35.498  1.00 61.23  ? 79  GLU L OE1 1 
ATOM   12781 O  OE2 . GLU L  1 78  ? 31.806 -79.899  -34.523  1.00 59.87  ? 79  GLU L OE2 1 
ATOM   12782 N  N   . ARG L  1 79  ? 30.486 -85.124  -34.044  1.00 49.50  ? 80  ARG L N   1 
ATOM   12783 C  CA  . ARG L  1 79  ? 29.466 -85.583  -33.096  1.00 47.04  ? 80  ARG L CA  1 
ATOM   12784 C  C   . ARG L  1 79  ? 29.907 -85.370  -31.659  1.00 47.64  ? 80  ARG L C   1 
ATOM   12785 O  O   . ARG L  1 79  ? 31.075 -85.143  -31.390  1.00 49.88  ? 80  ARG L O   1 
ATOM   12786 C  CB  . ARG L  1 79  ? 29.201 -87.071  -33.287  1.00 45.56  ? 80  ARG L CB  1 
ATOM   12787 C  CG  . ARG L  1 79  ? 30.431 -87.938  -33.153  1.00 47.03  ? 80  ARG L CG  1 
ATOM   12788 C  CD  . ARG L  1 79  ? 30.111 -89.431  -33.140  1.00 46.15  ? 80  ARG L CD  1 
ATOM   12789 N  NE  . ARG L  1 79  ? 29.807 -89.931  -31.808  1.00 45.06  ? 80  ARG L NE  1 
ATOM   12790 C  CZ  . ARG L  1 79  ? 29.703 -91.215  -31.488  1.00 44.93  ? 80  ARG L CZ  1 
ATOM   12791 N  NH1 . ARG L  1 79  ? 29.879 -92.160  -32.396  1.00 45.73  ? 80  ARG L NH1 1 
ATOM   12792 N  NH2 . ARG L  1 79  ? 29.421 -91.561  -30.242  1.00 44.71  ? 80  ARG L NH2 1 
ATOM   12793 N  N   . HIS L  1 80  ? 28.969 -85.473  -30.729  1.00 46.19  ? 81  HIS L N   1 
ATOM   12794 C  CA  . HIS L  1 80  ? 29.309 -85.579  -29.303  1.00 46.68  ? 81  HIS L CA  1 
ATOM   12795 C  C   . HIS L  1 80  ? 29.808 -86.986  -29.019  1.00 46.25  ? 81  HIS L C   1 
ATOM   12796 O  O   . HIS L  1 80  ? 29.344 -87.939  -29.612  1.00 45.15  ? 81  HIS L O   1 
ATOM   12797 C  CB  . HIS L  1 80  ? 28.095 -85.308  -28.399  1.00 45.60  ? 81  HIS L CB  1 
ATOM   12798 C  CG  . HIS L  1 80  ? 27.504 -83.931  -28.540  1.00 46.32  ? 81  HIS L CG  1 
ATOM   12799 N  ND1 . HIS L  1 80  ? 26.161 -83.673  -28.368  1.00 45.14  ? 81  HIS L ND1 1 
ATOM   12800 C  CD2 . HIS L  1 80  ? 28.081 -82.738  -28.813  1.00 48.55  ? 81  HIS L CD2 1 
ATOM   12801 C  CE1 . HIS L  1 80  ? 25.940 -82.382  -28.531  1.00 46.78  ? 81  HIS L CE1 1 
ATOM   12802 N  NE2 . HIS L  1 80  ? 27.087 -81.792  -28.803  1.00 48.74  ? 81  HIS L NE2 1 
ATOM   12803 N  N   . VAL L  1 81  ? 30.741 -87.131  -28.101  1.00 47.77  ? 82  VAL L N   1 
ATOM   12804 C  CA  . VAL L  1 81  ? 31.218 -88.477  -27.744  1.00 47.94  ? 82  VAL L CA  1 
ATOM   12805 C  C   . VAL L  1 81  ? 30.045 -89.374  -27.360  1.00 45.57  ? 82  VAL L C   1 
ATOM   12806 O  O   . VAL L  1 81  ? 30.008 -90.548  -27.684  1.00 45.07  ? 82  VAL L O   1 
ATOM   12807 C  CB  . VAL L  1 81  ? 32.270 -88.435  -26.588  1.00 50.31  ? 82  VAL L CB  1 
ATOM   12808 C  CG1 . VAL L  1 81  ? 32.635 -89.841  -26.106  1.00 50.38  ? 82  VAL L CG1 1 
ATOM   12809 C  CG2 . VAL L  1 81  ? 33.522 -87.694  -27.040  1.00 53.19  ? 82  VAL L CG2 1 
ATOM   12810 N  N   . GLY L  1 82  ? 29.083 -88.793  -26.674  1.00 44.68  ? 83  GLY L N   1 
ATOM   12811 C  CA  . GLY L  1 82  ? 27.955 -89.553  -26.166  1.00 43.54  ? 83  GLY L CA  1 
ATOM   12812 C  C   . GLY L  1 82  ? 26.800 -89.775  -27.119  1.00 41.88  ? 83  GLY L C   1 
ATOM   12813 O  O   . GLY L  1 82  ? 25.816 -90.417  -26.751  1.00 41.14  ? 83  GLY L O   1 
ATOM   12814 N  N   . ASP L  1 83  ? 26.907 -89.250  -28.337  1.00 41.70  ? 84  ASP L N   1 
ATOM   12815 C  CA  . ASP L  1 83  ? 25.817 -89.353  -29.324  1.00 40.31  ? 84  ASP L CA  1 
ATOM   12816 C  C   . ASP L  1 83  ? 25.757 -90.731  -29.941  1.00 40.09  ? 84  ASP L C   1 
ATOM   12817 O  O   . ASP L  1 83  ? 26.395 -90.975  -30.942  1.00 40.77  ? 84  ASP L O   1 
ATOM   12818 C  CB  . ASP L  1 83  ? 25.994 -88.327  -30.431  1.00 40.47  ? 84  ASP L CB  1 
ATOM   12819 C  CG  . ASP L  1 83  ? 25.679 -86.935  -29.985  1.00 40.81  ? 84  ASP L CG  1 
ATOM   12820 O  OD1 . ASP L  1 83  ? 25.096 -86.735  -28.914  1.00 40.44  ? 84  ASP L OD1 1 
ATOM   12821 O  OD2 . ASP L  1 83  ? 26.011 -85.998  -30.712  1.00 42.01  ? 84  ASP L OD2 1 
ATOM   12822 N  N   . LEU L  1 84  ? 24.983 -91.628  -29.349  1.00 39.79  ? 85  LEU L N   1 
ATOM   12823 C  CA  . LEU L  1 84  ? 24.828 -92.988  -29.877  1.00 40.15  ? 85  LEU L CA  1 
ATOM   12824 C  C   . LEU L  1 84  ? 23.655 -93.129  -30.846  1.00 39.62  ? 85  LEU L C   1 
ATOM   12825 O  O   . LEU L  1 84  ? 23.331 -94.227  -31.276  1.00 40.22  ? 85  LEU L O   1 
ATOM   12826 C  CB  . LEU L  1 84  ? 24.682 -93.984  -28.735  1.00 40.78  ? 85  LEU L CB  1 
ATOM   12827 C  CG  . LEU L  1 84  ? 25.966 -94.284  -27.995  1.00 41.77  ? 85  LEU L CG  1 
ATOM   12828 C  CD1 . LEU L  1 84  ? 25.688 -95.226  -26.863  1.00 42.62  ? 85  LEU L CD1 1 
ATOM   12829 C  CD2 . LEU L  1 84  ? 26.953 -94.865  -28.948  1.00 42.88  ? 85  LEU L CD2 1 
ATOM   12830 N  N   . GLY L  1 85  ? 23.029 -92.014  -31.196  1.00 39.02  ? 86  GLY L N   1 
ATOM   12831 C  CA  . GLY L  1 85  ? 21.994 -91.999  -32.225  1.00 38.87  ? 86  GLY L CA  1 
ATOM   12832 C  C   . GLY L  1 85  ? 20.639 -92.476  -31.743  1.00 38.95  ? 86  GLY L C   1 
ATOM   12833 O  O   . GLY L  1 85  ? 20.164 -92.048  -30.697  1.00 38.91  ? 86  GLY L O   1 
ATOM   12834 N  N   . ASN L  1 86  ? 20.013 -93.364  -32.513  1.00 39.57  ? 87  ASN L N   1 
ATOM   12835 C  CA  . ASN L  1 86  ? 18.642 -93.811  -32.237  1.00 40.09  ? 87  ASN L CA  1 
ATOM   12836 C  C   . ASN L  1 86  ? 18.531 -95.265  -31.893  1.00 41.24  ? 87  ASN L C   1 
ATOM   12837 O  O   . ASN L  1 86  ? 19.384 -96.034  -32.252  1.00 41.85  ? 87  ASN L O   1 
ATOM   12838 C  CB  . ASN L  1 86  ? 17.744 -93.538  -33.434  1.00 40.48  ? 87  ASN L CB  1 
ATOM   12839 C  CG  . ASN L  1 86  ? 17.367 -92.087  -33.538  1.00 39.95  ? 87  ASN L CG  1 
ATOM   12840 O  OD1 . ASN L  1 86  ? 16.898 -91.492  -32.583  1.00 40.20  ? 87  ASN L OD1 1 
ATOM   12841 N  ND2 . ASN L  1 86  ? 17.573 -91.508  -34.695  1.00 40.16  ? 87  ASN L ND2 1 
ATOM   12842 N  N   . VAL L  1 87  ? 17.465 -95.614  -31.185  1.00 42.30  ? 88  VAL L N   1 
ATOM   12843 C  CA  . VAL L  1 87  ? 17.047 -97.005  -30.972  1.00 44.41  ? 88  VAL L CA  1 
ATOM   12844 C  C   . VAL L  1 87  ? 15.605 -97.172  -31.450  1.00 46.02  ? 88  VAL L C   1 
ATOM   12845 O  O   . VAL L  1 87  ? 14.780 -96.277  -31.260  1.00 45.80  ? 88  VAL L O   1 
ATOM   12846 C  CB  . VAL L  1 87  ? 17.097 -97.410  -29.512  1.00 45.03  ? 88  VAL L CB  1 
ATOM   12847 C  CG1 . VAL L  1 87  ? 18.513 -97.431  -29.025  1.00 44.18  ? 88  VAL L CG1 1 
ATOM   12848 C  CG2 . VAL L  1 87  ? 16.258 -96.474  -28.688  1.00 44.94  ? 88  VAL L CG2 1 
ATOM   12849 N  N   . THR L  1 88  ? 15.301 -98.318  -32.057  1.00 48.12  ? 89  THR L N   1 
ATOM   12850 C  CA  . THR L  1 88  ? 13.991 -98.539  -32.694  1.00 50.16  ? 89  THR L CA  1 
ATOM   12851 C  C   . THR L  1 88  ? 13.055 -99.453  -31.893  1.00 53.08  ? 89  THR L C   1 
ATOM   12852 O  O   . THR L  1 88  ? 13.400 -100.583 -31.546  1.00 54.86  ? 89  THR L O   1 
ATOM   12853 C  CB  . THR L  1 88  ? 14.136 -99.113  -34.099  1.00 51.23  ? 89  THR L CB  1 
ATOM   12854 O  OG1 . THR L  1 88  ? 14.703 -98.124  -34.968  1.00 49.18  ? 89  THR L OG1 1 
ATOM   12855 C  CG2 . THR L  1 88  ? 12.784 -99.528  -34.629  1.00 54.13  ? 89  THR L CG2 1 
ATOM   12856 N  N   . ALA L  1 89  ? 11.858 -98.951  -31.625  1.00 54.11  ? 90  ALA L N   1 
ATOM   12857 C  CA  . ALA L  1 89  ? 10.876 -99.659  -30.813  1.00 57.31  ? 90  ALA L CA  1 
ATOM   12858 C  C   . ALA L  1 89  ? 9.784  -100.289 -31.695  1.00 60.72  ? 90  ALA L C   1 
ATOM   12859 O  O   . ALA L  1 89  ? 9.207  -99.616  -32.571  1.00 60.73  ? 90  ALA L O   1 
ATOM   12860 C  CB  . ALA L  1 89  ? 10.259 -98.696  -29.796  1.00 57.12  ? 90  ALA L CB  1 
ATOM   12861 N  N   . ASP L  1 90  ? 9.491  -101.568 -31.447  1.00 64.00  ? 91  ASP L N   1 
ATOM   12862 C  CA  . ASP L  1 90  ? 8.445  -102.295 -32.196  1.00 67.98  ? 91  ASP L CA  1 
ATOM   12863 C  C   . ASP L  1 90  ? 7.046  -102.225 -31.545  1.00 71.32  ? 91  ASP L C   1 
ATOM   12864 O  O   . ASP L  1 90  ? 6.905  -101.931 -30.348  1.00 71.26  ? 91  ASP L O   1 
ATOM   12865 C  CB  . ASP L  1 90  ? 8.871  -103.756 -32.452  1.00 70.68  ? 91  ASP L CB  1 
ATOM   12866 C  CG  . ASP L  1 90  ? 8.856  -104.635 -31.186  1.00 73.16  ? 91  ASP L CG  1 
ATOM   12867 O  OD1 . ASP L  1 90  ? 9.147  -105.837 -31.319  1.00 76.24  ? 91  ASP L OD1 1 
ATOM   12868 O  OD2 . ASP L  1 90  ? 8.571  -104.161 -30.066  1.00 72.63  ? 91  ASP L OD2 1 
ATOM   12869 N  N   . LYS L  1 91  ? 6.030  -102.506 -32.359  1.00 74.64  ? 92  LYS L N   1 
ATOM   12870 C  CA  . LYS L  1 91  ? 4.602  -102.499 -31.949  1.00 78.81  ? 92  LYS L CA  1 
ATOM   12871 C  C   . LYS L  1 91  ? 4.362  -102.538 -30.445  1.00 79.88  ? 92  LYS L C   1 
ATOM   12872 O  O   . LYS L  1 91  ? 3.828  -101.594 -29.869  1.00 79.55  ? 92  LYS L O   1 
ATOM   12873 C  CB  . LYS L  1 91  ? 3.828  -103.699 -32.545  1.00 84.39  ? 92  LYS L CB  1 
ATOM   12874 C  CG  . LYS L  1 91  ? 4.369  -104.336 -33.841  1.00 84.88  ? 92  LYS L CG  1 
ATOM   12875 C  CD  . LYS L  1 91  ? 4.181  -103.423 -35.066  1.00 83.49  ? 92  LYS L CD  1 
ATOM   12876 C  CE  . LYS L  1 91  ? 4.236  -104.218 -36.405  1.00 85.91  ? 92  LYS L CE  1 
ATOM   12877 N  NZ  . LYS L  1 91  ? 2.917  -104.780 -36.859  1.00 91.85  ? 92  LYS L NZ  1 
ATOM   12878 N  N   . ASP L  1 92  ? 4.760  -103.649 -29.827  1.00 81.67  ? 93  ASP L N   1 
ATOM   12879 C  CA  . ASP L  1 92  ? 4.444  -103.925 -28.408  1.00 84.21  ? 93  ASP L CA  1 
ATOM   12880 C  C   . ASP L  1 92  ? 5.392  -103.177 -27.456  1.00 79.97  ? 93  ASP L C   1 
ATOM   12881 O  O   . ASP L  1 92  ? 5.503  -103.535 -26.274  1.00 81.67  ? 93  ASP L O   1 
ATOM   12882 C  CB  . ASP L  1 92  ? 4.370  -105.454 -28.077  1.00 88.86  ? 93  ASP L CB  1 
ATOM   12883 C  CG  . ASP L  1 92  ? 4.733  -106.349 -29.269  1.00 90.20  ? 93  ASP L CG  1 
ATOM   12884 O  OD1 . ASP L  1 92  ? 5.917  -106.382 -29.654  1.00 86.92  ? 93  ASP L OD1 1 
ATOM   12885 O  OD2 . ASP L  1 92  ? 3.833  -107.013 -29.831  1.00 94.93  ? 93  ASP L OD2 1 
ATOM   12886 N  N   . GLY L  1 93  ? 6.062  -102.144 -27.969  1.00 75.00  ? 94  GLY L N   1 
ATOM   12887 C  CA  . GLY L  1 93  ? 6.799  -101.203 -27.137  1.00 71.37  ? 94  GLY L CA  1 
ATOM   12888 C  C   . GLY L  1 93  ? 8.207  -101.620 -26.786  1.00 68.80  ? 94  GLY L C   1 
ATOM   12889 O  O   . GLY L  1 93  ? 8.875  -100.944 -26.021  1.00 66.27  ? 94  GLY L O   1 
ATOM   12890 N  N   . VAL L  1 94  ? 8.643  -102.749 -27.327  1.00 70.04  ? 95  VAL L N   1 
ATOM   12891 C  CA  . VAL L  1 94  ? 9.958  -103.320 -27.035  1.00 68.65  ? 95  VAL L CA  1 
ATOM   12892 C  C   . VAL L  1 94  ? 11.007 -102.782 -28.025  1.00 64.79  ? 95  VAL L C   1 
ATOM   12893 O  O   . VAL L  1 94  ? 10.730 -102.653 -29.222  1.00 64.96  ? 95  VAL L O   1 
ATOM   12894 C  CB  . VAL L  1 94  ? 9.886  -104.867 -27.100  1.00 72.81  ? 95  VAL L CB  1 
ATOM   12895 C  CG1 . VAL L  1 94  ? 11.207 -105.465 -27.601  1.00 71.72  ? 95  VAL L CG1 1 
ATOM   12896 C  CG2 . VAL L  1 94  ? 9.461  -105.433 -25.734  1.00 75.84  ? 95  VAL L CG2 1 
ATOM   12897 N  N   . ALA L  1 95  ? 12.196 -102.444 -27.531  1.00 61.80  ? 96  ALA L N   1 
ATOM   12898 C  CA  . ALA L  1 95  ? 13.284 -101.982 -28.393  1.00 58.48  ? 96  ALA L CA  1 
ATOM   12899 C  C   . ALA L  1 95  ? 14.467 -102.885 -28.124  1.00 58.97  ? 96  ALA L C   1 
ATOM   12900 O  O   . ALA L  1 95  ? 15.049 -102.831 -27.035  1.00 58.57  ? 96  ALA L O   1 
ATOM   12901 C  CB  . ALA L  1 95  ? 13.629 -100.537 -28.104  1.00 54.89  ? 96  ALA L CB  1 
ATOM   12902 N  N   . ASP L  1 96  ? 14.795 -103.743 -29.089  1.00 60.32  ? 97  ASP L N   1 
ATOM   12903 C  CA  . ASP L  1 96  ? 15.915 -104.673 -28.920  1.00 61.59  ? 97  ASP L CA  1 
ATOM   12904 C  C   . ASP L  1 96  ? 17.222 -104.047 -29.358  1.00 58.52  ? 97  ASP L C   1 
ATOM   12905 O  O   . ASP L  1 96  ? 17.603 -104.159 -30.505  1.00 58.79  ? 97  ASP L O   1 
ATOM   12906 C  CB  . ASP L  1 96  ? 15.645 -105.975 -29.660  1.00 65.64  ? 97  ASP L CB  1 
ATOM   12907 C  CG  . ASP L  1 96  ? 14.727 -106.903 -28.865  1.00 70.40  ? 97  ASP L CG  1 
ATOM   12908 O  OD1 . ASP L  1 96  ? 15.030 -107.148 -27.661  1.00 71.18  ? 97  ASP L OD1 1 
ATOM   12909 O  OD2 . ASP L  1 96  ? 13.699 -107.375 -29.433  1.00 73.64  ? 97  ASP L OD2 1 
ATOM   12910 N  N   . VAL L  1 97  ? 17.911 -103.402 -28.424  1.00 56.32  ? 98  VAL L N   1 
ATOM   12911 C  CA  . VAL L  1 97  ? 19.090 -102.608 -28.745  1.00 53.57  ? 98  VAL L CA  1 
ATOM   12912 C  C   . VAL L  1 97  ? 20.278 -103.461 -29.130  1.00 55.18  ? 98  VAL L C   1 
ATOM   12913 O  O   . VAL L  1 97  ? 20.606 -104.410 -28.424  1.00 57.68  ? 98  VAL L O   1 
ATOM   12914 C  CB  . VAL L  1 97  ? 19.530 -101.763 -27.558  1.00 51.75  ? 98  VAL L CB  1 
ATOM   12915 C  CG1 . VAL L  1 97  ? 20.742 -100.939 -27.938  1.00 49.60  ? 98  VAL L CG1 1 
ATOM   12916 C  CG2 . VAL L  1 97  ? 18.403 -100.861 -27.092  1.00 50.92  ? 98  VAL L CG2 1 
ATOM   12917 N  N   . SER L  1 98  ? 20.920 -103.113 -30.247  1.00 54.21  ? 99  SER L N   1 
ATOM   12918 C  CA  . SER L  1 98  ? 22.198 -103.723 -30.643  1.00 55.89  ? 99  SER L CA  1 
ATOM   12919 C  C   . SER L  1 98  ? 23.038 -102.758 -31.465  1.00 53.87  ? 99  SER L C   1 
ATOM   12920 O  O   . SER L  1 98  ? 22.961 -102.730 -32.687  1.00 54.28  ? 99  SER L O   1 
ATOM   12921 C  CB  . SER L  1 98  ? 22.003 -105.015 -31.430  1.00 59.66  ? 99  SER L CB  1 
ATOM   12922 O  OG  . SER L  1 98  ? 23.256 -105.516 -31.898  1.00 61.21  ? 99  SER L OG  1 
ATOM   12923 N  N   . ILE L  1 99  ? 23.842 -101.971 -30.769  1.00 52.12  ? 100 ILE L N   1 
ATOM   12924 C  CA  . ILE L  1 99  ? 24.709 -100.984 -31.382  1.00 50.46  ? 100 ILE L CA  1 
ATOM   12925 C  C   . ILE L  1 99  ? 26.139 -101.427 -31.197  1.00 52.43  ? 100 ILE L C   1 
ATOM   12926 O  O   . ILE L  1 99  ? 26.436 -102.197 -30.303  1.00 54.39  ? 100 ILE L O   1 
ATOM   12927 C  CB  . ILE L  1 99  ? 24.526 -99.612  -30.717  1.00 47.48  ? 100 ILE L CB  1 
ATOM   12928 C  CG1 . ILE L  1 99  ? 23.140 -99.062  -31.010  1.00 46.02  ? 100 ILE L CG1 1 
ATOM   12929 C  CG2 . ILE L  1 99  ? 25.525 -98.633  -31.210  1.00 46.69  ? 100 ILE L CG2 1 
ATOM   12930 C  CD1 . ILE L  1 99  ? 23.021 -97.571  -30.825  1.00 43.51  ? 100 ILE L CD1 1 
ATOM   12931 N  N   . GLU L  1 100 ? 27.018 -100.960 -32.075  1.00 52.73  ? 101 GLU L N   1 
ATOM   12932 C  CA  . GLU L  1 100 ? 28.473 -101.098 -31.912  1.00 54.53  ? 101 GLU L CA  1 
ATOM   12933 C  C   . GLU L  1 100 ? 29.113 -99.751  -32.244  1.00 52.78  ? 101 GLU L C   1 
ATOM   12934 O  O   . GLU L  1 100 ? 28.881 -99.198  -33.317  1.00 52.09  ? 101 GLU L O   1 
ATOM   12935 C  CB  . GLU L  1 100 ? 29.030 -102.208 -32.824  1.00 58.28  ? 101 GLU L CB  1 
ATOM   12936 C  CG  . GLU L  1 100 ? 30.522 -102.504 -32.605  1.00 61.71  ? 101 GLU L CG  1 
ATOM   12937 C  CD  . GLU L  1 100 ? 31.027 -103.766 -33.323  1.00 66.65  ? 101 GLU L CD  1 
ATOM   12938 O  OE1 . GLU L  1 100 ? 32.212 -104.143 -33.105  1.00 69.53  ? 101 GLU L OE1 1 
ATOM   12939 O  OE2 . GLU L  1 100 ? 30.248 -104.376 -34.094  1.00 67.60  ? 101 GLU L OE2 1 
ATOM   12940 N  N   . ASP L  1 101 ? 29.901 -99.219  -31.322  1.00 52.52  ? 102 ASP L N   1 
ATOM   12941 C  CA  . ASP L  1 101 ? 30.426 -97.870  -31.481  1.00 51.35  ? 102 ASP L CA  1 
ATOM   12942 C  C   . ASP L  1 101 ? 31.896 -97.772  -31.151  1.00 53.78  ? 102 ASP L C   1 
ATOM   12943 O  O   . ASP L  1 101 ? 32.398 -98.507  -30.319  1.00 55.60  ? 102 ASP L O   1 
ATOM   12944 C  CB  . ASP L  1 101 ? 29.650 -96.892  -30.611  1.00 48.58  ? 102 ASP L CB  1 
ATOM   12945 C  CG  . ASP L  1 101 ? 29.889 -95.449  -31.003  1.00 47.27  ? 102 ASP L CG  1 
ATOM   12946 O  OD1 . ASP L  1 101 ? 29.563 -95.074  -32.135  1.00 46.62  ? 102 ASP L OD1 1 
ATOM   12947 O  OD2 . ASP L  1 101 ? 30.403 -94.680  -30.187  1.00 47.24  ? 102 ASP L OD2 1 
ATOM   12948 N  N   . SER L  1 102 ? 32.570 -96.827  -31.796  1.00 54.21  ? 103 SER L N   1 
ATOM   12949 C  CA  . SER L  1 102 ? 34.017 -96.654  -31.668  1.00 57.05  ? 103 SER L CA  1 
ATOM   12950 C  C   . SER L  1 102 ? 34.468 -95.360  -31.009  1.00 56.32  ? 103 SER L C   1 
ATOM   12951 O  O   . SER L  1 102 ? 35.627 -95.244  -30.660  1.00 59.02  ? 103 SER L O   1 
ATOM   12952 C  CB  . SER L  1 102 ? 34.635 -96.725  -33.048  1.00 59.46  ? 103 SER L CB  1 
ATOM   12953 O  OG  . SER L  1 102 ? 34.194 -97.898  -33.694  1.00 60.69  ? 103 SER L OG  1 
ATOM   12954 N  N   . VAL L  1 103 ? 33.572 -94.394  -30.851  1.00 53.33  ? 104 VAL L N   1 
ATOM   12955 C  CA  . VAL L  1 103 ? 33.911 -93.135  -30.188  1.00 53.19  ? 104 VAL L CA  1 
ATOM   12956 C  C   . VAL L  1 103 ? 33.838 -93.261  -28.671  1.00 53.02  ? 104 VAL L C   1 
ATOM   12957 O  O   . VAL L  1 103 ? 34.725 -92.802  -27.975  1.00 55.08  ? 104 VAL L O   1 
ATOM   12958 C  CB  . VAL L  1 103 ? 32.994 -91.987  -30.600  1.00 50.80  ? 104 VAL L CB  1 
ATOM   12959 C  CG1 . VAL L  1 103 ? 33.429 -90.709  -29.925  1.00 51.31  ? 104 VAL L CG1 1 
ATOM   12960 C  CG2 . VAL L  1 103 ? 33.025 -91.797  -32.076  1.00 51.63  ? 104 VAL L CG2 1 
ATOM   12961 N  N   . ILE L  1 104 ? 32.774 -93.857  -28.152  1.00 51.09  ? 105 ILE L N   1 
ATOM   12962 C  CA  . ILE L  1 104 ? 32.659 -94.070  -26.708  1.00 51.17  ? 105 ILE L CA  1 
ATOM   12963 C  C   . ILE L  1 104 ? 33.684 -95.088  -26.242  1.00 54.16  ? 105 ILE L C   1 
ATOM   12964 O  O   . ILE L  1 104 ? 34.197 -95.868  -27.034  1.00 55.76  ? 105 ILE L O   1 
ATOM   12965 C  CB  . ILE L  1 104 ? 31.253 -94.566  -26.267  1.00 49.12  ? 105 ILE L CB  1 
ATOM   12966 C  CG1 . ILE L  1 104 ? 30.930 -95.953  -26.861  1.00 49.67  ? 105 ILE L CG1 1 
ATOM   12967 C  CG2 . ILE L  1 104 ? 30.197 -93.541  -26.621  1.00 46.52  ? 105 ILE L CG2 1 
ATOM   12968 C  CD1 . ILE L  1 104 ? 29.802 -96.701  -26.148  1.00 48.52  ? 105 ILE L CD1 1 
ATOM   12969 N  N   . SER L  1 105 ? 33.972 -95.085  -24.949  1.00 55.34  ? 106 SER L N   1 
ATOM   12970 C  CA  . SER L  1 105 ? 34.885 -96.068  -24.375  1.00 58.51  ? 106 SER L CA  1 
ATOM   12971 C  C   . SER L  1 105 ? 34.618 -96.329  -22.900  1.00 59.01  ? 106 SER L C   1 
ATOM   12972 O  O   . SER L  1 105 ? 34.066 -95.489  -22.191  1.00 57.65  ? 106 SER L O   1 
ATOM   12973 C  CB  . SER L  1 105 ? 36.339 -95.626  -24.555  1.00 61.57  ? 106 SER L CB  1 
ATOM   12974 O  OG  . SER L  1 105 ? 37.214 -96.689  -24.232  1.00 64.84  ? 106 SER L OG  1 
ATOM   12975 N  N   . LEU L  1 106 ? 35.038 -97.505  -22.448  1.00 61.47  ? 107 LEU L N   1 
ATOM   12976 C  CA  . LEU L  1 106 ? 34.961 -97.884  -21.031  1.00 62.81  ? 107 LEU L CA  1 
ATOM   12977 C  C   . LEU L  1 106 ? 36.271 -97.589  -20.270  1.00 66.23  ? 107 LEU L C   1 
ATOM   12978 O  O   . LEU L  1 106 ? 36.491 -98.098  -19.163  1.00 68.44  ? 107 LEU L O   1 
ATOM   12979 C  CB  . LEU L  1 106 ? 34.604 -99.367  -20.913  1.00 64.07  ? 107 LEU L CB  1 
ATOM   12980 C  CG  . LEU L  1 106 ? 33.286 -99.763  -21.567  1.00 61.29  ? 107 LEU L CG  1 
ATOM   12981 C  CD1 . LEU L  1 106 ? 33.028 -101.244 -21.352  1.00 63.67  ? 107 LEU L CD1 1 
ATOM   12982 C  CD2 . LEU L  1 106 ? 32.132 -98.926  -21.031  1.00 58.17  ? 107 LEU L CD2 1 
ATOM   12983 N  N   . SER L  1 107 ? 37.134 -96.766  -20.872  1.00 67.05  ? 108 SER L N   1 
ATOM   12984 C  CA  . SER L  1 107 ? 38.435 -96.400  -20.284  1.00 70.57  ? 108 SER L CA  1 
ATOM   12985 C  C   . SER L  1 107 ? 39.037 -95.121  -20.896  1.00 70.69  ? 108 SER L C   1 
ATOM   12986 O  O   . SER L  1 107 ? 38.981 -94.889  -22.089  1.00 69.46  ? 108 SER L O   1 
ATOM   12987 C  CB  . SER L  1 107 ? 39.442 -97.562  -20.395  1.00 74.55  ? 108 SER L CB  1 
ATOM   12988 O  OG  . SER L  1 107 ? 39.635 -97.994  -21.731  1.00 74.55  ? 108 SER L OG  1 
ATOM   12989 N  N   . GLY L  1 108 ? 39.601 -94.283  -20.048  1.00 72.69  ? 109 GLY L N   1 
ATOM   12990 C  CA  . GLY L  1 108 ? 40.345 -93.121  -20.509  1.00 74.26  ? 109 GLY L CA  1 
ATOM   12991 C  C   . GLY L  1 108 ? 39.553 -91.838  -20.676  1.00 71.51  ? 109 GLY L C   1 
ATOM   12992 O  O   . GLY L  1 108 ? 38.548 -91.621  -20.019  1.00 69.17  ? 109 GLY L O   1 
ATOM   12993 N  N   . ASP L  1 109 ? 40.049 -90.973  -21.552  1.00 72.47  ? 110 ASP L N   1 
ATOM   12994 C  CA  . ASP L  1 109 ? 39.470 -89.644  -21.787  1.00 70.95  ? 110 ASP L CA  1 
ATOM   12995 C  C   . ASP L  1 109 ? 37.971 -89.704  -22.108  1.00 66.17  ? 110 ASP L C   1 
ATOM   12996 O  O   . ASP L  1 109 ? 37.168 -88.889  -21.623  1.00 64.49  ? 110 ASP L O   1 
ATOM   12997 C  CB  . ASP L  1 109 ? 40.193 -88.975  -22.965  1.00 72.85  ? 110 ASP L CB  1 
ATOM   12998 C  CG  . ASP L  1 109 ? 40.164 -87.448  -22.885  1.00 74.26  ? 110 ASP L CG  1 
ATOM   12999 O  OD1 . ASP L  1 109 ? 39.213 -86.824  -23.433  1.00 71.40  ? 110 ASP L OD1 1 
ATOM   13000 O  OD2 . ASP L  1 109 ? 41.098 -86.879  -22.265  1.00 78.56  ? 110 ASP L OD2 1 
ATOM   13001 N  N   . HIS L  1 110 ? 37.625 -90.681  -22.942  1.00 64.34  ? 111 HIS L N   1 
ATOM   13002 C  CA  . HIS L  1 110 ? 36.251 -90.909  -23.418  1.00 60.43  ? 111 HIS L CA  1 
ATOM   13003 C  C   . HIS L  1 110 ? 35.420 -91.821  -22.484  1.00 59.02  ? 111 HIS L C   1 
ATOM   13004 O  O   . HIS L  1 110 ? 34.319 -92.250  -22.838  1.00 56.24  ? 111 HIS L O   1 
ATOM   13005 C  CB  . HIS L  1 110 ? 36.318 -91.557  -24.806  1.00 59.91  ? 111 HIS L CB  1 
ATOM   13006 C  CG  . HIS L  1 110 ? 36.864 -90.657  -25.883  1.00 61.12  ? 111 HIS L CG  1 
ATOM   13007 N  ND1 . HIS L  1 110 ? 36.763 -90.968  -27.224  1.00 60.51  ? 111 HIS L ND1 1 
ATOM   13008 C  CD2 . HIS L  1 110 ? 37.490 -89.454  -25.825  1.00 63.04  ? 111 HIS L CD2 1 
ATOM   13009 C  CE1 . HIS L  1 110 ? 37.313 -90.006  -27.944  1.00 61.89  ? 111 HIS L CE1 1 
ATOM   13010 N  NE2 . HIS L  1 110 ? 37.762 -89.074  -27.120  1.00 63.66  ? 111 HIS L NE2 1 
ATOM   13011 N  N   . CYS L  1 111 ? 35.951 -92.106  -21.295  1.00 61.27  ? 112 CYS L N   1 
ATOM   13012 C  CA  . CYS L  1 111 ? 35.329 -93.061  -20.367  1.00 60.78  ? 112 CYS L CA  1 
ATOM   13013 C  C   . CYS L  1 111 ? 33.906 -92.635  -20.018  1.00 57.89  ? 112 CYS L C   1 
ATOM   13014 O  O   . CYS L  1 111 ? 33.689 -91.561  -19.445  1.00 57.91  ? 112 CYS L O   1 
ATOM   13015 C  CB  . CYS L  1 111 ? 36.158 -93.204  -19.081  1.00 64.24  ? 112 CYS L CB  1 
ATOM   13016 S  SG  . CYS L  1 111 ? 35.685 -94.605  -17.994  1.00 64.90  ? 112 CYS L SG  1 
ATOM   13017 N  N   . ILE L  1 112 ? 32.952 -93.486  -20.380  1.00 55.88  ? 113 ILE L N   1 
ATOM   13018 C  CA  . ILE L  1 112 ? 31.526 -93.245  -20.094  1.00 53.73  ? 113 ILE L CA  1 
ATOM   13019 C  C   . ILE L  1 112 ? 31.074 -93.818  -18.741  1.00 54.86  ? 113 ILE L C   1 
ATOM   13020 O  O   . ILE L  1 112 ? 29.974 -93.521  -18.270  1.00 53.82  ? 113 ILE L O   1 
ATOM   13021 C  CB  . ILE L  1 112 ? 30.594 -93.807  -21.211  1.00 51.33  ? 113 ILE L CB  1 
ATOM   13022 C  CG1 . ILE L  1 112 ? 30.750 -95.321  -21.368  1.00 52.20  ? 113 ILE L CG1 1 
ATOM   13023 C  CG2 . ILE L  1 112 ? 30.881 -93.111  -22.530  1.00 50.28  ? 113 ILE L CG2 1 
ATOM   13024 C  CD1 . ILE L  1 112 ? 29.534 -95.962  -21.957  1.00 50.55  ? 113 ILE L CD1 1 
ATOM   13025 N  N   . ILE L  1 113 ? 31.922 -94.640  -18.131  1.00 57.31  ? 114 ILE L N   1 
ATOM   13026 C  CA  . ILE L  1 113 ? 31.587 -95.273  -16.860  1.00 58.89  ? 114 ILE L CA  1 
ATOM   13027 C  C   . ILE L  1 113 ? 31.431 -94.227  -15.772  1.00 59.76  ? 114 ILE L C   1 
ATOM   13028 O  O   . ILE L  1 113 ? 32.276 -93.352  -15.616  1.00 60.97  ? 114 ILE L O   1 
ATOM   13029 C  CB  . ILE L  1 113 ? 32.659 -96.275  -16.421  1.00 62.04  ? 114 ILE L CB  1 
ATOM   13030 C  CG1 . ILE L  1 113 ? 32.577 -97.531  -17.268  1.00 61.96  ? 114 ILE L CG1 1 
ATOM   13031 C  CG2 . ILE L  1 113 ? 32.488 -96.661  -14.970  1.00 64.36  ? 114 ILE L CG2 1 
ATOM   13032 C  CD1 . ILE L  1 113 ? 33.726 -98.497  -17.007  1.00 65.83  ? 114 ILE L CD1 1 
ATOM   13033 N  N   . GLY L  1 114 ? 30.352 -94.343  -15.010  1.00 59.64  ? 115 GLY L N   1 
ATOM   13034 C  CA  . GLY L  1 114 ? 30.025 -93.369  -13.972  1.00 60.85  ? 115 GLY L CA  1 
ATOM   13035 C  C   . GLY L  1 114 ? 29.171 -92.229  -14.504  1.00 58.73  ? 115 GLY L C   1 
ATOM   13036 O  O   . GLY L  1 114 ? 28.849 -91.288  -13.780  1.00 59.79  ? 115 GLY L O   1 
ATOM   13037 N  N   . ARG L  1 115 ? 28.812 -92.307  -15.780  1.00 56.09  ? 116 ARG L N   1 
ATOM   13038 C  CA  . ARG L  1 115 ? 27.948 -91.308  -16.395  1.00 54.35  ? 116 ARG L CA  1 
ATOM   13039 C  C   . ARG L  1 115 ? 26.591 -91.931  -16.699  1.00 52.84  ? 116 ARG L C   1 
ATOM   13040 O  O   . ARG L  1 115 ? 26.407 -93.139  -16.536  1.00 53.13  ? 116 ARG L O   1 
ATOM   13041 C  CB  . ARG L  1 115 ? 28.594 -90.743  -17.658  1.00 52.92  ? 116 ARG L CB  1 
ATOM   13042 C  CG  . ARG L  1 115 ? 29.975 -90.173  -17.405  1.00 55.11  ? 116 ARG L CG  1 
ATOM   13043 C  CD  . ARG L  1 115 ? 30.572 -89.508  -18.637  1.00 54.47  ? 116 ARG L CD  1 
ATOM   13044 N  NE  . ARG L  1 115 ? 31.978 -89.139  -18.430  1.00 56.90  ? 116 ARG L NE  1 
ATOM   13045 C  CZ  . ARG L  1 115 ? 32.401 -88.024  -17.832  1.00 59.01  ? 116 ARG L CZ  1 
ATOM   13046 N  NH1 . ARG L  1 115 ? 31.548 -87.119  -17.365  1.00 59.05  ? 116 ARG L NH1 1 
ATOM   13047 N  NH2 . ARG L  1 115 ? 33.700 -87.811  -17.709  1.00 61.99  ? 116 ARG L NH2 1 
ATOM   13048 N  N   . THR L  1 116 ? 25.647 -91.095  -17.132  1.00 51.67  ? 117 THR L N   1 
ATOM   13049 C  CA  . THR L  1 116 ? 24.244 -91.510  -17.338  1.00 50.75  ? 117 THR L CA  1 
ATOM   13050 C  C   . THR L  1 116 ? 23.900 -91.838  -18.795  1.00 48.36  ? 117 THR L C   1 
ATOM   13051 O  O   . THR L  1 116 ? 24.226 -91.089  -19.714  1.00 47.26  ? 117 THR L O   1 
ATOM   13052 C  CB  . THR L  1 116 ? 23.260 -90.428  -16.869  1.00 51.49  ? 117 THR L CB  1 
ATOM   13053 O  OG1 . THR L  1 116 ? 23.369 -90.254  -15.457  1.00 54.08  ? 117 THR L OG1 1 
ATOM   13054 C  CG2 . THR L  1 116 ? 21.866 -90.836  -17.181  1.00 50.90  ? 117 THR L CG2 1 
ATOM   13055 N  N   . LEU L  1 117 ? 23.259 -92.979  -18.991  1.00 48.18  ? 118 LEU L N   1 
ATOM   13056 C  CA  . LEU L  1 117 ? 22.649 -93.331  -20.272  1.00 46.39  ? 118 LEU L CA  1 
ATOM   13057 C  C   . LEU L  1 117 ? 21.218 -92.834  -20.231  1.00 46.38  ? 118 LEU L C   1 
ATOM   13058 O  O   . LEU L  1 117 ? 20.627 -92.802  -19.181  1.00 48.30  ? 118 LEU L O   1 
ATOM   13059 C  CB  . LEU L  1 117 ? 22.675 -94.850  -20.483  1.00 46.91  ? 118 LEU L CB  1 
ATOM   13060 C  CG  . LEU L  1 117 ? 22.143 -95.357  -21.820  1.00 45.51  ? 118 LEU L CG  1 
ATOM   13061 C  CD1 . LEU L  1 117 ? 22.961 -94.774  -22.924  1.00 44.10  ? 118 LEU L CD1 1 
ATOM   13062 C  CD2 . LEU L  1 117 ? 22.168 -96.860  -21.891  1.00 46.79  ? 118 LEU L CD2 1 
ATOM   13063 N  N   . VAL L  1 118 ? 20.660 -92.453  -21.367  1.00 44.84  ? 119 VAL L N   1 
ATOM   13064 C  CA  . VAL L  1 118 ? 19.331 -91.835  -21.401  1.00 45.24  ? 119 VAL L CA  1 
ATOM   13065 C  C   . VAL L  1 118 ? 18.558 -92.148  -22.677  1.00 44.35  ? 119 VAL L C   1 
ATOM   13066 O  O   . VAL L  1 118 ? 19.022 -91.851  -23.754  1.00 43.15  ? 119 VAL L O   1 
ATOM   13067 C  CB  . VAL L  1 118 ? 19.442 -90.318  -21.312  1.00 45.24  ? 119 VAL L CB  1 
ATOM   13068 C  CG1 . VAL L  1 118 ? 18.132 -89.669  -21.638  1.00 45.86  ? 119 VAL L CG1 1 
ATOM   13069 C  CG2 . VAL L  1 118 ? 19.891 -89.913  -19.951  1.00 47.14  ? 119 VAL L CG2 1 
ATOM   13070 N  N   . VAL L  1 119 ? 17.375 -92.736  -22.562  1.00 45.56  ? 120 VAL L N   1 
ATOM   13071 C  CA  . VAL L  1 119 ? 16.520 -92.991  -23.724  1.00 45.15  ? 120 VAL L CA  1 
ATOM   13072 C  C   . VAL L  1 119 ? 15.495 -91.881  -23.786  1.00 45.95  ? 120 VAL L C   1 
ATOM   13073 O  O   . VAL L  1 119 ? 15.072 -91.378  -22.759  1.00 47.64  ? 120 VAL L O   1 
ATOM   13074 C  CB  . VAL L  1 119 ? 15.836 -94.363  -23.644  1.00 46.73  ? 120 VAL L CB  1 
ATOM   13075 C  CG1 . VAL L  1 119 ? 14.713 -94.347  -22.627  1.00 49.61  ? 120 VAL L CG1 1 
ATOM   13076 C  CG2 . VAL L  1 119 ? 15.302 -94.775  -24.982  1.00 46.40  ? 120 VAL L CG2 1 
ATOM   13077 N  N   . HIS L  1 120 ? 15.092 -91.505  -24.991  1.00 45.24  ? 121 HIS L N   1 
ATOM   13078 C  CA  . HIS L  1 120 ? 14.389 -90.238  -25.210  1.00 45.98  ? 121 HIS L CA  1 
ATOM   13079 C  C   . HIS L  1 120 ? 12.987 -90.343  -25.782  1.00 47.63  ? 121 HIS L C   1 
ATOM   13080 O  O   . HIS L  1 120 ? 12.619 -91.353  -26.385  1.00 47.63  ? 121 HIS L O   1 
ATOM   13081 C  CB  . HIS L  1 120 ? 15.205 -89.348  -26.135  1.00 44.26  ? 121 HIS L CB  1 
ATOM   13082 C  CG  . HIS L  1 120 ? 16.200 -88.509  -25.421  1.00 43.78  ? 121 HIS L CG  1 
ATOM   13083 N  ND1 . HIS L  1 120 ? 16.061 -87.149  -25.288  1.00 45.07  ? 121 HIS L ND1 1 
ATOM   13084 C  CD2 . HIS L  1 120 ? 17.335 -88.840  -24.771  1.00 43.16  ? 121 HIS L CD2 1 
ATOM   13085 C  CE1 . HIS L  1 120 ? 17.077 -86.674  -24.591  1.00 45.06  ? 121 HIS L CE1 1 
ATOM   13086 N  NE2 . HIS L  1 120 ? 17.861 -87.682  -24.260  1.00 43.90  ? 121 HIS L NE2 1 
ATOM   13087 N  N   . GLU L  1 121 ? 12.239 -89.245  -25.608  1.00 49.34  ? 122 GLU L N   1 
ATOM   13088 C  CA  . GLU L  1 121 ? 10.822 -89.133  -26.008  1.00 51.65  ? 122 GLU L CA  1 
ATOM   13089 C  C   . GLU L  1 121 ? 10.658 -89.341  -27.504  1.00 50.53  ? 122 GLU L C   1 
ATOM   13090 O  O   . GLU L  1 121 ? 10.040 -90.293  -27.939  1.00 51.24  ? 122 GLU L O   1 
ATOM   13091 C  CB  . GLU L  1 121 ? 10.256 -87.759  -25.592  1.00 53.82  ? 122 GLU L CB  1 
ATOM   13092 C  CG  . GLU L  1 121 ? 8.808  -87.486  -26.046  1.00 56.91  ? 122 GLU L CG  1 
ATOM   13093 C  CD  . GLU L  1 121 ? 8.350  -86.043  -25.827  1.00 59.55  ? 122 GLU L CD  1 
ATOM   13094 O  OE1 . GLU L  1 121 ? 9.163  -85.180  -25.441  1.00 58.93  ? 122 GLU L OE1 1 
ATOM   13095 O  OE2 . GLU L  1 121 ? 7.162  -85.764  -26.066  1.00 62.55  ? 122 GLU L OE2 1 
ATOM   13096 N  N   . LYS L  1 122 ? 11.233 -88.424  -28.269  1.00 49.26  ? 123 LYS L N   1 
ATOM   13097 C  CA  . LYS L  1 122 ? 11.149 -88.424  -29.726  1.00 48.58  ? 123 LYS L CA  1 
ATOM   13098 C  C   . LYS L  1 122 ? 12.416 -89.025  -30.316  1.00 45.95  ? 123 LYS L C   1 
ATOM   13099 O  O   . LYS L  1 122 ? 13.308 -89.439  -29.591  1.00 44.93  ? 123 LYS L O   1 
ATOM   13100 C  CB  . LYS L  1 122 ? 10.999 -86.996  -30.272  1.00 49.32  ? 123 LYS L CB  1 
ATOM   13101 C  CG  . LYS L  1 122 ? 9.912  -86.139  -29.639  1.00 52.62  ? 123 LYS L CG  1 
ATOM   13102 C  CD  . LYS L  1 122 ? 9.902  -84.714  -30.225  1.00 53.79  ? 123 LYS L CD  1 
ATOM   13103 C  CE  . LYS L  1 122 ? 8.980  -83.774  -29.443  1.00 57.36  ? 123 LYS L CE  1 
ATOM   13104 N  NZ  . LYS L  1 122 ? 8.747  -82.498  -30.171  1.00 59.03  ? 123 LYS L NZ  1 
ATOM   13105 N  N   . ALA L  1 123 ? 12.485 -89.063  -31.641  1.00 45.29  ? 124 ALA L N   1 
ATOM   13106 C  CA  . ALA L  1 123 ? 13.656 -89.555  -32.346  1.00 43.26  ? 124 ALA L CA  1 
ATOM   13107 C  C   . ALA L  1 123 ? 14.712 -88.466  -32.488  1.00 42.21  ? 124 ALA L C   1 
ATOM   13108 O  O   . ALA L  1 123 ? 14.373 -87.301  -32.662  1.00 42.94  ? 124 ALA L O   1 
ATOM   13109 C  CB  . ALA L  1 123 ? 13.253 -90.055  -33.705  1.00 43.80  ? 124 ALA L CB  1 
ATOM   13110 N  N   . ASP L  1 124 ? 15.988 -88.867  -32.424  1.00 40.94  ? 125 ASP L N   1 
ATOM   13111 C  CA  . ASP L  1 124 ? 17.149 -87.978  -32.622  1.00 40.16  ? 125 ASP L CA  1 
ATOM   13112 C  C   . ASP L  1 124 ? 17.320 -87.700  -34.113  1.00 40.32  ? 125 ASP L C   1 
ATOM   13113 O  O   . ASP L  1 124 ? 17.484 -88.615  -34.891  1.00 40.14  ? 125 ASP L O   1 
ATOM   13114 C  CB  . ASP L  1 124 ? 18.419 -88.630  -32.054  1.00 39.15  ? 125 ASP L CB  1 
ATOM   13115 C  CG  . ASP L  1 124 ? 19.648 -87.747  -32.176  1.00 39.12  ? 125 ASP L CG  1 
ATOM   13116 O  OD1 . ASP L  1 124 ? 19.513 -86.657  -32.737  1.00 39.92  ? 125 ASP L OD1 1 
ATOM   13117 O  OD2 . ASP L  1 124 ? 20.760 -88.133  -31.741  1.00 38.55  ? 125 ASP L OD2 1 
ATOM   13118 N  N   . ASP L  1 125 ? 17.288 -86.432  -34.507  1.00 41.15  ? 126 ASP L N   1 
ATOM   13119 C  CA  . ASP L  1 125 ? 17.351 -86.056  -35.931  1.00 41.70  ? 126 ASP L CA  1 
ATOM   13120 C  C   . ASP L  1 125 ? 18.766 -86.084  -36.470  1.00 41.25  ? 126 ASP L C   1 
ATOM   13121 O  O   . ASP L  1 125 ? 19.011 -85.658  -37.580  1.00 42.07  ? 126 ASP L O   1 
ATOM   13122 C  CB  . ASP L  1 125 ? 16.701 -84.682  -36.178  1.00 43.37  ? 126 ASP L CB  1 
ATOM   13123 C  CG  . ASP L  1 125 ? 17.542 -83.540  -35.707  1.00 43.77  ? 126 ASP L CG  1 
ATOM   13124 O  OD1 . ASP L  1 125 ? 18.763 -83.700  -35.652  1.00 43.15  ? 126 ASP L OD1 1 
ATOM   13125 O  OD2 . ASP L  1 125 ? 16.981 -82.475  -35.409  1.00 45.12  ? 126 ASP L OD2 1 
ATOM   13126 N  N   . LEU L  1 126 ? 19.696 -86.568  -35.660  1.00 40.38  ? 127 LEU L N   1 
ATOM   13127 C  CA  . LEU L  1 126 ? 21.100 -86.725  -36.045  1.00 40.46  ? 127 LEU L CA  1 
ATOM   13128 C  C   . LEU L  1 126 ? 21.744 -85.425  -36.543  1.00 41.82  ? 127 LEU L C   1 
ATOM   13129 O  O   . LEU L  1 126 ? 22.654 -85.433  -37.364  1.00 42.83  ? 127 LEU L O   1 
ATOM   13130 C  CB  . LEU L  1 126 ? 21.267 -87.832  -37.091  1.00 40.50  ? 127 LEU L CB  1 
ATOM   13131 C  CG  . LEU L  1 126 ? 20.593 -89.158  -36.768  1.00 39.98  ? 127 LEU L CG  1 
ATOM   13132 C  CD1 . LEU L  1 126 ? 21.011 -90.227  -37.777  1.00 41.01  ? 127 LEU L CD1 1 
ATOM   13133 C  CD2 . LEU L  1 126 ? 20.887 -89.609  -35.351  1.00 39.14  ? 127 LEU L CD2 1 
ATOM   13134 N  N   . GLY L  1 127 ? 21.279 -84.304  -36.026  1.00 42.52  ? 128 GLY L N   1 
ATOM   13135 C  CA  . GLY L  1 127 ? 21.892 -83.010  -36.317  1.00 44.34  ? 128 GLY L CA  1 
ATOM   13136 C  C   . GLY L  1 127 ? 21.504 -82.391  -37.638  1.00 45.73  ? 128 GLY L C   1 
ATOM   13137 O  O   . GLY L  1 127 ? 21.855 -81.255  -37.908  1.00 47.61  ? 128 GLY L O   1 
ATOM   13138 N  N   . LYS L  1 128 ? 20.738 -83.116  -38.440  1.00 45.18  ? 129 LYS L N   1 
ATOM   13139 C  CA  . LYS L  1 128 ? 20.361 -82.646  -39.774  1.00 46.88  ? 129 LYS L CA  1 
ATOM   13140 C  C   . LYS L  1 128 ? 19.051 -81.879  -39.787  1.00 47.97  ? 129 LYS L C   1 
ATOM   13141 O  O   . LYS L  1 128 ? 18.403 -81.795  -40.830  1.00 48.85  ? 129 LYS L O   1 
ATOM   13142 C  CB  . LYS L  1 128 ? 20.240 -83.822  -40.738  1.00 46.50  ? 129 LYS L CB  1 
ATOM   13143 C  CG  . LYS L  1 128 ? 21.440 -84.751  -40.767  1.00 46.20  ? 129 LYS L CG  1 
ATOM   13144 C  CD  . LYS L  1 128 ? 21.493 -85.606  -42.038  1.00 47.24  ? 129 LYS L CD  1 
ATOM   13145 C  CE  . LYS L  1 128 ? 22.629 -86.623  -41.970  1.00 47.42  ? 129 LYS L CE  1 
ATOM   13146 N  NZ  . LYS L  1 128 ? 22.945 -87.208  -43.293  1.00 49.34  ? 129 LYS L NZ  1 
ATOM   13147 N  N   . GLY L  1 129 ? 18.685 -81.313  -38.633  1.00 48.17  ? 130 GLY L N   1 
ATOM   13148 C  CA  . GLY L  1 129 ? 17.362 -80.708  -38.419  1.00 49.45  ? 130 GLY L CA  1 
ATOM   13149 C  C   . GLY L  1 129 ? 17.203 -79.316  -39.010  1.00 52.34  ? 130 GLY L C   1 
ATOM   13150 O  O   . GLY L  1 129 ? 16.093 -78.898  -39.371  1.00 53.89  ? 130 GLY L O   1 
ATOM   13151 N  N   . GLY L  1 130 ? 18.313 -78.589  -39.087  1.00 53.45  ? 131 GLY L N   1 
ATOM   13152 C  CA  . GLY L  1 130 ? 18.319 -77.242  -39.648  1.00 56.80  ? 131 GLY L CA  1 
ATOM   13153 C  C   . GLY L  1 130 ? 18.111 -76.148  -38.622  1.00 58.91  ? 131 GLY L C   1 
ATOM   13154 O  O   . GLY L  1 130 ? 18.576 -75.038  -38.814  1.00 62.03  ? 131 GLY L O   1 
ATOM   13155 N  N   . ASN L  1 131 ? 17.414 -76.453  -37.536  1.00 57.86  ? 132 ASN L N   1 
ATOM   13156 C  CA  . ASN L  1 131 ? 17.222 -75.492  -36.466  1.00 60.25  ? 132 ASN L CA  1 
ATOM   13157 C  C   . ASN L  1 131 ? 18.384 -75.441  -35.467  1.00 59.75  ? 132 ASN L C   1 
ATOM   13158 O  O   . ASN L  1 131 ? 19.324 -76.228  -35.544  1.00 57.34  ? 132 ASN L O   1 
ATOM   13159 C  CB  . ASN L  1 131 ? 15.894 -75.741  -35.742  1.00 60.46  ? 132 ASN L CB  1 
ATOM   13160 C  CG  . ASN L  1 131 ? 15.939 -76.916  -34.793  1.00 57.35  ? 132 ASN L CG  1 
ATOM   13161 O  OD1 . ASN L  1 131 ? 16.949 -77.569  -34.660  1.00 55.08  ? 132 ASN L OD1 1 
ATOM   13162 N  ND2 . ASN L  1 131 ? 14.829 -77.182  -34.121  1.00 58.04  ? 132 ASN L ND2 1 
ATOM   13163 N  N   . GLU L  1 132 ? 18.307 -74.489  -34.542  1.00 62.47  ? 133 GLU L N   1 
ATOM   13164 C  CA  . GLU L  1 132 ? 19.345 -74.261  -33.544  1.00 62.98  ? 133 GLU L CA  1 
ATOM   13165 C  C   . GLU L  1 132 ? 19.522 -75.491  -32.675  1.00 59.39  ? 133 GLU L C   1 
ATOM   13166 O  O   . GLU L  1 132 ? 20.627 -76.013  -32.487  1.00 57.75  ? 133 GLU L O   1 
ATOM   13167 C  CB  . GLU L  1 132 ? 18.983 -73.022  -32.694  1.00 67.20  ? 133 GLU L CB  1 
ATOM   13168 C  CG  . GLU L  1 132 ? 19.777 -72.861  -31.392  1.00 68.63  ? 133 GLU L CG  1 
ATOM   13169 C  CD  . GLU L  1 132 ? 21.182 -72.254  -31.589  1.00 71.19  ? 133 GLU L CD  1 
ATOM   13170 O  OE1 . GLU L  1 132 ? 21.588 -71.945  -32.751  1.00 72.07  ? 133 GLU L OE1 1 
ATOM   13171 O  OE2 . GLU L  1 132 ? 21.892 -72.099  -30.554  1.00 72.41  ? 133 GLU L OE2 1 
ATOM   13172 N  N   . GLU L  1 133 ? 18.400 -75.943  -32.151  1.00 58.63  ? 134 GLU L N   1 
ATOM   13173 C  CA  . GLU L  1 133 ? 18.380 -76.998  -31.134  1.00 56.27  ? 134 GLU L CA  1 
ATOM   13174 C  C   . GLU L  1 133 ? 18.894 -78.342  -31.658  1.00 52.47  ? 134 GLU L C   1 
ATOM   13175 O  O   . GLU L  1 133 ? 19.409 -79.140  -30.894  1.00 50.77  ? 134 GLU L O   1 
ATOM   13176 C  CB  . GLU L  1 133 ? 16.953 -77.143  -30.562  1.00 57.10  ? 134 GLU L CB  1 
ATOM   13177 C  CG  . GLU L  1 133 ? 16.846 -77.914  -29.229  1.00 56.28  ? 134 GLU L CG  1 
ATOM   13178 C  CD  . GLU L  1 133 ? 17.414 -77.141  -28.026  1.00 59.09  ? 134 GLU L CD  1 
ATOM   13179 O  OE1 . GLU L  1 133 ? 17.721 -75.940  -28.173  1.00 62.29  ? 134 GLU L OE1 1 
ATOM   13180 O  OE2 . GLU L  1 133 ? 17.555 -77.725  -26.922  1.00 58.38  ? 134 GLU L OE2 1 
ATOM   13181 N  N   . SER L  1 134 ? 18.752 -78.582  -32.958  1.00 51.69  ? 135 SER L N   1 
ATOM   13182 C  CA  . SER L  1 134 ? 19.194 -79.844  -33.583  1.00 48.80  ? 135 SER L CA  1 
ATOM   13183 C  C   . SER L  1 134 ? 20.679 -80.028  -33.452  1.00 48.18  ? 135 SER L C   1 
ATOM   13184 O  O   . SER L  1 134 ? 21.182 -81.146  -33.396  1.00 46.07  ? 135 SER L O   1 
ATOM   13185 C  CB  . SER L  1 134 ? 18.821 -79.890  -35.070  1.00 48.91  ? 135 SER L CB  1 
ATOM   13186 O  OG  . SER L  1 134 ? 19.455 -80.951  -35.749  1.00 46.65  ? 135 SER L OG  1 
ATOM   13187 N  N   . THR L  1 135 ? 21.375 -78.903  -33.409  1.00 50.60  ? 136 THR L N   1 
ATOM   13188 C  CA  . THR L  1 135 ? 22.823 -78.882  -33.205  1.00 51.07  ? 136 THR L CA  1 
ATOM   13189 C  C   . THR L  1 135 ? 23.258 -79.210  -31.759  1.00 50.68  ? 136 THR L C   1 
ATOM   13190 O  O   . THR L  1 135 ? 24.434 -79.409  -31.485  1.00 51.04  ? 136 THR L O   1 
ATOM   13191 C  CB  . THR L  1 135 ? 23.366 -77.514  -33.618  1.00 54.28  ? 136 THR L CB  1 
ATOM   13192 O  OG1 . THR L  1 135 ? 23.465 -77.470  -35.038  1.00 54.65  ? 136 THR L OG1 1 
ATOM   13193 C  CG2 . THR L  1 135 ? 24.711 -77.256  -33.020  1.00 55.74  ? 136 THR L CG2 1 
ATOM   13194 N  N   . LYS L  1 136 ? 22.305 -79.276  -30.844  1.00 50.42  ? 137 LYS L N   1 
ATOM   13195 C  CA  . LYS L  1 136 ? 22.597 -79.490  -29.440  1.00 50.54  ? 137 LYS L CA  1 
ATOM   13196 C  C   . LYS L  1 136 ? 22.044 -80.816  -28.935  1.00 47.90  ? 137 LYS L C   1 
ATOM   13197 O  O   . LYS L  1 136 ? 22.785 -81.720  -28.567  1.00 46.51  ? 137 LYS L O   1 
ATOM   13198 C  CB  . LYS L  1 136 ? 21.979 -78.347  -28.615  1.00 53.61  ? 137 LYS L CB  1 
ATOM   13199 C  CG  . LYS L  1 136 ? 22.693 -76.986  -28.692  1.00 57.48  ? 137 LYS L CG  1 
ATOM   13200 C  CD  . LYS L  1 136 ? 21.977 -75.936  -27.794  1.00 61.02  ? 137 LYS L CD  1 
ATOM   13201 C  CE  . LYS L  1 136 ? 22.893 -74.784  -27.361  1.00 64.79  ? 137 LYS L CE  1 
ATOM   13202 N  NZ  . LYS L  1 136 ? 22.847 -73.695  -28.330  1.00 67.56  ? 137 LYS L NZ  1 
ATOM   13203 N  N   . THR L  1 137 ? 20.719 -80.904  -28.916  1.00 47.77  ? 138 THR L N   1 
ATOM   13204 C  CA  . THR L  1 137 ? 19.995 -82.011  -28.284  1.00 46.35  ? 138 THR L CA  1 
ATOM   13205 C  C   . THR L  1 137 ? 19.533 -83.073  -29.286  1.00 44.27  ? 138 THR L C   1 
ATOM   13206 O  O   . THR L  1 137 ? 19.174 -84.182  -28.890  1.00 43.04  ? 138 THR L O   1 
ATOM   13207 C  CB  . THR L  1 137 ? 18.759 -81.499  -27.523  1.00 48.12  ? 138 THR L CB  1 
ATOM   13208 O  OG1 . THR L  1 137 ? 17.790 -80.997  -28.442  1.00 48.90  ? 138 THR L OG1 1 
ATOM   13209 C  CG2 . THR L  1 137 ? 19.122 -80.394  -26.608  1.00 51.00  ? 138 THR L CG2 1 
ATOM   13210 N  N   . GLY L  1 138 ? 19.551 -82.714  -30.569  1.00 44.20  ? 139 GLY L N   1 
ATOM   13211 C  CA  . GLY L  1 138 ? 19.067 -83.567  -31.642  1.00 42.89  ? 139 GLY L CA  1 
ATOM   13212 C  C   . GLY L  1 138 ? 17.569 -83.495  -31.839  1.00 43.68  ? 139 GLY L C   1 
ATOM   13213 O  O   . GLY L  1 138 ? 17.004 -84.250  -32.597  1.00 43.01  ? 139 GLY L O   1 
ATOM   13214 N  N   . ASN L  1 139 ? 16.929 -82.563  -31.155  1.00 45.74  ? 140 ASN L N   1 
ATOM   13215 C  CA  . ASN L  1 139 ? 15.467 -82.435  -31.136  1.00 47.28  ? 140 ASN L CA  1 
ATOM   13216 C  C   . ASN L  1 139 ? 14.741 -83.704  -30.698  1.00 46.44  ? 140 ASN L C   1 
ATOM   13217 O  O   . ASN L  1 139 ? 13.590 -83.898  -31.037  1.00 47.49  ? 140 ASN L O   1 
ATOM   13218 C  CB  . ASN L  1 139 ? 14.947 -81.939  -32.490  1.00 48.20  ? 140 ASN L CB  1 
ATOM   13219 C  CG  . ASN L  1 139 ? 15.131 -80.440  -32.686  1.00 50.31  ? 140 ASN L CG  1 
ATOM   13220 O  OD1 . ASN L  1 139 ? 15.291 -79.967  -33.792  1.00 50.89  ? 140 ASN L OD1 1 
ATOM   13221 N  ND2 . ASN L  1 139 ? 15.087 -79.695  -31.614  1.00 51.89  ? 140 ASN L ND2 1 
ATOM   13222 N  N   . ALA L  1 140 ? 15.410 -84.530  -29.900  1.00 45.09  ? 141 ALA L N   1 
ATOM   13223 C  CA  . ALA L  1 140 ? 14.883 -85.835  -29.482  1.00 44.62  ? 141 ALA L CA  1 
ATOM   13224 C  C   . ALA L  1 140 ? 13.968 -85.767  -28.270  1.00 46.62  ? 141 ALA L C   1 
ATOM   13225 O  O   . ALA L  1 140 ? 13.461 -86.791  -27.822  1.00 46.75  ? 141 ALA L O   1 
ATOM   13226 C  CB  . ALA L  1 140 ? 16.000 -86.778  -29.192  1.00 42.89  ? 141 ALA L CB  1 
ATOM   13227 N  N   . GLY L  1 141 ? 13.783 -84.570  -27.724  1.00 48.56  ? 142 GLY L N   1 
ATOM   13228 C  CA  . GLY L  1 141 ? 12.752 -84.328  -26.718  1.00 51.22  ? 142 GLY L CA  1 
ATOM   13229 C  C   . GLY L  1 141 ? 13.115 -84.742  -25.303  1.00 51.62  ? 142 GLY L C   1 
ATOM   13230 O  O   . GLY L  1 141 ? 14.281 -84.843  -24.955  1.00 50.15  ? 142 GLY L O   1 
ATOM   13231 N  N   . SER L  1 142 ? 12.093 -84.980  -24.491  1.00 54.07  ? 143 SER L N   1 
ATOM   13232 C  CA  . SER L  1 142 ? 12.250 -85.201  -23.052  1.00 55.34  ? 143 SER L CA  1 
ATOM   13233 C  C   . SER L  1 142 ? 12.929 -86.510  -22.722  1.00 53.27  ? 143 SER L C   1 
ATOM   13234 O  O   . SER L  1 142 ? 13.118 -87.354  -23.580  1.00 51.28  ? 143 SER L O   1 
ATOM   13235 C  CB  . SER L  1 142 ? 10.888 -85.169  -22.366  1.00 59.13  ? 143 SER L CB  1 
ATOM   13236 O  OG  . SER L  1 142 ? 10.151 -86.351  -22.634  1.00 59.22  ? 143 SER L OG  1 
ATOM   13237 N  N   . ARG L  1 143 ? 13.271 -86.673  -21.457  1.00 54.25  ? 144 ARG L N   1 
ATOM   13238 C  CA  . ARG L  1 143 ? 13.995 -87.848  -20.998  1.00 52.99  ? 144 ARG L CA  1 
ATOM   13239 C  C   . ARG L  1 143 ? 13.056 -88.842  -20.334  1.00 55.13  ? 144 ARG L C   1 
ATOM   13240 O  O   . ARG L  1 143 ? 12.598 -88.635  -19.217  1.00 58.14  ? 144 ARG L O   1 
ATOM   13241 C  CB  . ARG L  1 143 ? 15.087 -87.424  -20.034  1.00 53.29  ? 144 ARG L CB  1 
ATOM   13242 C  CG  . ARG L  1 143 ? 16.088 -86.496  -20.682  1.00 51.86  ? 144 ARG L CG  1 
ATOM   13243 C  CD  . ARG L  1 143 ? 17.081 -85.908  -19.709  1.00 52.94  ? 144 ARG L CD  1 
ATOM   13244 N  NE  . ARG L  1 143 ? 17.911 -84.897  -20.359  1.00 52.07  ? 144 ARG L NE  1 
ATOM   13245 C  CZ  . ARG L  1 143 ? 18.944 -84.291  -19.785  1.00 53.29  ? 144 ARG L CZ  1 
ATOM   13246 N  NH1 . ARG L  1 143 ? 19.278 -84.571  -18.532  1.00 55.30  ? 144 ARG L NH1 1 
ATOM   13247 N  NH2 . ARG L  1 143 ? 19.652 -83.395  -20.454  1.00 53.39  ? 144 ARG L NH2 1 
ATOM   13248 N  N   . LEU L  1 144 ? 12.778 -89.936  -21.025  1.00 54.11  ? 145 LEU L N   1 
ATOM   13249 C  CA  . LEU L  1 144 ? 11.789 -90.907  -20.568  1.00 56.56  ? 145 LEU L CA  1 
ATOM   13250 C  C   . LEU L  1 144 ? 12.319 -91.763  -19.444  1.00 57.42  ? 145 LEU L C   1 
ATOM   13251 O  O   . LEU L  1 144 ? 11.673 -91.887  -18.410  1.00 60.69  ? 145 LEU L O   1 
ATOM   13252 C  CB  . LEU L  1 144 ? 11.354 -91.824  -21.714  1.00 55.81  ? 145 LEU L CB  1 
ATOM   13253 C  CG  . LEU L  1 144 ? 10.513 -91.185  -22.820  1.00 56.14  ? 145 LEU L CG  1 
ATOM   13254 C  CD1 . LEU L  1 144 ? 9.981  -92.257  -23.815  1.00 56.01  ? 145 LEU L CD1 1 
ATOM   13255 C  CD2 . LEU L  1 144 ? 9.359  -90.356  -22.229  1.00 59.53  ? 145 LEU L CD2 1 
ATOM   13256 N  N   . ALA L  1 145 ? 13.480 -92.374  -19.670  1.00 55.06  ? 146 ALA L N   1 
ATOM   13257 C  CA  . ALA L  1 145 ? 14.100 -93.292  -18.700  1.00 55.97  ? 146 ALA L CA  1 
ATOM   13258 C  C   . ALA L  1 145 ? 15.594 -93.178  -18.765  1.00 53.56  ? 146 ALA L C   1 
ATOM   13259 O  O   . ALA L  1 145 ? 16.136 -92.988  -19.835  1.00 51.33  ? 146 ALA L O   1 
ATOM   13260 C  CB  . ALA L  1 145 ? 13.697 -94.733  -18.976  1.00 56.82  ? 146 ALA L CB  1 
ATOM   13261 N  N   . CYS L  1 146 ? 16.257 -93.314  -17.625  1.00 54.66  ? 147 CYS L N   1 
ATOM   13262 C  CA  . CYS L  1 146 ? 17.703 -93.203  -17.573  1.00 53.00  ? 147 CYS L CA  1 
ATOM   13263 C  C   . CYS L  1 146 ? 18.300 -94.015  -16.456  1.00 54.91  ? 147 CYS L C   1 
ATOM   13264 O  O   . CYS L  1 146 ? 17.584 -94.516  -15.603  1.00 57.73  ? 147 CYS L O   1 
ATOM   13265 C  CB  . CYS L  1 146 ? 18.108 -91.750  -17.425  1.00 52.60  ? 147 CYS L CB  1 
ATOM   13266 S  SG  . CYS L  1 146 ? 17.603 -90.990  -15.940  1.00 55.30  ? 147 CYS L SG  1 
ATOM   13267 N  N   . GLY L  1 147 ? 19.621 -94.149  -16.478  1.00 53.99  ? 148 GLY L N   1 
ATOM   13268 C  CA  . GLY L  1 147 ? 20.349 -94.853  -15.427  1.00 56.05  ? 148 GLY L CA  1 
ATOM   13269 C  C   . GLY L  1 147 ? 21.833 -94.572  -15.474  1.00 55.13  ? 148 GLY L C   1 
ATOM   13270 O  O   . GLY L  1 147 ? 22.362 -94.260  -16.527  1.00 52.88  ? 148 GLY L O   1 
ATOM   13271 N  N   . VAL L  1 148 ? 22.496 -94.677  -14.323  1.00 57.35  ? 149 VAL L N   1 
ATOM   13272 C  CA  . VAL L  1 148 ? 23.955 -94.487  -14.234  1.00 57.18  ? 149 VAL L CA  1 
ATOM   13273 C  C   . VAL L  1 148 ? 24.706 -95.737  -14.702  1.00 57.06  ? 149 VAL L C   1 
ATOM   13274 O  O   . VAL L  1 148 ? 24.376 -96.861  -14.323  1.00 58.53  ? 149 VAL L O   1 
ATOM   13275 C  CB  . VAL L  1 148 ? 24.405 -94.148  -12.812  1.00 59.94  ? 149 VAL L CB  1 
ATOM   13276 C  CG1 . VAL L  1 148 ? 25.880 -93.977  -12.777  1.00 60.27  ? 149 VAL L CG1 1 
ATOM   13277 C  CG2 . VAL L  1 148 ? 23.733 -92.887  -12.341  1.00 60.77  ? 149 VAL L CG2 1 
ATOM   13278 N  N   . ILE L  1 149 ? 25.722 -95.522  -15.532  1.00 55.73  ? 150 ILE L N   1 
ATOM   13279 C  CA  . ILE L  1 149 ? 26.472 -96.624  -16.138  1.00 55.89  ? 150 ILE L CA  1 
ATOM   13280 C  C   . ILE L  1 149 ? 27.467 -97.144  -15.143  1.00 58.72  ? 150 ILE L C   1 
ATOM   13281 O  O   . ILE L  1 149 ? 28.294 -96.384  -14.641  1.00 59.61  ? 150 ILE L O   1 
ATOM   13282 C  CB  . ILE L  1 149 ? 27.246 -96.201  -17.393  1.00 54.00  ? 150 ILE L CB  1 
ATOM   13283 C  CG1 . ILE L  1 149 ? 26.298 -95.883  -18.535  1.00 51.45  ? 150 ILE L CG1 1 
ATOM   13284 C  CG2 . ILE L  1 149 ? 28.155 -97.319  -17.848  1.00 55.06  ? 150 ILE L CG2 1 
ATOM   13285 C  CD1 . ILE L  1 149 ? 26.999 -95.269  -19.708  1.00 49.96  ? 150 ILE L CD1 1 
ATOM   13286 N  N   . GLY L  1 150 ? 27.408 -98.444  -14.890  1.00 60.60  ? 151 GLY L N   1 
ATOM   13287 C  CA  . GLY L  1 150 ? 28.208 -99.060  -13.827  1.00 64.03  ? 151 GLY L CA  1 
ATOM   13288 C  C   . GLY L  1 150 ? 29.108 -100.192 -14.283  1.00 65.55  ? 151 GLY L C   1 
ATOM   13289 O  O   . GLY L  1 150 ? 28.852 -100.830 -15.313  1.00 64.55  ? 151 GLY L O   1 
ATOM   13290 N  N   . ILE L  1 151 ? 30.164 -100.429 -13.502  1.00 68.37  ? 152 ILE L N   1 
ATOM   13291 C  CA  . ILE L  1 151 ? 31.121 -101.502 -13.784  1.00 70.82  ? 152 ILE L CA  1 
ATOM   13292 C  C   . ILE L  1 151 ? 30.492 -102.850 -13.501  1.00 73.13  ? 152 ILE L C   1 
ATOM   13293 O  O   . ILE L  1 151 ? 29.939 -103.068 -12.430  1.00 74.98  ? 152 ILE L O   1 
ATOM   13294 C  CB  . ILE L  1 151 ? 32.398 -101.398 -12.940  1.00 73.96  ? 152 ILE L CB  1 
ATOM   13295 C  CG1 . ILE L  1 151 ? 33.126 -100.074 -13.228  1.00 72.52  ? 152 ILE L CG1 1 
ATOM   13296 C  CG2 . ILE L  1 151 ? 33.299 -102.586 -13.232  1.00 76.91  ? 152 ILE L CG2 1 
ATOM   13297 C  CD1 . ILE L  1 151 ? 34.400 -99.883  -12.442  1.00 75.93  ? 152 ILE L CD1 1 
ATOM   13298 N  N   . ALA L  1 152 ? 30.594 -103.754 -14.468  1.00 73.64  ? 153 ALA L N   1 
ATOM   13299 C  CA  . ALA L  1 152 ? 29.914 -105.056 -14.410  1.00 76.05  ? 153 ALA L CA  1 
ATOM   13300 C  C   . ALA L  1 152 ? 30.899 -106.215 -14.314  1.00 80.44  ? 153 ALA L C   1 
ATOM   13301 O  O   . ALA L  1 152 ? 32.068 -106.093 -14.693  1.00 81.10  ? 153 ALA L O   1 
ATOM   13302 C  CB  . ALA L  1 152 ? 29.020 -105.235 -15.631  1.00 73.64  ? 153 ALA L CB  1 
ATOM   13303 N  N   . GLN L  1 153 ? 30.420 -107.349 -13.820  1.00 83.95  ? 154 GLN L N   1 
ATOM   13304 C  CA  . GLN L  1 153 ? 31.280 -108.528 -13.683  1.00 89.05  ? 154 GLN L CA  1 
ATOM   13305 C  C   . GLN L  1 153 ? 31.542 -109.165 -15.035  1.00 89.42  ? 154 GLN L C   1 
ATOM   13306 O  O   . GLN L  1 153 ? 30.617 -109.366 -15.815  1.00 87.86  ? 154 GLN L O   1 
ATOM   13307 C  CB  . GLN L  1 153 ? 30.669 -109.582 -12.752  1.00 93.46  ? 154 GLN L CB  1 
ATOM   13308 C  CG  . GLN L  1 153 ? 31.587 -110.818 -12.534  1.00 99.38  ? 154 GLN L CG  1 
ATOM   13309 C  CD  . GLN L  1 153 ? 31.047 -111.819 -11.504  1.00 104.33 ? 154 GLN L CD  1 
ATOM   13310 O  OE1 . GLN L  1 153 ? 30.908 -111.495 -10.319  1.00 105.38 ? 154 GLN L OE1 1 
ATOM   13311 N  NE2 . GLN L  1 153 ? 30.759 -113.044 -11.955  1.00 107.69 ? 154 GLN L NE2 1 
ATOM   13312 O  OXT . GLN L  1 153 ? 32.676 -109.514 -15.363  1.00 91.91  ? 154 GLN L OXT 1 
HETATM 13313 CU CU  A CU  M  2 .   ? 21.560 -53.147  -25.953  1.00 58.29  ? 155 CU  A CU  1 
HETATM 13314 ZN ZN  . ZN  N  3 .   ? 27.186 -56.108  -26.973  1.00 35.07  ? 156 ZN  A ZN  1 
HETATM 13315 CU CU  A CU  O  2 .   ? 19.981 -20.214  -25.091  1.00 46.54  ? 155 CU  B CU  1 
HETATM 13316 ZN ZN  . ZN  P  3 .   ? 25.333 -16.724  -25.430  1.00 20.56  ? 156 ZN  B ZN  1 
HETATM 13317 S  S   . SO4 Q  4 .   ? 26.120 -5.781   -37.527  1.00 114.23 ? 1   SO4 B S   1 
HETATM 13318 O  O1  . SO4 Q  4 .   ? 26.296 -6.575   -38.741  1.00 114.16 ? 1   SO4 B O1  1 
HETATM 13319 O  O2  . SO4 Q  4 .   ? 26.571 -4.410   -37.756  1.00 114.01 ? 1   SO4 B O2  1 
HETATM 13320 O  O3  . SO4 Q  4 .   ? 24.702 -5.750   -37.205  1.00 114.74 ? 1   SO4 B O3  1 
HETATM 13321 O  O4  . SO4 Q  4 .   ? 26.857 -6.376   -36.411  1.00 113.67 ? 1   SO4 B O4  1 
HETATM 13322 S  S   . SO4 R  4 .   ? 18.459 -18.654  -20.156  1.00 114.07 ? 157 SO4 B S   1 
HETATM 13323 O  O1  . SO4 R  4 .   ? 19.769 -19.274  -20.348  1.00 113.89 ? 157 SO4 B O1  1 
HETATM 13324 O  O2  . SO4 R  4 .   ? 18.327 -17.610  -21.168  1.00 115.11 ? 157 SO4 B O2  1 
HETATM 13325 O  O3  . SO4 R  4 .   ? 17.407 -19.637  -20.366  1.00 113.92 ? 157 SO4 B O3  1 
HETATM 13326 O  O4  . SO4 R  4 .   ? 18.302 -18.113  -18.802  1.00 113.07 ? 157 SO4 B O4  1 
HETATM 13327 CU CU  A CU  S  2 .   ? 19.821 10.655   -29.149  1.00 72.11  ? 155 CU  C CU  1 
HETATM 13328 ZN ZN  . ZN  T  3 .   ? 24.205 9.614    -33.631  1.00 33.00  ? 156 ZN  C ZN  1 
HETATM 13329 CU CU  A CU  U  2 .   ? 28.690 25.916   -3.160   1.00 277.39 ? 155 CU  D CU  1 
HETATM 13330 ZN ZN  . ZN  V  3 .   ? 35.611 28.213   -0.148   1.00 149.18 ? 156 ZN  D ZN  1 
HETATM 13331 CU CU  A CU  W  2 .   ? 10.286 7.205    -82.162  1.00 121.29 ? 155 CU  E CU  1 
HETATM 13332 ZN ZN  . ZN  X  3 .   ? 15.803 8.284    -85.924  1.00 126.31 ? 156 ZN  E ZN  1 
HETATM 13333 CU CU  A CU  Y  2 .   ? 14.100 -8.339   -53.395  1.00 53.46  ? 155 CU  F CU  1 
HETATM 13334 ZN ZN  . ZN  Z  3 .   ? 19.925 -11.036  -51.618  1.00 23.13  ? 156 ZN  F ZN  1 
HETATM 13335 CU CU  A CU  AA 2 .   ? 16.007 -42.094  -53.483  1.00 78.43  ? 155 CU  G CU  1 
HETATM 13336 ZN ZN  . ZN  BA 3 .   ? 21.811 -39.629  -54.786  1.00 68.62  ? 156 ZN  G ZN  1 
HETATM 13337 CU CU  A CU  CA 2 .   ? 13.875 -75.595  -53.368  1.00 58.04  ? 155 CU  H CU  1 
HETATM 13338 ZN ZN  . ZN  DA 3 .   ? 18.763 -79.286  -55.356  1.00 28.72  ? 156 ZN  H ZN  1 
HETATM 13339 CU CU  A CU  EA 2 .   ? 10.874 -123.753 -77.292  1.00 59.40  ? 155 CU  I CU  1 
HETATM 13340 ZN ZN  . ZN  FA 3 .   ? 16.040 -125.104 -81.074  1.00 39.47  ? 156 ZN  I ZN  1 
HETATM 13341 CU CU  A CU  GA 2 .   ? 15.132 -106.783 -49.005  1.00 46.73  ? 155 CU  J CU  1 
HETATM 13342 ZN ZN  . ZN  HA 3 .   ? 21.025 -105.513 -46.810  1.00 21.92  ? 156 ZN  J ZN  1 
HETATM 13343 S  S   . SO4 IA 4 .   ? 24.417 -89.870  -44.344  1.00 98.31  ? 157 SO4 J S   1 
HETATM 13344 O  O1  . SO4 IA 4 .   ? 23.022 -89.761  -43.933  1.00 97.65  ? 157 SO4 J O1  1 
HETATM 13345 O  O2  . SO4 IA 4 .   ? 24.912 -91.202  -44.017  1.00 98.61  ? 157 SO4 J O2  1 
HETATM 13346 O  O3  . SO4 IA 4 .   ? 24.497 -89.642  -45.784  1.00 98.66  ? 157 SO4 J O3  1 
HETATM 13347 O  O4  . SO4 IA 4 .   ? 25.261 -88.894  -43.658  1.00 98.02  ? 157 SO4 J O4  1 
HETATM 13348 CU CU  A CU  JA 2 .   ? 28.987 -104.320 2.599    1.00 110.69 ? 155 CU  K CU  1 
HETATM 13349 ZN ZN  . ZN  KA 3 .   ? 34.916 -106.002 3.535    1.00 148.54 ? 156 ZN  K ZN  1 
HETATM 13350 CU CU  A CU  LA 2 .   ? 20.310 -87.631  -24.796  1.00 55.32  ? 155 CU  L CU  1 
HETATM 13351 ZN ZN  . ZN  MA 3 .   ? 24.609 -85.108  -28.777  1.00 25.53  ? 156 ZN  L ZN  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   2   2   ALA ALA A . n 
A 1 2   THR 2   3   3   THR THR A . n 
A 1 3   LYS 3   4   4   LYS LYS A . n 
A 1 4   ALA 4   5   5   ALA ALA A . n 
A 1 5   VAL 5   6   6   VAL VAL A . n 
A 1 6   CYS 6   7   7   CYS CYS A . n 
A 1 7   VAL 7   8   8   VAL VAL A . n 
A 1 8   LEU 8   9   9   LEU LEU A . n 
A 1 9   LYS 9   10  10  LYS LYS A . n 
A 1 10  GLY 10  11  11  GLY GLY A . n 
A 1 11  ASP 11  12  12  ASP ASP A . n 
A 1 12  GLY 12  13  13  GLY GLY A . n 
A 1 13  PRO 13  14  14  PRO PRO A . n 
A 1 14  VAL 14  15  15  VAL VAL A . n 
A 1 15  GLN 15  16  16  GLN GLN A . n 
A 1 16  GLY 16  17  17  GLY GLY A . n 
A 1 17  ILE 17  18  18  ILE ILE A . n 
A 1 18  ILE 18  19  19  ILE ILE A . n 
A 1 19  ASN 19  20  20  ASN ASN A . n 
A 1 20  PHE 20  21  21  PHE PHE A . n 
A 1 21  GLU 21  22  22  GLU GLU A . n 
A 1 22  GLN 22  23  23  GLN GLN A . n 
A 1 23  LYS 23  24  24  LYS LYS A . n 
A 1 24  GLU 24  25  25  GLU GLU A . n 
A 1 25  SER 25  26  26  SER SER A . n 
A 1 26  ASN 26  27  27  ASN ASN A . n 
A 1 27  GLY 27  28  28  GLY GLY A . n 
A 1 28  PRO 28  29  29  PRO PRO A . n 
A 1 29  VAL 29  30  30  VAL VAL A . n 
A 1 30  LYS 30  31  31  LYS LYS A . n 
A 1 31  VAL 31  32  32  VAL VAL A . n 
A 1 32  TRP 32  33  33  TRP TRP A . n 
A 1 33  GLY 33  34  34  GLY GLY A . n 
A 1 34  SER 34  35  35  SER SER A . n 
A 1 35  ILE 35  36  36  ILE ILE A . n 
A 1 36  LYS 36  37  37  LYS LYS A . n 
A 1 37  GLY 37  38  38  GLY GLY A . n 
A 1 38  LEU 38  39  39  LEU LEU A . n 
A 1 39  THR 39  40  40  THR THR A . n 
A 1 40  GLU 40  41  41  GLU GLU A . n 
A 1 41  GLY 41  42  42  GLY GLY A . n 
A 1 42  LEU 42  43  43  LEU LEU A . n 
A 1 43  HIS 43  44  44  HIS HIS A . n 
A 1 44  GLY 44  45  45  GLY GLY A . n 
A 1 45  PHE 45  46  46  PHE PHE A . n 
A 1 46  HIS 46  47  47  HIS HIS A . n 
A 1 47  VAL 47  48  48  VAL VAL A . n 
A 1 48  HIS 48  49  49  HIS HIS A . n 
A 1 49  GLU 49  50  50  GLU GLU A . n 
A 1 50  PHE 50  51  51  PHE PHE A . n 
A 1 51  GLY 51  52  52  GLY GLY A . n 
A 1 52  ASP 52  53  53  ASP ASP A . n 
A 1 53  ASN 53  54  54  ASN ASN A . n 
A 1 54  THR 54  55  55  THR THR A . n 
A 1 55  ALA 55  56  56  ALA ALA A . n 
A 1 56  GLY 56  57  57  GLY GLY A . n 
A 1 57  CYS 57  58  58  CYS CYS A . n 
A 1 58  THR 58  59  59  THR THR A . n 
A 1 59  SER 59  60  60  SER SER A . n 
A 1 60  ALA 60  61  61  ALA ALA A . n 
A 1 61  GLY 61  62  62  GLY GLY A . n 
A 1 62  PRO 62  63  63  PRO PRO A . n 
A 1 63  HIS 63  64  64  HIS HIS A . n 
A 1 64  PHE 64  65  65  PHE PHE A . n 
A 1 65  ASN 65  66  66  ASN ASN A . n 
A 1 66  PRO 66  67  67  PRO PRO A . n 
A 1 67  LEU 67  68  68  LEU LEU A . n 
A 1 68  SER 68  69  69  SER SER A . n 
A 1 69  ARG 69  70  70  ARG ARG A . n 
A 1 70  LYS 70  71  71  LYS LYS A . n 
A 1 71  HIS 71  72  72  HIS HIS A . n 
A 1 72  GLY 72  73  73  GLY GLY A . n 
A 1 73  GLY 73  74  74  GLY GLY A . n 
A 1 74  PRO 74  75  75  PRO PRO A . n 
A 1 75  LYS 75  76  76  LYS LYS A . n 
A 1 76  ASP 76  77  77  ASP ASP A . n 
A 1 77  GLU 77  78  78  GLU GLU A . n 
A 1 78  GLU 78  79  79  GLU GLU A . n 
A 1 79  ARG 79  80  80  ARG ARG A . n 
A 1 80  HIS 80  81  81  HIS HIS A . n 
A 1 81  VAL 81  82  82  VAL VAL A . n 
A 1 82  GLY 82  83  83  GLY GLY A . n 
A 1 83  ASP 83  84  84  ASP ASP A . n 
A 1 84  LEU 84  85  85  LEU LEU A . n 
A 1 85  GLY 85  86  86  GLY GLY A . n 
A 1 86  ASN 86  87  87  ASN ASN A . n 
A 1 87  VAL 87  88  88  VAL VAL A . n 
A 1 88  THR 88  89  89  THR THR A . n 
A 1 89  ALA 89  90  90  ALA ALA A . n 
A 1 90  ASP 90  91  91  ASP ASP A . n 
A 1 91  LYS 91  92  92  LYS LYS A . n 
A 1 92  ASP 92  93  93  ASP ASP A . n 
A 1 93  GLY 93  94  94  GLY GLY A . n 
A 1 94  VAL 94  95  95  VAL VAL A . n 
A 1 95  ALA 95  96  96  ALA ALA A . n 
A 1 96  ASP 96  97  97  ASP ASP A . n 
A 1 97  VAL 97  98  98  VAL VAL A . n 
A 1 98  SER 98  99  99  SER SER A . n 
A 1 99  ILE 99  100 100 ILE ILE A . n 
A 1 100 GLU 100 101 101 GLU GLU A . n 
A 1 101 ASP 101 102 102 ASP ASP A . n 
A 1 102 SER 102 103 103 SER SER A . n 
A 1 103 VAL 103 104 104 VAL VAL A . n 
A 1 104 ILE 104 105 105 ILE ILE A . n 
A 1 105 SER 105 106 106 SER SER A . n 
A 1 106 LEU 106 107 107 LEU LEU A . n 
A 1 107 SER 107 108 108 SER SER A . n 
A 1 108 GLY 108 109 109 GLY GLY A . n 
A 1 109 ASP 109 110 110 ASP ASP A . n 
A 1 110 HIS 110 111 111 HIS HIS A . n 
A 1 111 CYS 111 112 112 CYS CYS A . n 
A 1 112 ILE 112 113 113 ILE ILE A . n 
A 1 113 ILE 113 114 114 ILE ILE A . n 
A 1 114 GLY 114 115 115 GLY GLY A . n 
A 1 115 ARG 115 116 116 ARG ARG A . n 
A 1 116 THR 116 117 117 THR THR A . n 
A 1 117 LEU 117 118 118 LEU LEU A . n 
A 1 118 VAL 118 119 119 VAL VAL A . n 
A 1 119 VAL 119 120 120 VAL VAL A . n 
A 1 120 HIS 120 121 121 HIS HIS A . n 
A 1 121 GLU 121 122 122 GLU GLU A . n 
A 1 122 LYS 122 123 123 LYS LYS A . n 
A 1 123 ALA 123 124 124 ALA ALA A . n 
A 1 124 ASP 124 125 125 ASP ASP A . n 
A 1 125 ASP 125 126 126 ASP ASP A . n 
A 1 126 LEU 126 127 127 LEU LEU A . n 
A 1 127 GLY 127 128 128 GLY GLY A . n 
A 1 128 LYS 128 129 129 LYS LYS A . n 
A 1 129 GLY 129 130 130 GLY GLY A . n 
A 1 130 GLY 130 131 131 GLY GLY A . n 
A 1 131 ASN 131 132 132 ASN ASN A . n 
A 1 132 GLU 132 133 133 GLU GLU A . n 
A 1 133 GLU 133 134 134 GLU GLU A . n 
A 1 134 SER 134 135 135 SER SER A . n 
A 1 135 THR 135 136 136 THR THR A . n 
A 1 136 LYS 136 137 137 LYS LYS A . n 
A 1 137 THR 137 138 138 THR THR A . n 
A 1 138 GLY 138 139 139 GLY GLY A . n 
A 1 139 ASN 139 140 140 ASN ASN A . n 
A 1 140 ALA 140 141 141 ALA ALA A . n 
A 1 141 GLY 141 142 142 GLY GLY A . n 
A 1 142 SER 142 143 143 SER SER A . n 
A 1 143 ARG 143 144 144 ARG ARG A . n 
A 1 144 LEU 144 145 145 LEU LEU A . n 
A 1 145 ALA 145 146 146 ALA ALA A . n 
A 1 146 CYS 146 147 147 CYS CYS A . n 
A 1 147 GLY 147 148 148 GLY GLY A . n 
A 1 148 VAL 148 149 149 VAL VAL A . n 
A 1 149 ILE 149 150 150 ILE ILE A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 ILE 151 152 152 ILE ILE A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 GLN 153 154 154 GLN GLN A . n 
B 1 1   ALA 1   2   2   ALA ALA B . n 
B 1 2   THR 2   3   3   THR THR B . n 
B 1 3   LYS 3   4   4   LYS LYS B . n 
B 1 4   ALA 4   5   5   ALA ALA B . n 
B 1 5   VAL 5   6   6   VAL VAL B . n 
B 1 6   CYS 6   7   7   CYS CYS B . n 
B 1 7   VAL 7   8   8   VAL VAL B . n 
B 1 8   LEU 8   9   9   LEU LEU B . n 
B 1 9   LYS 9   10  10  LYS LYS B . n 
B 1 10  GLY 10  11  11  GLY GLY B . n 
B 1 11  ASP 11  12  12  ASP ASP B . n 
B 1 12  GLY 12  13  13  GLY GLY B . n 
B 1 13  PRO 13  14  14  PRO PRO B . n 
B 1 14  VAL 14  15  15  VAL VAL B . n 
B 1 15  GLN 15  16  16  GLN GLN B . n 
B 1 16  GLY 16  17  17  GLY GLY B . n 
B 1 17  ILE 17  18  18  ILE ILE B . n 
B 1 18  ILE 18  19  19  ILE ILE B . n 
B 1 19  ASN 19  20  20  ASN ASN B . n 
B 1 20  PHE 20  21  21  PHE PHE B . n 
B 1 21  GLU 21  22  22  GLU GLU B . n 
B 1 22  GLN 22  23  23  GLN GLN B . n 
B 1 23  LYS 23  24  24  LYS LYS B . n 
B 1 24  GLU 24  25  25  GLU GLU B . n 
B 1 25  SER 25  26  26  SER SER B . n 
B 1 26  ASN 26  27  27  ASN ASN B . n 
B 1 27  GLY 27  28  28  GLY GLY B . n 
B 1 28  PRO 28  29  29  PRO PRO B . n 
B 1 29  VAL 29  30  30  VAL VAL B . n 
B 1 30  LYS 30  31  31  LYS LYS B . n 
B 1 31  VAL 31  32  32  VAL VAL B . n 
B 1 32  TRP 32  33  33  TRP TRP B . n 
B 1 33  GLY 33  34  34  GLY GLY B . n 
B 1 34  SER 34  35  35  SER SER B . n 
B 1 35  ILE 35  36  36  ILE ILE B . n 
B 1 36  LYS 36  37  37  LYS LYS B . n 
B 1 37  GLY 37  38  38  GLY GLY B . n 
B 1 38  LEU 38  39  39  LEU LEU B . n 
B 1 39  THR 39  40  40  THR THR B . n 
B 1 40  GLU 40  41  41  GLU GLU B . n 
B 1 41  GLY 41  42  42  GLY GLY B . n 
B 1 42  LEU 42  43  43  LEU LEU B . n 
B 1 43  HIS 43  44  44  HIS HIS B . n 
B 1 44  GLY 44  45  45  GLY GLY B . n 
B 1 45  PHE 45  46  46  PHE PHE B . n 
B 1 46  HIS 46  47  47  HIS HIS B . n 
B 1 47  VAL 47  48  48  VAL VAL B . n 
B 1 48  HIS 48  49  49  HIS HIS B . n 
B 1 49  GLU 49  50  50  GLU GLU B . n 
B 1 50  PHE 50  51  51  PHE PHE B . n 
B 1 51  GLY 51  52  52  GLY GLY B . n 
B 1 52  ASP 52  53  53  ASP ASP B . n 
B 1 53  ASN 53  54  54  ASN ASN B . n 
B 1 54  THR 54  55  55  THR THR B . n 
B 1 55  ALA 55  56  56  ALA ALA B . n 
B 1 56  GLY 56  57  57  GLY GLY B . n 
B 1 57  CYS 57  58  58  CYS CYS B . n 
B 1 58  THR 58  59  59  THR THR B . n 
B 1 59  SER 59  60  60  SER SER B . n 
B 1 60  ALA 60  61  61  ALA ALA B . n 
B 1 61  GLY 61  62  62  GLY GLY B . n 
B 1 62  PRO 62  63  63  PRO PRO B . n 
B 1 63  HIS 63  64  64  HIS HIS B . n 
B 1 64  PHE 64  65  65  PHE PHE B . n 
B 1 65  ASN 65  66  66  ASN ASN B . n 
B 1 66  PRO 66  67  67  PRO PRO B . n 
B 1 67  LEU 67  68  68  LEU LEU B . n 
B 1 68  SER 68  69  69  SER SER B . n 
B 1 69  ARG 69  70  70  ARG ARG B . n 
B 1 70  LYS 70  71  71  LYS LYS B . n 
B 1 71  HIS 71  72  72  HIS HIS B . n 
B 1 72  GLY 72  73  73  GLY GLY B . n 
B 1 73  GLY 73  74  74  GLY GLY B . n 
B 1 74  PRO 74  75  75  PRO PRO B . n 
B 1 75  LYS 75  76  76  LYS LYS B . n 
B 1 76  ASP 76  77  77  ASP ASP B . n 
B 1 77  GLU 77  78  78  GLU GLU B . n 
B 1 78  GLU 78  79  79  GLU GLU B . n 
B 1 79  ARG 79  80  80  ARG ARG B . n 
B 1 80  HIS 80  81  81  HIS HIS B . n 
B 1 81  VAL 81  82  82  VAL VAL B . n 
B 1 82  GLY 82  83  83  GLY GLY B . n 
B 1 83  ASP 83  84  84  ASP ASP B . n 
B 1 84  LEU 84  85  85  LEU LEU B . n 
B 1 85  GLY 85  86  86  GLY GLY B . n 
B 1 86  ASN 86  87  87  ASN ASN B . n 
B 1 87  VAL 87  88  88  VAL VAL B . n 
B 1 88  THR 88  89  89  THR THR B . n 
B 1 89  ALA 89  90  90  ALA ALA B . n 
B 1 90  ASP 90  91  91  ASP ASP B . n 
B 1 91  LYS 91  92  92  LYS LYS B . n 
B 1 92  ASP 92  93  93  ASP ASP B . n 
B 1 93  GLY 93  94  94  GLY GLY B . n 
B 1 94  VAL 94  95  95  VAL VAL B . n 
B 1 95  ALA 95  96  96  ALA ALA B . n 
B 1 96  ASP 96  97  97  ASP ASP B . n 
B 1 97  VAL 97  98  98  VAL VAL B . n 
B 1 98  SER 98  99  99  SER SER B . n 
B 1 99  ILE 99  100 100 ILE ILE B . n 
B 1 100 GLU 100 101 101 GLU GLU B . n 
B 1 101 ASP 101 102 102 ASP ASP B . n 
B 1 102 SER 102 103 103 SER SER B . n 
B 1 103 VAL 103 104 104 VAL VAL B . n 
B 1 104 ILE 104 105 105 ILE ILE B . n 
B 1 105 SER 105 106 106 SER SER B . n 
B 1 106 LEU 106 107 107 LEU LEU B . n 
B 1 107 SER 107 108 108 SER SER B . n 
B 1 108 GLY 108 109 109 GLY GLY B . n 
B 1 109 ASP 109 110 110 ASP ASP B . n 
B 1 110 HIS 110 111 111 HIS HIS B . n 
B 1 111 CYS 111 112 112 CYS CYS B . n 
B 1 112 ILE 112 113 113 ILE ILE B . n 
B 1 113 ILE 113 114 114 ILE ILE B . n 
B 1 114 GLY 114 115 115 GLY GLY B . n 
B 1 115 ARG 115 116 116 ARG ARG B . n 
B 1 116 THR 116 117 117 THR THR B . n 
B 1 117 LEU 117 118 118 LEU LEU B . n 
B 1 118 VAL 118 119 119 VAL VAL B . n 
B 1 119 VAL 119 120 120 VAL VAL B . n 
B 1 120 HIS 120 121 121 HIS HIS B . n 
B 1 121 GLU 121 122 122 GLU GLU B . n 
B 1 122 LYS 122 123 123 LYS LYS B . n 
B 1 123 ALA 123 124 124 ALA ALA B . n 
B 1 124 ASP 124 125 125 ASP ASP B . n 
B 1 125 ASP 125 126 126 ASP ASP B . n 
B 1 126 LEU 126 127 127 LEU LEU B . n 
B 1 127 GLY 127 128 128 GLY GLY B . n 
B 1 128 LYS 128 129 129 LYS LYS B . n 
B 1 129 GLY 129 130 130 GLY GLY B . n 
B 1 130 GLY 130 131 131 GLY GLY B . n 
B 1 131 ASN 131 132 132 ASN ASN B . n 
B 1 132 GLU 132 133 133 GLU GLU B . n 
B 1 133 GLU 133 134 134 GLU GLU B . n 
B 1 134 SER 134 135 135 SER SER B . n 
B 1 135 THR 135 136 136 THR THR B . n 
B 1 136 LYS 136 137 137 LYS LYS B . n 
B 1 137 THR 137 138 138 THR THR B . n 
B 1 138 GLY 138 139 139 GLY GLY B . n 
B 1 139 ASN 139 140 140 ASN ASN B . n 
B 1 140 ALA 140 141 141 ALA ALA B . n 
B 1 141 GLY 141 142 142 GLY GLY B . n 
B 1 142 SER 142 143 143 SER SER B . n 
B 1 143 ARG 143 144 144 ARG ARG B . n 
B 1 144 LEU 144 145 145 LEU LEU B . n 
B 1 145 ALA 145 146 146 ALA ALA B . n 
B 1 146 CYS 146 147 147 CYS CYS B . n 
B 1 147 GLY 147 148 148 GLY GLY B . n 
B 1 148 VAL 148 149 149 VAL VAL B . n 
B 1 149 ILE 149 150 150 ILE ILE B . n 
B 1 150 GLY 150 151 151 GLY GLY B . n 
B 1 151 ILE 151 152 152 ILE ILE B . n 
B 1 152 ALA 152 153 153 ALA ALA B . n 
B 1 153 GLN 153 154 154 GLN GLN B . n 
C 1 1   ALA 1   2   2   ALA ALA C . n 
C 1 2   THR 2   3   3   THR THR C . n 
C 1 3   LYS 3   4   4   LYS LYS C . n 
C 1 4   ALA 4   5   5   ALA ALA C . n 
C 1 5   VAL 5   6   6   VAL VAL C . n 
C 1 6   CYS 6   7   7   CYS CYS C . n 
C 1 7   VAL 7   8   8   VAL VAL C . n 
C 1 8   LEU 8   9   9   LEU LEU C . n 
C 1 9   LYS 9   10  10  LYS LYS C . n 
C 1 10  GLY 10  11  11  GLY GLY C . n 
C 1 11  ASP 11  12  12  ASP ASP C . n 
C 1 12  GLY 12  13  13  GLY GLY C . n 
C 1 13  PRO 13  14  14  PRO PRO C . n 
C 1 14  VAL 14  15  15  VAL VAL C . n 
C 1 15  GLN 15  16  16  GLN GLN C . n 
C 1 16  GLY 16  17  17  GLY GLY C . n 
C 1 17  ILE 17  18  18  ILE ILE C . n 
C 1 18  ILE 18  19  19  ILE ILE C . n 
C 1 19  ASN 19  20  20  ASN ASN C . n 
C 1 20  PHE 20  21  21  PHE PHE C . n 
C 1 21  GLU 21  22  22  GLU GLU C . n 
C 1 22  GLN 22  23  23  GLN GLN C . n 
C 1 23  LYS 23  24  24  LYS LYS C . n 
C 1 24  GLU 24  25  25  GLU GLU C . n 
C 1 25  SER 25  26  26  SER SER C . n 
C 1 26  ASN 26  27  27  ASN ASN C . n 
C 1 27  GLY 27  28  28  GLY GLY C . n 
C 1 28  PRO 28  29  29  PRO PRO C . n 
C 1 29  VAL 29  30  30  VAL VAL C . n 
C 1 30  LYS 30  31  31  LYS LYS C . n 
C 1 31  VAL 31  32  32  VAL VAL C . n 
C 1 32  TRP 32  33  33  TRP TRP C . n 
C 1 33  GLY 33  34  34  GLY GLY C . n 
C 1 34  SER 34  35  35  SER SER C . n 
C 1 35  ILE 35  36  36  ILE ILE C . n 
C 1 36  LYS 36  37  37  LYS LYS C . n 
C 1 37  GLY 37  38  38  GLY GLY C . n 
C 1 38  LEU 38  39  39  LEU LEU C . n 
C 1 39  THR 39  40  40  THR THR C . n 
C 1 40  GLU 40  41  41  GLU GLU C . n 
C 1 41  GLY 41  42  42  GLY GLY C . n 
C 1 42  LEU 42  43  43  LEU LEU C . n 
C 1 43  HIS 43  44  44  HIS HIS C . n 
C 1 44  GLY 44  45  45  GLY GLY C . n 
C 1 45  PHE 45  46  46  PHE PHE C . n 
C 1 46  HIS 46  47  47  HIS HIS C . n 
C 1 47  VAL 47  48  48  VAL VAL C . n 
C 1 48  HIS 48  49  49  HIS HIS C . n 
C 1 49  GLU 49  50  50  GLU GLU C . n 
C 1 50  PHE 50  51  51  PHE PHE C . n 
C 1 51  GLY 51  52  52  GLY GLY C . n 
C 1 52  ASP 52  53  53  ASP ASP C . n 
C 1 53  ASN 53  54  54  ASN ASN C . n 
C 1 54  THR 54  55  55  THR THR C . n 
C 1 55  ALA 55  56  56  ALA ALA C . n 
C 1 56  GLY 56  57  57  GLY GLY C . n 
C 1 57  CYS 57  58  58  CYS CYS C . n 
C 1 58  THR 58  59  59  THR THR C . n 
C 1 59  SER 59  60  60  SER SER C . n 
C 1 60  ALA 60  61  61  ALA ALA C . n 
C 1 61  GLY 61  62  62  GLY GLY C . n 
C 1 62  PRO 62  63  63  PRO PRO C . n 
C 1 63  HIS 63  64  64  HIS HIS C . n 
C 1 64  PHE 64  65  65  PHE PHE C . n 
C 1 65  ASN 65  66  66  ASN ASN C . n 
C 1 66  PRO 66  67  67  PRO PRO C . n 
C 1 67  LEU 67  68  68  LEU LEU C . n 
C 1 68  SER 68  69  69  SER SER C . n 
C 1 69  ARG 69  70  70  ARG ARG C . n 
C 1 70  LYS 70  71  71  LYS LYS C . n 
C 1 71  HIS 71  72  72  HIS HIS C . n 
C 1 72  GLY 72  73  73  GLY GLY C . n 
C 1 73  GLY 73  74  74  GLY GLY C . n 
C 1 74  PRO 74  75  75  PRO PRO C . n 
C 1 75  LYS 75  76  76  LYS LYS C . n 
C 1 76  ASP 76  77  77  ASP ASP C . n 
C 1 77  GLU 77  78  78  GLU GLU C . n 
C 1 78  GLU 78  79  79  GLU GLU C . n 
C 1 79  ARG 79  80  80  ARG ARG C . n 
C 1 80  HIS 80  81  81  HIS HIS C . n 
C 1 81  VAL 81  82  82  VAL VAL C . n 
C 1 82  GLY 82  83  83  GLY GLY C . n 
C 1 83  ASP 83  84  84  ASP ASP C . n 
C 1 84  LEU 84  85  85  LEU LEU C . n 
C 1 85  GLY 85  86  86  GLY GLY C . n 
C 1 86  ASN 86  87  87  ASN ASN C . n 
C 1 87  VAL 87  88  88  VAL VAL C . n 
C 1 88  THR 88  89  89  THR THR C . n 
C 1 89  ALA 89  90  90  ALA ALA C . n 
C 1 90  ASP 90  91  91  ASP ASP C . n 
C 1 91  LYS 91  92  92  LYS LYS C . n 
C 1 92  ASP 92  93  93  ASP ASP C . n 
C 1 93  GLY 93  94  94  GLY GLY C . n 
C 1 94  VAL 94  95  95  VAL VAL C . n 
C 1 95  ALA 95  96  96  ALA ALA C . n 
C 1 96  ASP 96  97  97  ASP ASP C . n 
C 1 97  VAL 97  98  98  VAL VAL C . n 
C 1 98  SER 98  99  99  SER SER C . n 
C 1 99  ILE 99  100 100 ILE ILE C . n 
C 1 100 GLU 100 101 101 GLU GLU C . n 
C 1 101 ASP 101 102 102 ASP ASP C . n 
C 1 102 SER 102 103 103 SER SER C . n 
C 1 103 VAL 103 104 104 VAL VAL C . n 
C 1 104 ILE 104 105 105 ILE ILE C . n 
C 1 105 SER 105 106 106 SER SER C . n 
C 1 106 LEU 106 107 107 LEU LEU C . n 
C 1 107 SER 107 108 108 SER SER C . n 
C 1 108 GLY 108 109 109 GLY GLY C . n 
C 1 109 ASP 109 110 110 ASP ASP C . n 
C 1 110 HIS 110 111 111 HIS HIS C . n 
C 1 111 CYS 111 112 112 CYS CYS C . n 
C 1 112 ILE 112 113 113 ILE ILE C . n 
C 1 113 ILE 113 114 114 ILE ILE C . n 
C 1 114 GLY 114 115 115 GLY GLY C . n 
C 1 115 ARG 115 116 116 ARG ARG C . n 
C 1 116 THR 116 117 117 THR THR C . n 
C 1 117 LEU 117 118 118 LEU LEU C . n 
C 1 118 VAL 118 119 119 VAL VAL C . n 
C 1 119 VAL 119 120 120 VAL VAL C . n 
C 1 120 HIS 120 121 121 HIS HIS C . n 
C 1 121 GLU 121 122 122 GLU GLU C . n 
C 1 122 LYS 122 123 123 LYS LYS C . n 
C 1 123 ALA 123 124 124 ALA ALA C . n 
C 1 124 ASP 124 125 125 ASP ASP C . n 
C 1 125 ASP 125 126 126 ASP ASP C . n 
C 1 126 LEU 126 127 127 LEU LEU C . n 
C 1 127 GLY 127 128 128 GLY GLY C . n 
C 1 128 LYS 128 129 129 LYS LYS C . n 
C 1 129 GLY 129 130 130 GLY GLY C . n 
C 1 130 GLY 130 131 131 GLY GLY C . n 
C 1 131 ASN 131 132 132 ASN ASN C . n 
C 1 132 GLU 132 133 133 GLU GLU C . n 
C 1 133 GLU 133 134 134 GLU GLU C . n 
C 1 134 SER 134 135 135 SER SER C . n 
C 1 135 THR 135 136 136 THR THR C . n 
C 1 136 LYS 136 137 137 LYS LYS C . n 
C 1 137 THR 137 138 138 THR THR C . n 
C 1 138 GLY 138 139 139 GLY GLY C . n 
C 1 139 ASN 139 140 140 ASN ASN C . n 
C 1 140 ALA 140 141 141 ALA ALA C . n 
C 1 141 GLY 141 142 142 GLY GLY C . n 
C 1 142 SER 142 143 143 SER SER C . n 
C 1 143 ARG 143 144 144 ARG ARG C . n 
C 1 144 LEU 144 145 145 LEU LEU C . n 
C 1 145 ALA 145 146 146 ALA ALA C . n 
C 1 146 CYS 146 147 147 CYS CYS C . n 
C 1 147 GLY 147 148 148 GLY GLY C . n 
C 1 148 VAL 148 149 149 VAL VAL C . n 
C 1 149 ILE 149 150 150 ILE ILE C . n 
C 1 150 GLY 150 151 151 GLY GLY C . n 
C 1 151 ILE 151 152 152 ILE ILE C . n 
C 1 152 ALA 152 153 153 ALA ALA C . n 
C 1 153 GLN 153 154 154 GLN GLN C . n 
D 1 1   ALA 1   2   2   ALA ALA D . n 
D 1 2   THR 2   3   3   THR THR D . n 
D 1 3   LYS 3   4   4   LYS LYS D . n 
D 1 4   ALA 4   5   5   ALA ALA D . n 
D 1 5   VAL 5   6   6   VAL VAL D . n 
D 1 6   CYS 6   7   7   CYS CYS D . n 
D 1 7   VAL 7   8   8   VAL VAL D . n 
D 1 8   LEU 8   9   9   LEU LEU D . n 
D 1 9   LYS 9   10  10  LYS LYS D . n 
D 1 10  GLY 10  11  11  GLY GLY D . n 
D 1 11  ASP 11  12  12  ASP ASP D . n 
D 1 12  GLY 12  13  13  GLY GLY D . n 
D 1 13  PRO 13  14  14  PRO PRO D . n 
D 1 14  VAL 14  15  15  VAL VAL D . n 
D 1 15  GLN 15  16  16  GLN GLN D . n 
D 1 16  GLY 16  17  17  GLY GLY D . n 
D 1 17  ILE 17  18  18  ILE ILE D . n 
D 1 18  ILE 18  19  19  ILE ILE D . n 
D 1 19  ASN 19  20  20  ASN ASN D . n 
D 1 20  PHE 20  21  21  PHE PHE D . n 
D 1 21  GLU 21  22  22  GLU GLU D . n 
D 1 22  GLN 22  23  23  GLN GLN D . n 
D 1 23  LYS 23  24  24  LYS LYS D . n 
D 1 24  GLU 24  25  25  GLU GLU D . n 
D 1 25  SER 25  26  26  SER SER D . n 
D 1 26  ASN 26  27  27  ASN ASN D . n 
D 1 27  GLY 27  28  28  GLY GLY D . n 
D 1 28  PRO 28  29  29  PRO PRO D . n 
D 1 29  VAL 29  30  30  VAL VAL D . n 
D 1 30  LYS 30  31  31  LYS LYS D . n 
D 1 31  VAL 31  32  32  VAL VAL D . n 
D 1 32  TRP 32  33  33  TRP TRP D . n 
D 1 33  GLY 33  34  34  GLY GLY D . n 
D 1 34  SER 34  35  35  SER SER D . n 
D 1 35  ILE 35  36  36  ILE ILE D . n 
D 1 36  LYS 36  37  37  LYS LYS D . n 
D 1 37  GLY 37  38  38  GLY GLY D . n 
D 1 38  LEU 38  39  39  LEU LEU D . n 
D 1 39  THR 39  40  40  THR THR D . n 
D 1 40  GLU 40  41  41  GLU GLU D . n 
D 1 41  GLY 41  42  42  GLY GLY D . n 
D 1 42  LEU 42  43  43  LEU LEU D . n 
D 1 43  HIS 43  44  44  HIS HIS D . n 
D 1 44  GLY 44  45  45  GLY GLY D . n 
D 1 45  PHE 45  46  46  PHE PHE D . n 
D 1 46  HIS 46  47  47  HIS HIS D . n 
D 1 47  VAL 47  48  48  VAL VAL D . n 
D 1 48  HIS 48  49  49  HIS HIS D . n 
D 1 49  GLU 49  50  50  GLU GLU D . n 
D 1 50  PHE 50  51  51  PHE PHE D . n 
D 1 51  GLY 51  52  52  GLY GLY D . n 
D 1 52  ASP 52  53  53  ASP ASP D . n 
D 1 53  ASN 53  54  54  ASN ASN D . n 
D 1 54  THR 54  55  55  THR THR D . n 
D 1 55  ALA 55  56  56  ALA ALA D . n 
D 1 56  GLY 56  57  57  GLY GLY D . n 
D 1 57  CYS 57  58  58  CYS CYS D . n 
D 1 58  THR 58  59  59  THR THR D . n 
D 1 59  SER 59  60  60  SER SER D . n 
D 1 60  ALA 60  61  61  ALA ALA D . n 
D 1 61  GLY 61  62  62  GLY GLY D . n 
D 1 62  PRO 62  63  63  PRO PRO D . n 
D 1 63  HIS 63  64  64  HIS HIS D . n 
D 1 64  PHE 64  65  65  PHE PHE D . n 
D 1 65  ASN 65  66  66  ASN ASN D . n 
D 1 66  PRO 66  67  67  PRO PRO D . n 
D 1 67  LEU 67  68  68  LEU LEU D . n 
D 1 68  SER 68  69  69  SER SER D . n 
D 1 69  ARG 69  70  70  ARG ARG D . n 
D 1 70  LYS 70  71  71  LYS LYS D . n 
D 1 71  HIS 71  72  72  HIS HIS D . n 
D 1 72  GLY 72  73  73  GLY GLY D . n 
D 1 73  GLY 73  74  74  GLY GLY D . n 
D 1 74  PRO 74  75  75  PRO PRO D . n 
D 1 75  LYS 75  76  76  LYS LYS D . n 
D 1 76  ASP 76  77  77  ASP ASP D . n 
D 1 77  GLU 77  78  78  GLU GLU D . n 
D 1 78  GLU 78  79  79  GLU GLU D . n 
D 1 79  ARG 79  80  80  ARG ARG D . n 
D 1 80  HIS 80  81  81  HIS HIS D . n 
D 1 81  VAL 81  82  82  VAL VAL D . n 
D 1 82  GLY 82  83  83  GLY GLY D . n 
D 1 83  ASP 83  84  84  ASP ASP D . n 
D 1 84  LEU 84  85  85  LEU LEU D . n 
D 1 85  GLY 85  86  86  GLY GLY D . n 
D 1 86  ASN 86  87  87  ASN ASN D . n 
D 1 87  VAL 87  88  88  VAL VAL D . n 
D 1 88  THR 88  89  89  THR THR D . n 
D 1 89  ALA 89  90  90  ALA ALA D . n 
D 1 90  ASP 90  91  91  ASP ASP D . n 
D 1 91  LYS 91  92  92  LYS LYS D . n 
D 1 92  ASP 92  93  93  ASP ASP D . n 
D 1 93  GLY 93  94  94  GLY GLY D . n 
D 1 94  VAL 94  95  95  VAL VAL D . n 
D 1 95  ALA 95  96  96  ALA ALA D . n 
D 1 96  ASP 96  97  97  ASP ASP D . n 
D 1 97  VAL 97  98  98  VAL VAL D . n 
D 1 98  SER 98  99  99  SER SER D . n 
D 1 99  ILE 99  100 100 ILE ILE D . n 
D 1 100 GLU 100 101 101 GLU GLU D . n 
D 1 101 ASP 101 102 102 ASP ASP D . n 
D 1 102 SER 102 103 103 SER SER D . n 
D 1 103 VAL 103 104 104 VAL VAL D . n 
D 1 104 ILE 104 105 105 ILE ILE D . n 
D 1 105 SER 105 106 106 SER SER D . n 
D 1 106 LEU 106 107 107 LEU LEU D . n 
D 1 107 SER 107 108 108 SER SER D . n 
D 1 108 GLY 108 109 109 GLY GLY D . n 
D 1 109 ASP 109 110 110 ASP ASP D . n 
D 1 110 HIS 110 111 111 HIS HIS D . n 
D 1 111 CYS 111 112 112 CYS CYS D . n 
D 1 112 ILE 112 113 113 ILE ILE D . n 
D 1 113 ILE 113 114 114 ILE ILE D . n 
D 1 114 GLY 114 115 115 GLY GLY D . n 
D 1 115 ARG 115 116 116 ARG ARG D . n 
D 1 116 THR 116 117 117 THR THR D . n 
D 1 117 LEU 117 118 118 LEU LEU D . n 
D 1 118 VAL 118 119 119 VAL VAL D . n 
D 1 119 VAL 119 120 120 VAL VAL D . n 
D 1 120 HIS 120 121 121 HIS HIS D . n 
D 1 121 GLU 121 122 122 GLU GLU D . n 
D 1 122 LYS 122 123 123 LYS LYS D . n 
D 1 123 ALA 123 124 124 ALA ALA D . n 
D 1 124 ASP 124 125 125 ASP ASP D . n 
D 1 125 ASP 125 126 126 ASP ASP D . n 
D 1 126 LEU 126 127 127 LEU LEU D . n 
D 1 127 GLY 127 128 128 GLY GLY D . n 
D 1 128 LYS 128 129 129 LYS LYS D . n 
D 1 129 GLY 129 130 130 GLY GLY D . n 
D 1 130 GLY 130 131 131 GLY GLY D . n 
D 1 131 ASN 131 132 132 ASN ASN D . n 
D 1 132 GLU 132 133 133 GLU GLU D . n 
D 1 133 GLU 133 134 134 GLU GLU D . n 
D 1 134 SER 134 135 135 SER SER D . n 
D 1 135 THR 135 136 136 THR THR D . n 
D 1 136 LYS 136 137 137 LYS LYS D . n 
D 1 137 THR 137 138 138 THR THR D . n 
D 1 138 GLY 138 139 139 GLY GLY D . n 
D 1 139 ASN 139 140 140 ASN ASN D . n 
D 1 140 ALA 140 141 141 ALA ALA D . n 
D 1 141 GLY 141 142 142 GLY GLY D . n 
D 1 142 SER 142 143 143 SER SER D . n 
D 1 143 ARG 143 144 144 ARG ARG D . n 
D 1 144 LEU 144 145 145 LEU LEU D . n 
D 1 145 ALA 145 146 146 ALA ALA D . n 
D 1 146 CYS 146 147 147 CYS CYS D . n 
D 1 147 GLY 147 148 148 GLY GLY D . n 
D 1 148 VAL 148 149 149 VAL VAL D . n 
D 1 149 ILE 149 150 150 ILE ILE D . n 
D 1 150 GLY 150 151 151 GLY GLY D . n 
D 1 151 ILE 151 152 152 ILE ILE D . n 
D 1 152 ALA 152 153 153 ALA ALA D . n 
D 1 153 GLN 153 154 154 GLN GLN D . n 
E 1 1   ALA 1   2   2   ALA ALA E . n 
E 1 2   THR 2   3   3   THR THR E . n 
E 1 3   LYS 3   4   4   LYS LYS E . n 
E 1 4   ALA 4   5   5   ALA ALA E . n 
E 1 5   VAL 5   6   6   VAL VAL E . n 
E 1 6   CYS 6   7   7   CYS CYS E . n 
E 1 7   VAL 7   8   8   VAL VAL E . n 
E 1 8   LEU 8   9   9   LEU LEU E . n 
E 1 9   LYS 9   10  10  LYS LYS E . n 
E 1 10  GLY 10  11  11  GLY GLY E . n 
E 1 11  ASP 11  12  12  ASP ASP E . n 
E 1 12  GLY 12  13  13  GLY GLY E . n 
E 1 13  PRO 13  14  14  PRO PRO E . n 
E 1 14  VAL 14  15  15  VAL VAL E . n 
E 1 15  GLN 15  16  16  GLN GLN E . n 
E 1 16  GLY 16  17  17  GLY GLY E . n 
E 1 17  ILE 17  18  18  ILE ILE E . n 
E 1 18  ILE 18  19  19  ILE ILE E . n 
E 1 19  ASN 19  20  20  ASN ASN E . n 
E 1 20  PHE 20  21  21  PHE PHE E . n 
E 1 21  GLU 21  22  22  GLU GLU E . n 
E 1 22  GLN 22  23  23  GLN GLN E . n 
E 1 23  LYS 23  24  24  LYS LYS E . n 
E 1 24  GLU 24  25  25  GLU GLU E . n 
E 1 25  SER 25  26  26  SER SER E . n 
E 1 26  ASN 26  27  27  ASN ASN E . n 
E 1 27  GLY 27  28  28  GLY GLY E . n 
E 1 28  PRO 28  29  29  PRO PRO E . n 
E 1 29  VAL 29  30  30  VAL VAL E . n 
E 1 30  LYS 30  31  31  LYS LYS E . n 
E 1 31  VAL 31  32  32  VAL VAL E . n 
E 1 32  TRP 32  33  33  TRP TRP E . n 
E 1 33  GLY 33  34  34  GLY GLY E . n 
E 1 34  SER 34  35  35  SER SER E . n 
E 1 35  ILE 35  36  36  ILE ILE E . n 
E 1 36  LYS 36  37  37  LYS LYS E . n 
E 1 37  GLY 37  38  38  GLY GLY E . n 
E 1 38  LEU 38  39  39  LEU LEU E . n 
E 1 39  THR 39  40  40  THR THR E . n 
E 1 40  GLU 40  41  41  GLU GLU E . n 
E 1 41  GLY 41  42  42  GLY GLY E . n 
E 1 42  LEU 42  43  43  LEU LEU E . n 
E 1 43  HIS 43  44  44  HIS HIS E . n 
E 1 44  GLY 44  45  45  GLY GLY E . n 
E 1 45  PHE 45  46  46  PHE PHE E . n 
E 1 46  HIS 46  47  47  HIS HIS E . n 
E 1 47  VAL 47  48  48  VAL VAL E . n 
E 1 48  HIS 48  49  49  HIS HIS E . n 
E 1 49  GLU 49  50  50  GLU GLU E . n 
E 1 50  PHE 50  51  51  PHE PHE E . n 
E 1 51  GLY 51  52  52  GLY GLY E . n 
E 1 52  ASP 52  53  53  ASP ASP E . n 
E 1 53  ASN 53  54  54  ASN ASN E . n 
E 1 54  THR 54  55  55  THR THR E . n 
E 1 55  ALA 55  56  56  ALA ALA E . n 
E 1 56  GLY 56  57  57  GLY GLY E . n 
E 1 57  CYS 57  58  58  CYS CYS E . n 
E 1 58  THR 58  59  59  THR THR E . n 
E 1 59  SER 59  60  60  SER SER E . n 
E 1 60  ALA 60  61  61  ALA ALA E . n 
E 1 61  GLY 61  62  62  GLY GLY E . n 
E 1 62  PRO 62  63  63  PRO PRO E . n 
E 1 63  HIS 63  64  64  HIS HIS E . n 
E 1 64  PHE 64  65  65  PHE PHE E . n 
E 1 65  ASN 65  66  66  ASN ASN E . n 
E 1 66  PRO 66  67  67  PRO PRO E . n 
E 1 67  LEU 67  68  68  LEU LEU E . n 
E 1 68  SER 68  69  69  SER SER E . n 
E 1 69  ARG 69  70  70  ARG ARG E . n 
E 1 70  LYS 70  71  71  LYS LYS E . n 
E 1 71  HIS 71  72  72  HIS HIS E . n 
E 1 72  GLY 72  73  73  GLY GLY E . n 
E 1 73  GLY 73  74  74  GLY GLY E . n 
E 1 74  PRO 74  75  75  PRO PRO E . n 
E 1 75  LYS 75  76  76  LYS LYS E . n 
E 1 76  ASP 76  77  77  ASP ASP E . n 
E 1 77  GLU 77  78  78  GLU GLU E . n 
E 1 78  GLU 78  79  79  GLU GLU E . n 
E 1 79  ARG 79  80  80  ARG ARG E . n 
E 1 80  HIS 80  81  81  HIS HIS E . n 
E 1 81  VAL 81  82  82  VAL VAL E . n 
E 1 82  GLY 82  83  83  GLY GLY E . n 
E 1 83  ASP 83  84  84  ASP ASP E . n 
E 1 84  LEU 84  85  85  LEU LEU E . n 
E 1 85  GLY 85  86  86  GLY GLY E . n 
E 1 86  ASN 86  87  87  ASN ASN E . n 
E 1 87  VAL 87  88  88  VAL VAL E . n 
E 1 88  THR 88  89  89  THR THR E . n 
E 1 89  ALA 89  90  90  ALA ALA E . n 
E 1 90  ASP 90  91  91  ASP ASP E . n 
E 1 91  LYS 91  92  92  LYS LYS E . n 
E 1 92  ASP 92  93  93  ASP ASP E . n 
E 1 93  GLY 93  94  94  GLY GLY E . n 
E 1 94  VAL 94  95  95  VAL ALA E . n 
E 1 95  ALA 95  96  96  ALA ALA E . n 
E 1 96  ASP 96  97  97  ASP ASP E . n 
E 1 97  VAL 97  98  98  VAL VAL E . n 
E 1 98  SER 98  99  99  SER SER E . n 
E 1 99  ILE 99  100 100 ILE ILE E . n 
E 1 100 GLU 100 101 101 GLU GLU E . n 
E 1 101 ASP 101 102 102 ASP ASP E . n 
E 1 102 SER 102 103 103 SER SER E . n 
E 1 103 VAL 103 104 104 VAL VAL E . n 
E 1 104 ILE 104 105 105 ILE ILE E . n 
E 1 105 SER 105 106 106 SER SER E . n 
E 1 106 LEU 106 107 107 LEU LEU E . n 
E 1 107 SER 107 108 108 SER SER E . n 
E 1 108 GLY 108 109 109 GLY GLY E . n 
E 1 109 ASP 109 110 110 ASP ASP E . n 
E 1 110 HIS 110 111 111 HIS HIS E . n 
E 1 111 CYS 111 112 112 CYS CYS E . n 
E 1 112 ILE 112 113 113 ILE ILE E . n 
E 1 113 ILE 113 114 114 ILE ILE E . n 
E 1 114 GLY 114 115 115 GLY GLY E . n 
E 1 115 ARG 115 116 116 ARG ARG E . n 
E 1 116 THR 116 117 117 THR THR E . n 
E 1 117 LEU 117 118 118 LEU LEU E . n 
E 1 118 VAL 118 119 119 VAL VAL E . n 
E 1 119 VAL 119 120 120 VAL VAL E . n 
E 1 120 HIS 120 121 121 HIS HIS E . n 
E 1 121 GLU 121 122 122 GLU GLU E . n 
E 1 122 LYS 122 123 123 LYS LYS E . n 
E 1 123 ALA 123 124 124 ALA ALA E . n 
E 1 124 ASP 124 125 125 ASP ASP E . n 
E 1 125 ASP 125 126 126 ASP ASP E . n 
E 1 126 LEU 126 127 127 LEU LEU E . n 
E 1 127 GLY 127 128 128 GLY GLY E . n 
E 1 128 LYS 128 129 129 LYS LYS E . n 
E 1 129 GLY 129 130 130 GLY GLY E . n 
E 1 130 GLY 130 131 131 GLY GLY E . n 
E 1 131 ASN 131 132 132 ASN ASN E . n 
E 1 132 GLU 132 133 133 GLU GLU E . n 
E 1 133 GLU 133 134 134 GLU GLU E . n 
E 1 134 SER 134 135 135 SER SER E . n 
E 1 135 THR 135 136 136 THR THR E . n 
E 1 136 LYS 136 137 137 LYS LYS E . n 
E 1 137 THR 137 138 138 THR THR E . n 
E 1 138 GLY 138 139 139 GLY GLY E . n 
E 1 139 ASN 139 140 140 ASN ASN E . n 
E 1 140 ALA 140 141 141 ALA ALA E . n 
E 1 141 GLY 141 142 142 GLY GLY E . n 
E 1 142 SER 142 143 143 SER SER E . n 
E 1 143 ARG 143 144 144 ARG ARG E . n 
E 1 144 LEU 144 145 145 LEU LEU E . n 
E 1 145 ALA 145 146 146 ALA ALA E . n 
E 1 146 CYS 146 147 147 CYS CYS E . n 
E 1 147 GLY 147 148 148 GLY GLY E . n 
E 1 148 VAL 148 149 149 VAL VAL E . n 
E 1 149 ILE 149 150 150 ILE ILE E . n 
E 1 150 GLY 150 151 151 GLY GLY E . n 
E 1 151 ILE 151 152 152 ILE ILE E . n 
E 1 152 ALA 152 153 153 ALA ALA E . n 
E 1 153 GLN 153 154 154 GLN GLN E . n 
F 1 1   ALA 1   2   2   ALA ALA F . n 
F 1 2   THR 2   3   3   THR THR F . n 
F 1 3   LYS 3   4   4   LYS LYS F . n 
F 1 4   ALA 4   5   5   ALA ALA F . n 
F 1 5   VAL 5   6   6   VAL VAL F . n 
F 1 6   CYS 6   7   7   CYS CYS F . n 
F 1 7   VAL 7   8   8   VAL VAL F . n 
F 1 8   LEU 8   9   9   LEU LEU F . n 
F 1 9   LYS 9   10  10  LYS LYS F . n 
F 1 10  GLY 10  11  11  GLY GLY F . n 
F 1 11  ASP 11  12  12  ASP ASP F . n 
F 1 12  GLY 12  13  13  GLY GLY F . n 
F 1 13  PRO 13  14  14  PRO PRO F . n 
F 1 14  VAL 14  15  15  VAL VAL F . n 
F 1 15  GLN 15  16  16  GLN GLN F . n 
F 1 16  GLY 16  17  17  GLY GLY F . n 
F 1 17  ILE 17  18  18  ILE ILE F . n 
F 1 18  ILE 18  19  19  ILE ILE F . n 
F 1 19  ASN 19  20  20  ASN ASN F . n 
F 1 20  PHE 20  21  21  PHE PHE F . n 
F 1 21  GLU 21  22  22  GLU GLU F . n 
F 1 22  GLN 22  23  23  GLN GLN F . n 
F 1 23  LYS 23  24  24  LYS LYS F . n 
F 1 24  GLU 24  25  25  GLU GLU F . n 
F 1 25  SER 25  26  26  SER SER F . n 
F 1 26  ASN 26  27  27  ASN ASN F . n 
F 1 27  GLY 27  28  28  GLY GLY F . n 
F 1 28  PRO 28  29  29  PRO PRO F . n 
F 1 29  VAL 29  30  30  VAL VAL F . n 
F 1 30  LYS 30  31  31  LYS LYS F . n 
F 1 31  VAL 31  32  32  VAL VAL F . n 
F 1 32  TRP 32  33  33  TRP TRP F . n 
F 1 33  GLY 33  34  34  GLY GLY F . n 
F 1 34  SER 34  35  35  SER SER F . n 
F 1 35  ILE 35  36  36  ILE ILE F . n 
F 1 36  LYS 36  37  37  LYS LYS F . n 
F 1 37  GLY 37  38  38  GLY GLY F . n 
F 1 38  LEU 38  39  39  LEU LEU F . n 
F 1 39  THR 39  40  40  THR THR F . n 
F 1 40  GLU 40  41  41  GLU GLU F . n 
F 1 41  GLY 41  42  42  GLY GLY F . n 
F 1 42  LEU 42  43  43  LEU LEU F . n 
F 1 43  HIS 43  44  44  HIS HIS F . n 
F 1 44  GLY 44  45  45  GLY GLY F . n 
F 1 45  PHE 45  46  46  PHE PHE F . n 
F 1 46  HIS 46  47  47  HIS HIS F . n 
F 1 47  VAL 47  48  48  VAL VAL F . n 
F 1 48  HIS 48  49  49  HIS HIS F . n 
F 1 49  GLU 49  50  50  GLU GLU F . n 
F 1 50  PHE 50  51  51  PHE PHE F . n 
F 1 51  GLY 51  52  52  GLY GLY F . n 
F 1 52  ASP 52  53  53  ASP ASP F . n 
F 1 53  ASN 53  54  54  ASN ASN F . n 
F 1 54  THR 54  55  55  THR THR F . n 
F 1 55  ALA 55  56  56  ALA ALA F . n 
F 1 56  GLY 56  57  57  GLY GLY F . n 
F 1 57  CYS 57  58  58  CYS CYS F . n 
F 1 58  THR 58  59  59  THR THR F . n 
F 1 59  SER 59  60  60  SER SER F . n 
F 1 60  ALA 60  61  61  ALA ALA F . n 
F 1 61  GLY 61  62  62  GLY GLY F . n 
F 1 62  PRO 62  63  63  PRO PRO F . n 
F 1 63  HIS 63  64  64  HIS HIS F . n 
F 1 64  PHE 64  65  65  PHE PHE F . n 
F 1 65  ASN 65  66  66  ASN ASN F . n 
F 1 66  PRO 66  67  67  PRO PRO F . n 
F 1 67  LEU 67  68  68  LEU LEU F . n 
F 1 68  SER 68  69  69  SER SER F . n 
F 1 69  ARG 69  70  70  ARG ARG F . n 
F 1 70  LYS 70  71  71  LYS LYS F . n 
F 1 71  HIS 71  72  72  HIS HIS F . n 
F 1 72  GLY 72  73  73  GLY GLY F . n 
F 1 73  GLY 73  74  74  GLY GLY F . n 
F 1 74  PRO 74  75  75  PRO PRO F . n 
F 1 75  LYS 75  76  76  LYS LYS F . n 
F 1 76  ASP 76  77  77  ASP ASP F . n 
F 1 77  GLU 77  78  78  GLU GLU F . n 
F 1 78  GLU 78  79  79  GLU GLU F . n 
F 1 79  ARG 79  80  80  ARG ARG F . n 
F 1 80  HIS 80  81  81  HIS HIS F . n 
F 1 81  VAL 81  82  82  VAL VAL F . n 
F 1 82  GLY 82  83  83  GLY GLY F . n 
F 1 83  ASP 83  84  84  ASP ASP F . n 
F 1 84  LEU 84  85  85  LEU LEU F . n 
F 1 85  GLY 85  86  86  GLY GLY F . n 
F 1 86  ASN 86  87  87  ASN ASN F . n 
F 1 87  VAL 87  88  88  VAL VAL F . n 
F 1 88  THR 88  89  89  THR THR F . n 
F 1 89  ALA 89  90  90  ALA ALA F . n 
F 1 90  ASP 90  91  91  ASP ASP F . n 
F 1 91  LYS 91  92  92  LYS LYS F . n 
F 1 92  ASP 92  93  93  ASP ASP F . n 
F 1 93  GLY 93  94  94  GLY GLY F . n 
F 1 94  VAL 94  95  95  VAL VAL F . n 
F 1 95  ALA 95  96  96  ALA ALA F . n 
F 1 96  ASP 96  97  97  ASP ASP F . n 
F 1 97  VAL 97  98  98  VAL VAL F . n 
F 1 98  SER 98  99  99  SER SER F . n 
F 1 99  ILE 99  100 100 ILE ILE F . n 
F 1 100 GLU 100 101 101 GLU GLU F . n 
F 1 101 ASP 101 102 102 ASP ASP F . n 
F 1 102 SER 102 103 103 SER SER F . n 
F 1 103 VAL 103 104 104 VAL VAL F . n 
F 1 104 ILE 104 105 105 ILE ILE F . n 
F 1 105 SER 105 106 106 SER SER F . n 
F 1 106 LEU 106 107 107 LEU LEU F . n 
F 1 107 SER 107 108 108 SER SER F . n 
F 1 108 GLY 108 109 109 GLY GLY F . n 
F 1 109 ASP 109 110 110 ASP ASP F . n 
F 1 110 HIS 110 111 111 HIS HIS F . n 
F 1 111 CYS 111 112 112 CYS CYS F . n 
F 1 112 ILE 112 113 113 ILE ILE F . n 
F 1 113 ILE 113 114 114 ILE ILE F . n 
F 1 114 GLY 114 115 115 GLY GLY F . n 
F 1 115 ARG 115 116 116 ARG ARG F . n 
F 1 116 THR 116 117 117 THR THR F . n 
F 1 117 LEU 117 118 118 LEU LEU F . n 
F 1 118 VAL 118 119 119 VAL VAL F . n 
F 1 119 VAL 119 120 120 VAL VAL F . n 
F 1 120 HIS 120 121 121 HIS HIS F . n 
F 1 121 GLU 121 122 122 GLU GLU F . n 
F 1 122 LYS 122 123 123 LYS LYS F . n 
F 1 123 ALA 123 124 124 ALA ALA F . n 
F 1 124 ASP 124 125 125 ASP ASP F . n 
F 1 125 ASP 125 126 126 ASP ASP F . n 
F 1 126 LEU 126 127 127 LEU LEU F . n 
F 1 127 GLY 127 128 128 GLY GLY F . n 
F 1 128 LYS 128 129 129 LYS LYS F . n 
F 1 129 GLY 129 130 130 GLY GLY F . n 
F 1 130 GLY 130 131 131 GLY GLY F . n 
F 1 131 ASN 131 132 132 ASN ASN F . n 
F 1 132 GLU 132 133 133 GLU GLU F . n 
F 1 133 GLU 133 134 134 GLU GLU F . n 
F 1 134 SER 134 135 135 SER SER F . n 
F 1 135 THR 135 136 136 THR THR F . n 
F 1 136 LYS 136 137 137 LYS LYS F . n 
F 1 137 THR 137 138 138 THR THR F . n 
F 1 138 GLY 138 139 139 GLY GLY F . n 
F 1 139 ASN 139 140 140 ASN ASN F . n 
F 1 140 ALA 140 141 141 ALA ALA F . n 
F 1 141 GLY 141 142 142 GLY GLY F . n 
F 1 142 SER 142 143 143 SER SER F . n 
F 1 143 ARG 143 144 144 ARG ARG F . n 
F 1 144 LEU 144 145 145 LEU LEU F . n 
F 1 145 ALA 145 146 146 ALA ALA F . n 
F 1 146 CYS 146 147 147 CYS CYS F . n 
F 1 147 GLY 147 148 148 GLY GLY F . n 
F 1 148 VAL 148 149 149 VAL VAL F . n 
F 1 149 ILE 149 150 150 ILE ILE F . n 
F 1 150 GLY 150 151 151 GLY GLY F . n 
F 1 151 ILE 151 152 152 ILE ILE F . n 
F 1 152 ALA 152 153 153 ALA ALA F . n 
F 1 153 GLN 153 154 154 GLN GLN F . n 
G 1 1   ALA 1   2   2   ALA ALA G . n 
G 1 2   THR 2   3   3   THR THR G . n 
G 1 3   LYS 3   4   4   LYS LYS G . n 
G 1 4   ALA 4   5   5   ALA ALA G . n 
G 1 5   VAL 5   6   6   VAL VAL G . n 
G 1 6   CYS 6   7   7   CYS CYS G . n 
G 1 7   VAL 7   8   8   VAL VAL G . n 
G 1 8   LEU 8   9   9   LEU LEU G . n 
G 1 9   LYS 9   10  10  LYS LYS G . n 
G 1 10  GLY 10  11  11  GLY GLY G . n 
G 1 11  ASP 11  12  12  ASP ASP G . n 
G 1 12  GLY 12  13  13  GLY GLY G . n 
G 1 13  PRO 13  14  14  PRO PRO G . n 
G 1 14  VAL 14  15  15  VAL VAL G . n 
G 1 15  GLN 15  16  16  GLN GLN G . n 
G 1 16  GLY 16  17  17  GLY GLY G . n 
G 1 17  ILE 17  18  18  ILE ILE G . n 
G 1 18  ILE 18  19  19  ILE ILE G . n 
G 1 19  ASN 19  20  20  ASN ASN G . n 
G 1 20  PHE 20  21  21  PHE PHE G . n 
G 1 21  GLU 21  22  22  GLU GLU G . n 
G 1 22  GLN 22  23  23  GLN GLN G . n 
G 1 23  LYS 23  24  24  LYS LYS G . n 
G 1 24  GLU 24  25  25  GLU GLU G . n 
G 1 25  SER 25  26  26  SER SER G . n 
G 1 26  ASN 26  27  27  ASN ASN G . n 
G 1 27  GLY 27  28  28  GLY GLY G . n 
G 1 28  PRO 28  29  29  PRO PRO G . n 
G 1 29  VAL 29  30  30  VAL VAL G . n 
G 1 30  LYS 30  31  31  LYS LYS G . n 
G 1 31  VAL 31  32  32  VAL VAL G . n 
G 1 32  TRP 32  33  33  TRP TRP G . n 
G 1 33  GLY 33  34  34  GLY GLY G . n 
G 1 34  SER 34  35  35  SER SER G . n 
G 1 35  ILE 35  36  36  ILE ILE G . n 
G 1 36  LYS 36  37  37  LYS LYS G . n 
G 1 37  GLY 37  38  38  GLY GLY G . n 
G 1 38  LEU 38  39  39  LEU LEU G . n 
G 1 39  THR 39  40  40  THR THR G . n 
G 1 40  GLU 40  41  41  GLU GLU G . n 
G 1 41  GLY 41  42  42  GLY GLY G . n 
G 1 42  LEU 42  43  43  LEU LEU G . n 
G 1 43  HIS 43  44  44  HIS HIS G . n 
G 1 44  GLY 44  45  45  GLY GLY G . n 
G 1 45  PHE 45  46  46  PHE PHE G . n 
G 1 46  HIS 46  47  47  HIS HIS G . n 
G 1 47  VAL 47  48  48  VAL VAL G . n 
G 1 48  HIS 48  49  49  HIS HIS G . n 
G 1 49  GLU 49  50  50  GLU GLU G . n 
G 1 50  PHE 50  51  51  PHE PHE G . n 
G 1 51  GLY 51  52  52  GLY GLY G . n 
G 1 52  ASP 52  53  53  ASP ASP G . n 
G 1 53  ASN 53  54  54  ASN ASN G . n 
G 1 54  THR 54  55  55  THR THR G . n 
G 1 55  ALA 55  56  56  ALA ALA G . n 
G 1 56  GLY 56  57  57  GLY GLY G . n 
G 1 57  CYS 57  58  58  CYS CYS G . n 
G 1 58  THR 58  59  59  THR THR G . n 
G 1 59  SER 59  60  60  SER SER G . n 
G 1 60  ALA 60  61  61  ALA ALA G . n 
G 1 61  GLY 61  62  62  GLY GLY G . n 
G 1 62  PRO 62  63  63  PRO PRO G . n 
G 1 63  HIS 63  64  64  HIS HIS G . n 
G 1 64  PHE 64  65  65  PHE PHE G . n 
G 1 65  ASN 65  66  66  ASN ASN G . n 
G 1 66  PRO 66  67  67  PRO PRO G . n 
G 1 67  LEU 67  68  68  LEU LEU G . n 
G 1 68  SER 68  69  69  SER SER G . n 
G 1 69  ARG 69  70  70  ARG ARG G . n 
G 1 70  LYS 70  71  71  LYS LYS G . n 
G 1 71  HIS 71  72  72  HIS HIS G . n 
G 1 72  GLY 72  73  73  GLY GLY G . n 
G 1 73  GLY 73  74  74  GLY GLY G . n 
G 1 74  PRO 74  75  75  PRO PRO G . n 
G 1 75  LYS 75  76  76  LYS LYS G . n 
G 1 76  ASP 76  77  77  ASP ASP G . n 
G 1 77  GLU 77  78  78  GLU GLU G . n 
G 1 78  GLU 78  79  79  GLU GLU G . n 
G 1 79  ARG 79  80  80  ARG ARG G . n 
G 1 80  HIS 80  81  81  HIS HIS G . n 
G 1 81  VAL 81  82  82  VAL VAL G . n 
G 1 82  GLY 82  83  83  GLY GLY G . n 
G 1 83  ASP 83  84  84  ASP ASP G . n 
G 1 84  LEU 84  85  85  LEU LEU G . n 
G 1 85  GLY 85  86  86  GLY GLY G . n 
G 1 86  ASN 86  87  87  ASN ASN G . n 
G 1 87  VAL 87  88  88  VAL VAL G . n 
G 1 88  THR 88  89  89  THR THR G . n 
G 1 89  ALA 89  90  90  ALA ALA G . n 
G 1 90  ASP 90  91  91  ASP ASP G . n 
G 1 91  LYS 91  92  92  LYS LYS G . n 
G 1 92  ASP 92  93  93  ASP ASP G . n 
G 1 93  GLY 93  94  94  GLY GLY G . n 
G 1 94  VAL 94  95  95  VAL VAL G . n 
G 1 95  ALA 95  96  96  ALA ALA G . n 
G 1 96  ASP 96  97  97  ASP ASP G . n 
G 1 97  VAL 97  98  98  VAL VAL G . n 
G 1 98  SER 98  99  99  SER SER G . n 
G 1 99  ILE 99  100 100 ILE ILE G . n 
G 1 100 GLU 100 101 101 GLU GLU G . n 
G 1 101 ASP 101 102 102 ASP ASP G . n 
G 1 102 SER 102 103 103 SER SER G . n 
G 1 103 VAL 103 104 104 VAL VAL G . n 
G 1 104 ILE 104 105 105 ILE ILE G . n 
G 1 105 SER 105 106 106 SER SER G . n 
G 1 106 LEU 106 107 107 LEU LEU G . n 
G 1 107 SER 107 108 108 SER SER G . n 
G 1 108 GLY 108 109 109 GLY GLY G . n 
G 1 109 ASP 109 110 110 ASP ASP G . n 
G 1 110 HIS 110 111 111 HIS HIS G . n 
G 1 111 CYS 111 112 112 CYS CYS G . n 
G 1 112 ILE 112 113 113 ILE ILE G . n 
G 1 113 ILE 113 114 114 ILE ILE G . n 
G 1 114 GLY 114 115 115 GLY GLY G . n 
G 1 115 ARG 115 116 116 ARG ARG G . n 
G 1 116 THR 116 117 117 THR THR G . n 
G 1 117 LEU 117 118 118 LEU LEU G . n 
G 1 118 VAL 118 119 119 VAL VAL G . n 
G 1 119 VAL 119 120 120 VAL VAL G . n 
G 1 120 HIS 120 121 121 HIS HIS G . n 
G 1 121 GLU 121 122 122 GLU GLU G . n 
G 1 122 LYS 122 123 123 LYS LYS G . n 
G 1 123 ALA 123 124 124 ALA ALA G . n 
G 1 124 ASP 124 125 125 ASP ASP G . n 
G 1 125 ASP 125 126 126 ASP ASP G . n 
G 1 126 LEU 126 127 127 LEU LEU G . n 
G 1 127 GLY 127 128 128 GLY GLY G . n 
G 1 128 LYS 128 129 129 LYS LYS G . n 
G 1 129 GLY 129 130 130 GLY GLY G . n 
G 1 130 GLY 130 131 131 GLY GLY G . n 
G 1 131 ASN 131 132 132 ASN ASN G . n 
G 1 132 GLU 132 133 133 GLU GLU G . n 
G 1 133 GLU 133 134 134 GLU GLU G . n 
G 1 134 SER 134 135 135 SER SER G . n 
G 1 135 THR 135 136 136 THR THR G . n 
G 1 136 LYS 136 137 137 LYS LYS G . n 
G 1 137 THR 137 138 138 THR THR G . n 
G 1 138 GLY 138 139 139 GLY GLY G . n 
G 1 139 ASN 139 140 140 ASN ASN G . n 
G 1 140 ALA 140 141 141 ALA ALA G . n 
G 1 141 GLY 141 142 142 GLY GLY G . n 
G 1 142 SER 142 143 143 SER SER G . n 
G 1 143 ARG 143 144 144 ARG ARG G . n 
G 1 144 LEU 144 145 145 LEU LEU G . n 
G 1 145 ALA 145 146 146 ALA ALA G . n 
G 1 146 CYS 146 147 147 CYS CYS G . n 
G 1 147 GLY 147 148 148 GLY GLY G . n 
G 1 148 VAL 148 149 149 VAL VAL G . n 
G 1 149 ILE 149 150 150 ILE ILE G . n 
G 1 150 GLY 150 151 151 GLY GLY G . n 
G 1 151 ILE 151 152 152 ILE ILE G . n 
G 1 152 ALA 152 153 153 ALA ALA G . n 
G 1 153 GLN 153 154 154 GLN GLN G . n 
H 1 1   ALA 1   2   2   ALA ALA H . n 
H 1 2   THR 2   3   3   THR THR H . n 
H 1 3   LYS 3   4   4   LYS LYS H . n 
H 1 4   ALA 4   5   5   ALA ALA H . n 
H 1 5   VAL 5   6   6   VAL VAL H . n 
H 1 6   CYS 6   7   7   CYS CYS H . n 
H 1 7   VAL 7   8   8   VAL VAL H . n 
H 1 8   LEU 8   9   9   LEU LEU H . n 
H 1 9   LYS 9   10  10  LYS LYS H . n 
H 1 10  GLY 10  11  11  GLY GLY H . n 
H 1 11  ASP 11  12  12  ASP ASP H . n 
H 1 12  GLY 12  13  13  GLY GLY H . n 
H 1 13  PRO 13  14  14  PRO PRO H . n 
H 1 14  VAL 14  15  15  VAL VAL H . n 
H 1 15  GLN 15  16  16  GLN GLN H . n 
H 1 16  GLY 16  17  17  GLY GLY H . n 
H 1 17  ILE 17  18  18  ILE ILE H . n 
H 1 18  ILE 18  19  19  ILE ILE H . n 
H 1 19  ASN 19  20  20  ASN ASN H . n 
H 1 20  PHE 20  21  21  PHE PHE H . n 
H 1 21  GLU 21  22  22  GLU GLU H . n 
H 1 22  GLN 22  23  23  GLN GLN H . n 
H 1 23  LYS 23  24  24  LYS LYS H . n 
H 1 24  GLU 24  25  25  GLU GLU H . n 
H 1 25  SER 25  26  26  SER SER H . n 
H 1 26  ASN 26  27  27  ASN ASN H . n 
H 1 27  GLY 27  28  28  GLY GLY H . n 
H 1 28  PRO 28  29  29  PRO PRO H . n 
H 1 29  VAL 29  30  30  VAL VAL H . n 
H 1 30  LYS 30  31  31  LYS LYS H . n 
H 1 31  VAL 31  32  32  VAL VAL H . n 
H 1 32  TRP 32  33  33  TRP TRP H . n 
H 1 33  GLY 33  34  34  GLY GLY H . n 
H 1 34  SER 34  35  35  SER SER H . n 
H 1 35  ILE 35  36  36  ILE ILE H . n 
H 1 36  LYS 36  37  37  LYS LYS H . n 
H 1 37  GLY 37  38  38  GLY GLY H . n 
H 1 38  LEU 38  39  39  LEU LEU H . n 
H 1 39  THR 39  40  40  THR THR H . n 
H 1 40  GLU 40  41  41  GLU GLU H . n 
H 1 41  GLY 41  42  42  GLY GLY H . n 
H 1 42  LEU 42  43  43  LEU LEU H . n 
H 1 43  HIS 43  44  44  HIS HIS H . n 
H 1 44  GLY 44  45  45  GLY GLY H . n 
H 1 45  PHE 45  46  46  PHE PHE H . n 
H 1 46  HIS 46  47  47  HIS HIS H . n 
H 1 47  VAL 47  48  48  VAL VAL H . n 
H 1 48  HIS 48  49  49  HIS HIS H . n 
H 1 49  GLU 49  50  50  GLU GLU H . n 
H 1 50  PHE 50  51  51  PHE PHE H . n 
H 1 51  GLY 51  52  52  GLY GLY H . n 
H 1 52  ASP 52  53  53  ASP ASP H . n 
H 1 53  ASN 53  54  54  ASN ASN H . n 
H 1 54  THR 54  55  55  THR THR H . n 
H 1 55  ALA 55  56  56  ALA ALA H . n 
H 1 56  GLY 56  57  57  GLY GLY H . n 
H 1 57  CYS 57  58  58  CYS CYS H . n 
H 1 58  THR 58  59  59  THR THR H . n 
H 1 59  SER 59  60  60  SER SER H . n 
H 1 60  ALA 60  61  61  ALA ALA H . n 
H 1 61  GLY 61  62  62  GLY GLY H . n 
H 1 62  PRO 62  63  63  PRO PRO H . n 
H 1 63  HIS 63  64  64  HIS HIS H . n 
H 1 64  PHE 64  65  65  PHE PHE H . n 
H 1 65  ASN 65  66  66  ASN ASN H . n 
H 1 66  PRO 66  67  67  PRO PRO H . n 
H 1 67  LEU 67  68  68  LEU LEU H . n 
H 1 68  SER 68  69  69  SER SER H . n 
H 1 69  ARG 69  70  70  ARG ARG H . n 
H 1 70  LYS 70  71  71  LYS LYS H . n 
H 1 71  HIS 71  72  72  HIS HIS H . n 
H 1 72  GLY 72  73  73  GLY GLY H . n 
H 1 73  GLY 73  74  74  GLY GLY H . n 
H 1 74  PRO 74  75  75  PRO PRO H . n 
H 1 75  LYS 75  76  76  LYS LYS H . n 
H 1 76  ASP 76  77  77  ASP ASP H . n 
H 1 77  GLU 77  78  78  GLU GLU H . n 
H 1 78  GLU 78  79  79  GLU GLU H . n 
H 1 79  ARG 79  80  80  ARG ARG H . n 
H 1 80  HIS 80  81  81  HIS HIS H . n 
H 1 81  VAL 81  82  82  VAL VAL H . n 
H 1 82  GLY 82  83  83  GLY GLY H . n 
H 1 83  ASP 83  84  84  ASP ASP H . n 
H 1 84  LEU 84  85  85  LEU LEU H . n 
H 1 85  GLY 85  86  86  GLY GLY H . n 
H 1 86  ASN 86  87  87  ASN ASN H . n 
H 1 87  VAL 87  88  88  VAL VAL H . n 
H 1 88  THR 88  89  89  THR THR H . n 
H 1 89  ALA 89  90  90  ALA ALA H . n 
H 1 90  ASP 90  91  91  ASP ASP H . n 
H 1 91  LYS 91  92  92  LYS LYS H . n 
H 1 92  ASP 92  93  93  ASP ASP H . n 
H 1 93  GLY 93  94  94  GLY GLY H . n 
H 1 94  VAL 94  95  95  VAL VAL H . n 
H 1 95  ALA 95  96  96  ALA ALA H . n 
H 1 96  ASP 96  97  97  ASP ASP H . n 
H 1 97  VAL 97  98  98  VAL VAL H . n 
H 1 98  SER 98  99  99  SER SER H . n 
H 1 99  ILE 99  100 100 ILE ILE H . n 
H 1 100 GLU 100 101 101 GLU GLU H . n 
H 1 101 ASP 101 102 102 ASP ASP H . n 
H 1 102 SER 102 103 103 SER SER H . n 
H 1 103 VAL 103 104 104 VAL VAL H . n 
H 1 104 ILE 104 105 105 ILE ILE H . n 
H 1 105 SER 105 106 106 SER SER H . n 
H 1 106 LEU 106 107 107 LEU LEU H . n 
H 1 107 SER 107 108 108 SER SER H . n 
H 1 108 GLY 108 109 109 GLY GLY H . n 
H 1 109 ASP 109 110 110 ASP ASP H . n 
H 1 110 HIS 110 111 111 HIS HIS H . n 
H 1 111 CYS 111 112 112 CYS CYS H . n 
H 1 112 ILE 112 113 113 ILE ILE H . n 
H 1 113 ILE 113 114 114 ILE ILE H . n 
H 1 114 GLY 114 115 115 GLY GLY H . n 
H 1 115 ARG 115 116 116 ARG ARG H . n 
H 1 116 THR 116 117 117 THR THR H . n 
H 1 117 LEU 117 118 118 LEU LEU H . n 
H 1 118 VAL 118 119 119 VAL VAL H . n 
H 1 119 VAL 119 120 120 VAL VAL H . n 
H 1 120 HIS 120 121 121 HIS HIS H . n 
H 1 121 GLU 121 122 122 GLU GLU H . n 
H 1 122 LYS 122 123 123 LYS LYS H . n 
H 1 123 ALA 123 124 124 ALA ALA H . n 
H 1 124 ASP 124 125 125 ASP ASP H . n 
H 1 125 ASP 125 126 126 ASP ASP H . n 
H 1 126 LEU 126 127 127 LEU LEU H . n 
H 1 127 GLY 127 128 128 GLY GLY H . n 
H 1 128 LYS 128 129 129 LYS LYS H . n 
H 1 129 GLY 129 130 130 GLY GLY H . n 
H 1 130 GLY 130 131 131 GLY GLY H . n 
H 1 131 ASN 131 132 132 ASN ASN H . n 
H 1 132 GLU 132 133 133 GLU GLU H . n 
H 1 133 GLU 133 134 134 GLU GLU H . n 
H 1 134 SER 134 135 135 SER SER H . n 
H 1 135 THR 135 136 136 THR THR H . n 
H 1 136 LYS 136 137 137 LYS LYS H . n 
H 1 137 THR 137 138 138 THR THR H . n 
H 1 138 GLY 138 139 139 GLY GLY H . n 
H 1 139 ASN 139 140 140 ASN ASN H . n 
H 1 140 ALA 140 141 141 ALA ALA H . n 
H 1 141 GLY 141 142 142 GLY GLY H . n 
H 1 142 SER 142 143 143 SER SER H . n 
H 1 143 ARG 143 144 144 ARG ARG H . n 
H 1 144 LEU 144 145 145 LEU LEU H . n 
H 1 145 ALA 145 146 146 ALA ALA H . n 
H 1 146 CYS 146 147 147 CYS CYS H . n 
H 1 147 GLY 147 148 148 GLY GLY H . n 
H 1 148 VAL 148 149 149 VAL VAL H . n 
H 1 149 ILE 149 150 150 ILE ILE H . n 
H 1 150 GLY 150 151 151 GLY GLY H . n 
H 1 151 ILE 151 152 152 ILE ILE H . n 
H 1 152 ALA 152 153 153 ALA ALA H . n 
H 1 153 GLN 153 154 154 GLN GLN H . n 
I 1 1   ALA 1   2   2   ALA ALA I . n 
I 1 2   THR 2   3   3   THR THR I . n 
I 1 3   LYS 3   4   4   LYS LYS I . n 
I 1 4   ALA 4   5   5   ALA ALA I . n 
I 1 5   VAL 5   6   6   VAL VAL I . n 
I 1 6   CYS 6   7   7   CYS CYS I . n 
I 1 7   VAL 7   8   8   VAL VAL I . n 
I 1 8   LEU 8   9   9   LEU LEU I . n 
I 1 9   LYS 9   10  10  LYS LYS I . n 
I 1 10  GLY 10  11  11  GLY GLY I . n 
I 1 11  ASP 11  12  12  ASP ASP I . n 
I 1 12  GLY 12  13  13  GLY GLY I . n 
I 1 13  PRO 13  14  14  PRO PRO I . n 
I 1 14  VAL 14  15  15  VAL VAL I . n 
I 1 15  GLN 15  16  16  GLN GLN I . n 
I 1 16  GLY 16  17  17  GLY GLY I . n 
I 1 17  ILE 17  18  18  ILE ILE I . n 
I 1 18  ILE 18  19  19  ILE ILE I . n 
I 1 19  ASN 19  20  20  ASN ASN I . n 
I 1 20  PHE 20  21  21  PHE PHE I . n 
I 1 21  GLU 21  22  22  GLU GLU I . n 
I 1 22  GLN 22  23  23  GLN GLN I . n 
I 1 23  LYS 23  24  24  LYS LYS I . n 
I 1 24  GLU 24  25  25  GLU GLU I . n 
I 1 25  SER 25  26  26  SER SER I . n 
I 1 26  ASN 26  27  27  ASN ASN I . n 
I 1 27  GLY 27  28  28  GLY GLY I . n 
I 1 28  PRO 28  29  29  PRO PRO I . n 
I 1 29  VAL 29  30  30  VAL VAL I . n 
I 1 30  LYS 30  31  31  LYS LYS I . n 
I 1 31  VAL 31  32  32  VAL VAL I . n 
I 1 32  TRP 32  33  33  TRP TRP I . n 
I 1 33  GLY 33  34  34  GLY GLY I . n 
I 1 34  SER 34  35  35  SER SER I . n 
I 1 35  ILE 35  36  36  ILE ILE I . n 
I 1 36  LYS 36  37  37  LYS LYS I . n 
I 1 37  GLY 37  38  38  GLY GLY I . n 
I 1 38  LEU 38  39  39  LEU LEU I . n 
I 1 39  THR 39  40  40  THR THR I . n 
I 1 40  GLU 40  41  41  GLU GLU I . n 
I 1 41  GLY 41  42  42  GLY GLY I . n 
I 1 42  LEU 42  43  43  LEU LEU I . n 
I 1 43  HIS 43  44  44  HIS HIS I . n 
I 1 44  GLY 44  45  45  GLY GLY I . n 
I 1 45  PHE 45  46  46  PHE PHE I . n 
I 1 46  HIS 46  47  47  HIS HIS I . n 
I 1 47  VAL 47  48  48  VAL VAL I . n 
I 1 48  HIS 48  49  49  HIS HIS I . n 
I 1 49  GLU 49  50  50  GLU GLU I . n 
I 1 50  PHE 50  51  51  PHE PHE I . n 
I 1 51  GLY 51  52  52  GLY GLY I . n 
I 1 52  ASP 52  53  53  ASP ASP I . n 
I 1 53  ASN 53  54  54  ASN ASN I . n 
I 1 54  THR 54  55  55  THR THR I . n 
I 1 55  ALA 55  56  56  ALA ALA I . n 
I 1 56  GLY 56  57  57  GLY GLY I . n 
I 1 57  CYS 57  58  58  CYS CYS I . n 
I 1 58  THR 58  59  59  THR THR I . n 
I 1 59  SER 59  60  60  SER SER I . n 
I 1 60  ALA 60  61  61  ALA ALA I . n 
I 1 61  GLY 61  62  62  GLY GLY I . n 
I 1 62  PRO 62  63  63  PRO PRO I . n 
I 1 63  HIS 63  64  64  HIS HIS I . n 
I 1 64  PHE 64  65  65  PHE PHE I . n 
I 1 65  ASN 65  66  66  ASN ASN I . n 
I 1 66  PRO 66  67  67  PRO PRO I . n 
I 1 67  LEU 67  68  68  LEU LEU I . n 
I 1 68  SER 68  69  69  SER SER I . n 
I 1 69  ARG 69  70  70  ARG ARG I . n 
I 1 70  LYS 70  71  71  LYS LYS I . n 
I 1 71  HIS 71  72  72  HIS HIS I . n 
I 1 72  GLY 72  73  73  GLY GLY I . n 
I 1 73  GLY 73  74  74  GLY GLY I . n 
I 1 74  PRO 74  75  75  PRO PRO I . n 
I 1 75  LYS 75  76  76  LYS LYS I . n 
I 1 76  ASP 76  77  77  ASP ASP I . n 
I 1 77  GLU 77  78  78  GLU GLU I . n 
I 1 78  GLU 78  79  79  GLU GLU I . n 
I 1 79  ARG 79  80  80  ARG ARG I . n 
I 1 80  HIS 80  81  81  HIS HIS I . n 
I 1 81  VAL 81  82  82  VAL VAL I . n 
I 1 82  GLY 82  83  83  GLY GLY I . n 
I 1 83  ASP 83  84  84  ASP ASP I . n 
I 1 84  LEU 84  85  85  LEU LEU I . n 
I 1 85  GLY 85  86  86  GLY GLY I . n 
I 1 86  ASN 86  87  87  ASN ASN I . n 
I 1 87  VAL 87  88  88  VAL VAL I . n 
I 1 88  THR 88  89  89  THR THR I . n 
I 1 89  ALA 89  90  90  ALA ALA I . n 
I 1 90  ASP 90  91  91  ASP ASP I . n 
I 1 91  LYS 91  92  92  LYS LYS I . n 
I 1 92  ASP 92  93  93  ASP ASP I . n 
I 1 93  GLY 93  94  94  GLY GLY I . n 
I 1 94  VAL 94  95  95  VAL VAL I . n 
I 1 95  ALA 95  96  96  ALA ALA I . n 
I 1 96  ASP 96  97  97  ASP ASP I . n 
I 1 97  VAL 97  98  98  VAL VAL I . n 
I 1 98  SER 98  99  99  SER SER I . n 
I 1 99  ILE 99  100 100 ILE ILE I . n 
I 1 100 GLU 100 101 101 GLU GLU I . n 
I 1 101 ASP 101 102 102 ASP ASP I . n 
I 1 102 SER 102 103 103 SER SER I . n 
I 1 103 VAL 103 104 104 VAL VAL I . n 
I 1 104 ILE 104 105 105 ILE ILE I . n 
I 1 105 SER 105 106 106 SER SER I . n 
I 1 106 LEU 106 107 107 LEU LEU I . n 
I 1 107 SER 107 108 108 SER SER I . n 
I 1 108 GLY 108 109 109 GLY GLY I . n 
I 1 109 ASP 109 110 110 ASP ASP I . n 
I 1 110 HIS 110 111 111 HIS HIS I . n 
I 1 111 CYS 111 112 112 CYS CYS I . n 
I 1 112 ILE 112 113 113 ILE ILE I . n 
I 1 113 ILE 113 114 114 ILE ILE I . n 
I 1 114 GLY 114 115 115 GLY GLY I . n 
I 1 115 ARG 115 116 116 ARG ARG I . n 
I 1 116 THR 116 117 117 THR THR I . n 
I 1 117 LEU 117 118 118 LEU LEU I . n 
I 1 118 VAL 118 119 119 VAL VAL I . n 
I 1 119 VAL 119 120 120 VAL VAL I . n 
I 1 120 HIS 120 121 121 HIS HIS I . n 
I 1 121 GLU 121 122 122 GLU GLU I . n 
I 1 122 LYS 122 123 123 LYS LYS I . n 
I 1 123 ALA 123 124 124 ALA ALA I . n 
I 1 124 ASP 124 125 125 ASP ASP I . n 
I 1 125 ASP 125 126 126 ASP ASP I . n 
I 1 126 LEU 126 127 127 LEU LEU I . n 
I 1 127 GLY 127 128 128 GLY GLY I . n 
I 1 128 LYS 128 129 129 LYS LYS I . n 
I 1 129 GLY 129 130 130 GLY GLY I . n 
I 1 130 GLY 130 131 131 GLY GLY I . n 
I 1 131 ASN 131 132 132 ASN ASN I . n 
I 1 132 GLU 132 133 133 GLU GLU I . n 
I 1 133 GLU 133 134 134 GLU GLU I . n 
I 1 134 SER 134 135 135 SER SER I . n 
I 1 135 THR 135 136 136 THR THR I . n 
I 1 136 LYS 136 137 137 LYS LYS I . n 
I 1 137 THR 137 138 138 THR THR I . n 
I 1 138 GLY 138 139 139 GLY GLY I . n 
I 1 139 ASN 139 140 140 ASN ASN I . n 
I 1 140 ALA 140 141 141 ALA ALA I . n 
I 1 141 GLY 141 142 142 GLY GLY I . n 
I 1 142 SER 142 143 143 SER SER I . n 
I 1 143 ARG 143 144 144 ARG ARG I . n 
I 1 144 LEU 144 145 145 LEU LEU I . n 
I 1 145 ALA 145 146 146 ALA ALA I . n 
I 1 146 CYS 146 147 147 CYS CYS I . n 
I 1 147 GLY 147 148 148 GLY GLY I . n 
I 1 148 VAL 148 149 149 VAL VAL I . n 
I 1 149 ILE 149 150 150 ILE ILE I . n 
I 1 150 GLY 150 151 151 GLY GLY I . n 
I 1 151 ILE 151 152 152 ILE ILE I . n 
I 1 152 ALA 152 153 153 ALA ALA I . n 
I 1 153 GLN 153 154 154 GLN GLN I . n 
J 1 1   ALA 1   2   2   ALA ALA J . n 
J 1 2   THR 2   3   3   THR THR J . n 
J 1 3   LYS 3   4   4   LYS LYS J . n 
J 1 4   ALA 4   5   5   ALA ALA J . n 
J 1 5   VAL 5   6   6   VAL VAL J . n 
J 1 6   CYS 6   7   7   CYS CYS J . n 
J 1 7   VAL 7   8   8   VAL VAL J . n 
J 1 8   LEU 8   9   9   LEU LEU J . n 
J 1 9   LYS 9   10  10  LYS LYS J . n 
J 1 10  GLY 10  11  11  GLY GLY J . n 
J 1 11  ASP 11  12  12  ASP ASP J . n 
J 1 12  GLY 12  13  13  GLY GLY J . n 
J 1 13  PRO 13  14  14  PRO PRO J . n 
J 1 14  VAL 14  15  15  VAL VAL J . n 
J 1 15  GLN 15  16  16  GLN GLN J . n 
J 1 16  GLY 16  17  17  GLY GLY J . n 
J 1 17  ILE 17  18  18  ILE ILE J . n 
J 1 18  ILE 18  19  19  ILE ILE J . n 
J 1 19  ASN 19  20  20  ASN ASN J . n 
J 1 20  PHE 20  21  21  PHE PHE J . n 
J 1 21  GLU 21  22  22  GLU GLU J . n 
J 1 22  GLN 22  23  23  GLN GLN J . n 
J 1 23  LYS 23  24  24  LYS LYS J . n 
J 1 24  GLU 24  25  25  GLU GLU J . n 
J 1 25  SER 25  26  26  SER SER J . n 
J 1 26  ASN 26  27  27  ASN ASN J . n 
J 1 27  GLY 27  28  28  GLY GLY J . n 
J 1 28  PRO 28  29  29  PRO PRO J . n 
J 1 29  VAL 29  30  30  VAL VAL J . n 
J 1 30  LYS 30  31  31  LYS LYS J . n 
J 1 31  VAL 31  32  32  VAL VAL J . n 
J 1 32  TRP 32  33  33  TRP TRP J . n 
J 1 33  GLY 33  34  34  GLY GLY J . n 
J 1 34  SER 34  35  35  SER SER J . n 
J 1 35  ILE 35  36  36  ILE ILE J . n 
J 1 36  LYS 36  37  37  LYS LYS J . n 
J 1 37  GLY 37  38  38  GLY GLY J . n 
J 1 38  LEU 38  39  39  LEU LEU J . n 
J 1 39  THR 39  40  40  THR THR J . n 
J 1 40  GLU 40  41  41  GLU GLU J . n 
J 1 41  GLY 41  42  42  GLY GLY J . n 
J 1 42  LEU 42  43  43  LEU LEU J . n 
J 1 43  HIS 43  44  44  HIS HIS J . n 
J 1 44  GLY 44  45  45  GLY GLY J . n 
J 1 45  PHE 45  46  46  PHE PHE J . n 
J 1 46  HIS 46  47  47  HIS HIS J . n 
J 1 47  VAL 47  48  48  VAL VAL J . n 
J 1 48  HIS 48  49  49  HIS HIS J . n 
J 1 49  GLU 49  50  50  GLU GLU J . n 
J 1 50  PHE 50  51  51  PHE PHE J . n 
J 1 51  GLY 51  52  52  GLY GLY J . n 
J 1 52  ASP 52  53  53  ASP ASP J . n 
J 1 53  ASN 53  54  54  ASN ASN J . n 
J 1 54  THR 54  55  55  THR THR J . n 
J 1 55  ALA 55  56  56  ALA ALA J . n 
J 1 56  GLY 56  57  57  GLY GLY J . n 
J 1 57  CYS 57  58  58  CYS CYS J . n 
J 1 58  THR 58  59  59  THR THR J . n 
J 1 59  SER 59  60  60  SER SER J . n 
J 1 60  ALA 60  61  61  ALA ALA J . n 
J 1 61  GLY 61  62  62  GLY GLY J . n 
J 1 62  PRO 62  63  63  PRO PRO J . n 
J 1 63  HIS 63  64  64  HIS HIS J . n 
J 1 64  PHE 64  65  65  PHE PHE J . n 
J 1 65  ASN 65  66  66  ASN ASN J . n 
J 1 66  PRO 66  67  67  PRO PRO J . n 
J 1 67  LEU 67  68  68  LEU LEU J . n 
J 1 68  SER 68  69  69  SER SER J . n 
J 1 69  ARG 69  70  70  ARG ARG J . n 
J 1 70  LYS 70  71  71  LYS LYS J . n 
J 1 71  HIS 71  72  72  HIS HIS J . n 
J 1 72  GLY 72  73  73  GLY GLY J . n 
J 1 73  GLY 73  74  74  GLY GLY J . n 
J 1 74  PRO 74  75  75  PRO PRO J . n 
J 1 75  LYS 75  76  76  LYS LYS J . n 
J 1 76  ASP 76  77  77  ASP ASP J . n 
J 1 77  GLU 77  78  78  GLU GLU J . n 
J 1 78  GLU 78  79  79  GLU GLU J . n 
J 1 79  ARG 79  80  80  ARG ARG J . n 
J 1 80  HIS 80  81  81  HIS HIS J . n 
J 1 81  VAL 81  82  82  VAL VAL J . n 
J 1 82  GLY 82  83  83  GLY GLY J . n 
J 1 83  ASP 83  84  84  ASP ASP J . n 
J 1 84  LEU 84  85  85  LEU LEU J . n 
J 1 85  GLY 85  86  86  GLY GLY J . n 
J 1 86  ASN 86  87  87  ASN ASN J . n 
J 1 87  VAL 87  88  88  VAL VAL J . n 
J 1 88  THR 88  89  89  THR THR J . n 
J 1 89  ALA 89  90  90  ALA ALA J . n 
J 1 90  ASP 90  91  91  ASP ASP J . n 
J 1 91  LYS 91  92  92  LYS LYS J . n 
J 1 92  ASP 92  93  93  ASP ASP J . n 
J 1 93  GLY 93  94  94  GLY GLY J . n 
J 1 94  VAL 94  95  95  VAL VAL J . n 
J 1 95  ALA 95  96  96  ALA ALA J . n 
J 1 96  ASP 96  97  97  ASP ASP J . n 
J 1 97  VAL 97  98  98  VAL VAL J . n 
J 1 98  SER 98  99  99  SER SER J . n 
J 1 99  ILE 99  100 100 ILE ILE J . n 
J 1 100 GLU 100 101 101 GLU GLU J . n 
J 1 101 ASP 101 102 102 ASP ASP J . n 
J 1 102 SER 102 103 103 SER SER J . n 
J 1 103 VAL 103 104 104 VAL VAL J . n 
J 1 104 ILE 104 105 105 ILE ILE J . n 
J 1 105 SER 105 106 106 SER SER J . n 
J 1 106 LEU 106 107 107 LEU LEU J . n 
J 1 107 SER 107 108 108 SER SER J . n 
J 1 108 GLY 108 109 109 GLY GLY J . n 
J 1 109 ASP 109 110 110 ASP ASP J . n 
J 1 110 HIS 110 111 111 HIS HIS J . n 
J 1 111 CYS 111 112 112 CYS CYS J . n 
J 1 112 ILE 112 113 113 ILE ILE J . n 
J 1 113 ILE 113 114 114 ILE ILE J . n 
J 1 114 GLY 114 115 115 GLY GLY J . n 
J 1 115 ARG 115 116 116 ARG ARG J . n 
J 1 116 THR 116 117 117 THR THR J . n 
J 1 117 LEU 117 118 118 LEU LEU J . n 
J 1 118 VAL 118 119 119 VAL VAL J . n 
J 1 119 VAL 119 120 120 VAL VAL J . n 
J 1 120 HIS 120 121 121 HIS HIS J . n 
J 1 121 GLU 121 122 122 GLU GLU J . n 
J 1 122 LYS 122 123 123 LYS LYS J . n 
J 1 123 ALA 123 124 124 ALA ALA J . n 
J 1 124 ASP 124 125 125 ASP ASP J . n 
J 1 125 ASP 125 126 126 ASP ASP J . n 
J 1 126 LEU 126 127 127 LEU LEU J . n 
J 1 127 GLY 127 128 128 GLY GLY J . n 
J 1 128 LYS 128 129 129 LYS LYS J . n 
J 1 129 GLY 129 130 130 GLY GLY J . n 
J 1 130 GLY 130 131 131 GLY GLY J . n 
J 1 131 ASN 131 132 132 ASN ASN J . n 
J 1 132 GLU 132 133 133 GLU GLU J . n 
J 1 133 GLU 133 134 134 GLU GLU J . n 
J 1 134 SER 134 135 135 SER SER J . n 
J 1 135 THR 135 136 136 THR THR J . n 
J 1 136 LYS 136 137 137 LYS LYS J . n 
J 1 137 THR 137 138 138 THR THR J . n 
J 1 138 GLY 138 139 139 GLY GLY J . n 
J 1 139 ASN 139 140 140 ASN ASN J . n 
J 1 140 ALA 140 141 141 ALA ALA J . n 
J 1 141 GLY 141 142 142 GLY GLY J . n 
J 1 142 SER 142 143 143 SER SER J . n 
J 1 143 ARG 143 144 144 ARG ARG J . n 
J 1 144 LEU 144 145 145 LEU LEU J . n 
J 1 145 ALA 145 146 146 ALA ALA J . n 
J 1 146 CYS 146 147 147 CYS CYS J . n 
J 1 147 GLY 147 148 148 GLY GLY J . n 
J 1 148 VAL 148 149 149 VAL VAL J . n 
J 1 149 ILE 149 150 150 ILE ILE J . n 
J 1 150 GLY 150 151 151 GLY GLY J . n 
J 1 151 ILE 151 152 152 ILE ILE J . n 
J 1 152 ALA 152 153 153 ALA ALA J . n 
J 1 153 GLN 153 154 154 GLN GLN J . n 
K 1 1   ALA 1   2   2   ALA ALA K . n 
K 1 2   THR 2   3   3   THR THR K . n 
K 1 3   LYS 3   4   4   LYS LYS K . n 
K 1 4   ALA 4   5   5   ALA ALA K . n 
K 1 5   VAL 5   6   6   VAL VAL K . n 
K 1 6   CYS 6   7   7   CYS CYS K . n 
K 1 7   VAL 7   8   8   VAL VAL K . n 
K 1 8   LEU 8   9   9   LEU LEU K . n 
K 1 9   LYS 9   10  10  LYS LYS K . n 
K 1 10  GLY 10  11  11  GLY GLY K . n 
K 1 11  ASP 11  12  12  ASP ASP K . n 
K 1 12  GLY 12  13  13  GLY GLY K . n 
K 1 13  PRO 13  14  14  PRO PRO K . n 
K 1 14  VAL 14  15  15  VAL VAL K . n 
K 1 15  GLN 15  16  16  GLN GLN K . n 
K 1 16  GLY 16  17  17  GLY GLY K . n 
K 1 17  ILE 17  18  18  ILE ILE K . n 
K 1 18  ILE 18  19  19  ILE ILE K . n 
K 1 19  ASN 19  20  20  ASN ASN K . n 
K 1 20  PHE 20  21  21  PHE PHE K . n 
K 1 21  GLU 21  22  22  GLU GLU K . n 
K 1 22  GLN 22  23  23  GLN GLN K . n 
K 1 23  LYS 23  24  24  LYS LYS K . n 
K 1 24  GLU 24  25  25  GLU GLU K . n 
K 1 25  SER 25  26  26  SER SER K . n 
K 1 26  ASN 26  27  27  ASN ASN K . n 
K 1 27  GLY 27  28  28  GLY GLY K . n 
K 1 28  PRO 28  29  29  PRO PRO K . n 
K 1 29  VAL 29  30  30  VAL VAL K . n 
K 1 30  LYS 30  31  31  LYS LYS K . n 
K 1 31  VAL 31  32  32  VAL VAL K . n 
K 1 32  TRP 32  33  33  TRP TRP K . n 
K 1 33  GLY 33  34  34  GLY GLY K . n 
K 1 34  SER 34  35  35  SER SER K . n 
K 1 35  ILE 35  36  36  ILE ILE K . n 
K 1 36  LYS 36  37  37  LYS LYS K . n 
K 1 37  GLY 37  38  38  GLY GLY K . n 
K 1 38  LEU 38  39  39  LEU LEU K . n 
K 1 39  THR 39  40  40  THR THR K . n 
K 1 40  GLU 40  41  41  GLU GLU K . n 
K 1 41  GLY 41  42  42  GLY GLY K . n 
K 1 42  LEU 42  43  43  LEU LEU K . n 
K 1 43  HIS 43  44  44  HIS HIS K . n 
K 1 44  GLY 44  45  45  GLY GLY K . n 
K 1 45  PHE 45  46  46  PHE PHE K . n 
K 1 46  HIS 46  47  47  HIS HIS K . n 
K 1 47  VAL 47  48  48  VAL VAL K . n 
K 1 48  HIS 48  49  49  HIS HIS K . n 
K 1 49  GLU 49  50  50  GLU GLU K . n 
K 1 50  PHE 50  51  51  PHE PHE K . n 
K 1 51  GLY 51  52  52  GLY GLY K . n 
K 1 52  ASP 52  53  53  ASP ASP K . n 
K 1 53  ASN 53  54  54  ASN ASN K . n 
K 1 54  THR 54  55  55  THR THR K . n 
K 1 55  ALA 55  56  56  ALA ALA K . n 
K 1 56  GLY 56  57  57  GLY GLY K . n 
K 1 57  CYS 57  58  58  CYS CYS K . n 
K 1 58  THR 58  59  59  THR THR K . n 
K 1 59  SER 59  60  60  SER SER K . n 
K 1 60  ALA 60  61  61  ALA ALA K . n 
K 1 61  GLY 61  62  62  GLY GLY K . n 
K 1 62  PRO 62  63  63  PRO PRO K . n 
K 1 63  HIS 63  64  64  HIS HIS K . n 
K 1 64  PHE 64  65  65  PHE PHE K . n 
K 1 65  ASN 65  66  66  ASN ASN K . n 
K 1 66  PRO 66  67  67  PRO PRO K . n 
K 1 67  LEU 67  68  68  LEU LEU K . n 
K 1 68  SER 68  69  69  SER SER K . n 
K 1 69  ARG 69  70  70  ARG ARG K . n 
K 1 70  LYS 70  71  71  LYS LYS K . n 
K 1 71  HIS 71  72  72  HIS HIS K . n 
K 1 72  GLY 72  73  73  GLY GLY K . n 
K 1 73  GLY 73  74  74  GLY GLY K . n 
K 1 74  PRO 74  75  75  PRO PRO K . n 
K 1 75  LYS 75  76  76  LYS LYS K . n 
K 1 76  ASP 76  77  77  ASP ASP K . n 
K 1 77  GLU 77  78  78  GLU GLU K . n 
K 1 78  GLU 78  79  79  GLU GLU K . n 
K 1 79  ARG 79  80  80  ARG ARG K . n 
K 1 80  HIS 80  81  81  HIS HIS K . n 
K 1 81  VAL 81  82  82  VAL VAL K . n 
K 1 82  GLY 82  83  83  GLY GLY K . n 
K 1 83  ASP 83  84  84  ASP ASP K . n 
K 1 84  LEU 84  85  85  LEU LEU K . n 
K 1 85  GLY 85  86  86  GLY GLY K . n 
K 1 86  ASN 86  87  87  ASN ASN K . n 
K 1 87  VAL 87  88  88  VAL VAL K . n 
K 1 88  THR 88  89  89  THR THR K . n 
K 1 89  ALA 89  90  90  ALA ALA K . n 
K 1 90  ASP 90  91  91  ASP ASP K . n 
K 1 91  LYS 91  92  92  LYS LYS K . n 
K 1 92  ASP 92  93  93  ASP ASP K . n 
K 1 93  GLY 93  94  94  GLY GLY K . n 
K 1 94  VAL 94  95  95  VAL VAL K . n 
K 1 95  ALA 95  96  96  ALA ALA K . n 
K 1 96  ASP 96  97  97  ASP ASP K . n 
K 1 97  VAL 97  98  98  VAL VAL K . n 
K 1 98  SER 98  99  99  SER SER K . n 
K 1 99  ILE 99  100 100 ILE ILE K . n 
K 1 100 GLU 100 101 101 GLU GLU K . n 
K 1 101 ASP 101 102 102 ASP ASP K . n 
K 1 102 SER 102 103 103 SER SER K . n 
K 1 103 VAL 103 104 104 VAL VAL K . n 
K 1 104 ILE 104 105 105 ILE ILE K . n 
K 1 105 SER 105 106 106 SER SER K . n 
K 1 106 LEU 106 107 107 LEU LEU K . n 
K 1 107 SER 107 108 108 SER SER K . n 
K 1 108 GLY 108 109 109 GLY GLY K . n 
K 1 109 ASP 109 110 110 ASP ASP K . n 
K 1 110 HIS 110 111 111 HIS HIS K . n 
K 1 111 CYS 111 112 112 CYS CYS K . n 
K 1 112 ILE 112 113 113 ILE ILE K . n 
K 1 113 ILE 113 114 114 ILE ILE K . n 
K 1 114 GLY 114 115 115 GLY GLY K . n 
K 1 115 ARG 115 116 116 ARG ARG K . n 
K 1 116 THR 116 117 117 THR THR K . n 
K 1 117 LEU 117 118 118 LEU LEU K . n 
K 1 118 VAL 118 119 119 VAL VAL K . n 
K 1 119 VAL 119 120 120 VAL VAL K . n 
K 1 120 HIS 120 121 121 HIS HIS K . n 
K 1 121 GLU 121 122 122 GLU GLU K . n 
K 1 122 LYS 122 123 123 LYS LYS K . n 
K 1 123 ALA 123 124 124 ALA ALA K . n 
K 1 124 ASP 124 125 125 ASP ASP K . n 
K 1 125 ASP 125 126 126 ASP ASP K . n 
K 1 126 LEU 126 127 127 LEU LEU K . n 
K 1 127 GLY 127 128 128 GLY GLY K . n 
K 1 128 LYS 128 129 129 LYS LYS K . n 
K 1 129 GLY 129 130 130 GLY GLY K . n 
K 1 130 GLY 130 131 131 GLY GLY K . n 
K 1 131 ASN 131 132 132 ASN ASN K . n 
K 1 132 GLU 132 133 133 GLU GLU K . n 
K 1 133 GLU 133 134 134 GLU GLU K . n 
K 1 134 SER 134 135 135 SER SER K . n 
K 1 135 THR 135 136 136 THR THR K . n 
K 1 136 LYS 136 137 137 LYS LYS K . n 
K 1 137 THR 137 138 138 THR THR K . n 
K 1 138 GLY 138 139 139 GLY GLY K . n 
K 1 139 ASN 139 140 140 ASN ASN K . n 
K 1 140 ALA 140 141 141 ALA ALA K . n 
K 1 141 GLY 141 142 142 GLY GLY K . n 
K 1 142 SER 142 143 143 SER SER K . n 
K 1 143 ARG 143 144 144 ARG ARG K . n 
K 1 144 LEU 144 145 145 LEU LEU K . n 
K 1 145 ALA 145 146 146 ALA ALA K . n 
K 1 146 CYS 146 147 147 CYS CYS K . n 
K 1 147 GLY 147 148 148 GLY GLY K . n 
K 1 148 VAL 148 149 149 VAL VAL K . n 
K 1 149 ILE 149 150 150 ILE ILE K . n 
K 1 150 GLY 150 151 151 GLY GLY K . n 
K 1 151 ILE 151 152 152 ILE ILE K . n 
K 1 152 ALA 152 153 153 ALA ALA K . n 
K 1 153 GLN 153 154 154 GLN GLN K . n 
L 1 1   ALA 1   2   2   ALA ALA L . n 
L 1 2   THR 2   3   3   THR THR L . n 
L 1 3   LYS 3   4   4   LYS LYS L . n 
L 1 4   ALA 4   5   5   ALA ALA L . n 
L 1 5   VAL 5   6   6   VAL VAL L . n 
L 1 6   CYS 6   7   7   CYS CYS L . n 
L 1 7   VAL 7   8   8   VAL VAL L . n 
L 1 8   LEU 8   9   9   LEU LEU L . n 
L 1 9   LYS 9   10  10  LYS LYS L . n 
L 1 10  GLY 10  11  11  GLY GLY L . n 
L 1 11  ASP 11  12  12  ASP ASP L . n 
L 1 12  GLY 12  13  13  GLY GLY L . n 
L 1 13  PRO 13  14  14  PRO PRO L . n 
L 1 14  VAL 14  15  15  VAL VAL L . n 
L 1 15  GLN 15  16  16  GLN GLN L . n 
L 1 16  GLY 16  17  17  GLY GLY L . n 
L 1 17  ILE 17  18  18  ILE ILE L . n 
L 1 18  ILE 18  19  19  ILE ILE L . n 
L 1 19  ASN 19  20  20  ASN ASN L . n 
L 1 20  PHE 20  21  21  PHE PHE L . n 
L 1 21  GLU 21  22  22  GLU GLU L . n 
L 1 22  GLN 22  23  23  GLN GLN L . n 
L 1 23  LYS 23  24  24  LYS LYS L . n 
L 1 24  GLU 24  25  25  GLU GLU L . n 
L 1 25  SER 25  26  26  SER SER L . n 
L 1 26  ASN 26  27  27  ASN ASN L . n 
L 1 27  GLY 27  28  28  GLY GLY L . n 
L 1 28  PRO 28  29  29  PRO PRO L . n 
L 1 29  VAL 29  30  30  VAL VAL L . n 
L 1 30  LYS 30  31  31  LYS LYS L . n 
L 1 31  VAL 31  32  32  VAL VAL L . n 
L 1 32  TRP 32  33  33  TRP TRP L . n 
L 1 33  GLY 33  34  34  GLY GLY L . n 
L 1 34  SER 34  35  35  SER SER L . n 
L 1 35  ILE 35  36  36  ILE ILE L . n 
L 1 36  LYS 36  37  37  LYS LYS L . n 
L 1 37  GLY 37  38  38  GLY GLY L . n 
L 1 38  LEU 38  39  39  LEU LEU L . n 
L 1 39  THR 39  40  40  THR THR L . n 
L 1 40  GLU 40  41  41  GLU GLU L . n 
L 1 41  GLY 41  42  42  GLY GLY L . n 
L 1 42  LEU 42  43  43  LEU LEU L . n 
L 1 43  HIS 43  44  44  HIS HIS L . n 
L 1 44  GLY 44  45  45  GLY GLY L . n 
L 1 45  PHE 45  46  46  PHE PHE L . n 
L 1 46  HIS 46  47  47  HIS HIS L . n 
L 1 47  VAL 47  48  48  VAL VAL L . n 
L 1 48  HIS 48  49  49  HIS HIS L . n 
L 1 49  GLU 49  50  50  GLU GLU L . n 
L 1 50  PHE 50  51  51  PHE PHE L . n 
L 1 51  GLY 51  52  52  GLY GLY L . n 
L 1 52  ASP 52  53  53  ASP ASP L . n 
L 1 53  ASN 53  54  54  ASN ASN L . n 
L 1 54  THR 54  55  55  THR THR L . n 
L 1 55  ALA 55  56  56  ALA ALA L . n 
L 1 56  GLY 56  57  57  GLY GLY L . n 
L 1 57  CYS 57  58  58  CYS CYS L . n 
L 1 58  THR 58  59  59  THR THR L . n 
L 1 59  SER 59  60  60  SER SER L . n 
L 1 60  ALA 60  61  61  ALA ALA L . n 
L 1 61  GLY 61  62  62  GLY GLY L . n 
L 1 62  PRO 62  63  63  PRO PRO L . n 
L 1 63  HIS 63  64  64  HIS HIS L . n 
L 1 64  PHE 64  65  65  PHE PHE L . n 
L 1 65  ASN 65  66  66  ASN ASN L . n 
L 1 66  PRO 66  67  67  PRO PRO L . n 
L 1 67  LEU 67  68  68  LEU LEU L . n 
L 1 68  SER 68  69  69  SER SER L . n 
L 1 69  ARG 69  70  70  ARG ARG L . n 
L 1 70  LYS 70  71  71  LYS LYS L . n 
L 1 71  HIS 71  72  72  HIS HIS L . n 
L 1 72  GLY 72  73  73  GLY GLY L . n 
L 1 73  GLY 73  74  74  GLY GLY L . n 
L 1 74  PRO 74  75  75  PRO PRO L . n 
L 1 75  LYS 75  76  76  LYS LYS L . n 
L 1 76  ASP 76  77  77  ASP ASP L . n 
L 1 77  GLU 77  78  78  GLU GLU L . n 
L 1 78  GLU 78  79  79  GLU GLU L . n 
L 1 79  ARG 79  80  80  ARG ARG L . n 
L 1 80  HIS 80  81  81  HIS HIS L . n 
L 1 81  VAL 81  82  82  VAL VAL L . n 
L 1 82  GLY 82  83  83  GLY GLY L . n 
L 1 83  ASP 83  84  84  ASP ASP L . n 
L 1 84  LEU 84  85  85  LEU LEU L . n 
L 1 85  GLY 85  86  86  GLY GLY L . n 
L 1 86  ASN 86  87  87  ASN ASN L . n 
L 1 87  VAL 87  88  88  VAL VAL L . n 
L 1 88  THR 88  89  89  THR THR L . n 
L 1 89  ALA 89  90  90  ALA ALA L . n 
L 1 90  ASP 90  91  91  ASP ASP L . n 
L 1 91  LYS 91  92  92  LYS LYS L . n 
L 1 92  ASP 92  93  93  ASP ASP L . n 
L 1 93  GLY 93  94  94  GLY GLY L . n 
L 1 94  VAL 94  95  95  VAL VAL L . n 
L 1 95  ALA 95  96  96  ALA ALA L . n 
L 1 96  ASP 96  97  97  ASP ASP L . n 
L 1 97  VAL 97  98  98  VAL VAL L . n 
L 1 98  SER 98  99  99  SER SER L . n 
L 1 99  ILE 99  100 100 ILE ILE L . n 
L 1 100 GLU 100 101 101 GLU GLU L . n 
L 1 101 ASP 101 102 102 ASP ASP L . n 
L 1 102 SER 102 103 103 SER SER L . n 
L 1 103 VAL 103 104 104 VAL VAL L . n 
L 1 104 ILE 104 105 105 ILE ILE L . n 
L 1 105 SER 105 106 106 SER SER L . n 
L 1 106 LEU 106 107 107 LEU LEU L . n 
L 1 107 SER 107 108 108 SER SER L . n 
L 1 108 GLY 108 109 109 GLY GLY L . n 
L 1 109 ASP 109 110 110 ASP ASP L . n 
L 1 110 HIS 110 111 111 HIS HIS L . n 
L 1 111 CYS 111 112 112 CYS CYS L . n 
L 1 112 ILE 112 113 113 ILE ILE L . n 
L 1 113 ILE 113 114 114 ILE ILE L . n 
L 1 114 GLY 114 115 115 GLY GLY L . n 
L 1 115 ARG 115 116 116 ARG ARG L . n 
L 1 116 THR 116 117 117 THR THR L . n 
L 1 117 LEU 117 118 118 LEU LEU L . n 
L 1 118 VAL 118 119 119 VAL VAL L . n 
L 1 119 VAL 119 120 120 VAL VAL L . n 
L 1 120 HIS 120 121 121 HIS HIS L . n 
L 1 121 GLU 121 122 122 GLU GLU L . n 
L 1 122 LYS 122 123 123 LYS LYS L . n 
L 1 123 ALA 123 124 124 ALA ALA L . n 
L 1 124 ASP 124 125 125 ASP ASP L . n 
L 1 125 ASP 125 126 126 ASP ASP L . n 
L 1 126 LEU 126 127 127 LEU LEU L . n 
L 1 127 GLY 127 128 128 GLY GLY L . n 
L 1 128 LYS 128 129 129 LYS LYS L . n 
L 1 129 GLY 129 130 130 GLY GLY L . n 
L 1 130 GLY 130 131 131 GLY GLY L . n 
L 1 131 ASN 131 132 132 ASN ASN L . n 
L 1 132 GLU 132 133 133 GLU GLU L . n 
L 1 133 GLU 133 134 134 GLU GLU L . n 
L 1 134 SER 134 135 135 SER SER L . n 
L 1 135 THR 135 136 136 THR THR L . n 
L 1 136 LYS 136 137 137 LYS LYS L . n 
L 1 137 THR 137 138 138 THR THR L . n 
L 1 138 GLY 138 139 139 GLY GLY L . n 
L 1 139 ASN 139 140 140 ASN ASN L . n 
L 1 140 ALA 140 141 141 ALA ALA L . n 
L 1 141 GLY 141 142 142 GLY GLY L . n 
L 1 142 SER 142 143 143 SER SER L . n 
L 1 143 ARG 143 144 144 ARG ARG L . n 
L 1 144 LEU 144 145 145 LEU LEU L . n 
L 1 145 ALA 145 146 146 ALA ALA L . n 
L 1 146 CYS 146 147 147 CYS CYS L . n 
L 1 147 GLY 147 148 148 GLY GLY L . n 
L 1 148 VAL 148 149 149 VAL VAL L . n 
L 1 149 ILE 149 150 150 ILE ILE L . n 
L 1 150 GLY 150 151 151 GLY GLY L . n 
L 1 151 ILE 151 152 152 ILE ILE L . n 
L 1 152 ALA 152 153 153 ALA ALA L . n 
L 1 153 GLN 153 154 154 GLN GLN L . n 
# 
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 PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
3 author_and_software_defined_assembly PISA dimeric 2 
4 author_and_software_defined_assembly PISA dimeric 2 
5 author_and_software_defined_assembly PISA dimeric 2 
6 author_and_software_defined_assembly PISA 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,B,M,N,O,P,Q,R    
2 1 C,D,S,T,U,V        
3 1 E,F,W,X,Y,Z        
4 1 G,H,AA,BA,CA,DA    
5 1 I,J,EA,FA,GA,HA,IA 
6 1 K,L,JA,KA,LA,MA    
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1600  ? 
1 MORE         -30   ? 
1 'SSA (A^2)'  14170 ? 
2 'ABSA (A^2)' 1560  ? 
2 MORE         -55   ? 
2 'SSA (A^2)'  14260 ? 
3 'ABSA (A^2)' 1340  ? 
3 MORE         -10   ? 
3 'SSA (A^2)'  14110 ? 
4 'ABSA (A^2)' 1460  ? 
4 MORE         -22   ? 
4 'SSA (A^2)'  14050 ? 
5 'ABSA (A^2)' 1470  ? 
5 MORE         -15   ? 
5 'SSA (A^2)'  14190 ? 
6 'ABSA (A^2)' 1340  ? 
6 MORE         -10   ? 
6 'SSA (A^2)'  14100 ? 
# 
_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 48  ? A HIS 49  ? 1_555 CU A M  CU . ? A CU 155 ? 1_555 NE2 ? A HIS 120 ? A HIS 121 ? 1_555 96.4  ? 
2   NE2 ? A HIS 48  ? A HIS 49  ? 1_555 CU A M  CU . ? A CU 155 ? 1_555 ND1 ? A HIS 46  ? A HIS 47  ? 1_555 144.2 ? 
3   NE2 ? A HIS 120 ? A HIS 121 ? 1_555 CU A M  CU . ? A CU 155 ? 1_555 ND1 ? A HIS 46  ? A HIS 47  ? 1_555 100.0 ? 
4   ND1 ? A HIS 63  ? A HIS 64  ? 1_555 ZN ? N  ZN . ? A ZN 156 ? 1_555 ND1 ? A HIS 71  ? A HIS 72  ? 1_555 107.3 ? 
5   ND1 ? A HIS 63  ? A HIS 64  ? 1_555 ZN ? N  ZN . ? A ZN 156 ? 1_555 ND1 ? A HIS 80  ? A HIS 81  ? 1_555 122.4 ? 
6   ND1 ? A HIS 71  ? A HIS 72  ? 1_555 ZN ? N  ZN . ? A ZN 156 ? 1_555 ND1 ? A HIS 80  ? A HIS 81  ? 1_555 118.6 ? 
7   ND1 ? A HIS 63  ? A HIS 64  ? 1_555 ZN ? N  ZN . ? A ZN 156 ? 1_555 OD1 ? A ASP 83  ? A ASP 84  ? 1_555 90.1  ? 
8   ND1 ? A HIS 71  ? A HIS 72  ? 1_555 ZN ? N  ZN . ? A ZN 156 ? 1_555 OD1 ? A ASP 83  ? A ASP 84  ? 1_555 91.2  ? 
9   ND1 ? A HIS 80  ? A HIS 81  ? 1_555 ZN ? N  ZN . ? A ZN 156 ? 1_555 OD1 ? A ASP 83  ? A ASP 84  ? 1_555 120.0 ? 
10  ND1 ? A HIS 63  ? A HIS 64  ? 1_555 ZN ? N  ZN . ? A ZN 156 ? 1_555 OD2 ? A ASP 83  ? A ASP 84  ? 1_555 141.7 ? 
11  ND1 ? A HIS 71  ? A HIS 72  ? 1_555 ZN ? N  ZN . ? A ZN 156 ? 1_555 OD2 ? A ASP 83  ? A ASP 84  ? 1_555 72.2  ? 
12  ND1 ? A HIS 80  ? A HIS 81  ? 1_555 ZN ? N  ZN . ? A ZN 156 ? 1_555 OD2 ? A ASP 83  ? A ASP 84  ? 1_555 86.9  ? 
13  OD1 ? A ASP 83  ? A ASP 84  ? 1_555 ZN ? N  ZN . ? A ZN 156 ? 1_555 OD2 ? A ASP 83  ? A ASP 84  ? 1_555 52.1  ? 
14  ND1 ? B HIS 46  ? B HIS 47  ? 1_555 CU A O  CU . ? B CU 155 ? 1_555 NE2 ? B HIS 120 ? B HIS 121 ? 1_555 104.5 ? 
15  ND1 ? B HIS 46  ? B HIS 47  ? 1_555 CU A O  CU . ? B CU 155 ? 1_555 NE2 ? B HIS 48  ? B HIS 49  ? 1_555 145.6 ? 
16  NE2 ? B HIS 120 ? B HIS 121 ? 1_555 CU A O  CU . ? B CU 155 ? 1_555 NE2 ? B HIS 48  ? B HIS 49  ? 1_555 95.5  ? 
17  ND1 ? B HIS 63  ? B HIS 64  ? 1_555 ZN ? P  ZN . ? B ZN 156 ? 1_555 ND1 ? B HIS 71  ? B HIS 72  ? 1_555 113.0 ? 
18  ND1 ? B HIS 63  ? B HIS 64  ? 1_555 ZN ? P  ZN . ? B ZN 156 ? 1_555 ND1 ? B HIS 80  ? B HIS 81  ? 1_555 114.6 ? 
19  ND1 ? B HIS 71  ? B HIS 72  ? 1_555 ZN ? P  ZN . ? B ZN 156 ? 1_555 ND1 ? B HIS 80  ? B HIS 81  ? 1_555 114.7 ? 
20  ND1 ? B HIS 63  ? B HIS 64  ? 1_555 ZN ? P  ZN . ? B ZN 156 ? 1_555 OD1 ? B ASP 83  ? B ASP 84  ? 1_555 94.1  ? 
21  ND1 ? B HIS 71  ? B HIS 72  ? 1_555 ZN ? P  ZN . ? B ZN 156 ? 1_555 OD1 ? B ASP 83  ? B ASP 84  ? 1_555 101.9 ? 
22  ND1 ? B HIS 80  ? B HIS 81  ? 1_555 ZN ? P  ZN . ? B ZN 156 ? 1_555 OD1 ? B ASP 83  ? B ASP 84  ? 1_555 116.2 ? 
23  ND1 ? B HIS 63  ? B HIS 64  ? 1_555 ZN ? P  ZN . ? B ZN 156 ? 1_555 OD2 ? B ASP 83  ? B ASP 84  ? 1_555 148.8 ? 
24  ND1 ? B HIS 71  ? B HIS 72  ? 1_555 ZN ? P  ZN . ? B ZN 156 ? 1_555 OD2 ? B ASP 83  ? B ASP 84  ? 1_555 72.9  ? 
25  ND1 ? B HIS 80  ? B HIS 81  ? 1_555 ZN ? P  ZN . ? B ZN 156 ? 1_555 OD2 ? B ASP 83  ? B ASP 84  ? 1_555 87.4  ? 
26  OD1 ? B ASP 83  ? B ASP 84  ? 1_555 ZN ? P  ZN . ? B ZN 156 ? 1_555 OD2 ? B ASP 83  ? B ASP 84  ? 1_555 55.2  ? 
27  ND1 ? C HIS 46  ? C HIS 47  ? 1_555 CU A S  CU . ? C CU 155 ? 1_555 NE2 ? C HIS 120 ? C HIS 121 ? 1_555 108.3 ? 
28  ND1 ? C HIS 63  ? C HIS 64  ? 1_555 ZN ? T  ZN . ? C ZN 156 ? 1_555 ND1 ? C HIS 71  ? C HIS 72  ? 1_555 107.7 ? 
29  ND1 ? C HIS 63  ? C HIS 64  ? 1_555 ZN ? T  ZN . ? C ZN 156 ? 1_555 ND1 ? C HIS 80  ? C HIS 81  ? 1_555 111.4 ? 
30  ND1 ? C HIS 71  ? C HIS 72  ? 1_555 ZN ? T  ZN . ? C ZN 156 ? 1_555 ND1 ? C HIS 80  ? C HIS 81  ? 1_555 124.6 ? 
31  ND1 ? C HIS 63  ? C HIS 64  ? 1_555 ZN ? T  ZN . ? C ZN 156 ? 1_555 OD1 ? C ASP 83  ? C ASP 84  ? 1_555 86.8  ? 
32  ND1 ? C HIS 71  ? C HIS 72  ? 1_555 ZN ? T  ZN . ? C ZN 156 ? 1_555 OD1 ? C ASP 83  ? C ASP 84  ? 1_555 102.3 ? 
33  ND1 ? C HIS 80  ? C HIS 81  ? 1_555 ZN ? T  ZN . ? C ZN 156 ? 1_555 OD1 ? C ASP 83  ? C ASP 84  ? 1_555 117.4 ? 
34  ND1 ? C HIS 63  ? C HIS 64  ? 1_555 ZN ? T  ZN . ? C ZN 156 ? 1_555 OD2 ? C ASP 83  ? C ASP 84  ? 1_555 143.5 ? 
35  ND1 ? C HIS 71  ? C HIS 72  ? 1_555 ZN ? T  ZN . ? C ZN 156 ? 1_555 OD2 ? C ASP 83  ? C ASP 84  ? 1_555 76.2  ? 
36  ND1 ? C HIS 80  ? C HIS 81  ? 1_555 ZN ? T  ZN . ? C ZN 156 ? 1_555 OD2 ? C ASP 83  ? C ASP 84  ? 1_555 93.4  ? 
37  OD1 ? C ASP 83  ? C ASP 84  ? 1_555 ZN ? T  ZN . ? C ZN 156 ? 1_555 OD2 ? C ASP 83  ? C ASP 84  ? 1_555 57.5  ? 
38  ND1 ? E HIS 46  ? E HIS 47  ? 1_555 CU A W  CU . ? E CU 155 ? 1_555 NE2 ? E HIS 48  ? E HIS 49  ? 1_555 146.5 ? 
39  ND1 ? E HIS 46  ? E HIS 47  ? 1_555 CU A W  CU . ? E CU 155 ? 1_555 NE2 ? E HIS 120 ? E HIS 121 ? 1_555 98.2  ? 
40  NE2 ? E HIS 48  ? E HIS 49  ? 1_555 CU A W  CU . ? E CU 155 ? 1_555 NE2 ? E HIS 120 ? E HIS 121 ? 1_555 88.3  ? 
41  ND1 ? E HIS 80  ? E HIS 81  ? 1_555 ZN ? X  ZN . ? E ZN 156 ? 1_555 OD2 ? E ASP 83  ? E ASP 84  ? 1_555 116.5 ? 
42  ND1 ? E HIS 80  ? E HIS 81  ? 1_555 ZN ? X  ZN . ? E ZN 156 ? 1_555 ND1 ? E HIS 71  ? E HIS 72  ? 1_555 113.0 ? 
43  OD2 ? E ASP 83  ? E ASP 84  ? 1_555 ZN ? X  ZN . ? E ZN 156 ? 1_555 ND1 ? E HIS 71  ? E HIS 72  ? 1_555 79.7  ? 
44  ND1 ? E HIS 80  ? E HIS 81  ? 1_555 ZN ? X  ZN . ? E ZN 156 ? 1_555 ND1 ? E HIS 63  ? E HIS 64  ? 1_555 101.8 ? 
45  OD2 ? E ASP 83  ? E ASP 84  ? 1_555 ZN ? X  ZN . ? E ZN 156 ? 1_555 ND1 ? E HIS 63  ? E HIS 64  ? 1_555 141.6 ? 
46  ND1 ? E HIS 71  ? E HIS 72  ? 1_555 ZN ? X  ZN . ? E ZN 156 ? 1_555 ND1 ? E HIS 63  ? E HIS 64  ? 1_555 83.4  ? 
47  ND1 ? F HIS 46  ? F HIS 47  ? 1_555 CU A Y  CU . ? F CU 155 ? 1_555 NE2 ? F HIS 120 ? F HIS 121 ? 1_555 108.2 ? 
48  ND1 ? F HIS 46  ? F HIS 47  ? 1_555 CU A Y  CU . ? F CU 155 ? 1_555 NE2 ? F HIS 48  ? F HIS 49  ? 1_555 148.8 ? 
49  NE2 ? F HIS 120 ? F HIS 121 ? 1_555 CU A Y  CU . ? F CU 155 ? 1_555 NE2 ? F HIS 48  ? F HIS 49  ? 1_555 95.9  ? 
50  ND1 ? F HIS 63  ? F HIS 64  ? 1_555 ZN ? Z  ZN . ? F ZN 156 ? 1_555 ND1 ? F HIS 71  ? F HIS 72  ? 1_555 115.3 ? 
51  ND1 ? F HIS 63  ? F HIS 64  ? 1_555 ZN ? Z  ZN . ? F ZN 156 ? 1_555 ND1 ? F HIS 80  ? F HIS 81  ? 1_555 110.5 ? 
52  ND1 ? F HIS 71  ? F HIS 72  ? 1_555 ZN ? Z  ZN . ? F ZN 156 ? 1_555 ND1 ? F HIS 80  ? F HIS 81  ? 1_555 126.4 ? 
53  ND1 ? F HIS 63  ? F HIS 64  ? 1_555 ZN ? Z  ZN . ? F ZN 156 ? 1_555 OD1 ? F ASP 83  ? F ASP 84  ? 1_555 81.9  ? 
54  ND1 ? F HIS 71  ? F HIS 72  ? 1_555 ZN ? Z  ZN . ? F ZN 156 ? 1_555 OD1 ? F ASP 83  ? F ASP 84  ? 1_555 103.5 ? 
55  ND1 ? F HIS 80  ? F HIS 81  ? 1_555 ZN ? Z  ZN . ? F ZN 156 ? 1_555 OD1 ? F ASP 83  ? F ASP 84  ? 1_555 109.2 ? 
56  ND1 ? F HIS 63  ? F HIS 64  ? 1_555 ZN ? Z  ZN . ? F ZN 156 ? 1_555 OD2 ? F ASP 83  ? F ASP 84  ? 1_555 136.9 ? 
57  ND1 ? F HIS 71  ? F HIS 72  ? 1_555 ZN ? Z  ZN . ? F ZN 156 ? 1_555 OD2 ? F ASP 83  ? F ASP 84  ? 1_555 74.9  ? 
58  ND1 ? F HIS 80  ? F HIS 81  ? 1_555 ZN ? Z  ZN . ? F ZN 156 ? 1_555 OD2 ? F ASP 83  ? F ASP 84  ? 1_555 90.3  ? 
59  OD1 ? F ASP 83  ? F ASP 84  ? 1_555 ZN ? Z  ZN . ? F ZN 156 ? 1_555 OD2 ? F ASP 83  ? F ASP 84  ? 1_555 55.3  ? 
60  ND1 ? G HIS 46  ? G HIS 47  ? 1_555 CU A AA CU . ? G CU 155 ? 1_555 NE2 ? G HIS 120 ? G HIS 121 ? 1_555 109.7 ? 
61  ND1 ? G HIS 63  ? G HIS 64  ? 1_555 ZN ? BA ZN . ? G ZN 156 ? 1_555 ND1 ? G HIS 71  ? G HIS 72  ? 1_555 102.4 ? 
62  ND1 ? G HIS 63  ? G HIS 64  ? 1_555 ZN ? BA ZN . ? G ZN 156 ? 1_555 ND1 ? G HIS 80  ? G HIS 81  ? 1_555 119.8 ? 
63  ND1 ? G HIS 71  ? G HIS 72  ? 1_555 ZN ? BA ZN . ? G ZN 156 ? 1_555 ND1 ? G HIS 80  ? G HIS 81  ? 1_555 116.9 ? 
64  ND1 ? G HIS 63  ? G HIS 64  ? 1_555 ZN ? BA ZN . ? G ZN 156 ? 1_555 OD1 ? G ASP 83  ? G ASP 84  ? 1_555 89.8  ? 
65  ND1 ? G HIS 71  ? G HIS 72  ? 1_555 ZN ? BA ZN . ? G ZN 156 ? 1_555 OD1 ? G ASP 83  ? G ASP 84  ? 1_555 91.4  ? 
66  ND1 ? G HIS 80  ? G HIS 81  ? 1_555 ZN ? BA ZN . ? G ZN 156 ? 1_555 OD1 ? G ASP 83  ? G ASP 84  ? 1_555 129.8 ? 
67  ND1 ? G HIS 63  ? G HIS 64  ? 1_555 ZN ? BA ZN . ? G ZN 156 ? 1_555 OD2 ? G ASP 83  ? G ASP 84  ? 1_555 143.8 ? 
68  ND1 ? G HIS 71  ? G HIS 72  ? 1_555 ZN ? BA ZN . ? G ZN 156 ? 1_555 OD2 ? G ASP 83  ? G ASP 84  ? 1_555 70.6  ? 
69  ND1 ? G HIS 80  ? G HIS 81  ? 1_555 ZN ? BA ZN . ? G ZN 156 ? 1_555 OD2 ? G ASP 83  ? G ASP 84  ? 1_555 93.6  ? 
70  OD1 ? G ASP 83  ? G ASP 84  ? 1_555 ZN ? BA ZN . ? G ZN 156 ? 1_555 OD2 ? G ASP 83  ? G ASP 84  ? 1_555 55.9  ? 
71  ND1 ? H HIS 46  ? H HIS 47  ? 1_555 CU A CA CU . ? H CU 155 ? 1_555 NE2 ? H HIS 120 ? H HIS 121 ? 1_555 105.4 ? 
72  ND1 ? H HIS 46  ? H HIS 47  ? 1_555 CU A CA CU . ? H CU 155 ? 1_555 NE2 ? H HIS 48  ? H HIS 49  ? 1_555 142.5 ? 
73  NE2 ? H HIS 120 ? H HIS 121 ? 1_555 CU A CA CU . ? H CU 155 ? 1_555 NE2 ? H HIS 48  ? H HIS 49  ? 1_555 91.6  ? 
74  ND1 ? H HIS 63  ? H HIS 64  ? 1_555 ZN ? DA ZN . ? H ZN 156 ? 1_555 ND1 ? H HIS 71  ? H HIS 72  ? 1_555 113.3 ? 
75  ND1 ? H HIS 63  ? H HIS 64  ? 1_555 ZN ? DA ZN . ? H ZN 156 ? 1_555 ND1 ? H HIS 80  ? H HIS 81  ? 1_555 115.3 ? 
76  ND1 ? H HIS 71  ? H HIS 72  ? 1_555 ZN ? DA ZN . ? H ZN 156 ? 1_555 ND1 ? H HIS 80  ? H HIS 81  ? 1_555 128.0 ? 
77  ND1 ? H HIS 63  ? H HIS 64  ? 1_555 ZN ? DA ZN . ? H ZN 156 ? 1_555 OD1 ? H ASP 83  ? H ASP 84  ? 1_555 82.8  ? 
78  ND1 ? H HIS 71  ? H HIS 72  ? 1_555 ZN ? DA ZN . ? H ZN 156 ? 1_555 OD1 ? H ASP 83  ? H ASP 84  ? 1_555 95.7  ? 
79  ND1 ? H HIS 80  ? H HIS 81  ? 1_555 ZN ? DA ZN . ? H ZN 156 ? 1_555 OD1 ? H ASP 83  ? H ASP 84  ? 1_555 107.3 ? 
80  ND1 ? I HIS 46  ? I HIS 47  ? 1_555 CU A EA CU . ? I CU 155 ? 1_555 NE2 ? I HIS 120 ? I HIS 121 ? 1_555 107.2 ? 
81  ND1 ? I HIS 46  ? I HIS 47  ? 1_555 CU A EA CU . ? I CU 155 ? 1_555 NE2 ? I HIS 48  ? I HIS 49  ? 1_555 141.0 ? 
82  NE2 ? I HIS 120 ? I HIS 121 ? 1_555 CU A EA CU . ? I CU 155 ? 1_555 NE2 ? I HIS 48  ? I HIS 49  ? 1_555 91.5  ? 
83  ND1 ? I HIS 63  ? I HIS 64  ? 1_555 ZN ? FA ZN . ? I ZN 156 ? 1_555 ND1 ? I HIS 71  ? I HIS 72  ? 1_555 106.6 ? 
84  ND1 ? I HIS 63  ? I HIS 64  ? 1_555 ZN ? FA ZN . ? I ZN 156 ? 1_555 ND1 ? I HIS 80  ? I HIS 81  ? 1_555 113.2 ? 
85  ND1 ? I HIS 71  ? I HIS 72  ? 1_555 ZN ? FA ZN . ? I ZN 156 ? 1_555 ND1 ? I HIS 80  ? I HIS 81  ? 1_555 125.3 ? 
86  ND1 ? I HIS 63  ? I HIS 64  ? 1_555 ZN ? FA ZN . ? I ZN 156 ? 1_555 OD1 ? I ASP 83  ? I ASP 84  ? 1_555 84.7  ? 
87  ND1 ? I HIS 71  ? I HIS 72  ? 1_555 ZN ? FA ZN . ? I ZN 156 ? 1_555 OD1 ? I ASP 83  ? I ASP 84  ? 1_555 100.1 ? 
88  ND1 ? I HIS 80  ? I HIS 81  ? 1_555 ZN ? FA ZN . ? I ZN 156 ? 1_555 OD1 ? I ASP 83  ? I ASP 84  ? 1_555 119.1 ? 
89  ND1 ? I HIS 63  ? I HIS 64  ? 1_555 ZN ? FA ZN . ? I ZN 156 ? 1_555 OD2 ? I ASP 83  ? I ASP 84  ? 1_555 141.2 ? 
90  ND1 ? I HIS 71  ? I HIS 72  ? 1_555 ZN ? FA ZN . ? I ZN 156 ? 1_555 OD2 ? I ASP 83  ? I ASP 84  ? 1_555 77.7  ? 
91  ND1 ? I HIS 80  ? I HIS 81  ? 1_555 ZN ? FA ZN . ? I ZN 156 ? 1_555 OD2 ? I ASP 83  ? I ASP 84  ? 1_555 92.4  ? 
92  OD1 ? I ASP 83  ? I ASP 84  ? 1_555 ZN ? FA ZN . ? I ZN 156 ? 1_555 OD2 ? I ASP 83  ? I ASP 84  ? 1_555 56.9  ? 
93  ND1 ? J HIS 46  ? J HIS 47  ? 1_555 CU A GA CU . ? J CU 155 ? 1_555 NE2 ? J HIS 120 ? J HIS 121 ? 1_555 105.9 ? 
94  ND1 ? J HIS 46  ? J HIS 47  ? 1_555 CU A GA CU . ? J CU 155 ? 1_555 NE2 ? J HIS 48  ? J HIS 49  ? 1_555 146.2 ? 
95  NE2 ? J HIS 120 ? J HIS 121 ? 1_555 CU A GA CU . ? J CU 155 ? 1_555 NE2 ? J HIS 48  ? J HIS 49  ? 1_555 90.7  ? 
96  ND1 ? J HIS 63  ? J HIS 64  ? 1_555 ZN ? HA ZN . ? J ZN 156 ? 1_555 ND1 ? J HIS 71  ? J HIS 72  ? 1_555 111.0 ? 
97  ND1 ? J HIS 63  ? J HIS 64  ? 1_555 ZN ? HA ZN . ? J ZN 156 ? 1_555 ND1 ? J HIS 80  ? J HIS 81  ? 1_555 115.6 ? 
98  ND1 ? J HIS 71  ? J HIS 72  ? 1_555 ZN ? HA ZN . ? J ZN 156 ? 1_555 ND1 ? J HIS 80  ? J HIS 81  ? 1_555 121.5 ? 
99  ND1 ? J HIS 63  ? J HIS 64  ? 1_555 ZN ? HA ZN . ? J ZN 156 ? 1_555 OD1 ? J ASP 83  ? J ASP 84  ? 1_555 84.8  ? 
100 ND1 ? J HIS 71  ? J HIS 72  ? 1_555 ZN ? HA ZN . ? J ZN 156 ? 1_555 OD1 ? J ASP 83  ? J ASP 84  ? 1_555 100.7 ? 
101 ND1 ? J HIS 80  ? J HIS 81  ? 1_555 ZN ? HA ZN . ? J ZN 156 ? 1_555 OD1 ? J ASP 83  ? J ASP 84  ? 1_555 116.5 ? 
102 ND1 ? J HIS 63  ? J HIS 64  ? 1_555 ZN ? HA ZN . ? J ZN 156 ? 1_555 OD2 ? J ASP 83  ? J ASP 84  ? 1_555 140.4 ? 
103 ND1 ? J HIS 71  ? J HIS 72  ? 1_555 ZN ? HA ZN . ? J ZN 156 ? 1_555 OD2 ? J ASP 83  ? J ASP 84  ? 1_555 74.0  ? 
104 ND1 ? J HIS 80  ? J HIS 81  ? 1_555 ZN ? HA ZN . ? J ZN 156 ? 1_555 OD2 ? J ASP 83  ? J ASP 84  ? 1_555 90.4  ? 
105 OD1 ? J ASP 83  ? J ASP 84  ? 1_555 ZN ? HA ZN . ? J ZN 156 ? 1_555 OD2 ? J ASP 83  ? J ASP 84  ? 1_555 56.2  ? 
106 ND1 ? K HIS 46  ? K HIS 47  ? 1_555 CU A JA CU . ? K CU 155 ? 1_555 NE2 ? K HIS 120 ? K HIS 121 ? 1_555 98.7  ? 
107 ND1 ? K HIS 46  ? K HIS 47  ? 1_555 CU A JA CU . ? K CU 155 ? 1_555 NE2 ? K HIS 48  ? K HIS 49  ? 1_555 134.7 ? 
108 NE2 ? K HIS 120 ? K HIS 121 ? 1_555 CU A JA CU . ? K CU 155 ? 1_555 NE2 ? K HIS 48  ? K HIS 49  ? 1_555 87.4  ? 
109 ND1 ? K HIS 46  ? K HIS 47  ? 1_555 CU A JA CU . ? K CU 155 ? 1_555 NE2 ? K HIS 63  ? K HIS 64  ? 1_555 95.6  ? 
110 NE2 ? K HIS 120 ? K HIS 121 ? 1_555 CU A JA CU . ? K CU 155 ? 1_555 NE2 ? K HIS 63  ? K HIS 64  ? 1_555 139.1 ? 
111 NE2 ? K HIS 48  ? K HIS 49  ? 1_555 CU A JA CU . ? K CU 155 ? 1_555 NE2 ? K HIS 63  ? K HIS 64  ? 1_555 108.6 ? 
112 ND1 ? K HIS 63  ? K HIS 64  ? 1_555 ZN ? KA ZN . ? K ZN 156 ? 1_555 ND1 ? K HIS 71  ? K HIS 72  ? 1_555 106.6 ? 
113 ND1 ? K HIS 63  ? K HIS 64  ? 1_555 ZN ? KA ZN . ? K ZN 156 ? 1_555 ND1 ? K HIS 80  ? K HIS 81  ? 1_555 126.7 ? 
114 ND1 ? K HIS 71  ? K HIS 72  ? 1_555 ZN ? KA ZN . ? K ZN 156 ? 1_555 ND1 ? K HIS 80  ? K HIS 81  ? 1_555 125.2 ? 
115 ND1 ? K HIS 63  ? K HIS 64  ? 1_555 ZN ? KA ZN . ? K ZN 156 ? 1_555 OD1 ? K ASP 83  ? K ASP 84  ? 1_555 71.9  ? 
116 ND1 ? K HIS 71  ? K HIS 72  ? 1_555 ZN ? KA ZN . ? K ZN 156 ? 1_555 OD1 ? K ASP 83  ? K ASP 84  ? 1_555 81.0  ? 
117 ND1 ? K HIS 80  ? K HIS 81  ? 1_555 ZN ? KA ZN . ? K ZN 156 ? 1_555 OD1 ? K ASP 83  ? K ASP 84  ? 1_555 102.2 ? 
118 ND1 ? L HIS 46  ? L HIS 47  ? 1_555 CU A LA CU . ? L CU 155 ? 1_555 NE2 ? L HIS 48  ? L HIS 49  ? 1_555 158.8 ? 
119 ND1 ? L HIS 46  ? L HIS 47  ? 1_555 CU A LA CU . ? L CU 155 ? 1_555 NE2 ? L HIS 120 ? L HIS 121 ? 1_555 99.5  ? 
120 NE2 ? L HIS 48  ? L HIS 49  ? 1_555 CU A LA CU . ? L CU 155 ? 1_555 NE2 ? L HIS 120 ? L HIS 121 ? 1_555 95.2  ? 
121 ND1 ? L HIS 63  ? L HIS 64  ? 1_555 ZN ? MA ZN . ? L ZN 156 ? 1_555 ND1 ? L HIS 71  ? L HIS 72  ? 1_555 112.6 ? 
122 ND1 ? L HIS 63  ? L HIS 64  ? 1_555 ZN ? MA ZN . ? L ZN 156 ? 1_555 ND1 ? L HIS 80  ? L HIS 81  ? 1_555 113.0 ? 
123 ND1 ? L HIS 71  ? L HIS 72  ? 1_555 ZN ? MA ZN . ? L ZN 156 ? 1_555 ND1 ? L HIS 80  ? L HIS 81  ? 1_555 112.5 ? 
124 ND1 ? L HIS 63  ? L HIS 64  ? 1_555 ZN ? MA ZN . ? L ZN 156 ? 1_555 OD1 ? L ASP 83  ? L ASP 84  ? 1_555 95.2  ? 
125 ND1 ? L HIS 71  ? L HIS 72  ? 1_555 ZN ? MA ZN . ? L ZN 156 ? 1_555 OD1 ? L ASP 83  ? L ASP 84  ? 1_555 105.8 ? 
126 ND1 ? L HIS 80  ? L HIS 81  ? 1_555 ZN ? MA ZN . ? L ZN 156 ? 1_555 OD1 ? L ASP 83  ? L ASP 84  ? 1_555 116.5 ? 
127 ND1 ? L HIS 63  ? L HIS 64  ? 1_555 ZN ? MA ZN . ? L ZN 156 ? 1_555 OD2 ? L ASP 83  ? L ASP 84  ? 1_555 150.7 ? 
128 ND1 ? L HIS 71  ? L HIS 72  ? 1_555 ZN ? MA ZN . ? L ZN 156 ? 1_555 OD2 ? L ASP 83  ? L ASP 84  ? 1_555 73.1  ? 
129 ND1 ? L HIS 80  ? L HIS 81  ? 1_555 ZN ? MA ZN . ? L ZN 156 ? 1_555 OD2 ? L ASP 83  ? L ASP 84  ? 1_555 88.9  ? 
130 OD1 ? L ASP 83  ? L ASP 84  ? 1_555 ZN ? MA ZN . ? L ZN 156 ? 1_555 OD2 ? L ASP 83  ? L ASP 84  ? 1_555 56.5  ? 
131 ND1 ? D HIS 80  ? D HIS 81  ? 1_555 ZN ? V  ZN . ? D ZN 156 ? 1_555 OD1 ? D ASP 83  ? D ASP 84  ? 1_555 125.8 ? 
# 
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 2010-08-11 
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         ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Version format compliance' 
# 
loop_
_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[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.pdbx_refine_id 
1  ? refined 24.4313 -49.9097  -21.1910 0.4139 0.1781 0.3514 -0.0350 -0.0667 0.0303  3.2744 7.2183 3.7510 0.7487  0.3096  0.1411  
0.1558  -0.0308 -0.1251 -0.0448 -0.5022 -0.2409 0.7686  0.4991  0.1612  'X-RAY DIFFRACTION' 
2  ? refined 21.9960 -23.2487  -30.3087 0.0521 0.2187 0.1735 -0.0983 -0.0167 0.0016  2.1522 7.2689 3.1711 -0.9171 0.4097  -0.7853 
0.1215  -0.1554 0.0339  -0.0481 -0.1694 -0.1793 0.1525  -0.1192 0.1804  'X-RAY DIFFRACTION' 
3  ? refined 23.7635 8.2147    -24.7897 0.7980 0.2997 0.3946 -0.2973 0.2961  -0.1415 5.9731 8.2655 7.4126 4.1013  0.5654  0.8692  
1.3358  -1.1060 -0.2298 -0.7736 0.6771  0.5968  1.5519  -0.5194 -0.0183 'X-RAY DIFFRACTION' 
4  ? refined 29.5329 29.4846   -7.0148  1.8306 0.7554 0.9753 -0.7285 0.5790  -0.6373 2.4899 1.8470 2.4108 0.5688  -1.4693 -1.9231 
0.3452  -0.0927 -0.2525 -0.4842 0.9601  0.1022  0.8305  -0.6618 0.0694  'X-RAY DIFFRACTION' 
5  ? refined 12.1561 1.1889    -81.9817 0.5932 1.9314 0.3790 0.1944  -0.1393 0.1829  4.8288 4.8750 6.8400 0.6980  0.8190  -0.7047 
0.1499  -0.0060 -0.1439 1.7489  0.5114  0.3482  -0.7859 -0.5637 -0.9815 'X-RAY DIFFRACTION' 
6  ? refined 17.0676 -2.9103   -54.3841 0.0942 0.4460 0.2699 0.0973  -0.0879 -0.0472 4.7782 4.0620 7.4643 0.0312  -1.3737 -1.5419 
0.1908  -0.1887 -0.0021 0.9023  0.2463  0.1255  -0.1229 -0.3568 -0.0593 'X-RAY DIFFRACTION' 
7  ? refined 16.8071 -45.7141  -58.8609 0.9679 0.3148 0.5406 0.2679  -0.2116 -0.0870 1.7988 7.1795 5.2668 -1.0241 -0.5424 -0.2508 
0.2991  -0.2947 -0.0044 0.2318  0.3372  0.4657  -1.3705 -0.6551 -0.2638 'X-RAY DIFFRACTION' 
8  ? refined 17.8359 -72.4777  -49.3801 0.2917 0.1758 0.2744 0.1320  -0.1746 -0.1223 2.7682 7.8526 4.0150 1.2791  -0.6031 0.4899  
0.2017  -0.3597 0.1580  0.0302  -0.0697 0.3328  -0.7080 -0.3704 -0.1084 'X-RAY DIFFRACTION' 
9  ? refined 14.1661 -126.2632 -72.3537 0.3979 0.1912 0.3902 0.0320  0.0712  -0.1226 4.3934 4.4077 5.1304 1.1024  2.0547  1.4769  
0.0676  -0.0648 -0.0028 0.2312  -0.3905 -0.1320 -0.1605 0.7952  0.0384  'X-RAY DIFFRACTION' 
10 ? refined 16.7888 -104.3244 -54.6040 0.0031 0.1188 0.3528 0.0096  -0.0167 -0.0682 3.3692 4.4276 5.8625 -0.7387 0.3815  2.3823  
0.0318  -0.0480 0.0163  -0.0969 0.0174  -0.1752 -0.0600 -0.0627 0.2816  'X-RAY DIFFRACTION' 
11 ? refined 30.3584 -97.9055  1.6761   0.6855 1.4958 0.3328 -0.0340 0.0007  0.2584  5.2207 4.2830 7.1028 0.9784  -1.3866 -0.8843 
-0.0246 -0.2963 0.3209  -1.5516 -0.5334 -0.1015 0.8752  0.6845  0.9814  'X-RAY DIFFRACTION' 
12 ? refined 23.1565 -93.0065  -25.2774 0.1773 0.4100 0.2611 -0.1199 0.0519  -0.0512 4.3295 3.5343 7.6604 -0.2018 1.5269  -1.2132 
0.1032  -0.2509 0.1477  -0.4247 -0.2909 0.1062  0.3294  0.1552  0.3157  'X-RAY DIFFRACTION' 
# 
loop_
_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.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.selection_details 
1  1  A 2 A 154 ? . . . . 'X-RAY DIFFRACTION' ? 
2  2  B 2 B 154 ? . . . . 'X-RAY DIFFRACTION' ? 
3  3  C 2 C 154 ? . . . . 'X-RAY DIFFRACTION' ? 
4  4  D 2 D 154 ? . . . . 'X-RAY DIFFRACTION' ? 
5  5  E 2 E 154 ? . . . . 'X-RAY DIFFRACTION' ? 
6  6  F 2 F 154 ? . . . . 'X-RAY DIFFRACTION' ? 
7  7  G 2 G 154 ? . . . . 'X-RAY DIFFRACTION' ? 
8  8  H 2 H 154 ? . . . . 'X-RAY DIFFRACTION' ? 
9  9  I 2 I 154 ? . . . . 'X-RAY DIFFRACTION' ? 
10 10 J 2 J 154 ? . . . . 'X-RAY DIFFRACTION' ? 
11 11 K 2 K 154 ? . . . . 'X-RAY DIFFRACTION' ? 
12 12 L 2 L 154 ? . . . . 'X-RAY DIFFRACTION' ? 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
XSCALE      .        ?               package 'Wolfgang Kabsch'    ?                     'data scaling'    
http://www.mpimf-heidelberg.mpg.de/~kabsch/xds/html_doc/xscale_program.html ?          ? 1 
REFMAC      5.5.0102 ?               program 'Garib N. Murshudov' garib@ysbl.york.ac.uk refinement        
http://www.ccp4.ac.uk/dist/html/refmac5.html                                Fortran_77 ? 2 
PDB_EXTRACT 3.006    'June 11, 2008' package PDB                  help@deposit.rcsb.org 'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                   C++        ? 3 
XDS         .        ?               ?       ?                    ?                     'data reduction'  ? ?          ? 4 
# 
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 E ASP 84 ? ? ZN  E ZN  156 ? ? 1.69 
2 1 O   D LYS 10 ? ? O   D CYS 147 ? ? 2.02 
3 1 O   D PHE 51 ? ? OG1 D THR 117 ? ? 2.15 
# 
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 CD1 A TRP 33 ? ? 1_555 OE1 I GLU 133 ? ? 2_545 2.05 
2 1 CB  F PRO 14 ? ? 1_555 OE1 H GLU 41  ? ? 3_554 2.17 
# 
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 ALA A 56  ? ? -102.28 47.66   
2  1 LYS A 92  ? ? -18.56  -64.15  
3  1 SER A 99  ? ? -151.39 86.86   
4  1 ALA B 56  ? ? -105.90 49.52   
5  1 LYS B 92  ? ? -15.81  -65.03  
6  1 SER B 99  ? ? -151.10 88.99   
7  1 ALA C 56  ? ? -102.99 52.13   
8  1 LYS C 92  ? ? -18.00  -62.80  
9  1 SER C 99  ? ? -152.33 82.21   
10 1 LYS D 10  ? ? -65.68  -168.96 
11 1 ASP D 12  ? ? -143.32 31.90   
12 1 PRO D 14  ? ? -99.97  33.27   
13 1 VAL D 32  ? ? -170.92 103.69  
14 1 SER D 35  ? ? 162.20  -177.39 
15 1 ILE D 36  ? ? -158.26 85.33   
16 1 THR D 40  ? ? -81.39  -128.59 
17 1 ASP D 53  ? ? -152.79 71.41   
18 1 LEU D 68  ? ? -96.81  -71.02  
19 1 SER D 69  ? ? 158.30  33.63   
20 1 HIS D 72  ? ? -47.74  150.61  
21 1 VAL D 82  ? ? -54.83  -7.64   
22 1 VAL D 95  ? ? -108.03 60.70   
23 1 SER D 99  ? ? -161.69 59.46   
24 1 LEU D 107 ? ? -105.93 54.93   
25 1 SER D 108 ? ? 178.74  151.43  
26 1 CYS D 112 ? ? -40.48  105.11  
27 1 LYS D 137 ? ? -144.49 -55.08  
28 1 ALA E 56  ? ? -101.04 50.08   
29 1 LYS E 92  ? ? -17.13  -65.73  
30 1 VAL E 95  ? ? 85.87   -154.66 
31 1 SER E 99  ? ? -152.13 87.64   
32 1 ALA F 56  ? ? -99.00  47.39   
33 1 LYS F 92  ? ? -16.13  -64.41  
34 1 SER F 99  ? ? -151.27 88.12   
35 1 ALA G 56  ? ? -103.50 48.71   
36 1 LYS G 92  ? ? -17.65  -64.16  
37 1 SER G 99  ? ? -151.62 87.32   
38 1 ALA H 56  ? ? -102.01 47.69   
39 1 LYS H 92  ? ? -18.45  -64.65  
40 1 SER H 99  ? ? -152.75 89.59   
41 1 ALA I 56  ? ? -102.35 48.79   
42 1 LYS I 92  ? ? -17.35  -64.17  
43 1 SER I 99  ? ? -151.34 86.59   
44 1 ALA J 56  ? ? -101.09 47.07   
45 1 LYS J 92  ? ? -17.61  -64.12  
46 1 SER J 99  ? ? -153.62 87.65   
47 1 ALA K 56  ? ? -101.10 48.60   
48 1 LYS K 92  ? ? -16.38  -65.02  
49 1 SER K 99  ? ? -153.85 86.52   
50 1 ALA L 56  ? ? -102.15 48.66   
51 1 LYS L 92  ? ? -16.73  -64.92  
52 1 SER L 99  ? ? -151.17 88.93   
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   VAL 
_pdbx_validate_peptide_omega.auth_asym_id_1   E 
_pdbx_validate_peptide_omega.auth_seq_id_1    95 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   ALA 
_pdbx_validate_peptide_omega.auth_asym_id_2   E 
_pdbx_validate_peptide_omega.auth_seq_id_2    96 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -46.39 
# 
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 E VAL 95 ? CG1 ? E VAL 94 CG1 
2 1 Y 1 E VAL 95 ? CG2 ? E VAL 94 CG2 
3 1 Y 1 K ARG 70 ? CG  ? K ARG 69 CG  
4 1 Y 1 K ARG 70 ? CD  ? K ARG 69 CD  
5 1 Y 1 K ARG 70 ? NE  ? K ARG 69 NE  
6 1 Y 1 K ARG 70 ? CZ  ? K ARG 69 CZ  
7 1 Y 1 K ARG 70 ? NH1 ? K ARG 69 NH1 
8 1 Y 1 K ARG 70 ? NH2 ? K ARG 69 NH2 
# 
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 'SULFATE ION'     SO4 
# 
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 
M  2 CU  1 155 155 CU  CU  A . 
N  3 ZN  1 156 156 ZN  ZN  A . 
O  2 CU  1 155 155 CU  CU  B . 
P  3 ZN  1 156 156 ZN  ZN  B . 
Q  4 SO4 1 1   1   SO4 SO4 B . 
R  4 SO4 1 157 1   SO4 SO4 B . 
S  2 CU  1 155 155 CU  CU  C . 
T  3 ZN  1 156 156 ZN  ZN  C . 
U  2 CU  1 155 155 CU  CU  D . 
V  3 ZN  1 156 156 ZN  ZN  D . 
W  2 CU  1 155 155 CU  CU  E . 
X  3 ZN  1 156 156 ZN  ZN  E . 
Y  2 CU  1 155 155 CU  CU  F . 
Z  3 ZN  1 156 156 ZN  ZN  F . 
AA 2 CU  1 155 155 CU  CU  G . 
BA 3 ZN  1 156 156 ZN  ZN  G . 
CA 2 CU  1 155 155 CU  CU  H . 
DA 3 ZN  1 156 156 ZN  ZN  H . 
EA 2 CU  1 155 155 CU  CU  I . 
FA 3 ZN  1 156 156 ZN  ZN  I . 
GA 2 CU  1 155 155 CU  CU  J . 
HA 3 ZN  1 156 156 ZN  ZN  J . 
IA 4 SO4 1 157 2   SO4 SO4 J . 
JA 2 CU  1 155 155 CU  CU  K . 
KA 3 ZN  1 156 156 ZN  ZN  K . 
LA 2 CU  1 155 155 CU  CU  L . 
MA 3 ZN  1 156 156 ZN  ZN  L . 
# 
