data_3GTV
# 
_entry.id   3GTV 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.283 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3GTV         
RCSB  RCSB052299   
WWPDB D_1000052299 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 3GTT . unspecified 
PDB 3GTW . unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        3GTV 
_pdbx_database_status.recvd_initial_deposition_date   2009-03-28 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Seetharaman, S.V.' 1 
'Taylor, A.B.'      2 
'Hart, P.J.'        3 
# 
_citation.id                        primary 
_citation.title                     'Structures of mouse SOD1 and human/mouse SOD1 chimeras.' 
_citation.journal_abbrev            Arch.Biochem.Biophys. 
_citation.journal_volume            503 
_citation.page_first                183 
_citation.page_last                 190 
_citation.year                      2010 
_citation.journal_id_ASTM           ABBIA4 
_citation.country                   US 
_citation.journal_id_ISSN           0003-9861 
_citation.journal_id_CSD            0158 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   20727846 
_citation.pdbx_database_id_DOI      10.1016/j.abb.2010.08.014 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Seetharaman, S.V.' 1 
primary 'Taylor, A.B.'      2 
primary 'Holloway, S.'      3 
primary 'Hart, P.J.'        4 
# 
_cell.entry_id           3GTV 
_cell.length_a           112.625 
_cell.length_b           144.007 
_cell.length_c           112.613 
_cell.angle_alpha        90.00 
_cell.angle_beta         119.82 
_cell.angle_gamma        90.00 
_cell.Z_PDB              24 
_cell.pdbx_unique_axis   ? 
_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                         3GTV 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_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]' 15911.709 12   1.15.1.1 ? 
'residues 2-81 from human protein, residues 82-154 from mouse protein' ? 
2 non-polymer syn 'ZINC ION'                     65.409    12   ?        ? ? ? 
3 water       nat water                          18.015    1808 ?        ? ? ? 
# 
_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
VGDLGNVTAGKDGVANVSIEDRVISLSGEHSIIGRTMVVHEKQDDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTAGKDGVANVSIEDRVISLSGEHSIIGRTMVVHEKQDDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_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  GLY n 
1 91  LYS n 
1 92  ASP n 
1 93  GLY n 
1 94  VAL n 
1 95  ALA n 
1 96  ASN n 
1 97  VAL n 
1 98  SER n 
1 99  ILE n 
1 100 GLU n 
1 101 ASP n 
1 102 ARG 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 GLU n 
1 110 HIS n 
1 111 SER n 
1 112 ILE n 
1 113 ILE n 
1 114 GLY n 
1 115 ARG n 
1 116 THR n 
1 117 MET n 
1 118 VAL n 
1 119 VAL n 
1 120 HIS n 
1 121 GLU n 
1 122 LYS n 
1 123 GLN 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 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_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 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
_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 
_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 
1 1 sample ? 1  80  'human, mouse' ? SOD1 ? ? ? ? ? ? 'Homo sapiens' 9606  ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? 
'BL21(DE3)' ? ? ? ? ? ? ? plasmid ? ? ? pKA8H ? ? 
1 2 sample ? 81 153 'human, mouse' ? SOD1 ? ? ? ? ? ? 'Mus musculus' 10090 ? ? ? ? ? ? ? ? 'Escherichia coli' 562 ? ? ? ? ? ? 
'BL21(DE3)' ? ? ? ? ? ? ? plasmid ? ? ? pKA8H ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
_struct_ref.pdbx_db_isoform 
1 UNP SODC_HUMAN P00441 1 
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH

;
2  ? 
2 UNP SODC_MOUSE P08228 1 VGDLGNVTAGKDGVANVSIEDRVISLSGEHSIIGRTMVVHEKQDDLGKGGNEESTKTGNAGSRLACGVIGIAQ           82 ? 
# 
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 3GTV A 1  ? 80  ? P00441 2  ? 81  ? 1  80  
2  2 3GTV A 81 ? 153 ? P08228 82 ? 154 ? 81 153 
3  1 3GTV B 1  ? 80  ? P00441 2  ? 81  ? 1  80  
4  2 3GTV B 81 ? 153 ? P08228 82 ? 154 ? 81 153 
5  1 3GTV C 1  ? 80  ? P00441 2  ? 81  ? 1  80  
6  2 3GTV C 81 ? 153 ? P08228 82 ? 154 ? 81 153 
7  1 3GTV D 1  ? 80  ? P00441 2  ? 81  ? 1  80  
8  2 3GTV D 81 ? 153 ? P08228 82 ? 154 ? 81 153 
9  1 3GTV E 1  ? 80  ? P00441 2  ? 81  ? 1  80  
10 2 3GTV E 81 ? 153 ? P08228 82 ? 154 ? 81 153 
11 1 3GTV F 1  ? 80  ? P00441 2  ? 81  ? 1  80  
12 2 3GTV F 81 ? 153 ? P08228 82 ? 154 ? 81 153 
13 1 3GTV G 1  ? 80  ? P00441 2  ? 81  ? 1  80  
14 2 3GTV G 81 ? 153 ? P08228 82 ? 154 ? 81 153 
15 1 3GTV H 1  ? 80  ? P00441 2  ? 81  ? 1  80  
16 2 3GTV H 81 ? 153 ? P08228 82 ? 154 ? 81 153 
17 1 3GTV I 1  ? 80  ? P00441 2  ? 81  ? 1  80  
18 2 3GTV I 81 ? 153 ? P08228 82 ? 154 ? 81 153 
19 1 3GTV J 1  ? 80  ? P00441 2  ? 81  ? 1  80  
20 2 3GTV J 81 ? 153 ? P08228 82 ? 154 ? 81 153 
21 1 3GTV K 1  ? 80  ? P00441 2  ? 81  ? 1  80  
22 2 3GTV K 81 ? 153 ? P08228 82 ? 154 ? 81 153 
23 1 3GTV L 1  ? 80  ? P00441 2  ? 81  ? 1  80  
24 2 3GTV L 81 ? 153 ? P08228 82 ? 154 ? 81 153 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'      ? 'Zn 2'           65.409  
# 
_exptl.entry_id          3GTV 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      4.15 
_exptl_crystal.density_percent_sol   70.36 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    '0.1 m HEPES, 25% PEG 8000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   'RIGAKU RAXIS VII' 
_diffrn_detector.pdbx_collection_date   2008-12-12 
_diffrn_detector.details                MIRRORS 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'CONFOCAL OPTICS' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.type                        'RIGAKU MICROMAX-007 HF' 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_wavelength             1.5418 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.entry_id                     3GTV 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             50.000 
_reflns.d_resolution_high            2.198 
_reflns.number_obs                   148445 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         94.0 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.11100 
_reflns.pdbx_netI_over_sigmaI        8.9000 
_reflns.B_iso_Wilson_estimate        30.70 
_reflns.pdbx_redundancy              3.400 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             2.20 
_reflns_shell.d_res_low              2.28 
_reflns_shell.percent_possible_all   90.0 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        0.47600 
_reflns_shell.meanI_over_sigI_obs    2.500 
_reflns_shell.pdbx_redundancy        3.20 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 3GTV 
_refine.ls_number_reflns_obs                     148404 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.380 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             40.35 
_refine.ls_d_res_high                            2.20 
_refine.ls_percent_reflns_obs                    93.8 
_refine.ls_R_factor_obs                          0.186 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.184 
_refine.ls_R_factor_R_free                       0.231 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.310 
_refine.ls_number_reflns_R_free                  7885 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               28.00 
_refine.aniso_B[1][1]                            -9.19820 
_refine.aniso_B[2][2]                            9.95210 
_refine.aniso_B[3][3]                            -2.32960 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            1.07200 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 0.34 
_refine.solvent_model_param_bsol                 36.20 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      2VR7 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             isotropic 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        13392 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         12 
_refine_hist.number_atoms_solvent             1808 
_refine_hist.number_atoms_total               15212 
_refine_hist.d_res_high                       2.20 
_refine_hist.d_res_low                        40.35 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
f_bond_d           0.008  ? ? 13614 'X-RAY DIFFRACTION' ? 
f_angle_d          1.171  ? ? 18334 'X-RAY DIFFRACTION' ? 
f_dihedral_angle_d 18.215 ? ? 4948  'X-RAY DIFFRACTION' ? 
f_chiral_restr     0.077  ? ? 1993  'X-RAY DIFFRACTION' ? 
f_plane_restr      0.004  ? ? 2486  'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
'X-RAY DIFFRACTION' . 2.2106 2.2481 6335 0.2551 84.00 0.2942 . . 498 . . 
'X-RAY DIFFRACTION' . 2.2481 2.2883 6677 0.2508 87.00 0.2950 . . 249 . . 
'X-RAY DIFFRACTION' . 2.2883 2.3316 6360 0.2534 84.00 0.2966 . . 498 . . 
'X-RAY DIFFRACTION' . 2.3316 2.3783 6666 0.2431 88.00 0.2715 . . 249 . . 
'X-RAY DIFFRACTION' . 2.3783 2.4289 6677 0.2412 88.00 0.2957 . . 249 . . 
'X-RAY DIFFRACTION' . 2.4289 2.4842 6402 0.2358 84.00 0.2945 . . 498 . . 
'X-RAY DIFFRACTION' . 2.4842 2.5449 6671 0.2345 87.00 0.2873 . . 249 . . 
'X-RAY DIFFRACTION' . 2.5449 2.6120 6478 0.2359 84.00 0.2951 . . 498 . . 
'X-RAY DIFFRACTION' . 2.6120 2.6868 6710 0.2242 88.00 0.2658 . . 249 . . 
'X-RAY DIFFRACTION' . 2.6868 2.7710 6792 0.2159 89.00 0.2946 . . 249 . . 
'X-RAY DIFFRACTION' . 2.7710 2.8668 6701 0.2118 88.00 0.2713 . . 498 . . 
'X-RAY DIFFRACTION' . 2.8668 2.9774 7043 0.2029 92.00 0.2849 . . 249 . . 
'X-RAY DIFFRACTION' . 2.9774 3.1073 6892 0.1828 90.00 0.2427 . . 498 . . 
'X-RAY DIFFRACTION' . 3.1073 3.2634 7146 0.1677 94.00 0.2062 . . 249 . . 
'X-RAY DIFFRACTION' . 3.2634 3.4565 6917 0.1564 91.00 0.2106 . . 498 . . 
'X-RAY DIFFRACTION' . 3.4565 3.7052 7195 0.1500 94.00 0.2042 . . 249 . . 
'X-RAY DIFFRACTION' . 3.7052 4.0456 7053 0.1442 91.00 0.1877 . . 498 . . 
'X-RAY DIFFRACTION' . 4.0456 4.5601 7260 0.1298 95.00 0.1923 . . 249 . . 
'X-RAY DIFFRACTION' . 4.5601 5.5065 7077 0.1486 92.00 0.1861 . . 498 . . 
'X-RAY DIFFRACTION' . 5.5065 8.8709 7190 0.1916 93.00 0.1957 . . 498 . . 
# 
_struct.entry_id                  3GTV 
_struct.title                     'Human-mouse SOD1 chimera' 
_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        3GTV 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            
;OXIDOREDUCTASE, human, MOUSE CU, ZN SUPEROXIDE DISMUTASE, ANTIOXIDANT, METAL-BINDING, AMYOTROPHIC LATERAL SCLEROSIS, Disease mutation, Disulfide bond, Phosphoprotein
;
# 
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 2 ? 
O  N N 2 ? 
P  N N 2 ? 
Q  N N 2 ? 
R  N N 2 ? 
S  N N 2 ? 
T  N N 2 ? 
U  N N 2 ? 
V  N N 2 ? 
W  N N 2 ? 
X  N N 2 ? 
Y  N N 3 ? 
Z  N N 3 ? 
AA N N 3 ? 
BA N N 3 ? 
CA N N 3 ? 
DA N N 3 ? 
EA N N 3 ? 
FA N N 3 ? 
GA N N 3 ? 
HA N N 3 ? 
IA N N 3 ? 
JA N N 3 ? 
# 
_struct_biol.id   1 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  ALA A 55  ? GLY A 61  ? ALA A 55  GLY A 61  5 ? 7 
HELX_P HELX_P2  2  ASN A 131 ? GLY A 138 ? ASN A 131 GLY A 138 1 ? 8 
HELX_P HELX_P3  3  ALA B 55  ? GLY B 61  ? ALA B 55  GLY B 61  5 ? 7 
HELX_P HELX_P4  4  GLU B 133 ? GLY B 138 ? GLU B 133 GLY B 138 1 ? 6 
HELX_P HELX_P5  5  ALA C 55  ? GLY C 61  ? ALA C 55  GLY C 61  5 ? 7 
HELX_P HELX_P6  6  SER C 107 ? SER C 111 ? SER C 107 SER C 111 5 ? 5 
HELX_P HELX_P7  7  GLU C 133 ? GLY C 138 ? GLU C 133 GLY C 138 1 ? 6 
HELX_P HELX_P8  8  ALA D 55  ? GLY D 61  ? ALA D 55  GLY D 61  5 ? 7 
HELX_P HELX_P9  9  GLU D 133 ? GLY D 138 ? GLU D 133 GLY D 138 1 ? 6 
HELX_P HELX_P10 10 ALA E 55  ? GLY E 61  ? ALA E 55  GLY E 61  5 ? 7 
HELX_P HELX_P11 11 GLU E 132 ? LYS E 136 ? GLU E 132 LYS E 136 5 ? 5 
HELX_P HELX_P12 12 GLY F 56  ? GLY F 61  ? GLY F 56  GLY F 61  5 ? 6 
HELX_P HELX_P13 13 GLU F 133 ? GLY F 138 ? GLU F 133 GLY F 138 1 ? 6 
HELX_P HELX_P14 14 CYS G 57  ? GLY G 61  ? CYS G 57  GLY G 61  5 ? 5 
HELX_P HELX_P15 15 ASN G 131 ? GLY G 138 ? ASN G 131 GLY G 138 1 ? 8 
HELX_P HELX_P16 16 ALA H 55  ? GLY H 61  ? ALA H 55  GLY H 61  5 ? 7 
HELX_P HELX_P17 17 ALA I 55  ? GLY I 61  ? ALA I 55  GLY I 61  5 ? 7 
HELX_P HELX_P18 18 GLU I 133 ? GLY I 138 ? GLU I 133 GLY I 138 1 ? 6 
HELX_P HELX_P19 19 ALA J 55  ? GLY J 61  ? ALA J 55  GLY J 61  5 ? 7 
HELX_P HELX_P20 20 ALA K 55  ? GLY K 61  ? ALA K 55  GLY K 61  5 ? 7 
HELX_P HELX_P21 21 ALA L 55  ? GLY L 61  ? ALA L 55  GLY L 61  5 ? 7 
HELX_P HELX_P22 22 SER L 107 ? SER L 111 ? SER L 107 SER L 111 5 ? 5 
HELX_P HELX_P23 23 GLU L 132 ? LYS L 136 ? GLU L 132 LYS L 136 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 57 A CYS 146 1_555 ? ? ? ? ? ? ? 2.723 ? 
disulf2  disulf ? ? B CYS 57 SG  ? ? ? 1_555 B CYS 146 SG ? ? B CYS 57 B CYS 146 1_555 ? ? ? ? ? ? ? 2.901 ? 
disulf3  disulf ? ? C CYS 57 SG  ? ? ? 1_555 C CYS 146 SG ? ? C CYS 57 C CYS 146 1_555 ? ? ? ? ? ? ? 2.714 ? 
disulf4  disulf ? ? D CYS 57 SG  ? ? ? 1_555 D CYS 146 SG ? ? D CYS 57 D CYS 146 1_555 ? ? ? ? ? ? ? 2.739 ? 
disulf5  disulf ? ? E CYS 57 SG  ? ? ? 1_555 E CYS 146 SG ? ? E CYS 57 E CYS 146 1_555 ? ? ? ? ? ? ? 2.937 ? 
disulf6  disulf ? ? F CYS 57 SG  ? ? ? 1_555 F CYS 146 SG ? ? F CYS 57 F CYS 146 1_555 ? ? ? ? ? ? ? 2.650 ? 
disulf7  disulf ? ? G CYS 57 SG  ? ? ? 1_555 G CYS 146 SG ? ? G CYS 57 G CYS 146 1_555 ? ? ? ? ? ? ? 2.719 ? 
disulf8  disulf ? ? H CYS 57 SG  ? ? ? 1_555 H CYS 146 SG ? ? H CYS 57 H CYS 146 1_555 ? ? ? ? ? ? ? 2.716 ? 
disulf9  disulf ? ? I CYS 57 SG  ? ? ? 1_555 I CYS 146 SG ? ? I CYS 57 I CYS 146 1_555 ? ? ? ? ? ? ? 2.685 ? 
disulf10 disulf ? ? J CYS 57 SG  ? ? ? 1_555 J CYS 146 SG ? ? J CYS 57 J CYS 146 1_555 ? ? ? ? ? ? ? 2.747 ? 
disulf11 disulf ? ? L CYS 57 SG  ? ? ? 1_555 L CYS 146 SG ? ? L CYS 57 L CYS 146 1_555 ? ? ? ? ? ? ? 2.892 ? 
metalc1  metalc ? ? A HIS 63 ND1 ? ? ? 1_555 M ZN  .   ZN ? ? A HIS 63 A ZN  155 1_555 ? ? ? ? ? ? ? 2.095 ? 
metalc2  metalc ? ? A HIS 71 ND1 ? ? ? 1_555 M ZN  .   ZN ? ? A HIS 71 A ZN  155 1_555 ? ? ? ? ? ? ? 2.229 ? 
metalc3  metalc ? ? A HIS 80 ND1 ? ? ? 1_555 M ZN  .   ZN ? ? A HIS 80 A ZN  155 1_555 ? ? ? ? ? ? ? 2.190 ? 
metalc4  metalc ? ? A ASP 83 OD1 ? ? ? 1_555 M ZN  .   ZN ? ? A ASP 83 A ZN  155 1_555 ? ? ? ? ? ? ? 1.958 ? 
metalc5  metalc ? ? B HIS 63 ND1 ? ? ? 1_555 N ZN  .   ZN ? ? B HIS 63 B ZN  155 1_555 ? ? ? ? ? ? ? 2.238 ? 
metalc6  metalc ? ? B HIS 71 ND1 ? ? ? 1_555 N ZN  .   ZN ? ? B HIS 71 B ZN  155 1_555 ? ? ? ? ? ? ? 2.228 ? 
metalc7  metalc ? ? B HIS 80 ND1 ? ? ? 1_555 N ZN  .   ZN ? ? B HIS 80 B ZN  155 1_555 ? ? ? ? ? ? ? 2.106 ? 
metalc8  metalc ? ? B ASP 83 OD1 ? ? ? 1_555 N ZN  .   ZN ? ? B ASP 83 B ZN  155 1_555 ? ? ? ? ? ? ? 1.996 ? 
metalc9  metalc ? ? C HIS 63 ND1 ? ? ? 1_555 O ZN  .   ZN ? ? C HIS 63 C ZN  155 1_555 ? ? ? ? ? ? ? 2.181 ? 
metalc10 metalc ? ? C HIS 71 ND1 ? ? ? 1_555 O ZN  .   ZN ? ? C HIS 71 C ZN  155 1_555 ? ? ? ? ? ? ? 2.187 ? 
metalc11 metalc ? ? C HIS 80 ND1 ? ? ? 1_555 O ZN  .   ZN ? ? C HIS 80 C ZN  155 1_555 ? ? ? ? ? ? ? 2.210 ? 
metalc12 metalc ? ? C ASP 83 OD1 ? ? ? 1_555 O ZN  .   ZN ? ? C ASP 83 C ZN  155 1_555 ? ? ? ? ? ? ? 1.946 ? 
metalc13 metalc ? ? D HIS 63 ND1 ? ? ? 1_555 P ZN  .   ZN ? ? D HIS 63 D ZN  155 1_555 ? ? ? ? ? ? ? 2.276 ? 
metalc14 metalc ? ? D HIS 71 ND1 ? ? ? 1_555 P ZN  .   ZN ? ? D HIS 71 D ZN  155 1_555 ? ? ? ? ? ? ? 2.241 ? 
metalc15 metalc ? ? D HIS 80 ND1 ? ? ? 1_555 P ZN  .   ZN ? ? D HIS 80 D ZN  155 1_555 ? ? ? ? ? ? ? 2.190 ? 
metalc16 metalc ? ? D ASP 83 OD1 ? ? ? 1_555 P ZN  .   ZN ? ? D ASP 83 D ZN  155 1_555 ? ? ? ? ? ? ? 2.034 ? 
metalc17 metalc ? ? E HIS 63 ND1 ? ? ? 1_555 Q ZN  .   ZN ? ? E HIS 63 E ZN  155 1_555 ? ? ? ? ? ? ? 2.153 ? 
metalc18 metalc ? ? E HIS 80 ND1 ? ? ? 1_555 Q ZN  .   ZN ? ? E HIS 80 E ZN  155 1_555 ? ? ? ? ? ? ? 2.202 ? 
metalc19 metalc ? ? E ASP 83 OD1 ? ? ? 1_555 Q ZN  .   ZN ? ? E ASP 83 E ZN  155 1_555 ? ? ? ? ? ? ? 2.050 ? 
metalc20 metalc ? ? F HIS 63 ND1 ? ? ? 1_555 R ZN  .   ZN ? ? F HIS 63 F ZN  155 1_555 ? ? ? ? ? ? ? 2.096 ? 
metalc21 metalc ? ? F HIS 80 ND1 ? ? ? 1_555 R ZN  .   ZN ? ? F HIS 80 F ZN  155 1_555 ? ? ? ? ? ? ? 2.183 ? 
metalc22 metalc ? ? F ASP 83 OD1 ? ? ? 1_555 R ZN  .   ZN ? ? F ASP 83 F ZN  155 1_555 ? ? ? ? ? ? ? 1.969 ? 
metalc23 metalc ? ? G HIS 63 ND1 ? ? ? 1_555 S ZN  .   ZN ? ? G HIS 63 G ZN  155 1_555 ? ? ? ? ? ? ? 2.293 ? 
metalc24 metalc ? ? G HIS 71 ND1 ? ? ? 1_555 S ZN  .   ZN ? ? G HIS 71 G ZN  155 1_555 ? ? ? ? ? ? ? 2.226 ? 
metalc25 metalc ? ? G HIS 80 ND1 ? ? ? 1_555 S ZN  .   ZN ? ? G HIS 80 G ZN  155 1_555 ? ? ? ? ? ? ? 2.023 ? 
metalc26 metalc ? ? G ASP 83 OD1 ? ? ? 1_555 S ZN  .   ZN ? ? G ASP 83 G ZN  155 1_555 ? ? ? ? ? ? ? 2.018 ? 
metalc27 metalc ? ? H HIS 63 ND1 ? ? ? 1_555 T ZN  .   ZN ? ? H HIS 63 H ZN  155 1_555 ? ? ? ? ? ? ? 2.207 ? 
metalc28 metalc ? ? H HIS 71 ND1 ? ? ? 1_555 T ZN  .   ZN ? ? H HIS 71 H ZN  155 1_555 ? ? ? ? ? ? ? 2.288 ? 
metalc29 metalc ? ? H HIS 80 ND1 ? ? ? 1_555 T ZN  .   ZN ? ? H HIS 80 H ZN  155 1_555 ? ? ? ? ? ? ? 2.169 ? 
metalc30 metalc ? ? H ASP 83 OD1 ? ? ? 1_555 T ZN  .   ZN ? ? H ASP 83 H ZN  155 1_555 ? ? ? ? ? ? ? 1.978 ? 
metalc31 metalc ? ? I HIS 63 ND1 ? ? ? 1_555 U ZN  .   ZN ? ? I HIS 63 I ZN  155 1_555 ? ? ? ? ? ? ? 2.246 ? 
metalc32 metalc ? ? I HIS 71 ND1 ? ? ? 1_555 U ZN  .   ZN ? ? I HIS 71 I ZN  155 1_555 ? ? ? ? ? ? ? 2.167 ? 
metalc33 metalc ? ? I HIS 80 ND1 ? ? ? 1_555 U ZN  .   ZN ? ? I HIS 80 I ZN  155 1_555 ? ? ? ? ? ? ? 1.962 ? 
metalc34 metalc ? ? I ASP 83 OD1 ? ? ? 1_555 U ZN  .   ZN ? ? I ASP 83 I ZN  155 1_555 ? ? ? ? ? ? ? 1.992 ? 
metalc35 metalc ? ? J HIS 63 ND1 ? ? ? 1_555 V ZN  .   ZN ? ? J HIS 63 J ZN  155 1_555 ? ? ? ? ? ? ? 2.238 ? 
metalc36 metalc ? ? J HIS 71 ND1 ? ? ? 1_555 V ZN  .   ZN ? ? J HIS 71 J ZN  155 1_555 ? ? ? ? ? ? ? 2.301 ? 
metalc37 metalc ? ? J HIS 80 ND1 ? ? ? 1_555 V ZN  .   ZN ? ? J HIS 80 J ZN  155 1_555 ? ? ? ? ? ? ? 2.189 ? 
metalc38 metalc ? ? J ASP 83 OD1 ? ? ? 1_555 V ZN  .   ZN ? ? J ASP 83 J ZN  155 1_555 ? ? ? ? ? ? ? 2.007 ? 
metalc39 metalc ? ? K HIS 63 ND1 ? ? ? 1_555 W ZN  .   ZN ? ? K HIS 63 K ZN  155 1_555 ? ? ? ? ? ? ? 2.233 ? 
metalc40 metalc ? ? K HIS 71 ND1 ? ? ? 1_555 W ZN  .   ZN ? ? K HIS 71 K ZN  155 1_555 ? ? ? ? ? ? ? 2.141 ? 
metalc41 metalc ? ? K HIS 80 ND1 ? ? ? 1_555 W ZN  .   ZN ? ? K HIS 80 K ZN  155 1_555 ? ? ? ? ? ? ? 2.177 ? 
metalc42 metalc ? ? K ASP 83 OD1 ? ? ? 1_555 W ZN  .   ZN ? ? K ASP 83 K ZN  155 1_555 ? ? ? ? ? ? ? 2.049 ? 
metalc43 metalc ? ? L HIS 63 ND1 ? ? ? 1_555 X ZN  .   ZN ? ? L HIS 63 L ZN  155 1_555 ? ? ? ? ? ? ? 2.258 ? 
metalc44 metalc ? ? L HIS 71 ND1 ? ? ? 1_555 X ZN  .   ZN ? ? L HIS 71 L ZN  155 1_555 ? ? ? ? ? ? ? 2.260 ? 
metalc45 metalc ? ? L HIS 80 ND1 ? ? ? 1_555 X ZN  .   ZN ? ? L HIS 80 L ZN  155 1_555 ? ? ? ? ? ? ? 2.309 ? 
metalc46 metalc ? ? L ASP 83 OD1 ? ? ? 1_555 X ZN  .   ZN ? ? L ASP 83 L ZN  155 1_555 ? ? ? ? ? ? ? 1.957 ? 
metalc47 metalc ? ? E HIS 71 ND1 ? ? ? 1_555 Q ZN  .   ZN ? ? E HIS 71 E ZN  155 1_555 ? ? ? ? ? ? ? 2.425 ? 
metalc48 metalc ? ? F HIS 71 ND1 ? ? ? 1_555 R ZN  .   ZN ? ? F HIS 71 F ZN  155 1_555 ? ? ? ? ? ? ? 2.474 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 5 ? 
B ? 4 ? 
C ? 9 ? 
D ? 5 ? 
E ? 4 ? 
F ? 5 ? 
G ? 4 ? 
H ? 5 ? 
I ? 4 ? 
J ? 5 ? 
K ? 4 ? 
L ? 5 ? 
M ? 4 ? 
N ? 5 ? 
O ? 4 ? 
P ? 5 ? 
Q ? 4 ? 
R ? 5 ? 
S ? 4 ? 
T ? 5 ? 
U ? 4 ? 
V ? 5 ? 
W ? 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 
C 5 6 ? anti-parallel 
C 6 7 ? anti-parallel 
C 7 8 ? anti-parallel 
C 8 9 ? anti-parallel 
D 1 2 ? anti-parallel 
D 2 3 ? anti-parallel 
D 3 4 ? anti-parallel 
D 4 5 ? anti-parallel 
E 1 2 ? anti-parallel 
E 2 3 ? anti-parallel 
E 3 4 ? anti-parallel 
F 1 2 ? anti-parallel 
F 2 3 ? anti-parallel 
F 3 4 ? anti-parallel 
F 4 5 ? anti-parallel 
G 1 2 ? anti-parallel 
G 2 3 ? anti-parallel 
G 3 4 ? anti-parallel 
H 1 2 ? anti-parallel 
H 2 3 ? anti-parallel 
H 3 4 ? anti-parallel 
H 4 5 ? anti-parallel 
I 1 2 ? anti-parallel 
I 2 3 ? anti-parallel 
I 3 4 ? anti-parallel 
J 1 2 ? anti-parallel 
J 2 3 ? anti-parallel 
J 3 4 ? anti-parallel 
J 4 5 ? anti-parallel 
K 1 2 ? anti-parallel 
K 2 3 ? anti-parallel 
K 3 4 ? anti-parallel 
L 1 2 ? anti-parallel 
L 2 3 ? anti-parallel 
L 3 4 ? anti-parallel 
L 4 5 ? anti-parallel 
M 1 2 ? anti-parallel 
M 2 3 ? anti-parallel 
M 3 4 ? anti-parallel 
N 1 2 ? anti-parallel 
N 2 3 ? anti-parallel 
N 3 4 ? anti-parallel 
N 4 5 ? anti-parallel 
O 1 2 ? anti-parallel 
O 2 3 ? anti-parallel 
O 3 4 ? anti-parallel 
P 1 2 ? anti-parallel 
P 2 3 ? anti-parallel 
P 3 4 ? anti-parallel 
P 4 5 ? anti-parallel 
Q 1 2 ? anti-parallel 
Q 2 3 ? anti-parallel 
Q 3 4 ? anti-parallel 
R 1 2 ? anti-parallel 
R 2 3 ? anti-parallel 
R 3 4 ? anti-parallel 
R 4 5 ? anti-parallel 
S 1 2 ? anti-parallel 
S 2 3 ? anti-parallel 
S 3 4 ? anti-parallel 
T 1 2 ? anti-parallel 
T 2 3 ? anti-parallel 
T 3 4 ? anti-parallel 
T 4 5 ? anti-parallel 
U 1 2 ? anti-parallel 
U 2 3 ? anti-parallel 
U 3 4 ? anti-parallel 
V 1 2 ? anti-parallel 
V 2 3 ? anti-parallel 
V 3 4 ? anti-parallel 
V 4 5 ? anti-parallel 
W 1 2 ? anti-parallel 
W 2 3 ? anti-parallel 
W 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 95  ASP A 101 
A 2 VAL A 29  ? LYS A 36  ? VAL A 29  LYS A 36  
A 3 GLN A 15  ? GLN A 22  ? GLN A 15  GLN A 22  
A 4 THR A 2   ? LYS A 9   ? THR A 2   LYS A 9   
A 5 GLY A 150 ? ILE A 151 ? GLY A 150 ILE A 151 
B 1 ASP A 83  ? ALA A 89  ? ASP A 83  ALA A 89  
B 2 GLY A 41  ? HIS A 48  ? GLY A 41  HIS A 48  
B 3 THR A 116 ? HIS A 120 ? THR A 116 HIS A 120 
B 4 ARG A 143 ? VAL A 148 ? ARG A 143 VAL A 148 
C 1 THR B 2   ? LYS B 9   ? THR B 2   LYS B 9   
C 2 GLN B 15  ? GLN B 22  ? GLN B 15  GLN B 22  
C 3 VAL B 29  ? LYS B 36  ? VAL B 29  LYS B 36  
C 4 ALA B 95  ? ASP B 101 ? ALA B 95  ASP B 101 
C 5 ASP B 83  ? ALA B 89  ? ASP B 83  ALA B 89  
C 6 GLY B 41  ? HIS B 48  ? GLY B 41  HIS B 48  
C 7 THR B 116 ? HIS B 120 ? THR B 116 HIS B 120 
C 8 ARG B 143 ? ILE B 151 ? ARG B 143 ILE B 151 
C 9 THR B 2   ? LYS B 9   ? THR B 2   LYS B 9   
D 1 ALA C 95  ? ASP C 101 ? ALA C 95  ASP C 101 
D 2 VAL C 29  ? LYS C 36  ? VAL C 29  LYS C 36  
D 3 GLN C 15  ? GLN C 22  ? GLN C 15  GLN C 22  
D 4 THR C 2   ? LEU C 8   ? THR C 2   LEU C 8   
D 5 GLY C 150 ? ILE C 151 ? GLY C 150 ILE C 151 
E 1 ASP C 83  ? ALA C 89  ? ASP C 83  ALA C 89  
E 2 GLY C 41  ? HIS C 48  ? GLY C 41  HIS C 48  
E 3 THR C 116 ? HIS C 120 ? THR C 116 HIS C 120 
E 4 ARG C 143 ? VAL C 148 ? ARG C 143 VAL C 148 
F 1 ALA D 95  ? ASP D 101 ? ALA D 95  ASP D 101 
F 2 VAL D 29  ? LYS D 36  ? VAL D 29  LYS D 36  
F 3 GLN D 15  ? GLN D 22  ? GLN D 15  GLN D 22  
F 4 THR D 2   ? LEU D 8   ? THR D 2   LEU D 8   
F 5 GLY D 150 ? ILE D 151 ? GLY D 150 ILE D 151 
G 1 ASP D 83  ? ALA D 89  ? ASP D 83  ALA D 89  
G 2 GLY D 41  ? HIS D 48  ? GLY D 41  HIS D 48  
G 3 THR D 116 ? HIS D 120 ? THR D 116 HIS D 120 
G 4 ARG D 143 ? VAL D 148 ? ARG D 143 VAL D 148 
H 1 ALA E 95  ? ASP E 101 ? ALA E 95  ASP E 101 
H 2 VAL E 29  ? LYS E 36  ? VAL E 29  LYS E 36  
H 3 GLN E 15  ? GLN E 22  ? GLN E 15  GLN E 22  
H 4 THR E 2   ? LEU E 8   ? THR E 2   LEU E 8   
H 5 GLY E 150 ? ILE E 151 ? GLY E 150 ILE E 151 
I 1 ASP E 83  ? ALA E 89  ? ASP E 83  ALA E 89  
I 2 GLY E 41  ? HIS E 48  ? GLY E 41  HIS E 48  
I 3 THR E 116 ? HIS E 120 ? THR E 116 HIS E 120 
I 4 ARG E 143 ? VAL E 148 ? ARG E 143 VAL E 148 
J 1 SER F 98  ? ASP F 101 ? SER F 98  ASP F 101 
J 2 VAL F 29  ? LYS F 36  ? VAL F 29  LYS F 36  
J 3 GLN F 15  ? GLN F 22  ? GLN F 15  GLN F 22  
J 4 THR F 2   ? LEU F 8   ? THR F 2   LEU F 8   
J 5 GLY F 150 ? ILE F 151 ? GLY F 150 ILE F 151 
K 1 ASP F 83  ? ALA F 89  ? ASP F 83  ALA F 89  
K 2 GLY F 41  ? HIS F 48  ? GLY F 41  HIS F 48  
K 3 THR F 116 ? HIS F 120 ? THR F 116 HIS F 120 
K 4 ARG F 143 ? VAL F 148 ? ARG F 143 VAL F 148 
L 1 ALA G 95  ? ASP G 101 ? ALA G 95  ASP G 101 
L 2 VAL G 29  ? LYS G 36  ? VAL G 29  LYS G 36  
L 3 GLN G 15  ? GLN G 22  ? GLN G 15  GLN G 22  
L 4 THR G 2   ? LYS G 9   ? THR G 2   LYS G 9   
L 5 GLY G 150 ? ILE G 151 ? GLY G 150 ILE G 151 
M 1 ASP G 83  ? ALA G 89  ? ASP G 83  ALA G 89  
M 2 GLY G 41  ? HIS G 48  ? GLY G 41  HIS G 48  
M 3 THR G 116 ? HIS G 120 ? THR G 116 HIS G 120 
M 4 ARG G 143 ? VAL G 148 ? ARG G 143 VAL G 148 
N 1 ALA H 95  ? ASP H 101 ? ALA H 95  ASP H 101 
N 2 VAL H 29  ? LYS H 36  ? VAL H 29  LYS H 36  
N 3 GLN H 15  ? GLN H 22  ? GLN H 15  GLN H 22  
N 4 THR H 2   ? LEU H 8   ? THR H 2   LEU H 8   
N 5 GLY H 150 ? ALA H 152 ? GLY H 150 ALA H 152 
O 1 ASP H 83  ? ALA H 89  ? ASP H 83  ALA H 89  
O 2 GLY H 41  ? HIS H 48  ? GLY H 41  HIS H 48  
O 3 THR H 116 ? HIS H 120 ? THR H 116 HIS H 120 
O 4 ARG H 143 ? VAL H 148 ? ARG H 143 VAL H 148 
P 1 ALA I 95  ? ASP I 101 ? ALA I 95  ASP I 101 
P 2 VAL I 29  ? LYS I 36  ? VAL I 29  LYS I 36  
P 3 GLN I 15  ? GLN I 22  ? GLN I 15  GLN I 22  
P 4 THR I 2   ? LEU I 8   ? THR I 2   LEU I 8   
P 5 GLY I 150 ? ILE I 151 ? GLY I 150 ILE I 151 
Q 1 ASP I 83  ? ALA I 89  ? ASP I 83  ALA I 89  
Q 2 GLY I 41  ? HIS I 48  ? GLY I 41  HIS I 48  
Q 3 THR I 116 ? HIS I 120 ? THR I 116 HIS I 120 
Q 4 ARG I 143 ? VAL I 148 ? ARG I 143 VAL I 148 
R 1 ALA J 95  ? ASP J 101 ? ALA J 95  ASP J 101 
R 2 VAL J 29  ? LYS J 36  ? VAL J 29  LYS J 36  
R 3 GLN J 15  ? GLN J 22  ? GLN J 15  GLN J 22  
R 4 THR J 2   ? LEU J 8   ? THR J 2   LEU J 8   
R 5 GLY J 150 ? ILE J 151 ? GLY J 150 ILE J 151 
S 1 ASP J 83  ? ALA J 89  ? ASP J 83  ALA J 89  
S 2 GLY J 41  ? HIS J 48  ? GLY J 41  HIS J 48  
S 3 THR J 116 ? HIS J 120 ? THR J 116 HIS J 120 
S 4 ARG J 143 ? VAL J 148 ? ARG J 143 VAL J 148 
T 1 ALA K 95  ? ASP K 101 ? ALA K 95  ASP K 101 
T 2 VAL K 29  ? LYS K 36  ? VAL K 29  LYS K 36  
T 3 GLN K 15  ? GLN K 22  ? GLN K 15  GLN K 22  
T 4 THR K 2   ? LEU K 8   ? THR K 2   LEU K 8   
T 5 GLY K 150 ? ILE K 151 ? GLY K 150 ILE K 151 
U 1 ASP K 83  ? ALA K 89  ? ASP K 83  ALA K 89  
U 2 GLY K 41  ? HIS K 48  ? GLY K 41  HIS K 48  
U 3 THR K 116 ? HIS K 120 ? THR K 116 HIS K 120 
U 4 ARG K 143 ? VAL K 148 ? ARG K 143 VAL K 148 
V 1 ALA L 95  ? ASP L 101 ? ALA L 95  ASP L 101 
V 2 VAL L 29  ? LYS L 36  ? VAL L 29  LYS L 36  
V 3 GLN L 15  ? GLN L 22  ? GLN L 15  GLN L 22  
V 4 THR L 2   ? LYS L 9   ? THR L 2   LYS L 9   
V 5 GLY L 150 ? ILE L 151 ? GLY L 150 ILE L 151 
W 1 ASP L 83  ? ALA L 89  ? ASP L 83  ALA L 89  
W 2 GLY L 41  ? HIS L 48  ? GLY L 41  HIS L 48  
W 3 THR L 116 ? HIS L 120 ? THR L 116 HIS L 120 
W 4 ARG L 143 ? VAL L 148 ? ARG L 143 VAL L 148 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 O ASP A 101 ? O ASP A 101 N VAL A 29  ? N VAL A 29  
A 2 3 O TRP A 32  ? O TRP A 32  N ASN A 19  ? N ASN A 19  
A 3 4 O ILE A 18  ? O ILE A 18  N CYS A 6   ? N CYS A 6   
A 4 5 N VAL A 5   ? N VAL A 5   O GLY A 150 ? O GLY A 150 
B 1 2 O ALA A 89  ? O ALA A 89  N GLY A 41  ? N GLY A 41  
B 2 3 N HIS A 48  ? N HIS A 48  O THR A 116 ? O THR A 116 
B 3 4 N VAL A 119 ? N VAL A 119 O LEU A 144 ? O LEU A 144 
C 1 2 N ALA B 4   ? N ALA B 4   O PHE B 20  ? O PHE B 20  
C 2 3 N ASN B 19  ? N ASN B 19  O TRP B 32  ? O TRP B 32  
C 3 4 N VAL B 31  ? N VAL B 31  O ILE B 99  ? O ILE B 99  
C 4 5 O ASN B 96  ? O ASN B 96  N THR B 88  ? N THR B 88  
C 5 6 O ALA B 89  ? O ALA B 89  N GLY B 41  ? N GLY B 41  
C 6 7 N HIS B 48  ? N HIS B 48  O THR B 116 ? O THR B 116 
C 7 8 N VAL B 119 ? N VAL B 119 O ALA B 145 ? O ALA B 145 
C 8 9 O GLY B 150 ? O GLY B 150 N VAL B 5   ? N VAL B 5   
D 1 2 O ILE C 99  ? O ILE C 99  N VAL C 31  ? N VAL C 31  
D 2 3 O TRP C 32  ? O TRP C 32  N ASN C 19  ? N ASN C 19  
D 3 4 O ILE C 18  ? O ILE C 18  N CYS C 6   ? N CYS C 6   
D 4 5 N VAL C 5   ? N VAL C 5   O GLY C 150 ? O GLY C 150 
E 1 2 O ALA C 89  ? O ALA C 89  N GLY C 41  ? N GLY C 41  
E 2 3 N HIS C 48  ? N HIS C 48  O THR C 116 ? O THR C 116 
E 3 4 N VAL C 119 ? N VAL C 119 O LEU C 144 ? O LEU C 144 
F 1 2 O ILE D 99  ? O ILE D 99  N VAL D 31  ? N VAL D 31  
F 2 3 O TRP D 32  ? O TRP D 32  N ASN D 19  ? N ASN D 19  
F 3 4 O ILE D 18  ? O ILE D 18  N CYS D 6   ? N CYS D 6   
F 4 5 N VAL D 5   ? N VAL D 5   O GLY D 150 ? O GLY D 150 
G 1 2 O GLY D 85  ? O GLY D 85  N PHE D 45  ? N PHE D 45  
G 2 3 N GLY D 44  ? N GLY D 44  O HIS D 120 ? O HIS D 120 
G 3 4 N VAL D 119 ? N VAL D 119 O LEU D 144 ? O LEU D 144 
H 1 2 O ASP E 101 ? O ASP E 101 N VAL E 29  ? N VAL E 29  
H 2 3 O TRP E 32  ? O TRP E 32  N ASN E 19  ? N ASN E 19  
H 3 4 O ILE E 18  ? O ILE E 18  N CYS E 6   ? N CYS E 6   
H 4 5 N VAL E 5   ? N VAL E 5   O GLY E 150 ? O GLY E 150 
I 1 2 O GLY E 85  ? O GLY E 85  N PHE E 45  ? N PHE E 45  
I 2 3 N HIS E 48  ? N HIS E 48  O THR E 116 ? O THR E 116 
I 3 4 N MET E 117 ? N MET E 117 O GLY E 147 ? O GLY E 147 
J 1 2 O ILE F 99  ? O ILE F 99  N VAL F 31  ? N VAL F 31  
J 2 3 O TRP F 32  ? O TRP F 32  N ASN F 19  ? N ASN F 19  
J 3 4 O PHE F 20  ? O PHE F 20  N ALA F 4   ? N ALA F 4   
J 4 5 N VAL F 5   ? N VAL F 5   O GLY F 150 ? O GLY F 150 
K 1 2 O GLY F 85  ? O GLY F 85  N PHE F 45  ? N PHE F 45  
K 2 3 N HIS F 48  ? N HIS F 48  O THR F 116 ? O THR F 116 
K 3 4 N MET F 117 ? N MET F 117 O GLY F 147 ? O GLY F 147 
L 1 2 O ALA G 95  ? O ALA G 95  N ILE G 35  ? N ILE G 35  
L 2 3 O TRP G 32  ? O TRP G 32  N ASN G 19  ? N ASN G 19  
L 3 4 O ILE G 18  ? O ILE G 18  N CYS G 6   ? N CYS G 6   
L 4 5 N VAL G 5   ? N VAL G 5   O GLY G 150 ? O GLY G 150 
M 1 2 O ALA G 89  ? O ALA G 89  N GLY G 41  ? N GLY G 41  
M 2 3 N HIS G 48  ? N HIS G 48  O THR G 116 ? O THR G 116 
M 3 4 N VAL G 119 ? N VAL G 119 O ALA G 145 ? O ALA G 145 
N 1 2 O ASP H 101 ? O ASP H 101 N VAL H 29  ? N VAL H 29  
N 2 3 O TRP H 32  ? O TRP H 32  N ASN H 19  ? N ASN H 19  
N 3 4 O GLY H 16  ? O GLY H 16  N LEU H 8   ? N LEU H 8   
N 4 5 N VAL H 5   ? N VAL H 5   O GLY H 150 ? O GLY H 150 
O 1 2 O ALA H 89  ? O ALA H 89  N GLY H 41  ? N GLY H 41  
O 2 3 N HIS H 48  ? N HIS H 48  O THR H 116 ? O THR H 116 
O 3 4 N MET H 117 ? N MET H 117 O GLY H 147 ? O GLY H 147 
P 1 2 O ASP I 101 ? O ASP I 101 N VAL I 29  ? N VAL I 29  
P 2 3 O TRP I 32  ? O TRP I 32  N ASN I 19  ? N ASN I 19  
P 3 4 O GLY I 16  ? O GLY I 16  N LEU I 8   ? N LEU I 8   
P 4 5 N VAL I 5   ? N VAL I 5   O GLY I 150 ? O GLY I 150 
Q 1 2 O GLY I 85  ? O GLY I 85  N PHE I 45  ? N PHE I 45  
Q 2 3 N HIS I 48  ? N HIS I 48  O THR I 116 ? O THR I 116 
Q 3 4 N MET I 117 ? N MET I 117 O GLY I 147 ? O GLY I 147 
R 1 2 O ALA J 95  ? O ALA J 95  N ILE J 35  ? N ILE J 35  
R 2 3 O LYS J 36  ? O LYS J 36  N GLN J 15  ? N GLN J 15  
R 3 4 O GLN J 22  ? O GLN J 22  N THR J 2   ? N THR J 2   
R 4 5 N VAL J 5   ? N VAL J 5   O GLY J 150 ? O GLY J 150 
S 1 2 O GLY J 85  ? O GLY J 85  N PHE J 45  ? N PHE J 45  
S 2 3 N HIS J 48  ? N HIS J 48  O THR J 116 ? O THR J 116 
S 3 4 N VAL J 119 ? N VAL J 119 O LEU J 144 ? O LEU J 144 
T 1 2 O ALA K 95  ? O ALA K 95  N ILE K 35  ? N ILE K 35  
T 2 3 O TRP K 32  ? O TRP K 32  N ASN K 19  ? N ASN K 19  
T 3 4 O GLY K 16  ? O GLY K 16  N LEU K 8   ? N LEU K 8   
T 4 5 N VAL K 5   ? N VAL K 5   O GLY K 150 ? O GLY K 150 
U 1 2 O ALA K 89  ? O ALA K 89  N GLY K 41  ? N GLY K 41  
U 2 3 N GLY K 44  ? N GLY K 44  O HIS K 120 ? O HIS K 120 
U 3 4 N MET K 117 ? N MET K 117 O GLY K 147 ? O GLY K 147 
V 1 2 O ILE L 99  ? O ILE L 99  N VAL L 31  ? N VAL L 31  
V 2 3 O TRP L 32  ? O TRP L 32  N ASN L 19  ? N ASN L 19  
V 3 4 O ILE L 18  ? O ILE L 18  N CYS L 6   ? N CYS L 6   
V 4 5 N VAL L 5   ? N VAL L 5   O GLY L 150 ? O GLY L 150 
W 1 2 O VAL L 87  ? O VAL L 87  N HIS L 43  ? N HIS L 43  
W 2 3 N GLY L 44  ? N GLY L 44  O HIS L 120 ? O HIS L 120 
W 3 4 N MET L 117 ? N MET L 117 O GLY L 147 ? O GLY L 147 
# 
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 ZN A 155' 
AC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN B 155' 
AC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN C 155' 
AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN D 155' 
AC5 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN E 155' 
AC6 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN F 155' 
AC7 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN G 155' 
AC8 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN H 155' 
AC9 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN I 155' 
BC1 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN J 155' 
BC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN K 155' 
BC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN L 155' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4 HIS A 63  ? HIS A 63  . ? 1_555 ? 
2  AC1 4 HIS A 71  ? HIS A 71  . ? 1_555 ? 
3  AC1 4 HIS A 80  ? HIS A 80  . ? 1_555 ? 
4  AC1 4 ASP A 83  ? ASP A 83  . ? 1_555 ? 
5  AC2 4 HIS B 63  ? HIS B 63  . ? 1_555 ? 
6  AC2 4 HIS B 71  ? HIS B 71  . ? 1_555 ? 
7  AC2 4 HIS B 80  ? HIS B 80  . ? 1_555 ? 
8  AC2 4 ASP B 83  ? ASP B 83  . ? 1_555 ? 
9  AC3 4 HIS C 63  ? HIS C 63  . ? 1_555 ? 
10 AC3 4 HIS C 71  ? HIS C 71  . ? 1_555 ? 
11 AC3 4 HIS C 80  ? HIS C 80  . ? 1_555 ? 
12 AC3 4 ASP C 83  ? ASP C 83  . ? 1_555 ? 
13 AC4 4 HIS D 63  ? HIS D 63  . ? 1_555 ? 
14 AC4 4 HIS D 71  ? HIS D 71  . ? 1_555 ? 
15 AC4 4 HIS D 80  ? HIS D 80  . ? 1_555 ? 
16 AC4 4 ASP D 83  ? ASP D 83  . ? 1_555 ? 
17 AC5 5 HIS E 63  ? HIS E 63  . ? 1_555 ? 
18 AC5 5 HIS E 71  ? HIS E 71  . ? 1_555 ? 
19 AC5 5 HIS E 80  ? HIS E 80  . ? 1_555 ? 
20 AC5 5 ASP E 83  ? ASP E 83  . ? 1_555 ? 
21 AC5 5 LYS E 136 ? LYS E 136 . ? 1_555 ? 
22 AC6 5 HIS F 63  ? HIS F 63  . ? 1_555 ? 
23 AC6 5 HIS F 71  ? HIS F 71  . ? 1_555 ? 
24 AC6 5 HIS F 80  ? HIS F 80  . ? 1_555 ? 
25 AC6 5 ASP F 83  ? ASP F 83  . ? 1_555 ? 
26 AC6 5 LYS F 136 ? LYS F 136 . ? 1_555 ? 
27 AC7 4 HIS G 63  ? HIS G 63  . ? 1_555 ? 
28 AC7 4 HIS G 71  ? HIS G 71  . ? 1_555 ? 
29 AC7 4 HIS G 80  ? HIS G 80  . ? 1_555 ? 
30 AC7 4 ASP G 83  ? ASP G 83  . ? 1_555 ? 
31 AC8 4 HIS H 63  ? HIS H 63  . ? 1_555 ? 
32 AC8 4 HIS H 71  ? HIS H 71  . ? 1_555 ? 
33 AC8 4 HIS H 80  ? HIS H 80  . ? 1_555 ? 
34 AC8 4 ASP H 83  ? ASP H 83  . ? 1_555 ? 
35 AC9 4 HIS I 63  ? HIS I 63  . ? 1_555 ? 
36 AC9 4 HIS I 71  ? HIS I 71  . ? 1_555 ? 
37 AC9 4 HIS I 80  ? HIS I 80  . ? 1_555 ? 
38 AC9 4 ASP I 83  ? ASP I 83  . ? 1_555 ? 
39 BC1 4 HIS J 63  ? HIS J 63  . ? 1_555 ? 
40 BC1 4 HIS J 71  ? HIS J 71  . ? 1_555 ? 
41 BC1 4 HIS J 80  ? HIS J 80  . ? 1_555 ? 
42 BC1 4 ASP J 83  ? ASP J 83  . ? 1_555 ? 
43 BC2 4 HIS K 63  ? HIS K 63  . ? 1_555 ? 
44 BC2 4 HIS K 71  ? HIS K 71  . ? 1_555 ? 
45 BC2 4 HIS K 80  ? HIS K 80  . ? 1_555 ? 
46 BC2 4 ASP K 83  ? ASP K 83  . ? 1_555 ? 
47 BC3 4 HIS L 63  ? HIS L 63  . ? 1_555 ? 
48 BC3 4 HIS L 71  ? HIS L 71  . ? 1_555 ? 
49 BC3 4 HIS L 80  ? HIS L 80  . ? 1_555 ? 
50 BC3 4 ASP L 83  ? ASP L 83  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          3GTV 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    3GTV 
_atom_sites.fract_transf_matrix[1][1]   0.008879 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005088 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006944 
_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]   0.010235 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
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   ? 35.329  -22.652 -1.682  1.00 35.90 ? 1    ALA A N   1 
ATOM   2     C  CA  . ALA A  1 1   ? 34.912  -23.835 -2.437  1.00 37.98 ? 1    ALA A CA  1 
ATOM   3     C  C   . ALA A  1 1   ? 35.702  -25.080 -2.030  1.00 35.02 ? 1    ALA A C   1 
ATOM   4     O  O   . ALA A  1 1   ? 35.999  -25.931 -2.875  1.00 38.82 ? 1    ALA A O   1 
ATOM   5     C  CB  . ALA A  1 1   ? 35.059  -23.584 -3.952  1.00 38.80 ? 1    ALA A CB  1 
ATOM   6     N  N   . THR A  1 2   ? 36.026  -25.193 -0.743  1.00 29.79 ? 2    THR A N   1 
ATOM   7     C  CA  . THR A  1 2   ? 36.985  -26.198 -0.285  1.00 29.32 ? 2    THR A CA  1 
ATOM   8     C  C   . THR A  1 2   ? 36.359  -27.571 -0.055  1.00 25.46 ? 2    THR A C   1 
ATOM   9     O  O   . THR A  1 2   ? 35.210  -27.680 0.344   1.00 23.93 ? 2    THR A O   1 
ATOM   10    C  CB  . THR A  1 2   ? 37.718  -25.744 0.996   1.00 27.30 ? 2    THR A CB  1 
ATOM   11    O  OG1 . THR A  1 2   ? 38.249  -24.432 0.798   1.00 37.14 ? 2    THR A OG1 1 
ATOM   12    C  CG2 . THR A  1 2   ? 38.865  -26.685 1.329   1.00 29.15 ? 2    THR A CG2 1 
ATOM   13    N  N   . LYS A  1 3   ? 37.136  -28.612 -0.328  1.00 24.58 ? 3    LYS A N   1 
ATOM   14    C  CA  . LYS A  1 3   ? 36.729  -29.985 -0.070  1.00 21.25 ? 3    LYS A CA  1 
ATOM   15    C  C   . LYS A  1 3   ? 37.789  -30.688 0.762   1.00 20.57 ? 3    LYS A C   1 
ATOM   16    O  O   . LYS A  1 3   ? 38.985  -30.449 0.611   1.00 20.52 ? 3    LYS A O   1 
ATOM   17    C  CB  . LYS A  1 3   ? 36.528  -30.750 -1.374  1.00 22.63 ? 3    LYS A CB  1 
ATOM   18    C  CG  . LYS A  1 3   ? 35.458  -30.158 -2.279  1.00 28.02 ? 3    LYS A CG  1 
ATOM   19    C  CD  . LYS A  1 3   ? 35.322  -30.943 -3.574  1.00 31.34 ? 3    LYS A CD  1 
ATOM   20    C  CE  . LYS A  1 3   ? 33.970  -31.655 -3.682  1.00 36.66 ? 3    LYS A CE  1 
ATOM   21    N  NZ  . LYS A  1 3   ? 33.954  -33.019 -3.070  1.00 38.52 ? 3    LYS A NZ  1 
ATOM   22    N  N   . ALA A  1 4   ? 37.344  -31.548 1.660   1.00 19.52 ? 4    ALA A N   1 
ATOM   23    C  CA  . ALA A  1 4   ? 38.257  -32.376 2.418   1.00 16.77 ? 4    ALA A CA  1 
ATOM   24    C  C   . ALA A  1 4   ? 37.666  -33.782 2.497   1.00 17.32 ? 4    ALA A C   1 
ATOM   25    O  O   . ALA A  1 4   ? 36.526  -34.017 2.092   1.00 16.92 ? 4    ALA A O   1 
ATOM   26    C  CB  . ALA A  1 4   ? 38.489  -31.795 3.794   1.00 15.82 ? 4    ALA A CB  1 
ATOM   27    N  N   . VAL A  1 5   ? 38.459  -34.727 2.978   1.00 18.93 ? 5    VAL A N   1 
ATOM   28    C  CA  . VAL A  1 5   ? 38.034  -36.121 3.038   1.00 18.46 ? 5    VAL A CA  1 
ATOM   29    C  C   . VAL A  1 5   ? 38.793  -36.815 4.172   1.00 17.92 ? 5    VAL A C   1 
ATOM   30    O  O   . VAL A  1 5   ? 39.819  -36.327 4.646   1.00 16.29 ? 5    VAL A O   1 
ATOM   31    C  CB  . VAL A  1 5   ? 38.265  -36.848 1.678   1.00 18.64 ? 5    VAL A CB  1 
ATOM   32    C  CG1 . VAL A  1 5   ? 39.752  -37.022 1.413   1.00 15.74 ? 5    VAL A CG1 1 
ATOM   33    C  CG2 . VAL A  1 5   ? 37.532  -38.194 1.636   1.00 16.69 ? 5    VAL A CG2 1 
ATOM   34    N  N   . CYS A  1 6   ? 38.279  -37.956 4.602   1.00 19.25 ? 6    CYS A N   1 
ATOM   35    C  CA  . CYS A  1 6   ? 38.842  -38.657 5.729   1.00 15.42 ? 6    CYS A CA  1 
ATOM   36    C  C   . CYS A  1 6   ? 38.523  -40.138 5.576   1.00 16.57 ? 6    CYS A C   1 
ATOM   37    O  O   . CYS A  1 6   ? 37.374  -40.501 5.409   1.00 18.70 ? 6    CYS A O   1 
ATOM   38    C  CB  . CYS A  1 6   ? 38.183  -38.119 6.994   1.00 16.22 ? 6    CYS A CB  1 
ATOM   39    S  SG  . CYS A  1 6   ? 38.740  -38.850 8.503   1.00 23.13 ? 6    CYS A SG  1 
ATOM   40    N  N   . VAL A  1 7   ? 39.531  -40.993 5.634   1.00 18.33 ? 7    VAL A N   1 
ATOM   41    C  CA  . VAL A  1 7   ? 39.303  -42.434 5.716   1.00 18.76 ? 7    VAL A CA  1 
ATOM   42    C  C   . VAL A  1 7   ? 39.376  -42.879 7.192   1.00 18.42 ? 7    VAL A C   1 
ATOM   43    O  O   . VAL A  1 7   ? 40.422  -42.765 7.820   1.00 18.80 ? 7    VAL A O   1 
ATOM   44    C  CB  . VAL A  1 7   ? 40.329  -43.207 4.843   1.00 17.38 ? 7    VAL A CB  1 
ATOM   45    C  CG1 . VAL A  1 7   ? 40.060  -44.699 4.880   1.00 16.69 ? 7    VAL A CG1 1 
ATOM   46    C  CG2 . VAL A  1 7   ? 40.282  -42.684 3.409   1.00 19.43 ? 7    VAL A CG2 1 
ATOM   47    N  N   . LEU A  1 8   ? 38.264  -43.349 7.754   1.00 17.23 ? 8    LEU A N   1 
ATOM   48    C  CA  . LEU A  1 8   ? 38.260  -43.835 9.135   1.00 17.58 ? 8    LEU A CA  1 
ATOM   49    C  C   . LEU A  1 8   ? 38.646  -45.323 9.211   1.00 19.20 ? 8    LEU A C   1 
ATOM   50    O  O   . LEU A  1 8   ? 38.041  -46.161 8.556   1.00 18.65 ? 8    LEU A O   1 
ATOM   51    C  CB  . LEU A  1 8   ? 36.891  -43.613 9.821   1.00 18.38 ? 8    LEU A CB  1 
ATOM   52    C  CG  . LEU A  1 8   ? 36.123  -42.277 9.840   1.00 18.88 ? 8    LEU A CG  1 
ATOM   53    C  CD1 . LEU A  1 8   ? 34.783  -42.454 10.510  1.00 18.56 ? 8    LEU A CD1 1 
ATOM   54    C  CD2 . LEU A  1 8   ? 36.867  -41.169 10.533  1.00 18.58 ? 8    LEU A CD2 1 
ATOM   55    N  N   . LYS A  1 9   ? 39.661  -45.640 10.012  1.00 21.10 ? 9    LYS A N   1 
ATOM   56    C  CA  . LYS A  1 9   ? 40.058  -47.027 10.283  1.00 21.87 ? 9    LYS A CA  1 
ATOM   57    C  C   . LYS A  1 9   ? 40.328  -47.179 11.762  1.00 20.70 ? 9    LYS A C   1 
ATOM   58    O  O   . LYS A  1 9   ? 40.620  -46.199 12.442  1.00 19.85 ? 9    LYS A O   1 
ATOM   59    C  CB  . LYS A  1 9   ? 41.306  -47.426 9.489   1.00 22.34 ? 9    LYS A CB  1 
ATOM   60    C  CG  . LYS A  1 9   ? 41.021  -47.648 8.005   1.00 28.23 ? 9    LYS A CG  1 
ATOM   61    C  CD  . LYS A  1 9   ? 42.300  -47.843 7.184   1.00 34.80 ? 9    LYS A CD  1 
ATOM   62    C  CE  . LYS A  1 9   ? 41.956  -48.122 5.718   1.00 39.26 ? 9    LYS A CE  1 
ATOM   63    N  NZ  . LYS A  1 9   ? 41.070  -49.317 5.598   1.00 38.21 ? 9    LYS A NZ  1 
ATOM   64    N  N   . GLY A  1 10  ? 40.233  -48.410 12.258  1.00 23.59 ? 10   GLY A N   1 
ATOM   65    C  CA  . GLY A  1 10  ? 40.491  -48.701 13.665  1.00 24.52 ? 10   GLY A CA  1 
ATOM   66    C  C   . GLY A  1 10  ? 41.030  -50.112 13.824  1.00 28.19 ? 10   GLY A C   1 
ATOM   67    O  O   . GLY A  1 10  ? 41.555  -50.687 12.868  1.00 30.08 ? 10   GLY A O   1 
ATOM   68    N  N   . ASP A  1 11  ? 40.893  -50.683 15.017  1.00 27.95 ? 11   ASP A N   1 
ATOM   69    C  CA  . ASP A  1 11  ? 41.403  -52.034 15.281  1.00 28.84 ? 11   ASP A CA  1 
ATOM   70    C  C   . ASP A  1 11  ? 40.338  -53.107 15.058  1.00 26.75 ? 11   ASP A C   1 
ATOM   71    O  O   . ASP A  1 11  ? 40.641  -54.293 14.929  1.00 26.74 ? 11   ASP A O   1 
ATOM   72    C  CB  . ASP A  1 11  ? 41.942  -52.133 16.710  1.00 28.89 ? 11   ASP A CB  1 
ATOM   73    C  CG  . ASP A  1 11  ? 43.166  -51.266 16.933  1.00 34.48 ? 11   ASP A CG  1 
ATOM   74    O  OD1 . ASP A  1 11  ? 43.956  -51.082 15.978  1.00 35.12 ? 11   ASP A OD1 1 
ATOM   75    O  OD2 . ASP A  1 11  ? 43.340  -50.771 18.069  1.00 41.22 ? 11   ASP A OD2 1 
ATOM   76    N  N   . GLY A  1 12  ? 39.086  -52.678 15.011  1.00 24.60 ? 12   GLY A N   1 
ATOM   77    C  CA  . GLY A  1 12  ? 37.984  -53.595 14.828  1.00 23.37 ? 12   GLY A CA  1 
ATOM   78    C  C   . GLY A  1 12  ? 37.406  -53.497 13.434  1.00 23.55 ? 12   GLY A C   1 
ATOM   79    O  O   . GLY A  1 12  ? 38.129  -53.241 12.473  1.00 25.78 ? 12   GLY A O   1 
ATOM   80    N  N   . PRO A  1 13  ? 36.089  -53.699 13.318  1.00 23.29 ? 13   PRO A N   1 
ATOM   81    C  CA  . PRO A  1 13  ? 35.342  -53.760 12.063  1.00 21.37 ? 13   PRO A CA  1 
ATOM   82    C  C   . PRO A  1 13  ? 35.040  -52.384 11.454  1.00 19.44 ? 13   PRO A C   1 
ATOM   83    O  O   . PRO A  1 13  ? 34.786  -52.281 10.254  1.00 19.09 ? 13   PRO A O   1 
ATOM   84    C  CB  . PRO A  1 13  ? 34.022  -54.419 12.489  1.00 21.34 ? 13   PRO A CB  1 
ATOM   85    C  CG  . PRO A  1 13  ? 34.211  -54.873 13.858  1.00 18.41 ? 13   PRO A CG  1 
ATOM   86    C  CD  . PRO A  1 13  ? 35.214  -53.978 14.459  1.00 20.05 ? 13   PRO A CD  1 
ATOM   87    N  N   . VAL A  1 14  ? 35.046  -51.344 12.277  1.00 19.90 ? 14   VAL A N   1 
ATOM   88    C  CA  . VAL A  1 14  ? 34.605  -50.020 11.839  1.00 19.05 ? 14   VAL A CA  1 
ATOM   89    C  C   . VAL A  1 14  ? 35.564  -49.360 10.836  1.00 19.12 ? 14   VAL A C   1 
ATOM   90    O  O   . VAL A  1 14  ? 36.782  -49.319 11.031  1.00 19.43 ? 14   VAL A O   1 
ATOM   91    C  CB  . VAL A  1 14  ? 34.352  -49.093 13.051  1.00 17.20 ? 14   VAL A CB  1 
ATOM   92    C  CG1 . VAL A  1 14  ? 33.763  -47.756 12.602  1.00 15.80 ? 14   VAL A CG1 1 
ATOM   93    C  CG2 . VAL A  1 14  ? 33.440  -49.775 14.049  1.00 15.96 ? 14   VAL A CG2 1 
ATOM   94    N  N   . GLN A  1 15  ? 34.997  -48.851 9.752   1.00 21.68 ? 15   GLN A N   1 
ATOM   95    C  CA  . GLN A  1 15  ? 35.773  -48.182 8.717   1.00 20.33 ? 15   GLN A CA  1 
ATOM   96    C  C   . GLN A  1 15  ? 34.801  -47.425 7.833   1.00 18.40 ? 15   GLN A C   1 
ATOM   97    O  O   . GLN A  1 15  ? 33.679  -47.873 7.636   1.00 21.08 ? 15   GLN A O   1 
ATOM   98    C  CB  . GLN A  1 15  ? 36.553  -49.206 7.890   1.00 22.38 ? 15   GLN A CB  1 
ATOM   99    C  CG  . GLN A  1 15  ? 35.708  -50.008 6.903   1.00 23.93 ? 15   GLN A CG  1 
ATOM   100   C  CD  . GLN A  1 15  ? 36.554  -50.627 5.788   1.00 32.75 ? 15   GLN A CD  1 
ATOM   101   O  OE1 . GLN A  1 15  ? 36.570  -51.852 5.594   1.00 27.79 ? 15   GLN A OE1 1 
ATOM   102   N  NE2 . GLN A  1 15  ? 37.278  -49.777 5.060   1.00 33.65 ? 15   GLN A NE2 1 
ATOM   103   N  N   . GLY A  1 16  ? 35.215  -46.276 7.307   1.00 18.55 ? 16   GLY A N   1 
ATOM   104   C  CA  . GLY A  1 16  ? 34.352  -45.482 6.451   1.00 17.48 ? 16   GLY A CA  1 
ATOM   105   C  C   . GLY A  1 16  ? 35.117  -44.407 5.708   1.00 19.09 ? 16   GLY A C   1 
ATOM   106   O  O   . GLY A  1 16  ? 36.329  -44.302 5.835   1.00 18.14 ? 16   GLY A O   1 
ATOM   107   N  N   . ILE A  1 17  ? 34.406  -43.628 4.898   1.00 19.36 ? 17   ILE A N   1 
ATOM   108   C  CA  . ILE A  1 17  ? 34.981  -42.466 4.229   1.00 19.08 ? 17   ILE A CA  1 
ATOM   109   C  C   . ILE A  1 17  ? 34.052  -41.303 4.524   1.00 17.32 ? 17   ILE A C   1 
ATOM   110   O  O   . ILE A  1 17  ? 32.835  -41.426 4.368   1.00 18.12 ? 17   ILE A O   1 
ATOM   111   C  CB  . ILE A  1 17  ? 35.120  -42.664 2.692   1.00 19.19 ? 17   ILE A CB  1 
ATOM   112   C  CG1 . ILE A  1 17  ? 36.049  -43.839 2.377   1.00 18.64 ? 17   ILE A CG1 1 
ATOM   113   C  CG2 . ILE A  1 17  ? 35.650  -41.396 2.019   1.00 15.98 ? 17   ILE A CG2 1 
ATOM   114   C  CD1 . ILE A  1 17  ? 35.926  -44.322 0.952   1.00 16.53 ? 17   ILE A CD1 1 
ATOM   115   N  N   . ILE A  1 18  ? 34.614  -40.191 4.985   1.00 15.59 ? 18   ILE A N   1 
ATOM   116   C  CA  . ILE A  1 18  ? 33.812  -39.027 5.306   1.00 14.74 ? 18   ILE A CA  1 
ATOM   117   C  C   . ILE A  1 18  ? 34.276  -37.836 4.482   1.00 14.54 ? 18   ILE A C   1 
ATOM   118   O  O   . ILE A  1 18  ? 35.446  -37.495 4.487   1.00 15.28 ? 18   ILE A O   1 
ATOM   119   C  CB  . ILE A  1 18  ? 33.827  -38.712 6.821   1.00 14.84 ? 18   ILE A CB  1 
ATOM   120   C  CG1 . ILE A  1 18  ? 33.155  -39.847 7.601   1.00 16.97 ? 18   ILE A CG1 1 
ATOM   121   C  CG2 . ILE A  1 18  ? 33.095  -37.404 7.123   1.00 14.07 ? 18   ILE A CG2 1 
ATOM   122   C  CD1 . ILE A  1 18  ? 31.677  -40.033 7.279   1.00 13.16 ? 18   ILE A CD1 1 
ATOM   123   N  N   . ASN A  1 19  ? 33.343  -37.223 3.761   1.00 15.35 ? 19   ASN A N   1 
ATOM   124   C  CA  . ASN A  1 19  ? 33.635  -36.077 2.914   1.00 17.59 ? 19   ASN A CA  1 
ATOM   125   C  C   . ASN A  1 19  ? 33.194  -34.778 3.561   1.00 16.76 ? 19   ASN A C   1 
ATOM   126   O  O   . ASN A  1 19  ? 32.208  -34.751 4.283   1.00 15.39 ? 19   ASN A O   1 
ATOM   127   C  CB  . ASN A  1 19  ? 32.970  -36.249 1.551   1.00 17.25 ? 19   ASN A CB  1 
ATOM   128   C  CG  . ASN A  1 19  ? 33.372  -37.531 0.890   1.00 17.77 ? 19   ASN A CG  1 
ATOM   129   O  OD1 . ASN A  1 19  ? 34.451  -37.625 0.303   1.00 21.53 ? 19   ASN A OD1 1 
ATOM   130   N  ND2 . ASN A  1 19  ? 32.531  -38.550 1.018   1.00 18.75 ? 19   ASN A ND2 1 
ATOM   131   N  N   . PHE A  1 20  ? 33.953  -33.712 3.320   1.00 17.30 ? 20   PHE A N   1 
ATOM   132   C  CA  . PHE A  1 20  ? 33.614  -32.378 3.808   1.00 18.50 ? 20   PHE A CA  1 
ATOM   133   C  C   . PHE A  1 20  ? 33.562  -31.429 2.614   1.00 21.38 ? 20   PHE A C   1 
ATOM   134   O  O   . PHE A  1 20  ? 34.380  -31.528 1.712   1.00 22.32 ? 20   PHE A O   1 
ATOM   135   C  CB  . PHE A  1 20  ? 34.650  -31.870 4.819   1.00 17.58 ? 20   PHE A CB  1 
ATOM   136   C  CG  . PHE A  1 20  ? 34.955  -32.837 5.934   1.00 17.40 ? 20   PHE A CG  1 
ATOM   137   C  CD1 . PHE A  1 20  ? 35.721  -33.974 5.706   1.00 16.73 ? 20   PHE A CD1 1 
ATOM   138   C  CD2 . PHE A  1 20  ? 34.510  -32.593 7.212   1.00 16.76 ? 20   PHE A CD2 1 
ATOM   139   C  CE1 . PHE A  1 20  ? 36.014  -34.847 6.736   1.00 15.63 ? 20   PHE A CE1 1 
ATOM   140   C  CE2 . PHE A  1 20  ? 34.804  -33.469 8.237   1.00 16.02 ? 20   PHE A CE2 1 
ATOM   141   C  CZ  . PHE A  1 20  ? 35.553  -34.596 7.991   1.00 14.38 ? 20   PHE A CZ  1 
ATOM   142   N  N   . GLU A  1 21  ? 32.593  -30.523 2.604   1.00 22.83 ? 21   GLU A N   1 
ATOM   143   C  CA  . GLU A  1 21  ? 32.501  -29.524 1.550   1.00 24.29 ? 21   GLU A CA  1 
ATOM   144   C  C   . GLU A  1 21  ? 32.000  -28.202 2.106   1.00 24.69 ? 21   GLU A C   1 
ATOM   145   O  O   . GLU A  1 21  ? 30.967  -28.136 2.771   1.00 24.53 ? 21   GLU A O   1 
ATOM   146   C  CB  . GLU A  1 21  ? 31.588  -29.993 0.414   1.00 28.61 ? 21   GLU A CB  1 
ATOM   147   C  CG  . GLU A  1 21  ? 31.759  -29.196 -0.889  1.00 31.64 ? 21   GLU A CG  1 
ATOM   148   C  CD  . GLU A  1 21  ? 30.659  -29.500 -1.900  1.00 43.51 ? 21   GLU A CD  1 
ATOM   149   O  OE1 . GLU A  1 21  ? 30.141  -30.641 -1.895  1.00 46.77 ? 21   GLU A OE1 1 
ATOM   150   O  OE2 . GLU A  1 21  ? 30.311  -28.601 -2.700  1.00 49.11 ? 21   GLU A OE2 1 
ATOM   151   N  N   . GLN A  1 22  ? 32.751  -27.149 1.830   1.00 25.06 ? 22   GLN A N   1 
ATOM   152   C  CA  . GLN A  1 22  ? 32.379  -25.808 2.240   1.00 26.72 ? 22   GLN A CA  1 
ATOM   153   C  C   . GLN A  1 22  ? 32.315  -24.940 0.992   1.00 28.44 ? 22   GLN A C   1 
ATOM   154   O  O   . GLN A  1 22  ? 33.348  -24.592 0.430   1.00 28.79 ? 22   GLN A O   1 
ATOM   155   C  CB  . GLN A  1 22  ? 33.429  -25.267 3.202   1.00 24.64 ? 22   GLN A CB  1 
ATOM   156   C  CG  . GLN A  1 22  ? 32.955  -24.130 4.043   1.00 26.18 ? 22   GLN A CG  1 
ATOM   157   C  CD  . GLN A  1 22  ? 33.989  -23.717 5.043   1.00 22.86 ? 22   GLN A CD  1 
ATOM   158   O  OE1 . GLN A  1 22  ? 35.176  -23.963 4.845   1.00 24.62 ? 22   GLN A OE1 1 
ATOM   159   N  NE2 . GLN A  1 22  ? 33.554  -23.090 6.127   1.00 21.15 ? 22   GLN A NE2 1 
ATOM   160   N  N   . LYS A  1 23  ? 31.106  -24.620 0.541   1.00 30.18 ? 23   LYS A N   1 
ATOM   161   C  CA  . LYS A  1 23  ? 30.934  -23.848 -0.690  1.00 32.53 ? 23   LYS A CA  1 
ATOM   162   C  C   . LYS A  1 23  ? 31.441  -22.421 -0.514  1.00 33.10 ? 23   LYS A C   1 
ATOM   163   O  O   . LYS A  1 23  ? 32.056  -21.855 -1.419  1.00 31.23 ? 23   LYS A O   1 
ATOM   164   C  CB  . LYS A  1 23  ? 29.462  -23.792 -1.095  1.00 35.37 ? 23   LYS A CB  1 
ATOM   165   C  CG  . LYS A  1 23  ? 28.755  -25.130 -1.159  1.00 43.09 ? 23   LYS A CG  1 
ATOM   166   C  CD  . LYS A  1 23  ? 29.071  -25.879 -2.445  1.00 43.66 ? 23   LYS A CD  1 
ATOM   167   C  CE  . LYS A  1 23  ? 27.875  -26.727 -2.881  1.00 51.30 ? 23   LYS A CE  1 
ATOM   168   N  NZ  . LYS A  1 23  ? 26.662  -25.885 -3.156  1.00 56.42 ? 23   LYS A NZ  1 
ATOM   169   N  N   . GLU A  1 24  ? 31.155  -21.844 0.654   1.00 30.97 ? 24   GLU A N   1 
ATOM   170   C  CA  . GLU A  1 24  ? 31.507  -20.459 0.941   1.00 32.52 ? 24   GLU A CA  1 
ATOM   171   C  C   . GLU A  1 24  ? 32.506  -20.447 2.083   1.00 30.19 ? 24   GLU A C   1 
ATOM   172   O  O   . GLU A  1 24  ? 32.513  -21.348 2.904   1.00 28.84 ? 24   GLU A O   1 
ATOM   173   C  CB  . GLU A  1 24  ? 30.268  -19.632 1.334   1.00 32.60 ? 24   GLU A CB  1 
ATOM   174   C  CG  . GLU A  1 24  ? 28.976  -19.938 0.572   1.00 35.11 ? 24   GLU A CG  1 
ATOM   175   C  CD  . GLU A  1 24  ? 29.010  -19.494 -0.890  1.00 38.91 ? 24   GLU A CD  1 
ATOM   176   O  OE1 . GLU A  1 24  ? 28.162  -19.976 -1.678  1.00 41.25 ? 24   GLU A OE1 1 
ATOM   177   O  OE2 . GLU A  1 24  ? 29.884  -18.672 -1.253  1.00 41.34 ? 24   GLU A OE2 1 
ATOM   178   N  N   . SER A  1 25  ? 33.362  -19.437 2.139   1.00 32.56 ? 25   SER A N   1 
ATOM   179   C  CA  . SER A  1 25  ? 34.308  -19.373 3.235   1.00 31.57 ? 25   SER A CA  1 
ATOM   180   C  C   . SER A  1 25  ? 33.554  -18.788 4.417   1.00 33.65 ? 25   SER A C   1 
ATOM   181   O  O   . SER A  1 25  ? 32.751  -17.866 4.251   1.00 36.09 ? 25   SER A O   1 
ATOM   182   C  CB  . SER A  1 25  ? 35.558  -18.556 2.868   1.00 33.31 ? 25   SER A CB  1 
ATOM   183   O  OG  . SER A  1 25  ? 35.424  -17.194 3.224   1.00 32.31 ? 25   SER A OG  1 
ATOM   184   N  N   . ASN A  1 26  ? 33.784  -19.358 5.597   1.00 34.42 ? 26   ASN A N   1 
ATOM   185   C  CA  . ASN A  1 26  ? 33.034  -19.015 6.805   1.00 35.22 ? 26   ASN A CA  1 
ATOM   186   C  C   . ASN A  1 26  ? 31.559  -19.445 6.757   1.00 34.85 ? 26   ASN A C   1 
ATOM   187   O  O   . ASN A  1 26  ? 30.747  -19.046 7.603   1.00 37.03 ? 26   ASN A O   1 
ATOM   188   C  CB  . ASN A  1 26  ? 33.194  -17.526 7.157   1.00 36.19 ? 26   ASN A CB  1 
ATOM   189   C  CG  . ASN A  1 26  ? 34.494  -17.248 7.905   1.00 41.04 ? 26   ASN A CG  1 
ATOM   190   O  OD1 . ASN A  1 26  ? 35.572  -17.641 7.459   1.00 42.82 ? 26   ASN A OD1 1 
ATOM   191   N  ND2 . ASN A  1 26  ? 34.394  -16.594 9.061   1.00 42.47 ? 26   ASN A ND2 1 
ATOM   192   N  N   . GLY A  1 27  ? 31.226  -20.276 5.772   1.00 30.95 ? 27   GLY A N   1 
ATOM   193   C  CA  . GLY A  1 27  ? 29.874  -20.785 5.625   1.00 29.78 ? 27   GLY A CA  1 
ATOM   194   C  C   . GLY A  1 27  ? 29.749  -22.222 6.105   1.00 29.66 ? 27   GLY A C   1 
ATOM   195   O  O   . GLY A  1 27  ? 30.738  -22.840 6.501   1.00 29.05 ? 27   GLY A O   1 
ATOM   196   N  N   . PRO A  1 28  ? 28.528  -22.767 6.062   1.00 29.67 ? 28   PRO A N   1 
ATOM   197   C  CA  . PRO A  1 28  ? 28.235  -24.129 6.527   1.00 28.10 ? 28   PRO A CA  1 
ATOM   198   C  C   . PRO A  1 28  ? 29.198  -25.167 5.931   1.00 26.37 ? 28   PRO A C   1 
ATOM   199   O  O   . PRO A  1 28  ? 29.584  -25.055 4.774   1.00 28.10 ? 28   PRO A O   1 
ATOM   200   C  CB  . PRO A  1 28  ? 26.813  -24.384 5.998   1.00 30.69 ? 28   PRO A CB  1 
ATOM   201   C  CG  . PRO A  1 28  ? 26.231  -23.026 5.754   1.00 33.30 ? 28   PRO A CG  1 
ATOM   202   C  CD  . PRO A  1 28  ? 27.372  -22.128 5.405   1.00 30.25 ? 28   PRO A CD  1 
ATOM   203   N  N   . VAL A  1 29  ? 29.575  -26.165 6.721   1.00 26.54 ? 29   VAL A N   1 
ATOM   204   C  CA  . VAL A  1 29  ? 30.312  -27.321 6.217   1.00 25.40 ? 29   VAL A CA  1 
ATOM   205   C  C   . VAL A  1 29  ? 29.349  -28.527 6.118   1.00 22.78 ? 29   VAL A C   1 
ATOM   206   O  O   . VAL A  1 29  ? 28.624  -28.838 7.063   1.00 22.35 ? 29   VAL A O   1 
ATOM   207   C  CB  . VAL A  1 29  ? 31.553  -27.660 7.113   1.00 21.94 ? 29   VAL A CB  1 
ATOM   208   C  CG1 . VAL A  1 29  ? 32.346  -28.833 6.537   1.00 20.30 ? 29   VAL A CG1 1 
ATOM   209   C  CG2 . VAL A  1 29  ? 32.467  -26.445 7.260   1.00 20.17 ? 29   VAL A CG2 1 
ATOM   210   N  N   . LYS A  1 30  ? 29.322  -29.187 4.967   1.00 19.64 ? 30   LYS A N   1 
ATOM   211   C  CA  . LYS A  1 30  ? 28.548  -30.411 4.825   1.00 22.13 ? 30   LYS A CA  1 
ATOM   212   C  C   . LYS A  1 30  ? 29.481  -31.604 5.010   1.00 19.69 ? 30   LYS A C   1 
ATOM   213   O  O   . LYS A  1 30  ? 30.478  -31.729 4.302   1.00 22.15 ? 30   LYS A O   1 
ATOM   214   C  CB  . LYS A  1 30  ? 27.865  -30.449 3.452   1.00 25.99 ? 30   LYS A CB  1 
ATOM   215   C  CG  . LYS A  1 30  ? 26.848  -31.580 3.246   1.00 27.81 ? 30   LYS A CG  1 
ATOM   216   C  CD  . LYS A  1 30  ? 26.293  -31.522 1.816   1.00 33.54 ? 30   LYS A CD  1 
ATOM   217   C  CE  . LYS A  1 30  ? 25.232  -32.586 1.560   1.00 37.30 ? 30   LYS A CE  1 
ATOM   218   N  NZ  . LYS A  1 30  ? 25.813  -33.881 1.107   1.00 33.04 ? 30   LYS A NZ  1 
ATOM   219   N  N   . VAL A  1 31  ? 29.162  -32.455 5.982   1.00 18.28 ? 31   VAL A N   1 
ATOM   220   C  CA  . VAL A  1 31  ? 29.955  -33.635 6.335   1.00 18.27 ? 31   VAL A CA  1 
ATOM   221   C  C   . VAL A  1 31  ? 29.104  -34.843 6.002   1.00 18.82 ? 31   VAL A C   1 
ATOM   222   O  O   . VAL A  1 31  ? 28.097  -35.073 6.651   1.00 20.63 ? 31   VAL A O   1 
ATOM   223   C  CB  . VAL A  1 31  ? 30.284  -33.664 7.862   1.00 17.81 ? 31   VAL A CB  1 
ATOM   224   C  CG1 . VAL A  1 31  ? 31.138  -34.859 8.229   1.00 13.88 ? 31   VAL A CG1 1 
ATOM   225   C  CG2 . VAL A  1 31  ? 30.956  -32.375 8.305   1.00 17.44 ? 31   VAL A CG2 1 
ATOM   226   N  N   . TRP A  1 32  ? 29.478  -35.604 4.979   1.00 18.40 ? 32   TRP A N   1 
ATOM   227   C  CA  . TRP A  1 32  ? 28.654  -36.725 4.546   1.00 16.14 ? 32   TRP A CA  1 
ATOM   228   C  C   . TRP A  1 32  ? 29.496  -37.925 4.139   1.00 16.25 ? 32   TRP A C   1 
ATOM   229   O  O   . TRP A  1 32  ? 30.615  -37.789 3.674   1.00 17.82 ? 32   TRP A O   1 
ATOM   230   C  CB  . TRP A  1 32  ? 27.731  -36.303 3.394   1.00 19.59 ? 32   TRP A CB  1 
ATOM   231   C  CG  . TRP A  1 32  ? 28.404  -36.332 2.057   1.00 22.31 ? 32   TRP A CG  1 
ATOM   232   C  CD1 . TRP A  1 32  ? 28.434  -37.379 1.174   1.00 23.01 ? 32   TRP A CD1 1 
ATOM   233   C  CD2 . TRP A  1 32  ? 29.167  -35.281 1.456   1.00 20.60 ? 32   TRP A CD2 1 
ATOM   234   N  NE1 . TRP A  1 32  ? 29.169  -37.038 0.065   1.00 22.92 ? 32   TRP A NE1 1 
ATOM   235   C  CE2 . TRP A  1 32  ? 29.632  -35.758 0.216   1.00 22.20 ? 32   TRP A CE2 1 
ATOM   236   C  CE3 . TRP A  1 32  ? 29.505  -33.983 1.849   1.00 23.54 ? 32   TRP A CE3 1 
ATOM   237   C  CZ2 . TRP A  1 32  ? 30.414  -34.981 -0.639  1.00 29.22 ? 32   TRP A CZ2 1 
ATOM   238   C  CZ3 . TRP A  1 32  ? 30.281  -33.210 0.997   1.00 25.42 ? 32   TRP A CZ3 1 
ATOM   239   C  CH2 . TRP A  1 32  ? 30.728  -33.712 -0.231  1.00 27.39 ? 32   TRP A CH2 1 
ATOM   240   N  N   . GLY A  1 33  ? 28.951  -39.114 4.305   1.00 15.34 ? 33   GLY A N   1 
ATOM   241   C  CA  . GLY A  1 33  ? 29.675  -40.307 3.934   1.00 16.95 ? 33   GLY A CA  1 
ATOM   242   C  C   . GLY A  1 33  ? 28.984  -41.497 4.539   1.00 15.00 ? 33   GLY A C   1 
ATOM   243   O  O   . GLY A  1 33  ? 27.836  -41.402 4.890   1.00 18.04 ? 33   GLY A O   1 
ATOM   244   N  N   . SER A  1 34  ? 29.676  -42.618 4.648   1.00 18.53 ? 34   SER A N   1 
ATOM   245   C  CA  . SER A  1 34  ? 29.157  -43.755 5.394   1.00 20.59 ? 34   SER A CA  1 
ATOM   246   C  C   . SER A  1 34  ? 30.246  -44.460 6.213   1.00 20.99 ? 34   SER A C   1 
ATOM   247   O  O   . SER A  1 34  ? 31.435  -44.419 5.868   1.00 20.36 ? 34   SER A O   1 
ATOM   248   C  CB  . SER A  1 34  ? 28.424  -44.737 4.478   1.00 19.41 ? 34   SER A CB  1 
ATOM   249   O  OG  . SER A  1 34  ? 29.276  -45.143 3.443   1.00 27.41 ? 34   SER A OG  1 
ATOM   250   N  N   . ILE A  1 35  ? 29.821  -45.053 7.329   1.00 17.80 ? 35   ILE A N   1 
ATOM   251   C  CA  . ILE A  1 35  ? 30.672  -45.873 8.167   1.00 14.09 ? 35   ILE A CA  1 
ATOM   252   C  C   . ILE A  1 35  ? 29.988  -47.230 8.351   1.00 14.49 ? 35   ILE A C   1 
ATOM   253   O  O   . ILE A  1 35  ? 28.799  -47.302 8.609   1.00 15.29 ? 35   ILE A O   1 
ATOM   254   C  CB  . ILE A  1 35  ? 30.897  -45.210 9.543   1.00 16.54 ? 35   ILE A CB  1 
ATOM   255   C  CG1 . ILE A  1 35  ? 31.304  -43.741 9.383   1.00 15.98 ? 35   ILE A CG1 1 
ATOM   256   C  CG2 . ILE A  1 35  ? 31.931  -45.971 10.370  1.00 14.74 ? 35   ILE A CG2 1 
ATOM   257   C  CD1 . ILE A  1 35  ? 31.307  -42.968 10.711  1.00 15.39 ? 35   ILE A CD1 1 
ATOM   258   N  N   . LYS A  1 36  ? 30.731  -48.313 8.190   1.00 17.16 ? 36   LYS A N   1 
ATOM   259   C  CA  . LYS A  1 36  ? 30.194  -49.631 8.507   1.00 17.97 ? 36   LYS A CA  1 
ATOM   260   C  C   . LYS A  1 36  ? 30.875  -50.229 9.748   1.00 16.81 ? 36   LYS A C   1 
ATOM   261   O  O   . LYS A  1 36  ? 31.739  -49.588 10.339  1.00 16.57 ? 36   LYS A O   1 
ATOM   262   C  CB  . LYS A  1 36  ? 30.287  -50.559 7.291   1.00 18.97 ? 36   LYS A CB  1 
ATOM   263   C  CG  . LYS A  1 36  ? 31.455  -50.292 6.361   1.00 17.02 ? 36   LYS A CG  1 
ATOM   264   C  CD  . LYS A  1 36  ? 32.460  -51.424 6.414   1.00 20.98 ? 36   LYS A CD  1 
ATOM   265   C  CE  . LYS A  1 36  ? 31.774  -52.756 6.122   1.00 26.99 ? 36   LYS A CE  1 
ATOM   266   N  NZ  . LYS A  1 36  ? 32.555  -53.951 6.596   1.00 27.56 ? 36   LYS A NZ  1 
ATOM   267   N  N   . GLY A  1 37  ? 30.453  -51.430 10.152  1.00 16.58 ? 37   GLY A N   1 
ATOM   268   C  CA  . GLY A  1 37  ? 31.027  -52.130 11.291  1.00 14.76 ? 37   GLY A CA  1 
ATOM   269   C  C   . GLY A  1 37  ? 30.439  -51.747 12.640  1.00 17.12 ? 37   GLY A C   1 
ATOM   270   O  O   . GLY A  1 37  ? 30.913  -52.195 13.688  1.00 17.33 ? 37   GLY A O   1 
ATOM   271   N  N   . LEU A  1 38  ? 29.391  -50.927 12.625  1.00 16.32 ? 38   LEU A N   1 
ATOM   272   C  CA  . LEU A  1 38  ? 28.879  -50.328 13.854  1.00 15.61 ? 38   LEU A CA  1 
ATOM   273   C  C   . LEU A  1 38  ? 27.677  -51.075 14.417  1.00 16.62 ? 38   LEU A C   1 
ATOM   274   O  O   . LEU A  1 38  ? 26.901  -51.670 13.671  1.00 19.23 ? 38   LEU A O   1 
ATOM   275   C  CB  . LEU A  1 38  ? 28.486  -48.863 13.598  1.00 15.97 ? 38   LEU A CB  1 
ATOM   276   C  CG  . LEU A  1 38  ? 29.569  -47.832 13.270  1.00 13.50 ? 38   LEU A CG  1 
ATOM   277   C  CD1 . LEU A  1 38  ? 28.952  -46.628 12.615  1.00 13.19 ? 38   LEU A CD1 1 
ATOM   278   C  CD2 . LEU A  1 38  ? 30.334  -47.428 14.505  1.00 13.12 ? 38   LEU A CD2 1 
ATOM   279   N  N   . THR A  1 39  ? 27.514  -51.038 15.737  1.00 18.25 ? 39   THR A N   1 
ATOM   280   C  CA  . THR A  1 39  ? 26.275  -51.504 16.330  1.00 16.89 ? 39   THR A CA  1 
ATOM   281   C  C   . THR A  1 39  ? 25.155  -50.495 16.060  1.00 18.34 ? 39   THR A C   1 
ATOM   282   O  O   . THR A  1 39  ? 25.386  -49.278 16.045  1.00 17.72 ? 39   THR A O   1 
ATOM   283   C  CB  . THR A  1 39  ? 26.417  -51.708 17.826  1.00 17.61 ? 39   THR A CB  1 
ATOM   284   O  OG1 . THR A  1 39  ? 26.774  -50.461 18.438  1.00 20.16 ? 39   THR A OG1 1 
ATOM   285   C  CG2 . THR A  1 39  ? 27.478  -52.760 18.117  1.00 18.37 ? 39   THR A CG2 1 
ATOM   286   N  N   . GLU A  1 40  ? 23.946  -51.008 15.849  1.00 18.50 ? 40   GLU A N   1 
ATOM   287   C  CA  . GLU A  1 40  ? 22.810  -50.174 15.496  1.00 19.48 ? 40   GLU A CA  1 
ATOM   288   C  C   . GLU A  1 40  ? 22.576  -49.130 16.564  1.00 17.67 ? 40   GLU A C   1 
ATOM   289   O  O   . GLU A  1 40  ? 22.723  -49.388 17.752  1.00 17.92 ? 40   GLU A O   1 
ATOM   290   C  CB  . GLU A  1 40  ? 21.549  -51.025 15.282  1.00 22.69 ? 40   GLU A CB  1 
ATOM   291   C  CG  . GLU A  1 40  ? 20.310  -50.206 14.911  1.00 24.64 ? 40   GLU A CG  1 
ATOM   292   C  CD  . GLU A  1 40  ? 19.109  -51.056 14.501  1.00 30.65 ? 40   GLU A CD  1 
ATOM   293   O  OE1 . GLU A  1 40  ? 19.128  -52.290 14.716  1.00 33.26 ? 40   GLU A OE1 1 
ATOM   294   O  OE2 . GLU A  1 40  ? 18.139  -50.479 13.959  1.00 34.92 ? 40   GLU A OE2 1 
ATOM   295   N  N   . GLY A  1 41  ? 22.224  -47.931 16.138  1.00 18.29 ? 41   GLY A N   1 
ATOM   296   C  CA  . GLY A  1 41  ? 21.956  -46.871 17.086  1.00 17.31 ? 41   GLY A CA  1 
ATOM   297   C  C   . GLY A  1 41  ? 22.892  -45.706 16.907  1.00 16.71 ? 41   GLY A C   1 
ATOM   298   O  O   . GLY A  1 41  ? 23.640  -45.627 15.935  1.00 16.40 ? 41   GLY A O   1 
ATOM   299   N  N   . LEU A  1 42  ? 22.851  -44.809 17.881  1.00 18.86 ? 42   LEU A N   1 
ATOM   300   C  CA  . LEU A  1 42  ? 23.617  -43.573 17.853  1.00 18.51 ? 42   LEU A CA  1 
ATOM   301   C  C   . LEU A  1 42  ? 25.049  -43.733 18.375  1.00 17.70 ? 42   LEU A C   1 
ATOM   302   O  O   . LEU A  1 42  ? 25.297  -44.426 19.371  1.00 16.12 ? 42   LEU A O   1 
ATOM   303   C  CB  . LEU A  1 42  ? 22.876  -42.483 18.635  1.00 18.15 ? 42   LEU A CB  1 
ATOM   304   C  CG  . LEU A  1 42  ? 21.592  -41.957 17.994  1.00 17.34 ? 42   LEU A CG  1 
ATOM   305   C  CD1 . LEU A  1 42  ? 20.760  -41.176 18.988  1.00 22.31 ? 42   LEU A CD1 1 
ATOM   306   C  CD2 . LEU A  1 42  ? 21.920  -41.087 16.828  1.00 18.56 ? 42   LEU A CD2 1 
ATOM   307   N  N   . HIS A  1 43  ? 25.978  -43.071 17.687  1.00 16.13 ? 43   HIS A N   1 
ATOM   308   C  CA  . HIS A  1 43  ? 27.399  -43.160 17.984  1.00 16.76 ? 43   HIS A CA  1 
ATOM   309   C  C   . HIS A  1 43  ? 28.006  -41.770 17.960  1.00 17.62 ? 43   HIS A C   1 
ATOM   310   O  O   . HIS A  1 43  ? 27.778  -41.016 17.017  1.00 16.52 ? 43   HIS A O   1 
ATOM   311   C  CB  . HIS A  1 43  ? 28.105  -44.042 16.948  1.00 15.68 ? 43   HIS A CB  1 
ATOM   312   C  CG  . HIS A  1 43  ? 27.764  -45.498 17.056  1.00 16.13 ? 43   HIS A CG  1 
ATOM   313   N  ND1 . HIS A  1 43  ? 28.495  -46.375 17.827  1.00 17.08 ? 43   HIS A ND1 1 
ATOM   314   C  CD2 . HIS A  1 43  ? 26.775  -46.229 16.489  1.00 13.99 ? 43   HIS A CD2 1 
ATOM   315   C  CE1 . HIS A  1 43  ? 27.968  -47.585 17.731  1.00 17.55 ? 43   HIS A CE1 1 
ATOM   316   N  NE2 . HIS A  1 43  ? 26.927  -47.523 16.924  1.00 14.13 ? 43   HIS A NE2 1 
ATOM   317   N  N   . GLY A  1 44  ? 28.780  -41.435 18.993  1.00 17.98 ? 44   GLY A N   1 
ATOM   318   C  CA  . GLY A  1 44  ? 29.474  -40.159 19.048  1.00 17.24 ? 44   GLY A CA  1 
ATOM   319   C  C   . GLY A  1 44  ? 30.290  -39.918 17.795  1.00 18.54 ? 44   GLY A C   1 
ATOM   320   O  O   . GLY A  1 44  ? 30.919  -40.843 17.279  1.00 18.21 ? 44   GLY A O   1 
ATOM   321   N  N   . PHE A  1 45  ? 30.285  -38.680 17.303  1.00 18.38 ? 45   PHE A N   1 
ATOM   322   C  CA  . PHE A  1 45  ? 30.974  -38.340 16.062  1.00 14.51 ? 45   PHE A CA  1 
ATOM   323   C  C   . PHE A  1 45  ? 31.609  -36.957 16.189  1.00 17.84 ? 45   PHE A C   1 
ATOM   324   O  O   . PHE A  1 45  ? 30.923  -35.939 16.079  1.00 18.43 ? 45   PHE A O   1 
ATOM   325   C  CB  . PHE A  1 45  ? 29.973  -38.366 14.925  1.00 15.72 ? 45   PHE A CB  1 
ATOM   326   C  CG  . PHE A  1 45  ? 30.584  -38.290 13.556  1.00 16.53 ? 45   PHE A CG  1 
ATOM   327   C  CD1 . PHE A  1 45  ? 31.446  -39.274 13.114  1.00 16.90 ? 45   PHE A CD1 1 
ATOM   328   C  CD2 . PHE A  1 45  ? 30.259  -37.247 12.700  1.00 17.07 ? 45   PHE A CD2 1 
ATOM   329   C  CE1 . PHE A  1 45  ? 31.994  -39.221 11.845  1.00 17.78 ? 45   PHE A CE1 1 
ATOM   330   C  CE2 . PHE A  1 45  ? 30.800  -37.182 11.430  1.00 20.55 ? 45   PHE A CE2 1 
ATOM   331   C  CZ  . PHE A  1 45  ? 31.671  -38.177 10.999  1.00 17.94 ? 45   PHE A CZ  1 
ATOM   332   N  N   . HIS A  1 46  ? 32.919  -36.921 16.437  1.00 17.49 ? 46   HIS A N   1 
ATOM   333   C  CA  . HIS A  1 46  ? 33.588  -35.673 16.797  1.00 17.53 ? 46   HIS A CA  1 
ATOM   334   C  C   . HIS A  1 46  ? 34.929  -35.489 16.124  1.00 17.73 ? 46   HIS A C   1 
ATOM   335   O  O   . HIS A  1 46  ? 35.628  -36.463 15.812  1.00 15.89 ? 46   HIS A O   1 
ATOM   336   C  CB  . HIS A  1 46  ? 33.827  -35.611 18.306  1.00 19.71 ? 46   HIS A CB  1 
ATOM   337   C  CG  . HIS A  1 46  ? 32.659  -36.051 19.117  1.00 16.37 ? 46   HIS A CG  1 
ATOM   338   N  ND1 . HIS A  1 46  ? 32.605  -37.287 19.718  1.00 16.97 ? 46   HIS A ND1 1 
ATOM   339   C  CD2 . HIS A  1 46  ? 31.500  -35.426 19.421  1.00 16.62 ? 46   HIS A CD2 1 
ATOM   340   C  CE1 . HIS A  1 46  ? 31.455  -37.407 20.357  1.00 19.02 ? 46   HIS A CE1 1 
ATOM   341   N  NE2 . HIS A  1 46  ? 30.767  -36.291 20.193  1.00 17.16 ? 46   HIS A NE2 1 
ATOM   342   N  N   . VAL A  1 47  ? 35.277  -34.223 15.912  1.00 16.24 ? 47   VAL A N   1 
ATOM   343   C  CA  . VAL A  1 47  ? 36.605  -33.858 15.467  1.00 17.93 ? 47   VAL A CA  1 
ATOM   344   C  C   . VAL A  1 47  ? 37.494  -33.754 16.702  1.00 19.20 ? 47   VAL A C   1 
ATOM   345   O  O   . VAL A  1 47  ? 37.175  -33.048 17.660  1.00 18.49 ? 47   VAL A O   1 
ATOM   346   C  CB  . VAL A  1 47  ? 36.595  -32.533 14.685  1.00 17.33 ? 47   VAL A CB  1 
ATOM   347   C  CG1 . VAL A  1 47  ? 38.002  -32.168 14.214  1.00 16.60 ? 47   VAL A CG1 1 
ATOM   348   C  CG2 . VAL A  1 47  ? 35.662  -32.642 13.499  1.00 16.73 ? 47   VAL A CG2 1 
ATOM   349   N  N   . HIS A  1 48  ? 38.592  -34.501 16.691  1.00 18.81 ? 48   HIS A N   1 
ATOM   350   C  CA  . HIS A  1 48  ? 39.561  -34.452 17.765  1.00 17.21 ? 48   HIS A CA  1 
ATOM   351   C  C   . HIS A  1 48  ? 40.702  -33.559 17.322  1.00 17.59 ? 48   HIS A C   1 
ATOM   352   O  O   . HIS A  1 48  ? 40.821  -33.255 16.147  1.00 18.49 ? 48   HIS A O   1 
ATOM   353   C  CB  . HIS A  1 48  ? 40.020  -35.859 18.129  1.00 18.12 ? 48   HIS A CB  1 
ATOM   354   C  CG  . HIS A  1 48  ? 38.979  -36.640 18.865  1.00 19.01 ? 48   HIS A CG  1 
ATOM   355   N  ND1 . HIS A  1 48  ? 39.191  -37.171 20.118  1.00 20.26 ? 48   HIS A ND1 1 
ATOM   356   C  CD2 . HIS A  1 48  ? 37.699  -36.942 18.544  1.00 18.72 ? 48   HIS A CD2 1 
ATOM   357   C  CE1 . HIS A  1 48  ? 38.093  -37.778 20.528  1.00 18.91 ? 48   HIS A CE1 1 
ATOM   358   N  NE2 . HIS A  1 48  ? 37.172  -37.654 19.593  1.00 16.55 ? 48   HIS A NE2 1 
ATOM   359   N  N   . GLU A  1 49  ? 41.533  -33.134 18.261  1.00 18.80 ? 49   GLU A N   1 
ATOM   360   C  CA  . GLU A  1 49  ? 42.377  -31.966 18.037  1.00 18.57 ? 49   GLU A CA  1 
ATOM   361   C  C   . GLU A  1 49  ? 43.569  -32.193 17.115  1.00 19.77 ? 49   GLU A C   1 
ATOM   362   O  O   . GLU A  1 49  ? 43.914  -31.314 16.333  1.00 17.87 ? 49   GLU A O   1 
ATOM   363   C  CB  . GLU A  1 49  ? 42.855  -31.382 19.369  1.00 20.84 ? 49   GLU A CB  1 
ATOM   364   C  CG  . GLU A  1 49  ? 43.508  -30.015 19.220  1.00 24.02 ? 49   GLU A CG  1 
ATOM   365   C  CD  . GLU A  1 49  ? 44.189  -29.546 20.488  1.00 25.80 ? 49   GLU A CD  1 
ATOM   366   O  OE1 . GLU A  1 49  ? 43.927  -30.129 21.561  1.00 29.00 ? 49   GLU A OE1 1 
ATOM   367   O  OE2 . GLU A  1 49  ? 44.994  -28.594 20.407  1.00 29.68 ? 49   GLU A OE2 1 
ATOM   368   N  N   . PHE A  1 50  ? 44.192  -33.367 17.211  1.00 20.09 ? 50   PHE A N   1 
ATOM   369   C  CA  . PHE A  1 50  ? 45.435  -33.639 16.489  1.00 19.68 ? 50   PHE A CA  1 
ATOM   370   C  C   . PHE A  1 50  ? 45.310  -34.678 15.372  1.00 18.14 ? 50   PHE A C   1 
ATOM   371   O  O   . PHE A  1 50  ? 44.658  -35.705 15.538  1.00 20.13 ? 50   PHE A O   1 
ATOM   372   C  CB  . PHE A  1 50  ? 46.515  -34.093 17.472  1.00 21.14 ? 50   PHE A CB  1 
ATOM   373   C  CG  . PHE A  1 50  ? 46.713  -33.152 18.619  1.00 21.54 ? 50   PHE A CG  1 
ATOM   374   C  CD1 . PHE A  1 50  ? 47.107  -31.842 18.393  1.00 21.26 ? 50   PHE A CD1 1 
ATOM   375   C  CD2 . PHE A  1 50  ? 46.488  -33.571 19.920  1.00 23.27 ? 50   PHE A CD2 1 
ATOM   376   C  CE1 . PHE A  1 50  ? 47.277  -30.972 19.443  1.00 24.73 ? 50   PHE A CE1 1 
ATOM   377   C  CE2 . PHE A  1 50  ? 46.655  -32.702 20.985  1.00 26.19 ? 50   PHE A CE2 1 
ATOM   378   C  CZ  . PHE A  1 50  ? 47.050  -31.401 20.745  1.00 26.04 ? 50   PHE A CZ  1 
ATOM   379   N  N   . GLY A  1 51  ? 45.962  -34.412 14.247  1.00 17.30 ? 51   GLY A N   1 
ATOM   380   C  CA  . GLY A  1 51  ? 46.114  -35.395 13.190  1.00 18.76 ? 51   GLY A CA  1 
ATOM   381   C  C   . GLY A  1 51  ? 47.334  -36.270 13.422  1.00 18.08 ? 51   GLY A C   1 
ATOM   382   O  O   . GLY A  1 51  ? 48.204  -36.419 12.561  1.00 17.38 ? 51   GLY A O   1 
ATOM   383   N  N   . ASP A  1 52  ? 47.369  -36.851 14.611  1.00 18.90 ? 52   ASP A N   1 
ATOM   384   C  CA  . ASP A  1 52  ? 48.456  -37.686 15.084  1.00 17.98 ? 52   ASP A CA  1 
ATOM   385   C  C   . ASP A  1 52  ? 47.920  -39.108 15.303  1.00 19.86 ? 52   ASP A C   1 
ATOM   386   O  O   . ASP A  1 52  ? 47.178  -39.351 16.255  1.00 24.20 ? 52   ASP A O   1 
ATOM   387   C  CB  . ASP A  1 52  ? 48.981  -37.091 16.398  1.00 19.10 ? 52   ASP A CB  1 
ATOM   388   C  CG  . ASP A  1 52  ? 50.219  -37.775 16.905  1.00 17.27 ? 52   ASP A CG  1 
ATOM   389   O  OD1 . ASP A  1 52  ? 50.359  -38.989 16.716  1.00 17.59 ? 52   ASP A OD1 1 
ATOM   390   O  OD2 . ASP A  1 52  ? 51.062  -37.090 17.504  1.00 22.10 ? 52   ASP A OD2 1 
ATOM   391   N  N   . ASN A  1 53  ? 48.279  -40.030 14.411  1.00 19.29 ? 53   ASN A N   1 
ATOM   392   C  CA  . ASN A  1 53  ? 47.837  -41.421 14.469  1.00 19.31 ? 53   ASN A CA  1 
ATOM   393   C  C   . ASN A  1 53  ? 48.944  -42.379 14.923  1.00 21.95 ? 53   ASN A C   1 
ATOM   394   O  O   . ASN A  1 53  ? 48.865  -43.585 14.671  1.00 23.71 ? 53   ASN A O   1 
ATOM   395   C  CB  . ASN A  1 53  ? 47.308  -41.853 13.085  1.00 22.64 ? 53   ASN A CB  1 
ATOM   396   C  CG  . ASN A  1 53  ? 46.663  -43.240 13.094  1.00 26.41 ? 53   ASN A CG  1 
ATOM   397   O  OD1 . ASN A  1 53  ? 47.041  -44.120 12.319  1.00 29.84 ? 53   ASN A OD1 1 
ATOM   398   N  ND2 . ASN A  1 53  ? 45.683  -43.433 13.961  1.00 25.80 ? 53   ASN A ND2 1 
ATOM   399   N  N   . THR A  1 54  ? 49.963  -41.844 15.603  1.00 21.76 ? 54   THR A N   1 
ATOM   400   C  CA  . THR A  1 54  ? 51.174  -42.604 15.944  1.00 22.15 ? 54   THR A CA  1 
ATOM   401   C  C   . THR A  1 54  ? 50.956  -43.687 16.995  1.00 24.46 ? 54   THR A C   1 
ATOM   402   O  O   . THR A  1 54  ? 51.692  -44.669 17.048  1.00 26.97 ? 54   THR A O   1 
ATOM   403   C  CB  . THR A  1 54  ? 52.297  -41.682 16.412  1.00 22.24 ? 54   THR A CB  1 
ATOM   404   O  OG1 . THR A  1 54  ? 51.801  -40.825 17.440  1.00 19.81 ? 54   THR A OG1 1 
ATOM   405   C  CG2 . THR A  1 54  ? 52.809  -40.826 15.243  1.00 22.01 ? 54   THR A CG2 1 
ATOM   406   N  N   . ALA A  1 55  ? 49.941  -43.498 17.826  1.00 23.55 ? 55   ALA A N   1 
ATOM   407   C  CA  . ALA A  1 55  ? 49.521  -44.513 18.777  1.00 23.72 ? 55   ALA A CA  1 
ATOM   408   C  C   . ALA A  1 55  ? 48.047  -44.863 18.573  1.00 27.24 ? 55   ALA A C   1 
ATOM   409   O  O   . ALA A  1 55  ? 47.343  -45.128 19.548  1.00 31.38 ? 55   ALA A O   1 
ATOM   410   C  CB  . ALA A  1 55  ? 49.733  -44.021 20.210  1.00 24.35 ? 55   ALA A CB  1 
ATOM   411   N  N   . GLY A  1 56  ? 47.575  -44.867 17.327  1.00 23.52 ? 56   GLY A N   1 
ATOM   412   C  CA  . GLY A  1 56  ? 46.175  -45.142 17.069  1.00 25.08 ? 56   GLY A CA  1 
ATOM   413   C  C   . GLY A  1 56  ? 45.325  -43.911 17.330  1.00 25.64 ? 56   GLY A C   1 
ATOM   414   O  O   . GLY A  1 56  ? 45.844  -42.801 17.292  1.00 25.11 ? 56   GLY A O   1 
ATOM   415   N  N   . CYS A  1 57  ? 44.036  -44.104 17.613  1.00 23.57 ? 57   CYS A N   1 
ATOM   416   C  CA  . CYS A  1 57  ? 43.088  -42.991 17.762  1.00 23.75 ? 57   CYS A CA  1 
ATOM   417   C  C   . CYS A  1 57  ? 43.331  -42.162 19.016  1.00 26.42 ? 57   CYS A C   1 
ATOM   418   O  O   . CYS A  1 57  ? 42.844  -41.030 19.127  1.00 25.27 ? 57   CYS A O   1 
ATOM   419   C  CB  . CYS A  1 57  ? 41.645  -43.502 17.797  1.00 26.20 ? 57   CYS A CB  1 
ATOM   420   S  SG  . CYS A  1 57  ? 41.140  -44.497 16.377  1.00 31.23 ? 57   CYS A SG  1 
ATOM   421   N  N   . THR A  1 58  ? 44.063  -42.755 19.957  1.00 25.39 ? 58   THR A N   1 
ATOM   422   C  CA  . THR A  1 58  ? 44.434  -42.138 21.225  1.00 26.29 ? 58   THR A CA  1 
ATOM   423   C  C   . THR A  1 58  ? 45.232  -40.846 21.067  1.00 24.49 ? 58   THR A C   1 
ATOM   424   O  O   . THR A  1 58  ? 44.990  -39.854 21.763  1.00 22.43 ? 58   THR A O   1 
ATOM   425   C  CB  . THR A  1 58  ? 45.288  -43.132 22.026  1.00 28.48 ? 58   THR A CB  1 
ATOM   426   O  OG1 . THR A  1 58  ? 44.564  -44.357 22.168  1.00 34.44 ? 58   THR A OG1 1 
ATOM   427   C  CG2 . THR A  1 58  ? 45.638  -42.587 23.401  1.00 28.40 ? 58   THR A CG2 1 
ATOM   428   N  N   . SER A  1 59  ? 46.202  -40.877 20.158  1.00 24.99 ? 59   SER A N   1 
ATOM   429   C  CA  . SER A  1 59  ? 47.106  -39.749 19.961  1.00 24.12 ? 59   SER A CA  1 
ATOM   430   C  C   . SER A  1 59  ? 46.416  -38.564 19.295  1.00 22.87 ? 59   SER A C   1 
ATOM   431   O  O   . SER A  1 59  ? 47.028  -37.515 19.104  1.00 20.92 ? 59   SER A O   1 
ATOM   432   C  CB  . SER A  1 59  ? 48.346  -40.187 19.181  1.00 24.80 ? 59   SER A CB  1 
ATOM   433   O  OG  . SER A  1 59  ? 48.041  -41.286 18.336  1.00 25.01 ? 59   SER A OG  1 
ATOM   434   N  N   . ALA A  1 60  ? 45.130  -38.731 18.986  1.00 24.57 ? 60   ALA A N   1 
ATOM   435   C  CA  . ALA A  1 60  ? 44.311  -37.658 18.426  1.00 22.38 ? 60   ALA A CA  1 
ATOM   436   C  C   . ALA A  1 60  ? 43.955  -36.588 19.465  1.00 21.76 ? 60   ALA A C   1 
ATOM   437   O  O   . ALA A  1 60  ? 43.484  -35.517 19.111  1.00 23.08 ? 60   ALA A O   1 
ATOM   438   C  CB  . ALA A  1 60  ? 43.046  -38.225 17.791  1.00 18.22 ? 60   ALA A CB  1 
ATOM   439   N  N   . GLY A  1 61  ? 44.190  -36.877 20.740  1.00 22.96 ? 61   GLY A N   1 
ATOM   440   C  CA  . GLY A  1 61  ? 43.859  -35.951 21.811  1.00 22.85 ? 61   GLY A CA  1 
ATOM   441   C  C   . GLY A  1 61  ? 42.367  -35.823 22.070  1.00 22.57 ? 61   GLY A C   1 
ATOM   442   O  O   . GLY A  1 61  ? 41.601  -36.731 21.733  1.00 20.97 ? 61   GLY A O   1 
ATOM   443   N  N   . PRO A  1 62  ? 41.949  -34.689 22.670  1.00 25.25 ? 62   PRO A N   1 
ATOM   444   C  CA  . PRO A  1 62  ? 40.563  -34.404 23.073  1.00 24.13 ? 62   PRO A CA  1 
ATOM   445   C  C   . PRO A  1 62  ? 39.788  -33.838 21.890  1.00 21.87 ? 62   PRO A C   1 
ATOM   446   O  O   . PRO A  1 62  ? 40.389  -33.673 20.828  1.00 22.20 ? 62   PRO A O   1 
ATOM   447   C  CB  . PRO A  1 62  ? 40.726  -33.318 24.151  1.00 25.13 ? 62   PRO A CB  1 
ATOM   448   C  CG  . PRO A  1 62  ? 42.201  -32.901 24.132  1.00 23.09 ? 62   PRO A CG  1 
ATOM   449   C  CD  . PRO A  1 62  ? 42.833  -33.539 22.929  1.00 23.96 ? 62   PRO A CD  1 
ATOM   450   N  N   . HIS A  1 63  ? 38.498  -33.542 22.045  1.00 21.21 ? 63   HIS A N   1 
ATOM   451   C  CA  . HIS A  1 63  ? 37.758  -32.935 20.935  1.00 21.28 ? 63   HIS A CA  1 
ATOM   452   C  C   . HIS A  1 63  ? 38.411  -31.590 20.603  1.00 20.43 ? 63   HIS A C   1 
ATOM   453   O  O   . HIS A  1 63  ? 38.953  -30.924 21.484  1.00 21.56 ? 63   HIS A O   1 
ATOM   454   C  CB  . HIS A  1 63  ? 36.252  -32.765 21.240  1.00 19.66 ? 63   HIS A CB  1 
ATOM   455   C  CG  . HIS A  1 63  ? 35.553  -34.039 21.626  1.00 19.96 ? 63   HIS A CG  1 
ATOM   456   N  ND1 . HIS A  1 63  ? 34.371  -34.053 22.334  1.00 19.37 ? 63   HIS A ND1 1 
ATOM   457   C  CD2 . HIS A  1 63  ? 35.881  -35.337 21.424  1.00 20.86 ? 63   HIS A CD2 1 
ATOM   458   C  CE1 . HIS A  1 63  ? 33.995  -35.302 22.543  1.00 20.47 ? 63   HIS A CE1 1 
ATOM   459   N  NE2 . HIS A  1 63  ? 34.893  -36.102 22.001  1.00 19.37 ? 63   HIS A NE2 1 
ATOM   460   N  N   . PHE A  1 64  ? 38.388  -31.206 19.333  1.00 18.62 ? 64   PHE A N   1 
ATOM   461   C  CA  . PHE A  1 64  ? 38.932  -29.919 18.918  1.00 18.19 ? 64   PHE A CA  1 
ATOM   462   C  C   . PHE A  1 64  ? 38.227  -28.792 19.698  1.00 19.99 ? 64   PHE A C   1 
ATOM   463   O  O   . PHE A  1 64  ? 37.022  -28.610 19.581  1.00 21.36 ? 64   PHE A O   1 
ATOM   464   C  CB  . PHE A  1 64  ? 38.798  -29.787 17.397  1.00 16.86 ? 64   PHE A CB  1 
ATOM   465   C  CG  . PHE A  1 64  ? 39.320  -28.498 16.835  1.00 17.01 ? 64   PHE A CG  1 
ATOM   466   C  CD1 . PHE A  1 64  ? 40.434  -27.885 17.368  1.00 19.15 ? 64   PHE A CD1 1 
ATOM   467   C  CD2 . PHE A  1 64  ? 38.707  -27.916 15.743  1.00 17.93 ? 64   PHE A CD2 1 
ATOM   468   C  CE1 . PHE A  1 64  ? 40.898  -26.704 16.836  1.00 20.47 ? 64   PHE A CE1 1 
ATOM   469   C  CE2 . PHE A  1 64  ? 39.172  -26.742 15.216  1.00 18.67 ? 64   PHE A CE2 1 
ATOM   470   C  CZ  . PHE A  1 64  ? 40.264  -26.135 15.760  1.00 18.35 ? 64   PHE A CZ  1 
ATOM   471   N  N   . ASN A  1 65  ? 38.973  -28.068 20.532  1.00 23.10 ? 65   ASN A N   1 
ATOM   472   C  CA  . ASN A  1 65  ? 38.369  -27.107 21.474  1.00 25.77 ? 65   ASN A CA  1 
ATOM   473   C  C   . ASN A  1 65  ? 39.108  -25.765 21.584  1.00 24.92 ? 65   ASN A C   1 
ATOM   474   O  O   . ASN A  1 65  ? 39.543  -25.373 22.677  1.00 25.37 ? 65   ASN A O   1 
ATOM   475   C  CB  . ASN A  1 65  ? 38.230  -27.733 22.874  1.00 22.95 ? 65   ASN A CB  1 
ATOM   476   C  CG  . ASN A  1 65  ? 37.334  -26.912 23.802  1.00 24.57 ? 65   ASN A CG  1 
ATOM   477   O  OD1 . ASN A  1 65  ? 36.528  -26.093 23.358  1.00 24.51 ? 65   ASN A OD1 1 
ATOM   478   N  ND2 . ASN A  1 65  ? 37.473  -27.136 25.094  1.00 24.59 ? 65   ASN A ND2 1 
ATOM   479   N  N   . PRO A  1 66  ? 39.220  -25.042 20.459  1.00 22.37 ? 66   PRO A N   1 
ATOM   480   C  CA  . PRO A  1 66  ? 39.956  -23.776 20.397  1.00 25.68 ? 66   PRO A CA  1 
ATOM   481   C  C   . PRO A  1 66  ? 39.403  -22.703 21.352  1.00 28.79 ? 66   PRO A C   1 
ATOM   482   O  O   . PRO A  1 66  ? 40.160  -21.867 21.832  1.00 30.98 ? 66   PRO A O   1 
ATOM   483   C  CB  . PRO A  1 66  ? 39.783  -23.336 18.937  1.00 21.54 ? 66   PRO A CB  1 
ATOM   484   C  CG  . PRO A  1 66  ? 38.613  -24.051 18.452  1.00 22.29 ? 66   PRO A CG  1 
ATOM   485   C  CD  . PRO A  1 66  ? 38.496  -25.324 19.212  1.00 20.51 ? 66   PRO A CD  1 
ATOM   486   N  N   . LEU A  1 67  ? 38.104  -22.739 21.631  1.00 31.55 ? 67   LEU A N   1 
ATOM   487   C  CA  . LEU A  1 67  ? 37.464  -21.738 22.485  1.00 29.22 ? 67   LEU A CA  1 
ATOM   488   C  C   . LEU A  1 67  ? 37.354  -22.131 23.969  1.00 29.14 ? 67   LEU A C   1 
ATOM   489   O  O   . LEU A  1 67  ? 36.660  -21.472 24.741  1.00 31.94 ? 67   LEU A O   1 
ATOM   490   C  CB  . LEU A  1 67  ? 36.085  -21.398 21.922  1.00 27.13 ? 67   LEU A CB  1 
ATOM   491   C  CG  . LEU A  1 67  ? 36.062  -20.299 20.858  1.00 30.33 ? 67   LEU A CG  1 
ATOM   492   C  CD1 . LEU A  1 67  ? 37.421  -20.136 20.185  1.00 30.00 ? 67   LEU A CD1 1 
ATOM   493   C  CD2 . LEU A  1 67  ? 34.966  -20.565 19.847  1.00 30.07 ? 67   LEU A CD2 1 
ATOM   494   N  N   . SER A  1 68  ? 38.038  -23.201 24.357  1.00 28.07 ? 68   SER A N   1 
ATOM   495   C  CA  . SER A  1 68  ? 38.007  -23.698 25.733  1.00 29.73 ? 68   SER A CA  1 
ATOM   496   C  C   . SER A  1 68  ? 36.615  -23.786 26.330  1.00 32.11 ? 68   SER A C   1 
ATOM   497   O  O   . SER A  1 68  ? 36.397  -23.332 27.452  1.00 34.26 ? 68   SER A O   1 
ATOM   498   C  CB  . SER A  1 68  ? 38.885  -22.842 26.646  1.00 30.11 ? 68   SER A CB  1 
ATOM   499   O  OG  . SER A  1 68  ? 40.247  -22.981 26.301  1.00 34.95 ? 68   SER A OG  1 
ATOM   500   N  N   . ARG A  1 69  ? 35.680  -24.379 25.595  1.00 31.91 ? 69   ARG A N   1 
ATOM   501   C  CA  . ARG A  1 69  ? 34.329  -24.575 26.119  1.00 32.91 ? 69   ARG A CA  1 
ATOM   502   C  C   . ARG A  1 69  ? 34.091  -26.004 26.616  1.00 30.29 ? 69   ARG A C   1 
ATOM   503   O  O   . ARG A  1 69  ? 34.977  -26.852 26.548  1.00 28.44 ? 69   ARG A O   1 
ATOM   504   C  CB  . ARG A  1 69  ? 33.281  -24.148 25.092  1.00 30.11 ? 69   ARG A CB  1 
ATOM   505   C  CG  . ARG A  1 69  ? 33.134  -22.633 24.999  1.00 32.51 ? 69   ARG A CG  1 
ATOM   506   C  CD  . ARG A  1 69  ? 32.552  -22.195 23.668  1.00 35.91 ? 69   ARG A CD  1 
ATOM   507   N  NE  . ARG A  1 69  ? 32.502  -20.737 23.560  1.00 40.71 ? 69   ARG A NE  1 
ATOM   508   C  CZ  . ARG A  1 69  ? 32.065  -20.068 22.493  1.00 39.18 ? 69   ARG A CZ  1 
ATOM   509   N  NH1 . ARG A  1 69  ? 31.636  -20.723 21.422  1.00 44.25 ? 69   ARG A NH1 1 
ATOM   510   N  NH2 . ARG A  1 69  ? 32.057  -18.738 22.493  1.00 36.33 ? 69   ARG A NH2 1 
ATOM   511   N  N   . LYS A  1 70  ? 32.901  -26.256 27.145  1.00 31.22 ? 70   LYS A N   1 
ATOM   512   C  CA  . LYS A  1 70  ? 32.560  -27.588 27.619  1.00 30.82 ? 70   LYS A CA  1 
ATOM   513   C  C   . LYS A  1 70  ? 31.824  -28.363 26.537  1.00 27.26 ? 70   LYS A C   1 
ATOM   514   O  O   . LYS A  1 70  ? 31.220  -27.769 25.645  1.00 25.86 ? 70   LYS A O   1 
ATOM   515   C  CB  . LYS A  1 70  ? 31.724  -27.511 28.900  1.00 33.63 ? 70   LYS A CB  1 
ATOM   516   C  CG  . LYS A  1 70  ? 32.558  -27.629 30.158  1.00 33.24 ? 70   LYS A CG  1 
ATOM   517   C  CD  . LYS A  1 70  ? 31.797  -27.156 31.371  1.00 40.54 ? 70   LYS A CD  1 
ATOM   518   C  CE  . LYS A  1 70  ? 32.714  -27.146 32.581  1.00 46.40 ? 70   LYS A CE  1 
ATOM   519   N  NZ  . LYS A  1 70  ? 34.004  -26.486 32.244  1.00 52.07 ? 70   LYS A NZ  1 
ATOM   520   N  N   . HIS A  1 71  ? 31.883  -29.687 26.615  1.00 26.40 ? 71   HIS A N   1 
ATOM   521   C  CA  . HIS A  1 71  ? 31.227  -30.533 25.627  1.00 24.94 ? 71   HIS A CA  1 
ATOM   522   C  C   . HIS A  1 71  ? 29.740  -30.229 25.534  1.00 23.96 ? 71   HIS A C   1 
ATOM   523   O  O   . HIS A  1 71  ? 29.066  -30.062 26.547  1.00 27.82 ? 71   HIS A O   1 
ATOM   524   C  CB  . HIS A  1 71  ? 31.440  -32.020 25.938  1.00 23.92 ? 71   HIS A CB  1 
ATOM   525   C  CG  . HIS A  1 71  ? 30.791  -32.938 24.946  1.00 25.18 ? 71   HIS A CG  1 
ATOM   526   N  ND1 . HIS A  1 71  ? 31.349  -33.225 23.717  1.00 24.60 ? 71   HIS A ND1 1 
ATOM   527   C  CD2 . HIS A  1 71  ? 29.625  -33.623 24.998  1.00 22.71 ? 71   HIS A CD2 1 
ATOM   528   C  CE1 . HIS A  1 71  ? 30.558  -34.052 23.057  1.00 22.95 ? 71   HIS A CE1 1 
ATOM   529   N  NE2 . HIS A  1 71  ? 29.504  -34.305 23.812  1.00 24.93 ? 71   HIS A NE2 1 
ATOM   530   N  N   . GLY A  1 72  ? 29.238  -30.151 24.309  1.00 25.40 ? 72   GLY A N   1 
ATOM   531   C  CA  . GLY A  1 72  ? 27.822  -29.946 24.071  1.00 25.15 ? 72   GLY A CA  1 
ATOM   532   C  C   . GLY A  1 72  ? 27.408  -30.699 22.825  1.00 26.02 ? 72   GLY A C   1 
ATOM   533   O  O   . GLY A  1 72  ? 28.212  -31.435 22.254  1.00 26.02 ? 72   GLY A O   1 
ATOM   534   N  N   . GLY A  1 73  ? 26.156  -30.540 22.412  1.00 26.30 ? 73   GLY A N   1 
ATOM   535   C  CA  . GLY A  1 73  ? 25.735  -31.029 21.117  1.00 25.78 ? 73   GLY A CA  1 
ATOM   536   C  C   . GLY A  1 73  ? 25.943  -29.921 20.100  1.00 27.36 ? 73   GLY A C   1 
ATOM   537   O  O   . GLY A  1 73  ? 26.210  -28.787 20.487  1.00 30.05 ? 73   GLY A O   1 
ATOM   538   N  N   . PRO A  1 74  ? 25.827  -30.243 18.801  1.00 24.60 ? 74   PRO A N   1 
ATOM   539   C  CA  . PRO A  1 74  ? 26.011  -29.312 17.677  1.00 25.36 ? 74   PRO A CA  1 
ATOM   540   C  C   . PRO A  1 74  ? 25.074  -28.108 17.742  1.00 27.98 ? 74   PRO A C   1 
ATOM   541   O  O   . PRO A  1 74  ? 25.398  -27.048 17.209  1.00 28.53 ? 74   PRO A O   1 
ATOM   542   C  CB  . PRO A  1 74  ? 25.635  -30.155 16.455  1.00 26.23 ? 74   PRO A CB  1 
ATOM   543   C  CG  . PRO A  1 74  ? 25.730  -31.557 16.888  1.00 24.47 ? 74   PRO A CG  1 
ATOM   544   C  CD  . PRO A  1 74  ? 25.506  -31.609 18.355  1.00 23.61 ? 74   PRO A CD  1 
ATOM   545   N  N   . LYS A  1 75  ? 23.913  -28.289 18.367  1.00 31.15 ? 75   LYS A N   1 
ATOM   546   C  CA  . LYS A  1 75  ? 22.888  -27.250 18.454  1.00 31.16 ? 75   LYS A CA  1 
ATOM   547   C  C   . LYS A  1 75  ? 23.142  -26.322 19.638  1.00 31.93 ? 75   LYS A C   1 
ATOM   548   O  O   . LYS A  1 75  ? 22.603  -25.215 19.691  1.00 32.48 ? 75   LYS A O   1 
ATOM   549   C  CB  . LYS A  1 75  ? 21.496  -27.886 18.595  1.00 35.96 ? 75   LYS A CB  1 
ATOM   550   C  CG  . LYS A  1 75  ? 20.579  -27.891 17.345  1.00 34.09 ? 75   LYS A CG  1 
ATOM   551   C  CD  . LYS A  1 75  ? 21.308  -28.204 16.037  1.00 35.59 ? 75   LYS A CD  1 
ATOM   552   C  CE  . LYS A  1 75  ? 21.675  -26.924 15.274  1.00 36.50 ? 75   LYS A CE  1 
ATOM   553   N  NZ  . LYS A  1 75  ? 22.158  -27.195 13.881  1.00 38.31 ? 75   LYS A NZ  1 
ATOM   554   N  N   . ASP A  1 76  ? 23.968  -26.781 20.580  1.00 34.81 ? 76   ASP A N   1 
ATOM   555   C  CA  . ASP A  1 76  ? 24.231  -26.056 21.828  1.00 35.27 ? 76   ASP A CA  1 
ATOM   556   C  C   . ASP A  1 76  ? 25.135  -24.845 21.612  1.00 35.25 ? 76   ASP A C   1 
ATOM   557   O  O   . ASP A  1 76  ? 25.905  -24.792 20.651  1.00 35.70 ? 76   ASP A O   1 
ATOM   558   C  CB  . ASP A  1 76  ? 24.827  -26.988 22.890  1.00 30.60 ? 76   ASP A CB  1 
ATOM   559   C  CG  . ASP A  1 76  ? 23.836  -28.041 23.378  1.00 34.61 ? 76   ASP A CG  1 
ATOM   560   O  OD1 . ASP A  1 76  ? 22.608  -27.799 23.325  1.00 39.39 ? 76   ASP A OD1 1 
ATOM   561   O  OD2 . ASP A  1 76  ? 24.288  -29.121 23.820  1.00 36.17 ? 76   ASP A OD2 1 
ATOM   562   N  N   . GLU A  1 77  ? 25.022  -23.861 22.498  1.00 37.74 ? 77   GLU A N   1 
ATOM   563   C  CA  . GLU A  1 77  ? 25.852  -22.666 22.409  1.00 41.23 ? 77   GLU A CA  1 
ATOM   564   C  C   . GLU A  1 77  ? 27.173  -22.971 23.093  1.00 34.56 ? 77   GLU A C   1 
ATOM   565   O  O   . GLU A  1 77  ? 28.248  -22.593 22.630  1.00 35.50 ? 77   GLU A O   1 
ATOM   566   C  CB  . GLU A  1 77  ? 25.153  -21.479 23.075  1.00 46.61 ? 77   GLU A CB  1 
ATOM   567   C  CG  . GLU A  1 77  ? 25.326  -20.145 22.340  1.00 49.10 ? 77   GLU A CG  1 
ATOM   568   C  CD  . GLU A  1 77  ? 26.643  -19.456 22.668  1.00 54.67 ? 77   GLU A CD  1 
ATOM   569   O  OE1 . GLU A  1 77  ? 26.723  -18.217 22.498  1.00 57.92 ? 77   GLU A OE1 1 
ATOM   570   O  OE2 . GLU A  1 77  ? 27.594  -20.148 23.100  1.00 48.62 ? 77   GLU A OE2 1 
ATOM   571   N  N   . GLU A  1 78  ? 27.071  -23.684 24.205  1.00 37.57 ? 78   GLU A N   1 
ATOM   572   C  CA  . GLU A  1 78  ? 28.240  -24.205 24.887  1.00 35.11 ? 78   GLU A CA  1 
ATOM   573   C  C   . GLU A  1 78  ? 28.606  -25.559 24.258  1.00 33.27 ? 78   GLU A C   1 
ATOM   574   O  O   . GLU A  1 78  ? 28.099  -26.611 24.664  1.00 30.66 ? 78   GLU A O   1 
ATOM   575   C  CB  . GLU A  1 78  ? 27.951  -24.336 26.387  1.00 35.35 ? 78   GLU A CB  1 
ATOM   576   C  CG  . GLU A  1 78  ? 29.129  -24.806 27.237  1.00 39.52 ? 78   GLU A CG  1 
ATOM   577   C  CD  . GLU A  1 78  ? 30.289  -23.801 27.289  1.00 42.17 ? 78   GLU A CD  1 
ATOM   578   O  OE1 . GLU A  1 78  ? 30.265  -22.786 26.543  1.00 42.24 ? 78   GLU A OE1 1 
ATOM   579   O  OE2 . GLU A  1 78  ? 31.231  -24.037 28.083  1.00 40.16 ? 78   GLU A OE2 1 
ATOM   580   N  N   . ARG A  1 79  ? 29.461  -25.518 23.239  1.00 30.22 ? 79   ARG A N   1 
ATOM   581   C  CA  . ARG A  1 79  ? 29.997  -26.732 22.633  1.00 27.44 ? 79   ARG A CA  1 
ATOM   582   C  C   . ARG A  1 79  ? 31.470  -26.563 22.269  1.00 26.47 ? 79   ARG A C   1 
ATOM   583   O  O   . ARG A  1 79  ? 31.958  -25.435 22.127  1.00 28.19 ? 79   ARG A O   1 
ATOM   584   C  CB  . ARG A  1 79  ? 29.205  -27.106 21.378  1.00 26.68 ? 79   ARG A CB  1 
ATOM   585   C  CG  . ARG A  1 79  ? 29.163  -26.021 20.324  1.00 25.09 ? 79   ARG A CG  1 
ATOM   586   C  CD  . ARG A  1 79  ? 28.640  -26.550 19.008  1.00 24.61 ? 79   ARG A CD  1 
ATOM   587   N  NE  . ARG A  1 79  ? 29.694  -27.089 18.149  1.00 25.61 ? 79   ARG A NE  1 
ATOM   588   C  CZ  . ARG A  1 79  ? 29.544  -27.315 16.845  1.00 23.23 ? 79   ARG A CZ  1 
ATOM   589   N  NH1 . ARG A  1 79  ? 28.389  -27.043 16.259  1.00 24.37 ? 79   ARG A NH1 1 
ATOM   590   N  NH2 . ARG A  1 79  ? 30.545  -27.799 16.119  1.00 22.24 ? 79   ARG A NH2 1 
ATOM   591   N  N   . HIS A  1 80  ? 32.171  -27.686 22.127  1.00 23.49 ? 80   HIS A N   1 
ATOM   592   C  CA  . HIS A  1 80  ? 33.469  -27.699 21.466  1.00 23.19 ? 80   HIS A CA  1 
ATOM   593   C  C   . HIS A  1 80  ? 33.227  -27.502 19.963  1.00 23.35 ? 80   HIS A C   1 
ATOM   594   O  O   . HIS A  1 80  ? 32.146  -27.817 19.459  1.00 22.93 ? 80   HIS A O   1 
ATOM   595   C  CB  . HIS A  1 80  ? 34.188  -29.029 21.691  1.00 20.21 ? 80   HIS A CB  1 
ATOM   596   C  CG  . HIS A  1 80  ? 34.405  -29.381 23.129  1.00 22.46 ? 80   HIS A CG  1 
ATOM   597   N  ND1 . HIS A  1 80  ? 34.119  -30.628 23.639  1.00 23.98 ? 80   HIS A ND1 1 
ATOM   598   C  CD2 . HIS A  1 80  ? 34.914  -28.665 24.161  1.00 25.83 ? 80   HIS A CD2 1 
ATOM   599   C  CE1 . HIS A  1 80  ? 34.434  -30.665 24.923  1.00 22.69 ? 80   HIS A CE1 1 
ATOM   600   N  NE2 . HIS A  1 80  ? 34.915  -29.484 25.266  1.00 23.70 ? 80   HIS A NE2 1 
ATOM   601   N  N   . VAL A  1 81  ? 34.222  -26.974 19.251  1.00 23.35 ? 81   VAL A N   1 
ATOM   602   C  CA  . VAL A  1 81  ? 34.141  -26.835 17.798  1.00 21.99 ? 81   VAL A CA  1 
ATOM   603   C  C   . VAL A  1 81  ? 33.971  -28.208 17.135  1.00 22.00 ? 81   VAL A C   1 
ATOM   604   O  O   . VAL A  1 81  ? 33.207  -28.352 16.189  1.00 25.18 ? 81   VAL A O   1 
ATOM   605   C  CB  . VAL A  1 81  ? 35.377  -26.084 17.236  1.00 20.21 ? 81   VAL A CB  1 
ATOM   606   C  CG1 . VAL A  1 81  ? 35.527  -26.287 15.745  1.00 21.72 ? 81   VAL A CG1 1 
ATOM   607   C  CG2 . VAL A  1 81  ? 35.280  -24.612 17.545  1.00 24.47 ? 81   VAL A CG2 1 
ATOM   608   N  N   . GLY A  1 82  ? 34.660  -29.222 17.649  1.00 21.02 ? 82   GLY A N   1 
ATOM   609   C  CA  . GLY A  1 82  ? 34.613  -30.553 17.070  1.00 17.97 ? 82   GLY A CA  1 
ATOM   610   C  C   . GLY A  1 82  ? 33.401  -31.368 17.460  1.00 20.73 ? 82   GLY A C   1 
ATOM   611   O  O   . GLY A  1 82  ? 33.322  -32.551 17.149  1.00 21.63 ? 82   GLY A O   1 
ATOM   612   N  N   . ASP A  1 83  ? 32.447  -30.731 18.133  1.00 23.55 ? 83   ASP A N   1 
ATOM   613   C  CA  . ASP A  1 83  ? 31.260  -31.408 18.650  1.00 20.11 ? 83   ASP A CA  1 
ATOM   614   C  C   . ASP A  1 83  ? 30.177  -31.581 17.593  1.00 22.80 ? 83   ASP A C   1 
ATOM   615   O  O   . ASP A  1 83  ? 29.291  -30.743 17.472  1.00 23.43 ? 83   ASP A O   1 
ATOM   616   C  CB  . ASP A  1 83  ? 30.690  -30.636 19.841  1.00 21.36 ? 83   ASP A CB  1 
ATOM   617   C  CG  . ASP A  1 83  ? 31.476  -30.881 21.114  1.00 22.47 ? 83   ASP A CG  1 
ATOM   618   O  OD1 . ASP A  1 83  ? 32.339  -31.766 21.081  1.00 18.67 ? 83   ASP A OD1 1 
ATOM   619   O  OD2 . ASP A  1 83  ? 31.240  -30.207 22.142  1.00 23.97 ? 83   ASP A OD2 1 
ATOM   620   N  N   . LEU A  1 84  ? 30.241  -32.681 16.845  1.00 19.99 ? 84   LEU A N   1 
ATOM   621   C  CA  . LEU A  1 84  ? 29.274  -32.931 15.780  1.00 22.14 ? 84   LEU A CA  1 
ATOM   622   C  C   . LEU A  1 84  ? 28.081  -33.844 16.167  1.00 21.81 ? 84   LEU A C   1 
ATOM   623   O  O   . LEU A  1 84  ? 27.287  -34.221 15.300  1.00 21.84 ? 84   LEU A O   1 
ATOM   624   C  CB  . LEU A  1 84  ? 29.993  -33.448 14.521  1.00 20.32 ? 84   LEU A CB  1 
ATOM   625   C  CG  . LEU A  1 84  ? 30.963  -32.454 13.861  1.00 21.71 ? 84   LEU A CG  1 
ATOM   626   C  CD1 . LEU A  1 84  ? 31.577  -33.011 12.576  1.00 20.18 ? 84   LEU A CD1 1 
ATOM   627   C  CD2 . LEU A  1 84  ? 30.260  -31.139 13.589  1.00 21.26 ? 84   LEU A CD2 1 
ATOM   628   N  N   . GLY A  1 85  ? 27.948  -34.178 17.454  1.00 19.19 ? 85   GLY A N   1 
ATOM   629   C  CA  . GLY A  1 85  ? 26.822  -34.965 17.940  1.00 17.42 ? 85   GLY A CA  1 
ATOM   630   C  C   . GLY A  1 85  ? 26.918  -36.464 17.704  1.00 15.84 ? 85   GLY A C   1 
ATOM   631   O  O   . GLY A  1 85  ? 27.951  -37.071 17.902  1.00 17.04 ? 85   GLY A O   1 
ATOM   632   N  N   . ASN A  1 86  ? 25.822  -37.062 17.267  1.00 19.42 ? 86   ASN A N   1 
ATOM   633   C  CA  . ASN A  1 86  ? 25.778  -38.485 16.933  1.00 18.23 ? 86   ASN A CA  1 
ATOM   634   C  C   . ASN A  1 86  ? 25.538  -38.783 15.450  1.00 19.15 ? 86   ASN A C   1 
ATOM   635   O  O   . ASN A  1 86  ? 24.984  -37.973 14.705  1.00 17.85 ? 86   ASN A O   1 
ATOM   636   C  CB  . ASN A  1 86  ? 24.655  -39.159 17.708  1.00 19.23 ? 86   ASN A CB  1 
ATOM   637   C  CG  . ASN A  1 86  ? 24.905  -39.192 19.185  1.00 20.11 ? 86   ASN A CG  1 
ATOM   638   O  OD1 . ASN A  1 86  ? 25.747  -39.949 19.671  1.00 20.13 ? 86   ASN A OD1 1 
ATOM   639   N  ND2 . ASN A  1 86  ? 24.156  -38.384 19.922  1.00 20.98 ? 86   ASN A ND2 1 
ATOM   640   N  N   . VAL A  1 87  ? 25.960  -39.968 15.035  1.00 17.80 ? 87   VAL A N   1 
ATOM   641   C  CA  . VAL A  1 87  ? 25.565  -40.493 13.749  1.00 16.56 ? 87   VAL A CA  1 
ATOM   642   C  C   . VAL A  1 87  ? 24.801  -41.778 14.025  1.00 16.31 ? 87   VAL A C   1 
ATOM   643   O  O   . VAL A  1 87  ? 24.936  -42.357 15.104  1.00 16.22 ? 87   VAL A O   1 
ATOM   644   C  CB  . VAL A  1 87  ? 26.767  -40.718 12.812  1.00 17.58 ? 87   VAL A CB  1 
ATOM   645   C  CG1 . VAL A  1 87  ? 27.506  -39.405 12.597  1.00 16.10 ? 87   VAL A CG1 1 
ATOM   646   C  CG2 . VAL A  1 87  ? 27.701  -41.791 13.357  1.00 15.33 ? 87   VAL A CG2 1 
ATOM   647   N  N   . THR A  1 88  ? 23.971  -42.197 13.072  1.00 16.36 ? 88   THR A N   1 
ATOM   648   C  CA  . THR A  1 88  ? 23.065  -43.320 13.285  1.00 17.33 ? 88   THR A CA  1 
ATOM   649   C  C   . THR A  1 88  ? 23.428  -44.520 12.418  1.00 16.66 ? 88   THR A C   1 
ATOM   650   O  O   . THR A  1 88  ? 23.457  -44.406 11.201  1.00 19.44 ? 88   THR A O   1 
ATOM   651   C  CB  . THR A  1 88  ? 21.584  -42.917 13.002  1.00 17.80 ? 88   THR A CB  1 
ATOM   652   O  OG1 . THR A  1 88  ? 21.254  -41.736 13.741  1.00 17.54 ? 88   THR A OG1 1 
ATOM   653   C  CG2 . THR A  1 88  ? 20.623  -44.024 13.404  1.00 18.94 ? 88   THR A CG2 1 
ATOM   654   N  N   . ALA A  1 89  ? 23.697  -45.661 13.047  1.00 15.83 ? 89   ALA A N   1 
ATOM   655   C  CA  . ALA A  1 89  ? 23.923  -46.893 12.315  1.00 16.09 ? 89   ALA A CA  1 
ATOM   656   C  C   . ALA A  1 89  ? 22.636  -47.701 12.222  1.00 18.39 ? 89   ALA A C   1 
ATOM   657   O  O   . ALA A  1 89  ? 21.953  -47.902 13.213  1.00 23.19 ? 89   ALA A O   1 
ATOM   658   C  CB  . ALA A  1 89  ? 25.026  -47.717 12.957  1.00 15.85 ? 89   ALA A CB  1 
ATOM   659   N  N   . GLY A  1 90  ? 22.307  -48.142 11.016  1.00 19.22 ? 90   GLY A N   1 
ATOM   660   C  CA  . GLY A  1 90  ? 21.137  -48.951 10.780  1.00 19.51 ? 90   GLY A CA  1 
ATOM   661   C  C   . GLY A  1 90  ? 21.411  -50.368 11.209  1.00 21.83 ? 90   GLY A C   1 
ATOM   662   O  O   . GLY A  1 90  ? 22.446  -50.646 11.809  1.00 21.99 ? 90   GLY A O   1 
ATOM   663   N  N   . LYS A  1 91  ? 20.485  -51.262 10.885  1.00 23.44 ? 91   LYS A N   1 
ATOM   664   C  CA  . LYS A  1 91  ? 20.531  -52.654 11.323  1.00 24.89 ? 91   LYS A CA  1 
ATOM   665   C  C   . LYS A  1 91  ? 21.694  -53.415 10.699  1.00 24.04 ? 91   LYS A C   1 
ATOM   666   O  O   . LYS A  1 91  ? 22.144  -54.427 11.227  1.00 24.36 ? 91   LYS A O   1 
ATOM   667   C  CB  . LYS A  1 91  ? 19.217  -53.336 10.931  1.00 26.78 ? 91   LYS A CB  1 
ATOM   668   C  CG  . LYS A  1 91  ? 18.753  -54.408 11.870  1.00 30.10 ? 91   LYS A CG  1 
ATOM   669   C  CD  . LYS A  1 91  ? 17.255  -54.289 12.071  1.00 36.40 ? 91   LYS A CD  1 
ATOM   670   C  CE  . LYS A  1 91  ? 16.900  -52.850 12.470  1.00 39.59 ? 91   LYS A CE  1 
ATOM   671   N  NZ  . LYS A  1 91  ? 15.459  -52.650 12.797  1.00 43.29 ? 91   LYS A NZ  1 
ATOM   672   N  N   . ASP A  1 92  ? 22.158  -52.932 9.553   1.00 24.53 ? 92   ASP A N   1 
ATOM   673   C  CA  . ASP A  1 92  ? 23.200  -53.604 8.795   1.00 22.68 ? 92   ASP A CA  1 
ATOM   674   C  C   . ASP A  1 92  ? 24.572  -53.119 9.237   1.00 23.31 ? 92   ASP A C   1 
ATOM   675   O  O   . ASP A  1 92  ? 25.597  -53.515 8.682   1.00 24.51 ? 92   ASP A O   1 
ATOM   676   C  CB  . ASP A  1 92  ? 22.986  -53.409 7.283   1.00 23.53 ? 92   ASP A CB  1 
ATOM   677   C  CG  . ASP A  1 92  ? 22.939  -51.930 6.855   1.00 24.59 ? 92   ASP A CG  1 
ATOM   678   O  OD1 . ASP A  1 92  ? 22.899  -51.016 7.712   1.00 21.98 ? 92   ASP A OD1 1 
ATOM   679   O  OD2 . ASP A  1 92  ? 22.944  -51.685 5.629   1.00 26.88 ? 92   ASP A OD2 1 
ATOM   680   N  N   . GLY A  1 93  ? 24.581  -52.272 10.261  1.00 22.20 ? 93   GLY A N   1 
ATOM   681   C  CA  . GLY A  1 93  ? 25.813  -51.715 10.780  1.00 20.20 ? 93   GLY A CA  1 
ATOM   682   C  C   . GLY A  1 93  ? 26.313  -50.530 9.977   1.00 17.18 ? 93   GLY A C   1 
ATOM   683   O  O   . GLY A  1 93  ? 27.402  -50.028 10.229  1.00 18.30 ? 93   GLY A O   1 
ATOM   684   N  N   . VAL A  1 94  ? 25.527  -50.071 9.010   1.00 19.97 ? 94   VAL A N   1 
ATOM   685   C  CA  . VAL A  1 94  ? 25.954  -48.944 8.176   1.00 19.83 ? 94   VAL A CA  1 
ATOM   686   C  C   . VAL A  1 94  ? 25.318  -47.625 8.597   1.00 18.11 ? 94   VAL A C   1 
ATOM   687   O  O   . VAL A  1 94  ? 24.099  -47.524 8.736   1.00 20.10 ? 94   VAL A O   1 
ATOM   688   C  CB  . VAL A  1 94  ? 25.700  -49.174 6.658   1.00 18.60 ? 94   VAL A CB  1 
ATOM   689   C  CG1 . VAL A  1 94  ? 26.218  -47.988 5.861   1.00 15.82 ? 94   VAL A CG1 1 
ATOM   690   C  CG2 . VAL A  1 94  ? 26.372  -50.445 6.178   1.00 17.44 ? 94   VAL A CG2 1 
ATOM   691   N  N   . ALA A  1 95  ? 26.165  -46.622 8.797   1.00 17.56 ? 95   ALA A N   1 
ATOM   692   C  CA  . ALA A  1 95  ? 25.725  -45.278 9.145   1.00 17.71 ? 95   ALA A CA  1 
ATOM   693   C  C   . ALA A  1 95  ? 25.869  -44.350 7.951   1.00 18.23 ? 95   ALA A C   1 
ATOM   694   O  O   . ALA A  1 95  ? 26.993  -44.071 7.531   1.00 19.84 ? 95   ALA A O   1 
ATOM   695   C  CB  . ALA A  1 95  ? 26.553  -44.744 10.321  1.00 15.08 ? 95   ALA A CB  1 
ATOM   696   N  N   . ASN A  1 96  ? 24.749  -43.888 7.396   1.00 18.59 ? 96   ASN A N   1 
ATOM   697   C  CA  . ASN A  1 96  ? 24.786  -42.832 6.388   1.00 18.44 ? 96   ASN A CA  1 
ATOM   698   C  C   . ASN A  1 96  ? 24.894  -41.538 7.126   1.00 18.79 ? 96   ASN A C   1 
ATOM   699   O  O   . ASN A  1 96  ? 24.010  -41.187 7.895   1.00 22.02 ? 96   ASN A O   1 
ATOM   700   C  CB  . ASN A  1 96  ? 23.517  -42.780 5.544   1.00 21.57 ? 96   ASN A CB  1 
ATOM   701   C  CG  . ASN A  1 96  ? 23.206  -44.087 4.894   1.00 25.89 ? 96   ASN A CG  1 
ATOM   702   O  OD1 . ASN A  1 96  ? 24.082  -44.730 4.304   1.00 27.99 ? 96   ASN A OD1 1 
ATOM   703   N  ND2 . ASN A  1 96  ? 21.948  -44.510 5.003   1.00 30.62 ? 96   ASN A ND2 1 
ATOM   704   N  N   . VAL A  1 97  ? 25.987  -40.834 6.915   1.00 17.13 ? 97   VAL A N   1 
ATOM   705   C  CA  . VAL A  1 97  ? 26.216  -39.606 7.642   1.00 17.03 ? 97   VAL A CA  1 
ATOM   706   C  C   . VAL A  1 97  ? 25.833  -38.486 6.716   1.00 18.22 ? 97   VAL A C   1 
ATOM   707   O  O   . VAL A  1 97  ? 26.170  -38.515 5.548   1.00 20.12 ? 97   VAL A O   1 
ATOM   708   C  CB  . VAL A  1 97  ? 27.686  -39.493 8.075   1.00 15.47 ? 97   VAL A CB  1 
ATOM   709   C  CG1 . VAL A  1 97  ? 27.979  -38.125 8.684   1.00 15.73 ? 97   VAL A CG1 1 
ATOM   710   C  CG2 . VAL A  1 97  ? 28.019  -40.620 9.049   1.00 15.34 ? 97   VAL A CG2 1 
ATOM   711   N  N   . SER A  1 98  ? 25.073  -37.528 7.215   1.00 19.18 ? 98   SER A N   1 
ATOM   712   C  CA  . SER A  1 98  ? 24.831  -36.308 6.463   1.00 19.69 ? 98   SER A CA  1 
ATOM   713   C  C   . SER A  1 98  ? 24.617  -35.209 7.477   1.00 20.69 ? 98   SER A C   1 
ATOM   714   O  O   . SER A  1 98  ? 23.558  -35.119 8.091   1.00 24.51 ? 98   SER A O   1 
ATOM   715   C  CB  . SER A  1 98  ? 23.618  -36.438 5.554   1.00 22.59 ? 98   SER A CB  1 
ATOM   716   O  OG  . SER A  1 98  ? 23.497  -35.279 4.749   1.00 28.14 ? 98   SER A OG  1 
ATOM   717   N  N   . ILE A  1 99  ? 25.648  -34.404 7.685   1.00 19.38 ? 99   ILE A N   1 
ATOM   718   C  CA  . ILE A  1 99  ? 25.595  -33.330 8.663   1.00 22.40 ? 99   ILE A CA  1 
ATOM   719   C  C   . ILE A  1 99  ? 25.885  -31.974 8.009   1.00 21.93 ? 99   ILE A C   1 
ATOM   720   O  O   . ILE A  1 99  ? 26.724  -31.870 7.120   1.00 23.11 ? 99   ILE A O   1 
ATOM   721   C  CB  . ILE A  1 99  ? 26.569  -33.597 9.843   1.00 19.27 ? 99   ILE A CB  1 
ATOM   722   C  CG1 . ILE A  1 99  ? 26.054  -34.761 10.699  1.00 18.94 ? 99   ILE A CG1 1 
ATOM   723   C  CG2 . ILE A  1 99  ? 26.722  -32.367 10.696  1.00 20.27 ? 99   ILE A CG2 1 
ATOM   724   C  CD1 . ILE A  1 99  ? 27.003  -35.193 11.807  1.00 19.11 ? 99   ILE A CD1 1 
ATOM   725   N  N   . GLU A  1 100 ? 25.156  -30.945 8.423   1.00 24.70 ? 100  GLU A N   1 
ATOM   726   C  CA  . GLU A  1 100 ? 25.497  -29.576 8.056   1.00 24.79 ? 100  GLU A CA  1 
ATOM   727   C  C   . GLU A  1 100 ? 25.867  -28.825 9.339   1.00 25.82 ? 100  GLU A C   1 
ATOM   728   O  O   . GLU A  1 100 ? 25.044  -28.719 10.255  1.00 25.01 ? 100  GLU A O   1 
ATOM   729   C  CB  . GLU A  1 100 ? 24.335  -28.887 7.331   1.00 23.55 ? 100  GLU A CB  1 
ATOM   730   C  CG  . GLU A  1 100 ? 24.639  -27.443 6.928   1.00 30.38 ? 100  GLU A CG  1 
ATOM   731   C  CD  . GLU A  1 100 ? 23.383  -26.593 6.755   1.00 37.79 ? 100  GLU A CD  1 
ATOM   732   O  OE1 . GLU A  1 100 ? 22.373  -27.133 6.252   1.00 45.18 ? 100  GLU A OE1 1 
ATOM   733   O  OE2 . GLU A  1 100 ? 23.398  -25.389 7.113   1.00 36.23 ? 100  GLU A OE2 1 
ATOM   734   N  N   . ASP A  1 101 ? 27.103  -28.327 9.420   1.00 23.24 ? 101  ASP A N   1 
ATOM   735   C  CA  . ASP A  1 101 ? 27.534  -27.571 10.589  1.00 22.86 ? 101  ASP A CA  1 
ATOM   736   C  C   . ASP A  1 101 ? 28.067  -26.182 10.213  1.00 26.30 ? 101  ASP A C   1 
ATOM   737   O  O   . ASP A  1 101 ? 28.612  -25.991 9.124   1.00 24.20 ? 101  ASP A O   1 
ATOM   738   C  CB  . ASP A  1 101 ? 28.584  -28.354 11.374  1.00 20.87 ? 101  ASP A CB  1 
ATOM   739   C  CG  . ASP A  1 101 ? 28.733  -27.864 12.803  1.00 25.06 ? 101  ASP A CG  1 
ATOM   740   O  OD1 . ASP A  1 101 ? 27.799  -28.068 13.630  1.00 25.94 ? 101  ASP A OD1 1 
ATOM   741   O  OD2 . ASP A  1 101 ? 29.798  -27.290 13.104  1.00 23.87 ? 101  ASP A OD2 1 
ATOM   742   N  N   . ARG A  1 102 ? 27.915  -25.221 11.123  1.00 27.63 ? 102  ARG A N   1 
ATOM   743   C  CA  . ARG A  1 102 ? 28.387  -23.852 10.893  1.00 29.05 ? 102  ARG A CA  1 
ATOM   744   C  C   . ARG A  1 102 ? 29.564  -23.435 11.797  1.00 27.92 ? 102  ARG A C   1 
ATOM   745   O  O   . ARG A  1 102 ? 30.121  -22.341 11.634  1.00 30.07 ? 102  ARG A O   1 
ATOM   746   C  CB  . ARG A  1 102 ? 27.225  -22.861 11.026  1.00 30.34 ? 102  ARG A CB  1 
ATOM   747   C  CG  . ARG A  1 102 ? 26.095  -23.122 10.036  1.00 33.36 ? 102  ARG A CG  1 
ATOM   748   C  CD  . ARG A  1 102 ? 25.210  -21.904 9.844   1.00 37.87 ? 102  ARG A CD  1 
ATOM   749   N  NE  . ARG A  1 102 ? 24.841  -21.740 8.438   1.00 43.52 ? 102  ARG A NE  1 
ATOM   750   C  CZ  . ARG A  1 102 ? 24.693  -20.561 7.836   1.00 43.49 ? 102  ARG A CZ  1 
ATOM   751   N  NH1 . ARG A  1 102 ? 24.873  -19.441 8.532   1.00 40.43 ? 102  ARG A NH1 1 
ATOM   752   N  NH2 . ARG A  1 102 ? 24.373  -20.499 6.542   1.00 41.95 ? 102  ARG A NH2 1 
ATOM   753   N  N   . VAL A  1 103 ? 29.944  -24.316 12.724  1.00 24.86 ? 103  VAL A N   1 
ATOM   754   C  CA  . VAL A  1 103 ? 31.001  -24.042 13.706  1.00 23.72 ? 103  VAL A CA  1 
ATOM   755   C  C   . VAL A  1 103 ? 32.382  -24.568 13.270  1.00 26.25 ? 103  VAL A C   1 
ATOM   756   O  O   . VAL A  1 103 ? 33.372  -23.824 13.279  1.00 24.15 ? 103  VAL A O   1 
ATOM   757   C  CB  . VAL A  1 103 ? 30.614  -24.586 15.100  1.00 24.15 ? 103  VAL A CB  1 
ATOM   758   C  CG1 . VAL A  1 103 ? 31.746  -24.427 16.075  1.00 24.75 ? 103  VAL A CG1 1 
ATOM   759   C  CG2 . VAL A  1 103 ? 29.375  -23.867 15.599  1.00 24.05 ? 103  VAL A CG2 1 
ATOM   760   N  N   . ILE A  1 104 ? 32.449  -25.842 12.886  1.00 24.13 ? 104  ILE A N   1 
ATOM   761   C  CA  . ILE A  1 104 ? 33.633  -26.342 12.198  1.00 23.32 ? 104  ILE A CA  1 
ATOM   762   C  C   . ILE A  1 104 ? 33.773  -25.584 10.877  1.00 21.57 ? 104  ILE A C   1 
ATOM   763   O  O   . ILE A  1 104 ? 32.788  -25.077 10.337  1.00 21.43 ? 104  ILE A O   1 
ATOM   764   C  CB  . ILE A  1 104 ? 33.572  -27.864 11.897  1.00 20.35 ? 104  ILE A CB  1 
ATOM   765   C  CG1 . ILE A  1 104 ? 32.454  -28.180 10.910  1.00 18.56 ? 104  ILE A CG1 1 
ATOM   766   C  CG2 . ILE A  1 104 ? 33.417  -28.676 13.164  1.00 19.45 ? 104  ILE A CG2 1 
ATOM   767   C  CD1 . ILE A  1 104 ? 32.587  -29.552 10.278  1.00 19.05 ? 104  ILE A CD1 1 
ATOM   768   N  N   . SER A  1 105 ? 34.999  -25.505 10.371  1.00 20.29 ? 105  SER A N   1 
ATOM   769   C  CA  . SER A  1 105 ? 35.281  -24.866 9.101   1.00 21.18 ? 105  SER A CA  1 
ATOM   770   C  C   . SER A  1 105 ? 36.362  -25.663 8.378   1.00 21.44 ? 105  SER A C   1 
ATOM   771   O  O   . SER A  1 105 ? 36.953  -26.564 8.949   1.00 20.47 ? 105  SER A O   1 
ATOM   772   C  CB  . SER A  1 105 ? 35.745  -23.424 9.326   1.00 23.24 ? 105  SER A CB  1 
ATOM   773   O  OG  . SER A  1 105 ? 35.742  -22.688 8.112   1.00 22.61 ? 105  SER A OG  1 
ATOM   774   N  N   . LEU A  1 106 ? 36.613  -25.337 7.115   1.00 26.18 ? 106  LEU A N   1 
ATOM   775   C  CA  . LEU A  1 106 ? 37.710  -25.957 6.361   1.00 24.55 ? 106  LEU A CA  1 
ATOM   776   C  C   . LEU A  1 106 ? 38.874  -24.974 6.194   1.00 25.03 ? 106  LEU A C   1 
ATOM   777   O  O   . LEU A  1 106 ? 39.854  -25.277 5.519   1.00 27.90 ? 106  LEU A O   1 
ATOM   778   C  CB  . LEU A  1 106 ? 37.238  -26.509 4.998   1.00 21.54 ? 106  LEU A CB  1 
ATOM   779   C  CG  . LEU A  1 106 ? 36.215  -27.661 4.995   1.00 20.15 ? 106  LEU A CG  1 
ATOM   780   C  CD1 . LEU A  1 106 ? 35.986  -28.223 3.610   1.00 20.52 ? 106  LEU A CD1 1 
ATOM   781   C  CD2 . LEU A  1 106 ? 36.633  -28.787 5.929   1.00 18.25 ? 106  LEU A CD2 1 
ATOM   782   N  N   . SER A  1 107 ? 38.748  -23.796 6.803   1.00 25.75 ? 107  SER A N   1 
ATOM   783   C  CA  . SER A  1 107 ? 39.832  -22.816 6.853   1.00 27.06 ? 107  SER A CA  1 
ATOM   784   C  C   . SER A  1 107 ? 39.755  -21.951 8.119   1.00 30.85 ? 107  SER A C   1 
ATOM   785   O  O   . SER A  1 107 ? 38.886  -22.156 8.960   1.00 30.74 ? 107  SER A O   1 
ATOM   786   C  CB  . SER A  1 107 ? 39.897  -21.967 5.575   1.00 29.15 ? 107  SER A CB  1 
ATOM   787   O  OG  . SER A  1 107 ? 38.666  -21.332 5.282   1.00 34.55 ? 107  SER A OG  1 
ATOM   788   N  N   . GLY A  1 108 ? 40.683  -21.012 8.274   1.00 31.45 ? 108  GLY A N   1 
ATOM   789   C  CA  . GLY A  1 108 ? 40.714  -20.166 9.452   1.00 30.77 ? 108  GLY A CA  1 
ATOM   790   C  C   . GLY A  1 108 ? 41.005  -20.923 10.737  1.00 34.51 ? 108  GLY A C   1 
ATOM   791   O  O   . GLY A  1 108 ? 41.398  -22.082 10.697  1.00 33.28 ? 108  GLY A O   1 
ATOM   792   N  N   . GLU A  1 109 ? 40.790  -20.277 11.883  1.00 33.70 ? 109  GLU A N   1 
ATOM   793   C  CA  . GLU A  1 109 ? 41.169  -20.852 13.178  1.00 36.92 ? 109  GLU A CA  1 
ATOM   794   C  C   . GLU A  1 109 ? 40.370  -22.102 13.574  1.00 34.22 ? 109  GLU A C   1 
ATOM   795   O  O   . GLU A  1 109 ? 40.869  -22.963 14.303  1.00 33.58 ? 109  GLU A O   1 
ATOM   796   C  CB  . GLU A  1 109 ? 41.069  -19.798 14.290  1.00 43.54 ? 109  GLU A CB  1 
ATOM   797   C  CG  . GLU A  1 109 ? 41.421  -18.378 13.855  1.00 47.06 ? 109  GLU A CG  1 
ATOM   798   C  CD  . GLU A  1 109 ? 40.280  -17.709 13.097  1.00 54.90 ? 109  GLU A CD  1 
ATOM   799   O  OE1 . GLU A  1 109 ? 39.151  -17.650 13.652  1.00 55.34 ? 109  GLU A OE1 1 
ATOM   800   O  OE2 . GLU A  1 109 ? 40.517  -17.242 11.954  1.00 51.75 ? 109  GLU A OE2 1 
ATOM   801   N  N   . HIS A  1 110 ? 39.130  -22.187 13.102  1.00 35.04 ? 110  HIS A N   1 
ATOM   802   C  CA  . HIS A  1 110 ? 38.255  -23.324 13.390  1.00 31.29 ? 110  HIS A CA  1 
ATOM   803   C  C   . HIS A  1 110 ? 38.373  -24.406 12.309  1.00 26.27 ? 110  HIS A C   1 
ATOM   804   O  O   . HIS A  1 110 ? 37.513  -25.282 12.209  1.00 24.73 ? 110  HIS A O   1 
ATOM   805   C  CB  . HIS A  1 110 ? 36.798  -22.850 13.513  1.00 30.25 ? 110  HIS A CB  1 
ATOM   806   C  CG  . HIS A  1 110 ? 36.527  -22.036 14.744  1.00 34.41 ? 110  HIS A CG  1 
ATOM   807   N  ND1 . HIS A  1 110 ? 35.252  -21.818 15.229  1.00 33.73 ? 110  HIS A ND1 1 
ATOM   808   C  CD2 . HIS A  1 110 ? 37.370  -21.409 15.602  1.00 32.34 ? 110  HIS A CD2 1 
ATOM   809   C  CE1 . HIS A  1 110 ? 35.322  -21.087 16.328  1.00 33.13 ? 110  HIS A CE1 1 
ATOM   810   N  NE2 . HIS A  1 110 ? 36.595  -20.826 16.576  1.00 35.89 ? 110  HIS A NE2 1 
ATOM   811   N  N   . SER A  1 111 ? 39.436  -24.322 11.507  1.00 25.32 ? 111  SER A N   1 
ATOM   812   C  CA  . SER A  1 111 ? 39.726  -25.283 10.448  1.00 24.22 ? 111  SER A CA  1 
ATOM   813   C  C   . SER A  1 111 ? 40.014  -26.678 10.979  1.00 21.08 ? 111  SER A C   1 
ATOM   814   O  O   . SER A  1 111 ? 40.835  -26.855 11.873  1.00 23.40 ? 111  SER A O   1 
ATOM   815   C  CB  . SER A  1 111 ? 40.944  -24.818 9.663   1.00 26.12 ? 111  SER A CB  1 
ATOM   816   O  OG  . SER A  1 111 ? 41.304  -25.781 8.700   1.00 25.89 ? 111  SER A OG  1 
ATOM   817   N  N   . ILE A  1 112 ? 39.356  -27.678 10.416  1.00 19.98 ? 112  ILE A N   1 
ATOM   818   C  CA  . ILE A  1 112 ? 39.552  -29.045 10.877  1.00 18.30 ? 112  ILE A CA  1 
ATOM   819   C  C   . ILE A  1 112 ? 40.505  -29.803 9.966   1.00 16.56 ? 112  ILE A C   1 
ATOM   820   O  O   . ILE A  1 112 ? 40.680  -31.005 10.097  1.00 16.97 ? 112  ILE A O   1 
ATOM   821   C  CB  . ILE A  1 112 ? 38.209  -29.796 11.015  1.00 19.25 ? 112  ILE A CB  1 
ATOM   822   C  CG1 . ILE A  1 112 ? 37.409  -29.740 9.711   1.00 17.19 ? 112  ILE A CG1 1 
ATOM   823   C  CG2 . ILE A  1 112 ? 37.370  -29.195 12.158  1.00 19.49 ? 112  ILE A CG2 1 
ATOM   824   C  CD1 . ILE A  1 112 ? 36.107  -30.504 9.779   1.00 15.52 ? 112  ILE A CD1 1 
ATOM   825   N  N   . ILE A  1 113 ? 41.120  -29.088 9.033   1.00 20.35 ? 113  ILE A N   1 
ATOM   826   C  CA  . ILE A  1 113 ? 42.118  -29.686 8.154   1.00 20.34 ? 113  ILE A CA  1 
ATOM   827   C  C   . ILE A  1 113 ? 43.368  -30.078 8.964   1.00 20.68 ? 113  ILE A C   1 
ATOM   828   O  O   . ILE A  1 113 ? 43.915  -29.286 9.746   1.00 20.04 ? 113  ILE A O   1 
ATOM   829   C  CB  . ILE A  1 113 ? 42.482  -28.759 6.969   1.00 20.16 ? 113  ILE A CB  1 
ATOM   830   C  CG1 . ILE A  1 113 ? 41.231  -28.403 6.163   1.00 21.27 ? 113  ILE A CG1 1 
ATOM   831   C  CG2 . ILE A  1 113 ? 43.528  -29.414 6.064   1.00 18.92 ? 113  ILE A CG2 1 
ATOM   832   C  CD1 . ILE A  1 113 ? 40.723  -29.503 5.299   1.00 19.10 ? 113  ILE A CD1 1 
ATOM   833   N  N   . GLY A  1 114 ? 43.791  -31.324 8.801   1.00 19.82 ? 114  GLY A N   1 
ATOM   834   C  CA  . GLY A  1 114 ? 44.921  -31.828 9.548   1.00 17.43 ? 114  GLY A CA  1 
ATOM   835   C  C   . GLY A  1 114 ? 44.547  -32.301 10.933  1.00 16.92 ? 114  GLY A C   1 
ATOM   836   O  O   . GLY A  1 114 ? 45.424  -32.573 11.745  1.00 17.62 ? 114  GLY A O   1 
ATOM   837   N  N   . ARG A  1 115 ? 43.255  -32.406 11.221  1.00 16.83 ? 115  ARG A N   1 
ATOM   838   C  CA  . ARG A  1 115 ? 42.843  -32.945 12.517  1.00 16.95 ? 115  ARG A CA  1 
ATOM   839   C  C   . ARG A  1 115 ? 42.190  -34.314 12.331  1.00 15.48 ? 115  ARG A C   1 
ATOM   840   O  O   . ARG A  1 115 ? 42.198  -34.849 11.221  1.00 16.88 ? 115  ARG A O   1 
ATOM   841   C  CB  . ARG A  1 115 ? 41.970  -31.938 13.284  1.00 18.03 ? 115  ARG A CB  1 
ATOM   842   C  CG  . ARG A  1 115 ? 42.720  -30.626 13.561  1.00 16.93 ? 115  ARG A CG  1 
ATOM   843   C  CD  . ARG A  1 115 ? 41.816  -29.541 14.086  1.00 18.12 ? 115  ARG A CD  1 
ATOM   844   N  NE  . ARG A  1 115 ? 42.494  -28.245 14.112  1.00 20.76 ? 115  ARG A NE  1 
ATOM   845   C  CZ  . ARG A  1 115 ? 43.489  -27.930 14.943  1.00 21.00 ? 115  ARG A CZ  1 
ATOM   846   N  NH1 . ARG A  1 115 ? 43.939  -28.816 15.817  1.00 17.58 ? 115  ARG A NH1 1 
ATOM   847   N  NH2 . ARG A  1 115 ? 44.033  -26.721 14.900  1.00 20.33 ? 115  ARG A NH2 1 
ATOM   848   N  N   . THR A  1 116 ? 41.640  -34.889 13.394  1.00 15.45 ? 116  THR A N   1 
ATOM   849   C  CA  . THR A  1 116 ? 41.149  -36.268 13.319  1.00 17.85 ? 116  THR A CA  1 
ATOM   850   C  C   . THR A  1 116 ? 39.628  -36.403 13.453  1.00 17.49 ? 116  THR A C   1 
ATOM   851   O  O   . THR A  1 116 ? 39.048  -35.874 14.392  1.00 19.15 ? 116  THR A O   1 
ATOM   852   C  CB  . THR A  1 116 ? 41.852  -37.154 14.375  1.00 17.37 ? 116  THR A CB  1 
ATOM   853   O  OG1 . THR A  1 116 ? 43.268  -37.161 14.123  1.00 16.25 ? 116  THR A OG1 1 
ATOM   854   C  CG2 . THR A  1 116 ? 41.323  -38.580 14.348  1.00 16.24 ? 116  THR A CG2 1 
ATOM   855   N  N   . MET A  1 117 ? 38.985  -37.091 12.505  1.00 17.56 ? 117  MET A N   1 
ATOM   856   C  CA  . MET A  1 117 ? 37.593  -37.528 12.679  1.00 17.61 ? 117  MET A CA  1 
ATOM   857   C  C   . MET A  1 117 ? 37.572  -38.806 13.494  1.00 16.77 ? 117  MET A C   1 
ATOM   858   O  O   . MET A  1 117 ? 38.171  -39.799 13.099  1.00 15.22 ? 117  MET A O   1 
ATOM   859   C  CB  . MET A  1 117 ? 36.922  -37.861 11.338  1.00 17.56 ? 117  MET A CB  1 
ATOM   860   C  CG  . MET A  1 117 ? 35.997  -36.824 10.783  1.00 17.62 ? 117  MET A CG  1 
ATOM   861   S  SD  . MET A  1 117 ? 34.668  -36.317 11.871  1.00 25.66 ? 117  MET A SD  1 
ATOM   862   C  CE  . MET A  1 117 ? 34.267  -34.763 11.108  1.00 22.20 ? 117  MET A CE  1 
ATOM   863   N  N   . VAL A  1 118 ? 36.855  -38.804 14.607  1.00 19.36 ? 118  VAL A N   1 
ATOM   864   C  CA  . VAL A  1 118 ? 36.659  -40.041 15.346  1.00 19.49 ? 118  VAL A CA  1 
ATOM   865   C  C   . VAL A  1 118 ? 35.165  -40.411 15.434  1.00 19.21 ? 118  VAL A C   1 
ATOM   866   O  O   . VAL A  1 118 ? 34.327  -39.562 15.741  1.00 15.38 ? 118  VAL A O   1 
ATOM   867   C  CB  . VAL A  1 118 ? 37.311  -39.984 16.752  1.00 18.21 ? 118  VAL A CB  1 
ATOM   868   C  CG1 . VAL A  1 118 ? 37.279  -41.360 17.399  1.00 17.94 ? 118  VAL A CG1 1 
ATOM   869   C  CG2 . VAL A  1 118 ? 38.747  -39.485 16.652  1.00 17.06 ? 118  VAL A CG2 1 
ATOM   870   N  N   . VAL A  1 119 ? 34.850  -41.670 15.116  1.00 17.58 ? 119  VAL A N   1 
ATOM   871   C  CA  . VAL A  1 119 ? 33.555  -42.260 15.454  1.00 17.15 ? 119  VAL A CA  1 
ATOM   872   C  C   . VAL A  1 119 ? 33.667  -43.076 16.771  1.00 17.18 ? 119  VAL A C   1 
ATOM   873   O  O   . VAL A  1 119 ? 34.570  -43.888 16.936  1.00 17.33 ? 119  VAL A O   1 
ATOM   874   C  CB  . VAL A  1 119 ? 32.951  -43.085 14.263  1.00 17.18 ? 119  VAL A CB  1 
ATOM   875   C  CG1 . VAL A  1 119 ? 33.776  -44.331 13.961  1.00 15.36 ? 119  VAL A CG1 1 
ATOM   876   C  CG2 . VAL A  1 119 ? 31.484  -43.450 14.533  1.00 15.52 ? 119  VAL A CG2 1 
ATOM   877   N  N   . HIS A  1 120 ? 32.748  -42.855 17.706  1.00 18.44 ? 120  HIS A N   1 
ATOM   878   C  CA  . HIS A  1 120 ? 32.835  -43.476 19.030  1.00 19.66 ? 120  HIS A CA  1 
ATOM   879   C  C   . HIS A  1 120 ? 31.912  -44.691 19.261  1.00 19.31 ? 120  HIS A C   1 
ATOM   880   O  O   . HIS A  1 120 ? 30.979  -44.960 18.485  1.00 17.57 ? 120  HIS A O   1 
ATOM   881   C  CB  . HIS A  1 120 ? 32.609  -42.421 20.131  1.00 19.98 ? 120  HIS A CB  1 
ATOM   882   C  CG  . HIS A  1 120 ? 33.715  -41.416 20.245  1.00 18.63 ? 120  HIS A CG  1 
ATOM   883   N  ND1 . HIS A  1 120 ? 34.786  -41.580 21.097  1.00 19.46 ? 120  HIS A ND1 1 
ATOM   884   C  CD2 . HIS A  1 120 ? 33.913  -40.230 19.620  1.00 19.09 ? 120  HIS A CD2 1 
ATOM   885   C  CE1 . HIS A  1 120 ? 35.597  -40.543 20.990  1.00 20.59 ? 120  HIS A CE1 1 
ATOM   886   N  NE2 . HIS A  1 120 ? 35.093  -39.710 20.098  1.00 18.50 ? 120  HIS A NE2 1 
ATOM   887   N  N   . GLU A  1 121 ? 32.184  -45.384 20.369  1.00 19.78 ? 121  GLU A N   1 
ATOM   888   C  CA  . GLU A  1 121 ? 31.536  -46.639 20.768  1.00 20.34 ? 121  GLU A CA  1 
ATOM   889   C  C   . GLU A  1 121 ? 30.070  -46.504 21.156  1.00 19.67 ? 121  GLU A C   1 
ATOM   890   O  O   . GLU A  1 121 ? 29.224  -47.289 20.721  1.00 20.94 ? 121  GLU A O   1 
ATOM   891   C  CB  . GLU A  1 121 ? 32.299  -47.232 21.960  1.00 21.38 ? 121  GLU A CB  1 
ATOM   892   C  CG  . GLU A  1 121 ? 31.454  -48.070 22.924  1.00 24.54 ? 121  GLU A CG  1 
ATOM   893   C  CD  . GLU A  1 121 ? 32.182  -48.390 24.227  1.00 27.16 ? 121  GLU A CD  1 
ATOM   894   O  OE1 . GLU A  1 121 ? 32.948  -47.532 24.721  1.00 26.91 ? 121  GLU A OE1 1 
ATOM   895   O  OE2 . GLU A  1 121 ? 31.991  -49.506 24.758  1.00 30.62 ? 121  GLU A OE2 1 
ATOM   896   N  N   . LYS A  1 122 ? 29.800  -45.508 21.994  1.00 20.48 ? 122  LYS A N   1 
ATOM   897   C  CA  . LYS A  1 122 ? 28.516  -45.308 22.646  1.00 19.59 ? 122  LYS A CA  1 
ATOM   898   C  C   . LYS A  1 122 ? 27.921  -44.012 22.156  1.00 20.51 ? 122  LYS A C   1 
ATOM   899   O  O   . LYS A  1 122 ? 28.537  -43.274 21.393  1.00 19.40 ? 122  LYS A O   1 
ATOM   900   C  CB  . LYS A  1 122 ? 28.689  -45.176 24.173  1.00 22.50 ? 122  LYS A CB  1 
ATOM   901   C  CG  . LYS A  1 122 ? 29.059  -46.448 24.925  1.00 24.74 ? 122  LYS A CG  1 
ATOM   902   C  CD  . LYS A  1 122 ? 29.667  -46.144 26.291  1.00 28.36 ? 122  LYS A CD  1 
ATOM   903   C  CE  . LYS A  1 122 ? 28.823  -45.161 27.118  1.00 36.76 ? 122  LYS A CE  1 
ATOM   904   N  NZ  . LYS A  1 122 ? 27.538  -45.724 27.662  1.00 41.42 ? 122  LYS A NZ  1 
ATOM   905   N  N   . GLN A  1 123 ? 26.723  -43.723 22.640  1.00 21.43 ? 123  GLN A N   1 
ATOM   906   C  CA  . GLN A  1 123 ? 26.007  -42.523 22.263  1.00 20.97 ? 123  GLN A CA  1 
ATOM   907   C  C   . GLN A  1 123 ? 26.588  -41.311 22.962  1.00 19.87 ? 123  GLN A C   1 
ATOM   908   O  O   . GLN A  1 123 ? 26.981  -41.379 24.124  1.00 22.13 ? 123  GLN A O   1 
ATOM   909   C  CB  . GLN A  1 123 ? 24.536  -42.677 22.645  1.00 21.94 ? 123  GLN A CB  1 
ATOM   910   C  CG  . GLN A  1 123 ? 23.675  -41.496 22.293  1.00 21.90 ? 123  GLN A CG  1 
ATOM   911   C  CD  . GLN A  1 123 ? 22.212  -41.823 22.405  1.00 24.00 ? 123  GLN A CD  1 
ATOM   912   O  OE1 . GLN A  1 123 ? 21.815  -42.988 22.301  1.00 23.64 ? 123  GLN A OE1 1 
ATOM   913   N  NE2 . GLN A  1 123 ? 21.393  -40.800 22.623  1.00 23.59 ? 123  GLN A NE2 1 
ATOM   914   N  N   . ASP A  1 124 ? 26.639  -40.200 22.246  1.00 19.60 ? 124  ASP A N   1 
ATOM   915   C  CA  . ASP A  1 124 ? 27.053  -38.926 22.817  1.00 20.22 ? 124  ASP A CA  1 
ATOM   916   C  C   . ASP A  1 124 ? 25.874  -38.335 23.619  1.00 23.59 ? 124  ASP A C   1 
ATOM   917   O  O   . ASP A  1 124 ? 24.779  -38.126 23.074  1.00 23.12 ? 124  ASP A O   1 
ATOM   918   C  CB  . ASP A  1 124 ? 27.479  -38.004 21.677  1.00 19.08 ? 124  ASP A CB  1 
ATOM   919   C  CG  . ASP A  1 124 ? 27.996  -36.671 22.153  1.00 22.64 ? 124  ASP A CG  1 
ATOM   920   O  OD1 . ASP A  1 124 ? 27.855  -36.353 23.348  1.00 21.54 ? 124  ASP A OD1 1 
ATOM   921   O  OD2 . ASP A  1 124 ? 28.553  -35.933 21.315  1.00 24.44 ? 124  ASP A OD2 1 
ATOM   922   N  N   . ASP A  1 125 ? 26.086  -38.083 24.914  1.00 25.07 ? 125  ASP A N   1 
ATOM   923   C  CA  . ASP A  1 125 ? 25.015  -37.569 25.775  1.00 25.85 ? 125  ASP A CA  1 
ATOM   924   C  C   . ASP A  1 125 ? 24.827  -36.050 25.657  1.00 25.65 ? 125  ASP A C   1 
ATOM   925   O  O   . ASP A  1 125 ? 23.958  -35.465 26.299  1.00 26.12 ? 125  ASP A O   1 
ATOM   926   C  CB  . ASP A  1 125 ? 25.159  -38.049 27.241  1.00 28.05 ? 125  ASP A CB  1 
ATOM   927   C  CG  . ASP A  1 125 ? 26.322  -37.388 28.002  1.00 27.76 ? 125  ASP A CG  1 
ATOM   928   O  OD1 . ASP A  1 125 ? 26.824  -36.319 27.589  1.00 26.50 ? 125  ASP A OD1 1 
ATOM   929   O  OD2 . ASP A  1 125 ? 26.719  -37.943 29.053  1.00 27.71 ? 125  ASP A OD2 1 
ATOM   930   N  N   . LEU A  1 126 ? 25.643  -35.443 24.803  1.00 24.81 ? 126  LEU A N   1 
ATOM   931   C  CA  . LEU A  1 126 ? 25.597  -34.015 24.483  1.00 23.63 ? 126  LEU A CA  1 
ATOM   932   C  C   . LEU A  1 126 ? 25.982  -33.085 25.635  1.00 23.05 ? 126  LEU A C   1 
ATOM   933   O  O   . LEU A  1 126 ? 25.614  -31.916 25.637  1.00 24.51 ? 126  LEU A O   1 
ATOM   934   C  CB  . LEU A  1 126 ? 24.255  -33.626 23.866  1.00 23.79 ? 126  LEU A CB  1 
ATOM   935   C  CG  . LEU A  1 126 ? 23.771  -34.447 22.662  1.00 24.57 ? 126  LEU A CG  1 
ATOM   936   C  CD1 . LEU A  1 126 ? 22.439  -33.902 22.171  1.00 23.21 ? 126  LEU A CD1 1 
ATOM   937   C  CD2 . LEU A  1 126 ? 24.788  -34.471 21.532  1.00 22.79 ? 126  LEU A CD2 1 
ATOM   938   N  N   . GLY A  1 127 ? 26.733  -33.612 26.599  1.00 24.30 ? 127  GLY A N   1 
ATOM   939   C  CA  . GLY A  1 127 ? 27.286  -32.812 27.682  1.00 27.77 ? 127  GLY A CA  1 
ATOM   940   C  C   . GLY A  1 127 ? 26.397  -32.722 28.913  1.00 30.53 ? 127  GLY A C   1 
ATOM   941   O  O   . GLY A  1 127 ? 26.659  -31.959 29.862  1.00 32.88 ? 127  GLY A O   1 
ATOM   942   N  N   . LYS A  1 128 ? 25.350  -33.533 28.906  1.00 28.18 ? 128  LYS A N   1 
ATOM   943   C  CA  . LYS A  1 128 ? 24.291  -33.449 29.893  1.00 28.35 ? 128  LYS A CA  1 
ATOM   944   C  C   . LYS A  1 128 ? 24.193  -34.722 30.737  1.00 29.38 ? 128  LYS A C   1 
ATOM   945   O  O   . LYS A  1 128 ? 23.136  -35.032 31.300  1.00 32.96 ? 128  LYS A O   1 
ATOM   946   C  CB  . LYS A  1 128 ? 22.975  -33.201 29.162  1.00 25.85 ? 128  LYS A CB  1 
ATOM   947   C  CG  . LYS A  1 128 ? 23.011  -31.960 28.315  1.00 25.89 ? 128  LYS A CG  1 
ATOM   948   C  CD  . LYS A  1 128 ? 21.811  -31.844 27.411  1.00 28.78 ? 128  LYS A CD  1 
ATOM   949   C  CE  . LYS A  1 128 ? 21.887  -30.552 26.620  1.00 31.33 ? 128  LYS A CE  1 
ATOM   950   N  NZ  . LYS A  1 128 ? 22.076  -29.392 27.546  1.00 34.61 ? 128  LYS A NZ  1 
ATOM   951   N  N   . GLY A  1 129 ? 25.290  -35.461 30.825  1.00 26.47 ? 129  GLY A N   1 
ATOM   952   C  CA  . GLY A  1 129 ? 25.282  -36.723 31.540  1.00 28.53 ? 129  GLY A CA  1 
ATOM   953   C  C   . GLY A  1 129 ? 25.402  -36.560 33.039  1.00 29.17 ? 129  GLY A C   1 
ATOM   954   O  O   . GLY A  1 129 ? 25.250  -37.528 33.786  1.00 29.36 ? 129  GLY A O   1 
ATOM   955   N  N   . GLY A  1 130 ? 25.692  -35.335 33.477  1.00 29.66 ? 130  GLY A N   1 
ATOM   956   C  CA  . GLY A  1 130 ? 25.797  -35.020 34.892  1.00 28.73 ? 130  GLY A CA  1 
ATOM   957   C  C   . GLY A  1 130 ? 27.072  -35.488 35.572  1.00 28.67 ? 130  GLY A C   1 
ATOM   958   O  O   . GLY A  1 130 ? 27.058  -35.813 36.756  1.00 28.13 ? 130  GLY A O   1 
ATOM   959   N  N   . ASN A  1 131 ? 28.171  -35.541 34.827  1.00 28.48 ? 131  ASN A N   1 
ATOM   960   C  CA  . ASN A  1 131 ? 29.476  -35.826 35.413  1.00 28.23 ? 131  ASN A CA  1 
ATOM   961   C  C   . ASN A  1 131 ? 30.590  -35.153 34.637  1.00 29.46 ? 131  ASN A C   1 
ATOM   962   O  O   . ASN A  1 131 ? 30.337  -34.380 33.714  1.00 29.88 ? 131  ASN A O   1 
ATOM   963   C  CB  . ASN A  1 131 ? 29.734  -37.339 35.585  1.00 28.23 ? 131  ASN A CB  1 
ATOM   964   C  CG  . ASN A  1 131 ? 29.604  -38.123 34.294  1.00 27.18 ? 131  ASN A CG  1 
ATOM   965   O  OD1 . ASN A  1 131 ? 29.700  -37.570 33.206  1.00 30.27 ? 131  ASN A OD1 1 
ATOM   966   N  ND2 . ASN A  1 131 ? 29.391  -39.427 34.413  1.00 25.16 ? 131  ASN A ND2 1 
ATOM   967   N  N   . GLU A  1 132 ? 31.826  -35.428 35.031  1.00 33.81 ? 132  GLU A N   1 
ATOM   968   C  CA  . GLU A  1 132 ? 32.979  -34.856 34.337  1.00 36.56 ? 132  GLU A CA  1 
ATOM   969   C  C   . GLU A  1 132 ? 33.193  -35.431 32.937  1.00 30.71 ? 132  GLU A C   1 
ATOM   970   O  O   . GLU A  1 132 ? 33.490  -34.676 32.016  1.00 29.44 ? 132  GLU A O   1 
ATOM   971   C  CB  . GLU A  1 132 ? 34.260  -34.952 35.172  1.00 35.26 ? 132  GLU A CB  1 
ATOM   972   C  CG  . GLU A  1 132 ? 34.682  -33.626 35.797  1.00 39.53 ? 132  GLU A CG  1 
ATOM   973   C  CD  . GLU A  1 132 ? 36.204  -33.444 35.805  1.00 54.30 ? 132  GLU A CD  1 
ATOM   974   O  OE1 . GLU A  1 132 ? 36.940  -34.460 35.797  1.00 54.78 ? 132  GLU A OE1 1 
ATOM   975   O  OE2 . GLU A  1 132 ? 36.670  -32.282 35.814  1.00 59.91 ? 132  GLU A OE2 1 
ATOM   976   N  N   . GLU A  1 133 ? 33.045  -36.749 32.778  1.00 28.33 ? 133  GLU A N   1 
ATOM   977   C  CA  . GLU A  1 133 ? 33.166  -37.368 31.462  1.00 30.18 ? 133  GLU A CA  1 
ATOM   978   C  C   . GLU A  1 133 ? 32.216  -36.703 30.476  1.00 30.49 ? 133  GLU A C   1 
ATOM   979   O  O   . GLU A  1 133 ? 32.603  -36.363 29.359  1.00 30.73 ? 133  GLU A O   1 
ATOM   980   C  CB  . GLU A  1 133 ? 32.910  -38.878 31.507  1.00 27.48 ? 133  GLU A CB  1 
ATOM   981   C  CG  . GLU A  1 133 ? 34.174  -39.720 31.494  1.00 32.73 ? 133  GLU A CG  1 
ATOM   982   C  CD  . GLU A  1 133 ? 35.184  -39.285 30.426  1.00 38.60 ? 133  GLU A CD  1 
ATOM   983   O  OE1 . GLU A  1 133 ? 36.345  -38.981 30.784  1.00 42.28 ? 133  GLU A OE1 1 
ATOM   984   O  OE2 . GLU A  1 133 ? 34.828  -39.241 29.228  1.00 36.99 ? 133  GLU A OE2 1 
ATOM   985   N  N   . SER A  1 134 ? 30.974  -36.506 30.901  1.00 29.59 ? 134  SER A N   1 
ATOM   986   C  CA  . SER A  1 134 ? 29.979  -35.848 30.070  1.00 27.63 ? 134  SER A CA  1 
ATOM   987   C  C   . SER A  1 134 ? 30.473  -34.519 29.477  1.00 28.52 ? 134  SER A C   1 
ATOM   988   O  O   . SER A  1 134 ? 30.309  -34.261 28.281  1.00 26.83 ? 134  SER A O   1 
ATOM   989   C  CB  . SER A  1 134 ? 28.699  -35.620 30.872  1.00 28.86 ? 134  SER A CB  1 
ATOM   990   O  OG  . SER A  1 134 ? 27.687  -35.069 30.049  1.00 29.98 ? 134  SER A OG  1 
ATOM   991   N  N   . THR A  1 135 ? 31.066  -33.678 30.319  1.00 28.38 ? 135  THR A N   1 
ATOM   992   C  CA  . THR A  1 135 ? 31.490  -32.338 29.918  1.00 28.92 ? 135  THR A CA  1 
ATOM   993   C  C   . THR A  1 135 ? 32.778  -32.358 29.103  1.00 30.12 ? 135  THR A C   1 
ATOM   994   O  O   . THR A  1 135 ? 33.208  -31.325 28.573  1.00 28.69 ? 135  THR A O   1 
ATOM   995   C  CB  . THR A  1 135 ? 31.720  -31.428 31.148  1.00 32.73 ? 135  THR A CB  1 
ATOM   996   O  OG1 . THR A  1 135 ? 32.883  -31.868 31.863  1.00 32.49 ? 135  THR A OG1 1 
ATOM   997   C  CG2 . THR A  1 135 ? 30.521  -31.465 32.073  1.00 32.10 ? 135  THR A CG2 1 
ATOM   998   N  N   . LYS A  1 136 ? 33.402  -33.533 29.031  1.00 29.76 ? 136  LYS A N   1 
ATOM   999   C  CA  . LYS A  1 136 ? 34.612  -33.725 28.241  1.00 28.32 ? 136  LYS A CA  1 
ATOM   1000  C  C   . LYS A  1 136 ? 34.306  -34.446 26.925  1.00 27.84 ? 136  LYS A C   1 
ATOM   1001  O  O   . LYS A  1 136 ? 34.569  -33.919 25.845  1.00 27.78 ? 136  LYS A O   1 
ATOM   1002  C  CB  . LYS A  1 136 ? 35.672  -34.511 29.024  1.00 29.92 ? 136  LYS A CB  1 
ATOM   1003  C  CG  . LYS A  1 136 ? 36.666  -33.654 29.804  1.00 31.94 ? 136  LYS A CG  1 
ATOM   1004  C  CD  . LYS A  1 136 ? 36.497  -33.800 31.310  1.00 35.88 ? 136  LYS A CD  1 
ATOM   1005  C  CE  . LYS A  1 136 ? 37.265  -35.010 31.864  1.00 41.46 ? 136  LYS A CE  1 
ATOM   1006  N  NZ  . LYS A  1 136 ? 38.664  -34.679 32.295  1.00 43.66 ? 136  LYS A NZ  1 
ATOM   1007  N  N   . THR A  1 137 ? 33.733  -35.644 27.024  1.00 27.90 ? 137  THR A N   1 
ATOM   1008  C  CA  . THR A  1 137 ? 33.608  -36.540 25.875  1.00 25.68 ? 137  THR A CA  1 
ATOM   1009  C  C   . THR A  1 137 ? 32.166  -36.896 25.483  1.00 25.66 ? 137  THR A C   1 
ATOM   1010  O  O   . THR A  1 137 ? 31.938  -37.513 24.437  1.00 22.68 ? 137  THR A O   1 
ATOM   1011  C  CB  . THR A  1 137 ? 34.394  -37.852 26.127  1.00 28.53 ? 137  THR A CB  1 
ATOM   1012  O  OG1 . THR A  1 137 ? 33.732  -38.637 27.130  1.00 25.22 ? 137  THR A OG1 1 
ATOM   1013  C  CG2 . THR A  1 137 ? 35.815  -37.542 26.595  1.00 30.63 ? 137  THR A CG2 1 
ATOM   1014  N  N   . GLY A  1 138 ? 31.202  -36.511 26.317  1.00 25.76 ? 138  GLY A N   1 
ATOM   1015  C  CA  . GLY A  1 138 ? 29.816  -36.868 26.096  1.00 23.01 ? 138  GLY A CA  1 
ATOM   1016  C  C   . GLY A  1 138 ? 29.558  -38.315 26.477  1.00 23.81 ? 138  GLY A C   1 
ATOM   1017  O  O   . GLY A  1 138 ? 28.553  -38.907 26.079  1.00 22.13 ? 138  GLY A O   1 
ATOM   1018  N  N   . ASN A  1 139 ? 30.463  -38.886 27.265  1.00 24.52 ? 139  ASN A N   1 
ATOM   1019  C  CA  . ASN A  1 139 ? 30.372  -40.297 27.626  1.00 25.70 ? 139  ASN A CA  1 
ATOM   1020  C  C   . ASN A  1 139 ? 30.204  -41.174 26.384  1.00 25.68 ? 139  ASN A C   1 
ATOM   1021  O  O   . ASN A  1 139 ? 29.514  -42.198 26.426  1.00 25.37 ? 139  ASN A O   1 
ATOM   1022  C  CB  . ASN A  1 139 ? 29.218  -40.523 28.610  1.00 26.88 ? 139  ASN A CB  1 
ATOM   1023  C  CG  . ASN A  1 139 ? 29.597  -40.184 30.040  1.00 26.36 ? 139  ASN A CG  1 
ATOM   1024  O  OD1 . ASN A  1 139 ? 30.340  -40.926 30.676  1.00 27.84 ? 139  ASN A OD1 1 
ATOM   1025  N  ND2 . ASN A  1 139 ? 29.096  -39.056 30.546  1.00 24.28 ? 139  ASN A ND2 1 
ATOM   1026  N  N   . ALA A  1 140 ? 30.837  -40.762 25.282  1.00 23.86 ? 140  ALA A N   1 
ATOM   1027  C  CA  . ALA A  1 140 ? 30.707  -41.452 23.996  1.00 19.61 ? 140  ALA A CA  1 
ATOM   1028  C  C   . ALA A  1 140 ? 31.550  -42.729 23.917  1.00 19.40 ? 140  ALA A C   1 
ATOM   1029  O  O   . ALA A  1 140 ? 31.487  -43.467 22.947  1.00 20.42 ? 140  ALA A O   1 
ATOM   1030  C  CB  . ALA A  1 140 ? 31.049  -40.512 22.859  1.00 18.00 ? 140  ALA A CB  1 
ATOM   1031  N  N   . GLY A  1 141 ? 32.344  -42.984 24.947  1.00 22.71 ? 141  GLY A N   1 
ATOM   1032  C  CA  . GLY A  1 141 ? 33.112  -44.212 25.033  1.00 22.39 ? 141  GLY A CA  1 
ATOM   1033  C  C   . GLY A  1 141 ? 34.359  -44.205 24.179  1.00 22.20 ? 141  GLY A C   1 
ATOM   1034  O  O   . GLY A  1 141 ? 34.892  -43.142 23.856  1.00 22.18 ? 141  GLY A O   1 
ATOM   1035  N  N   . SER A  1 142 ? 34.815  -45.400 23.809  1.00 21.52 ? 142  SER A N   1 
ATOM   1036  C  CA  . SER A  1 142 ? 36.070  -45.576 23.080  1.00 21.08 ? 142  SER A CA  1 
ATOM   1037  C  C   . SER A  1 142 ? 36.017  -45.122 21.623  1.00 20.73 ? 142  SER A C   1 
ATOM   1038  O  O   . SER A  1 142 ? 34.949  -44.943 21.052  1.00 19.62 ? 142  SER A O   1 
ATOM   1039  C  CB  . SER A  1 142 ? 36.550  -47.034 23.157  1.00 21.20 ? 142  SER A CB  1 
ATOM   1040  O  OG  . SER A  1 142 ? 35.699  -47.912 22.438  1.00 20.38 ? 142  SER A OG  1 
ATOM   1041  N  N   . ARG A  1 143 ? 37.202  -44.944 21.044  1.00 21.36 ? 143  ARG A N   1 
ATOM   1042  C  CA  . ARG A  1 143 ? 37.374  -44.529 19.657  1.00 20.18 ? 143  ARG A CA  1 
ATOM   1043  C  C   . ARG A  1 143 ? 37.438  -45.763 18.766  1.00 19.39 ? 143  ARG A C   1 
ATOM   1044  O  O   . ARG A  1 143 ? 38.372  -46.552 18.856  1.00 18.77 ? 143  ARG A O   1 
ATOM   1045  C  CB  . ARG A  1 143 ? 38.641  -43.670 19.523  1.00 19.55 ? 143  ARG A CB  1 
ATOM   1046  C  CG  . ARG A  1 143 ? 38.597  -42.396 20.383  1.00 21.78 ? 143  ARG A CG  1 
ATOM   1047  C  CD  . ARG A  1 143 ? 39.981  -41.765 20.654  1.00 23.67 ? 143  ARG A CD  1 
ATOM   1048  N  NE  . ARG A  1 143 ? 39.930  -40.887 21.828  1.00 23.68 ? 143  ARG A NE  1 
ATOM   1049  C  CZ  . ARG A  1 143 ? 40.646  -39.777 21.988  1.00 21.71 ? 143  ARG A CZ  1 
ATOM   1050  N  NH1 . ARG A  1 143 ? 41.488  -39.377 21.050  1.00 20.83 ? 143  ARG A NH1 1 
ATOM   1051  N  NH2 . ARG A  1 143 ? 40.500  -39.050 23.082  1.00 21.78 ? 143  ARG A NH2 1 
ATOM   1052  N  N   . LEU A  1 144 ? 36.431  -45.920 17.910  1.00 19.62 ? 144  LEU A N   1 
ATOM   1053  C  CA  . LEU A  1 144 ? 36.236  -47.142 17.125  1.00 18.23 ? 144  LEU A CA  1 
ATOM   1054  C  C   . LEU A  1 144 ? 36.965  -47.105 15.781  1.00 19.10 ? 144  LEU A C   1 
ATOM   1055  O  O   . LEU A  1 144 ? 37.478  -48.121 15.305  1.00 19.42 ? 144  LEU A O   1 
ATOM   1056  C  CB  . LEU A  1 144 ? 34.734  -47.393 16.898  1.00 17.71 ? 144  LEU A CB  1 
ATOM   1057  C  CG  . LEU A  1 144 ? 33.862  -47.755 18.097  1.00 14.75 ? 144  LEU A CG  1 
ATOM   1058  C  CD1 . LEU A  1 144 ? 32.483  -48.123 17.613  1.00 16.63 ? 144  LEU A CD1 1 
ATOM   1059  C  CD2 . LEU A  1 144 ? 34.483  -48.900 18.865  1.00 16.44 ? 144  LEU A CD2 1 
ATOM   1060  N  N   . ALA A  1 145 ? 36.987  -45.929 15.167  1.00 16.65 ? 145  ALA A N   1 
ATOM   1061  C  CA  . ALA A  1 145 ? 37.764  -45.700 13.963  1.00 17.74 ? 145  ALA A CA  1 
ATOM   1062  C  C   . ALA A  1 145 ? 38.104  -44.217 13.896  1.00 17.29 ? 145  ALA A C   1 
ATOM   1063  O  O   . ALA A  1 145 ? 37.427  -43.386 14.497  1.00 18.44 ? 145  ALA A O   1 
ATOM   1064  C  CB  . ALA A  1 145 ? 36.985  -46.134 12.722  1.00 17.79 ? 145  ALA A CB  1 
ATOM   1065  N  N   . CYS A  1 146 ? 39.160  -43.885 13.171  1.00 18.87 ? 146  CYS A N   1 
ATOM   1066  C  CA  . CYS A  1 146 ? 39.531  -42.491 12.979  1.00 19.02 ? 146  CYS A CA  1 
ATOM   1067  C  C   . CYS A  1 146 ? 40.404  -42.335 11.747  1.00 17.97 ? 146  CYS A C   1 
ATOM   1068  O  O   . CYS A  1 146 ? 40.889  -43.320 11.189  1.00 17.36 ? 146  CYS A O   1 
ATOM   1069  C  CB  . CYS A  1 146 ? 40.248  -41.933 14.219  1.00 18.59 ? 146  CYS A CB  1 
ATOM   1070  S  SG  . CYS A  1 146 ? 41.902  -42.621 14.556  1.00 23.90 ? 146  CYS A SG  1 
ATOM   1071  N  N   . GLY A  1 147 ? 40.586  -41.088 11.326  1.00 16.52 ? 147  GLY A N   1 
ATOM   1072  C  CA  . GLY A  1 147 ? 41.491  -40.758 10.250  1.00 15.12 ? 147  GLY A CA  1 
ATOM   1073  C  C   . GLY A  1 147 ? 41.815  -39.275 10.297  1.00 16.50 ? 147  GLY A C   1 
ATOM   1074  O  O   . GLY A  1 147 ? 41.062  -38.472 10.847  1.00 17.89 ? 147  GLY A O   1 
ATOM   1075  N  N   . VAL A  1 148 ? 42.945  -38.908 9.719   1.00 15.50 ? 148  VAL A N   1 
ATOM   1076  C  CA  . VAL A  1 148 ? 43.296  -37.505 9.560   1.00 16.41 ? 148  VAL A CA  1 
ATOM   1077  C  C   . VAL A  1 148 ? 42.493  -36.884 8.399   1.00 16.94 ? 148  VAL A C   1 
ATOM   1078  O  O   . VAL A  1 148 ? 42.292  -37.514 7.347   1.00 13.60 ? 148  VAL A O   1 
ATOM   1079  C  CB  . VAL A  1 148 ? 44.825  -37.356 9.366   1.00 15.11 ? 148  VAL A CB  1 
ATOM   1080  C  CG1 . VAL A  1 148 ? 45.236  -35.896 9.243   1.00 15.07 ? 148  VAL A CG1 1 
ATOM   1081  C  CG2 . VAL A  1 148 ? 45.555  -38.027 10.534  1.00 17.97 ? 148  VAL A CG2 1 
ATOM   1082  N  N   . ILE A  1 149 ? 42.014  -35.658 8.612   1.00 16.53 ? 149  ILE A N   1 
ATOM   1083  C  CA  . ILE A  1 149 ? 41.245  -34.939 7.604   1.00 15.31 ? 149  ILE A CA  1 
ATOM   1084  C  C   . ILE A  1 149 ? 42.211  -34.230 6.655   1.00 16.31 ? 149  ILE A C   1 
ATOM   1085  O  O   . ILE A  1 149 ? 43.031  -33.413 7.084   1.00 15.09 ? 149  ILE A O   1 
ATOM   1086  C  CB  . ILE A  1 149 ? 40.244  -33.922 8.246   1.00 18.99 ? 149  ILE A CB  1 
ATOM   1087  C  CG1 . ILE A  1 149 ? 39.276  -34.637 9.207   1.00 16.36 ? 149  ILE A CG1 1 
ATOM   1088  C  CG2 . ILE A  1 149 ? 39.477  -33.153 7.168   1.00 14.10 ? 149  ILE A CG2 1 
ATOM   1089  C  CD1 . ILE A  1 149 ? 38.683  -33.758 10.303  1.00 14.88 ? 149  ILE A CD1 1 
ATOM   1090  N  N   . GLY A  1 150 ? 42.119  -34.561 5.368   1.00 15.36 ? 150  GLY A N   1 
ATOM   1091  C  CA  . GLY A  1 150 ? 43.023  -34.021 4.375   1.00 15.52 ? 150  GLY A CA  1 
ATOM   1092  C  C   . GLY A  1 150 ? 42.327  -33.302 3.239   1.00 16.49 ? 150  GLY A C   1 
ATOM   1093  O  O   . GLY A  1 150 ? 41.141  -33.519 2.972   1.00 16.06 ? 150  GLY A O   1 
ATOM   1094  N  N   . ILE A  1 151 ? 43.078  -32.433 2.568   1.00 16.86 ? 151  ILE A N   1 
ATOM   1095  C  CA  . ILE A  1 151 ? 42.580  -31.690 1.408   1.00 19.11 ? 151  ILE A CA  1 
ATOM   1096  C  C   . ILE A  1 151 ? 42.210  -32.624 0.245   1.00 17.74 ? 151  ILE A C   1 
ATOM   1097  O  O   . ILE A  1 151 ? 43.006  -33.460 -0.164  1.00 16.89 ? 151  ILE A O   1 
ATOM   1098  C  CB  . ILE A  1 151 ? 43.621  -30.648 0.926   1.00 20.17 ? 151  ILE A CB  1 
ATOM   1099  C  CG1 . ILE A  1 151 ? 44.054  -29.753 2.090   1.00 17.52 ? 151  ILE A CG1 1 
ATOM   1100  C  CG2 . ILE A  1 151 ? 43.053  -29.824 -0.226  1.00 17.34 ? 151  ILE A CG2 1 
ATOM   1101  C  CD1 . ILE A  1 151 ? 45.016  -28.667 1.689   1.00 18.55 ? 151  ILE A CD1 1 
ATOM   1102  N  N   . ALA A  1 152 ? 40.992  -32.489 -0.265  1.00 18.38 ? 152  ALA A N   1 
ATOM   1103  C  CA  . ALA A  1 152 ? 40.520  -33.331 -1.357  1.00 21.11 ? 152  ALA A CA  1 
ATOM   1104  C  C   . ALA A  1 152 ? 40.435  -32.510 -2.643  1.00 21.40 ? 152  ALA A C   1 
ATOM   1105  O  O   . ALA A  1 152 ? 40.427  -31.277 -2.595  1.00 21.08 ? 152  ALA A O   1 
ATOM   1106  C  CB  . ALA A  1 152 ? 39.158  -33.923 -1.017  1.00 19.17 ? 152  ALA A CB  1 
ATOM   1107  N  N   . GLN A  1 153 ? 40.395  -33.191 -3.787  1.00 21.86 ? 153  GLN A N   1 
ATOM   1108  C  CA  . GLN A  1 153 ? 40.232  -32.518 -5.074  1.00 25.62 ? 153  GLN A CA  1 
ATOM   1109  C  C   . GLN A  1 153 ? 38.795  -31.996 -5.190  1.00 31.16 ? 153  GLN A C   1 
ATOM   1110  O  O   . GLN A  1 153 ? 38.559  -30.792 -5.384  1.00 33.04 ? 153  GLN A O   1 
ATOM   1111  C  CB  . GLN A  1 153 ? 40.567  -33.476 -6.230  1.00 31.47 ? 153  GLN A CB  1 
ATOM   1112  C  CG  . GLN A  1 153 ? 40.574  -32.840 -7.634  1.00 33.68 ? 153  GLN A CG  1 
ATOM   1113  C  CD  . GLN A  1 153 ? 41.273  -33.712 -8.679  1.00 35.43 ? 153  GLN A CD  1 
ATOM   1114  O  OE1 . GLN A  1 153 ? 42.102  -33.226 -9.453  1.00 37.97 ? 153  GLN A OE1 1 
ATOM   1115  N  NE2 . GLN A  1 153 ? 40.947  -35.002 -8.697  1.00 32.86 ? 153  GLN A NE2 1 
ATOM   1116  O  OXT . GLN A  1 153 ? 37.835  -32.770 -5.047  1.00 30.40 ? 153  GLN A OXT 1 
ATOM   1117  N  N   . ALA B  1 1   ? 54.978  -21.652 16.756  1.00 37.05 ? 1    ALA B N   1 
ATOM   1118  C  CA  . ALA B  1 1   ? 55.822  -22.831 16.554  1.00 37.17 ? 1    ALA B CA  1 
ATOM   1119  C  C   . ALA B  1 1   ? 54.999  -24.050 16.135  1.00 36.29 ? 1    ALA B C   1 
ATOM   1120  O  O   . ALA B  1 1   ? 54.729  -24.935 16.944  1.00 36.17 ? 1    ALA B O   1 
ATOM   1121  C  CB  . ALA B  1 1   ? 56.655  -23.140 17.818  1.00 33.65 ? 1    ALA B CB  1 
ATOM   1122  N  N   . THR B  1 2   ? 54.618  -24.103 14.862  1.00 36.76 ? 2    THR B N   1 
ATOM   1123  C  CA  . THR B  1 2   ? 53.802  -25.202 14.358  1.00 31.50 ? 2    THR B CA  1 
ATOM   1124  C  C   . THR B  1 2   ? 54.555  -26.547 14.352  1.00 27.81 ? 2    THR B C   1 
ATOM   1125  O  O   . THR B  1 2   ? 55.781  -26.611 14.214  1.00 25.34 ? 2    THR B O   1 
ATOM   1126  C  CB  . THR B  1 2   ? 53.207  -24.905 12.946  1.00 29.37 ? 2    THR B CB  1 
ATOM   1127  O  OG1 . THR B  1 2   ? 53.011  -23.494 12.773  1.00 31.33 ? 2    THR B OG1 1 
ATOM   1128  C  CG2 . THR B  1 2   ? 51.872  -25.599 12.785  1.00 31.44 ? 2    THR B CG2 1 
ATOM   1129  N  N   . LYS B  1 3   ? 53.783  -27.614 14.511  1.00 28.71 ? 3    LYS B N   1 
ATOM   1130  C  CA  . LYS B  1 3   ? 54.271  -28.985 14.511  1.00 26.05 ? 3    LYS B CA  1 
ATOM   1131  C  C   . LYS B  1 3   ? 53.290  -29.858 13.717  1.00 22.60 ? 3    LYS B C   1 
ATOM   1132  O  O   . LYS B  1 3   ? 52.079  -29.674 13.806  1.00 20.68 ? 3    LYS B O   1 
ATOM   1133  C  CB  . LYS B  1 3   ? 54.371  -29.496 15.951  1.00 24.72 ? 3    LYS B CB  1 
ATOM   1134  C  CG  . LYS B  1 3   ? 55.766  -29.493 16.531  1.00 27.71 ? 3    LYS B CG  1 
ATOM   1135  C  CD  . LYS B  1 3   ? 55.734  -29.223 18.026  1.00 35.19 ? 3    LYS B CD  1 
ATOM   1136  C  CE  . LYS B  1 3   ? 56.834  -29.982 18.759  1.00 43.14 ? 3    LYS B CE  1 
ATOM   1137  N  NZ  . LYS B  1 3   ? 56.486  -31.433 18.945  1.00 41.35 ? 3    LYS B NZ  1 
ATOM   1138  N  N   . ALA B  1 4   ? 53.802  -30.795 12.932  1.00 18.26 ? 4    ALA B N   1 
ATOM   1139  C  CA  . ALA B  1 4   ? 52.927  -31.760 12.289  1.00 16.89 ? 4    ALA B CA  1 
ATOM   1140  C  C   . ALA B  1 4   ? 53.484  -33.173 12.434  1.00 16.94 ? 4    ALA B C   1 
ATOM   1141  O  O   . ALA B  1 4   ? 54.625  -33.350 12.834  1.00 17.38 ? 4    ALA B O   1 
ATOM   1142  C  CB  . ALA B  1 4   ? 52.715  -31.399 10.825  1.00 16.30 ? 4    ALA B CB  1 
ATOM   1143  N  N   . VAL B  1 5   ? 52.660  -34.177 12.151  1.00 18.42 ? 5    VAL B N   1 
ATOM   1144  C  CA  . VAL B  1 5   ? 53.119  -35.563 12.092  1.00 17.17 ? 5    VAL B CA  1 
ATOM   1145  C  C   . VAL B  1 5   ? 52.437  -36.313 10.942  1.00 18.11 ? 5    VAL B C   1 
ATOM   1146  O  O   . VAL B  1 5   ? 51.361  -35.952 10.504  1.00 18.15 ? 5    VAL B O   1 
ATOM   1147  C  CB  . VAL B  1 5   ? 52.884  -36.326 13.410  1.00 16.71 ? 5    VAL B CB  1 
ATOM   1148  C  CG1 . VAL B  1 5   ? 51.425  -36.415 13.687  1.00 18.60 ? 5    VAL B CG1 1 
ATOM   1149  C  CG2 . VAL B  1 5   ? 53.477  -37.721 13.322  1.00 18.57 ? 5    VAL B CG2 1 
ATOM   1150  N  N   . CYS B  1 6   ? 53.095  -37.353 10.454  1.00 18.92 ? 6    CYS B N   1 
ATOM   1151  C  CA  . CYS B  1 6   ? 52.583  -38.166 9.377   1.00 16.86 ? 6    CYS B CA  1 
ATOM   1152  C  C   . CYS B  1 6   ? 52.900  -39.629 9.678   1.00 18.06 ? 6    CYS B C   1 
ATOM   1153  O  O   . CYS B  1 6   ? 54.039  -39.973 9.911   1.00 16.98 ? 6    CYS B O   1 
ATOM   1154  C  CB  . CYS B  1 6   ? 53.274  -37.763 8.082   1.00 16.81 ? 6    CYS B CB  1 
ATOM   1155  S  SG  . CYS B  1 6   ? 52.558  -38.514 6.626   1.00 22.93 ? 6    CYS B SG  1 
ATOM   1156  N  N   . VAL B  1 7   ? 51.898  -40.498 9.675   1.00 19.88 ? 7    VAL B N   1 
ATOM   1157  C  CA  . VAL B  1 7   ? 52.176  -41.929 9.800   1.00 20.75 ? 7    VAL B CA  1 
ATOM   1158  C  C   . VAL B  1 7   ? 52.086  -42.588 8.423   1.00 17.99 ? 7    VAL B C   1 
ATOM   1159  O  O   . VAL B  1 7   ? 51.041  -42.576 7.789   1.00 18.76 ? 7    VAL B O   1 
ATOM   1160  C  CB  . VAL B  1 7   ? 51.232  -42.637 10.822  1.00 22.19 ? 7    VAL B CB  1 
ATOM   1161  C  CG1 . VAL B  1 7   ? 51.620  -44.106 10.968  1.00 22.07 ? 7    VAL B CG1 1 
ATOM   1162  C  CG2 . VAL B  1 7   ? 51.281  -41.936 12.170  1.00 18.77 ? 7    VAL B CG2 1 
ATOM   1163  N  N   . LEU B  1 8   ? 53.203  -43.134 7.955   1.00 21.33 ? 8    LEU B N   1 
ATOM   1164  C  CA  . LEU B  1 8   ? 53.278  -43.715 6.615   1.00 19.75 ? 8    LEU B CA  1 
ATOM   1165  C  C   . LEU B  1 8   ? 52.910  -45.214 6.580   1.00 21.66 ? 8    LEU B C   1 
ATOM   1166  O  O   . LEU B  1 8   ? 53.506  -46.022 7.276   1.00 21.75 ? 8    LEU B O   1 
ATOM   1167  C  CB  . LEU B  1 8   ? 54.672  -43.506 5.999   1.00 21.68 ? 8    LEU B CB  1 
ATOM   1168  C  CG  . LEU B  1 8   ? 55.361  -42.133 5.845   1.00 22.07 ? 8    LEU B CG  1 
ATOM   1169  C  CD1 . LEU B  1 8   ? 56.365  -42.172 4.685   1.00 20.93 ? 8    LEU B CD1 1 
ATOM   1170  C  CD2 . LEU B  1 8   ? 54.379  -41.032 5.596   1.00 21.20 ? 8    LEU B CD2 1 
ATOM   1171  N  N   . LYS B  1 9   ? 51.927  -45.564 5.750   1.00 23.22 ? 9    LYS B N   1 
ATOM   1172  C  CA  . LYS B  1 9   ? 51.503  -46.947 5.542   1.00 23.49 ? 9    LYS B CA  1 
ATOM   1173  C  C   . LYS B  1 9   ? 51.305  -47.194 4.051   1.00 23.31 ? 9    LYS B C   1 
ATOM   1174  O  O   . LYS B  1 9   ? 50.897  -46.303 3.316   1.00 22.83 ? 9    LYS B O   1 
ATOM   1175  C  CB  . LYS B  1 9   ? 50.193  -47.241 6.285   1.00 27.24 ? 9    LYS B CB  1 
ATOM   1176  C  CG  . LYS B  1 9   ? 50.298  -47.108 7.799   1.00 28.55 ? 9    LYS B CG  1 
ATOM   1177  C  CD  . LYS B  1 9   ? 48.934  -47.306 8.483   1.00 38.34 ? 9    LYS B CD  1 
ATOM   1178  C  CE  . LYS B  1 9   ? 49.029  -47.179 10.018  1.00 39.35 ? 9    LYS B CE  1 
ATOM   1179  N  NZ  . LYS B  1 9   ? 50.170  -47.967 10.588  1.00 41.18 ? 9    LYS B NZ  1 
ATOM   1180  N  N   . GLY B  1 10  ? 51.599  -48.407 3.605   1.00 23.46 ? 10   GLY B N   1 
ATOM   1181  C  CA  . GLY B  1 10  ? 51.389  -48.773 2.221   1.00 24.13 ? 10   GLY B CA  1 
ATOM   1182  C  C   . GLY B  1 10  ? 50.801  -50.168 2.116   1.00 28.62 ? 10   GLY B C   1 
ATOM   1183  O  O   . GLY B  1 10  ? 50.239  -50.690 3.075   1.00 27.24 ? 10   GLY B O   1 
ATOM   1184  N  N   . ASP B  1 11  ? 50.924  -50.782 0.948   1.00 28.44 ? 11   ASP B N   1 
ATOM   1185  C  CA  . ASP B  1 11  ? 50.395  -52.122 0.763   1.00 29.00 ? 11   ASP B CA  1 
ATOM   1186  C  C   . ASP B  1 11  ? 51.404  -53.197 1.178   1.00 28.67 ? 11   ASP B C   1 
ATOM   1187  O  O   . ASP B  1 11  ? 51.057  -54.365 1.323   1.00 32.41 ? 11   ASP B O   1 
ATOM   1188  C  CB  . ASP B  1 11  ? 49.939  -52.310 -0.688  1.00 29.59 ? 11   ASP B CB  1 
ATOM   1189  C  CG  . ASP B  1 11  ? 48.661  -51.538 -0.997  1.00 35.32 ? 11   ASP B CG  1 
ATOM   1190  O  OD1 . ASP B  1 11  ? 47.881  -51.277 -0.044  1.00 34.89 ? 11   ASP B OD1 1 
ATOM   1191  O  OD2 . ASP B  1 11  ? 48.431  -51.199 -2.181  1.00 35.24 ? 11   ASP B OD2 1 
ATOM   1192  N  N   . GLY B  1 12  ? 52.650  -52.791 1.383   1.00 27.18 ? 12   GLY B N   1 
ATOM   1193  C  CA  . GLY B  1 12  ? 53.721  -53.718 1.685   1.00 25.51 ? 12   GLY B CA  1 
ATOM   1194  C  C   . GLY B  1 12  ? 54.319  -53.532 3.066   1.00 26.77 ? 12   GLY B C   1 
ATOM   1195  O  O   . GLY B  1 12  ? 53.607  -53.166 4.012   1.00 27.68 ? 12   GLY B O   1 
ATOM   1196  N  N   . PRO B  1 13  ? 55.636  -53.786 3.193   1.00 24.37 ? 13   PRO B N   1 
ATOM   1197  C  CA  . PRO B  1 13  ? 56.348  -53.741 4.477   1.00 25.35 ? 13   PRO B CA  1 
ATOM   1198  C  C   . PRO B  1 13  ? 56.735  -52.323 4.901   1.00 23.44 ? 13   PRO B C   1 
ATOM   1199  O  O   . PRO B  1 13  ? 57.078  -52.112 6.062   1.00 21.85 ? 13   PRO B O   1 
ATOM   1200  C  CB  . PRO B  1 13  ? 57.627  -54.544 4.203   1.00 24.06 ? 13   PRO B CB  1 
ATOM   1201  C  CG  . PRO B  1 13  ? 57.582  -54.937 2.746   1.00 25.41 ? 13   PRO B CG  1 
ATOM   1202  C  CD  . PRO B  1 13  ? 56.534  -54.128 2.081   1.00 22.70 ? 13   PRO B CD  1 
ATOM   1203  N  N   . VAL B  1 14  ? 56.689  -51.381 3.961   1.00 24.31 ? 14   VAL B N   1 
ATOM   1204  C  CA  . VAL B  1 14  ? 57.141  -50.012 4.198   1.00 22.80 ? 14   VAL B CA  1 
ATOM   1205  C  C   . VAL B  1 14  ? 56.196  -49.227 5.112   1.00 22.33 ? 14   VAL B C   1 
ATOM   1206  O  O   . VAL B  1 14  ? 55.020  -49.045 4.812   1.00 24.15 ? 14   VAL B O   1 
ATOM   1207  C  CB  . VAL B  1 14  ? 57.358  -49.261 2.865   1.00 21.85 ? 14   VAL B CB  1 
ATOM   1208  C  CG1 . VAL B  1 14  ? 58.017  -47.906 3.104   1.00 18.54 ? 14   VAL B CG1 1 
ATOM   1209  C  CG2 . VAL B  1 14  ? 58.199  -50.104 1.938   1.00 21.23 ? 14   VAL B CG2 1 
ATOM   1210  N  N   . GLN B  1 15  ? 56.730  -48.771 6.236   1.00 23.46 ? 15   GLN B N   1 
ATOM   1211  C  CA  . GLN B  1 15  ? 55.972  -48.016 7.218   1.00 24.30 ? 15   GLN B CA  1 
ATOM   1212  C  C   . GLN B  1 15  ? 56.952  -47.065 7.913   1.00 22.04 ? 15   GLN B C   1 
ATOM   1213  O  O   . GLN B  1 15  ? 58.153  -47.315 7.901   1.00 22.07 ? 15   GLN B O   1 
ATOM   1214  C  CB  . GLN B  1 15  ? 55.366  -48.977 8.241   1.00 26.39 ? 15   GLN B CB  1 
ATOM   1215  C  CG  . GLN B  1 15  ? 56.433  -49.673 9.095   1.00 30.58 ? 15   GLN B CG  1 
ATOM   1216  C  CD  . GLN B  1 15  ? 55.873  -50.472 10.259  1.00 40.07 ? 15   GLN B CD  1 
ATOM   1217  O  OE1 . GLN B  1 15  ? 56.375  -51.552 10.575  1.00 46.24 ? 15   GLN B OE1 1 
ATOM   1218  N  NE2 . GLN B  1 15  ? 54.835  -49.943 10.909  1.00 46.24 ? 15   GLN B NE2 1 
ATOM   1219  N  N   . GLY B  1 16  ? 56.449  -45.982 8.504   1.00 22.46 ? 16   GLY B N   1 
ATOM   1220  C  CA  . GLY B  1 16  ? 57.274  -45.074 9.284   1.00 21.01 ? 16   GLY B CA  1 
ATOM   1221  C  C   . GLY B  1 16  ? 56.525  -43.898 9.883   1.00 21.47 ? 16   GLY B C   1 
ATOM   1222  O  O   . GLY B  1 16  ? 55.319  -43.760 9.697   1.00 21.87 ? 16   GLY B O   1 
ATOM   1223  N  N   . ILE B  1 17  ? 57.244  -43.047 10.609  1.00 20.17 ? 17   ILE B N   1 
ATOM   1224  C  CA  . ILE B  1 17  ? 56.662  -41.857 11.231  1.00 20.55 ? 17   ILE B CA  1 
ATOM   1225  C  C   . ILE B  1 17  ? 57.513  -40.619 10.946  1.00 20.34 ? 17   ILE B C   1 
ATOM   1226  O  O   . ILE B  1 17  ? 58.689  -40.557 11.307  1.00 18.96 ? 17   ILE B O   1 
ATOM   1227  C  CB  . ILE B  1 17  ? 56.525  -42.009 12.754  1.00 19.81 ? 17   ILE B CB  1 
ATOM   1228  C  CG1 . ILE B  1 17  ? 55.568  -43.145 13.094  1.00 19.69 ? 17   ILE B CG1 1 
ATOM   1229  C  CG2 . ILE B  1 17  ? 56.043  -40.699 13.379  1.00 19.84 ? 17   ILE B CG2 1 
ATOM   1230  C  CD1 . ILE B  1 17  ? 55.552  -43.470 14.539  1.00 26.31 ? 17   ILE B CD1 1 
ATOM   1231  N  N   . ILE B  1 18  ? 56.923  -39.637 10.281  1.00 18.65 ? 18   ILE B N   1 
ATOM   1232  C  CA  . ILE B  1 18  ? 57.664  -38.442 9.912   1.00 17.97 ? 18   ILE B CA  1 
ATOM   1233  C  C   . ILE B  1 18  ? 57.143  -37.263 10.727  1.00 19.09 ? 18   ILE B C   1 
ATOM   1234  O  O   . ILE B  1 18  ? 55.945  -37.028 10.796  1.00 17.56 ? 18   ILE B O   1 
ATOM   1235  C  CB  . ILE B  1 18  ? 57.622  -38.194 8.365   1.00 18.86 ? 18   ILE B CB  1 
ATOM   1236  C  CG1 . ILE B  1 18  ? 58.337  -39.325 7.611   1.00 16.90 ? 18   ILE B CG1 1 
ATOM   1237  C  CG2 . ILE B  1 18  ? 58.266  -36.874 7.992   1.00 19.19 ? 18   ILE B CG2 1 
ATOM   1238  C  CD1 . ILE B  1 18  ? 59.856  -39.424 7.888   1.00 15.18 ? 18   ILE B CD1 1 
ATOM   1239  N  N   . ASN B  1 19  ? 58.059  -36.557 11.382  1.00 19.63 ? 19   ASN B N   1 
ATOM   1240  C  CA  . ASN B  1 19  ? 57.720  -35.402 12.193  1.00 19.05 ? 19   ASN B CA  1 
ATOM   1241  C  C   . ASN B  1 19  ? 58.045  -34.134 11.418  1.00 17.10 ? 19   ASN B C   1 
ATOM   1242  O  O   . ASN B  1 19  ? 58.971  -34.137 10.629  1.00 17.66 ? 19   ASN B O   1 
ATOM   1243  C  CB  . ASN B  1 19  ? 58.513  -35.463 13.502  1.00 22.21 ? 19   ASN B CB  1 
ATOM   1244  C  CG  . ASN B  1 19  ? 58.161  -36.695 14.341  1.00 22.88 ? 19   ASN B CG  1 
ATOM   1245  O  OD1 . ASN B  1 19  ? 57.045  -36.806 14.868  1.00 22.29 ? 19   ASN B OD1 1 
ATOM   1246  N  ND2 . ASN B  1 19  ? 59.106  -37.621 14.462  1.00 19.02 ? 19   ASN B ND2 1 
ATOM   1247  N  N   . PHE B  1 20  ? 57.274  -33.066 11.611  1.00 17.49 ? 20   PHE B N   1 
ATOM   1248  C  CA  . PHE B  1 20  ? 57.539  -31.773 10.953  1.00 18.57 ? 20   PHE B CA  1 
ATOM   1249  C  C   . PHE B  1 20  ? 57.511  -30.651 11.975  1.00 20.46 ? 20   PHE B C   1 
ATOM   1250  O  O   . PHE B  1 20  ? 56.609  -30.593 12.809  1.00 22.97 ? 20   PHE B O   1 
ATOM   1251  C  CB  . PHE B  1 20  ? 56.501  -31.420 9.870   1.00 17.13 ? 20   PHE B CB  1 
ATOM   1252  C  CG  . PHE B  1 20  ? 56.274  -32.494 8.852   1.00 17.35 ? 20   PHE B CG  1 
ATOM   1253  C  CD1 . PHE B  1 20  ? 55.430  -33.560 9.126   1.00 17.23 ? 20   PHE B CD1 1 
ATOM   1254  C  CD2 . PHE B  1 20  ? 56.880  -32.427 7.611   1.00 17.94 ? 20   PHE B CD2 1 
ATOM   1255  C  CE1 . PHE B  1 20  ? 55.220  -34.549 8.202   1.00 16.34 ? 20   PHE B CE1 1 
ATOM   1256  C  CE2 . PHE B  1 20  ? 56.665  -33.421 6.664   1.00 18.23 ? 20   PHE B CE2 1 
ATOM   1257  C  CZ  . PHE B  1 20  ? 55.839  -34.482 6.965   1.00 16.17 ? 20   PHE B CZ  1 
ATOM   1258  N  N   . GLU B  1 21  ? 58.465  -29.732 11.887  1.00 20.33 ? 21   GLU B N   1 
ATOM   1259  C  CA  . GLU B  1 21  ? 58.507  -28.639 12.835  1.00 22.76 ? 21   GLU B CA  1 
ATOM   1260  C  C   . GLU B  1 21  ? 58.926  -27.333 12.205  1.00 22.82 ? 21   GLU B C   1 
ATOM   1261  O  O   . GLU B  1 21  ? 59.917  -27.273 11.492  1.00 22.76 ? 21   GLU B O   1 
ATOM   1262  C  CB  . GLU B  1 21  ? 59.465  -28.972 13.969  1.00 25.83 ? 21   GLU B CB  1 
ATOM   1263  C  CG  . GLU B  1 21  ? 59.464  -27.926 15.034  1.00 32.56 ? 21   GLU B CG  1 
ATOM   1264  C  CD  . GLU B  1 21  ? 60.378  -28.273 16.173  1.00 39.30 ? 21   GLU B CD  1 
ATOM   1265  O  OE1 . GLU B  1 21  ? 60.869  -29.426 16.216  1.00 38.32 ? 21   GLU B OE1 1 
ATOM   1266  O  OE2 . GLU B  1 21  ? 60.597  -27.387 17.022  1.00 47.32 ? 21   GLU B OE2 1 
ATOM   1267  N  N   . GLN B  1 22  ? 58.182  -26.277 12.510  1.00 25.21 ? 22   GLN B N   1 
ATOM   1268  C  CA  . GLN B  1 22  ? 58.478  -24.946 12.003  1.00 24.46 ? 22   GLN B CA  1 
ATOM   1269  C  C   . GLN B  1 22  ? 58.414  -23.963 13.162  1.00 30.22 ? 22   GLN B C   1 
ATOM   1270  O  O   . GLN B  1 22  ? 57.330  -23.574 13.606  1.00 31.41 ? 22   GLN B O   1 
ATOM   1271  C  CB  . GLN B  1 22  ? 57.457  -24.567 10.950  1.00 24.07 ? 22   GLN B CB  1 
ATOM   1272  C  CG  . GLN B  1 22  ? 57.846  -23.412 10.061  1.00 21.17 ? 22   GLN B CG  1 
ATOM   1273  C  CD  . GLN B  1 22  ? 56.765  -23.146 9.055   1.00 22.17 ? 22   GLN B CD  1 
ATOM   1274  O  OE1 . GLN B  1 22  ? 55.586  -23.361 9.341   1.00 21.73 ? 22   GLN B OE1 1 
ATOM   1275  N  NE2 . GLN B  1 22  ? 57.145  -22.692 7.869   1.00 20.89 ? 22   GLN B NE2 1 
ATOM   1276  N  N   . LYS B  1 23  ? 59.582  -23.574 13.662  1.00 33.71 ? 23   LYS B N   1 
ATOM   1277  C  CA  . LYS B  1 23  ? 59.664  -22.743 14.862  1.00 34.44 ? 23   LYS B CA  1 
ATOM   1278  C  C   . LYS B  1 23  ? 59.420  -21.265 14.565  1.00 33.64 ? 23   LYS B C   1 
ATOM   1279  O  O   . LYS B  1 23  ? 59.052  -20.497 15.451  1.00 35.08 ? 23   LYS B O   1 
ATOM   1280  C  CB  . LYS B  1 23  ? 61.009  -22.947 15.564  1.00 38.86 ? 23   LYS B CB  1 
ATOM   1281  C  CG  . LYS B  1 23  ? 61.217  -24.366 16.105  1.00 41.28 ? 23   LYS B CG  1 
ATOM   1282  C  CD  . LYS B  1 23  ? 62.528  -24.476 16.896  1.00 53.27 ? 23   LYS B CD  1 
ATOM   1283  C  CE  . LYS B  1 23  ? 62.389  -23.874 18.307  1.00 61.99 ? 23   LYS B CE  1 
ATOM   1284  N  NZ  . LYS B  1 23  ? 63.650  -23.928 19.116  1.00 56.14 ? 23   LYS B NZ  1 
ATOM   1285  N  N   . GLU B  1 24  ? 59.613  -20.879 13.309  1.00 32.51 ? 24   GLU B N   1 
ATOM   1286  C  CA  . GLU B  1 24  ? 59.349  -19.516 12.877  1.00 34.35 ? 24   GLU B CA  1 
ATOM   1287  C  C   . GLU B  1 24  ? 58.278  -19.541 11.806  1.00 33.63 ? 24   GLU B C   1 
ATOM   1288  O  O   . GLU B  1 24  ? 58.232  -20.470 11.001  1.00 32.39 ? 24   GLU B O   1 
ATOM   1289  C  CB  . GLU B  1 24  ? 60.626  -18.871 12.332  1.00 36.83 ? 24   GLU B CB  1 
ATOM   1290  C  CG  . GLU B  1 24  ? 61.615  -18.444 13.409  1.00 38.77 ? 24   GLU B CG  1 
ATOM   1291  C  CD  . GLU B  1 24  ? 61.051  -17.359 14.331  1.00 46.49 ? 24   GLU B CD  1 
ATOM   1292  O  OE1 . GLU B  1 24  ? 61.231  -17.453 15.571  1.00 47.32 ? 24   GLU B OE1 1 
ATOM   1293  O  OE2 . GLU B  1 24  ? 60.419  -16.411 13.811  1.00 52.19 ? 24   GLU B OE2 1 
ATOM   1294  N  N   . SER B  1 25  ? 57.412  -18.530 11.790  1.00 37.10 ? 25   SER B N   1 
ATOM   1295  C  CA  . SER B  1 25  ? 56.373  -18.459 10.757  1.00 36.91 ? 25   SER B CA  1 
ATOM   1296  C  C   . SER B  1 25  ? 56.955  -18.262 9.356   1.00 34.07 ? 25   SER B C   1 
ATOM   1297  O  O   . SER B  1 25  ? 57.622  -17.266 9.057   1.00 33.41 ? 25   SER B O   1 
ATOM   1298  C  CB  . SER B  1 25  ? 55.342  -17.368 11.055  1.00 40.90 ? 25   SER B CB  1 
ATOM   1299  O  OG  . SER B  1 25  ? 54.288  -17.414 10.105  1.00 39.35 ? 25   SER B OG  1 
ATOM   1300  N  N   . ASN B  1 26  ? 56.686  -19.234 8.499   1.00 32.16 ? 26   ASN B N   1 
ATOM   1301  C  CA  . ASN B  1 26  ? 57.203  -19.226 7.137   1.00 32.34 ? 26   ASN B CA  1 
ATOM   1302  C  C   . ASN B  1 26  ? 58.731  -19.371 7.068   1.00 26.27 ? 26   ASN B C   1 
ATOM   1303  O  O   . ASN B  1 26  ? 59.339  -19.127 6.038   1.00 26.64 ? 26   ASN B O   1 
ATOM   1304  C  CB  . ASN B  1 26  ? 56.653  -18.026 6.348   1.00 32.81 ? 26   ASN B CB  1 
ATOM   1305  C  CG  . ASN B  1 26  ? 55.180  -18.223 5.945   1.00 37.33 ? 26   ASN B CG  1 
ATOM   1306  O  OD1 . ASN B  1 26  ? 54.775  -19.330 5.545   1.00 32.19 ? 26   ASN B OD1 1 
ATOM   1307  N  ND2 . ASN B  1 26  ? 54.377  -17.155 6.052   1.00 32.76 ? 26   ASN B ND2 1 
ATOM   1308  N  N   . GLY B  1 27  ? 59.328  -19.806 8.177   1.00 24.99 ? 27   GLY B N   1 
ATOM   1309  C  CA  . GLY B  1 27  ? 60.743  -20.123 8.238   1.00 23.01 ? 27   GLY B CA  1 
ATOM   1310  C  C   . GLY B  1 27  ? 60.987  -21.563 7.806   1.00 23.28 ? 27   GLY B C   1 
ATOM   1311  O  O   . GLY B  1 27  ? 60.078  -22.223 7.300   1.00 22.83 ? 27   GLY B O   1 
ATOM   1312  N  N   . PRO B  1 28  ? 62.215  -22.062 7.989   1.00 20.23 ? 28   PRO B N   1 
ATOM   1313  C  CA  . PRO B  1 28  ? 62.482  -23.432 7.539   1.00 21.05 ? 28   PRO B CA  1 
ATOM   1314  C  C   . PRO B  1 28  ? 61.576  -24.443 8.233   1.00 21.77 ? 28   PRO B C   1 
ATOM   1315  O  O   . PRO B  1 28  ? 61.173  -24.219 9.372   1.00 21.31 ? 28   PRO B O   1 
ATOM   1316  C  CB  . PRO B  1 28  ? 63.937  -23.677 7.950   1.00 20.63 ? 28   PRO B CB  1 
ATOM   1317  C  CG  . PRO B  1 28  ? 64.493  -22.363 8.318   1.00 23.88 ? 28   PRO B CG  1 
ATOM   1318  C  CD  . PRO B  1 28  ? 63.384  -21.420 8.607   1.00 21.70 ? 28   PRO B CD  1 
ATOM   1319  N  N   . VAL B  1 29  ? 61.267  -25.545 7.556   1.00 21.01 ? 29   VAL B N   1 
ATOM   1320  C  CA  . VAL B  1 29  ? 60.579  -26.666 8.190   1.00 20.69 ? 29   VAL B CA  1 
ATOM   1321  C  C   . VAL B  1 29  ? 61.558  -27.817 8.382   1.00 20.82 ? 29   VAL B C   1 
ATOM   1322  O  O   . VAL B  1 29  ? 62.167  -28.271 7.416   1.00 20.09 ? 29   VAL B O   1 
ATOM   1323  C  CB  . VAL B  1 29  ? 59.385  -27.158 7.342   1.00 19.74 ? 29   VAL B CB  1 
ATOM   1324  C  CG1 . VAL B  1 29  ? 58.781  -28.414 7.948   1.00 16.55 ? 29   VAL B CG1 1 
ATOM   1325  C  CG2 . VAL B  1 29  ? 58.343  -26.066 7.226   1.00 18.35 ? 29   VAL B CG2 1 
ATOM   1326  N  N   . LYS B  1 30  ? 61.725  -28.276 9.624   1.00 21.25 ? 30   LYS B N   1 
ATOM   1327  C  CA  . LYS B  1 30  ? 62.550  -29.453 9.896   1.00 20.50 ? 30   LYS B CA  1 
ATOM   1328  C  C   . LYS B  1 30  ? 61.705  -30.719 9.773   1.00 20.32 ? 30   LYS B C   1 
ATOM   1329  O  O   . LYS B  1 30  ? 60.642  -30.839 10.386  1.00 19.82 ? 30   LYS B O   1 
ATOM   1330  C  CB  . LYS B  1 30  ? 63.218  -29.376 11.272  1.00 21.98 ? 30   LYS B CB  1 
ATOM   1331  C  CG  . LYS B  1 30  ? 64.355  -30.391 11.466  1.00 27.53 ? 30   LYS B CG  1 
ATOM   1332  C  CD  . LYS B  1 30  ? 64.622  -30.650 12.950  1.00 34.82 ? 30   LYS B CD  1 
ATOM   1333  C  CE  . LYS B  1 30  ? 65.450  -31.926 13.189  1.00 35.68 ? 30   LYS B CE  1 
ATOM   1334  N  NZ  . LYS B  1 30  ? 65.438  -32.336 14.640  1.00 36.01 ? 30   LYS B NZ  1 
ATOM   1335  N  N   . VAL B  1 31  ? 62.183  -31.648 8.952   1.00 21.52 ? 31   VAL B N   1 
ATOM   1336  C  CA  . VAL B  1 31  ? 61.486  -32.891 8.659   1.00 19.89 ? 31   VAL B CA  1 
ATOM   1337  C  C   . VAL B  1 31  ? 62.386  -34.017 9.149   1.00 22.49 ? 31   VAL B C   1 
ATOM   1338  O  O   . VAL B  1 31  ? 63.541  -34.119 8.742   1.00 22.24 ? 31   VAL B O   1 
ATOM   1339  C  CB  . VAL B  1 31  ? 61.236  -33.044 7.147   1.00 19.10 ? 31   VAL B CB  1 
ATOM   1340  C  CG1 . VAL B  1 31  ? 60.460  -34.330 6.845   1.00 17.50 ? 31   VAL B CG1 1 
ATOM   1341  C  CG2 . VAL B  1 31  ? 60.529  -31.814 6.601   1.00 17.26 ? 31   VAL B CG2 1 
ATOM   1342  N  N   . TRP B  1 32  ? 61.875  -34.842 10.055  1.00 22.86 ? 32   TRP B N   1 
ATOM   1343  C  CA  . TRP B  1 32  ? 62.689  -35.905 10.622  1.00 19.75 ? 32   TRP B CA  1 
ATOM   1344  C  C   . TRP B  1 32  ? 61.841  -37.079 11.079  1.00 17.94 ? 32   TRP B C   1 
ATOM   1345  O  O   . TRP B  1 32  ? 60.691  -36.923 11.479  1.00 19.70 ? 32   TRP B O   1 
ATOM   1346  C  CB  . TRP B  1 32  ? 63.581  -35.366 11.754  1.00 21.98 ? 32   TRP B CB  1 
ATOM   1347  C  CG  . TRP B  1 32  ? 62.942  -35.296 13.116  1.00 22.84 ? 32   TRP B CG  1 
ATOM   1348  C  CD1 . TRP B  1 32  ? 63.094  -36.198 14.142  1.00 21.51 ? 32   TRP B CD1 1 
ATOM   1349  C  CD2 . TRP B  1 32  ? 62.068  -34.267 13.613  1.00 22.49 ? 32   TRP B CD2 1 
ATOM   1350  N  NE1 . TRP B  1 32  ? 62.365  -35.792 15.235  1.00 21.05 ? 32   TRP B NE1 1 
ATOM   1351  C  CE2 . TRP B  1 32  ? 61.730  -34.615 14.943  1.00 23.64 ? 32   TRP B CE2 1 
ATOM   1352  C  CE3 . TRP B  1 32  ? 61.537  -33.095 13.065  1.00 22.96 ? 32   TRP B CE3 1 
ATOM   1353  C  CZ2 . TRP B  1 32  ? 60.883  -33.827 15.731  1.00 25.92 ? 32   TRP B CZ2 1 
ATOM   1354  C  CZ3 . TRP B  1 32  ? 60.694  -32.313 13.847  1.00 23.27 ? 32   TRP B CZ3 1 
ATOM   1355  C  CH2 . TRP B  1 32  ? 60.376  -32.683 15.169  1.00 27.77 ? 32   TRP B CH2 1 
ATOM   1356  N  N   . GLY B  1 33  ? 62.412  -38.266 10.992  1.00 17.35 ? 33   GLY B N   1 
ATOM   1357  C  CA  . GLY B  1 33  ? 61.707  -39.458 11.382  1.00 16.39 ? 33   GLY B CA  1 
ATOM   1358  C  C   . GLY B  1 33  ? 62.453  -40.669 10.888  1.00 18.48 ? 33   GLY B C   1 
ATOM   1359  O  O   . GLY B  1 33  ? 63.645  -40.608 10.621  1.00 21.31 ? 33   GLY B O   1 
ATOM   1360  N  N   . SER B  1 34  ? 61.732  -41.772 10.755  1.00 19.35 ? 34   SER B N   1 
ATOM   1361  C  CA  . SER B  1 34  ? 62.322  -43.043 10.399  1.00 20.63 ? 34   SER B CA  1 
ATOM   1362  C  C   . SER B  1 34  ? 61.304  -43.810 9.566   1.00 21.31 ? 34   SER B C   1 
ATOM   1363  O  O   . SER B  1 34  ? 60.108  -43.763 9.851   1.00 20.27 ? 34   SER B O   1 
ATOM   1364  C  CB  . SER B  1 34  ? 62.673  -43.808 11.678  1.00 22.83 ? 34   SER B CB  1 
ATOM   1365  O  OG  . SER B  1 34  ? 62.839  -45.190 11.434  1.00 28.63 ? 34   SER B OG  1 
ATOM   1366  N  N   . ILE B  1 35  ? 61.780  -44.481 8.517   1.00 22.12 ? 35   ILE B N   1 
ATOM   1367  C  CA  . ILE B  1 35  ? 60.945  -45.324 7.665   1.00 20.41 ? 35   ILE B CA  1 
ATOM   1368  C  C   . ILE B  1 35  ? 61.616  -46.693 7.546   1.00 20.18 ? 35   ILE B C   1 
ATOM   1369  O  O   . ILE B  1 35  ? 62.802  -46.778 7.263   1.00 20.08 ? 35   ILE B O   1 
ATOM   1370  C  CB  . ILE B  1 35  ? 60.786  -44.705 6.269   1.00 19.66 ? 35   ILE B CB  1 
ATOM   1371  C  CG1 . ILE B  1 35  ? 60.445  -43.220 6.384   1.00 18.64 ? 35   ILE B CG1 1 
ATOM   1372  C  CG2 . ILE B  1 35  ? 59.730  -45.454 5.453   1.00 20.42 ? 35   ILE B CG2 1 
ATOM   1373  C  CD1 . ILE B  1 35  ? 60.594  -42.479 5.080   1.00 17.44 ? 35   ILE B CD1 1 
ATOM   1374  N  N   . LYS B  1 36  ? 60.863  -47.759 7.781   1.00 20.60 ? 36   LYS B N   1 
ATOM   1375  C  CA  . LYS B  1 36  ? 61.426  -49.110 7.780   1.00 22.79 ? 36   LYS B CA  1 
ATOM   1376  C  C   . LYS B  1 36  ? 60.769  -49.964 6.693   1.00 22.11 ? 36   LYS B C   1 
ATOM   1377  O  O   . LYS B  1 36  ? 59.675  -49.652 6.251   1.00 22.00 ? 36   LYS B O   1 
ATOM   1378  C  CB  . LYS B  1 36  ? 61.294  -49.769 9.176   1.00 24.06 ? 36   LYS B CB  1 
ATOM   1379  C  CG  . LYS B  1 36  ? 59.861  -49.942 9.695   1.00 28.27 ? 36   LYS B CG  1 
ATOM   1380  C  CD  . LYS B  1 36  ? 59.777  -50.445 11.152  1.00 35.19 ? 36   LYS B CD  1 
ATOM   1381  C  CE  . LYS B  1 36  ? 59.877  -49.292 12.169  1.00 44.80 ? 36   LYS B CE  1 
ATOM   1382  N  NZ  . LYS B  1 36  ? 59.543  -49.674 13.593  1.00 40.61 ? 36   LYS B NZ  1 
ATOM   1383  N  N   . GLY B  1 37  ? 61.441  -51.025 6.253   1.00 20.56 ? 37   GLY B N   1 
ATOM   1384  C  CA  . GLY B  1 37  ? 60.882  -51.915 5.249   1.00 20.10 ? 37   GLY B CA  1 
ATOM   1385  C  C   . GLY B  1 37  ? 61.337  -51.641 3.824   1.00 23.00 ? 37   GLY B C   1 
ATOM   1386  O  O   . GLY B  1 37  ? 60.936  -52.321 2.873   1.00 21.98 ? 37   GLY B O   1 
ATOM   1387  N  N   . LEU B  1 38  ? 62.194  -50.634 3.689   1.00 25.56 ? 38   LEU B N   1 
ATOM   1388  C  CA  . LEU B  1 38  ? 62.734  -50.199 2.412   1.00 21.63 ? 38   LEU B CA  1 
ATOM   1389  C  C   . LEU B  1 38  ? 63.871  -51.104 1.919   1.00 24.76 ? 38   LEU B C   1 
ATOM   1390  O  O   . LEU B  1 38  ? 64.585  -51.748 2.702   1.00 24.45 ? 38   LEU B O   1 
ATOM   1391  C  CB  . LEU B  1 38  ? 63.291  -48.779 2.563   1.00 21.21 ? 38   LEU B CB  1 
ATOM   1392  C  CG  . LEU B  1 38  ? 62.467  -47.518 2.304   1.00 20.41 ? 38   LEU B CG  1 
ATOM   1393  C  CD1 . LEU B  1 38  ? 61.022  -47.827 2.298   1.00 22.04 ? 38   LEU B CD1 1 
ATOM   1394  C  CD2 . LEU B  1 38  ? 62.804  -46.425 3.320   1.00 17.31 ? 38   LEU B CD2 1 
ATOM   1395  N  N   . THR B  1 39  ? 64.049  -51.123 0.606   1.00 25.38 ? 39   THR B N   1 
ATOM   1396  C  CA  . THR B  1 39  ? 65.234  -51.707 0.019   1.00 25.26 ? 39   THR B CA  1 
ATOM   1397  C  C   . THR B  1 39  ? 66.365  -50.698 0.176   1.00 25.02 ? 39   THR B C   1 
ATOM   1398  O  O   . THR B  1 39  ? 66.116  -49.495 0.246   1.00 25.35 ? 39   THR B O   1 
ATOM   1399  C  CB  . THR B  1 39  ? 64.994  -52.026 -1.452  1.00 25.17 ? 39   THR B CB  1 
ATOM   1400  O  OG1 . THR B  1 39  ? 64.764  -50.806 -2.172  1.00 23.55 ? 39   THR B OG1 1 
ATOM   1401  C  CG2 . THR B  1 39  ? 63.783  -52.946 -1.575  1.00 22.87 ? 39   THR B CG2 1 
ATOM   1402  N  N   . GLU B  1 40  ? 67.599  -51.194 0.257   1.00 26.42 ? 40   GLU B N   1 
ATOM   1403  C  CA  . GLU B  1 40  ? 68.770  -50.353 0.515   1.00 24.56 ? 40   GLU B CA  1 
ATOM   1404  C  C   . GLU B  1 40  ? 68.958  -49.338 -0.603  1.00 23.25 ? 40   GLU B C   1 
ATOM   1405  O  O   . GLU B  1 40  ? 68.881  -49.688 -1.779  1.00 24.41 ? 40   GLU B O   1 
ATOM   1406  C  CB  . GLU B  1 40  ? 70.031  -51.221 0.671   1.00 23.76 ? 40   GLU B CB  1 
ATOM   1407  C  CG  . GLU B  1 40  ? 71.286  -50.441 1.063   1.00 29.24 ? 40   GLU B CG  1 
ATOM   1408  C  CD  . GLU B  1 40  ? 72.505  -51.328 1.300   1.00 31.20 ? 40   GLU B CD  1 
ATOM   1409  O  OE1 . GLU B  1 40  ? 72.405  -52.559 1.077   1.00 31.10 ? 40   GLU B OE1 1 
ATOM   1410  O  OE2 . GLU B  1 40  ? 73.559  -50.782 1.709   1.00 29.47 ? 40   GLU B OE2 1 
ATOM   1411  N  N   . GLY B  1 41  ? 69.196  -48.080 -0.247  1.00 22.20 ? 41   GLY B N   1 
ATOM   1412  C  CA  . GLY B  1 41  ? 69.437  -47.064 -1.261  1.00 24.54 ? 41   GLY B CA  1 
ATOM   1413  C  C   . GLY B  1 41  ? 68.505  -45.871 -1.223  1.00 21.75 ? 41   GLY B C   1 
ATOM   1414  O  O   . GLY B  1 41  ? 67.854  -45.630 -0.217  1.00 24.48 ? 41   GLY B O   1 
ATOM   1415  N  N   . LEU B  1 42  ? 68.449  -45.125 -2.326  1.00 25.37 ? 42   LEU B N   1 
ATOM   1416  C  CA  . LEU B  1 42  ? 67.711  -43.861 -2.390  1.00 21.42 ? 42   LEU B CA  1 
ATOM   1417  C  C   . LEU B  1 42  ? 66.262  -44.044 -2.812  1.00 20.37 ? 42   LEU B C   1 
ATOM   1418  O  O   . LEU B  1 42  ? 65.962  -44.782 -3.748  1.00 20.71 ? 42   LEU B O   1 
ATOM   1419  C  CB  . LEU B  1 42  ? 68.418  -42.859 -3.316  1.00 20.34 ? 42   LEU B CB  1 
ATOM   1420  C  CG  . LEU B  1 42  ? 69.754  -42.310 -2.805  1.00 21.64 ? 42   LEU B CG  1 
ATOM   1421  C  CD1 . LEU B  1 42  ? 70.809  -43.381 -2.901  1.00 27.40 ? 42   LEU B CD1 1 
ATOM   1422  C  CD2 . LEU B  1 42  ? 70.196  -41.088 -3.575  1.00 25.55 ? 42   LEU B CD2 1 
ATOM   1423  N  N   . HIS B  1 43  ? 65.366  -43.371 -2.097  1.00 20.76 ? 43   HIS B N   1 
ATOM   1424  C  CA  . HIS B  1 43  ? 63.943  -43.400 -2.406  1.00 18.80 ? 43   HIS B CA  1 
ATOM   1425  C  C   . HIS B  1 43  ? 63.367  -42.003 -2.452  1.00 17.78 ? 43   HIS B C   1 
ATOM   1426  O  O   . HIS B  1 43  ? 63.594  -41.195 -1.561  1.00 16.92 ? 43   HIS B O   1 
ATOM   1427  C  CB  . HIS B  1 43  ? 63.185  -44.216 -1.377  1.00 15.95 ? 43   HIS B CB  1 
ATOM   1428  C  CG  . HIS B  1 43  ? 63.602  -45.650 -1.321  1.00 19.74 ? 43   HIS B CG  1 
ATOM   1429  N  ND1 . HIS B  1 43  ? 62.911  -46.647 -1.973  1.00 21.42 ? 43   HIS B ND1 1 
ATOM   1430  C  CD2 . HIS B  1 43  ? 64.625  -46.257 -0.675  1.00 19.37 ? 43   HIS B CD2 1 
ATOM   1431  C  CE1 . HIS B  1 43  ? 63.497  -47.810 -1.740  1.00 21.76 ? 43   HIS B CE1 1 
ATOM   1432  N  NE2 . HIS B  1 43  ? 64.537  -47.601 -0.954  1.00 22.60 ? 43   HIS B NE2 1 
ATOM   1433  N  N   . GLY B  1 44  ? 62.622  -41.723 -3.510  1.00 18.36 ? 44   GLY B N   1 
ATOM   1434  C  CA  . GLY B  1 44  ? 61.969  -40.440 -3.650  1.00 17.57 ? 44   GLY B CA  1 
ATOM   1435  C  C   . GLY B  1 44  ? 61.092  -40.157 -2.453  1.00 18.01 ? 44   GLY B C   1 
ATOM   1436  O  O   . GLY B  1 44  ? 60.443  -41.045 -1.905  1.00 15.43 ? 44   GLY B O   1 
ATOM   1437  N  N   . PHE B  1 45  ? 61.055  -38.895 -2.063  1.00 18.16 ? 45   PHE B N   1 
ATOM   1438  C  CA  . PHE B  1 45  ? 60.365  -38.501 -0.868  1.00 15.42 ? 45   PHE B CA  1 
ATOM   1439  C  C   . PHE B  1 45  ? 59.729  -37.151 -1.156  1.00 18.02 ? 45   PHE B C   1 
ATOM   1440  O  O   . PHE B  1 45  ? 60.417  -36.126 -1.217  1.00 17.09 ? 45   PHE B O   1 
ATOM   1441  C  CB  . PHE B  1 45  ? 61.394  -38.426 0.257   1.00 18.78 ? 45   PHE B CB  1 
ATOM   1442  C  CG  . PHE B  1 45  ? 60.804  -38.283 1.607   1.00 17.59 ? 45   PHE B CG  1 
ATOM   1443  C  CD1 . PHE B  1 45  ? 60.001  -39.284 2.134   1.00 17.31 ? 45   PHE B CD1 1 
ATOM   1444  C  CD2 . PHE B  1 45  ? 61.053  -37.144 2.360   1.00 17.90 ? 45   PHE B CD2 1 
ATOM   1445  C  CE1 . PHE B  1 45  ? 59.445  -39.145 3.379   1.00 17.89 ? 45   PHE B CE1 1 
ATOM   1446  C  CE2 . PHE B  1 45  ? 60.503  -36.999 3.613   1.00 17.46 ? 45   PHE B CE2 1 
ATOM   1447  C  CZ  . PHE B  1 45  ? 59.699  -38.004 4.125   1.00 18.92 ? 45   PHE B CZ  1 
ATOM   1448  N  N   . HIS B  1 46  ? 58.416  -37.163 -1.377  1.00 17.21 ? 46   HIS B N   1 
ATOM   1449  C  CA  . HIS B  1 46  ? 57.701  -35.978 -1.842  1.00 18.04 ? 46   HIS B CA  1 
ATOM   1450  C  C   . HIS B  1 46  ? 56.385  -35.753 -1.095  1.00 20.48 ? 46   HIS B C   1 
ATOM   1451  O  O   . HIS B  1 46  ? 55.742  -36.716 -0.648  1.00 16.38 ? 46   HIS B O   1 
ATOM   1452  C  CB  . HIS B  1 46  ? 57.382  -36.085 -3.335  1.00 16.31 ? 46   HIS B CB  1 
ATOM   1453  C  CG  . HIS B  1 46  ? 58.483  -36.678 -4.164  1.00 18.17 ? 46   HIS B CG  1 
ATOM   1454  N  ND1 . HIS B  1 46  ? 58.388  -37.927 -4.745  1.00 16.99 ? 46   HIS B ND1 1 
ATOM   1455  C  CD2 . HIS B  1 46  ? 59.690  -36.185 -4.531  1.00 18.65 ? 46   HIS B CD2 1 
ATOM   1456  C  CE1 . HIS B  1 46  ? 59.496  -38.182 -5.422  1.00 16.93 ? 46   HIS B CE1 1 
ATOM   1457  N  NE2 . HIS B  1 46  ? 60.302  -37.140 -5.309  1.00 16.78 ? 46   HIS B NE2 1 
ATOM   1458  N  N   . VAL B  1 47  ? 56.001  -34.478 -0.964  1.00 18.16 ? 47   VAL B N   1 
ATOM   1459  C  CA  . VAL B  1 47  ? 54.652  -34.128 -0.534  1.00 19.05 ? 47   VAL B CA  1 
ATOM   1460  C  C   . VAL B  1 47  ? 53.772  -34.133 -1.789  1.00 18.72 ? 47   VAL B C   1 
ATOM   1461  O  O   . VAL B  1 47  ? 54.089  -33.467 -2.766  1.00 18.57 ? 47   VAL B O   1 
ATOM   1462  C  CB  . VAL B  1 47  ? 54.589  -32.738 0.173   1.00 19.01 ? 47   VAL B CB  1 
ATOM   1463  C  CG1 . VAL B  1 47  ? 53.250  -32.545 0.925   1.00 15.38 ? 47   VAL B CG1 1 
ATOM   1464  C  CG2 . VAL B  1 47  ? 55.770  -32.556 1.127   1.00 18.08 ? 47   VAL B CG2 1 
ATOM   1465  N  N   . HIS B  1 48  ? 52.694  -34.911 -1.771  1.00 17.34 ? 48   HIS B N   1 
ATOM   1466  C  CA  . HIS B  1 48  ? 51.743  -34.952 -2.874  1.00 16.69 ? 48   HIS B CA  1 
ATOM   1467  C  C   . HIS B  1 48  ? 50.550  -34.053 -2.551  1.00 17.23 ? 48   HIS B C   1 
ATOM   1468  O  O   . HIS B  1 48  ? 50.324  -33.712 -1.403  1.00 15.20 ? 48   HIS B O   1 
ATOM   1469  C  CB  . HIS B  1 48  ? 51.316  -36.396 -3.155  1.00 16.98 ? 48   HIS B CB  1 
ATOM   1470  C  CG  . HIS B  1 48  ? 52.386  -37.217 -3.811  1.00 17.96 ? 48   HIS B CG  1 
ATOM   1471  N  ND1 . HIS B  1 48  ? 52.239  -37.777 -5.062  1.00 19.33 ? 48   HIS B ND1 1 
ATOM   1472  C  CD2 . HIS B  1 48  ? 53.632  -37.553 -3.398  1.00 18.17 ? 48   HIS B CD2 1 
ATOM   1473  C  CE1 . HIS B  1 48  ? 53.339  -38.431 -5.387  1.00 16.95 ? 48   HIS B CE1 1 
ATOM   1474  N  NE2 . HIS B  1 48  ? 54.203  -38.304 -4.398  1.00 17.16 ? 48   HIS B NE2 1 
ATOM   1475  N  N   . GLU B  1 49  ? 49.780  -33.673 -3.563  1.00 19.90 ? 49   GLU B N   1 
ATOM   1476  C  CA  . GLU B  1 49  ? 48.802  -32.597 -3.393  1.00 19.85 ? 49   GLU B CA  1 
ATOM   1477  C  C   . GLU B  1 49  ? 47.676  -32.850 -2.379  1.00 19.31 ? 49   GLU B C   1 
ATOM   1478  O  O   . GLU B  1 49  ? 47.410  -32.030 -1.497  1.00 16.56 ? 49   GLU B O   1 
ATOM   1479  C  CB  . GLU B  1 49  ? 48.202  -32.211 -4.741  1.00 19.09 ? 49   GLU B CB  1 
ATOM   1480  C  CG  . GLU B  1 49  ? 47.390  -30.941 -4.661  1.00 21.73 ? 49   GLU B CG  1 
ATOM   1481  C  CD  . GLU B  1 49  ? 46.865  -30.517 -6.004  1.00 22.71 ? 49   GLU B CD  1 
ATOM   1482  O  OE1 . GLU B  1 49  ? 47.320  -31.114 -6.999  1.00 24.97 ? 49   GLU B OE1 1 
ATOM   1483  O  OE2 . GLU B  1 49  ? 46.000  -29.606 -6.057  1.00 23.19 ? 49   GLU B OE2 1 
ATOM   1484  N  N   . PHE B  1 50  ? 47.012  -33.990 -2.522  1.00 20.73 ? 50   PHE B N   1 
ATOM   1485  C  CA  . PHE B  1 50  ? 45.801  -34.273 -1.765  1.00 18.26 ? 50   PHE B CA  1 
ATOM   1486  C  C   . PHE B  1 50  ? 46.048  -35.220 -0.595  1.00 15.42 ? 50   PHE B C   1 
ATOM   1487  O  O   . PHE B  1 50  ? 46.783  -36.192 -0.727  1.00 16.24 ? 50   PHE B O   1 
ATOM   1488  C  CB  . PHE B  1 50  ? 44.726  -34.838 -2.700  1.00 16.88 ? 50   PHE B CB  1 
ATOM   1489  C  CG  . PHE B  1 50  ? 44.556  -34.041 -3.948  1.00 19.53 ? 50   PHE B CG  1 
ATOM   1490  C  CD1 . PHE B  1 50  ? 44.096  -32.734 -3.888  1.00 20.11 ? 50   PHE B CD1 1 
ATOM   1491  C  CD2 . PHE B  1 50  ? 44.890  -34.578 -5.178  1.00 21.18 ? 50   PHE B CD2 1 
ATOM   1492  C  CE1 . PHE B  1 50  ? 43.961  -31.987 -5.025  1.00 22.62 ? 50   PHE B CE1 1 
ATOM   1493  C  CE2 . PHE B  1 50  ? 44.764  -33.831 -6.329  1.00 25.94 ? 50   PHE B CE2 1 
ATOM   1494  C  CZ  . PHE B  1 50  ? 44.295  -32.530 -6.250  1.00 26.06 ? 50   PHE B CZ  1 
ATOM   1495  N  N   . GLY B  1 51  ? 45.420  -34.920 0.541   1.00 14.13 ? 51   GLY B N   1 
ATOM   1496  C  CA  . GLY B  1 51  ? 45.434  -35.795 1.695   1.00 14.73 ? 51   GLY B CA  1 
ATOM   1497  C  C   . GLY B  1 51  ? 44.278  -36.775 1.596   1.00 16.56 ? 51   GLY B C   1 
ATOM   1498  O  O   . GLY B  1 51  ? 43.553  -37.025 2.562   1.00 15.79 ? 51   GLY B O   1 
ATOM   1499  N  N   . ASP B  1 52  ? 44.120  -37.326 0.400   1.00 16.31 ? 52   ASP B N   1 
ATOM   1500  C  CA  . ASP B  1 52  ? 43.033  -38.236 0.075   1.00 18.47 ? 52   ASP B CA  1 
ATOM   1501  C  C   . ASP B  1 52  ? 43.566  -39.666 -0.019  1.00 18.39 ? 52   ASP B C   1 
ATOM   1502  O  O   . ASP B  1 52  ? 44.312  -39.994 -0.929  1.00 20.34 ? 52   ASP B O   1 
ATOM   1503  C  CB  . ASP B  1 52  ? 42.402  -37.786 -1.238  1.00 14.95 ? 52   ASP B CB  1 
ATOM   1504  C  CG  . ASP B  1 52  ? 41.190  -38.578 -1.608  1.00 19.40 ? 52   ASP B CG  1 
ATOM   1505  O  OD1 . ASP B  1 52  ? 41.118  -39.766 -1.236  1.00 21.14 ? 52   ASP B OD1 1 
ATOM   1506  O  OD2 . ASP B  1 52  ? 40.312  -38.019 -2.297  1.00 21.29 ? 52   ASP B OD2 1 
ATOM   1507  N  N   . ASN B  1 53  ? 43.201  -40.514 0.939   1.00 21.28 ? 53   ASN B N   1 
ATOM   1508  C  CA  . ASN B  1 53  ? 43.696  -41.893 0.961   1.00 22.53 ? 53   ASN B CA  1 
ATOM   1509  C  C   . ASN B  1 53  ? 42.617  -42.898 0.591   1.00 22.85 ? 53   ASN B C   1 
ATOM   1510  O  O   . ASN B  1 53  ? 42.779  -44.094 0.830   1.00 24.79 ? 53   ASN B O   1 
ATOM   1511  C  CB  . ASN B  1 53  ? 44.276  -42.242 2.340   1.00 22.91 ? 53   ASN B CB  1 
ATOM   1512  C  CG  . ASN B  1 53  ? 44.944  -43.624 2.376   1.00 29.32 ? 53   ASN B CG  1 
ATOM   1513  O  OD1 . ASN B  1 53  ? 44.591  -44.485 3.196   1.00 30.97 ? 53   ASN B OD1 1 
ATOM   1514  N  ND2 . ASN B  1 53  ? 45.918  -43.833 1.499   1.00 24.60 ? 53   ASN B ND2 1 
ATOM   1515  N  N   . THR B  1 54  ? 41.520  -42.413 0.009   1.00 22.19 ? 54   THR B N   1 
ATOM   1516  C  CA  . THR B  1 54  ? 40.364  -43.262 -0.306  1.00 23.52 ? 54   THR B CA  1 
ATOM   1517  C  C   . THR B  1 54  ? 40.713  -44.429 -1.223  1.00 24.77 ? 54   THR B C   1 
ATOM   1518  O  O   . THR B  1 54  ? 40.079  -45.480 -1.162  1.00 25.71 ? 54   THR B O   1 
ATOM   1519  C  CB  . THR B  1 54  ? 39.191  -42.454 -0.919  1.00 20.81 ? 54   THR B CB  1 
ATOM   1520  O  OG1 . THR B  1 54  ? 39.658  -41.717 -2.054  1.00 22.76 ? 54   THR B OG1 1 
ATOM   1521  C  CG2 . THR B  1 54  ? 38.628  -41.477 0.101   1.00 20.80 ? 54   THR B CG2 1 
ATOM   1522  N  N   . ALA B  1 55  ? 41.733  -44.236 -2.054  1.00 25.31 ? 55   ALA B N   1 
ATOM   1523  C  CA  . ALA B  1 55  ? 42.182  -45.243 -3.008  1.00 24.59 ? 55   ALA B CA  1 
ATOM   1524  C  C   . ALA B  1 55  ? 43.657  -45.576 -2.798  1.00 24.58 ? 55   ALA B C   1 
ATOM   1525  O  O   . ALA B  1 55  ? 44.391  -45.800 -3.765  1.00 24.67 ? 55   ALA B O   1 
ATOM   1526  C  CB  . ALA B  1 55  ? 41.974  -44.731 -4.419  1.00 25.49 ? 55   ALA B CB  1 
ATOM   1527  N  N   . GLY B  1 56  ? 44.081  -45.611 -1.536  1.00 23.40 ? 56   GLY B N   1 
ATOM   1528  C  CA  . GLY B  1 56  ? 45.484  -45.769 -1.187  1.00 22.14 ? 56   GLY B CA  1 
ATOM   1529  C  C   . GLY B  1 56  ? 46.316  -44.549 -1.566  1.00 24.47 ? 56   GLY B C   1 
ATOM   1530  O  O   . GLY B  1 56  ? 45.811  -43.420 -1.614  1.00 21.94 ? 56   GLY B O   1 
ATOM   1531  N  N   . CYS B  1 57  ? 47.590  -44.780 -1.865  1.00 25.24 ? 57   CYS B N   1 
ATOM   1532  C  CA  . CYS B  1 57  ? 48.513  -43.707 -2.226  1.00 24.17 ? 57   CYS B CA  1 
ATOM   1533  C  C   . CYS B  1 57  ? 48.157  -43.023 -3.543  1.00 23.05 ? 57   CYS B C   1 
ATOM   1534  O  O   . CYS B  1 57  ? 48.519  -41.865 -3.755  1.00 23.07 ? 57   CYS B O   1 
ATOM   1535  C  CB  . CYS B  1 57  ? 49.948  -44.238 -2.305  1.00 27.59 ? 57   CYS B CB  1 
ATOM   1536  S  SG  . CYS B  1 57  ? 50.577  -44.994 -0.785  1.00 31.14 ? 57   CYS B SG  1 
ATOM   1537  N  N   . THR B  1 58  ? 47.443  -43.732 -4.418  1.00 26.23 ? 58   THR B N   1 
ATOM   1538  C  CA  . THR B  1 58  ? 47.104  -43.221 -5.755  1.00 22.84 ? 58   THR B CA  1 
ATOM   1539  C  C   . THR B  1 58  ? 46.288  -41.919 -5.751  1.00 22.98 ? 58   THR B C   1 
ATOM   1540  O  O   . THR B  1 58  ? 46.495  -41.047 -6.599  1.00 21.07 ? 58   THR B O   1 
ATOM   1541  C  CB  . THR B  1 58  ? 46.355  -44.292 -6.580  1.00 24.92 ? 58   THR B CB  1 
ATOM   1542  O  OG1 . THR B  1 58  ? 47.079  -45.527 -6.536  1.00 30.88 ? 58   THR B OG1 1 
ATOM   1543  C  CG2 . THR B  1 58  ? 46.213  -43.863 -8.020  1.00 24.24 ? 58   THR B CG2 1 
ATOM   1544  N  N   . SER B  1 59  ? 45.360  -41.790 -4.800  1.00 22.65 ? 59   SER B N   1 
ATOM   1545  C  CA  . SER B  1 59  ? 44.473  -40.627 -4.760  1.00 18.85 ? 59   SER B CA  1 
ATOM   1546  C  C   . SER B  1 59  ? 45.062  -39.392 -4.084  1.00 18.50 ? 59   SER B C   1 
ATOM   1547  O  O   . SER B  1 59  ? 44.350  -38.426 -3.833  1.00 17.67 ? 59   SER B O   1 
ATOM   1548  C  CB  . SER B  1 59  ? 43.150  -40.996 -4.122  1.00 19.19 ? 59   SER B CB  1 
ATOM   1549  O  OG  . SER B  1 59  ? 43.387  -41.896 -3.071  1.00 22.46 ? 59   SER B OG  1 
ATOM   1550  N  N   . ALA B  1 60  ? 46.366  -39.427 -3.829  1.00 20.08 ? 60   ALA B N   1 
ATOM   1551  C  CA  . ALA B  1 60  ? 47.111  -38.301 -3.271  1.00 19.65 ? 60   ALA B CA  1 
ATOM   1552  C  C   . ALA B  1 60  ? 47.509  -37.317 -4.389  1.00 20.80 ? 60   ALA B C   1 
ATOM   1553  O  O   . ALA B  1 60  ? 47.980  -36.200 -4.149  1.00 20.04 ? 60   ALA B O   1 
ATOM   1554  C  CB  . ALA B  1 60  ? 48.352  -38.811 -2.536  1.00 16.37 ? 60   ALA B CB  1 
ATOM   1555  N  N   . GLY B  1 61  ? 47.318  -37.745 -5.623  1.00 19.75 ? 61   GLY B N   1 
ATOM   1556  C  CA  . GLY B  1 61  ? 47.560  -36.873 -6.745  1.00 19.88 ? 61   GLY B CA  1 
ATOM   1557  C  C   . GLY B  1 61  ? 49.032  -36.715 -7.024  1.00 20.97 ? 61   GLY B C   1 
ATOM   1558  O  O   . GLY B  1 61  ? 49.839  -37.586 -6.664  1.00 21.13 ? 61   GLY B O   1 
ATOM   1559  N  N   . PRO B  1 62  ? 49.396  -35.595 -7.665  1.00 21.08 ? 62   PRO B N   1 
ATOM   1560  C  CA  . PRO B  1 62  ? 50.779  -35.358 -8.089  1.00 22.37 ? 62   PRO B CA  1 
ATOM   1561  C  C   . PRO B  1 62  ? 51.603  -34.676 -7.003  1.00 18.49 ? 62   PRO B C   1 
ATOM   1562  O  O   . PRO B  1 62  ? 51.048  -34.226 -6.004  1.00 18.30 ? 62   PRO B O   1 
ATOM   1563  C  CB  . PRO B  1 62  ? 50.616  -34.401 -9.285  1.00 21.94 ? 62   PRO B CB  1 
ATOM   1564  C  CG  . PRO B  1 62  ? 49.162  -33.993 -9.313  1.00 21.78 ? 62   PRO B CG  1 
ATOM   1565  C  CD  . PRO B  1 62  ? 48.515  -34.484 -8.057  1.00 20.11 ? 62   PRO B CD  1 
ATOM   1566  N  N   . HIS B  1 63  ? 52.911  -34.583 -7.210  1.00 16.93 ? 63   HIS B N   1 
ATOM   1567  C  CA  . HIS B  1 63  ? 53.740  -33.775 -6.338  1.00 17.05 ? 63   HIS B CA  1 
ATOM   1568  C  C   . HIS B  1 63  ? 53.058  -32.423 -6.170  1.00 18.29 ? 63   HIS B C   1 
ATOM   1569  O  O   . HIS B  1 63  ? 52.511  -31.868 -7.116  1.00 18.77 ? 63   HIS B O   1 
ATOM   1570  C  CB  . HIS B  1 63  ? 55.157  -33.631 -6.908  1.00 18.06 ? 63   HIS B CB  1 
ATOM   1571  C  CG  . HIS B  1 63  ? 55.881  -34.938 -7.057  1.00 16.26 ? 63   HIS B CG  1 
ATOM   1572  N  ND1 . HIS B  1 63  ? 57.233  -35.018 -7.295  1.00 17.31 ? 63   HIS B ND1 1 
ATOM   1573  C  CD2 . HIS B  1 63  ? 55.441  -36.216 -6.984  1.00 17.17 ? 63   HIS B CD2 1 
ATOM   1574  C  CE1 . HIS B  1 63  ? 57.594  -36.285 -7.376  1.00 17.08 ? 63   HIS B CE1 1 
ATOM   1575  N  NE2 . HIS B  1 63  ? 56.526  -37.035 -7.182  1.00 15.23 ? 63   HIS B NE2 1 
ATOM   1576  N  N   . PHE B  1 64  ? 53.057  -31.920 -4.945  1.00 20.24 ? 64   PHE B N   1 
ATOM   1577  C  CA  . PHE B  1 64  ? 52.393  -30.668 -4.621  1.00 19.45 ? 64   PHE B CA  1 
ATOM   1578  C  C   . PHE B  1 64  ? 53.075  -29.534 -5.384  1.00 18.78 ? 64   PHE B C   1 
ATOM   1579  O  O   . PHE B  1 64  ? 54.241  -29.236 -5.151  1.00 18.11 ? 64   PHE B O   1 
ATOM   1580  C  CB  . PHE B  1 64  ? 52.413  -30.453 -3.110  1.00 18.25 ? 64   PHE B CB  1 
ATOM   1581  C  CG  . PHE B  1 64  ? 51.843  -29.138 -2.673  1.00 18.31 ? 64   PHE B CG  1 
ATOM   1582  C  CD1 . PHE B  1 64  ? 50.668  -28.659 -3.216  1.00 16.98 ? 64   PHE B CD1 1 
ATOM   1583  C  CD2 . PHE B  1 64  ? 52.481  -28.394 -1.696  1.00 16.99 ? 64   PHE B CD2 1 
ATOM   1584  C  CE1 . PHE B  1 64  ? 50.153  -27.454 -2.805  1.00 20.60 ? 64   PHE B CE1 1 
ATOM   1585  C  CE2 . PHE B  1 64  ? 51.966  -27.189 -1.281  1.00 17.29 ? 64   PHE B CE2 1 
ATOM   1586  C  CZ  . PHE B  1 64  ? 50.804  -26.720 -1.831  1.00 17.86 ? 64   PHE B CZ  1 
ATOM   1587  N  N   . ASN B  1 65  ? 52.346  -28.926 -6.317  1.00 20.74 ? 65   ASN B N   1 
ATOM   1588  C  CA  . ASN B  1 65  ? 52.953  -27.990 -7.253  1.00 22.38 ? 65   ASN B CA  1 
ATOM   1589  C  C   . ASN B  1 65  ? 52.154  -26.700 -7.436  1.00 23.73 ? 65   ASN B C   1 
ATOM   1590  O  O   . ASN B  1 65  ? 51.724  -26.383 -8.537  1.00 26.36 ? 65   ASN B O   1 
ATOM   1591  C  CB  . ASN B  1 65  ? 53.148  -28.674 -8.606  1.00 22.06 ? 65   ASN B CB  1 
ATOM   1592  C  CG  . ASN B  1 65  ? 54.090  -27.914 -9.509  1.00 24.05 ? 65   ASN B CG  1 
ATOM   1593  O  OD1 . ASN B  1 65  ? 54.879  -27.085 -9.047  1.00 23.67 ? 65   ASN B OD1 1 
ATOM   1594  N  ND2 . ASN B  1 65  ? 54.025  -28.201 -10.804 1.00 23.50 ? 65   ASN B ND2 1 
ATOM   1595  N  N   . PRO B  1 66  ? 51.996  -25.928 -6.362  1.00 22.67 ? 66   PRO B N   1 
ATOM   1596  C  CA  . PRO B  1 66  ? 51.175  -24.715 -6.393  1.00 23.03 ? 66   PRO B CA  1 
ATOM   1597  C  C   . PRO B  1 66  ? 51.688  -23.659 -7.370  1.00 25.41 ? 66   PRO B C   1 
ATOM   1598  O  O   . PRO B  1 66  ? 50.901  -22.882 -7.881  1.00 29.73 ? 66   PRO B O   1 
ATOM   1599  C  CB  . PRO B  1 66  ? 51.286  -24.166 -4.961  1.00 25.09 ? 66   PRO B CB  1 
ATOM   1600  C  CG  . PRO B  1 66  ? 52.191  -25.107 -4.195  1.00 21.24 ? 66   PRO B CG  1 
ATOM   1601  C  CD  . PRO B  1 66  ? 52.865  -25.997 -5.176  1.00 21.57 ? 66   PRO B CD  1 
ATOM   1602  N  N   . LEU B  1 67  ? 52.991  -23.623 -7.613  1.00 27.31 ? 67   LEU B N   1 
ATOM   1603  C  CA  . LEU B  1 67  ? 53.594  -22.594 -8.456  1.00 26.52 ? 67   LEU B CA  1 
ATOM   1604  C  C   . LEU B  1 67  ? 53.843  -23.054 -9.898  1.00 29.15 ? 67   LEU B C   1 
ATOM   1605  O  O   . LEU B  1 67  ? 54.540  -22.389 -10.672 1.00 28.76 ? 67   LEU B O   1 
ATOM   1606  C  CB  . LEU B  1 67  ? 54.909  -22.142 -7.827  1.00 27.58 ? 67   LEU B CB  1 
ATOM   1607  C  CG  . LEU B  1 67  ? 54.707  -21.421 -6.503  1.00 27.55 ? 67   LEU B CG  1 
ATOM   1608  C  CD1 . LEU B  1 67  ? 56.033  -20.934 -5.972  1.00 28.79 ? 67   LEU B CD1 1 
ATOM   1609  C  CD2 . LEU B  1 67  ? 53.746  -20.261 -6.718  1.00 32.63 ? 67   LEU B CD2 1 
ATOM   1610  N  N   . SER B  1 68  ? 53.269  -24.204 -10.240 1.00 31.75 ? 68   SER B N   1 
ATOM   1611  C  CA  . SER B  1 68  ? 53.403  -24.813 -11.562 1.00 28.68 ? 68   SER B CA  1 
ATOM   1612  C  C   . SER B  1 68  ? 54.824  -24.802 -12.131 1.00 28.07 ? 68   SER B C   1 
ATOM   1613  O  O   . SER B  1 68  ? 55.074  -24.226 -13.190 1.00 29.50 ? 68   SER B O   1 
ATOM   1614  C  CB  . SER B  1 68  ? 52.398  -24.191 -12.535 1.00 28.04 ? 68   SER B CB  1 
ATOM   1615  O  OG  . SER B  1 68  ? 51.075  -24.335 -12.040 1.00 27.06 ? 68   SER B OG  1 
ATOM   1616  N  N   . ARG B  1 69  ? 55.740  -25.461 -11.420 1.00 28.70 ? 69   ARG B N   1 
ATOM   1617  C  CA  . ARG B  1 69  ? 57.126  -25.645 -11.863 1.00 26.79 ? 69   ARG B CA  1 
ATOM   1618  C  C   . ARG B  1 69  ? 57.367  -27.057 -12.388 1.00 25.00 ? 69   ARG B C   1 
ATOM   1619  O  O   . ARG B  1 69  ? 56.476  -27.907 -12.365 1.00 26.71 ? 69   ARG B O   1 
ATOM   1620  C  CB  . ARG B  1 69  ? 58.103  -25.384 -10.714 1.00 24.99 ? 69   ARG B CB  1 
ATOM   1621  C  CG  . ARG B  1 69  ? 58.072  -23.981 -10.171 1.00 28.00 ? 69   ARG B CG  1 
ATOM   1622  C  CD  . ARG B  1 69  ? 58.578  -22.986 -11.191 1.00 33.83 ? 69   ARG B CD  1 
ATOM   1623  N  NE  . ARG B  1 69  ? 58.794  -21.681 -10.582 1.00 38.84 ? 69   ARG B NE  1 
ATOM   1624  C  CZ  . ARG B  1 69  ? 59.940  -21.294 -10.032 1.00 38.84 ? 69   ARG B CZ  1 
ATOM   1625  N  NH1 . ARG B  1 69  ? 60.986  -22.111 -10.022 1.00 33.09 ? 69   ARG B NH1 1 
ATOM   1626  N  NH2 . ARG B  1 69  ? 60.044  -20.083 -9.499  1.00 37.98 ? 69   ARG B NH2 1 
ATOM   1627  N  N   . LYS B  1 70  ? 58.581  -27.293 -12.864 1.00 24.81 ? 70   LYS B N   1 
ATOM   1628  C  CA  . LYS B  1 70  ? 59.041  -28.626 -13.219 1.00 24.56 ? 70   LYS B CA  1 
ATOM   1629  C  C   . LYS B  1 70  ? 59.654  -29.308 -11.992 1.00 23.50 ? 70   LYS B C   1 
ATOM   1630  O  O   . LYS B  1 70  ? 60.076  -28.650 -11.034 1.00 22.54 ? 70   LYS B O   1 
ATOM   1631  C  CB  . LYS B  1 70  ? 60.096  -28.546 -14.327 1.00 24.20 ? 70   LYS B CB  1 
ATOM   1632  C  CG  . LYS B  1 70  ? 59.559  -28.274 -15.735 1.00 30.73 ? 70   LYS B CG  1 
ATOM   1633  C  CD  . LYS B  1 70  ? 60.711  -27.962 -16.704 1.00 31.91 ? 70   LYS B CD  1 
ATOM   1634  C  CE  . LYS B  1 70  ? 60.478  -28.529 -18.106 1.00 37.98 ? 70   LYS B CE  1 
ATOM   1635  N  NZ  . LYS B  1 70  ? 59.165  -28.139 -18.716 1.00 39.71 ? 70   LYS B NZ  1 
ATOM   1636  N  N   . HIS B  1 71  ? 59.716  -30.631 -12.037 1.00 22.20 ? 71   HIS B N   1 
ATOM   1637  C  CA  . HIS B  1 71  ? 60.294  -31.417 -10.958 1.00 21.66 ? 71   HIS B CA  1 
ATOM   1638  C  C   . HIS B  1 71  ? 61.800  -31.194 -10.770 1.00 23.25 ? 71   HIS B C   1 
ATOM   1639  O  O   . HIS B  1 71  ? 62.575  -31.193 -11.739 1.00 21.03 ? 71   HIS B O   1 
ATOM   1640  C  CB  . HIS B  1 71  ? 60.042  -32.897 -11.207 1.00 20.89 ? 71   HIS B CB  1 
ATOM   1641  C  CG  . HIS B  1 71  ? 60.632  -33.786 -10.163 1.00 20.19 ? 71   HIS B CG  1 
ATOM   1642  N  ND1 . HIS B  1 71  ? 60.034  -33.995 -8.940  1.00 19.55 ? 71   HIS B ND1 1 
ATOM   1643  C  CD2 . HIS B  1 71  ? 61.767  -34.520 -10.159 1.00 19.11 ? 71   HIS B CD2 1 
ATOM   1644  C  CE1 . HIS B  1 71  ? 60.775  -34.823 -8.226  1.00 19.25 ? 71   HIS B CE1 1 
ATOM   1645  N  NE2 . HIS B  1 71  ? 61.831  -35.154 -8.943  1.00 19.64 ? 71   HIS B NE2 1 
ATOM   1646  N  N   . GLY B  1 72  ? 62.203  -31.016 -9.513  1.00 20.89 ? 72   GLY B N   1 
ATOM   1647  C  CA  . GLY B  1 72  ? 63.599  -30.858 -9.171  1.00 20.74 ? 72   GLY B CA  1 
ATOM   1648  C  C   . GLY B  1 72  ? 63.948  -31.481 -7.829  1.00 23.87 ? 72   GLY B C   1 
ATOM   1649  O  O   . GLY B  1 72  ? 63.128  -32.153 -7.201  1.00 21.47 ? 72   GLY B O   1 
ATOM   1650  N  N   . GLY B  1 73  ? 65.187  -31.276 -7.393  1.00 23.22 ? 73   GLY B N   1 
ATOM   1651  C  CA  . GLY B  1 73  ? 65.587  -31.706 -6.074  1.00 21.95 ? 73   GLY B CA  1 
ATOM   1652  C  C   . GLY B  1 73  ? 65.396  -30.531 -5.143  1.00 22.94 ? 73   GLY B C   1 
ATOM   1653  O  O   . GLY B  1 73  ? 65.100  -29.425 -5.598  1.00 23.24 ? 73   GLY B O   1 
ATOM   1654  N  N   . PRO B  1 74  ? 65.567  -30.761 -3.837  1.00 19.50 ? 74   PRO B N   1 
ATOM   1655  C  CA  . PRO B  1 74  ? 65.297  -29.747 -2.815  1.00 21.57 ? 74   PRO B CA  1 
ATOM   1656  C  C   . PRO B  1 74  ? 66.111  -28.473 -3.020  1.00 22.72 ? 74   PRO B C   1 
ATOM   1657  O  O   . PRO B  1 74  ? 65.613  -27.375 -2.747  1.00 22.53 ? 74   PRO B O   1 
ATOM   1658  C  CB  . PRO B  1 74  ? 65.726  -30.438 -1.515  1.00 22.02 ? 74   PRO B CB  1 
ATOM   1659  C  CG  . PRO B  1 74  ? 65.697  -31.895 -1.817  1.00 23.25 ? 74   PRO B CG  1 
ATOM   1660  C  CD  . PRO B  1 74  ? 65.987  -32.051 -3.264  1.00 19.62 ? 74   PRO B CD  1 
ATOM   1661  N  N   . LYS B  1 75  ? 67.349  -28.637 -3.484  1.00 24.39 ? 75   LYS B N   1 
ATOM   1662  C  CA  . LYS B  1 75  ? 68.307  -27.540 -3.615  1.00 26.52 ? 75   LYS B CA  1 
ATOM   1663  C  C   . LYS B  1 75  ? 68.192  -26.817 -4.963  1.00 26.65 ? 75   LYS B C   1 
ATOM   1664  O  O   . LYS B  1 75  ? 68.958  -25.897 -5.254  1.00 26.73 ? 75   LYS B O   1 
ATOM   1665  C  CB  . LYS B  1 75  ? 69.741  -28.056 -3.427  1.00 27.84 ? 75   LYS B CB  1 
ATOM   1666  C  CG  . LYS B  1 75  ? 70.074  -28.597 -2.020  1.00 31.95 ? 75   LYS B CG  1 
ATOM   1667  C  CD  . LYS B  1 75  ? 70.093  -27.493 -0.933  1.00 40.91 ? 75   LYS B CD  1 
ATOM   1668  C  CE  . LYS B  1 75  ? 71.416  -26.702 -0.915  1.00 46.67 ? 75   LYS B CE  1 
ATOM   1669  N  NZ  . LYS B  1 75  ? 71.340  -25.415 -0.148  1.00 43.56 ? 75   LYS B NZ  1 
ATOM   1670  N  N   . ASP B  1 76  ? 67.238  -27.250 -5.782  1.00 24.78 ? 76   ASP B N   1 
ATOM   1671  C  CA  . ASP B  1 76  ? 66.970  -26.621 -7.067  1.00 25.26 ? 76   ASP B CA  1 
ATOM   1672  C  C   . ASP B  1 76  ? 65.981  -25.494 -6.871  1.00 25.61 ? 76   ASP B C   1 
ATOM   1673  O  O   . ASP B  1 76  ? 65.216  -25.492 -5.905  1.00 28.22 ? 76   ASP B O   1 
ATOM   1674  C  CB  . ASP B  1 76  ? 66.379  -27.633 -8.049  1.00 23.00 ? 76   ASP B CB  1 
ATOM   1675  C  CG  . ASP B  1 76  ? 67.403  -28.622 -8.553  1.00 26.80 ? 76   ASP B CG  1 
ATOM   1676  O  OD1 . ASP B  1 76  ? 68.434  -28.176 -9.095  1.00 33.47 ? 76   ASP B OD1 1 
ATOM   1677  O  OD2 . ASP B  1 76  ? 67.183  -29.844 -8.409  1.00 26.56 ? 76   ASP B OD2 1 
ATOM   1678  N  N   . GLU B  1 77  ? 65.996  -24.528 -7.778  1.00 25.34 ? 77   GLU B N   1 
ATOM   1679  C  CA  . GLU B  1 77  ? 64.999  -23.477 -7.738  1.00 27.05 ? 77   GLU B CA  1 
ATOM   1680  C  C   . GLU B  1 77  ? 63.867  -23.854 -8.669  1.00 28.25 ? 77   GLU B C   1 
ATOM   1681  O  O   . GLU B  1 77  ? 62.721  -23.441 -8.477  1.00 27.68 ? 77   GLU B O   1 
ATOM   1682  C  CB  . GLU B  1 77  ? 65.612  -22.120 -8.063  1.00 29.94 ? 77   GLU B CB  1 
ATOM   1683  C  CG  . GLU B  1 77  ? 66.635  -21.720 -7.012  1.00 33.21 ? 77   GLU B CG  1 
ATOM   1684  C  CD  . GLU B  1 77  ? 66.742  -20.233 -6.826  1.00 32.75 ? 77   GLU B CD  1 
ATOM   1685  O  OE1 . GLU B  1 77  ? 67.331  -19.592 -7.713  1.00 31.93 ? 77   GLU B OE1 1 
ATOM   1686  O  OE2 . GLU B  1 77  ? 66.252  -19.714 -5.792  1.00 34.26 ? 77   GLU B OE2 1 
ATOM   1687  N  N   . GLU B  1 78  ? 64.193  -24.678 -9.661  1.00 27.63 ? 78   GLU B N   1 
ATOM   1688  C  CA  . GLU B  1 78  ? 63.166  -25.382 -10.420 1.00 29.61 ? 78   GLU B CA  1 
ATOM   1689  C  C   . GLU B  1 78  ? 62.779  -26.655 -9.675  1.00 24.93 ? 78   GLU B C   1 
ATOM   1690  O  O   . GLU B  1 78  ? 63.521  -27.634 -9.658  1.00 22.53 ? 78   GLU B O   1 
ATOM   1691  C  CB  . GLU B  1 78  ? 63.633  -25.704 -11.841 1.00 30.31 ? 78   GLU B CB  1 
ATOM   1692  C  CG  . GLU B  1 78  ? 63.357  -24.591 -12.823 1.00 33.90 ? 78   GLU B CG  1 
ATOM   1693  C  CD  . GLU B  1 78  ? 61.888  -24.227 -12.881 1.00 34.87 ? 78   GLU B CD  1 
ATOM   1694  O  OE1 . GLU B  1 78  ? 61.083  -25.072 -13.339 1.00 30.88 ? 78   GLU B OE1 1 
ATOM   1695  O  OE2 . GLU B  1 78  ? 61.547  -23.088 -12.476 1.00 39.66 ? 78   GLU B OE2 1 
ATOM   1696  N  N   . ARG B  1 79  ? 61.609  -26.625 -9.053  1.00 25.94 ? 79   ARG B N   1 
ATOM   1697  C  CA  . ARG B  1 79  ? 61.134  -27.751 -8.259  1.00 24.57 ? 79   ARG B CA  1 
ATOM   1698  C  C   . ARG B  1 79  ? 59.662  -27.556 -7.920  1.00 22.18 ? 79   ARG B C   1 
ATOM   1699  O  O   . ARG B  1 79  ? 59.151  -26.430 -7.952  1.00 22.56 ? 79   ARG B O   1 
ATOM   1700  C  CB  . ARG B  1 79  ? 61.948  -27.872 -6.965  1.00 20.57 ? 79   ARG B CB  1 
ATOM   1701  C  CG  . ARG B  1 79  ? 61.945  -26.622 -6.101  1.00 21.43 ? 79   ARG B CG  1 
ATOM   1702  C  CD  . ARG B  1 79  ? 62.547  -26.894 -4.736  1.00 20.17 ? 79   ARG B CD  1 
ATOM   1703  N  NE  . ARG B  1 79  ? 61.558  -27.503 -3.843  1.00 22.83 ? 79   ARG B NE  1 
ATOM   1704  C  CZ  . ARG B  1 79  ? 61.722  -27.664 -2.535  1.00 18.85 ? 79   ARG B CZ  1 
ATOM   1705  N  NH1 . ARG B  1 79  ? 62.839  -27.264 -1.954  1.00 21.81 ? 79   ARG B NH1 1 
ATOM   1706  N  NH2 . ARG B  1 79  ? 60.769  -28.219 -1.809  1.00 17.81 ? 79   ARG B NH2 1 
ATOM   1707  N  N   . HIS B  1 80  ? 58.975  -28.650 -7.610  1.00 20.11 ? 80   HIS B N   1 
ATOM   1708  C  CA  . HIS B  1 80  ? 57.667  -28.535 -6.974  1.00 21.32 ? 80   HIS B CA  1 
ATOM   1709  C  C   . HIS B  1 80  ? 57.891  -28.193 -5.495  1.00 18.97 ? 80   HIS B C   1 
ATOM   1710  O  O   . HIS B  1 80  ? 58.920  -28.551 -4.924  1.00 18.72 ? 80   HIS B O   1 
ATOM   1711  C  CB  . HIS B  1 80  ? 56.870  -29.835 -7.113  1.00 19.88 ? 80   HIS B CB  1 
ATOM   1712  C  CG  . HIS B  1 80  ? 56.786  -30.351 -8.517  1.00 21.34 ? 80   HIS B CG  1 
ATOM   1713  N  ND1 . HIS B  1 80  ? 57.089  -31.652 -8.854  1.00 19.26 ? 80   HIS B ND1 1 
ATOM   1714  C  CD2 . HIS B  1 80  ? 56.425  -29.743 -9.671  1.00 21.57 ? 80   HIS B CD2 1 
ATOM   1715  C  CE1 . HIS B  1 80  ? 56.919  -31.826 -10.150 1.00 18.84 ? 80   HIS B CE1 1 
ATOM   1716  N  NE2 . HIS B  1 80  ? 56.514  -30.682 -10.669 1.00 20.21 ? 80   HIS B NE2 1 
ATOM   1717  N  N   . VAL B  1 81  ? 56.947  -27.492 -4.877  1.00 18.80 ? 81   VAL B N   1 
ATOM   1718  C  CA  . VAL B  1 81  ? 57.036  -27.215 -3.448  1.00 17.96 ? 81   VAL B CA  1 
ATOM   1719  C  C   . VAL B  1 81  ? 57.244  -28.537 -2.698  1.00 17.82 ? 81   VAL B C   1 
ATOM   1720  O  O   . VAL B  1 81  ? 57.955  -28.607 -1.695  1.00 18.15 ? 81   VAL B O   1 
ATOM   1721  C  CB  . VAL B  1 81  ? 55.777  -26.443 -2.957  1.00 18.48 ? 81   VAL B CB  1 
ATOM   1722  C  CG1 . VAL B  1 81  ? 55.573  -26.557 -1.449  1.00 14.66 ? 81   VAL B CG1 1 
ATOM   1723  C  CG2 . VAL B  1 81  ? 55.863  -24.980 -3.385  1.00 20.88 ? 81   VAL B CG2 1 
ATOM   1724  N  N   . GLY B  1 82  ? 56.647  -29.601 -3.219  1.00 18.63 ? 82   GLY B N   1 
ATOM   1725  C  CA  . GLY B  1 82  ? 56.664  -30.889 -2.547  1.00 15.24 ? 82   GLY B CA  1 
ATOM   1726  C  C   . GLY B  1 82  ? 57.883  -31.733 -2.817  1.00 16.78 ? 82   GLY B C   1 
ATOM   1727  O  O   . GLY B  1 82  ? 57.914  -32.901 -2.460  1.00 19.40 ? 82   GLY B O   1 
ATOM   1728  N  N   . ASP B  1 83  ? 58.893  -31.141 -3.443  1.00 19.22 ? 83   ASP B N   1 
ATOM   1729  C  CA  . ASP B  1 83  ? 60.108  -31.866 -3.814  1.00 19.50 ? 83   ASP B CA  1 
ATOM   1730  C  C   . ASP B  1 83  ? 61.141  -31.873 -2.701  1.00 19.34 ? 83   ASP B C   1 
ATOM   1731  O  O   . ASP B  1 83  ? 61.839  -30.879 -2.485  1.00 18.36 ? 83   ASP B O   1 
ATOM   1732  C  CB  . ASP B  1 83  ? 60.712  -31.287 -5.097  1.00 18.92 ? 83   ASP B CB  1 
ATOM   1733  C  CG  . ASP B  1 83  ? 59.942  -31.707 -6.321  1.00 21.13 ? 83   ASP B CG  1 
ATOM   1734  O  OD1 . ASP B  1 83  ? 59.181  -32.682 -6.196  1.00 21.83 ? 83   ASP B OD1 1 
ATOM   1735  O  OD2 . ASP B  1 83  ? 60.073  -31.078 -7.391  1.00 19.75 ? 83   ASP B OD2 1 
ATOM   1736  N  N   . LEU B  1 84  ? 61.220  -33.005 -2.005  1.00 19.60 ? 84   LEU B N   1 
ATOM   1737  C  CA  . LEU B  1 84  ? 62.129  -33.169 -0.875  1.00 18.87 ? 84   LEU B CA  1 
ATOM   1738  C  C   . LEU B  1 84  ? 63.328  -34.076 -1.205  1.00 19.34 ? 84   LEU B C   1 
ATOM   1739  O  O   . LEU B  1 84  ? 64.173  -34.347 -0.349  1.00 21.92 ? 84   LEU B O   1 
ATOM   1740  C  CB  . LEU B  1 84  ? 61.370  -33.669 0.367   1.00 16.62 ? 84   LEU B CB  1 
ATOM   1741  C  CG  . LEU B  1 84  ? 60.390  -32.687 1.014   1.00 19.37 ? 84   LEU B CG  1 
ATOM   1742  C  CD1 . LEU B  1 84  ? 59.782  -33.266 2.285   1.00 20.10 ? 84   LEU B CD1 1 
ATOM   1743  C  CD2 . LEU B  1 84  ? 61.070  -31.356 1.313   1.00 18.35 ? 84   LEU B CD2 1 
ATOM   1744  N  N   . GLY B  1 85  ? 63.411  -34.524 -2.450  1.00 17.38 ? 85   GLY B N   1 
ATOM   1745  C  CA  . GLY B  1 85  ? 64.541  -35.311 -2.904  1.00 19.03 ? 85   GLY B CA  1 
ATOM   1746  C  C   . GLY B  1 85  ? 64.485  -36.758 -2.455  1.00 18.97 ? 85   GLY B C   1 
ATOM   1747  O  O   . GLY B  1 85  ? 63.424  -37.376 -2.427  1.00 18.80 ? 85   GLY B O   1 
ATOM   1748  N  N   . ASN B  1 86  ? 65.644  -37.302 -2.108  1.00 20.17 ? 86   ASN B N   1 
ATOM   1749  C  CA  . ASN B  1 86  ? 65.739  -38.684 -1.661  1.00 19.43 ? 86   ASN B CA  1 
ATOM   1750  C  C   . ASN B  1 86  ? 65.947  -38.858 -0.172  1.00 17.46 ? 86   ASN B C   1 
ATOM   1751  O  O   . ASN B  1 86  ? 66.464  -37.971 0.524   1.00 14.84 ? 86   ASN B O   1 
ATOM   1752  C  CB  . ASN B  1 86  ? 66.876  -39.399 -2.379  1.00 19.13 ? 86   ASN B CB  1 
ATOM   1753  C  CG  . ASN B  1 86  ? 66.606  -39.574 -3.828  1.00 18.69 ? 86   ASN B CG  1 
ATOM   1754  O  OD1 . ASN B  1 86  ? 65.639  -40.222 -4.218  1.00 18.56 ? 86   ASN B OD1 1 
ATOM   1755  N  ND2 . ASN B  1 86  ? 67.452  -38.993 -4.650  1.00 20.38 ? 86   ASN B ND2 1 
ATOM   1756  N  N   . VAL B  1 87  ? 65.533  -40.026 0.300   1.00 15.95 ? 87   VAL B N   1 
ATOM   1757  C  CA  . VAL B  1 87  ? 65.914  -40.505 1.610   1.00 19.03 ? 87   VAL B CA  1 
ATOM   1758  C  C   . VAL B  1 87  ? 66.688  -41.793 1.356   1.00 17.99 ? 87   VAL B C   1 
ATOM   1759  O  O   . VAL B  1 87  ? 66.489  -42.438 0.339   1.00 16.90 ? 87   VAL B O   1 
ATOM   1760  C  CB  . VAL B  1 87  ? 64.704  -40.751 2.546   1.00 18.27 ? 87   VAL B CB  1 
ATOM   1761  C  CG1 . VAL B  1 87  ? 63.979  -39.438 2.858   1.00 15.66 ? 87   VAL B CG1 1 
ATOM   1762  C  CG2 . VAL B  1 87  ? 63.766  -41.790 1.953   1.00 14.68 ? 87   VAL B CG2 1 
ATOM   1763  N  N   . THR B  1 88  ? 67.584  -42.142 2.277   1.00 21.47 ? 88   THR B N   1 
ATOM   1764  C  CA  . THR B  1 88  ? 68.550  -43.215 2.063   1.00 21.36 ? 88   THR B CA  1 
ATOM   1765  C  C   . THR B  1 88  ? 68.326  -44.337 3.067   1.00 20.94 ? 88   THR B C   1 
ATOM   1766  O  O   . THR B  1 88  ? 68.457  -44.120 4.268   1.00 20.50 ? 88   THR B O   1 
ATOM   1767  C  CB  . THR B  1 88  ? 69.990  -42.674 2.238   1.00 22.00 ? 88   THR B CB  1 
ATOM   1768  O  OG1 . THR B  1 88  ? 70.180  -41.527 1.396   1.00 18.84 ? 88   THR B OG1 1 
ATOM   1769  C  CG2 . THR B  1 88  ? 71.035  -43.744 1.916   1.00 20.82 ? 88   THR B CG2 1 
ATOM   1770  N  N   . ALA B  1 89  ? 67.975  -45.528 2.578   1.00 21.75 ? 89   ALA B N   1 
ATOM   1771  C  CA  . ALA B  1 89  ? 67.850  -46.708 3.438   1.00 22.41 ? 89   ALA B CA  1 
ATOM   1772  C  C   . ALA B  1 89  ? 69.172  -47.473 3.491   1.00 23.67 ? 89   ALA B C   1 
ATOM   1773  O  O   . ALA B  1 89  ? 69.852  -47.636 2.466   1.00 25.73 ? 89   ALA B O   1 
ATOM   1774  C  CB  . ALA B  1 89  ? 66.730  -47.616 2.946   1.00 22.12 ? 89   ALA B CB  1 
ATOM   1775  N  N   . GLY B  1 90  ? 69.544  -47.924 4.685   1.00 25.56 ? 90   GLY B N   1 
ATOM   1776  C  CA  . GLY B  1 90  ? 70.748  -48.722 4.871   1.00 24.77 ? 90   GLY B CA  1 
ATOM   1777  C  C   . GLY B  1 90  ? 70.462  -50.184 4.582   1.00 27.23 ? 90   GLY B C   1 
ATOM   1778  O  O   . GLY B  1 90  ? 69.328  -50.526 4.205   1.00 25.18 ? 90   GLY B O   1 
ATOM   1779  N  N   . LYS B  1 91  ? 71.477  -51.040 4.738   1.00 27.82 ? 91   LYS B N   1 
ATOM   1780  C  CA  . LYS B  1 91  ? 71.307  -52.482 4.536   1.00 28.12 ? 91   LYS B CA  1 
ATOM   1781  C  C   . LYS B  1 91  ? 70.200  -52.949 5.479   1.00 29.58 ? 91   LYS B C   1 
ATOM   1782  O  O   . LYS B  1 91  ? 69.512  -53.943 5.239   1.00 31.38 ? 91   LYS B O   1 
ATOM   1783  C  CB  . LYS B  1 91  ? 72.621  -53.228 4.811   1.00 27.17 ? 91   LYS B CB  1 
ATOM   1784  C  CG  . LYS B  1 91  ? 72.586  -54.728 4.486   1.00 27.34 ? 91   LYS B CG  1 
ATOM   1785  C  CD  . LYS B  1 91  ? 73.853  -55.441 4.967   1.00 26.53 ? 91   LYS B CD  1 
ATOM   1786  C  CE  . LYS B  1 91  ? 75.117  -54.829 4.374   1.00 29.81 ? 91   LYS B CE  1 
ATOM   1787  N  NZ  . LYS B  1 91  ? 76.376  -55.550 4.764   1.00 25.92 ? 91   LYS B NZ  1 
ATOM   1788  N  N   . ASP B  1 92  ? 70.054  -52.185 6.553   1.00 28.78 ? 92   ASP B N   1 
ATOM   1789  C  CA  . ASP B  1 92  ? 69.008  -52.317 7.553   1.00 29.60 ? 92   ASP B CA  1 
ATOM   1790  C  C   . ASP B  1 92  ? 67.581  -52.315 6.977   1.00 27.01 ? 92   ASP B C   1 
ATOM   1791  O  O   . ASP B  1 92  ? 66.700  -53.009 7.471   1.00 27.52 ? 92   ASP B O   1 
ATOM   1792  C  CB  . ASP B  1 92  ? 69.152  -51.124 8.509   1.00 30.05 ? 92   ASP B CB  1 
ATOM   1793  C  CG  . ASP B  1 92  ? 68.716  -51.444 9.902   1.00 36.77 ? 92   ASP B CG  1 
ATOM   1794  O  OD1 . ASP B  1 92  ? 68.216  -52.574 10.120  1.00 39.81 ? 92   ASP B OD1 1 
ATOM   1795  O  OD2 . ASP B  1 92  ? 68.872  -50.566 10.778  1.00 41.20 ? 92   ASP B OD2 1 
ATOM   1796  N  N   . GLY B  1 93  ? 67.344  -51.509 5.949   1.00 24.61 ? 93   GLY B N   1 
ATOM   1797  C  CA  . GLY B  1 93  ? 65.991  -51.280 5.478   1.00 24.68 ? 93   GLY B CA  1 
ATOM   1798  C  C   . GLY B  1 93  ? 65.346  -50.084 6.161   1.00 22.69 ? 93   GLY B C   1 
ATOM   1799  O  O   . GLY B  1 93  ? 64.196  -49.740 5.897   1.00 23.40 ? 93   GLY B O   1 
ATOM   1800  N  N   . VAL B  1 94  ? 66.096  -49.444 7.045   1.00 23.00 ? 94   VAL B N   1 
ATOM   1801  C  CA  . VAL B  1 94  ? 65.628  -48.240 7.717   1.00 23.90 ? 94   VAL B CA  1 
ATOM   1802  C  C   . VAL B  1 94  ? 66.266  -47.003 7.089   1.00 22.44 ? 94   VAL B C   1 
ATOM   1803  O  O   . VAL B  1 94  ? 67.483  -46.958 6.897   1.00 21.98 ? 94   VAL B O   1 
ATOM   1804  C  CB  . VAL B  1 94  ? 65.967  -48.260 9.223   1.00 24.63 ? 94   VAL B CB  1 
ATOM   1805  C  CG1 . VAL B  1 94  ? 65.493  -46.971 9.894   1.00 24.89 ? 94   VAL B CG1 1 
ATOM   1806  C  CG2 . VAL B  1 94  ? 65.361  -49.489 9.894   1.00 24.63 ? 94   VAL B CG2 1 
ATOM   1807  N  N   . ALA B  1 95  ? 65.433  -46.024 6.745   1.00 21.21 ? 95   ALA B N   1 
ATOM   1808  C  CA  . ALA B  1 95  ? 65.909  -44.708 6.346   1.00 19.37 ? 95   ALA B CA  1 
ATOM   1809  C  C   . ALA B  1 95  ? 65.667  -43.748 7.488   1.00 19.47 ? 95   ALA B C   1 
ATOM   1810  O  O   . ALA B  1 95  ? 64.534  -43.501 7.866   1.00 20.84 ? 95   ALA B O   1 
ATOM   1811  C  CB  . ALA B  1 95  ? 65.192  -44.226 5.108   1.00 18.06 ? 95   ALA B CB  1 
ATOM   1812  N  N   . ASN B  1 96  ? 66.740  -43.231 8.061   1.00 22.35 ? 96   ASN B N   1 
ATOM   1813  C  CA  . ASN B  1 96  ? 66.616  -42.175 9.039   1.00 21.83 ? 96   ASN B CA  1 
ATOM   1814  C  C   . ASN B  1 96  ? 66.544  -40.878 8.265   1.00 20.31 ? 96   ASN B C   1 
ATOM   1815  O  O   . ASN B  1 96  ? 67.491  -40.480 7.612   1.00 23.06 ? 96   ASN B O   1 
ATOM   1816  C  CB  . ASN B  1 96  ? 67.795  -42.194 10.009  1.00 24.82 ? 96   ASN B CB  1 
ATOM   1817  C  CG  . ASN B  1 96  ? 68.123  -43.602 10.484  1.00 29.58 ? 96   ASN B CG  1 
ATOM   1818  O  OD1 . ASN B  1 96  ? 67.294  -44.271 11.115  1.00 28.45 ? 96   ASN B OD1 1 
ATOM   1819  N  ND2 . ASN B  1 96  ? 69.331  -44.070 10.157  1.00 31.59 ? 96   ASN B ND2 1 
ATOM   1820  N  N   . VAL B  1 97  ? 65.387  -40.248 8.303   1.00 19.72 ? 97   VAL B N   1 
ATOM   1821  C  CA  . VAL B  1 97  ? 65.145  -39.035 7.550   1.00 18.58 ? 97   VAL B CA  1 
ATOM   1822  C  C   . VAL B  1 97  ? 65.534  -37.841 8.410   1.00 21.45 ? 97   VAL B C   1 
ATOM   1823  O  O   . VAL B  1 97  ? 65.136  -37.751 9.583   1.00 22.44 ? 97   VAL B O   1 
ATOM   1824  C  CB  . VAL B  1 97  ? 63.648  -38.935 7.172   1.00 18.17 ? 97   VAL B CB  1 
ATOM   1825  C  CG1 . VAL B  1 97  ? 63.318  -37.587 6.553   1.00 17.97 ? 97   VAL B CG1 1 
ATOM   1826  C  CG2 . VAL B  1 97  ? 63.256  -40.084 6.256   1.00 18.66 ? 97   VAL B CG2 1 
ATOM   1827  N  N   . SER B  1 98  ? 66.336  -36.941 7.850   1.00 19.95 ? 98   SER B N   1 
ATOM   1828  C  CA  . SER B  1 98  ? 66.536  -35.633 8.469   1.00 21.82 ? 98   SER B CA  1 
ATOM   1829  C  C   . SER B  1 98  ? 66.702  -34.540 7.420   1.00 21.28 ? 98   SER B C   1 
ATOM   1830  O  O   . SER B  1 98  ? 67.771  -34.374 6.846   1.00 23.80 ? 98   SER B O   1 
ATOM   1831  C  CB  . SER B  1 98  ? 67.714  -35.625 9.440   1.00 21.70 ? 98   SER B CB  1 
ATOM   1832  O  OG  . SER B  1 98  ? 67.705  -34.407 10.170  1.00 24.97 ? 98   SER B OG  1 
ATOM   1833  N  N   . ILE B  1 99  ? 65.639  -33.789 7.174   1.00 20.46 ? 99   ILE B N   1 
ATOM   1834  C  CA  . ILE B  1 99  ? 65.666  -32.800 6.113   1.00 22.08 ? 99   ILE B CA  1 
ATOM   1835  C  C   . ILE B  1 99  ? 65.314  -31.432 6.693   1.00 20.95 ? 99   ILE B C   1 
ATOM   1836  O  O   . ILE B  1 99  ? 64.548  -31.331 7.635   1.00 21.42 ? 99   ILE B O   1 
ATOM   1837  C  CB  . ILE B  1 99  ? 64.726  -33.226 4.931   1.00 22.49 ? 99   ILE B CB  1 
ATOM   1838  C  CG1 . ILE B  1 99  ? 65.259  -34.499 4.257   1.00 20.38 ? 99   ILE B CG1 1 
ATOM   1839  C  CG2 . ILE B  1 99  ? 64.581  -32.123 3.892   1.00 20.94 ? 99   ILE B CG2 1 
ATOM   1840  C  CD1 . ILE B  1 99  ? 64.334  -35.105 3.222   1.00 17.17 ? 99   ILE B CD1 1 
ATOM   1841  N  N   . GLU B  1 100 ? 65.915  -30.384 6.150   1.00 23.95 ? 100  GLU B N   1 
ATOM   1842  C  CA  . GLU B  1 100 ? 65.533  -29.012 6.471   1.00 24.24 ? 100  GLU B CA  1 
ATOM   1843  C  C   . GLU B  1 100 ? 65.186  -28.313 5.159   1.00 23.10 ? 100  GLU B C   1 
ATOM   1844  O  O   . GLU B  1 100 ? 65.983  -28.331 4.216   1.00 22.54 ? 100  GLU B O   1 
ATOM   1845  C  CB  . GLU B  1 100 ? 66.687  -28.291 7.169   1.00 31.17 ? 100  GLU B CB  1 
ATOM   1846  C  CG  . GLU B  1 100 ? 66.321  -26.949 7.754   1.00 33.64 ? 100  GLU B CG  1 
ATOM   1847  C  CD  . GLU B  1 100 ? 67.277  -26.536 8.859   1.00 44.60 ? 100  GLU B CD  1 
ATOM   1848  O  OE1 . GLU B  1 100 ? 67.548  -27.382 9.747   1.00 46.84 ? 100  GLU B OE1 1 
ATOM   1849  O  OE2 . GLU B  1 100 ? 67.746  -25.371 8.842   1.00 42.99 ? 100  GLU B OE2 1 
ATOM   1850  N  N   . ASP B  1 101 ? 63.995  -27.720 5.088   1.00 21.38 ? 101  ASP B N   1 
ATOM   1851  C  CA  . ASP B  1 101 ? 63.510  -27.135 3.842   1.00 19.93 ? 101  ASP B CA  1 
ATOM   1852  C  C   . ASP B  1 101 ? 62.758  -25.820 4.044   1.00 19.93 ? 101  ASP B C   1 
ATOM   1853  O  O   . ASP B  1 101 ? 61.911  -25.720 4.926   1.00 19.82 ? 101  ASP B O   1 
ATOM   1854  C  CB  . ASP B  1 101 ? 62.604  -28.127 3.116   1.00 16.25 ? 101  ASP B CB  1 
ATOM   1855  C  CG  . ASP B  1 101 ? 62.449  -27.797 1.660   1.00 18.75 ? 101  ASP B CG  1 
ATOM   1856  O  OD1 . ASP B  1 101 ? 63.400  -28.073 0.900   1.00 21.19 ? 101  ASP B OD1 1 
ATOM   1857  O  OD2 . ASP B  1 101 ? 61.395  -27.247 1.273   1.00 19.04 ? 101  ASP B OD2 1 
ATOM   1858  N  N   . ARG B  1 102 ? 63.041  -24.833 3.196   1.00 20.84 ? 102  ARG B N   1 
ATOM   1859  C  CA  . ARG B  1 102 ? 62.432  -23.506 3.315   1.00 20.75 ? 102  ARG B CA  1 
ATOM   1860  C  C   . ARG B  1 102 ? 61.264  -23.288 2.357   1.00 22.42 ? 102  ARG B C   1 
ATOM   1861  O  O   . ARG B  1 102 ? 60.582  -22.263 2.440   1.00 25.26 ? 102  ARG B O   1 
ATOM   1862  C  CB  . ARG B  1 102 ? 63.475  -22.406 3.092   1.00 21.09 ? 102  ARG B CB  1 
ATOM   1863  C  CG  . ARG B  1 102 ? 64.681  -22.484 4.017   1.00 23.80 ? 102  ARG B CG  1 
ATOM   1864  C  CD  . ARG B  1 102 ? 65.656  -21.324 3.792   1.00 24.38 ? 102  ARG B CD  1 
ATOM   1865  N  NE  . ARG B  1 102 ? 66.849  -21.453 4.626   1.00 29.94 ? 102  ARG B NE  1 
ATOM   1866  C  CZ  . ARG B  1 102 ? 67.008  -20.877 5.817   1.00 25.69 ? 102  ARG B CZ  1 
ATOM   1867  N  NH1 . ARG B  1 102 ? 66.057  -20.112 6.338   1.00 23.23 ? 102  ARG B NH1 1 
ATOM   1868  N  NH2 . ARG B  1 102 ? 68.129  -21.062 6.485   1.00 30.85 ? 102  ARG B NH2 1 
ATOM   1869  N  N   . VAL B  1 103 ? 61.031  -24.242 1.453   1.00 20.51 ? 103  VAL B N   1 
ATOM   1870  C  CA  . VAL B  1 103 ? 59.977  -24.102 0.447   1.00 19.61 ? 103  VAL B CA  1 
ATOM   1871  C  C   . VAL B  1 103 ? 58.628  -24.662 0.938   1.00 20.41 ? 103  VAL B C   1 
ATOM   1872  O  O   . VAL B  1 103 ? 57.595  -23.995 0.844   1.00 18.95 ? 103  VAL B O   1 
ATOM   1873  C  CB  . VAL B  1 103 ? 60.423  -24.675 -0.944  1.00 20.95 ? 103  VAL B CB  1 
ATOM   1874  C  CG1 . VAL B  1 103 ? 59.330  -24.515 -1.986  1.00 18.89 ? 103  VAL B CG1 1 
ATOM   1875  C  CG2 . VAL B  1 103 ? 61.685  -23.969 -1.415  1.00 17.97 ? 103  VAL B CG2 1 
ATOM   1876  N  N   . ILE B  1 104 ? 58.634  -25.877 1.478   1.00 20.09 ? 104  ILE B N   1 
ATOM   1877  C  CA  . ILE B  1 104 ? 57.444  -26.368 2.150   1.00 18.26 ? 104  ILE B CA  1 
ATOM   1878  C  C   . ILE B  1 104 ? 57.188  -25.444 3.335   1.00 19.60 ? 104  ILE B C   1 
ATOM   1879  O  O   . ILE B  1 104 ? 58.110  -24.794 3.825   1.00 20.09 ? 104  ILE B O   1 
ATOM   1880  C  CB  . ILE B  1 104 ? 57.581  -27.841 2.641   1.00 16.69 ? 104  ILE B CB  1 
ATOM   1881  C  CG1 . ILE B  1 104 ? 58.704  -27.976 3.669   1.00 14.99 ? 104  ILE B CG1 1 
ATOM   1882  C  CG2 . ILE B  1 104 ? 57.782  -28.797 1.474   1.00 13.65 ? 104  ILE B CG2 1 
ATOM   1883  C  CD1 . ILE B  1 104 ? 58.748  -29.328 4.359   1.00 14.92 ? 104  ILE B CD1 1 
ATOM   1884  N  N   . SER B  1 105 ? 55.935  -25.369 3.776   1.00 21.66 ? 105  SER B N   1 
ATOM   1885  C  CA  . SER B  1 105 ? 55.577  -24.630 4.983   1.00 20.53 ? 105  SER B CA  1 
ATOM   1886  C  C   . SER B  1 105 ? 54.519  -25.422 5.712   1.00 18.81 ? 105  SER B C   1 
ATOM   1887  O  O   . SER B  1 105 ? 53.985  -26.369 5.158   1.00 18.86 ? 105  SER B O   1 
ATOM   1888  C  CB  . SER B  1 105 ? 55.041  -23.239 4.640   1.00 21.08 ? 105  SER B CB  1 
ATOM   1889  O  OG  . SER B  1 105 ? 54.891  -22.456 5.811   1.00 21.18 ? 105  SER B OG  1 
ATOM   1890  N  N   . LEU B  1 106 ? 54.240  -25.046 6.960   1.00 21.99 ? 106  LEU B N   1 
ATOM   1891  C  CA  . LEU B  1 106 ? 53.135  -25.624 7.733   1.00 22.30 ? 106  LEU B CA  1 
ATOM   1892  C  C   . LEU B  1 106 ? 51.992  -24.613 7.934   1.00 22.40 ? 106  LEU B C   1 
ATOM   1893  O  O   . LEU B  1 106 ? 51.082  -24.837 8.721   1.00 22.48 ? 106  LEU B O   1 
ATOM   1894  C  CB  . LEU B  1 106 ? 53.623  -26.158 9.081   1.00 20.79 ? 106  LEU B CB  1 
ATOM   1895  C  CG  . LEU B  1 106 ? 54.777  -27.171 9.063   1.00 20.44 ? 106  LEU B CG  1 
ATOM   1896  C  CD1 . LEU B  1 106 ? 55.122  -27.616 10.465  1.00 20.16 ? 106  LEU B CD1 1 
ATOM   1897  C  CD2 . LEU B  1 106 ? 54.463  -28.374 8.187   1.00 17.58 ? 106  LEU B CD2 1 
ATOM   1898  N  N   . SER B  1 107 ? 52.049  -23.504 7.206   1.00 21.97 ? 107  SER B N   1 
ATOM   1899  C  CA  . SER B  1 107 ? 50.992  -22.505 7.239   1.00 26.08 ? 107  SER B CA  1 
ATOM   1900  C  C   . SER B  1 107 ? 50.926  -21.735 5.916   1.00 25.17 ? 107  SER B C   1 
ATOM   1901  O  O   . SER B  1 107 ? 51.903  -21.669 5.178   1.00 27.05 ? 107  SER B O   1 
ATOM   1902  C  CB  . SER B  1 107 ? 51.231  -21.526 8.382   1.00 24.81 ? 107  SER B CB  1 
ATOM   1903  O  OG  . SER B  1 107 ? 52.277  -20.630 8.055   1.00 28.66 ? 107  SER B OG  1 
ATOM   1904  N  N   . GLY B  1 108 ? 49.774  -21.154 5.614   1.00 23.71 ? 108  GLY B N   1 
ATOM   1905  C  CA  . GLY B  1 108 ? 49.652  -20.327 4.431   1.00 26.96 ? 108  GLY B CA  1 
ATOM   1906  C  C   . GLY B  1 108 ? 49.466  -21.124 3.150   1.00 29.94 ? 108  GLY B C   1 
ATOM   1907  O  O   . GLY B  1 108 ? 49.063  -22.291 3.185   1.00 31.06 ? 108  GLY B O   1 
ATOM   1908  N  N   . GLU B  1 109 ? 49.762  -20.494 2.013   1.00 31.46 ? 109  GLU B N   1 
ATOM   1909  C  CA  . GLU B  1 109 ? 49.471  -21.072 0.697   1.00 26.39 ? 109  GLU B CA  1 
ATOM   1910  C  C   . GLU B  1 109 ? 50.303  -22.319 0.379   1.00 28.68 ? 109  GLU B C   1 
ATOM   1911  O  O   . GLU B  1 109 ? 49.828  -23.220 -0.311  1.00 29.95 ? 109  GLU B O   1 
ATOM   1912  C  CB  . GLU B  1 109 ? 49.625  -20.013 -0.406  1.00 29.11 ? 109  GLU B CB  1 
ATOM   1913  C  CG  . GLU B  1 109 ? 51.066  -19.709 -0.794  1.00 34.55 ? 109  GLU B CG  1 
ATOM   1914  C  CD  . GLU B  1 109 ? 51.183  -18.780 -1.995  1.00 36.43 ? 109  GLU B CD  1 
ATOM   1915  O  OE1 . GLU B  1 109 ? 51.364  -17.563 -1.787  1.00 31.99 ? 109  GLU B OE1 1 
ATOM   1916  O  OE2 . GLU B  1 109 ? 51.096  -19.274 -3.147  1.00 44.53 ? 109  GLU B OE2 1 
ATOM   1917  N  N   . HIS B  1 110 ? 51.536  -22.372 0.881   1.00 29.16 ? 110  HIS B N   1 
ATOM   1918  C  CA  . HIS B  1 110 ? 52.408  -23.528 0.658   1.00 28.02 ? 110  HIS B CA  1 
ATOM   1919  C  C   . HIS B  1 110 ? 52.368  -24.524 1.805   1.00 22.62 ? 110  HIS B C   1 
ATOM   1920  O  O   . HIS B  1 110 ? 53.272  -25.345 1.946   1.00 21.48 ? 110  HIS B O   1 
ATOM   1921  C  CB  . HIS B  1 110 ? 53.866  -23.103 0.388   1.00 28.09 ? 110  HIS B CB  1 
ATOM   1922  C  CG  . HIS B  1 110 ? 54.054  -22.362 -0.904  1.00 32.29 ? 110  HIS B CG  1 
ATOM   1923  N  ND1 . HIS B  1 110 ? 53.069  -22.283 -1.873  1.00 30.80 ? 110  HIS B ND1 1 
ATOM   1924  C  CD2 . HIS B  1 110 ? 55.115  -21.679 -1.395  1.00 30.78 ? 110  HIS B CD2 1 
ATOM   1925  C  CE1 . HIS B  1 110 ? 53.513  -21.568 -2.888  1.00 31.99 ? 110  HIS B CE1 1 
ATOM   1926  N  NE2 . HIS B  1 110 ? 54.751  -21.188 -2.623  1.00 30.27 ? 110  HIS B NE2 1 
ATOM   1927  N  N   . SER B  1 111 ? 51.329  -24.450 2.625   1.00 22.29 ? 111  SER B N   1 
ATOM   1928  C  CA  . SER B  1 111 ? 51.185  -25.402 3.716   1.00 22.90 ? 111  SER B CA  1 
ATOM   1929  C  C   . SER B  1 111 ? 50.968  -26.824 3.194   1.00 22.05 ? 111  SER B C   1 
ATOM   1930  O  O   . SER B  1 111 ? 50.248  -27.060 2.220   1.00 22.22 ? 111  SER B O   1 
ATOM   1931  C  CB  . SER B  1 111 ? 50.042  -25.011 4.657   1.00 22.74 ? 111  SER B CB  1 
ATOM   1932  O  OG  . SER B  1 111 ? 49.855  -26.002 5.653   1.00 19.81 ? 111  SER B OG  1 
ATOM   1933  N  N   . ILE B  1 112 ? 51.598  -27.770 3.872   1.00 22.27 ? 112  ILE B N   1 
ATOM   1934  C  CA  . ILE B  1 112 ? 51.502  -29.177 3.527   1.00 19.23 ? 112  ILE B CA  1 
ATOM   1935  C  C   . ILE B  1 112 ? 50.654  -29.880 4.581   1.00 17.58 ? 112  ILE B C   1 
ATOM   1936  O  O   . ILE B  1 112 ? 50.557  -31.099 4.588   1.00 16.51 ? 112  ILE B O   1 
ATOM   1937  C  CB  . ILE B  1 112 ? 52.903  -29.806 3.483   1.00 20.09 ? 112  ILE B CB  1 
ATOM   1938  C  CG1 . ILE B  1 112 ? 53.581  -29.659 4.854   1.00 17.68 ? 112  ILE B CG1 1 
ATOM   1939  C  CG2 . ILE B  1 112 ? 53.747  -29.141 2.387   1.00 16.21 ? 112  ILE B CG2 1 
ATOM   1940  C  CD1 . ILE B  1 112 ? 54.881  -30.405 5.009   1.00 14.74 ? 112  ILE B CD1 1 
ATOM   1941  N  N   . ILE B  1 113 ? 50.056  -29.107 5.486   1.00 17.19 ? 113  ILE B N   1 
ATOM   1942  C  CA  . ILE B  1 113 ? 49.109  -29.677 6.431   1.00 18.64 ? 113  ILE B CA  1 
ATOM   1943  C  C   . ILE B  1 113 ? 47.903  -30.135 5.627   1.00 18.01 ? 113  ILE B C   1 
ATOM   1944  O  O   . ILE B  1 113 ? 47.387  -29.395 4.784   1.00 16.52 ? 113  ILE B O   1 
ATOM   1945  C  CB  . ILE B  1 113 ? 48.664  -28.671 7.545   1.00 20.71 ? 113  ILE B CB  1 
ATOM   1946  C  CG1 . ILE B  1 113 ? 49.866  -28.160 8.356   1.00 20.42 ? 113  ILE B CG1 1 
ATOM   1947  C  CG2 . ILE B  1 113 ? 47.628  -29.304 8.483   1.00 17.80 ? 113  ILE B CG2 1 
ATOM   1948  C  CD1 . ILE B  1 113 ? 50.455  -29.148 9.291   1.00 17.69 ? 113  ILE B CD1 1 
ATOM   1949  N  N   . GLY B  1 114 ? 47.469  -31.366 5.873   1.00 18.19 ? 114  GLY B N   1 
ATOM   1950  C  CA  . GLY B  1 114 ? 46.320  -31.915 5.182   1.00 15.39 ? 114  GLY B CA  1 
ATOM   1951  C  C   . GLY B  1 114 ? 46.695  -32.559 3.864   1.00 15.85 ? 114  GLY B C   1 
ATOM   1952  O  O   . GLY B  1 114 ? 45.833  -33.042 3.132   1.00 17.86 ? 114  GLY B O   1 
ATOM   1953  N  N   . ARG B  1 115 ? 47.983  -32.566 3.548   1.00 14.06 ? 115  ARG B N   1 
ATOM   1954  C  CA  . ARG B  1 115 ? 48.440  -33.166 2.308   1.00 14.44 ? 115  ARG B CA  1 
ATOM   1955  C  C   . ARG B  1 115 ? 49.115  -34.507 2.610   1.00 15.31 ? 115  ARG B C   1 
ATOM   1956  O  O   . ARG B  1 115 ? 49.032  -34.990 3.742   1.00 14.84 ? 115  ARG B O   1 
ATOM   1957  C  CB  . ARG B  1 115 ? 49.313  -32.178 1.520   1.00 14.95 ? 115  ARG B CB  1 
ATOM   1958  C  CG  . ARG B  1 115 ? 48.618  -30.809 1.342   1.00 16.19 ? 115  ARG B CG  1 
ATOM   1959  C  CD  . ARG B  1 115 ? 49.255  -29.940 0.268   1.00 17.01 ? 115  ARG B CD  1 
ATOM   1960  N  NE  . ARG B  1 115 ? 48.617  -28.633 0.103   1.00 16.98 ? 115  ARG B NE  1 
ATOM   1961  C  CZ  . ARG B  1 115 ? 47.604  -28.382 -0.732  1.00 19.33 ? 115  ARG B CZ  1 
ATOM   1962  N  NH1 . ARG B  1 115 ? 47.089  -29.354 -1.474  1.00 16.17 ? 115  ARG B NH1 1 
ATOM   1963  N  NH2 . ARG B  1 115 ? 47.101  -27.152 -0.826  1.00 19.21 ? 115  ARG B NH2 1 
ATOM   1964  N  N   . THR B  1 116 ? 49.725  -35.134 1.606   1.00 15.52 ? 116  THR B N   1 
ATOM   1965  C  CA  . THR B  1 116 ? 50.267  -36.481 1.789   1.00 16.24 ? 116  THR B CA  1 
ATOM   1966  C  C   . THR B  1 116 ? 51.779  -36.587 1.575   1.00 16.42 ? 116  THR B C   1 
ATOM   1967  O  O   . THR B  1 116 ? 52.306  -36.143 0.561   1.00 17.95 ? 116  THR B O   1 
ATOM   1968  C  CB  . THR B  1 116 ? 49.571  -37.490 0.864   1.00 15.80 ? 116  THR B CB  1 
ATOM   1969  O  OG1 . THR B  1 116 ? 48.161  -37.410 1.068   1.00 18.25 ? 116  THR B OG1 1 
ATOM   1970  C  CG2 . THR B  1 116 ? 50.040  -38.910 1.148   1.00 14.64 ? 116  THR B CG2 1 
ATOM   1971  N  N   . MET B  1 117 ? 52.462  -37.181 2.544   1.00 15.46 ? 117  MET B N   1 
ATOM   1972  C  CA  . MET B  1 117 ? 53.854  -37.550 2.405   1.00 15.33 ? 117  MET B CA  1 
ATOM   1973  C  C   . MET B  1 117 ? 53.876  -38.938 1.765   1.00 17.30 ? 117  MET B C   1 
ATOM   1974  O  O   . MET B  1 117 ? 53.256  -39.867 2.275   1.00 15.37 ? 117  MET B O   1 
ATOM   1975  C  CB  . MET B  1 117 ? 54.513  -37.573 3.794   1.00 16.48 ? 117  MET B CB  1 
ATOM   1976  C  CG  . MET B  1 117 ? 56.040  -37.487 3.820   1.00 16.89 ? 117  MET B CG  1 
ATOM   1977  S  SD  . MET B  1 117 ? 56.810  -36.216 2.774   1.00 27.52 ? 117  MET B SD  1 
ATOM   1978  C  CE  . MET B  1 117 ? 56.051  -34.750 3.433   1.00 19.34 ? 117  MET B CE  1 
ATOM   1979  N  N   . VAL B  1 118 ? 54.563  -39.073 0.628   1.00 19.22 ? 118  VAL B N   1 
ATOM   1980  C  CA  . VAL B  1 118 ? 54.741  -40.376 -0.017  1.00 16.98 ? 118  VAL B CA  1 
ATOM   1981  C  C   . VAL B  1 118 ? 56.226  -40.708 -0.080  1.00 16.32 ? 118  VAL B C   1 
ATOM   1982  O  O   . VAL B  1 118 ? 57.038  -39.844 -0.400  1.00 17.60 ? 118  VAL B O   1 
ATOM   1983  C  CB  . VAL B  1 118 ? 54.102  -40.434 -1.458  1.00 16.77 ? 118  VAL B CB  1 
ATOM   1984  C  CG1 . VAL B  1 118 ? 54.305  -41.800 -2.103  1.00 15.49 ? 118  VAL B CG1 1 
ATOM   1985  C  CG2 . VAL B  1 118 ? 52.623  -40.122 -1.394  1.00 14.65 ? 118  VAL B CG2 1 
ATOM   1986  N  N   . VAL B  1 119 ? 56.578  -41.945 0.266   1.00 15.51 ? 119  VAL B N   1 
ATOM   1987  C  CA  . VAL B  1 119 ? 57.910  -42.476 -0.018  1.00 17.51 ? 119  VAL B CA  1 
ATOM   1988  C  C   . VAL B  1 119 ? 57.786  -43.413 -1.220  1.00 18.31 ? 119  VAL B C   1 
ATOM   1989  O  O   . VAL B  1 119 ? 56.837  -44.199 -1.308  1.00 16.06 ? 119  VAL B O   1 
ATOM   1990  C  CB  . VAL B  1 119 ? 58.630  -43.126 1.233   1.00 15.90 ? 119  VAL B CB  1 
ATOM   1991  C  CG1 . VAL B  1 119 ? 57.849  -44.276 1.820   1.00 17.21 ? 119  VAL B CG1 1 
ATOM   1992  C  CG2 . VAL B  1 119 ? 60.045  -43.573 0.873   1.00 16.88 ? 119  VAL B CG2 1 
ATOM   1993  N  N   . HIS B  1 120 ? 58.724  -43.284 -2.159  1.00 16.93 ? 120  HIS B N   1 
ATOM   1994  C  CA  . HIS B  1 120 ? 58.649  -43.970 -3.440  1.00 17.54 ? 120  HIS B CA  1 
ATOM   1995  C  C   . HIS B  1 120 ? 59.612  -45.145 -3.570  1.00 20.58 ? 120  HIS B C   1 
ATOM   1996  O  O   . HIS B  1 120 ? 60.580  -45.290 -2.812  1.00 17.95 ? 120  HIS B O   1 
ATOM   1997  C  CB  . HIS B  1 120 ? 58.913  -43.003 -4.599  1.00 16.73 ? 120  HIS B CB  1 
ATOM   1998  C  CG  . HIS B  1 120 ? 57.822  -42.012 -4.820  1.00 17.99 ? 120  HIS B CG  1 
ATOM   1999  N  ND1 . HIS B  1 120 ? 56.853  -42.174 -5.790  1.00 18.56 ? 120  HIS B ND1 1 
ATOM   2000  C  CD2 . HIS B  1 120 ? 57.535  -40.850 -4.189  1.00 18.20 ? 120  HIS B CD2 1 
ATOM   2001  C  CE1 . HIS B  1 120 ? 56.020  -41.149 -5.748  1.00 18.40 ? 120  HIS B CE1 1 
ATOM   2002  N  NE2 . HIS B  1 120 ? 56.405  -40.338 -4.780  1.00 17.95 ? 120  HIS B NE2 1 
ATOM   2003  N  N   . GLU B  1 121 ? 59.325  -45.951 -4.587  1.00 19.37 ? 121  GLU B N   1 
ATOM   2004  C  CA  . GLU B  1 121 ? 60.011  -47.189 -4.905  1.00 18.72 ? 121  GLU B CA  1 
ATOM   2005  C  C   . GLU B  1 121 ? 61.467  -46.999 -5.317  1.00 20.54 ? 121  GLU B C   1 
ATOM   2006  O  O   . GLU B  1 121 ? 62.365  -47.742 -4.920  1.00 21.79 ? 121  GLU B O   1 
ATOM   2007  C  CB  . GLU B  1 121 ? 59.241  -47.813 -6.068  1.00 20.10 ? 121  GLU B CB  1 
ATOM   2008  C  CG  . GLU B  1 121 ? 59.865  -49.014 -6.700  1.00 22.49 ? 121  GLU B CG  1 
ATOM   2009  C  CD  . GLU B  1 121 ? 59.325  -49.266 -8.089  1.00 23.99 ? 121  GLU B CD  1 
ATOM   2010  O  OE1 . GLU B  1 121 ? 58.584  -48.396 -8.609  1.00 22.59 ? 121  GLU B OE1 1 
ATOM   2011  O  OE2 . GLU B  1 121 ? 59.645  -50.331 -8.656  1.00 26.45 ? 121  GLU B OE2 1 
ATOM   2012  N  N   . LYS B  1 122 ? 61.692  -45.988 -6.138  1.00 21.82 ? 122  LYS B N   1 
ATOM   2013  C  CA  . LYS B  1 122 ? 62.952  -45.839 -6.816  1.00 22.05 ? 122  LYS B CA  1 
ATOM   2014  C  C   . LYS B  1 122 ? 63.573  -44.514 -6.431  1.00 21.30 ? 122  LYS B C   1 
ATOM   2015  O  O   . LYS B  1 122 ? 62.917  -43.633 -5.884  1.00 18.96 ? 122  LYS B O   1 
ATOM   2016  C  CB  . LYS B  1 122 ? 62.740  -45.884 -8.345  1.00 21.80 ? 122  LYS B CB  1 
ATOM   2017  C  CG  . LYS B  1 122 ? 62.580  -47.283 -8.943  1.00 23.63 ? 122  LYS B CG  1 
ATOM   2018  C  CD  . LYS B  1 122 ? 62.011  -47.274 -10.376 1.00 29.04 ? 122  LYS B CD  1 
ATOM   2019  C  CE  . LYS B  1 122 ? 62.833  -46.423 -11.343 1.00 35.88 ? 122  LYS B CE  1 
ATOM   2020  N  NZ  . LYS B  1 122 ? 64.195  -46.989 -11.659 1.00 39.68 ? 122  LYS B NZ  1 
ATOM   2021  N  N   . GLN B  1 123 ? 64.845  -44.380 -6.758  1.00 21.15 ? 123  GLN B N   1 
ATOM   2022  C  CA  . GLN B  1 123 ? 65.564  -43.150 -6.570  1.00 20.15 ? 123  GLN B CA  1 
ATOM   2023  C  C   . GLN B  1 123 ? 64.961  -42.024 -7.406  1.00 19.16 ? 123  GLN B C   1 
ATOM   2024  O  O   . GLN B  1 123 ? 64.684  -42.193 -8.590  1.00 18.61 ? 123  GLN B O   1 
ATOM   2025  C  CB  . GLN B  1 123 ? 67.015  -43.373 -6.974  1.00 20.36 ? 123  GLN B CB  1 
ATOM   2026  C  CG  . GLN B  1 123 ? 67.827  -42.115 -7.013  1.00 20.63 ? 123  GLN B CG  1 
ATOM   2027  C  CD  . GLN B  1 123 ? 69.258  -42.401 -7.309  1.00 21.85 ? 123  GLN B CD  1 
ATOM   2028  O  OE1 . GLN B  1 123 ? 69.669  -43.559 -7.347  1.00 24.80 ? 123  GLN B OE1 1 
ATOM   2029  N  NE2 . GLN B  1 123 ? 70.036  -41.354 -7.533  1.00 22.86 ? 123  GLN B NE2 1 
ATOM   2030  N  N   . ASP B  1 124 ? 64.760  -40.878 -6.769  1.00 19.43 ? 124  ASP B N   1 
ATOM   2031  C  CA  . ASP B  1 124 ? 64.337  -39.658 -7.441  1.00 18.75 ? 124  ASP B CA  1 
ATOM   2032  C  C   . ASP B  1 124 ? 65.527  -39.139 -8.282  1.00 20.99 ? 124  ASP B C   1 
ATOM   2033  O  O   . ASP B  1 124 ? 66.618  -38.912 -7.739  1.00 20.57 ? 124  ASP B O   1 
ATOM   2034  C  CB  . ASP B  1 124 ? 63.908  -38.640 -6.365  1.00 16.18 ? 124  ASP B CB  1 
ATOM   2035  C  CG  . ASP B  1 124 ? 63.308  -37.374 -6.942  1.00 18.60 ? 124  ASP B CG  1 
ATOM   2036  O  OD1 . ASP B  1 124 ? 63.384  -37.160 -8.171  1.00 16.67 ? 124  ASP B OD1 1 
ATOM   2037  O  OD2 . ASP B  1 124 ? 62.758  -36.575 -6.157  1.00 17.33 ? 124  ASP B OD2 1 
ATOM   2038  N  N   . ASP B  1 125 ? 65.343  -38.974 -9.598  1.00 18.72 ? 125  ASP B N   1 
ATOM   2039  C  CA  . ASP B  1 125 ? 66.416  -38.419 -10.434 1.00 20.37 ? 125  ASP B CA  1 
ATOM   2040  C  C   . ASP B  1 125 ? 66.576  -36.881 -10.383 1.00 22.14 ? 125  ASP B C   1 
ATOM   2041  O  O   . ASP B  1 125 ? 67.482  -36.329 -11.019 1.00 23.89 ? 125  ASP B O   1 
ATOM   2042  C  CB  . ASP B  1 125 ? 66.393  -38.964 -11.881 1.00 20.66 ? 125  ASP B CB  1 
ATOM   2043  C  CG  . ASP B  1 125 ? 65.305  -38.340 -12.752 1.00 20.64 ? 125  ASP B CG  1 
ATOM   2044  O  OD1 . ASP B  1 125 ? 64.784  -37.260 -12.413 1.00 20.92 ? 125  ASP B OD1 1 
ATOM   2045  O  OD2 . ASP B  1 125 ? 64.978  -38.935 -13.799 1.00 20.81 ? 125  ASP B OD2 1 
ATOM   2046  N  N   . LEU B  1 126 ? 65.726  -36.212 -9.602  1.00 20.24 ? 126  LEU B N   1 
ATOM   2047  C  CA  . LEU B  1 126 ? 65.808  -34.761 -9.388  1.00 19.92 ? 126  LEU B CA  1 
ATOM   2048  C  C   . LEU B  1 126 ? 65.712  -33.947 -10.683 1.00 23.15 ? 126  LEU B C   1 
ATOM   2049  O  O   . LEU B  1 126 ? 66.231  -32.831 -10.764 1.00 25.46 ? 126  LEU B O   1 
ATOM   2050  C  CB  . LEU B  1 126 ? 67.065  -34.380 -8.593  1.00 19.94 ? 126  LEU B CB  1 
ATOM   2051  C  CG  . LEU B  1 126 ? 67.388  -35.247 -7.370  1.00 20.24 ? 126  LEU B CG  1 
ATOM   2052  C  CD1 . LEU B  1 126 ? 68.761  -34.928 -6.836  1.00 19.95 ? 126  LEU B CD1 1 
ATOM   2053  C  CD2 . LEU B  1 126 ? 66.340  -35.107 -6.255  1.00 20.66 ? 126  LEU B CD2 1 
ATOM   2054  N  N   . GLY B  1 127 ? 65.024  -34.506 -11.678 1.00 21.32 ? 127  GLY B N   1 
ATOM   2055  C  CA  . GLY B  1 127 ? 64.716  -33.801 -12.908 1.00 21.54 ? 127  GLY B CA  1 
ATOM   2056  C  C   . GLY B  1 127 ? 65.843  -33.777 -13.924 1.00 22.04 ? 127  GLY B C   1 
ATOM   2057  O  O   . GLY B  1 127 ? 65.861  -32.911 -14.791 1.00 22.56 ? 127  GLY B O   1 
ATOM   2058  N  N   . LYS B  1 128 ? 66.770  -34.729 -13.813 1.00 20.83 ? 128  LYS B N   1 
ATOM   2059  C  CA  . LYS B  1 128 ? 67.951  -34.802 -14.674 1.00 21.47 ? 128  LYS B CA  1 
ATOM   2060  C  C   . LYS B  1 128 ? 68.004  -36.108 -15.480 1.00 22.57 ? 128  LYS B C   1 
ATOM   2061  O  O   . LYS B  1 128 ? 69.053  -36.467 -16.019 1.00 21.71 ? 128  LYS B O   1 
ATOM   2062  C  CB  . LYS B  1 128 ? 69.245  -34.694 -13.848 1.00 23.21 ? 128  LYS B CB  1 
ATOM   2063  C  CG  . LYS B  1 128 ? 69.325  -33.521 -12.886 1.00 25.97 ? 128  LYS B CG  1 
ATOM   2064  C  CD  . LYS B  1 128 ? 70.604  -33.560 -12.069 1.00 31.70 ? 128  LYS B CD  1 
ATOM   2065  C  CE  . LYS B  1 128 ? 70.381  -33.060 -10.630 1.00 37.36 ? 128  LYS B CE  1 
ATOM   2066  N  NZ  . LYS B  1 128 ? 69.341  -31.977 -10.486 1.00 33.35 ? 128  LYS B NZ  1 
ATOM   2067  N  N   . GLY B  1 129 ? 66.882  -36.817 -15.556 1.00 21.54 ? 129  GLY B N   1 
ATOM   2068  C  CA  . GLY B  1 129 ? 66.812  -38.052 -16.323 1.00 21.46 ? 129  GLY B CA  1 
ATOM   2069  C  C   . GLY B  1 129 ? 66.574  -37.830 -17.806 1.00 20.51 ? 129  GLY B C   1 
ATOM   2070  O  O   . GLY B  1 129 ? 66.539  -38.779 -18.577 1.00 21.57 ? 129  GLY B O   1 
ATOM   2071  N  N   . GLY B  1 130 ? 66.388  -36.575 -18.205 1.00 21.57 ? 130  GLY B N   1 
ATOM   2072  C  CA  . GLY B  1 130 ? 66.348  -36.221 -19.616 1.00 19.88 ? 130  GLY B CA  1 
ATOM   2073  C  C   . GLY B  1 130 ? 65.148  -36.733 -20.374 1.00 22.22 ? 130  GLY B C   1 
ATOM   2074  O  O   . GLY B  1 130 ? 65.207  -36.977 -21.564 1.00 20.68 ? 130  GLY B O   1 
ATOM   2075  N  N   . ASN B  1 131 ? 64.044  -36.901 -19.666 1.00 27.61 ? 131  ASN B N   1 
ATOM   2076  C  CA  . ASN B  1 131 ? 62.773  -37.248 -20.281 1.00 22.96 ? 131  ASN B CA  1 
ATOM   2077  C  C   . ASN B  1 131 ? 61.654  -36.503 -19.557 1.00 24.94 ? 131  ASN B C   1 
ATOM   2078  O  O   . ASN B  1 131 ? 61.903  -35.786 -18.589 1.00 25.07 ? 131  ASN B O   1 
ATOM   2079  C  CB  . ASN B  1 131 ? 62.559  -38.771 -20.320 1.00 22.03 ? 131  ASN B CB  1 
ATOM   2080  C  CG  . ASN B  1 131 ? 62.430  -39.387 -18.955 1.00 23.54 ? 131  ASN B CG  1 
ATOM   2081  O  OD1 . ASN B  1 131 ? 62.118  -38.706 -17.982 1.00 24.82 ? 131  ASN B OD1 1 
ATOM   2082  N  ND2 . ASN B  1 131 ? 62.641  -40.693 -18.876 1.00 22.91 ? 131  ASN B ND2 1 
ATOM   2083  N  N   . GLU B  1 132 ? 60.429  -36.642 -20.040 1.00 29.50 ? 132  GLU B N   1 
ATOM   2084  C  CA  . GLU B  1 132 ? 59.316  -35.863 -19.508 1.00 29.49 ? 132  GLU B CA  1 
ATOM   2085  C  C   . GLU B  1 132 ? 58.873  -36.349 -18.122 1.00 25.90 ? 132  GLU B C   1 
ATOM   2086  O  O   . GLU B  1 132 ? 58.476  -35.541 -17.283 1.00 24.80 ? 132  GLU B O   1 
ATOM   2087  C  CB  . GLU B  1 132 ? 58.151  -35.852 -20.503 1.00 30.31 ? 132  GLU B CB  1 
ATOM   2088  C  CG  . GLU B  1 132 ? 57.273  -34.618 -20.414 1.00 38.45 ? 132  GLU B CG  1 
ATOM   2089  C  CD  . GLU B  1 132 ? 55.966  -34.775 -21.184 1.00 49.52 ? 132  GLU B CD  1 
ATOM   2090  O  OE1 . GLU B  1 132 ? 54.888  -34.515 -20.592 1.00 50.01 ? 132  GLU B OE1 1 
ATOM   2091  O  OE2 . GLU B  1 132 ? 56.022  -35.173 -22.374 1.00 48.14 ? 132  GLU B OE2 1 
ATOM   2092  N  N   . GLU B  1 133 ? 58.943  -37.660 -17.886 1.00 24.25 ? 133  GLU B N   1 
ATOM   2093  C  CA  . GLU B  1 133 ? 58.688  -38.228 -16.554 1.00 26.33 ? 133  GLU B CA  1 
ATOM   2094  C  C   . GLU B  1 133 ? 59.652  -37.682 -15.481 1.00 24.66 ? 133  GLU B C   1 
ATOM   2095  O  O   . GLU B  1 133 ? 59.267  -37.445 -14.341 1.00 24.81 ? 133  GLU B O   1 
ATOM   2096  C  CB  . GLU B  1 133 ? 58.760  -39.763 -16.583 1.00 24.80 ? 133  GLU B CB  1 
ATOM   2097  C  CG  . GLU B  1 133 ? 57.482  -40.443 -17.035 1.00 32.67 ? 133  GLU B CG  1 
ATOM   2098  C  CD  . GLU B  1 133 ? 56.331  -40.238 -16.056 1.00 33.01 ? 133  GLU B CD  1 
ATOM   2099  O  OE1 . GLU B  1 133 ? 56.613  -39.962 -14.873 1.00 30.65 ? 133  GLU B OE1 1 
ATOM   2100  O  OE2 . GLU B  1 133 ? 55.149  -40.352 -16.462 1.00 39.27 ? 133  GLU B OE2 1 
ATOM   2101  N  N   . SER B  1 134 ? 60.913  -37.509 -15.847 1.00 23.72 ? 134  SER B N   1 
ATOM   2102  C  CA  . SER B  1 134 ? 61.881  -36.885 -14.966 1.00 21.85 ? 134  SER B CA  1 
ATOM   2103  C  C   . SER B  1 134 ? 61.385  -35.523 -14.452 1.00 22.01 ? 134  SER B C   1 
ATOM   2104  O  O   . SER B  1 134 ? 61.491  -35.222 -13.262 1.00 24.47 ? 134  SER B O   1 
ATOM   2105  C  CB  . SER B  1 134 ? 63.222  -36.729 -15.696 1.00 21.69 ? 134  SER B CB  1 
ATOM   2106  O  OG  . SER B  1 134 ? 64.270  -36.433 -14.789 1.00 22.85 ? 134  SER B OG  1 
ATOM   2107  N  N   . THR B  1 135 ? 60.849  -34.701 -15.347 1.00 20.64 ? 135  THR B N   1 
ATOM   2108  C  CA  . THR B  1 135 ? 60.448  -33.344 -14.995 1.00 22.51 ? 135  THR B CA  1 
ATOM   2109  C  C   . THR B  1 135 ? 59.086  -33.369 -14.313 1.00 24.74 ? 135  THR B C   1 
ATOM   2110  O  O   . THR B  1 135 ? 58.521  -32.327 -13.970 1.00 25.11 ? 135  THR B O   1 
ATOM   2111  C  CB  . THR B  1 135 ? 60.430  -32.388 -16.230 1.00 27.94 ? 135  THR B CB  1 
ATOM   2112  O  OG1 . THR B  1 135 ? 59.312  -32.685 -17.072 1.00 30.58 ? 135  THR B OG1 1 
ATOM   2113  C  CG2 . THR B  1 135 ? 61.697  -32.525 -17.049 1.00 27.74 ? 135  THR B CG2 1 
ATOM   2114  N  N   . LYS B  1 136 ? 58.582  -34.579 -14.091 1.00 24.63 ? 136  LYS B N   1 
ATOM   2115  C  CA  . LYS B  1 136 ? 57.254  -34.789 -13.533 1.00 23.10 ? 136  LYS B CA  1 
ATOM   2116  C  C   . LYS B  1 136 ? 57.362  -35.460 -12.160 1.00 21.67 ? 136  LYS B C   1 
ATOM   2117  O  O   . LYS B  1 136 ? 56.928  -34.908 -11.153 1.00 18.35 ? 136  LYS B O   1 
ATOM   2118  C  CB  . LYS B  1 136 ? 56.445  -35.683 -14.480 1.00 25.20 ? 136  LYS B CB  1 
ATOM   2119  C  CG  . LYS B  1 136 ? 54.959  -35.460 -14.470 1.00 29.12 ? 136  LYS B CG  1 
ATOM   2120  C  CD  . LYS B  1 136 ? 54.481  -34.846 -15.785 1.00 34.75 ? 136  LYS B CD  1 
ATOM   2121  C  CE  . LYS B  1 136 ? 54.494  -35.873 -16.914 1.00 35.79 ? 136  LYS B CE  1 
ATOM   2122  N  NZ  . LYS B  1 136 ? 53.909  -37.193 -16.503 1.00 34.79 ? 136  LYS B NZ  1 
ATOM   2123  N  N   . THR B  1 137 ? 57.951  -36.652 -12.142 1.00 20.51 ? 137  THR B N   1 
ATOM   2124  C  CA  . THR B  1 137 ? 57.985  -37.509 -10.961 1.00 18.55 ? 137  THR B CA  1 
ATOM   2125  C  C   . THR B  1 137 ? 59.421  -37.872 -10.508 1.00 21.75 ? 137  THR B C   1 
ATOM   2126  O  O   . THR B  1 137 ? 59.624  -38.499 -9.445  1.00 19.58 ? 137  THR B O   1 
ATOM   2127  C  CB  . THR B  1 137 ? 57.207  -38.807 -11.241 1.00 20.24 ? 137  THR B CB  1 
ATOM   2128  O  OG1 . THR B  1 137 ? 57.868  -39.542 -12.276 1.00 21.70 ? 137  THR B OG1 1 
ATOM   2129  C  CG2 . THR B  1 137 ? 55.804  -38.490 -11.706 1.00 19.81 ? 137  THR B CG2 1 
ATOM   2130  N  N   . GLY B  1 138 ? 60.408  -37.475 -11.318 1.00 21.40 ? 138  GLY B N   1 
ATOM   2131  C  CA  . GLY B  1 138 ? 61.804  -37.769 -11.059 1.00 17.67 ? 138  GLY B CA  1 
ATOM   2132  C  C   . GLY B  1 138 ? 62.130  -39.210 -11.382 1.00 18.55 ? 138  GLY B C   1 
ATOM   2133  O  O   . GLY B  1 138 ? 63.212  -39.694 -11.073 1.00 18.56 ? 138  GLY B O   1 
ATOM   2134  N  N   . ASN B  1 139 ? 61.190  -39.887 -12.034 1.00 21.98 ? 139  ASN B N   1 
ATOM   2135  C  CA  . ASN B  1 139 ? 61.312  -41.311 -12.345 1.00 22.00 ? 139  ASN B CA  1 
ATOM   2136  C  C   . ASN B  1 139 ? 61.363  -42.119 -11.055 1.00 21.37 ? 139  ASN B C   1 
ATOM   2137  O  O   . ASN B  1 139 ? 61.983  -43.185 -10.989 1.00 22.72 ? 139  ASN B O   1 
ATOM   2138  C  CB  . ASN B  1 139 ? 62.530  -41.592 -13.241 1.00 20.85 ? 139  ASN B CB  1 
ATOM   2139  C  CG  . ASN B  1 139 ? 62.274  -41.246 -14.710 1.00 22.00 ? 139  ASN B CG  1 
ATOM   2140  O  OD1 . ASN B  1 139 ? 61.412  -41.834 -15.354 1.00 23.71 ? 139  ASN B OD1 1 
ATOM   2141  N  ND2 . ASN B  1 139 ? 63.027  -40.284 -15.238 1.00 21.45 ? 139  ASN B ND2 1 
ATOM   2142  N  N   . ALA B  1 140 ? 60.693  -41.598 -10.029 1.00 20.52 ? 140  ALA B N   1 
ATOM   2143  C  CA  . ALA B  1 140 ? 60.800  -42.155 -8.690  1.00 18.77 ? 140  ALA B CA  1 
ATOM   2144  C  C   . ALA B  1 140 ? 59.972  -43.425 -8.521  1.00 19.31 ? 140  ALA B C   1 
ATOM   2145  O  O   . ALA B  1 140 ? 60.156  -44.177 -7.578  1.00 21.39 ? 140  ALA B O   1 
ATOM   2146  C  CB  . ALA B  1 140 ? 60.429  -41.115 -7.653  1.00 18.55 ? 140  ALA B CB  1 
ATOM   2147  N  N   . GLY B  1 141 ? 59.058  -43.671 -9.441  1.00 22.08 ? 141  GLY B N   1 
ATOM   2148  C  CA  . GLY B  1 141 ? 58.359  -44.938 -9.450  1.00 21.53 ? 141  GLY B CA  1 
ATOM   2149  C  C   . GLY B  1 141 ? 57.131  -44.968 -8.572  1.00 21.52 ? 141  GLY B C   1 
ATOM   2150  O  O   . GLY B  1 141 ? 56.536  -43.929 -8.272  1.00 21.13 ? 141  GLY B O   1 
ATOM   2151  N  N   . SER B  1 142 ? 56.763  -46.176 -8.151  1.00 21.09 ? 142  SER B N   1 
ATOM   2152  C  CA  . SER B  1 142 ? 55.517  -46.400 -7.439  1.00 21.01 ? 142  SER B CA  1 
ATOM   2153  C  C   . SER B  1 142 ? 55.573  -45.884 -5.999  1.00 21.00 ? 142  SER B C   1 
ATOM   2154  O  O   . SER B  1 142 ? 56.653  -45.600 -5.475  1.00 19.19 ? 142  SER B O   1 
ATOM   2155  C  CB  . SER B  1 142 ? 55.141  -47.888 -7.471  1.00 20.49 ? 142  SER B CB  1 
ATOM   2156  O  OG  . SER B  1 142 ? 55.728  -48.575 -6.381  1.00 22.67 ? 142  SER B OG  1 
ATOM   2157  N  N   . ARG B  1 143 ? 54.394  -45.764 -5.387  1.00 20.96 ? 143  ARG B N   1 
ATOM   2158  C  CA  . ARG B  1 143 ? 54.236  -45.248 -4.032  1.00 20.31 ? 143  ARG B CA  1 
ATOM   2159  C  C   . ARG B  1 143 ? 54.167  -46.385 -3.023  1.00 20.33 ? 143  ARG B C   1 
ATOM   2160  O  O   . ARG B  1 143 ? 53.223  -47.169 -3.008  1.00 22.84 ? 143  ARG B O   1 
ATOM   2161  C  CB  . ARG B  1 143 ? 52.994  -44.361 -3.963  1.00 19.60 ? 143  ARG B CB  1 
ATOM   2162  C  CG  . ARG B  1 143 ? 52.893  -43.493 -5.196  1.00 18.88 ? 143  ARG B CG  1 
ATOM   2163  C  CD  . ARG B  1 143 ? 51.682  -42.598 -5.233  1.00 19.15 ? 143  ARG B CD  1 
ATOM   2164  N  NE  . ARG B  1 143 ? 51.774  -41.725 -6.399  1.00 23.20 ? 143  ARG B NE  1 
ATOM   2165  C  CZ  . ARG B  1 143 ? 50.925  -40.744 -6.684  1.00 22.54 ? 143  ARG B CZ  1 
ATOM   2166  N  NH1 . ARG B  1 143 ? 49.897  -40.496 -5.882  1.00 23.56 ? 143  ARG B NH1 1 
ATOM   2167  N  NH2 . ARG B  1 143 ? 51.109  -40.002 -7.766  1.00 20.35 ? 143  ARG B NH2 1 
ATOM   2168  N  N   . LEU B  1 144 ? 55.194  -46.475 -2.193  1.00 18.71 ? 144  LEU B N   1 
ATOM   2169  C  CA  . LEU B  1 144 ? 55.371  -47.606 -1.311  1.00 20.30 ? 144  LEU B CA  1 
ATOM   2170  C  C   . LEU B  1 144 ? 54.610  -47.404 -0.013  1.00 21.91 ? 144  LEU B C   1 
ATOM   2171  O  O   . LEU B  1 144 ? 54.153  -48.367 0.598   1.00 24.87 ? 144  LEU B O   1 
ATOM   2172  C  CB  . LEU B  1 144 ? 56.862  -47.810 -1.019  1.00 21.22 ? 144  LEU B CB  1 
ATOM   2173  C  CG  . LEU B  1 144 ? 57.757  -48.163 -2.209  1.00 19.72 ? 144  LEU B CG  1 
ATOM   2174  C  CD1 . LEU B  1 144 ? 59.205  -48.181 -1.792  1.00 19.91 ? 144  LEU B CD1 1 
ATOM   2175  C  CD2 . LEU B  1 144 ? 57.354  -49.501 -2.788  1.00 22.00 ? 144  LEU B CD2 1 
ATOM   2176  N  N   . ALA B  1 145 ? 54.476  -46.152 0.412   1.00 18.47 ? 145  ALA B N   1 
ATOM   2177  C  CA  . ALA B  1 145 ? 53.830  -45.859 1.680   1.00 18.97 ? 145  ALA B CA  1 
ATOM   2178  C  C   . ALA B  1 145 ? 53.536  -44.369 1.795   1.00 18.98 ? 145  ALA B C   1 
ATOM   2179  O  O   . ALA B  1 145 ? 54.267  -43.546 1.275   1.00 18.85 ? 145  ALA B O   1 
ATOM   2180  C  CB  . ALA B  1 145 ? 54.693  -46.324 2.824   1.00 19.70 ? 145  ALA B CB  1 
ATOM   2181  N  N   . CYS B  1 146 ? 52.452  -44.028 2.471   1.00 19.09 ? 146  CYS B N   1 
ATOM   2182  C  CA  . CYS B  1 146 ? 52.022  -42.643 2.561   1.00 19.26 ? 146  CYS B CA  1 
ATOM   2183  C  C   . CYS B  1 146 ? 51.135  -42.445 3.785   1.00 18.78 ? 146  CYS B C   1 
ATOM   2184  O  O   . CYS B  1 146 ? 50.728  -43.403 4.439   1.00 19.31 ? 146  CYS B O   1 
ATOM   2185  C  CB  . CYS B  1 146 ? 51.254  -42.234 1.291   1.00 18.48 ? 146  CYS B CB  1 
ATOM   2186  S  SG  . CYS B  1 146 ? 49.609  -43.006 1.093   1.00 20.60 ? 146  CYS B SG  1 
ATOM   2187  N  N   . GLY B  1 147 ? 50.843  -41.188 4.089   1.00 17.16 ? 147  GLY B N   1 
ATOM   2188  C  CA  . GLY B  1 147 ? 49.913  -40.854 5.145   1.00 17.91 ? 147  GLY B CA  1 
ATOM   2189  C  C   . GLY B  1 147 ? 49.591  -39.384 5.025   1.00 18.61 ? 147  GLY B C   1 
ATOM   2190  O  O   . GLY B  1 147 ? 50.351  -38.627 4.429   1.00 17.36 ? 147  GLY B O   1 
ATOM   2191  N  N   . VAL B  1 148 ? 48.455  -38.980 5.566   1.00 17.43 ? 148  VAL B N   1 
ATOM   2192  C  CA  . VAL B  1 148 ? 48.097  -37.573 5.613   1.00 16.03 ? 148  VAL B CA  1 
ATOM   2193  C  C   . VAL B  1 148 ? 48.892  -36.874 6.726   1.00 17.94 ? 148  VAL B C   1 
ATOM   2194  O  O   . VAL B  1 148 ? 49.044  -37.402 7.841   1.00 16.50 ? 148  VAL B O   1 
ATOM   2195  C  CB  . VAL B  1 148 ? 46.570  -37.415 5.838   1.00 15.90 ? 148  VAL B CB  1 
ATOM   2196  C  CG1 . VAL B  1 148 ? 46.127  -35.975 5.680   1.00 13.23 ? 148  VAL B CG1 1 
ATOM   2197  C  CG2 . VAL B  1 148 ? 45.819  -38.311 4.883   1.00 15.07 ? 148  VAL B CG2 1 
ATOM   2198  N  N   . ILE B  1 149 ? 49.391  -35.679 6.410   1.00 18.29 ? 149  ILE B N   1 
ATOM   2199  C  CA  . ILE B  1 149 ? 50.122  -34.839 7.352   1.00 16.08 ? 149  ILE B CA  1 
ATOM   2200  C  C   . ILE B  1 149 ? 49.154  -34.113 8.291   1.00 16.10 ? 149  ILE B C   1 
ATOM   2201  O  O   . ILE B  1 149 ? 48.341  -33.293 7.866   1.00 17.01 ? 149  ILE B O   1 
ATOM   2202  C  CB  . ILE B  1 149 ? 51.017  -33.826 6.593   1.00 18.77 ? 149  ILE B CB  1 
ATOM   2203  C  CG1 . ILE B  1 149 ? 52.049  -34.568 5.741   1.00 16.00 ? 149  ILE B CG1 1 
ATOM   2204  C  CG2 . ILE B  1 149 ? 51.711  -32.857 7.562   1.00 17.80 ? 149  ILE B CG2 1 
ATOM   2205  C  CD1 . ILE B  1 149 ? 52.891  -33.669 4.886   1.00 16.11 ? 149  ILE B CD1 1 
ATOM   2206  N  N   . GLY B  1 150 ? 49.240  -34.425 9.575   1.00 17.35 ? 150  GLY B N   1 
ATOM   2207  C  CA  . GLY B  1 150 ? 48.345  -33.838 10.556  1.00 18.55 ? 150  GLY B CA  1 
ATOM   2208  C  C   . GLY B  1 150 ? 49.000  -32.933 11.579  1.00 16.46 ? 150  GLY B C   1 
ATOM   2209  O  O   . GLY B  1 150 ? 50.179  -33.071 11.882  1.00 16.48 ? 150  GLY B O   1 
ATOM   2210  N  N   . ILE B  1 151 ? 48.212  -32.003 12.108  1.00 17.93 ? 151  ILE B N   1 
ATOM   2211  C  CA  . ILE B  1 151 ? 48.629  -31.136 13.200  1.00 18.37 ? 151  ILE B CA  1 
ATOM   2212  C  C   . ILE B  1 151 ? 49.014  -31.960 14.423  1.00 20.34 ? 151  ILE B C   1 
ATOM   2213  O  O   . ILE B  1 151 ? 48.256  -32.838 14.830  1.00 21.55 ? 151  ILE B O   1 
ATOM   2214  C  CB  . ILE B  1 151 ? 47.498  -30.173 13.592  1.00 16.75 ? 151  ILE B CB  1 
ATOM   2215  C  CG1 . ILE B  1 151 ? 47.291  -29.137 12.489  1.00 15.40 ? 151  ILE B CG1 1 
ATOM   2216  C  CG2 . ILE B  1 151 ? 47.845  -29.479 14.892  1.00 17.67 ? 151  ILE B CG2 1 
ATOM   2217  C  CD1 . ILE B  1 151 ? 45.985  -28.425 12.553  1.00 14.71 ? 151  ILE B CD1 1 
ATOM   2218  N  N   . ALA B  1 152 ? 50.197  -31.689 14.988  1.00 21.95 ? 152  ALA B N   1 
ATOM   2219  C  CA  . ALA B  1 152 ? 50.693  -32.386 16.176  1.00 19.99 ? 152  ALA B CA  1 
ATOM   2220  C  C   . ALA B  1 152 ? 50.881  -31.436 17.354  1.00 22.29 ? 152  ALA B C   1 
ATOM   2221  O  O   . ALA B  1 152 ? 50.935  -30.218 17.178  1.00 22.85 ? 152  ALA B O   1 
ATOM   2222  C  CB  . ALA B  1 152 ? 52.000  -33.085 15.875  1.00 19.04 ? 152  ALA B CB  1 
ATOM   2223  N  N   . GLN B  1 153 ? 50.969  -31.996 18.558  1.00 25.28 ? 153  GLN B N   1 
ATOM   2224  C  CA  . GLN B  1 153 ? 51.334  -31.206 19.738  1.00 32.18 ? 153  GLN B CA  1 
ATOM   2225  C  C   . GLN B  1 153 ? 52.835  -31.317 20.071  1.00 36.16 ? 153  GLN B C   1 
ATOM   2226  O  O   . GLN B  1 153 ? 53.421  -30.388 20.642  1.00 37.69 ? 153  GLN B O   1 
ATOM   2227  C  CB  . GLN B  1 153 ? 50.461  -31.558 20.958  1.00 32.68 ? 153  GLN B CB  1 
ATOM   2228  C  CG  . GLN B  1 153 ? 50.838  -32.842 21.699  1.00 37.35 ? 153  GLN B CG  1 
ATOM   2229  C  CD  . GLN B  1 153 ? 50.415  -32.822 23.177  1.00 37.85 ? 153  GLN B CD  1 
ATOM   2230  O  OE1 . GLN B  1 153 ? 49.929  -31.810 23.684  1.00 35.61 ? 153  GLN B OE1 1 
ATOM   2231  N  NE2 . GLN B  1 153 ? 50.608  -33.945 23.867  1.00 40.03 ? 153  GLN B NE2 1 
ATOM   2232  O  OXT . GLN B  1 153 ? 53.509  -32.316 19.768  1.00 37.19 ? 153  GLN B OXT 1 
ATOM   2233  N  N   . ALA C  1 1   ? -13.330 -23.163 21.276  1.00 40.81 ? 1    ALA C N   1 
ATOM   2234  C  CA  . ALA C  1 1   ? -13.656 -24.464 21.855  1.00 40.92 ? 1    ALA C CA  1 
ATOM   2235  C  C   . ALA C  1 1   ? -13.676 -25.578 20.797  1.00 37.37 ? 1    ALA C C   1 
ATOM   2236  O  O   . ALA C  1 1   ? -14.453 -26.527 20.906  1.00 39.77 ? 1    ALA C O   1 
ATOM   2237  C  CB  . ALA C  1 1   ? -14.997 -24.392 22.592  1.00 42.03 ? 1    ALA C CB  1 
ATOM   2238  N  N   . THR C  1 2   ? -12.823 -25.457 19.780  1.00 35.82 ? 2    THR C N   1 
ATOM   2239  C  CA  . THR C  1 2   ? -12.744 -26.443 18.700  1.00 28.83 ? 2    THR C CA  1 
ATOM   2240  C  C   . THR C  1 2   ? -12.361 -27.808 19.267  1.00 26.74 ? 2    THR C C   1 
ATOM   2241  O  O   . THR C  1 2   ? -11.688 -27.907 20.286  1.00 29.16 ? 2    THR C O   1 
ATOM   2242  C  CB  . THR C  1 2   ? -11.707 -26.027 17.634  1.00 30.54 ? 2    THR C CB  1 
ATOM   2243  O  OG1 . THR C  1 2   ? -11.672 -24.600 17.528  1.00 36.58 ? 2    THR C OG1 1 
ATOM   2244  C  CG2 . THR C  1 2   ? -12.052 -26.608 16.276  1.00 31.20 ? 2    THR C CG2 1 
ATOM   2245  N  N   . LYS C  1 3   ? -12.795 -28.860 18.591  1.00 25.78 ? 3    LYS C N   1 
ATOM   2246  C  CA  . LYS C  1 3   ? -12.606 -30.230 19.045  1.00 23.34 ? 3    LYS C CA  1 
ATOM   2247  C  C   . LYS C  1 3   ? -12.432 -31.077 17.773  1.00 24.85 ? 3    LYS C C   1 
ATOM   2248  O  O   . LYS C  1 3   ? -13.057 -30.790 16.736  1.00 25.39 ? 3    LYS C O   1 
ATOM   2249  C  CB  . LYS C  1 3   ? -13.852 -30.664 19.827  1.00 27.08 ? 3    LYS C CB  1 
ATOM   2250  C  CG  . LYS C  1 3   ? -13.621 -31.498 21.088  1.00 29.83 ? 3    LYS C CG  1 
ATOM   2251  C  CD  . LYS C  1 3   ? -14.823 -31.369 22.049  1.00 34.72 ? 3    LYS C CD  1 
ATOM   2252  C  CE  . LYS C  1 3   ? -15.309 -32.725 22.619  1.00 39.13 ? 3    LYS C CE  1 
ATOM   2253  N  NZ  . LYS C  1 3   ? -14.291 -33.489 23.417  1.00 44.92 ? 3    LYS C NZ  1 
ATOM   2254  N  N   . ALA C  1 4   ? -11.568 -32.088 17.821  1.00 20.90 ? 4    ALA C N   1 
ATOM   2255  C  CA  . ALA C  1 4   ? -11.363 -32.945 16.654  1.00 21.27 ? 4    ALA C CA  1 
ATOM   2256  C  C   . ALA C  1 4   ? -11.082 -34.385 17.055  1.00 20.06 ? 4    ALA C C   1 
ATOM   2257  O  O   . ALA C  1 4   ? -10.838 -34.680 18.219  1.00 20.39 ? 4    ALA C O   1 
ATOM   2258  C  CB  . ALA C  1 4   ? -10.250 -32.408 15.771  1.00 19.75 ? 4    ALA C CB  1 
ATOM   2259  N  N   . VAL C  1 5   ? -11.127 -35.285 16.085  1.00 19.19 ? 5    VAL C N   1 
ATOM   2260  C  CA  . VAL C  1 5   ? -10.959 -36.705 16.376  1.00 20.25 ? 5    VAL C CA  1 
ATOM   2261  C  C   . VAL C  1 5   ? -10.258 -37.417 15.204  1.00 21.98 ? 5    VAL C C   1 
ATOM   2262  O  O   . VAL C  1 5   ? -10.336 -36.973 14.047  1.00 19.28 ? 5    VAL C O   1 
ATOM   2263  C  CB  . VAL C  1 5   ? -12.318 -37.383 16.758  1.00 20.27 ? 5    VAL C CB  1 
ATOM   2264  C  CG1 . VAL C  1 5   ? -13.218 -37.541 15.542  1.00 17.87 ? 5    VAL C CG1 1 
ATOM   2265  C  CG2 . VAL C  1 5   ? -12.104 -38.726 17.477  1.00 21.12 ? 5    VAL C CG2 1 
ATOM   2266  N  N   . CYS C  1 6   ? -9.555  -38.501 15.528  1.00 20.94 ? 6    CYS C N   1 
ATOM   2267  C  CA  . CYS C  1 6   ? -8.768  -39.256 14.566  1.00 21.65 ? 6    CYS C CA  1 
ATOM   2268  C  C   . CYS C  1 6   ? -8.782  -40.749 14.903  1.00 19.32 ? 6    CYS C C   1 
ATOM   2269  O  O   . CYS C  1 6   ? -8.436  -41.142 16.012  1.00 17.83 ? 6    CYS C O   1 
ATOM   2270  C  CB  . CYS C  1 6   ? -7.324  -38.749 14.566  1.00 20.06 ? 6    CYS C CB  1 
ATOM   2271  S  SG  . CYS C  1 6   ? -6.341  -39.369 13.210  1.00 24.09 ? 6    CYS C SG  1 
ATOM   2272  N  N   . VAL C  1 7   ? -9.179  -41.571 13.937  1.00 18.58 ? 7    VAL C N   1 
ATOM   2273  C  CA  . VAL C  1 7   ? -9.158  -43.024 14.082  1.00 18.81 ? 7    VAL C CA  1 
ATOM   2274  C  C   . VAL C  1 7   ? -7.977  -43.589 13.287  1.00 18.99 ? 7    VAL C C   1 
ATOM   2275  O  O   . VAL C  1 7   ? -7.942  -43.468 12.065  1.00 22.34 ? 7    VAL C O   1 
ATOM   2276  C  CB  . VAL C  1 7   ? -10.488 -43.656 13.579  1.00 20.53 ? 7    VAL C CB  1 
ATOM   2277  C  CG1 . VAL C  1 7   ? -10.459 -45.181 13.677  1.00 21.78 ? 7    VAL C CG1 1 
ATOM   2278  C  CG2 . VAL C  1 7   ? -11.651 -43.108 14.357  1.00 18.94 ? 7    VAL C CG2 1 
ATOM   2279  N  N   . LEU C  1 8   ? -7.012  -44.195 13.977  1.00 18.73 ? 8    LEU C N   1 
ATOM   2280  C  CA  . LEU C  1 8   ? -5.830  -44.750 13.323  1.00 17.80 ? 8    LEU C CA  1 
ATOM   2281  C  C   . LEU C  1 8   ? -6.006  -46.224 12.917  1.00 18.41 ? 8    LEU C C   1 
ATOM   2282  O  O   . LEU C  1 8   ? -6.303  -47.079 13.740  1.00 19.52 ? 8    LEU C O   1 
ATOM   2283  C  CB  . LEU C  1 8   ? -4.590  -44.587 14.215  1.00 17.22 ? 8    LEU C CB  1 
ATOM   2284  C  CG  . LEU C  1 8   ? -4.282  -43.245 14.902  1.00 18.59 ? 8    LEU C CG  1 
ATOM   2285  C  CD1 . LEU C  1 8   ? -3.209  -43.412 15.997  1.00 19.96 ? 8    LEU C CD1 1 
ATOM   2286  C  CD2 . LEU C  1 8   ? -3.852  -42.171 13.933  1.00 17.04 ? 8    LEU C CD2 1 
ATOM   2287  N  N   . LYS C  1 9   ? -5.817  -46.503 11.631  1.00 20.42 ? 9    LYS C N   1 
ATOM   2288  C  CA  . LYS C  1 9   ? -5.860  -47.858 11.088  1.00 19.89 ? 9    LYS C CA  1 
ATOM   2289  C  C   . LYS C  1 9   ? -4.681  -48.028 10.138  1.00 17.34 ? 9    LYS C C   1 
ATOM   2290  O  O   . LYS C  1 9   ? -4.127  -47.044 9.647   1.00 16.65 ? 9    LYS C O   1 
ATOM   2291  C  CB  . LYS C  1 9   ? -7.169  -48.094 10.328  1.00 19.45 ? 9    LYS C CB  1 
ATOM   2292  C  CG  . LYS C  1 9   ? -8.381  -48.109 11.219  1.00 22.92 ? 9    LYS C CG  1 
ATOM   2293  C  CD  . LYS C  1 9   ? -9.674  -48.109 10.433  1.00 26.72 ? 9    LYS C CD  1 
ATOM   2294  C  CE  . LYS C  1 9   ? -10.851 -48.238 11.387  1.00 33.53 ? 9    LYS C CE  1 
ATOM   2295  N  NZ  . LYS C  1 9   ? -10.657 -49.368 12.356  1.00 31.51 ? 9    LYS C NZ  1 
ATOM   2296  N  N   . GLY C  1 10  ? -4.311  -49.273 9.875   1.00 15.13 ? 10   GLY C N   1 
ATOM   2297  C  CA  . GLY C  1 10  ? -3.198  -49.577 8.993   1.00 16.98 ? 10   GLY C CA  1 
ATOM   2298  C  C   . GLY C  1 10  ? -3.320  -51.010 8.526   1.00 20.07 ? 10   GLY C C   1 
ATOM   2299  O  O   . GLY C  1 10  ? -4.373  -51.625 8.684   1.00 20.37 ? 10   GLY C O   1 
ATOM   2300  N  N   . ASP C  1 11  ? -2.259  -51.560 7.952   1.00 21.35 ? 11   ASP C N   1 
ATOM   2301  C  CA  . ASP C  1 11  ? -2.371  -52.886 7.342   1.00 22.64 ? 11   ASP C CA  1 
ATOM   2302  C  C   . ASP C  1 11  ? -1.977  -54.022 8.278   1.00 21.14 ? 11   ASP C C   1 
ATOM   2303  O  O   . ASP C  1 11  ? -1.964  -55.180 7.881   1.00 21.78 ? 11   ASP C O   1 
ATOM   2304  C  CB  . ASP C  1 11  ? -1.581  -52.947 6.033   1.00 26.01 ? 11   ASP C CB  1 
ATOM   2305  C  CG  . ASP C  1 11  ? -2.070  -51.930 5.012   1.00 31.01 ? 11   ASP C CG  1 
ATOM   2306  O  OD1 . ASP C  1 11  ? -3.301  -51.687 4.942   1.00 29.31 ? 11   ASP C OD1 1 
ATOM   2307  O  OD2 . ASP C  1 11  ? -1.217  -51.369 4.286   1.00 34.36 ? 11   ASP C OD2 1 
ATOM   2308  N  N   . GLY C  1 12  ? -1.683  -53.666 9.525   1.00 21.82 ? 12   GLY C N   1 
ATOM   2309  C  CA  . GLY C  1 12  ? -1.286  -54.600 10.566  1.00 19.53 ? 12   GLY C CA  1 
ATOM   2310  C  C   . GLY C  1 12  ? -2.181  -54.487 11.786  1.00 18.62 ? 12   GLY C C   1 
ATOM   2311  O  O   . GLY C  1 12  ? -3.368  -54.188 11.651  1.00 20.18 ? 12   GLY C O   1 
ATOM   2312  N  N   . PRO C  1 13  ? -1.615  -54.718 12.984  1.00 18.10 ? 13   PRO C N   1 
ATOM   2313  C  CA  . PRO C  1 13  ? -2.320  -54.803 14.267  1.00 17.26 ? 13   PRO C CA  1 
ATOM   2314  C  C   . PRO C  1 13  ? -2.622  -53.448 14.883  1.00 17.86 ? 13   PRO C C   1 
ATOM   2315  O  O   . PRO C  1 13  ? -3.444  -53.365 15.799  1.00 17.77 ? 13   PRO C O   1 
ATOM   2316  C  CB  . PRO C  1 13  ? -1.312  -55.512 15.180  1.00 18.45 ? 13   PRO C CB  1 
ATOM   2317  C  CG  . PRO C  1 13  ? -0.083  -55.735 14.381  1.00 17.74 ? 13   PRO C CG  1 
ATOM   2318  C  CD  . PRO C  1 13  ? -0.169  -54.929 13.148  1.00 20.98 ? 13   PRO C CD  1 
ATOM   2319  N  N   . VAL C  1 14  ? -1.953  -52.408 14.402  1.00 15.67 ? 14   VAL C N   1 
ATOM   2320  C  CA  . VAL C  1 14  ? -2.016  -51.101 15.040  1.00 16.31 ? 14   VAL C CA  1 
ATOM   2321  C  C   . VAL C  1 14  ? -3.315  -50.316 14.784  1.00 18.81 ? 14   VAL C C   1 
ATOM   2322  O  O   . VAL C  1 14  ? -3.705  -50.088 13.635  1.00 15.37 ? 14   VAL C O   1 
ATOM   2323  C  CB  . VAL C  1 14  ? -0.788  -50.259 14.663  1.00 16.34 ? 14   VAL C CB  1 
ATOM   2324  C  CG1 . VAL C  1 14  ? -0.799  -48.950 15.431  1.00 17.27 ? 14   VAL C CG1 1 
ATOM   2325  C  CG2 . VAL C  1 14  ? 0.486   -51.047 14.958  1.00 12.88 ? 14   VAL C CG2 1 
ATOM   2326  N  N   . GLN C  1 15  ? -3.989  -49.936 15.873  1.00 18.92 ? 15   GLN C N   1 
ATOM   2327  C  CA  . GLN C  1 15  ? -5.157  -49.055 15.820  1.00 18.60 ? 15   GLN C CA  1 
ATOM   2328  C  C   . GLN C  1 15  ? -5.350  -48.248 17.110  1.00 21.33 ? 15   GLN C C   1 
ATOM   2329  O  O   . GLN C  1 15  ? -4.904  -48.650 18.174  1.00 19.56 ? 15   GLN C O   1 
ATOM   2330  C  CB  . GLN C  1 15  ? -6.430  -49.822 15.451  1.00 22.51 ? 15   GLN C CB  1 
ATOM   2331  C  CG  . GLN C  1 15  ? -6.754  -51.034 16.306  1.00 25.65 ? 15   GLN C CG  1 
ATOM   2332  C  CD  . GLN C  1 15  ? -7.815  -51.936 15.661  1.00 24.03 ? 15   GLN C CD  1 
ATOM   2333  O  OE1 . GLN C  1 15  ? -8.102  -51.819 14.475  1.00 26.60 ? 15   GLN C OE1 1 
ATOM   2334  N  NE2 . GLN C  1 15  ? -8.387  -52.840 16.444  1.00 24.23 ? 15   GLN C NE2 1 
ATOM   2335  N  N   . GLY C  1 16  ? -6.010  -47.099 16.999  1.00 23.08 ? 16   GLY C N   1 
ATOM   2336  C  CA  . GLY C  1 16  ? -6.245  -46.223 18.134  1.00 18.43 ? 16   GLY C CA  1 
ATOM   2337  C  C   . GLY C  1 16  ? -7.242  -45.109 17.841  1.00 20.69 ? 16   GLY C C   1 
ATOM   2338  O  O   . GLY C  1 16  ? -7.745  -44.975 16.719  1.00 21.27 ? 16   GLY C O   1 
ATOM   2339  N  N   . ILE C  1 17  ? -7.549  -44.328 18.871  1.00 22.29 ? 17   ILE C N   1 
ATOM   2340  C  CA  . ILE C  1 17  ? -8.402  -43.152 18.751  1.00 21.93 ? 17   ILE C CA  1 
ATOM   2341  C  C   . ILE C  1 17  ? -7.691  -41.986 19.424  1.00 21.27 ? 17   ILE C C   1 
ATOM   2342  O  O   . ILE C  1 17  ? -7.265  -42.092 20.576  1.00 19.60 ? 17   ILE C O   1 
ATOM   2343  C  CB  . ILE C  1 17  ? -9.776  -43.355 19.428  1.00 21.04 ? 17   ILE C CB  1 
ATOM   2344  C  CG1 . ILE C  1 17  ? -10.527 -44.517 18.781  1.00 20.84 ? 17   ILE C CG1 1 
ATOM   2345  C  CG2 . ILE C  1 17  ? -10.605 -42.079 19.353  1.00 18.39 ? 17   ILE C CG2 1 
ATOM   2346  C  CD1 . ILE C  1 17  ? -11.785 -44.875 19.501  1.00 19.82 ? 17   ILE C CD1 1 
ATOM   2347  N  N   . ILE C  1 18  ? -7.553  -40.886 18.695  1.00 18.28 ? 18   ILE C N   1 
ATOM   2348  C  CA  . ILE C  1 18  ? -6.884  -39.706 19.212  1.00 18.82 ? 18   ILE C CA  1 
ATOM   2349  C  C   . ILE C  1 18  ? -7.893  -38.575 19.260  1.00 20.00 ? 18   ILE C C   1 
ATOM   2350  O  O   . ILE C  1 18  ? -8.589  -38.323 18.281  1.00 21.62 ? 18   ILE C O   1 
ATOM   2351  C  CB  . ILE C  1 18  ? -5.653  -39.306 18.340  1.00 19.21 ? 18   ILE C CB  1 
ATOM   2352  C  CG1 . ILE C  1 18  ? -4.647  -40.465 18.248  1.00 19.40 ? 18   ILE C CG1 1 
ATOM   2353  C  CG2 . ILE C  1 18  ? -4.965  -38.066 18.882  1.00 18.83 ? 18   ILE C CG2 1 
ATOM   2354  C  CD1 . ILE C  1 18  ? -3.914  -40.786 19.561  1.00 18.11 ? 18   ILE C CD1 1 
ATOM   2355  N  N   . ASN C  1 19  ? -7.988  -37.918 20.415  1.00 20.70 ? 19   ASN C N   1 
ATOM   2356  C  CA  . ASN C  1 19  ? -8.833  -36.749 20.582  1.00 19.29 ? 19   ASN C CA  1 
ATOM   2357  C  C   . ASN C  1 19  ? -7.993  -35.482 20.604  1.00 17.10 ? 19   ASN C C   1 
ATOM   2358  O  O   . ASN C  1 19  ? -6.884  -35.503 21.072  1.00 18.26 ? 19   ASN C O   1 
ATOM   2359  C  CB  . ASN C  1 19  ? -9.630  -36.879 21.873  1.00 20.17 ? 19   ASN C CB  1 
ATOM   2360  C  CG  . ASN C  1 19  ? -10.473 -38.132 21.910  1.00 21.47 ? 19   ASN C CG  1 
ATOM   2361  O  OD1 . ASN C  1 19  ? -11.574 -38.165 21.363  1.00 24.05 ? 19   ASN C OD1 1 
ATOM   2362  N  ND2 . ASN C  1 19  ? -9.968  -39.171 22.568  1.00 21.59 ? 19   ASN C ND2 1 
ATOM   2363  N  N   . PHE C  1 20  ? -8.520  -34.382 20.084  1.00 20.35 ? 20   PHE C N   1 
ATOM   2364  C  CA  . PHE C  1 20  ? -7.830  -33.089 20.113  1.00 20.46 ? 20   PHE C CA  1 
ATOM   2365  C  C   . PHE C  1 20  ? -8.794  -32.054 20.639  1.00 22.41 ? 20   PHE C C   1 
ATOM   2366  O  O   . PHE C  1 20  ? -9.979  -32.109 20.349  1.00 25.13 ? 20   PHE C O   1 
ATOM   2367  C  CB  . PHE C  1 20  ? -7.410  -32.633 18.711  1.00 19.89 ? 20   PHE C CB  1 
ATOM   2368  C  CG  . PHE C  1 20  ? -6.673  -33.672 17.917  1.00 19.87 ? 20   PHE C CG  1 
ATOM   2369  C  CD1 . PHE C  1 20  ? -7.350  -34.737 17.340  1.00 20.25 ? 20   PHE C CD1 1 
ATOM   2370  C  CD2 . PHE C  1 20  ? -5.306  -33.571 17.724  1.00 20.18 ? 20   PHE C CD2 1 
ATOM   2371  C  CE1 . PHE C  1 20  ? -6.674  -35.694 16.603  1.00 20.86 ? 20   PHE C CE1 1 
ATOM   2372  C  CE2 . PHE C  1 20  ? -4.619  -34.525 16.985  1.00 19.10 ? 20   PHE C CE2 1 
ATOM   2373  C  CZ  . PHE C  1 20  ? -5.305  -35.587 16.421  1.00 21.55 ? 20   PHE C CZ  1 
ATOM   2374  N  N   . GLU C  1 21  ? -8.294  -31.088 21.385  1.00 23.39 ? 21   GLU C N   1 
ATOM   2375  C  CA  . GLU C  1 21  ? -9.153  -30.029 21.861  1.00 24.40 ? 21   GLU C CA  1 
ATOM   2376  C  C   . GLU C  1 21  ? -8.430  -28.703 21.986  1.00 24.47 ? 21   GLU C C   1 
ATOM   2377  O  O   . GLU C  1 21  ? -7.331  -28.626 22.506  1.00 26.46 ? 21   GLU C O   1 
ATOM   2378  C  CB  . GLU C  1 21  ? -9.762  -30.416 23.198  1.00 29.87 ? 21   GLU C CB  1 
ATOM   2379  C  CG  . GLU C  1 21  ? -10.855 -29.484 23.635  1.00 33.77 ? 21   GLU C CG  1 
ATOM   2380  C  CD  . GLU C  1 21  ? -11.275 -29.757 25.049  1.00 42.26 ? 21   GLU C CD  1 
ATOM   2381  O  OE1 . GLU C  1 21  ? -11.657 -30.912 25.348  1.00 41.86 ? 21   GLU C OE1 1 
ATOM   2382  O  OE2 . GLU C  1 21  ? -11.214 -28.811 25.859  1.00 46.49 ? 21   GLU C OE2 1 
ATOM   2383  N  N   . GLN C  1 22  ? -9.059  -27.644 21.517  1.00 26.78 ? 22   GLN C N   1 
ATOM   2384  C  CA  . GLN C  1 22  ? -8.429  -26.342 21.574  1.00 29.25 ? 22   GLN C CA  1 
ATOM   2385  C  C   . GLN C  1 22  ? -9.414  -25.281 22.049  1.00 33.56 ? 22   GLN C C   1 
ATOM   2386  O  O   . GLN C  1 22  ? -10.268 -24.827 21.296  1.00 34.60 ? 22   GLN C O   1 
ATOM   2387  C  CB  . GLN C  1 22  ? -7.869  -25.980 20.211  1.00 27.26 ? 22   GLN C CB  1 
ATOM   2388  C  CG  . GLN C  1 22  ? -7.072  -24.717 20.193  1.00 30.73 ? 22   GLN C CG  1 
ATOM   2389  C  CD  . GLN C  1 22  ? -6.668  -24.355 18.791  1.00 29.99 ? 22   GLN C CD  1 
ATOM   2390  O  OE1 . GLN C  1 22  ? -7.363  -24.690 17.843  1.00 29.14 ? 22   GLN C OE1 1 
ATOM   2391  N  NE2 . GLN C  1 22  ? -5.536  -23.680 18.647  1.00 31.16 ? 22   GLN C NE2 1 
ATOM   2392  N  N   . LYS C  1 23  ? -9.284  -24.892 23.309  1.00 36.85 ? 23   LYS C N   1 
ATOM   2393  C  CA  . LYS C  1 23  ? -10.161 -23.891 23.901  1.00 41.69 ? 23   LYS C CA  1 
ATOM   2394  C  C   . LYS C  1 23  ? -10.037 -22.524 23.226  1.00 40.84 ? 23   LYS C C   1 
ATOM   2395  O  O   . LYS C  1 23  ? -11.035 -21.926 22.838  1.00 43.41 ? 23   LYS C O   1 
ATOM   2396  C  CB  . LYS C  1 23  ? -9.894  -23.778 25.407  1.00 45.12 ? 23   LYS C CB  1 
ATOM   2397  C  CG  . LYS C  1 23  ? -10.241 -25.038 26.193  1.00 45.50 ? 23   LYS C CG  1 
ATOM   2398  C  CD  . LYS C  1 23  ? -11.727 -25.367 26.078  1.00 47.91 ? 23   LYS C CD  1 
ATOM   2399  C  CE  . LYS C  1 23  ? -12.156 -26.447 27.075  1.00 51.64 ? 23   LYS C CE  1 
ATOM   2400  N  NZ  . LYS C  1 23  ? -11.886 -26.095 28.501  1.00 51.35 ? 23   LYS C NZ  1 
ATOM   2401  N  N   . GLU C  1 24  ? -8.810  -22.041 23.075  1.00 42.27 ? 24   GLU C N   1 
ATOM   2402  C  CA  . GLU C  1 24  ? -8.571  -20.723 22.495  1.00 43.35 ? 24   GLU C CA  1 
ATOM   2403  C  C   . GLU C  1 24  ? -8.130  -20.826 21.045  1.00 41.22 ? 24   GLU C C   1 
ATOM   2404  O  O   . GLU C  1 24  ? -7.286  -21.650 20.714  1.00 40.53 ? 24   GLU C O   1 
ATOM   2405  C  CB  . GLU C  1 24  ? -7.492  -19.984 23.286  1.00 50.11 ? 24   GLU C CB  1 
ATOM   2406  C  CG  . GLU C  1 24  ? -7.615  -20.120 24.794  1.00 53.37 ? 24   GLU C CG  1 
ATOM   2407  C  CD  . GLU C  1 24  ? -8.867  -19.453 25.328  1.00 62.46 ? 24   GLU C CD  1 
ATOM   2408  O  OE1 . GLU C  1 24  ? -9.283  -19.788 26.465  1.00 66.25 ? 24   GLU C OE1 1 
ATOM   2409  O  OE2 . GLU C  1 24  ? -9.432  -18.597 24.604  1.00 62.40 ? 24   GLU C OE2 1 
ATOM   2410  N  N   . SER C  1 25  ? -8.681  -19.962 20.196  1.00 42.70 ? 25   SER C N   1 
ATOM   2411  C  CA  . SER C  1 25  ? -8.435  -20.010 18.755  1.00 44.39 ? 25   SER C CA  1 
ATOM   2412  C  C   . SER C  1 25  ? -6.964  -20.276 18.415  1.00 43.17 ? 25   SER C C   1 
ATOM   2413  O  O   . SER C  1 25  ? -6.644  -21.234 17.708  1.00 44.26 ? 25   SER C O   1 
ATOM   2414  C  CB  . SER C  1 25  ? -8.929  -18.724 18.066  1.00 45.87 ? 25   SER C CB  1 
ATOM   2415  O  OG  . SER C  1 25  ? -7.866  -17.818 17.805  1.00 48.23 ? 25   SER C OG  1 
ATOM   2416  N  N   . ASN C  1 26  ? -6.069  -19.432 18.909  1.00 44.09 ? 26   ASN C N   1 
ATOM   2417  C  CA  . ASN C  1 26  ? -4.651  -19.653 18.667  1.00 46.46 ? 26   ASN C CA  1 
ATOM   2418  C  C   . ASN C  1 26  ? -3.897  -20.009 19.948  1.00 42.40 ? 26   ASN C C   1 
ATOM   2419  O  O   . ASN C  1 26  ? -2.814  -19.495 20.228  1.00 44.09 ? 26   ASN C O   1 
ATOM   2420  C  CB  . ASN C  1 26  ? -4.028  -18.470 17.923  1.00 52.96 ? 26   ASN C CB  1 
ATOM   2421  C  CG  . ASN C  1 26  ? -4.496  -18.387 16.470  1.00 53.63 ? 26   ASN C CG  1 
ATOM   2422  O  OD1 . ASN C  1 26  ? -4.420  -19.370 15.716  1.00 49.69 ? 26   ASN C OD1 1 
ATOM   2423  N  ND2 . ASN C  1 26  ? -4.984  -17.211 16.074  1.00 49.87 ? 26   ASN C ND2 1 
ATOM   2424  N  N   . GLY C  1 27  ? -4.498  -20.914 20.711  1.00 38.54 ? 27   GLY C N   1 
ATOM   2425  C  CA  . GLY C  1 27  ? -3.933  -21.385 21.953  1.00 37.41 ? 27   GLY C CA  1 
ATOM   2426  C  C   . GLY C  1 27  ? -3.562  -22.849 21.849  1.00 38.48 ? 27   GLY C C   1 
ATOM   2427  O  O   . GLY C  1 27  ? -3.637  -23.443 20.765  1.00 36.17 ? 27   GLY C O   1 
ATOM   2428  N  N   . PRO C  1 28  ? -3.168  -23.440 22.987  1.00 37.44 ? 28   PRO C N   1 
ATOM   2429  C  CA  . PRO C  1 28  ? -2.686  -24.822 23.090  1.00 34.13 ? 28   PRO C CA  1 
ATOM   2430  C  C   . PRO C  1 28  ? -3.718  -25.823 22.575  1.00 33.30 ? 28   PRO C C   1 
ATOM   2431  O  O   . PRO C  1 28  ? -4.924  -25.641 22.767  1.00 32.79 ? 28   PRO C O   1 
ATOM   2432  C  CB  . PRO C  1 28  ? -2.500  -25.025 24.598  1.00 36.67 ? 28   PRO C CB  1 
ATOM   2433  C  CG  . PRO C  1 28  ? -2.514  -23.666 25.198  1.00 36.08 ? 28   PRO C CG  1 
ATOM   2434  C  CD  . PRO C  1 28  ? -3.315  -22.798 24.305  1.00 37.19 ? 28   PRO C CD  1 
ATOM   2435  N  N   . VAL C  1 29  ? -3.242  -26.877 21.925  1.00 30.35 ? 29   VAL C N   1 
ATOM   2436  C  CA  . VAL C  1 29  ? -4.105  -27.981 21.552  1.00 27.13 ? 29   VAL C CA  1 
ATOM   2437  C  C   . VAL C  1 29  ? -3.772  -29.156 22.455  1.00 25.92 ? 29   VAL C C   1 
ATOM   2438  O  O   . VAL C  1 29  ? -2.614  -29.563 22.562  1.00 25.29 ? 29   VAL C O   1 
ATOM   2439  C  CB  . VAL C  1 29  ? -3.917  -28.363 20.077  1.00 26.33 ? 29   VAL C CB  1 
ATOM   2440  C  CG1 . VAL C  1 29  ? -4.968  -29.389 19.647  1.00 22.67 ? 29   VAL C CG1 1 
ATOM   2441  C  CG2 . VAL C  1 29  ? -3.981  -27.115 19.205  1.00 24.20 ? 29   VAL C CG2 1 
ATOM   2442  N  N   . LYS C  1 30  ? -4.782  -29.672 23.138  1.00 22.83 ? 30   LYS C N   1 
ATOM   2443  C  CA  . LYS C  1 30  ? -4.603  -30.832 23.995  1.00 23.91 ? 30   LYS C CA  1 
ATOM   2444  C  C   . LYS C  1 30  ? -4.894  -32.077 23.151  1.00 22.79 ? 30   LYS C C   1 
ATOM   2445  O  O   . LYS C  1 30  ? -5.895  -32.126 22.443  1.00 21.93 ? 30   LYS C O   1 
ATOM   2446  C  CB  . LYS C  1 30  ? -5.525  -30.726 25.225  1.00 26.92 ? 30   LYS C CB  1 
ATOM   2447  C  CG  . LYS C  1 30  ? -5.390  -31.845 26.255  1.00 32.04 ? 30   LYS C CG  1 
ATOM   2448  C  CD  . LYS C  1 30  ? -6.664  -32.002 27.107  1.00 39.84 ? 30   LYS C CD  1 
ATOM   2449  C  CE  . LYS C  1 30  ? -6.698  -33.328 27.889  1.00 36.10 ? 30   LYS C CE  1 
ATOM   2450  N  NZ  . LYS C  1 30  ? -7.972  -33.486 28.653  1.00 33.72 ? 30   LYS C NZ  1 
ATOM   2451  N  N   . VAL C  1 31  ? -4.000  -33.061 23.203  1.00 22.14 ? 31   VAL C N   1 
ATOM   2452  C  CA  . VAL C  1 31  ? -4.102  -34.260 22.371  1.00 21.85 ? 31   VAL C CA  1 
ATOM   2453  C  C   . VAL C  1 31  ? -4.094  -35.469 23.301  1.00 21.76 ? 31   VAL C C   1 
ATOM   2454  O  O   . VAL C  1 31  ? -3.160  -35.642 24.064  1.00 26.16 ? 31   VAL C O   1 
ATOM   2455  C  CB  . VAL C  1 31  ? -2.912  -34.356 21.345  1.00 20.47 ? 31   VAL C CB  1 
ATOM   2456  C  CG1 . VAL C  1 31  ? -2.976  -35.637 20.515  1.00 15.15 ? 31   VAL C CG1 1 
ATOM   2457  C  CG2 . VAL C  1 31  ? -2.855  -33.127 20.440  1.00 19.46 ? 31   VAL C CG2 1 
ATOM   2458  N  N   . TRP C  1 32  ? -5.139  -36.287 23.281  1.00 20.00 ? 32   TRP C N   1 
ATOM   2459  C  CA  . TRP C  1 32  ? -5.161  -37.449 24.162  1.00 21.44 ? 32   TRP C CA  1 
ATOM   2460  C  C   . TRP C  1 32  ? -5.815  -38.643 23.506  1.00 19.27 ? 32   TRP C C   1 
ATOM   2461  O  O   . TRP C  1 32  ? -6.521  -38.499 22.520  1.00 21.88 ? 32   TRP C O   1 
ATOM   2462  C  CB  . TRP C  1 32  ? -5.825  -37.131 25.515  1.00 22.15 ? 32   TRP C CB  1 
ATOM   2463  C  CG  . TRP C  1 32  ? -7.318  -37.091 25.492  1.00 22.12 ? 32   TRP C CG  1 
ATOM   2464  C  CD1 . TRP C  1 32  ? -8.177  -38.095 25.853  1.00 21.85 ? 32   TRP C CD1 1 
ATOM   2465  C  CD2 . TRP C  1 32  ? -8.135  -35.987 25.090  1.00 23.68 ? 32   TRP C CD2 1 
ATOM   2466  N  NE1 . TRP C  1 32  ? -9.478  -37.680 25.694  1.00 24.37 ? 32   TRP C NE1 1 
ATOM   2467  C  CE2 . TRP C  1 32  ? -9.479  -36.391 25.223  1.00 24.39 ? 32   TRP C CE2 1 
ATOM   2468  C  CE3 . TRP C  1 32  ? -7.860  -34.696 24.626  1.00 26.29 ? 32   TRP C CE3 1 
ATOM   2469  C  CZ2 . TRP C  1 32  ? -10.548 -35.544 24.910  1.00 29.66 ? 32   TRP C CZ2 1 
ATOM   2470  C  CZ3 . TRP C  1 32  ? -8.932  -33.852 24.311  1.00 27.07 ? 32   TRP C CZ3 1 
ATOM   2471  C  CH2 . TRP C  1 32  ? -10.254 -34.283 24.455  1.00 27.72 ? 32   TRP C CH2 1 
ATOM   2472  N  N   . GLY C  1 33  ? -5.564  -39.827 24.047  1.00 17.29 ? 33   GLY C N   1 
ATOM   2473  C  CA  . GLY C  1 33  ? -6.164  -41.029 23.520  1.00 19.53 ? 33   GLY C CA  1 
ATOM   2474  C  C   . GLY C  1 33  ? -5.317  -42.247 23.790  1.00 18.87 ? 33   GLY C C   1 
ATOM   2475  O  O   . GLY C  1 33  ? -4.453  -42.216 24.638  1.00 20.97 ? 33   GLY C O   1 
ATOM   2476  N  N   . SER C  1 34  ? -5.574  -43.332 23.077  1.00 18.71 ? 34   SER C N   1 
ATOM   2477  C  CA  . SER C  1 34  ? -4.704  -44.492 23.166  1.00 22.03 ? 34   SER C CA  1 
ATOM   2478  C  C   . SER C  1 34  ? -4.557  -45.229 21.830  1.00 21.11 ? 34   SER C C   1 
ATOM   2479  O  O   . SER C  1 34  ? -5.397  -45.108 20.941  1.00 23.36 ? 34   SER C O   1 
ATOM   2480  C  CB  . SER C  1 34  ? -5.127  -45.440 24.305  1.00 23.86 ? 34   SER C CB  1 
ATOM   2481  O  OG  . SER C  1 34  ? -6.263  -46.213 23.969  1.00 23.85 ? 34   SER C OG  1 
ATOM   2482  N  N   . ILE C  1 35  ? -3.459  -45.967 21.708  1.00 21.56 ? 35   ILE C N   1 
ATOM   2483  C  CA  . ILE C  1 35  ? -3.155  -46.784 20.552  1.00 19.21 ? 35   ILE C CA  1 
ATOM   2484  C  C   . ILE C  1 35  ? -2.792  -48.176 21.063  1.00 19.36 ? 35   ILE C C   1 
ATOM   2485  O  O   . ILE C  1 35  ? -2.166  -48.319 22.101  1.00 20.71 ? 35   ILE C O   1 
ATOM   2486  C  CB  . ILE C  1 35  ? -1.970  -46.187 19.769  1.00 18.48 ? 35   ILE C CB  1 
ATOM   2487  C  CG1 . ILE C  1 35  ? -2.203  -44.689 19.525  1.00 19.72 ? 35   ILE C CG1 1 
ATOM   2488  C  CG2 . ILE C  1 35  ? -1.731  -46.952 18.475  1.00 17.78 ? 35   ILE C CG2 1 
ATOM   2489  C  CD1 . ILE C  1 35  ? -0.980  -43.938 19.056  1.00 16.90 ? 35   ILE C CD1 1 
ATOM   2490  N  N   . LYS C  1 36  ? -3.192  -49.209 20.340  1.00 21.12 ? 36   LYS C N   1 
ATOM   2491  C  CA  . LYS C  1 36  ? -2.875  -50.568 20.749  1.00 22.19 ? 36   LYS C CA  1 
ATOM   2492  C  C   . LYS C  1 36  ? -2.236  -51.322 19.586  1.00 19.05 ? 36   LYS C C   1 
ATOM   2493  O  O   . LYS C  1 36  ? -2.188  -50.813 18.478  1.00 15.11 ? 36   LYS C O   1 
ATOM   2494  C  CB  . LYS C  1 36  ? -4.131  -51.279 21.249  1.00 23.37 ? 36   LYS C CB  1 
ATOM   2495  C  CG  . LYS C  1 36  ? -5.252  -51.375 20.216  1.00 23.92 ? 36   LYS C CG  1 
ATOM   2496  C  CD  . LYS C  1 36  ? -6.560  -51.731 20.900  1.00 29.26 ? 36   LYS C CD  1 
ATOM   2497  C  CE  . LYS C  1 36  ? -7.442  -52.570 19.999  1.00 34.63 ? 36   LYS C CE  1 
ATOM   2498  N  NZ  . LYS C  1 36  ? -8.400  -53.372 20.819  1.00 34.30 ? 36   LYS C NZ  1 
ATOM   2499  N  N   . GLY C  1 37  ? -1.723  -52.520 19.857  1.00 21.52 ? 37   GLY C N   1 
ATOM   2500  C  CA  . GLY C  1 37  ? -1.065  -53.335 18.844  1.00 18.09 ? 37   GLY C CA  1 
ATOM   2501  C  C   . GLY C  1 37  ? 0.379   -52.949 18.597  1.00 18.39 ? 37   GLY C C   1 
ATOM   2502  O  O   . GLY C  1 37  ? 1.007   -53.441 17.663  1.00 20.16 ? 37   GLY C O   1 
ATOM   2503  N  N   . LEU C  1 38  ? 0.907   -52.075 19.449  1.00 19.19 ? 38   LEU C N   1 
ATOM   2504  C  CA  . LEU C  1 38  ? 2.254   -51.536 19.298  1.00 18.51 ? 38   LEU C CA  1 
ATOM   2505  C  C   . LEU C  1 38  ? 3.317   -52.371 20.017  1.00 20.92 ? 38   LEU C C   1 
ATOM   2506  O  O   . LEU C  1 38  ? 3.037   -53.073 20.987  1.00 22.15 ? 38   LEU C O   1 
ATOM   2507  C  CB  . LEU C  1 38  ? 2.316   -50.089 19.821  1.00 16.51 ? 38   LEU C CB  1 
ATOM   2508  C  CG  . LEU C  1 38  ? 1.658   -48.978 19.000  1.00 14.47 ? 38   LEU C CG  1 
ATOM   2509  C  CD1 . LEU C  1 38  ? 1.611   -47.694 19.811  1.00 15.31 ? 38   LEU C CD1 1 
ATOM   2510  C  CD2 . LEU C  1 38  ? 2.370   -48.773 17.656  1.00 11.64 ? 38   LEU C CD2 1 
ATOM   2511  N  N   . THR C  1 39  ? 4.548   -52.289 19.528  1.00 21.40 ? 39   THR C N   1 
ATOM   2512  C  CA  . THR C  1 39  ? 5.674   -52.866 20.237  1.00 22.13 ? 39   THR C CA  1 
ATOM   2513  C  C   . THR C  1 39  ? 6.062   -51.952 21.395  1.00 22.27 ? 39   THR C C   1 
ATOM   2514  O  O   . THR C  1 39  ? 6.079   -50.718 21.253  1.00 20.47 ? 39   THR C O   1 
ATOM   2515  C  CB  . THR C  1 39  ? 6.874   -53.069 19.294  1.00 22.54 ? 39   THR C CB  1 
ATOM   2516  O  OG1 . THR C  1 39  ? 7.008   -51.922 18.441  1.00 22.70 ? 39   THR C OG1 1 
ATOM   2517  C  CG2 . THR C  1 39  ? 6.657   -54.292 18.415  1.00 20.29 ? 39   THR C CG2 1 
ATOM   2518  N  N   . GLU C  1 40  ? 6.344   -52.569 22.544  1.00 23.53 ? 40   GLU C N   1 
ATOM   2519  C  CA  . GLU C  1 40  ? 6.819   -51.861 23.730  1.00 21.39 ? 40   GLU C CA  1 
ATOM   2520  C  C   . GLU C  1 40  ? 7.906   -50.861 23.360  1.00 21.29 ? 40   GLU C C   1 
ATOM   2521  O  O   . GLU C  1 40  ? 8.802   -51.166 22.568  1.00 23.71 ? 40   GLU C O   1 
ATOM   2522  C  CB  . GLU C  1 40  ? 7.366   -52.861 24.747  1.00 20.57 ? 40   GLU C CB  1 
ATOM   2523  C  CG  . GLU C  1 40  ? 7.960   -52.225 25.982  1.00 24.91 ? 40   GLU C CG  1 
ATOM   2524  C  CD  . GLU C  1 40  ? 8.424   -53.237 27.027  1.00 30.17 ? 40   GLU C CD  1 
ATOM   2525  O  OE1 . GLU C  1 40  ? 8.725   -54.408 26.682  1.00 30.79 ? 40   GLU C OE1 1 
ATOM   2526  O  OE2 . GLU C  1 40  ? 8.491   -52.848 28.209  1.00 31.51 ? 40   GLU C OE2 1 
ATOM   2527  N  N   . GLY C  1 41  ? 7.830   -49.662 23.923  1.00 20.34 ? 41   GLY C N   1 
ATOM   2528  C  CA  . GLY C  1 41  ? 8.830   -48.651 23.643  1.00 19.45 ? 41   GLY C CA  1 
ATOM   2529  C  C   . GLY C  1 41  ? 8.288   -47.420 22.954  1.00 19.62 ? 41   GLY C C   1 
ATOM   2530  O  O   . GLY C  1 41  ? 7.087   -47.186 22.965  1.00 19.17 ? 41   GLY C O   1 
ATOM   2531  N  N   . LEU C  1 42  ? 9.183   -46.643 22.348  1.00 19.23 ? 42   LEU C N   1 
ATOM   2532  C  CA  . LEU C  1 42  ? 8.857   -45.329 21.800  1.00 19.25 ? 42   LEU C CA  1 
ATOM   2533  C  C   . LEU C  1 42  ? 8.552   -45.386 20.309  1.00 18.17 ? 42   LEU C C   1 
ATOM   2534  O  O   . LEU C  1 42  ? 9.231   -46.087 19.565  1.00 19.56 ? 42   LEU C O   1 
ATOM   2535  C  CB  . LEU C  1 42  ? 10.004  -44.331 22.043  1.00 18.99 ? 42   LEU C CB  1 
ATOM   2536  C  CG  . LEU C  1 42  ? 10.211  -43.788 23.456  1.00 19.34 ? 42   LEU C CG  1 
ATOM   2537  C  CD1 . LEU C  1 42  ? 11.211  -42.667 23.445  1.00 19.10 ? 42   LEU C CD1 1 
ATOM   2538  C  CD2 . LEU C  1 42  ? 8.908   -43.291 24.021  1.00 22.61 ? 42   LEU C CD2 1 
ATOM   2539  N  N   . HIS C  1 43  ? 7.531   -44.636 19.888  1.00 19.30 ? 43   HIS C N   1 
ATOM   2540  C  CA  . HIS C  1 43  ? 7.080   -44.587 18.493  1.00 17.69 ? 43   HIS C CA  1 
ATOM   2541  C  C   . HIS C  1 43  ? 6.858   -43.160 18.006  1.00 17.12 ? 43   HIS C C   1 
ATOM   2542  O  O   . HIS C  1 43  ? 6.232   -42.362 18.701  1.00 18.01 ? 43   HIS C O   1 
ATOM   2543  C  CB  . HIS C  1 43  ? 5.780   -45.371 18.343  1.00 17.47 ? 43   HIS C CB  1 
ATOM   2544  C  CG  . HIS C  1 43  ? 5.939   -46.836 18.594  1.00 18.05 ? 43   HIS C CG  1 
ATOM   2545  N  ND1 . HIS C  1 43  ? 6.097   -47.748 17.572  1.00 16.52 ? 43   HIS C ND1 1 
ATOM   2546  C  CD2 . HIS C  1 43  ? 5.983   -47.543 19.748  1.00 17.89 ? 43   HIS C CD2 1 
ATOM   2547  C  CE1 . HIS C  1 43  ? 6.225   -48.957 18.088  1.00 17.66 ? 43   HIS C CE1 1 
ATOM   2548  N  NE2 . HIS C  1 43  ? 6.163   -48.861 19.406  1.00 17.42 ? 43   HIS C NE2 1 
ATOM   2549  N  N   . GLY C  1 44  ? 7.361   -42.842 16.814  1.00 17.03 ? 44   GLY C N   1 
ATOM   2550  C  CA  . GLY C  1 44  ? 7.195   -41.513 16.242  1.00 15.41 ? 44   GLY C CA  1 
ATOM   2551  C  C   . GLY C  1 44  ? 5.724   -41.195 16.070  1.00 18.23 ? 44   GLY C C   1 
ATOM   2552  O  O   . GLY C  1 44  ? 4.942   -42.074 15.740  1.00 18.66 ? 44   GLY C O   1 
ATOM   2553  N  N   . PHE C  1 45  ? 5.338   -39.945 16.301  1.00 17.97 ? 45   PHE C N   1 
ATOM   2554  C  CA  . PHE C  1 45  ? 3.926   -39.565 16.296  1.00 16.75 ? 45   PHE C CA  1 
ATOM   2555  C  C   . PHE C  1 45  ? 3.798   -38.177 15.671  1.00 18.77 ? 45   PHE C C   1 
ATOM   2556  O  O   . PHE C  1 45  ? 4.063   -37.163 16.322  1.00 17.29 ? 45   PHE C O   1 
ATOM   2557  C  CB  . PHE C  1 45  ? 3.391   -39.598 17.729  1.00 18.43 ? 45   PHE C CB  1 
ATOM   2558  C  CG  . PHE C  1 45  ? 1.893   -39.462 17.848  1.00 19.30 ? 45   PHE C CG  1 
ATOM   2559  C  CD1 . PHE C  1 45  ? 1.040   -40.436 17.335  1.00 17.76 ? 45   PHE C CD1 1 
ATOM   2560  C  CD2 . PHE C  1 45  ? 1.336   -38.372 18.515  1.00 18.00 ? 45   PHE C CD2 1 
ATOM   2561  C  CE1 . PHE C  1 45  ? -0.341  -40.313 17.468  1.00 17.58 ? 45   PHE C CE1 1 
ATOM   2562  C  CE2 . PHE C  1 45  ? -0.050  -38.241 18.644  1.00 17.89 ? 45   PHE C CE2 1 
ATOM   2563  C  CZ  . PHE C  1 45  ? -0.883  -39.213 18.125  1.00 18.69 ? 45   PHE C CZ  1 
ATOM   2564  N  N   . HIS C  1 46  ? 3.412   -38.145 14.394  1.00 18.37 ? 46   HIS C N   1 
ATOM   2565  C  CA  . HIS C  1 46  ? 3.515   -36.927 13.589  1.00 19.89 ? 46   HIS C CA  1 
ATOM   2566  C  C   . HIS C  1 46  ? 2.262   -36.637 12.786  1.00 20.54 ? 46   HIS C C   1 
ATOM   2567  O  O   . HIS C  1 46  ? 1.590   -37.555 12.317  1.00 22.37 ? 46   HIS C O   1 
ATOM   2568  C  CB  . HIS C  1 46  ? 4.698   -37.015 12.622  1.00 17.88 ? 46   HIS C CB  1 
ATOM   2569  C  CG  . HIS C  1 46  ? 5.977   -37.424 13.280  1.00 22.06 ? 46   HIS C CG  1 
ATOM   2570  N  ND1 . HIS C  1 46  ? 6.609   -38.620 13.003  1.00 20.69 ? 46   HIS C ND1 1 
ATOM   2571  C  CD2 . HIS C  1 46  ? 6.729   -36.809 14.226  1.00 18.13 ? 46   HIS C CD2 1 
ATOM   2572  C  CE1 . HIS C  1 46  ? 7.701   -38.715 13.742  1.00 18.00 ? 46   HIS C CE1 1 
ATOM   2573  N  NE2 . HIS C  1 46  ? 7.795   -37.632 14.494  1.00 17.93 ? 46   HIS C NE2 1 
ATOM   2574  N  N   . VAL C  1 47  ? 1.961   -35.351 12.632  1.00 18.78 ? 47   VAL C N   1 
ATOM   2575  C  CA  . VAL C  1 47  ? 0.943   -34.911 11.692  1.00 19.75 ? 47   VAL C CA  1 
ATOM   2576  C  C   . VAL C  1 47  ? 1.583   -34.807 10.316  1.00 17.06 ? 47   VAL C C   1 
ATOM   2577  O  O   . VAL C  1 47  ? 2.586   -34.125 10.141  1.00 17.99 ? 47   VAL C O   1 
ATOM   2578  C  CB  . VAL C  1 47  ? 0.334   -33.540 12.078  1.00 19.50 ? 47   VAL C CB  1 
ATOM   2579  C  CG1 . VAL C  1 47  ? -0.882  -33.248 11.227  1.00 16.79 ? 47   VAL C CG1 1 
ATOM   2580  C  CG2 . VAL C  1 47  ? -0.021  -33.503 13.560  1.00 19.32 ? 47   VAL C CG2 1 
ATOM   2581  N  N   . HIS C  1 48  ? 1.000   -35.510 9.347   1.00 20.43 ? 48   HIS C N   1 
ATOM   2582  C  CA  . HIS C  1 48  ? 1.445   -35.474 7.962   1.00 17.78 ? 48   HIS C CA  1 
ATOM   2583  C  C   . HIS C  1 48  ? 0.551   -34.547 7.148   1.00 19.07 ? 48   HIS C C   1 
ATOM   2584  O  O   . HIS C  1 48  ? -0.597  -34.284 7.526   1.00 18.04 ? 48   HIS C O   1 
ATOM   2585  C  CB  . HIS C  1 48  ? 1.457   -36.884 7.371   1.00 17.85 ? 48   HIS C CB  1 
ATOM   2586  C  CG  . HIS C  1 48  ? 2.593   -37.721 7.856   1.00 18.48 ? 48   HIS C CG  1 
ATOM   2587  N  ND1 . HIS C  1 48  ? 3.555   -38.231 7.012   1.00 20.07 ? 48   HIS C ND1 1 
ATOM   2588  C  CD2 . HIS C  1 48  ? 2.947   -38.103 9.106   1.00 17.30 ? 48   HIS C CD2 1 
ATOM   2589  C  CE1 . HIS C  1 48  ? 4.444   -38.905 7.720   1.00 20.28 ? 48   HIS C CE1 1 
ATOM   2590  N  NE2 . HIS C  1 48  ? 4.097   -38.845 8.993   1.00 17.32 ? 48   HIS C NE2 1 
ATOM   2591  N  N   . GLU C  1 49  ? 1.074   -34.085 6.015   1.00 19.61 ? 49   GLU C N   1 
ATOM   2592  C  CA  . GLU C  1 49  ? 0.462   -32.992 5.260   1.00 21.07 ? 49   GLU C CA  1 
ATOM   2593  C  C   . GLU C  1 49  ? -0.931  -33.262 4.690   1.00 21.04 ? 49   GLU C C   1 
ATOM   2594  O  O   . GLU C  1 49  ? -1.823  -32.416 4.819   1.00 20.32 ? 49   GLU C O   1 
ATOM   2595  C  CB  . GLU C  1 49  ? 1.400   -32.510 4.144   1.00 22.58 ? 49   GLU C CB  1 
ATOM   2596  C  CG  . GLU C  1 49  ? 1.098   -31.094 3.679   1.00 24.15 ? 49   GLU C CG  1 
ATOM   2597  C  CD  . GLU C  1 49  ? 1.900   -30.682 2.444   1.00 29.45 ? 49   GLU C CD  1 
ATOM   2598  O  OE1 . GLU C  1 49  ? 3.044   -31.178 2.260   1.00 29.75 ? 49   GLU C OE1 1 
ATOM   2599  O  OE2 . GLU C  1 49  ? 1.374   -29.852 1.662   1.00 28.01 ? 49   GLU C OE2 1 
ATOM   2600  N  N   . PHE C  1 50  ? -1.132  -34.412 4.046   1.00 19.71 ? 50   PHE C N   1 
ATOM   2601  C  CA  . PHE C  1 50  ? -2.412  -34.639 3.370   1.00 18.90 ? 50   PHE C CA  1 
ATOM   2602  C  C   . PHE C  1 50  ? -3.339  -35.633 4.075   1.00 17.42 ? 50   PHE C C   1 
ATOM   2603  O  O   . PHE C  1 50  ? -2.890  -36.646 4.605   1.00 19.25 ? 50   PHE C O   1 
ATOM   2604  C  CB  . PHE C  1 50  ? -2.197  -35.016 1.886   1.00 20.00 ? 50   PHE C CB  1 
ATOM   2605  C  CG  . PHE C  1 50  ? -1.189  -34.146 1.196   1.00 21.66 ? 50   PHE C CG  1 
ATOM   2606  C  CD1 . PHE C  1 50  ? -1.479  -32.815 0.916   1.00 22.05 ? 50   PHE C CD1 1 
ATOM   2607  C  CD2 . PHE C  1 50  ? 0.066   -34.643 0.860   1.00 21.22 ? 50   PHE C CD2 1 
ATOM   2608  C  CE1 . PHE C  1 50  ? -0.535  -32.008 0.305   1.00 24.49 ? 50   PHE C CE1 1 
ATOM   2609  C  CE2 . PHE C  1 50  ? 1.009   -33.840 0.251   1.00 22.28 ? 50   PHE C CE2 1 
ATOM   2610  C  CZ  . PHE C  1 50  ? 0.712   -32.524 -0.028  1.00 23.67 ? 50   PHE C CZ  1 
ATOM   2611  N  N   . GLY C  1 51  ? -4.636  -35.328 4.071   1.00 17.21 ? 51   GLY C N   1 
ATOM   2612  C  CA  . GLY C  1 51  ? -5.657  -36.246 4.546   1.00 16.12 ? 51   GLY C CA  1 
ATOM   2613  C  C   . GLY C  1 51  ? -6.105  -37.164 3.424   1.00 19.22 ? 51   GLY C C   1 
ATOM   2614  O  O   . GLY C  1 51  ? -7.302  -37.308 3.142   1.00 16.82 ? 51   GLY C O   1 
ATOM   2615  N  N   . ASP C  1 52  ? -5.117  -37.783 2.786   1.00 19.48 ? 52   ASP C N   1 
ATOM   2616  C  CA  . ASP C  1 52  ? -5.316  -38.610 1.599   1.00 19.56 ? 52   ASP C CA  1 
ATOM   2617  C  C   . ASP C  1 52  ? -4.946  -40.069 1.907   1.00 21.41 ? 52   ASP C C   1 
ATOM   2618  O  O   . ASP C  1 52  ? -3.769  -40.388 2.103   1.00 22.93 ? 52   ASP C O   1 
ATOM   2619  C  CB  . ASP C  1 52  ? -4.462  -38.051 0.445   1.00 18.23 ? 52   ASP C CB  1 
ATOM   2620  C  CG  . ASP C  1 52  ? -4.648  -38.810 -0.862  1.00 20.37 ? 52   ASP C CG  1 
ATOM   2621  O  OD1 . ASP C  1 52  ? -5.003  -40.010 -0.833  1.00 21.44 ? 52   ASP C OD1 1 
ATOM   2622  O  OD2 . ASP C  1 52  ? -4.418  -38.206 -1.928  1.00 20.13 ? 52   ASP C OD2 1 
ATOM   2623  N  N   . ASN C  1 53  ? -5.949  -40.947 1.958   1.00 20.73 ? 53   ASN C N   1 
ATOM   2624  C  CA  . ASN C  1 53  ? -5.734  -42.368 2.256   1.00 20.01 ? 53   ASN C CA  1 
ATOM   2625  C  C   . ASN C  1 53  ? -5.980  -43.241 1.021   1.00 22.38 ? 53   ASN C C   1 
ATOM   2626  O  O   . ASN C  1 53  ? -6.311  -44.422 1.136   1.00 21.67 ? 53   ASN C O   1 
ATOM   2627  C  CB  . ASN C  1 53  ? -6.652  -42.818 3.403   1.00 20.79 ? 53   ASN C CB  1 
ATOM   2628  C  CG  . ASN C  1 53  ? -6.226  -44.147 4.025   1.00 25.90 ? 53   ASN C CG  1 
ATOM   2629  O  OD1 . ASN C  1 53  ? -5.255  -44.205 4.783   1.00 31.38 ? 53   ASN C OD1 1 
ATOM   2630  N  ND2 . ASN C  1 53  ? -6.966  -45.214 3.728   1.00 27.06 ? 53   ASN C ND2 1 
ATOM   2631  N  N   . THR C  1 54  ? -5.823  -42.659 -0.165  1.00 20.60 ? 54   THR C N   1 
ATOM   2632  C  CA  . THR C  1 54  ? -6.063  -43.410 -1.400  1.00 23.33 ? 54   THR C CA  1 
ATOM   2633  C  C   . THR C  1 54  ? -5.073  -44.562 -1.565  1.00 23.64 ? 54   THR C C   1 
ATOM   2634  O  O   . THR C  1 54  ? -5.409  -45.612 -2.100  1.00 26.83 ? 54   THR C O   1 
ATOM   2635  C  CB  . THR C  1 54  ? -6.033  -42.501 -2.647  1.00 20.86 ? 54   THR C CB  1 
ATOM   2636  O  OG1 . THR C  1 54  ? -4.839  -41.712 -2.636  1.00 19.61 ? 54   THR C OG1 1 
ATOM   2637  C  CG2 . THR C  1 54  ? -7.236  -41.569 -2.642  1.00 22.84 ? 54   THR C CG2 1 
ATOM   2638  N  N   . ALA C  1 55  ? -3.854  -44.365 -1.081  1.00 25.84 ? 55   ALA C N   1 
ATOM   2639  C  CA  . ALA C  1 55  ? -2.834  -45.400 -1.162  1.00 26.16 ? 55   ALA C CA  1 
ATOM   2640  C  C   . ALA C  1 55  ? -2.274  -45.799 0.201   1.00 24.70 ? 55   ALA C C   1 
ATOM   2641  O  O   . ALA C  1 55  ? -1.078  -46.025 0.325   1.00 31.49 ? 55   ALA C O   1 
ATOM   2642  C  CB  . ALA C  1 55  ? -1.696  -44.954 -2.094  1.00 28.09 ? 55   ALA C CB  1 
ATOM   2643  N  N   . GLY C  1 56  ? -3.131  -45.907 1.208   1.00 23.57 ? 56   GLY C N   1 
ATOM   2644  C  CA  . GLY C  1 56  ? -2.684  -46.210 2.553   1.00 23.46 ? 56   GLY C CA  1 
ATOM   2645  C  C   . GLY C  1 56  ? -2.043  -44.994 3.193   1.00 26.91 ? 56   GLY C C   1 
ATOM   2646  O  O   . GLY C  1 56  ? -2.307  -43.857 2.787   1.00 24.23 ? 56   GLY C O   1 
ATOM   2647  N  N   . CYS C  1 57  ? -1.181  -45.222 4.180   1.00 26.45 ? 57   CYS C N   1 
ATOM   2648  C  CA  . CYS C  1 57  ? -0.574  -44.114 4.914   1.00 24.54 ? 57   CYS C CA  1 
ATOM   2649  C  C   . CYS C  1 57  ? 0.408   -43.314 4.048   1.00 21.11 ? 57   CYS C C   1 
ATOM   2650  O  O   . CYS C  1 57  ? 0.678   -42.141 4.318   1.00 22.35 ? 57   CYS C O   1 
ATOM   2651  C  CB  . CYS C  1 57  ? 0.102   -44.610 6.209   1.00 27.87 ? 57   CYS C CB  1 
ATOM   2652  S  SG  . CYS C  1 57  ? -0.929  -45.677 7.284   1.00 24.64 ? 57   CYS C SG  1 
ATOM   2653  N  N   . THR C  1 58  ? 0.921   -43.940 2.998   1.00 21.62 ? 58   THR C N   1 
ATOM   2654  C  CA  . THR C  1 58  ? 1.891   -43.294 2.111   1.00 23.43 ? 58   THR C CA  1 
ATOM   2655  C  C   . THR C  1 58  ? 1.431   -41.958 1.501   1.00 23.35 ? 58   THR C C   1 
ATOM   2656  O  O   . THR C  1 58  ? 2.207   -40.995 1.484   1.00 24.42 ? 58   THR C O   1 
ATOM   2657  C  CB  . THR C  1 58  ? 2.370   -44.276 1.015   1.00 26.19 ? 58   THR C CB  1 
ATOM   2658  O  OG1 . THR C  1 58  ? 3.011   -45.399 1.635   1.00 30.25 ? 58   THR C OG1 1 
ATOM   2659  C  CG2 . THR C  1 58  ? 3.354   -43.614 0.078   1.00 23.69 ? 58   THR C CG2 1 
ATOM   2660  N  N   . SER C  1 59  ? 0.182   -41.900 1.015   1.00 23.73 ? 59   SER C N   1 
ATOM   2661  C  CA  . SER C  1 59  ? -0.408  -40.677 0.424   1.00 19.26 ? 59   SER C CA  1 
ATOM   2662  C  C   . SER C  1 59  ? -0.578  -39.492 1.383   1.00 21.57 ? 59   SER C C   1 
ATOM   2663  O  O   . SER C  1 59  ? -0.897  -38.377 0.956   1.00 20.21 ? 59   SER C O   1 
ATOM   2664  C  CB  . SER C  1 59  ? -1.744  -40.985 -0.255  1.00 20.07 ? 59   SER C CB  1 
ATOM   2665  O  OG  . SER C  1 59  ? -2.302  -42.189 0.242   1.00 20.92 ? 59   SER C OG  1 
ATOM   2666  N  N   . ALA C  1 60  ? -0.350  -39.741 2.670   1.00 21.98 ? 60   ALA C N   1 
ATOM   2667  C  CA  . ALA C  1 60  ? -0.359  -38.697 3.690   1.00 20.33 ? 60   ALA C CA  1 
ATOM   2668  C  C   . ALA C  1 60  ? 0.748   -37.663 3.448   1.00 20.80 ? 60   ALA C C   1 
ATOM   2669  O  O   . ALA C  1 60  ? 0.675   -36.531 3.936   1.00 19.06 ? 60   ALA C O   1 
ATOM   2670  C  CB  . ALA C  1 60  ? -0.213  -39.320 5.067   1.00 18.29 ? 60   ALA C CB  1 
ATOM   2671  N  N   . GLY C  1 61  ? 1.766   -38.065 2.689   1.00 22.61 ? 61   GLY C N   1 
ATOM   2672  C  CA  . GLY C  1 61  ? 2.886   -37.201 2.364   1.00 22.23 ? 61   GLY C CA  1 
ATOM   2673  C  C   . GLY C  1 61  ? 3.911   -37.024 3.466   1.00 23.90 ? 61   GLY C C   1 
ATOM   2674  O  O   . GLY C  1 61  ? 4.054   -37.885 4.348   1.00 24.44 ? 61   GLY C O   1 
ATOM   2675  N  N   . PRO C  1 62  ? 4.637   -35.895 3.424   1.00 21.69 ? 62   PRO C N   1 
ATOM   2676  C  CA  . PRO C  1 62  ? 5.679   -35.545 4.390   1.00 21.93 ? 62   PRO C CA  1 
ATOM   2677  C  C   . PRO C  1 62  ? 5.083   -35.084 5.709   1.00 20.20 ? 62   PRO C C   1 
ATOM   2678  O  O   . PRO C  1 62  ? 3.865   -34.953 5.833   1.00 19.04 ? 62   PRO C O   1 
ATOM   2679  C  CB  . PRO C  1 62  ? 6.389   -34.351 3.731   1.00 23.64 ? 62   PRO C CB  1 
ATOM   2680  C  CG  . PRO C  1 62  ? 5.723   -34.116 2.435   1.00 24.36 ? 62   PRO C CG  1 
ATOM   2681  C  CD  . PRO C  1 62  ? 4.428   -34.833 2.435   1.00 21.82 ? 62   PRO C CD  1 
ATOM   2682  N  N   . HIS C  1 63  ? 5.929   -34.819 6.694   1.00 18.98 ? 63   HIS C N   1 
ATOM   2683  C  CA  . HIS C  1 63  ? 5.425   -34.169 7.892   1.00 18.85 ? 63   HIS C CA  1 
ATOM   2684  C  C   . HIS C  1 63  ? 4.870   -32.799 7.494   1.00 20.25 ? 63   HIS C C   1 
ATOM   2685  O  O   . HIS C  1 63  ? 5.407   -32.136 6.607   1.00 19.61 ? 63   HIS C O   1 
ATOM   2686  C  CB  . HIS C  1 63  ? 6.500   -34.063 8.970   1.00 18.05 ? 63   HIS C CB  1 
ATOM   2687  C  CG  . HIS C  1 63  ? 6.999   -35.391 9.452   1.00 18.50 ? 63   HIS C CG  1 
ATOM   2688  N  ND1 . HIS C  1 63  ? 7.967   -35.517 10.422  1.00 17.23 ? 63   HIS C ND1 1 
ATOM   2689  C  CD2 . HIS C  1 63  ? 6.662   -36.651 9.094   1.00 19.12 ? 63   HIS C CD2 1 
ATOM   2690  C  CE1 . HIS C  1 63  ? 8.207   -36.797 10.639  1.00 18.54 ? 63   HIS C CE1 1 
ATOM   2691  N  NE2 . HIS C  1 63  ? 7.430   -37.507 9.845   1.00 17.78 ? 63   HIS C NE2 1 
ATOM   2692  N  N   . PHE C  1 64  ? 3.765   -32.412 8.126   1.00 20.66 ? 64   PHE C N   1 
ATOM   2693  C  CA  . PHE C  1 64  ? 3.159   -31.117 7.904   1.00 18.54 ? 64   PHE C CA  1 
ATOM   2694  C  C   . PHE C  1 64  ? 4.197   -30.077 8.245   1.00 18.54 ? 64   PHE C C   1 
ATOM   2695  O  O   . PHE C  1 64  ? 4.638   -30.000 9.376   1.00 21.77 ? 64   PHE C O   1 
ATOM   2696  C  CB  . PHE C  1 64  ? 1.938   -30.956 8.802   1.00 20.92 ? 64   PHE C CB  1 
ATOM   2697  C  CG  . PHE C  1 64  ? 1.208   -29.645 8.620   1.00 20.86 ? 64   PHE C CG  1 
ATOM   2698  C  CD1 . PHE C  1 64  ? 1.118   -29.046 7.370   1.00 22.79 ? 64   PHE C CD1 1 
ATOM   2699  C  CD2 . PHE C  1 64  ? 0.592   -29.027 9.697   1.00 19.93 ? 64   PHE C CD2 1 
ATOM   2700  C  CE1 . PHE C  1 64  ? 0.441   -27.845 7.208   1.00 21.85 ? 64   PHE C CE1 1 
ATOM   2701  C  CE2 . PHE C  1 64  ? -0.082  -27.826 9.535   1.00 20.26 ? 64   PHE C CE2 1 
ATOM   2702  C  CZ  . PHE C  1 64  ? -0.158  -27.239 8.296   1.00 18.44 ? 64   PHE C CZ  1 
ATOM   2703  N  N   . ASN C  1 65  ? 4.575   -29.272 7.263   1.00 20.28 ? 65   ASN C N   1 
ATOM   2704  C  CA  . ASN C  1 65  ? 5.718   -28.388 7.387   1.00 20.16 ? 65   ASN C CA  1 
ATOM   2705  C  C   . ASN C  1 65  ? 5.527   -27.115 6.554   1.00 23.48 ? 65   ASN C C   1 
ATOM   2706  O  O   . ASN C  1 65  ? 6.230   -26.905 5.570   1.00 28.01 ? 65   ASN C O   1 
ATOM   2707  C  CB  . ASN C  1 65  ? 6.955   -29.151 6.919   1.00 21.39 ? 65   ASN C CB  1 
ATOM   2708  C  CG  . ASN C  1 65  ? 8.212   -28.333 6.991   1.00 21.72 ? 65   ASN C CG  1 
ATOM   2709  O  OD1 . ASN C  1 65  ? 8.419   -27.565 7.931   1.00 21.86 ? 65   ASN C OD1 1 
ATOM   2710  N  ND2 . ASN C  1 65  ? 9.071   -28.496 5.996   1.00 23.29 ? 65   ASN C ND2 1 
ATOM   2711  N  N   . PRO C  1 66  ? 4.559   -26.266 6.938   1.00 23.41 ? 66   PRO C N   1 
ATOM   2712  C  CA  . PRO C  1 66  ? 4.213   -25.017 6.244   1.00 25.30 ? 66   PRO C CA  1 
ATOM   2713  C  C   . PRO C  1 66  ? 5.385   -24.033 6.181   1.00 26.38 ? 66   PRO C C   1 
ATOM   2714  O  O   . PRO C  1 66  ? 5.585   -23.365 5.163   1.00 28.36 ? 66   PRO C O   1 
ATOM   2715  C  CB  . PRO C  1 66  ? 3.117   -24.410 7.121   1.00 24.14 ? 66   PRO C CB  1 
ATOM   2716  C  CG  . PRO C  1 66  ? 2.660   -25.471 7.992   1.00 24.00 ? 66   PRO C CG  1 
ATOM   2717  C  CD  . PRO C  1 66  ? 3.768   -26.444 8.160   1.00 22.57 ? 66   PRO C CD  1 
ATOM   2718  N  N   . LEU C  1 67  ? 6.146   -23.955 7.265   1.00 24.34 ? 67   LEU C N   1 
ATOM   2719  C  CA  . LEU C  1 67  ? 7.279   -23.039 7.365   1.00 24.37 ? 67   LEU C CA  1 
ATOM   2720  C  C   . LEU C  1 67  ? 8.555   -23.502 6.629   1.00 28.17 ? 67   LEU C C   1 
ATOM   2721  O  O   . LEU C  1 67  ? 9.549   -22.782 6.592   1.00 29.24 ? 67   LEU C O   1 
ATOM   2722  C  CB  . LEU C  1 67  ? 7.567   -22.753 8.835   1.00 26.02 ? 67   LEU C CB  1 
ATOM   2723  C  CG  . LEU C  1 67  ? 6.296   -22.310 9.574   1.00 26.55 ? 67   LEU C CG  1 
ATOM   2724  C  CD1 . LEU C  1 67  ? 6.577   -21.817 10.974  1.00 24.41 ? 67   LEU C CD1 1 
ATOM   2725  C  CD2 . LEU C  1 67  ? 5.586   -21.237 8.764   1.00 24.04 ? 67   LEU C CD2 1 
ATOM   2726  N  N   . SER C  1 68  ? 8.514   -24.691 6.032   1.00 27.09 ? 68   SER C N   1 
ATOM   2727  C  CA  . SER C  1 68  ? 9.649   -25.233 5.294   1.00 24.14 ? 68   SER C CA  1 
ATOM   2728  C  C   . SER C  1 68  ? 10.893  -25.352 6.164   1.00 26.69 ? 68   SER C C   1 
ATOM   2729  O  O   . SER C  1 68  ? 11.983  -24.937 5.762   1.00 26.81 ? 68   SER C O   1 
ATOM   2730  C  CB  . SER C  1 68  ? 9.949   -24.392 4.048   1.00 27.01 ? 68   SER C CB  1 
ATOM   2731  O  OG  . SER C  1 68  ? 9.121   -24.757 2.950   1.00 33.47 ? 68   SER C OG  1 
ATOM   2732  N  N   . ARG C  1 69  ? 10.719  -25.932 7.349   1.00 25.85 ? 69   ARG C N   1 
ATOM   2733  C  CA  . ARG C  1 69  ? 11.793  -26.092 8.317   1.00 23.06 ? 69   ARG C CA  1 
ATOM   2734  C  C   . ARG C  1 69  ? 12.276  -27.545 8.417   1.00 23.86 ? 69   ARG C C   1 
ATOM   2735  O  O   . ARG C  1 69  ? 11.785  -28.416 7.713   1.00 24.58 ? 69   ARG C O   1 
ATOM   2736  C  CB  . ARG C  1 69  ? 11.327  -25.600 9.678   1.00 24.34 ? 69   ARG C CB  1 
ATOM   2737  C  CG  . ARG C  1 69  ? 11.142  -24.099 9.754   1.00 27.38 ? 69   ARG C CG  1 
ATOM   2738  C  CD  . ARG C  1 69  ? 11.017  -23.669 11.196  1.00 32.30 ? 69   ARG C CD  1 
ATOM   2739  N  NE  . ARG C  1 69  ? 10.934  -22.218 11.346  1.00 38.19 ? 69   ARG C NE  1 
ATOM   2740  C  CZ  . ARG C  1 69  ? 10.435  -21.617 12.423  1.00 42.11 ? 69   ARG C CZ  1 
ATOM   2741  N  NH1 . ARG C  1 69  ? 9.974   -22.347 13.435  1.00 43.25 ? 69   ARG C NH1 1 
ATOM   2742  N  NH2 . ARG C  1 69  ? 10.387  -20.292 12.490  1.00 41.83 ? 69   ARG C NH2 1 
ATOM   2743  N  N   . LYS C  1 70  ? 13.250  -27.804 9.283   1.00 24.89 ? 70   LYS C N   1 
ATOM   2744  C  CA  . LYS C  1 70  ? 13.750  -29.163 9.455   1.00 21.80 ? 70   LYS C CA  1 
ATOM   2745  C  C   . LYS C  1 70  ? 13.143  -29.845 10.676  1.00 19.39 ? 70   LYS C C   1 
ATOM   2746  O  O   . LYS C  1 70  ? 12.692  -29.197 11.615  1.00 19.04 ? 70   LYS C O   1 
ATOM   2747  C  CB  . LYS C  1 70  ? 15.280  -29.191 9.536   1.00 24.16 ? 70   LYS C CB  1 
ATOM   2748  C  CG  . LYS C  1 70  ? 16.005  -28.736 8.267   1.00 25.03 ? 70   LYS C CG  1 
ATOM   2749  C  CD  . LYS C  1 70  ? 17.370  -29.393 8.177   1.00 27.22 ? 70   LYS C CD  1 
ATOM   2750  C  CE  . LYS C  1 70  ? 18.365  -28.574 7.368   1.00 37.64 ? 70   LYS C CE  1 
ATOM   2751  N  NZ  . LYS C  1 70  ? 19.044  -27.518 8.183   1.00 41.57 ? 70   LYS C NZ  1 
ATOM   2752  N  N   . HIS C  1 71  ? 13.146  -31.170 10.644  1.00 19.61 ? 71   HIS C N   1 
ATOM   2753  C  CA  . HIS C  1 71  ? 12.535  -31.994 11.678  1.00 18.13 ? 71   HIS C CA  1 
ATOM   2754  C  C   . HIS C  1 71  ? 13.165  -31.777 13.036  1.00 18.51 ? 71   HIS C C   1 
ATOM   2755  O  O   . HIS C  1 71  ? 14.383  -31.692 13.161  1.00 20.15 ? 71   HIS C O   1 
ATOM   2756  C  CB  . HIS C  1 71  ? 12.671  -33.463 11.285  1.00 18.13 ? 71   HIS C CB  1 
ATOM   2757  C  CG  . HIS C  1 71  ? 12.023  -34.416 12.239  1.00 17.57 ? 71   HIS C CG  1 
ATOM   2758  N  ND1 . HIS C  1 71  ? 10.668  -34.661 12.242  1.00 18.11 ? 71   HIS C ND1 1 
ATOM   2759  C  CD2 . HIS C  1 71  ? 12.549  -35.211 13.201  1.00 18.75 ? 71   HIS C CD2 1 
ATOM   2760  C  CE1 . HIS C  1 71  ? 10.383  -35.556 13.172  1.00 18.88 ? 71   HIS C CE1 1 
ATOM   2761  N  NE2 . HIS C  1 71  ? 11.507  -35.901 13.772  1.00 18.34 ? 71   HIS C NE2 1 
ATOM   2762  N  N   . GLY C  1 72  ? 12.329  -31.708 14.064  1.00 20.15 ? 72   GLY C N   1 
ATOM   2763  C  CA  . GLY C  1 72  ? 12.812  -31.560 15.425  1.00 19.49 ? 72   GLY C CA  1 
ATOM   2764  C  C   . GLY C  1 72  ? 11.901  -32.250 16.415  1.00 18.89 ? 72   GLY C C   1 
ATOM   2765  O  O   . GLY C  1 72  ? 11.015  -33.004 16.043  1.00 20.26 ? 72   GLY C O   1 
ATOM   2766  N  N   . GLY C  1 73  ? 12.127  -31.994 17.691  1.00 21.93 ? 73   GLY C N   1 
ATOM   2767  C  CA  . GLY C  1 73  ? 11.243  -32.491 18.725  1.00 23.87 ? 73   GLY C CA  1 
ATOM   2768  C  C   . GLY C  1 73  ? 10.187  -31.436 18.985  1.00 25.06 ? 73   GLY C C   1 
ATOM   2769  O  O   . GLY C  1 73  ? 10.337  -30.296 18.525  1.00 23.66 ? 73   GLY C O   1 
ATOM   2770  N  N   . PRO C  1 74  ? 9.127   -31.800 19.732  1.00 21.62 ? 74   PRO C N   1 
ATOM   2771  C  CA  . PRO C  1 74  ? 7.995   -30.909 20.014  1.00 23.15 ? 74   PRO C CA  1 
ATOM   2772  C  C   . PRO C  1 74  ? 8.456   -29.560 20.570  1.00 25.38 ? 74   PRO C C   1 
ATOM   2773  O  O   . PRO C  1 74  ? 7.781   -28.559 20.353  1.00 23.75 ? 74   PRO C O   1 
ATOM   2774  C  CB  . PRO C  1 74  ? 7.197   -31.655 21.089  1.00 23.41 ? 74   PRO C CB  1 
ATOM   2775  C  CG  . PRO C  1 74  ? 7.714   -33.029 21.118  1.00 22.34 ? 74   PRO C CG  1 
ATOM   2776  C  CD  . PRO C  1 74  ? 9.033   -33.086 20.441  1.00 22.14 ? 74   PRO C CD  1 
ATOM   2777  N  N   . LYS C  1 75  ? 9.585   -29.543 21.280  1.00 27.01 ? 75   LYS C N   1 
ATOM   2778  C  CA  . LYS C  1 75  ? 10.053  -28.328 21.941  1.00 28.55 ? 75   LYS C CA  1 
ATOM   2779  C  C   . LYS C  1 75  ? 11.299  -27.718 21.290  1.00 31.06 ? 75   LYS C C   1 
ATOM   2780  O  O   . LYS C  1 75  ? 11.940  -26.845 21.875  1.00 33.58 ? 75   LYS C O   1 
ATOM   2781  C  CB  . LYS C  1 75  ? 10.302  -28.578 23.432  1.00 27.13 ? 75   LYS C CB  1 
ATOM   2782  C  CG  . LYS C  1 75  ? 9.070   -29.035 24.196  1.00 32.22 ? 75   LYS C CG  1 
ATOM   2783  C  CD  . LYS C  1 75  ? 7.957   -27.981 24.214  1.00 35.88 ? 75   LYS C CD  1 
ATOM   2784  C  CE  . LYS C  1 75  ? 6.728   -28.432 25.026  1.00 38.14 ? 75   LYS C CE  1 
ATOM   2785  N  NZ  . LYS C  1 75  ? 6.947   -28.396 26.517  1.00 39.83 ? 75   LYS C NZ  1 
ATOM   2786  N  N   . ASP C  1 76  ? 11.647  -28.167 20.088  1.00 28.02 ? 76   ASP C N   1 
ATOM   2787  C  CA  . ASP C  1 76  ? 12.743  -27.527 19.364  1.00 32.33 ? 76   ASP C CA  1 
ATOM   2788  C  C   . ASP C  1 76  ? 12.229  -26.306 18.600  1.00 32.05 ? 76   ASP C C   1 
ATOM   2789  O  O   . ASP C  1 76  ? 11.059  -26.246 18.234  1.00 32.99 ? 76   ASP C O   1 
ATOM   2790  C  CB  . ASP C  1 76  ? 13.456  -28.508 18.423  1.00 28.95 ? 76   ASP C CB  1 
ATOM   2791  C  CG  . ASP C  1 76  ? 14.239  -29.576 19.175  1.00 32.01 ? 76   ASP C CG  1 
ATOM   2792  O  OD1 . ASP C  1 76  ? 14.576  -29.353 20.362  1.00 37.25 ? 76   ASP C OD1 1 
ATOM   2793  O  OD2 . ASP C  1 76  ? 14.517  -30.644 18.589  1.00 32.43 ? 76   ASP C OD2 1 
ATOM   2794  N  N   . GLU C  1 77  ? 13.096  -25.326 18.375  1.00 32.87 ? 77   GLU C N   1 
ATOM   2795  C  CA  . GLU C  1 77  ? 12.711  -24.157 17.598  1.00 34.76 ? 77   GLU C CA  1 
ATOM   2796  C  C   . GLU C  1 77  ? 12.578  -24.528 16.127  1.00 32.85 ? 77   GLU C C   1 
ATOM   2797  O  O   . GLU C  1 77  ? 11.615  -24.124 15.454  1.00 34.95 ? 77   GLU C O   1 
ATOM   2798  C  CB  . GLU C  1 77  ? 13.720  -23.026 17.791  1.00 45.68 ? 77   GLU C CB  1 
ATOM   2799  C  CG  . GLU C  1 77  ? 13.319  -22.060 18.891  1.00 52.01 ? 77   GLU C CG  1 
ATOM   2800  C  CD  . GLU C  1 77  ? 12.072  -21.259 18.528  1.00 58.45 ? 77   GLU C CD  1 
ATOM   2801  O  OE1 . GLU C  1 77  ? 12.176  -20.376 17.646  1.00 62.44 ? 77   GLU C OE1 1 
ATOM   2802  O  OE2 . GLU C  1 77  ? 10.996  -21.508 19.126  1.00 54.05 ? 77   GLU C OE2 1 
ATOM   2803  N  N   . GLU C  1 78  ? 13.546  -25.299 15.634  1.00 26.99 ? 78   GLU C N   1 
ATOM   2804  C  CA  . GLU C  1 78  ? 13.430  -25.910 14.316  1.00 29.19 ? 78   GLU C CA  1 
ATOM   2805  C  C   . GLU C  1 78  ? 12.657  -27.189 14.480  1.00 26.01 ? 78   GLU C C   1 
ATOM   2806  O  O   . GLU C  1 78  ? 13.102  -28.092 15.174  1.00 24.64 ? 78   GLU C O   1 
ATOM   2807  C  CB  . GLU C  1 78  ? 14.790  -26.238 13.710  1.00 27.78 ? 78   GLU C CB  1 
ATOM   2808  C  CG  . GLU C  1 78  ? 15.418  -25.101 12.938  1.00 38.35 ? 78   GLU C CG  1 
ATOM   2809  C  CD  . GLU C  1 78  ? 14.751  -24.842 11.603  1.00 33.48 ? 78   GLU C CD  1 
ATOM   2810  O  OE1 . GLU C  1 78  ? 14.814  -25.725 10.714  1.00 26.87 ? 78   GLU C OE1 1 
ATOM   2811  O  OE2 . GLU C  1 78  ? 14.186  -23.734 11.447  1.00 39.63 ? 78   GLU C OE2 1 
ATOM   2812  N  N   . ARG C  1 79  ? 11.493  -27.245 13.843  1.00 25.59 ? 79   ARG C N   1 
ATOM   2813  C  CA  . ARG C  1 79  ? 10.635  -28.414 13.869  1.00 22.24 ? 79   ARG C CA  1 
ATOM   2814  C  C   . ARG C  1 79  ? 9.576   -28.212 12.810  1.00 20.49 ? 79   ARG C C   1 
ATOM   2815  O  O   . ARG C  1 79  ? 9.267   -27.081 12.434  1.00 19.86 ? 79   ARG C O   1 
ATOM   2816  C  CB  . ARG C  1 79  ? 9.993   -28.617 15.251  1.00 20.97 ? 79   ARG C CB  1 
ATOM   2817  C  CG  . ARG C  1 79  ? 9.106   -27.475 15.715  1.00 20.91 ? 79   ARG C CG  1 
ATOM   2818  C  CD  . ARG C  1 79  ? 8.166   -27.907 16.822  1.00 20.11 ? 79   ARG C CD  1 
ATOM   2819  N  NE  . ARG C  1 79  ? 6.889   -28.387 16.305  1.00 18.53 ? 79   ARG C NE  1 
ATOM   2820  C  CZ  . ARG C  1 79  ? 5.846   -28.708 17.063  1.00 20.95 ? 79   ARG C CZ  1 
ATOM   2821  N  NH1 . ARG C  1 79  ? 5.927   -28.617 18.383  1.00 24.69 ? 79   ARG C NH1 1 
ATOM   2822  N  NH2 . ARG C  1 79  ? 4.711   -29.120 16.509  1.00 22.69 ? 79   ARG C NH2 1 
ATOM   2823  N  N   . HIS C  1 80  ? 9.040   -29.313 12.311  1.00 19.79 ? 80   HIS C N   1 
ATOM   2824  C  CA  . HIS C  1 80  ? 7.921   -29.247 11.402  1.00 20.21 ? 80   HIS C CA  1 
ATOM   2825  C  C   . HIS C  1 80  ? 6.730   -28.915 12.264  1.00 18.94 ? 80   HIS C C   1 
ATOM   2826  O  O   . HIS C  1 80  ? 6.740   -29.217 13.447  1.00 20.96 ? 80   HIS C O   1 
ATOM   2827  C  CB  . HIS C  1 80  ? 7.722   -30.596 10.710  1.00 20.73 ? 80   HIS C CB  1 
ATOM   2828  C  CG  . HIS C  1 80  ? 8.867   -30.998 9.832   1.00 20.02 ? 80   HIS C CG  1 
ATOM   2829  N  ND1 . HIS C  1 80  ? 9.217   -32.314 9.620   1.00 18.60 ? 80   HIS C ND1 1 
ATOM   2830  C  CD2 . HIS C  1 80  ? 9.743   -30.257 9.113   1.00 19.43 ? 80   HIS C CD2 1 
ATOM   2831  C  CE1 . HIS C  1 80  ? 10.258  -32.368 8.810   1.00 19.18 ? 80   HIS C CE1 1 
ATOM   2832  N  NE2 . HIS C  1 80  ? 10.599  -31.133 8.489   1.00 20.49 ? 80   HIS C NE2 1 
ATOM   2833  N  N   . VAL C  1 81  ? 5.701   -28.295 11.702  1.00 19.25 ? 81   VAL C N   1 
ATOM   2834  C  CA  . VAL C  1 81  ? 4.494   -28.068 12.493  1.00 20.98 ? 81   VAL C CA  1 
ATOM   2835  C  C   . VAL C  1 81  ? 3.944   -29.393 13.071  1.00 21.05 ? 81   VAL C C   1 
ATOM   2836  O  O   . VAL C  1 81  ? 3.506   -29.444 14.225  1.00 21.51 ? 81   VAL C O   1 
ATOM   2837  C  CB  . VAL C  1 81  ? 3.401   -27.287 11.712  1.00 21.44 ? 81   VAL C CB  1 
ATOM   2838  C  CG1 . VAL C  1 81  ? 2.081   -27.327 12.470  1.00 22.57 ? 81   VAL C CG1 1 
ATOM   2839  C  CG2 . VAL C  1 81  ? 3.836   -25.840 11.483  1.00 23.72 ? 81   VAL C CG2 1 
ATOM   2840  N  N   . GLY C  1 82  ? 4.015   -30.469 12.286  1.00 19.55 ? 82   GLY C N   1 
ATOM   2841  C  CA  . GLY C  1 82  ? 3.494   -31.761 12.707  1.00 18.58 ? 82   GLY C CA  1 
ATOM   2842  C  C   . GLY C  1 82  ? 4.348   -32.578 13.664  1.00 18.65 ? 82   GLY C C   1 
ATOM   2843  O  O   . GLY C  1 82  ? 4.017   -33.724 13.948  1.00 18.02 ? 82   GLY C O   1 
ATOM   2844  N  N   . ASP C  1 83  ? 5.430   -31.991 14.178  1.00 22.48 ? 83   ASP C N   1 
ATOM   2845  C  CA  . ASP C  1 83  ? 6.408   -32.710 15.007  1.00 18.54 ? 83   ASP C CA  1 
ATOM   2846  C  C   . ASP C  1 83  ? 5.967   -32.841 16.448  1.00 21.30 ? 83   ASP C C   1 
ATOM   2847  O  O   . ASP C  1 83  ? 6.254   -31.983 17.275  1.00 20.07 ? 83   ASP C O   1 
ATOM   2848  C  CB  . ASP C  1 83  ? 7.787   -32.044 14.931  1.00 18.68 ? 83   ASP C CB  1 
ATOM   2849  C  CG  . ASP C  1 83  ? 8.478   -32.293 13.604  1.00 20.24 ? 83   ASP C CG  1 
ATOM   2850  O  OD1 . ASP C  1 83  ? 7.961   -33.121 12.836  1.00 18.09 ? 83   ASP C OD1 1 
ATOM   2851  O  OD2 . ASP C  1 83  ? 9.533   -31.675 13.332  1.00 20.71 ? 83   ASP C OD2 1 
ATOM   2852  N  N   . LEU C  1 84  ? 5.267   -33.934 16.739  1.00 22.80 ? 84   LEU C N   1 
ATOM   2853  C  CA  . LEU C  1 84  ? 4.738   -34.166 18.077  1.00 23.37 ? 84   LEU C CA  1 
ATOM   2854  C  C   . LEU C  1 84  ? 5.587   -35.142 18.913  1.00 21.77 ? 84   LEU C C   1 
ATOM   2855  O  O   . LEU C  1 84  ? 5.247   -35.437 20.059  1.00 23.42 ? 84   LEU C O   1 
ATOM   2856  C  CB  . LEU C  1 84  ? 3.255   -34.587 18.019  1.00 21.93 ? 84   LEU C CB  1 
ATOM   2857  C  CG  . LEU C  1 84  ? 2.287   -33.506 17.510  1.00 22.54 ? 84   LEU C CG  1 
ATOM   2858  C  CD1 . LEU C  1 84  ? 0.838   -33.953 17.656  1.00 22.89 ? 84   LEU C CD1 1 
ATOM   2859  C  CD2 . LEU C  1 84  ? 2.497   -32.187 18.245  1.00 19.95 ? 84   LEU C CD2 1 
ATOM   2860  N  N   . GLY C  1 85  ? 6.698   -35.621 18.353  1.00 21.83 ? 85   GLY C N   1 
ATOM   2861  C  CA  . GLY C  1 85  ? 7.646   -36.425 19.116  1.00 20.98 ? 85   GLY C CA  1 
ATOM   2862  C  C   . GLY C  1 85  ? 7.305   -37.907 19.171  1.00 19.22 ? 85   GLY C C   1 
ATOM   2863  O  O   . GLY C  1 85  ? 6.897   -38.494 18.168  1.00 18.17 ? 85   GLY C O   1 
ATOM   2864  N  N   . ASN C  1 86  ? 7.482   -38.512 20.344  1.00 21.14 ? 86   ASN C N   1 
ATOM   2865  C  CA  . ASN C  1 86  ? 7.179   -39.927 20.546  1.00 18.45 ? 86   ASN C CA  1 
ATOM   2866  C  C   . ASN C  1 86  ? 6.009   -40.163 21.492  1.00 21.01 ? 86   ASN C C   1 
ATOM   2867  O  O   . ASN C  1 86  ? 5.764   -39.392 22.429  1.00 19.62 ? 86   ASN C O   1 
ATOM   2868  C  CB  . ASN C  1 86  ? 8.385   -40.671 21.122  1.00 18.18 ? 86   ASN C CB  1 
ATOM   2869  C  CG  . ASN C  1 86  ? 9.572   -40.681 20.192  1.00 17.67 ? 86   ASN C CG  1 
ATOM   2870  O  OD1 . ASN C  1 86  ? 9.559   -41.353 19.171  1.00 17.77 ? 86   ASN C OD1 1 
ATOM   2871  N  ND2 . ASN C  1 86  ? 10.614  -39.945 20.550  1.00 16.56 ? 86   ASN C ND2 1 
ATOM   2872  N  N   . VAL C  1 87  ? 5.297   -41.252 21.235  1.00 20.10 ? 87   VAL C N   1 
ATOM   2873  C  CA  . VAL C  1 87  ? 4.409   -41.834 22.223  1.00 21.75 ? 87   VAL C CA  1 
ATOM   2874  C  C   . VAL C  1 87  ? 5.073   -43.123 22.724  1.00 18.77 ? 87   VAL C C   1 
ATOM   2875  O  O   . VAL C  1 87  ? 5.900   -43.698 22.015  1.00 19.18 ? 87   VAL C O   1 
ATOM   2876  C  CB  . VAL C  1 87  ? 3.006   -42.138 21.635  1.00 21.23 ? 87   VAL C CB  1 
ATOM   2877  C  CG1 . VAL C  1 87  ? 2.310   -40.854 21.232  1.00 17.85 ? 87   VAL C CG1 1 
ATOM   2878  C  CG2 . VAL C  1 87  ? 3.111   -43.104 20.455  1.00 18.75 ? 87   VAL C CG2 1 
ATOM   2879  N  N   . THR C  1 88  ? 4.705   -43.576 23.925  1.00 17.97 ? 88   THR C N   1 
ATOM   2880  C  CA  . THR C  1 88  ? 5.349   -44.723 24.555  1.00 18.08 ? 88   THR C CA  1 
ATOM   2881  C  C   . THR C  1 88  ? 4.376   -45.865 24.805  1.00 19.59 ? 88   THR C C   1 
ATOM   2882  O  O   . THR C  1 88  ? 3.367   -45.699 25.490  1.00 20.67 ? 88   THR C O   1 
ATOM   2883  C  CB  . THR C  1 88  ? 5.978   -44.342 25.917  1.00 21.48 ? 88   THR C CB  1 
ATOM   2884  O  OG1 . THR C  1 88  ? 6.885   -43.246 25.757  1.00 20.74 ? 88   THR C OG1 1 
ATOM   2885  C  CG2 . THR C  1 88  ? 6.714   -45.532 26.527  1.00 21.54 ? 88   THR C CG2 1 
ATOM   2886  N  N   . ALA C  1 89  ? 4.699   -47.036 24.275  1.00 19.62 ? 89   ALA C N   1 
ATOM   2887  C  CA  . ALA C  1 89  ? 3.868   -48.218 24.469  1.00 18.49 ? 89   ALA C CA  1 
ATOM   2888  C  C   . ALA C  1 89  ? 4.345   -49.007 25.678  1.00 21.43 ? 89   ALA C C   1 
ATOM   2889  O  O   . ALA C  1 89  ? 5.541   -49.089 25.933  1.00 25.23 ? 89   ALA C O   1 
ATOM   2890  C  CB  . ALA C  1 89  ? 3.888   -49.094 23.213  1.00 19.43 ? 89   ALA C CB  1 
ATOM   2891  N  N   . GLY C  1 90  ? 3.420   -49.582 26.433  1.00 21.50 ? 90   GLY C N   1 
ATOM   2892  C  CA  . GLY C  1 90  ? 3.814   -50.445 27.527  1.00 24.27 ? 90   GLY C CA  1 
ATOM   2893  C  C   . GLY C  1 90  ? 4.018   -51.871 27.055  1.00 23.84 ? 90   GLY C C   1 
ATOM   2894  O  O   . GLY C  1 90  ? 3.851   -52.167 25.885  1.00 23.71 ? 90   GLY C O   1 
ATOM   2895  N  N   . LYS C  1 91  ? 4.372   -52.760 27.976  1.00 27.62 ? 91   LYS C N   1 
ATOM   2896  C  CA  . LYS C  1 91  ? 4.548   -54.177 27.668  1.00 25.90 ? 91   LYS C CA  1 
ATOM   2897  C  C   . LYS C  1 91  ? 3.299   -54.769 27.062  1.00 23.45 ? 91   LYS C C   1 
ATOM   2898  O  O   . LYS C  1 91  ? 3.366   -55.785 26.373  1.00 23.02 ? 91   LYS C O   1 
ATOM   2899  C  CB  . LYS C  1 91  ? 4.915   -54.970 28.928  1.00 30.04 ? 91   LYS C CB  1 
ATOM   2900  C  CG  . LYS C  1 91  ? 6.267   -54.624 29.489  1.00 30.75 ? 91   LYS C CG  1 
ATOM   2901  C  CD  . LYS C  1 91  ? 6.567   -55.394 30.757  1.00 33.82 ? 91   LYS C CD  1 
ATOM   2902  C  CE  . LYS C  1 91  ? 7.818   -54.837 31.416  1.00 35.64 ? 91   LYS C CE  1 
ATOM   2903  N  NZ  . LYS C  1 91  ? 9.022   -55.049 30.563  1.00 36.82 ? 91   LYS C NZ  1 
ATOM   2904  N  N   . ASP C  1 92  ? 2.155   -54.145 27.330  1.00 24.84 ? 92   ASP C N   1 
ATOM   2905  C  CA  . ASP C  1 92  ? 0.889   -54.624 26.779  1.00 25.49 ? 92   ASP C CA  1 
ATOM   2906  C  C   . ASP C  1 92  ? 0.630   -54.078 25.371  1.00 25.67 ? 92   ASP C C   1 
ATOM   2907  O  O   . ASP C  1 92  ? -0.358  -54.426 24.723  1.00 27.50 ? 92   ASP C O   1 
ATOM   2908  C  CB  . ASP C  1 92  ? -0.278  -54.311 27.713  1.00 23.34 ? 92   ASP C CB  1 
ATOM   2909  C  CG  . ASP C  1 92  ? -0.459  -52.826 27.949  1.00 28.27 ? 92   ASP C CG  1 
ATOM   2910  O  OD1 . ASP C  1 92  ? 0.394   -52.024 27.507  1.00 27.47 ? 92   ASP C OD1 1 
ATOM   2911  O  OD2 . ASP C  1 92  ? -1.466  -52.459 28.592  1.00 32.17 ? 92   ASP C OD2 1 
ATOM   2912  N  N   . GLY C  1 93  ? 1.532   -53.230 24.894  1.00 25.07 ? 93   GLY C N   1 
ATOM   2913  C  CA  . GLY C  1 93  ? 1.458   -52.733 23.533  1.00 22.95 ? 93   GLY C CA  1 
ATOM   2914  C  C   . GLY C  1 93  ? 0.537   -51.542 23.402  1.00 21.38 ? 93   GLY C C   1 
ATOM   2915  O  O   . GLY C  1 93  ? 0.193   -51.127 22.297  1.00 22.46 ? 93   GLY C O   1 
ATOM   2916  N  N   . VAL C  1 94  ? 0.142   -50.982 24.534  1.00 21.43 ? 94   VAL C N   1 
ATOM   2917  C  CA  . VAL C  1 94  ? -0.765  -49.853 24.526  1.00 23.05 ? 94   VAL C CA  1 
ATOM   2918  C  C   . VAL C  1 94  ? 0.011   -48.579 24.779  1.00 22.90 ? 94   VAL C C   1 
ATOM   2919  O  O   . VAL C  1 94  ? 0.814   -48.505 25.712  1.00 24.43 ? 94   VAL C O   1 
ATOM   2920  C  CB  . VAL C  1 94  ? -1.875  -50.003 25.588  1.00 21.36 ? 94   VAL C CB  1 
ATOM   2921  C  CG1 . VAL C  1 94  ? -2.805  -48.810 25.551  1.00 20.30 ? 94   VAL C CG1 1 
ATOM   2922  C  CG2 . VAL C  1 94  ? -2.644  -51.278 25.351  1.00 22.81 ? 94   VAL C CG2 1 
ATOM   2923  N  N   . ALA C  1 95  ? -0.217  -47.581 23.931  1.00 21.08 ? 95   ALA C N   1 
ATOM   2924  C  CA  . ALA C  1 95  ? 0.327   -46.258 24.172  1.00 20.51 ? 95   ALA C CA  1 
ATOM   2925  C  C   . ALA C  1 95  ? -0.799  -45.335 24.618  1.00 23.20 ? 95   ALA C C   1 
ATOM   2926  O  O   . ALA C  1 95  ? -1.766  -45.131 23.888  1.00 20.53 ? 95   ALA C O   1 
ATOM   2927  C  CB  . ALA C  1 95  ? 1.004   -45.715 22.930  1.00 17.18 ? 95   ALA C CB  1 
ATOM   2928  N  N   . ASN C  1 96  ? -0.683  -44.810 25.833  1.00 23.33 ? 96   ASN C N   1 
ATOM   2929  C  CA  . ASN C  1 96  ? -1.601  -43.786 26.305  1.00 25.03 ? 96   ASN C CA  1 
ATOM   2930  C  C   . ASN C  1 96  ? -1.034  -42.408 25.993  1.00 24.70 ? 96   ASN C C   1 
ATOM   2931  O  O   . ASN C  1 96  ? 0.001   -42.010 26.520  1.00 25.36 ? 96   ASN C O   1 
ATOM   2932  C  CB  . ASN C  1 96  ? -1.897  -43.959 27.796  1.00 27.77 ? 96   ASN C CB  1 
ATOM   2933  C  CG  . ASN C  1 96  ? -2.653  -45.245 28.089  1.00 35.17 ? 96   ASN C CG  1 
ATOM   2934  O  OD1 . ASN C  1 96  ? -2.075  -46.221 28.577  1.00 44.37 ? 96   ASN C OD1 1 
ATOM   2935  N  ND2 . ASN C  1 96  ? -3.947  -45.262 27.770  1.00 33.08 ? 96   ASN C ND2 1 
ATOM   2936  N  N   . VAL C  1 97  ? -1.714  -41.703 25.100  1.00 23.83 ? 97   VAL C N   1 
ATOM   2937  C  CA  . VAL C  1 97  ? -1.254  -40.420 24.584  1.00 22.11 ? 97   VAL C CA  1 
ATOM   2938  C  C   . VAL C  1 97  ? -1.782  -39.270 25.439  1.00 22.24 ? 97   VAL C C   1 
ATOM   2939  O  O   . VAL C  1 97  ? -2.952  -39.235 25.803  1.00 26.67 ? 97   VAL C O   1 
ATOM   2940  C  CB  . VAL C  1 97  ? -1.695  -40.245 23.091  1.00 20.59 ? 97   VAL C CB  1 
ATOM   2941  C  CG1 . VAL C  1 97  ? -1.106  -38.982 22.476  1.00 21.06 ? 97   VAL C CG1 1 
ATOM   2942  C  CG2 . VAL C  1 97  ? -1.314  -41.475 22.263  1.00 18.37 ? 97   VAL C CG2 1 
ATOM   2943  N  N   . SER C  1 98  ? -0.910  -38.338 25.776  1.00 24.20 ? 98   SER C N   1 
ATOM   2944  C  CA  . SER C  1 98  ? -1.307  -37.142 26.503  1.00 26.96 ? 98   SER C CA  1 
ATOM   2945  C  C   . SER C  1 98  ? -0.322  -36.054 26.116  1.00 29.69 ? 98   SER C C   1 
ATOM   2946  O  O   . SER C  1 98  ? 0.664   -35.814 26.812  1.00 32.64 ? 98   SER C O   1 
ATOM   2947  C  CB  . SER C  1 98  ? -1.273  -37.375 28.014  1.00 29.84 ? 98   SER C CB  1 
ATOM   2948  O  OG  . SER C  1 98  ? -1.953  -36.343 28.711  1.00 34.23 ? 98   SER C OG  1 
ATOM   2949  N  N   . ILE C  1 99  ? -0.587  -35.423 24.977  1.00 27.19 ? 99   ILE C N   1 
ATOM   2950  C  CA  . ILE C  1 99  ? 0.283   -34.396 24.422  1.00 25.80 ? 99   ILE C CA  1 
ATOM   2951  C  C   . ILE C  1 99  ? -0.394  -33.030 24.572  1.00 27.28 ? 99   ILE C C   1 
ATOM   2952  O  O   . ILE C  1 99  ? -1.624  -32.931 24.534  1.00 27.39 ? 99   ILE C O   1 
ATOM   2953  C  CB  . ILE C  1 99  ? 0.603   -34.711 22.934  1.00 22.04 ? 99   ILE C CB  1 
ATOM   2954  C  CG1 . ILE C  1 99  ? 1.442   -35.988 22.829  1.00 22.39 ? 99   ILE C CG1 1 
ATOM   2955  C  CG2 . ILE C  1 99  ? 1.318   -33.559 22.255  1.00 22.88 ? 99   ILE C CG2 1 
ATOM   2956  C  CD1 . ILE C  1 99  ? 1.659   -36.480 21.404  1.00 21.58 ? 99   ILE C CD1 1 
ATOM   2957  N  N   . GLU C  1 100 ? 0.403   -31.993 24.797  1.00 25.91 ? 100  GLU C N   1 
ATOM   2958  C  CA  . GLU C  1 100 ? -0.087  -30.628 24.776  1.00 26.42 ? 100  GLU C CA  1 
ATOM   2959  C  C   . GLU C  1 100 ? 0.899   -29.794 23.949  1.00 27.97 ? 100  GLU C C   1 
ATOM   2960  O  O   . GLU C  1 100 ? 2.085   -29.708 24.273  1.00 30.61 ? 100  GLU C O   1 
ATOM   2961  C  CB  . GLU C  1 100 ? -0.250  -30.079 26.195  1.00 30.32 ? 100  GLU C CB  1 
ATOM   2962  C  CG  . GLU C  1 100 ? -0.979  -28.722 26.262  1.00 34.27 ? 100  GLU C CG  1 
ATOM   2963  C  CD  . GLU C  1 100 ? -1.482  -28.379 27.666  1.00 42.08 ? 100  GLU C CD  1 
ATOM   2964  O  OE1 . GLU C  1 100 ? -1.669  -29.312 28.482  1.00 45.12 ? 100  GLU C OE1 1 
ATOM   2965  O  OE2 . GLU C  1 100 ? -1.701  -27.179 27.951  1.00 42.02 ? 100  GLU C OE2 1 
ATOM   2966  N  N   . ASP C  1 101 ? 0.407   -29.207 22.862  1.00 27.37 ? 101  ASP C N   1 
ATOM   2967  C  CA  . ASP C  1 101 ? 1.264   -28.564 21.865  1.00 30.04 ? 101  ASP C CA  1 
ATOM   2968  C  C   . ASP C  1 101 ? 0.748   -27.192 21.399  1.00 29.04 ? 101  ASP C C   1 
ATOM   2969  O  O   . ASP C  1 101 ? -0.437  -27.023 21.110  1.00 25.69 ? 101  ASP C O   1 
ATOM   2970  C  CB  . ASP C  1 101 ? 1.433   -29.476 20.647  1.00 25.34 ? 101  ASP C CB  1 
ATOM   2971  C  CG  . ASP C  1 101 ? 2.588   -29.054 19.766  1.00 25.20 ? 101  ASP C CG  1 
ATOM   2972  O  OD1 . ASP C  1 101 ? 3.755   -29.176 20.211  1.00 27.61 ? 101  ASP C OD1 1 
ATOM   2973  O  OD2 . ASP C  1 101 ? 2.335   -28.601 18.632  1.00 25.97 ? 101  ASP C OD2 1 
ATOM   2974  N  N   . ARG C  1 102 ? 1.661   -26.231 21.298  1.00 28.81 ? 102  ARG C N   1 
ATOM   2975  C  CA  . ARG C  1 102 ? 1.315   -24.859 20.963  1.00 27.60 ? 102  ARG C CA  1 
ATOM   2976  C  C   . ARG C  1 102 ? 1.610   -24.495 19.510  1.00 26.86 ? 102  ARG C C   1 
ATOM   2977  O  O   . ARG C  1 102 ? 1.319   -23.375 19.095  1.00 30.13 ? 102  ARG C O   1 
ATOM   2978  C  CB  . ARG C  1 102 ? 2.067   -23.903 21.895  1.00 32.22 ? 102  ARG C CB  1 
ATOM   2979  C  CG  . ARG C  1 102 ? 1.960   -24.261 23.372  1.00 37.64 ? 102  ARG C CG  1 
ATOM   2980  C  CD  . ARG C  1 102 ? 2.774   -23.298 24.247  1.00 47.72 ? 102  ARG C CD  1 
ATOM   2981  N  NE  . ARG C  1 102 ? 2.442   -23.423 25.670  1.00 54.72 ? 102  ARG C NE  1 
ATOM   2982  C  CZ  . ARG C  1 102 ? 1.422   -22.801 26.265  1.00 50.88 ? 102  ARG C CZ  1 
ATOM   2983  N  NH1 . ARG C  1 102 ? 0.620   -22.005 25.569  1.00 47.74 ? 102  ARG C NH1 1 
ATOM   2984  N  NH2 . ARG C  1 102 ? 1.198   -22.978 27.559  1.00 52.66 ? 102  ARG C NH2 1 
ATOM   2985  N  N   . VAL C  1 103 ? 2.191   -25.421 18.743  1.00 26.52 ? 103  VAL C N   1 
ATOM   2986  C  CA  . VAL C  1 103 ? 2.533   -25.150 17.336  1.00 26.87 ? 103  VAL C CA  1 
ATOM   2987  C  C   . VAL C  1 103 ? 1.450   -25.600 16.336  1.00 26.44 ? 103  VAL C C   1 
ATOM   2988  O  O   . VAL C  1 103 ? 1.161   -24.901 15.361  1.00 25.29 ? 103  VAL C O   1 
ATOM   2989  C  CB  . VAL C  1 103 ? 3.916   -25.743 16.947  1.00 25.40 ? 103  VAL C CB  1 
ATOM   2990  C  CG1 . VAL C  1 103 ? 4.223   -25.493 15.481  1.00 24.08 ? 103  VAL C CG1 1 
ATOM   2991  C  CG2 . VAL C  1 103 ? 5.006   -25.139 17.809  1.00 26.83 ? 103  VAL C CG2 1 
ATOM   2992  N  N   . ILE C  1 104 ? 0.863   -26.768 16.578  1.00 25.31 ? 104  ILE C N   1 
ATOM   2993  C  CA  . ILE C  1 104 ? -0.310  -27.199 15.831  1.00 24.42 ? 104  ILE C CA  1 
ATOM   2994  C  C   . ILE C  1 104 ? -1.524  -26.412 16.315  1.00 28.61 ? 104  ILE C C   1 
ATOM   2995  O  O   . ILE C  1 104 ? -1.510  -25.875 17.427  1.00 29.28 ? 104  ILE C O   1 
ATOM   2996  C  CB  . ILE C  1 104 ? -0.598  -28.709 16.021  1.00 25.66 ? 104  ILE C CB  1 
ATOM   2997  C  CG1 . ILE C  1 104 ? -0.696  -29.056 17.510  1.00 21.98 ? 104  ILE C CG1 1 
ATOM   2998  C  CG2 . ILE C  1 104 ? 0.466   -29.562 15.325  1.00 23.84 ? 104  ILE C CG2 1 
ATOM   2999  C  CD1 . ILE C  1 104 ? -1.288  -30.419 17.767  1.00 21.70 ? 104  ILE C CD1 1 
ATOM   3000  N  N   . SER C  1 105 ? -2.571  -26.354 15.486  1.00 29.29 ? 105  SER C N   1 
ATOM   3001  C  CA  . SER C  1 105 ? -3.824  -25.696 15.842  1.00 24.46 ? 105  SER C CA  1 
ATOM   3002  C  C   . SER C  1 105 ? -4.996  -26.450 15.222  1.00 25.01 ? 105  SER C C   1 
ATOM   3003  O  O   . SER C  1 105 ? -4.799  -27.307 14.368  1.00 25.55 ? 105  SER C O   1 
ATOM   3004  C  CB  . SER C  1 105 ? -3.809  -24.251 15.347  1.00 27.57 ? 105  SER C CB  1 
ATOM   3005  O  OG  . SER C  1 105 ? -4.906  -23.518 15.860  1.00 30.84 ? 105  SER C OG  1 
ATOM   3006  N  N   . LEU C  1 106 ? -6.215  -26.135 15.645  1.00 26.31 ? 106  LEU C N   1 
ATOM   3007  C  CA  . LEU C  1 106 ? -7.406  -26.722 15.033  1.00 23.48 ? 106  LEU C CA  1 
ATOM   3008  C  C   . LEU C  1 106 ? -8.124  -25.695 14.153  1.00 24.68 ? 106  LEU C C   1 
ATOM   3009  O  O   . LEU C  1 106 ? -9.214  -25.950 13.641  1.00 25.58 ? 106  LEU C O   1 
ATOM   3010  C  CB  . LEU C  1 106 ? -8.348  -27.321 16.086  1.00 25.41 ? 106  LEU C CB  1 
ATOM   3011  C  CG  . LEU C  1 106 ? -7.814  -28.468 16.954  1.00 24.17 ? 106  LEU C CG  1 
ATOM   3012  C  CD1 . LEU C  1 106 ? -8.949  -29.162 17.690  1.00 19.37 ? 106  LEU C CD1 1 
ATOM   3013  C  CD2 . LEU C  1 106 ? -7.003  -29.468 16.112  1.00 21.35 ? 106  LEU C CD2 1 
ATOM   3014  N  N   . SER C  1 107 ? -7.487  -24.540 13.971  1.00 26.91 ? 107  SER C N   1 
ATOM   3015  C  CA  . SER C  1 107 ? -7.970  -23.501 13.065  1.00 29.41 ? 107  SER C CA  1 
ATOM   3016  C  C   . SER C  1 107 ? -6.811  -22.686 12.486  1.00 28.26 ? 107  SER C C   1 
ATOM   3017  O  O   . SER C  1 107 ? -5.684  -22.763 12.952  1.00 30.25 ? 107  SER C O   1 
ATOM   3018  C  CB  . SER C  1 107 ? -8.977  -22.572 13.767  1.00 31.24 ? 107  SER C CB  1 
ATOM   3019  O  OG  . SER C  1 107 ? -8.374  -21.831 14.821  1.00 33.87 ? 107  SER C OG  1 
ATOM   3020  N  N   . GLY C  1 108 ? -7.096  -21.904 11.459  1.00 31.15 ? 108  GLY C N   1 
ATOM   3021  C  CA  . GLY C  1 108 ? -6.089  -21.062 10.849  1.00 32.21 ? 108  GLY C CA  1 
ATOM   3022  C  C   . GLY C  1 108 ? -5.149  -21.785 9.906   1.00 32.79 ? 108  GLY C C   1 
ATOM   3023  O  O   . GLY C  1 108 ? -5.386  -22.915 9.475   1.00 31.49 ? 108  GLY C O   1 
ATOM   3024  N  N   . GLU C  1 109 ? -4.054  -21.107 9.604   1.00 33.74 ? 109  GLU C N   1 
ATOM   3025  C  CA  . GLU C  1 109 ? -3.065  -21.551 8.627   1.00 34.40 ? 109  GLU C CA  1 
ATOM   3026  C  C   . GLU C  1 109 ? -2.289  -22.788 9.085   1.00 34.02 ? 109  GLU C C   1 
ATOM   3027  O  O   . GLU C  1 109 ? -1.731  -23.521 8.270   1.00 32.10 ? 109  GLU C O   1 
ATOM   3028  C  CB  . GLU C  1 109 ? -2.091  -20.399 8.345   1.00 37.25 ? 109  GLU C CB  1 
ATOM   3029  C  CG  . GLU C  1 109 ? -2.731  -18.989 8.382   1.00 45.69 ? 109  GLU C CG  1 
ATOM   3030  C  CD  . GLU C  1 109 ? -3.429  -18.652 9.718   1.00 46.42 ? 109  GLU C CD  1 
ATOM   3031  O  OE1 . GLU C  1 109 ? -4.560  -18.111 9.684   1.00 45.55 ? 109  GLU C OE1 1 
ATOM   3032  O  OE2 . GLU C  1 109 ? -2.858  -18.938 10.800  1.00 51.11 ? 109  GLU C OE2 1 
ATOM   3033  N  N   . HIS C  1 110 ? -2.246  -23.011 10.396  1.00 35.96 ? 110  HIS C N   1 
ATOM   3034  C  CA  . HIS C  1 110 ? -1.525  -24.155 10.955  1.00 33.37 ? 110  HIS C CA  1 
ATOM   3035  C  C   . HIS C  1 110 ? -2.472  -25.244 11.464  1.00 28.21 ? 110  HIS C C   1 
ATOM   3036  O  O   . HIS C  1 110 ? -2.086  -26.075 12.288  1.00 27.51 ? 110  HIS C O   1 
ATOM   3037  C  CB  . HIS C  1 110 ? -0.541  -23.691 12.040  1.00 33.27 ? 110  HIS C CB  1 
ATOM   3038  C  CG  . HIS C  1 110 ? 0.653   -22.972 11.486  1.00 35.45 ? 110  HIS C CG  1 
ATOM   3039  N  ND1 . HIS C  1 110 ? 1.770   -22.683 12.238  1.00 32.77 ? 110  HIS C ND1 1 
ATOM   3040  C  CD2 . HIS C  1 110 ? 0.912   -22.513 10.235  1.00 34.09 ? 110  HIS C CD2 1 
ATOM   3041  C  CE1 . HIS C  1 110 ? 2.659   -22.063 11.480  1.00 32.84 ? 110  HIS C CE1 1 
ATOM   3042  N  NE2 . HIS C  1 110 ? 2.160   -21.945 10.262  1.00 33.11 ? 110  HIS C NE2 1 
ATOM   3043  N  N   . SER C  1 111 ? -3.702  -25.231 10.945  1.00 27.98 ? 111  SER C N   1 
ATOM   3044  C  CA  . SER C  1 111 ? -4.735  -26.177 11.340  1.00 25.44 ? 111  SER C CA  1 
ATOM   3045  C  C   . SER C  1 111 ? -4.429  -27.544 10.764  1.00 23.56 ? 111  SER C C   1 
ATOM   3046  O  O   . SER C  1 111 ? -4.049  -27.678 9.594   1.00 21.30 ? 111  SER C O   1 
ATOM   3047  C  CB  . SER C  1 111 ? -6.121  -25.714 10.869  1.00 26.27 ? 111  SER C CB  1 
ATOM   3048  O  OG  . SER C  1 111 ? -7.127  -26.662 11.209  1.00 22.88 ? 111  SER C OG  1 
ATOM   3049  N  N   . ILE C  1 112 ? -4.612  -28.562 11.593  1.00 22.41 ? 112  ILE C N   1 
ATOM   3050  C  CA  . ILE C  1 112 ? -4.339  -29.921 11.179  1.00 18.83 ? 112  ILE C CA  1 
ATOM   3051  C  C   . ILE C  1 112 ? -5.639  -30.657 10.904  1.00 19.31 ? 112  ILE C C   1 
ATOM   3052  O  O   . ILE C  1 112 ? -5.637  -31.867 10.746  1.00 20.64 ? 112  ILE C O   1 
ATOM   3053  C  CB  . ILE C  1 112 ? -3.501  -30.669 12.227  1.00 21.00 ? 112  ILE C CB  1 
ATOM   3054  C  CG1 . ILE C  1 112 ? -4.296  -30.866 13.522  1.00 19.33 ? 112  ILE C CG1 1 
ATOM   3055  C  CG2 . ILE C  1 112 ? -2.173  -29.922 12.493  1.00 21.72 ? 112  ILE C CG2 1 
ATOM   3056  C  CD1 . ILE C  1 112 ? -3.459  -31.406 14.678  1.00 19.20 ? 112  ILE C CD1 1 
ATOM   3057  N  N   . ILE C  1 113 ? -6.746  -29.917 10.844  1.00 20.08 ? 113  ILE C N   1 
ATOM   3058  C  CA  . ILE C  1 113 ? -8.024  -30.481 10.411  1.00 20.18 ? 113  ILE C CA  1 
ATOM   3059  C  C   . ILE C  1 113 ? -7.942  -30.845 8.922   1.00 19.94 ? 113  ILE C C   1 
ATOM   3060  O  O   . ILE C  1 113 ? -7.514  -30.022 8.088   1.00 20.49 ? 113  ILE C O   1 
ATOM   3061  C  CB  . ILE C  1 113 ? -9.212  -29.511 10.670  1.00 20.21 ? 113  ILE C CB  1 
ATOM   3062  C  CG1 . ILE C  1 113 ? -9.286  -29.124 12.152  1.00 21.64 ? 113  ILE C CG1 1 
ATOM   3063  C  CG2 . ILE C  1 113 ? -10.524 -30.147 10.265  1.00 18.35 ? 113  ILE C CG2 1 
ATOM   3064  C  CD1 . ILE C  1 113 ? -9.915  -30.167 13.022  1.00 19.44 ? 113  ILE C CD1 1 
ATOM   3065  N  N   . GLY C  1 114 ? -8.341  -32.076 8.594   1.00 17.05 ? 114  GLY C N   1 
ATOM   3066  C  CA  . GLY C  1 114 ? -8.252  -32.569 7.234   1.00 15.33 ? 114  GLY C CA  1 
ATOM   3067  C  C   . GLY C  1 114 ? -6.876  -33.096 6.880   1.00 15.72 ? 114  GLY C C   1 
ATOM   3068  O  O   . GLY C  1 114 ? -6.601  -33.402 5.725   1.00 17.09 ? 114  GLY C O   1 
ATOM   3069  N  N   . ARG C  1 115 ? -5.994  -33.193 7.871   1.00 16.18 ? 115  ARG C N   1 
ATOM   3070  C  CA  . ARG C  1 115 ? -4.680  -33.787 7.644   1.00 16.58 ? 115  ARG C CA  1 
ATOM   3071  C  C   . ARG C  1 115 ? -4.618  -35.172 8.283   1.00 14.61 ? 115  ARG C C   1 
ATOM   3072  O  O   . ARG C  1 115 ? -5.655  -35.736 8.608   1.00 14.25 ? 115  ARG C O   1 
ATOM   3073  C  CB  . ARG C  1 115 ? -3.566  -32.841 8.084   1.00 15.97 ? 115  ARG C CB  1 
ATOM   3074  C  CG  . ARG C  1 115 ? -3.768  -31.445 7.493   1.00 14.97 ? 115  ARG C CG  1 
ATOM   3075  C  CD  . ARG C  1 115 ? -2.532  -30.591 7.547   1.00 17.72 ? 115  ARG C CD  1 
ATOM   3076  N  NE  . ARG C  1 115 ? -2.801  -29.224 7.108   1.00 18.19 ? 115  ARG C NE  1 
ATOM   3077  C  CZ  . ARG C  1 115 ? -2.549  -28.764 5.884   1.00 19.53 ? 115  ARG C CZ  1 
ATOM   3078  N  NH1 . ARG C  1 115 ? -2.029  -29.563 4.965   1.00 21.46 ? 115  ARG C NH1 1 
ATOM   3079  N  NH2 . ARG C  1 115 ? -2.814  -27.504 5.574   1.00 19.45 ? 115  ARG C NH2 1 
ATOM   3080  N  N   . THR C  1 116 ? -3.434  -35.753 8.410   1.00 15.53 ? 116  THR C N   1 
ATOM   3081  C  CA  . THR C  1 116 ? -3.340  -37.150 8.870   1.00 18.56 ? 116  THR C CA  1 
ATOM   3082  C  C   . THR C  1 116 ? -2.437  -37.328 10.100  1.00 18.09 ? 116  THR C C   1 
ATOM   3083  O  O   . THR C  1 116 ? -1.323  -36.825 10.114  1.00 20.33 ? 116  THR C O   1 
ATOM   3084  C  CB  . THR C  1 116 ? -2.816  -38.074 7.728   1.00 16.57 ? 116  THR C CB  1 
ATOM   3085  O  OG1 . THR C  1 116 ? -3.759  -38.108 6.652   1.00 15.91 ? 116  THR C OG1 1 
ATOM   3086  C  CG2 . THR C  1 116 ? -2.570  -39.492 8.222   1.00 15.93 ? 116  THR C CG2 1 
ATOM   3087  N  N   . MET C  1 117 ? -2.908  -38.040 11.127  1.00 18.52 ? 117  MET C N   1 
ATOM   3088  C  CA  . MET C  1 117 ? -2.017  -38.504 12.198  1.00 18.89 ? 117  MET C CA  1 
ATOM   3089  C  C   . MET C  1 117 ? -1.391  -39.820 11.758  1.00 17.82 ? 117  MET C C   1 
ATOM   3090  O  O   . MET C  1 117 ? -2.096  -40.718 11.305  1.00 18.47 ? 117  MET C O   1 
ATOM   3091  C  CB  . MET C  1 117 ? -2.783  -38.797 13.494  1.00 21.80 ? 117  MET C CB  1 
ATOM   3092  C  CG  . MET C  1 117 ? -3.083  -37.621 14.391  1.00 26.71 ? 117  MET C CG  1 
ATOM   3093  S  SD  . MET C  1 117 ? -1.685  -36.551 14.742  1.00 36.03 ? 117  MET C SD  1 
ATOM   3094  C  CE  . MET C  1 117 ? -0.437  -37.705 15.281  1.00 22.90 ? 117  MET C CE  1 
ATOM   3095  N  N   . VAL C  1 118 ? -0.079  -39.959 11.891  1.00 19.83 ? 118  VAL C N   1 
ATOM   3096  C  CA  . VAL C  1 118 ? 0.513   -41.289 11.756  1.00 18.06 ? 118  VAL C CA  1 
ATOM   3097  C  C   . VAL C  1 118 ? 1.400   -41.669 12.939  1.00 19.61 ? 118  VAL C C   1 
ATOM   3098  O  O   . VAL C  1 118 ? 2.123   -40.833 13.501  1.00 20.52 ? 118  VAL C O   1 
ATOM   3099  C  CB  . VAL C  1 118 ? 1.139   -41.599 10.332  1.00 18.74 ? 118  VAL C CB  1 
ATOM   3100  C  CG1 . VAL C  1 118 ? 1.163   -40.386 9.440   1.00 18.22 ? 118  VAL C CG1 1 
ATOM   3101  C  CG2 . VAL C  1 118 ? 2.489   -42.296 10.429  1.00 16.21 ? 118  VAL C CG2 1 
ATOM   3102  N  N   . VAL C  1 119 ? 1.254   -42.921 13.367  1.00 19.45 ? 119  VAL C N   1 
ATOM   3103  C  CA  . VAL C  1 119 ? 2.166   -43.516 14.327  1.00 16.75 ? 119  VAL C CA  1 
ATOM   3104  C  C   . VAL C  1 119 ? 3.129   -44.407 13.542  1.00 17.66 ? 119  VAL C C   1 
ATOM   3105  O  O   . VAL C  1 119 ? 2.731   -45.119 12.598  1.00 16.07 ? 119  VAL C O   1 
ATOM   3106  C  CB  . VAL C  1 119 ? 1.434   -44.247 15.496  1.00 16.93 ? 119  VAL C CB  1 
ATOM   3107  C  CG1 . VAL C  1 119 ? 0.512   -45.355 14.997  1.00 14.42 ? 119  VAL C CG1 1 
ATOM   3108  C  CG2 . VAL C  1 119 ? 2.449   -44.769 16.532  1.00 15.53 ? 119  VAL C CG2 1 
ATOM   3109  N  N   . HIS C  1 120 ? 4.402   -44.332 13.921  1.00 17.11 ? 120  HIS C N   1 
ATOM   3110  C  CA  . HIS C  1 120 ? 5.480   -44.890 13.124  1.00 16.75 ? 120  HIS C CA  1 
ATOM   3111  C  C   . HIS C  1 120 ? 6.093   -46.133 13.749  1.00 17.21 ? 120  HIS C C   1 
ATOM   3112  O  O   . HIS C  1 120 ? 5.940   -46.385 14.941  1.00 19.91 ? 120  HIS C O   1 
ATOM   3113  C  CB  . HIS C  1 120 ? 6.564   -43.829 12.895  1.00 15.27 ? 120  HIS C CB  1 
ATOM   3114  C  CG  . HIS C  1 120 ? 6.171   -42.761 11.925  1.00 16.72 ? 120  HIS C CG  1 
ATOM   3115  N  ND1 . HIS C  1 120 ? 6.308   -42.909 10.561  1.00 15.87 ? 120  HIS C ND1 1 
ATOM   3116  C  CD2 . HIS C  1 120 ? 5.633   -41.533 12.118  1.00 16.56 ? 120  HIS C CD2 1 
ATOM   3117  C  CE1 . HIS C  1 120 ? 5.879   -41.813 9.957   1.00 18.05 ? 120  HIS C CE1 1 
ATOM   3118  N  NE2 . HIS C  1 120 ? 5.464   -40.965 10.880  1.00 17.99 ? 120  HIS C NE2 1 
ATOM   3119  N  N   . GLU C  1 121 ? 6.808   -46.885 12.918  1.00 19.76 ? 121  GLU C N   1 
ATOM   3120  C  CA  . GLU C  1 121 ? 7.555   -48.085 13.308  1.00 20.19 ? 121  GLU C CA  1 
ATOM   3121  C  C   . GLU C  1 121 ? 8.427   -47.961 14.571  1.00 20.05 ? 121  GLU C C   1 
ATOM   3122  O  O   . GLU C  1 121 ? 8.307   -48.741 15.517  1.00 18.48 ? 121  GLU C O   1 
ATOM   3123  C  CB  . GLU C  1 121 ? 8.448   -48.506 12.137  1.00 19.09 ? 121  GLU C CB  1 
ATOM   3124  C  CG  . GLU C  1 121 ? 9.285   -49.754 12.390  1.00 21.45 ? 121  GLU C CG  1 
ATOM   3125  C  CD  . GLU C  1 121 ? 10.317  -49.997 11.295  1.00 23.64 ? 121  GLU C CD  1 
ATOM   3126  O  OE1 . GLU C  1 121 ? 10.462  -49.128 10.401  1.00 23.41 ? 121  GLU C OE1 1 
ATOM   3127  O  OE2 . GLU C  1 121 ? 10.991  -51.052 11.332  1.00 28.30 ? 121  GLU C OE2 1 
ATOM   3128  N  N   . LYS C  1 122 ? 9.345   -47.005 14.560  1.00 21.88 ? 122  LYS C N   1 
ATOM   3129  C  CA  . LYS C  1 122 ? 10.298  -46.895 15.645  1.00 20.34 ? 122  LYS C CA  1 
ATOM   3130  C  C   . LYS C  1 122 ? 10.401  -45.481 16.209  1.00 19.13 ? 122  LYS C C   1 
ATOM   3131  O  O   . LYS C  1 122 ? 9.518   -44.639 16.012  1.00 17.01 ? 122  LYS C O   1 
ATOM   3132  C  CB  . LYS C  1 122 ? 11.674  -47.426 15.212  1.00 21.93 ? 122  LYS C CB  1 
ATOM   3133  C  CG  . LYS C  1 122 ? 12.220  -46.818 13.938  1.00 21.44 ? 122  LYS C CG  1 
ATOM   3134  C  CD  . LYS C  1 122 ? 13.220  -47.745 13.285  1.00 22.95 ? 122  LYS C CD  1 
ATOM   3135  C  CE  . LYS C  1 122 ? 13.854  -47.099 12.075  1.00 27.70 ? 122  LYS C CE  1 
ATOM   3136  N  NZ  . LYS C  1 122 ? 14.837  -47.999 11.416  1.00 34.92 ? 122  LYS C NZ  1 
ATOM   3137  N  N   . GLN C  1 123 ? 11.491  -45.236 16.921  1.00 18.55 ? 123  GLN C N   1 
ATOM   3138  C  CA  . GLN C  1 123 ? 11.606  -44.038 17.724  1.00 17.61 ? 123  GLN C CA  1 
ATOM   3139  C  C   . GLN C  1 123 ? 12.103  -42.874 16.909  1.00 16.13 ? 123  GLN C C   1 
ATOM   3140  O  O   . GLN C  1 123 ? 13.036  -43.009 16.143  1.00 18.77 ? 123  GLN C O   1 
ATOM   3141  C  CB  . GLN C  1 123 ? 12.539  -44.292 18.898  1.00 20.29 ? 123  GLN C CB  1 
ATOM   3142  C  CG  . GLN C  1 123 ? 12.738  -43.108 19.794  1.00 19.10 ? 123  GLN C CG  1 
ATOM   3143  C  CD  . GLN C  1 123 ? 13.742  -43.409 20.866  1.00 21.41 ? 123  GLN C CD  1 
ATOM   3144  O  OE1 . GLN C  1 123 ? 13.956  -44.569 21.213  1.00 22.59 ? 123  GLN C OE1 1 
ATOM   3145  N  NE2 . GLN C  1 123 ? 14.374  -42.375 21.392  1.00 21.97 ? 123  GLN C NE2 1 
ATOM   3146  N  N   . ASP C  1 124 ? 11.455  -41.732 17.091  1.00 16.27 ? 124  ASP C N   1 
ATOM   3147  C  CA  . ASP C  1 124 ? 11.836  -40.477 16.465  1.00 16.87 ? 124  ASP C CA  1 
ATOM   3148  C  C   . ASP C  1 124 ? 13.078  -39.933 17.183  1.00 16.89 ? 124  ASP C C   1 
ATOM   3149  O  O   . ASP C  1 124 ? 13.081  -39.774 18.400  1.00 18.98 ? 124  ASP C O   1 
ATOM   3150  C  CB  . ASP C  1 124 ? 10.630  -39.531 16.554  1.00 16.55 ? 124  ASP C CB  1 
ATOM   3151  C  CG  . ASP C  1 124 ? 10.927  -38.127 16.095  1.00 17.75 ? 124  ASP C CG  1 
ATOM   3152  O  OD1 . ASP C  1 124 ? 12.099  -37.789 15.831  1.00 17.75 ? 124  ASP C OD1 1 
ATOM   3153  O  OD2 . ASP C  1 124 ? 9.960   -37.344 16.011  1.00 18.38 ? 124  ASP C OD2 1 
ATOM   3154  N  N   . ASP C  1 125 ? 14.146  -39.679 16.440  1.00 18.25 ? 125  ASP C N   1 
ATOM   3155  C  CA  . ASP C  1 125 ? 15.390  -39.189 17.052  1.00 18.97 ? 125  ASP C CA  1 
ATOM   3156  C  C   . ASP C  1 125 ? 15.423  -37.669 17.194  1.00 20.03 ? 125  ASP C C   1 
ATOM   3157  O  O   . ASP C  1 125 ? 16.460  -37.095 17.535  1.00 18.54 ? 125  ASP C O   1 
ATOM   3158  C  CB  . ASP C  1 125 ? 16.642  -39.695 16.310  1.00 20.32 ? 125  ASP C CB  1 
ATOM   3159  C  CG  . ASP C  1 125 ? 16.690  -39.278 14.830  1.00 19.84 ? 125  ASP C CG  1 
ATOM   3160  O  OD1 . ASP C  1 125 ? 16.096  -38.248 14.441  1.00 17.70 ? 125  ASP C OD1 1 
ATOM   3161  O  OD2 . ASP C  1 125 ? 17.365  -39.984 14.050  1.00 20.80 ? 125  ASP C OD2 1 
ATOM   3162  N  N   . LEU C  1 126 ? 14.277  -37.038 16.925  1.00 21.31 ? 126  LEU C N   1 
ATOM   3163  C  CA  . LEU C  1 126 ? 14.086  -35.601 17.109  1.00 21.51 ? 126  LEU C CA  1 
ATOM   3164  C  C   . LEU C  1 126 ? 15.045  -34.736 16.255  1.00 21.18 ? 126  LEU C C   1 
ATOM   3165  O  O   . LEU C  1 126 ? 15.392  -33.612 16.635  1.00 20.99 ? 126  LEU C O   1 
ATOM   3166  C  CB  . LEU C  1 126 ? 14.164  -35.240 18.605  1.00 21.08 ? 126  LEU C CB  1 
ATOM   3167  C  CG  . LEU C  1 126 ? 13.394  -36.071 19.651  1.00 20.80 ? 126  LEU C CG  1 
ATOM   3168  C  CD1 . LEU C  1 126 ? 13.637  -35.518 21.051  1.00 20.42 ? 126  LEU C CD1 1 
ATOM   3169  C  CD2 . LEU C  1 126 ? 11.895  -36.160 19.388  1.00 19.08 ? 126  LEU C CD2 1 
ATOM   3170  N  N   . GLY C  1 127 ? 15.459  -35.263 15.101  1.00 19.27 ? 127  GLY C N   1 
ATOM   3171  C  CA  . GLY C  1 127 ? 16.296  -34.523 14.169  1.00 18.13 ? 127  GLY C CA  1 
ATOM   3172  C  C   . GLY C  1 127 ? 17.784  -34.499 14.493  1.00 20.46 ? 127  GLY C C   1 
ATOM   3173  O  O   . GLY C  1 127 ? 18.571  -33.809 13.841  1.00 21.92 ? 127  GLY C O   1 
ATOM   3174  N  N   . LYS C  1 128 ? 18.173  -35.259 15.510  1.00 25.75 ? 128  LYS C N   1 
ATOM   3175  C  CA  . LYS C  1 128 ? 19.551  -35.262 15.995  1.00 22.51 ? 128  LYS C CA  1 
ATOM   3176  C  C   . LYS C  1 128 ? 20.264  -36.587 15.731  1.00 21.25 ? 128  LYS C C   1 
ATOM   3177  O  O   . LYS C  1 128 ? 21.097  -37.019 16.535  1.00 24.08 ? 128  LYS C O   1 
ATOM   3178  C  CB  . LYS C  1 128 ? 19.584  -34.950 17.490  1.00 21.51 ? 128  LYS C CB  1 
ATOM   3179  C  CG  . LYS C  1 128 ? 18.757  -33.744 17.872  1.00 24.63 ? 128  LYS C CG  1 
ATOM   3180  C  CD  . LYS C  1 128 ? 19.124  -33.223 19.238  1.00 28.01 ? 128  LYS C CD  1 
ATOM   3181  C  CE  . LYS C  1 128 ? 17.878  -32.908 20.044  1.00 33.78 ? 128  LYS C CE  1 
ATOM   3182  N  NZ  . LYS C  1 128 ? 16.802  -32.268 19.228  1.00 40.15 ? 128  LYS C NZ  1 
ATOM   3183  N  N   . GLY C  1 129 ? 19.952  -37.212 14.600  1.00 19.52 ? 129  GLY C N   1 
ATOM   3184  C  CA  . GLY C  1 129 ? 20.524  -38.497 14.249  1.00 19.80 ? 129  GLY C CA  1 
ATOM   3185  C  C   . GLY C  1 129 ? 21.714  -38.467 13.301  1.00 17.94 ? 129  GLY C C   1 
ATOM   3186  O  O   . GLY C  1 129 ? 22.266  -39.507 12.995  1.00 16.35 ? 129  GLY C O   1 
ATOM   3187  N  N   . GLY C  1 130 ? 22.106  -37.285 12.835  1.00 18.39 ? 130  GLY C N   1 
ATOM   3188  C  CA  . GLY C  1 130 ? 23.313  -37.142 12.038  1.00 18.57 ? 130  GLY C CA  1 
ATOM   3189  C  C   . GLY C  1 130 ? 23.195  -37.560 10.580  1.00 19.80 ? 130  GLY C C   1 
ATOM   3190  O  O   . GLY C  1 130 ? 24.191  -37.842 9.917   1.00 17.55 ? 130  GLY C O   1 
ATOM   3191  N  N   . ASN C  1 131 ? 21.970  -37.621 10.077  1.00 21.34 ? 131  ASN C N   1 
ATOM   3192  C  CA  . ASN C  1 131 ? 21.753  -37.914 8.662   1.00 21.29 ? 131  ASN C CA  1 
ATOM   3193  C  C   . ASN C  1 131 ? 20.520  -37.235 8.081   1.00 21.11 ? 131  ASN C C   1 
ATOM   3194  O  O   . ASN C  1 131 ? 19.720  -36.639 8.803   1.00 21.24 ? 131  ASN C O   1 
ATOM   3195  C  CB  . ASN C  1 131 ? 21.769  -39.424 8.359   1.00 19.45 ? 131  ASN C CB  1 
ATOM   3196  C  CG  . ASN C  1 131 ? 20.643  -40.175 9.016   1.00 19.45 ? 131  ASN C CG  1 
ATOM   3197  O  OD1 . ASN C  1 131 ? 19.630  -39.596 9.419   1.00 18.95 ? 131  ASN C OD1 1 
ATOM   3198  N  ND2 . ASN C  1 131 ? 20.807  -41.482 9.126   1.00 18.76 ? 131  ASN C ND2 1 
ATOM   3199  N  N   . GLU C  1 132 ? 20.394  -37.312 6.766   1.00 22.19 ? 132  GLU C N   1 
ATOM   3200  C  CA  . GLU C  1 132 ? 19.327  -36.625 6.075   1.00 26.07 ? 132  GLU C CA  1 
ATOM   3201  C  C   . GLU C  1 132 ? 17.948  -37.174 6.445   1.00 25.49 ? 132  GLU C C   1 
ATOM   3202  O  O   . GLU C  1 132 ? 17.005  -36.396 6.564   1.00 26.35 ? 132  GLU C O   1 
ATOM   3203  C  CB  . GLU C  1 132 ? 19.554  -36.684 4.568   1.00 32.95 ? 132  GLU C CB  1 
ATOM   3204  C  CG  . GLU C  1 132 ? 18.757  -35.668 3.773   1.00 41.17 ? 132  GLU C CG  1 
ATOM   3205  C  CD  . GLU C  1 132 ? 18.760  -35.985 2.290   1.00 51.65 ? 132  GLU C CD  1 
ATOM   3206  O  OE1 . GLU C  1 132 ? 18.948  -37.174 1.929   1.00 50.45 ? 132  GLU C OE1 1 
ATOM   3207  O  OE2 . GLU C  1 132 ? 18.573  -35.047 1.487   1.00 60.02 ? 132  GLU C OE2 1 
ATOM   3208  N  N   . GLU C  1 133 ? 17.816  -38.493 6.625   1.00 23.05 ? 133  GLU C N   1 
ATOM   3209  C  CA  . GLU C  1 133 ? 16.541  -39.053 7.116   1.00 24.83 ? 133  GLU C CA  1 
ATOM   3210  C  C   . GLU C  1 133 ? 16.120  -38.435 8.457   1.00 21.60 ? 133  GLU C C   1 
ATOM   3211  O  O   . GLU C  1 133 ? 14.944  -38.163 8.688   1.00 23.41 ? 133  GLU C O   1 
ATOM   3212  C  CB  . GLU C  1 133 ? 16.583  -40.586 7.250   1.00 25.68 ? 133  GLU C CB  1 
ATOM   3213  C  CG  . GLU C  1 133 ? 16.122  -41.373 6.014   1.00 31.40 ? 133  GLU C CG  1 
ATOM   3214  C  CD  . GLU C  1 133 ? 14.685  -41.087 5.615   1.00 31.23 ? 133  GLU C CD  1 
ATOM   3215  O  OE1 . GLU C  1 133 ? 13.835  -40.877 6.501   1.00 27.91 ? 133  GLU C OE1 1 
ATOM   3216  O  OE2 . GLU C  1 133 ? 14.403  -41.083 4.399   1.00 43.83 ? 133  GLU C OE2 1 
ATOM   3217  N  N   . SER C  1 134 ? 17.085  -38.225 9.343   1.00 21.50 ? 134  SER C N   1 
ATOM   3218  C  CA  . SER C  1 134 ? 16.826  -37.584 10.632  1.00 21.29 ? 134  SER C CA  1 
ATOM   3219  C  C   . SER C  1 134 ? 16.160  -36.208 10.498  1.00 22.27 ? 134  SER C C   1 
ATOM   3220  O  O   . SER C  1 134 ? 15.227  -35.890 11.239  1.00 18.88 ? 134  SER C O   1 
ATOM   3221  C  CB  . SER C  1 134 ? 18.130  -37.443 11.410  1.00 20.05 ? 134  SER C CB  1 
ATOM   3222  O  OG  . SER C  1 134 ? 17.889  -37.045 12.753  1.00 22.20 ? 134  SER C OG  1 
ATOM   3223  N  N   . THR C  1 135 ? 16.648  -35.405 9.549   1.00 22.24 ? 135  THR C N   1 
ATOM   3224  C  CA  . THR C  1 135 ? 16.190  -34.024 9.355   1.00 23.65 ? 135  THR C CA  1 
ATOM   3225  C  C   . THR C  1 135 ? 14.861  -33.974 8.613   1.00 22.81 ? 135  THR C C   1 
ATOM   3226  O  O   . THR C  1 135 ? 14.326  -32.890 8.363   1.00 23.20 ? 135  THR C O   1 
ATOM   3227  C  CB  . THR C  1 135 ? 17.225  -33.171 8.568   1.00 24.14 ? 135  THR C CB  1 
ATOM   3228  O  OG1 . THR C  1 135 ? 17.208  -33.539 7.180   1.00 27.18 ? 135  THR C OG1 1 
ATOM   3229  C  CG2 . THR C  1 135 ? 18.636  -33.360 9.129   1.00 24.53 ? 135  THR C CG2 1 
ATOM   3230  N  N   . LYS C  1 136 ? 14.344  -35.154 8.268   1.00 24.57 ? 136  LYS C N   1 
ATOM   3231  C  CA  . LYS C  1 136 ? 13.082  -35.299 7.550   1.00 20.36 ? 136  LYS C CA  1 
ATOM   3232  C  C   . LYS C  1 136 ? 12.020  -36.013 8.380   1.00 19.25 ? 136  LYS C C   1 
ATOM   3233  O  O   . LYS C  1 136 ? 10.949  -35.471 8.610   1.00 17.53 ? 136  LYS C O   1 
ATOM   3234  C  CB  . LYS C  1 136 ? 13.288  -36.078 6.251   1.00 22.74 ? 136  LYS C CB  1 
ATOM   3235  C  CG  . LYS C  1 136 ? 13.067  -35.275 4.998   1.00 29.25 ? 136  LYS C CG  1 
ATOM   3236  C  CD  . LYS C  1 136 ? 14.374  -34.879 4.353   1.00 32.22 ? 136  LYS C CD  1 
ATOM   3237  C  CE  . LYS C  1 136 ? 14.937  -36.042 3.580   1.00 37.37 ? 136  LYS C CE  1 
ATOM   3238  N  NZ  . LYS C  1 136 ? 13.959  -36.501 2.555   1.00 48.22 ? 136  LYS C NZ  1 
ATOM   3239  N  N   . THR C  1 137 ? 12.323  -37.240 8.793   1.00 19.17 ? 137  THR C N   1 
ATOM   3240  C  CA  . THR C  1 137 ? 11.374  -38.103 9.483   1.00 19.78 ? 137  THR C CA  1 
ATOM   3241  C  C   . THR C  1 137 ? 11.799  -38.438 10.921  1.00 21.40 ? 137  THR C C   1 
ATOM   3242  O  O   . THR C  1 137 ? 11.055  -39.083 11.680  1.00 21.19 ? 137  THR C O   1 
ATOM   3243  C  CB  . THR C  1 137 ? 11.181  -39.428 8.720   1.00 20.31 ? 137  THR C CB  1 
ATOM   3244  O  OG1 . THR C  1 137 ? 12.397  -40.193 8.762   1.00 23.06 ? 137  THR C OG1 1 
ATOM   3245  C  CG2 . THR C  1 137 ? 10.806  -39.152 7.275   1.00 23.44 ? 137  THR C CG2 1 
ATOM   3246  N  N   . GLY C  1 138 ? 12.996  -38.008 11.297  1.00 19.85 ? 138  GLY C N   1 
ATOM   3247  C  CA  . GLY C  1 138 ? 13.533  -38.373 12.586  1.00 17.27 ? 138  GLY C CA  1 
ATOM   3248  C  C   . GLY C  1 138 ? 13.813  -39.865 12.658  1.00 19.24 ? 138  GLY C C   1 
ATOM   3249  O  O   . GLY C  1 138 ? 13.886  -40.442 13.744  1.00 17.88 ? 138  GLY C O   1 
ATOM   3250  N  N   . ASN C  1 139 ? 13.992  -40.493 11.500  1.00 20.45 ? 139  ASN C N   1 
ATOM   3251  C  CA  . ASN C  1 139 ? 14.265  -41.923 11.451  1.00 19.79 ? 139  ASN C CA  1 
ATOM   3252  C  C   . ASN C  1 139 ? 13.220  -42.743 12.216  1.00 20.70 ? 139  ASN C C   1 
ATOM   3253  O  O   . ASN C  1 139 ? 13.560  -43.765 12.816  1.00 21.77 ? 139  ASN C O   1 
ATOM   3254  C  CB  . ASN C  1 139 ? 15.671  -42.228 12.000  1.00 21.73 ? 139  ASN C CB  1 
ATOM   3255  C  CG  . ASN C  1 139 ? 16.786  -41.923 10.991  1.00 21.26 ? 139  ASN C CG  1 
ATOM   3256  O  OD1 . ASN C  1 139 ? 16.875  -42.557 9.936   1.00 22.18 ? 139  ASN C OD1 1 
ATOM   3257  N  ND2 . ASN C  1 139 ? 17.649  -40.963 11.328  1.00 18.55 ? 139  ASN C ND2 1 
ATOM   3258  N  N   . ALA C  1 140 ? 11.960  -42.302 12.189  1.00 18.89 ? 140  ALA C N   1 
ATOM   3259  C  CA  . ALA C  1 140 ? 10.887  -42.983 12.915  1.00 18.29 ? 140  ALA C CA  1 
ATOM   3260  C  C   . ALA C  1 140 ? 10.385  -44.238 12.204  1.00 17.53 ? 140  ALA C C   1 
ATOM   3261  O  O   . ALA C  1 140 ? 9.650   -45.032 12.774  1.00 17.40 ? 140  ALA C O   1 
ATOM   3262  C  CB  . ALA C  1 140 ? 9.742   -42.038 13.190  1.00 15.52 ? 140  ALA C CB  1 
ATOM   3263  N  N   . GLY C  1 141 ? 10.781  -44.412 10.952  1.00 20.79 ? 141  GLY C N   1 
ATOM   3264  C  CA  . GLY C  1 141 ? 10.500  -45.641 10.238  1.00 19.63 ? 141  GLY C CA  1 
ATOM   3265  C  C   . GLY C  1 141 ? 9.170   -45.628 9.524   1.00 20.27 ? 141  GLY C C   1 
ATOM   3266  O  O   . GLY C  1 141 ? 8.634   -44.572 9.204   1.00 19.15 ? 141  GLY C O   1 
ATOM   3267  N  N   . SER C  1 142 ? 8.631   -46.820 9.286   1.00 20.81 ? 142  SER C N   1 
ATOM   3268  C  CA  . SER C  1 142 ? 7.445   -46.977 8.459   1.00 19.48 ? 142  SER C CA  1 
ATOM   3269  C  C   . SER C  1 142 ? 6.180   -46.471 9.127   1.00 19.34 ? 142  SER C C   1 
ATOM   3270  O  O   . SER C  1 142 ? 6.149   -46.190 10.326  1.00 18.62 ? 142  SER C O   1 
ATOM   3271  C  CB  . SER C  1 142 ? 7.274   -48.435 8.009   1.00 18.86 ? 142  SER C CB  1 
ATOM   3272  O  OG  . SER C  1 142 ? 6.875   -49.257 9.085   1.00 20.81 ? 142  SER C OG  1 
ATOM   3273  N  N   . ARG C  1 143 ? 5.135   -46.361 8.322   1.00 21.52 ? 143  ARG C N   1 
ATOM   3274  C  CA  . ARG C  1 143 ? 3.855   -45.864 8.787   1.00 20.63 ? 143  ARG C CA  1 
ATOM   3275  C  C   . ARG C  1 143 ? 3.009   -47.058 9.215   1.00 20.26 ? 143  ARG C C   1 
ATOM   3276  O  O   . ARG C  1 143 ? 2.681   -47.913 8.389   1.00 20.22 ? 143  ARG C O   1 
ATOM   3277  C  CB  . ARG C  1 143 ? 3.213   -45.021 7.683   1.00 17.80 ? 143  ARG C CB  1 
ATOM   3278  C  CG  . ARG C  1 143 ? 4.208   -43.991 7.172   1.00 19.02 ? 143  ARG C CG  1 
ATOM   3279  C  CD  . ARG C  1 143 ? 3.646   -43.001 6.196   1.00 18.66 ? 143  ARG C CD  1 
ATOM   3280  N  NE  . ARG C  1 143 ? 4.670   -42.018 5.844   1.00 21.48 ? 143  ARG C NE  1 
ATOM   3281  C  CZ  . ARG C  1 143 ? 4.466   -40.969 5.049   1.00 22.00 ? 143  ARG C CZ  1 
ATOM   3282  N  NH1 . ARG C  1 143 ? 3.276   -40.758 4.506   1.00 21.28 ? 143  ARG C NH1 1 
ATOM   3283  N  NH2 . ARG C  1 143 ? 5.453   -40.129 4.790   1.00 22.11 ? 143  ARG C NH2 1 
ATOM   3284  N  N   . LEU C  1 144 ? 2.706   -47.138 10.514  1.00 17.13 ? 144  LEU C N   1 
ATOM   3285  C  CA  . LEU C  1 144 ? 2.009   -48.301 11.062  1.00 17.52 ? 144  LEU C CA  1 
ATOM   3286  C  C   . LEU C  1 144 ? 0.495   -48.148 11.048  1.00 15.47 ? 144  LEU C C   1 
ATOM   3287  O  O   . LEU C  1 144 ? -0.237  -49.118 10.914  1.00 15.03 ? 144  LEU C O   1 
ATOM   3288  C  CB  . LEU C  1 144 ? 2.454   -48.567 12.502  1.00 17.73 ? 144  LEU C CB  1 
ATOM   3289  C  CG  . LEU C  1 144 ? 3.891   -48.940 12.841  1.00 16.48 ? 144  LEU C CG  1 
ATOM   3290  C  CD1 . LEU C  1 144 ? 3.902   -49.177 14.327  1.00 15.60 ? 144  LEU C CD1 1 
ATOM   3291  C  CD2 . LEU C  1 144 ? 4.350   -50.167 12.076  1.00 13.87 ? 144  LEU C CD2 1 
ATOM   3292  N  N   . ALA C  1 145 ? 0.035   -46.922 11.226  1.00 15.36 ? 145  ALA C N   1 
ATOM   3293  C  CA  . ALA C  1 145 ? -1.386  -46.636 11.266  1.00 17.45 ? 145  ALA C CA  1 
ATOM   3294  C  C   . ALA C  1 145 ? -1.586  -45.124 11.155  1.00 17.15 ? 145  ALA C C   1 
ATOM   3295  O  O   . ALA C  1 145 ? -0.730  -44.340 11.575  1.00 15.36 ? 145  ALA C O   1 
ATOM   3296  C  CB  . ALA C  1 145 ? -2.002  -47.173 12.550  1.00 17.98 ? 145  ALA C CB  1 
ATOM   3297  N  N   . CYS C  1 146 ? -2.710  -44.723 10.569  1.00 17.13 ? 146  CYS C N   1 
ATOM   3298  C  CA  . CYS C  1 146 ? -2.962  -43.317 10.294  1.00 18.58 ? 146  CYS C CA  1 
ATOM   3299  C  C   . CYS C  1 146 ? -4.443  -43.098 10.178  1.00 17.32 ? 146  CYS C C   1 
ATOM   3300  O  O   . CYS C  1 146 ? -5.199  -44.039 9.997   1.00 18.87 ? 146  CYS C O   1 
ATOM   3301  C  CB  . CYS C  1 146 ? -2.269  -42.865 8.996   1.00 20.34 ? 146  CYS C CB  1 
ATOM   3302  S  SG  . CYS C  1 146 ? -2.806  -43.727 7.488   1.00 20.75 ? 146  CYS C SG  1 
ATOM   3303  N  N   . GLY C  1 147 ? -4.853  -41.847 10.284  1.00 16.82 ? 147  GLY C N   1 
ATOM   3304  C  CA  . GLY C  1 147 ? -6.246  -41.503 10.134  1.00 17.82 ? 147  GLY C CA  1 
ATOM   3305  C  C   . GLY C  1 147 ? -6.352  -40.026 9.832   1.00 19.82 ? 147  GLY C C   1 
ATOM   3306  O  O   . GLY C  1 147 ? -5.520  -39.223 10.302  1.00 17.65 ? 147  GLY C O   1 
ATOM   3307  N  N   . VAL C  1 148 ? -7.360  -39.670 9.035   1.00 18.21 ? 148  VAL C N   1 
ATOM   3308  C  CA  . VAL C  1 148 ? -7.644  -38.271 8.758   1.00 16.38 ? 148  VAL C CA  1 
ATOM   3309  C  C   . VAL C  1 148 ? -8.250  -37.602 9.984   1.00 17.16 ? 148  VAL C C   1 
ATOM   3310  O  O   . VAL C  1 148 ? -9.176  -38.129 10.620  1.00 17.29 ? 148  VAL C O   1 
ATOM   3311  C  CB  . VAL C  1 148 ? -8.586  -38.094 7.555   1.00 17.45 ? 148  VAL C CB  1 
ATOM   3312  C  CG1 . VAL C  1 148 ? -8.819  -36.612 7.275   1.00 16.12 ? 148  VAL C CG1 1 
ATOM   3313  C  CG2 . VAL C  1 148 ? -8.006  -38.762 6.334   1.00 17.06 ? 148  VAL C CG2 1 
ATOM   3314  N  N   . ILE C  1 149 ? -7.703  -36.437 10.315  1.00 18.06 ? 149  ILE C N   1 
ATOM   3315  C  CA  . ILE C  1 149 ? -8.175  -35.635 11.429  1.00 17.96 ? 149  ILE C CA  1 
ATOM   3316  C  C   . ILE C  1 149 ? -9.425  -34.860 11.029  1.00 18.67 ? 149  ILE C C   1 
ATOM   3317  O  O   . ILE C  1 149 ? -9.354  -33.914 10.244  1.00 20.23 ? 149  ILE C O   1 
ATOM   3318  C  CB  . ILE C  1 149 ? -7.089  -34.650 11.914  1.00 16.65 ? 149  ILE C CB  1 
ATOM   3319  C  CG1 . ILE C  1 149 ? -5.772  -35.390 12.146  1.00 16.22 ? 149  ILE C CG1 1 
ATOM   3320  C  CG2 . ILE C  1 149 ? -7.542  -33.933 13.194  1.00 17.69 ? 149  ILE C CG2 1 
ATOM   3321  C  CD1 . ILE C  1 149 ? -4.568  -34.521 12.009  1.00 17.58 ? 149  ILE C CD1 1 
ATOM   3322  N  N   . GLY C  1 150 ? -10.563 -35.249 11.593  1.00 17.90 ? 150  GLY C N   1 
ATOM   3323  C  CA  . GLY C  1 150 ? -11.808 -34.575 11.311  1.00 18.15 ? 150  GLY C CA  1 
ATOM   3324  C  C   . GLY C  1 150 ? -12.409 -33.863 12.501  1.00 20.05 ? 150  GLY C C   1 
ATOM   3325  O  O   . GLY C  1 150 ? -12.079 -34.142 13.653  1.00 20.86 ? 150  GLY C O   1 
ATOM   3326  N  N   . ILE C  1 151 ? -13.298 -32.925 12.194  1.00 22.72 ? 151  ILE C N   1 
ATOM   3327  C  CA  . ILE C  1 151 ? -14.080 -32.174 13.175  1.00 23.07 ? 151  ILE C CA  1 
ATOM   3328  C  C   . ILE C  1 151 ? -14.926 -33.097 14.051  1.00 21.26 ? 151  ILE C C   1 
ATOM   3329  O  O   . ILE C  1 151 ? -15.611 -33.987 13.543  1.00 22.68 ? 151  ILE C O   1 
ATOM   3330  C  CB  . ILE C  1 151 ? -15.006 -31.154 12.450  1.00 22.68 ? 151  ILE C CB  1 
ATOM   3331  C  CG1 . ILE C  1 151 ? -14.169 -30.167 11.626  1.00 20.21 ? 151  ILE C CG1 1 
ATOM   3332  C  CG2 . ILE C  1 151 ? -15.892 -30.441 13.443  1.00 22.12 ? 151  ILE C CG2 1 
ATOM   3333  C  CD1 . ILE C  1 151 ? -14.947 -29.371 10.598  1.00 19.22 ? 151  ILE C CD1 1 
ATOM   3334  N  N   . ALA C  1 152 ? -14.858 -32.895 15.365  1.00 20.92 ? 152  ALA C N   1 
ATOM   3335  C  CA  . ALA C  1 152 ? -15.594 -33.721 16.306  1.00 22.62 ? 152  ALA C CA  1 
ATOM   3336  C  C   . ALA C  1 152 ? -16.591 -32.877 17.103  1.00 25.53 ? 152  ALA C C   1 
ATOM   3337  O  O   . ALA C  1 152 ? -16.426 -31.655 17.235  1.00 25.87 ? 152  ALA C O   1 
ATOM   3338  C  CB  . ALA C  1 152 ? -14.642 -34.432 17.238  1.00 22.22 ? 152  ALA C CB  1 
ATOM   3339  N  N   . GLN C  1 153 ? -17.632 -33.518 17.625  1.00 24.34 ? 153  GLN C N   1 
ATOM   3340  C  CA  . GLN C  1 153 ? -18.575 -32.794 18.478  1.00 33.13 ? 153  GLN C CA  1 
ATOM   3341  C  C   . GLN C  1 153 ? -18.146 -32.735 19.944  1.00 34.92 ? 153  GLN C C   1 
ATOM   3342  O  O   . GLN C  1 153 ? -18.401 -31.731 20.619  1.00 37.24 ? 153  GLN C O   1 
ATOM   3343  C  CB  . GLN C  1 153 ? -20.005 -33.338 18.354  1.00 34.45 ? 153  GLN C CB  1 
ATOM   3344  C  CG  . GLN C  1 153 ? -20.267 -34.704 18.963  1.00 36.57 ? 153  GLN C CG  1 
ATOM   3345  C  CD  . GLN C  1 153 ? -21.760 -35.055 18.951  1.00 42.52 ? 153  GLN C CD  1 
ATOM   3346  O  OE1 . GLN C  1 153 ? -22.626 -34.182 19.123  1.00 35.37 ? 153  GLN C OE1 1 
ATOM   3347  N  NE2 . GLN C  1 153 ? -22.062 -36.339 18.744  1.00 45.15 ? 153  GLN C NE2 1 
ATOM   3348  O  OXT . GLN C  1 153 ? -17.537 -33.672 20.475  1.00 35.74 ? 153  GLN C OXT 1 
ATOM   3349  N  N   . ALA D  1 1   ? -7.585  -22.641 -4.885  1.00 44.88 ? 1    ALA D N   1 
ATOM   3350  C  CA  . ALA D  1 1   ? -7.099  -23.768 -5.681  1.00 43.32 ? 1    ALA D CA  1 
ATOM   3351  C  C   . ALA D  1 1   ? -7.150  -25.057 -4.867  1.00 39.11 ? 1    ALA D C   1 
ATOM   3352  O  O   . ALA D  1 1   ? -6.485  -26.040 -5.202  1.00 36.83 ? 1    ALA D O   1 
ATOM   3353  C  CB  . ALA D  1 1   ? -5.674  -23.502 -6.194  1.00 45.66 ? 1    ALA D CB  1 
ATOM   3354  N  N   . THR D  1 2   ? -7.956  -25.044 -3.808  1.00 36.95 ? 2    THR D N   1 
ATOM   3355  C  CA  . THR D  1 2   ? -7.999  -26.153 -2.869  1.00 32.61 ? 2    THR D CA  1 
ATOM   3356  C  C   . THR D  1 2   ? -8.452  -27.456 -3.555  1.00 28.46 ? 2    THR D C   1 
ATOM   3357  O  O   . THR D  1 2   ? -9.183  -27.447 -4.542  1.00 25.47 ? 2    THR D O   1 
ATOM   3358  C  CB  . THR D  1 2   ? -8.867  -25.818 -1.600  1.00 32.35 ? 2    THR D CB  1 
ATOM   3359  O  OG1 . THR D  1 2   ? -8.996  -24.401 -1.450  1.00 33.46 ? 2    THR D OG1 1 
ATOM   3360  C  CG2 . THR D  1 2   ? -8.235  -26.387 -0.324  1.00 33.78 ? 2    THR D CG2 1 
ATOM   3361  N  N   . LYS D  1 3   ? -7.953  -28.571 -3.038  1.00 26.89 ? 3    LYS D N   1 
ATOM   3362  C  CA  . LYS D  1 3   ? -8.368  -29.898 -3.454  1.00 23.05 ? 3    LYS D CA  1 
ATOM   3363  C  C   . LYS D  1 3   ? -8.579  -30.681 -2.169  1.00 22.69 ? 3    LYS D C   1 
ATOM   3364  O  O   . LYS D  1 3   ? -7.936  -30.397 -1.148  1.00 22.68 ? 3    LYS D O   1 
ATOM   3365  C  CB  . LYS D  1 3   ? -7.300  -30.563 -4.319  1.00 22.32 ? 3    LYS D CB  1 
ATOM   3366  C  CG  . LYS D  1 3   ? -7.102  -29.887 -5.664  1.00 30.63 ? 3    LYS D CG  1 
ATOM   3367  C  CD  . LYS D  1 3   ? -5.802  -30.296 -6.346  1.00 32.13 ? 3    LYS D CD  1 
ATOM   3368  C  CE  . LYS D  1 3   ? -5.784  -31.782 -6.733  1.00 37.81 ? 3    LYS D CE  1 
ATOM   3369  N  NZ  . LYS D  1 3   ? -6.694  -32.129 -7.876  1.00 41.54 ? 3    LYS D NZ  1 
ATOM   3370  N  N   . ALA D  1 4   ? -9.507  -31.631 -2.210  1.00 19.43 ? 4    ALA D N   1 
ATOM   3371  C  CA  . ALA D  1 4   ? -9.750  -32.520 -1.086  1.00 17.87 ? 4    ALA D CA  1 
ATOM   3372  C  C   . ALA D  1 4   ? -9.971  -33.911 -1.637  1.00 17.95 ? 4    ALA D C   1 
ATOM   3373  O  O   . ALA D  1 4   ? -10.138 -34.099 -2.841  1.00 18.21 ? 4    ALA D O   1 
ATOM   3374  C  CB  . ALA D  1 4   ? -10.954 -32.067 -0.284  1.00 17.95 ? 4    ALA D CB  1 
ATOM   3375  N  N   . VAL D  1 5   ? -9.936  -34.900 -0.763  1.00 17.69 ? 5    VAL D N   1 
ATOM   3376  C  CA  . VAL D  1 5   ? -10.156 -36.277 -1.180  1.00 17.55 ? 5    VAL D CA  1 
ATOM   3377  C  C   . VAL D  1 5   ? -10.804 -37.010 -0.018  1.00 18.09 ? 5    VAL D C   1 
ATOM   3378  O  O   . VAL D  1 5   ? -10.775 -36.556 1.122   1.00 17.32 ? 5    VAL D O   1 
ATOM   3379  C  CB  . VAL D  1 5   ? -8.843  -36.971 -1.675  1.00 16.83 ? 5    VAL D CB  1 
ATOM   3380  C  CG1 . VAL D  1 5   ? -7.811  -37.026 -0.577  1.00 18.43 ? 5    VAL D CG1 1 
ATOM   3381  C  CG2 . VAL D  1 5   ? -9.117  -38.359 -2.239  1.00 19.26 ? 5    VAL D CG2 1 
ATOM   3382  N  N   . CYS D  1 6   ? -11.421 -38.134 -0.321  1.00 20.50 ? 6    CYS D N   1 
ATOM   3383  C  CA  . CYS D  1 6   ? -12.162 -38.880 0.668   1.00 21.10 ? 6    CYS D CA  1 
ATOM   3384  C  C   . CYS D  1 6   ? -12.174 -40.320 0.183   1.00 21.20 ? 6    CYS D C   1 
ATOM   3385  O  O   . CYS D  1 6   ? -12.508 -40.577 -0.972  1.00 20.88 ? 6    CYS D O   1 
ATOM   3386  C  CB  . CYS D  1 6   ? -13.593 -38.341 0.732   1.00 20.86 ? 6    CYS D CB  1 
ATOM   3387  S  SG  . CYS D  1 6   ? -14.614 -39.054 1.999   1.00 23.25 ? 6    CYS D SG  1 
ATOM   3388  N  N   . VAL D  1 7   ? -11.789 -41.245 1.055   1.00 19.59 ? 7    VAL D N   1 
ATOM   3389  C  CA  . VAL D  1 7   ? -11.891 -42.667 0.764   1.00 19.01 ? 7    VAL D CA  1 
ATOM   3390  C  C   . VAL D  1 7   ? -13.046 -43.263 1.583   1.00 19.63 ? 7    VAL D C   1 
ATOM   3391  O  O   . VAL D  1 7   ? -13.028 -43.246 2.808   1.00 18.79 ? 7    VAL D O   1 
ATOM   3392  C  CB  . VAL D  1 7   ? -10.563 -43.379 1.062   1.00 17.94 ? 7    VAL D CB  1 
ATOM   3393  C  CG1 . VAL D  1 7   ? -10.718 -44.878 0.967   1.00 19.26 ? 7    VAL D CG1 1 
ATOM   3394  C  CG2 . VAL D  1 7   ? -9.502  -42.893 0.110   1.00 19.17 ? 7    VAL D CG2 1 
ATOM   3395  N  N   . LEU D  1 8   ? -14.070 -43.756 0.894   1.00 21.51 ? 8    LEU D N   1 
ATOM   3396  C  CA  . LEU D  1 8   ? -15.234 -44.338 1.556   1.00 21.13 ? 8    LEU D CA  1 
ATOM   3397  C  C   . LEU D  1 8   ? -15.007 -45.815 1.868   1.00 21.67 ? 8    LEU D C   1 
ATOM   3398  O  O   . LEU D  1 8   ? -14.709 -46.601 0.971   1.00 23.43 ? 8    LEU D O   1 
ATOM   3399  C  CB  . LEU D  1 8   ? -16.493 -44.173 0.692   1.00 20.40 ? 8    LEU D CB  1 
ATOM   3400  C  CG  . LEU D  1 8   ? -16.880 -42.804 0.113   1.00 21.62 ? 8    LEU D CG  1 
ATOM   3401  C  CD1 . LEU D  1 8   ? -18.153 -42.937 -0.719  1.00 23.79 ? 8    LEU D CD1 1 
ATOM   3402  C  CD2 . LEU D  1 8   ? -17.072 -41.758 1.186   1.00 18.02 ? 8    LEU D CD2 1 
ATOM   3403  N  N   . LYS D  1 9   ? -15.126 -46.167 3.149   1.00 24.87 ? 9    LYS D N   1 
ATOM   3404  C  CA  . LYS D  1 9   ? -15.001 -47.544 3.625   1.00 25.10 ? 9    LYS D CA  1 
ATOM   3405  C  C   . LYS D  1 9   ? -16.162 -47.858 4.563   1.00 24.62 ? 9    LYS D C   1 
ATOM   3406  O  O   . LYS D  1 9   ? -16.721 -46.970 5.205   1.00 20.81 ? 9    LYS D O   1 
ATOM   3407  C  CB  . LYS D  1 9   ? -13.693 -47.757 4.386   1.00 23.49 ? 9    LYS D CB  1 
ATOM   3408  C  CG  . LYS D  1 9   ? -12.418 -47.666 3.564   1.00 27.69 ? 9    LYS D CG  1 
ATOM   3409  C  CD  . LYS D  1 9   ? -11.195 -47.625 4.494   1.00 28.11 ? 9    LYS D CD  1 
ATOM   3410  C  CE  . LYS D  1 9   ? -9.942  -47.057 3.821   1.00 32.69 ? 9    LYS D CE  1 
ATOM   3411  N  NZ  . LYS D  1 9   ? -9.195  -48.071 3.008   1.00 32.46 ? 9    LYS D NZ  1 
ATOM   3412  N  N   . GLY D  1 10  ? -16.517 -49.131 4.648   1.00 23.19 ? 10   GLY D N   1 
ATOM   3413  C  CA  . GLY D  1 10  ? -17.612 -49.536 5.496   1.00 25.72 ? 10   GLY D CA  1 
ATOM   3414  C  C   . GLY D  1 10  ? -17.413 -50.968 5.919   1.00 29.21 ? 10   GLY D C   1 
ATOM   3415  O  O   . GLY D  1 10  ? -16.299 -51.483 5.850   1.00 28.87 ? 10   GLY D O   1 
ATOM   3416  N  N   . ASP D  1 11  ? -18.493 -51.615 6.345   1.00 33.14 ? 11   ASP D N   1 
ATOM   3417  C  CA  . ASP D  1 11  ? -18.415 -52.985 6.844   1.00 33.35 ? 11   ASP D CA  1 
ATOM   3418  C  C   . ASP D  1 11  ? -18.794 -53.995 5.766   1.00 32.70 ? 11   ASP D C   1 
ATOM   3419  O  O   . ASP D  1 11  ? -18.684 -55.195 5.971   1.00 38.08 ? 11   ASP D O   1 
ATOM   3420  C  CB  . ASP D  1 11  ? -19.275 -53.159 8.104   1.00 34.59 ? 11   ASP D CB  1 
ATOM   3421  C  CG  . ASP D  1 11  ? -18.835 -52.242 9.247   1.00 36.96 ? 11   ASP D CG  1 
ATOM   3422  O  OD1 . ASP D  1 11  ? -17.641 -52.263 9.619   1.00 33.69 ? 11   ASP D OD1 1 
ATOM   3423  O  OD2 . ASP D  1 11  ? -19.685 -51.491 9.773   1.00 40.41 ? 11   ASP D OD2 1 
ATOM   3424  N  N   . GLY D  1 12  ? -19.218 -53.497 4.609   1.00 29.89 ? 12   GLY D N   1 
ATOM   3425  C  CA  . GLY D  1 12  ? -19.535 -54.344 3.472   1.00 28.24 ? 12   GLY D CA  1 
ATOM   3426  C  C   . GLY D  1 12  ? -18.581 -54.087 2.322   1.00 30.55 ? 12   GLY D C   1 
ATOM   3427  O  O   . GLY D  1 12  ? -17.469 -53.614 2.549   1.00 30.87 ? 12   GLY D O   1 
ATOM   3428  N  N   . PRO D  1 13  ? -19.014 -54.366 1.077   1.00 29.37 ? 13   PRO D N   1 
ATOM   3429  C  CA  . PRO D  1 13  ? -18.125 -54.283 -0.082  1.00 28.91 ? 13   PRO D CA  1 
ATOM   3430  C  C   . PRO D  1 13  ? -18.106 -52.899 -0.749  1.00 25.57 ? 13   PRO D C   1 
ATOM   3431  O  O   . PRO D  1 13  ? -17.430 -52.729 -1.759  1.00 25.30 ? 13   PRO D O   1 
ATOM   3432  C  CB  . PRO D  1 13  ? -18.740 -55.291 -1.053  1.00 26.64 ? 13   PRO D CB  1 
ATOM   3433  C  CG  . PRO D  1 13  ? -20.156 -55.508 -0.571  1.00 29.67 ? 13   PRO D CG  1 
ATOM   3434  C  CD  . PRO D  1 13  ? -20.383 -54.691 0.660   1.00 28.13 ? 13   PRO D CD  1 
ATOM   3435  N  N   . VAL D  1 14  ? -18.844 -51.936 -0.212  1.00 25.59 ? 14   VAL D N   1 
ATOM   3436  C  CA  . VAL D  1 14  ? -18.906 -50.615 -0.827  1.00 24.31 ? 14   VAL D CA  1 
ATOM   3437  C  C   . VAL D  1 14  ? -17.685 -49.787 -0.441  1.00 27.34 ? 14   VAL D C   1 
ATOM   3438  O  O   . VAL D  1 14  ? -17.353 -49.648 0.749   1.00 22.98 ? 14   VAL D O   1 
ATOM   3439  C  CB  . VAL D  1 14  ? -20.211 -49.863 -0.472  1.00 24.31 ? 14   VAL D CB  1 
ATOM   3440  C  CG1 . VAL D  1 14  ? -20.203 -48.475 -1.085  1.00 22.21 ? 14   VAL D CG1 1 
ATOM   3441  C  CG2 . VAL D  1 14  ? -21.432 -50.659 -0.936  1.00 23.14 ? 14   VAL D CG2 1 
ATOM   3442  N  N   . GLN D  1 15  ? -17.017 -49.254 -1.464  1.00 25.71 ? 15   GLN D N   1 
ATOM   3443  C  CA  . GLN D  1 15  ? -15.799 -48.482 -1.288  1.00 26.09 ? 15   GLN D CA  1 
ATOM   3444  C  C   . GLN D  1 15  ? -15.594 -47.604 -2.503  1.00 23.89 ? 15   GLN D C   1 
ATOM   3445  O  O   . GLN D  1 15  ? -16.076 -47.911 -3.592  1.00 25.49 ? 15   GLN D O   1 
ATOM   3446  C  CB  . GLN D  1 15  ? -14.593 -49.406 -1.101  1.00 27.86 ? 15   GLN D CB  1 
ATOM   3447  C  CG  . GLN D  1 15  ? -14.150 -50.109 -2.369  1.00 31.03 ? 15   GLN D CG  1 
ATOM   3448  C  CD  . GLN D  1 15  ? -13.493 -51.446 -2.091  1.00 40.05 ? 15   GLN D CD  1 
ATOM   3449  O  OE1 . GLN D  1 15  ? -13.647 -52.398 -2.863  1.00 42.18 ? 15   GLN D OE1 1 
ATOM   3450  N  NE2 . GLN D  1 15  ? -12.771 -51.534 -0.973  1.00 42.31 ? 15   GLN D NE2 1 
ATOM   3451  N  N   . GLY D  1 16  ? -14.884 -46.501 -2.321  1.00 22.69 ? 16   GLY D N   1 
ATOM   3452  C  CA  . GLY D  1 16  ? -14.628 -45.612 -3.433  1.00 22.85 ? 16   GLY D CA  1 
ATOM   3453  C  C   . GLY D  1 16  ? -13.791 -44.427 -3.032  1.00 20.51 ? 16   GLY D C   1 
ATOM   3454  O  O   . GLY D  1 16  ? -13.515 -44.219 -1.848  1.00 20.64 ? 16   GLY D O   1 
ATOM   3455  N  N   . ILE D  1 17  ? -13.389 -43.651 -4.032  1.00 21.23 ? 17   ILE D N   1 
ATOM   3456  C  CA  . ILE D  1 17  ? -12.562 -42.477 -3.824  1.00 19.33 ? 17   ILE D CA  1 
ATOM   3457  C  C   . ILE D  1 17  ? -13.258 -41.284 -4.446  1.00 20.75 ? 17   ILE D C   1 
ATOM   3458  O  O   . ILE D  1 17  ? -13.635 -41.314 -5.621  1.00 20.84 ? 17   ILE D O   1 
ATOM   3459  C  CB  . ILE D  1 17  ? -11.169 -42.659 -4.460  1.00 21.82 ? 17   ILE D CB  1 
ATOM   3460  C  CG1 . ILE D  1 17  ? -10.428 -43.824 -3.811  1.00 19.89 ? 17   ILE D CG1 1 
ATOM   3461  C  CG2 . ILE D  1 17  ? -10.332 -41.388 -4.329  1.00 21.54 ? 17   ILE D CG2 1 
ATOM   3462  C  CD1 . ILE D  1 17  ? -8.998  -43.926 -4.269  1.00 23.48 ? 17   ILE D CD1 1 
ATOM   3463  N  N   . ILE D  1 18  ? -13.457 -40.241 -3.652  1.00 19.21 ? 18   ILE D N   1 
ATOM   3464  C  CA  . ILE D  1 18  ? -14.128 -39.049 -4.139  1.00 19.36 ? 18   ILE D CA  1 
ATOM   3465  C  C   . ILE D  1 18  ? -13.155 -37.884 -4.041  1.00 18.75 ? 18   ILE D C   1 
ATOM   3466  O  O   . ILE D  1 18  ? -12.510 -37.689 -3.019  1.00 20.07 ? 18   ILE D O   1 
ATOM   3467  C  CB  . ILE D  1 18  ? -15.476 -38.768 -3.384  1.00 19.17 ? 18   ILE D CB  1 
ATOM   3468  C  CG1 . ILE D  1 18  ? -16.445 -39.949 -3.537  1.00 19.53 ? 18   ILE D CG1 1 
ATOM   3469  C  CG2 . ILE D  1 18  ? -16.175 -37.510 -3.922  1.00 16.51 ? 18   ILE D CG2 1 
ATOM   3470  C  CD1 . ILE D  1 18  ? -17.219 -39.959 -4.836  1.00 15.54 ? 18   ILE D CD1 1 
ATOM   3471  N  N   . ASN D  1 19  ? -13.036 -37.136 -5.130  1.00 17.88 ? 19   ASN D N   1 
ATOM   3472  C  CA  . ASN D  1 19  ? -12.150 -35.992 -5.205  1.00 18.57 ? 19   ASN D CA  1 
ATOM   3473  C  C   . ASN D  1 19  ? -12.995 -34.733 -5.161  1.00 18.22 ? 19   ASN D C   1 
ATOM   3474  O  O   . ASN D  1 19  ? -14.131 -34.741 -5.602  1.00 20.12 ? 19   ASN D O   1 
ATOM   3475  C  CB  . ASN D  1 19  ? -11.324 -36.053 -6.496  1.00 20.02 ? 19   ASN D CB  1 
ATOM   3476  C  CG  . ASN D  1 19  ? -10.600 -37.386 -6.664  1.00 20.88 ? 19   ASN D CG  1 
ATOM   3477  O  OD1 . ASN D  1 19  ? -9.554  -37.615 -6.058  1.00 24.08 ? 19   ASN D OD1 1 
ATOM   3478  N  ND2 . ASN D  1 19  ? -11.155 -38.268 -7.489  1.00 19.96 ? 19   ASN D ND2 1 
ATOM   3479  N  N   . PHE D  1 20  ? -12.455 -33.664 -4.595  1.00 19.52 ? 20   PHE D N   1 
ATOM   3480  C  CA  . PHE D  1 20  ? -13.134 -32.375 -4.544  1.00 19.22 ? 20   PHE D CA  1 
ATOM   3481  C  C   . PHE D  1 20  ? -12.163 -31.330 -5.041  1.00 23.02 ? 20   PHE D C   1 
ATOM   3482  O  O   . PHE D  1 20  ? -10.962 -31.420 -4.785  1.00 24.10 ? 20   PHE D O   1 
ATOM   3483  C  CB  . PHE D  1 20  ? -13.549 -31.996 -3.119  1.00 20.32 ? 20   PHE D CB  1 
ATOM   3484  C  CG  . PHE D  1 20  ? -14.372 -33.041 -2.415  1.00 20.31 ? 20   PHE D CG  1 
ATOM   3485  C  CD1 . PHE D  1 20  ? -13.777 -34.183 -1.898  1.00 19.43 ? 20   PHE D CD1 1 
ATOM   3486  C  CD2 . PHE D  1 20  ? -15.736 -32.871 -2.254  1.00 22.83 ? 20   PHE D CD2 1 
ATOM   3487  C  CE1 . PHE D  1 20  ? -14.525 -35.151 -1.251  1.00 19.35 ? 20   PHE D CE1 1 
ATOM   3488  C  CE2 . PHE D  1 20  ? -16.493 -33.832 -1.607  1.00 25.28 ? 20   PHE D CE2 1 
ATOM   3489  C  CZ  . PHE D  1 20  ? -15.879 -34.979 -1.103  1.00 23.25 ? 20   PHE D CZ  1 
ATOM   3490  N  N   . GLU D  1 21  ? -12.678 -30.336 -5.749  1.00 23.76 ? 21   GLU D N   1 
ATOM   3491  C  CA  . GLU D  1 21  ? -11.843 -29.253 -6.210  1.00 23.06 ? 21   GLU D CA  1 
ATOM   3492  C  C   . GLU D  1 21  ? -12.587 -27.938 -6.214  1.00 25.42 ? 21   GLU D C   1 
ATOM   3493  O  O   . GLU D  1 21  ? -13.628 -27.808 -6.846  1.00 27.88 ? 21   GLU D O   1 
ATOM   3494  C  CB  . GLU D  1 21  ? -11.321 -29.541 -7.611  1.00 27.96 ? 21   GLU D CB  1 
ATOM   3495  C  CG  . GLU D  1 21  ? -10.499 -28.398 -8.158  1.00 32.04 ? 21   GLU D CG  1 
ATOM   3496  C  CD  . GLU D  1 21  ? -9.470  -28.850 -9.164  1.00 39.84 ? 21   GLU D CD  1 
ATOM   3497  O  OE1 . GLU D  1 21  ? -9.342  -30.078 -9.391  1.00 39.87 ? 21   GLU D OE1 1 
ATOM   3498  O  OE2 . GLU D  1 21  ? -8.784  -27.968 -9.720  1.00 45.10 ? 21   GLU D OE2 1 
ATOM   3499  N  N   . GLN D  1 22  ? -12.044 -26.960 -5.504  1.00 26.65 ? 22   GLN D N   1 
ATOM   3500  C  CA  . GLN D  1 22  ? -12.588 -25.622 -5.523  1.00 25.38 ? 22   GLN D CA  1 
ATOM   3501  C  C   . GLN D  1 22  ? -11.502 -24.640 -5.905  1.00 32.12 ? 22   GLN D C   1 
ATOM   3502  O  O   . GLN D  1 22  ? -10.704 -24.219 -5.063  1.00 31.65 ? 22   GLN D O   1 
ATOM   3503  C  CB  . GLN D  1 22  ? -13.140 -25.265 -4.165  1.00 27.49 ? 22   GLN D CB  1 
ATOM   3504  C  CG  . GLN D  1 22  ? -13.942 -24.004 -4.173  1.00 28.63 ? 22   GLN D CG  1 
ATOM   3505  C  CD  . GLN D  1 22  ? -14.517 -23.712 -2.824  1.00 26.76 ? 22   GLN D CD  1 
ATOM   3506  O  OE1 . GLN D  1 22  ? -13.904 -24.016 -1.810  1.00 30.12 ? 22   GLN D OE1 1 
ATOM   3507  N  NE2 . GLN D  1 22  ? -15.700 -23.129 -2.795  1.00 28.78 ? 22   GLN D NE2 1 
ATOM   3508  N  N   . LYS D  1 23  ? -11.493 -24.281 -7.190  1.00 38.16 ? 23   LYS D N   1 
ATOM   3509  C  CA  . LYS D  1 23  ? -10.477 -23.412 -7.783  1.00 38.10 ? 23   LYS D CA  1 
ATOM   3510  C  C   . LYS D  1 23  ? -10.612 -21.940 -7.389  1.00 39.68 ? 23   LYS D C   1 
ATOM   3511  O  O   . LYS D  1 23  ? -9.714  -21.157 -7.656  1.00 44.85 ? 23   LYS D O   1 
ATOM   3512  C  CB  . LYS D  1 23  ? -10.482 -23.545 -9.310  1.00 40.57 ? 23   LYS D CB  1 
ATOM   3513  C  CG  . LYS D  1 23  ? -10.556 -24.989 -9.812  1.00 43.45 ? 23   LYS D CG  1 
ATOM   3514  C  CD  . LYS D  1 23  ? -10.013 -25.137 -11.239 1.00 46.26 ? 23   LYS D CD  1 
ATOM   3515  C  CE  . LYS D  1 23  ? -11.050 -24.790 -12.306 1.00 48.19 ? 23   LYS D CE  1 
ATOM   3516  N  NZ  . LYS D  1 23  ? -11.423 -23.350 -12.273 1.00 50.17 ? 23   LYS D NZ  1 
ATOM   3517  N  N   . GLU D  1 24  ? -11.728 -21.565 -6.764  1.00 39.45 ? 24   GLU D N   1 
ATOM   3518  C  CA  . GLU D  1 24  ? -11.915 -20.198 -6.263  1.00 38.96 ? 24   GLU D CA  1 
ATOM   3519  C  C   . GLU D  1 24  ? -12.613 -20.223 -4.910  1.00 37.33 ? 24   GLU D C   1 
ATOM   3520  O  O   . GLU D  1 24  ? -13.491 -21.046 -4.681  1.00 35.54 ? 24   GLU D O   1 
ATOM   3521  C  CB  . GLU D  1 24  ? -12.750 -19.348 -7.232  1.00 43.46 ? 24   GLU D CB  1 
ATOM   3522  C  CG  . GLU D  1 24  ? -12.374 -19.458 -8.707  1.00 46.95 ? 24   GLU D CG  1 
ATOM   3523  C  CD  . GLU D  1 24  ? -11.009 -18.862 -9.032  1.00 49.58 ? 24   GLU D CD  1 
ATOM   3524  O  OE1 . GLU D  1 24  ? -10.516 -19.113 -10.154 1.00 47.88 ? 24   GLU D OE1 1 
ATOM   3525  O  OE2 . GLU D  1 24  ? -10.432 -18.146 -8.177  1.00 50.20 ? 24   GLU D OE2 1 
ATOM   3526  N  N   . SER D  1 25  ? -12.237 -19.304 -4.028  1.00 39.67 ? 25   SER D N   1 
ATOM   3527  C  CA  . SER D  1 25  ? -12.773 -19.262 -2.664  1.00 41.62 ? 25   SER D CA  1 
ATOM   3528  C  C   . SER D  1 25  ? -14.312 -19.317 -2.570  1.00 43.35 ? 25   SER D C   1 
ATOM   3529  O  O   . SER D  1 25  ? -14.863 -19.983 -1.682  1.00 42.27 ? 25   SER D O   1 
ATOM   3530  C  CB  . SER D  1 25  ? -12.222 -18.036 -1.917  1.00 41.50 ? 25   SER D CB  1 
ATOM   3531  O  OG  . SER D  1 25  ? -13.034 -17.702 -0.800  1.00 46.58 ? 25   SER D OG  1 
ATOM   3532  N  N   . ASN D  1 26  ? -14.998 -18.617 -3.473  1.00 41.95 ? 26   ASN D N   1 
ATOM   3533  C  CA  . ASN D  1 26  ? -16.464 -18.558 -3.457  1.00 41.67 ? 26   ASN D CA  1 
ATOM   3534  C  C   . ASN D  1 26  ? -17.068 -19.195 -4.702  1.00 38.23 ? 26   ASN D C   1 
ATOM   3535  O  O   . ASN D  1 26  ? -18.223 -18.939 -5.050  1.00 36.01 ? 26   ASN D O   1 
ATOM   3536  C  CB  . ASN D  1 26  ? -16.954 -17.109 -3.357  1.00 42.57 ? 26   ASN D CB  1 
ATOM   3537  C  CG  . ASN D  1 26  ? -16.537 -16.435 -2.068  1.00 44.07 ? 26   ASN D CG  1 
ATOM   3538  O  OD1 . ASN D  1 26  ? -16.546 -17.046 -0.998  1.00 46.94 ? 26   ASN D OD1 1 
ATOM   3539  N  ND2 . ASN D  1 26  ? -16.173 -15.159 -2.163  1.00 47.83 ? 26   ASN D ND2 1 
ATOM   3540  N  N   . GLY D  1 27  ? -16.267 -19.999 -5.386  1.00 35.71 ? 27   GLY D N   1 
ATOM   3541  C  CA  . GLY D  1 27  ? -16.721 -20.698 -6.565  1.00 34.22 ? 27   GLY D CA  1 
ATOM   3542  C  C   . GLY D  1 27  ? -17.354 -22.019 -6.188  1.00 29.95 ? 27   GLY D C   1 
ATOM   3543  O  O   . GLY D  1 27  ? -17.383 -22.396 -5.022  1.00 27.48 ? 27   GLY D O   1 
ATOM   3544  N  N   . PRO D  1 28  ? -17.860 -22.738 -7.187  1.00 33.57 ? 28   PRO D N   1 
ATOM   3545  C  CA  . PRO D  1 28  ? -18.448 -24.054 -6.931  1.00 30.62 ? 28   PRO D CA  1 
ATOM   3546  C  C   . PRO D  1 28  ? -17.357 -25.073 -6.591  1.00 28.61 ? 28   PRO D C   1 
ATOM   3547  O  O   . PRO D  1 28  ? -16.164 -24.843 -6.856  1.00 27.04 ? 28   PRO D O   1 
ATOM   3548  C  CB  . PRO D  1 28  ? -19.096 -24.425 -8.278  1.00 34.51 ? 28   PRO D CB  1 
ATOM   3549  C  CG  . PRO D  1 28  ? -18.817 -23.262 -9.235  1.00 33.78 ? 28   PRO D CG  1 
ATOM   3550  C  CD  . PRO D  1 28  ? -17.730 -22.441 -8.626  1.00 33.42 ? 28   PRO D CD  1 
ATOM   3551  N  N   . VAL D  1 29  ? -17.773 -26.195 -6.019  1.00 24.38 ? 29   VAL D N   1 
ATOM   3552  C  CA  . VAL D  1 29  ? -16.868 -27.296 -5.768  1.00 22.61 ? 29   VAL D CA  1 
ATOM   3553  C  C   . VAL D  1 29  ? -17.225 -28.434 -6.720  1.00 23.05 ? 29   VAL D C   1 
ATOM   3554  O  O   . VAL D  1 29  ? -18.371 -28.853 -6.775  1.00 22.77 ? 29   VAL D O   1 
ATOM   3555  C  CB  . VAL D  1 29  ? -16.966 -27.765 -4.297  1.00 22.66 ? 29   VAL D CB  1 
ATOM   3556  C  CG1 . VAL D  1 29  ? -15.948 -28.886 -3.989  1.00 21.31 ? 29   VAL D CG1 1 
ATOM   3557  C  CG2 . VAL D  1 29  ? -16.771 -26.581 -3.353  1.00 21.77 ? 29   VAL D CG2 1 
ATOM   3558  N  N   . LYS D  1 30  ? -16.249 -28.923 -7.478  1.00 22.32 ? 30   LYS D N   1 
ATOM   3559  C  CA  . LYS D  1 30  ? -16.464 -30.090 -8.320  1.00 21.80 ? 30   LYS D CA  1 
ATOM   3560  C  C   . LYS D  1 30  ? -16.185 -31.365 -7.547  1.00 22.13 ? 30   LYS D C   1 
ATOM   3561  O  O   . LYS D  1 30  ? -15.125 -31.526 -6.963  1.00 26.23 ? 30   LYS D O   1 
ATOM   3562  C  CB  . LYS D  1 30  ? -15.595 -30.052 -9.579  1.00 25.15 ? 30   LYS D CB  1 
ATOM   3563  C  CG  . LYS D  1 30  ? -16.005 -31.122 -10.598 1.00 31.53 ? 30   LYS D CG  1 
ATOM   3564  C  CD  . LYS D  1 30  ? -14.938 -31.372 -11.666 1.00 38.81 ? 30   LYS D CD  1 
ATOM   3565  C  CE  . LYS D  1 30  ? -15.204 -32.695 -12.400 1.00 37.74 ? 30   LYS D CE  1 
ATOM   3566  N  NZ  . LYS D  1 30  ? -14.143 -33.032 -13.406 1.00 39.78 ? 30   LYS D NZ  1 
ATOM   3567  N  N   . VAL D  1 31  ? -17.141 -32.278 -7.549  1.00 23.16 ? 31   VAL D N   1 
ATOM   3568  C  CA  . VAL D  1 31  ? -17.034 -33.499 -6.762  1.00 23.08 ? 31   VAL D CA  1 
ATOM   3569  C  C   . VAL D  1 31  ? -17.054 -34.699 -7.689  1.00 19.25 ? 31   VAL D C   1 
ATOM   3570  O  O   . VAL D  1 31  ? -18.055 -34.947 -8.316  1.00 20.85 ? 31   VAL D O   1 
ATOM   3571  C  CB  . VAL D  1 31  ? -18.219 -33.612 -5.766  1.00 20.26 ? 31   VAL D CB  1 
ATOM   3572  C  CG1 . VAL D  1 31  ? -18.103 -34.877 -4.928  1.00 18.23 ? 31   VAL D CG1 1 
ATOM   3573  C  CG2 . VAL D  1 31  ? -18.290 -32.376 -4.888  1.00 19.27 ? 31   VAL D CG2 1 
ATOM   3574  N  N   . TRP D  1 32  ? -15.953 -35.437 -7.796  1.00 19.91 ? 32   TRP D N   1 
ATOM   3575  C  CA  . TRP D  1 32  ? -15.943 -36.592 -8.685  1.00 19.37 ? 32   TRP D CA  1 
ATOM   3576  C  C   . TRP D  1 32  ? -15.159 -37.771 -8.160  1.00 18.17 ? 32   TRP D C   1 
ATOM   3577  O  O   . TRP D  1 32  ? -14.272 -37.621 -7.337  1.00 22.09 ? 32   TRP D O   1 
ATOM   3578  C  CB  . TRP D  1 32  ? -15.422 -36.211 -10.078 1.00 25.23 ? 32   TRP D CB  1 
ATOM   3579  C  CG  . TRP D  1 32  ? -13.925 -36.123 -10.184 1.00 24.00 ? 32   TRP D CG  1 
ATOM   3580  C  CD1 . TRP D  1 32  ? -13.073 -37.055 -10.734 1.00 23.77 ? 32   TRP D CD1 1 
ATOM   3581  C  CD2 . TRP D  1 32  ? -13.104 -35.046 -9.731  1.00 23.11 ? 32   TRP D CD2 1 
ATOM   3582  N  NE1 . TRP D  1 32  ? -11.769 -36.616 -10.634 1.00 25.33 ? 32   TRP D NE1 1 
ATOM   3583  C  CE2 . TRP D  1 32  ? -11.762 -35.384 -10.033 1.00 22.10 ? 32   TRP D CE2 1 
ATOM   3584  C  CE3 . TRP D  1 32  ? -13.368 -33.829 -9.095  1.00 23.54 ? 32   TRP D CE3 1 
ATOM   3585  C  CZ2 . TRP D  1 32  ? -10.698 -34.547 -9.724  1.00 26.02 ? 32   TRP D CZ2 1 
ATOM   3586  C  CZ3 . TRP D  1 32  ? -12.308 -33.000 -8.783  1.00 24.02 ? 32   TRP D CZ3 1 
ATOM   3587  C  CH2 . TRP D  1 32  ? -10.988 -33.359 -9.100  1.00 27.09 ? 32   TRP D CH2 1 
ATOM   3588  N  N   . GLY D  1 33  ? -15.486 -38.946 -8.666  1.00 16.97 ? 33   GLY D N   1 
ATOM   3589  C  CA  . GLY D  1 33  ? -14.837 -40.167 -8.260  1.00 17.72 ? 33   GLY D CA  1 
ATOM   3590  C  C   . GLY D  1 33  ? -15.675 -41.345 -8.704  1.00 21.01 ? 33   GLY D C   1 
ATOM   3591  O  O   . GLY D  1 33  ? -16.447 -41.233 -9.637  1.00 24.03 ? 33   GLY D O   1 
ATOM   3592  N  N   . SER D  1 34  ? -15.509 -42.482 -8.049  1.00 21.14 ? 34   SER D N   1 
ATOM   3593  C  CA  . SER D  1 34  ? -16.391 -43.607 -8.259  1.00 21.81 ? 34   SER D CA  1 
ATOM   3594  C  C   . SER D  1 34  ? -16.598 -44.357 -6.943  1.00 24.36 ? 34   SER D C   1 
ATOM   3595  O  O   . SER D  1 34  ? -15.806 -44.245 -6.015  1.00 25.27 ? 34   SER D O   1 
ATOM   3596  C  CB  . SER D  1 34  ? -15.851 -44.534 -9.353  1.00 24.70 ? 34   SER D CB  1 
ATOM   3597  O  OG  . SER D  1 34  ? -14.705 -45.241 -8.924  1.00 31.10 ? 34   SER D OG  1 
ATOM   3598  N  N   . ILE D  1 35  ? -17.699 -45.085 -6.854  1.00 24.97 ? 35   ILE D N   1 
ATOM   3599  C  CA  . ILE D  1 35  ? -17.953 -45.943 -5.721  1.00 24.39 ? 35   ILE D CA  1 
ATOM   3600  C  C   . ILE D  1 35  ? -18.326 -47.286 -6.324  1.00 25.07 ? 35   ILE D C   1 
ATOM   3601  O  O   . ILE D  1 35  ? -19.064 -47.325 -7.305  1.00 23.68 ? 35   ILE D O   1 
ATOM   3602  C  CB  . ILE D  1 35  ? -19.116 -45.405 -4.879  1.00 23.22 ? 35   ILE D CB  1 
ATOM   3603  C  CG1 . ILE D  1 35  ? -18.846 -43.949 -4.474  1.00 22.92 ? 35   ILE D CG1 1 
ATOM   3604  C  CG2 . ILE D  1 35  ? -19.355 -46.288 -3.681  1.00 20.00 ? 35   ILE D CG2 1 
ATOM   3605  C  CD1 . ILE D  1 35  ? -20.047 -43.264 -3.855  1.00 19.94 ? 35   ILE D CD1 1 
ATOM   3606  N  N   . LYS D  1 36  ? -17.793 -48.371 -5.766  1.00 24.50 ? 36   LYS D N   1 
ATOM   3607  C  CA  . LYS D  1 36  ? -18.103 -49.712 -6.248  1.00 24.53 ? 36   LYS D CA  1 
ATOM   3608  C  C   . LYS D  1 36  ? -18.704 -50.559 -5.133  1.00 25.92 ? 36   LYS D C   1 
ATOM   3609  O  O   . LYS D  1 36  ? -18.630 -50.198 -3.953  1.00 23.86 ? 36   LYS D O   1 
ATOM   3610  C  CB  . LYS D  1 36  ? -16.857 -50.383 -6.842  1.00 27.76 ? 36   LYS D CB  1 
ATOM   3611  C  CG  . LYS D  1 36  ? -15.708 -50.562 -5.875  1.00 32.57 ? 36   LYS D CG  1 
ATOM   3612  C  CD  . LYS D  1 36  ? -14.552 -51.358 -6.485  1.00 36.65 ? 36   LYS D CD  1 
ATOM   3613  C  CE  . LYS D  1 36  ? -13.926 -50.628 -7.680  1.00 50.25 ? 36   LYS D CE  1 
ATOM   3614  N  NZ  . LYS D  1 36  ? -12.771 -51.375 -8.294  1.00 49.28 ? 36   LYS D NZ  1 
ATOM   3615  N  N   . GLY D  1 37  ? -19.325 -51.672 -5.513  1.00 27.42 ? 37   GLY D N   1 
ATOM   3616  C  CA  . GLY D  1 37  ? -19.955 -52.569 -4.559  1.00 23.04 ? 37   GLY D CA  1 
ATOM   3617  C  C   . GLY D  1 37  ? -21.360 -52.154 -4.177  1.00 24.14 ? 37   GLY D C   1 
ATOM   3618  O  O   . GLY D  1 37  ? -21.899 -52.633 -3.177  1.00 26.37 ? 37   GLY D O   1 
ATOM   3619  N  N   . LEU D  1 38  ? -21.946 -51.259 -4.972  1.00 24.70 ? 38   LEU D N   1 
ATOM   3620  C  CA  . LEU D  1 38  ? -23.283 -50.721 -4.728  1.00 23.07 ? 38   LEU D CA  1 
ATOM   3621  C  C   . LEU D  1 38  ? -24.379 -51.535 -5.436  1.00 26.04 ? 38   LEU D C   1 
ATOM   3622  O  O   . LEU D  1 38  ? -24.174 -52.041 -6.545  1.00 25.41 ? 38   LEU D O   1 
ATOM   3623  C  CB  . LEU D  1 38  ? -23.361 -49.268 -5.221  1.00 22.21 ? 38   LEU D CB  1 
ATOM   3624  C  CG  . LEU D  1 38  ? -22.631 -48.151 -4.471  1.00 22.91 ? 38   LEU D CG  1 
ATOM   3625  C  CD1 . LEU D  1 38  ? -22.819 -46.815 -5.199  1.00 18.46 ? 38   LEU D CD1 1 
ATOM   3626  C  CD2 . LEU D  1 38  ? -23.097 -48.063 -3.007  1.00 18.56 ? 38   LEU D CD2 1 
ATOM   3627  N  N   . THR D  1 39  ? -25.544 -51.653 -4.798  1.00 25.89 ? 39   THR D N   1 
ATOM   3628  C  CA  . THR D  1 39  ? -26.723 -52.184 -5.475  1.00 26.69 ? 39   THR D CA  1 
ATOM   3629  C  C   . THR D  1 39  ? -27.090 -51.214 -6.590  1.00 28.48 ? 39   THR D C   1 
ATOM   3630  O  O   . THR D  1 39  ? -26.861 -50.003 -6.466  1.00 29.25 ? 39   THR D O   1 
ATOM   3631  C  CB  . THR D  1 39  ? -27.928 -52.349 -4.522  1.00 23.45 ? 39   THR D CB  1 
ATOM   3632  O  OG1 . THR D  1 39  ? -28.052 -51.184 -3.702  1.00 25.77 ? 39   THR D OG1 1 
ATOM   3633  C  CG2 . THR D  1 39  ? -27.743 -53.559 -3.639  1.00 18.73 ? 39   THR D CG2 1 
ATOM   3634  N  N   . GLU D  1 40  ? -27.634 -51.739 -7.684  1.00 27.59 ? 40   GLU D N   1 
ATOM   3635  C  CA  . GLU D  1 40  ? -27.946 -50.900 -8.835  1.00 27.76 ? 40   GLU D CA  1 
ATOM   3636  C  C   . GLU D  1 40  ? -29.094 -49.968 -8.483  1.00 27.79 ? 40   GLU D C   1 
ATOM   3637  O  O   . GLU D  1 40  ? -30.046 -50.363 -7.808  1.00 28.43 ? 40   GLU D O   1 
ATOM   3638  C  CB  . GLU D  1 40  ? -28.291 -51.743 -10.070 1.00 27.59 ? 40   GLU D CB  1 
ATOM   3639  C  CG  . GLU D  1 40  ? -28.716 -50.927 -11.290 1.00 30.04 ? 40   GLU D CG  1 
ATOM   3640  C  CD  . GLU D  1 40  ? -29.361 -51.777 -12.381 1.00 35.35 ? 40   GLU D CD  1 
ATOM   3641  O  OE1 . GLU D  1 40  ? -29.606 -52.978 -12.131 1.00 35.88 ? 40   GLU D OE1 1 
ATOM   3642  O  OE2 . GLU D  1 40  ? -29.623 -51.243 -13.487 1.00 37.41 ? 40   GLU D OE2 1 
ATOM   3643  N  N   . GLY D  1 41  ? -28.989 -48.724 -8.936  1.00 28.21 ? 41   GLY D N   1 
ATOM   3644  C  CA  . GLY D  1 41  ? -30.020 -47.741 -8.693  1.00 24.65 ? 41   GLY D CA  1 
ATOM   3645  C  C   . GLY D  1 41  ? -29.468 -46.504 -8.023  1.00 22.60 ? 41   GLY D C   1 
ATOM   3646  O  O   . GLY D  1 41  ? -28.258 -46.329 -7.909  1.00 22.16 ? 41   GLY D O   1 
ATOM   3647  N  N   . LEU D  1 42  ? -30.376 -45.644 -7.579  1.00 24.71 ? 42   LEU D N   1 
ATOM   3648  C  CA  . LEU D  1 42  ? -30.015 -44.394 -6.931  1.00 23.54 ? 42   LEU D CA  1 
ATOM   3649  C  C   . LEU D  1 42  ? -29.683 -44.595 -5.456  1.00 20.40 ? 42   LEU D C   1 
ATOM   3650  O  O   . LEU D  1 42  ? -30.303 -45.418 -4.776  1.00 19.14 ? 42   LEU D O   1 
ATOM   3651  C  CB  . LEU D  1 42  ? -31.146 -43.365 -7.083  1.00 23.93 ? 42   LEU D CB  1 
ATOM   3652  C  CG  . LEU D  1 42  ? -31.484 -42.778 -8.459  1.00 21.66 ? 42   LEU D CG  1 
ATOM   3653  C  CD1 . LEU D  1 42  ? -32.128 -41.421 -8.263  1.00 26.09 ? 42   LEU D CD1 1 
ATOM   3654  C  CD2 . LEU D  1 42  ? -30.269 -42.632 -9.338  1.00 22.64 ? 42   LEU D CD2 1 
ATOM   3655  N  N   . HIS D  1 43  ? -28.708 -43.819 -4.977  1.00 19.86 ? 43   HIS D N   1 
ATOM   3656  C  CA  . HIS D  1 43  ? -28.174 -43.940 -3.626  1.00 16.41 ? 43   HIS D CA  1 
ATOM   3657  C  C   . HIS D  1 43  ? -27.909 -42.575 -3.024  1.00 17.04 ? 43   HIS D C   1 
ATOM   3658  O  O   . HIS D  1 43  ? -27.187 -41.784 -3.618  1.00 17.49 ? 43   HIS D O   1 
ATOM   3659  C  CB  . HIS D  1 43  ? -26.858 -44.712 -3.655  1.00 15.77 ? 43   HIS D CB  1 
ATOM   3660  C  CG  . HIS D  1 43  ? -27.024 -46.186 -3.834  1.00 17.19 ? 43   HIS D CG  1 
ATOM   3661  N  ND1 . HIS D  1 43  ? -27.370 -47.025 -2.798  1.00 19.11 ? 43   HIS D ND1 1 
ATOM   3662  C  CD2 . HIS D  1 43  ? -26.881 -46.976 -4.921  1.00 19.72 ? 43   HIS D CD2 1 
ATOM   3663  C  CE1 . HIS D  1 43  ? -27.444 -48.266 -3.241  1.00 18.13 ? 43   HIS D CE1 1 
ATOM   3664  N  NE2 . HIS D  1 43  ? -27.151 -48.264 -4.526  1.00 21.00 ? 43   HIS D NE2 1 
ATOM   3665  N  N   . GLY D  1 44  ? -28.457 -42.309 -1.835  1.00 16.88 ? 44   GLY D N   1 
ATOM   3666  C  CA  . GLY D  1 44  ? -28.193 -41.064 -1.132  1.00 16.20 ? 44   GLY D CA  1 
ATOM   3667  C  C   . GLY D  1 44  ? -26.710 -40.757 -0.919  1.00 17.64 ? 44   GLY D C   1 
ATOM   3668  O  O   . GLY D  1 44  ? -25.926 -41.634 -0.544  1.00 16.23 ? 44   GLY D O   1 
ATOM   3669  N  N   . PHE D  1 45  ? -26.331 -39.498 -1.145  1.00 16.34 ? 45   PHE D N   1 
ATOM   3670  C  CA  . PHE D  1 45  ? -24.931 -39.077 -1.130  1.00 14.99 ? 45   PHE D CA  1 
ATOM   3671  C  C   . PHE D  1 45  ? -24.852 -37.742 -0.413  1.00 15.39 ? 45   PHE D C   1 
ATOM   3672  O  O   . PHE D  1 45  ? -25.238 -36.718 -0.961  1.00 14.99 ? 45   PHE D O   1 
ATOM   3673  C  CB  . PHE D  1 45  ? -24.410 -38.969 -2.577  1.00 17.10 ? 45   PHE D CB  1 
ATOM   3674  C  CG  . PHE D  1 45  ? -22.904 -38.860 -2.705  1.00 18.10 ? 45   PHE D CG  1 
ATOM   3675  C  CD1 . PHE D  1 45  ? -22.074 -39.906 -2.339  1.00 17.32 ? 45   PHE D CD1 1 
ATOM   3676  C  CD2 . PHE D  1 45  ? -22.320 -37.709 -3.245  1.00 21.27 ? 45   PHE D CD2 1 
ATOM   3677  C  CE1 . PHE D  1 45  ? -20.677 -39.788 -2.480  1.00 18.56 ? 45   PHE D CE1 1 
ATOM   3678  C  CE2 . PHE D  1 45  ? -20.931 -37.590 -3.389  1.00 17.08 ? 45   PHE D CE2 1 
ATOM   3679  C  CZ  . PHE D  1 45  ? -20.114 -38.631 -3.014  1.00 16.34 ? 45   PHE D CZ  1 
ATOM   3680  N  N   . HIS D  1 46  ? -24.378 -37.762 0.831   1.00 16.80 ? 46   HIS D N   1 
ATOM   3681  C  CA  . HIS D  1 46  ? -24.410 -36.570 1.683   1.00 17.77 ? 46   HIS D CA  1 
ATOM   3682  C  C   . HIS D  1 46  ? -23.129 -36.344 2.493   1.00 19.16 ? 46   HIS D C   1 
ATOM   3683  O  O   . HIS D  1 46  ? -22.464 -37.290 2.924   1.00 16.69 ? 46   HIS D O   1 
ATOM   3684  C  CB  . HIS D  1 46  ? -25.568 -36.606 2.697   1.00 16.37 ? 46   HIS D CB  1 
ATOM   3685  C  CG  . HIS D  1 46  ? -26.863 -37.157 2.172   1.00 16.41 ? 46   HIS D CG  1 
ATOM   3686  N  ND1 . HIS D  1 46  ? -27.276 -38.449 2.424   1.00 16.00 ? 46   HIS D ND1 1 
ATOM   3687  C  CD2 . HIS D  1 46  ? -27.859 -36.576 1.464   1.00 17.67 ? 46   HIS D CD2 1 
ATOM   3688  C  CE1 . HIS D  1 46  ? -28.462 -38.646 1.874   1.00 17.03 ? 46   HIS D CE1 1 
ATOM   3689  N  NE2 . HIS D  1 46  ? -28.834 -37.528 1.277   1.00 16.84 ? 46   HIS D NE2 1 
ATOM   3690  N  N   . VAL D  1 47  ? -22.815 -35.069 2.713   1.00 17.14 ? 47   VAL D N   1 
ATOM   3691  C  CA  . VAL D  1 47  ? -21.825 -34.677 3.688   1.00 17.15 ? 47   VAL D CA  1 
ATOM   3692  C  C   . VAL D  1 47  ? -22.510 -34.658 5.056   1.00 18.66 ? 47   VAL D C   1 
ATOM   3693  O  O   . VAL D  1 47  ? -23.550 -34.026 5.235   1.00 19.76 ? 47   VAL D O   1 
ATOM   3694  C  CB  . VAL D  1 47  ? -21.202 -33.286 3.355   1.00 17.62 ? 47   VAL D CB  1 
ATOM   3695  C  CG1 . VAL D  1 47  ? -20.012 -33.002 4.237   1.00 15.53 ? 47   VAL D CG1 1 
ATOM   3696  C  CG2 . VAL D  1 47  ? -20.752 -33.240 1.921   1.00 17.38 ? 47   VAL D CG2 1 
ATOM   3697  N  N   . HIS D  1 48  ? -21.927 -35.368 6.016   1.00 21.25 ? 48   HIS D N   1 
ATOM   3698  C  CA  . HIS D  1 48  ? -22.393 -35.363 7.401   1.00 18.28 ? 48   HIS D CA  1 
ATOM   3699  C  C   . HIS D  1 48  ? -21.479 -34.501 8.249   1.00 17.80 ? 48   HIS D C   1 
ATOM   3700  O  O   . HIS D  1 48  ? -20.354 -34.202 7.859   1.00 17.71 ? 48   HIS D O   1 
ATOM   3701  C  CB  . HIS D  1 48  ? -22.478 -36.789 7.948   1.00 17.62 ? 48   HIS D CB  1 
ATOM   3702  C  CG  . HIS D  1 48  ? -23.536 -37.619 7.281   1.00 18.41 ? 48   HIS D CG  1 
ATOM   3703  N  ND1 . HIS D  1 48  ? -24.544 -38.248 7.981   1.00 17.58 ? 48   HIS D ND1 1 
ATOM   3704  C  CD2 . HIS D  1 48  ? -23.764 -37.884 5.974   1.00 15.79 ? 48   HIS D CD2 1 
ATOM   3705  C  CE1 . HIS D  1 48  ? -25.333 -38.885 7.133   1.00 17.78 ? 48   HIS D CE1 1 
ATOM   3706  N  NE2 . HIS D  1 48  ? -24.877 -38.686 5.910   1.00 15.69 ? 48   HIS D NE2 1 
ATOM   3707  N  N   . GLU D  1 49  ? -21.977 -34.113 9.414   1.00 19.04 ? 49   GLU D N   1 
ATOM   3708  C  CA  . GLU D  1 49  ? -21.381 -33.049 10.197  1.00 19.42 ? 49   GLU D CA  1 
ATOM   3709  C  C   . GLU D  1 49  ? -19.995 -33.336 10.767  1.00 19.71 ? 49   GLU D C   1 
ATOM   3710  O  O   . GLU D  1 49  ? -19.127 -32.460 10.752  1.00 17.38 ? 49   GLU D O   1 
ATOM   3711  C  CB  . GLU D  1 49  ? -22.309 -32.654 11.333  1.00 17.04 ? 49   GLU D CB  1 
ATOM   3712  C  CG  . GLU D  1 49  ? -21.842 -31.416 12.023  1.00 19.16 ? 49   GLU D CG  1 
ATOM   3713  C  CD  . GLU D  1 49  ? -22.821 -30.940 13.060  1.00 24.19 ? 49   GLU D CD  1 
ATOM   3714  O  OE1 . GLU D  1 49  ? -23.837 -31.645 13.279  1.00 24.39 ? 49   GLU D OE1 1 
ATOM   3715  O  OE2 . GLU D  1 49  ? -22.568 -29.866 13.655  1.00 26.89 ? 49   GLU D OE2 1 
ATOM   3716  N  N   . PHE D  1 50  ? -19.786 -34.544 11.286  1.00 20.65 ? 50   PHE D N   1 
ATOM   3717  C  CA  . PHE D  1 50  ? -18.542 -34.835 12.000  1.00 19.92 ? 50   PHE D CA  1 
ATOM   3718  C  C   . PHE D  1 50  ? -17.635 -35.820 11.284  1.00 19.33 ? 50   PHE D C   1 
ATOM   3719  O  O   . PHE D  1 50  ? -18.082 -36.884 10.855  1.00 18.50 ? 50   PHE D O   1 
ATOM   3720  C  CB  . PHE D  1 50  ? -18.828 -35.318 13.430  1.00 19.49 ? 50   PHE D CB  1 
ATOM   3721  C  CG  . PHE D  1 50  ? -19.700 -34.388 14.207  1.00 20.72 ? 50   PHE D CG  1 
ATOM   3722  C  CD1 . PHE D  1 50  ? -19.272 -33.101 14.491  1.00 22.04 ? 50   PHE D CD1 1 
ATOM   3723  C  CD2 . PHE D  1 50  ? -20.958 -34.791 14.643  1.00 21.83 ? 50   PHE D CD2 1 
ATOM   3724  C  CE1 . PHE D  1 50  ? -20.078 -32.231 15.207  1.00 24.24 ? 50   PHE D CE1 1 
ATOM   3725  C  CE2 . PHE D  1 50  ? -21.770 -33.932 15.348  1.00 24.04 ? 50   PHE D CE2 1 
ATOM   3726  C  CZ  . PHE D  1 50  ? -21.333 -32.647 15.634  1.00 24.70 ? 50   PHE D CZ  1 
ATOM   3727  N  N   . GLY D  1 51  ? -16.357 -35.454 11.166  1.00 20.50 ? 51   GLY D N   1 
ATOM   3728  C  CA  . GLY D  1 51  ? -15.333 -36.362 10.674  1.00 19.80 ? 51   GLY D CA  1 
ATOM   3729  C  C   . GLY D  1 51  ? -14.942 -37.341 11.772  1.00 20.88 ? 51   GLY D C   1 
ATOM   3730  O  O   . GLY D  1 51  ? -13.764 -37.519 12.085  1.00 17.78 ? 51   GLY D O   1 
ATOM   3731  N  N   . ASP D  1 52  ? -15.962 -37.976 12.346  1.00 21.81 ? 52   ASP D N   1 
ATOM   3732  C  CA  . ASP D  1 52  ? -15.825 -38.853 13.500  1.00 19.48 ? 52   ASP D CA  1 
ATOM   3733  C  C   . ASP D  1 52  ? -16.164 -40.307 13.114  1.00 21.97 ? 52   ASP D C   1 
ATOM   3734  O  O   . ASP D  1 52  ? -17.329 -40.628 12.835  1.00 19.79 ? 52   ASP D O   1 
ATOM   3735  C  CB  . ASP D  1 52  ? -16.754 -38.346 14.607  1.00 19.36 ? 52   ASP D CB  1 
ATOM   3736  C  CG  . ASP D  1 52  ? -16.526 -39.031 15.930  1.00 20.54 ? 52   ASP D CG  1 
ATOM   3737  O  OD1 . ASP D  1 52  ? -16.172 -40.231 15.922  1.00 18.83 ? 52   ASP D OD1 1 
ATOM   3738  O  OD2 . ASP D  1 52  ? -16.725 -38.369 16.977  1.00 20.14 ? 52   ASP D OD2 1 
ATOM   3739  N  N   . ASN D  1 53  ? -15.149 -41.178 13.088  1.00 20.67 ? 53   ASN D N   1 
ATOM   3740  C  CA  . ASN D  1 53  ? -15.344 -42.583 12.709  1.00 20.57 ? 53   ASN D CA  1 
ATOM   3741  C  C   . ASN D  1 53  ? -15.141 -43.584 13.849  1.00 21.70 ? 53   ASN D C   1 
ATOM   3742  O  O   . ASN D  1 53  ? -14.901 -44.772 13.613  1.00 23.33 ? 53   ASN D O   1 
ATOM   3743  C  CB  . ASN D  1 53  ? -14.444 -42.956 11.528  1.00 19.94 ? 53   ASN D CB  1 
ATOM   3744  C  CG  . ASN D  1 53  ? -14.831 -44.287 10.892  1.00 24.74 ? 53   ASN D CG  1 
ATOM   3745  O  OD1 . ASN D  1 53  ? -16.008 -44.650 10.839  1.00 27.08 ? 53   ASN D OD1 1 
ATOM   3746  N  ND2 . ASN D  1 53  ? -13.844 -45.016 10.403  1.00 28.10 ? 53   ASN D ND2 1 
ATOM   3747  N  N   . THR D  1 54  ? -15.252 -43.099 15.080  1.00 20.73 ? 54   THR D N   1 
ATOM   3748  C  CA  . THR D  1 54  ? -14.992 -43.894 16.273  1.00 22.68 ? 54   THR D CA  1 
ATOM   3749  C  C   . THR D  1 54  ? -16.037 -44.990 16.505  1.00 25.58 ? 54   THR D C   1 
ATOM   3750  O  O   . THR D  1 54  ? -15.769 -45.970 17.194  1.00 25.88 ? 54   THR D O   1 
ATOM   3751  C  CB  . THR D  1 54  ? -14.893 -42.982 17.518  1.00 22.86 ? 54   THR D CB  1 
ATOM   3752  O  OG1 . THR D  1 54  ? -16.073 -42.177 17.610  1.00 25.58 ? 54   THR D OG1 1 
ATOM   3753  C  CG2 . THR D  1 54  ? -13.685 -42.059 17.406  1.00 20.36 ? 54   THR D CG2 1 
ATOM   3754  N  N   . ALA D  1 55  ? -17.225 -44.816 15.921  1.00 27.47 ? 55   ALA D N   1 
ATOM   3755  C  CA  . ALA D  1 55  ? -18.276 -45.839 15.947  1.00 24.35 ? 55   ALA D CA  1 
ATOM   3756  C  C   . ALA D  1 55  ? -18.723 -46.188 14.535  1.00 25.30 ? 55   ALA D C   1 
ATOM   3757  O  O   . ALA D  1 55  ? -19.863 -46.587 14.326  1.00 30.24 ? 55   ALA D O   1 
ATOM   3758  C  CB  . ALA D  1 55  ? -19.477 -45.373 16.774  1.00 25.70 ? 55   ALA D CB  1 
ATOM   3759  N  N   . GLY D  1 56  ? -17.826 -46.041 13.567  1.00 24.26 ? 56   GLY D N   1 
ATOM   3760  C  CA  . GLY D  1 56  ? -18.186 -46.231 12.176  1.00 24.15 ? 56   GLY D CA  1 
ATOM   3761  C  C   . GLY D  1 56  ? -18.902 -44.999 11.644  1.00 26.50 ? 56   GLY D C   1 
ATOM   3762  O  O   . GLY D  1 56  ? -18.653 -43.881 12.110  1.00 24.93 ? 56   GLY D O   1 
ATOM   3763  N  N   . CYS D  1 57  ? -19.805 -45.203 10.686  1.00 25.56 ? 57   CYS D N   1 
ATOM   3764  C  CA  . CYS D  1 57  ? -20.465 -44.104 9.994   1.00 24.52 ? 57   CYS D CA  1 
ATOM   3765  C  C   . CYS D  1 57  ? -21.461 -43.388 10.889  1.00 22.19 ? 57   CYS D C   1 
ATOM   3766  O  O   . CYS D  1 57  ? -21.749 -42.199 10.693  1.00 19.78 ? 57   CYS D O   1 
ATOM   3767  C  CB  . CYS D  1 57  ? -21.169 -44.616 8.735   1.00 26.05 ? 57   CYS D CB  1 
ATOM   3768  S  SG  . CYS D  1 57  ? -20.091 -45.506 7.599   1.00 30.10 ? 57   CYS D SG  1 
ATOM   3769  N  N   . THR D  1 58  ? -21.979 -44.130 11.861  1.00 21.91 ? 58   THR D N   1 
ATOM   3770  C  CA  . THR D  1 58  ? -22.930 -43.623 12.844  1.00 22.18 ? 58   THR D CA  1 
ATOM   3771  C  C   . THR D  1 58  ? -22.482 -42.328 13.529  1.00 22.36 ? 58   THR D C   1 
ATOM   3772  O  O   . THR D  1 58  ? -23.271 -41.382 13.666  1.00 22.25 ? 58   THR D O   1 
ATOM   3773  C  CB  . THR D  1 58  ? -23.242 -44.716 13.904  1.00 26.50 ? 58   THR D CB  1 
ATOM   3774  O  OG1 . THR D  1 58  ? -23.979 -45.788 13.292  1.00 28.78 ? 58   THR D OG1 1 
ATOM   3775  C  CG2 . THR D  1 58  ? -24.052 -44.151 15.060  1.00 24.63 ? 58   THR D CG2 1 
ATOM   3776  N  N   . SER D  1 59  ? -21.223 -42.288 13.961  1.00 20.24 ? 59   SER D N   1 
ATOM   3777  C  CA  . SER D  1 59  ? -20.686 -41.136 14.690  1.00 18.31 ? 59   SER D CA  1 
ATOM   3778  C  C   . SER D  1 59  ? -20.492 -39.900 13.828  1.00 18.26 ? 59   SER D C   1 
ATOM   3779  O  O   . SER D  1 59  ? -20.098 -38.849 14.327  1.00 17.86 ? 59   SER D O   1 
ATOM   3780  C  CB  . SER D  1 59  ? -19.380 -41.494 15.401  1.00 21.06 ? 59   SER D CB  1 
ATOM   3781  O  OG  . SER D  1 59  ? -18.882 -42.745 14.965  1.00 21.99 ? 59   SER D OG  1 
ATOM   3782  N  N   . ALA D  1 60  ? -20.789 -40.039 12.536  1.00 21.32 ? 60   ALA D N   1 
ATOM   3783  C  CA  . ALA D  1 60  ? -20.692 -38.952 11.572  1.00 17.70 ? 60   ALA D CA  1 
ATOM   3784  C  C   . ALA D  1 60  ? -21.795 -37.922 11.788  1.00 18.40 ? 60   ALA D C   1 
ATOM   3785  O  O   . ALA D  1 60  ? -21.716 -36.807 11.280  1.00 19.83 ? 60   ALA D O   1 
ATOM   3786  C  CB  . ALA D  1 60  ? -20.752 -39.501 10.181  1.00 17.08 ? 60   ALA D CB  1 
ATOM   3787  N  N   . GLY D  1 61  ? -22.809 -38.296 12.562  1.00 17.27 ? 61   GLY D N   1 
ATOM   3788  C  CA  . GLY D  1 61  ? -23.897 -37.401 12.878  1.00 17.57 ? 61   GLY D CA  1 
ATOM   3789  C  C   . GLY D  1 61  ? -24.841 -37.146 11.712  1.00 21.95 ? 61   GLY D C   1 
ATOM   3790  O  O   . GLY D  1 61  ? -24.811 -37.867 10.697  1.00 20.21 ? 61   GLY D O   1 
ATOM   3791  N  N   . PRO D  1 62  ? -25.675 -36.092 11.843  1.00 22.49 ? 62   PRO D N   1 
ATOM   3792  C  CA  . PRO D  1 62  ? -26.737 -35.754 10.893  1.00 19.78 ? 62   PRO D CA  1 
ATOM   3793  C  C   . PRO D  1 62  ? -26.080 -35.190 9.662   1.00 17.13 ? 62   PRO D C   1 
ATOM   3794  O  O   . PRO D  1 62  ? -24.867 -35.036 9.683   1.00 18.79 ? 62   PRO D O   1 
ATOM   3795  C  CB  . PRO D  1 62  ? -27.503 -34.631 11.609  1.00 21.46 ? 62   PRO D CB  1 
ATOM   3796  C  CG  . PRO D  1 62  ? -26.629 -34.202 12.800  1.00 20.70 ? 62   PRO D CG  1 
ATOM   3797  C  CD  . PRO D  1 62  ? -25.361 -34.966 12.746  1.00 20.11 ? 62   PRO D CD  1 
ATOM   3798  N  N   . HIS D  1 63  ? -26.826 -34.868 8.614   1.00 17.42 ? 63   HIS D N   1 
ATOM   3799  C  CA  . HIS D  1 63  ? -26.185 -34.191 7.491   1.00 19.42 ? 63   HIS D CA  1 
ATOM   3800  C  C   . HIS D  1 63  ? -25.705 -32.824 7.968   1.00 21.03 ? 63   HIS D C   1 
ATOM   3801  O  O   . HIS D  1 63  ? -26.290 -32.221 8.881   1.00 20.15 ? 63   HIS D O   1 
ATOM   3802  C  CB  . HIS D  1 63  ? -27.110 -34.022 6.283   1.00 18.10 ? 63   HIS D CB  1 
ATOM   3803  C  CG  . HIS D  1 63  ? -27.751 -35.290 5.821   1.00 16.33 ? 63   HIS D CG  1 
ATOM   3804  N  ND1 . HIS D  1 63  ? -28.851 -35.302 4.994   1.00 15.59 ? 63   HIS D ND1 1 
ATOM   3805  C  CD2 . HIS D  1 63  ? -27.468 -36.584 6.086   1.00 16.51 ? 63   HIS D CD2 1 
ATOM   3806  C  CE1 . HIS D  1 63  ? -29.209 -36.550 4.759   1.00 18.12 ? 63   HIS D CE1 1 
ATOM   3807  N  NE2 . HIS D  1 63  ? -28.388 -37.349 5.415   1.00 15.41 ? 63   HIS D NE2 1 
ATOM   3808  N  N   . PHE D  1 64  ? -24.632 -32.343 7.355   1.00 19.68 ? 64   PHE D N   1 
ATOM   3809  C  CA  . PHE D  1 64  ? -24.087 -31.048 7.720   1.00 20.30 ? 64   PHE D CA  1 
ATOM   3810  C  C   . PHE D  1 64  ? -25.169 -29.993 7.479   1.00 21.18 ? 64   PHE D C   1 
ATOM   3811  O  O   . PHE D  1 64  ? -25.661 -29.856 6.369   1.00 21.84 ? 64   PHE D O   1 
ATOM   3812  C  CB  . PHE D  1 64  ? -22.809 -30.773 6.926   1.00 17.40 ? 64   PHE D CB  1 
ATOM   3813  C  CG  . PHE D  1 64  ? -22.139 -29.484 7.280   1.00 19.24 ? 64   PHE D CG  1 
ATOM   3814  C  CD1 . PHE D  1 64  ? -21.961 -29.121 8.598   1.00 19.99 ? 64   PHE D CD1 1 
ATOM   3815  C  CD2 . PHE D  1 64  ? -21.677 -28.637 6.288   1.00 19.61 ? 64   PHE D CD2 1 
ATOM   3816  C  CE1 . PHE D  1 64  ? -21.349 -27.931 8.921   1.00 21.08 ? 64   PHE D CE1 1 
ATOM   3817  C  CE2 . PHE D  1 64  ? -21.065 -27.452 6.604   1.00 19.65 ? 64   PHE D CE2 1 
ATOM   3818  C  CZ  . PHE D  1 64  ? -20.900 -27.096 7.918   1.00 21.24 ? 64   PHE D CZ  1 
ATOM   3819  N  N   . ASN D  1 65  ? -25.549 -29.265 8.525   1.00 20.60 ? 65   ASN D N   1 
ATOM   3820  C  CA  . ASN D  1 65  ? -26.677 -28.349 8.437   1.00 22.86 ? 65   ASN D CA  1 
ATOM   3821  C  C   . ASN D  1 65  ? -26.448 -27.054 9.229   1.00 23.20 ? 65   ASN D C   1 
ATOM   3822  O  O   . ASN D  1 65  ? -27.197 -26.749 10.144  1.00 26.51 ? 65   ASN D O   1 
ATOM   3823  C  CB  . ASN D  1 65  ? -27.931 -29.077 8.943   1.00 22.65 ? 65   ASN D CB  1 
ATOM   3824  C  CG  . ASN D  1 65  ? -29.229 -28.319 8.667   1.00 22.55 ? 65   ASN D CG  1 
ATOM   3825  O  OD1 . ASN D  1 65  ? -29.305 -27.438 7.807   1.00 21.47 ? 65   ASN D OD1 1 
ATOM   3826  N  ND2 . ASN D  1 65  ? -30.265 -28.684 9.401   1.00 23.95 ? 65   ASN D ND2 1 
ATOM   3827  N  N   . PRO D  1 66  ? -25.422 -26.274 8.862   1.00 22.83 ? 66   PRO D N   1 
ATOM   3828  C  CA  . PRO D  1 66  ? -25.080 -25.052 9.603   1.00 26.52 ? 66   PRO D CA  1 
ATOM   3829  C  C   . PRO D  1 66  ? -26.239 -24.056 9.708   1.00 27.86 ? 66   PRO D C   1 
ATOM   3830  O  O   . PRO D  1 66  ? -26.362 -23.349 10.714  1.00 30.49 ? 66   PRO D O   1 
ATOM   3831  C  CB  . PRO D  1 66  ? -23.957 -24.419 8.761   1.00 26.53 ? 66   PRO D CB  1 
ATOM   3832  C  CG  . PRO D  1 66  ? -23.541 -25.422 7.796   1.00 25.68 ? 66   PRO D CG  1 
ATOM   3833  C  CD  . PRO D  1 66  ? -24.663 -26.391 7.609   1.00 23.13 ? 66   PRO D CD  1 
ATOM   3834  N  N   . LEU D  1 67  ? -27.064 -23.992 8.668   1.00 29.07 ? 67   LEU D N   1 
ATOM   3835  C  CA  . LEU D  1 67  ? -28.136 -22.994 8.578   1.00 29.44 ? 67   LEU D CA  1 
ATOM   3836  C  C   . LEU D  1 67  ? -29.472 -23.474 9.149   1.00 30.23 ? 67   LEU D C   1 
ATOM   3837  O  O   . LEU D  1 67  ? -30.497 -22.815 8.973   1.00 29.39 ? 67   LEU D O   1 
ATOM   3838  C  CB  . LEU D  1 67  ? -28.305 -22.525 7.129   1.00 28.32 ? 67   LEU D CB  1 
ATOM   3839  C  CG  . LEU D  1 67  ? -26.998 -21.990 6.534   1.00 27.14 ? 67   LEU D CG  1 
ATOM   3840  C  CD1 . LEU D  1 67  ? -27.174 -21.552 5.088   1.00 30.24 ? 67   LEU D CD1 1 
ATOM   3841  C  CD2 . LEU D  1 67  ? -26.468 -20.848 7.388   1.00 27.94 ? 67   LEU D CD2 1 
ATOM   3842  N  N   . SER D  1 68  ? -29.445 -24.609 9.847   1.00 28.86 ? 68   SER D N   1 
ATOM   3843  C  CA  . SER D  1 68  ? -30.631 -25.176 10.488  1.00 28.47 ? 68   SER D CA  1 
ATOM   3844  C  C   . SER D  1 68  ? -31.848 -25.154 9.586   1.00 29.99 ? 68   SER D C   1 
ATOM   3845  O  O   . SER D  1 68  ? -32.870 -24.551 9.915   1.00 32.34 ? 68   SER D O   1 
ATOM   3846  C  CB  . SER D  1 68  ? -30.942 -24.460 11.795  1.00 28.17 ? 68   SER D CB  1 
ATOM   3847  O  OG  . SER D  1 68  ? -30.061 -24.884 12.816  1.00 37.31 ? 68   SER D OG  1 
ATOM   3848  N  N   . ARG D  1 69  ? -31.730 -25.814 8.442   1.00 28.68 ? 69   ARG D N   1 
ATOM   3849  C  CA  . ARG D  1 69  ? -32.847 -25.938 7.523   1.00 28.98 ? 69   ARG D CA  1 
ATOM   3850  C  C   . ARG D  1 69  ? -33.296 -27.389 7.428   1.00 28.73 ? 69   ARG D C   1 
ATOM   3851  O  O   . ARG D  1 69  ? -32.768 -28.259 8.140   1.00 26.33 ? 69   ARG D O   1 
ATOM   3852  C  CB  . ARG D  1 69  ? -32.474 -25.385 6.146   1.00 28.96 ? 69   ARG D CB  1 
ATOM   3853  C  CG  . ARG D  1 69  ? -32.461 -23.872 6.109   1.00 28.93 ? 69   ARG D CG  1 
ATOM   3854  C  CD  . ARG D  1 69  ? -31.880 -23.360 4.819   1.00 30.93 ? 69   ARG D CD  1 
ATOM   3855  N  NE  . ARG D  1 69  ? -31.579 -21.933 4.915   1.00 37.34 ? 69   ARG D NE  1 
ATOM   3856  C  CZ  . ARG D  1 69  ? -31.031 -21.214 3.938   1.00 36.70 ? 69   ARG D CZ  1 
ATOM   3857  N  NH1 . ARG D  1 69  ? -30.727 -21.786 2.780   1.00 36.63 ? 69   ARG D NH1 1 
ATOM   3858  N  NH2 . ARG D  1 69  ? -30.789 -19.920 4.117   1.00 37.52 ? 69   ARG D NH2 1 
ATOM   3859  N  N   . LYS D  1 70  ? -34.282 -27.637 6.568   1.00 27.07 ? 70   LYS D N   1 
ATOM   3860  C  CA  . LYS D  1 70  ? -34.774 -28.987 6.336   1.00 25.67 ? 70   LYS D CA  1 
ATOM   3861  C  C   . LYS D  1 70  ? -34.116 -29.599 5.108   1.00 22.26 ? 70   LYS D C   1 
ATOM   3862  O  O   . LYS D  1 70  ? -33.574 -28.895 4.257   1.00 21.46 ? 70   LYS D O   1 
ATOM   3863  C  CB  . LYS D  1 70  ? -36.298 -29.007 6.207   1.00 24.18 ? 70   LYS D CB  1 
ATOM   3864  C  CG  . LYS D  1 70  ? -36.989 -28.415 7.411   1.00 26.50 ? 70   LYS D CG  1 
ATOM   3865  C  CD  . LYS D  1 70  ? -38.457 -28.756 7.457   1.00 33.20 ? 70   LYS D CD  1 
ATOM   3866  C  CE  . LYS D  1 70  ? -39.185 -27.918 8.499   1.00 36.53 ? 70   LYS D CE  1 
ATOM   3867  N  NZ  . LYS D  1 70  ? -39.461 -26.532 8.000   1.00 43.17 ? 70   LYS D NZ  1 
ATOM   3868  N  N   . HIS D  1 71  ? -34.163 -30.920 5.044   1.00 18.69 ? 71   HIS D N   1 
ATOM   3869  C  CA  . HIS D  1 71  ? -33.509 -31.681 3.998   1.00 17.33 ? 71   HIS D CA  1 
ATOM   3870  C  C   . HIS D  1 71  ? -34.182 -31.439 2.651   1.00 20.49 ? 71   HIS D C   1 
ATOM   3871  O  O   . HIS D  1 71  ? -35.397 -31.285 2.584   1.00 22.57 ? 71   HIS D O   1 
ATOM   3872  C  CB  . HIS D  1 71  ? -33.567 -33.166 4.365   1.00 17.26 ? 71   HIS D CB  1 
ATOM   3873  C  CG  . HIS D  1 71  ? -33.088 -34.081 3.288   1.00 18.92 ? 71   HIS D CG  1 
ATOM   3874  N  ND1 . HIS D  1 71  ? -31.759 -34.400 3.122   1.00 18.08 ? 71   HIS D ND1 1 
ATOM   3875  C  CD2 . HIS D  1 71  ? -33.759 -34.752 2.321   1.00 19.81 ? 71   HIS D CD2 1 
ATOM   3876  C  CE1 . HIS D  1 71  ? -31.631 -35.227 2.099   1.00 19.26 ? 71   HIS D CE1 1 
ATOM   3877  N  NE2 . HIS D  1 71  ? -32.828 -35.454 1.595   1.00 18.49 ? 71   HIS D NE2 1 
ATOM   3878  N  N   . GLY D  1 72  ? -33.387 -31.395 1.587   1.00 19.92 ? 72   GLY D N   1 
ATOM   3879  C  CA  . GLY D  1 72  ? -33.904 -31.354 0.235   1.00 20.19 ? 72   GLY D CA  1 
ATOM   3880  C  C   . GLY D  1 72  ? -32.864 -31.899 -0.731  1.00 21.48 ? 72   GLY D C   1 
ATOM   3881  O  O   . GLY D  1 72  ? -31.904 -32.544 -0.318  1.00 22.06 ? 72   GLY D O   1 
ATOM   3882  N  N   . GLY D  1 73  ? -33.050 -31.646 -2.022  1.00 22.75 ? 73   GLY D N   1 
ATOM   3883  C  CA  . GLY D  1 73  ? -32.059 -32.013 -3.012  1.00 21.69 ? 73   GLY D CA  1 
ATOM   3884  C  C   . GLY D  1 73  ? -31.118 -30.845 -3.193  1.00 23.87 ? 73   GLY D C   1 
ATOM   3885  O  O   . GLY D  1 73  ? -31.372 -29.772 -2.635  1.00 24.84 ? 73   GLY D O   1 
ATOM   3886  N  N   . PRO D  1 74  ? -30.029 -31.048 -3.967  1.00 24.53 ? 74   PRO D N   1 
ATOM   3887  C  CA  . PRO D  1 74  ? -28.975 -30.055 -4.244  1.00 24.90 ? 74   PRO D CA  1 
ATOM   3888  C  C   . PRO D  1 74  ? -29.476 -28.812 -4.984  1.00 26.87 ? 74   PRO D C   1 
ATOM   3889  O  O   . PRO D  1 74  ? -28.907 -27.730 -4.828  1.00 28.40 ? 74   PRO D O   1 
ATOM   3890  C  CB  . PRO D  1 74  ? -27.986 -30.814 -5.131  1.00 23.57 ? 74   PRO D CB  1 
ATOM   3891  C  CG  . PRO D  1 74  ? -28.280 -32.259 -4.921  1.00 23.48 ? 74   PRO D CG  1 
ATOM   3892  C  CD  . PRO D  1 74  ? -29.735 -32.356 -4.579  1.00 21.96 ? 74   PRO D CD  1 
ATOM   3893  N  N   . LYS D  1 75  ? -30.529 -28.960 -5.779  1.00 29.53 ? 75   LYS D N   1 
ATOM   3894  C  CA  . LYS D  1 75  ? -31.055 -27.835 -6.551  1.00 30.57 ? 75   LYS D CA  1 
ATOM   3895  C  C   . LYS D  1 75  ? -32.179 -27.094 -5.826  1.00 31.78 ? 75   LYS D C   1 
ATOM   3896  O  O   . LYS D  1 75  ? -32.682 -26.091 -6.333  1.00 33.59 ? 75   LYS D O   1 
ATOM   3897  C  CB  . LYS D  1 75  ? -31.517 -28.293 -7.931  1.00 32.10 ? 75   LYS D CB  1 
ATOM   3898  C  CG  . LYS D  1 75  ? -30.435 -28.986 -8.744  1.00 35.84 ? 75   LYS D CG  1 
ATOM   3899  C  CD  . LYS D  1 75  ? -29.071 -28.272 -8.658  1.00 41.11 ? 75   LYS D CD  1 
ATOM   3900  C  CE  . LYS D  1 75  ? -29.055 -26.921 -9.388  1.00 41.72 ? 75   LYS D CE  1 
ATOM   3901  N  NZ  . LYS D  1 75  ? -27.660 -26.526 -9.769  1.00 41.01 ? 75   LYS D NZ  1 
ATOM   3902  N  N   . ASP D  1 76  ? -32.558 -27.589 -4.645  1.00 27.84 ? 76   ASP D N   1 
ATOM   3903  C  CA  . ASP D  1 76  ? -33.533 -26.926 -3.783  1.00 28.65 ? 76   ASP D CA  1 
ATOM   3904  C  C   . ASP D  1 76  ? -32.857 -25.805 -2.996  1.00 28.41 ? 76   ASP D C   1 
ATOM   3905  O  O   . ASP D  1 76  ? -31.681 -25.896 -2.668  1.00 26.05 ? 76   ASP D O   1 
ATOM   3906  C  CB  . ASP D  1 76  ? -34.160 -27.916 -2.786  1.00 26.94 ? 76   ASP D CB  1 
ATOM   3907  C  CG  . ASP D  1 76  ? -34.938 -29.044 -3.463  1.00 32.94 ? 76   ASP D CG  1 
ATOM   3908  O  OD1 . ASP D  1 76  ? -35.354 -28.892 -4.642  1.00 34.05 ? 76   ASP D OD1 1 
ATOM   3909  O  OD2 . ASP D  1 76  ? -35.152 -30.087 -2.797  1.00 31.46 ? 76   ASP D OD2 1 
ATOM   3910  N  N   . GLU D  1 77  ? -33.617 -24.756 -2.697  1.00 29.58 ? 77   GLU D N   1 
ATOM   3911  C  CA  . GLU D  1 77  ? -33.184 -23.657 -1.836  1.00 33.33 ? 77   GLU D CA  1 
ATOM   3912  C  C   . GLU D  1 77  ? -33.253 -24.051 -0.346  1.00 32.91 ? 77   GLU D C   1 
ATOM   3913  O  O   . GLU D  1 77  ? -32.409 -23.656 0.466   1.00 33.29 ? 77   GLU D O   1 
ATOM   3914  C  CB  . GLU D  1 77  ? -34.068 -22.433 -2.105  1.00 37.87 ? 77   GLU D CB  1 
ATOM   3915  C  CG  . GLU D  1 77  ? -33.709 -21.189 -1.298  1.00 44.39 ? 77   GLU D CG  1 
ATOM   3916  C  CD  . GLU D  1 77  ? -32.331 -20.650 -1.627  1.00 44.44 ? 77   GLU D CD  1 
ATOM   3917  O  OE1 . GLU D  1 77  ? -32.071 -20.358 -2.814  1.00 43.84 ? 77   GLU D OE1 1 
ATOM   3918  O  OE2 . GLU D  1 77  ? -31.508 -20.515 -0.693  1.00 48.37 ? 77   GLU D OE2 1 
ATOM   3919  N  N   . GLU D  1 78  ? -34.273 -24.831 0.000   1.00 33.00 ? 78   GLU D N   1 
ATOM   3920  C  CA  . GLU D  1 78  ? -34.348 -25.460 1.311   1.00 30.57 ? 78   GLU D CA  1 
ATOM   3921  C  C   . GLU D  1 78  ? -33.632 -26.804 1.247   1.00 26.38 ? 78   GLU D C   1 
ATOM   3922  O  O   . GLU D  1 78  ? -34.192 -27.814 0.810   1.00 23.72 ? 78   GLU D O   1 
ATOM   3923  C  CB  . GLU D  1 78  ? -35.806 -25.658 1.744   1.00 31.04 ? 78   GLU D CB  1 
ATOM   3924  C  CG  . GLU D  1 78  ? -35.988 -26.176 3.161   1.00 29.90 ? 78   GLU D CG  1 
ATOM   3925  C  CD  . GLU D  1 78  ? -35.927 -25.072 4.204   1.00 35.58 ? 78   GLU D CD  1 
ATOM   3926  O  OE1 . GLU D  1 78  ? -35.574 -23.923 3.840   1.00 38.43 ? 78   GLU D OE1 1 
ATOM   3927  O  OE2 . GLU D  1 78  ? -36.235 -25.357 5.386   1.00 31.16 ? 78   GLU D OE2 1 
ATOM   3928  N  N   . ARG D  1 79  ? -32.378 -26.798 1.675   1.00 25.56 ? 79   ARG D N   1 
ATOM   3929  C  CA  . ARG D  1 79  ? -31.585 -28.014 1.766   1.00 23.48 ? 79   ARG D CA  1 
ATOM   3930  C  C   . ARG D  1 79  ? -30.601 -27.867 2.906   1.00 24.86 ? 79   ARG D C   1 
ATOM   3931  O  O   . ARG D  1 79  ? -30.446 -26.780 3.480   1.00 23.90 ? 79   ARG D O   1 
ATOM   3932  C  CB  . ARG D  1 79  ? -30.816 -28.267 0.468   1.00 24.90 ? 79   ARG D CB  1 
ATOM   3933  C  CG  . ARG D  1 79  ? -29.920 -27.110 0.043   1.00 23.01 ? 79   ARG D CG  1 
ATOM   3934  C  CD  . ARG D  1 79  ? -29.062 -27.474 -1.132  1.00 22.48 ? 79   ARG D CD  1 
ATOM   3935  N  NE  . ARG D  1 79  ? -27.806 -28.091 -0.718  1.00 23.04 ? 79   ARG D NE  1 
ATOM   3936  C  CZ  . ARG D  1 79  ? -26.739 -28.200 -1.505  1.00 22.70 ? 79   ARG D CZ  1 
ATOM   3937  N  NH1 . ARG D  1 79  ? -26.781 -27.735 -2.742  1.00 22.69 ? 79   ARG D NH1 1 
ATOM   3938  N  NH2 . ARG D  1 79  ? -25.625 -28.762 -1.054  1.00 22.99 ? 79   ARG D NH2 1 
ATOM   3939  N  N   . HIS D  1 80  ? -29.949 -28.974 3.238   1.00 23.54 ? 80   HIS D N   1 
ATOM   3940  C  CA  . HIS D  1 80  ? -28.811 -28.950 4.126   1.00 19.61 ? 80   HIS D CA  1 
ATOM   3941  C  C   . HIS D  1 80  ? -27.594 -28.631 3.259   1.00 21.31 ? 80   HIS D C   1 
ATOM   3942  O  O   . HIS D  1 80  ? -27.554 -29.014 2.094   1.00 22.30 ? 80   HIS D O   1 
ATOM   3943  C  CB  . HIS D  1 80  ? -28.644 -30.321 4.776   1.00 21.52 ? 80   HIS D CB  1 
ATOM   3944  C  CG  . HIS D  1 80  ? -29.758 -30.697 5.705   1.00 22.35 ? 80   HIS D CG  1 
ATOM   3945  N  ND1 . HIS D  1 80  ? -30.236 -31.986 5.811   1.00 18.81 ? 80   HIS D ND1 1 
ATOM   3946  C  CD2 . HIS D  1 80  ? -30.481 -29.958 6.581   1.00 20.41 ? 80   HIS D CD2 1 
ATOM   3947  C  CE1 . HIS D  1 80  ? -31.199 -32.024 6.712   1.00 18.97 ? 80   HIS D CE1 1 
ATOM   3948  N  NE2 . HIS D  1 80  ? -31.369 -30.806 7.192   1.00 20.09 ? 80   HIS D NE2 1 
ATOM   3949  N  N   . VAL D  1 81  ? -26.610 -27.923 3.808   1.00 24.20 ? 81   VAL D N   1 
ATOM   3950  C  CA  . VAL D  1 81  ? -25.350 -27.693 3.094   1.00 22.13 ? 81   VAL D CA  1 
ATOM   3951  C  C   . VAL D  1 81  ? -24.839 -29.033 2.550   1.00 22.36 ? 81   VAL D C   1 
ATOM   3952  O  O   . VAL D  1 81  ? -24.447 -29.134 1.389   1.00 21.56 ? 81   VAL D O   1 
ATOM   3953  C  CB  . VAL D  1 81  ? -24.268 -27.029 4.003   1.00 20.56 ? 81   VAL D CB  1 
ATOM   3954  C  CG1 . VAL D  1 81  ? -22.902 -27.107 3.361   1.00 23.87 ? 81   VAL D CG1 1 
ATOM   3955  C  CG2 . VAL D  1 81  ? -24.608 -25.581 4.286   1.00 22.47 ? 81   VAL D CG2 1 
ATOM   3956  N  N   . GLY D  1 82  ? -24.867 -30.065 3.388   1.00 21.02 ? 82   GLY D N   1 
ATOM   3957  C  CA  . GLY D  1 82  ? -24.404 -31.388 2.998   1.00 20.58 ? 82   GLY D CA  1 
ATOM   3958  C  C   . GLY D  1 82  ? -25.276 -32.204 2.047   1.00 19.40 ? 82   GLY D C   1 
ATOM   3959  O  O   . GLY D  1 82  ? -24.992 -33.375 1.791   1.00 19.82 ? 82   GLY D O   1 
ATOM   3960  N  N   . ASP D  1 83  ? -26.326 -31.598 1.500   1.00 23.61 ? 83   ASP D N   1 
ATOM   3961  C  CA  . ASP D  1 83  ? -27.262 -32.318 0.623   1.00 21.38 ? 83   ASP D CA  1 
ATOM   3962  C  C   . ASP D  1 83  ? -26.834 -32.388 -0.833  1.00 19.52 ? 83   ASP D C   1 
ATOM   3963  O  O   . ASP D  1 83  ? -27.078 -31.456 -1.592  1.00 19.35 ? 83   ASP D O   1 
ATOM   3964  C  CB  . ASP D  1 83  ? -28.660 -31.710 0.726   1.00 20.98 ? 83   ASP D CB  1 
ATOM   3965  C  CG  . ASP D  1 83  ? -29.328 -32.048 2.030   1.00 20.61 ? 83   ASP D CG  1 
ATOM   3966  O  OD1 . ASP D  1 83  ? -28.850 -32.999 2.679   1.00 20.17 ? 83   ASP D OD1 1 
ATOM   3967  O  OD2 . ASP D  1 83  ? -30.307 -31.377 2.414   1.00 20.85 ? 83   ASP D OD2 1 
ATOM   3968  N  N   . LEU D  1 84  ? -26.223 -33.507 -1.224  1.00 17.31 ? 84   LEU D N   1 
ATOM   3969  C  CA  . LEU D  1 84  ? -25.677 -33.631 -2.576  1.00 19.06 ? 84   LEU D CA  1 
ATOM   3970  C  C   . LEU D  1 84  ? -26.516 -34.532 -3.483  1.00 20.42 ? 84   LEU D C   1 
ATOM   3971  O  O   . LEU D  1 84  ? -26.150 -34.792 -4.630  1.00 21.52 ? 84   LEU D O   1 
ATOM   3972  C  CB  . LEU D  1 84  ? -24.206 -34.079 -2.555  1.00 20.44 ? 84   LEU D CB  1 
ATOM   3973  C  CG  . LEU D  1 84  ? -23.187 -33.141 -1.895  1.00 19.10 ? 84   LEU D CG  1 
ATOM   3974  C  CD1 . LEU D  1 84  ? -21.783 -33.608 -2.214  1.00 20.32 ? 84   LEU D CD1 1 
ATOM   3975  C  CD2 . LEU D  1 84  ? -23.382 -31.714 -2.364  1.00 19.81 ? 84   LEU D CD2 1 
ATOM   3976  N  N   . GLY D  1 85  ? -27.647 -35.001 -2.967  1.00 20.36 ? 85   GLY D N   1 
ATOM   3977  C  CA  . GLY D  1 85  ? -28.575 -35.776 -3.768  1.00 18.75 ? 85   GLY D CA  1 
ATOM   3978  C  C   . GLY D  1 85  ? -28.268 -37.256 -3.841  1.00 17.15 ? 85   GLY D C   1 
ATOM   3979  O  O   . GLY D  1 85  ? -27.896 -37.887 -2.855  1.00 15.91 ? 85   GLY D O   1 
ATOM   3980  N  N   . ASN D  1 86  ? -28.439 -37.807 -5.035  1.00 20.62 ? 86   ASN D N   1 
ATOM   3981  C  CA  . ASN D  1 86  ? -28.236 -39.232 -5.282  1.00 20.96 ? 86   ASN D CA  1 
ATOM   3982  C  C   . ASN D  1 86  ? -27.059 -39.446 -6.219  1.00 18.83 ? 86   ASN D C   1 
ATOM   3983  O  O   . ASN D  1 86  ? -26.726 -38.567 -7.004  1.00 17.16 ? 86   ASN D O   1 
ATOM   3984  C  CB  . ASN D  1 86  ? -29.488 -39.852 -5.924  1.00 20.53 ? 86   ASN D CB  1 
ATOM   3985  C  CG  . ASN D  1 86  ? -30.658 -39.949 -4.966  1.00 19.39 ? 86   ASN D CG  1 
ATOM   3986  O  OD1 . ASN D  1 86  ? -30.614 -40.687 -3.994  1.00 19.91 ? 86   ASN D OD1 1 
ATOM   3987  N  ND2 . ASN D  1 86  ? -31.719 -39.207 -5.248  1.00 22.59 ? 86   ASN D ND2 1 
ATOM   3988  N  N   . VAL D  1 87  ? -26.437 -40.615 -6.130  1.00 17.89 ? 87   VAL D N   1 
ATOM   3989  C  CA  . VAL D  1 87  ? -25.527 -41.083 -7.167  1.00 19.91 ? 87   VAL D CA  1 
ATOM   3990  C  C   . VAL D  1 87  ? -26.132 -42.341 -7.806  1.00 19.63 ? 87   VAL D C   1 
ATOM   3991  O  O   . VAL D  1 87  ? -26.941 -43.020 -7.176  1.00 20.25 ? 87   VAL D O   1 
ATOM   3992  C  CB  . VAL D  1 87  ? -24.092 -41.344 -6.621  1.00 19.40 ? 87   VAL D CB  1 
ATOM   3993  C  CG1 . VAL D  1 87  ? -23.444 -40.034 -6.150  1.00 17.29 ? 87   VAL D CG1 1 
ATOM   3994  C  CG2 . VAL D  1 87  ? -24.104 -42.395 -5.523  1.00 17.03 ? 87   VAL D CG2 1 
ATOM   3995  N  N   . THR D  1 88  ? -25.769 -42.644 -9.054  1.00 21.61 ? 88   THR D N   1 
ATOM   3996  C  CA  . THR D  1 88  ? -26.414 -43.749 -9.764  1.00 21.90 ? 88   THR D CA  1 
ATOM   3997  C  C   . THR D  1 88  ? -25.466 -44.911 -10.055 1.00 22.57 ? 88   THR D C   1 
ATOM   3998  O  O   . THR D  1 88  ? -24.485 -44.759 -10.773 1.00 23.86 ? 88   THR D O   1 
ATOM   3999  C  CB  . THR D  1 88  ? -27.071 -43.267 -11.071 1.00 23.91 ? 88   THR D CB  1 
ATOM   4000  O  OG1 . THR D  1 88  ? -27.717 -42.010 -10.840 1.00 22.63 ? 88   THR D OG1 1 
ATOM   4001  C  CG2 . THR D  1 88  ? -28.090 -44.290 -11.581 1.00 24.50 ? 88   THR D CG2 1 
ATOM   4002  N  N   . ALA D  1 89  ? -25.775 -46.074 -9.495  1.00 23.54 ? 89   ALA D N   1 
ATOM   4003  C  CA  . ALA D  1 89  ? -24.957 -47.267 -9.683  1.00 22.42 ? 89   ALA D CA  1 
ATOM   4004  C  C   . ALA D  1 89  ? -25.497 -48.138 -10.809 1.00 23.61 ? 89   ALA D C   1 
ATOM   4005  O  O   . ALA D  1 89  ? -26.675 -48.468 -10.812 1.00 26.69 ? 89   ALA D O   1 
ATOM   4006  C  CB  . ALA D  1 89  ? -24.896 -48.073 -8.380  1.00 22.41 ? 89   ALA D CB  1 
ATOM   4007  N  N   . GLY D  1 90  ? -24.629 -48.519 -11.748 1.00 25.65 ? 90   GLY D N   1 
ATOM   4008  C  CA  . GLY D  1 90  ? -24.997 -49.388 -12.856 1.00 25.87 ? 90   GLY D CA  1 
ATOM   4009  C  C   . GLY D  1 90  ? -25.210 -50.833 -12.432 1.00 29.06 ? 90   GLY D C   1 
ATOM   4010  O  O   . GLY D  1 90  ? -25.117 -51.140 -11.247 1.00 28.82 ? 90   GLY D O   1 
ATOM   4011  N  N   . LYS D  1 91  ? -25.516 -51.719 -13.385 1.00 30.86 ? 91   LYS D N   1 
ATOM   4012  C  CA  . LYS D  1 91  ? -25.662 -53.152 -13.085 1.00 30.61 ? 91   LYS D CA  1 
ATOM   4013  C  C   . LYS D  1 91  ? -24.303 -53.684 -12.655 1.00 31.54 ? 91   LYS D C   1 
ATOM   4014  O  O   . LYS D  1 91  ? -24.166 -54.818 -12.204 1.00 31.41 ? 91   LYS D O   1 
ATOM   4015  C  CB  . LYS D  1 91  ? -26.171 -53.926 -14.306 1.00 31.21 ? 91   LYS D CB  1 
ATOM   4016  C  CG  . LYS D  1 91  ? -27.454 -53.368 -14.911 1.00 40.85 ? 91   LYS D CG  1 
ATOM   4017  C  CD  . LYS D  1 91  ? -28.206 -54.425 -15.740 1.00 47.96 ? 91   LYS D CD  1 
ATOM   4018  C  CE  . LYS D  1 91  ? -29.634 -53.967 -16.099 1.00 54.04 ? 91   LYS D CE  1 
ATOM   4019  N  NZ  . LYS D  1 91  ? -30.601 -54.030 -14.954 1.00 41.33 ? 91   LYS D NZ  1 
ATOM   4020  N  N   . ASP D  1 92  ? -23.310 -52.821 -12.836 1.00 32.47 ? 92   ASP D N   1 
ATOM   4021  C  CA  . ASP D  1 92  ? -21.921 -53.005 -12.445 1.00 32.65 ? 92   ASP D CA  1 
ATOM   4022  C  C   . ASP D  1 92  ? -21.780 -52.984 -10.913 1.00 31.80 ? 92   ASP D C   1 
ATOM   4023  O  O   . ASP D  1 92  ? -20.934 -53.666 -10.327 1.00 31.59 ? 92   ASP D O   1 
ATOM   4024  C  CB  . ASP D  1 92  ? -21.163 -51.796 -12.996 1.00 30.53 ? 92   ASP D CB  1 
ATOM   4025  C  CG  . ASP D  1 92  ? -19.898 -52.171 -13.686 1.00 39.77 ? 92   ASP D CG  1 
ATOM   4026  O  OD1 . ASP D  1 92  ? -19.659 -53.390 -13.844 1.00 46.19 ? 92   ASP D OD1 1 
ATOM   4027  O  OD2 . ASP D  1 92  ? -19.153 -51.244 -14.080 1.00 41.72 ? 92   ASP D OD2 1 
ATOM   4028  N  N   . GLY D  1 93  ? -22.621 -52.172 -10.281 1.00 28.32 ? 93   GLY D N   1 
ATOM   4029  C  CA  . GLY D  1 93  ? -22.504 -51.861 -8.875  1.00 26.88 ? 93   GLY D CA  1 
ATOM   4030  C  C   . GLY D  1 93  ? -21.639 -50.624 -8.720  1.00 27.63 ? 93   GLY D C   1 
ATOM   4031  O  O   . GLY D  1 93  ? -21.287 -50.223 -7.598  1.00 26.33 ? 93   GLY D O   1 
ATOM   4032  N  N   . VAL D  1 94  ? -21.290 -50.019 -9.853  1.00 23.84 ? 94   VAL D N   1 
ATOM   4033  C  CA  . VAL D  1 94  ? -20.366 -48.891 -9.851  1.00 24.35 ? 94   VAL D CA  1 
ATOM   4034  C  C   . VAL D  1 94  ? -21.074 -47.605 -10.185 1.00 23.99 ? 94   VAL D C   1 
ATOM   4035  O  O   . VAL D  1 94  ? -21.794 -47.522 -11.170 1.00 25.04 ? 94   VAL D O   1 
ATOM   4036  C  CB  . VAL D  1 94  ? -19.218 -49.065 -10.854 1.00 22.32 ? 94   VAL D CB  1 
ATOM   4037  C  CG1 . VAL D  1 94  ? -18.308 -47.849 -10.812 1.00 22.36 ? 94   VAL D CG1 1 
ATOM   4038  C  CG2 . VAL D  1 94  ? -18.446 -50.332 -10.560 1.00 26.64 ? 94   VAL D CG2 1 
ATOM   4039  N  N   . ALA D  1 95  ? -20.843 -46.593 -9.366  1.00 24.10 ? 95   ALA D N   1 
ATOM   4040  C  CA  . ALA D  1 95  ? -21.468 -45.298 -9.556  1.00 23.03 ? 95   ALA D CA  1 
ATOM   4041  C  C   . ALA D  1 95  ? -20.377 -44.303 -9.846  1.00 23.59 ? 95   ALA D C   1 
ATOM   4042  O  O   . ALA D  1 95  ? -19.572 -43.998 -8.977  1.00 26.59 ? 95   ALA D O   1 
ATOM   4043  C  CB  . ALA D  1 95  ? -22.230 -44.891 -8.300  1.00 22.44 ? 95   ALA D CB  1 
ATOM   4044  N  N   . ASN D  1 96  ? -20.340 -43.797 -11.067 1.00 25.41 ? 96   ASN D N   1 
ATOM   4045  C  CA  . ASN D  1 96  ? -19.375 -42.772 -11.409 1.00 25.38 ? 96   ASN D CA  1 
ATOM   4046  C  C   . ASN D  1 96  ? -19.940 -41.449 -10.974 1.00 23.39 ? 96   ASN D C   1 
ATOM   4047  O  O   . ASN D  1 96  ? -20.978 -41.018 -11.444 1.00 28.18 ? 96   ASN D O   1 
ATOM   4048  C  CB  . ASN D  1 96  ? -19.048 -42.795 -12.908 1.00 28.35 ? 96   ASN D CB  1 
ATOM   4049  C  CG  . ASN D  1 96  ? -18.395 -44.110 -13.341 1.00 31.99 ? 96   ASN D CG  1 
ATOM   4050  O  OD1 . ASN D  1 96  ? -17.435 -44.586 -12.719 1.00 31.86 ? 96   ASN D OD1 1 
ATOM   4051  N  ND2 . ASN D  1 96  ? -18.926 -44.711 -14.400 1.00 39.19 ? 96   ASN D ND2 1 
ATOM   4052  N  N   . VAL D  1 97  ? -19.284 -40.824 -10.021 1.00 22.03 ? 97   VAL D N   1 
ATOM   4053  C  CA  . VAL D  1 97  ? -19.811 -39.606 -9.455  1.00 22.34 ? 97   VAL D CA  1 
ATOM   4054  C  C   . VAL D  1 97  ? -19.240 -38.421 -10.204 1.00 22.53 ? 97   VAL D C   1 
ATOM   4055  O  O   . VAL D  1 97  ? -18.066 -38.407 -10.571 1.00 24.15 ? 97   VAL D O   1 
ATOM   4056  C  CB  . VAL D  1 97  ? -19.482 -39.506 -7.950  1.00 20.74 ? 97   VAL D CB  1 
ATOM   4057  C  CG1 . VAL D  1 97  ? -19.993 -38.212 -7.375  1.00 17.38 ? 97   VAL D CG1 1 
ATOM   4058  C  CG2 . VAL D  1 97  ? -20.068 -40.688 -7.215  1.00 21.32 ? 97   VAL D CG2 1 
ATOM   4059  N  N   . SER D  1 98  ? -20.082 -37.431 -10.448 1.00 24.30 ? 98   SER D N   1 
ATOM   4060  C  CA  . SER D  1 98  ? -19.615 -36.146 -10.946 1.00 24.76 ? 98   SER D CA  1 
ATOM   4061  C  C   . SER D  1 98  ? -20.700 -35.130 -10.638 1.00 26.04 ? 98   SER D C   1 
ATOM   4062  O  O   . SER D  1 98  ? -21.766 -35.138 -11.256 1.00 27.26 ? 98   SER D O   1 
ATOM   4063  C  CB  . SER D  1 98  ? -19.298 -36.205 -12.442 1.00 26.45 ? 98   SER D CB  1 
ATOM   4064  O  OG  . SER D  1 98  ? -18.941 -34.925 -12.941 1.00 28.31 ? 98   SER D OG  1 
ATOM   4065  N  N   . ILE D  1 99  ? -20.432 -34.279 -9.652  1.00 21.68 ? 99   ILE D N   1 
ATOM   4066  C  CA  . ILE D  1 99  ? -21.410 -33.323 -9.158  1.00 22.08 ? 99   ILE D CA  1 
ATOM   4067  C  C   . ILE D  1 99  ? -20.696 -31.990 -9.158  1.00 22.67 ? 99   ILE D C   1 
ATOM   4068  O  O   . ILE D  1 99  ? -19.482 -31.951 -9.045  1.00 24.91 ? 99   ILE D O   1 
ATOM   4069  C  CB  . ILE D  1 99  ? -21.897 -33.713 -7.713  1.00 21.57 ? 99   ILE D CB  1 
ATOM   4070  C  CG1 . ILE D  1 99  ? -22.562 -35.096 -7.723  1.00 22.49 ? 99   ILE D CG1 1 
ATOM   4071  C  CG2 . ILE D  1 99  ? -22.845 -32.688 -7.125  1.00 22.81 ? 99   ILE D CG2 1 
ATOM   4072  C  CD1 . ILE D  1 99  ? -23.038 -35.578 -6.389  1.00 20.22 ? 99   ILE D CD1 1 
ATOM   4073  N  N   . GLU D  1 100 ? -21.427 -30.902 -9.345  1.00 23.84 ? 100  GLU D N   1 
ATOM   4074  C  CA  . GLU D  1 100 ? -20.878 -29.588 -9.074  1.00 22.52 ? 100  GLU D CA  1 
ATOM   4075  C  C   . GLU D  1 100 ? -21.871 -28.835 -8.207  1.00 25.73 ? 100  GLU D C   1 
ATOM   4076  O  O   . GLU D  1 100 ? -23.044 -28.732 -8.555  1.00 28.67 ? 100  GLU D O   1 
ATOM   4077  C  CB  . GLU D  1 100 ? -20.598 -28.815 -10.353 1.00 24.90 ? 100  GLU D CB  1 
ATOM   4078  C  CG  . GLU D  1 100 ? -20.126 -27.399 -10.051 1.00 32.80 ? 100  GLU D CG  1 
ATOM   4079  C  CD  . GLU D  1 100 ? -19.935 -26.555 -11.290 1.00 42.11 ? 100  GLU D CD  1 
ATOM   4080  O  OE1 . GLU D  1 100 ? -19.036 -26.885 -12.097 1.00 46.00 ? 100  GLU D OE1 1 
ATOM   4081  O  OE2 . GLU D  1 100 ? -20.674 -25.554 -11.445 1.00 43.77 ? 100  GLU D OE2 1 
ATOM   4082  N  N   . ASP D  1 101 ? -21.409 -28.320 -7.074  1.00 24.50 ? 101  ASP D N   1 
ATOM   4083  C  CA  . ASP D  1 101 ? -22.292 -27.701 -6.095  1.00 24.90 ? 101  ASP D CA  1 
ATOM   4084  C  C   . ASP D  1 101 ? -21.769 -26.317 -5.724  1.00 25.58 ? 101  ASP D C   1 
ATOM   4085  O  O   . ASP D  1 101 ? -20.562 -26.113 -5.690  1.00 26.08 ? 101  ASP D O   1 
ATOM   4086  C  CB  . ASP D  1 101 ? -22.380 -28.589 -4.847  1.00 24.62 ? 101  ASP D CB  1 
ATOM   4087  C  CG  . ASP D  1 101 ? -23.529 -28.203 -3.933  1.00 26.70 ? 101  ASP D CG  1 
ATOM   4088  O  OD1 . ASP D  1 101 ? -24.694 -28.269 -4.388  1.00 30.14 ? 101  ASP D OD1 1 
ATOM   4089  O  OD2 . ASP D  1 101 ? -23.273 -27.840 -2.764  1.00 24.56 ? 101  ASP D OD2 1 
ATOM   4090  N  N   . ARG D  1 102 ? -22.667 -25.372 -5.448  1.00 26.07 ? 102  ARG D N   1 
ATOM   4091  C  CA  . ARG D  1 102 ? -22.261 -24.012 -5.085  1.00 24.61 ? 102  ARG D CA  1 
ATOM   4092  C  C   . ARG D  1 102 ? -22.449 -23.698 -3.604  1.00 26.32 ? 102  ARG D C   1 
ATOM   4093  O  O   . ARG D  1 102 ? -22.116 -22.598 -3.143  1.00 28.04 ? 102  ARG D O   1 
ATOM   4094  C  CB  . ARG D  1 102 ? -23.036 -22.996 -5.915  1.00 28.56 ? 102  ARG D CB  1 
ATOM   4095  C  CG  . ARG D  1 102 ? -22.997 -23.268 -7.409  1.00 37.51 ? 102  ARG D CG  1 
ATOM   4096  C  CD  . ARG D  1 102 ? -23.429 -22.038 -8.210  1.00 47.11 ? 102  ARG D CD  1 
ATOM   4097  N  NE  . ARG D  1 102 ? -22.718 -21.949 -9.489  1.00 49.34 ? 102  ARG D NE  1 
ATOM   4098  C  CZ  . ARG D  1 102 ? -21.638 -21.197 -9.693  1.00 44.74 ? 102  ARG D CZ  1 
ATOM   4099  N  NH1 . ARG D  1 102 ? -21.148 -20.454 -8.701  1.00 39.27 ? 102  ARG D NH1 1 
ATOM   4100  N  NH2 . ARG D  1 102 ? -21.049 -21.184 -10.888 1.00 40.72 ? 102  ARG D NH2 1 
ATOM   4101  N  N   . VAL D  1 103 ? -22.987 -24.665 -2.866  1.00 25.47 ? 103  VAL D N   1 
ATOM   4102  C  CA  . VAL D  1 103 ? -23.340 -24.472 -1.463  1.00 22.24 ? 103  VAL D CA  1 
ATOM   4103  C  C   . VAL D  1 103 ? -22.256 -25.018 -0.525  1.00 23.60 ? 103  VAL D C   1 
ATOM   4104  O  O   . VAL D  1 103 ? -21.863 -24.351 0.437   1.00 24.91 ? 103  VAL D O   1 
ATOM   4105  C  CB  . VAL D  1 103 ? -24.718 -25.088 -1.153  1.00 21.56 ? 103  VAL D CB  1 
ATOM   4106  C  CG1 . VAL D  1 103 ? -24.967 -25.127 0.342   1.00 22.78 ? 103  VAL D CG1 1 
ATOM   4107  C  CG2 . VAL D  1 103 ? -25.810 -24.284 -1.852  1.00 20.18 ? 103  VAL D CG2 1 
ATOM   4108  N  N   . ILE D  1 104 ? -21.771 -26.225 -0.804  1.00 22.15 ? 104  ILE D N   1 
ATOM   4109  C  CA  . ILE D  1 104 ? -20.609 -26.744 -0.090  1.00 23.91 ? 104  ILE D CA  1 
ATOM   4110  C  C   . ILE D  1 104 ? -19.382 -25.917 -0.469  1.00 25.20 ? 104  ILE D C   1 
ATOM   4111  O  O   . ILE D  1 104 ? -19.355 -25.296 -1.539  1.00 23.84 ? 104  ILE D O   1 
ATOM   4112  C  CB  . ILE D  1 104 ? -20.330 -28.246 -0.392  1.00 22.69 ? 104  ILE D CB  1 
ATOM   4113  C  CG1 . ILE D  1 104 ? -20.071 -28.464 -1.889  1.00 20.44 ? 104  ILE D CG1 1 
ATOM   4114  C  CG2 . ILE D  1 104 ? -21.462 -29.137 0.149   1.00 18.71 ? 104  ILE D CG2 1 
ATOM   4115  C  CD1 . ILE D  1 104 ? -19.562 -29.840 -2.228  1.00 18.17 ? 104  ILE D CD1 1 
ATOM   4116  N  N   . SER D  1 105 ? -18.383 -25.908 0.417   1.00 24.38 ? 105  SER D N   1 
ATOM   4117  C  CA  . SER D  1 105 ? -17.128 -25.205 0.184   1.00 23.26 ? 105  SER D CA  1 
ATOM   4118  C  C   . SER D  1 105 ? -15.951 -25.984 0.772   1.00 24.57 ? 105  SER D C   1 
ATOM   4119  O  O   . SER D  1 105 ? -16.147 -26.942 1.507   1.00 23.94 ? 105  SER D O   1 
ATOM   4120  C  CB  . SER D  1 105 ? -17.187 -23.808 0.794   1.00 25.84 ? 105  SER D CB  1 
ATOM   4121  O  OG  . SER D  1 105 ? -16.062 -23.042 0.397   1.00 30.25 ? 105  SER D OG  1 
ATOM   4122  N  N   . LEU D  1 106 ? -14.729 -25.571 0.446   1.00 25.61 ? 106  LEU D N   1 
ATOM   4123  C  CA  . LEU D  1 106 ? -13.535 -26.209 0.993   1.00 25.17 ? 106  LEU D CA  1 
ATOM   4124  C  C   . LEU D  1 106 ? -12.826 -25.278 1.979   1.00 28.30 ? 106  LEU D C   1 
ATOM   4125  O  O   . LEU D  1 106 ? -11.755 -25.601 2.514   1.00 27.61 ? 106  LEU D O   1 
ATOM   4126  C  CB  . LEU D  1 106 ? -12.587 -26.668 -0.124  1.00 25.28 ? 106  LEU D CB  1 
ATOM   4127  C  CG  . LEU D  1 106 ? -13.117 -27.786 -1.027  1.00 22.36 ? 106  LEU D CG  1 
ATOM   4128  C  CD1 . LEU D  1 106 ? -12.006 -28.340 -1.880  1.00 20.61 ? 106  LEU D CD1 1 
ATOM   4129  C  CD2 . LEU D  1 106 ? -13.765 -28.893 -0.190  1.00 21.15 ? 106  LEU D CD2 1 
ATOM   4130  N  N   . SER D  1 107 ? -13.450 -24.131 2.227   1.00 29.30 ? 107  SER D N   1 
ATOM   4131  C  CA  . SER D  1 107 ? -12.928 -23.134 3.158   1.00 31.19 ? 107  SER D CA  1 
ATOM   4132  C  C   . SER D  1 107 ? -14.090 -22.356 3.746   1.00 28.96 ? 107  SER D C   1 
ATOM   4133  O  O   . SER D  1 107 ? -15.159 -22.291 3.151   1.00 32.09 ? 107  SER D O   1 
ATOM   4134  C  CB  . SER D  1 107 ? -11.988 -22.170 2.436   1.00 30.19 ? 107  SER D CB  1 
ATOM   4135  O  OG  . SER D  1 107 ? -12.659 -21.542 1.352   1.00 34.80 ? 107  SER D OG  1 
ATOM   4136  N  N   . GLY D  1 108 ? -13.880 -21.768 4.915   1.00 28.84 ? 108  GLY D N   1 
ATOM   4137  C  CA  . GLY D  1 108 ? -14.857 -20.873 5.501   1.00 31.77 ? 108  GLY D CA  1 
ATOM   4138  C  C   . GLY D  1 108 ? -15.892 -21.542 6.384   1.00 34.75 ? 108  GLY D C   1 
ATOM   4139  O  O   . GLY D  1 108 ? -15.747 -22.699 6.776   1.00 32.48 ? 108  GLY D O   1 
ATOM   4140  N  N   . GLU D  1 109 ? -16.942 -20.788 6.696   1.00 35.48 ? 109  GLU D N   1 
ATOM   4141  C  CA  . GLU D  1 109 ? -18.092 -21.271 7.453   1.00 32.93 ? 109  GLU D CA  1 
ATOM   4142  C  C   . GLU D  1 109 ? -18.623 -22.620 6.942   1.00 31.71 ? 109  GLU D C   1 
ATOM   4143  O  O   . GLU D  1 109 ? -18.865 -23.539 7.727   1.00 30.59 ? 109  GLU D O   1 
ATOM   4144  C  CB  . GLU D  1 109 ? -19.217 -20.221 7.414   1.00 36.41 ? 109  GLU D CB  1 
ATOM   4145  C  CG  . GLU D  1 109 ? -18.838 -18.815 7.936   1.00 47.80 ? 109  GLU D CG  1 
ATOM   4146  C  CD  . GLU D  1 109 ? -17.964 -17.984 6.960   1.00 53.94 ? 109  GLU D CD  1 
ATOM   4147  O  OE1 . GLU D  1 109 ? -17.844 -18.349 5.760   1.00 49.44 ? 109  GLU D OE1 1 
ATOM   4148  O  OE2 . GLU D  1 109 ? -17.399 -16.952 7.401   1.00 50.54 ? 109  GLU D OE2 1 
ATOM   4149  N  N   . HIS D  1 110 ? -18.794 -22.743 5.628   1.00 30.33 ? 110  HIS D N   1 
ATOM   4150  C  CA  . HIS D  1 110 ? -19.436 -23.925 5.050   1.00 28.28 ? 110  HIS D CA  1 
ATOM   4151  C  C   . HIS D  1 110 ? -18.474 -25.013 4.576   1.00 25.06 ? 110  HIS D C   1 
ATOM   4152  O  O   . HIS D  1 110 ? -18.845 -25.884 3.797   1.00 24.27 ? 110  HIS D O   1 
ATOM   4153  C  CB  . HIS D  1 110 ? -20.406 -23.506 3.939   1.00 27.58 ? 110  HIS D CB  1 
ATOM   4154  C  CG  . HIS D  1 110 ? -21.629 -22.810 4.456   1.00 30.52 ? 110  HIS D CG  1 
ATOM   4155  N  ND1 . HIS D  1 110 ? -22.736 -22.552 3.673   1.00 30.23 ? 110  HIS D ND1 1 
ATOM   4156  C  CD2 . HIS D  1 110 ? -21.925 -22.341 5.692   1.00 29.26 ? 110  HIS D CD2 1 
ATOM   4157  C  CE1 . HIS D  1 110 ? -23.652 -21.940 4.402   1.00 27.89 ? 110  HIS D CE1 1 
ATOM   4158  N  NE2 . HIS D  1 110 ? -23.188 -21.805 5.631   1.00 30.95 ? 110  HIS D NE2 1 
ATOM   4159  N  N   . SER D  1 111 ? -17.247 -24.968 5.075   1.00 27.38 ? 111  SER D N   1 
ATOM   4160  C  CA  . SER D  1 111 ? -16.226 -25.931 4.680   1.00 27.63 ? 111  SER D CA  1 
ATOM   4161  C  C   . SER D  1 111 ? -16.532 -27.347 5.152   1.00 22.15 ? 111  SER D C   1 
ATOM   4162  O  O   . SER D  1 111 ? -16.973 -27.569 6.277   1.00 22.59 ? 111  SER D O   1 
ATOM   4163  C  CB  . SER D  1 111 ? -14.850 -25.515 5.195   1.00 24.80 ? 111  SER D CB  1 
ATOM   4164  O  OG  . SER D  1 111 ? -13.883 -26.488 4.839   1.00 23.09 ? 111  SER D OG  1 
ATOM   4165  N  N   . ILE D  1 112 ? -16.263 -28.302 4.276   1.00 21.27 ? 112  ILE D N   1 
ATOM   4166  C  CA  . ILE D  1 112 ? -16.529 -29.698 4.556   1.00 21.80 ? 112  ILE D CA  1 
ATOM   4167  C  C   . ILE D  1 112 ? -15.234 -30.489 4.808   1.00 19.87 ? 112  ILE D C   1 
ATOM   4168  O  O   . ILE D  1 112 ? -15.268 -31.705 4.998   1.00 19.02 ? 112  ILE D O   1 
ATOM   4169  C  CB  . ILE D  1 112 ? -17.338 -30.319 3.408   1.00 22.45 ? 112  ILE D CB  1 
ATOM   4170  C  CG1 . ILE D  1 112 ? -16.552 -30.232 2.093   1.00 21.90 ? 112  ILE D CG1 1 
ATOM   4171  C  CG2 . ILE D  1 112 ? -18.706 -29.607 3.267   1.00 23.69 ? 112  ILE D CG2 1 
ATOM   4172  C  CD1 . ILE D  1 112 ? -17.165 -31.031 0.968   1.00 20.50 ? 112  ILE D CD1 1 
ATOM   4173  N  N   . ILE D  1 113 ? -14.096 -29.795 4.797   1.00 18.95 ? 113  ILE D N   1 
ATOM   4174  C  CA  . ILE D  1 113 ? -12.822 -30.402 5.190   1.00 20.29 ? 113  ILE D CA  1 
ATOM   4175  C  C   . ILE D  1 113 ? -12.937 -30.831 6.653   1.00 18.31 ? 113  ILE D C   1 
ATOM   4176  O  O   . ILE D  1 113 ? -13.286 -30.022 7.508   1.00 18.51 ? 113  ILE D O   1 
ATOM   4177  C  CB  . ILE D  1 113 ? -11.611 -29.424 5.003   1.00 20.56 ? 113  ILE D CB  1 
ATOM   4178  C  CG1 . ILE D  1 113 ? -11.611 -28.804 3.603   1.00 18.95 ? 113  ILE D CG1 1 
ATOM   4179  C  CG2 . ILE D  1 113 ? -10.284 -30.137 5.214   1.00 18.50 ? 113  ILE D CG2 1 
ATOM   4180  C  CD1 . ILE D  1 113 ? -10.957 -29.660 2.556   1.00 19.84 ? 113  ILE D CD1 1 
ATOM   4181  N  N   . GLY D  1 114 ? -12.683 -32.110 6.931   1.00 17.92 ? 114  GLY D N   1 
ATOM   4182  C  CA  . GLY D  1 114 ? -12.767 -32.619 8.288   1.00 16.93 ? 114  GLY D CA  1 
ATOM   4183  C  C   . GLY D  1 114 ? -14.129 -33.166 8.655   1.00 18.16 ? 114  GLY D C   1 
ATOM   4184  O  O   . GLY D  1 114 ? -14.364 -33.576 9.787   1.00 19.12 ? 114  GLY D O   1 
ATOM   4185  N  N   . ARG D  1 115 ? -15.040 -33.161 7.692   1.00 18.43 ? 115  ARG D N   1 
ATOM   4186  C  CA  . ARG D  1 115 ? -16.364 -33.730 7.888   1.00 17.11 ? 115  ARG D CA  1 
ATOM   4187  C  C   . ARG D  1 115 ? -16.414 -35.034 7.096   1.00 16.85 ? 115  ARG D C   1 
ATOM   4188  O  O   . ARG D  1 115 ? -15.392 -35.481 6.586   1.00 19.02 ? 115  ARG D O   1 
ATOM   4189  C  CB  . ARG D  1 115 ? -17.441 -32.722 7.466   1.00 16.16 ? 115  ARG D CB  1 
ATOM   4190  C  CG  . ARG D  1 115 ? -17.314 -31.402 8.246   1.00 17.35 ? 115  ARG D CG  1 
ATOM   4191  C  CD  . ARG D  1 115 ? -18.337 -30.335 7.872   1.00 16.22 ? 115  ARG D CD  1 
ATOM   4192  N  NE  . ARG D  1 115 ? -18.084 -29.067 8.573   1.00 17.66 ? 115  ARG D NE  1 
ATOM   4193  C  CZ  . ARG D  1 115 ? -18.349 -28.837 9.867   1.00 19.50 ? 115  ARG D CZ  1 
ATOM   4194  N  NH1 . ARG D  1 115 ? -18.866 -29.787 10.631  1.00 18.00 ? 115  ARG D NH1 1 
ATOM   4195  N  NH2 . ARG D  1 115 ? -18.093 -27.648 10.410  1.00 18.66 ? 115  ARG D NH2 1 
ATOM   4196  N  N   . THR D  1 116 ? -17.581 -35.649 6.978   1.00 16.94 ? 116  THR D N   1 
ATOM   4197  C  CA  . THR D  1 116 ? -17.654 -37.011 6.437   1.00 19.56 ? 116  THR D CA  1 
ATOM   4198  C  C   . THR D  1 116 ? -18.537 -37.144 5.182   1.00 19.55 ? 116  THR D C   1 
ATOM   4199  O  O   . THR D  1 116 ? -19.668 -36.682 5.190   1.00 20.99 ? 116  THR D O   1 
ATOM   4200  C  CB  . THR D  1 116 ? -18.149 -37.978 7.551   1.00 16.87 ? 116  THR D CB  1 
ATOM   4201  O  OG1 . THR D  1 116 ? -17.150 -38.054 8.575   1.00 17.75 ? 116  THR D OG1 1 
ATOM   4202  C  CG2 . THR D  1 116 ? -18.432 -39.360 7.019   1.00 15.69 ? 116  THR D CG2 1 
ATOM   4203  N  N   . MET D  1 117 ? -18.025 -37.758 4.113   1.00 15.66 ? 117  MET D N   1 
ATOM   4204  C  CA  . MET D  1 117 ? -18.878 -38.167 2.993   1.00 18.06 ? 117  MET D CA  1 
ATOM   4205  C  C   . MET D  1 117 ? -19.526 -39.513 3.309   1.00 18.73 ? 117  MET D C   1 
ATOM   4206  O  O   . MET D  1 117 ? -18.822 -40.461 3.647   1.00 19.07 ? 117  MET D O   1 
ATOM   4207  C  CB  . MET D  1 117 ? -18.067 -38.352 1.700   1.00 18.89 ? 117  MET D CB  1 
ATOM   4208  C  CG  . MET D  1 117 ? -17.788 -37.093 0.883   1.00 23.51 ? 117  MET D CG  1 
ATOM   4209  S  SD  . MET D  1 117 ? -19.264 -36.134 0.503   1.00 30.43 ? 117  MET D SD  1 
ATOM   4210  C  CE  . MET D  1 117 ? -20.272 -37.361 -0.267  1.00 21.32 ? 117  MET D CE  1 
ATOM   4211  N  N   . VAL D  1 118 ? -20.846 -39.629 3.192   1.00 18.58 ? 118  VAL D N   1 
ATOM   4212  C  CA  . VAL D  1 118 ? -21.436 -40.972 3.250   1.00 19.40 ? 118  VAL D CA  1 
ATOM   4213  C  C   . VAL D  1 118 ? -22.327 -41.305 2.056   1.00 20.46 ? 118  VAL D C   1 
ATOM   4214  O  O   . VAL D  1 118 ? -22.995 -40.427 1.491   1.00 19.47 ? 118  VAL D O   1 
ATOM   4215  C  CB  . VAL D  1 118 ? -21.992 -41.409 4.693   1.00 20.03 ? 118  VAL D CB  1 
ATOM   4216  C  CG1 . VAL D  1 118 ? -21.974 -40.275 5.695   1.00 19.72 ? 118  VAL D CG1 1 
ATOM   4217  C  CG2 . VAL D  1 118 ? -23.339 -42.125 4.642   1.00 17.34 ? 118  VAL D CG2 1 
ATOM   4218  N  N   . VAL D  1 119 ? -22.250 -42.564 1.619   1.00 19.40 ? 119  VAL D N   1 
ATOM   4219  C  CA  . VAL D  1 119 ? -23.137 -43.065 0.575   1.00 19.35 ? 119  VAL D CA  1 
ATOM   4220  C  C   . VAL D  1 119 ? -24.133 -43.995 1.242   1.00 20.28 ? 119  VAL D C   1 
ATOM   4221  O  O   . VAL D  1 119 ? -23.762 -44.835 2.075   1.00 20.20 ? 119  VAL D O   1 
ATOM   4222  C  CB  . VAL D  1 119 ? -22.381 -43.762 -0.589  1.00 22.07 ? 119  VAL D CB  1 
ATOM   4223  C  CG1 . VAL D  1 119 ? -21.602 -44.975 -0.093  1.00 21.22 ? 119  VAL D CG1 1 
ATOM   4224  C  CG2 . VAL D  1 119 ? -23.353 -44.146 -1.723  1.00 18.25 ? 119  VAL D CG2 1 
ATOM   4225  N  N   . HIS D  1 120 ? -25.404 -43.828 0.892   1.00 18.87 ? 120  HIS D N   1 
ATOM   4226  C  CA  . HIS D  1 120 ? -26.476 -44.443 1.653   1.00 18.02 ? 120  HIS D CA  1 
ATOM   4227  C  C   . HIS D  1 120 ? -27.080 -45.653 0.968   1.00 18.92 ? 120  HIS D C   1 
ATOM   4228  O  O   . HIS D  1 120 ? -26.895 -45.876 -0.227  1.00 19.41 ? 120  HIS D O   1 
ATOM   4229  C  CB  . HIS D  1 120 ? -27.549 -43.409 2.005   1.00 17.28 ? 120  HIS D CB  1 
ATOM   4230  C  CG  . HIS D  1 120 ? -27.102 -42.411 3.029   1.00 16.49 ? 120  HIS D CG  1 
ATOM   4231  N  ND1 . HIS D  1 120 ? -27.395 -42.539 4.370   1.00 17.42 ? 120  HIS D ND1 1 
ATOM   4232  C  CD2 . HIS D  1 120 ? -26.362 -41.283 2.913   1.00 17.45 ? 120  HIS D CD2 1 
ATOM   4233  C  CE1 . HIS D  1 120 ? -26.862 -41.530 5.036   1.00 17.42 ? 120  HIS D CE1 1 
ATOM   4234  N  NE2 . HIS D  1 120 ? -26.227 -40.755 4.177   1.00 18.91 ? 120  HIS D NE2 1 
ATOM   4235  N  N   . GLU D  1 121 ? -27.799 -46.433 1.758   1.00 18.47 ? 121  GLU D N   1 
ATOM   4236  C  CA  . GLU D  1 121 ? -28.385 -47.681 1.314   1.00 19.98 ? 121  GLU D CA  1 
ATOM   4237  C  C   . GLU D  1 121 ? -29.447 -47.503 0.227   1.00 23.52 ? 121  GLU D C   1 
ATOM   4238  O  O   . GLU D  1 121 ? -29.497 -48.286 -0.720  1.00 24.29 ? 121  GLU D O   1 
ATOM   4239  C  CB  . GLU D  1 121 ? -28.976 -48.398 2.519   1.00 23.32 ? 121  GLU D CB  1 
ATOM   4240  C  CG  . GLU D  1 121 ? -29.940 -49.504 2.196   1.00 27.77 ? 121  GLU D CG  1 
ATOM   4241  C  CD  . GLU D  1 121 ? -30.878 -49.783 3.352   1.00 32.44 ? 121  GLU D CD  1 
ATOM   4242  O  OE1 . GLU D  1 121 ? -30.999 -48.913 4.257   1.00 30.11 ? 121  GLU D OE1 1 
ATOM   4243  O  OE2 . GLU D  1 121 ? -31.497 -50.868 3.352   1.00 37.69 ? 121  GLU D OE2 1 
ATOM   4244  N  N   . LYS D  1 122 ? -30.300 -46.485 0.360   1.00 23.12 ? 122  LYS D N   1 
ATOM   4245  C  CA  . LYS D  1 122 ? -31.417 -46.297 -0.573  1.00 22.38 ? 122  LYS D CA  1 
ATOM   4246  C  C   . LYS D  1 122 ? -31.391 -44.929 -1.240  1.00 21.23 ? 122  LYS D C   1 
ATOM   4247  O  O   . LYS D  1 122 ? -30.518 -44.095 -0.994  1.00 18.45 ? 122  LYS D O   1 
ATOM   4248  C  CB  . LYS D  1 122 ? -32.778 -46.424 0.132   1.00 22.27 ? 122  LYS D CB  1 
ATOM   4249  C  CG  . LYS D  1 122 ? -33.025 -47.678 0.916   1.00 22.75 ? 122  LYS D CG  1 
ATOM   4250  C  CD  . LYS D  1 122 ? -33.477 -47.300 2.309   1.00 27.68 ? 122  LYS D CD  1 
ATOM   4251  C  CE  . LYS D  1 122 ? -34.974 -47.164 2.418   1.00 32.90 ? 122  LYS D CE  1 
ATOM   4252  N  NZ  . LYS D  1 122 ? -35.522 -48.336 3.152   1.00 40.09 ? 122  LYS D NZ  1 
ATOM   4253  N  N   . GLN D  1 123 ? -32.405 -44.706 -2.062  1.00 21.54 ? 123  GLN D N   1 
ATOM   4254  C  CA  . GLN D  1 123 ? -32.576 -43.465 -2.789  1.00 20.67 ? 123  GLN D CA  1 
ATOM   4255  C  C   . GLN D  1 123 ? -33.023 -42.359 -1.856  1.00 20.66 ? 123  GLN D C   1 
ATOM   4256  O  O   . GLN D  1 123 ? -33.833 -42.574 -0.958  1.00 22.40 ? 123  GLN D O   1 
ATOM   4257  C  CB  . GLN D  1 123 ? -33.604 -43.650 -3.909  1.00 23.19 ? 123  GLN D CB  1 
ATOM   4258  C  CG  . GLN D  1 123 ? -34.020 -42.350 -4.571  1.00 24.12 ? 123  GLN D CG  1 
ATOM   4259  C  CD  . GLN D  1 123 ? -34.745 -42.562 -5.873  1.00 25.56 ? 123  GLN D CD  1 
ATOM   4260  O  OE1 . GLN D  1 123 ? -34.734 -43.658 -6.439  1.00 28.14 ? 123  GLN D OE1 1 
ATOM   4261  N  NE2 . GLN D  1 123 ? -35.371 -41.507 -6.368  1.00 25.57 ? 123  GLN D NE2 1 
ATOM   4262  N  N   . ASP D  1 124 ? -32.482 -41.170 -2.082  1.00 20.97 ? 124  ASP D N   1 
ATOM   4263  C  CA  . ASP D  1 124 ? -32.826 -39.994 -1.303  1.00 20.71 ? 124  ASP D CA  1 
ATOM   4264  C  C   . ASP D  1 124 ? -34.072 -39.367 -1.954  1.00 20.36 ? 124  ASP D C   1 
ATOM   4265  O  O   . ASP D  1 124 ? -34.047 -39.005 -3.125  1.00 20.77 ? 124  ASP D O   1 
ATOM   4266  C  CB  . ASP D  1 124 ? -31.611 -39.046 -1.284  1.00 18.30 ? 124  ASP D CB  1 
ATOM   4267  C  CG  . ASP D  1 124 ? -31.851 -37.762 -0.496  1.00 21.38 ? 124  ASP D CG  1 
ATOM   4268  O  OD1 . ASP D  1 124 ? -32.983 -37.524 -0.028  1.00 21.70 ? 124  ASP D OD1 1 
ATOM   4269  O  OD2 . ASP D  1 124 ? -30.889 -36.971 -0.357  1.00 21.75 ? 124  ASP D OD2 1 
ATOM   4270  N  N   . ASP D  1 125 ? -35.164 -39.259 -1.196  1.00 21.87 ? 125  ASP D N   1 
ATOM   4271  C  CA  . ASP D  1 125 ? -36.433 -38.748 -1.732  1.00 22.61 ? 125  ASP D CA  1 
ATOM   4272  C  C   . ASP D  1 125 ? -36.493 -37.213 -1.831  1.00 21.21 ? 125  ASP D C   1 
ATOM   4273  O  O   . ASP D  1 125 ? -37.519 -36.641 -2.196  1.00 18.97 ? 125  ASP D O   1 
ATOM   4274  C  CB  . ASP D  1 125 ? -37.637 -39.332 -0.959  1.00 22.10 ? 125  ASP D CB  1 
ATOM   4275  C  CG  . ASP D  1 125 ? -37.713 -38.848 0.484   1.00 21.33 ? 125  ASP D CG  1 
ATOM   4276  O  OD1 . ASP D  1 125 ? -37.137 -37.778 0.785   1.00 22.55 ? 125  ASP D OD1 1 
ATOM   4277  O  OD2 . ASP D  1 125 ? -38.367 -39.521 1.316   1.00 20.23 ? 125  ASP D OD2 1 
ATOM   4278  N  N   . LEU D  1 126 ? -35.370 -36.572 -1.516  1.00 24.02 ? 126  LEU D N   1 
ATOM   4279  C  CA  . LEU D  1 126 ? -35.180 -35.123 -1.662  1.00 21.89 ? 126  LEU D CA  1 
ATOM   4280  C  C   . LEU D  1 126 ? -36.126 -34.262 -0.819  1.00 21.95 ? 126  LEU D C   1 
ATOM   4281  O  O   . LEU D  1 126 ? -36.384 -33.092 -1.150  1.00 22.33 ? 126  LEU D O   1 
ATOM   4282  C  CB  . LEU D  1 126 ? -35.219 -34.719 -3.133  1.00 21.57 ? 126  LEU D CB  1 
ATOM   4283  C  CG  . LEU D  1 126 ? -34.200 -35.462 -3.999  1.00 23.31 ? 126  LEU D CG  1 
ATOM   4284  C  CD1 . LEU D  1 126 ? -34.245 -34.971 -5.453  1.00 25.13 ? 126  LEU D CD1 1 
ATOM   4285  C  CD2 . LEU D  1 126 ? -32.790 -35.337 -3.410  1.00 21.05 ? 126  LEU D CD2 1 
ATOM   4286  N  N   . GLY D  1 127 ? -36.616 -34.843 0.278   1.00 19.87 ? 127  GLY D N   1 
ATOM   4287  C  CA  . GLY D  1 127 ? -37.489 -34.146 1.200   1.00 18.41 ? 127  GLY D CA  1 
ATOM   4288  C  C   . GLY D  1 127 ? -38.951 -34.147 0.786   1.00 21.74 ? 127  GLY D C   1 
ATOM   4289  O  O   . GLY D  1 127 ? -39.744 -33.368 1.318   1.00 23.88 ? 127  GLY D O   1 
ATOM   4290  N  N   . LYS D  1 128 ? -39.310 -35.020 -0.159  1.00 23.01 ? 128  LYS D N   1 
ATOM   4291  C  CA  . LYS D  1 128 ? -40.670 -35.067 -0.726  1.00 22.37 ? 128  LYS D CA  1 
ATOM   4292  C  C   . LYS D  1 128 ? -41.422 -36.369 -0.430  1.00 19.26 ? 128  LYS D C   1 
ATOM   4293  O  O   . LYS D  1 128 ? -42.245 -36.804 -1.228  1.00 22.60 ? 128  LYS D O   1 
ATOM   4294  C  CB  . LYS D  1 128 ? -40.631 -34.875 -2.249  1.00 25.51 ? 128  LYS D CB  1 
ATOM   4295  C  CG  . LYS D  1 128 ? -39.771 -33.721 -2.741  1.00 26.59 ? 128  LYS D CG  1 
ATOM   4296  C  CD  . LYS D  1 128 ? -40.118 -33.364 -4.176  1.00 35.36 ? 128  LYS D CD  1 
ATOM   4297  C  CE  . LYS D  1 128 ? -38.962 -32.609 -4.845  1.00 49.28 ? 128  LYS D CE  1 
ATOM   4298  N  NZ  . LYS D  1 128 ? -38.255 -31.615 -3.955  1.00 41.35 ? 128  LYS D NZ  1 
ATOM   4299  N  N   . GLY D  1 129 ? -41.137 -36.994 0.705   1.00 18.95 ? 129  GLY D N   1 
ATOM   4300  C  CA  . GLY D  1 129 ? -41.722 -38.280 1.029   1.00 17.68 ? 129  GLY D CA  1 
ATOM   4301  C  C   . GLY D  1 129 ? -42.873 -38.176 2.000   1.00 17.54 ? 129  GLY D C   1 
ATOM   4302  O  O   . GLY D  1 129 ? -43.411 -39.191 2.423   1.00 19.94 ? 129  GLY D O   1 
ATOM   4303  N  N   . GLY D  1 130 ? -43.240 -36.947 2.358   1.00 17.66 ? 130  GLY D N   1 
ATOM   4304  C  CA  . GLY D  1 130 ? -44.433 -36.690 3.152   1.00 17.72 ? 130  GLY D CA  1 
ATOM   4305  C  C   . GLY D  1 130 ? -44.349 -37.184 4.577   1.00 20.33 ? 130  GLY D C   1 
ATOM   4306  O  O   . GLY D  1 130 ? -45.336 -37.634 5.157   1.00 19.05 ? 130  GLY D O   1 
ATOM   4307  N  N   . ASN D  1 131 ? -43.151 -37.112 5.148   1.00 22.27 ? 131  ASN D N   1 
ATOM   4308  C  CA  . ASN D  1 131 ? -42.958 -37.449 6.555   1.00 21.76 ? 131  ASN D CA  1 
ATOM   4309  C  C   . ASN D  1 131 ? -41.736 -36.768 7.115   1.00 23.11 ? 131  ASN D C   1 
ATOM   4310  O  O   . ASN D  1 131 ? -41.014 -36.075 6.397   1.00 25.35 ? 131  ASN D O   1 
ATOM   4311  C  CB  . ASN D  1 131 ? -42.930 -38.968 6.811   1.00 20.93 ? 131  ASN D CB  1 
ATOM   4312  C  CG  . ASN D  1 131 ? -41.718 -39.651 6.228   1.00 21.01 ? 131  ASN D CG  1 
ATOM   4313  O  OD1 . ASN D  1 131 ? -40.726 -39.013 5.905   1.00 21.42 ? 131  ASN D OD1 1 
ATOM   4314  N  ND2 . ASN D  1 131 ? -41.794 -40.971 6.097   1.00 18.96 ? 131  ASN D ND2 1 
ATOM   4315  N  N   . GLU D  1 132 ? -41.516 -36.972 8.405   1.00 24.60 ? 132  GLU D N   1 
ATOM   4316  C  CA  . GLU D  1 132 ? -40.472 -36.272 9.139   1.00 28.67 ? 132  GLU D CA  1 
ATOM   4317  C  C   . GLU D  1 132 ? -39.056 -36.809 8.843   1.00 26.04 ? 132  GLU D C   1 
ATOM   4318  O  O   . GLU D  1 132 ? -38.089 -36.040 8.858   1.00 24.37 ? 132  GLU D O   1 
ATOM   4319  C  CB  . GLU D  1 132 ? -40.791 -36.325 10.632  1.00 31.11 ? 132  GLU D CB  1 
ATOM   4320  C  CG  . GLU D  1 132 ? -40.320 -35.131 11.438  1.00 36.01 ? 132  GLU D CG  1 
ATOM   4321  C  CD  . GLU D  1 132 ? -40.574 -35.322 12.929  1.00 47.04 ? 132  GLU D CD  1 
ATOM   4322  O  OE1 . GLU D  1 132 ? -39.583 -35.455 13.697  1.00 43.20 ? 132  GLU D OE1 1 
ATOM   4323  O  OE2 . GLU D  1 132 ? -41.770 -35.361 13.316  1.00 47.27 ? 132  GLU D OE2 1 
ATOM   4324  N  N   . GLU D  1 133 ? -38.930 -38.114 8.580   1.00 22.31 ? 133  GLU D N   1 
ATOM   4325  C  CA  . GLU D  1 133 ? -37.643 -38.660 8.141   1.00 24.87 ? 133  GLU D CA  1 
ATOM   4326  C  C   . GLU D  1 133 ? -37.208 -38.067 6.802   1.00 22.77 ? 133  GLU D C   1 
ATOM   4327  O  O   . GLU D  1 133 ? -36.021 -37.828 6.566   1.00 21.90 ? 133  GLU D O   1 
ATOM   4328  C  CB  . GLU D  1 133 ? -37.670 -40.192 8.056   1.00 25.13 ? 133  GLU D CB  1 
ATOM   4329  C  CG  . GLU D  1 133 ? -37.038 -40.868 9.256   1.00 30.85 ? 133  GLU D CG  1 
ATOM   4330  C  CD  . GLU D  1 133 ? -35.609 -40.412 9.476   1.00 33.15 ? 133  GLU D CD  1 
ATOM   4331  O  OE1 . GLU D  1 133 ? -34.841 -40.467 8.499   1.00 32.79 ? 133  GLU D OE1 1 
ATOM   4332  O  OE2 . GLU D  1 133 ? -35.254 -39.997 10.611  1.00 40.00 ? 133  GLU D OE2 1 
ATOM   4333  N  N   . SER D  1 134 ? -38.184 -37.838 5.929   1.00 20.92 ? 134  SER D N   1 
ATOM   4334  C  CA  . SER D  1 134 ? -37.941 -37.206 4.655   1.00 19.46 ? 134  SER D CA  1 
ATOM   4335  C  C   . SER D  1 134 ? -37.238 -35.853 4.833   1.00 19.70 ? 134  SER D C   1 
ATOM   4336  O  O   . SER D  1 134 ? -36.223 -35.583 4.186   1.00 21.23 ? 134  SER D O   1 
ATOM   4337  C  CB  . SER D  1 134 ? -39.259 -37.046 3.893   1.00 19.18 ? 134  SER D CB  1 
ATOM   4338  O  OG  . SER D  1 134 ? -39.011 -36.830 2.517   1.00 18.78 ? 134  SER D OG  1 
ATOM   4339  N  N   . THR D  1 135 ? -37.770 -35.014 5.715   1.00 19.40 ? 135  THR D N   1 
ATOM   4340  C  CA  . THR D  1 135 ? -37.250 -33.662 5.929   1.00 19.72 ? 135  THR D CA  1 
ATOM   4341  C  C   . THR D  1 135 ? -35.966 -33.672 6.762   1.00 22.11 ? 135  THR D C   1 
ATOM   4342  O  O   . THR D  1 135 ? -35.465 -32.620 7.165   1.00 21.52 ? 135  THR D O   1 
ATOM   4343  C  CB  . THR D  1 135 ? -38.298 -32.758 6.644   1.00 24.68 ? 135  THR D CB  1 
ATOM   4344  O  OG1 . THR D  1 135 ? -38.590 -33.284 7.948   1.00 27.93 ? 135  THR D OG1 1 
ATOM   4345  C  CG2 . THR D  1 135 ? -39.591 -32.665 5.847   1.00 25.60 ? 135  THR D CG2 1 
ATOM   4346  N  N   . LYS D  1 136 ? -35.436 -34.869 7.008   1.00 23.12 ? 136  LYS D N   1 
ATOM   4347  C  CA  . LYS D  1 136 ? -34.256 -35.054 7.858   1.00 23.82 ? 136  LYS D CA  1 
ATOM   4348  C  C   . LYS D  1 136 ? -33.089 -35.771 7.132   1.00 23.11 ? 136  LYS D C   1 
ATOM   4349  O  O   . LYS D  1 136 ? -31.976 -35.241 7.021   1.00 19.38 ? 136  LYS D O   1 
ATOM   4350  C  CB  . LYS D  1 136 ? -34.656 -35.871 9.087   1.00 23.87 ? 136  LYS D CB  1 
ATOM   4351  C  CG  . LYS D  1 136 ? -33.830 -35.616 10.319  1.00 31.54 ? 136  LYS D CG  1 
ATOM   4352  C  CD  . LYS D  1 136 ? -34.629 -34.819 11.346  1.00 36.07 ? 136  LYS D CD  1 
ATOM   4353  C  CE  . LYS D  1 136 ? -35.697 -35.698 11.947  1.00 33.54 ? 136  LYS D CE  1 
ATOM   4354  N  NZ  . LYS D  1 136 ? -35.078 -36.990 12.398  1.00 38.53 ? 136  LYS D NZ  1 
ATOM   4355  N  N   . THR D  1 137 ? -33.370 -36.985 6.659   1.00 22.52 ? 137  THR D N   1 
ATOM   4356  C  CA  . THR D  1 137 ? -32.382 -37.868 6.065   1.00 19.70 ? 137  THR D CA  1 
ATOM   4357  C  C   . THR D  1 137 ? -32.743 -38.220 4.633   1.00 19.81 ? 137  THR D C   1 
ATOM   4358  O  O   . THR D  1 137 ? -31.983 -38.903 3.953   1.00 20.28 ? 137  THR D O   1 
ATOM   4359  C  CB  . THR D  1 137 ? -32.320 -39.219 6.811   1.00 22.99 ? 137  THR D CB  1 
ATOM   4360  O  OG1 . THR D  1 137 ? -33.538 -39.952 6.583   1.00 22.34 ? 137  THR D OG1 1 
ATOM   4361  C  CG2 . THR D  1 137 ? -32.092 -39.019 8.310   1.00 23.22 ? 137  THR D CG2 1 
ATOM   4362  N  N   . GLY D  1 138 ? -33.921 -37.790 4.194   1.00 19.84 ? 138  GLY D N   1 
ATOM   4363  C  CA  . GLY D  1 138 ? -34.425 -38.119 2.871   1.00 18.52 ? 138  GLY D CA  1 
ATOM   4364  C  C   . GLY D  1 138 ? -34.863 -39.566 2.715   1.00 21.05 ? 138  GLY D C   1 
ATOM   4365  O  O   . GLY D  1 138 ? -35.109 -40.023 1.601   1.00 21.88 ? 138  GLY D O   1 
ATOM   4366  N  N   . ASN D  1 139 ? -34.964 -40.292 3.825   1.00 22.96 ? 139  ASN D N   1 
ATOM   4367  C  CA  . ASN D  1 139 ? -35.301 -41.718 3.786   1.00 24.18 ? 139  ASN D CA  1 
ATOM   4368  C  C   . ASN D  1 139 ? -34.268 -42.548 3.038   1.00 22.72 ? 139  ASN D C   1 
ATOM   4369  O  O   . ASN D  1 139 ? -34.612 -43.543 2.391   1.00 24.93 ? 139  ASN D O   1 
ATOM   4370  C  CB  . ASN D  1 139 ? -36.687 -41.934 3.166   1.00 22.89 ? 139  ASN D CB  1 
ATOM   4371  C  CG  . ASN D  1 139 ? -37.804 -41.723 4.160   1.00 22.06 ? 139  ASN D CG  1 
ATOM   4372  O  OD1 . ASN D  1 139 ? -37.936 -42.480 5.115   1.00 23.86 ? 139  ASN D OD1 1 
ATOM   4373  N  ND2 . ASN D  1 139 ? -38.612 -40.686 3.946   1.00 20.99 ? 139  ASN D ND2 1 
ATOM   4374  N  N   . ALA D  1 140 ? -33.006 -42.136 3.121   1.00 21.17 ? 140  ALA D N   1 
ATOM   4375  C  CA  . ALA D  1 140 ? -31.950 -42.760 2.323   1.00 19.34 ? 140  ALA D CA  1 
ATOM   4376  C  C   . ALA D  1 140 ? -31.391 -44.001 3.019   1.00 21.22 ? 140  ALA D C   1 
ATOM   4377  O  O   . ALA D  1 140 ? -30.513 -44.672 2.494   1.00 20.13 ? 140  ALA D O   1 
ATOM   4378  C  CB  . ALA D  1 140 ? -30.841 -41.762 2.005   1.00 14.61 ? 140  ALA D CB  1 
ATOM   4379  N  N   . GLY D  1 141 ? -31.912 -44.296 4.205   1.00 24.53 ? 141  GLY D N   1 
ATOM   4380  C  CA  . GLY D  1 141 ? -31.587 -45.525 4.900   1.00 21.87 ? 141  GLY D CA  1 
ATOM   4381  C  C   . GLY D  1 141 ? -30.200 -45.551 5.482   1.00 22.15 ? 141  GLY D C   1 
ATOM   4382  O  O   . GLY D  1 141 ? -29.634 -44.508 5.810   1.00 20.95 ? 141  GLY D O   1 
ATOM   4383  N  N   . SER D  1 142 ? -29.639 -46.749 5.593   1.00 21.09 ? 142  SER D N   1 
ATOM   4384  C  CA  . SER D  1 142 ? -28.411 -46.934 6.352   1.00 21.93 ? 142  SER D CA  1 
ATOM   4385  C  C   . SER D  1 142 ? -27.170 -46.440 5.620   1.00 21.86 ? 142  SER D C   1 
ATOM   4386  O  O   . SER D  1 142 ? -27.206 -46.143 4.424   1.00 19.38 ? 142  SER D O   1 
ATOM   4387  C  CB  . SER D  1 142 ? -28.240 -48.396 6.779   1.00 23.70 ? 142  SER D CB  1 
ATOM   4388  O  OG  . SER D  1 142 ? -27.655 -49.158 5.739   1.00 26.51 ? 142  SER D OG  1 
ATOM   4389  N  N   . ARG D  1 143 ? -26.074 -46.351 6.362   1.00 21.14 ? 143  ARG D N   1 
ATOM   4390  C  CA  . ARG D  1 143 ? -24.827 -45.834 5.832   1.00 19.51 ? 143  ARG D CA  1 
ATOM   4391  C  C   . ARG D  1 143 ? -23.979 -47.011 5.350   1.00 20.53 ? 143  ARG D C   1 
ATOM   4392  O  O   . ARG D  1 143 ? -23.645 -47.906 6.119   1.00 24.60 ? 143  ARG D O   1 
ATOM   4393  C  CB  . ARG D  1 143 ? -24.142 -44.981 6.909   1.00 19.98 ? 143  ARG D CB  1 
ATOM   4394  C  CG  . ARG D  1 143 ? -25.129 -43.999 7.546   1.00 18.30 ? 143  ARG D CG  1 
ATOM   4395  C  CD  . ARG D  1 143 ? -24.571 -43.068 8.619   1.00 16.69 ? 143  ARG D CD  1 
ATOM   4396  N  NE  . ARG D  1 143 ? -25.654 -42.234 9.154   1.00 20.83 ? 143  ARG D NE  1 
ATOM   4397  C  CZ  . ARG D  1 143 ? -25.494 -41.144 9.905   1.00 18.44 ? 143  ARG D CZ  1 
ATOM   4398  N  NH1 . ARG D  1 143 ? -24.285 -40.726 10.241  1.00 18.39 ? 143  ARG D NH1 1 
ATOM   4399  N  NH2 . ARG D  1 143 ? -26.551 -40.464 10.327  1.00 18.41 ? 143  ARG D NH2 1 
ATOM   4400  N  N   . LEU D  1 144 ? -23.670 -47.037 4.058   1.00 23.17 ? 144  LEU D N   1 
ATOM   4401  C  CA  . LEU D  1 144 ? -22.969 -48.178 3.459   1.00 21.42 ? 144  LEU D CA  1 
ATOM   4402  C  C   . LEU D  1 144 ? -21.453 -48.043 3.556   1.00 21.56 ? 144  LEU D C   1 
ATOM   4403  O  O   . LEU D  1 144 ? -20.735 -49.024 3.761   1.00 21.64 ? 144  LEU D O   1 
ATOM   4404  C  CB  . LEU D  1 144 ? -23.368 -48.345 1.987   1.00 20.89 ? 144  LEU D CB  1 
ATOM   4405  C  CG  . LEU D  1 144 ? -24.810 -48.688 1.615   1.00 19.31 ? 144  LEU D CG  1 
ATOM   4406  C  CD1 . LEU D  1 144 ? -24.907 -48.817 0.110   1.00 22.70 ? 144  LEU D CD1 1 
ATOM   4407  C  CD2 . LEU D  1 144 ? -25.271 -49.967 2.284   1.00 20.59 ? 144  LEU D CD2 1 
ATOM   4408  N  N   . ALA D  1 145 ? -20.977 -46.817 3.393   1.00 20.09 ? 145  ALA D N   1 
ATOM   4409  C  CA  . ALA D  1 145 ? -19.560 -46.518 3.426   1.00 19.43 ? 145  ALA D CA  1 
ATOM   4410  C  C   . ALA D  1 145 ? -19.406 -45.033 3.707   1.00 19.70 ? 145  ALA D C   1 
ATOM   4411  O  O   . ALA D  1 145 ? -20.316 -44.255 3.458   1.00 22.61 ? 145  ALA D O   1 
ATOM   4412  C  CB  . ALA D  1 145 ? -18.913 -46.881 2.106   1.00 19.56 ? 145  ALA D CB  1 
ATOM   4413  N  N   . CYS D  1 146 ? -18.264 -44.646 4.251   1.00 19.49 ? 146  CYS D N   1 
ATOM   4414  C  CA  . CYS D  1 146 ? -17.982 -43.245 4.549   1.00 21.86 ? 146  CYS D CA  1 
ATOM   4415  C  C   . CYS D  1 146 ? -16.480 -43.053 4.720   1.00 19.52 ? 146  CYS D C   1 
ATOM   4416  O  O   . CYS D  1 146 ? -15.742 -44.022 4.869   1.00 21.07 ? 146  CYS D O   1 
ATOM   4417  C  CB  . CYS D  1 146 ? -18.722 -42.792 5.817   1.00 22.25 ? 146  CYS D CB  1 
ATOM   4418  S  SG  . CYS D  1 146 ? -18.150 -43.589 7.357   1.00 26.29 ? 146  CYS D SG  1 
ATOM   4419  N  N   . GLY D  1 147 ? -16.038 -41.803 4.691   1.00 17.14 ? 147  GLY D N   1 
ATOM   4420  C  CA  . GLY D  1 147 ? -14.649 -41.474 4.927   1.00 15.92 ? 147  GLY D CA  1 
ATOM   4421  C  C   . GLY D  1 147 ? -14.593 -40.023 5.339   1.00 16.88 ? 147  GLY D C   1 
ATOM   4422  O  O   . GLY D  1 147 ? -15.519 -39.272 5.071   1.00 16.10 ? 147  GLY D O   1 
ATOM   4423  N  N   . VAL D  1 148 ? -13.518 -39.627 6.010   1.00 20.18 ? 148  VAL D N   1 
ATOM   4424  C  CA  . VAL D  1 148 ? -13.347 -38.238 6.413   1.00 17.07 ? 148  VAL D CA  1 
ATOM   4425  C  C   . VAL D  1 148 ? -12.755 -37.437 5.250   1.00 18.22 ? 148  VAL D C   1 
ATOM   4426  O  O   . VAL D  1 148 ? -11.820 -37.892 4.572   1.00 16.38 ? 148  VAL D O   1 
ATOM   4427  C  CB  . VAL D  1 148 ? -12.448 -38.120 7.672   1.00 15.64 ? 148  VAL D CB  1 
ATOM   4428  C  CG1 . VAL D  1 148 ? -12.258 -36.656 8.071   1.00 14.35 ? 148  VAL D CG1 1 
ATOM   4429  C  CG2 . VAL D  1 148 ? -13.042 -38.914 8.819   1.00 17.33 ? 148  VAL D CG2 1 
ATOM   4430  N  N   . ILE D  1 149 ? -13.310 -36.253 5.006   1.00 18.79 ? 149  ILE D N   1 
ATOM   4431  C  CA  . ILE D  1 149 ? -12.843 -35.412 3.904   1.00 18.50 ? 149  ILE D CA  1 
ATOM   4432  C  C   . ILE D  1 149 ? -11.535 -34.717 4.276   1.00 17.43 ? 149  ILE D C   1 
ATOM   4433  O  O   . ILE D  1 149 ? -11.487 -33.893 5.198   1.00 16.25 ? 149  ILE D O   1 
ATOM   4434  C  CB  . ILE D  1 149 ? -13.916 -34.380 3.456   1.00 20.00 ? 149  ILE D CB  1 
ATOM   4435  C  CG1 . ILE D  1 149 ? -15.136 -35.099 2.880   1.00 18.93 ? 149  ILE D CG1 1 
ATOM   4436  C  CG2 . ILE D  1 149 ? -13.344 -33.409 2.423   1.00 17.23 ? 149  ILE D CG2 1 
ATOM   4437  C  CD1 . ILE D  1 149 ? -16.354 -34.217 2.752   1.00 18.94 ? 149  ILE D CD1 1 
ATOM   4438  N  N   . GLY D  1 150 ? -10.479 -35.052 3.540   1.00 18.07 ? 150  GLY D N   1 
ATOM   4439  C  CA  . GLY D  1 150 ? -9.153  -34.561 3.849   1.00 16.78 ? 150  GLY D CA  1 
ATOM   4440  C  C   . GLY D  1 150 ? -8.540  -33.687 2.782   1.00 19.77 ? 150  GLY D C   1 
ATOM   4441  O  O   . GLY D  1 150 ? -8.904  -33.757 1.595   1.00 18.44 ? 150  GLY D O   1 
ATOM   4442  N  N   . ILE D  1 151 ? -7.599  -32.856 3.222   1.00 19.69 ? 151  ILE D N   1 
ATOM   4443  C  CA  . ILE D  1 151 ? -6.838  -31.987 2.336   1.00 19.45 ? 151  ILE D CA  1 
ATOM   4444  C  C   . ILE D  1 151 ? -5.959  -32.809 1.405   1.00 19.21 ? 151  ILE D C   1 
ATOM   4445  O  O   . ILE D  1 151 ? -5.178  -33.634 1.870   1.00 19.44 ? 151  ILE D O   1 
ATOM   4446  C  CB  . ILE D  1 151 ? -5.949  -31.037 3.153   1.00 19.24 ? 151  ILE D CB  1 
ATOM   4447  C  CG1 . ILE D  1 151 ? -6.814  -30.076 3.958   1.00 16.93 ? 151  ILE D CG1 1 
ATOM   4448  C  CG2 . ILE D  1 151 ? -5.017  -30.278 2.237   1.00 20.74 ? 151  ILE D CG2 1 
ATOM   4449  C  CD1 . ILE D  1 151 ? -6.049  -29.047 4.683   1.00 18.42 ? 151  ILE D CD1 1 
ATOM   4450  N  N   . ALA D  1 152 ? -6.094  -32.605 0.095   1.00 20.23 ? 152  ALA D N   1 
ATOM   4451  C  CA  . ALA D  1 152 ? -5.245  -33.305 -0.857  1.00 19.28 ? 152  ALA D CA  1 
ATOM   4452  C  C   . ALA D  1 152 ? -4.353  -32.325 -1.617  1.00 22.30 ? 152  ALA D C   1 
ATOM   4453  O  O   . ALA D  1 152 ? -4.541  -31.105 -1.557  1.00 19.79 ? 152  ALA D O   1 
ATOM   4454  C  CB  . ALA D  1 152 ? -6.078  -34.122 -1.810  1.00 19.19 ? 152  ALA D CB  1 
ATOM   4455  N  N   . GLN D  1 153 ? -3.349  -32.858 -2.302  1.00 24.75 ? 153  GLN D N   1 
ATOM   4456  C  CA  . GLN D  1 153 ? -2.526  -32.019 -3.167  1.00 29.55 ? 153  GLN D CA  1 
ATOM   4457  C  C   . GLN D  1 153 ? -2.961  -32.135 -4.628  1.00 35.78 ? 153  GLN D C   1 
ATOM   4458  O  O   . GLN D  1 153 ? -2.858  -31.153 -5.372  1.00 39.76 ? 153  GLN D O   1 
ATOM   4459  C  CB  . GLN D  1 153 ? -1.028  -32.320 -3.004  1.00 31.54 ? 153  GLN D CB  1 
ATOM   4460  C  CG  . GLN D  1 153 ? -0.516  -33.581 -3.687  1.00 32.87 ? 153  GLN D CG  1 
ATOM   4461  C  CD  . GLN D  1 153 ? 1.007   -33.595 -3.782  1.00 33.44 ? 153  GLN D CD  1 
ATOM   4462  O  OE1 . GLN D  1 153 ? 1.668   -32.599 -3.476  1.00 32.38 ? 153  GLN D OE1 1 
ATOM   4463  N  NE2 . GLN D  1 153 ? 1.568   -34.721 -4.206  1.00 33.69 ? 153  GLN D NE2 1 
ATOM   4464  O  OXT . GLN D  1 153 ? -3.442  -33.189 -5.087  1.00 36.13 ? 153  GLN D OXT 1 
ATOM   4465  N  N   . ALA E  1 1   ? 33.071  -21.211 53.191  1.00 46.94 ? 1    ALA E N   1 
ATOM   4466  C  CA  . ALA E  1 1   ? 32.878  -22.392 52.351  1.00 45.05 ? 1    ALA E CA  1 
ATOM   4467  C  C   . ALA E  1 1   ? 31.860  -23.368 52.946  1.00 41.19 ? 1    ALA E C   1 
ATOM   4468  O  O   . ALA E  1 1   ? 32.238  -24.421 53.467  1.00 40.24 ? 1    ALA E O   1 
ATOM   4469  C  CB  . ALA E  1 1   ? 34.217  -23.103 52.109  1.00 46.22 ? 1    ALA E CB  1 
ATOM   4470  N  N   . THR E  1 2   ? 30.575  -23.013 52.870  1.00 38.40 ? 2    THR E N   1 
ATOM   4471  C  CA  . THR E  1 2   ? 29.504  -23.892 53.326  1.00 31.71 ? 2    THR E CA  1 
ATOM   4472  C  C   . THR E  1 2   ? 29.648  -25.257 52.669  1.00 31.94 ? 2    THR E C   1 
ATOM   4473  O  O   . THR E  1 2   ? 30.258  -25.387 51.616  1.00 33.65 ? 2    THR E O   1 
ATOM   4474  C  CB  . THR E  1 2   ? 28.122  -23.306 53.031  1.00 32.25 ? 2    THR E CB  1 
ATOM   4475  O  OG1 . THR E  1 2   ? 28.029  -22.004 53.616  1.00 41.17 ? 2    THR E OG1 1 
ATOM   4476  C  CG2 . THR E  1 2   ? 27.044  -24.166 53.629  1.00 32.45 ? 2    THR E CG2 1 
ATOM   4477  N  N   . LYS E  1 3   ? 29.085  -26.277 53.300  1.00 30.98 ? 3    LYS E N   1 
ATOM   4478  C  CA  . LYS E  1 3   ? 29.372  -27.652 52.940  1.00 27.07 ? 3    LYS E CA  1 
ATOM   4479  C  C   . LYS E  1 3   ? 28.189  -28.497 53.403  1.00 26.63 ? 3    LYS E C   1 
ATOM   4480  O  O   . LYS E  1 3   ? 27.683  -28.317 54.512  1.00 28.46 ? 3    LYS E O   1 
ATOM   4481  C  CB  . LYS E  1 3   ? 30.665  -28.082 53.639  1.00 29.80 ? 3    LYS E CB  1 
ATOM   4482  C  CG  . LYS E  1 3   ? 31.686  -28.805 52.779  1.00 31.53 ? 3    LYS E CG  1 
ATOM   4483  C  CD  . LYS E  1 3   ? 33.115  -28.484 53.235  1.00 35.53 ? 3    LYS E CD  1 
ATOM   4484  C  CE  . LYS E  1 3   ? 34.033  -29.715 53.226  1.00 41.81 ? 3    LYS E CE  1 
ATOM   4485  N  NZ  . LYS E  1 3   ? 34.089  -30.451 51.926  1.00 43.85 ? 3    LYS E NZ  1 
ATOM   4486  N  N   . ALA E  1 4   ? 27.714  -29.390 52.544  1.00 25.21 ? 4    ALA E N   1 
ATOM   4487  C  CA  . ALA E  1 4   ? 26.590  -30.251 52.900  1.00 23.14 ? 4    ALA E CA  1 
ATOM   4488  C  C   . ALA E  1 4   ? 26.798  -31.671 52.363  1.00 23.69 ? 4    ALA E C   1 
ATOM   4489  O  O   . ALA E  1 4   ? 27.796  -31.955 51.702  1.00 23.84 ? 4    ALA E O   1 
ATOM   4490  C  CB  . ALA E  1 4   ? 25.274  -29.656 52.407  1.00 20.82 ? 4    ALA E CB  1 
ATOM   4491  N  N   . VAL E  1 5   ? 25.869  -32.564 52.676  1.00 21.76 ? 5    VAL E N   1 
ATOM   4492  C  CA  . VAL E  1 5   ? 25.987  -33.956 52.274  1.00 21.99 ? 5    VAL E CA  1 
ATOM   4493  C  C   . VAL E  1 5   ? 24.599  -34.577 52.291  1.00 22.20 ? 5    VAL E C   1 
ATOM   4494  O  O   . VAL E  1 5   ? 23.669  -34.029 52.872  1.00 22.90 ? 5    VAL E O   1 
ATOM   4495  C  CB  . VAL E  1 5   ? 26.963  -34.747 53.193  1.00 25.66 ? 5    VAL E CB  1 
ATOM   4496  C  CG1 . VAL E  1 5   ? 26.355  -34.978 54.572  1.00 21.78 ? 5    VAL E CG1 1 
ATOM   4497  C  CG2 . VAL E  1 5   ? 27.372  -36.080 52.550  1.00 25.38 ? 5    VAL E CG2 1 
ATOM   4498  N  N   . CYS E  1 6   ? 24.465  -35.723 51.643  1.00 24.06 ? 6    CYS E N   1 
ATOM   4499  C  CA  . CYS E  1 6   ? 23.184  -36.391 51.498  1.00 23.58 ? 6    CYS E CA  1 
ATOM   4500  C  C   . CYS E  1 6   ? 23.455  -37.884 51.346  1.00 24.74 ? 6    CYS E C   1 
ATOM   4501  O  O   . CYS E  1 6   ? 24.266  -38.286 50.520  1.00 25.80 ? 6    CYS E O   1 
ATOM   4502  C  CB  . CYS E  1 6   ? 22.478  -35.869 50.244  1.00 25.83 ? 6    CYS E CB  1 
ATOM   4503  S  SG  . CYS E  1 6   ? 20.760  -36.316 50.076  1.00 28.24 ? 6    CYS E SG  1 
ATOM   4504  N  N   . VAL E  1 7   ? 22.803  -38.705 52.157  1.00 26.91 ? 7    VAL E N   1 
ATOM   4505  C  CA  . VAL E  1 7   ? 22.853  -40.147 51.962  1.00 26.24 ? 7    VAL E CA  1 
ATOM   4506  C  C   . VAL E  1 7   ? 21.517  -40.568 51.368  1.00 27.32 ? 7    VAL E C   1 
ATOM   4507  O  O   . VAL E  1 7   ? 20.475  -40.406 52.005  1.00 28.49 ? 7    VAL E O   1 
ATOM   4508  C  CB  . VAL E  1 7   ? 23.120  -40.913 53.280  1.00 27.16 ? 7    VAL E CB  1 
ATOM   4509  C  CG1 . VAL E  1 7   ? 23.086  -42.415 53.033  1.00 29.27 ? 7    VAL E CG1 1 
ATOM   4510  C  CG2 . VAL E  1 7   ? 24.465  -40.493 53.883  1.00 24.44 ? 7    VAL E CG2 1 
ATOM   4511  N  N   . LEU E  1 8   ? 21.550  -41.068 50.132  1.00 29.18 ? 8    LEU E N   1 
ATOM   4512  C  CA  . LEU E  1 8   ? 20.340  -41.469 49.417  1.00 28.73 ? 8    LEU E CA  1 
ATOM   4513  C  C   . LEU E  1 8   ? 19.970  -42.929 49.711  1.00 29.82 ? 8    LEU E C   1 
ATOM   4514  O  O   . LEU E  1 8   ? 20.799  -43.830 49.568  1.00 28.60 ? 8    LEU E O   1 
ATOM   4515  C  CB  . LEU E  1 8   ? 20.504  -41.248 47.909  1.00 28.68 ? 8    LEU E CB  1 
ATOM   4516  C  CG  . LEU E  1 8   ? 20.786  -39.838 47.367  1.00 30.14 ? 8    LEU E CG  1 
ATOM   4517  C  CD1 . LEU E  1 8   ? 21.721  -39.921 46.182  1.00 31.72 ? 8    LEU E CD1 1 
ATOM   4518  C  CD2 . LEU E  1 8   ? 19.514  -39.116 46.970  1.00 28.06 ? 8    LEU E CD2 1 
ATOM   4519  N  N   . LYS E  1 9   ? 18.725  -43.141 50.135  1.00 28.01 ? 9    LYS E N   1 
ATOM   4520  C  CA  . LYS E  1 9   ? 18.202  -44.468 50.429  1.00 29.90 ? 9    LYS E CA  1 
ATOM   4521  C  C   . LYS E  1 9   ? 16.743  -44.590 49.993  1.00 31.01 ? 9    LYS E C   1 
ATOM   4522  O  O   . LYS E  1 9   ? 16.011  -43.604 49.971  1.00 31.29 ? 9    LYS E O   1 
ATOM   4523  C  CB  . LYS E  1 9   ? 18.320  -44.772 51.929  1.00 34.24 ? 9    LYS E CB  1 
ATOM   4524  C  CG  . LYS E  1 9   ? 19.620  -45.436 52.333  1.00 36.86 ? 9    LYS E CG  1 
ATOM   4525  C  CD  . LYS E  1 9   ? 19.730  -45.569 53.841  1.00 40.40 ? 9    LYS E CD  1 
ATOM   4526  C  CE  . LYS E  1 9   ? 21.046  -46.227 54.233  1.00 45.66 ? 9    LYS E CE  1 
ATOM   4527  N  NZ  . LYS E  1 9   ? 20.999  -47.701 54.008  1.00 49.14 ? 9    LYS E NZ  1 
ATOM   4528  N  N   . GLY E  1 10  ? 16.319  -45.801 49.647  1.00 32.26 ? 10   GLY E N   1 
ATOM   4529  C  CA  . GLY E  1 10  ? 14.936  -46.029 49.267  1.00 36.91 ? 10   GLY E CA  1 
ATOM   4530  C  C   . GLY E  1 10  ? 14.442  -47.433 49.567  1.00 43.25 ? 10   GLY E C   1 
ATOM   4531  O  O   . GLY E  1 10  ? 15.039  -48.148 50.381  1.00 41.89 ? 10   GLY E O   1 
ATOM   4532  N  N   . ASP E  1 11  ? 13.349  -47.823 48.907  1.00 45.39 ? 11   ASP E N   1 
ATOM   4533  C  CA  . ASP E  1 11  ? 12.779  -49.167 49.037  1.00 45.68 ? 11   ASP E CA  1 
ATOM   4534  C  C   . ASP E  1 11  ? 13.766  -50.265 48.623  1.00 47.57 ? 11   ASP E C   1 
ATOM   4535  O  O   . ASP E  1 11  ? 14.025  -51.206 49.374  1.00 50.52 ? 11   ASP E O   1 
ATOM   4536  C  CB  . ASP E  1 11  ? 11.502  -49.295 48.198  1.00 48.47 ? 11   ASP E CB  1 
ATOM   4537  C  CG  . ASP E  1 11  ? 10.336  -48.474 48.752  1.00 59.30 ? 11   ASP E CG  1 
ATOM   4538  O  OD1 . ASP E  1 11  ? 10.380  -48.072 49.940  1.00 58.21 ? 11   ASP E OD1 1 
ATOM   4539  O  OD2 . ASP E  1 11  ? 9.365   -48.239 47.991  1.00 64.46 ? 11   ASP E OD2 1 
ATOM   4540  N  N   . GLY E  1 12  ? 14.321  -50.139 47.425  1.00 45.79 ? 12   GLY E N   1 
ATOM   4541  C  CA  . GLY E  1 12  ? 15.189  -51.171 46.892  1.00 46.94 ? 12   GLY E CA  1 
ATOM   4542  C  C   . GLY E  1 12  ? 16.674  -51.038 47.198  1.00 47.86 ? 12   GLY E C   1 
ATOM   4543  O  O   . GLY E  1 12  ? 17.064  -50.712 48.331  1.00 42.71 ? 12   GLY E O   1 
ATOM   4544  N  N   . PRO E  1 13  ? 17.512  -51.304 46.176  1.00 44.96 ? 13   PRO E N   1 
ATOM   4545  C  CA  . PRO E  1 13  ? 18.971  -51.422 46.241  1.00 41.20 ? 13   PRO E CA  1 
ATOM   4546  C  C   . PRO E  1 13  ? 19.688  -50.117 45.950  1.00 38.30 ? 13   PRO E C   1 
ATOM   4547  O  O   . PRO E  1 13  ? 20.918  -50.086 46.030  1.00 39.17 ? 13   PRO E O   1 
ATOM   4548  C  CB  . PRO E  1 13  ? 19.293  -52.407 45.103  1.00 40.44 ? 13   PRO E CB  1 
ATOM   4549  C  CG  . PRO E  1 13  ? 17.967  -52.712 44.421  1.00 42.91 ? 13   PRO E CG  1 
ATOM   4550  C  CD  . PRO E  1 13  ? 17.023  -51.634 44.833  1.00 39.48 ? 13   PRO E CD  1 
ATOM   4551  N  N   . VAL E  1 14  ? 18.957  -49.065 45.594  1.00 37.24 ? 14   VAL E N   1 
ATOM   4552  C  CA  . VAL E  1 14  ? 19.623  -47.825 45.219  1.00 36.31 ? 14   VAL E CA  1 
ATOM   4553  C  C   . VAL E  1 14  ? 20.084  -47.050 46.438  1.00 36.68 ? 14   VAL E C   1 
ATOM   4554  O  O   . VAL E  1 14  ? 19.276  -46.693 47.298  1.00 35.11 ? 14   VAL E O   1 
ATOM   4555  C  CB  . VAL E  1 14  ? 18.746  -46.907 44.373  1.00 35.11 ? 14   VAL E CB  1 
ATOM   4556  C  CG1 . VAL E  1 14  ? 19.461  -45.577 44.171  1.00 31.70 ? 14   VAL E CG1 1 
ATOM   4557  C  CG2 . VAL E  1 14  ? 18.416  -47.563 43.027  1.00 35.72 ? 14   VAL E CG2 1 
ATOM   4558  N  N   . GLN E  1 15  ? 21.388  -46.792 46.502  1.00 33.72 ? 15   GLN E N   1 
ATOM   4559  C  CA  . GLN E  1 15  ? 21.955  -45.994 47.580  1.00 34.35 ? 15   GLN E CA  1 
ATOM   4560  C  C   . GLN E  1 15  ? 23.239  -45.275 47.157  1.00 33.28 ? 15   GLN E C   1 
ATOM   4561  O  O   . GLN E  1 15  ? 24.070  -45.832 46.445  1.00 31.00 ? 15   GLN E O   1 
ATOM   4562  C  CB  . GLN E  1 15  ? 22.194  -46.856 48.824  1.00 38.14 ? 15   GLN E CB  1 
ATOM   4563  C  CG  . GLN E  1 15  ? 23.163  -48.014 48.627  1.00 42.37 ? 15   GLN E CG  1 
ATOM   4564  C  CD  . GLN E  1 15  ? 23.395  -48.788 49.912  1.00 48.96 ? 15   GLN E CD  1 
ATOM   4565  O  OE1 . GLN E  1 15  ? 23.433  -48.210 51.000  1.00 53.28 ? 15   GLN E OE1 1 
ATOM   4566  N  NE2 . GLN E  1 15  ? 23.550  -50.102 49.793  1.00 54.27 ? 15   GLN E NE2 1 
ATOM   4567  N  N   . GLY E  1 16  ? 23.390  -44.032 47.603  1.00 31.17 ? 16   GLY E N   1 
ATOM   4568  C  CA  . GLY E  1 16  ? 24.571  -43.249 47.295  1.00 28.12 ? 16   GLY E CA  1 
ATOM   4569  C  C   . GLY E  1 16  ? 24.835  -42.147 48.307  1.00 27.21 ? 16   GLY E C   1 
ATOM   4570  O  O   . GLY E  1 16  ? 24.075  -41.950 49.244  1.00 27.91 ? 16   GLY E O   1 
ATOM   4571  N  N   . ILE E  1 17  ? 25.937  -41.437 48.122  1.00 25.76 ? 17   ILE E N   1 
ATOM   4572  C  CA  . ILE E  1 17  ? 26.256  -40.288 48.944  1.00 25.91 ? 17   ILE E CA  1 
ATOM   4573  C  C   . ILE E  1 17  ? 26.548  -39.128 48.005  1.00 25.41 ? 17   ILE E C   1 
ATOM   4574  O  O   . ILE E  1 17  ? 27.305  -39.261 47.052  1.00 24.23 ? 17   ILE E O   1 
ATOM   4575  C  CB  . ILE E  1 17  ? 27.465  -40.570 49.865  1.00 26.32 ? 17   ILE E CB  1 
ATOM   4576  C  CG1 . ILE E  1 17  ? 27.200  -41.831 50.692  1.00 25.29 ? 17   ILE E CG1 1 
ATOM   4577  C  CG2 . ILE E  1 17  ? 27.757  -39.373 50.768  1.00 23.60 ? 17   ILE E CG2 1 
ATOM   4578  C  CD1 . ILE E  1 17  ? 28.392  -42.316 51.465  1.00 24.70 ? 17   ILE E CD1 1 
ATOM   4579  N  N   . ILE E  1 18  ? 25.921  -37.995 48.269  1.00 23.66 ? 18   ILE E N   1 
ATOM   4580  C  CA  . ILE E  1 18  ? 26.108  -36.816 47.453  1.00 21.66 ? 18   ILE E CA  1 
ATOM   4581  C  C   . ILE E  1 18  ? 26.686  -35.703 48.309  1.00 23.44 ? 18   ILE E C   1 
ATOM   4582  O  O   . ILE E  1 18  ? 26.186  -35.425 49.394  1.00 24.71 ? 18   ILE E O   1 
ATOM   4583  C  CB  . ILE E  1 18  ? 24.771  -36.371 46.809  1.00 25.18 ? 18   ILE E CB  1 
ATOM   4584  C  CG1 . ILE E  1 18  ? 24.289  -37.415 45.786  1.00 26.19 ? 18   ILE E CG1 1 
ATOM   4585  C  CG2 . ILE E  1 18  ? 24.907  -35.009 46.147  1.00 22.67 ? 18   ILE E CG2 1 
ATOM   4586  C  CD1 . ILE E  1 18  ? 25.207  -37.559 44.547  1.00 24.10 ? 18   ILE E CD1 1 
ATOM   4587  N  N   . ASN E  1 19  ? 27.755  -35.082 47.826  1.00 24.32 ? 19   ASN E N   1 
ATOM   4588  C  CA  . ASN E  1 19  ? 28.392  -33.973 48.520  1.00 22.83 ? 19   ASN E CA  1 
ATOM   4589  C  C   . ASN E  1 19  ? 28.094  -32.633 47.866  1.00 21.85 ? 19   ASN E C   1 
ATOM   4590  O  O   . ASN E  1 19  ? 28.013  -32.541 46.650  1.00 23.56 ? 19   ASN E O   1 
ATOM   4591  C  CB  . ASN E  1 19  ? 29.899  -34.201 48.582  1.00 23.78 ? 19   ASN E CB  1 
ATOM   4592  C  CG  . ASN E  1 19  ? 30.263  -35.486 49.302  1.00 26.72 ? 19   ASN E CG  1 
ATOM   4593  O  OD1 . ASN E  1 19  ? 30.335  -35.518 50.536  1.00 29.01 ? 19   ASN E OD1 1 
ATOM   4594  N  ND2 . ASN E  1 19  ? 30.500  -36.553 48.537  1.00 24.34 ? 19   ASN E ND2 1 
ATOM   4595  N  N   . PHE E  1 20  ? 27.934  -31.598 48.684  1.00 23.99 ? 20   PHE E N   1 
ATOM   4596  C  CA  . PHE E  1 20  ? 27.687  -30.234 48.215  1.00 24.04 ? 20   PHE E CA  1 
ATOM   4597  C  C   . PHE E  1 20  ? 28.720  -29.296 48.819  1.00 27.23 ? 20   PHE E C   1 
ATOM   4598  O  O   . PHE E  1 20  ? 29.052  -29.420 50.000  1.00 27.13 ? 20   PHE E O   1 
ATOM   4599  C  CB  . PHE E  1 20  ? 26.316  -29.739 48.674  1.00 23.23 ? 20   PHE E CB  1 
ATOM   4600  C  CG  . PHE E  1 20  ? 25.173  -30.621 48.274  1.00 22.73 ? 20   PHE E CG  1 
ATOM   4601  C  CD1 . PHE E  1 20  ? 24.870  -31.761 48.999  1.00 22.74 ? 20   PHE E CD1 1 
ATOM   4602  C  CD2 . PHE E  1 20  ? 24.381  -30.294 47.191  1.00 22.29 ? 20   PHE E CD2 1 
ATOM   4603  C  CE1 . PHE E  1 20  ? 23.805  -32.576 48.639  1.00 22.02 ? 20   PHE E CE1 1 
ATOM   4604  C  CE2 . PHE E  1 20  ? 23.321  -31.105 46.829  1.00 25.48 ? 20   PHE E CE2 1 
ATOM   4605  C  CZ  . PHE E  1 20  ? 23.036  -32.248 47.558  1.00 23.34 ? 20   PHE E CZ  1 
ATOM   4606  N  N   . GLU E  1 21  ? 29.207  -28.342 48.031  1.00 27.11 ? 21   GLU E N   1 
ATOM   4607  C  CA  . GLU E  1 21  ? 30.131  -27.345 48.550  1.00 27.52 ? 21   GLU E CA  1 
ATOM   4608  C  C   . GLU E  1 21  ? 29.953  -25.985 47.889  1.00 28.97 ? 21   GLU E C   1 
ATOM   4609  O  O   . GLU E  1 21  ? 29.972  -25.865 46.673  1.00 31.49 ? 21   GLU E O   1 
ATOM   4610  C  CB  . GLU E  1 21  ? 31.574  -27.819 48.395  1.00 30.40 ? 21   GLU E CB  1 
ATOM   4611  C  CG  . GLU E  1 21  ? 32.583  -26.977 49.169  1.00 35.97 ? 21   GLU E CG  1 
ATOM   4612  C  CD  . GLU E  1 21  ? 34.017  -27.331 48.831  1.00 41.44 ? 21   GLU E CD  1 
ATOM   4613  O  OE1 . GLU E  1 21  ? 34.317  -28.542 48.693  1.00 42.71 ? 21   GLU E OE1 1 
ATOM   4614  O  OE2 . GLU E  1 21  ? 34.839  -26.395 48.705  1.00 43.18 ? 21   GLU E OE2 1 
ATOM   4615  N  N   . GLN E  1 22  ? 29.799  -24.955 48.703  1.00 30.54 ? 22   GLN E N   1 
ATOM   4616  C  CA  . GLN E  1 22  ? 29.647  -23.608 48.190  1.00 35.33 ? 22   GLN E CA  1 
ATOM   4617  C  C   . GLN E  1 22  ? 30.664  -22.679 48.834  1.00 40.34 ? 22   GLN E C   1 
ATOM   4618  O  O   . GLN E  1 22  ? 30.550  -22.360 50.012  1.00 39.48 ? 22   GLN E O   1 
ATOM   4619  C  CB  . GLN E  1 22  ? 28.244  -23.103 48.490  1.00 34.06 ? 22   GLN E CB  1 
ATOM   4620  C  CG  . GLN E  1 22  ? 27.923  -21.786 47.828  1.00 35.76 ? 22   GLN E CG  1 
ATOM   4621  C  CD  . GLN E  1 22  ? 26.499  -21.377 48.069  1.00 35.04 ? 22   GLN E CD  1 
ATOM   4622  O  OE1 . GLN E  1 22  ? 26.002  -21.474 49.187  1.00 37.37 ? 22   GLN E OE1 1 
ATOM   4623  N  NE2 . GLN E  1 22  ? 25.828  -20.917 47.025  1.00 36.78 ? 22   GLN E NE2 1 
ATOM   4624  N  N   . LYS E  1 23  ? 31.651  -22.234 48.062  1.00 44.06 ? 23   LYS E N   1 
ATOM   4625  C  CA  . LYS E  1 23  ? 32.725  -21.390 48.600  1.00 47.25 ? 23   LYS E CA  1 
ATOM   4626  C  C   . LYS E  1 23  ? 32.299  -19.951 48.914  1.00 48.26 ? 23   LYS E C   1 
ATOM   4627  O  O   . LYS E  1 23  ? 32.670  -19.406 49.954  1.00 46.84 ? 23   LYS E O   1 
ATOM   4628  C  CB  . LYS E  1 23  ? 33.928  -21.372 47.650  1.00 50.66 ? 23   LYS E CB  1 
ATOM   4629  C  CG  . LYS E  1 23  ? 34.485  -22.748 47.332  1.00 51.12 ? 23   LYS E CG  1 
ATOM   4630  C  CD  . LYS E  1 23  ? 35.003  -23.429 48.591  1.00 52.16 ? 23   LYS E CD  1 
ATOM   4631  C  CE  . LYS E  1 23  ? 36.188  -22.666 49.187  1.00 57.48 ? 23   LYS E CE  1 
ATOM   4632  N  NZ  . LYS E  1 23  ? 37.408  -22.749 48.327  1.00 57.50 ? 23   LYS E NZ  1 
ATOM   4633  N  N   . GLU E  1 24  ? 31.536  -19.337 48.010  1.00 48.08 ? 24   GLU E N   1 
ATOM   4634  C  CA  . GLU E  1 24  ? 31.141  -17.937 48.171  1.00 49.12 ? 24   GLU E CA  1 
ATOM   4635  C  C   . GLU E  1 24  ? 29.698  -17.845 48.627  1.00 46.40 ? 24   GLU E C   1 
ATOM   4636  O  O   . GLU E  1 24  ? 28.905  -18.747 48.375  1.00 42.42 ? 24   GLU E O   1 
ATOM   4637  C  CB  . GLU E  1 24  ? 31.316  -17.148 46.865  1.00 49.68 ? 24   GLU E CB  1 
ATOM   4638  C  CG  . GLU E  1 24  ? 32.465  -17.616 45.960  1.00 55.35 ? 24   GLU E CG  1 
ATOM   4639  C  CD  . GLU E  1 24  ? 33.847  -17.400 46.571  1.00 62.40 ? 24   GLU E CD  1 
ATOM   4640  O  OE1 . GLU E  1 24  ? 34.716  -18.292 46.415  1.00 59.20 ? 24   GLU E OE1 1 
ATOM   4641  O  OE2 . GLU E  1 24  ? 34.064  -16.343 47.206  1.00 69.25 ? 24   GLU E OE2 1 
ATOM   4642  N  N   . SER E  1 25  ? 29.365  -16.742 49.288  1.00 49.69 ? 25   SER E N   1 
ATOM   4643  C  CA  . SER E  1 25  ? 28.026  -16.538 49.833  1.00 52.00 ? 25   SER E CA  1 
ATOM   4644  C  C   . SER E  1 25  ? 26.933  -17.037 48.898  1.00 48.75 ? 25   SER E C   1 
ATOM   4645  O  O   . SER E  1 25  ? 26.139  -17.908 49.255  1.00 50.52 ? 25   SER E O   1 
ATOM   4646  C  CB  . SER E  1 25  ? 27.796  -15.059 50.137  1.00 53.97 ? 25   SER E CB  1 
ATOM   4647  O  OG  . SER E  1 25  ? 26.408  -14.786 50.257  1.00 61.96 ? 25   SER E OG  1 
ATOM   4648  N  N   . ASN E  1 26  ? 26.898  -16.473 47.698  1.00 49.98 ? 26   ASN E N   1 
ATOM   4649  C  CA  . ASN E  1 26  ? 25.874  -16.809 46.722  1.00 47.06 ? 26   ASN E CA  1 
ATOM   4650  C  C   . ASN E  1 26  ? 26.504  -17.322 45.427  1.00 46.23 ? 26   ASN E C   1 
ATOM   4651  O  O   . ASN E  1 26  ? 25.945  -17.170 44.343  1.00 46.85 ? 26   ASN E O   1 
ATOM   4652  C  CB  . ASN E  1 26  ? 25.004  -15.583 46.448  1.00 51.55 ? 26   ASN E CB  1 
ATOM   4653  C  CG  . ASN E  1 26  ? 25.822  -14.374 45.987  1.00 57.21 ? 26   ASN E CG  1 
ATOM   4654  O  OD1 . ASN E  1 26  ? 26.977  -14.507 45.562  1.00 54.30 ? 26   ASN E OD1 1 
ATOM   4655  N  ND2 . ASN E  1 26  ? 25.217  -13.190 46.060  1.00 55.56 ? 26   ASN E ND2 1 
ATOM   4656  N  N   . GLY E  1 27  ? 27.677  -17.931 45.551  1.00 45.35 ? 27   GLY E N   1 
ATOM   4657  C  CA  . GLY E  1 27  ? 28.382  -18.467 44.405  1.00 40.70 ? 27   GLY E CA  1 
ATOM   4658  C  C   . GLY E  1 27  ? 27.945  -19.873 44.029  1.00 41.64 ? 27   GLY E C   1 
ATOM   4659  O  O   . GLY E  1 27  ? 27.032  -20.444 44.636  1.00 36.56 ? 27   GLY E O   1 
ATOM   4660  N  N   . PRO E  1 28  ? 28.608  -20.440 43.011  1.00 41.74 ? 28   PRO E N   1 
ATOM   4661  C  CA  . PRO E  1 28  ? 28.372  -21.792 42.488  1.00 39.09 ? 28   PRO E CA  1 
ATOM   4662  C  C   . PRO E  1 28  ? 28.432  -22.858 43.585  1.00 38.48 ? 28   PRO E C   1 
ATOM   4663  O  O   . PRO E  1 28  ? 29.306  -22.806 44.457  1.00 38.60 ? 28   PRO E O   1 
ATOM   4664  C  CB  . PRO E  1 28  ? 29.540  -22.003 41.526  1.00 39.14 ? 28   PRO E CB  1 
ATOM   4665  C  CG  . PRO E  1 28  ? 29.983  -20.646 41.152  1.00 41.14 ? 28   PRO E CG  1 
ATOM   4666  C  CD  . PRO E  1 28  ? 29.701  -19.750 42.305  1.00 39.04 ? 28   PRO E CD  1 
ATOM   4667  N  N   . VAL E  1 29  ? 27.512  -23.815 43.529  1.00 34.14 ? 29   VAL E N   1 
ATOM   4668  C  CA  . VAL E  1 29  ? 27.558  -24.974 44.404  1.00 30.42 ? 29   VAL E CA  1 
ATOM   4669  C  C   . VAL E  1 29  ? 28.067  -26.183 43.621  1.00 29.83 ? 29   VAL E C   1 
ATOM   4670  O  O   . VAL E  1 29  ? 27.516  -26.539 42.590  1.00 32.49 ? 29   VAL E O   1 
ATOM   4671  C  CB  . VAL E  1 29  ? 26.168  -25.278 44.985  1.00 29.90 ? 29   VAL E CB  1 
ATOM   4672  C  CG1 . VAL E  1 29  ? 26.216  -26.514 45.882  1.00 27.48 ? 29   VAL E CG1 1 
ATOM   4673  C  CG2 . VAL E  1 29  ? 25.639  -24.071 45.749  1.00 30.39 ? 29   VAL E CG2 1 
ATOM   4674  N  N   . LYS E  1 30  ? 29.132  -26.804 44.106  1.00 30.54 ? 30   LYS E N   1 
ATOM   4675  C  CA  . LYS E  1 30  ? 29.637  -28.048 43.533  1.00 28.06 ? 30   LYS E CA  1 
ATOM   4676  C  C   . LYS E  1 30  ? 28.869  -29.221 44.149  1.00 28.47 ? 30   LYS E C   1 
ATOM   4677  O  O   . LYS E  1 30  ? 28.691  -29.286 45.363  1.00 29.88 ? 30   LYS E O   1 
ATOM   4678  C  CB  . LYS E  1 30  ? 31.149  -28.170 43.802  1.00 31.00 ? 30   LYS E CB  1 
ATOM   4679  C  CG  . LYS E  1 30  ? 31.785  -29.532 43.476  1.00 36.60 ? 30   LYS E CG  1 
ATOM   4680  C  CD  . LYS E  1 30  ? 33.264  -29.615 43.956  1.00 42.93 ? 30   LYS E CD  1 
ATOM   4681  C  CE  . LYS E  1 30  ? 33.968  -30.910 43.485  1.00 40.05 ? 30   LYS E CE  1 
ATOM   4682  N  NZ  . LYS E  1 30  ? 35.206  -31.262 44.262  1.00 33.27 ? 30   LYS E NZ  1 
ATOM   4683  N  N   . VAL E  1 31  ? 28.391  -30.132 43.311  1.00 28.20 ? 31   VAL E N   1 
ATOM   4684  C  CA  . VAL E  1 31  ? 27.681  -31.317 43.775  1.00 24.51 ? 31   VAL E CA  1 
ATOM   4685  C  C   . VAL E  1 31  ? 28.384  -32.547 43.234  1.00 25.86 ? 31   VAL E C   1 
ATOM   4686  O  O   . VAL E  1 31  ? 28.626  -32.632 42.043  1.00 29.48 ? 31   VAL E O   1 
ATOM   4687  C  CB  . VAL E  1 31  ? 26.260  -31.339 43.234  1.00 25.17 ? 31   VAL E CB  1 
ATOM   4688  C  CG1 . VAL E  1 31  ? 25.516  -32.558 43.766  1.00 21.75 ? 31   VAL E CG1 1 
ATOM   4689  C  CG2 . VAL E  1 31  ? 25.545  -30.034 43.567  1.00 23.54 ? 31   VAL E CG2 1 
ATOM   4690  N  N   . TRP E  1 32  ? 28.722  -33.503 44.087  1.00 23.49 ? 32   TRP E N   1 
ATOM   4691  C  CA  . TRP E  1 32  ? 29.472  -34.655 43.609  1.00 23.19 ? 32   TRP E CA  1 
ATOM   4692  C  C   . TRP E  1 32  ? 29.330  -35.840 44.539  1.00 22.93 ? 32   TRP E C   1 
ATOM   4693  O  O   . TRP E  1 32  ? 29.022  -35.676 45.706  1.00 24.43 ? 32   TRP E O   1 
ATOM   4694  C  CB  . TRP E  1 32  ? 30.951  -34.296 43.439  1.00 23.77 ? 32   TRP E CB  1 
ATOM   4695  C  CG  . TRP E  1 32  ? 31.769  -34.374 44.695  1.00 24.56 ? 32   TRP E CG  1 
ATOM   4696  C  CD1 . TRP E  1 32  ? 32.501  -35.447 45.135  1.00 27.05 ? 32   TRP E CD1 1 
ATOM   4697  C  CD2 . TRP E  1 32  ? 31.957  -33.336 45.668  1.00 25.55 ? 32   TRP E CD2 1 
ATOM   4698  N  NE1 . TRP E  1 32  ? 33.125  -35.140 46.327  1.00 28.55 ? 32   TRP E NE1 1 
ATOM   4699  C  CE2 . TRP E  1 32  ? 32.807  -33.852 46.674  1.00 27.27 ? 32   TRP E CE2 1 
ATOM   4700  C  CE3 . TRP E  1 32  ? 31.483  -32.025 45.790  1.00 27.65 ? 32   TRP E CE3 1 
ATOM   4701  C  CZ2 . TRP E  1 32  ? 33.189  -33.101 47.795  1.00 32.54 ? 32   TRP E CZ2 1 
ATOM   4702  C  CZ3 . TRP E  1 32  ? 31.863  -31.277 46.906  1.00 31.10 ? 32   TRP E CZ3 1 
ATOM   4703  C  CH2 . TRP E  1 32  ? 32.710  -31.819 47.894  1.00 32.19 ? 32   TRP E CH2 1 
ATOM   4704  N  N   . GLY E  1 33  ? 29.560  -37.036 44.023  1.00 21.15 ? 33   GLY E N   1 
ATOM   4705  C  CA  . GLY E  1 33  ? 29.450  -38.228 44.828  1.00 21.72 ? 33   GLY E CA  1 
ATOM   4706  C  C   . GLY E  1 33  ? 29.249  -39.447 43.967  1.00 24.08 ? 33   GLY E C   1 
ATOM   4707  O  O   . GLY E  1 33  ? 29.638  -39.464 42.810  1.00 27.40 ? 33   GLY E O   1 
ATOM   4708  N  N   . SER E  1 34  ? 28.633  -40.474 44.530  1.00 25.49 ? 34   SER E N   1 
ATOM   4709  C  CA  . SER E  1 34  ? 28.427  -41.709 43.795  1.00 27.69 ? 34   SER E CA  1 
ATOM   4710  C  C   . SER E  1 34  ? 27.098  -42.344 44.188  1.00 29.45 ? 34   SER E C   1 
ATOM   4711  O  O   . SER E  1 34  ? 26.733  -42.341 45.360  1.00 32.45 ? 34   SER E O   1 
ATOM   4712  C  CB  . SER E  1 34  ? 29.573  -42.669 44.084  1.00 26.78 ? 34   SER E CB  1 
ATOM   4713  O  OG  . SER E  1 34  ? 29.744  -43.590 43.025  1.00 33.12 ? 34   SER E OG  1 
ATOM   4714  N  N   . ILE E  1 35  ? 26.365  -42.858 43.205  1.00 28.50 ? 35   ILE E N   1 
ATOM   4715  C  CA  . ILE E  1 35  ? 25.169  -43.655 43.453  1.00 27.30 ? 35   ILE E CA  1 
ATOM   4716  C  C   . ILE E  1 35  ? 25.391  -45.057 42.865  1.00 29.53 ? 35   ILE E C   1 
ATOM   4717  O  O   . ILE E  1 35  ? 26.101  -45.206 41.878  1.00 33.38 ? 35   ILE E O   1 
ATOM   4718  C  CB  . ILE E  1 35  ? 23.910  -43.011 42.821  1.00 25.61 ? 35   ILE E CB  1 
ATOM   4719  C  CG1 . ILE E  1 35  ? 23.805  -41.536 43.212  1.00 26.34 ? 35   ILE E CG1 1 
ATOM   4720  C  CG2 . ILE E  1 35  ? 22.655  -43.776 43.217  1.00 24.65 ? 35   ILE E CG2 1 
ATOM   4721  C  CD1 . ILE E  1 35  ? 22.577  -40.828 42.649  1.00 23.13 ? 35   ILE E CD1 1 
ATOM   4722  N  N   . LYS E  1 36  ? 24.802  -46.080 43.473  1.00 28.69 ? 36   LYS E N   1 
ATOM   4723  C  CA  . LYS E  1 36  ? 24.890  -47.442 42.947  1.00 31.03 ? 36   LYS E CA  1 
ATOM   4724  C  C   . LYS E  1 36  ? 23.536  -48.153 43.058  1.00 33.65 ? 36   LYS E C   1 
ATOM   4725  O  O   . LYS E  1 36  ? 22.587  -47.601 43.616  1.00 33.49 ? 36   LYS E O   1 
ATOM   4726  C  CB  . LYS E  1 36  ? 26.017  -48.242 43.626  1.00 33.81 ? 36   LYS E CB  1 
ATOM   4727  C  CG  . LYS E  1 36  ? 25.822  -48.541 45.121  1.00 39.70 ? 36   LYS E CG  1 
ATOM   4728  C  CD  . LYS E  1 36  ? 26.930  -49.466 45.641  1.00 43.12 ? 36   LYS E CD  1 
ATOM   4729  C  CE  . LYS E  1 36  ? 26.474  -50.294 46.838  1.00 48.18 ? 36   LYS E CE  1 
ATOM   4730  N  NZ  . LYS E  1 36  ? 27.461  -51.366 47.182  1.00 49.80 ? 36   LYS E NZ  1 
ATOM   4731  N  N   . GLY E  1 37  ? 23.443  -49.359 42.502  1.00 35.32 ? 37   GLY E N   1 
ATOM   4732  C  CA  . GLY E  1 37  ? 22.186  -50.090 42.451  1.00 33.68 ? 37   GLY E CA  1 
ATOM   4733  C  C   . GLY E  1 37  ? 21.236  -49.610 41.358  1.00 35.46 ? 37   GLY E C   1 
ATOM   4734  O  O   . GLY E  1 37  ? 20.122  -50.122 41.215  1.00 35.24 ? 37   GLY E O   1 
ATOM   4735  N  N   . LEU E  1 38  ? 21.675  -48.619 40.588  1.00 35.34 ? 38   LEU E N   1 
ATOM   4736  C  CA  . LEU E  1 38  ? 20.860  -48.046 39.518  1.00 36.62 ? 38   LEU E CA  1 
ATOM   4737  C  C   . LEU E  1 38  ? 20.962  -48.848 38.212  1.00 38.90 ? 38   LEU E C   1 
ATOM   4738  O  O   . LEU E  1 38  ? 21.969  -49.512 37.941  1.00 37.69 ? 38   LEU E O   1 
ATOM   4739  C  CB  . LEU E  1 38  ? 21.270  -46.592 39.239  1.00 34.15 ? 38   LEU E CB  1 
ATOM   4740  C  CG  . LEU E  1 38  ? 20.969  -45.473 40.236  1.00 29.64 ? 38   LEU E CG  1 
ATOM   4741  C  CD1 . LEU E  1 38  ? 21.834  -44.267 39.926  1.00 28.77 ? 38   LEU E CD1 1 
ATOM   4742  C  CD2 . LEU E  1 38  ? 19.509  -45.094 40.196  1.00 27.98 ? 38   LEU E CD2 1 
ATOM   4743  N  N   . THR E  1 39  ? 19.908  -48.775 37.406  1.00 38.05 ? 39   THR E N   1 
ATOM   4744  C  CA  . THR E  1 39  ? 19.916  -49.347 36.071  1.00 36.19 ? 39   THR E CA  1 
ATOM   4745  C  C   . THR E  1 39  ? 20.803  -48.486 35.169  1.00 39.38 ? 39   THR E C   1 
ATOM   4746  O  O   . THR E  1 39  ? 20.932  -47.279 35.389  1.00 38.72 ? 39   THR E O   1 
ATOM   4747  C  CB  . THR E  1 39  ? 18.498  -49.381 35.497  1.00 35.91 ? 39   THR E CB  1 
ATOM   4748  O  OG1 . THR E  1 39  ? 17.882  -48.105 35.709  1.00 37.40 ? 39   THR E OG1 1 
ATOM   4749  C  CG2 . THR E  1 39  ? 17.668  -50.460 36.182  1.00 29.89 ? 39   THR E CG2 1 
ATOM   4750  N  N   . GLU E  1 40  ? 21.414  -49.101 34.160  1.00 37.81 ? 40   GLU E N   1 
ATOM   4751  C  CA  . GLU E  1 40  ? 22.362  -48.393 33.307  1.00 36.42 ? 40   GLU E CA  1 
ATOM   4752  C  C   . GLU E  1 40  ? 21.666  -47.313 32.468  1.00 38.27 ? 40   GLU E C   1 
ATOM   4753  O  O   . GLU E  1 40  ? 20.613  -47.557 31.872  1.00 39.47 ? 40   GLU E O   1 
ATOM   4754  C  CB  . GLU E  1 40  ? 23.103  -49.379 32.403  1.00 39.02 ? 40   GLU E CB  1 
ATOM   4755  C  CG  . GLU E  1 40  ? 24.006  -48.697 31.386  1.00 43.71 ? 40   GLU E CG  1 
ATOM   4756  C  CD  . GLU E  1 40  ? 24.704  -49.667 30.448  1.00 47.51 ? 40   GLU E CD  1 
ATOM   4757  O  OE1 . GLU E  1 40  ? 24.311  -50.858 30.404  1.00 46.73 ? 40   GLU E OE1 1 
ATOM   4758  O  OE2 . GLU E  1 40  ? 25.649  -49.223 29.754  1.00 49.09 ? 40   GLU E OE2 1 
ATOM   4759  N  N   . GLY E  1 41  ? 22.242  -46.116 32.426  1.00 33.00 ? 41   GLY E N   1 
ATOM   4760  C  CA  . GLY E  1 41  ? 21.652  -45.044 31.644  1.00 35.61 ? 41   GLY E CA  1 
ATOM   4761  C  C   . GLY E  1 41  ? 21.423  -43.768 32.428  1.00 33.30 ? 41   GLY E C   1 
ATOM   4762  O  O   . GLY E  1 41  ? 22.051  -43.551 33.456  1.00 32.12 ? 41   GLY E O   1 
ATOM   4763  N  N   . LEU E  1 42  ? 20.518  -42.924 31.941  1.00 36.08 ? 42   LEU E N   1 
ATOM   4764  C  CA  . LEU E  1 42  ? 20.255  -41.626 32.571  1.00 35.24 ? 42   LEU E CA  1 
ATOM   4765  C  C   . LEU E  1 42  ? 19.099  -41.650 33.576  1.00 34.08 ? 42   LEU E C   1 
ATOM   4766  O  O   . LEU E  1 42  ? 18.031  -42.195 33.294  1.00 35.37 ? 42   LEU E O   1 
ATOM   4767  C  CB  . LEU E  1 42  ? 19.985  -40.555 31.513  1.00 33.23 ? 42   LEU E CB  1 
ATOM   4768  C  CG  . LEU E  1 42  ? 21.152  -40.108 30.633  1.00 32.66 ? 42   LEU E CG  1 
ATOM   4769  C  CD1 . LEU E  1 42  ? 20.621  -39.465 29.356  1.00 36.46 ? 42   LEU E CD1 1 
ATOM   4770  C  CD2 . LEU E  1 42  ? 22.056  -39.151 31.378  1.00 29.74 ? 42   LEU E CD2 1 
ATOM   4771  N  N   . HIS E  1 43  ? 19.326  -41.043 34.741  1.00 35.00 ? 43   HIS E N   1 
ATOM   4772  C  CA  . HIS E  1 43  ? 18.330  -40.979 35.811  1.00 32.93 ? 43   HIS E CA  1 
ATOM   4773  C  C   . HIS E  1 43  ? 18.111  -39.552 36.292  1.00 29.16 ? 43   HIS E C   1 
ATOM   4774  O  O   . HIS E  1 43  ? 19.068  -38.836 36.559  1.00 28.78 ? 43   HIS E O   1 
ATOM   4775  C  CB  . HIS E  1 43  ? 18.768  -41.854 36.981  1.00 28.21 ? 43   HIS E CB  1 
ATOM   4776  C  CG  . HIS E  1 43  ? 18.705  -43.317 36.685  1.00 30.27 ? 43   HIS E CG  1 
ATOM   4777  N  ND1 . HIS E  1 43  ? 17.548  -44.051 36.827  1.00 29.56 ? 43   HIS E ND1 1 
ATOM   4778  C  CD2 . HIS E  1 43  ? 19.647  -44.179 36.238  1.00 29.13 ? 43   HIS E CD2 1 
ATOM   4779  C  CE1 . HIS E  1 43  ? 17.782  -45.306 36.487  1.00 30.52 ? 43   HIS E CE1 1 
ATOM   4780  N  NE2 . HIS E  1 43  ? 19.048  -45.410 36.128  1.00 31.30 ? 43   HIS E NE2 1 
ATOM   4781  N  N   . GLY E  1 44  ? 16.850  -39.147 36.400  1.00 29.34 ? 44   GLY E N   1 
ATOM   4782  C  CA  . GLY E  1 44  ? 16.515  -37.835 36.922  1.00 29.03 ? 44   GLY E CA  1 
ATOM   4783  C  C   . GLY E  1 44  ? 17.119  -37.578 38.294  1.00 27.53 ? 44   GLY E C   1 
ATOM   4784  O  O   . GLY E  1 44  ? 17.130  -38.451 39.162  1.00 26.14 ? 44   GLY E O   1 
ATOM   4785  N  N   . PHE E  1 45  ? 17.614  -36.361 38.484  1.00 27.15 ? 45   PHE E N   1 
ATOM   4786  C  CA  . PHE E  1 45  ? 18.354  -35.998 39.682  1.00 26.63 ? 45   PHE E CA  1 
ATOM   4787  C  C   . PHE E  1 45  ? 17.917  -34.605 40.118  1.00 28.11 ? 45   PHE E C   1 
ATOM   4788  O  O   . PHE E  1 45  ? 18.398  -33.608 39.580  1.00 25.75 ? 45   PHE E O   1 
ATOM   4789  C  CB  . PHE E  1 45  ? 19.864  -36.032 39.393  1.00 26.27 ? 45   PHE E CB  1 
ATOM   4790  C  CG  . PHE E  1 45  ? 20.736  -36.038 40.631  1.00 29.60 ? 45   PHE E CG  1 
ATOM   4791  C  CD1 . PHE E  1 45  ? 20.731  -37.120 41.505  1.00 27.40 ? 45   PHE E CD1 1 
ATOM   4792  C  CD2 . PHE E  1 45  ? 21.584  -34.966 40.909  1.00 28.94 ? 45   PHE E CD2 1 
ATOM   4793  C  CE1 . PHE E  1 45  ? 21.544  -37.121 42.639  1.00 26.61 ? 45   PHE E CE1 1 
ATOM   4794  C  CE2 . PHE E  1 45  ? 22.403  -34.973 42.044  1.00 23.77 ? 45   PHE E CE2 1 
ATOM   4795  C  CZ  . PHE E  1 45  ? 22.382  -36.049 42.896  1.00 23.18 ? 45   PHE E CZ  1 
ATOM   4796  N  N   . HIS E  1 46  ? 17.000  -34.535 41.087  1.00 28.58 ? 46   HIS E N   1 
ATOM   4797  C  CA  . HIS E  1 46  ? 16.444  -33.247 41.489  1.00 26.61 ? 46   HIS E CA  1 
ATOM   4798  C  C   . HIS E  1 46  ? 16.348  -33.020 42.996  1.00 26.87 ? 46   HIS E C   1 
ATOM   4799  O  O   . HIS E  1 46  ? 16.179  -33.957 43.773  1.00 27.90 ? 46   HIS E O   1 
ATOM   4800  C  CB  . HIS E  1 46  ? 15.056  -33.045 40.881  1.00 25.19 ? 46   HIS E CB  1 
ATOM   4801  C  CG  . HIS E  1 46  ? 14.860  -33.721 39.561  1.00 28.23 ? 46   HIS E CG  1 
ATOM   4802  N  ND1 . HIS E  1 46  ? 14.222  -34.937 39.436  1.00 27.81 ? 46   HIS E ND1 1 
ATOM   4803  C  CD2 . HIS E  1 46  ? 15.190  -33.339 38.304  1.00 28.86 ? 46   HIS E CD2 1 
ATOM   4804  C  CE1 . HIS E  1 46  ? 14.184  -35.283 38.162  1.00 29.15 ? 46   HIS E CE1 1 
ATOM   4805  N  NE2 . HIS E  1 46  ? 14.764  -34.331 37.454  1.00 27.44 ? 46   HIS E NE2 1 
ATOM   4806  N  N   . VAL E  1 47  ? 16.436  -31.749 43.384  1.00 26.31 ? 47   VAL E N   1 
ATOM   4807  C  CA  . VAL E  1 47  ? 16.116  -31.306 44.736  1.00 28.28 ? 47   VAL E CA  1 
ATOM   4808  C  C   . VAL E  1 47  ? 14.604  -31.119 44.877  1.00 29.12 ? 47   VAL E C   1 
ATOM   4809  O  O   . VAL E  1 47  ? 13.988  -30.347 44.133  1.00 27.56 ? 47   VAL E O   1 
ATOM   4810  C  CB  . VAL E  1 47  ? 16.833  -29.975 45.091  1.00 26.73 ? 47   VAL E CB  1 
ATOM   4811  C  CG1 . VAL E  1 47  ? 16.652  -29.644 46.564  1.00 25.22 ? 47   VAL E CG1 1 
ATOM   4812  C  CG2 . VAL E  1 47  ? 18.322  -30.062 44.745  1.00 27.27 ? 47   VAL E CG2 1 
ATOM   4813  N  N   . HIS E  1 48  ? 14.018  -31.849 45.829  1.00 31.21 ? 48   HIS E N   1 
ATOM   4814  C  CA  . HIS E  1 48  ? 12.600  -31.735 46.178  1.00 28.09 ? 48   HIS E CA  1 
ATOM   4815  C  C   . HIS E  1 48  ? 12.428  -30.908 47.458  1.00 29.09 ? 48   HIS E C   1 
ATOM   4816  O  O   . HIS E  1 48  ? 13.315  -30.894 48.323  1.00 28.82 ? 48   HIS E O   1 
ATOM   4817  C  CB  . HIS E  1 48  ? 11.981  -33.118 46.373  1.00 28.70 ? 48   HIS E CB  1 
ATOM   4818  C  CG  . HIS E  1 48  ? 11.833  -33.905 45.110  1.00 27.38 ? 48   HIS E CG  1 
ATOM   4819  N  ND1 . HIS E  1 48  ? 10.605  -34.277 44.605  1.00 29.70 ? 48   HIS E ND1 1 
ATOM   4820  C  CD2 . HIS E  1 48  ? 12.755  -34.393 44.248  1.00 26.69 ? 48   HIS E CD2 1 
ATOM   4821  C  CE1 . HIS E  1 48  ? 10.779  -34.966 43.492  1.00 29.10 ? 48   HIS E CE1 1 
ATOM   4822  N  NE2 . HIS E  1 48  ? 12.074  -35.055 43.255  1.00 26.98 ? 48   HIS E NE2 1 
ATOM   4823  N  N   . GLU E  1 49  ? 11.267  -30.265 47.583  1.00 25.73 ? 49   GLU E N   1 
ATOM   4824  C  CA  . GLU E  1 49  ? 11.039  -29.171 48.532  1.00 30.65 ? 49   GLU E CA  1 
ATOM   4825  C  C   . GLU E  1 49  ? 11.156  -29.445 50.055  1.00 30.82 ? 49   GLU E C   1 
ATOM   4826  O  O   . GLU E  1 49  ? 11.597  -28.577 50.823  1.00 29.29 ? 49   GLU E O   1 
ATOM   4827  C  CB  . GLU E  1 49  ? 9.671   -28.545 48.250  1.00 30.15 ? 49   GLU E CB  1 
ATOM   4828  C  CG  . GLU E  1 49  ? 9.347   -27.381 49.159  1.00 30.06 ? 49   GLU E CG  1 
ATOM   4829  C  CD  . GLU E  1 49  ? 8.023   -26.752 48.827  1.00 32.70 ? 49   GLU E CD  1 
ATOM   4830  O  OE1 . GLU E  1 49  ? 7.203   -27.429 48.163  1.00 32.00 ? 49   GLU E OE1 1 
ATOM   4831  O  OE2 . GLU E  1 49  ? 7.812   -25.584 49.227  1.00 33.45 ? 49   GLU E OE2 1 
ATOM   4832  N  N   . PHE E  1 50  ? 10.728  -30.625 50.494  1.00 29.39 ? 50   PHE E N   1 
ATOM   4833  C  CA  . PHE E  1 50  ? 10.647  -30.913 51.920  1.00 26.89 ? 50   PHE E CA  1 
ATOM   4834  C  C   . PHE E  1 50  ? 11.619  -32.013 52.305  1.00 26.65 ? 50   PHE E C   1 
ATOM   4835  O  O   . PHE E  1 50  ? 11.714  -33.026 51.627  1.00 28.01 ? 50   PHE E O   1 
ATOM   4836  C  CB  . PHE E  1 50  ? 9.223   -31.344 52.306  1.00 29.62 ? 50   PHE E CB  1 
ATOM   4837  C  CG  . PHE E  1 50  ? 8.148   -30.363 51.901  1.00 32.07 ? 50   PHE E CG  1 
ATOM   4838  C  CD1 . PHE E  1 50  ? 8.164   -29.053 52.372  1.00 31.95 ? 50   PHE E CD1 1 
ATOM   4839  C  CD2 . PHE E  1 50  ? 7.111   -30.756 51.063  1.00 32.68 ? 50   PHE E CD2 1 
ATOM   4840  C  CE1 . PHE E  1 50  ? 7.171   -28.150 52.008  1.00 32.60 ? 50   PHE E CE1 1 
ATOM   4841  C  CE2 . PHE E  1 50  ? 6.117   -29.860 50.692  1.00 32.93 ? 50   PHE E CE2 1 
ATOM   4842  C  CZ  . PHE E  1 50  ? 6.148   -28.554 51.165  1.00 32.57 ? 50   PHE E CZ  1 
ATOM   4843  N  N   . GLY E  1 51  ? 12.332  -31.822 53.406  1.00 26.31 ? 51   GLY E N   1 
ATOM   4844  C  CA  . GLY E  1 51  ? 13.133  -32.889 53.978  1.00 27.17 ? 51   GLY E CA  1 
ATOM   4845  C  C   . GLY E  1 51  ? 12.282  -33.766 54.882  1.00 27.75 ? 51   GLY E C   1 
ATOM   4846  O  O   . GLY E  1 51  ? 12.594  -33.960 56.062  1.00 25.70 ? 51   GLY E O   1 
ATOM   4847  N  N   . ASP E  1 52  ? 11.199  -34.290 54.311  1.00 28.72 ? 52   ASP E N   1 
ATOM   4848  C  CA  . ASP E  1 52  ? 10.236  -35.122 55.021  1.00 28.15 ? 52   ASP E CA  1 
ATOM   4849  C  C   . ASP E  1 52  ? 10.259  -36.525 54.426  1.00 28.84 ? 52   ASP E C   1 
ATOM   4850  O  O   . ASP E  1 52  ? 10.007  -36.712 53.236  1.00 29.93 ? 52   ASP E O   1 
ATOM   4851  C  CB  . ASP E  1 52  ? 8.834   -34.507 54.896  1.00 30.55 ? 52   ASP E CB  1 
ATOM   4852  C  CG  . ASP E  1 52  ? 7.796   -35.191 55.789  1.00 31.31 ? 52   ASP E CG  1 
ATOM   4853  O  OD1 . ASP E  1 52  ? 7.950   -36.393 56.100  1.00 32.93 ? 52   ASP E OD1 1 
ATOM   4854  O  OD2 . ASP E  1 52  ? 6.812   -34.522 56.170  1.00 31.71 ? 52   ASP E OD2 1 
ATOM   4855  N  N   . ASN E  1 53  ? 10.573  -37.513 55.255  1.00 27.61 ? 53   ASN E N   1 
ATOM   4856  C  CA  . ASN E  1 53  ? 10.711  -38.882 54.784  1.00 27.44 ? 53   ASN E CA  1 
ATOM   4857  C  C   . ASN E  1 53  ? 9.753   -39.786 55.525  1.00 29.20 ? 53   ASN E C   1 
ATOM   4858  O  O   . ASN E  1 53  ? 9.925   -41.011 55.546  1.00 30.23 ? 53   ASN E O   1 
ATOM   4859  C  CB  . ASN E  1 53  ? 12.147  -39.367 54.996  1.00 32.22 ? 53   ASN E CB  1 
ATOM   4860  C  CG  . ASN E  1 53  ? 12.489  -40.599 54.167  1.00 34.75 ? 53   ASN E CG  1 
ATOM   4861  O  OD1 . ASN E  1 53  ? 12.225  -40.653 52.962  1.00 33.29 ? 53   ASN E OD1 1 
ATOM   4862  N  ND2 . ASN E  1 53  ? 13.110  -41.583 54.809  1.00 32.55 ? 53   ASN E ND2 1 
ATOM   4863  N  N   . THR E  1 54  ? 8.738   -39.176 56.133  1.00 29.00 ? 54   THR E N   1 
ATOM   4864  C  CA  . THR E  1 54  ? 7.795   -39.919 56.964  1.00 30.92 ? 54   THR E CA  1 
ATOM   4865  C  C   . THR E  1 54  ? 7.147   -41.047 56.177  1.00 31.84 ? 54   THR E C   1 
ATOM   4866  O  O   . THR E  1 54  ? 7.098   -42.186 56.637  1.00 34.00 ? 54   THR E O   1 
ATOM   4867  C  CB  . THR E  1 54  ? 6.731   -39.000 57.572  1.00 29.40 ? 54   THR E CB  1 
ATOM   4868  O  OG1 . THR E  1 54  ? 6.103   -38.245 56.533  1.00 33.58 ? 54   THR E OG1 1 
ATOM   4869  C  CG2 . THR E  1 54  ? 7.376   -38.036 58.559  1.00 31.39 ? 54   THR E CG2 1 
ATOM   4870  N  N   . ALA E  1 55  ? 6.682   -40.727 54.972  1.00 32.42 ? 55   ALA E N   1 
ATOM   4871  C  CA  . ALA E  1 55  ? 6.071   -41.713 54.088  1.00 32.24 ? 55   ALA E CA  1 
ATOM   4872  C  C   . ALA E  1 55  ? 6.936   -41.997 52.858  1.00 33.88 ? 55   ALA E C   1 
ATOM   4873  O  O   . ALA E  1 55  ? 6.473   -41.860 51.728  1.00 38.32 ? 55   ALA E O   1 
ATOM   4874  C  CB  . ALA E  1 55  ? 4.692   -41.237 53.660  1.00 30.66 ? 55   ALA E CB  1 
ATOM   4875  N  N   . GLY E  1 56  ? 8.185   -42.396 53.076  1.00 34.42 ? 56   GLY E N   1 
ATOM   4876  C  CA  . GLY E  1 56  ? 9.110   -42.656 51.985  1.00 32.02 ? 56   GLY E CA  1 
ATOM   4877  C  C   . GLY E  1 56  ? 9.502   -41.391 51.235  1.00 35.15 ? 56   GLY E C   1 
ATOM   4878  O  O   . GLY E  1 56  ? 9.477   -40.291 51.799  1.00 33.08 ? 56   GLY E O   1 
ATOM   4879  N  N   . CYS E  1 57  ? 9.857   -41.541 49.959  1.00 32.38 ? 57   CYS E N   1 
ATOM   4880  C  CA  . CYS E  1 57  ? 10.313  -40.407 49.165  1.00 32.71 ? 57   CYS E CA  1 
ATOM   4881  C  C   . CYS E  1 57  ? 9.152   -39.509 48.769  1.00 32.75 ? 57   CYS E C   1 
ATOM   4882  O  O   . CYS E  1 57  ? 9.336   -38.319 48.511  1.00 32.81 ? 57   CYS E O   1 
ATOM   4883  C  CB  . CYS E  1 57  ? 11.048  -40.886 47.915  1.00 33.90 ? 57   CYS E CB  1 
ATOM   4884  S  SG  . CYS E  1 57  ? 12.405  -42.038 48.234  1.00 39.24 ? 57   CYS E SG  1 
ATOM   4885  N  N   . THR E  1 58  ? 7.959   -40.093 48.723  1.00 34.27 ? 58   THR E N   1 
ATOM   4886  C  CA  . THR E  1 58  ? 6.745   -39.374 48.347  1.00 33.53 ? 58   THR E CA  1 
ATOM   4887  C  C   . THR E  1 58  ? 6.545   -38.092 49.148  1.00 34.05 ? 58   THR E C   1 
ATOM   4888  O  O   . THR E  1 58  ? 6.065   -37.089 48.607  1.00 34.56 ? 58   THR E O   1 
ATOM   4889  C  CB  . THR E  1 58  ? 5.488   -40.254 48.523  1.00 35.57 ? 58   THR E CB  1 
ATOM   4890  O  OG1 . THR E  1 58  ? 5.641   -41.480 47.792  1.00 36.98 ? 58   THR E OG1 1 
ATOM   4891  C  CG2 . THR E  1 58  ? 4.241   -39.513 48.033  1.00 34.59 ? 58   THR E CG2 1 
ATOM   4892  N  N   . SER E  1 59  ? 6.906   -38.123 50.434  1.00 33.74 ? 59   SER E N   1 
ATOM   4893  C  CA  . SER E  1 59  ? 6.697   -36.962 51.306  1.00 31.24 ? 59   SER E CA  1 
ATOM   4894  C  C   . SER E  1 59  ? 7.644   -35.793 51.017  1.00 30.53 ? 59   SER E C   1 
ATOM   4895  O  O   . SER E  1 59  ? 7.442   -34.690 51.519  1.00 33.07 ? 59   SER E O   1 
ATOM   4896  C  CB  . SER E  1 59  ? 6.703   -37.346 52.795  1.00 29.59 ? 59   SER E CB  1 
ATOM   4897  O  OG  . SER E  1 59  ? 7.122   -38.684 52.996  1.00 29.89 ? 59   SER E OG  1 
ATOM   4898  N  N   . ALA E  1 60  ? 8.644   -36.026 50.173  1.00 31.03 ? 60   ALA E N   1 
ATOM   4899  C  CA  . ALA E  1 60  ? 9.573   -34.972 49.779  1.00 28.74 ? 60   ALA E CA  1 
ATOM   4900  C  C   . ALA E  1 60  ? 8.873   -33.850 49.021  1.00 29.52 ? 60   ALA E C   1 
ATOM   4901  O  O   . ALA E  1 60  ? 9.396   -32.746 48.910  1.00 29.07 ? 60   ALA E O   1 
ATOM   4902  C  CB  . ALA E  1 60  ? 10.706  -35.547 48.947  1.00 29.31 ? 60   ALA E CB  1 
ATOM   4903  N  N   . GLY E  1 61  ? 7.689   -34.132 48.496  1.00 29.70 ? 61   GLY E N   1 
ATOM   4904  C  CA  . GLY E  1 61  ? 6.941   -33.130 47.760  1.00 31.66 ? 61   GLY E CA  1 
ATOM   4905  C  C   . GLY E  1 61  ? 7.460   -32.986 46.345  1.00 31.38 ? 61   GLY E C   1 
ATOM   4906  O  O   . GLY E  1 61  ? 8.075   -33.921 45.823  1.00 29.16 ? 61   GLY E O   1 
ATOM   4907  N  N   . PRO E  1 62  ? 7.229   -31.805 45.729  1.00 33.33 ? 62   PRO E N   1 
ATOM   4908  C  CA  . PRO E  1 62  ? 7.572   -31.490 44.331  1.00 32.56 ? 62   PRO E CA  1 
ATOM   4909  C  C   . PRO E  1 62  ? 9.036   -31.109 44.181  1.00 30.47 ? 62   PRO E C   1 
ATOM   4910  O  O   . PRO E  1 62  ? 9.737   -30.945 45.177  1.00 30.29 ? 62   PRO E O   1 
ATOM   4911  C  CB  . PRO E  1 62  ? 6.725   -30.241 44.021  1.00 30.82 ? 62   PRO E CB  1 
ATOM   4912  C  CG  . PRO E  1 62  ? 6.032   -29.855 45.307  1.00 30.53 ? 62   PRO E CG  1 
ATOM   4913  C  CD  . PRO E  1 62  ? 6.674   -30.633 46.427  1.00 30.46 ? 62   PRO E CD  1 
ATOM   4914  N  N   . HIS E  1 63  ? 9.490   -30.958 42.944  1.00 28.98 ? 63   HIS E N   1 
ATOM   4915  C  CA  . HIS E  1 63  ? 10.791  -30.356 42.712  1.00 28.63 ? 63   HIS E CA  1 
ATOM   4916  C  C   . HIS E  1 63  ? 10.754  -28.974 43.385  1.00 31.13 ? 63   HIS E C   1 
ATOM   4917  O  O   . HIS E  1 63  ? 9.797   -28.214 43.216  1.00 29.91 ? 63   HIS E O   1 
ATOM   4918  C  CB  . HIS E  1 63  ? 11.090  -30.247 41.204  1.00 31.70 ? 63   HIS E CB  1 
ATOM   4919  C  CG  . HIS E  1 63  ? 11.170  -31.572 40.489  1.00 30.32 ? 63   HIS E CG  1 
ATOM   4920  N  ND1 . HIS E  1 63  ? 11.570  -31.685 39.174  1.00 27.34 ? 63   HIS E ND1 1 
ATOM   4921  C  CD2 . HIS E  1 63  ? 10.908  -32.833 40.908  1.00 30.20 ? 63   HIS E CD2 1 
ATOM   4922  C  CE1 . HIS E  1 63  ? 11.540  -32.954 38.810  1.00 27.33 ? 63   HIS E CE1 1 
ATOM   4923  N  NE2 . HIS E  1 63  ? 11.146  -33.673 39.844  1.00 30.25 ? 63   HIS E NE2 1 
ATOM   4924  N  N   . PHE E  1 64  ? 11.775  -28.675 44.184  1.00 30.73 ? 64   PHE E N   1 
ATOM   4925  C  CA  . PHE E  1 64  ? 11.864  -27.393 44.870  1.00 30.60 ? 64   PHE E CA  1 
ATOM   4926  C  C   . PHE E  1 64  ? 11.670  -26.264 43.849  1.00 32.13 ? 64   PHE E C   1 
ATOM   4927  O  O   . PHE E  1 64  ? 12.406  -26.162 42.863  1.00 31.12 ? 64   PHE E O   1 
ATOM   4928  C  CB  . PHE E  1 64  ? 13.202  -27.292 45.618  1.00 29.68 ? 64   PHE E CB  1 
ATOM   4929  C  CG  . PHE E  1 64  ? 13.388  -26.013 46.405  1.00 30.15 ? 64   PHE E CG  1 
ATOM   4930  C  CD1 . PHE E  1 64  ? 12.361  -25.487 47.169  1.00 29.04 ? 64   PHE E CD1 1 
ATOM   4931  C  CD2 . PHE E  1 64  ? 14.616  -25.359 46.402  1.00 31.44 ? 64   PHE E CD2 1 
ATOM   4932  C  CE1 . PHE E  1 64  ? 12.553  -24.319 47.889  1.00 28.47 ? 64   PHE E CE1 1 
ATOM   4933  C  CE2 . PHE E  1 64  ? 14.811  -24.188 47.123  1.00 28.42 ? 64   PHE E CE2 1 
ATOM   4934  C  CZ  . PHE E  1 64  ? 13.783  -23.671 47.862  1.00 29.15 ? 64   PHE E CZ  1 
ATOM   4935  N  N   . ASN E  1 65  ? 10.658  -25.435 44.088  1.00 35.57 ? 65   ASN E N   1 
ATOM   4936  C  CA  . ASN E  1 65  ? 10.219  -24.423 43.132  1.00 35.39 ? 65   ASN E CA  1 
ATOM   4937  C  C   . ASN E  1 65  ? 9.683   -23.170 43.835  1.00 36.43 ? 65   ASN E C   1 
ATOM   4938  O  O   . ASN E  1 65  ? 8.491   -22.873 43.759  1.00 39.23 ? 65   ASN E O   1 
ATOM   4939  C  CB  . ASN E  1 65  ? 9.132   -25.017 42.226  1.00 34.56 ? 65   ASN E CB  1 
ATOM   4940  C  CG  . ASN E  1 65  ? 8.829   -24.150 41.010  1.00 33.44 ? 65   ASN E CG  1 
ATOM   4941  O  OD1 . ASN E  1 65  ? 9.678   -23.404 40.527  1.00 30.28 ? 65   ASN E OD1 1 
ATOM   4942  N  ND2 . ASN E  1 65  ? 7.611   -24.267 40.500  1.00 34.22 ? 65   ASN E ND2 1 
ATOM   4943  N  N   . PRO E  1 66  ? 10.566  -22.434 44.522  1.00 34.55 ? 66   PRO E N   1 
ATOM   4944  C  CA  . PRO E  1 66  ? 10.200  -21.222 45.268  1.00 35.18 ? 66   PRO E CA  1 
ATOM   4945  C  C   . PRO E  1 66  ? 9.850   -20.076 44.333  1.00 39.02 ? 66   PRO E C   1 
ATOM   4946  O  O   . PRO E  1 66  ? 9.313   -19.058 44.785  1.00 38.94 ? 66   PRO E O   1 
ATOM   4947  C  CB  . PRO E  1 66  ? 11.502  -20.871 46.000  1.00 34.71 ? 66   PRO E CB  1 
ATOM   4948  C  CG  . PRO E  1 66  ? 12.569  -21.441 45.113  1.00 35.78 ? 66   PRO E CG  1 
ATOM   4949  C  CD  . PRO E  1 66  ? 11.992  -22.759 44.690  1.00 32.97 ? 66   PRO E CD  1 
ATOM   4950  N  N   . LEU E  1 67  ? 10.170  -20.252 43.050  1.00 39.45 ? 67   LEU E N   1 
ATOM   4951  C  CA  . LEU E  1 67  ? 10.063  -19.199 42.035  1.00 39.21 ? 67   LEU E CA  1 
ATOM   4952  C  C   . LEU E  1 67  ? 8.925   -19.432 41.042  1.00 40.49 ? 67   LEU E C   1 
ATOM   4953  O  O   . LEU E  1 67  ? 8.688   -18.611 40.152  1.00 41.17 ? 67   LEU E O   1 
ATOM   4954  C  CB  . LEU E  1 67  ? 11.384  -19.055 41.274  1.00 37.96 ? 67   LEU E CB  1 
ATOM   4955  C  CG  . LEU E  1 67  ? 12.285  -17.859 41.589  1.00 41.38 ? 67   LEU E CG  1 
ATOM   4956  C  CD1 . LEU E  1 67  ? 12.461  -17.679 43.085  1.00 40.41 ? 67   LEU E CD1 1 
ATOM   4957  C  CD2 . LEU E  1 67  ? 13.637  -17.994 40.884  1.00 42.03 ? 67   LEU E CD2 1 
ATOM   4958  N  N   . SER E  1 68  ? 8.247   -20.567 41.178  1.00 38.82 ? 68   SER E N   1 
ATOM   4959  C  CA  . SER E  1 68  ? 6.984   -20.791 40.489  1.00 39.82 ? 68   SER E CA  1 
ATOM   4960  C  C   . SER E  1 68  ? 7.111   -20.843 38.960  1.00 43.03 ? 68   SER E C   1 
ATOM   4961  O  O   . SER E  1 68  ? 6.276   -20.305 38.218  1.00 42.86 ? 68   SER E O   1 
ATOM   4962  C  CB  . SER E  1 68  ? 5.986   -19.727 40.931  1.00 42.93 ? 68   SER E CB  1 
ATOM   4963  O  OG  . SER E  1 68  ? 5.960   -19.654 42.348  1.00 47.82 ? 68   SER E OG  1 
ATOM   4964  N  N   . ARG E  1 69  ? 8.158   -21.521 38.503  1.00 41.47 ? 69   ARG E N   1 
ATOM   4965  C  CA  . ARG E  1 69  ? 8.423   -21.672 37.086  1.00 38.45 ? 69   ARG E CA  1 
ATOM   4966  C  C   . ARG E  1 69  ? 8.167   -23.111 36.665  1.00 36.57 ? 69   ARG E C   1 
ATOM   4967  O  O   . ARG E  1 69  ? 7.672   -23.910 37.451  1.00 35.89 ? 69   ARG E O   1 
ATOM   4968  C  CB  . ARG E  1 69  ? 9.854   -21.238 36.777  1.00 39.06 ? 69   ARG E CB  1 
ATOM   4969  C  CG  . ARG E  1 69  ? 10.130  -19.823 37.266  1.00 41.88 ? 69   ARG E CG  1 
ATOM   4970  C  CD  . ARG E  1 69  ? 11.340  -19.197 36.621  1.00 48.23 ? 69   ARG E CD  1 
ATOM   4971  N  NE  . ARG E  1 69  ? 11.617  -17.886 37.199  1.00 52.59 ? 69   ARG E NE  1 
ATOM   4972  C  CZ  . ARG E  1 69  ? 12.778  -17.244 37.082  1.00 60.15 ? 69   ARG E CZ  1 
ATOM   4973  N  NH1 . ARG E  1 69  ? 13.780  -17.793 36.399  1.00 58.76 ? 69   ARG E NH1 1 
ATOM   4974  N  NH2 . ARG E  1 69  ? 12.936  -16.053 37.652  1.00 60.62 ? 69   ARG E NH2 1 
ATOM   4975  N  N   . LYS E  1 70  ? 8.483   -23.435 35.418  1.00 37.17 ? 70   LYS E N   1 
ATOM   4976  C  CA  . LYS E  1 70  ? 8.223   -24.770 34.913  1.00 37.93 ? 70   LYS E CA  1 
ATOM   4977  C  C   . LYS E  1 70  ? 9.509   -25.559 34.869  1.00 31.14 ? 70   LYS E C   1 
ATOM   4978  O  O   . LYS E  1 70  ? 10.588  -24.988 34.867  1.00 32.88 ? 70   LYS E O   1 
ATOM   4979  C  CB  . LYS E  1 70  ? 7.604   -24.728 33.512  1.00 41.06 ? 70   LYS E CB  1 
ATOM   4980  C  CG  . LYS E  1 70  ? 6.428   -23.795 33.365  1.00 41.43 ? 70   LYS E CG  1 
ATOM   4981  C  CD  . LYS E  1 70  ? 6.047   -23.711 31.906  1.00 48.93 ? 70   LYS E CD  1 
ATOM   4982  C  CE  . LYS E  1 70  ? 5.757   -22.279 31.498  1.00 58.62 ? 70   LYS E CE  1 
ATOM   4983  N  NZ  . LYS E  1 70  ? 6.963   -21.412 31.653  1.00 55.07 ? 70   LYS E NZ  1 
ATOM   4984  N  N   . HIS E  1 71  ? 9.372   -26.877 34.814  1.00 28.57 ? 71   HIS E N   1 
ATOM   4985  C  CA  . HIS E  1 71  ? 10.500  -27.786 34.813  1.00 29.14 ? 71   HIS E CA  1 
ATOM   4986  C  C   . HIS E  1 71  ? 11.410  -27.577 33.611  1.00 33.74 ? 71   HIS E C   1 
ATOM   4987  O  O   . HIS E  1 71  ? 10.947  -27.298 32.499  1.00 38.13 ? 71   HIS E O   1 
ATOM   4988  C  CB  . HIS E  1 71  ? 9.990   -29.226 34.832  1.00 29.32 ? 71   HIS E CB  1 
ATOM   4989  C  CG  . HIS E  1 71  ? 11.070  -30.255 34.735  1.00 29.92 ? 71   HIS E CG  1 
ATOM   4990  N  ND1 . HIS E  1 71  ? 11.948  -30.514 35.766  1.00 29.98 ? 71   HIS E ND1 1 
ATOM   4991  C  CD2 . HIS E  1 71  ? 11.404  -31.103 33.736  1.00 30.75 ? 71   HIS E CD2 1 
ATOM   4992  C  CE1 . HIS E  1 71  ? 12.782  -31.472 35.403  1.00 30.19 ? 71   HIS E CE1 1 
ATOM   4993  N  NE2 . HIS E  1 71  ? 12.475  -31.845 34.174  1.00 31.32 ? 71   HIS E NE2 1 
ATOM   4994  N  N   . GLY E  1 72  ? 12.709  -27.714 33.841  1.00 31.31 ? 72   GLY E N   1 
ATOM   4995  C  CA  . GLY E  1 72  ? 13.673  -27.688 32.762  1.00 33.03 ? 72   GLY E CA  1 
ATOM   4996  C  C   . GLY E  1 72  ? 14.917  -28.484 33.117  1.00 33.00 ? 72   GLY E C   1 
ATOM   4997  O  O   . GLY E  1 72  ? 14.921  -29.239 34.090  1.00 32.93 ? 72   GLY E O   1 
ATOM   4998  N  N   . GLY E  1 73  ? 15.966  -28.328 32.311  1.00 33.16 ? 73   GLY E N   1 
ATOM   4999  C  CA  . GLY E  1 73  ? 17.284  -28.825 32.656  1.00 32.41 ? 73   GLY E CA  1 
ATOM   5000  C  C   . GLY E  1 73  ? 18.017  -27.723 33.395  1.00 31.91 ? 73   GLY E C   1 
ATOM   5001  O  O   . GLY E  1 73  ? 17.578  -26.574 33.382  1.00 31.66 ? 73   GLY E O   1 
ATOM   5002  N  N   . PRO E  1 74  ? 19.152  -28.058 34.027  1.00 33.90 ? 74   PRO E N   1 
ATOM   5003  C  CA  . PRO E  1 74  ? 19.904  -27.103 34.860  1.00 31.38 ? 74   PRO E CA  1 
ATOM   5004  C  C   . PRO E  1 74  ? 20.413  -25.895 34.070  1.00 32.08 ? 74   PRO E C   1 
ATOM   5005  O  O   . PRO E  1 74  ? 20.616  -24.818 34.635  1.00 29.93 ? 74   PRO E O   1 
ATOM   5006  C  CB  . PRO E  1 74  ? 21.097  -27.924 35.367  1.00 30.26 ? 74   PRO E CB  1 
ATOM   5007  C  CG  . PRO E  1 74  ? 20.870  -29.338 34.907  1.00 30.52 ? 74   PRO E CG  1 
ATOM   5008  C  CD  . PRO E  1 74  ? 19.887  -29.313 33.795  1.00 32.43 ? 74   PRO E CD  1 
ATOM   5009  N  N   . LYS E  1 75  ? 20.616  -26.082 32.769  1.00 36.70 ? 75   LYS E N   1 
ATOM   5010  C  CA  . LYS E  1 75  ? 21.196  -25.047 31.916  1.00 38.50 ? 75   LYS E CA  1 
ATOM   5011  C  C   . LYS E  1 75  ? 20.136  -24.116 31.312  1.00 38.08 ? 75   LYS E C   1 
ATOM   5012  O  O   . LYS E  1 75  ? 20.466  -23.137 30.646  1.00 37.98 ? 75   LYS E O   1 
ATOM   5013  C  CB  . LYS E  1 75  ? 22.044  -25.695 30.820  1.00 40.68 ? 75   LYS E CB  1 
ATOM   5014  C  CG  . LYS E  1 75  ? 23.191  -26.551 31.349  1.00 40.48 ? 75   LYS E CG  1 
ATOM   5015  C  CD  . LYS E  1 75  ? 24.368  -25.690 31.785  1.00 45.10 ? 75   LYS E CD  1 
ATOM   5016  C  CE  . LYS E  1 75  ? 25.062  -25.061 30.574  1.00 56.75 ? 75   LYS E CE  1 
ATOM   5017  N  NZ  . LYS E  1 75  ? 26.230  -24.196 30.945  1.00 59.64 ? 75   LYS E NZ  1 
ATOM   5018  N  N   . ASP E  1 76  ? 18.868  -24.420 31.570  1.00 37.71 ? 76   ASP E N   1 
ATOM   5019  C  CA  . ASP E  1 76  ? 17.748  -23.609 31.094  1.00 39.32 ? 76   ASP E CA  1 
ATOM   5020  C  C   . ASP E  1 76  ? 17.366  -22.498 32.074  1.00 40.21 ? 76   ASP E C   1 
ATOM   5021  O  O   . ASP E  1 76  ? 17.371  -22.701 33.287  1.00 41.23 ? 76   ASP E O   1 
ATOM   5022  C  CB  . ASP E  1 76  ? 16.520  -24.498 30.867  1.00 37.65 ? 76   ASP E CB  1 
ATOM   5023  C  CG  . ASP E  1 76  ? 16.696  -25.464 29.710  1.00 40.60 ? 76   ASP E CG  1 
ATOM   5024  O  OD1 . ASP E  1 76  ? 17.398  -25.115 28.732  1.00 42.20 ? 76   ASP E OD1 1 
ATOM   5025  O  OD2 . ASP E  1 76  ? 16.114  -26.571 29.777  1.00 42.57 ? 76   ASP E OD2 1 
ATOM   5026  N  N   . GLU E  1 77  ? 17.014  -21.329 31.547  1.00 40.99 ? 77   GLU E N   1 
ATOM   5027  C  CA  . GLU E  1 77  ? 16.478  -20.249 32.377  1.00 49.11 ? 77   GLU E CA  1 
ATOM   5028  C  C   . GLU E  1 77  ? 15.094  -20.571 32.988  1.00 48.71 ? 77   GLU E C   1 
ATOM   5029  O  O   . GLU E  1 77  ? 14.810  -20.199 34.134  1.00 48.22 ? 77   GLU E O   1 
ATOM   5030  C  CB  . GLU E  1 77  ? 16.429  -18.939 31.583  1.00 56.32 ? 77   GLU E CB  1 
ATOM   5031  C  CG  . GLU E  1 77  ? 17.545  -17.954 31.910  1.00 59.54 ? 77   GLU E CG  1 
ATOM   5032  C  CD  . GLU E  1 77  ? 17.145  -16.941 32.982  1.00 68.93 ? 77   GLU E CD  1 
ATOM   5033  O  OE1 . GLU E  1 77  ? 17.800  -15.878 33.073  1.00 72.21 ? 77   GLU E OE1 1 
ATOM   5034  O  OE2 . GLU E  1 77  ? 16.170  -17.201 33.726  1.00 67.17 ? 77   GLU E OE2 1 
ATOM   5035  N  N   . GLU E  1 78  ? 14.230  -21.243 32.228  1.00 44.89 ? 78   GLU E N   1 
ATOM   5036  C  CA  . GLU E  1 78  ? 12.972  -21.724 32.794  1.00 44.92 ? 78   GLU E CA  1 
ATOM   5037  C  C   . GLU E  1 78  ? 13.198  -23.076 33.442  1.00 40.57 ? 78   GLU E C   1 
ATOM   5038  O  O   . GLU E  1 78  ? 13.294  -24.102 32.766  1.00 39.01 ? 78   GLU E O   1 
ATOM   5039  C  CB  . GLU E  1 78  ? 11.847  -21.810 31.748  1.00 49.39 ? 78   GLU E CB  1 
ATOM   5040  C  CG  . GLU E  1 78  ? 10.871  -20.614 31.749  1.00 51.15 ? 78   GLU E CG  1 
ATOM   5041  C  CD  . GLU E  1 78  ? 9.909   -20.620 32.938  1.00 49.78 ? 78   GLU E CD  1 
ATOM   5042  O  OE1 . GLU E  1 78  ? 9.083   -21.554 33.028  1.00 47.61 ? 78   GLU E OE1 1 
ATOM   5043  O  OE2 . GLU E  1 78  ? 9.971   -19.684 33.773  1.00 48.92 ? 78   GLU E OE2 1 
ATOM   5044  N  N   . ARG E  1 79  ? 13.289  -23.066 34.763  1.00 37.58 ? 79   ARG E N   1 
ATOM   5045  C  CA  . ARG E  1 79  ? 13.509  -24.288 35.515  1.00 37.39 ? 79   ARG E CA  1 
ATOM   5046  C  C   . ARG E  1 79  ? 13.116  -24.086 36.969  1.00 32.40 ? 79   ARG E C   1 
ATOM   5047  O  O   . ARG E  1 79  ? 13.023  -22.953 37.452  1.00 31.88 ? 79   ARG E O   1 
ATOM   5048  C  CB  . ARG E  1 79  ? 14.984  -24.705 35.437  1.00 35.46 ? 79   ARG E CB  1 
ATOM   5049  C  CG  . ARG E  1 79  ? 15.934  -23.629 35.949  1.00 32.52 ? 79   ARG E CG  1 
ATOM   5050  C  CD  . ARG E  1 79  ? 17.342  -24.142 36.148  1.00 32.60 ? 79   ARG E CD  1 
ATOM   5051  N  NE  . ARG E  1 79  ? 17.528  -24.825 37.426  1.00 32.87 ? 79   ARG E NE  1 
ATOM   5052  C  CZ  . ARG E  1 79  ? 18.722  -25.098 37.939  1.00 33.14 ? 79   ARG E CZ  1 
ATOM   5053  N  NH1 . ARG E  1 79  ? 19.808  -24.740 37.274  1.00 33.80 ? 79   ARG E NH1 1 
ATOM   5054  N  NH2 . ARG E  1 79  ? 18.838  -25.717 39.108  1.00 30.95 ? 79   ARG E NH2 1 
ATOM   5055  N  N   . HIS E  1 80  ? 12.879  -25.199 37.652  1.00 30.80 ? 80   HIS E N   1 
ATOM   5056  C  CA  . HIS E  1 80  ? 12.810  -25.211 39.099  1.00 30.46 ? 80   HIS E CA  1 
ATOM   5057  C  C   . HIS E  1 80  ? 14.223  -25.044 39.643  1.00 31.23 ? 80   HIS E C   1 
ATOM   5058  O  O   . HIS E  1 80  ? 15.198  -25.348 38.956  1.00 32.56 ? 80   HIS E O   1 
ATOM   5059  C  CB  . HIS E  1 80  ? 12.232  -26.533 39.578  1.00 29.11 ? 80   HIS E CB  1 
ATOM   5060  C  CG  . HIS E  1 80  ? 10.878  -26.825 39.026  1.00 28.07 ? 80   HIS E CG  1 
ATOM   5061  N  ND1 . HIS E  1 80  ? 10.499  -28.081 38.610  1.00 28.04 ? 80   HIS E ND1 1 
ATOM   5062  C  CD2 . HIS E  1 80  ? 9.812   -26.020 38.816  1.00 29.56 ? 80   HIS E CD2 1 
ATOM   5063  C  CE1 . HIS E  1 80  ? 9.256   -28.040 38.168  1.00 29.65 ? 80   HIS E CE1 1 
ATOM   5064  N  NE2 . HIS E  1 80  ? 8.815   -26.800 38.281  1.00 31.88 ? 80   HIS E NE2 1 
ATOM   5065  N  N   . VAL E  1 81  ? 14.336  -24.556 40.872  1.00 33.63 ? 81   VAL E N   1 
ATOM   5066  C  CA  . VAL E  1 81  ? 15.628  -24.476 41.545  1.00 31.64 ? 81   VAL E CA  1 
ATOM   5067  C  C   . VAL E  1 81  ? 16.216  -25.881 41.735  1.00 31.03 ? 81   VAL E C   1 
ATOM   5068  O  O   . VAL E  1 81  ? 17.425  -26.083 41.622  1.00 29.91 ? 81   VAL E O   1 
ATOM   5069  C  CB  . VAL E  1 81  ? 15.504  -23.757 42.911  1.00 30.76 ? 81   VAL E CB  1 
ATOM   5070  C  CG1 . VAL E  1 81  ? 16.823  -23.812 43.679  1.00 31.18 ? 81   VAL E CG1 1 
ATOM   5071  C  CG2 . VAL E  1 81  ? 15.059  -22.323 42.710  1.00 30.77 ? 81   VAL E CG2 1 
ATOM   5072  N  N   . GLY E  1 82  ? 15.351  -26.852 42.015  1.00 30.92 ? 82   GLY E N   1 
ATOM   5073  C  CA  . GLY E  1 82  ? 15.784  -28.217 42.253  1.00 28.58 ? 82   GLY E CA  1 
ATOM   5074  C  C   . GLY E  1 82  ? 16.019  -29.029 40.996  1.00 28.32 ? 82   GLY E C   1 
ATOM   5075  O  O   . GLY E  1 82  ? 16.172  -30.243 41.060  1.00 27.19 ? 82   GLY E O   1 
ATOM   5076  N  N   . ASP E  1 83  ? 16.045  -28.356 39.850  1.00 29.30 ? 83   ASP E N   1 
ATOM   5077  C  CA  . ASP E  1 83  ? 16.295  -29.007 38.567  1.00 28.99 ? 83   ASP E CA  1 
ATOM   5078  C  C   . ASP E  1 83  ? 17.773  -29.147 38.294  1.00 29.01 ? 83   ASP E C   1 
ATOM   5079  O  O   . ASP E  1 83  ? 18.427  -28.194 37.886  1.00 29.04 ? 83   ASP E O   1 
ATOM   5080  C  CB  . ASP E  1 83  ? 15.671  -28.201 37.436  1.00 31.73 ? 83   ASP E CB  1 
ATOM   5081  C  CG  . ASP E  1 83  ? 14.172  -28.309 37.415  1.00 32.55 ? 83   ASP E CG  1 
ATOM   5082  O  OD1 . ASP E  1 83  ? 13.632  -29.104 38.219  1.00 31.79 ? 83   ASP E OD1 1 
ATOM   5083  O  OD2 . ASP E  1 83  ? 13.542  -27.604 36.597  1.00 34.11 ? 83   ASP E OD2 1 
ATOM   5084  N  N   . LEU E  1 84  ? 18.299  -30.339 38.529  1.00 30.12 ? 84   LEU E N   1 
ATOM   5085  C  CA  . LEU E  1 84  ? 19.711  -30.595 38.315  1.00 29.32 ? 84   LEU E CA  1 
ATOM   5086  C  C   . LEU E  1 84  ? 19.910  -31.642 37.218  1.00 30.71 ? 84   LEU E C   1 
ATOM   5087  O  O   . LEU E  1 84  ? 20.999  -32.210 37.101  1.00 32.76 ? 84   LEU E O   1 
ATOM   5088  C  CB  . LEU E  1 84  ? 20.386  -31.056 39.614  1.00 30.23 ? 84   LEU E CB  1 
ATOM   5089  C  CG  . LEU E  1 84  ? 20.458  -30.103 40.815  1.00 29.06 ? 84   LEU E CG  1 
ATOM   5090  C  CD1 . LEU E  1 84  ? 21.359  -30.701 41.892  1.00 26.68 ? 84   LEU E CD1 1 
ATOM   5091  C  CD2 . LEU E  1 84  ? 20.953  -28.717 40.408  1.00 27.52 ? 84   LEU E CD2 1 
ATOM   5092  N  N   . GLY E  1 85  ? 18.861  -31.900 36.428  1.00 28.26 ? 85   GLY E N   1 
ATOM   5093  C  CA  . GLY E  1 85  ? 18.956  -32.764 35.261  1.00 27.50 ? 85   GLY E CA  1 
ATOM   5094  C  C   . GLY E  1 85  ? 19.108  -34.256 35.523  1.00 28.39 ? 85   GLY E C   1 
ATOM   5095  O  O   . GLY E  1 85  ? 18.366  -34.836 36.308  1.00 27.95 ? 85   GLY E O   1 
ATOM   5096  N  N   . ASN E  1 86  ? 20.069  -34.884 34.850  1.00 28.91 ? 86   ASN E N   1 
ATOM   5097  C  CA  . ASN E  1 86  ? 20.262  -36.328 34.955  1.00 29.12 ? 86   ASN E CA  1 
ATOM   5098  C  C   . ASN E  1 86  ? 21.633  -36.714 35.476  1.00 31.25 ? 86   ASN E C   1 
ATOM   5099  O  O   . ASN E  1 86  ? 22.607  -35.962 35.357  1.00 30.97 ? 86   ASN E O   1 
ATOM   5100  C  CB  . ASN E  1 86  ? 20.091  -37.011 33.594  1.00 32.07 ? 86   ASN E CB  1 
ATOM   5101  C  CG  . ASN E  1 86  ? 18.656  -37.021 33.105  1.00 32.39 ? 86   ASN E CG  1 
ATOM   5102  O  OD1 . ASN E  1 86  ? 17.847  -37.857 33.518  1.00 31.26 ? 86   ASN E OD1 1 
ATOM   5103  N  ND2 . ASN E  1 86  ? 18.346  -36.116 32.177  1.00 32.25 ? 86   ASN E ND2 1 
ATOM   5104  N  N   . VAL E  1 87  ? 21.704  -37.919 36.025  1.00 32.27 ? 87   VAL E N   1 
ATOM   5105  C  CA  . VAL E  1 87  ? 22.982  -38.538 36.330  1.00 32.92 ? 87   VAL E CA  1 
ATOM   5106  C  C   . VAL E  1 87  ? 23.128  -39.832 35.532  1.00 32.65 ? 87   VAL E C   1 
ATOM   5107  O  O   . VAL E  1 87  ? 22.142  -40.516 35.254  1.00 30.00 ? 87   VAL E O   1 
ATOM   5108  C  CB  . VAL E  1 87  ? 23.152  -38.814 37.842  1.00 30.29 ? 87   VAL E CB  1 
ATOM   5109  C  CG1 . VAL E  1 87  ? 23.359  -37.516 38.582  1.00 28.21 ? 87   VAL E CG1 1 
ATOM   5110  C  CG2 . VAL E  1 87  ? 21.960  -39.583 38.388  1.00 27.57 ? 87   VAL E CG2 1 
ATOM   5111  N  N   . THR E  1 88  ? 24.368  -40.158 35.176  1.00 36.56 ? 88   THR E N   1 
ATOM   5112  C  CA  . THR E  1 88  ? 24.664  -41.307 34.326  1.00 34.64 ? 88   THR E CA  1 
ATOM   5113  C  C   . THR E  1 88  ? 25.234  -42.458 35.145  1.00 35.23 ? 88   THR E C   1 
ATOM   5114  O  O   . THR E  1 88  ? 26.268  -42.303 35.812  1.00 31.92 ? 88   THR E O   1 
ATOM   5115  C  CB  . THR E  1 88  ? 25.683  -40.923 33.236  1.00 32.41 ? 88   THR E CB  1 
ATOM   5116  O  OG1 . THR E  1 88  ? 25.205  -39.776 32.530  1.00 31.28 ? 88   THR E OG1 1 
ATOM   5117  C  CG2 . THR E  1 88  ? 25.895  -42.069 32.253  1.00 34.51 ? 88   THR E CG2 1 
ATOM   5118  N  N   . ALA E  1 89  ? 24.545  -43.600 35.102  1.00 32.10 ? 89   ALA E N   1 
ATOM   5119  C  CA  . ALA E  1 89  ? 25.051  -44.839 35.684  1.00 33.84 ? 89   ALA E CA  1 
ATOM   5120  C  C   . ALA E  1 89  ? 25.645  -45.724 34.576  1.00 35.42 ? 89   ALA E C   1 
ATOM   5121  O  O   . ALA E  1 89  ? 25.034  -45.884 33.524  1.00 36.93 ? 89   ALA E O   1 
ATOM   5122  C  CB  . ALA E  1 89  ? 23.937  -45.577 36.428  1.00 30.99 ? 89   ALA E CB  1 
ATOM   5123  N  N   . GLY E  1 90  ? 26.832  -46.287 34.810  1.00 37.08 ? 90   GLY E N   1 
ATOM   5124  C  CA  . GLY E  1 90  ? 27.471  -47.167 33.844  1.00 38.96 ? 90   GLY E CA  1 
ATOM   5125  C  C   . GLY E  1 90  ? 26.946  -48.595 33.882  1.00 42.01 ? 90   GLY E C   1 
ATOM   5126  O  O   . GLY E  1 90  ? 26.036  -48.896 34.655  1.00 37.78 ? 90   GLY E O   1 
ATOM   5127  N  N   . LYS E  1 91  ? 27.511  -49.468 33.039  1.00 47.78 ? 91   LYS E N   1 
ATOM   5128  C  CA  . LYS E  1 91  ? 27.194  -50.907 33.048  1.00 48.69 ? 91   LYS E CA  1 
ATOM   5129  C  C   . LYS E  1 91  ? 27.374  -51.462 34.456  1.00 45.49 ? 91   LYS E C   1 
ATOM   5130  O  O   . LYS E  1 91  ? 27.021  -52.601 34.760  1.00 44.93 ? 91   LYS E O   1 
ATOM   5131  C  CB  . LYS E  1 91  ? 28.113  -51.667 32.085  1.00 45.99 ? 91   LYS E CB  1 
ATOM   5132  C  CG  . LYS E  1 91  ? 27.681  -51.606 30.628  1.00 53.33 ? 91   LYS E CG  1 
ATOM   5133  C  CD  . LYS E  1 91  ? 28.879  -51.543 29.678  1.00 55.16 ? 91   LYS E CD  1 
ATOM   5134  C  CE  . LYS E  1 91  ? 29.426  -50.114 29.541  1.00 56.54 ? 91   LYS E CE  1 
ATOM   5135  N  NZ  . LYS E  1 91  ? 28.439  -49.156 28.931  1.00 49.96 ? 91   LYS E NZ  1 
ATOM   5136  N  N   . ASP E  1 92  ? 27.933  -50.612 35.302  1.00 43.13 ? 92   ASP E N   1 
ATOM   5137  C  CA  . ASP E  1 92  ? 28.302  -50.921 36.668  1.00 44.28 ? 92   ASP E CA  1 
ATOM   5138  C  C   . ASP E  1 92  ? 27.082  -50.906 37.597  1.00 43.11 ? 92   ASP E C   1 
ATOM   5139  O  O   . ASP E  1 92  ? 27.013  -51.640 38.592  1.00 39.17 ? 92   ASP E O   1 
ATOM   5140  C  CB  . ASP E  1 92  ? 29.282  -49.838 37.115  1.00 41.74 ? 92   ASP E CB  1 
ATOM   5141  C  CG  . ASP E  1 92  ? 30.283  -50.339 38.105  1.00 45.45 ? 92   ASP E CG  1 
ATOM   5142  O  OD1 . ASP E  1 92  ? 30.163  -51.514 38.517  1.00 48.59 ? 92   ASP E OD1 1 
ATOM   5143  O  OD2 . ASP E  1 92  ? 31.188  -49.555 38.463  1.00 44.93 ? 92   ASP E OD2 1 
ATOM   5144  N  N   . GLY E  1 93  ? 26.119  -50.058 37.256  1.00 42.94 ? 93   GLY E N   1 
ATOM   5145  C  CA  . GLY E  1 93  ? 25.024  -49.745 38.149  1.00 39.59 ? 93   GLY E CA  1 
ATOM   5146  C  C   . GLY E  1 93  ? 25.400  -48.515 38.952  1.00 34.94 ? 93   GLY E C   1 
ATOM   5147  O  O   . GLY E  1 93  ? 24.596  -47.994 39.718  1.00 36.03 ? 93   GLY E O   1 
ATOM   5148  N  N   . VAL E  1 94  ? 26.627  -48.044 38.760  1.00 32.61 ? 94   VAL E N   1 
ATOM   5149  C  CA  . VAL E  1 94  ? 27.156  -46.939 39.545  1.00 34.31 ? 94   VAL E CA  1 
ATOM   5150  C  C   . VAL E  1 94  ? 27.179  -45.638 38.748  1.00 35.08 ? 94   VAL E C   1 
ATOM   5151  O  O   . VAL E  1 94  ? 27.545  -45.627 37.574  1.00 35.92 ? 94   VAL E O   1 
ATOM   5152  C  CB  . VAL E  1 94  ? 28.575  -47.256 40.083  1.00 34.94 ? 94   VAL E CB  1 
ATOM   5153  C  CG1 . VAL E  1 94  ? 29.155  -46.056 40.806  1.00 32.65 ? 94   VAL E CG1 1 
ATOM   5154  C  CG2 . VAL E  1 94  ? 28.538  -48.464 41.008  1.00 35.03 ? 94   VAL E CG2 1 
ATOM   5155  N  N   . ALA E  1 95  ? 26.782  -44.545 39.396  1.00 33.13 ? 95   ALA E N   1 
ATOM   5156  C  CA  . ALA E  1 95  ? 26.802  -43.226 38.779  1.00 31.00 ? 95   ALA E CA  1 
ATOM   5157  C  C   . ALA E  1 95  ? 27.877  -42.329 39.394  1.00 30.72 ? 95   ALA E C   1 
ATOM   5158  O  O   . ALA E  1 95  ? 27.756  -41.941 40.542  1.00 30.98 ? 95   ALA E O   1 
ATOM   5159  C  CB  . ALA E  1 95  ? 25.438  -42.572 38.930  1.00 27.52 ? 95   ALA E CB  1 
ATOM   5160  N  N   . ASN E  1 96  ? 28.926  -41.994 38.646  1.00 32.42 ? 96   ASN E N   1 
ATOM   5161  C  CA  . ASN E  1 96  ? 29.837  -40.947 39.103  1.00 31.85 ? 96   ASN E CA  1 
ATOM   5162  C  C   . ASN E  1 96  ? 29.134  -39.615 38.918  1.00 29.25 ? 96   ASN E C   1 
ATOM   5163  O  O   . ASN E  1 96  ? 28.912  -39.192 37.795  1.00 30.22 ? 96   ASN E O   1 
ATOM   5164  C  CB  . ASN E  1 96  ? 31.147  -40.913 38.304  1.00 33.61 ? 96   ASN E CB  1 
ATOM   5165  C  CG  . ASN E  1 96  ? 31.876  -42.251 38.283  1.00 42.87 ? 96   ASN E CG  1 
ATOM   5166  O  OD1 . ASN E  1 96  ? 31.344  -43.283 38.702  1.00 44.09 ? 96   ASN E OD1 1 
ATOM   5167  N  ND2 . ASN E  1 96  ? 33.109  -42.237 37.774  1.00 44.65 ? 96   ASN E ND2 1 
ATOM   5168  N  N   . VAL E  1 97  ? 28.770  -38.952 40.009  1.00 27.67 ? 97   VAL E N   1 
ATOM   5169  C  CA  . VAL E  1 97  ? 28.104  -37.659 39.898  1.00 26.03 ? 97   VAL E CA  1 
ATOM   5170  C  C   . VAL E  1 97  ? 29.086  -36.503 40.066  1.00 26.31 ? 97   VAL E C   1 
ATOM   5171  O  O   . VAL E  1 97  ? 29.945  -36.522 40.952  1.00 29.14 ? 97   VAL E O   1 
ATOM   5172  C  CB  . VAL E  1 97  ? 26.958  -37.523 40.917  1.00 25.16 ? 97   VAL E CB  1 
ATOM   5173  C  CG1 . VAL E  1 97  ? 26.161  -36.250 40.659  1.00 24.64 ? 97   VAL E CG1 1 
ATOM   5174  C  CG2 . VAL E  1 97  ? 26.060  -38.745 40.853  1.00 25.52 ? 97   VAL E CG2 1 
ATOM   5175  N  N   . SER E  1 98  ? 28.959  -35.497 39.209  1.00 26.61 ? 98   SER E N   1 
ATOM   5176  C  CA  . SER E  1 98  ? 29.825  -34.326 39.257  1.00 26.37 ? 98   SER E CA  1 
ATOM   5177  C  C   . SER E  1 98  ? 29.200  -33.185 38.467  1.00 28.49 ? 98   SER E C   1 
ATOM   5178  O  O   . SER E  1 98  ? 29.352  -33.086 37.257  1.00 31.19 ? 98   SER E O   1 
ATOM   5179  C  CB  . SER E  1 98  ? 31.216  -34.649 38.727  1.00 28.38 ? 98   SER E CB  1 
ATOM   5180  O  OG  . SER E  1 98  ? 32.083  -33.547 38.919  1.00 35.62 ? 98   SER E OG  1 
ATOM   5181  N  N   . ILE E  1 99  ? 28.502  -32.321 39.188  1.00 30.15 ? 99   ILE E N   1 
ATOM   5182  C  CA  . ILE E  1 99  ? 27.637  -31.303 38.615  1.00 31.44 ? 99   ILE E CA  1 
ATOM   5183  C  C   . ILE E  1 99  ? 28.046  -29.968 39.205  1.00 31.00 ? 99   ILE E C   1 
ATOM   5184  O  O   . ILE E  1 99  ? 28.561  -29.919 40.316  1.00 31.23 ? 99   ILE E O   1 
ATOM   5185  C  CB  . ILE E  1 99  ? 26.172  -31.592 39.008  1.00 29.30 ? 99   ILE E CB  1 
ATOM   5186  C  CG1 . ILE E  1 99  ? 25.682  -32.856 38.298  1.00 30.80 ? 99   ILE E CG1 1 
ATOM   5187  C  CG2 . ILE E  1 99  ? 25.274  -30.400 38.728  1.00 29.00 ? 99   ILE E CG2 1 
ATOM   5188  C  CD1 . ILE E  1 99  ? 24.285  -33.273 38.674  1.00 30.07 ? 99   ILE E CD1 1 
ATOM   5189  N  N   . GLU E  1 100 ? 27.840  -28.884 38.471  1.00 31.80 ? 100  GLU E N   1 
ATOM   5190  C  CA  . GLU E  1 100 ? 28.048  -27.568 39.053  1.00 34.41 ? 100  GLU E CA  1 
ATOM   5191  C  C   . GLU E  1 100 ? 26.854  -26.693 38.734  1.00 32.54 ? 100  GLU E C   1 
ATOM   5192  O  O   . GLU E  1 100 ? 26.425  -26.624 37.586  1.00 35.70 ? 100  GLU E O   1 
ATOM   5193  C  CB  . GLU E  1 100 ? 29.353  -26.925 38.568  1.00 36.30 ? 100  GLU E CB  1 
ATOM   5194  C  CG  . GLU E  1 100 ? 29.605  -25.539 39.169  1.00 41.34 ? 100  GLU E CG  1 
ATOM   5195  C  CD  . GLU E  1 100 ? 30.907  -24.901 38.687  1.00 53.95 ? 100  GLU E CD  1 
ATOM   5196  O  OE1 . GLU E  1 100 ? 31.925  -25.625 38.564  1.00 57.61 ? 100  GLU E OE1 1 
ATOM   5197  O  OE2 . GLU E  1 100 ? 30.910  -23.670 38.444  1.00 53.78 ? 100  GLU E OE2 1 
ATOM   5198  N  N   . ASP E  1 101 ? 26.314  -26.037 39.755  1.00 33.39 ? 101  ASP E N   1 
ATOM   5199  C  CA  . ASP E  1 101 ? 25.112  -25.235 39.604  1.00 32.75 ? 101  ASP E CA  1 
ATOM   5200  C  C   . ASP E  1 101 ? 25.234  -23.916 40.359  1.00 34.23 ? 101  ASP E C   1 
ATOM   5201  O  O   . ASP E  1 101 ? 25.918  -23.835 41.375  1.00 34.85 ? 101  ASP E O   1 
ATOM   5202  C  CB  . ASP E  1 101 ? 23.888  -26.010 40.106  1.00 34.99 ? 101  ASP E CB  1 
ATOM   5203  C  CG  . ASP E  1 101 ? 22.582  -25.480 39.530  1.00 35.96 ? 101  ASP E CG  1 
ATOM   5204  O  OD1 . ASP E  1 101 ? 22.341  -25.695 38.317  1.00 37.28 ? 101  ASP E OD1 1 
ATOM   5205  O  OD2 . ASP E  1 101 ? 21.801  -24.855 40.284  1.00 32.70 ? 101  ASP E OD2 1 
ATOM   5206  N  N   . ARG E  1 102 ? 24.557  -22.888 39.855  1.00 37.44 ? 102  ARG E N   1 
ATOM   5207  C  CA  . ARG E  1 102 ? 24.581  -21.560 40.462  1.00 36.33 ? 102  ARG E CA  1 
ATOM   5208  C  C   . ARG E  1 102 ? 23.171  -21.096 40.845  1.00 35.12 ? 102  ARG E C   1 
ATOM   5209  O  O   . ARG E  1 102 ? 22.986  -19.960 41.282  1.00 37.28 ? 102  ARG E O   1 
ATOM   5210  C  CB  . ARG E  1 102 ? 25.255  -20.560 39.515  1.00 36.91 ? 102  ARG E CB  1 
ATOM   5211  C  CG  . ARG E  1 102 ? 26.490  -21.134 38.808  1.00 42.72 ? 102  ARG E CG  1 
ATOM   5212  C  CD  . ARG E  1 102 ? 27.290  -20.097 38.014  1.00 47.50 ? 102  ARG E CD  1 
ATOM   5213  N  NE  . ARG E  1 102 ? 28.624  -20.604 37.684  1.00 55.94 ? 102  ARG E NE  1 
ATOM   5214  C  CZ  . ARG E  1 102 ? 29.664  -19.849 37.330  1.00 59.21 ? 102  ARG E CZ  1 
ATOM   5215  N  NH1 . ARG E  1 102 ? 29.539  -18.529 37.247  1.00 60.11 ? 102  ARG E NH1 1 
ATOM   5216  N  NH2 . ARG E  1 102 ? 30.837  -20.416 37.061  1.00 55.83 ? 102  ARG E NH2 1 
ATOM   5217  N  N   . VAL E  1 103 ? 22.188  -21.984 40.686  1.00 33.43 ? 103  VAL E N   1 
ATOM   5218  C  CA  . VAL E  1 103 ? 20.797  -21.695 41.050  1.00 36.43 ? 103  VAL E CA  1 
ATOM   5219  C  C   . VAL E  1 103 ? 20.443  -22.192 42.471  1.00 36.58 ? 103  VAL E C   1 
ATOM   5220  O  O   . VAL E  1 103 ? 19.840  -21.461 43.271  1.00 37.74 ? 103  VAL E O   1 
ATOM   5221  C  CB  . VAL E  1 103 ? 19.813  -22.254 39.987  1.00 34.51 ? 103  VAL E CB  1 
ATOM   5222  C  CG1 . VAL E  1 103 ? 18.367  -22.162 40.466  1.00 34.16 ? 103  VAL E CG1 1 
ATOM   5223  C  CG2 . VAL E  1 103 ? 19.990  -21.504 38.684  1.00 33.39 ? 103  VAL E CG2 1 
ATOM   5224  N  N   . ILE E  1 104 ? 20.823  -23.428 42.788  1.00 34.34 ? 104  ILE E N   1 
ATOM   5225  C  CA  . ILE E  1 104 ? 20.737  -23.890 44.165  1.00 31.13 ? 104  ILE E CA  1 
ATOM   5226  C  C   . ILE E  1 104 ? 21.717  -23.080 45.005  1.00 31.97 ? 104  ILE E C   1 
ATOM   5227  O  O   . ILE E  1 104 ? 22.690  -22.531 44.478  1.00 33.02 ? 104  ILE E O   1 
ATOM   5228  C  CB  . ILE E  1 104 ? 21.066  -25.393 44.310  1.00 27.22 ? 104  ILE E CB  1 
ATOM   5229  C  CG1 . ILE E  1 104 ? 22.460  -25.696 43.758  1.00 26.32 ? 104  ILE E CG1 1 
ATOM   5230  C  CG2 . ILE E  1 104 ? 20.000  -26.250 43.633  1.00 29.25 ? 104  ILE E CG2 1 
ATOM   5231  C  CD1 . ILE E  1 104 ? 22.832  -27.162 43.805  1.00 25.32 ? 104  ILE E CD1 1 
ATOM   5232  N  N   . SER E  1 105 ? 21.446  -22.993 46.304  1.00 31.32 ? 105  SER E N   1 
ATOM   5233  C  CA  . SER E  1 105 ? 22.383  -22.400 47.250  1.00 32.24 ? 105  SER E CA  1 
ATOM   5234  C  C   . SER E  1 105 ? 22.409  -23.253 48.501  1.00 29.74 ? 105  SER E C   1 
ATOM   5235  O  O   . SER E  1 105 ? 21.526  -24.079 48.713  1.00 32.09 ? 105  SER E O   1 
ATOM   5236  C  CB  . SER E  1 105 ? 21.982  -20.968 47.608  1.00 33.98 ? 105  SER E CB  1 
ATOM   5237  O  OG  . SER E  1 105 ? 23.014  -20.319 48.332  1.00 34.16 ? 105  SER E OG  1 
ATOM   5238  N  N   . LEU E  1 106 ? 23.424  -23.051 49.326  1.00 31.59 ? 106  LEU E N   1 
ATOM   5239  C  CA  . LEU E  1 106 ? 23.542  -23.768 50.587  1.00 31.24 ? 106  LEU E CA  1 
ATOM   5240  C  C   . LEU E  1 106 ? 23.194  -22.826 51.743  1.00 33.36 ? 106  LEU E C   1 
ATOM   5241  O  O   . LEU E  1 106 ? 23.269  -23.209 52.910  1.00 35.47 ? 106  LEU E O   1 
ATOM   5242  C  CB  . LEU E  1 106 ? 24.951  -24.357 50.754  1.00 27.78 ? 106  LEU E CB  1 
ATOM   5243  C  CG  . LEU E  1 106 ? 25.361  -25.502 49.822  1.00 26.81 ? 106  LEU E CG  1 
ATOM   5244  C  CD1 . LEU E  1 106 ? 26.670  -26.099 50.260  1.00 25.94 ? 106  LEU E CD1 1 
ATOM   5245  C  CD2 . LEU E  1 106 ? 24.287  -26.586 49.762  1.00 25.22 ? 106  LEU E CD2 1 
ATOM   5246  N  N   . SER E  1 107 ? 22.804  -21.597 51.401  1.00 32.81 ? 107  SER E N   1 
ATOM   5247  C  CA  . SER E  1 107 ? 22.401  -20.591 52.386  1.00 34.49 ? 107  SER E CA  1 
ATOM   5248  C  C   . SER E  1 107 ? 21.358  -19.610 51.838  1.00 38.04 ? 107  SER E C   1 
ATOM   5249  O  O   . SER E  1 107 ? 21.117  -19.534 50.629  1.00 39.11 ? 107  SER E O   1 
ATOM   5250  C  CB  . SER E  1 107 ? 23.617  -19.808 52.878  1.00 35.58 ? 107  SER E CB  1 
ATOM   5251  O  OG  . SER E  1 107 ? 24.002  -18.831 51.927  1.00 38.56 ? 107  SER E OG  1 
ATOM   5252  N  N   . GLY E  1 108 ? 20.747  -18.852 52.739  1.00 40.25 ? 108  GLY E N   1 
ATOM   5253  C  CA  . GLY E  1 108 ? 19.746  -17.874 52.360  1.00 39.63 ? 108  GLY E CA  1 
ATOM   5254  C  C   . GLY E  1 108 ? 18.421  -18.461 51.906  1.00 41.71 ? 108  GLY E C   1 
ATOM   5255  O  O   . GLY E  1 108 ? 18.131  -19.640 52.112  1.00 36.02 ? 108  GLY E O   1 
ATOM   5256  N  N   . GLU E  1 109 ? 17.626  -17.603 51.272  1.00 45.96 ? 109  GLU E N   1 
ATOM   5257  C  CA  . GLU E  1 109 ? 16.271  -17.902 50.806  1.00 45.34 ? 109  GLU E CA  1 
ATOM   5258  C  C   . GLU E  1 109 ? 16.148  -19.241 50.071  1.00 42.73 ? 109  GLU E C   1 
ATOM   5259  O  O   . GLU E  1 109 ? 15.216  -20.010 50.314  1.00 40.14 ? 109  GLU E O   1 
ATOM   5260  C  CB  . GLU E  1 109 ? 15.785  -16.768 49.882  1.00 46.28 ? 109  GLU E CB  1 
ATOM   5261  C  CG  . GLU E  1 109 ? 16.430  -15.384 50.145  1.00 53.16 ? 109  GLU E CG  1 
ATOM   5262  C  CD  . GLU E  1 109 ? 17.902  -15.256 49.664  1.00 56.55 ? 109  GLU E CD  1 
ATOM   5263  O  OE1 . GLU E  1 109 ? 18.305  -15.944 48.693  1.00 54.46 ? 109  GLU E OE1 1 
ATOM   5264  O  OE2 . GLU E  1 109 ? 18.658  -14.447 50.256  1.00 53.52 ? 109  GLU E OE2 1 
ATOM   5265  N  N   . HIS E  1 110 ? 17.088  -19.502 49.165  1.00 43.95 ? 110  HIS E N   1 
ATOM   5266  C  CA  . HIS E  1 110 ? 17.027  -20.668 48.284  1.00 42.45 ? 110  HIS E CA  1 
ATOM   5267  C  C   . HIS E  1 110 ? 17.921  -21.793 48.767  1.00 35.51 ? 110  HIS E C   1 
ATOM   5268  O  O   . HIS E  1 110 ? 18.325  -22.646 47.979  1.00 34.29 ? 110  HIS E O   1 
ATOM   5269  C  CB  . HIS E  1 110 ? 17.437  -20.283 46.856  1.00 44.67 ? 110  HIS E CB  1 
ATOM   5270  C  CG  . HIS E  1 110 ? 16.451  -19.395 46.159  1.00 47.03 ? 110  HIS E CG  1 
ATOM   5271  N  ND1 . HIS E  1 110 ? 16.015  -19.634 44.873  1.00 50.20 ? 110  HIS E ND1 1 
ATOM   5272  C  CD2 . HIS E  1 110 ? 15.811  -18.275 46.571  1.00 48.26 ? 110  HIS E CD2 1 
ATOM   5273  C  CE1 . HIS E  1 110 ? 15.154  -18.695 44.520  1.00 53.09 ? 110  HIS E CE1 1 
ATOM   5274  N  NE2 . HIS E  1 110 ? 15.013  -17.858 45.534  1.00 53.74 ? 110  HIS E NE2 1 
ATOM   5275  N  N   . SER E  1 111 ? 18.241  -21.788 50.057  1.00 34.25 ? 111  SER E N   1 
ATOM   5276  C  CA  . SER E  1 111 ? 19.065  -22.839 50.624  1.00 29.95 ? 111  SER E CA  1 
ATOM   5277  C  C   . SER E  1 111 ? 18.365  -24.173 50.441  1.00 27.69 ? 111  SER E C   1 
ATOM   5278  O  O   . SER E  1 111 ? 17.183  -24.303 50.736  1.00 27.43 ? 111  SER E O   1 
ATOM   5279  C  CB  . SER E  1 111 ? 19.317  -22.584 52.104  1.00 31.17 ? 111  SER E CB  1 
ATOM   5280  O  OG  . SER E  1 111 ? 20.313  -23.460 52.598  1.00 31.74 ? 111  SER E OG  1 
ATOM   5281  N  N   . ILE E  1 112 ? 19.087  -25.160 49.930  1.00 27.26 ? 112  ILE E N   1 
ATOM   5282  C  CA  . ILE E  1 112 ? 18.552  -26.512 49.850  1.00 26.33 ? 112  ILE E CA  1 
ATOM   5283  C  C   . ILE E  1 112 ? 18.887  -27.337 51.100  1.00 24.77 ? 112  ILE E C   1 
ATOM   5284  O  O   . ILE E  1 112 ? 18.647  -28.538 51.129  1.00 23.79 ? 112  ILE E O   1 
ATOM   5285  C  CB  . ILE E  1 112 ? 19.034  -27.251 48.580  1.00 27.74 ? 112  ILE E CB  1 
ATOM   5286  C  CG1 . ILE E  1 112 ? 20.557  -27.414 48.593  1.00 25.33 ? 112  ILE E CG1 1 
ATOM   5287  C  CG2 . ILE E  1 112 ? 18.563  -26.513 47.318  1.00 28.01 ? 112  ILE E CG2 1 
ATOM   5288  C  CD1 . ILE E  1 112 ? 21.091  -28.237 47.439  1.00 23.98 ? 112  ILE E CD1 1 
ATOM   5289  N  N   . ILE E  1 113 ? 19.436  -26.691 52.130  1.00 25.74 ? 113  ILE E N   1 
ATOM   5290  C  CA  . ILE E  1 113 ? 19.723  -27.381 53.390  1.00 26.58 ? 113  ILE E CA  1 
ATOM   5291  C  C   . ILE E  1 113 ? 18.425  -27.731 54.111  1.00 26.84 ? 113  ILE E C   1 
ATOM   5292  O  O   . ILE E  1 113 ? 17.575  -26.862 54.328  1.00 26.29 ? 113  ILE E O   1 
ATOM   5293  C  CB  . ILE E  1 113 ? 20.605  -26.550 54.353  1.00 28.88 ? 113  ILE E CB  1 
ATOM   5294  C  CG1 . ILE E  1 113 ? 21.942  -26.201 53.707  1.00 27.35 ? 113  ILE E CG1 1 
ATOM   5295  C  CG2 . ILE E  1 113 ? 20.870  -27.342 55.626  1.00 26.40 ? 113  ILE E CG2 1 
ATOM   5296  C  CD1 . ILE E  1 113 ? 22.810  -27.389 53.498  1.00 27.41 ? 113  ILE E CD1 1 
ATOM   5297  N  N   . GLY E  1 114 ? 18.282  -29.001 54.485  1.00 24.20 ? 114  GLY E N   1 
ATOM   5298  C  CA  . GLY E  1 114 ? 17.062  -29.482 55.098  1.00 21.63 ? 114  GLY E CA  1 
ATOM   5299  C  C   . GLY E  1 114 ? 15.984  -29.842 54.091  1.00 25.00 ? 114  GLY E C   1 
ATOM   5300  O  O   . GLY E  1 114 ? 14.808  -29.936 54.442  1.00 26.18 ? 114  GLY E O   1 
ATOM   5301  N  N   . ARG E  1 115 ? 16.371  -30.038 52.835  1.00 25.23 ? 115  ARG E N   1 
ATOM   5302  C  CA  . ARG E  1 115 ? 15.434  -30.501 51.809  1.00 24.45 ? 115  ARG E CA  1 
ATOM   5303  C  C   . ARG E  1 115 ? 15.889  -31.869 51.317  1.00 23.03 ? 115  ARG E C   1 
ATOM   5304  O  O   . ARG E  1 115 ? 16.765  -32.466 51.933  1.00 23.22 ? 115  ARG E O   1 
ATOM   5305  C  CB  . ARG E  1 115 ? 15.287  -29.473 50.681  1.00 22.59 ? 115  ARG E CB  1 
ATOM   5306  C  CG  . ARG E  1 115 ? 14.957  -28.081 51.216  1.00 24.17 ? 115  ARG E CG  1 
ATOM   5307  C  CD  . ARG E  1 115 ? 14.548  -27.102 50.133  1.00 27.17 ? 115  ARG E CD  1 
ATOM   5308  N  NE  . ARG E  1 115 ? 14.366  -25.751 50.667  1.00 26.96 ? 115  ARG E NE  1 
ATOM   5309  C  CZ  . ARG E  1 115 ? 13.221  -25.290 51.163  1.00 28.29 ? 115  ARG E CZ  1 
ATOM   5310  N  NH1 . ARG E  1 115 ? 12.150  -26.079 51.193  1.00 29.62 ? 115  ARG E NH1 1 
ATOM   5311  N  NH2 . ARG E  1 115 ? 13.137  -24.044 51.627  1.00 25.08 ? 115  ARG E NH2 1 
ATOM   5312  N  N   . THR E  1 116 ? 15.301  -32.372 50.230  1.00 27.57 ? 116  THR E N   1 
ATOM   5313  C  CA  . THR E  1 116 ? 15.536  -33.766 49.818  1.00 27.40 ? 116  THR E CA  1 
ATOM   5314  C  C   . THR E  1 116 ? 16.121  -33.932 48.411  1.00 27.96 ? 116  THR E C   1 
ATOM   5315  O  O   . THR E  1 116 ? 15.629  -33.335 47.459  1.00 26.84 ? 116  THR E O   1 
ATOM   5316  C  CB  . THR E  1 116 ? 14.243  -34.613 49.933  1.00 25.94 ? 116  THR E CB  1 
ATOM   5317  O  OG1 . THR E  1 116 ? 13.772  -34.584 51.285  1.00 28.17 ? 116  THR E OG1 1 
ATOM   5318  C  CG2 . THR E  1 116 ? 14.498  -36.054 49.533  1.00 26.99 ? 116  THR E CG2 1 
ATOM   5319  N  N   . MET E  1 117 ? 17.187  -34.728 48.297  1.00 28.28 ? 117  MET E N   1 
ATOM   5320  C  CA  . MET E  1 117 ? 17.698  -35.147 46.995  1.00 27.93 ? 117  MET E CA  1 
ATOM   5321  C  C   . MET E  1 117 ? 17.040  -36.458 46.595  1.00 28.21 ? 117  MET E C   1 
ATOM   5322  O  O   . MET E  1 117 ? 17.060  -37.421 47.362  1.00 25.94 ? 117  MET E O   1 
ATOM   5323  C  CB  . MET E  1 117 ? 19.222  -35.349 47.018  1.00 27.53 ? 117  MET E CB  1 
ATOM   5324  C  CG  . MET E  1 117 ? 20.063  -34.081 46.821  1.00 31.12 ? 117  MET E CG  1 
ATOM   5325  S  SD  . MET E  1 117 ? 19.793  -33.125 45.302  1.00 33.69 ? 117  MET E SD  1 
ATOM   5326  C  CE  . MET E  1 117 ? 19.799  -34.419 44.074  1.00 28.52 ? 117  MET E CE  1 
ATOM   5327  N  N   . VAL E  1 118 ? 16.453  -36.509 45.401  1.00 28.37 ? 118  VAL E N   1 
ATOM   5328  C  CA  . VAL E  1 118 ? 16.025  -37.806 44.867  1.00 29.85 ? 118  VAL E CA  1 
ATOM   5329  C  C   . VAL E  1 118 ? 16.567  -38.117 43.474  1.00 28.19 ? 118  VAL E C   1 
ATOM   5330  O  O   . VAL E  1 118 ? 16.633  -37.263 42.594  1.00 28.59 ? 118  VAL E O   1 
ATOM   5331  C  CB  . VAL E  1 118 ? 14.477  -38.105 45.029  1.00 28.38 ? 118  VAL E CB  1 
ATOM   5332  C  CG1 . VAL E  1 118 ? 13.666  -36.853 44.951  1.00 28.13 ? 118  VAL E CG1 1 
ATOM   5333  C  CG2 . VAL E  1 118 ? 13.990  -39.146 44.027  1.00 27.23 ? 118  VAL E CG2 1 
ATOM   5334  N  N   . VAL E  1 119 ? 17.023  -39.352 43.328  1.00 27.10 ? 119  VAL E N   1 
ATOM   5335  C  CA  . VAL E  1 119 ? 17.393  -39.902 42.044  1.00 28.36 ? 119  VAL E CA  1 
ATOM   5336  C  C   . VAL E  1 119 ? 16.161  -40.673 41.584  1.00 29.13 ? 119  VAL E C   1 
ATOM   5337  O  O   . VAL E  1 119 ? 15.541  -41.389 42.381  1.00 27.83 ? 119  VAL E O   1 
ATOM   5338  C  CB  . VAL E  1 119 ? 18.667  -40.799 42.159  1.00 28.63 ? 119  VAL E CB  1 
ATOM   5339  C  CG1 . VAL E  1 119 ? 18.516  -41.855 43.249  1.00 26.83 ? 119  VAL E CG1 1 
ATOM   5340  C  CG2 . VAL E  1 119 ? 19.029  -41.427 40.814  1.00 29.07 ? 119  VAL E CG2 1 
ATOM   5341  N  N   . HIS E  1 120 ? 15.783  -40.495 40.320  1.00 26.29 ? 120  HIS E N   1 
ATOM   5342  C  CA  . HIS E  1 120 ? 14.522  -41.043 39.808  1.00 30.18 ? 120  HIS E CA  1 
ATOM   5343  C  C   . HIS E  1 120 ? 14.697  -42.341 39.005  1.00 34.12 ? 120  HIS E C   1 
ATOM   5344  O  O   . HIS E  1 120 ? 15.838  -42.766 38.734  1.00 32.74 ? 120  HIS E O   1 
ATOM   5345  C  CB  . HIS E  1 120 ? 13.773  -40.000 38.969  1.00 27.97 ? 120  HIS E CB  1 
ATOM   5346  C  CG  . HIS E  1 120 ? 13.020  -38.997 39.782  1.00 28.95 ? 120  HIS E CG  1 
ATOM   5347  N  ND1 . HIS E  1 120 ? 13.604  -37.857 40.290  1.00 28.56 ? 120  HIS E ND1 1 
ATOM   5348  C  CD2 . HIS E  1 120 ? 11.724  -38.959 40.168  1.00 31.29 ? 120  HIS E CD2 1 
ATOM   5349  C  CE1 . HIS E  1 120 ? 12.702  -37.165 40.960  1.00 28.29 ? 120  HIS E CE1 1 
ATOM   5350  N  NE2 . HIS E  1 120 ? 11.551  -37.812 40.901  1.00 29.76 ? 120  HIS E NE2 1 
ATOM   5351  N  N   . GLU E  1 121 ? 13.557  -42.939 38.629  1.00 31.85 ? 121  GLU E N   1 
ATOM   5352  C  CA  . GLU E  1 121 ? 13.471  -44.213 37.891  1.00 33.09 ? 121  GLU E CA  1 
ATOM   5353  C  C   . GLU E  1 121 ? 13.940  -44.139 36.426  1.00 35.23 ? 121  GLU E C   1 
ATOM   5354  O  O   . GLU E  1 121 ? 14.601  -45.057 35.925  1.00 34.66 ? 121  GLU E O   1 
ATOM   5355  C  CB  . GLU E  1 121 ? 12.025  -44.745 37.938  1.00 35.99 ? 121  GLU E CB  1 
ATOM   5356  C  CG  . GLU E  1 121 ? 11.666  -45.790 36.855  1.00 38.78 ? 121  GLU E CG  1 
ATOM   5357  C  CD  . GLU E  1 121 ? 10.161  -45.860 36.533  1.00 38.36 ? 121  GLU E CD  1 
ATOM   5358  O  OE1 . GLU E  1 121 ? 9.449   -44.847 36.721  1.00 38.79 ? 121  GLU E OE1 1 
ATOM   5359  O  OE2 . GLU E  1 121 ? 9.691   -46.928 36.076  1.00 39.36 ? 121  GLU E OE2 1 
ATOM   5360  N  N   . LYS E  1 122 ? 13.583  -43.055 35.743  1.00 33.46 ? 122  LYS E N   1 
ATOM   5361  C  CA  . LYS E  1 122 ? 13.895  -42.902 34.334  1.00 32.35 ? 122  LYS E CA  1 
ATOM   5362  C  C   . LYS E  1 122 ? 14.631  -41.592 34.074  1.00 34.21 ? 122  LYS E C   1 
ATOM   5363  O  O   . LYS E  1 122 ? 14.972  -40.846 34.996  1.00 31.47 ? 122  LYS E O   1 
ATOM   5364  C  CB  . LYS E  1 122 ? 12.612  -42.915 33.489  1.00 34.23 ? 122  LYS E CB  1 
ATOM   5365  C  CG  . LYS E  1 122 ? 11.457  -43.723 34.065  1.00 37.63 ? 122  LYS E CG  1 
ATOM   5366  C  CD  . LYS E  1 122 ? 10.123  -43.026 33.818  1.00 39.10 ? 122  LYS E CD  1 
ATOM   5367  C  CE  . LYS E  1 122 ? 9.423   -43.570 32.593  1.00 43.15 ? 122  LYS E CE  1 
ATOM   5368  N  NZ  . LYS E  1 122 ? 8.992   -44.984 32.815  1.00 49.19 ? 122  LYS E NZ  1 
ATOM   5369  N  N   . GLN E  1 123 ? 14.838  -41.317 32.791  1.00 32.06 ? 123  GLN E N   1 
ATOM   5370  C  CA  . GLN E  1 123 ? 15.546  -40.137 32.325  1.00 32.77 ? 123  GLN E CA  1 
ATOM   5371  C  C   . GLN E  1 123 ? 14.663  -38.895 32.400  1.00 32.49 ? 123  GLN E C   1 
ATOM   5372  O  O   . GLN E  1 123 ? 13.505  -38.916 31.989  1.00 33.89 ? 123  GLN E O   1 
ATOM   5373  C  CB  . GLN E  1 123 ? 16.007  -40.373 30.881  1.00 33.04 ? 123  GLN E CB  1 
ATOM   5374  C  CG  . GLN E  1 123 ? 16.874  -39.286 30.289  1.00 35.07 ? 123  GLN E CG  1 
ATOM   5375  C  CD  . GLN E  1 123 ? 17.054  -39.450 28.793  1.00 32.53 ? 123  GLN E CD  1 
ATOM   5376  O  OE1 . GLN E  1 123 ? 16.860  -40.541 28.253  1.00 35.01 ? 123  GLN E OE1 1 
ATOM   5377  N  NE2 . GLN E  1 123 ? 17.423  -38.368 28.115  1.00 27.63 ? 123  GLN E NE2 1 
ATOM   5378  N  N   . ASP E  1 124 ? 15.214  -37.814 32.936  1.00 31.54 ? 124  ASP E N   1 
ATOM   5379  C  CA  . ASP E  1 124 ? 14.520  -36.536 32.975  1.00 29.92 ? 124  ASP E CA  1 
ATOM   5380  C  C   . ASP E  1 124 ? 14.617  -35.888 31.588  1.00 32.83 ? 124  ASP E C   1 
ATOM   5381  O  O   . ASP E  1 124 ? 15.720  -35.602 31.115  1.00 34.36 ? 124  ASP E O   1 
ATOM   5382  C  CB  . ASP E  1 124 ? 15.166  -35.662 34.057  1.00 28.35 ? 124  ASP E CB  1 
ATOM   5383  C  CG  . ASP E  1 124 ? 14.713  -34.215 34.010  1.00 30.50 ? 124  ASP E CG  1 
ATOM   5384  O  OD1 . ASP E  1 124 ? 13.923  -33.836 33.124  1.00 29.32 ? 124  ASP E OD1 1 
ATOM   5385  O  OD2 . ASP E  1 124 ? 15.158  -33.444 34.882  1.00 33.17 ? 124  ASP E OD2 1 
ATOM   5386  N  N   . ASP E  1 125 ? 13.476  -35.664 30.931  1.00 32.29 ? 125  ASP E N   1 
ATOM   5387  C  CA  . ASP E  1 125 ? 13.481  -35.104 29.574  1.00 30.86 ? 125  ASP E CA  1 
ATOM   5388  C  C   . ASP E  1 125 ? 13.729  -33.600 29.530  1.00 31.15 ? 125  ASP E C   1 
ATOM   5389  O  O   . ASP E  1 125 ? 13.666  -32.986 28.467  1.00 33.67 ? 125  ASP E O   1 
ATOM   5390  C  CB  . ASP E  1 125 ? 12.193  -35.453 28.816  1.00 31.95 ? 125  ASP E CB  1 
ATOM   5391  C  CG  . ASP E  1 125 ? 10.964  -34.781 29.396  1.00 34.36 ? 125  ASP E CG  1 
ATOM   5392  O  OD1 . ASP E  1 125 ? 11.101  -33.761 30.111  1.00 34.55 ? 125  ASP E OD1 1 
ATOM   5393  O  OD2 . ASP E  1 125 ? 9.850   -35.279 29.131  1.00 36.20 ? 125  ASP E OD2 1 
ATOM   5394  N  N   . LEU E  1 126 ? 13.997  -33.015 30.691  1.00 31.88 ? 126  LEU E N   1 
ATOM   5395  C  CA  . LEU E  1 126 ? 14.365  -31.603 30.806  1.00 30.96 ? 126  LEU E CA  1 
ATOM   5396  C  C   . LEU E  1 126 ? 13.282  -30.633 30.344  1.00 31.07 ? 126  LEU E C   1 
ATOM   5397  O  O   . LEU E  1 126 ? 13.589  -29.506 29.953  1.00 33.76 ? 126  LEU E O   1 
ATOM   5398  C  CB  . LEU E  1 126 ? 15.675  -31.324 30.063  1.00 32.80 ? 126  LEU E CB  1 
ATOM   5399  C  CG  . LEU E  1 126 ? 16.834  -32.296 30.318  1.00 33.28 ? 126  LEU E CG  1 
ATOM   5400  C  CD1 . LEU E  1 126 ? 18.038  -31.929 29.466  1.00 33.72 ? 126  LEU E CD1 1 
ATOM   5401  C  CD2 . LEU E  1 126 ? 17.212  -32.335 31.794  1.00 29.36 ? 126  LEU E CD2 1 
ATOM   5402  N  N   . GLY E  1 127 ? 12.022  -31.063 30.387  1.00 29.09 ? 127  GLY E N   1 
ATOM   5403  C  CA  . GLY E  1 127 ? 10.920  -30.200 29.990  1.00 32.68 ? 127  GLY E CA  1 
ATOM   5404  C  C   . GLY E  1 127 ? 10.742  -30.031 28.488  1.00 32.91 ? 127  GLY E C   1 
ATOM   5405  O  O   . GLY E  1 127 ? 10.234  -29.014 28.011  1.00 33.20 ? 127  GLY E O   1 
ATOM   5406  N  N   . LYS E  1 128 ? 11.161  -31.043 27.738  1.00 35.62 ? 128  LYS E N   1 
ATOM   5407  C  CA  . LYS E  1 128 ? 11.138  -31.000 26.281  1.00 35.14 ? 128  LYS E CA  1 
ATOM   5408  C  C   . LYS E  1 128 ? 10.328  -32.175 25.766  1.00 36.39 ? 128  LYS E C   1 
ATOM   5409  O  O   . LYS E  1 128 ? 10.406  -32.533 24.580  1.00 37.69 ? 128  LYS E O   1 
ATOM   5410  C  CB  . LYS E  1 128 ? 12.564  -31.039 25.726  1.00 34.57 ? 128  LYS E CB  1 
ATOM   5411  C  CG  . LYS E  1 128 ? 13.490  -30.067 26.437  1.00 36.29 ? 128  LYS E CG  1 
ATOM   5412  C  CD  . LYS E  1 128 ? 14.471  -29.423 25.498  1.00 37.68 ? 128  LYS E CD  1 
ATOM   5413  C  CE  . LYS E  1 128 ? 14.985  -28.120 26.093  1.00 43.60 ? 128  LYS E CE  1 
ATOM   5414  N  NZ  . LYS E  1 128 ? 13.959  -27.036 26.068  1.00 41.46 ? 128  LYS E NZ  1 
ATOM   5415  N  N   . GLY E  1 129 ? 9.531   -32.746 26.668  1.00 34.58 ? 129  GLY E N   1 
ATOM   5416  C  CA  . GLY E  1 129 ? 8.772   -33.946 26.384  1.00 34.33 ? 129  GLY E CA  1 
ATOM   5417  C  C   . GLY E  1 129 ? 7.453   -33.719 25.677  1.00 35.40 ? 129  GLY E C   1 
ATOM   5418  O  O   . GLY E  1 129 ? 6.838   -34.679 25.205  1.00 39.71 ? 129  GLY E O   1 
ATOM   5419  N  N   . GLY E  1 130 ? 7.000   -32.472 25.603  1.00 29.74 ? 130  GLY E N   1 
ATOM   5420  C  CA  . GLY E  1 130 ? 5.777   -32.191 24.868  1.00 35.43 ? 130  GLY E CA  1 
ATOM   5421  C  C   . GLY E  1 130 ? 4.464   -32.649 25.498  1.00 36.45 ? 130  GLY E C   1 
ATOM   5422  O  O   . GLY E  1 130 ? 3.406   -32.505 24.901  1.00 35.23 ? 130  GLY E O   1 
ATOM   5423  N  N   . ASN E  1 131 ? 4.523   -33.214 26.697  1.00 37.72 ? 131  ASN E N   1 
ATOM   5424  C  CA  . ASN E  1 131 ? 3.319   -33.402 27.499  1.00 36.98 ? 131  ASN E CA  1 
ATOM   5425  C  C   . ASN E  1 131 ? 3.326   -32.506 28.746  1.00 40.80 ? 131  ASN E C   1 
ATOM   5426  O  O   . ASN E  1 131 ? 4.307   -31.808 29.013  1.00 41.51 ? 131  ASN E O   1 
ATOM   5427  C  CB  . ASN E  1 131 ? 3.125   -34.875 27.873  1.00 38.20 ? 131  ASN E CB  1 
ATOM   5428  C  CG  . ASN E  1 131 ? 4.218   -35.404 28.787  1.00 42.55 ? 131  ASN E CG  1 
ATOM   5429  O  OD1 . ASN E  1 131 ? 5.167   -34.690 29.126  1.00 40.74 ? 131  ASN E OD1 1 
ATOM   5430  N  ND2 . ASN E  1 131 ? 4.087   -36.668 29.194  1.00 43.14 ? 131  ASN E ND2 1 
ATOM   5431  N  N   . GLU E  1 132 ? 2.231   -32.519 29.499  1.00 42.30 ? 132  GLU E N   1 
ATOM   5432  C  CA  . GLU E  1 132 ? 2.111   -31.685 30.696  1.00 44.36 ? 132  GLU E CA  1 
ATOM   5433  C  C   . GLU E  1 132 ? 3.076   -32.129 31.825  1.00 43.28 ? 132  GLU E C   1 
ATOM   5434  O  O   . GLU E  1 132 ? 3.611   -31.288 32.560  1.00 40.32 ? 132  GLU E O   1 
ATOM   5435  C  CB  . GLU E  1 132 ? 0.652   -31.658 31.189  1.00 45.81 ? 132  GLU E CB  1 
ATOM   5436  C  CG  . GLU E  1 132 ? 0.357   -30.579 32.236  1.00 48.92 ? 132  GLU E CG  1 
ATOM   5437  C  CD  . GLU E  1 132 ? -0.993  -30.765 32.947  1.00 58.10 ? 132  GLU E CD  1 
ATOM   5438  O  OE1 . GLU E  1 132 ? -1.842  -31.535 32.440  1.00 62.95 ? 132  GLU E OE1 1 
ATOM   5439  O  OE2 . GLU E  1 132 ? -1.207  -30.134 34.012  1.00 56.70 ? 132  GLU E OE2 1 
ATOM   5440  N  N   . GLU E  1 133 ? 3.293   -33.443 31.951  1.00 40.98 ? 133  GLU E N   1 
ATOM   5441  C  CA  . GLU E  1 133 ? 4.238   -34.003 32.929  1.00 40.97 ? 133  GLU E CA  1 
ATOM   5442  C  C   . GLU E  1 133 ? 5.648   -33.444 32.786  1.00 38.26 ? 133  GLU E C   1 
ATOM   5443  O  O   . GLU E  1 133 ? 6.338   -33.220 33.770  1.00 34.17 ? 133  GLU E O   1 
ATOM   5444  C  CB  . GLU E  1 133 ? 4.315   -35.528 32.807  1.00 41.81 ? 133  GLU E CB  1 
ATOM   5445  C  CG  . GLU E  1 133 ? 3.292   -36.251 33.626  1.00 47.19 ? 133  GLU E CG  1 
ATOM   5446  C  CD  . GLU E  1 133 ? 3.272   -35.756 35.048  1.00 46.55 ? 133  GLU E CD  1 
ATOM   5447  O  OE1 . GLU E  1 133 ? 4.350   -35.742 35.686  1.00 46.31 ? 133  GLU E OE1 1 
ATOM   5448  O  OE2 . GLU E  1 133 ? 2.178   -35.374 35.519  1.00 51.62 ? 133  GLU E OE2 1 
ATOM   5449  N  N   . SER E  1 134 ? 6.059   -33.246 31.540  1.00 38.23 ? 134  SER E N   1 
ATOM   5450  C  CA  . SER E  1 134 ? 7.381   -32.766 31.199  1.00 34.69 ? 134  SER E CA  1 
ATOM   5451  C  C   . SER E  1 134 ? 7.651   -31.397 31.818  1.00 34.53 ? 134  SER E C   1 
ATOM   5452  O  O   . SER E  1 134 ? 8.768   -31.115 32.242  1.00 34.91 ? 134  SER E O   1 
ATOM   5453  C  CB  . SER E  1 134 ? 7.503   -32.710 29.673  1.00 35.03 ? 134  SER E CB  1 
ATOM   5454  O  OG  . SER E  1 134 ? 8.780   -32.280 29.247  1.00 35.70 ? 134  SER E OG  1 
ATOM   5455  N  N   . THR E  1 135 ? 6.629   -30.547 31.868  1.00 36.44 ? 135  THR E N   1 
ATOM   5456  C  CA  . THR E  1 135 ? 6.753   -29.212 32.462  1.00 36.37 ? 135  THR E CA  1 
ATOM   5457  C  C   . THR E  1 135 ? 6.656   -29.277 33.997  1.00 35.20 ? 135  THR E C   1 
ATOM   5458  O  O   . THR E  1 135 ? 6.539   -28.252 34.675  1.00 32.56 ? 135  THR E O   1 
ATOM   5459  C  CB  . THR E  1 135 ? 5.648   -28.255 31.941  1.00 39.51 ? 135  THR E CB  1 
ATOM   5460  O  OG1 . THR E  1 135 ? 4.378   -28.628 32.502  1.00 38.04 ? 135  THR E OG1 1 
ATOM   5461  C  CG2 . THR E  1 135 ? 5.563   -28.285 30.417  1.00 36.24 ? 135  THR E CG2 1 
ATOM   5462  N  N   . LYS E  1 136 ? 6.705   -30.493 34.532  1.00 35.55 ? 136  LYS E N   1 
ATOM   5463  C  CA  . LYS E  1 136 ? 6.470   -30.730 35.948  1.00 34.37 ? 136  LYS E CA  1 
ATOM   5464  C  C   . LYS E  1 136 ? 7.602   -31.543 36.564  1.00 30.41 ? 136  LYS E C   1 
ATOM   5465  O  O   . LYS E  1 136 ? 8.296   -31.077 37.458  1.00 28.58 ? 136  LYS E O   1 
ATOM   5466  C  CB  . LYS E  1 136 ? 5.166   -31.512 36.116  1.00 35.61 ? 136  LYS E CB  1 
ATOM   5467  C  CG  . LYS E  1 136 ? 4.266   -31.019 37.214  1.00 37.09 ? 136  LYS E CG  1 
ATOM   5468  C  CD  . LYS E  1 136 ? 3.175   -30.130 36.641  1.00 43.92 ? 136  LYS E CD  1 
ATOM   5469  C  CE  . LYS E  1 136 ? 2.128   -30.959 35.894  1.00 47.49 ? 136  LYS E CE  1 
ATOM   5470  N  NZ  . LYS E  1 136 ? 1.517   -32.013 36.763  1.00 46.54 ? 136  LYS E NZ  1 
ATOM   5471  N  N   . THR E  1 137 ? 7.758   -32.773 36.081  1.00 30.98 ? 137  THR E N   1 
ATOM   5472  C  CA  . THR E  1 137 ? 8.690   -33.735 36.650  1.00 29.37 ? 137  THR E CA  1 
ATOM   5473  C  C   . THR E  1 137 ? 9.778   -34.173 35.657  1.00 31.51 ? 137  THR E C   1 
ATOM   5474  O  O   . THR E  1 137 ? 10.715  -34.888 36.025  1.00 29.05 ? 137  THR E O   1 
ATOM   5475  C  CB  . THR E  1 137 ? 7.945   -34.993 37.166  1.00 31.08 ? 137  THR E CB  1 
ATOM   5476  O  OG1 . THR E  1 137 ? 7.463   -35.774 36.066  1.00 27.54 ? 137  THR E OG1 1 
ATOM   5477  C  CG2 . THR E  1 137 ? 6.776   -34.599 38.045  1.00 32.09 ? 137  THR E CG2 1 
ATOM   5478  N  N   . GLY E  1 138 ? 9.647   -33.740 34.406  1.00 30.65 ? 138  GLY E N   1 
ATOM   5479  C  CA  . GLY E  1 138 ? 10.555  -34.144 33.353  1.00 30.27 ? 138  GLY E CA  1 
ATOM   5480  C  C   . GLY E  1 138 ? 10.277  -35.557 32.875  1.00 32.64 ? 138  GLY E C   1 
ATOM   5481  O  O   . GLY E  1 138 ? 11.040  -36.121 32.082  1.00 32.28 ? 138  GLY E O   1 
ATOM   5482  N  N   . ASN E  1 139 ? 9.174   -36.128 33.352  1.00 31.78 ? 139  ASN E N   1 
ATOM   5483  C  CA  . ASN E  1 139 ? 8.799   -37.497 33.015  1.00 32.30 ? 139  ASN E CA  1 
ATOM   5484  C  C   . ASN E  1 139 ? 9.727   -38.518 33.654  1.00 33.27 ? 139  ASN E C   1 
ATOM   5485  O  O   . ASN E  1 139 ? 9.708   -39.698 33.304  1.00 34.38 ? 139  ASN E O   1 
ATOM   5486  C  CB  . ASN E  1 139 ? 8.756   -37.688 31.497  1.00 35.84 ? 139  ASN E CB  1 
ATOM   5487  C  CG  . ASN E  1 139 ? 7.476   -37.169 30.882  1.00 34.96 ? 139  ASN E CG  1 
ATOM   5488  O  OD1 . ASN E  1 139 ? 6.397   -37.718 31.114  1.00 33.47 ? 139  ASN E OD1 1 
ATOM   5489  N  ND2 . ASN E  1 139 ? 7.586   -36.109 30.088  1.00 34.52 ? 139  ASN E ND2 1 
ATOM   5490  N  N   . ALA E  1 140 ? 10.523  -38.061 34.615  1.00 34.06 ? 140  ALA E N   1 
ATOM   5491  C  CA  . ALA E  1 140 ? 11.583  -38.886 35.171  1.00 33.22 ? 140  ALA E CA  1 
ATOM   5492  C  C   . ALA E  1 140 ? 11.048  -40.085 35.957  1.00 35.10 ? 140  ALA E C   1 
ATOM   5493  O  O   . ALA E  1 140 ? 11.794  -41.014 36.260  1.00 35.38 ? 140  ALA E O   1 
ATOM   5494  C  CB  . ALA E  1 140 ? 12.530  -38.041 36.018  1.00 30.55 ? 140  ALA E CB  1 
ATOM   5495  N  N   . GLY E  1 141 ? 9.759   -40.067 36.279  1.00 34.69 ? 141  GLY E N   1 
ATOM   5496  C  CA  . GLY E  1 141 ? 9.121   -41.213 36.904  1.00 34.96 ? 141  GLY E CA  1 
ATOM   5497  C  C   . GLY E  1 141 ? 9.270   -41.321 38.415  1.00 36.78 ? 141  GLY E C   1 
ATOM   5498  O  O   . GLY E  1 141 ? 9.325   -40.307 39.126  1.00 35.61 ? 141  GLY E O   1 
ATOM   5499  N  N   . SER E  1 142 ? 9.338   -42.561 38.904  1.00 37.59 ? 142  SER E N   1 
ATOM   5500  C  CA  . SER E  1 142 ? 9.315   -42.843 40.344  1.00 37.81 ? 142  SER E CA  1 
ATOM   5501  C  C   . SER E  1 142 ? 10.606  -42.482 41.080  1.00 35.38 ? 142  SER E C   1 
ATOM   5502  O  O   . SER E  1 142 ? 11.659  -42.300 40.458  1.00 33.63 ? 142  SER E O   1 
ATOM   5503  C  CB  . SER E  1 142 ? 8.958   -44.314 40.604  1.00 36.30 ? 142  SER E CB  1 
ATOM   5504  O  OG  . SER E  1 142 ? 9.991   -45.184 40.174  1.00 35.31 ? 142  SER E OG  1 
ATOM   5505  N  N   . ARG E  1 143 ? 10.505  -42.406 42.410  1.00 35.45 ? 143  ARG E N   1 
ATOM   5506  C  CA  . ARG E  1 143 ? 11.622  -42.029 43.283  1.00 32.91 ? 143  ARG E CA  1 
ATOM   5507  C  C   . ARG E  1 143 ? 12.357  -43.248 43.866  1.00 32.67 ? 143  ARG E C   1 
ATOM   5508  O  O   . ARG E  1 143 ? 11.860  -43.922 44.770  1.00 34.97 ? 143  ARG E O   1 
ATOM   5509  C  CB  . ARG E  1 143 ? 11.120  -41.097 44.387  1.00 29.06 ? 143  ARG E CB  1 
ATOM   5510  C  CG  . ARG E  1 143 ? 10.150  -40.057 43.856  1.00 26.82 ? 143  ARG E CG  1 
ATOM   5511  C  CD  . ARG E  1 143 ? 9.700   -39.039 44.891  1.00 28.26 ? 143  ARG E CD  1 
ATOM   5512  N  NE  . ARG E  1 143 ? 8.885   -38.013 44.250  1.00 28.26 ? 143  ARG E NE  1 
ATOM   5513  C  CZ  . ARG E  1 143 ? 8.307   -36.994 44.877  1.00 29.97 ? 143  ARG E CZ  1 
ATOM   5514  N  NH1 . ARG E  1 143 ? 8.434   -36.853 46.190  1.00 30.13 ? 143  ARG E NH1 1 
ATOM   5515  N  NH2 . ARG E  1 143 ? 7.590   -36.117 44.184  1.00 27.55 ? 143  ARG E NH2 1 
ATOM   5516  N  N   . LEU E  1 144 ? 13.546  -43.513 43.332  1.00 31.42 ? 144  LEU E N   1 
ATOM   5517  C  CA  . LEU E  1 144 ? 14.318  -44.713 43.651  1.00 30.69 ? 144  LEU E CA  1 
ATOM   5518  C  C   . LEU E  1 144 ? 15.011  -44.611 45.005  1.00 34.92 ? 144  LEU E C   1 
ATOM   5519  O  O   . LEU E  1 144 ? 15.075  -45.592 45.752  1.00 33.84 ? 144  LEU E O   1 
ATOM   5520  C  CB  . LEU E  1 144 ? 15.380  -44.962 42.574  1.00 29.22 ? 144  LEU E CB  1 
ATOM   5521  C  CG  . LEU E  1 144 ? 14.886  -45.193 41.146  1.00 32.25 ? 144  LEU E CG  1 
ATOM   5522  C  CD1 . LEU E  1 144 ? 16.046  -45.475 40.206  1.00 30.71 ? 144  LEU E CD1 1 
ATOM   5523  C  CD2 . LEU E  1 144 ? 13.889  -46.335 41.131  1.00 36.40 ? 144  LEU E CD2 1 
ATOM   5524  N  N   . ALA E  1 145 ? 15.555  -43.431 45.295  1.00 31.98 ? 145  ALA E N   1 
ATOM   5525  C  CA  . ALA E  1 145 ? 16.273  -43.184 46.543  1.00 32.14 ? 145  ALA E CA  1 
ATOM   5526  C  C   . ALA E  1 145 ? 16.219  -41.704 46.875  1.00 29.12 ? 145  ALA E C   1 
ATOM   5527  O  O   . ALA E  1 145 ? 16.032  -40.873 45.996  1.00 30.55 ? 145  ALA E O   1 
ATOM   5528  C  CB  . ALA E  1 145 ? 17.736  -43.658 46.439  1.00 31.54 ? 145  ALA E CB  1 
ATOM   5529  N  N   . CYS E  1 146 ? 16.378  -41.375 48.148  1.00 31.97 ? 146  CYS E N   1 
ATOM   5530  C  CA  . CYS E  1 146 ? 16.426  -39.981 48.560  1.00 29.39 ? 146  CYS E CA  1 
ATOM   5531  C  C   . CYS E  1 146 ? 17.070  -39.841 49.933  1.00 26.63 ? 146  CYS E C   1 
ATOM   5532  O  O   . CYS E  1 146 ? 17.300  -40.823 50.642  1.00 26.00 ? 146  CYS E O   1 
ATOM   5533  C  CB  . CYS E  1 146 ? 15.024  -39.374 48.576  1.00 28.96 ? 146  CYS E CB  1 
ATOM   5534  S  SG  . CYS E  1 146 ? 13.952  -40.113 49.824  1.00 34.31 ? 146  CYS E SG  1 
ATOM   5535  N  N   . GLY E  1 147 ? 17.360  -38.605 50.300  1.00 24.68 ? 147  GLY E N   1 
ATOM   5536  C  CA  . GLY E  1 147 ? 17.952  -38.326 51.584  1.00 24.32 ? 147  GLY E CA  1 
ATOM   5537  C  C   . GLY E  1 147 ? 17.780  -36.860 51.877  1.00 23.89 ? 147  GLY E C   1 
ATOM   5538  O  O   . GLY E  1 147 ? 17.556  -36.057 50.969  1.00 23.37 ? 147  GLY E O   1 
ATOM   5539  N  N   . VAL E  1 148 ? 17.874  -36.502 53.149  1.00 24.87 ? 148  VAL E N   1 
ATOM   5540  C  CA  . VAL E  1 148 ? 17.791  -35.099 53.512  1.00 24.07 ? 148  VAL E CA  1 
ATOM   5541  C  C   . VAL E  1 148 ? 19.173  -34.460 53.450  1.00 21.80 ? 148  VAL E C   1 
ATOM   5542  O  O   . VAL E  1 148 ? 20.175  -35.058 53.867  1.00 20.29 ? 148  VAL E O   1 
ATOM   5543  C  CB  . VAL E  1 148 ? 17.105  -34.916 54.862  1.00 21.24 ? 148  VAL E CB  1 
ATOM   5544  C  CG1 . VAL E  1 148 ? 16.959  -33.435 55.180  1.00 20.62 ? 148  VAL E CG1 1 
ATOM   5545  C  CG2 . VAL E  1 148 ? 15.747  -35.586 54.799  1.00 21.68 ? 148  VAL E CG2 1 
ATOM   5546  N  N   . ILE E  1 149 ? 19.221  -33.263 52.873  1.00 21.81 ? 149  ILE E N   1 
ATOM   5547  C  CA  . ILE E  1 149 ? 20.476  -32.555 52.680  1.00 22.30 ? 149  ILE E CA  1 
ATOM   5548  C  C   . ILE E  1 149 ? 20.899  -31.931 53.999  1.00 21.55 ? 149  ILE E C   1 
ATOM   5549  O  O   . ILE E  1 149 ? 20.239  -31.035 54.505  1.00 21.74 ? 149  ILE E O   1 
ATOM   5550  C  CB  . ILE E  1 149 ? 20.356  -31.466 51.593  1.00 23.24 ? 149  ILE E CB  1 
ATOM   5551  C  CG1 . ILE E  1 149 ? 19.911  -32.088 50.256  1.00 24.55 ? 149  ILE E CG1 1 
ATOM   5552  C  CG2 . ILE E  1 149 ? 21.680  -30.710 51.459  1.00 20.94 ? 149  ILE E CG2 1 
ATOM   5553  C  CD1 . ILE E  1 149 ? 19.235  -31.115 49.307  1.00 22.41 ? 149  ILE E CD1 1 
ATOM   5554  N  N   . GLY E  1 150 ? 21.998  -32.420 54.556  1.00 22.38 ? 150  GLY E N   1 
ATOM   5555  C  CA  . GLY E  1 150 ? 22.410  -32.008 55.875  1.00 19.86 ? 150  GLY E CA  1 
ATOM   5556  C  C   . GLY E  1 150 ? 23.720  -31.254 55.923  1.00 20.87 ? 150  GLY E C   1 
ATOM   5557  O  O   . GLY E  1 150 ? 24.557  -31.392 55.040  1.00 21.60 ? 150  GLY E O   1 
ATOM   5558  N  N   . ILE E  1 151 ? 23.877  -30.453 56.975  1.00 21.31 ? 151  ILE E N   1 
ATOM   5559  C  CA  . ILE E  1 151 ? 25.087  -29.690 57.239  1.00 22.11 ? 151  ILE E CA  1 
ATOM   5560  C  C   . ILE E  1 151 ? 26.243  -30.648 57.456  1.00 20.73 ? 151  ILE E C   1 
ATOM   5561  O  O   . ILE E  1 151 ? 26.154  -31.546 58.287  1.00 22.29 ? 151  ILE E O   1 
ATOM   5562  C  CB  . ILE E  1 151 ? 24.897  -28.790 58.485  1.00 21.71 ? 151  ILE E CB  1 
ATOM   5563  C  CG1 . ILE E  1 151 ? 23.795  -27.765 58.225  1.00 21.07 ? 151  ILE E CG1 1 
ATOM   5564  C  CG2 . ILE E  1 151 ? 26.186  -28.087 58.845  1.00 22.58 ? 151  ILE E CG2 1 
ATOM   5565  C  CD1 . ILE E  1 151 ? 23.377  -26.968 59.446  1.00 21.61 ? 151  ILE E CD1 1 
ATOM   5566  N  N   . ALA E  1 152 ? 27.316  -30.472 56.689  1.00 21.54 ? 152  ALA E N   1 
ATOM   5567  C  CA  . ALA E  1 152 ? 28.490  -31.331 56.791  1.00 23.29 ? 152  ALA E CA  1 
ATOM   5568  C  C   . ALA E  1 152 ? 29.674  -30.534 57.325  1.00 25.11 ? 152  ALA E C   1 
ATOM   5569  O  O   . ALA E  1 152 ? 29.705  -29.304 57.220  1.00 23.81 ? 152  ALA E O   1 
ATOM   5570  C  CB  . ALA E  1 152 ? 28.833  -31.942 55.423  1.00 22.42 ? 152  ALA E CB  1 
ATOM   5571  N  N   . GLN E  1 153 ? 30.652  -31.221 57.908  1.00 25.50 ? 153  GLN E N   1 
ATOM   5572  C  CA  . GLN E  1 153 ? 31.860  -30.512 58.317  1.00 30.59 ? 153  GLN E CA  1 
ATOM   5573  C  C   . GLN E  1 153 ? 32.863  -30.463 57.169  1.00 35.69 ? 153  GLN E C   1 
ATOM   5574  O  O   . GLN E  1 153 ? 33.518  -29.434 56.965  1.00 45.37 ? 153  GLN E O   1 
ATOM   5575  C  CB  . GLN E  1 153 ? 32.475  -31.072 59.622  1.00 30.94 ? 153  GLN E CB  1 
ATOM   5576  C  CG  . GLN E  1 153 ? 33.463  -32.231 59.483  1.00 33.33 ? 153  GLN E CG  1 
ATOM   5577  C  CD  . GLN E  1 153 ? 34.228  -32.496 60.775  1.00 31.72 ? 153  GLN E CD  1 
ATOM   5578  O  OE1 . GLN E  1 153 ? 34.484  -31.579 61.558  1.00 26.78 ? 153  GLN E OE1 1 
ATOM   5579  N  NE2 . GLN E  1 153 ? 34.596  -33.753 60.998  1.00 31.11 ? 153  GLN E NE2 1 
ATOM   5580  O  OXT . GLN E  1 153 ? 33.015  -31.427 56.404  1.00 35.01 ? 153  GLN E OXT 1 
ATOM   5581  N  N   . ALA F  1 1   ? 4.588   -19.967 60.371  1.00 47.68 ? 1    ALA F N   1 
ATOM   5582  C  CA  . ALA F  1 1   ? 5.136   -20.831 61.416  1.00 47.06 ? 1    ALA F CA  1 
ATOM   5583  C  C   . ALA F  1 1   ? 6.067   -21.903 60.846  1.00 41.71 ? 1    ALA F C   1 
ATOM   5584  O  O   . ALA F  1 1   ? 5.660   -22.705 60.001  1.00 44.40 ? 1    ALA F O   1 
ATOM   5585  C  CB  . ALA F  1 1   ? 4.003   -21.480 62.224  1.00 48.11 ? 1    ALA F CB  1 
ATOM   5586  N  N   . THR F  1 2   ? 7.308   -21.929 61.318  1.00 40.20 ? 2    THR F N   1 
ATOM   5587  C  CA  . THR F  1 2   ? 8.261   -22.940 60.861  1.00 38.50 ? 2    THR F CA  1 
ATOM   5588  C  C   . THR F  1 2   ? 7.914   -24.333 61.402  1.00 36.67 ? 2    THR F C   1 
ATOM   5589  O  O   . THR F  1 2   ? 7.324   -24.489 62.475  1.00 35.80 ? 2    THR F O   1 
ATOM   5590  C  CB  . THR F  1 2   ? 9.718   -22.589 61.226  1.00 33.48 ? 2    THR F CB  1 
ATOM   5591  O  OG1 . THR F  1 2   ? 9.885   -21.168 61.239  1.00 39.06 ? 2    THR F OG1 1 
ATOM   5592  C  CG2 . THR F  1 2   ? 10.680  -23.188 60.212  1.00 34.19 ? 2    THR F CG2 1 
ATOM   5593  N  N   . LYS F  1 3   ? 8.302   -25.344 60.642  1.00 35.83 ? 3    LYS F N   1 
ATOM   5594  C  CA  . LYS F  1 3   ? 7.918   -26.714 60.921  1.00 31.57 ? 3    LYS F CA  1 
ATOM   5595  C  C   . LYS F  1 3   ? 9.011   -27.617 60.350  1.00 31.19 ? 3    LYS F C   1 
ATOM   5596  O  O   . LYS F  1 3   ? 9.466   -27.415 59.209  1.00 31.82 ? 3    LYS F O   1 
ATOM   5597  C  CB  . LYS F  1 3   ? 6.566   -26.998 60.262  1.00 31.30 ? 3    LYS F CB  1 
ATOM   5598  C  CG  . LYS F  1 3   ? 5.640   -27.890 61.047  1.00 35.32 ? 3    LYS F CG  1 
ATOM   5599  C  CD  . LYS F  1 3   ? 4.189   -27.772 60.566  1.00 42.02 ? 3    LYS F CD  1 
ATOM   5600  C  CE  . LYS F  1 3   ? 3.365   -29.047 60.868  1.00 50.77 ? 3    LYS F CE  1 
ATOM   5601  N  NZ  . LYS F  1 3   ? 3.060   -29.292 62.326  1.00 41.70 ? 3    LYS F NZ  1 
ATOM   5602  N  N   . ALA F  1 4   ? 9.456   -28.585 61.151  1.00 25.67 ? 4    ALA F N   1 
ATOM   5603  C  CA  . ALA F  1 4   ? 10.468  -29.542 60.716  1.00 25.72 ? 4    ALA F CA  1 
ATOM   5604  C  C   . ALA F  1 4   ? 10.063  -30.961 61.075  1.00 27.11 ? 4    ALA F C   1 
ATOM   5605  O  O   . ALA F  1 4   ? 9.166   -31.168 61.888  1.00 26.95 ? 4    ALA F O   1 
ATOM   5606  C  CB  . ALA F  1 4   ? 11.819  -29.210 61.333  1.00 24.68 ? 4    ALA F CB  1 
ATOM   5607  N  N   . VAL F  1 5   ? 10.725  -31.944 60.472  1.00 27.31 ? 5    VAL F N   1 
ATOM   5608  C  CA  . VAL F  1 5   ? 10.456  -33.342 60.797  1.00 25.22 ? 5    VAL F CA  1 
ATOM   5609  C  C   . VAL F  1 5   ? 11.737  -34.172 60.740  1.00 26.18 ? 5    VAL F C   1 
ATOM   5610  O  O   . VAL F  1 5   ? 12.695  -33.823 60.049  1.00 25.73 ? 5    VAL F O   1 
ATOM   5611  C  CB  . VAL F  1 5   ? 9.362   -33.955 59.878  1.00 25.21 ? 5    VAL F CB  1 
ATOM   5612  C  CG1 . VAL F  1 5   ? 9.850   -34.040 58.449  1.00 25.84 ? 5    VAL F CG1 1 
ATOM   5613  C  CG2 . VAL F  1 5   ? 8.930   -35.326 60.390  1.00 24.64 ? 5    VAL F CG2 1 
ATOM   5614  N  N   . CYS F  1 6   ? 11.742  -35.279 61.465  1.00 21.39 ? 6    CYS F N   1 
ATOM   5615  C  CA  . CYS F  1 6   ? 12.886  -36.158 61.484  1.00 21.35 ? 6    CYS F CA  1 
ATOM   5616  C  C   . CYS F  1 6   ? 12.388  -37.594 61.493  1.00 21.23 ? 6    CYS F C   1 
ATOM   5617  O  O   . CYS F  1 6   ? 11.405  -37.910 62.141  1.00 23.12 ? 6    CYS F O   1 
ATOM   5618  C  CB  . CYS F  1 6   ? 13.714  -35.881 62.742  1.00 26.06 ? 6    CYS F CB  1 
ATOM   5619  S  SG  . CYS F  1 6   ? 15.278  -36.718 62.816  1.00 27.15 ? 6    CYS F SG  1 
ATOM   5620  N  N   . VAL F  1 7   ? 13.062  -38.462 60.760  1.00 22.56 ? 7    VAL F N   1 
ATOM   5621  C  CA  . VAL F  1 7   ? 12.748  -39.881 60.776  1.00 22.28 ? 7    VAL F CA  1 
ATOM   5622  C  C   . VAL F  1 7   ? 14.007  -40.566 61.282  1.00 23.67 ? 7    VAL F C   1 
ATOM   5623  O  O   . VAL F  1 7   ? 15.077  -40.406 60.702  1.00 25.86 ? 7    VAL F O   1 
ATOM   5624  C  CB  . VAL F  1 7   ? 12.386  -40.393 59.357  1.00 26.74 ? 7    VAL F CB  1 
ATOM   5625  C  CG1 . VAL F  1 7   ? 12.264  -41.904 59.340  1.00 26.95 ? 7    VAL F CG1 1 
ATOM   5626  C  CG2 . VAL F  1 7   ? 11.101  -39.726 58.844  1.00 23.67 ? 7    VAL F CG2 1 
ATOM   5627  N  N   . LEU F  1 8   ? 13.899  -41.304 62.379  1.00 24.06 ? 8    LEU F N   1 
ATOM   5628  C  CA  . LEU F  1 8   ? 15.070  -41.952 62.962  1.00 23.64 ? 8    LEU F CA  1 
ATOM   5629  C  C   . LEU F  1 8   ? 15.183  -43.407 62.508  1.00 24.10 ? 8    LEU F C   1 
ATOM   5630  O  O   . LEU F  1 8   ? 14.201  -44.136 62.507  1.00 24.72 ? 8    LEU F O   1 
ATOM   5631  C  CB  . LEU F  1 8   ? 15.038  -41.858 64.499  1.00 24.75 ? 8    LEU F CB  1 
ATOM   5632  C  CG  . LEU F  1 8   ? 14.956  -40.464 65.146  1.00 21.12 ? 8    LEU F CG  1 
ATOM   5633  C  CD1 . LEU F  1 8   ? 13.865  -40.437 66.184  1.00 22.95 ? 8    LEU F CD1 1 
ATOM   5634  C  CD2 . LEU F  1 8   ? 16.271  -40.028 65.748  1.00 22.15 ? 8    LEU F CD2 1 
ATOM   5635  N  N   . LYS F  1 9   ? 16.390  -43.814 62.121  1.00 24.40 ? 9    LYS F N   1 
ATOM   5636  C  CA  . LYS F  1 9   ? 16.668  -45.184 61.707  1.00 24.01 ? 9    LYS F CA  1 
ATOM   5637  C  C   . LYS F  1 9   ? 18.072  -45.523 62.154  1.00 25.32 ? 9    LYS F C   1 
ATOM   5638  O  O   . LYS F  1 9   ? 18.903  -44.633 62.355  1.00 25.19 ? 9    LYS F O   1 
ATOM   5639  C  CB  . LYS F  1 9   ? 16.564  -45.330 60.176  1.00 31.34 ? 9    LYS F CB  1 
ATOM   5640  C  CG  . LYS F  1 9   ? 15.194  -44.951 59.578  1.00 29.50 ? 9    LYS F CG  1 
ATOM   5641  C  CD  . LYS F  1 9   ? 15.194  -45.032 58.056  1.00 36.66 ? 9    LYS F CD  1 
ATOM   5642  C  CE  . LYS F  1 9   ? 14.028  -44.244 57.431  1.00 35.95 ? 9    LYS F CE  1 
ATOM   5643  N  NZ  . LYS F  1 9   ? 12.698  -44.903 57.612  1.00 30.54 ? 9    LYS F NZ  1 
ATOM   5644  N  N   . GLY F  1 10  ? 18.343  -46.811 62.316  1.00 27.76 ? 10   GLY F N   1 
ATOM   5645  C  CA  . GLY F  1 10  ? 19.671  -47.277 62.689  1.00 28.86 ? 10   GLY F CA  1 
ATOM   5646  C  C   . GLY F  1 10  ? 19.872  -48.696 62.192  1.00 31.94 ? 10   GLY F C   1 
ATOM   5647  O  O   . GLY F  1 10  ? 19.154  -49.150 61.296  1.00 34.81 ? 10   GLY F O   1 
ATOM   5648  N  N   . ASP F  1 11  ? 20.834  -49.405 62.775  1.00 34.46 ? 11   ASP F N   1 
ATOM   5649  C  CA  . ASP F  1 11  ? 21.124  -50.780 62.357  1.00 36.15 ? 11   ASP F CA  1 
ATOM   5650  C  C   . ASP F  1 11  ? 20.289  -51.844 63.085  1.00 37.53 ? 11   ASP F C   1 
ATOM   5651  O  O   . ASP F  1 11  ? 20.320  -53.016 62.714  1.00 42.02 ? 11   ASP F O   1 
ATOM   5652  C  CB  . ASP F  1 11  ? 22.610  -51.097 62.529  1.00 35.68 ? 11   ASP F CB  1 
ATOM   5653  C  CG  . ASP F  1 11  ? 23.506  -50.129 61.785  1.00 41.16 ? 11   ASP F CG  1 
ATOM   5654  O  OD1 . ASP F  1 11  ? 23.082  -49.616 60.727  1.00 41.58 ? 11   ASP F OD1 1 
ATOM   5655  O  OD2 . ASP F  1 11  ? 24.643  -49.891 62.256  1.00 44.34 ? 11   ASP F OD2 1 
ATOM   5656  N  N   . GLY F  1 12  ? 19.557  -51.439 64.120  1.00 36.21 ? 12   GLY F N   1 
ATOM   5657  C  CA  . GLY F  1 12  ? 18.700  -52.347 64.863  1.00 31.74 ? 12   GLY F CA  1 
ATOM   5658  C  C   . GLY F  1 12  ? 17.223  -52.040 64.683  1.00 32.97 ? 12   GLY F C   1 
ATOM   5659  O  O   . GLY F  1 12  ? 16.828  -51.470 63.661  1.00 31.43 ? 12   GLY F O   1 
ATOM   5660  N  N   . PRO F  1 13  ? 16.399  -52.394 65.692  1.00 34.52 ? 13   PRO F N   1 
ATOM   5661  C  CA  . PRO F  1 13  ? 14.930  -52.315 65.638  1.00 30.36 ? 13   PRO F CA  1 
ATOM   5662  C  C   . PRO F  1 13  ? 14.375  -50.922 65.975  1.00 30.65 ? 13   PRO F C   1 
ATOM   5663  O  O   . PRO F  1 13  ? 13.166  -50.702 65.865  1.00 29.43 ? 13   PRO F O   1 
ATOM   5664  C  CB  . PRO F  1 13  ? 14.486  -53.312 66.722  1.00 29.67 ? 13   PRO F CB  1 
ATOM   5665  C  CG  . PRO F  1 13  ? 15.772  -53.742 67.462  1.00 32.78 ? 13   PRO F CG  1 
ATOM   5666  C  CD  . PRO F  1 13  ? 16.864  -52.824 67.023  1.00 30.55 ? 13   PRO F CD  1 
ATOM   5667  N  N   . VAL F  1 14  ? 15.254  -50.004 66.375  1.00 30.75 ? 14   VAL F N   1 
ATOM   5668  C  CA  . VAL F  1 14  ? 14.859  -48.675 66.845  1.00 29.78 ? 14   VAL F CA  1 
ATOM   5669  C  C   . VAL F  1 14  ? 14.521  -47.731 65.688  1.00 30.45 ? 14   VAL F C   1 
ATOM   5670  O  O   . VAL F  1 14  ? 15.355  -47.480 64.810  1.00 30.02 ? 14   VAL F O   1 
ATOM   5671  C  CB  . VAL F  1 14  ? 15.972  -48.053 67.727  1.00 27.49 ? 14   VAL F CB  1 
ATOM   5672  C  CG1 . VAL F  1 14  ? 15.501  -46.761 68.367  1.00 26.45 ? 14   VAL F CG1 1 
ATOM   5673  C  CG2 . VAL F  1 14  ? 16.415  -49.044 68.792  1.00 25.59 ? 14   VAL F CG2 1 
ATOM   5674  N  N   . GLN F  1 15  ? 13.293  -47.214 65.690  1.00 31.22 ? 15   GLN F N   1 
ATOM   5675  C  CA  . GLN F  1 15  ? 12.848  -46.275 64.663  1.00 30.69 ? 15   GLN F CA  1 
ATOM   5676  C  C   . GLN F  1 15  ? 11.637  -45.459 65.099  1.00 28.36 ? 15   GLN F C   1 
ATOM   5677  O  O   . GLN F  1 15  ? 10.741  -45.973 65.757  1.00 29.70 ? 15   GLN F O   1 
ATOM   5678  C  CB  . GLN F  1 15  ? 12.533  -47.013 63.359  1.00 36.25 ? 15   GLN F CB  1 
ATOM   5679  C  CG  . GLN F  1 15  ? 11.363  -47.980 63.448  1.00 37.81 ? 15   GLN F CG  1 
ATOM   5680  C  CD  . GLN F  1 15  ? 10.970  -48.533 62.089  1.00 42.88 ? 15   GLN F CD  1 
ATOM   5681  O  OE1 . GLN F  1 15  ? 10.797  -47.778 61.130  1.00 40.68 ? 15   GLN F OE1 1 
ATOM   5682  N  NE2 . GLN F  1 15  ? 10.827  -49.856 61.999  1.00 45.90 ? 15   GLN F NE2 1 
ATOM   5683  N  N   . GLY F  1 16  ? 11.606  -44.188 64.708  1.00 26.69 ? 16   GLY F N   1 
ATOM   5684  C  CA  . GLY F  1 16  ? 10.467  -43.333 64.991  1.00 25.79 ? 16   GLY F CA  1 
ATOM   5685  C  C   . GLY F  1 16  ? 10.371  -42.087 64.129  1.00 25.79 ? 16   GLY F C   1 
ATOM   5686  O  O   . GLY F  1 16  ? 11.134  -41.911 63.175  1.00 25.20 ? 16   GLY F O   1 
ATOM   5687  N  N   . ILE F  1 17  ? 9.417   -41.226 64.472  1.00 23.23 ? 17   ILE F N   1 
ATOM   5688  C  CA  . ILE F  1 17  ? 9.173   -39.986 63.750  1.00 24.40 ? 17   ILE F CA  1 
ATOM   5689  C  C   . ILE F  1 17  ? 9.024   -38.862 64.757  1.00 24.43 ? 17   ILE F C   1 
ATOM   5690  O  O   . ILE F  1 17  ? 8.209   -38.951 65.667  1.00 23.05 ? 17   ILE F O   1 
ATOM   5691  C  CB  . ILE F  1 17  ? 7.885   -40.063 62.888  1.00 26.83 ? 17   ILE F CB  1 
ATOM   5692  C  CG1 . ILE F  1 17  ? 8.041   -41.104 61.777  1.00 25.87 ? 17   ILE F CG1 1 
ATOM   5693  C  CG2 . ILE F  1 17  ? 7.542   -38.699 62.284  1.00 25.24 ? 17   ILE F CG2 1 
ATOM   5694  C  CD1 . ILE F  1 17  ? 7.001   -40.981 60.689  1.00 26.36 ? 17   ILE F CD1 1 
ATOM   5695  N  N   . ILE F  1 18  ? 9.817   -37.808 64.594  1.00 22.97 ? 18   ILE F N   1 
ATOM   5696  C  CA  . ILE F  1 18  ? 9.788   -36.676 65.511  1.00 22.24 ? 18   ILE F CA  1 
ATOM   5697  C  C   . ILE F  1 18  ? 9.417   -35.422 64.715  1.00 24.49 ? 18   ILE F C   1 
ATOM   5698  O  O   . ILE F  1 18  ? 9.975   -35.174 63.647  1.00 28.26 ? 18   ILE F O   1 
ATOM   5699  C  CB  . ILE F  1 18  ? 11.161  -36.512 66.238  1.00 22.91 ? 18   ILE F CB  1 
ATOM   5700  C  CG1 . ILE F  1 18  ? 11.535  -37.795 67.004  1.00 22.74 ? 18   ILE F CG1 1 
ATOM   5701  C  CG2 . ILE F  1 18  ? 11.177  -35.287 67.173  1.00 22.19 ? 18   ILE F CG2 1 
ATOM   5702  C  CD1 . ILE F  1 18  ? 10.662  -38.114 68.219  1.00 19.16 ? 18   ILE F CD1 1 
ATOM   5703  N  N   . ASN F  1 19  ? 8.448   -34.656 65.204  1.00 23.47 ? 19   ASN F N   1 
ATOM   5704  C  CA  . ASN F  1 19  ? 8.010   -33.449 64.516  1.00 23.81 ? 19   ASN F CA  1 
ATOM   5705  C  C   . ASN F  1 19  ? 8.498   -32.251 65.313  1.00 23.64 ? 19   ASN F C   1 
ATOM   5706  O  O   . ASN F  1 19  ? 8.736   -32.369 66.510  1.00 23.47 ? 19   ASN F O   1 
ATOM   5707  C  CB  . ASN F  1 19  ? 6.485   -33.419 64.381  1.00 24.91 ? 19   ASN F CB  1 
ATOM   5708  C  CG  . ASN F  1 19  ? 5.928   -34.667 63.712  1.00 26.36 ? 19   ASN F CG  1 
ATOM   5709  O  OD1 . ASN F  1 19  ? 5.938   -34.779 62.493  1.00 29.20 ? 19   ASN F OD1 1 
ATOM   5710  N  ND2 . ASN F  1 19  ? 5.420   -35.603 64.513  1.00 27.13 ? 19   ASN F ND2 1 
ATOM   5711  N  N   . PHE F  1 20  ? 8.665   -31.113 64.652  1.00 22.79 ? 20   PHE F N   1 
ATOM   5712  C  CA  . PHE F  1 20  ? 9.141   -29.900 65.303  1.00 24.48 ? 20   PHE F CA  1 
ATOM   5713  C  C   . PHE F  1 20  ? 8.251   -28.758 64.854  1.00 27.08 ? 20   PHE F C   1 
ATOM   5714  O  O   . PHE F  1 20  ? 7.821   -28.709 63.708  1.00 27.31 ? 20   PHE F O   1 
ATOM   5715  C  CB  . PHE F  1 20  ? 10.583  -29.567 64.901  1.00 24.48 ? 20   PHE F CB  1 
ATOM   5716  C  CG  . PHE F  1 20  ? 11.596  -30.628 65.247  1.00 24.48 ? 20   PHE F CG  1 
ATOM   5717  C  CD1 . PHE F  1 20  ? 11.837  -31.692 64.385  1.00 24.02 ? 20   PHE F CD1 1 
ATOM   5718  C  CD2 . PHE F  1 20  ? 12.343  -30.536 66.410  1.00 24.25 ? 20   PHE F CD2 1 
ATOM   5719  C  CE1 . PHE F  1 20  ? 12.778  -32.656 64.689  1.00 22.28 ? 20   PHE F CE1 1 
ATOM   5720  C  CE2 . PHE F  1 20  ? 13.297  -31.504 66.721  1.00 22.35 ? 20   PHE F CE2 1 
ATOM   5721  C  CZ  . PHE F  1 20  ? 13.510  -32.561 65.864  1.00 22.72 ? 20   PHE F CZ  1 
ATOM   5722  N  N   . GLU F  1 21  ? 7.980   -27.818 65.743  1.00 29.11 ? 21   GLU F N   1 
ATOM   5723  C  CA  . GLU F  1 21  ? 7.100   -26.728 65.364  1.00 32.99 ? 21   GLU F CA  1 
ATOM   5724  C  C   . GLU F  1 21  ? 7.422   -25.469 66.139  1.00 31.93 ? 21   GLU F C   1 
ATOM   5725  O  O   . GLU F  1 21  ? 7.444   -25.467 67.367  1.00 27.55 ? 21   GLU F O   1 
ATOM   5726  C  CB  . GLU F  1 21  ? 5.640   -27.129 65.565  1.00 31.72 ? 21   GLU F CB  1 
ATOM   5727  C  CG  . GLU F  1 21  ? 4.645   -26.097 65.082  1.00 38.94 ? 21   GLU F CG  1 
ATOM   5728  C  CD  . GLU F  1 21  ? 3.212   -26.552 65.271  1.00 45.86 ? 21   GLU F CD  1 
ATOM   5729  O  OE1 . GLU F  1 21  ? 2.930   -27.753 65.042  1.00 45.53 ? 21   GLU F OE1 1 
ATOM   5730  O  OE2 . GLU F  1 21  ? 2.373   -25.710 65.649  1.00 47.56 ? 21   GLU F OE2 1 
ATOM   5731  N  N   . GLN F  1 22  ? 7.676   -24.395 65.408  1.00 32.63 ? 22   GLN F N   1 
ATOM   5732  C  CA  . GLN F  1 22  ? 8.000   -23.130 66.033  1.00 33.97 ? 22   GLN F CA  1 
ATOM   5733  C  C   . GLN F  1 22  ? 7.151   -22.062 65.362  1.00 36.20 ? 22   GLN F C   1 
ATOM   5734  O  O   . GLN F  1 22  ? 7.399   -21.692 64.218  1.00 36.89 ? 22   GLN F O   1 
ATOM   5735  C  CB  . GLN F  1 22  ? 9.491   -22.835 65.873  1.00 28.91 ? 22   GLN F CB  1 
ATOM   5736  C  CG  . GLN F  1 22  ? 10.036  -21.844 66.859  1.00 31.41 ? 22   GLN F CG  1 
ATOM   5737  C  CD  . GLN F  1 22  ? 11.519  -21.581 66.661  1.00 31.28 ? 22   GLN F CD  1 
ATOM   5738  O  OE1 . GLN F  1 22  ? 12.054  -21.767 65.571  1.00 32.29 ? 22   GLN F OE1 1 
ATOM   5739  N  NE2 . GLN F  1 22  ? 12.184  -21.135 67.711  1.00 31.83 ? 22   GLN F NE2 1 
ATOM   5740  N  N   . LYS F  1 23  ? 6.131   -21.582 66.066  1.00 38.04 ? 23   LYS F N   1 
ATOM   5741  C  CA  . LYS F  1 23  ? 5.201   -20.623 65.479  1.00 41.54 ? 23   LYS F CA  1 
ATOM   5742  C  C   . LYS F  1 23  ? 5.805   -19.226 65.504  1.00 42.49 ? 23   LYS F C   1 
ATOM   5743  O  O   . LYS F  1 23  ? 5.560   -18.418 64.608  1.00 46.44 ? 23   LYS F O   1 
ATOM   5744  C  CB  . LYS F  1 23  ? 3.850   -20.642 66.207  1.00 47.98 ? 23   LYS F CB  1 
ATOM   5745  C  CG  . LYS F  1 23  ? 3.351   -22.044 66.575  1.00 49.37 ? 23   LYS F CG  1 
ATOM   5746  C  CD  . LYS F  1 23  ? 2.776   -22.777 65.377  1.00 46.77 ? 23   LYS F CD  1 
ATOM   5747  C  CE  . LYS F  1 23  ? 1.286   -23.041 65.563  1.00 57.49 ? 23   LYS F CE  1 
ATOM   5748  N  NZ  . LYS F  1 23  ? 0.658   -22.124 66.560  1.00 67.25 ? 23   LYS F NZ  1 
ATOM   5749  N  N   . GLU F  1 24  ? 6.599   -18.947 66.532  1.00 41.28 ? 24   GLU F N   1 
ATOM   5750  C  CA  . GLU F  1 24  ? 7.280   -17.661 66.635  1.00 46.19 ? 24   GLU F CA  1 
ATOM   5751  C  C   . GLU F  1 24  ? 8.768   -17.818 66.371  1.00 42.85 ? 24   GLU F C   1 
ATOM   5752  O  O   . GLU F  1 24  ? 9.337   -18.884 66.589  1.00 39.82 ? 24   GLU F O   1 
ATOM   5753  C  CB  . GLU F  1 24  ? 7.038   -17.012 68.000  1.00 51.28 ? 24   GLU F CB  1 
ATOM   5754  C  CG  . GLU F  1 24  ? 5.636   -16.427 68.169  1.00 57.43 ? 24   GLU F CG  1 
ATOM   5755  C  CD  . GLU F  1 24  ? 5.407   -15.191 67.304  1.00 62.08 ? 24   GLU F CD  1 
ATOM   5756  O  OE1 . GLU F  1 24  ? 4.229   -14.878 66.998  1.00 60.83 ? 24   GLU F OE1 1 
ATOM   5757  O  OE2 . GLU F  1 24  ? 6.409   -14.533 66.935  1.00 61.03 ? 24   GLU F OE2 1 
ATOM   5758  N  N   . SER F  1 25  ? 9.398   -16.750 65.905  1.00 44.37 ? 25   SER F N   1 
ATOM   5759  C  CA  . SER F  1 25  ? 10.770  -16.850 65.427  1.00 45.03 ? 25   SER F CA  1 
ATOM   5760  C  C   . SER F  1 25  ? 11.799  -17.142 66.530  1.00 45.68 ? 25   SER F C   1 
ATOM   5761  O  O   . SER F  1 25  ? 12.608  -18.055 66.389  1.00 48.08 ? 25   SER F O   1 
ATOM   5762  C  CB  . SER F  1 25  ? 11.151  -15.616 64.604  1.00 47.52 ? 25   SER F CB  1 
ATOM   5763  O  OG  . SER F  1 25  ? 12.063  -15.967 63.579  1.00 49.99 ? 25   SER F OG  1 
ATOM   5764  N  N   . ASN F  1 26  ? 11.785  -16.379 67.619  1.00 47.29 ? 26   ASN F N   1 
ATOM   5765  C  CA  . ASN F  1 26  ? 12.648  -16.708 68.760  1.00 48.32 ? 26   ASN F CA  1 
ATOM   5766  C  C   . ASN F  1 26  ? 11.823  -17.231 69.941  1.00 48.07 ? 26   ASN F C   1 
ATOM   5767  O  O   . ASN F  1 26  ? 12.113  -16.941 71.103  1.00 52.40 ? 26   ASN F O   1 
ATOM   5768  C  CB  . ASN F  1 26  ? 13.535  -15.517 69.165  1.00 52.33 ? 26   ASN F CB  1 
ATOM   5769  C  CG  . ASN F  1 26  ? 14.640  -15.904 70.162  1.00 51.62 ? 26   ASN F CG  1 
ATOM   5770  O  OD1 . ASN F  1 26  ? 15.113  -17.045 70.180  1.00 48.93 ? 26   ASN F OD1 1 
ATOM   5771  N  ND2 . ASN F  1 26  ? 15.057  -14.942 70.988  1.00 47.40 ? 26   ASN F ND2 1 
ATOM   5772  N  N   . GLY F  1 27  ? 10.784  -18.000 69.618  1.00 46.27 ? 27   GLY F N   1 
ATOM   5773  C  CA  . GLY F  1 27  ? 9.955   -18.657 70.609  1.00 39.53 ? 27   GLY F CA  1 
ATOM   5774  C  C   . GLY F  1 27  ? 10.333  -20.116 70.795  1.00 38.32 ? 27   GLY F C   1 
ATOM   5775  O  O   . GLY F  1 27  ? 11.310  -20.597 70.218  1.00 35.42 ? 27   GLY F O   1 
ATOM   5776  N  N   . PRO F  1 28  ? 9.563   -20.827 71.630  1.00 41.42 ? 28   PRO F N   1 
ATOM   5777  C  CA  . PRO F  1 28  ? 9.760   -22.246 71.946  1.00 36.89 ? 28   PRO F CA  1 
ATOM   5778  C  C   . PRO F  1 28  ? 9.485   -23.186 70.777  1.00 31.20 ? 28   PRO F C   1 
ATOM   5779  O  O   . PRO F  1 28  ? 8.621   -22.929 69.945  1.00 30.66 ? 28   PRO F O   1 
ATOM   5780  C  CB  . PRO F  1 28  ? 8.739   -22.494 73.059  1.00 38.63 ? 28   PRO F CB  1 
ATOM   5781  C  CG  . PRO F  1 28  ? 8.505   -21.160 73.660  1.00 41.92 ? 28   PRO F CG  1 
ATOM   5782  C  CD  . PRO F  1 28  ? 8.567   -20.207 72.518  1.00 39.99 ? 28   PRO F CD  1 
ATOM   5783  N  N   . VAL F  1 29  ? 10.223  -24.287 70.748  1.00 29.67 ? 29   VAL F N   1 
ATOM   5784  C  CA  . VAL F  1 29  ? 10.058  -25.318 69.739  1.00 26.63 ? 29   VAL F CA  1 
ATOM   5785  C  C   . VAL F  1 29  ? 9.355   -26.513 70.369  1.00 24.00 ? 29   VAL F C   1 
ATOM   5786  O  O   . VAL F  1 29  ? 9.810   -27.046 71.367  1.00 23.94 ? 29   VAL F O   1 
ATOM   5787  C  CB  . VAL F  1 29  ? 11.439  -25.755 69.169  1.00 25.27 ? 29   VAL F CB  1 
ATOM   5788  C  CG1 . VAL F  1 29  ? 11.296  -26.868 68.135  1.00 22.95 ? 29   VAL F CG1 1 
ATOM   5789  C  CG2 . VAL F  1 29  ? 12.171  -24.563 68.577  1.00 26.78 ? 29   VAL F CG2 1 
ATOM   5790  N  N   . LYS F  1 30  ? 8.234   -26.924 69.792  1.00 25.27 ? 30   LYS F N   1 
ATOM   5791  C  CA  . LYS F  1 30  ? 7.565   -28.136 70.233  1.00 25.33 ? 30   LYS F CA  1 
ATOM   5792  C  C   . LYS F  1 30  ? 8.188   -29.316 69.528  1.00 23.77 ? 30   LYS F C   1 
ATOM   5793  O  O   . LYS F  1 30  ? 8.257   -29.346 68.307  1.00 25.46 ? 30   LYS F O   1 
ATOM   5794  C  CB  . LYS F  1 30  ? 6.052   -28.098 69.960  1.00 28.96 ? 30   LYS F CB  1 
ATOM   5795  C  CG  . LYS F  1 30  ? 5.264   -29.194 70.721  1.00 33.46 ? 30   LYS F CG  1 
ATOM   5796  C  CD  . LYS F  1 30  ? 3.793   -29.319 70.273  1.00 36.42 ? 30   LYS F CD  1 
ATOM   5797  C  CE  . LYS F  1 30  ? 3.071   -30.481 70.992  1.00 36.48 ? 30   LYS F CE  1 
ATOM   5798  N  NZ  . LYS F  1 30  ? 1.803   -30.891 70.295  1.00 36.30 ? 30   LYS F NZ  1 
ATOM   5799  N  N   . VAL F  1 31  ? 8.648   -30.279 70.312  1.00 23.22 ? 31   VAL F N   1 
ATOM   5800  C  CA  . VAL F  1 31  ? 9.265   -31.477 69.789  1.00 22.92 ? 31   VAL F CA  1 
ATOM   5801  C  C   . VAL F  1 31  ? 8.435   -32.662 70.225  1.00 23.94 ? 31   VAL F C   1 
ATOM   5802  O  O   . VAL F  1 31  ? 8.334   -32.935 71.413  1.00 27.69 ? 31   VAL F O   1 
ATOM   5803  C  CB  . VAL F  1 31  ? 10.669  -31.639 70.352  1.00 21.47 ? 31   VAL F CB  1 
ATOM   5804  C  CG1 . VAL F  1 31  ? 11.313  -32.894 69.795  1.00 22.38 ? 31   VAL F CG1 1 
ATOM   5805  C  CG2 . VAL F  1 31  ? 11.496  -30.412 70.043  1.00 21.55 ? 31   VAL F CG2 1 
ATOM   5806  N  N   . TRP F  1 32  ? 7.825   -33.360 69.276  1.00 22.77 ? 32   TRP F N   1 
ATOM   5807  C  CA  . TRP F  1 32  ? 6.886   -34.417 69.618  1.00 22.00 ? 32   TRP F CA  1 
ATOM   5808  C  C   . TRP F  1 32  ? 6.888   -35.538 68.600  1.00 21.90 ? 32   TRP F C   1 
ATOM   5809  O  O   . TRP F  1 32  ? 7.118   -35.317 67.420  1.00 26.35 ? 32   TRP F O   1 
ATOM   5810  C  CB  . TRP F  1 32  ? 5.472   -33.839 69.776  1.00 26.54 ? 32   TRP F CB  1 
ATOM   5811  C  CG  . TRP F  1 32  ? 4.676   -33.637 68.491  1.00 26.91 ? 32   TRP F CG  1 
ATOM   5812  C  CD1 . TRP F  1 32  ? 3.787   -34.519 67.929  1.00 28.52 ? 32   TRP F CD1 1 
ATOM   5813  C  CD2 . TRP F  1 32  ? 4.664   -32.472 67.647  1.00 26.41 ? 32   TRP F CD2 1 
ATOM   5814  N  NE1 . TRP F  1 32  ? 3.241   -33.982 66.783  1.00 29.93 ? 32   TRP F NE1 1 
ATOM   5815  C  CE2 . TRP F  1 32  ? 3.763   -32.731 66.587  1.00 29.84 ? 32   TRP F CE2 1 
ATOM   5816  C  CE3 . TRP F  1 32  ? 5.336   -31.248 67.674  1.00 27.82 ? 32   TRP F CE3 1 
ATOM   5817  C  CZ2 . TRP F  1 32  ? 3.519   -31.802 65.566  1.00 32.29 ? 32   TRP F CZ2 1 
ATOM   5818  C  CZ3 . TRP F  1 32  ? 5.087   -30.325 66.658  1.00 29.66 ? 32   TRP F CZ3 1 
ATOM   5819  C  CH2 . TRP F  1 32  ? 4.186   -30.610 65.620  1.00 31.53 ? 32   TRP F CH2 1 
ATOM   5820  N  N   . GLY F  1 33  ? 6.615   -36.748 69.049  1.00 20.52 ? 33   GLY F N   1 
ATOM   5821  C  CA  . GLY F  1 33  ? 6.638   -37.875 68.148  1.00 20.22 ? 33   GLY F CA  1 
ATOM   5822  C  C   . GLY F  1 33  ? 6.517   -39.158 68.918  1.00 21.11 ? 33   GLY F C   1 
ATOM   5823  O  O   . GLY F  1 33  ? 5.890   -39.204 69.965  1.00 24.55 ? 33   GLY F O   1 
ATOM   5824  N  N   . SER F  1 34  ? 7.118   -40.204 68.385  1.00 21.30 ? 34   SER F N   1 
ATOM   5825  C  CA  . SER F  1 34  ? 7.045   -41.529 68.970  1.00 25.23 ? 34   SER F CA  1 
ATOM   5826  C  C   . SER F  1 34  ? 8.222   -42.309 68.445  1.00 24.19 ? 34   SER F C   1 
ATOM   5827  O  O   . SER F  1 34  ? 8.581   -42.148 67.285  1.00 26.57 ? 34   SER F O   1 
ATOM   5828  C  CB  . SER F  1 34  ? 5.770   -42.228 68.519  1.00 27.54 ? 34   SER F CB  1 
ATOM   5829  O  OG  . SER F  1 34  ? 6.004   -43.620 68.374  1.00 33.09 ? 34   SER F OG  1 
ATOM   5830  N  N   . ILE F  1 35  ? 8.818   -43.147 69.284  1.00 23.95 ? 35   ILE F N   1 
ATOM   5831  C  CA  . ILE F  1 35  ? 9.932   -43.995 68.877  1.00 21.57 ? 35   ILE F CA  1 
ATOM   5832  C  C   . ILE F  1 35  ? 9.694   -45.415 69.398  1.00 25.50 ? 35   ILE F C   1 
ATOM   5833  O  O   . ILE F  1 35  ? 9.457   -45.609 70.579  1.00 28.26 ? 35   ILE F O   1 
ATOM   5834  C  CB  . ILE F  1 35  ? 11.265  -43.453 69.424  1.00 23.37 ? 35   ILE F CB  1 
ATOM   5835  C  CG1 . ILE F  1 35  ? 11.438  -41.969 69.068  1.00 22.34 ? 35   ILE F CG1 1 
ATOM   5836  C  CG2 . ILE F  1 35  ? 12.449  -44.279 68.917  1.00 23.56 ? 35   ILE F CG2 1 
ATOM   5837  C  CD1 . ILE F  1 35  ? 12.620  -41.307 69.777  1.00 23.33 ? 35   ILE F CD1 1 
ATOM   5838  N  N   . LYS F  1 36  ? 9.747   -46.403 68.512  1.00 28.62 ? 36   LYS F N   1 
ATOM   5839  C  CA  . LYS F  1 36  ? 9.493   -47.799 68.867  1.00 27.99 ? 36   LYS F CA  1 
ATOM   5840  C  C   . LYS F  1 36  ? 10.815  -48.546 68.865  1.00 28.03 ? 36   LYS F C   1 
ATOM   5841  O  O   . LYS F  1 36  ? 11.818  -48.018 68.389  1.00 27.64 ? 36   LYS F O   1 
ATOM   5842  C  CB  . LYS F  1 36  ? 8.547   -48.448 67.842  1.00 30.39 ? 36   LYS F CB  1 
ATOM   5843  C  CG  . LYS F  1 36  ? 9.241   -48.864 66.520  1.00 36.26 ? 36   LYS F CG  1 
ATOM   5844  C  CD  . LYS F  1 36  ? 8.269   -49.341 65.408  1.00 36.63 ? 36   LYS F CD  1 
ATOM   5845  C  CE  . LYS F  1 36  ? 7.968   -48.222 64.408  1.00 40.38 ? 36   LYS F CE  1 
ATOM   5846  N  NZ  . LYS F  1 36  ? 6.841   -48.538 63.484  1.00 40.63 ? 36   LYS F NZ  1 
ATOM   5847  N  N   . GLY F  1 37  ? 10.822  -49.770 69.394  1.00 27.72 ? 37   GLY F N   1 
ATOM   5848  C  CA  . GLY F  1 37  ? 11.988  -50.641 69.311  1.00 28.90 ? 37   GLY F CA  1 
ATOM   5849  C  C   . GLY F  1 37  ? 12.997  -50.548 70.439  1.00 27.92 ? 37   GLY F C   1 
ATOM   5850  O  O   . GLY F  1 37  ? 14.002  -51.261 70.454  1.00 28.49 ? 37   GLY F O   1 
ATOM   5851  N  N   . LEU F  1 38  ? 12.718  -49.679 71.400  1.00 28.26 ? 38   LEU F N   1 
ATOM   5852  C  CA  . LEU F  1 38  ? 13.659  -49.392 72.476  1.00 29.55 ? 38   LEU F CA  1 
ATOM   5853  C  C   . LEU F  1 38  ? 13.486  -50.324 73.679  1.00 29.72 ? 38   LEU F C   1 
ATOM   5854  O  O   . LEU F  1 38  ? 12.419  -50.909 73.885  1.00 32.90 ? 38   LEU F O   1 
ATOM   5855  C  CB  . LEU F  1 38  ? 13.494  -47.933 72.915  1.00 27.93 ? 38   LEU F CB  1 
ATOM   5856  C  CG  . LEU F  1 38  ? 13.865  -46.854 71.897  1.00 24.99 ? 38   LEU F CG  1 
ATOM   5857  C  CD1 . LEU F  1 38  ? 13.132  -45.559 72.208  1.00 24.65 ? 38   LEU F CD1 1 
ATOM   5858  C  CD2 . LEU F  1 38  ? 15.371  -46.640 71.895  1.00 23.83 ? 38   LEU F CD2 1 
ATOM   5859  N  N   . THR F  1 39  ? 14.539  -50.468 74.473  1.00 30.38 ? 39   THR F N   1 
ATOM   5860  C  CA  . THR F  1 39  ? 14.405  -51.146 75.753  1.00 30.39 ? 39   THR F CA  1 
ATOM   5861  C  C   . THR F  1 39  ? 13.692  -50.211 76.716  1.00 31.23 ? 39   THR F C   1 
ATOM   5862  O  O   . THR F  1 39  ? 13.845  -48.994 76.632  1.00 29.72 ? 39   THR F O   1 
ATOM   5863  C  CB  . THR F  1 39  ? 15.763  -51.520 76.353  1.00 29.31 ? 39   THR F CB  1 
ATOM   5864  O  OG1 . THR F  1 39  ? 16.589  -50.353 76.428  1.00 27.40 ? 39   THR F OG1 1 
ATOM   5865  C  CG2 . THR F  1 39  ? 16.443  -52.575 75.506  1.00 29.63 ? 39   THR F CG2 1 
ATOM   5866  N  N   . GLU F  1 40  ? 12.918  -50.784 77.631  1.00 28.22 ? 40   GLU F N   1 
ATOM   5867  C  CA  . GLU F  1 40  ? 12.179  -50.000 78.612  1.00 30.45 ? 40   GLU F CA  1 
ATOM   5868  C  C   . GLU F  1 40  ? 13.099  -49.113 79.445  1.00 31.59 ? 40   GLU F C   1 
ATOM   5869  O  O   . GLU F  1 40  ? 14.202  -49.518 79.840  1.00 33.25 ? 40   GLU F O   1 
ATOM   5870  C  CB  . GLU F  1 40  ? 11.354  -50.921 79.527  1.00 34.62 ? 40   GLU F CB  1 
ATOM   5871  C  CG  . GLU F  1 40  ? 10.574  -50.209 80.637  1.00 35.75 ? 40   GLU F CG  1 
ATOM   5872  C  CD  . GLU F  1 40  ? 9.682   -51.166 81.442  1.00 44.28 ? 40   GLU F CD  1 
ATOM   5873  O  OE1 . GLU F  1 40  ? 9.942   -52.398 81.429  1.00 41.48 ? 40   GLU F OE1 1 
ATOM   5874  O  OE2 . GLU F  1 40  ? 8.722   -50.679 82.087  1.00 43.78 ? 40   GLU F OE2 1 
ATOM   5875  N  N   . GLY F  1 41  ? 12.637  -47.898 79.717  1.00 29.65 ? 41   GLY F N   1 
ATOM   5876  C  CA  . GLY F  1 41  ? 13.398  -46.975 80.535  1.00 28.92 ? 41   GLY F CA  1 
ATOM   5877  C  C   . GLY F  1 41  ? 13.833  -45.741 79.772  1.00 27.86 ? 41   GLY F C   1 
ATOM   5878  O  O   . GLY F  1 41  ? 13.291  -45.432 78.697  1.00 24.63 ? 41   GLY F O   1 
ATOM   5879  N  N   . LEU F  1 42  ? 14.836  -45.058 80.327  1.00 28.06 ? 42   LEU F N   1 
ATOM   5880  C  CA  . LEU F  1 42  ? 15.272  -43.751 79.844  1.00 24.84 ? 42   LEU F CA  1 
ATOM   5881  C  C   . LEU F  1 42  ? 16.330  -43.885 78.776  1.00 25.43 ? 42   LEU F C   1 
ATOM   5882  O  O   . LEU F  1 42  ? 17.207  -44.746 78.858  1.00 24.58 ? 42   LEU F O   1 
ATOM   5883  C  CB  . LEU F  1 42  ? 15.831  -42.899 80.992  1.00 25.46 ? 42   LEU F CB  1 
ATOM   5884  C  CG  . LEU F  1 42  ? 14.897  -42.473 82.121  1.00 23.63 ? 42   LEU F CG  1 
ATOM   5885  C  CD1 . LEU F  1 42  ? 15.595  -41.458 82.994  1.00 23.37 ? 42   LEU F CD1 1 
ATOM   5886  C  CD2 . LEU F  1 42  ? 13.615  -41.894 81.557  1.00 25.35 ? 42   LEU F CD2 1 
ATOM   5887  N  N   . HIS F  1 43  ? 16.247  -43.010 77.781  1.00 23.55 ? 43   HIS F N   1 
ATOM   5888  C  CA  . HIS F  1 43  ? 17.167  -43.034 76.657  1.00 24.92 ? 43   HIS F CA  1 
ATOM   5889  C  C   . HIS F  1 43  ? 17.594  -41.628 76.271  1.00 22.67 ? 43   HIS F C   1 
ATOM   5890  O  O   . HIS F  1 43  ? 16.739  -40.787 75.979  1.00 24.74 ? 43   HIS F O   1 
ATOM   5891  C  CB  . HIS F  1 43  ? 16.496  -43.700 75.454  1.00 23.70 ? 43   HIS F CB  1 
ATOM   5892  C  CG  . HIS F  1 43  ? 16.252  -45.163 75.636  1.00 25.40 ? 43   HIS F CG  1 
ATOM   5893  N  ND1 . HIS F  1 43  ? 17.162  -46.121 75.247  1.00 25.67 ? 43   HIS F ND1 1 
ATOM   5894  C  CD2 . HIS F  1 43  ? 15.202  -45.831 76.167  1.00 23.96 ? 43   HIS F CD2 1 
ATOM   5895  C  CE1 . HIS F  1 43  ? 16.681  -47.319 75.530  1.00 25.65 ? 43   HIS F CE1 1 
ATOM   5896  N  NE2 . HIS F  1 43  ? 15.495  -47.169 76.088  1.00 25.86 ? 43   HIS F NE2 1 
ATOM   5897  N  N   . GLY F  1 44  ? 18.901  -41.375 76.249  1.00 20.59 ? 44   GLY F N   1 
ATOM   5898  C  CA  . GLY F  1 44  ? 19.414  -40.095 75.772  1.00 21.19 ? 44   GLY F CA  1 
ATOM   5899  C  C   . GLY F  1 44  ? 18.818  -39.663 74.433  1.00 19.90 ? 44   GLY F C   1 
ATOM   5900  O  O   . GLY F  1 44  ? 18.616  -40.473 73.529  1.00 18.08 ? 44   GLY F O   1 
ATOM   5901  N  N   . PHE F  1 45  ? 18.534  -38.371 74.311  1.00 20.27 ? 45   PHE F N   1 
ATOM   5902  C  CA  . PHE F  1 45  ? 17.841  -37.827 73.153  1.00 18.31 ? 45   PHE F CA  1 
ATOM   5903  C  C   . PHE F  1 45  ? 18.431  -36.462 72.778  1.00 19.89 ? 45   PHE F C   1 
ATOM   5904  O  O   . PHE F  1 45  ? 18.097  -35.449 73.385  1.00 18.24 ? 45   PHE F O   1 
ATOM   5905  C  CB  . PHE F  1 45  ? 16.354  -37.694 73.487  1.00 19.46 ? 45   PHE F CB  1 
ATOM   5906  C  CG  . PHE F  1 45  ? 15.488  -37.323 72.309  1.00 23.17 ? 45   PHE F CG  1 
ATOM   5907  C  CD1 . PHE F  1 45  ? 15.353  -38.188 71.219  1.00 20.54 ? 45   PHE F CD1 1 
ATOM   5908  C  CD2 . PHE F  1 45  ? 14.797  -36.117 72.296  1.00 21.05 ? 45   PHE F CD2 1 
ATOM   5909  C  CE1 . PHE F  1 45  ? 14.559  -37.850 70.138  1.00 21.31 ? 45   PHE F CE1 1 
ATOM   5910  C  CE2 . PHE F  1 45  ? 13.998  -35.770 71.210  1.00 22.45 ? 45   PHE F CE2 1 
ATOM   5911  C  CZ  . PHE F  1 45  ? 13.878  -36.639 70.133  1.00 20.85 ? 45   PHE F CZ  1 
ATOM   5912  N  N   . HIS F  1 46  ? 19.304  -36.430 71.771  1.00 21.99 ? 46   HIS F N   1 
ATOM   5913  C  CA  . HIS F  1 46  ? 20.072  -35.211 71.480  1.00 22.42 ? 46   HIS F CA  1 
ATOM   5914  C  C   . HIS F  1 46  ? 20.103  -34.786 70.012  1.00 22.31 ? 46   HIS F C   1 
ATOM   5915  O  O   . HIS F  1 46  ? 19.973  -35.614 69.103  1.00 19.98 ? 46   HIS F O   1 
ATOM   5916  C  CB  . HIS F  1 46  ? 21.528  -35.346 71.963  1.00 20.28 ? 46   HIS F CB  1 
ATOM   5917  C  CG  . HIS F  1 46  ? 21.667  -35.999 73.299  1.00 20.98 ? 46   HIS F CG  1 
ATOM   5918  N  ND1 . HIS F  1 46  ? 22.185  -37.268 73.457  1.00 22.00 ? 46   HIS F ND1 1 
ATOM   5919  C  CD2 . HIS F  1 46  ? 21.354  -35.565 74.543  1.00 21.26 ? 46   HIS F CD2 1 
ATOM   5920  C  CE1 . HIS F  1 46  ? 22.184  -37.585 74.738  1.00 20.21 ? 46   HIS F CE1 1 
ATOM   5921  N  NE2 . HIS F  1 46  ? 21.684  -36.569 75.419  1.00 20.49 ? 46   HIS F NE2 1 
ATOM   5922  N  N   . VAL F  1 47  ? 20.292  -33.482 69.800  1.00 21.93 ? 47   VAL F N   1 
ATOM   5923  C  CA  . VAL F  1 47  ? 20.670  -32.968 68.487  1.00 21.17 ? 47   VAL F CA  1 
ATOM   5924  C  C   . VAL F  1 47  ? 22.196  -32.995 68.358  1.00 19.22 ? 47   VAL F C   1 
ATOM   5925  O  O   . VAL F  1 47  ? 22.910  -32.367 69.139  1.00 19.76 ? 47   VAL F O   1 
ATOM   5926  C  CB  . VAL F  1 47  ? 20.138  -31.523 68.216  1.00 17.93 ? 47   VAL F CB  1 
ATOM   5927  C  CG1 . VAL F  1 47  ? 20.173  -31.211 66.731  1.00 15.24 ? 47   VAL F CG1 1 
ATOM   5928  C  CG2 . VAL F  1 47  ? 18.733  -31.370 68.733  1.00 19.87 ? 47   VAL F CG2 1 
ATOM   5929  N  N   . HIS F  1 48  ? 22.684  -33.734 67.369  1.00 19.17 ? 48   HIS F N   1 
ATOM   5930  C  CA  . HIS F  1 48  ? 24.095  -33.731 67.030  1.00 19.27 ? 48   HIS F CA  1 
ATOM   5931  C  C   . HIS F  1 48  ? 24.401  -32.743 65.916  1.00 18.62 ? 48   HIS F C   1 
ATOM   5932  O  O   . HIS F  1 48  ? 23.528  -32.363 65.145  1.00 17.41 ? 48   HIS F O   1 
ATOM   5933  C  CB  . HIS F  1 48  ? 24.548  -35.141 66.681  1.00 19.50 ? 48   HIS F CB  1 
ATOM   5934  C  CG  . HIS F  1 48  ? 24.552  -36.056 67.861  1.00 20.70 ? 48   HIS F CG  1 
ATOM   5935  N  ND1 . HIS F  1 48  ? 25.711  -36.558 68.411  1.00 21.80 ? 48   HIS F ND1 1 
ATOM   5936  C  CD2 . HIS F  1 48  ? 23.541  -36.501 68.642  1.00 20.30 ? 48   HIS F CD2 1 
ATOM   5937  C  CE1 . HIS F  1 48  ? 25.409  -37.309 69.454  1.00 20.48 ? 48   HIS F CE1 1 
ATOM   5938  N  NE2 . HIS F  1 48  ? 24.099  -37.289 69.617  1.00 20.45 ? 48   HIS F NE2 1 
ATOM   5939  N  N   . GLU F  1 49  ? 25.661  -32.352 65.826  1.00 20.75 ? 49   GLU F N   1 
ATOM   5940  C  CA  . GLU F  1 49  ? 26.042  -31.180 65.055  1.00 19.81 ? 49   GLU F CA  1 
ATOM   5941  C  C   . GLU F  1 49  ? 25.809  -31.286 63.552  1.00 21.00 ? 49   GLU F C   1 
ATOM   5942  O  O   . GLU F  1 49  ? 25.371  -30.325 62.909  1.00 20.54 ? 49   GLU F O   1 
ATOM   5943  C  CB  . GLU F  1 49  ? 27.508  -30.856 65.314  1.00 18.88 ? 49   GLU F CB  1 
ATOM   5944  C  CG  . GLU F  1 49  ? 27.849  -29.444 64.948  1.00 21.03 ? 49   GLU F CG  1 
ATOM   5945  C  CD  . GLU F  1 49  ? 29.313  -29.189 64.999  1.00 22.12 ? 49   GLU F CD  1 
ATOM   5946  O  OE1 . GLU F  1 49  ? 30.004  -29.923 65.732  1.00 26.46 ? 49   GLU F OE1 1 
ATOM   5947  O  OE2 . GLU F  1 49  ? 29.775  -28.262 64.308  1.00 24.30 ? 49   GLU F OE2 1 
ATOM   5948  N  N   . PHE F  1 50  ? 26.131  -32.439 62.978  1.00 19.58 ? 50   PHE F N   1 
ATOM   5949  C  CA  . PHE F  1 50  ? 26.104  -32.563 61.527  1.00 20.73 ? 50   PHE F CA  1 
ATOM   5950  C  C   . PHE F  1 50  ? 24.964  -33.437 61.030  1.00 22.16 ? 50   PHE F C   1 
ATOM   5951  O  O   . PHE F  1 50  ? 24.637  -34.450 61.655  1.00 20.32 ? 50   PHE F O   1 
ATOM   5952  C  CB  . PHE F  1 50  ? 27.439  -33.088 60.999  1.00 18.56 ? 50   PHE F CB  1 
ATOM   5953  C  CG  . PHE F  1 50  ? 28.611  -32.291 61.456  1.00 18.98 ? 50   PHE F CG  1 
ATOM   5954  C  CD1 . PHE F  1 50  ? 28.697  -30.946 61.159  1.00 20.01 ? 50   PHE F CD1 1 
ATOM   5955  C  CD2 . PHE F  1 50  ? 29.618  -32.882 62.187  1.00 19.62 ? 50   PHE F CD2 1 
ATOM   5956  C  CE1 . PHE F  1 50  ? 29.756  -30.209 61.585  1.00 20.06 ? 50   PHE F CE1 1 
ATOM   5957  C  CE2 . PHE F  1 50  ? 30.674  -32.156 62.608  1.00 20.17 ? 50   PHE F CE2 1 
ATOM   5958  C  CZ  . PHE F  1 50  ? 30.748  -30.813 62.305  1.00 21.57 ? 50   PHE F CZ  1 
ATOM   5959  N  N   . GLY F  1 51  ? 24.360  -33.023 59.913  1.00 20.66 ? 51   GLY F N   1 
ATOM   5960  C  CA  . GLY F  1 51  ? 23.383  -33.838 59.220  1.00 19.35 ? 51   GLY F CA  1 
ATOM   5961  C  C   . GLY F  1 51  ? 24.101  -34.779 58.270  1.00 20.51 ? 51   GLY F C   1 
ATOM   5962  O  O   . GLY F  1 51  ? 23.774  -34.875 57.078  1.00 22.24 ? 51   GLY F O   1 
ATOM   5963  N  N   . ASP F  1 52  ? 25.093  -35.475 58.805  1.00 17.57 ? 52   ASP F N   1 
ATOM   5964  C  CA  . ASP F  1 52  ? 25.921  -36.367 58.018  1.00 20.19 ? 52   ASP F CA  1 
ATOM   5965  C  C   . ASP F  1 52  ? 25.711  -37.806 58.504  1.00 22.83 ? 52   ASP F C   1 
ATOM   5966  O  O   . ASP F  1 52  ? 26.025  -38.139 59.639  1.00 24.06 ? 52   ASP F O   1 
ATOM   5967  C  CB  . ASP F  1 52  ? 27.385  -35.916 58.128  1.00 19.33 ? 52   ASP F CB  1 
ATOM   5968  C  CG  . ASP F  1 52  ? 28.337  -36.753 57.305  1.00 21.84 ? 52   ASP F CG  1 
ATOM   5969  O  OD1 . ASP F  1 52  ? 27.993  -37.901 56.965  1.00 24.37 ? 52   ASP F OD1 1 
ATOM   5970  O  OD2 . ASP F  1 52  ? 29.452  -36.263 57.010  1.00 23.08 ? 52   ASP F OD2 1 
ATOM   5971  N  N   . ASN F  1 53  ? 25.157  -38.657 57.652  1.00 22.94 ? 53   ASN F N   1 
ATOM   5972  C  CA  . ASN F  1 53  ? 24.957  -40.054 58.011  1.00 24.46 ? 53   ASN F CA  1 
ATOM   5973  C  C   . ASN F  1 53  ? 25.770  -41.023 57.150  1.00 26.93 ? 53   ASN F C   1 
ATOM   5974  O  O   . ASN F  1 53  ? 25.466  -42.215 57.076  1.00 27.18 ? 53   ASN F O   1 
ATOM   5975  C  CB  . ASN F  1 53  ? 23.480  -40.420 57.920  1.00 27.50 ? 53   ASN F CB  1 
ATOM   5976  C  CG  . ASN F  1 53  ? 23.174  -41.734 58.601  1.00 33.35 ? 53   ASN F CG  1 
ATOM   5977  O  OD1 . ASN F  1 53  ? 22.722  -42.696 57.965  1.00 40.45 ? 53   ASN F OD1 1 
ATOM   5978  N  ND2 . ASN F  1 53  ? 23.445  -41.796 59.902  1.00 32.72 ? 53   ASN F ND2 1 
ATOM   5979  N  N   . THR F  1 54  ? 26.814  -40.504 56.513  1.00 26.93 ? 54   THR F N   1 
ATOM   5980  C  CA  . THR F  1 54  ? 27.629  -41.277 55.574  1.00 26.57 ? 54   THR F CA  1 
ATOM   5981  C  C   . THR F  1 54  ? 28.262  -42.548 56.173  1.00 29.48 ? 54   THR F C   1 
ATOM   5982  O  O   . THR F  1 54  ? 28.378  -43.570 55.493  1.00 29.50 ? 54   THR F O   1 
ATOM   5983  C  CB  . THR F  1 54  ? 28.709  -40.389 54.939  1.00 23.98 ? 54   THR F CB  1 
ATOM   5984  O  OG1 . THR F  1 54  ? 29.495  -39.793 55.970  1.00 27.74 ? 54   THR F OG1 1 
ATOM   5985  C  CG2 . THR F  1 54  ? 28.073  -39.277 54.117  1.00 25.71 ? 54   THR F CG2 1 
ATOM   5986  N  N   . ALA F  1 55  ? 28.664  -42.488 57.439  1.00 28.83 ? 55   ALA F N   1 
ATOM   5987  C  CA  . ALA F  1 55  ? 29.190  -43.667 58.126  1.00 27.32 ? 55   ALA F CA  1 
ATOM   5988  C  C   . ALA F  1 55  ? 28.279  -44.094 59.283  1.00 29.36 ? 55   ALA F C   1 
ATOM   5989  O  O   . ALA F  1 55  ? 28.734  -44.689 60.270  1.00 31.27 ? 55   ALA F O   1 
ATOM   5990  C  CB  . ALA F  1 55  ? 30.609  -43.413 58.618  1.00 26.72 ? 55   ALA F CB  1 
ATOM   5991  N  N   . GLY F  1 56  ? 26.987  -43.802 59.151  1.00 29.01 ? 56   GLY F N   1 
ATOM   5992  C  CA  . GLY F  1 56  ? 26.032  -44.117 60.195  1.00 26.19 ? 56   GLY F CA  1 
ATOM   5993  C  C   . GLY F  1 56  ? 25.846  -42.965 61.162  1.00 27.45 ? 56   GLY F C   1 
ATOM   5994  O  O   . GLY F  1 56  ? 26.247  -41.840 60.888  1.00 28.46 ? 56   GLY F O   1 
ATOM   5995  N  N   . CYS F  1 57  ? 25.239  -43.251 62.307  1.00 29.40 ? 57   CYS F N   1 
ATOM   5996  C  CA  . CYS F  1 57  ? 24.928  -42.225 63.294  1.00 27.60 ? 57   CYS F CA  1 
ATOM   5997  C  C   . CYS F  1 57  ? 26.196  -41.543 63.766  1.00 23.99 ? 57   CYS F C   1 
ATOM   5998  O  O   . CYS F  1 57  ? 26.199  -40.359 64.131  1.00 21.16 ? 57   CYS F O   1 
ATOM   5999  C  CB  . CYS F  1 57  ? 24.163  -42.854 64.459  1.00 26.41 ? 57   CYS F CB  1 
ATOM   6000  S  SG  . CYS F  1 57  ? 22.614  -43.651 63.912  1.00 32.24 ? 57   CYS F SG  1 
ATOM   6001  N  N   . THR F  1 58  ? 27.279  -42.306 63.720  1.00 24.90 ? 58   THR F N   1 
ATOM   6002  C  CA  . THR F  1 58  ? 28.606  -41.825 64.096  1.00 28.91 ? 58   THR F CA  1 
ATOM   6003  C  C   . THR F  1 58  ? 29.099  -40.564 63.344  1.00 27.07 ? 58   THR F C   1 
ATOM   6004  O  O   . THR F  1 58  ? 29.868  -39.765 63.895  1.00 24.23 ? 58   THR F O   1 
ATOM   6005  C  CB  . THR F  1 58  ? 29.634  -42.979 63.995  1.00 30.97 ? 58   THR F CB  1 
ATOM   6006  O  OG1 . THR F  1 58  ? 29.611  -43.747 65.213  1.00 34.37 ? 58   THR F OG1 1 
ATOM   6007  C  CG2 . THR F  1 58  ? 31.035  -42.444 63.762  1.00 30.81 ? 58   THR F CG2 1 
ATOM   6008  N  N   . SER F  1 59  ? 28.640  -40.367 62.109  1.00 23.76 ? 59   SER F N   1 
ATOM   6009  C  CA  . SER F  1 59  ? 29.065  -39.210 61.319  1.00 22.21 ? 59   SER F CA  1 
ATOM   6010  C  C   . SER F  1 59  ? 28.390  -37.898 61.737  1.00 23.79 ? 59   SER F C   1 
ATOM   6011  O  O   . SER F  1 59  ? 28.804  -36.818 61.299  1.00 23.06 ? 59   SER F O   1 
ATOM   6012  C  CB  . SER F  1 59  ? 28.806  -39.466 59.844  1.00 23.77 ? 59   SER F CB  1 
ATOM   6013  O  OG  . SER F  1 59  ? 29.153  -40.794 59.520  1.00 27.73 ? 59   SER F OG  1 
ATOM   6014  N  N   . ALA F  1 60  ? 27.359  -38.003 62.581  1.00 23.36 ? 60   ALA F N   1 
ATOM   6015  C  CA  . ALA F  1 60  ? 26.600  -36.846 63.069  1.00 21.65 ? 60   ALA F CA  1 
ATOM   6016  C  C   . ALA F  1 60  ? 27.453  -35.943 63.956  1.00 20.88 ? 60   ALA F C   1 
ATOM   6017  O  O   . ALA F  1 60  ? 27.111  -34.792 64.192  1.00 20.76 ? 60   ALA F O   1 
ATOM   6018  C  CB  . ALA F  1 60  ? 25.368  -37.311 63.830  1.00 18.98 ? 60   ALA F CB  1 
ATOM   6019  N  N   . GLY F  1 61  ? 28.564  -36.478 64.448  1.00 20.41 ? 61   GLY F N   1 
ATOM   6020  C  CA  . GLY F  1 61  ? 29.459  -35.730 65.303  1.00 19.36 ? 61   GLY F CA  1 
ATOM   6021  C  C   . GLY F  1 61  ? 28.988  -35.636 66.737  1.00 23.75 ? 61   GLY F C   1 
ATOM   6022  O  O   . GLY F  1 61  ? 28.235  -36.490 67.221  1.00 23.59 ? 61   GLY F O   1 
ATOM   6023  N  N   . PRO F  1 62  ? 29.411  -34.572 67.427  1.00 23.14 ? 62   PRO F N   1 
ATOM   6024  C  CA  . PRO F  1 62  ? 29.096  -34.378 68.843  1.00 23.22 ? 62   PRO F CA  1 
ATOM   6025  C  C   . PRO F  1 62  ? 27.734  -33.725 68.995  1.00 20.29 ? 62   PRO F C   1 
ATOM   6026  O  O   . PRO F  1 62  ? 27.128  -33.342 68.005  1.00 21.83 ? 62   PRO F O   1 
ATOM   6027  C  CB  . PRO F  1 62  ? 30.182  -33.396 69.303  1.00 24.65 ? 62   PRO F CB  1 
ATOM   6028  C  CG  . PRO F  1 62  ? 30.901  -32.928 68.019  1.00 22.73 ? 62   PRO F CG  1 
ATOM   6029  C  CD  . PRO F  1 62  ? 30.095  -33.400 66.862  1.00 20.83 ? 62   PRO F CD  1 
ATOM   6030  N  N   . HIS F  1 63  ? 27.254  -33.575 70.219  1.00 21.60 ? 63   HIS F N   1 
ATOM   6031  C  CA  . HIS F  1 63  ? 26.038  -32.809 70.413  1.00 20.37 ? 63   HIS F CA  1 
ATOM   6032  C  C   . HIS F  1 63  ? 26.252  -31.400 69.846  1.00 19.77 ? 63   HIS F C   1 
ATOM   6033  O  O   . HIS F  1 63  ? 27.319  -30.812 69.997  1.00 19.72 ? 63   HIS F O   1 
ATOM   6034  C  CB  . HIS F  1 63  ? 25.646  -32.745 71.897  1.00 21.50 ? 63   HIS F CB  1 
ATOM   6035  C  CG  . HIS F  1 63  ? 25.470  -34.088 72.549  1.00 22.19 ? 63   HIS F CG  1 
ATOM   6036  N  ND1 . HIS F  1 63  ? 25.332  -34.239 73.913  1.00 20.95 ? 63   HIS F ND1 1 
ATOM   6037  C  CD2 . HIS F  1 63  ? 25.430  -35.338 72.029  1.00 21.26 ? 63   HIS F CD2 1 
ATOM   6038  C  CE1 . HIS F  1 63  ? 25.210  -35.522 74.205  1.00 22.70 ? 63   HIS F CE1 1 
ATOM   6039  N  NE2 . HIS F  1 63  ? 25.269  -36.211 73.080  1.00 22.28 ? 63   HIS F NE2 1 
ATOM   6040  N  N   . PHE F  1 64  ? 25.242  -30.876 69.167  1.00 19.66 ? 64   PHE F N   1 
ATOM   6041  C  CA  . PHE F  1 64  ? 25.280  -29.510 68.677  1.00 19.84 ? 64   PHE F CA  1 
ATOM   6042  C  C   . PHE F  1 64  ? 25.668  -28.582 69.825  1.00 18.81 ? 64   PHE F C   1 
ATOM   6043  O  O   . PHE F  1 64  ? 24.981  -28.535 70.841  1.00 21.49 ? 64   PHE F O   1 
ATOM   6044  C  CB  . PHE F  1 64  ? 23.912  -29.127 68.106  1.00 18.49 ? 64   PHE F CB  1 
ATOM   6045  C  CG  . PHE F  1 64  ? 23.880  -27.768 67.491  1.00 19.32 ? 64   PHE F CG  1 
ATOM   6046  C  CD1 . PHE F  1 64  ? 24.990  -27.274 66.829  1.00 17.17 ? 64   PHE F CD1 1 
ATOM   6047  C  CD2 . PHE F  1 64  ? 22.735  -26.981 67.561  1.00 22.79 ? 64   PHE F CD2 1 
ATOM   6048  C  CE1 . PHE F  1 64  ? 24.976  -26.019 66.262  1.00 18.15 ? 64   PHE F CE1 1 
ATOM   6049  C  CE2 . PHE F  1 64  ? 22.707  -25.718 66.984  1.00 22.11 ? 64   PHE F CE2 1 
ATOM   6050  C  CZ  . PHE F  1 64  ? 23.833  -25.239 66.332  1.00 20.37 ? 64   PHE F CZ  1 
ATOM   6051  N  N   . ASN F  1 65  ? 26.771  -27.855 69.684  1.00 19.72 ? 65   ASN F N   1 
ATOM   6052  C  CA  . ASN F  1 65  ? 27.273  -27.058 70.803  1.00 21.18 ? 65   ASN F CA  1 
ATOM   6053  C  C   . ASN F  1 65  ? 27.943  -25.748 70.392  1.00 19.79 ? 65   ASN F C   1 
ATOM   6054  O  O   . ASN F  1 65  ? 29.129  -25.571 70.608  1.00 22.01 ? 65   ASN F O   1 
ATOM   6055  C  CB  . ASN F  1 65  ? 28.228  -27.924 71.635  1.00 20.15 ? 65   ASN F CB  1 
ATOM   6056  C  CG  . ASN F  1 65  ? 28.805  -27.200 72.826  1.00 21.67 ? 65   ASN F CG  1 
ATOM   6057  O  OD1 . ASN F  1 65  ? 28.146  -26.370 73.459  1.00 20.98 ? 65   ASN F OD1 1 
ATOM   6058  N  ND2 . ASN F  1 65  ? 30.050  -27.531 73.155  1.00 22.65 ? 65   ASN F ND2 1 
ATOM   6059  N  N   . PRO F  1 66  ? 27.176  -24.818 69.806  1.00 21.35 ? 66   PRO F N   1 
ATOM   6060  C  CA  . PRO F  1 66  ? 27.740  -23.572 69.263  1.00 21.90 ? 66   PRO F CA  1 
ATOM   6061  C  C   . PRO F  1 66  ? 28.234  -22.565 70.305  1.00 24.25 ? 66   PRO F C   1 
ATOM   6062  O  O   . PRO F  1 66  ? 28.876  -21.586 69.927  1.00 26.88 ? 66   PRO F O   1 
ATOM   6063  C  CB  . PRO F  1 66  ? 26.552  -22.966 68.504  1.00 23.13 ? 66   PRO F CB  1 
ATOM   6064  C  CG  . PRO F  1 66  ? 25.363  -23.507 69.202  1.00 20.89 ? 66   PRO F CG  1 
ATOM   6065  C  CD  . PRO F  1 66  ? 25.747  -24.940 69.466  1.00 20.90 ? 66   PRO F CD  1 
ATOM   6066  N  N   . LEU F  1 67  ? 27.927  -22.788 71.579  1.00 25.35 ? 67   LEU F N   1 
ATOM   6067  C  CA  . LEU F  1 67  ? 28.322  -21.865 72.646  1.00 26.11 ? 67   LEU F CA  1 
ATOM   6068  C  C   . LEU F  1 67  ? 29.431  -22.465 73.500  1.00 24.55 ? 67   LEU F C   1 
ATOM   6069  O  O   . LEU F  1 67  ? 29.819  -21.913 74.530  1.00 23.88 ? 67   LEU F O   1 
ATOM   6070  C  CB  . LEU F  1 67  ? 27.116  -21.479 73.510  1.00 26.03 ? 67   LEU F CB  1 
ATOM   6071  C  CG  . LEU F  1 67  ? 26.127  -20.518 72.843  1.00 26.69 ? 67   LEU F CG  1 
ATOM   6072  C  CD1 . LEU F  1 67  ? 24.915  -20.257 73.732  1.00 30.34 ? 67   LEU F CD1 1 
ATOM   6073  C  CD2 . LEU F  1 67  ? 26.825  -19.221 72.498  1.00 26.73 ? 67   LEU F CD2 1 
ATOM   6074  N  N   . SER F  1 68  ? 29.935  -23.602 73.044  1.00 24.36 ? 68   SER F N   1 
ATOM   6075  C  CA  . SER F  1 68  ? 31.066  -24.270 73.667  1.00 26.04 ? 68   SER F CA  1 
ATOM   6076  C  C   . SER F  1 68  ? 30.859  -24.448 75.160  1.00 27.30 ? 68   SER F C   1 
ATOM   6077  O  O   . SER F  1 68  ? 31.741  -24.155 75.967  1.00 29.03 ? 68   SER F O   1 
ATOM   6078  C  CB  . SER F  1 68  ? 32.353  -23.517 73.366  1.00 27.34 ? 68   SER F CB  1 
ATOM   6079  O  OG  . SER F  1 68  ? 32.480  -23.353 71.964  1.00 29.53 ? 68   SER F OG  1 
ATOM   6080  N  N   . ARG F  1 69  ? 29.670  -24.936 75.500  1.00 25.48 ? 69   ARG F N   1 
ATOM   6081  C  CA  . ARG F  1 69  ? 29.309  -25.267 76.865  1.00 26.54 ? 69   ARG F CA  1 
ATOM   6082  C  C   . ARG F  1 69  ? 29.541  -26.740 77.107  1.00 27.48 ? 69   ARG F C   1 
ATOM   6083  O  O   . ARG F  1 69  ? 29.887  -27.480 76.179  1.00 25.68 ? 69   ARG F O   1 
ATOM   6084  C  CB  . ARG F  1 69  ? 27.839  -24.959 77.106  1.00 25.08 ? 69   ARG F CB  1 
ATOM   6085  C  CG  . ARG F  1 69  ? 27.606  -23.886 78.106  1.00 27.47 ? 69   ARG F CG  1 
ATOM   6086  C  CD  . ARG F  1 69  ? 27.929  -22.526 77.588  1.00 29.05 ? 69   ARG F CD  1 
ATOM   6087  N  NE  . ARG F  1 69  ? 28.236  -21.650 78.710  1.00 34.38 ? 69   ARG F NE  1 
ATOM   6088  C  CZ  . ARG F  1 69  ? 28.332  -20.329 78.632  1.00 37.78 ? 69   ARG F CZ  1 
ATOM   6089  N  NH1 . ARG F  1 69  ? 28.140  -19.711 77.471  1.00 36.93 ? 69   ARG F NH1 1 
ATOM   6090  N  NH2 . ARG F  1 69  ? 28.622  -19.627 79.721  1.00 39.06 ? 69   ARG F NH2 1 
ATOM   6091  N  N   . LYS F  1 70  ? 29.340  -27.161 78.354  1.00 27.64 ? 70   LYS F N   1 
ATOM   6092  C  CA  . LYS F  1 70  ? 29.426  -28.571 78.700  1.00 27.02 ? 70   LYS F CA  1 
ATOM   6093  C  C   . LYS F  1 70  ? 28.058  -29.238 78.698  1.00 24.34 ? 70   LYS F C   1 
ATOM   6094  O  O   . LYS F  1 70  ? 27.020  -28.574 78.668  1.00 21.80 ? 70   LYS F O   1 
ATOM   6095  C  CB  . LYS F  1 70  ? 30.136  -28.773 80.037  1.00 27.40 ? 70   LYS F CB  1 
ATOM   6096  C  CG  . LYS F  1 70  ? 31.602  -28.403 79.972  1.00 28.84 ? 70   LYS F CG  1 
ATOM   6097  C  CD  . LYS F  1 70  ? 32.358  -28.916 81.172  1.00 37.06 ? 70   LYS F CD  1 
ATOM   6098  C  CE  . LYS F  1 70  ? 33.867  -28.712 81.010  1.00 42.06 ? 70   LYS F CE  1 
ATOM   6099  N  NZ  . LYS F  1 70  ? 34.298  -27.335 81.408  1.00 47.14 ? 70   LYS F NZ  1 
ATOM   6100  N  N   . HIS F  1 71  ? 28.078  -30.565 78.717  1.00 23.08 ? 71   HIS F N   1 
ATOM   6101  C  CA  . HIS F  1 71  ? 26.859  -31.343 78.673  1.00 21.11 ? 71   HIS F CA  1 
ATOM   6102  C  C   . HIS F  1 71  ? 25.980  -31.103 79.882  1.00 23.45 ? 71   HIS F C   1 
ATOM   6103  O  O   . HIS F  1 71  ? 26.443  -31.125 81.019  1.00 26.73 ? 71   HIS F O   1 
ATOM   6104  C  CB  . HIS F  1 71  ? 27.175  -32.828 78.581  1.00 21.58 ? 71   HIS F CB  1 
ATOM   6105  C  CG  . HIS F  1 71  ? 25.959  -33.688 78.585  1.00 21.87 ? 71   HIS F CG  1 
ATOM   6106  N  ND1 . HIS F  1 71  ? 25.119  -33.787 77.498  1.00 22.42 ? 71   HIS F ND1 1 
ATOM   6107  C  CD2 . HIS F  1 71  ? 25.426  -34.474 79.551  1.00 22.05 ? 71   HIS F CD2 1 
ATOM   6108  C  CE1 . HIS F  1 71  ? 24.120  -34.603 77.791  1.00 23.39 ? 71   HIS F CE1 1 
ATOM   6109  N  NE2 . HIS F  1 71  ? 24.284  -35.031 79.030  1.00 24.17 ? 71   HIS F NE2 1 
ATOM   6110  N  N   . GLY F  1 72  ? 24.696  -30.885 79.639  1.00 26.23 ? 72   GLY F N   1 
ATOM   6111  C  CA  . GLY F  1 72  ? 23.751  -30.799 80.729  1.00 22.71 ? 72   GLY F CA  1 
ATOM   6112  C  C   . GLY F  1 72  ? 22.414  -31.401 80.376  1.00 21.67 ? 72   GLY F C   1 
ATOM   6113  O  O   . GLY F  1 72  ? 22.276  -32.089 79.359  1.00 22.82 ? 72   GLY F O   1 
ATOM   6114  N  N   . GLY F  1 73  ? 21.428  -31.146 81.234  1.00 23.36 ? 73   GLY F N   1 
ATOM   6115  C  CA  . GLY F  1 73  ? 20.044  -31.485 80.960  1.00 21.75 ? 73   GLY F CA  1 
ATOM   6116  C  C   . GLY F  1 73  ? 19.403  -30.233 80.410  1.00 23.74 ? 73   GLY F C   1 
ATOM   6117  O  O   . GLY F  1 73  ? 19.971  -29.154 80.535  1.00 23.34 ? 73   GLY F O   1 
ATOM   6118  N  N   . PRO F  1 74  ? 18.216  -30.365 79.799  1.00 25.51 ? 74   PRO F N   1 
ATOM   6119  C  CA  . PRO F  1 74  ? 17.556  -29.267 79.083  1.00 21.70 ? 74   PRO F CA  1 
ATOM   6120  C  C   . PRO F  1 74  ? 17.320  -28.052 79.966  1.00 26.85 ? 74   PRO F C   1 
ATOM   6121  O  O   . PRO F  1 74  ? 17.225  -26.930 79.457  1.00 25.09 ? 74   PRO F O   1 
ATOM   6122  C  CB  . PRO F  1 74  ? 16.211  -29.864 78.686  1.00 23.00 ? 74   PRO F CB  1 
ATOM   6123  C  CG  . PRO F  1 74  ? 16.389  -31.331 78.789  1.00 22.90 ? 74   PRO F CG  1 
ATOM   6124  C  CD  . PRO F  1 74  ? 17.394  -31.584 79.836  1.00 20.63 ? 74   PRO F CD  1 
ATOM   6125  N  N   . LYS F  1 75  ? 17.228  -28.280 81.278  1.00 32.41 ? 75   LYS F N   1 
ATOM   6126  C  CA  . LYS F  1 75  ? 16.865  -27.225 82.223  1.00 32.05 ? 75   LYS F CA  1 
ATOM   6127  C  C   . LYS F  1 75  ? 18.081  -26.470 82.740  1.00 30.78 ? 75   LYS F C   1 
ATOM   6128  O  O   . LYS F  1 75  ? 17.938  -25.465 83.437  1.00 30.44 ? 75   LYS F O   1 
ATOM   6129  C  CB  . LYS F  1 75  ? 16.074  -27.789 83.402  1.00 34.78 ? 75   LYS F CB  1 
ATOM   6130  C  CG  . LYS F  1 75  ? 14.861  -28.619 83.014  1.00 38.44 ? 75   LYS F CG  1 
ATOM   6131  C  CD  . LYS F  1 75  ? 14.184  -28.099 81.735  1.00 39.16 ? 75   LYS F CD  1 
ATOM   6132  C  CE  . LYS F  1 75  ? 13.172  -26.989 82.003  1.00 42.97 ? 75   LYS F CE  1 
ATOM   6133  N  NZ  . LYS F  1 75  ? 12.290  -26.781 80.818  1.00 41.61 ? 75   LYS F NZ  1 
ATOM   6134  N  N   . ASP F  1 76  ? 19.271  -26.949 82.382  1.00 29.10 ? 76   ASP F N   1 
ATOM   6135  C  CA  . ASP F  1 76  ? 20.511  -26.347 82.851  1.00 29.21 ? 76   ASP F CA  1 
ATOM   6136  C  C   . ASP F  1 76  ? 20.957  -25.139 82.014  1.00 31.90 ? 76   ASP F C   1 
ATOM   6137  O  O   . ASP F  1 76  ? 20.559  -24.989 80.848  1.00 32.92 ? 76   ASP F O   1 
ATOM   6138  C  CB  . ASP F  1 76  ? 21.624  -27.400 82.908  1.00 28.00 ? 76   ASP F CB  1 
ATOM   6139  C  CG  . ASP F  1 76  ? 21.296  -28.563 83.850  1.00 32.83 ? 76   ASP F CG  1 
ATOM   6140  O  OD1 . ASP F  1 76  ? 20.296  -28.495 84.610  1.00 31.28 ? 76   ASP F OD1 1 
ATOM   6141  O  OD2 . ASP F  1 76  ? 22.052  -29.556 83.824  1.00 34.19 ? 76   ASP F OD2 1 
ATOM   6142  N  N   . GLU F  1 77  ? 21.767  -24.276 82.628  1.00 30.65 ? 77   GLU F N   1 
ATOM   6143  C  CA  . GLU F  1 77  ? 22.410  -23.172 81.923  1.00 34.17 ? 77   GLU F CA  1 
ATOM   6144  C  C   . GLU F  1 77  ? 23.688  -23.659 81.225  1.00 32.90 ? 77   GLU F C   1 
ATOM   6145  O  O   . GLU F  1 77  ? 24.005  -23.233 80.109  1.00 33.19 ? 77   GLU F O   1 
ATOM   6146  C  CB  . GLU F  1 77  ? 22.698  -22.002 82.881  1.00 38.65 ? 77   GLU F CB  1 
ATOM   6147  C  CG  . GLU F  1 77  ? 21.630  -20.877 82.871  1.00 41.52 ? 77   GLU F CG  1 
ATOM   6148  C  CD  . GLU F  1 77  ? 22.155  -19.533 82.324  1.00 44.94 ? 77   GLU F CD  1 
ATOM   6149  O  OE1 . GLU F  1 77  ? 23.377  -19.266 82.474  1.00 47.09 ? 77   GLU F OE1 1 
ATOM   6150  O  OE2 . GLU F  1 77  ? 21.347  -18.741 81.769  1.00 35.43 ? 77   GLU F OE2 1 
ATOM   6151  N  N   . GLU F  1 78  ? 24.422  -24.545 81.892  1.00 30.31 ? 78   GLU F N   1 
ATOM   6152  C  CA  . GLU F  1 78  ? 25.493  -25.292 81.246  1.00 29.09 ? 78   GLU F CA  1 
ATOM   6153  C  C   . GLU F  1 78  ? 24.881  -26.486 80.557  1.00 28.00 ? 78   GLU F C   1 
ATOM   6154  O  O   . GLU F  1 78  ? 24.755  -27.558 81.144  1.00 27.01 ? 78   GLU F O   1 
ATOM   6155  C  CB  . GLU F  1 78  ? 26.546  -25.785 82.244  1.00 29.53 ? 78   GLU F CB  1 
ATOM   6156  C  CG  . GLU F  1 78  ? 27.713  -24.837 82.454  1.00 35.60 ? 78   GLU F CG  1 
ATOM   6157  C  CD  . GLU F  1 78  ? 28.674  -24.806 81.274  1.00 35.42 ? 78   GLU F CD  1 
ATOM   6158  O  OE1 . GLU F  1 78  ? 29.237  -25.864 80.920  1.00 34.34 ? 78   GLU F OE1 1 
ATOM   6159  O  OE2 . GLU F  1 78  ? 28.884  -23.711 80.707  1.00 41.82 ? 78   GLU F OE2 1 
ATOM   6160  N  N   . ARG F  1 79  ? 24.486  -26.289 79.309  1.00 28.06 ? 79   ARG F N   1 
ATOM   6161  C  CA  . ARG F  1 79  ? 24.074  -27.391 78.464  1.00 24.74 ? 79   ARG F CA  1 
ATOM   6162  C  C   . ARG F  1 79  ? 24.543  -27.093 77.058  1.00 25.51 ? 79   ARG F C   1 
ATOM   6163  O  O   . ARG F  1 79  ? 24.780  -25.932 76.697  1.00 26.18 ? 79   ARG F O   1 
ATOM   6164  C  CB  . ARG F  1 79  ? 22.556  -27.535 78.472  1.00 23.47 ? 79   ARG F CB  1 
ATOM   6165  C  CG  . ARG F  1 79  ? 21.853  -26.265 78.059  1.00 24.33 ? 79   ARG F CG  1 
ATOM   6166  C  CD  . ARG F  1 79  ? 20.381  -26.486 77.837  1.00 24.02 ? 79   ARG F CD  1 
ATOM   6167  N  NE  . ARG F  1 79  ? 20.095  -27.023 76.512  1.00 22.53 ? 79   ARG F NE  1 
ATOM   6168  C  CZ  . ARG F  1 79  ? 18.867  -27.169 76.032  1.00 20.87 ? 79   ARG F CZ  1 
ATOM   6169  N  NH1 . ARG F  1 79  ? 17.832  -26.826 76.776  1.00 20.50 ? 79   ARG F NH1 1 
ATOM   6170  N  NH2 . ARG F  1 79  ? 18.670  -27.652 74.811  1.00 22.53 ? 79   ARG F NH2 1 
ATOM   6171  N  N   . HIS F  1 80  ? 24.682  -28.145 76.263  1.00 23.04 ? 80   HIS F N   1 
ATOM   6172  C  CA  . HIS F  1 80  ? 24.823  -27.984 74.834  1.00 22.18 ? 80   HIS F CA  1 
ATOM   6173  C  C   . HIS F  1 80  ? 23.461  -27.528 74.310  1.00 21.95 ? 80   HIS F C   1 
ATOM   6174  O  O   . HIS F  1 80  ? 22.445  -27.793 74.945  1.00 22.06 ? 80   HIS F O   1 
ATOM   6175  C  CB  . HIS F  1 80  ? 25.258  -29.310 74.210  1.00 19.68 ? 80   HIS F CB  1 
ATOM   6176  C  CG  . HIS F  1 80  ? 26.573  -29.817 74.730  1.00 21.58 ? 80   HIS F CG  1 
ATOM   6177  N  ND1 . HIS F  1 80  ? 26.802  -31.145 75.021  1.00 20.01 ? 80   HIS F ND1 1 
ATOM   6178  C  CD2 . HIS F  1 80  ? 27.730  -29.169 75.008  1.00 21.78 ? 80   HIS F CD2 1 
ATOM   6179  C  CE1 . HIS F  1 80  ? 28.044  -31.296 75.446  1.00 21.48 ? 80   HIS F CE1 1 
ATOM   6180  N  NE2 . HIS F  1 80  ? 28.627  -30.112 75.455  1.00 20.42 ? 80   HIS F NE2 1 
ATOM   6181  N  N   . VAL F  1 81  ? 23.429  -26.825 73.179  1.00 23.09 ? 81   VAL F N   1 
ATOM   6182  C  CA  . VAL F  1 81  ? 22.156  -26.494 72.539  1.00 20.31 ? 81   VAL F CA  1 
ATOM   6183  C  C   . VAL F  1 81  ? 21.323  -27.753 72.276  1.00 21.00 ? 81   VAL F C   1 
ATOM   6184  O  O   . VAL F  1 81  ? 20.114  -27.777 72.535  1.00 20.73 ? 81   VAL F O   1 
ATOM   6185  C  CB  . VAL F  1 81  ? 22.362  -25.681 71.241  1.00 21.09 ? 81   VAL F CB  1 
ATOM   6186  C  CG1 . VAL F  1 81  ? 21.118  -25.688 70.380  1.00 19.87 ? 81   VAL F CG1 1 
ATOM   6187  C  CG2 . VAL F  1 81  ? 22.751  -24.262 71.582  1.00 24.26 ? 81   VAL F CG2 1 
ATOM   6188  N  N   . GLY F  1 82  ? 21.979  -28.813 71.811  1.00 21.14 ? 82   GLY F N   1 
ATOM   6189  C  CA  . GLY F  1 82  ? 21.286  -30.051 71.498  1.00 20.25 ? 82   GLY F CA  1 
ATOM   6190  C  C   . GLY F  1 82  ? 20.995  -31.019 72.632  1.00 19.44 ? 82   GLY F C   1 
ATOM   6191  O  O   . GLY F  1 82  ? 20.706  -32.184 72.386  1.00 21.16 ? 82   GLY F O   1 
ATOM   6192  N  N   . ASP F  1 83  ? 21.075  -30.544 73.872  1.00 23.07 ? 83   ASP F N   1 
ATOM   6193  C  CA  . ASP F  1 83  ? 20.785  -31.360 75.063  1.00 22.28 ? 83   ASP F CA  1 
ATOM   6194  C  C   . ASP F  1 83  ? 19.299  -31.344 75.399  1.00 20.71 ? 83   ASP F C   1 
ATOM   6195  O  O   . ASP F  1 83  ? 18.829  -30.456 76.107  1.00 20.85 ? 83   ASP F O   1 
ATOM   6196  C  CB  . ASP F  1 83  ? 21.558  -30.841 76.278  1.00 20.78 ? 83   ASP F CB  1 
ATOM   6197  C  CG  . ASP F  1 83  ? 23.029  -31.171 76.222  1.00 22.47 ? 83   ASP F CG  1 
ATOM   6198  O  OD1 . ASP F  1 83  ? 23.410  -32.005 75.389  1.00 19.54 ? 83   ASP F OD1 1 
ATOM   6199  O  OD2 . ASP F  1 83  ? 23.801  -30.604 77.024  1.00 23.51 ? 83   ASP F OD2 1 
ATOM   6200  N  N   . LEU F  1 84  ? 18.555  -32.318 74.890  1.00 19.99 ? 84   LEU F N   1 
ATOM   6201  C  CA  . LEU F  1 84  ? 17.123  -32.380 75.159  1.00 20.87 ? 84   LEU F CA  1 
ATOM   6202  C  C   . LEU F  1 84  ? 16.846  -33.448 76.218  1.00 21.25 ? 84   LEU F C   1 
ATOM   6203  O  O   . LEU F  1 84  ? 15.694  -33.711 76.585  1.00 19.91 ? 84   LEU F O   1 
ATOM   6204  C  CB  . LEU F  1 84  ? 16.324  -32.614 73.867  1.00 18.08 ? 84   LEU F CB  1 
ATOM   6205  C  CG  . LEU F  1 84  ? 16.496  -31.521 72.802  1.00 19.97 ? 84   LEU F CG  1 
ATOM   6206  C  CD1 . LEU F  1 84  ? 15.732  -31.866 71.518  1.00 19.74 ? 84   LEU F CD1 1 
ATOM   6207  C  CD2 . LEU F  1 84  ? 16.102  -30.138 73.327  1.00 17.72 ? 84   LEU F CD2 1 
ATOM   6208  N  N   . GLY F  1 85  ? 17.928  -34.046 76.708  1.00 19.78 ? 85   GLY F N   1 
ATOM   6209  C  CA  . GLY F  1 85  ? 17.856  -34.964 77.821  1.00 19.34 ? 85   GLY F CA  1 
ATOM   6210  C  C   . GLY F  1 85  ? 17.380  -36.358 77.476  1.00 20.33 ? 85   GLY F C   1 
ATOM   6211  O  O   . GLY F  1 85  ? 17.893  -36.993 76.567  1.00 18.51 ? 85   GLY F O   1 
ATOM   6212  N  N   . ASN F  1 86  ? 16.389  -36.827 78.229  1.00 23.62 ? 86   ASN F N   1 
ATOM   6213  C  CA  . ASN F  1 86  ? 15.916  -38.201 78.160  1.00 21.94 ? 86   ASN F CA  1 
ATOM   6214  C  C   . ASN F  1 86  ? 14.494  -38.340 77.621  1.00 21.02 ? 86   ASN F C   1 
ATOM   6215  O  O   . ASN F  1 86  ? 13.623  -37.506 77.892  1.00 16.66 ? 86   ASN F O   1 
ATOM   6216  C  CB  . ASN F  1 86  ? 15.950  -38.812 79.556  1.00 20.76 ? 86   ASN F CB  1 
ATOM   6217  C  CG  . ASN F  1 86  ? 17.303  -39.326 79.929  1.00 19.87 ? 86   ASN F CG  1 
ATOM   6218  O  OD1 . ASN F  1 86  ? 17.860  -40.174 79.246  1.00 22.82 ? 86   ASN F OD1 1 
ATOM   6219  N  ND2 . ASN F  1 86  ? 17.838  -38.833 81.033  1.00 22.57 ? 86   ASN F ND2 1 
ATOM   6220  N  N   . VAL F  1 87  ? 14.265  -39.409 76.864  1.00 20.01 ? 87   VAL F N   1 
ATOM   6221  C  CA  . VAL F  1 87  ? 12.905  -39.846 76.553  1.00 21.64 ? 87   VAL F CA  1 
ATOM   6222  C  C   . VAL F  1 87  ? 12.611  -41.137 77.349  1.00 20.98 ? 87   VAL F C   1 
ATOM   6223  O  O   . VAL F  1 87  ? 13.549  -41.860 77.722  1.00 21.47 ? 87   VAL F O   1 
ATOM   6224  C  CB  . VAL F  1 87  ? 12.686  -40.028 75.017  1.00 20.63 ? 87   VAL F CB  1 
ATOM   6225  C  CG1 . VAL F  1 87  ? 12.654  -38.673 74.317  1.00 19.45 ? 87   VAL F CG1 1 
ATOM   6226  C  CG2 . VAL F  1 87  ? 13.753  -40.928 74.411  1.00 18.47 ? 87   VAL F CG2 1 
ATOM   6227  N  N   . THR F  1 88  ? 11.332  -41.410 77.638  1.00 20.62 ? 88   THR F N   1 
ATOM   6228  C  CA  . THR F  1 88  ? 10.943  -42.616 78.394  1.00 23.82 ? 88   THR F CA  1 
ATOM   6229  C  C   . THR F  1 88  ? 10.147  -43.590 77.531  1.00 21.60 ? 88   THR F C   1 
ATOM   6230  O  O   . THR F  1 88  ? 9.172   -43.209 76.905  1.00 23.29 ? 88   THR F O   1 
ATOM   6231  C  CB  . THR F  1 88  ? 10.089  -42.306 79.663  1.00 24.44 ? 88   THR F CB  1 
ATOM   6232  O  OG1 . THR F  1 88  ? 10.715  -41.291 80.462  1.00 22.72 ? 88   THR F OG1 1 
ATOM   6233  C  CG2 . THR F  1 88  ? 9.899   -43.574 80.507  1.00 20.61 ? 88   THR F CG2 1 
ATOM   6234  N  N   . ALA F  1 89  ? 10.570  -44.848 77.518  1.00 24.37 ? 89   ALA F N   1 
ATOM   6235  C  CA  . ALA F  1 89  ? 9.939   -45.877 76.704  1.00 24.18 ? 89   ALA F CA  1 
ATOM   6236  C  C   . ALA F  1 89  ? 9.172   -46.866 77.562  1.00 24.21 ? 89   ALA F C   1 
ATOM   6237  O  O   . ALA F  1 89  ? 9.742   -47.467 78.449  1.00 28.35 ? 89   ALA F O   1 
ATOM   6238  C  CB  . ALA F  1 89  ? 10.992  -46.606 75.888  1.00 24.06 ? 89   ALA F CB  1 
ATOM   6239  N  N   . GLY F  1 90  ? 7.880   -47.032 77.297  1.00 29.56 ? 90   GLY F N   1 
ATOM   6240  C  CA  . GLY F  1 90  ? 7.076   -48.019 78.001  1.00 28.87 ? 90   GLY F CA  1 
ATOM   6241  C  C   . GLY F  1 90  ? 7.634   -49.426 77.862  1.00 33.18 ? 90   GLY F C   1 
ATOM   6242  O  O   . GLY F  1 90  ? 8.720   -49.617 77.305  1.00 32.03 ? 90   GLY F O   1 
ATOM   6243  N  N   . LYS F  1 91  ? 6.909   -50.413 78.392  1.00 38.50 ? 91   LYS F N   1 
ATOM   6244  C  CA  . LYS F  1 91  ? 7.276   -51.827 78.233  1.00 41.74 ? 91   LYS F CA  1 
ATOM   6245  C  C   . LYS F  1 91  ? 6.985   -52.222 76.793  1.00 40.88 ? 91   LYS F C   1 
ATOM   6246  O  O   . LYS F  1 91  ? 7.528   -53.186 76.253  1.00 41.34 ? 91   LYS F O   1 
ATOM   6247  C  CB  . LYS F  1 91  ? 6.460   -52.713 79.182  1.00 47.14 ? 91   LYS F CB  1 
ATOM   6248  C  CG  . LYS F  1 91  ? 6.484   -52.282 80.638  1.00 49.52 ? 91   LYS F CG  1 
ATOM   6249  C  CD  . LYS F  1 91  ? 6.238   -53.474 81.570  1.00 61.69 ? 91   LYS F CD  1 
ATOM   6250  C  CE  . LYS F  1 91  ? 4.787   -53.961 81.534  1.00 67.75 ? 91   LYS F CE  1 
ATOM   6251  N  NZ  . LYS F  1 91  ? 3.903   -53.276 82.531  1.00 64.32 ? 91   LYS F NZ  1 
ATOM   6252  N  N   . ASP F  1 92  ? 6.076   -51.457 76.208  1.00 38.45 ? 92   ASP F N   1 
ATOM   6253  C  CA  . ASP F  1 92  ? 5.780   -51.456 74.794  1.00 37.17 ? 92   ASP F CA  1 
ATOM   6254  C  C   . ASP F  1 92  ? 7.048   -51.404 73.931  1.00 38.42 ? 92   ASP F C   1 
ATOM   6255  O  O   . ASP F  1 92  ? 7.090   -51.962 72.834  1.00 36.18 ? 92   ASP F O   1 
ATOM   6256  C  CB  . ASP F  1 92  ? 4.942   -50.205 74.517  1.00 37.90 ? 92   ASP F CB  1 
ATOM   6257  C  CG  . ASP F  1 92  ? 4.032   -50.361 73.323  1.00 48.84 ? 92   ASP F CG  1 
ATOM   6258  O  OD1 . ASP F  1 92  ? 4.068   -51.436 72.676  1.00 54.21 ? 92   ASP F OD1 1 
ATOM   6259  O  OD2 . ASP F  1 92  ? 3.277   -49.403 73.033  1.00 48.57 ? 92   ASP F OD2 1 
ATOM   6260  N  N   . GLY F  1 93  ? 8.077   -50.722 74.433  1.00 38.11 ? 93   GLY F N   1 
ATOM   6261  C  CA  . GLY F  1 93  ? 9.240   -50.363 73.637  1.00 31.25 ? 93   GLY F CA  1 
ATOM   6262  C  C   . GLY F  1 93  ? 9.015   -48.993 73.017  1.00 27.99 ? 93   GLY F C   1 
ATOM   6263  O  O   . GLY F  1 93  ? 9.890   -48.438 72.360  1.00 29.02 ? 93   GLY F O   1 
ATOM   6264  N  N   . VAL F  1 94  ? 7.830   -48.440 73.245  1.00 29.20 ? 94   VAL F N   1 
ATOM   6265  C  CA  . VAL F  1 94  ? 7.420   -47.192 72.610  1.00 28.59 ? 94   VAL F CA  1 
ATOM   6266  C  C   . VAL F  1 94  ? 7.631   -45.977 73.492  1.00 26.28 ? 94   VAL F C   1 
ATOM   6267  O  O   . VAL F  1 94  ? 7.074   -45.902 74.574  1.00 29.91 ? 94   VAL F O   1 
ATOM   6268  C  CB  . VAL F  1 94  ? 5.934   -47.233 72.231  1.00 31.09 ? 94   VAL F CB  1 
ATOM   6269  C  CG1 . VAL F  1 94  ? 5.457   -45.859 71.759  1.00 27.50 ? 94   VAL F CG1 1 
ATOM   6270  C  CG2 . VAL F  1 94  ? 5.697   -48.292 71.175  1.00 32.91 ? 94   VAL F CG2 1 
ATOM   6271  N  N   . ALA F  1 95  ? 8.434   -45.027 73.019  1.00 25.74 ? 95   ALA F N   1 
ATOM   6272  C  CA  . ALA F  1 95  ? 8.648   -43.760 73.712  1.00 24.35 ? 95   ALA F CA  1 
ATOM   6273  C  C   . ALA F  1 95  ? 7.817   -42.659 73.089  1.00 24.39 ? 95   ALA F C   1 
ATOM   6274  O  O   . ALA F  1 95  ? 8.107   -42.233 71.981  1.00 28.33 ? 95   ALA F O   1 
ATOM   6275  C  CB  . ALA F  1 95  ? 10.120  -43.372 73.664  1.00 20.62 ? 95   ALA F CB  1 
ATOM   6276  N  N   . ASN F  1 96  ? 6.790   -42.190 73.790  1.00 23.78 ? 96   ASN F N   1 
ATOM   6277  C  CA  . ASN F  1 96  ? 5.989   -41.077 73.290  1.00 24.02 ? 96   ASN F CA  1 
ATOM   6278  C  C   . ASN F  1 96  ? 6.605   -39.730 73.653  1.00 23.97 ? 96   ASN F C   1 
ATOM   6279  O  O   . ASN F  1 96  ? 6.275   -39.141 74.659  1.00 27.14 ? 96   ASN F O   1 
ATOM   6280  C  CB  . ASN F  1 96  ? 4.554   -41.139 73.817  1.00 28.71 ? 96   ASN F CB  1 
ATOM   6281  C  CG  . ASN F  1 96  ? 3.901   -42.496 73.596  1.00 32.83 ? 96   ASN F CG  1 
ATOM   6282  O  OD1 . ASN F  1 96  ? 3.810   -42.980 72.463  1.00 31.65 ? 96   ASN F OD1 1 
ATOM   6283  N  ND2 . ASN F  1 96  ? 3.435   -43.117 74.689  1.00 35.78 ? 96   ASN F ND2 1 
ATOM   6284  N  N   . VAL F  1 97  ? 7.487   -39.242 72.802  1.00 23.65 ? 97   VAL F N   1 
ATOM   6285  C  CA  . VAL F  1 97  ? 8.204   -37.996 73.017  1.00 21.16 ? 97   VAL F CA  1 
ATOM   6286  C  C   . VAL F  1 97  ? 7.294   -36.773 72.956  1.00 22.98 ? 97   VAL F C   1 
ATOM   6287  O  O   . VAL F  1 97  ? 6.504   -36.615 72.022  1.00 27.11 ? 97   VAL F O   1 
ATOM   6288  C  CB  . VAL F  1 97  ? 9.303   -37.858 71.940  1.00 22.56 ? 97   VAL F CB  1 
ATOM   6289  C  CG1 . VAL F  1 97  ? 10.081  -36.555 72.094  1.00 21.81 ? 97   VAL F CG1 1 
ATOM   6290  C  CG2 . VAL F  1 97  ? 10.220  -39.068 71.986  1.00 20.39 ? 97   VAL F CG2 1 
ATOM   6291  N  N   . SER F  1 98  ? 7.404   -35.903 73.948  1.00 21.94 ? 98   SER F N   1 
ATOM   6292  C  CA  . SER F  1 98  ? 6.697   -34.630 73.920  1.00 23.09 ? 98   SER F CA  1 
ATOM   6293  C  C   . SER F  1 98  ? 7.470   -33.636 74.758  1.00 26.08 ? 98   SER F C   1 
ATOM   6294  O  O   . SER F  1 98  ? 7.395   -33.630 75.994  1.00 27.79 ? 98   SER F O   1 
ATOM   6295  C  CB  . SER F  1 98  ? 5.256   -34.765 74.416  1.00 26.11 ? 98   SER F CB  1 
ATOM   6296  O  OG  . SER F  1 98  ? 4.598   -33.504 74.402  1.00 31.56 ? 98   SER F OG  1 
ATOM   6297  N  N   . ILE F  1 99  ? 8.230   -32.803 74.066  1.00 25.90 ? 99   ILE F N   1 
ATOM   6298  C  CA  . ILE F  1 99  ? 9.203   -31.926 74.695  1.00 25.29 ? 99   ILE F CA  1 
ATOM   6299  C  C   . ILE F  1 99  ? 8.908   -30.500 74.251  1.00 24.91 ? 99   ILE F C   1 
ATOM   6300  O  O   . ILE F  1 99  ? 8.207   -30.292 73.268  1.00 26.47 ? 99   ILE F O   1 
ATOM   6301  C  CB  . ILE F  1 99  ? 10.637  -32.363 74.301  1.00 22.91 ? 99   ILE F CB  1 
ATOM   6302  C  CG1 . ILE F  1 99  ? 11.089  -33.524 75.191  1.00 24.20 ? 99   ILE F CG1 1 
ATOM   6303  C  CG2 . ILE F  1 99  ? 11.612  -31.217 74.394  1.00 23.67 ? 99   ILE F CG2 1 
ATOM   6304  C  CD1 . ILE F  1 99  ? 12.204  -34.364 74.606  1.00 23.19 ? 99   ILE F CD1 1 
ATOM   6305  N  N   . GLU F  1 100 ? 9.393   -29.516 74.990  1.00 24.30 ? 100  GLU F N   1 
ATOM   6306  C  CA  . GLU F  1 100 ? 9.283   -28.149 74.525  1.00 25.95 ? 100  GLU F CA  1 
ATOM   6307  C  C   . GLU F  1 100 ? 10.532  -27.404 74.953  1.00 26.56 ? 100  GLU F C   1 
ATOM   6308  O  O   . GLU F  1 100 ? 10.898  -27.444 76.125  1.00 26.48 ? 100  GLU F O   1 
ATOM   6309  C  CB  . GLU F  1 100 ? 8.026   -27.488 75.077  1.00 28.84 ? 100  GLU F CB  1 
ATOM   6310  C  CG  . GLU F  1 100 ? 7.841   -26.064 74.603  1.00 32.59 ? 100  GLU F CG  1 
ATOM   6311  C  CD  . GLU F  1 100 ? 6.524   -25.469 75.055  1.00 45.14 ? 100  GLU F CD  1 
ATOM   6312  O  OE1 . GLU F  1 100 ? 5.552   -26.237 75.235  1.00 49.15 ? 100  GLU F OE1 1 
ATOM   6313  O  OE2 . GLU F  1 100 ? 6.460   -24.234 75.229  1.00 47.52 ? 100  GLU F OE2 1 
ATOM   6314  N  N   . ASP F  1 101 ? 11.186  -26.730 74.010  1.00 24.84 ? 101  ASP F N   1 
ATOM   6315  C  CA  . ASP F  1 101 ? 12.510  -26.177 74.274  1.00 26.47 ? 101  ASP F CA  1 
ATOM   6316  C  C   . ASP F  1 101 ? 12.724  -24.772 73.694  1.00 27.27 ? 101  ASP F C   1 
ATOM   6317  O  O   . ASP F  1 101 ? 12.327  -24.499 72.568  1.00 27.15 ? 101  ASP F O   1 
ATOM   6318  C  CB  . ASP F  1 101 ? 13.577  -27.149 73.749  1.00 24.08 ? 101  ASP F CB  1 
ATOM   6319  C  CG  . ASP F  1 101 ? 14.965  -26.846 74.287  1.00 25.29 ? 101  ASP F CG  1 
ATOM   6320  O  OD1 . ASP F  1 101 ? 15.285  -27.280 75.420  1.00 22.91 ? 101  ASP F OD1 1 
ATOM   6321  O  OD2 . ASP F  1 101 ? 15.741  -26.178 73.569  1.00 23.63 ? 101  ASP F OD2 1 
ATOM   6322  N  N   . ARG F  1 102 ? 13.374  -23.903 74.470  1.00 28.92 ? 102  ARG F N   1 
ATOM   6323  C  CA  . ARG F  1 102 ? 13.605  -22.500 74.103  1.00 28.59 ? 102  ARG F CA  1 
ATOM   6324  C  C   . ARG F  1 102 ? 15.022  -22.245 73.641  1.00 26.70 ? 102  ARG F C   1 
ATOM   6325  O  O   . ARG F  1 102 ? 15.331  -21.142 73.184  1.00 28.83 ? 102  ARG F O   1 
ATOM   6326  C  CB  . ARG F  1 102 ? 13.370  -21.578 75.300  1.00 38.10 ? 102  ARG F CB  1 
ATOM   6327  C  CG  . ARG F  1 102 ? 11.947  -21.522 75.800  1.00 44.87 ? 102  ARG F CG  1 
ATOM   6328  C  CD  . ARG F  1 102 ? 11.801  -20.511 76.931  1.00 47.49 ? 102  ARG F CD  1 
ATOM   6329  N  NE  . ARG F  1 102 ? 10.391  -20.275 77.222  1.00 55.09 ? 102  ARG F NE  1 
ATOM   6330  C  CZ  . ARG F  1 102 ? 9.586   -19.552 76.447  1.00 56.74 ? 102  ARG F CZ  1 
ATOM   6331  N  NH1 . ARG F  1 102 ? 10.054  -18.987 75.336  1.00 52.16 ? 102  ARG F NH1 1 
ATOM   6332  N  NH2 . ARG F  1 102 ? 8.311   -19.395 76.777  1.00 58.97 ? 102  ARG F NH2 1 
ATOM   6333  N  N   . VAL F  1 103 ? 15.882  -23.250 73.791  1.00 26.52 ? 103  VAL F N   1 
ATOM   6334  C  CA  . VAL F  1 103 ? 17.294  -23.135 73.423  1.00 25.34 ? 103  VAL F CA  1 
ATOM   6335  C  C   . VAL F  1 103 ? 17.571  -23.554 71.973  1.00 26.61 ? 103  VAL F C   1 
ATOM   6336  O  O   . VAL F  1 103 ? 18.240  -22.831 71.240  1.00 24.80 ? 103  VAL F O   1 
ATOM   6337  C  CB  . VAL F  1 103 ? 18.198  -23.928 74.382  1.00 23.40 ? 103  VAL F CB  1 
ATOM   6338  C  CG1 . VAL F  1 103 ? 19.582  -24.070 73.791  1.00 21.09 ? 103  VAL F CG1 1 
ATOM   6339  C  CG2 . VAL F  1 103 ? 18.248  -23.250 75.767  1.00 22.03 ? 103  VAL F CG2 1 
ATOM   6340  N  N   . ILE F  1 104 ? 17.066  -24.718 71.562  1.00 24.38 ? 104  ILE F N   1 
ATOM   6341  C  CA  . ILE F  1 104 ? 17.122  -25.088 70.155  1.00 22.44 ? 104  ILE F CA  1 
ATOM   6342  C  C   . ILE F  1 104 ? 16.169  -24.185 69.389  1.00 25.66 ? 104  ILE F C   1 
ATOM   6343  O  O   . ILE F  1 104 ? 15.167  -23.716 69.945  1.00 28.32 ? 104  ILE F O   1 
ATOM   6344  C  CB  . ILE F  1 104 ? 16.681  -26.544 69.890  1.00 21.39 ? 104  ILE F CB  1 
ATOM   6345  C  CG1 . ILE F  1 104 ? 15.222  -26.746 70.326  1.00 22.22 ? 104  ILE F CG1 1 
ATOM   6346  C  CG2 . ILE F  1 104 ? 17.645  -27.542 70.522  1.00 18.86 ? 104  ILE F CG2 1 
ATOM   6347  C  CD1 . ILE F  1 104 ? 14.537  -27.946 69.695  1.00 20.35 ? 104  ILE F CD1 1 
ATOM   6348  N  N   . SER F  1 105 ? 16.468  -23.953 68.113  1.00 24.82 ? 105  SER F N   1 
ATOM   6349  C  CA  . SER F  1 105 ? 15.594  -23.164 67.248  1.00 27.44 ? 105  SER F CA  1 
ATOM   6350  C  C   . SER F  1 105 ? 15.442  -23.831 65.878  1.00 25.10 ? 105  SER F C   1 
ATOM   6351  O  O   . SER F  1 105 ? 16.162  -24.777 65.570  1.00 25.86 ? 105  SER F O   1 
ATOM   6352  C  CB  . SER F  1 105 ? 16.159  -21.749 67.088  1.00 26.80 ? 105  SER F CB  1 
ATOM   6353  O  OG  . SER F  1 105 ? 15.181  -20.873 66.551  1.00 29.42 ? 105  SER F OG  1 
ATOM   6354  N  N   . LEU F  1 106 ? 14.506  -23.346 65.062  1.00 27.19 ? 106  LEU F N   1 
ATOM   6355  C  CA  . LEU F  1 106 ? 14.389  -23.787 63.656  1.00 27.87 ? 106  LEU F CA  1 
ATOM   6356  C  C   . LEU F  1 106 ? 14.865  -22.705 62.681  1.00 27.37 ? 106  LEU F C   1 
ATOM   6357  O  O   . LEU F  1 106 ? 14.611  -22.777 61.496  1.00 27.32 ? 106  LEU F O   1 
ATOM   6358  C  CB  . LEU F  1 106 ? 12.957  -24.208 63.303  1.00 25.72 ? 106  LEU F CB  1 
ATOM   6359  C  CG  . LEU F  1 106 ? 12.336  -25.379 64.070  1.00 23.81 ? 106  LEU F CG  1 
ATOM   6360  C  CD1 . LEU F  1 106 ? 10.987  -25.754 63.499  1.00 26.10 ? 106  LEU F CD1 1 
ATOM   6361  C  CD2 . LEU F  1 106 ? 13.278  -26.565 64.052  1.00 26.78 ? 106  LEU F CD2 1 
ATOM   6362  N  N   . SER F  1 107 ? 15.553  -21.700 63.206  1.00 30.66 ? 107  SER F N   1 
ATOM   6363  C  CA  . SER F  1 107 ? 16.106  -20.617 62.409  1.00 30.50 ? 107  SER F CA  1 
ATOM   6364  C  C   . SER F  1 107 ? 17.161  -19.917 63.259  1.00 30.91 ? 107  SER F C   1 
ATOM   6365  O  O   . SER F  1 107 ? 17.161  -20.059 64.472  1.00 33.19 ? 107  SER F O   1 
ATOM   6366  C  CB  . SER F  1 107 ? 15.006  -19.634 62.003  1.00 32.58 ? 107  SER F CB  1 
ATOM   6367  O  OG  . SER F  1 107 ? 14.410  -19.018 63.134  1.00 37.36 ? 107  SER F OG  1 
ATOM   6368  N  N   . GLY F  1 108 ? 18.079  -19.191 62.631  1.00 35.24 ? 108  GLY F N   1 
ATOM   6369  C  CA  . GLY F  1 108 ? 19.075  -18.435 63.373  1.00 35.98 ? 108  GLY F CA  1 
ATOM   6370  C  C   . GLY F  1 108 ? 20.291  -19.216 63.849  1.00 36.35 ? 108  GLY F C   1 
ATOM   6371  O  O   . GLY F  1 108 ? 20.502  -20.361 63.450  1.00 35.37 ? 108  GLY F O   1 
ATOM   6372  N  N   . GLU F  1 109 ? 21.081  -18.589 64.721  1.00 36.08 ? 109  GLU F N   1 
ATOM   6373  C  CA  . GLU F  1 109 ? 22.343  -19.154 65.207  1.00 38.42 ? 109  GLU F CA  1 
ATOM   6374  C  C   . GLU F  1 109 ? 22.218  -20.568 65.794  1.00 37.93 ? 109  GLU F C   1 
ATOM   6375  O  O   . GLU F  1 109 ? 23.160  -21.362 65.730  1.00 37.01 ? 109  GLU F O   1 
ATOM   6376  C  CB  . GLU F  1 109 ? 22.988  -18.235 66.261  1.00 41.64 ? 109  GLU F CB  1 
ATOM   6377  C  CG  . GLU F  1 109 ? 22.535  -16.771 66.237  1.00 49.10 ? 109  GLU F CG  1 
ATOM   6378  C  CD  . GLU F  1 109 ? 21.729  -16.362 67.480  1.00 52.55 ? 109  GLU F CD  1 
ATOM   6379  O  OE1 . GLU F  1 109 ? 20.522  -16.046 67.335  1.00 52.81 ? 109  GLU F OE1 1 
ATOM   6380  O  OE2 . GLU F  1 109 ? 22.304  -16.349 68.599  1.00 49.86 ? 109  GLU F OE2 1 
ATOM   6381  N  N   . HIS F  1 110 ? 21.069  -20.869 66.389  1.00 37.48 ? 110  HIS F N   1 
ATOM   6382  C  CA  . HIS F  1 110 ? 20.883  -22.136 67.089  1.00 32.98 ? 110  HIS F CA  1 
ATOM   6383  C  C   . HIS F  1 110 ? 19.979  -23.100 66.313  1.00 30.38 ? 110  HIS F C   1 
ATOM   6384  O  O   . HIS F  1 110 ? 19.384  -24.004 66.915  1.00 27.98 ? 110  HIS F O   1 
ATOM   6385  C  CB  . HIS F  1 110 ? 20.331  -21.885 68.502  1.00 30.57 ? 110  HIS F CB  1 
ATOM   6386  C  CG  . HIS F  1 110 ? 21.364  -21.419 69.491  1.00 33.92 ? 110  HIS F CG  1 
ATOM   6387  N  ND1 . HIS F  1 110 ? 21.266  -21.666 70.845  1.00 31.16 ? 110  HIS F ND1 1 
ATOM   6388  C  CD2 . HIS F  1 110 ? 22.518  -20.728 69.320  1.00 35.07 ? 110  HIS F CD2 1 
ATOM   6389  C  CE1 . HIS F  1 110 ? 22.311  -21.142 71.464  1.00 30.62 ? 110  HIS F CE1 1 
ATOM   6390  N  NE2 . HIS F  1 110 ? 23.086  -20.569 70.561  1.00 32.09 ? 110  HIS F NE2 1 
ATOM   6391  N  N   . SER F  1 111 ? 19.895  -22.907 64.990  1.00 28.35 ? 111  SER F N   1 
ATOM   6392  C  CA  . SER F  1 111 ? 18.986  -23.679 64.135  1.00 27.24 ? 111  SER F CA  1 
ATOM   6393  C  C   . SER F  1 111 ? 19.415  -25.130 63.936  1.00 25.91 ? 111  SER F C   1 
ATOM   6394  O  O   . SER F  1 111 ? 20.546  -25.403 63.547  1.00 27.33 ? 111  SER F O   1 
ATOM   6395  C  CB  . SER F  1 111 ? 18.829  -23.020 62.772  1.00 26.53 ? 111  SER F CB  1 
ATOM   6396  O  OG  . SER F  1 111 ? 17.958  -23.781 61.954  1.00 25.39 ? 111  SER F OG  1 
ATOM   6397  N  N   . ILE F  1 112 ? 18.501  -26.058 64.199  1.00 23.81 ? 112  ILE F N   1 
ATOM   6398  C  CA  . ILE F  1 112 ? 18.811  -27.477 64.109  1.00 23.03 ? 112  ILE F CA  1 
ATOM   6399  C  C   . ILE F  1 112 ? 18.426  -28.093 62.757  1.00 21.29 ? 112  ILE F C   1 
ATOM   6400  O  O   . ILE F  1 112 ? 18.600  -29.288 62.542  1.00 21.11 ? 112  ILE F O   1 
ATOM   6401  C  CB  . ILE F  1 112 ? 18.174  -28.259 65.280  1.00 20.64 ? 112  ILE F CB  1 
ATOM   6402  C  CG1 . ILE F  1 112 ? 16.649  -28.094 65.281  1.00 21.18 ? 112  ILE F CG1 1 
ATOM   6403  C  CG2 . ILE F  1 112 ? 18.777  -27.787 66.606  1.00 23.08 ? 112  ILE F CG2 1 
ATOM   6404  C  CD1 . ILE F  1 112 ? 15.933  -28.955 66.301  1.00 19.58 ? 112  ILE F CD1 1 
ATOM   6405  N  N   . ILE F  1 113 ? 17.912  -27.269 61.847  1.00 23.49 ? 113  ILE F N   1 
ATOM   6406  C  CA  . ILE F  1 113 ? 17.539  -27.728 60.503  1.00 25.83 ? 113  ILE F CA  1 
ATOM   6407  C  C   . ILE F  1 113 ? 18.790  -28.170 59.741  1.00 23.79 ? 113  ILE F C   1 
ATOM   6408  O  O   . ILE F  1 113 ? 19.750  -27.398 59.611  1.00 24.77 ? 113  ILE F O   1 
ATOM   6409  C  CB  . ILE F  1 113 ? 16.748  -26.631 59.704  1.00 25.97 ? 113  ILE F CB  1 
ATOM   6410  C  CG1 . ILE F  1 113 ? 15.511  -26.179 60.486  1.00 25.05 ? 113  ILE F CG1 1 
ATOM   6411  C  CG2 . ILE F  1 113 ? 16.307  -27.137 58.335  1.00 22.37 ? 113  ILE F CG2 1 
ATOM   6412  C  CD1 . ILE F  1 113 ? 14.285  -27.009 60.229  1.00 24.14 ? 113  ILE F CD1 1 
ATOM   6413  N  N   . GLY F  1 114 ? 18.786  -29.415 59.262  1.00 20.81 ? 114  GLY F N   1 
ATOM   6414  C  CA  . GLY F  1 114 ? 19.936  -29.970 58.570  1.00 18.36 ? 114  GLY F CA  1 
ATOM   6415  C  C   . GLY F  1 114 ? 20.941  -30.586 59.520  1.00 21.33 ? 114  GLY F C   1 
ATOM   6416  O  O   . GLY F  1 114 ? 22.064  -30.879 59.125  1.00 21.35 ? 114  GLY F O   1 
ATOM   6417  N  N   . ARG F  1 115 ? 20.547  -30.752 60.788  1.00 23.00 ? 115  ARG F N   1 
ATOM   6418  C  CA  . ARG F  1 115 ? 21.384  -31.413 61.789  1.00 21.11 ? 115  ARG F CA  1 
ATOM   6419  C  C   . ARG F  1 115 ? 20.732  -32.752 62.121  1.00 20.51 ? 115  ARG F C   1 
ATOM   6420  O  O   . ARG F  1 115 ? 19.809  -33.154 61.424  1.00 20.73 ? 115  ARG F O   1 
ATOM   6421  C  CB  . ARG F  1 115 ? 21.619  -30.510 63.013  1.00 20.82 ? 115  ARG F CB  1 
ATOM   6422  C  CG  . ARG F  1 115 ? 22.117  -29.103 62.595  1.00 22.08 ? 115  ARG F CG  1 
ATOM   6423  C  CD  . ARG F  1 115 ? 22.695  -28.309 63.745  1.00 20.89 ? 115  ARG F CD  1 
ATOM   6424  N  NE  . ARG F  1 115 ? 23.143  -26.971 63.350  1.00 21.78 ? 115  ARG F NE  1 
ATOM   6425  C  CZ  . ARG F  1 115 ? 24.394  -26.647 63.022  1.00 20.28 ? 115  ARG F CZ  1 
ATOM   6426  N  NH1 . ARG F  1 115 ? 25.361  -27.558 63.017  1.00 18.76 ? 115  ARG F NH1 1 
ATOM   6427  N  NH2 . ARG F  1 115 ? 24.683  -25.397 62.706  1.00 19.82 ? 115  ARG F NH2 1 
ATOM   6428  N  N   . THR F  1 116 ? 21.227  -33.462 63.134  1.00 20.17 ? 116  THR F N   1 
ATOM   6429  C  CA  . THR F  1 116 ? 20.794  -34.847 63.380  1.00 19.50 ? 116  THR F CA  1 
ATOM   6430  C  C   . THR F  1 116 ? 20.161  -35.067 64.754  1.00 18.39 ? 116  THR F C   1 
ATOM   6431  O  O   . THR F  1 116 ? 20.739  -34.715 65.764  1.00 19.23 ? 116  THR F O   1 
ATOM   6432  C  CB  . THR F  1 116 ? 21.985  -35.827 63.244  1.00 16.52 ? 116  THR F CB  1 
ATOM   6433  O  OG1 . THR F  1 116 ? 22.413  -35.880 61.879  1.00 21.37 ? 116  THR F OG1 1 
ATOM   6434  C  CG2 . THR F  1 116 ? 21.610  -37.212 63.696  1.00 15.52 ? 116  THR F CG2 1 
ATOM   6435  N  N   . MET F  1 117 ? 18.972  -35.657 64.793  1.00 20.04 ? 117  MET F N   1 
ATOM   6436  C  CA  . MET F  1 117 ? 18.446  -36.177 66.051  1.00 19.29 ? 117  MET F CA  1 
ATOM   6437  C  C   . MET F  1 117 ? 18.977  -37.588 66.256  1.00 19.99 ? 117  MET F C   1 
ATOM   6438  O  O   . MET F  1 117 ? 18.877  -38.437 65.359  1.00 18.76 ? 117  MET F O   1 
ATOM   6439  C  CB  . MET F  1 117 ? 16.912  -36.245 66.045  1.00 21.09 ? 117  MET F CB  1 
ATOM   6440  C  CG  . MET F  1 117 ? 16.188  -34.955 66.381  1.00 22.53 ? 117  MET F CG  1 
ATOM   6441  S  SD  . MET F  1 117 ? 16.629  -34.268 67.983  1.00 26.79 ? 117  MET F SD  1 
ATOM   6442  C  CE  . MET F  1 117 ? 16.724  -35.748 68.961  1.00 20.74 ? 117  MET F CE  1 
ATOM   6443  N  N   . VAL F  1 118 ? 19.541  -37.845 67.431  1.00 21.06 ? 118  VAL F N   1 
ATOM   6444  C  CA  . VAL F  1 118 ? 19.866  -39.218 67.813  1.00 21.60 ? 118  VAL F CA  1 
ATOM   6445  C  C   . VAL F  1 118 ? 19.294  -39.622 69.173  1.00 21.18 ? 118  VAL F C   1 
ATOM   6446  O  O   . VAL F  1 118 ? 19.279  -38.845 70.135  1.00 19.34 ? 118  VAL F O   1 
ATOM   6447  C  CB  . VAL F  1 118 ? 21.395  -39.636 67.616  1.00 21.58 ? 118  VAL F CB  1 
ATOM   6448  C  CG1 . VAL F  1 118 ? 22.258  -38.491 67.150  1.00 18.34 ? 118  VAL F CG1 1 
ATOM   6449  C  CG2 . VAL F  1 118 ? 21.959  -40.306 68.849  1.00 20.46 ? 118  VAL F CG2 1 
ATOM   6450  N  N   . VAL F  1 119 ? 18.768  -40.842 69.194  1.00 21.90 ? 119  VAL F N   1 
ATOM   6451  C  CA  . VAL F  1 119 ? 18.325  -41.501 70.407  1.00 21.49 ? 119  VAL F CA  1 
ATOM   6452  C  C   . VAL F  1 119 ? 19.385  -42.540 70.797  1.00 21.34 ? 119  VAL F C   1 
ATOM   6453  O  O   . VAL F  1 119 ? 19.842  -43.329 69.962  1.00 19.96 ? 119  VAL F O   1 
ATOM   6454  C  CB  . VAL F  1 119 ? 16.903  -42.119 70.248  1.00 20.35 ? 119  VAL F CB  1 
ATOM   6455  C  CG1 . VAL F  1 119 ? 16.858  -43.120 69.105  1.00 18.85 ? 119  VAL F CG1 1 
ATOM   6456  C  CG2 . VAL F  1 119 ? 16.430  -42.751 71.567  1.00 19.75 ? 119  VAL F CG2 1 
ATOM   6457  N  N   . HIS F  1 120 ? 19.790  -42.514 72.065  1.00 22.77 ? 120  HIS F N   1 
ATOM   6458  C  CA  . HIS F  1 120 ? 20.909  -43.326 72.528  1.00 21.35 ? 120  HIS F CA  1 
ATOM   6459  C  C   . HIS F  1 120 ? 20.480  -44.574 73.297  1.00 22.97 ? 120  HIS F C   1 
ATOM   6460  O  O   . HIS F  1 120 ? 19.301  -44.771 73.610  1.00 21.37 ? 120  HIS F O   1 
ATOM   6461  C  CB  . HIS F  1 120 ? 21.881  -42.498 73.377  1.00 20.95 ? 120  HIS F CB  1 
ATOM   6462  C  CG  . HIS F  1 120 ? 22.563  -41.398 72.624  1.00 21.13 ? 120  HIS F CG  1 
ATOM   6463  N  ND1 . HIS F  1 120 ? 23.819  -41.543 72.073  1.00 22.91 ? 120  HIS F ND1 1 
ATOM   6464  C  CD2 . HIS F  1 120 ? 22.170  -40.135 72.338  1.00 20.43 ? 120  HIS F CD2 1 
ATOM   6465  C  CE1 . HIS F  1 120 ? 24.166  -40.415 71.476  1.00 21.63 ? 120  HIS F CE1 1 
ATOM   6466  N  NE2 . HIS F  1 120 ? 23.182  -39.547 71.618  1.00 20.61 ? 120  HIS F NE2 1 
ATOM   6467  N  N   . GLU F  1 121 ? 21.481  -45.393 73.610  1.00 24.59 ? 121  GLU F N   1 
ATOM   6468  C  CA  . GLU F  1 121 ? 21.332  -46.706 74.238  1.00 25.47 ? 121  GLU F CA  1 
ATOM   6469  C  C   . GLU F  1 121 ? 20.900  -46.638 75.708  1.00 25.40 ? 121  GLU F C   1 
ATOM   6470  O  O   . GLU F  1 121 ? 20.016  -47.374 76.166  1.00 26.20 ? 121  GLU F O   1 
ATOM   6471  C  CB  . GLU F  1 121 ? 22.687  -47.397 74.142  1.00 23.52 ? 121  GLU F CB  1 
ATOM   6472  C  CG  . GLU F  1 121 ? 22.769  -48.771 74.699  1.00 26.39 ? 121  GLU F CG  1 
ATOM   6473  C  CD  . GLU F  1 121 ? 24.195  -49.100 75.074  1.00 31.35 ? 121  GLU F CD  1 
ATOM   6474  O  OE1 . GLU F  1 121 ? 24.979  -48.143 75.261  1.00 29.65 ? 121  GLU F OE1 1 
ATOM   6475  O  OE2 . GLU F  1 121 ? 24.532  -50.298 75.185  1.00 37.22 ? 121  GLU F OE2 1 
ATOM   6476  N  N   . LYS F  1 122 ? 21.543  -45.740 76.438  1.00 24.58 ? 122  LYS F N   1 
ATOM   6477  C  CA  . LYS F  1 122 ? 21.368  -45.637 77.868  1.00 25.17 ? 122  LYS F CA  1 
ATOM   6478  C  C   . LYS F  1 122 ? 20.766  -44.294 78.226  1.00 24.75 ? 122  LYS F C   1 
ATOM   6479  O  O   . LYS F  1 122 ? 20.497  -43.451 77.366  1.00 22.79 ? 122  LYS F O   1 
ATOM   6480  C  CB  . LYS F  1 122 ? 22.721  -45.759 78.593  1.00 24.45 ? 122  LYS F CB  1 
ATOM   6481  C  CG  . LYS F  1 122 ? 23.419  -47.083 78.443  1.00 26.29 ? 122  LYS F CG  1 
ATOM   6482  C  CD  . LYS F  1 122 ? 24.930  -46.951 78.666  1.00 29.77 ? 122  LYS F CD  1 
ATOM   6483  C  CE  . LYS F  1 122 ? 25.266  -46.006 79.823  1.00 36.73 ? 122  LYS F CE  1 
ATOM   6484  N  NZ  . LYS F  1 122 ? 25.045  -46.565 81.215  1.00 37.84 ? 122  LYS F NZ  1 
ATOM   6485  N  N   . GLN F  1 123 ? 20.599  -44.120 79.530  1.00 26.68 ? 123  GLN F N   1 
ATOM   6486  C  CA  . GLN F  1 123 ? 20.065  -42.923 80.128  1.00 24.15 ? 123  GLN F CA  1 
ATOM   6487  C  C   . GLN F  1 123 ? 21.135  -41.850 80.165  1.00 23.19 ? 123  GLN F C   1 
ATOM   6488  O  O   . GLN F  1 123 ? 22.301  -42.121 80.416  1.00 23.74 ? 123  GLN F O   1 
ATOM   6489  C  CB  . GLN F  1 123 ? 19.591  -43.248 81.543  1.00 26.84 ? 123  GLN F CB  1 
ATOM   6490  C  CG  . GLN F  1 123 ? 18.994  -42.081 82.318  1.00 26.16 ? 123  GLN F CG  1 
ATOM   6491  C  CD  . GLN F  1 123 ? 18.824  -42.413 83.782  1.00 26.40 ? 123  GLN F CD  1 
ATOM   6492  O  OE1 . GLN F  1 123 ? 18.523  -43.555 84.139  1.00 27.17 ? 123  GLN F OE1 1 
ATOM   6493  N  NE2 . GLN F  1 123 ? 19.032  -41.421 84.644  1.00 23.26 ? 123  GLN F NE2 1 
ATOM   6494  N  N   . ASP F  1 124 ? 20.717  -40.625 79.900  1.00 24.44 ? 124  ASP F N   1 
ATOM   6495  C  CA  . ASP F  1 124 ? 21.608  -39.486 79.873  1.00 22.90 ? 124  ASP F CA  1 
ATOM   6496  C  C   . ASP F  1 124 ? 21.694  -38.995 81.311  1.00 22.50 ? 124  ASP F C   1 
ATOM   6497  O  O   . ASP F  1 124 ? 20.678  -38.629 81.901  1.00 24.18 ? 124  ASP F O   1 
ATOM   6498  C  CB  . ASP F  1 124 ? 21.022  -38.437 78.917  1.00 20.05 ? 124  ASP F CB  1 
ATOM   6499  C  CG  . ASP F  1 124 ? 21.816  -37.155 78.874  1.00 21.38 ? 124  ASP F CG  1 
ATOM   6500  O  OD1 . ASP F  1 124 ? 22.769  -36.996 79.660  1.00 19.91 ? 124  ASP F OD1 1 
ATOM   6501  O  OD2 . ASP F  1 124 ? 21.472  -36.291 78.042  1.00 22.67 ? 124  ASP F OD2 1 
ATOM   6502  N  N   . ASP F  1 125 ? 22.902  -39.021 81.879  1.00 23.38 ? 125  ASP F N   1 
ATOM   6503  C  CA  . ASP F  1 125 ? 23.113  -38.709 83.293  1.00 20.19 ? 125  ASP F CA  1 
ATOM   6504  C  C   . ASP F  1 125 ? 23.165  -37.206 83.525  1.00 21.73 ? 125  ASP F C   1 
ATOM   6505  O  O   . ASP F  1 125 ? 23.407  -36.748 84.622  1.00 21.00 ? 125  ASP F O   1 
ATOM   6506  C  CB  . ASP F  1 125 ? 24.354  -39.427 83.849  1.00 21.56 ? 125  ASP F CB  1 
ATOM   6507  C  CG  . ASP F  1 125 ? 25.678  -38.870 83.310  1.00 24.40 ? 125  ASP F CG  1 
ATOM   6508  O  OD1 . ASP F  1 125 ? 25.739  -37.668 82.965  1.00 24.24 ? 125  ASP F OD1 1 
ATOM   6509  O  OD2 . ASP F  1 125 ? 26.672  -39.638 83.257  1.00 21.96 ? 125  ASP F OD2 1 
ATOM   6510  N  N   . LEU F  1 126 ? 22.913  -36.454 82.462  1.00 22.54 ? 126  LEU F N   1 
ATOM   6511  C  CA  . LEU F  1 126 ? 22.773  -35.000 82.500  1.00 21.18 ? 126  LEU F CA  1 
ATOM   6512  C  C   . LEU F  1 126 ? 23.997  -34.250 83.025  1.00 21.05 ? 126  LEU F C   1 
ATOM   6513  O  O   . LEU F  1 126 ? 23.870  -33.138 83.537  1.00 21.46 ? 126  LEU F O   1 
ATOM   6514  C  CB  . LEU F  1 126 ? 21.479  -34.573 83.220  1.00 20.98 ? 126  LEU F CB  1 
ATOM   6515  C  CG  . LEU F  1 126 ? 20.141  -35.276 82.891  1.00 21.15 ? 126  LEU F CG  1 
ATOM   6516  C  CD1 . LEU F  1 126 ? 19.012  -34.802 83.814  1.00 17.63 ? 126  LEU F CD1 1 
ATOM   6517  C  CD2 . LEU F  1 126 ? 19.714  -35.156 81.429  1.00 17.66 ? 126  LEU F CD2 1 
ATOM   6518  N  N   . GLY F  1 127 ? 25.177  -34.853 82.874  1.00 22.40 ? 127  GLY F N   1 
ATOM   6519  C  CA  . GLY F  1 127 ? 26.430  -34.215 83.254  1.00 22.20 ? 127  GLY F CA  1 
ATOM   6520  C  C   . GLY F  1 127 ? 26.749  -34.364 84.732  1.00 24.21 ? 127  GLY F C   1 
ATOM   6521  O  O   . GLY F  1 127 ? 27.575  -33.633 85.291  1.00 26.48 ? 127  GLY F O   1 
ATOM   6522  N  N   . LYS F  1 128 ? 26.083  -35.329 85.361  1.00 25.47 ? 128  LYS F N   1 
ATOM   6523  C  CA  . LYS F  1 128 ? 26.145  -35.533 86.802  1.00 20.48 ? 128  LYS F CA  1 
ATOM   6524  C  C   . LYS F  1 128 ? 26.744  -36.886 87.200  1.00 22.11 ? 128  LYS F C   1 
ATOM   6525  O  O   . LYS F  1 128 ? 26.487  -37.382 88.292  1.00 24.71 ? 128  LYS F O   1 
ATOM   6526  C  CB  . LYS F  1 128 ? 24.737  -35.464 87.363  1.00 22.07 ? 128  LYS F CB  1 
ATOM   6527  C  CG  . LYS F  1 128 ? 24.044  -34.145 87.171  1.00 22.18 ? 128  LYS F CG  1 
ATOM   6528  C  CD  . LYS F  1 128 ? 22.668  -34.184 87.807  1.00 25.36 ? 128  LYS F CD  1 
ATOM   6529  C  CE  . LYS F  1 128 ? 21.998  -32.838 87.693  1.00 29.87 ? 128  LYS F CE  1 
ATOM   6530  N  NZ  . LYS F  1 128 ? 23.032  -31.763 87.625  1.00 31.60 ? 128  LYS F NZ  1 
ATOM   6531  N  N   . GLY F  1 129 ? 27.537  -37.483 86.324  1.00 21.49 ? 129  GLY F N   1 
ATOM   6532  C  CA  . GLY F  1 129 ? 28.081  -38.805 86.575  1.00 22.72 ? 129  GLY F CA  1 
ATOM   6533  C  C   . GLY F  1 129 ? 29.505  -38.798 87.095  1.00 20.83 ? 129  GLY F C   1 
ATOM   6534  O  O   . GLY F  1 129 ? 30.102  -39.855 87.257  1.00 21.54 ? 129  GLY F O   1 
ATOM   6535  N  N   . GLY F  1 130 ? 30.046  -37.607 87.342  1.00 19.18 ? 130  GLY F N   1 
ATOM   6536  C  CA  . GLY F  1 130 ? 31.351  -37.456 87.948  1.00 18.94 ? 130  GLY F CA  1 
ATOM   6537  C  C   . GLY F  1 130 ? 32.559  -37.907 87.140  1.00 25.52 ? 130  GLY F C   1 
ATOM   6538  O  O   . GLY F  1 130 ? 33.637  -38.121 87.709  1.00 21.22 ? 130  GLY F O   1 
ATOM   6539  N  N   . ASN F  1 131 ? 32.388  -38.073 85.823  1.00 28.12 ? 131  ASN F N   1 
ATOM   6540  C  CA  . ASN F  1 131 ? 33.513  -38.336 84.917  1.00 24.66 ? 131  ASN F CA  1 
ATOM   6541  C  C   . ASN F  1 131 ? 33.501  -37.418 83.701  1.00 26.47 ? 131  ASN F C   1 
ATOM   6542  O  O   . ASN F  1 131 ? 32.711  -36.483 83.626  1.00 28.67 ? 131  ASN F O   1 
ATOM   6543  C  CB  . ASN F  1 131 ? 33.637  -39.820 84.525  1.00 22.58 ? 131  ASN F CB  1 
ATOM   6544  C  CG  . ASN F  1 131 ? 32.391  -40.376 83.908  1.00 25.31 ? 131  ASN F CG  1 
ATOM   6545  O  OD1 . ASN F  1 131 ? 31.542  -39.640 83.431  1.00 28.75 ? 131  ASN F OD1 1 
ATOM   6546  N  ND2 . ASN F  1 131 ? 32.270  -41.694 83.909  1.00 25.31 ? 131  ASN F ND2 1 
ATOM   6547  N  N   . GLU F  1 132 ? 34.393  -37.662 82.756  1.00 28.25 ? 132  GLU F N   1 
ATOM   6548  C  CA  . GLU F  1 132 ? 34.537  -36.740 81.637  1.00 30.65 ? 132  GLU F CA  1 
ATOM   6549  C  C   . GLU F  1 132 ? 33.600  -37.076 80.460  1.00 29.61 ? 132  GLU F C   1 
ATOM   6550  O  O   . GLU F  1 132 ? 33.213  -36.191 79.697  1.00 30.07 ? 132  GLU F O   1 
ATOM   6551  C  CB  . GLU F  1 132 ? 35.994  -36.679 81.192  1.00 32.48 ? 132  GLU F CB  1 
ATOM   6552  C  CG  . GLU F  1 132 ? 36.434  -35.332 80.669  1.00 33.89 ? 132  GLU F CG  1 
ATOM   6553  C  CD  . GLU F  1 132 ? 37.680  -35.459 79.826  1.00 43.29 ? 132  GLU F CD  1 
ATOM   6554  O  OE1 . GLU F  1 132 ? 38.401  -36.469 80.002  1.00 45.05 ? 132  GLU F OE1 1 
ATOM   6555  O  OE2 . GLU F  1 132 ? 37.931  -34.565 78.985  1.00 48.65 ? 132  GLU F OE2 1 
ATOM   6556  N  N   . GLU F  1 133 ? 33.245  -38.349 80.308  1.00 27.18 ? 133  GLU F N   1 
ATOM   6557  C  CA  . GLU F  1 133 ? 32.188  -38.714 79.381  1.00 29.86 ? 133  GLU F CA  1 
ATOM   6558  C  C   . GLU F  1 133 ? 30.901  -37.998 79.772  1.00 27.87 ? 133  GLU F C   1 
ATOM   6559  O  O   . GLU F  1 133 ? 30.158  -37.535 78.924  1.00 27.32 ? 133  GLU F O   1 
ATOM   6560  C  CB  . GLU F  1 133 ? 31.944  -40.220 79.382  1.00 31.26 ? 133  GLU F CB  1 
ATOM   6561  C  CG  . GLU F  1 133 ? 32.785  -40.980 78.375  1.00 40.19 ? 133  GLU F CG  1 
ATOM   6562  C  CD  . GLU F  1 133 ? 32.639  -40.444 76.962  1.00 36.58 ? 133  GLU F CD  1 
ATOM   6563  O  OE1 . GLU F  1 133 ? 31.494  -40.324 76.481  1.00 33.47 ? 133  GLU F OE1 1 
ATOM   6564  O  OE2 . GLU F  1 133 ? 33.675  -40.144 76.331  1.00 40.01 ? 133  GLU F OE2 1 
ATOM   6565  N  N   . SER F  1 134 ? 30.640  -37.910 81.068  1.00 27.46 ? 134  SER F N   1 
ATOM   6566  C  CA  . SER F  1 134 ? 29.429  -37.255 81.527  1.00 27.52 ? 134  SER F CA  1 
ATOM   6567  C  C   . SER F  1 134 ? 29.307  -35.841 80.940  1.00 25.44 ? 134  SER F C   1 
ATOM   6568  O  O   . SER F  1 134 ? 28.285  -35.502 80.353  1.00 26.93 ? 134  SER F O   1 
ATOM   6569  C  CB  . SER F  1 134 ? 29.343  -37.247 83.057  1.00 23.56 ? 134  SER F CB  1 
ATOM   6570  O  OG  . SER F  1 134 ? 28.084  -36.755 83.472  1.00 23.60 ? 134  SER F OG  1 
ATOM   6571  N  N   . THR F  1 135 ? 30.360  -35.038 81.073  1.00 27.14 ? 135  THR F N   1 
ATOM   6572  C  CA  . THR F  1 135 ? 30.344  -33.637 80.645  1.00 25.96 ? 135  THR F CA  1 
ATOM   6573  C  C   . THR F  1 135 ? 30.402  -33.461 79.128  1.00 26.11 ? 135  THR F C   1 
ATOM   6574  O  O   . THR F  1 135 ? 30.453  -32.332 78.634  1.00 25.04 ? 135  THR F O   1 
ATOM   6575  C  CB  . THR F  1 135 ? 31.538  -32.860 81.240  1.00 30.37 ? 135  THR F CB  1 
ATOM   6576  O  OG1 . THR F  1 135 ? 32.758  -33.342 80.650  1.00 30.81 ? 135  THR F OG1 1 
ATOM   6577  C  CG2 . THR F  1 135 ? 31.598  -33.020 82.753  1.00 26.79 ? 135  THR F CG2 1 
ATOM   6578  N  N   . LYS F  1 136 ? 30.408  -34.577 78.401  1.00 27.35 ? 136  LYS F N   1 
ATOM   6579  C  CA  . LYS F  1 136 ? 30.439  -34.572 76.935  1.00 25.32 ? 136  LYS F CA  1 
ATOM   6580  C  C   . LYS F  1 136 ? 29.187  -35.214 76.361  1.00 24.29 ? 136  LYS F C   1 
ATOM   6581  O  O   . LYS F  1 136 ? 28.412  -34.560 75.663  1.00 24.42 ? 136  LYS F O   1 
ATOM   6582  C  CB  . LYS F  1 136 ? 31.691  -35.290 76.404  1.00 27.31 ? 136  LYS F CB  1 
ATOM   6583  C  CG  . LYS F  1 136 ? 32.825  -34.339 75.987  1.00 34.81 ? 136  LYS F CG  1 
ATOM   6584  C  CD  . LYS F  1 136 ? 34.222  -34.784 76.457  1.00 37.10 ? 136  LYS F CD  1 
ATOM   6585  C  CE  . LYS F  1 136 ? 34.513  -36.258 76.158  1.00 40.37 ? 136  LYS F CE  1 
ATOM   6586  N  NZ  . LYS F  1 136 ? 34.489  -36.611 74.710  1.00 45.82 ? 136  LYS F NZ  1 
ATOM   6587  N  N   . THR F  1 137 ? 28.983  -36.491 76.673  1.00 24.60 ? 137  THR F N   1 
ATOM   6588  C  CA  . THR F  1 137 ? 27.886  -37.263 76.085  1.00 25.76 ? 137  THR F CA  1 
ATOM   6589  C  C   . THR F  1 137 ? 26.771  -37.629 77.078  1.00 24.75 ? 137  THR F C   1 
ATOM   6590  O  O   . THR F  1 137 ? 25.748  -38.184 76.688  1.00 24.63 ? 137  THR F O   1 
ATOM   6591  C  CB  . THR F  1 137 ? 28.407  -38.556 75.443  1.00 26.82 ? 137  THR F CB  1 
ATOM   6592  O  OG1 . THR F  1 137 ? 28.791  -39.477 76.470  1.00 25.07 ? 137  THR F OG1 1 
ATOM   6593  C  CG2 . THR F  1 137 ? 29.613  -38.268 74.550  1.00 24.50 ? 137  THR F CG2 1 
ATOM   6594  N  N   . GLY F  1 138 ? 26.960  -37.299 78.351  1.00 24.10 ? 138  GLY F N   1 
ATOM   6595  C  CA  . GLY F  1 138 ? 26.018  -37.699 79.375  1.00 23.66 ? 138  GLY F CA  1 
ATOM   6596  C  C   . GLY F  1 138 ? 26.044  -39.204 79.602  1.00 25.30 ? 138  GLY F C   1 
ATOM   6597  O  O   . GLY F  1 138 ? 25.113  -39.756 80.175  1.00 24.57 ? 138  GLY F O   1 
ATOM   6598  N  N   . ASN F  1 139 ? 27.110  -39.868 79.159  1.00 24.90 ? 139  ASN F N   1 
ATOM   6599  C  CA  . ASN F  1 139 ? 27.266  -41.310 79.363  1.00 25.64 ? 139  ASN F CA  1 
ATOM   6600  C  C   . ASN F  1 139 ? 26.079  -42.070 78.778  1.00 25.75 ? 139  ASN F C   1 
ATOM   6601  O  O   . ASN F  1 139 ? 25.686  -43.120 79.284  1.00 25.54 ? 139  ASN F O   1 
ATOM   6602  C  CB  . ASN F  1 139 ? 27.423  -41.643 80.861  1.00 30.24 ? 139  ASN F CB  1 
ATOM   6603  C  CG  . ASN F  1 139 ? 28.827  -41.334 81.409  1.00 27.96 ? 139  ASN F CG  1 
ATOM   6604  O  OD1 . ASN F  1 139 ? 29.832  -41.838 80.898  1.00 28.19 ? 139  ASN F OD1 1 
ATOM   6605  N  ND2 . ASN F  1 139 ? 28.888  -40.522 82.470  1.00 25.59 ? 139  ASN F ND2 1 
ATOM   6606  N  N   . ALA F  1 140 ? 25.505  -41.530 77.707  1.00 27.39 ? 140  ALA F N   1 
ATOM   6607  C  CA  . ALA F  1 140 ? 24.301  -42.098 77.101  1.00 24.66 ? 140  ALA F CA  1 
ATOM   6608  C  C   . ALA F  1 140 ? 24.577  -43.260 76.145  1.00 22.47 ? 140  ALA F C   1 
ATOM   6609  O  O   . ALA F  1 140 ? 23.662  -43.805 75.539  1.00 23.15 ? 140  ALA F O   1 
ATOM   6610  C  CB  . ALA F  1 140 ? 23.490  -41.008 76.404  1.00 20.64 ? 140  ALA F CB  1 
ATOM   6611  N  N   . GLY F  1 141 ? 25.841  -43.635 76.011  1.00 25.58 ? 141  GLY F N   1 
ATOM   6612  C  CA  . GLY F  1 141 ? 26.197  -44.800 75.224  1.00 25.28 ? 141  GLY F CA  1 
ATOM   6613  C  C   . GLY F  1 141 ? 26.052  -44.639 73.721  1.00 27.29 ? 141  GLY F C   1 
ATOM   6614  O  O   . GLY F  1 141 ? 26.192  -43.535 73.169  1.00 24.18 ? 141  GLY F O   1 
ATOM   6615  N  N   . SER F  1 142 ? 25.760  -45.755 73.056  1.00 27.42 ? 142  SER F N   1 
ATOM   6616  C  CA  . SER F  1 142 ? 25.761  -45.802 71.599  1.00 24.90 ? 142  SER F CA  1 
ATOM   6617  C  C   . SER F  1 142 ? 24.573  -45.070 70.992  1.00 25.19 ? 142  SER F C   1 
ATOM   6618  O  O   . SER F  1 142 ? 23.642  -44.685 71.697  1.00 23.79 ? 142  SER F O   1 
ATOM   6619  C  CB  . SER F  1 142 ? 25.806  -47.253 71.101  1.00 27.00 ? 142  SER F CB  1 
ATOM   6620  O  OG  . SER F  1 142 ? 24.513  -47.835 71.072  1.00 27.42 ? 142  SER F OG  1 
ATOM   6621  N  N   . ARG F  1 143 ? 24.630  -44.883 69.673  1.00 26.71 ? 143  ARG F N   1 
ATOM   6622  C  CA  . ARG F  1 143 ? 23.583  -44.208 68.916  1.00 23.67 ? 143  ARG F CA  1 
ATOM   6623  C  C   . ARG F  1 143 ? 22.746  -45.260 68.212  1.00 24.34 ? 143  ARG F C   1 
ATOM   6624  O  O   . ARG F  1 143 ? 23.190  -45.856 67.236  1.00 27.10 ? 143  ARG F O   1 
ATOM   6625  C  CB  . ARG F  1 143 ? 24.215  -43.253 67.908  1.00 21.15 ? 143  ARG F CB  1 
ATOM   6626  C  CG  . ARG F  1 143 ? 25.453  -42.585 68.475  1.00 21.50 ? 143  ARG F CG  1 
ATOM   6627  C  CD  . ARG F  1 143 ? 26.033  -41.534 67.568  1.00 20.39 ? 143  ARG F CD  1 
ATOM   6628  N  NE  . ARG F  1 143 ? 26.918  -40.654 68.314  1.00 22.42 ? 143  ARG F NE  1 
ATOM   6629  C  CZ  . ARG F  1 143 ? 27.526  -39.592 67.801  1.00 21.67 ? 143  ARG F CZ  1 
ATOM   6630  N  NH1 . ARG F  1 143 ? 27.349  -39.278 66.529  1.00 20.90 ? 143  ARG F NH1 1 
ATOM   6631  N  NH2 . ARG F  1 143 ? 28.312  -38.843 68.562  1.00 21.40 ? 143  ARG F NH2 1 
ATOM   6632  N  N   . LEU F  1 144 ? 21.544  -45.499 68.724  1.00 23.86 ? 144  LEU F N   1 
ATOM   6633  C  CA  . LEU F  1 144 ? 20.685  -46.570 68.229  1.00 24.24 ? 144  LEU F CA  1 
ATOM   6634  C  C   . LEU F  1 144 ? 19.981  -46.185 66.942  1.00 23.60 ? 144  LEU F C   1 
ATOM   6635  O  O   . LEU F  1 144 ? 19.701  -47.031 66.094  1.00 23.28 ? 144  LEU F O   1 
ATOM   6636  C  CB  . LEU F  1 144 ? 19.620  -46.909 69.269  1.00 24.26 ? 144  LEU F CB  1 
ATOM   6637  C  CG  . LEU F  1 144 ? 20.093  -47.305 70.661  1.00 22.61 ? 144  LEU F CG  1 
ATOM   6638  C  CD1 . LEU F  1 144 ? 18.896  -47.604 71.538  1.00 23.62 ? 144  LEU F CD1 1 
ATOM   6639  C  CD2 . LEU F  1 144 ? 21.002  -48.495 70.559  1.00 22.78 ? 144  LEU F CD2 1 
ATOM   6640  N  N   . ALA F  1 145 ? 19.667  -44.903 66.820  1.00 22.13 ? 145  ALA F N   1 
ATOM   6641  C  CA  . ALA F  1 145 ? 18.948  -44.414 65.661  1.00 22.56 ? 145  ALA F CA  1 
ATOM   6642  C  C   . ALA F  1 145 ? 19.130  -42.910 65.508  1.00 23.40 ? 145  ALA F C   1 
ATOM   6643  O  O   . ALA F  1 145 ? 19.300  -42.186 66.491  1.00 22.07 ? 145  ALA F O   1 
ATOM   6644  C  CB  . ALA F  1 145 ? 17.473  -44.774 65.763  1.00 23.08 ? 145  ALA F CB  1 
ATOM   6645  N  N   . CYS F  1 146 ? 19.109  -42.453 64.262  1.00 22.14 ? 146  CYS F N   1 
ATOM   6646  C  CA  . CYS F  1 146 ? 19.277  -41.043 63.965  1.00 20.98 ? 146  CYS F CA  1 
ATOM   6647  C  C   . CYS F  1 146 ? 18.604  -40.715 62.649  1.00 22.20 ? 146  CYS F C   1 
ATOM   6648  O  O   . CYS F  1 146 ? 18.184  -41.605 61.904  1.00 21.55 ? 146  CYS F O   1 
ATOM   6649  C  CB  . CYS F  1 146 ? 20.753  -40.666 63.894  1.00 21.24 ? 146  CYS F CB  1 
ATOM   6650  S  SG  . CYS F  1 146 ? 21.656  -41.551 62.610  1.00 28.58 ? 146  CYS F SG  1 
ATOM   6651  N  N   . GLY F  1 147 ? 18.489  -39.423 62.384  1.00 18.66 ? 147  GLY F N   1 
ATOM   6652  C  CA  . GLY F  1 147 ? 17.907  -38.959 61.155  1.00 21.40 ? 147  GLY F CA  1 
ATOM   6653  C  C   . GLY F  1 147 ? 18.226  -37.490 61.041  1.00 22.13 ? 147  GLY F C   1 
ATOM   6654  O  O   . GLY F  1 147 ? 18.453  -36.825 62.058  1.00 19.08 ? 147  GLY F O   1 
ATOM   6655  N  N   . VAL F  1 148 ? 18.244  -36.995 59.804  1.00 23.90 ? 148  VAL F N   1 
ATOM   6656  C  CA  . VAL F  1 148 ? 18.464  -35.582 59.533  1.00 20.16 ? 148  VAL F CA  1 
ATOM   6657  C  C   . VAL F  1 148 ? 17.157  -34.814 59.661  1.00 21.86 ? 148  VAL F C   1 
ATOM   6658  O  O   . VAL F  1 148 ? 16.101  -35.242 59.179  1.00 21.24 ? 148  VAL F O   1 
ATOM   6659  C  CB  . VAL F  1 148 ? 19.092  -35.361 58.143  1.00 18.50 ? 148  VAL F CB  1 
ATOM   6660  C  CG1 . VAL F  1 148 ? 19.501  -33.906 57.972  1.00 17.38 ? 148  VAL F CG1 1 
ATOM   6661  C  CG2 . VAL F  1 148 ? 20.292  -36.261 57.989  1.00 18.98 ? 148  VAL F CG2 1 
ATOM   6662  N  N   . ILE F  1 149 ? 17.243  -33.683 60.352  1.00 23.88 ? 149  ILE F N   1 
ATOM   6663  C  CA  . ILE F  1 149 ? 16.122  -32.774 60.535  1.00 24.42 ? 149  ILE F CA  1 
ATOM   6664  C  C   . ILE F  1 149 ? 15.861  -31.945 59.258  1.00 22.16 ? 149  ILE F C   1 
ATOM   6665  O  O   . ILE F  1 149 ? 16.670  -31.106 58.855  1.00 19.89 ? 149  ILE F O   1 
ATOM   6666  C  CB  . ILE F  1 149 ? 16.355  -31.894 61.786  1.00 21.28 ? 149  ILE F CB  1 
ATOM   6667  C  CG1 . ILE F  1 149 ? 16.660  -32.796 62.979  1.00 18.07 ? 149  ILE F CG1 1 
ATOM   6668  C  CG2 . ILE F  1 149 ? 15.144  -30.998 62.068  1.00 19.38 ? 149  ILE F CG2 1 
ATOM   6669  C  CD1 . ILE F  1 149 ? 17.308  -32.094 64.121  1.00 19.16 ? 149  ILE F CD1 1 
ATOM   6670  N  N   . GLY F  1 150 ? 14.720  -32.203 58.627  1.00 23.29 ? 150  GLY F N   1 
ATOM   6671  C  CA  . GLY F  1 150 ? 14.359  -31.527 57.399  1.00 23.83 ? 150  GLY F CA  1 
ATOM   6672  C  C   . GLY F  1 150 ? 13.162  -30.602 57.513  1.00 25.94 ? 150  GLY F C   1 
ATOM   6673  O  O   . GLY F  1 150 ? 12.358  -30.725 58.430  1.00 27.94 ? 150  GLY F O   1 
ATOM   6674  N  N   . ILE F  1 151 ? 13.059  -29.668 56.572  1.00 27.83 ? 151  ILE F N   1 
ATOM   6675  C  CA  . ILE F  1 151 ? 11.962  -28.712 56.514  1.00 26.82 ? 151  ILE F CA  1 
ATOM   6676  C  C   . ILE F  1 151 ? 10.702  -29.470 56.176  1.00 27.89 ? 151  ILE F C   1 
ATOM   6677  O  O   . ILE F  1 151 ? 10.689  -30.254 55.238  1.00 29.73 ? 151  ILE F O   1 
ATOM   6678  C  CB  . ILE F  1 151 ? 12.217  -27.659 55.412  1.00 23.98 ? 151  ILE F CB  1 
ATOM   6679  C  CG1 . ILE F  1 151 ? 13.531  -26.922 55.669  1.00 24.40 ? 151  ILE F CG1 1 
ATOM   6680  C  CG2 . ILE F  1 151 ? 11.073  -26.681 55.322  1.00 27.18 ? 151  ILE F CG2 1 
ATOM   6681  C  CD1 . ILE F  1 151 ? 14.004  -26.044 54.520  1.00 23.25 ? 151  ILE F CD1 1 
ATOM   6682  N  N   . ALA F  1 152 ? 9.643   -29.268 56.946  1.00 28.89 ? 152  ALA F N   1 
ATOM   6683  C  CA  . ALA F  1 152 ? 8.389   -29.943 56.646  1.00 30.10 ? 152  ALA F CA  1 
ATOM   6684  C  C   . ALA F  1 152 ? 7.340   -28.904 56.305  1.00 32.99 ? 152  ALA F C   1 
ATOM   6685  O  O   . ALA F  1 152 ? 7.505   -27.716 56.615  1.00 31.22 ? 152  ALA F O   1 
ATOM   6686  C  CB  . ALA F  1 152 ? 7.940   -30.825 57.819  1.00 28.40 ? 152  ALA F CB  1 
ATOM   6687  N  N   . GLN F  1 153 ? 6.277   -29.342 55.639  1.00 36.40 ? 153  GLN F N   1 
ATOM   6688  C  CA  . GLN F  1 153 ? 5.207   -28.423 55.281  1.00 42.31 ? 153  GLN F CA  1 
ATOM   6689  C  C   . GLN F  1 153 ? 4.125   -28.459 56.347  1.00 44.20 ? 153  GLN F C   1 
ATOM   6690  O  O   . GLN F  1 153 ? 3.420   -27.462 56.564  1.00 44.82 ? 153  GLN F O   1 
ATOM   6691  C  CB  . GLN F  1 153 ? 4.639   -28.708 53.875  1.00 43.18 ? 153  GLN F CB  1 
ATOM   6692  C  CG  . GLN F  1 153 ? 3.584   -29.818 53.757  1.00 45.39 ? 153  GLN F CG  1 
ATOM   6693  C  CD  . GLN F  1 153 ? 2.762   -29.709 52.465  1.00 45.98 ? 153  GLN F CD  1 
ATOM   6694  O  OE1 . GLN F  1 153 ? 2.522   -28.609 51.956  1.00 45.62 ? 153  GLN F OE1 1 
ATOM   6695  N  NE2 . GLN F  1 153 ? 2.327   -30.853 51.937  1.00 47.19 ? 153  GLN F NE2 1 
ATOM   6696  O  OXT . GLN F  1 153 ? 3.972   -29.491 57.019  1.00 43.95 ? 153  GLN F OXT 1 
ATOM   6697  N  N   . ALA G  1 1   ? 77.804  -16.023 3.592   1.00 34.86 ? 1    ALA G N   1 
ATOM   6698  C  CA  . ALA G  1 1   ? 77.170  -14.831 4.153   1.00 37.09 ? 1    ALA G CA  1 
ATOM   6699  C  C   . ALA G  1 1   ? 77.222  -13.603 3.230   1.00 35.47 ? 1    ALA G C   1 
ATOM   6700  O  O   . ALA G  1 1   ? 77.895  -12.621 3.542   1.00 38.48 ? 1    ALA G O   1 
ATOM   6701  C  CB  . ALA G  1 1   ? 77.779  -14.492 5.526   1.00 33.98 ? 1    ALA G CB  1 
ATOM   6702  N  N   . THR G  1 2   ? 76.497  -13.636 2.118   1.00 31.44 ? 2    THR G N   1 
ATOM   6703  C  CA  . THR G  1 2   ? 76.472  -12.482 1.218   1.00 30.07 ? 2    THR G CA  1 
ATOM   6704  C  C   . THR G  1 2   ? 76.062  -11.171 1.923   1.00 28.92 ? 2    THR G C   1 
ATOM   6705  O  O   . THR G  1 2   ? 75.201  -11.145 2.805   1.00 27.94 ? 2    THR G O   1 
ATOM   6706  C  CB  . THR G  1 2   ? 75.558  -12.704 -0.023  1.00 29.88 ? 2    THR G CB  1 
ATOM   6707  O  OG1 . THR G  1 2   ? 75.526  -14.090 -0.384  1.00 33.76 ? 2    THR G OG1 1 
ATOM   6708  C  CG2 . THR G  1 2   ? 76.060  -11.897 -1.219  1.00 30.95 ? 2    THR G CG2 1 
ATOM   6709  N  N   . LYS G  1 3   ? 76.718  -10.087 1.524   1.00 30.37 ? 3    LYS G N   1 
ATOM   6710  C  CA  . LYS G  1 3   ? 76.364  -8.731  1.918   1.00 24.26 ? 3    LYS G CA  1 
ATOM   6711  C  C   . LYS G  1 3   ? 76.158  -7.901  0.638   1.00 21.59 ? 3    LYS G C   1 
ATOM   6712  O  O   . LYS G  1 3   ? 76.746  -8.196  -0.393  1.00 25.00 ? 3    LYS G O   1 
ATOM   6713  C  CB  . LYS G  1 3   ? 77.463  -8.151  2.815   1.00 24.63 ? 3    LYS G CB  1 
ATOM   6714  C  CG  . LYS G  1 3   ? 77.367  -8.645  4.267   1.00 30.65 ? 3    LYS G CG  1 
ATOM   6715  C  CD  . LYS G  1 3   ? 78.675  -8.537  5.057   1.00 32.60 ? 3    LYS G CD  1 
ATOM   6716  C  CE  . LYS G  1 3   ? 79.109  -7.090  5.268   1.00 35.78 ? 3    LYS G CE  1 
ATOM   6717  N  NZ  . LYS G  1 3   ? 78.080  -6.258  5.960   1.00 42.53 ? 3    LYS G NZ  1 
ATOM   6718  N  N   . ALA G  1 4   ? 75.287  -6.905  0.681   1.00 20.33 ? 4    ALA G N   1 
ATOM   6719  C  CA  . ALA G  1 4   ? 75.151  -5.958  -0.429  1.00 19.30 ? 4    ALA G CA  1 
ATOM   6720  C  C   . ALA G  1 4   ? 74.850  -4.567  0.128   1.00 17.91 ? 4    ALA G C   1 
ATOM   6721  O  O   . ALA G  1 4   ? 74.642  -4.419  1.312   1.00 18.12 ? 4    ALA G O   1 
ATOM   6722  C  CB  . ALA G  1 4   ? 74.068  -6.401  -1.394  1.00 17.99 ? 4    ALA G CB  1 
ATOM   6723  N  N   . VAL G  1 5   ? 74.859  -3.540  -0.711  1.00 19.92 ? 5    VAL G N   1 
ATOM   6724  C  CA  . VAL G  1 5   ? 74.579  -2.189  -0.227  1.00 18.36 ? 5    VAL G CA  1 
ATOM   6725  C  C   . VAL G  1 5   ? 73.967  -1.326  -1.335  1.00 20.49 ? 5    VAL G C   1 
ATOM   6726  O  O   . VAL G  1 5   ? 74.155  -1.592  -2.523  1.00 17.61 ? 5    VAL G O   1 
ATOM   6727  C  CB  . VAL G  1 5   ? 75.839  -1.507  0.393   1.00 20.69 ? 5    VAL G CB  1 
ATOM   6728  C  CG1 . VAL G  1 5   ? 76.935  -1.332  -0.646  1.00 17.64 ? 5    VAL G CG1 1 
ATOM   6729  C  CG2 . VAL G  1 5   ? 75.480  -0.167  1.054   1.00 18.73 ? 5    VAL G CG2 1 
ATOM   6730  N  N   . CYS G  1 6   ? 73.205  -0.315  -0.927  1.00 21.13 ? 6    CYS G N   1 
ATOM   6731  C  CA  . CYS G  1 6   ? 72.579  0.610   -1.852  1.00 18.66 ? 6    CYS G CA  1 
ATOM   6732  C  C   . CYS G  1 6   ? 72.749  2.028   -1.343  1.00 19.79 ? 6    CYS G C   1 
ATOM   6733  O  O   . CYS G  1 6   ? 72.479  2.309   -0.182  1.00 19.58 ? 6    CYS G O   1 
ATOM   6734  C  CB  . CYS G  1 6   ? 71.088  0.310   -1.969  1.00 18.79 ? 6    CYS G CB  1 
ATOM   6735  S  SG  . CYS G  1 6   ? 70.364  0.957   -3.458  1.00 24.89 ? 6    CYS G SG  1 
ATOM   6736  N  N   . VAL G  1 7   ? 73.217  2.922   -2.204  1.00 22.02 ? 7    VAL G N   1 
ATOM   6737  C  CA  . VAL G  1 7   ? 73.215  4.343   -1.874  1.00 21.07 ? 7    VAL G CA  1 
ATOM   6738  C  C   . VAL G  1 7   ? 72.079  4.998   -2.674  1.00 21.38 ? 7    VAL G C   1 
ATOM   6739  O  O   . VAL G  1 7   ? 72.019  4.910   -3.901  1.00 21.94 ? 7    VAL G O   1 
ATOM   6740  C  CB  . VAL G  1 7   ? 74.596  5.004   -2.136  1.00 22.42 ? 7    VAL G CB  1 
ATOM   6741  C  CG1 . VAL G  1 7   ? 74.551  6.503   -1.855  1.00 21.22 ? 7    VAL G CG1 1 
ATOM   6742  C  CG2 . VAL G  1 7   ? 75.667  4.342   -1.284  1.00 20.92 ? 7    VAL G CG2 1 
ATOM   6743  N  N   . LEU G  1 8   ? 71.151  5.615   -1.962  1.00 20.98 ? 8    LEU G N   1 
ATOM   6744  C  CA  . LEU G  1 8   ? 69.980  6.200   -2.591  1.00 23.59 ? 8    LEU G CA  1 
ATOM   6745  C  C   . LEU G  1 8   ? 70.224  7.680   -2.830  1.00 21.89 ? 8    LEU G C   1 
ATOM   6746  O  O   . LEU G  1 8   ? 70.556  8.401   -1.909  1.00 24.10 ? 8    LEU G O   1 
ATOM   6747  C  CB  . LEU G  1 8   ? 68.739  6.002   -1.699  1.00 25.64 ? 8    LEU G CB  1 
ATOM   6748  C  CG  . LEU G  1 8   ? 68.179  4.602   -1.386  1.00 23.67 ? 8    LEU G CG  1 
ATOM   6749  C  CD1 . LEU G  1 8   ? 67.321  4.641   -0.131  1.00 26.42 ? 8    LEU G CD1 1 
ATOM   6750  C  CD2 . LEU G  1 8   ? 67.367  4.053   -2.535  1.00 21.88 ? 8    LEU G CD2 1 
ATOM   6751  N  N   . LYS G  1 9   ? 70.082  8.124   -4.069  1.00 22.02 ? 9    LYS G N   1 
ATOM   6752  C  CA  . LYS G  1 9   ? 70.085  9.546   -4.372  1.00 24.10 ? 9    LYS G CA  1 
ATOM   6753  C  C   . LYS G  1 9   ? 69.054  9.798   -5.463  1.00 23.47 ? 9    LYS G C   1 
ATOM   6754  O  O   . LYS G  1 9   ? 68.760  8.918   -6.261  1.00 20.89 ? 9    LYS G O   1 
ATOM   6755  C  CB  . LYS G  1 9   ? 71.452  10.012  -4.877  1.00 25.82 ? 9    LYS G CB  1 
ATOM   6756  C  CG  . LYS G  1 9   ? 72.621  9.867   -3.923  1.00 30.50 ? 9    LYS G CG  1 
ATOM   6757  C  CD  . LYS G  1 9   ? 73.932  10.232  -4.647  1.00 35.77 ? 9    LYS G CD  1 
ATOM   6758  C  CE  . LYS G  1 9   ? 75.167  9.569   -4.033  1.00 37.15 ? 9    LYS G CE  1 
ATOM   6759  N  NZ  . LYS G  1 9   ? 75.343  9.910   -2.592  1.00 37.40 ? 9    LYS G NZ  1 
ATOM   6760  N  N   . GLY G  1 10  ? 68.512  11.007  -5.497  1.00 26.31 ? 10   GLY G N   1 
ATOM   6761  C  CA  . GLY G  1 10  ? 67.621  11.420  -6.569  1.00 28.97 ? 10   GLY G CA  1 
ATOM   6762  C  C   . GLY G  1 10  ? 67.858  12.888  -6.874  1.00 32.82 ? 10   GLY G C   1 
ATOM   6763  O  O   . GLY G  1 10  ? 68.932  13.416  -6.559  1.00 30.15 ? 10   GLY G O   1 
ATOM   6764  N  N   . ASP G  1 11  ? 66.865  13.548  -7.475  1.00 37.04 ? 11   ASP G N   1 
ATOM   6765  C  CA  . ASP G  1 11  ? 66.956  14.984  -7.782  1.00 36.26 ? 11   ASP G CA  1 
ATOM   6766  C  C   . ASP G  1 11  ? 66.709  15.891  -6.578  1.00 34.17 ? 11   ASP G C   1 
ATOM   6767  O  O   . ASP G  1 11  ? 67.114  17.048  -6.581  1.00 36.71 ? 11   ASP G O   1 
ATOM   6768  C  CB  . ASP G  1 11  ? 65.984  15.369  -8.893  1.00 33.91 ? 11   ASP G CB  1 
ATOM   6769  C  CG  . ASP G  1 11  ? 66.263  14.649  -10.175 1.00 43.32 ? 11   ASP G CG  1 
ATOM   6770  O  OD1 . ASP G  1 11  ? 67.437  14.276  -10.401 1.00 44.74 ? 11   ASP G OD1 1 
ATOM   6771  O  OD2 . ASP G  1 11  ? 65.302  14.455  -10.951 1.00 50.44 ? 11   ASP G OD2 1 
ATOM   6772  N  N   . GLY G  1 12  ? 66.037  15.368  -5.559  1.00 36.55 ? 12   GLY G N   1 
ATOM   6773  C  CA  . GLY G  1 12  ? 65.673  16.156  -4.398  1.00 30.85 ? 12   GLY G CA  1 
ATOM   6774  C  C   . GLY G  1 12  ? 66.726  16.009  -3.332  1.00 29.72 ? 12   GLY G C   1 
ATOM   6775  O  O   . GLY G  1 12  ? 67.867  15.691  -3.662  1.00 30.13 ? 12   GLY G O   1 
ATOM   6776  N  N   . PRO G  1 13  ? 66.342  16.239  -2.056  1.00 30.63 ? 13   PRO G N   1 
ATOM   6777  C  CA  . PRO G  1 13  ? 67.161  16.156  -0.839  1.00 27.25 ? 13   PRO G CA  1 
ATOM   6778  C  C   . PRO G  1 13  ? 67.185  14.763  -0.220  1.00 26.47 ? 13   PRO G C   1 
ATOM   6779  O  O   . PRO G  1 13  ? 67.862  14.576  0.788   1.00 29.29 ? 13   PRO G O   1 
ATOM   6780  C  CB  . PRO G  1 13  ? 66.434  17.080  0.142   1.00 25.22 ? 13   PRO G CB  1 
ATOM   6781  C  CG  . PRO G  1 13  ? 65.121  17.413  -0.483  1.00 29.17 ? 13   PRO G CG  1 
ATOM   6782  C  CD  . PRO G  1 13  ? 64.958  16.616  -1.734  1.00 28.10 ? 13   PRO G CD  1 
ATOM   6783  N  N   . VAL G  1 14  ? 66.437  13.820  -0.785  1.00 26.38 ? 14   VAL G N   1 
ATOM   6784  C  CA  . VAL G  1 14  ? 66.317  12.486  -0.207  1.00 24.87 ? 14   VAL G CA  1 
ATOM   6785  C  C   . VAL G  1 14  ? 67.538  11.652  -0.536  1.00 24.73 ? 14   VAL G C   1 
ATOM   6786  O  O   . VAL G  1 14  ? 67.965  11.585  -1.685  1.00 26.43 ? 14   VAL G O   1 
ATOM   6787  C  CB  . VAL G  1 14  ? 65.051  11.760  -0.706  1.00 25.99 ? 14   VAL G CB  1 
ATOM   6788  C  CG1 . VAL G  1 14  ? 64.967  10.358  -0.104  1.00 25.06 ? 14   VAL G CG1 1 
ATOM   6789  C  CG2 . VAL G  1 14  ? 63.802  12.573  -0.372  1.00 24.26 ? 14   VAL G CG2 1 
ATOM   6790  N  N   . GLN G  1 15  ? 68.105  11.021  0.484   1.00 27.35 ? 15   GLN G N   1 
ATOM   6791  C  CA  . GLN G  1 15  ? 69.307  10.215  0.314   1.00 28.64 ? 15   GLN G CA  1 
ATOM   6792  C  C   . GLN G  1 15  ? 69.565  9.334   1.526   1.00 26.74 ? 15   GLN G C   1 
ATOM   6793  O  O   . GLN G  1 15  ? 69.244  9.706   2.648   1.00 26.68 ? 15   GLN G O   1 
ATOM   6794  C  CB  . GLN G  1 15  ? 70.516  11.110  0.071   1.00 31.65 ? 15   GLN G CB  1 
ATOM   6795  C  CG  . GLN G  1 15  ? 70.839  12.053  1.210   1.00 32.93 ? 15   GLN G CG  1 
ATOM   6796  C  CD  . GLN G  1 15  ? 71.973  12.996  0.848   1.00 40.56 ? 15   GLN G CD  1 
ATOM   6797  O  OE1 . GLN G  1 15  ? 72.457  12.993  -0.285  1.00 42.15 ? 15   GLN G OE1 1 
ATOM   6798  N  NE2 . GLN G  1 15  ? 72.403  13.806  1.806   1.00 44.39 ? 15   GLN G NE2 1 
ATOM   6799  N  N   . GLY G  1 16  ? 70.154  8.165   1.298   1.00 26.14 ? 16   GLY G N   1 
ATOM   6800  C  CA  . GLY G  1 16  ? 70.504  7.292   2.400   1.00 24.03 ? 16   GLY G CA  1 
ATOM   6801  C  C   . GLY G  1 16  ? 71.313  6.076   2.011   1.00 20.37 ? 16   GLY G C   1 
ATOM   6802  O  O   . GLY G  1 16  ? 71.627  5.868   0.849   1.00 19.50 ? 16   GLY G O   1 
ATOM   6803  N  N   . ILE G  1 17  ? 71.648  5.268   3.009   1.00 23.63 ? 17   ILE G N   1 
ATOM   6804  C  CA  . ILE G  1 17  ? 72.452  4.066   2.806   1.00 24.48 ? 17   ILE G CA  1 
ATOM   6805  C  C   . ILE G  1 17  ? 71.676  2.870   3.310   1.00 20.64 ? 17   ILE G C   1 
ATOM   6806  O  O   . ILE G  1 17  ? 71.309  2.821   4.473   1.00 21.91 ? 17   ILE G O   1 
ATOM   6807  C  CB  . ILE G  1 17  ? 73.808  4.140   3.556   1.00 22.20 ? 17   ILE G CB  1 
ATOM   6808  C  CG1 . ILE G  1 17  ? 74.719  5.190   2.920   1.00 23.61 ? 17   ILE G CG1 1 
ATOM   6809  C  CG2 . ILE G  1 17  ? 74.491  2.799   3.532   1.00 22.03 ? 17   ILE G CG2 1 
ATOM   6810  C  CD1 . ILE G  1 17  ? 75.896  5.574   3.787   1.00 23.14 ? 17   ILE G CD1 1 
ATOM   6811  N  N   . ILE G  1 18  ? 71.391  1.925   2.422   1.00 19.37 ? 18   ILE G N   1 
ATOM   6812  C  CA  . ILE G  1 18  ? 70.683  0.708   2.806   1.00 21.74 ? 18   ILE G CA  1 
ATOM   6813  C  C   . ILE G  1 18  ? 71.626  -0.497  2.721   1.00 18.94 ? 18   ILE G C   1 
ATOM   6814  O  O   . ILE G  1 18  ? 72.225  -0.752  1.682   1.00 17.97 ? 18   ILE G O   1 
ATOM   6815  C  CB  . ILE G  1 18  ? 69.414  0.484   1.935   1.00 19.40 ? 18   ILE G CB  1 
ATOM   6816  C  CG1 . ILE G  1 18  ? 68.560  1.748   1.908   1.00 19.35 ? 18   ILE G CG1 1 
ATOM   6817  C  CG2 . ILE G  1 18  ? 68.590  -0.676  2.467   1.00 18.24 ? 18   ILE G CG2 1 
ATOM   6818  C  CD1 . ILE G  1 18  ? 67.814  2.009   3.214   1.00 20.86 ? 18   ILE G CD1 1 
ATOM   6819  N  N   . ASN G  1 19  ? 71.775  -1.215  3.828   1.00 19.17 ? 19   ASN G N   1 
ATOM   6820  C  CA  . ASN G  1 19  ? 72.605  -2.410  3.855   1.00 19.20 ? 19   ASN G CA  1 
ATOM   6821  C  C   . ASN G  1 19  ? 71.743  -3.671  3.803   1.00 18.59 ? 19   ASN G C   1 
ATOM   6822  O  O   . ASN G  1 19  ? 70.627  -3.680  4.302   1.00 19.94 ? 19   ASN G O   1 
ATOM   6823  C  CB  . ASN G  1 19  ? 73.486  -2.403  5.101   1.00 20.63 ? 19   ASN G CB  1 
ATOM   6824  C  CG  . ASN G  1 19  ? 74.317  -1.135  5.222   1.00 23.45 ? 19   ASN G CG  1 
ATOM   6825  O  OD1 . ASN G  1 19  ? 75.265  -0.927  4.459   1.00 24.49 ? 19   ASN G OD1 1 
ATOM   6826  N  ND2 . ASN G  1 19  ? 73.975  -0.286  6.189   1.00 21.94 ? 19   ASN G ND2 1 
ATOM   6827  N  N   . PHE G  1 20  ? 72.260  -4.719  3.172   1.00 18.65 ? 20   PHE G N   1 
ATOM   6828  C  CA  . PHE G  1 20  ? 71.565  -6.001  3.028   1.00 19.41 ? 20   PHE G CA  1 
ATOM   6829  C  C   . PHE G  1 20  ? 72.495  -7.098  3.495   1.00 20.97 ? 20   PHE G C   1 
ATOM   6830  O  O   . PHE G  1 20  ? 73.680  -7.110  3.149   1.00 21.31 ? 20   PHE G O   1 
ATOM   6831  C  CB  . PHE G  1 20  ? 71.208  -6.287  1.564   1.00 16.11 ? 20   PHE G CB  1 
ATOM   6832  C  CG  . PHE G  1 20  ? 70.405  -5.208  0.918   1.00 15.76 ? 20   PHE G CG  1 
ATOM   6833  C  CD1 . PHE G  1 20  ? 70.998  -4.013  0.545   1.00 16.14 ? 20   PHE G CD1 1 
ATOM   6834  C  CD2 . PHE G  1 20  ? 69.058  -5.375  0.699   1.00 14.17 ? 20   PHE G CD2 1 
ATOM   6835  C  CE1 . PHE G  1 20  ? 70.264  -3.006  -0.031  1.00 17.22 ? 20   PHE G CE1 1 
ATOM   6836  C  CE2 . PHE G  1 20  ? 68.314  -4.361  0.125   1.00 15.42 ? 20   PHE G CE2 1 
ATOM   6837  C  CZ  . PHE G  1 20  ? 68.920  -3.176  -0.237  1.00 15.55 ? 20   PHE G CZ  1 
ATOM   6838  N  N   . GLU G  1 21  ? 71.967  -8.017  4.284   1.00 19.65 ? 21   GLU G N   1 
ATOM   6839  C  CA  . GLU G  1 21  ? 72.761  -9.151  4.698   1.00 24.24 ? 21   GLU G CA  1 
ATOM   6840  C  C   . GLU G  1 21  ? 71.933  -10.426 4.695   1.00 22.25 ? 21   GLU G C   1 
ATOM   6841  O  O   . GLU G  1 21  ? 70.770  -10.409 5.046   1.00 20.22 ? 21   GLU G O   1 
ATOM   6842  C  CB  . GLU G  1 21  ? 73.393  -8.914  6.071   1.00 25.92 ? 21   GLU G CB  1 
ATOM   6843  C  CG  . GLU G  1 21  ? 74.598  -9.812  6.289   1.00 33.85 ? 21   GLU G CG  1 
ATOM   6844  C  CD  . GLU G  1 21  ? 75.156  -9.744  7.691   1.00 38.57 ? 21   GLU G CD  1 
ATOM   6845  O  OE1 . GLU G  1 21  ? 74.844  -8.775  8.414   1.00 39.45 ? 21   GLU G OE1 1 
ATOM   6846  O  OE2 . GLU G  1 21  ? 75.915  -10.668 8.060   1.00 47.68 ? 21   GLU G OE2 1 
ATOM   6847  N  N   . GLN G  1 22  ? 72.554  -11.526 4.287   1.00 25.73 ? 22   GLN G N   1 
ATOM   6848  C  CA  . GLN G  1 22  ? 71.887  -12.811 4.215   1.00 23.98 ? 22   GLN G CA  1 
ATOM   6849  C  C   . GLN G  1 22  ? 72.829  -13.918 4.673   1.00 28.51 ? 22   GLN G C   1 
ATOM   6850  O  O   . GLN G  1 22  ? 73.640  -14.400 3.899   1.00 29.65 ? 22   GLN G O   1 
ATOM   6851  C  CB  . GLN G  1 22  ? 71.457  -13.071 2.784   1.00 24.61 ? 22   GLN G CB  1 
ATOM   6852  C  CG  . GLN G  1 22  ? 70.571  -14.269 2.619   1.00 23.56 ? 22   GLN G CG  1 
ATOM   6853  C  CD  . GLN G  1 22  ? 70.137  -14.470 1.181   1.00 21.79 ? 22   GLN G CD  1 
ATOM   6854  O  OE1 . GLN G  1 22  ? 70.898  -14.223 0.240   1.00 20.28 ? 22   GLN G OE1 1 
ATOM   6855  N  NE2 . GLN G  1 22  ? 68.909  -14.927 1.004   1.00 20.95 ? 22   GLN G NE2 1 
ATOM   6856  N  N   . LYS G  1 23  ? 72.704  -14.320 5.934   1.00 33.05 ? 23   LYS G N   1 
ATOM   6857  C  CA  . LYS G  1 23  ? 73.585  -15.316 6.547   1.00 35.58 ? 23   LYS G CA  1 
ATOM   6858  C  C   . LYS G  1 23  ? 73.583  -16.680 5.857   1.00 35.83 ? 23   LYS G C   1 
ATOM   6859  O  O   . LYS G  1 23  ? 74.638  -17.303 5.713   1.00 38.43 ? 23   LYS G O   1 
ATOM   6860  C  CB  . LYS G  1 23  ? 73.222  -15.509 8.024   1.00 36.81 ? 23   LYS G CB  1 
ATOM   6861  C  CG  . LYS G  1 23  ? 72.884  -14.223 8.753   1.00 42.58 ? 23   LYS G CG  1 
ATOM   6862  C  CD  . LYS G  1 23  ? 74.106  -13.325 8.909   1.00 49.32 ? 23   LYS G CD  1 
ATOM   6863  C  CE  . LYS G  1 23  ? 74.805  -13.565 10.245  1.00 53.18 ? 23   LYS G CE  1 
ATOM   6864  N  NZ  . LYS G  1 23  ? 75.303  -14.967 10.379  1.00 55.53 ? 23   LYS G NZ  1 
ATOM   6865  N  N   . GLU G  1 24  ? 72.404  -17.153 5.457   1.00 34.15 ? 24   GLU G N   1 
ATOM   6866  C  CA  . GLU G  1 24  ? 72.261  -18.510 4.925   1.00 33.59 ? 24   GLU G CA  1 
ATOM   6867  C  C   . GLU G  1 24  ? 71.897  -18.414 3.474   1.00 32.27 ? 24   GLU G C   1 
ATOM   6868  O  O   . GLU G  1 24  ? 71.257  -17.452 3.076   1.00 31.13 ? 24   GLU G O   1 
ATOM   6869  C  CB  . GLU G  1 24  ? 71.158  -19.284 5.654   1.00 33.94 ? 24   GLU G CB  1 
ATOM   6870  C  CG  . GLU G  1 24  ? 71.276  -19.312 7.182   1.00 39.43 ? 24   GLU G CG  1 
ATOM   6871  C  CD  . GLU G  1 24  ? 72.245  -20.382 7.697   1.00 46.80 ? 24   GLU G CD  1 
ATOM   6872  O  OE1 . GLU G  1 24  ? 72.605  -20.326 8.894   1.00 48.81 ? 24   GLU G OE1 1 
ATOM   6873  O  OE2 . GLU G  1 24  ? 72.643  -21.281 6.916   1.00 50.82 ? 24   GLU G OE2 1 
ATOM   6874  N  N   . SER G  1 25  ? 72.281  -19.423 2.695   1.00 37.75 ? 25   SER G N   1 
ATOM   6875  C  CA  . SER G  1 25  ? 72.081  -19.424 1.243   1.00 32.93 ? 25   SER G CA  1 
ATOM   6876  C  C   . SER G  1 25  ? 70.851  -18.653 0.800   1.00 33.77 ? 25   SER G C   1 
ATOM   6877  O  O   . SER G  1 25  ? 70.961  -17.540 0.263   1.00 37.86 ? 25   SER G O   1 
ATOM   6878  C  CB  . SER G  1 25  ? 71.974  -20.848 0.711   1.00 35.11 ? 25   SER G CB  1 
ATOM   6879  O  OG  . SER G  1 25  ? 71.435  -20.834 -0.604  1.00 34.70 ? 25   SER G OG  1 
ATOM   6880  N  N   . ASN G  1 26  ? 69.686  -19.264 1.002   1.00 29.53 ? 26   ASN G N   1 
ATOM   6881  C  CA  . ASN G  1 26  ? 68.410  -18.659 0.634   1.00 29.74 ? 26   ASN G CA  1 
ATOM   6882  C  C   . ASN G  1 26  ? 67.537  -18.410 1.860   1.00 30.22 ? 26   ASN G C   1 
ATOM   6883  O  O   . ASN G  1 26  ? 66.345  -18.735 1.878   1.00 31.25 ? 26   ASN G O   1 
ATOM   6884  C  CB  . ASN G  1 26  ? 67.668  -19.530 -0.383  1.00 31.17 ? 26   ASN G CB  1 
ATOM   6885  C  CG  . ASN G  1 26  ? 67.884  -19.072 -1.821  1.00 34.69 ? 26   ASN G CG  1 
ATOM   6886  O  OD1 . ASN G  1 26  ? 68.012  -17.873 -2.107  1.00 30.33 ? 26   ASN G OD1 1 
ATOM   6887  N  ND2 . ASN G  1 26  ? 67.910  -20.034 -2.741  1.00 39.58 ? 26   ASN G ND2 1 
ATOM   6888  N  N   . GLY G  1 27  ? 68.145  -17.835 2.890   1.00 26.90 ? 27   GLY G N   1 
ATOM   6889  C  CA  . GLY G  1 27  ? 67.448  -17.545 4.121   1.00 24.97 ? 27   GLY G CA  1 
ATOM   6890  C  C   . GLY G  1 27  ? 66.947  -16.118 4.139   1.00 25.92 ? 27   GLY G C   1 
ATOM   6891  O  O   . GLY G  1 27  ? 66.897  -15.459 3.086   1.00 24.50 ? 27   GLY G O   1 
ATOM   6892  N  N   . PRO G  1 28  ? 66.561  -15.637 5.332   1.00 22.35 ? 28   PRO G N   1 
ATOM   6893  C  CA  . PRO G  1 28  ? 66.074  -14.266 5.507   1.00 23.67 ? 28   PRO G CA  1 
ATOM   6894  C  C   . PRO G  1 28  ? 67.160  -13.248 5.190   1.00 21.75 ? 28   PRO G C   1 
ATOM   6895  O  O   . PRO G  1 28  ? 68.338  -13.489 5.425   1.00 23.02 ? 28   PRO G O   1 
ATOM   6896  C  CB  . PRO G  1 28  ? 65.691  -14.199 6.995   1.00 21.44 ? 28   PRO G CB  1 
ATOM   6897  C  CG  . PRO G  1 28  ? 65.548  -15.612 7.434   1.00 24.79 ? 28   PRO G CG  1 
ATOM   6898  C  CD  . PRO G  1 28  ? 66.488  -16.417 6.581   1.00 24.22 ? 28   PRO G CD  1 
ATOM   6899  N  N   . VAL G  1 29  ? 66.746  -12.115 4.642   1.00 24.42 ? 29   VAL G N   1 
ATOM   6900  C  CA  . VAL G  1 29  ? 67.645  -11.020 4.331   1.00 20.98 ? 29   VAL G CA  1 
ATOM   6901  C  C   . VAL G  1 29  ? 67.346  -9.888  5.303   1.00 20.94 ? 29   VAL G C   1 
ATOM   6902  O  O   . VAL G  1 29  ? 66.214  -9.450  5.395   1.00 22.80 ? 29   VAL G O   1 
ATOM   6903  C  CB  . VAL G  1 29  ? 67.408  -10.526 2.893   1.00 19.24 ? 29   VAL G CB  1 
ATOM   6904  C  CG1 . VAL G  1 29  ? 68.251  -9.298  2.601   1.00 18.64 ? 29   VAL G CG1 1 
ATOM   6905  C  CG2 . VAL G  1 29  ? 67.713  -11.625 1.900   1.00 19.12 ? 29   VAL G CG2 1 
ATOM   6906  N  N   . LYS G  1 30  ? 68.349  -9.441  6.051   1.00 21.13 ? 30   LYS G N   1 
ATOM   6907  C  CA  . LYS G  1 30  ? 68.221  -8.262  6.898   1.00 19.56 ? 30   LYS G CA  1 
ATOM   6908  C  C   . LYS G  1 30  ? 68.516  -7.046  6.038   1.00 20.74 ? 30   LYS G C   1 
ATOM   6909  O  O   . LYS G  1 30  ? 69.546  -6.983  5.375   1.00 22.34 ? 30   LYS G O   1 
ATOM   6910  C  CB  . LYS G  1 30  ? 69.202  -8.322  8.077   1.00 22.92 ? 30   LYS G CB  1 
ATOM   6911  C  CG  . LYS G  1 30  ? 69.023  -7.197  9.100   1.00 29.47 ? 30   LYS G CG  1 
ATOM   6912  C  CD  . LYS G  1 30  ? 70.294  -6.989  9.944   1.00 37.73 ? 30   LYS G CD  1 
ATOM   6913  C  CE  . LYS G  1 30  ? 70.045  -6.064  11.155  1.00 39.45 ? 30   LYS G CE  1 
ATOM   6914  N  NZ  . LYS G  1 30  ? 71.309  -5.671  11.858  1.00 40.36 ? 30   LYS G NZ  1 
ATOM   6915  N  N   . VAL G  1 31  ? 67.589  -6.097  6.025   1.00 22.15 ? 31   VAL G N   1 
ATOM   6916  C  CA  . VAL G  1 31  ? 67.730  -4.856  5.262   1.00 21.78 ? 31   VAL G CA  1 
ATOM   6917  C  C   . VAL G  1 31  ? 67.697  -3.715  6.281   1.00 21.59 ? 31   VAL G C   1 
ATOM   6918  O  O   . VAL G  1 31  ? 66.684  -3.492  6.933   1.00 21.90 ? 31   VAL G O   1 
ATOM   6919  C  CB  . VAL G  1 31  ? 66.589  -4.706  4.188   1.00 18.51 ? 31   VAL G CB  1 
ATOM   6920  C  CG1 . VAL G  1 31  ? 66.743  -3.431  3.385   1.00 16.73 ? 31   VAL G CG1 1 
ATOM   6921  C  CG2 . VAL G  1 31  ? 66.545  -5.922  3.252   1.00 16.25 ? 31   VAL G CG2 1 
ATOM   6922  N  N   . TRP G  1 32  ? 68.815  -3.020  6.456   1.00 24.37 ? 32   TRP G N   1 
ATOM   6923  C  CA  . TRP G  1 32  ? 68.874  -1.957  7.457   1.00 23.96 ? 32   TRP G CA  1 
ATOM   6924  C  C   . TRP G  1 32  ? 69.675  -0.752  6.981   1.00 21.64 ? 32   TRP G C   1 
ATOM   6925  O  O   . TRP G  1 32  ? 70.423  -0.834  6.021   1.00 23.26 ? 32   TRP G O   1 
ATOM   6926  C  CB  . TRP G  1 32  ? 69.425  -2.483  8.783   1.00 22.55 ? 32   TRP G CB  1 
ATOM   6927  C  CG  . TRP G  1 32  ? 70.898  -2.514  8.837   1.00 27.65 ? 32   TRP G CG  1 
ATOM   6928  C  CD1 . TRP G  1 32  ? 71.728  -1.549  9.359   1.00 28.45 ? 32   TRP G CD1 1 
ATOM   6929  C  CD2 . TRP G  1 32  ? 71.748  -3.565  8.364   1.00 26.09 ? 32   TRP G CD2 1 
ATOM   6930  N  NE1 . TRP G  1 32  ? 73.040  -1.944  9.224   1.00 28.62 ? 32   TRP G NE1 1 
ATOM   6931  C  CE2 . TRP G  1 32  ? 73.079  -3.176  8.625   1.00 25.93 ? 32   TRP G CE2 1 
ATOM   6932  C  CE3 . TRP G  1 32  ? 71.512  -4.792  7.742   1.00 25.19 ? 32   TRP G CE3 1 
ATOM   6933  C  CZ2 . TRP G  1 32  ? 74.168  -3.973  8.279   1.00 30.41 ? 32   TRP G CZ2 1 
ATOM   6934  C  CZ3 . TRP G  1 32  ? 72.592  -5.583  7.406   1.00 27.30 ? 32   TRP G CZ3 1 
ATOM   6935  C  CH2 . TRP G  1 32  ? 73.906  -5.172  7.670   1.00 28.80 ? 32   TRP G CH2 1 
ATOM   6936  N  N   . GLY G  1 33  ? 69.501  0.377   7.653   1.00 22.50 ? 33   GLY G N   1 
ATOM   6937  C  CA  . GLY G  1 33  ? 70.134  1.600   7.220   1.00 19.74 ? 33   GLY G CA  1 
ATOM   6938  C  C   . GLY G  1 33  ? 69.279  2.780   7.586   1.00 22.35 ? 33   GLY G C   1 
ATOM   6939  O  O   . GLY G  1 33  ? 68.501  2.715   8.532   1.00 24.08 ? 33   GLY G O   1 
ATOM   6940  N  N   . SER G  1 34  ? 69.402  3.852   6.818   1.00 21.16 ? 34   SER G N   1 
ATOM   6941  C  CA  . SER G  1 34  ? 68.761  5.102   7.160   1.00 21.83 ? 34   SER G CA  1 
ATOM   6942  C  C   . SER G  1 34  ? 68.525  5.936   5.911   1.00 22.20 ? 34   SER G C   1 
ATOM   6943  O  O   . SER G  1 34  ? 69.323  5.904   4.982   1.00 24.94 ? 34   SER G O   1 
ATOM   6944  C  CB  . SER G  1 34  ? 69.647  5.864   8.148   1.00 23.77 ? 34   SER G CB  1 
ATOM   6945  O  OG  . SER G  1 34  ? 69.190  7.190   8.325   1.00 27.57 ? 34   SER G OG  1 
ATOM   6946  N  N   . ILE G  1 35  ? 67.427  6.682   5.884   1.00 22.34 ? 35   ILE G N   1 
ATOM   6947  C  CA  . ILE G  1 35  ? 67.160  7.608   4.787   1.00 23.49 ? 35   ILE G CA  1 
ATOM   6948  C  C   . ILE G  1 35  ? 66.812  8.969   5.371   1.00 23.07 ? 35   ILE G C   1 
ATOM   6949  O  O   . ILE G  1 35  ? 66.077  9.053   6.337   1.00 26.11 ? 35   ILE G O   1 
ATOM   6950  C  CB  . ILE G  1 35  ? 65.978  7.136   3.901   1.00 21.50 ? 35   ILE G CB  1 
ATOM   6951  C  CG1 . ILE G  1 35  ? 66.181  5.695   3.431   1.00 22.52 ? 35   ILE G CG1 1 
ATOM   6952  C  CG2 . ILE G  1 35  ? 65.803  8.042   2.706   1.00 22.94 ? 35   ILE G CG2 1 
ATOM   6953  C  CD1 . ILE G  1 35  ? 65.056  5.176   2.553   1.00 19.07 ? 35   ILE G CD1 1 
ATOM   6954  N  N   . LYS G  1 36  ? 67.331  10.037  4.787   1.00 25.54 ? 36   LYS G N   1 
ATOM   6955  C  CA  . LYS G  1 36  ? 66.981  11.373  5.243   1.00 24.71 ? 36   LYS G CA  1 
ATOM   6956  C  C   . LYS G  1 36  ? 66.395  12.205  4.099   1.00 25.47 ? 36   LYS G C   1 
ATOM   6957  O  O   . LYS G  1 36  ? 66.367  11.758  2.950   1.00 24.04 ? 36   LYS G O   1 
ATOM   6958  C  CB  . LYS G  1 36  ? 68.203  12.049  5.864   1.00 28.08 ? 36   LYS G CB  1 
ATOM   6959  C  CG  . LYS G  1 36  ? 69.296  12.403  4.878   1.00 30.66 ? 36   LYS G CG  1 
ATOM   6960  C  CD  . LYS G  1 36  ? 70.536  12.876  5.611   1.00 37.69 ? 36   LYS G CD  1 
ATOM   6961  C  CE  . LYS G  1 36  ? 71.558  13.476  4.656   1.00 44.11 ? 36   LYS G CE  1 
ATOM   6962  N  NZ  . LYS G  1 36  ? 72.844  13.807  5.341   1.00 48.38 ? 36   LYS G NZ  1 
ATOM   6963  N  N   . GLY G  1 37  ? 65.900  13.399  4.419   1.00 26.65 ? 37   GLY G N   1 
ATOM   6964  C  CA  . GLY G  1 37  ? 65.364  14.299  3.410   1.00 22.05 ? 37   GLY G CA  1 
ATOM   6965  C  C   . GLY G  1 37  ? 63.889  14.087  3.107   1.00 25.63 ? 37   GLY G C   1 
ATOM   6966  O  O   . GLY G  1 37  ? 63.316  14.752  2.233   1.00 24.95 ? 37   GLY G O   1 
ATOM   6967  N  N   . LEU G  1 38  ? 63.273  13.165  3.845   1.00 27.13 ? 38   LEU G N   1 
ATOM   6968  C  CA  . LEU G  1 38  ? 61.901  12.721  3.587   1.00 28.45 ? 38   LEU G CA  1 
ATOM   6969  C  C   . LEU G  1 38  ? 60.862  13.575  4.318   1.00 29.30 ? 38   LEU G C   1 
ATOM   6970  O  O   . LEU G  1 38  ? 61.127  14.099  5.409   1.00 28.39 ? 38   LEU G O   1 
ATOM   6971  C  CB  . LEU G  1 38  ? 61.735  11.243  3.991   1.00 25.31 ? 38   LEU G CB  1 
ATOM   6972  C  CG  . LEU G  1 38  ? 62.404  10.161  3.130   1.00 22.54 ? 38   LEU G CG  1 
ATOM   6973  C  CD1 . LEU G  1 38  ? 62.400  8.819   3.841   1.00 22.14 ? 38   LEU G CD1 1 
ATOM   6974  C  CD2 . LEU G  1 38  ? 61.723  10.047  1.777   1.00 21.68 ? 38   LEU G CD2 1 
ATOM   6975  N  N   . THR G  1 39  ? 59.690  13.719  3.700   1.00 28.62 ? 39   THR G N   1 
ATOM   6976  C  CA  . THR G  1 39  ? 58.552  14.356  4.344   1.00 31.14 ? 39   THR G CA  1 
ATOM   6977  C  C   . THR G  1 39  ? 58.070  13.423  5.452   1.00 32.50 ? 39   THR G C   1 
ATOM   6978  O  O   . THR G  1 39  ? 58.112  12.204  5.293   1.00 32.24 ? 39   THR G O   1 
ATOM   6979  C  CB  . THR G  1 39  ? 57.433  14.634  3.335   1.00 31.06 ? 39   THR G CB  1 
ATOM   6980  O  OG1 . THR G  1 39  ? 57.162  13.440  2.592   1.00 32.62 ? 39   THR G OG1 1 
ATOM   6981  C  CG2 . THR G  1 39  ? 57.868  15.729  2.362   1.00 30.26 ? 39   THR G CG2 1 
ATOM   6982  N  N   . GLU G  1 40  ? 57.646  13.978  6.584   1.00 31.55 ? 40   GLU G N   1 
ATOM   6983  C  CA  . GLU G  1 40  ? 57.257  13.135  7.704   1.00 31.22 ? 40   GLU G CA  1 
ATOM   6984  C  C   . GLU G  1 40  ? 56.139  12.177  7.303   1.00 31.93 ? 40   GLU G C   1 
ATOM   6985  O  O   . GLU G  1 40  ? 55.238  12.548  6.554   1.00 32.83 ? 40   GLU G O   1 
ATOM   6986  C  CB  . GLU G  1 40  ? 56.833  13.975  8.914   1.00 34.29 ? 40   GLU G CB  1 
ATOM   6987  C  CG  . GLU G  1 40  ? 56.637  13.136  10.183  1.00 33.86 ? 40   GLU G CG  1 
ATOM   6988  C  CD  . GLU G  1 40  ? 55.934  13.886  11.298  1.00 33.81 ? 40   GLU G CD  1 
ATOM   6989  O  OE1 . GLU G  1 40  ? 55.841  15.130  11.205  1.00 33.34 ? 40   GLU G OE1 1 
ATOM   6990  O  OE2 . GLU G  1 40  ? 55.484  13.225  12.265  1.00 34.10 ? 40   GLU G OE2 1 
ATOM   6991  N  N   . GLY G  1 41  ? 56.202  10.944  7.795   1.00 30.11 ? 41   GLY G N   1 
ATOM   6992  C  CA  . GLY G  1 41  ? 55.164  9.969   7.516   1.00 30.87 ? 41   GLY G CA  1 
ATOM   6993  C  C   . GLY G  1 41  ? 55.660  8.690   6.865   1.00 30.30 ? 41   GLY G C   1 
ATOM   6994  O  O   . GLY G  1 41  ? 56.784  8.253   7.124   1.00 28.77 ? 41   GLY G O   1 
ATOM   6995  N  N   . LEU G  1 42  ? 54.815  8.092   6.017   1.00 30.98 ? 42   LEU G N   1 
ATOM   6996  C  CA  . LEU G  1 42  ? 55.105  6.791   5.401   1.00 26.89 ? 42   LEU G CA  1 
ATOM   6997  C  C   . LEU G  1 42  ? 55.452  6.914   3.910   1.00 25.84 ? 42   LEU G C   1 
ATOM   6998  O  O   . LEU G  1 42  ? 54.905  7.761   3.195   1.00 26.32 ? 42   LEU G O   1 
ATOM   6999  C  CB  . LEU G  1 42  ? 53.938  5.811   5.607   1.00 25.34 ? 42   LEU G CB  1 
ATOM   7000  C  CG  . LEU G  1 42  ? 53.476  5.457   7.026   1.00 22.96 ? 42   LEU G CG  1 
ATOM   7001  C  CD1 . LEU G  1 42  ? 52.182  4.692   6.968   1.00 30.17 ? 42   LEU G CD1 1 
ATOM   7002  C  CD2 . LEU G  1 42  ? 54.505  4.653   7.778   1.00 27.04 ? 42   LEU G CD2 1 
ATOM   7003  N  N   . HIS G  1 43  ? 56.369  6.070   3.452   1.00 22.56 ? 43   HIS G N   1 
ATOM   7004  C  CA  . HIS G  1 43  ? 56.868  6.154   2.086   1.00 20.88 ? 43   HIS G CA  1 
ATOM   7005  C  C   . HIS G  1 43  ? 57.094  4.758   1.534   1.00 20.36 ? 43   HIS G C   1 
ATOM   7006  O  O   . HIS G  1 43  ? 57.722  3.934   2.197   1.00 20.89 ? 43   HIS G O   1 
ATOM   7007  C  CB  . HIS G  1 43  ? 58.195  6.919   2.053   1.00 23.44 ? 43   HIS G CB  1 
ATOM   7008  C  CG  . HIS G  1 43  ? 58.076  8.368   2.410   1.00 23.34 ? 43   HIS G CG  1 
ATOM   7009  N  ND1 . HIS G  1 43  ? 58.093  9.370   1.464   1.00 22.92 ? 43   HIS G ND1 1 
ATOM   7010  C  CD2 . HIS G  1 43  ? 57.955  8.984   3.609   1.00 22.85 ? 43   HIS G CD2 1 
ATOM   7011  C  CE1 . HIS G  1 43  ? 57.976  10.542  2.063   1.00 22.83 ? 43   HIS G CE1 1 
ATOM   7012  N  NE2 . HIS G  1 43  ? 57.886  10.334  3.364   1.00 25.64 ? 43   HIS G NE2 1 
ATOM   7013  N  N   . GLY G  1 44  ? 56.587  4.501   0.326   1.00 21.11 ? 44   GLY G N   1 
ATOM   7014  C  CA  . GLY G  1 44  ? 56.772  3.222   -0.350  1.00 21.04 ? 44   GLY G CA  1 
ATOM   7015  C  C   . GLY G  1 44  ? 58.230  2.850   -0.594  1.00 20.54 ? 44   GLY G C   1 
ATOM   7016  O  O   . GLY G  1 44  ? 59.025  3.677   -1.017  1.00 19.88 ? 44   GLY G O   1 
ATOM   7017  N  N   . PHE G  1 45  ? 58.575  1.592   -0.339  1.00 20.80 ? 45   PHE G N   1 
ATOM   7018  C  CA  . PHE G  1 45  ? 59.968  1.147   -0.349  1.00 19.31 ? 45   PHE G CA  1 
ATOM   7019  C  C   . PHE G  1 45  ? 60.049  -0.204  -1.047  1.00 19.39 ? 45   PHE G C   1 
ATOM   7020  O  O   . PHE G  1 45  ? 59.605  -1.222  -0.508  1.00 18.69 ? 45   PHE G O   1 
ATOM   7021  C  CB  . PHE G  1 45  ? 60.483  1.058   1.092   1.00 19.10 ? 45   PHE G CB  1 
ATOM   7022  C  CG  . PHE G  1 45  ? 61.971  0.844   1.214   1.00 17.63 ? 45   PHE G CG  1 
ATOM   7023  C  CD1 . PHE G  1 45  ? 62.872  1.791   0.751   1.00 19.84 ? 45   PHE G CD1 1 
ATOM   7024  C  CD2 . PHE G  1 45  ? 62.465  -0.295  1.830   1.00 18.89 ? 45   PHE G CD2 1 
ATOM   7025  C  CE1 . PHE G  1 45  ? 64.251  1.601   0.885   1.00 20.86 ? 45   PHE G CE1 1 
ATOM   7026  C  CE2 . PHE G  1 45  ? 63.842  -0.499  1.965   1.00 21.44 ? 45   PHE G CE2 1 
ATOM   7027  C  CZ  . PHE G  1 45  ? 64.738  0.450   1.493   1.00 18.79 ? 45   PHE G CZ  1 
ATOM   7028  N  N   . HIS G  1 46  ? 60.605  -0.204  -2.256  1.00 19.59 ? 46   HIS G N   1 
ATOM   7029  C  CA  . HIS G  1 46  ? 60.477  -1.340  -3.160  1.00 19.19 ? 46   HIS G CA  1 
ATOM   7030  C  C   . HIS G  1 46  ? 61.722  -1.544  -3.979  1.00 19.58 ? 46   HIS G C   1 
ATOM   7031  O  O   . HIS G  1 46  ? 62.387  -0.574  -4.369  1.00 19.32 ? 46   HIS G O   1 
ATOM   7032  C  CB  . HIS G  1 46  ? 59.338  -1.116  -4.163  1.00 19.39 ? 46   HIS G CB  1 
ATOM   7033  C  CG  . HIS G  1 46  ? 58.094  -0.554  -3.558  1.00 19.37 ? 46   HIS G CG  1 
ATOM   7034  N  ND1 . HIS G  1 46  ? 57.641  0.716   -3.843  1.00 20.02 ? 46   HIS G ND1 1 
ATOM   7035  C  CD2 . HIS G  1 46  ? 57.205  -1.091  -2.693  1.00 17.02 ? 46   HIS G CD2 1 
ATOM   7036  C  CE1 . HIS G  1 46  ? 56.526  0.940   -3.172  1.00 18.59 ? 46   HIS G CE1 1 
ATOM   7037  N  NE2 . HIS G  1 46  ? 56.242  -0.141  -2.466  1.00 17.81 ? 46   HIS G NE2 1 
ATOM   7038  N  N   . VAL G  1 47  ? 62.005  -2.814  -4.266  1.00 19.20 ? 47   VAL G N   1 
ATOM   7039  C  CA  . VAL G  1 47  ? 63.048  -3.193  -5.216  1.00 18.59 ? 47   VAL G CA  1 
ATOM   7040  C  C   . VAL G  1 47  ? 62.420  -3.174  -6.591  1.00 17.48 ? 47   VAL G C   1 
ATOM   7041  O  O   . VAL G  1 47  ? 61.462  -3.888  -6.843  1.00 18.73 ? 47   VAL G O   1 
ATOM   7042  C  CB  . VAL G  1 47  ? 63.599  -4.613  -4.924  1.00 15.93 ? 47   VAL G CB  1 
ATOM   7043  C  CG1 . VAL G  1 47  ? 64.718  -4.967  -5.876  1.00 15.00 ? 47   VAL G CG1 1 
ATOM   7044  C  CG2 . VAL G  1 47  ? 64.061  -4.719  -3.478  1.00 16.95 ? 47   VAL G CG2 1 
ATOM   7045  N  N   . HIS G  1 48  ? 62.954  -2.344  -7.477  1.00 19.16 ? 48   HIS G N   1 
ATOM   7046  C  CA  . HIS G  1 48  ? 62.517  -2.316  -8.865  1.00 19.40 ? 48   HIS G CA  1 
ATOM   7047  C  C   . HIS G  1 48  ? 63.396  -3.219  -9.739  1.00 20.12 ? 48   HIS G C   1 
ATOM   7048  O  O   . HIS G  1 48  ? 64.530  -3.543  -9.377  1.00 18.93 ? 48   HIS G O   1 
ATOM   7049  C  CB  . HIS G  1 48  ? 62.476  -0.876  -9.388  1.00 19.87 ? 48   HIS G CB  1 
ATOM   7050  C  CG  . HIS G  1 48  ? 61.391  -0.044  -8.766  1.00 19.13 ? 48   HIS G CG  1 
ATOM   7051  N  ND1 . HIS G  1 48  ? 60.388  0.547   -9.502  1.00 18.22 ? 48   HIS G ND1 1 
ATOM   7052  C  CD2 . HIS G  1 48  ? 61.139  0.272   -7.475  1.00 17.98 ? 48   HIS G CD2 1 
ATOM   7053  C  CE1 . HIS G  1 48  ? 59.578  1.207   -8.696  1.00 17.38 ? 48   HIS G CE1 1 
ATOM   7054  N  NE2 . HIS G  1 48  ? 60.014  1.058   -7.459  1.00 17.80 ? 48   HIS G NE2 1 
ATOM   7055  N  N   . GLU G  1 49  ? 62.863  -3.619  -10.887 1.00 18.57 ? 49   GLU G N   1 
ATOM   7056  C  CA  . GLU G  1 49  ? 63.434  -4.713  -11.658 1.00 19.13 ? 49   GLU G CA  1 
ATOM   7057  C  C   . GLU G  1 49  ? 64.848  -4.449  -12.154 1.00 22.59 ? 49   GLU G C   1 
ATOM   7058  O  O   . GLU G  1 49  ? 65.714  -5.326  -12.055 1.00 22.04 ? 49   GLU G O   1 
ATOM   7059  C  CB  . GLU G  1 49  ? 62.533  -5.049  -12.839 1.00 18.80 ? 49   GLU G CB  1 
ATOM   7060  C  CG  . GLU G  1 49  ? 62.952  -6.281  -13.595 1.00 21.74 ? 49   GLU G CG  1 
ATOM   7061  C  CD  . GLU G  1 49  ? 61.943  -6.661  -14.671 1.00 26.47 ? 49   GLU G CD  1 
ATOM   7062  O  OE1 . GLU G  1 49  ? 60.842  -6.057  -14.708 1.00 26.22 ? 49   GLU G OE1 1 
ATOM   7063  O  OE2 . GLU G  1 49  ? 62.246  -7.573  -15.472 1.00 25.10 ? 49   GLU G OE2 1 
ATOM   7064  N  N   . PHE G  1 50  ? 65.091  -3.247  -12.681 1.00 22.21 ? 50   PHE G N   1 
ATOM   7065  C  CA  . PHE G  1 50  ? 66.365  -2.965  -13.345 1.00 20.41 ? 50   PHE G CA  1 
ATOM   7066  C  C   . PHE G  1 50  ? 67.300  -2.103  -12.508 1.00 18.82 ? 50   PHE G C   1 
ATOM   7067  O  O   . PHE G  1 50  ? 66.857  -1.149  -11.863 1.00 16.88 ? 50   PHE G O   1 
ATOM   7068  C  CB  . PHE G  1 50  ? 66.146  -2.325  -14.732 1.00 17.49 ? 50   PHE G CB  1 
ATOM   7069  C  CG  . PHE G  1 50  ? 65.155  -3.067  -15.590 1.00 21.54 ? 50   PHE G CG  1 
ATOM   7070  C  CD1 . PHE G  1 50  ? 65.360  -4.404  -15.912 1.00 20.87 ? 50   PHE G CD1 1 
ATOM   7071  C  CD2 . PHE G  1 50  ? 64.022  -2.436  -16.064 1.00 20.00 ? 50   PHE G CD2 1 
ATOM   7072  C  CE1 . PHE G  1 50  ? 64.459  -5.088  -16.676 1.00 19.97 ? 50   PHE G CE1 1 
ATOM   7073  C  CE2 . PHE G  1 50  ? 63.111  -3.120  -16.823 1.00 22.35 ? 50   PHE G CE2 1 
ATOM   7074  C  CZ  . PHE G  1 50  ? 63.329  -4.452  -17.131 1.00 24.48 ? 50   PHE G CZ  1 
ATOM   7075  N  N   . GLY G  1 51  ? 68.590  -2.453  -12.539 1.00 17.97 ? 51   GLY G N   1 
ATOM   7076  C  CA  . GLY G  1 51  ? 69.650  -1.614  -12.004 1.00 16.17 ? 51   GLY G CA  1 
ATOM   7077  C  C   . GLY G  1 51  ? 70.096  -0.653  -13.086 1.00 18.68 ? 51   GLY G C   1 
ATOM   7078  O  O   . GLY G  1 51  ? 71.279  -0.558  -13.425 1.00 16.66 ? 51   GLY G O   1 
ATOM   7079  N  N   . ASP G  1 52  ? 69.111  0.054   -13.631 1.00 19.07 ? 52   ASP G N   1 
ATOM   7080  C  CA  . ASP G  1 52  ? 69.286  0.961   -14.750 1.00 20.40 ? 52   ASP G CA  1 
ATOM   7081  C  C   . ASP G  1 52  ? 68.907  2.357   -14.270 1.00 21.29 ? 52   ASP G C   1 
ATOM   7082  O  O   . ASP G  1 52  ? 67.740  2.624   -14.009 1.00 20.19 ? 52   ASP G O   1 
ATOM   7083  C  CB  . ASP G  1 52  ? 68.386  0.507   -15.912 1.00 21.03 ? 52   ASP G CB  1 
ATOM   7084  C  CG  . ASP G  1 52  ? 68.686  1.222   -17.216 1.00 21.94 ? 52   ASP G CG  1 
ATOM   7085  O  OD1 . ASP G  1 52  ? 69.040  2.412   -17.178 1.00 24.94 ? 52   ASP G OD1 1 
ATOM   7086  O  OD2 . ASP G  1 52  ? 68.550  0.601   -18.291 1.00 24.64 ? 52   ASP G OD2 1 
ATOM   7087  N  N   . ASN G  1 53  ? 69.899  3.233   -14.123 1.00 20.69 ? 53   ASN G N   1 
ATOM   7088  C  CA  . ASN G  1 53  ? 69.659  4.604   -13.681 1.00 22.47 ? 53   ASN G CA  1 
ATOM   7089  C  C   . ASN G  1 53  ? 69.967  5.638   -14.766 1.00 23.84 ? 53   ASN G C   1 
ATOM   7090  O  O   . ASN G  1 53  ? 70.280  6.780   -14.448 1.00 26.65 ? 53   ASN G O   1 
ATOM   7091  C  CB  . ASN G  1 53  ? 70.494  4.895   -12.422 1.00 26.43 ? 53   ASN G CB  1 
ATOM   7092  C  CG  . ASN G  1 53  ? 70.254  6.296   -11.846 1.00 34.00 ? 53   ASN G CG  1 
ATOM   7093  O  OD1 . ASN G  1 53  ? 71.098  7.193   -11.982 1.00 36.60 ? 53   ASN G OD1 1 
ATOM   7094  N  ND2 . ASN G  1 53  ? 69.110  6.485   -11.193 1.00 32.34 ? 53   ASN G ND2 1 
ATOM   7095  N  N   . THR G  1 54  ? 69.869  5.245   -16.041 1.00 24.89 ? 54   THR G N   1 
ATOM   7096  C  CA  . THR G  1 54  ? 70.311  6.092   -17.159 1.00 23.89 ? 54   THR G CA  1 
ATOM   7097  C  C   . THR G  1 54  ? 69.475  7.356   -17.361 1.00 28.54 ? 54   THR G C   1 
ATOM   7098  O  O   . THR G  1 54  ? 69.970  8.380   -17.850 1.00 27.68 ? 54   THR G O   1 
ATOM   7099  C  CB  . THR G  1 54  ? 70.408  5.310   -18.506 1.00 23.37 ? 54   THR G CB  1 
ATOM   7100  O  OG1 . THR G  1 54  ? 69.198  4.575   -18.748 1.00 24.36 ? 54   THR G OG1 1 
ATOM   7101  C  CG2 . THR G  1 54  ? 71.586  4.359   -18.485 1.00 23.21 ? 54   THR G CG2 1 
ATOM   7102  N  N   . ALA G  1 55  ? 68.205  7.274   -16.986 1.00 28.54 ? 55   ALA G N   1 
ATOM   7103  C  CA  . ALA G  1 55  ? 67.302  8.402   -17.097 1.00 27.35 ? 55   ALA G CA  1 
ATOM   7104  C  C   . ALA G  1 55  ? 66.664  8.639   -15.751 1.00 25.02 ? 55   ALA G C   1 
ATOM   7105  O  O   . ALA G  1 55  ? 65.468  8.900   -15.675 1.00 31.36 ? 55   ALA G O   1 
ATOM   7106  C  CB  . ALA G  1 55  ? 66.232  8.123   -18.144 1.00 28.75 ? 55   ALA G CB  1 
ATOM   7107  N  N   . GLY G  1 56  ? 67.463  8.525   -14.690 1.00 28.80 ? 56   GLY G N   1 
ATOM   7108  C  CA  . GLY G  1 56  ? 66.999  8.725   -13.320 1.00 27.94 ? 56   GLY G CA  1 
ATOM   7109  C  C   . GLY G  1 56  ? 66.366  7.490   -12.702 1.00 25.90 ? 56   GLY G C   1 
ATOM   7110  O  O   . GLY G  1 56  ? 66.781  6.376   -12.973 1.00 28.04 ? 56   GLY G O   1 
ATOM   7111  N  N   . CYS G  1 57  ? 65.348  7.677   -11.873 1.00 27.09 ? 57   CYS G N   1 
ATOM   7112  C  CA  . CYS G  1 57  ? 64.714  6.543   -11.206 1.00 25.18 ? 57   CYS G CA  1 
ATOM   7113  C  C   . CYS G  1 57  ? 63.709  5.827   -12.103 1.00 24.78 ? 57   CYS G C   1 
ATOM   7114  O  O   . CYS G  1 57  ? 63.417  4.644   -11.914 1.00 26.76 ? 57   CYS G O   1 
ATOM   7115  C  CB  . CYS G  1 57  ? 64.057  6.994   -9.908  1.00 26.10 ? 57   CYS G CB  1 
ATOM   7116  S  SG  . CYS G  1 57  ? 65.249  7.588   -8.685  1.00 31.63 ? 57   CYS G SG  1 
ATOM   7117  N  N   . THR G  1 58  ? 63.199  6.553   -13.088 1.00 24.70 ? 58   THR G N   1 
ATOM   7118  C  CA  . THR G  1 58  ? 62.288  6.010   -14.091 1.00 23.54 ? 58   THR G CA  1 
ATOM   7119  C  C   . THR G  1 58  ? 62.793  4.748   -14.799 1.00 23.47 ? 58   THR G C   1 
ATOM   7120  O  O   . THR G  1 58  ? 62.005  3.838   -15.070 1.00 23.06 ? 58   THR G O   1 
ATOM   7121  C  CB  . THR G  1 58  ? 61.985  7.091   -15.144 1.00 24.72 ? 58   THR G CB  1 
ATOM   7122  O  OG1 . THR G  1 58  ? 61.415  8.234   -14.497 1.00 34.85 ? 58   THR G OG1 1 
ATOM   7123  C  CG2 . THR G  1 58  ? 61.027  6.592   -16.188 1.00 25.88 ? 58   THR G CG2 1 
ATOM   7124  N  N   . SER G  1 59  ? 64.093  4.698   -15.106 1.00 20.57 ? 59   SER G N   1 
ATOM   7125  C  CA  . SER G  1 59  ? 64.675  3.587   -15.864 1.00 19.48 ? 59   SER G CA  1 
ATOM   7126  C  C   . SER G  1 59  ? 64.666  2.270   -15.096 1.00 20.04 ? 59   SER G C   1 
ATOM   7127  O  O   . SER G  1 59  ? 64.876  1.206   -15.686 1.00 19.05 ? 59   SER G O   1 
ATOM   7128  C  CB  . SER G  1 59  ? 66.121  3.894   -16.263 1.00 20.56 ? 59   SER G CB  1 
ATOM   7129  O  OG  . SER G  1 59  ? 66.318  5.279   -16.447 1.00 23.88 ? 59   SER G OG  1 
ATOM   7130  N  N   . ALA G  1 60  ? 64.438  2.351   -13.783 1.00 22.32 ? 60   ALA G N   1 
ATOM   7131  C  CA  . ALA G  1 60  ? 64.450  1.183   -12.895 1.00 18.55 ? 60   ALA G CA  1 
ATOM   7132  C  C   . ALA G  1 60  ? 63.327  0.194   -13.211 1.00 21.46 ? 60   ALA G C   1 
ATOM   7133  O  O   . ALA G  1 60  ? 63.362  -0.960  -12.774 1.00 21.20 ? 60   ALA G O   1 
ATOM   7134  C  CB  . ALA G  1 60  ? 64.379  1.623   -11.448 1.00 19.19 ? 60   ALA G CB  1 
ATOM   7135  N  N   . GLY G  1 61  ? 62.335  0.644   -13.979 1.00 21.19 ? 61   GLY G N   1 
ATOM   7136  C  CA  . GLY G  1 61  ? 61.236  -0.220  -14.354 1.00 19.66 ? 61   GLY G CA  1 
ATOM   7137  C  C   . GLY G  1 61  ? 60.282  -0.401  -13.195 1.00 20.03 ? 61   GLY G C   1 
ATOM   7138  O  O   . GLY G  1 61  ? 60.273  0.417   -12.276 1.00 18.42 ? 61   GLY G O   1 
ATOM   7139  N  N   . PRO G  1 62  ? 59.475  -1.474  -13.232 1.00 21.32 ? 62   PRO G N   1 
ATOM   7140  C  CA  . PRO G  1 62  ? 58.400  -1.675  -12.259 1.00 21.99 ? 62   PRO G CA  1 
ATOM   7141  C  C   . PRO G  1 62  ? 58.935  -2.415  -11.043 1.00 19.84 ? 62   PRO G C   1 
ATOM   7142  O  O   . PRO G  1 62  ? 60.079  -2.845  -11.086 1.00 20.28 ? 62   PRO G O   1 
ATOM   7143  C  CB  . PRO G  1 62  ? 57.421  -2.562  -13.028 1.00 22.01 ? 62   PRO G CB  1 
ATOM   7144  C  CG  . PRO G  1 62  ? 58.284  -3.392  -13.909 1.00 21.12 ? 62   PRO G CG  1 
ATOM   7145  C  CD  . PRO G  1 62  ? 59.541  -2.579  -14.208 1.00 22.11 ? 62   PRO G CD  1 
ATOM   7146  N  N   . HIS G  1 63  ? 58.146  -2.553  -9.981  1.00 18.07 ? 63   HIS G N   1 
ATOM   7147  C  CA  . HIS G  1 63  ? 58.585  -3.378  -8.862  1.00 20.16 ? 63   HIS G CA  1 
ATOM   7148  C  C   . HIS G  1 63  ? 59.036  -4.738  -9.399  1.00 20.20 ? 63   HIS G C   1 
ATOM   7149  O  O   . HIS G  1 63  ? 58.489  -5.249  -10.379 1.00 20.53 ? 63   HIS G O   1 
ATOM   7150  C  CB  . HIS G  1 63  ? 57.488  -3.552  -7.807  1.00 19.67 ? 63   HIS G CB  1 
ATOM   7151  C  CG  . HIS G  1 63  ? 56.946  -2.262  -7.269  1.00 18.20 ? 63   HIS G CG  1 
ATOM   7152  N  ND1 . HIS G  1 63  ? 55.783  -2.193  -6.540  1.00 16.39 ? 63   HIS G ND1 1 
ATOM   7153  C  CD2 . HIS G  1 63  ? 57.403  -0.992  -7.366  1.00 18.19 ? 63   HIS G CD2 1 
ATOM   7154  C  CE1 . HIS G  1 63  ? 55.547  -0.939  -6.204  1.00 18.58 ? 63   HIS G CE1 1 
ATOM   7155  N  NE2 . HIS G  1 63  ? 56.518  -0.189  -6.691  1.00 16.34 ? 63   HIS G NE2 1 
ATOM   7156  N  N   . PHE G  1 64  ? 60.057  -5.303  -8.773  1.00 20.24 ? 64   PHE G N   1 
ATOM   7157  C  CA  . PHE G  1 64  ? 60.609  -6.577  -9.203  1.00 17.74 ? 64   PHE G CA  1 
ATOM   7158  C  C   . PHE G  1 64  ? 59.575  -7.680  -8.976  1.00 17.73 ? 64   PHE G C   1 
ATOM   7159  O  O   . PHE G  1 64  ? 59.117  -7.874  -7.860  1.00 18.60 ? 64   PHE G O   1 
ATOM   7160  C  CB  . PHE G  1 64  ? 61.906  -6.851  -8.453  1.00 17.02 ? 64   PHE G CB  1 
ATOM   7161  C  CG  . PHE G  1 64  ? 62.570  -8.128  -8.849  1.00 18.19 ? 64   PHE G CG  1 
ATOM   7162  C  CD1 . PHE G  1 64  ? 62.578  -8.534  -10.170 1.00 17.17 ? 64   PHE G CD1 1 
ATOM   7163  C  CD2 . PHE G  1 64  ? 63.190  -8.924  -7.895  1.00 18.38 ? 64   PHE G CD2 1 
ATOM   7164  C  CE1 . PHE G  1 64  ? 63.193  -9.720  -10.532 1.00 20.95 ? 64   PHE G CE1 1 
ATOM   7165  C  CE2 . PHE G  1 64  ? 63.810  -10.111 -8.251  1.00 18.40 ? 64   PHE G CE2 1 
ATOM   7166  C  CZ  . PHE G  1 64  ? 63.818  -10.505 -9.566  1.00 19.46 ? 64   PHE G CZ  1 
ATOM   7167  N  N   . ASN G  1 65  ? 59.204  -8.383  -10.047 1.00 21.45 ? 65   ASN G N   1 
ATOM   7168  C  CA  . ASN G  1 65  ? 58.039  -9.273  -10.039 1.00 22.32 ? 65   ASN G CA  1 
ATOM   7169  C  C   . ASN G  1 65  ? 58.238  -10.548 -10.849 1.00 21.24 ? 65   ASN G C   1 
ATOM   7170  O  O   . ASN G  1 65  ? 57.565  -10.752 -11.856 1.00 22.28 ? 65   ASN G O   1 
ATOM   7171  C  CB  . ASN G  1 65  ? 56.830  -8.527  -10.609 1.00 22.36 ? 65   ASN G CB  1 
ATOM   7172  C  CG  . ASN G  1 65  ? 55.514  -9.189  -10.260 1.00 21.52 ? 65   ASN G CG  1 
ATOM   7173  O  OD1 . ASN G  1 65  ? 55.406  -9.902  -9.259  1.00 20.28 ? 65   ASN G OD1 1 
ATOM   7174  N  ND2 . ASN G  1 65  ? 54.496  -8.932  -11.070 1.00 20.23 ? 65   ASN G ND2 1 
ATOM   7175  N  N   . PRO G  1 66  ? 59.158  -11.419 -10.406 1.00 21.50 ? 66   PRO G N   1 
ATOM   7176  C  CA  . PRO G  1 66  ? 59.542  -12.626 -11.150 1.00 22.81 ? 66   PRO G CA  1 
ATOM   7177  C  C   . PRO G  1 66  ? 58.423  -13.662 -11.237 1.00 22.84 ? 66   PRO G C   1 
ATOM   7178  O  O   . PRO G  1 66  ? 58.433  -14.499 -12.131 1.00 27.33 ? 66   PRO G O   1 
ATOM   7179  C  CB  . PRO G  1 66  ? 60.710  -13.190 -10.329 1.00 21.95 ? 66   PRO G CB  1 
ATOM   7180  C  CG  . PRO G  1 66  ? 61.107  -12.125 -9.403  1.00 19.21 ? 66   PRO G CG  1 
ATOM   7181  C  CD  . PRO G  1 66  ? 59.908  -11.299 -9.149  1.00 20.46 ? 66   PRO G CD  1 
ATOM   7182  N  N   . LEU G  1 67  ? 57.471  -13.591 -10.311 1.00 25.45 ? 67   LEU G N   1 
ATOM   7183  C  CA  . LEU G  1 67  ? 56.381  -14.561 -10.207 1.00 24.24 ? 67   LEU G CA  1 
ATOM   7184  C  C   . LEU G  1 67  ? 55.048  -14.061 -10.803 1.00 26.00 ? 67   LEU G C   1 
ATOM   7185  O  O   . LEU G  1 67  ? 54.017  -14.740 -10.727 1.00 26.47 ? 67   LEU G O   1 
ATOM   7186  C  CB  . LEU G  1 67  ? 56.202  -14.952 -8.734  1.00 23.09 ? 67   LEU G CB  1 
ATOM   7187  C  CG  . LEU G  1 67  ? 57.350  -15.806 -8.198  1.00 22.22 ? 67   LEU G CG  1 
ATOM   7188  C  CD1 . LEU G  1 67  ? 57.297  -15.975 -6.702  1.00 25.45 ? 67   LEU G CD1 1 
ATOM   7189  C  CD2 . LEU G  1 67  ? 57.297  -17.152 -8.882  1.00 29.29 ? 67   LEU G CD2 1 
ATOM   7190  N  N   . SER G  1 68  ? 55.077  -12.875 -11.402 1.00 23.71 ? 68   SER G N   1 
ATOM   7191  C  CA  . SER G  1 68  ? 53.879  -12.273 -11.976 1.00 23.57 ? 68   SER G CA  1 
ATOM   7192  C  C   . SER G  1 68  ? 52.669  -12.308 -11.026 1.00 25.64 ? 68   SER G C   1 
ATOM   7193  O  O   . SER G  1 68  ? 51.591  -12.804 -11.373 1.00 27.66 ? 68   SER G O   1 
ATOM   7194  C  CB  . SER G  1 68  ? 53.552  -12.931 -13.311 1.00 23.26 ? 68   SER G CB  1 
ATOM   7195  O  OG  . SER G  1 68  ? 54.550  -12.618 -14.268 1.00 28.19 ? 68   SER G OG  1 
ATOM   7196  N  N   . ARG G  1 69  ? 52.866  -11.763 -9.830  1.00 24.32 ? 69   ARG G N   1 
ATOM   7197  C  CA  . ARG G  1 69  ? 51.805  -11.626 -8.842  1.00 24.24 ? 69   ARG G CA  1 
ATOM   7198  C  C   . ARG G  1 69  ? 51.355  -10.170 -8.730  1.00 26.78 ? 69   ARG G C   1 
ATOM   7199  O  O   . ARG G  1 69  ? 51.906  -9.288  -9.388  1.00 24.58 ? 69   ARG G O   1 
ATOM   7200  C  CB  . ARG G  1 69  ? 52.263  -12.149 -7.483  1.00 24.06 ? 69   ARG G CB  1 
ATOM   7201  C  CG  . ARG G  1 69  ? 52.774  -13.559 -7.562  1.00 26.06 ? 69   ARG G CG  1 
ATOM   7202  C  CD  . ARG G  1 69  ? 53.277  -14.020 -6.235  1.00 28.58 ? 69   ARG G CD  1 
ATOM   7203  N  NE  . ARG G  1 69  ? 52.198  -14.568 -5.433  1.00 34.54 ? 69   ARG G NE  1 
ATOM   7204  C  CZ  . ARG G  1 69  ? 51.992  -15.866 -5.255  1.00 37.22 ? 69   ARG G CZ  1 
ATOM   7205  N  NH1 . ARG G  1 69  ? 52.805  -16.756 -5.822  1.00 38.15 ? 69   ARG G NH1 1 
ATOM   7206  N  NH2 . ARG G  1 69  ? 50.973  -16.270 -4.508  1.00 38.25 ? 69   ARG G NH2 1 
ATOM   7207  N  N   . LYS G  1 70  ? 50.334  -9.936  -7.914  1.00 23.93 ? 70   LYS G N   1 
ATOM   7208  C  CA  . LYS G  1 70  ? 49.794  -8.606  -7.735  1.00 25.69 ? 70   LYS G CA  1 
ATOM   7209  C  C   . LYS G  1 70  ? 50.480  -7.929  -6.560  1.00 23.78 ? 70   LYS G C   1 
ATOM   7210  O  O   . LYS G  1 70  ? 50.905  -8.586  -5.613  1.00 22.65 ? 70   LYS G O   1 
ATOM   7211  C  CB  . LYS G  1 70  ? 48.274  -8.664  -7.493  1.00 27.99 ? 70   LYS G CB  1 
ATOM   7212  C  CG  . LYS G  1 70  ? 47.415  -8.813  -8.744  1.00 24.87 ? 70   LYS G CG  1 
ATOM   7213  C  CD  . LYS G  1 70  ? 45.960  -8.612  -8.405  1.00 29.92 ? 70   LYS G CD  1 
ATOM   7214  C  CE  . LYS G  1 70  ? 45.114  -8.376  -9.658  1.00 40.59 ? 70   LYS G CE  1 
ATOM   7215  N  NZ  . LYS G  1 70  ? 45.007  -9.591  -10.518 1.00 44.91 ? 70   LYS G NZ  1 
ATOM   7216  N  N   . HIS G  1 71  ? 50.567  -6.608  -6.615  1.00 21.84 ? 71   HIS G N   1 
ATOM   7217  C  CA  . HIS G  1 71  ? 51.194  -5.845  -5.549  1.00 21.10 ? 71   HIS G CA  1 
ATOM   7218  C  C   . HIS G  1 71  ? 50.595  -6.120  -4.175  1.00 22.01 ? 71   HIS G C   1 
ATOM   7219  O  O   . HIS G  1 71  ? 49.384  -6.246  -4.037  1.00 23.05 ? 71   HIS G O   1 
ATOM   7220  C  CB  . HIS G  1 71  ? 51.093  -4.352  -5.850  1.00 22.86 ? 71   HIS G CB  1 
ATOM   7221  C  CG  . HIS G  1 71  ? 51.717  -3.484  -4.803  1.00 22.37 ? 71   HIS G CG  1 
ATOM   7222  N  ND1 . HIS G  1 71  ? 53.079  -3.288  -4.714  1.00 20.05 ? 71   HIS G ND1 1 
ATOM   7223  C  CD2 . HIS G  1 71  ? 51.164  -2.759  -3.803  1.00 20.24 ? 71   HIS G CD2 1 
ATOM   7224  C  CE1 . HIS G  1 71  ? 53.341  -2.479  -3.703  1.00 20.14 ? 71   HIS G CE1 1 
ATOM   7225  N  NE2 . HIS G  1 71  ? 52.196  -2.142  -3.137  1.00 21.36 ? 71   HIS G NE2 1 
ATOM   7226  N  N   . GLY G  1 72  ? 51.453  -6.193  -3.160  1.00 22.24 ? 72   GLY G N   1 
ATOM   7227  C  CA  . GLY G  1 72  ? 51.020  -6.348  -1.784  1.00 20.13 ? 72   GLY G CA  1 
ATOM   7228  C  C   . GLY G  1 72  ? 52.044  -5.798  -0.807  1.00 20.07 ? 72   GLY G C   1 
ATOM   7229  O  O   . GLY G  1 72  ? 52.999  -5.165  -1.206  1.00 21.22 ? 72   GLY G O   1 
ATOM   7230  N  N   . GLY G  1 73  ? 51.835  -6.021  0.484   1.00 21.50 ? 73   GLY G N   1 
ATOM   7231  C  CA  . GLY G  1 73  ? 52.829  -5.674  1.481   1.00 21.67 ? 73   GLY G CA  1 
ATOM   7232  C  C   . GLY G  1 73  ? 53.729  -6.874  1.700   1.00 22.38 ? 73   GLY G C   1 
ATOM   7233  O  O   . GLY G  1 73  ? 53.461  -7.947  1.162   1.00 20.44 ? 73   GLY G O   1 
ATOM   7234  N  N   . PRO G  1 74  ? 54.798  -6.705  2.495   1.00 22.15 ? 74   PRO G N   1 
ATOM   7235  C  CA  . PRO G  1 74  ? 55.792  -7.770  2.675   1.00 20.28 ? 74   PRO G CA  1 
ATOM   7236  C  C   . PRO G  1 74  ? 55.233  -8.965  3.438   1.00 23.82 ? 74   PRO G C   1 
ATOM   7237  O  O   . PRO G  1 74  ? 55.733  -10.080 3.244   1.00 22.42 ? 74   PRO G O   1 
ATOM   7238  C  CB  . PRO G  1 74  ? 56.905  -7.090  3.485   1.00 20.27 ? 74   PRO G CB  1 
ATOM   7239  C  CG  . PRO G  1 74  ? 56.633  -5.620  3.387   1.00 18.90 ? 74   PRO G CG  1 
ATOM   7240  C  CD  . PRO G  1 74  ? 55.168  -5.470  3.210   1.00 19.18 ? 74   PRO G CD  1 
ATOM   7241  N  N   . LYS G  1 75  ? 54.222  -8.737  4.283   1.00 25.48 ? 75   LYS G N   1 
ATOM   7242  C  CA  . LYS G  1 75  ? 53.629  -9.812  5.072   1.00 25.31 ? 75   LYS G CA  1 
ATOM   7243  C  C   . LYS G  1 75  ? 52.565  -10.558 4.271   1.00 25.98 ? 75   LYS G C   1 
ATOM   7244  O  O   . LYS G  1 75  ? 52.080  -11.604 4.702   1.00 28.24 ? 75   LYS G O   1 
ATOM   7245  C  CB  . LYS G  1 75  ? 53.010  -9.287  6.375   1.00 24.51 ? 75   LYS G CB  1 
ATOM   7246  C  CG  . LYS G  1 75  ? 53.858  -8.335  7.196   1.00 26.60 ? 75   LYS G CG  1 
ATOM   7247  C  CD  . LYS G  1 75  ? 55.281  -8.854  7.418   1.00 34.63 ? 75   LYS G CD  1 
ATOM   7248  C  CE  . LYS G  1 75  ? 55.355  -9.972  8.456   1.00 38.35 ? 75   LYS G CE  1 
ATOM   7249  N  NZ  . LYS G  1 75  ? 56.720  -10.588 8.491   1.00 34.75 ? 75   LYS G NZ  1 
ATOM   7250  N  N   . ASP G  1 76  ? 52.192  -10.015 3.115   1.00 24.45 ? 76   ASP G N   1 
ATOM   7251  C  CA  . ASP G  1 76  ? 51.196  -10.660 2.261   1.00 24.74 ? 76   ASP G CA  1 
ATOM   7252  C  C   . ASP G  1 76  ? 51.834  -11.727 1.392   1.00 24.52 ? 76   ASP G C   1 
ATOM   7253  O  O   . ASP G  1 76  ? 52.968  -11.582 0.948   1.00 23.41 ? 76   ASP G O   1 
ATOM   7254  C  CB  . ASP G  1 76  ? 50.492  -9.646  1.350   1.00 22.61 ? 76   ASP G CB  1 
ATOM   7255  C  CG  . ASP G  1 76  ? 49.785  -8.560  2.118   1.00 25.31 ? 76   ASP G CG  1 
ATOM   7256  O  OD1 . ASP G  1 76  ? 49.047  -8.868  3.086   1.00 30.53 ? 76   ASP G OD1 1 
ATOM   7257  O  OD2 . ASP G  1 76  ? 49.964  -7.386  1.744   1.00 24.77 ? 76   ASP G OD2 1 
ATOM   7258  N  N   . GLU G  1 77  ? 51.091  -12.794 1.128   1.00 27.49 ? 77   GLU G N   1 
ATOM   7259  C  CA  . GLU G  1 77  ? 51.579  -13.830 0.216   1.00 31.93 ? 77   GLU G CA  1 
ATOM   7260  C  C   . GLU G  1 77  ? 51.355  -13.500 -1.267  1.00 28.47 ? 77   GLU G C   1 
ATOM   7261  O  O   . GLU G  1 77  ? 52.161  -13.888 -2.113  1.00 29.99 ? 77   GLU G O   1 
ATOM   7262  C  CB  . GLU G  1 77  ? 51.036  -15.203 0.609   1.00 34.50 ? 77   GLU G CB  1 
ATOM   7263  C  CG  . GLU G  1 77  ? 51.579  -15.657 1.967   1.00 33.75 ? 77   GLU G CG  1 
ATOM   7264  C  CD  . GLU G  1 77  ? 51.366  -17.126 2.215   1.00 31.92 ? 77   GLU G CD  1 
ATOM   7265  O  OE1 . GLU G  1 77  ? 50.198  -17.557 2.173   1.00 33.83 ? 77   GLU G OE1 1 
ATOM   7266  O  OE2 . GLU G  1 77  ? 52.361  -17.846 2.446   1.00 32.16 ? 77   GLU G OE2 1 
ATOM   7267  N  N   . GLU G  1 78  ? 50.283  -12.769 -1.579  1.00 26.49 ? 78   GLU G N   1 
ATOM   7268  C  CA  . GLU G  1 78  ? 50.212  -12.066 -2.861  1.00 27.54 ? 78   GLU G CA  1 
ATOM   7269  C  C   . GLU G  1 78  ? 50.974  -10.761 -2.733  1.00 24.81 ? 78   GLU G C   1 
ATOM   7270  O  O   . GLU G  1 78  ? 50.483  -9.791  -2.151  1.00 21.96 ? 78   GLU G O   1 
ATOM   7271  C  CB  . GLU G  1 78  ? 48.779  -11.754 -3.288  1.00 29.58 ? 78   GLU G CB  1 
ATOM   7272  C  CG  . GLU G  1 78  ? 48.164  -12.794 -4.200  1.00 35.04 ? 78   GLU G CG  1 
ATOM   7273  C  CD  . GLU G  1 78  ? 48.851  -12.876 -5.542  1.00 32.90 ? 78   GLU G CD  1 
ATOM   7274  O  OE1 . GLU G  1 78  ? 48.950  -11.832 -6.217  1.00 33.82 ? 78   GLU G OE1 1 
ATOM   7275  O  OE2 . GLU G  1 78  ? 49.275  -13.992 -5.928  1.00 39.81 ? 78   GLU G OE2 1 
ATOM   7276  N  N   . ARG G  1 79  ? 52.177  -10.754 -3.288  1.00 24.23 ? 79   ARG G N   1 
ATOM   7277  C  CA  . ARG G  1 79  ? 53.021  -9.579  -3.301  1.00 23.32 ? 79   ARG G CA  1 
ATOM   7278  C  C   . ARG G  1 79  ? 54.000  -9.773  -4.431  1.00 21.66 ? 79   ARG G C   1 
ATOM   7279  O  O   . ARG G  1 79  ? 54.157  -10.889 -4.940  1.00 22.46 ? 79   ARG G O   1 
ATOM   7280  C  CB  . ARG G  1 79  ? 53.787  -9.458  -1.984  1.00 20.17 ? 79   ARG G CB  1 
ATOM   7281  C  CG  . ARG G  1 79  ? 54.555  -10.716 -1.627  1.00 20.07 ? 79   ARG G CG  1 
ATOM   7282  C  CD  . ARG G  1 79  ? 55.525  -10.473 -0.491  1.00 21.71 ? 79   ARG G CD  1 
ATOM   7283  N  NE  . ARG G  1 79  ? 56.804  -9.909  -0.926  1.00 19.80 ? 79   ARG G NE  1 
ATOM   7284  C  CZ  . ARG G  1 79  ? 57.821  -9.664  -0.103  1.00 19.49 ? 79   ARG G CZ  1 
ATOM   7285  N  NH1 . ARG G  1 79  ? 57.699  -9.926  1.190   1.00 18.22 ? 79   ARG G NH1 1 
ATOM   7286  N  NH2 . ARG G  1 79  ? 58.963  -9.170  -0.567  1.00 19.40 ? 79   ARG G NH2 1 
ATOM   7287  N  N   . HIS G  1 80  ? 54.638  -8.680  -4.830  1.00 20.06 ? 80   HIS G N   1 
ATOM   7288  C  CA  . HIS G  1 80  ? 55.811  -8.742  -5.668  1.00 18.03 ? 80   HIS G CA  1 
ATOM   7289  C  C   . HIS G  1 80  ? 57.004  -9.099  -4.777  1.00 20.72 ? 80   HIS G C   1 
ATOM   7290  O  O   . HIS G  1 80  ? 57.018  -8.777  -3.573  1.00 19.02 ? 80   HIS G O   1 
ATOM   7291  C  CB  . HIS G  1 80  ? 56.064  -7.387  -6.319  1.00 20.56 ? 80   HIS G CB  1 
ATOM   7292  C  CG  . HIS G  1 80  ? 54.916  -6.869  -7.129  1.00 21.04 ? 80   HIS G CG  1 
ATOM   7293  N  ND1 . HIS G  1 80  ? 54.632  -5.524  -7.233  1.00 20.25 ? 80   HIS G ND1 1 
ATOM   7294  C  CD2 . HIS G  1 80  ? 54.004  -7.505  -7.898  1.00 21.34 ? 80   HIS G CD2 1 
ATOM   7295  C  CE1 . HIS G  1 80  ? 53.584  -5.355  -8.021  1.00 21.17 ? 80   HIS G CE1 1 
ATOM   7296  N  NE2 . HIS G  1 80  ? 53.182  -6.541  -8.438  1.00 21.71 ? 80   HIS G NE2 1 
ATOM   7297  N  N   . VAL G  1 81  ? 58.007  -9.753  -5.361  1.00 19.06 ? 81   VAL G N   1 
ATOM   7298  C  CA  . VAL G  1 81  ? 59.245  -10.028 -4.648  1.00 17.78 ? 81   VAL G CA  1 
ATOM   7299  C  C   . VAL G  1 81  ? 59.830  -8.727  -4.094  1.00 18.78 ? 81   VAL G C   1 
ATOM   7300  O  O   . VAL G  1 81  ? 60.319  -8.693  -2.961  1.00 18.92 ? 81   VAL G O   1 
ATOM   7301  C  CB  . VAL G  1 81  ? 60.272  -10.777 -5.545  1.00 16.36 ? 81   VAL G CB  1 
ATOM   7302  C  CG1 . VAL G  1 81  ? 61.696  -10.591 -5.046  1.00 16.79 ? 81   VAL G CG1 1 
ATOM   7303  C  CG2 . VAL G  1 81  ? 59.937  -12.248 -5.622  1.00 17.82 ? 81   VAL G CG2 1 
ATOM   7304  N  N   . GLY G  1 82  ? 59.757  -7.659  -4.890  1.00 19.57 ? 82   GLY G N   1 
ATOM   7305  C  CA  . GLY G  1 82  ? 60.301  -6.361  -4.518  1.00 17.06 ? 82   GLY G CA  1 
ATOM   7306  C  C   . GLY G  1 82  ? 59.543  -5.568  -3.465  1.00 19.48 ? 82   GLY G C   1 
ATOM   7307  O  O   . GLY G  1 82  ? 60.029  -4.540  -2.996  1.00 21.05 ? 82   GLY G O   1 
ATOM   7308  N  N   . ASP G  1 83  ? 58.365  -6.039  -3.072  1.00 19.46 ? 83   ASP G N   1 
ATOM   7309  C  CA  . ASP G  1 83  ? 57.515  -5.317  -2.122  1.00 17.64 ? 83   ASP G CA  1 
ATOM   7310  C  C   . ASP G  1 83  ? 58.006  -5.323  -0.676  1.00 17.49 ? 83   ASP G C   1 
ATOM   7311  O  O   . ASP G  1 83  ? 57.751  -6.278  0.059   1.00 17.93 ? 83   ASP G O   1 
ATOM   7312  C  CB  . ASP G  1 83  ? 56.105  -5.901  -2.149  1.00 18.88 ? 83   ASP G CB  1 
ATOM   7313  C  CG  . ASP G  1 83  ? 55.384  -5.576  -3.409  1.00 19.41 ? 83   ASP G CG  1 
ATOM   7314  O  OD1 . ASP G  1 83  ? 55.851  -4.665  -4.107  1.00 18.87 ? 83   ASP G OD1 1 
ATOM   7315  O  OD2 . ASP G  1 83  ? 54.363  -6.223  -3.711  1.00 22.96 ? 83   ASP G OD2 1 
ATOM   7316  N  N   . LEU G  1 84  ? 58.669  -4.246  -0.256  1.00 16.80 ? 84   LEU G N   1 
ATOM   7317  C  CA  . LEU G  1 84  ? 59.127  -4.135  1.135   1.00 18.78 ? 84   LEU G CA  1 
ATOM   7318  C  C   . LEU G  1 84  ? 58.286  -3.196  2.018   1.00 18.57 ? 84   LEU G C   1 
ATOM   7319  O  O   . LEU G  1 84  ? 58.661  -2.902  3.149   1.00 21.75 ? 84   LEU G O   1 
ATOM   7320  C  CB  . LEU G  1 84  ? 60.635  -3.817  1.229   1.00 18.39 ? 84   LEU G CB  1 
ATOM   7321  C  CG  . LEU G  1 84  ? 61.573  -4.955  0.783   1.00 16.85 ? 84   LEU G CG  1 
ATOM   7322  C  CD1 . LEU G  1 84  ? 63.026  -4.513  0.779   1.00 15.31 ? 84   LEU G CD1 1 
ATOM   7323  C  CD2 . LEU G  1 84  ? 61.397  -6.226  1.623   1.00 14.15 ? 84   LEU G CD2 1 
ATOM   7324  N  N   . GLY G  1 85  ? 57.141  -2.750  1.511   1.00 20.04 ? 85   GLY G N   1 
ATOM   7325  C  CA  . GLY G  1 85  ? 56.197  -1.980  2.304   1.00 19.57 ? 85   GLY G CA  1 
ATOM   7326  C  C   . GLY G  1 85  ? 56.544  -0.515  2.484   1.00 18.81 ? 85   GLY G C   1 
ATOM   7327  O  O   . GLY G  1 85  ? 57.066  0.132   1.598   1.00 17.84 ? 85   GLY G O   1 
ATOM   7328  N  N   . ASN G  1 86  ? 56.246  0.006   3.662   1.00 21.61 ? 86   ASN G N   1 
ATOM   7329  C  CA  . ASN G  1 86  ? 56.546  1.391   3.989   1.00 23.00 ? 86   ASN G CA  1 
ATOM   7330  C  C   . ASN G  1 86  ? 57.738  1.566   4.933   1.00 20.70 ? 86   ASN G C   1 
ATOM   7331  O  O   . ASN G  1 86  ? 58.025  0.718   5.779   1.00 19.09 ? 86   ASN G O   1 
ATOM   7332  C  CB  . ASN G  1 86  ? 55.314  2.054   4.603   1.00 23.34 ? 86   ASN G CB  1 
ATOM   7333  C  CG  . ASN G  1 86  ? 54.240  2.305   3.588   1.00 23.27 ? 86   ASN G CG  1 
ATOM   7334  O  OD1 . ASN G  1 86  ? 54.465  3.012   2.615   1.00 23.74 ? 86   ASN G OD1 1 
ATOM   7335  N  ND2 . ASN G  1 86  ? 53.058  1.733   3.805   1.00 24.45 ? 86   ASN G ND2 1 
ATOM   7336  N  N   . VAL G  1 87  ? 58.442  2.674   4.761   1.00 22.09 ? 87   VAL G N   1 
ATOM   7337  C  CA  . VAL G  1 87  ? 59.405  3.111   5.754   1.00 23.75 ? 87   VAL G CA  1 
ATOM   7338  C  C   . VAL G  1 87  ? 58.793  4.341   6.407   1.00 25.15 ? 87   VAL G C   1 
ATOM   7339  O  O   . VAL G  1 87  ? 57.947  5.012   5.802   1.00 23.16 ? 87   VAL G O   1 
ATOM   7340  C  CB  . VAL G  1 87  ? 60.771  3.448   5.127   1.00 23.81 ? 87   VAL G CB  1 
ATOM   7341  C  CG1 . VAL G  1 87  ? 61.565  2.169   4.834   1.00 18.79 ? 87   VAL G CG1 1 
ATOM   7342  C  CG2 . VAL G  1 87  ? 60.586  4.269   3.865   1.00 22.15 ? 87   VAL G CG2 1 
ATOM   7343  N  N   . THR G  1 88  ? 59.204  4.620   7.644   1.00 27.07 ? 88   THR G N   1 
ATOM   7344  C  CA  . THR G  1 88  ? 58.591  5.673   8.445   1.00 24.36 ? 88   THR G CA  1 
ATOM   7345  C  C   . THR G  1 88  ? 59.596  6.789   8.725   1.00 22.64 ? 88   THR G C   1 
ATOM   7346  O  O   . THR G  1 88  ? 60.640  6.546   9.315   1.00 24.31 ? 88   THR G O   1 
ATOM   7347  C  CB  . THR G  1 88  ? 58.050  5.095   9.780   1.00 23.13 ? 88   THR G CB  1 
ATOM   7348  O  OG1 . THR G  1 88  ? 57.176  3.988   9.513   1.00 22.82 ? 88   THR G OG1 1 
ATOM   7349  C  CG2 . THR G  1 88  ? 57.313  6.162   10.592  1.00 24.24 ? 88   THR G CG2 1 
ATOM   7350  N  N   . ALA G  1 89  ? 59.283  8.005   8.284   1.00 26.63 ? 89   ALA G N   1 
ATOM   7351  C  CA  . ALA G  1 89  ? 60.104  9.183   8.582   1.00 26.86 ? 89   ALA G CA  1 
ATOM   7352  C  C   . ALA G  1 89  ? 59.505  9.992   9.736   1.00 28.78 ? 89   ALA G C   1 
ATOM   7353  O  O   . ALA G  1 89  ? 58.297  10.230  9.771   1.00 29.79 ? 89   ALA G O   1 
ATOM   7354  C  CB  . ALA G  1 89  ? 60.241  10.056  7.352   1.00 24.34 ? 89   ALA G CB  1 
ATOM   7355  N  N   . GLY G  1 90  ? 60.348  10.412  10.676  1.00 31.15 ? 90   GLY G N   1 
ATOM   7356  C  CA  . GLY G  1 90  ? 59.911  11.264  11.779  1.00 32.15 ? 90   GLY G CA  1 
ATOM   7357  C  C   . GLY G  1 90  ? 59.865  12.742  11.414  1.00 31.91 ? 90   GLY G C   1 
ATOM   7358  O  O   . GLY G  1 90  ? 59.974  13.106  10.233  1.00 30.42 ? 90   GLY G O   1 
ATOM   7359  N  N   . LYS G  1 91  ? 59.683  13.600  12.418  1.00 34.52 ? 91   LYS G N   1 
ATOM   7360  C  CA  . LYS G  1 91  ? 59.741  15.043  12.192  1.00 35.65 ? 91   LYS G CA  1 
ATOM   7361  C  C   . LYS G  1 91  ? 61.145  15.343  11.713  1.00 33.28 ? 91   LYS G C   1 
ATOM   7362  O  O   . LYS G  1 91  ? 61.375  16.272  10.946  1.00 33.06 ? 91   LYS G O   1 
ATOM   7363  C  CB  . LYS G  1 91  ? 59.491  15.820  13.482  1.00 41.00 ? 91   LYS G CB  1 
ATOM   7364  C  CG  . LYS G  1 91  ? 58.201  15.497  14.206  1.00 44.32 ? 91   LYS G CG  1 
ATOM   7365  C  CD  . LYS G  1 91  ? 57.721  16.715  14.996  1.00 44.00 ? 91   LYS G CD  1 
ATOM   7366  C  CE  . LYS G  1 91  ? 58.800  17.236  15.937  1.00 44.71 ? 91   LYS G CE  1 
ATOM   7367  N  NZ  . LYS G  1 91  ? 58.999  16.322  17.095  1.00 44.60 ? 91   LYS G NZ  1 
ATOM   7368  N  N   . ASP G  1 92  ? 62.074  14.531  12.208  1.00 33.70 ? 92   ASP G N   1 
ATOM   7369  C  CA  A ASP G  1 92  ? 63.480  14.581  11.823  0.49 32.47 ? 92   ASP G CA  1 
ATOM   7370  C  CA  B ASP G  1 92  ? 63.480  14.597  11.822  0.51 31.79 ? 92   ASP G CA  1 
ATOM   7371  C  C   . ASP G  1 92  ? 63.644  14.687  10.310  1.00 30.45 ? 92   ASP G C   1 
ATOM   7372  O  O   . ASP G  1 92  ? 64.501  15.409  9.815   1.00 31.32 ? 92   ASP G O   1 
ATOM   7373  C  CB  A ASP G  1 92  ? 64.160  13.300  12.309  0.49 30.42 ? 92   ASP G CB  1 
ATOM   7374  C  CB  B ASP G  1 92  ? 64.246  13.379  12.378  0.51 30.41 ? 92   ASP G CB  1 
ATOM   7375  C  CG  A ASP G  1 92  ? 65.511  13.552  12.928  0.49 30.55 ? 92   ASP G CG  1 
ATOM   7376  C  CG  B ASP G  1 92  ? 63.516  12.050  12.138  0.51 30.74 ? 92   ASP G CG  1 
ATOM   7377  O  OD1 A ASP G  1 92  ? 65.889  14.731  13.081  0.49 32.23 ? 92   ASP G OD1 1 
ATOM   7378  O  OD1 B ASP G  1 92  ? 62.739  11.954  11.170  0.51 31.04 ? 92   ASP G OD1 1 
ATOM   7379  O  OD2 A ASP G  1 92  ? 66.190  12.564  13.272  0.49 29.95 ? 92   ASP G OD2 1 
ATOM   7380  O  OD2 B ASP G  1 92  ? 63.722  11.089  12.912  0.51 30.08 ? 92   ASP G OD2 1 
ATOM   7381  N  N   . GLY G  1 93  ? 62.810  13.955  9.580   1.00 33.70 ? 93   GLY G N   1 
ATOM   7382  C  CA  . GLY G  1 93  ? 62.944  13.822  8.136   1.00 32.09 ? 93   GLY G CA  1 
ATOM   7383  C  C   . GLY G  1 93  ? 63.687  12.522  7.838   1.00 28.21 ? 93   GLY G C   1 
ATOM   7384  O  O   . GLY G  1 93  ? 63.820  12.107  6.685   1.00 27.95 ? 93   GLY G O   1 
ATOM   7385  N  N   . VAL G  1 94  ? 64.159  11.879  8.903   1.00 27.94 ? 94   VAL G N   1 
ATOM   7386  C  CA  . VAL G  1 94  ? 64.972  10.677  8.807   1.00 28.48 ? 94   VAL G CA  1 
ATOM   7387  C  C   . VAL G  1 94  ? 64.165  9.409   9.069   1.00 29.23 ? 94   VAL G C   1 
ATOM   7388  O  O   . VAL G  1 94  ? 63.469  9.298   10.082  1.00 30.75 ? 94   VAL G O   1 
ATOM   7389  C  CB  . VAL G  1 94  ? 66.124  10.712  9.813   1.00 27.19 ? 94   VAL G CB  1 
ATOM   7390  C  CG1 . VAL G  1 94  ? 66.985  9.464   9.680   1.00 25.89 ? 94   VAL G CG1 1 
ATOM   7391  C  CG2 . VAL G  1 94  ? 66.946  11.965  9.612   1.00 28.80 ? 94   VAL G CG2 1 
ATOM   7392  N  N   . ALA G  1 95  ? 64.270  8.453   8.151   1.00 25.83 ? 95   ALA G N   1 
ATOM   7393  C  CA  . ALA G  1 95  ? 63.636  7.158   8.318   1.00 25.42 ? 95   ALA G CA  1 
ATOM   7394  C  C   . ALA G  1 95  ? 64.657  6.082   8.658   1.00 25.58 ? 95   ALA G C   1 
ATOM   7395  O  O   . ALA G  1 95  ? 65.437  5.669   7.803   1.00 25.11 ? 95   ALA G O   1 
ATOM   7396  C  CB  . ALA G  1 95  ? 62.865  6.776   7.051   1.00 25.27 ? 95   ALA G CB  1 
ATOM   7397  N  N   . ASN G  1 96  ? 64.660  5.637   9.908   1.00 25.37 ? 96   ASN G N   1 
ATOM   7398  C  CA  . ASN G  1 96  ? 65.430  4.459   10.269  1.00 25.71 ? 96   ASN G CA  1 
ATOM   7399  C  C   . ASN G  1 96  ? 64.808  3.209   9.631   1.00 24.62 ? 96   ASN G C   1 
ATOM   7400  O  O   . ASN G  1 96  ? 63.594  3.049   9.595   1.00 23.36 ? 96   ASN G O   1 
ATOM   7401  C  CB  . ASN G  1 96  ? 65.523  4.334   11.790  1.00 25.80 ? 96   ASN G CB  1 
ATOM   7402  C  CG  . ASN G  1 96  ? 66.222  5.525   12.424  1.00 31.40 ? 96   ASN G CG  1 
ATOM   7403  O  OD1 . ASN G  1 96  ? 67.364  5.843   12.082  1.00 37.24 ? 96   ASN G OD1 1 
ATOM   7404  N  ND2 . ASN G  1 96  ? 65.537  6.200   13.340  1.00 33.14 ? 96   ASN G ND2 1 
ATOM   7405  N  N   . VAL G  1 97  ? 65.643  2.331   9.099   1.00 24.67 ? 97   VAL G N   1 
ATOM   7406  C  CA  . VAL G  1 97  ? 65.144  1.156   8.394   1.00 22.73 ? 97   VAL G CA  1 
ATOM   7407  C  C   . VAL G  1 97  ? 65.690  -0.112  9.039   1.00 21.42 ? 97   VAL G C   1 
ATOM   7408  O  O   . VAL G  1 97  ? 66.864  -0.197  9.373   1.00 24.81 ? 97   VAL G O   1 
ATOM   7409  C  CB  . VAL G  1 97  ? 65.515  1.211   6.886   1.00 23.10 ? 97   VAL G CB  1 
ATOM   7410  C  CG1 . VAL G  1 97  ? 65.021  -0.018  6.144   1.00 20.05 ? 97   VAL G CG1 1 
ATOM   7411  C  CG2 . VAL G  1 97  ? 64.967  2.486   6.251   1.00 20.78 ? 97   VAL G CG2 1 
ATOM   7412  N  N   . SER G  1 98  ? 64.812  -1.077  9.252   1.00 23.51 ? 98   SER G N   1 
ATOM   7413  C  CA  . SER G  1 98  ? 65.194  -2.402  9.728   1.00 24.54 ? 98   SER G CA  1 
ATOM   7414  C  C   . SER G  1 98  ? 64.055  -3.349  9.359   1.00 25.58 ? 98   SER G C   1 
ATOM   7415  O  O   . SER G  1 98  ? 62.957  -3.272  9.918   1.00 25.85 ? 98   SER G O   1 
ATOM   7416  C  CB  . SER G  1 98  ? 65.446  -2.417  11.237  1.00 22.92 ? 98   SER G CB  1 
ATOM   7417  O  OG  . SER G  1 98  ? 66.167  -3.581  11.609  1.00 25.88 ? 98   SER G OG  1 
ATOM   7418  N  N   . ILE G  1 99  ? 64.320  -4.215  8.387   1.00 23.28 ? 99   ILE G N   1 
ATOM   7419  C  CA  . ILE G  1 99  ? 63.321  -5.122  7.846   1.00 24.81 ? 99   ILE G CA  1 
ATOM   7420  C  C   . ILE G  1 99  ? 63.960  -6.505  7.758   1.00 24.06 ? 99   ILE G C   1 
ATOM   7421  O  O   . ILE G  1 99  ? 65.147  -6.618  7.489   1.00 22.75 ? 99   ILE G O   1 
ATOM   7422  C  CB  . ILE G  1 99  ? 62.860  -4.647  6.440   1.00 25.22 ? 99   ILE G CB  1 
ATOM   7423  C  CG1 . ILE G  1 99  ? 61.959  -3.414  6.557   1.00 21.01 ? 99   ILE G CG1 1 
ATOM   7424  C  CG2 . ILE G  1 99  ? 62.157  -5.759  5.672   1.00 22.11 ? 99   ILE G CG2 1 
ATOM   7425  C  CD1 . ILE G  1 99  ? 61.944  -2.564  5.308   1.00 20.76 ? 99   ILE G CD1 1 
ATOM   7426  N  N   . GLU G  1 100 ? 63.198  -7.555  8.034   1.00 24.93 ? 100  GLU G N   1 
ATOM   7427  C  CA  . GLU G  1 100 ? 63.677  -8.896  7.728   1.00 25.51 ? 100  GLU G CA  1 
ATOM   7428  C  C   . GLU G  1 100 ? 62.724  -9.510  6.714   1.00 27.05 ? 100  GLU G C   1 
ATOM   7429  O  O   . GLU G  1 100 ? 61.510  -9.571  6.951   1.00 28.45 ? 100  GLU G O   1 
ATOM   7430  C  CB  . GLU G  1 100 ? 63.806  -9.765  8.979   1.00 30.31 ? 100  GLU G CB  1 
ATOM   7431  C  CG  . GLU G  1 100 ? 64.499  -11.115 8.728   1.00 34.72 ? 100  GLU G CG  1 
ATOM   7432  C  CD  . GLU G  1 100 ? 65.202  -11.678 9.973   1.00 47.55 ? 100  GLU G CD  1 
ATOM   7433  O  OE1 . GLU G  1 100 ? 65.911  -10.909 10.671  1.00 47.12 ? 100  GLU G OE1 1 
ATOM   7434  O  OE2 . GLU G  1 100 ? 65.058  -12.898 10.240  1.00 47.69 ? 100  GLU G OE2 1 
ATOM   7435  N  N   . ASP G  1 101 ? 63.264  -9.921  5.566   1.00 23.53 ? 101  ASP G N   1 
ATOM   7436  C  CA  . ASP G  1 101 ? 62.439  -10.474 4.501   1.00 22.65 ? 101  ASP G CA  1 
ATOM   7437  C  C   . ASP G  1 101 ? 62.903  -11.839 3.993   1.00 22.61 ? 101  ASP G C   1 
ATOM   7438  O  O   . ASP G  1 101 ? 64.086  -12.041 3.726   1.00 20.69 ? 101  ASP G O   1 
ATOM   7439  C  CB  . ASP G  1 101 ? 62.350  -9.506  3.321   1.00 21.54 ? 101  ASP G CB  1 
ATOM   7440  C  CG  . ASP G  1 101 ? 61.186  -9.836  2.408   1.00 20.80 ? 101  ASP G CG  1 
ATOM   7441  O  OD1 . ASP G  1 101 ? 60.034  -9.768  2.888   1.00 23.89 ? 101  ASP G OD1 1 
ATOM   7442  O  OD2 . ASP G  1 101 ? 61.411  -10.194 1.238   1.00 19.48 ? 101  ASP G OD2 1 
ATOM   7443  N  N   . ARG G  1 102 ? 61.962  -12.762 3.821   1.00 23.55 ? 102  ARG G N   1 
ATOM   7444  C  CA  . ARG G  1 102 ? 62.296  -14.084 3.287   1.00 23.64 ? 102  ARG G CA  1 
ATOM   7445  C  C   . ARG G  1 102 ? 62.010  -14.261 1.787   1.00 21.00 ? 102  ARG G C   1 
ATOM   7446  O  O   . ARG G  1 102 ? 62.360  -15.296 1.216   1.00 21.24 ? 102  ARG G O   1 
ATOM   7447  C  CB  . ARG G  1 102 ? 61.589  -15.185 4.080   1.00 21.79 ? 102  ARG G CB  1 
ATOM   7448  C  CG  . ARG G  1 102 ? 61.993  -15.275 5.531   1.00 23.37 ? 102  ARG G CG  1 
ATOM   7449  C  CD  . ARG G  1 102 ? 61.215  -16.384 6.211   1.00 25.54 ? 102  ARG G CD  1 
ATOM   7450  N  NE  . ARG G  1 102 ? 61.241  -16.277 7.665   1.00 28.03 ? 102  ARG G NE  1 
ATOM   7451  C  CZ  . ARG G  1 102 ? 62.152  -16.855 8.434   1.00 26.07 ? 102  ARG G CZ  1 
ATOM   7452  N  NH1 . ARG G  1 102 ? 63.119  -17.577 7.887   1.00 25.25 ? 102  ARG G NH1 1 
ATOM   7453  N  NH2 . ARG G  1 102 ? 62.095  -16.709 9.749   1.00 32.49 ? 102  ARG G NH2 1 
ATOM   7454  N  N   . VAL G  1 103 ? 61.378  -13.271 1.157   1.00 20.18 ? 103  VAL G N   1 
ATOM   7455  C  CA  . VAL G  1 103 ? 61.020  -13.380 -0.262  1.00 19.32 ? 103  VAL G CA  1 
ATOM   7456  C  C   . VAL G  1 103 ? 62.125  -12.856 -1.210  1.00 21.91 ? 103  VAL G C   1 
ATOM   7457  O  O   . VAL G  1 103 ? 62.408  -13.474 -2.244  1.00 20.13 ? 103  VAL G O   1 
ATOM   7458  C  CB  . VAL G  1 103 ? 59.630  -12.745 -0.554  1.00 18.61 ? 103  VAL G CB  1 
ATOM   7459  C  CG1 . VAL G  1 103 ? 59.297  -12.803 -2.035  1.00 16.47 ? 103  VAL G CG1 1 
ATOM   7460  C  CG2 . VAL G  1 103 ? 58.567  -13.456 0.248   1.00 20.03 ? 103  VAL G CG2 1 
ATOM   7461  N  N   . ILE G  1 104 ? 62.747  -11.727 -0.854  1.00 20.35 ? 104  ILE G N   1 
ATOM   7462  C  CA  . ILE G  1 104 ? 63.919  -11.249 -1.583  1.00 19.11 ? 104  ILE G CA  1 
ATOM   7463  C  C   . ILE G  1 104 ? 65.095  -12.153 -1.245  1.00 19.27 ? 104  ILE G C   1 
ATOM   7464  O  O   . ILE G  1 104 ? 65.010  -12.959 -0.318  1.00 19.04 ? 104  ILE G O   1 
ATOM   7465  C  CB  . ILE G  1 104 ? 64.297  -9.760  -1.263  1.00 17.60 ? 104  ILE G CB  1 
ATOM   7466  C  CG1 . ILE G  1 104 ? 64.734  -9.588  0.190   1.00 18.86 ? 104  ILE G CG1 1 
ATOM   7467  C  CG2 . ILE G  1 104 ? 63.159  -8.804  -1.612  1.00 17.35 ? 104  ILE G CG2 1 
ATOM   7468  C  CD1 . ILE G  1 104 ? 65.341  -8.229  0.482   1.00 18.77 ? 104  ILE G CD1 1 
ATOM   7469  N  N   . SER G  1 105 ? 66.184  -12.008 -1.997  1.00 18.90 ? 105  SER G N   1 
ATOM   7470  C  CA  . SER G  1 105 ? 67.380  -12.822 -1.827  1.00 18.79 ? 105  SER G CA  1 
ATOM   7471  C  C   . SER G  1 105 ? 68.605  -12.079 -2.369  1.00 20.19 ? 105  SER G C   1 
ATOM   7472  O  O   . SER G  1 105 ? 68.473  -11.087 -3.079  1.00 20.84 ? 105  SER G O   1 
ATOM   7473  C  CB  . SER G  1 105 ? 67.211  -14.161 -2.544  1.00 17.96 ? 105  SER G CB  1 
ATOM   7474  O  OG  . SER G  1 105 ? 68.170  -15.111 -2.114  1.00 17.34 ? 105  SER G OG  1 
ATOM   7475  N  N   . LEU G  1 106 ? 69.795  -12.556 -2.024  1.00 20.96 ? 106  LEU G N   1 
ATOM   7476  C  CA  . LEU G  1 106 ? 71.031  -11.969 -2.525  1.00 19.63 ? 106  LEU G CA  1 
ATOM   7477  C  C   . LEU G  1 106 ? 71.751  -12.928 -3.481  1.00 21.37 ? 106  LEU G C   1 
ATOM   7478  O  O   . LEU G  1 106 ? 72.866  -12.659 -3.931  1.00 21.04 ? 106  LEU G O   1 
ATOM   7479  C  CB  . LEU G  1 106 ? 71.936  -11.557 -1.360  1.00 20.38 ? 106  LEU G CB  1 
ATOM   7480  C  CG  . LEU G  1 106 ? 71.381  -10.453 -0.448  1.00 18.22 ? 106  LEU G CG  1 
ATOM   7481  C  CD1 . LEU G  1 106 ? 72.426  -10.025 0.550   1.00 18.91 ? 106  LEU G CD1 1 
ATOM   7482  C  CD2 . LEU G  1 106 ? 70.913  -9.251  -1.263  1.00 17.23 ? 106  LEU G CD2 1 
ATOM   7483  N  N   . SER G  1 107 ? 71.088  -14.041 -3.788  1.00 21.26 ? 107  SER G N   1 
ATOM   7484  C  CA  . SER G  1 107 ? 71.573  -15.025 -4.752  1.00 23.34 ? 107  SER G CA  1 
ATOM   7485  C  C   . SER G  1 107 ? 70.372  -15.705 -5.405  1.00 25.12 ? 107  SER G C   1 
ATOM   7486  O  O   . SER G  1 107 ? 69.260  -15.627 -4.895  1.00 24.44 ? 107  SER G O   1 
ATOM   7487  C  CB  . SER G  1 107 ? 72.426  -16.084 -4.061  1.00 23.57 ? 107  SER G CB  1 
ATOM   7488  O  OG  . SER G  1 107 ? 71.610  -17.118 -3.535  1.00 28.47 ? 107  SER G OG  1 
ATOM   7489  N  N   . GLY G  1 108 ? 70.593  -16.371 -6.534  1.00 26.89 ? 108  GLY G N   1 
ATOM   7490  C  CA  . GLY G  1 108 ? 69.535  -17.145 -7.158  1.00 25.52 ? 108  GLY G CA  1 
ATOM   7491  C  C   . GLY G  1 108 ? 68.601  -16.279 -7.972  1.00 29.42 ? 108  GLY G C   1 
ATOM   7492  O  O   . GLY G  1 108 ? 68.893  -15.107 -8.215  1.00 30.23 ? 108  GLY G O   1 
ATOM   7493  N  N   . GLU G  1 109 ? 67.471  -16.850 -8.389  1.00 30.23 ? 109  GLU G N   1 
ATOM   7494  C  CA  . GLU G  1 109 ? 66.560  -16.167 -9.307  1.00 28.89 ? 109  GLU G CA  1 
ATOM   7495  C  C   . GLU G  1 109 ? 65.804  -14.974 -8.706  1.00 29.27 ? 109  GLU G C   1 
ATOM   7496  O  O   . GLU G  1 109 ? 65.324  -14.104 -9.438  1.00 27.77 ? 109  GLU G O   1 
ATOM   7497  C  CB  . GLU G  1 109 ? 65.588  -17.154 -9.963  1.00 30.19 ? 109  GLU G CB  1 
ATOM   7498  C  CG  . GLU G  1 109 ? 65.041  -18.213 -9.051  1.00 32.43 ? 109  GLU G CG  1 
ATOM   7499  C  CD  . GLU G  1 109 ? 63.630  -18.600 -9.428  1.00 35.91 ? 109  GLU G CD  1 
ATOM   7500  O  OE1 . GLU G  1 109 ? 62.772  -17.693 -9.441  1.00 41.52 ? 109  GLU G OE1 1 
ATOM   7501  O  OE2 . GLU G  1 109 ? 63.379  -19.790 -9.712  1.00 33.96 ? 109  GLU G OE2 1 
ATOM   7502  N  N   . HIS G  1 110 ? 65.701  -14.926 -7.382  1.00 29.72 ? 110  HIS G N   1 
ATOM   7503  C  CA  . HIS G  1 110 ? 65.115  -13.759 -6.730  1.00 27.86 ? 110  HIS G CA  1 
ATOM   7504  C  C   . HIS G  1 110 ? 66.173  -12.824 -6.132  1.00 25.05 ? 110  HIS G C   1 
ATOM   7505  O  O   . HIS G  1 110 ? 65.867  -12.065 -5.208  1.00 22.39 ? 110  HIS G O   1 
ATOM   7506  C  CB  . HIS G  1 110 ? 64.093  -14.167 -5.668  1.00 25.15 ? 110  HIS G CB  1 
ATOM   7507  C  CG  . HIS G  1 110 ? 62.897  -14.880 -6.224  1.00 27.33 ? 110  HIS G CG  1 
ATOM   7508  N  ND1 . HIS G  1 110 ? 61.944  -15.475 -5.424  1.00 29.87 ? 110  HIS G ND1 1 
ATOM   7509  C  CD2 . HIS G  1 110 ? 62.508  -15.100 -7.502  1.00 27.89 ? 110  HIS G CD2 1 
ATOM   7510  C  CE1 . HIS G  1 110 ? 61.015  -16.022 -6.185  1.00 30.88 ? 110  HIS G CE1 1 
ATOM   7511  N  NE2 . HIS G  1 110 ? 61.334  -15.810 -7.450  1.00 32.58 ? 110  HIS G NE2 1 
ATOM   7512  N  N   . SER G  1 111 ? 67.398  -12.876 -6.669  1.00 21.86 ? 111  SER G N   1 
ATOM   7513  C  CA  . SER G  1 111 ? 68.471  -11.975 -6.235  1.00 21.84 ? 111  SER G CA  1 
ATOM   7514  C  C   . SER G  1 111 ? 68.179  -10.536 -6.636  1.00 19.76 ? 111  SER G C   1 
ATOM   7515  O  O   . SER G  1 111 ? 67.754  -10.271 -7.752  1.00 19.45 ? 111  SER G O   1 
ATOM   7516  C  CB  . SER G  1 111 ? 69.822  -12.388 -6.819  1.00 22.03 ? 111  SER G CB  1 
ATOM   7517  O  OG  . SER G  1 111 ? 70.847  -11.518 -6.363  1.00 23.37 ? 111  SER G OG  1 
ATOM   7518  N  N   . ILE G  1 112 ? 68.405  -9.606  -5.717  1.00 21.12 ? 112  ILE G N   1 
ATOM   7519  C  CA  . ILE G  1 112 ? 68.114  -8.203  -5.974  1.00 16.47 ? 112  ILE G CA  1 
ATOM   7520  C  C   . ILE G  1 112 ? 69.405  -7.443  -6.253  1.00 17.01 ? 112  ILE G C   1 
ATOM   7521  O  O   . ILE G  1 112 ? 69.400  -6.228  -6.399  1.00 17.69 ? 112  ILE G O   1 
ATOM   7522  C  CB  . ILE G  1 112 ? 67.306  -7.573  -4.816  1.00 15.66 ? 112  ILE G CB  1 
ATOM   7523  C  CG1 . ILE G  1 112 ? 68.042  -7.730  -3.479  1.00 15.21 ? 112  ILE G CG1 1 
ATOM   7524  C  CG2 . ILE G  1 112 ? 65.923  -8.234  -4.733  1.00 17.11 ? 112  ILE G CG2 1 
ATOM   7525  C  CD1 . ILE G  1 112 ? 67.497  -6.829  -2.359  1.00 14.41 ? 112  ILE G CD1 1 
ATOM   7526  N  N   . ILE G  1 113 ? 70.512  -8.176  -6.324  1.00 18.03 ? 113  ILE G N   1 
ATOM   7527  C  CA  . ILE G  1 113 ? 71.799  -7.583  -6.662  1.00 19.25 ? 113  ILE G CA  1 
ATOM   7528  C  C   . ILE G  1 113 ? 71.755  -7.143  -8.119  1.00 19.96 ? 113  ILE G C   1 
ATOM   7529  O  O   . ILE G  1 113 ? 71.338  -7.909  -8.996  1.00 19.81 ? 113  ILE G O   1 
ATOM   7530  C  CB  . ILE G  1 113 ? 72.952  -8.589  -6.465  1.00 20.21 ? 113  ILE G CB  1 
ATOM   7531  C  CG1 . ILE G  1 113 ? 72.880  -9.228  -5.069  1.00 19.87 ? 113  ILE G CG1 1 
ATOM   7532  C  CG2 . ILE G  1 113 ? 74.296  -7.920  -6.702  1.00 18.86 ? 113  ILE G CG2 1 
ATOM   7533  C  CD1 . ILE G  1 113 ? 73.693  -8.548  -4.031  1.00 17.15 ? 113  ILE G CD1 1 
ATOM   7534  N  N   . GLY G  1 114 ? 72.166  -5.906  -8.380  1.00 17.61 ? 114  GLY G N   1 
ATOM   7535  C  CA  . GLY G  1 114 ? 72.102  -5.370  -9.723  1.00 15.79 ? 114  GLY G CA  1 
ATOM   7536  C  C   . GLY G  1 114 ? 70.726  -4.847  -10.060 1.00 16.66 ? 114  GLY G C   1 
ATOM   7537  O  O   . GLY G  1 114 ? 70.453  -4.505  -11.207 1.00 17.07 ? 114  GLY G O   1 
ATOM   7538  N  N   . ARG G  1 115 ? 69.842  -4.795  -9.065  1.00 18.31 ? 115  ARG G N   1 
ATOM   7539  C  CA  . ARG G  1 115 ? 68.524  -4.173  -9.241  1.00 18.88 ? 115  ARG G CA  1 
ATOM   7540  C  C   . ARG G  1 115 ? 68.476  -2.851  -8.449  1.00 18.04 ? 115  ARG G C   1 
ATOM   7541  O  O   . ARG G  1 115 ? 69.499  -2.430  -7.916  1.00 19.58 ? 115  ARG G O   1 
ATOM   7542  C  CB  . ARG G  1 115 ? 67.409  -5.160  -8.878  1.00 17.27 ? 115  ARG G CB  1 
ATOM   7543  C  CG  . ARG G  1 115 ? 67.533  -6.469  -9.673  1.00 17.80 ? 115  ARG G CG  1 
ATOM   7544  C  CD  . ARG G  1 115 ? 66.394  -7.448  -9.435  1.00 17.56 ? 115  ARG G CD  1 
ATOM   7545  N  NE  . ARG G  1 115 ? 66.585  -8.695  -10.184 1.00 20.36 ? 115  ARG G NE  1 
ATOM   7546  C  CZ  . ARG G  1 115 ? 66.336  -8.855  -11.485 1.00 18.65 ? 115  ARG G CZ  1 
ATOM   7547  N  NH1 . ARG G  1 115 ? 65.874  -7.855  -12.213 1.00 17.88 ? 115  ARG G NH1 1 
ATOM   7548  N  NH2 . ARG G  1 115 ? 66.536  -10.029 -12.061 1.00 17.78 ? 115  ARG G NH2 1 
ATOM   7549  N  N   . THR G  1 116 ? 67.323  -2.190  -8.376  1.00 17.20 ? 116  THR G N   1 
ATOM   7550  C  CA  . THR G  1 116 ? 67.258  -0.856  -7.759  1.00 19.05 ? 116  THR G CA  1 
ATOM   7551  C  C   . THR G  1 116 ? 66.342  -0.771  -6.529  1.00 19.85 ? 116  THR G C   1 
ATOM   7552  O  O   . THR G  1 116 ? 65.193  -1.199  -6.577  1.00 19.71 ? 116  THR G O   1 
ATOM   7553  C  CB  . THR G  1 116 ? 66.787  0.197   -8.788  1.00 18.64 ? 116  THR G CB  1 
ATOM   7554  O  OG1 . THR G  1 116 ? 67.671  0.184   -9.910  1.00 20.12 ? 116  THR G OG1 1 
ATOM   7555  C  CG2 . THR G  1 116 ? 66.766  1.604   -8.188  1.00 18.33 ? 116  THR G CG2 1 
ATOM   7556  N  N   . MET G  1 117 ? 66.851  -0.226  -5.425  1.00 19.04 ? 117  MET G N   1 
ATOM   7557  C  CA  . MET G  1 117 ? 65.971  0.193   -4.343  1.00 20.17 ? 117  MET G CA  1 
ATOM   7558  C  C   . MET G  1 117 ? 65.422  1.549   -4.740  1.00 23.87 ? 117  MET G C   1 
ATOM   7559  O  O   . MET G  1 117 ? 66.154  2.371   -5.285  1.00 23.61 ? 117  MET G O   1 
ATOM   7560  C  CB  . MET G  1 117 ? 66.720  0.368   -3.026  1.00 18.09 ? 117  MET G CB  1 
ATOM   7561  C  CG  . MET G  1 117 ? 66.879  -0.877  -2.194  1.00 22.85 ? 117  MET G CG  1 
ATOM   7562  S  SD  . MET G  1 117 ? 65.423  -1.924  -1.985  1.00 30.05 ? 117  MET G SD  1 
ATOM   7563  C  CE  . MET G  1 117 ? 64.180  -0.777  -1.447  1.00 22.95 ? 117  MET G CE  1 
ATOM   7564  N  N   . VAL G  1 118 ? 64.141  1.787   -4.486  1.00 21.61 ? 118  VAL G N   1 
ATOM   7565  C  CA  . VAL G  1 118 ? 63.627  3.143   -4.541  1.00 20.87 ? 118  VAL G CA  1 
ATOM   7566  C  C   . VAL G  1 118 ? 62.682  3.443   -3.373  1.00 23.88 ? 118  VAL G C   1 
ATOM   7567  O  O   . VAL G  1 118 ? 61.995  2.547   -2.855  1.00 21.83 ? 118  VAL G O   1 
ATOM   7568  C  CB  . VAL G  1 118 ? 63.071  3.547   -5.951  1.00 24.21 ? 118  VAL G CB  1 
ATOM   7569  C  CG1 . VAL G  1 118 ? 63.035  2.370   -6.895  1.00 20.81 ? 118  VAL G CG1 1 
ATOM   7570  C  CG2 . VAL G  1 118 ? 61.722  4.256   -5.860  1.00 22.48 ? 118  VAL G CG2 1 
ATOM   7571  N  N   . VAL G  1 119 ? 62.731  4.694   -2.914  1.00 23.49 ? 119  VAL G N   1 
ATOM   7572  C  CA  . VAL G  1 119 ? 61.881  5.180   -1.838  1.00 21.65 ? 119  VAL G CA  1 
ATOM   7573  C  C   . VAL G  1 119 ? 60.927  6.184   -2.467  1.00 23.26 ? 119  VAL G C   1 
ATOM   7574  O  O   . VAL G  1 119 ? 61.356  7.062   -3.208  1.00 23.23 ? 119  VAL G O   1 
ATOM   7575  C  CB  . VAL G  1 119 ? 62.705  5.812   -0.684  1.00 21.39 ? 119  VAL G CB  1 
ATOM   7576  C  CG1 . VAL G  1 119 ? 63.445  7.043   -1.151  1.00 19.89 ? 119  VAL G CG1 1 
ATOM   7577  C  CG2 . VAL G  1 119 ? 61.799  6.149   0.505   1.00 22.25 ? 119  VAL G CG2 1 
ATOM   7578  N  N   . HIS G  1 120 ? 59.632  6.043   -2.193  1.00 21.59 ? 120  HIS G N   1 
ATOM   7579  C  CA  . HIS G  1 120 ? 58.622  6.776   -2.941  1.00 21.46 ? 120  HIS G CA  1 
ATOM   7580  C  C   . HIS G  1 120 ? 58.071  8.003   -2.220  1.00 22.39 ? 120  HIS G C   1 
ATOM   7581  O  O   . HIS G  1 120 ? 58.248  8.168   -1.016  1.00 23.44 ? 120  HIS G O   1 
ATOM   7582  C  CB  . HIS G  1 120 ? 57.496  5.831   -3.361  1.00 19.75 ? 120  HIS G CB  1 
ATOM   7583  C  CG  . HIS G  1 120 ? 57.897  4.854   -4.424  1.00 22.25 ? 120  HIS G CG  1 
ATOM   7584  N  ND1 . HIS G  1 120 ? 57.542  5.007   -5.748  1.00 19.98 ? 120  HIS G ND1 1 
ATOM   7585  C  CD2 . HIS G  1 120 ? 58.634  3.718   -4.363  1.00 20.72 ? 120  HIS G CD2 1 
ATOM   7586  C  CE1 . HIS G  1 120 ? 58.027  4.001   -6.452  1.00 19.69 ? 120  HIS G CE1 1 
ATOM   7587  N  NE2 . HIS G  1 120 ? 58.700  3.208   -5.639  1.00 21.87 ? 120  HIS G NE2 1 
ATOM   7588  N  N   . GLU G  1 121 ? 57.404  8.853   -2.987  1.00 21.54 ? 121  GLU G N   1 
ATOM   7589  C  CA  . GLU G  1 121 ? 56.800  10.091  -2.513  1.00 22.50 ? 121  GLU G CA  1 
ATOM   7590  C  C   . GLU G  1 121 ? 55.751  9.873   -1.428  1.00 24.04 ? 121  GLU G C   1 
ATOM   7591  O  O   . GLU G  1 121 ? 55.667  10.611  -0.452  1.00 23.98 ? 121  GLU G O   1 
ATOM   7592  C  CB  . GLU G  1 121 ? 56.124  10.736  -3.719  1.00 26.14 ? 121  GLU G CB  1 
ATOM   7593  C  CG  . GLU G  1 121 ? 55.488  12.093  -3.504  1.00 29.56 ? 121  GLU G CG  1 
ATOM   7594  C  CD  . GLU G  1 121 ? 54.504  12.409  -4.616  1.00 29.99 ? 121  GLU G CD  1 
ATOM   7595  O  OE1 . GLU G  1 121 ? 54.006  11.447  -5.238  1.00 29.74 ? 121  GLU G OE1 1 
ATOM   7596  O  OE2 . GLU G  1 121 ? 54.232  13.601  -4.875  1.00 32.34 ? 121  GLU G OE2 1 
ATOM   7597  N  N   . LYS G  1 122 ? 54.939  8.845   -1.619  1.00 26.44 ? 122  LYS G N   1 
ATOM   7598  C  CA  . LYS G  1 122 ? 53.723  8.659   -0.847  1.00 24.62 ? 122  LYS G CA  1 
ATOM   7599  C  C   . LYS G  1 122 ? 53.730  7.292   -0.184  1.00 26.26 ? 122  LYS G C   1 
ATOM   7600  O  O   . LYS G  1 122 ? 54.584  6.453   -0.474  1.00 27.22 ? 122  LYS G O   1 
ATOM   7601  C  CB  . LYS G  1 122 ? 52.503  8.779   -1.771  1.00 25.20 ? 122  LYS G CB  1 
ATOM   7602  C  CG  . LYS G  1 122 ? 52.118  10.207  -2.127  1.00 25.76 ? 122  LYS G CG  1 
ATOM   7603  C  CD  . LYS G  1 122 ? 51.401  10.300  -3.460  1.00 28.10 ? 122  LYS G CD  1 
ATOM   7604  C  CE  . LYS G  1 122 ? 50.202  9.375   -3.529  1.00 32.66 ? 122  LYS G CE  1 
ATOM   7605  N  NZ  . LYS G  1 122 ? 49.049  9.856   -2.707  1.00 46.85 ? 122  LYS G NZ  1 
ATOM   7606  N  N   . GLN G  1 123 ? 52.768  7.085   0.709   1.00 28.54 ? 123  GLN G N   1 
ATOM   7607  C  CA  . GLN G  1 123 ? 52.570  5.822   1.415   1.00 24.29 ? 123  GLN G CA  1 
ATOM   7608  C  C   . GLN G  1 123 ? 52.085  4.731   0.470   1.00 23.66 ? 123  GLN G C   1 
ATOM   7609  O  O   . GLN G  1 123 ? 51.244  4.965   -0.396  1.00 21.63 ? 123  GLN G O   1 
ATOM   7610  C  CB  . GLN G  1 123 ? 51.551  6.033   2.529   1.00 24.63 ? 123  GLN G CB  1 
ATOM   7611  C  CG  . GLN G  1 123 ? 51.052  4.789   3.221   1.00 26.19 ? 123  GLN G CG  1 
ATOM   7612  C  CD  . GLN G  1 123 ? 50.024  5.123   4.285   1.00 28.14 ? 123  GLN G CD  1 
ATOM   7613  O  OE1 . GLN G  1 123 ? 49.739  6.294   4.536   1.00 30.29 ? 123  GLN G OE1 1 
ATOM   7614  N  NE2 . GLN G  1 123 ? 49.465  4.098   4.918   1.00 28.81 ? 123  GLN G NE2 1 
ATOM   7615  N  N   . ASP G  1 124 ? 52.636  3.537   0.647   1.00 24.04 ? 124  ASP G N   1 
ATOM   7616  C  CA  . ASP G  1 124 ? 52.266  2.372   -0.140  1.00 22.02 ? 124  ASP G CA  1 
ATOM   7617  C  C   . ASP G  1 124 ? 50.997  1.752   0.469   1.00 21.21 ? 124  ASP G C   1 
ATOM   7618  O  O   . ASP G  1 124 ? 50.998  1.329   1.627   1.00 23.00 ? 124  ASP G O   1 
ATOM   7619  C  CB  . ASP G  1 124 ? 53.443  1.391   -0.131  1.00 20.12 ? 124  ASP G CB  1 
ATOM   7620  C  CG  . ASP G  1 124 ? 53.164  0.111   -0.900  1.00 21.74 ? 124  ASP G CG  1 
ATOM   7621  O  OD1 . ASP G  1 124 ? 51.989  -0.189  -1.176  1.00 20.06 ? 124  ASP G OD1 1 
ATOM   7622  O  OD2 . ASP G  1 124 ? 54.135  -0.617  -1.211  1.00 21.25 ? 124  ASP G OD2 1 
ATOM   7623  N  N   . ASP G  1 125 ? 49.913  1.708   -0.306  1.00 22.50 ? 125  ASP G N   1 
ATOM   7624  C  CA  . ASP G  1 125 ? 48.618  1.239   0.211   1.00 23.43 ? 125  ASP G CA  1 
ATOM   7625  C  C   . ASP G  1 125 ? 48.530  -0.290  0.313   1.00 22.38 ? 125  ASP G C   1 
ATOM   7626  O  O   . ASP G  1 125 ? 47.480  -0.852  0.621   1.00 21.62 ? 125  ASP G O   1 
ATOM   7627  C  CB  . ASP G  1 125 ? 47.428  1.860   -0.554  1.00 24.53 ? 125  ASP G CB  1 
ATOM   7628  C  CG  . ASP G  1 125 ? 47.225  1.260   -1.930  1.00 22.53 ? 125  ASP G CG  1 
ATOM   7629  O  OD1 . ASP G  1 125 ? 47.845  0.216   -2.225  1.00 22.19 ? 125  ASP G OD1 1 
ATOM   7630  O  OD2 . ASP G  1 125 ? 46.434  1.826   -2.711  1.00 19.61 ? 125  ASP G OD2 1 
ATOM   7631  N  N   . LEU G  1 126 ? 49.669  -0.935  0.080   1.00 23.27 ? 126  LEU G N   1 
ATOM   7632  C  CA  . LEU G  1 126 ? 49.851  -2.368  0.289   1.00 22.38 ? 126  LEU G CA  1 
ATOM   7633  C  C   . LEU G  1 126 ? 48.832  -3.206  -0.470  1.00 22.97 ? 126  LEU G C   1 
ATOM   7634  O  O   . LEU G  1 126 ? 48.462  -4.301  -0.027  1.00 25.80 ? 126  LEU G O   1 
ATOM   7635  C  CB  . LEU G  1 126 ? 49.878  -2.717  1.789   1.00 23.16 ? 126  LEU G CB  1 
ATOM   7636  C  CG  . LEU G  1 126 ? 50.923  -1.991  2.657   1.00 22.73 ? 126  LEU G CG  1 
ATOM   7637  C  CD1 . LEU G  1 126 ? 50.776  -2.370  4.135   1.00 21.78 ? 126  LEU G CD1 1 
ATOM   7638  C  CD2 . LEU G  1 126 ? 52.357  -2.241  2.186   1.00 18.10 ? 126  LEU G CD2 1 
ATOM   7639  N  N   . GLY G  1 127 ? 48.396  -2.690  -1.619  1.00 22.05 ? 127  GLY G N   1 
ATOM   7640  C  CA  . GLY G  1 127 ? 47.501  -3.417  -2.505  1.00 21.78 ? 127  GLY G CA  1 
ATOM   7641  C  C   . GLY G  1 127 ? 46.023  -3.239  -2.230  1.00 22.50 ? 127  GLY G C   1 
ATOM   7642  O  O   . GLY G  1 127 ? 45.193  -3.705  -3.000  1.00 24.69 ? 127  GLY G O   1 
ATOM   7643  N  N   . LYS G  1 128 ? 45.696  -2.552  -1.138  1.00 24.94 ? 128  LYS G N   1 
ATOM   7644  C  CA  . LYS G  1 128 ? 44.313  -2.418  -0.662  1.00 23.60 ? 128  LYS G CA  1 
ATOM   7645  C  C   . LYS G  1 128 ? 43.634  -1.104  -1.096  1.00 21.65 ? 128  LYS G C   1 
ATOM   7646  O  O   . LYS G  1 128 ? 42.820  -0.533  -0.370  1.00 20.11 ? 128  LYS G O   1 
ATOM   7647  C  CB  . LYS G  1 128 ? 44.281  -2.542  0.872   1.00 24.37 ? 128  LYS G CB  1 
ATOM   7648  C  CG  . LYS G  1 128 ? 45.037  -3.735  1.435   1.00 23.60 ? 128  LYS G CG  1 
ATOM   7649  C  CD  . LYS G  1 128 ? 44.863  -3.839  2.933   1.00 30.27 ? 128  LYS G CD  1 
ATOM   7650  C  CE  . LYS G  1 128 ? 45.615  -5.045  3.473   1.00 36.48 ? 128  LYS G CE  1 
ATOM   7651  N  NZ  . LYS G  1 128 ? 45.604  -6.168  2.477   1.00 37.10 ? 128  LYS G NZ  1 
ATOM   7652  N  N   . GLY G  1 129 ? 43.973  -0.627  -2.286  1.00 24.46 ? 129  GLY G N   1 
ATOM   7653  C  CA  . GLY G  1 129 ? 43.496  0.669   -2.743  1.00 22.62 ? 129  GLY G CA  1 
ATOM   7654  C  C   . GLY G  1 129 ? 42.235  0.663   -3.574  1.00 19.96 ? 129  GLY G C   1 
ATOM   7655  O  O   . GLY G  1 129 ? 41.672  1.714   -3.816  1.00 21.28 ? 129  GLY G O   1 
ATOM   7656  N  N   . GLY G  1 130 ? 41.799  -0.510  -4.027  1.00 21.84 ? 130  GLY G N   1 
ATOM   7657  C  CA  . GLY G  1 130 ? 40.550  -0.624  -4.766  1.00 20.27 ? 130  GLY G CA  1 
ATOM   7658  C  C   . GLY G  1 130 ? 40.626  -0.198  -6.219  1.00 21.28 ? 130  GLY G C   1 
ATOM   7659  O  O   . GLY G  1 130 ? 39.613  0.010   -6.859  1.00 20.02 ? 130  GLY G O   1 
ATOM   7660  N  N   . ASN G  1 131 ? 41.834  -0.068  -6.750  1.00 24.83 ? 131  ASN G N   1 
ATOM   7661  C  CA  . ASN G  1 131 ? 42.009  0.231   -8.167  1.00 23.00 ? 131  ASN G CA  1 
ATOM   7662  C  C   . ASN G  1 131 ? 43.185  -0.518  -8.774  1.00 24.60 ? 131  ASN G C   1 
ATOM   7663  O  O   . ASN G  1 131 ? 43.947  -1.175  -8.064  1.00 22.79 ? 131  ASN G O   1 
ATOM   7664  C  CB  . ASN G  1 131 ? 42.097  1.751   -8.438  1.00 22.84 ? 131  ASN G CB  1 
ATOM   7665  C  CG  . ASN G  1 131 ? 43.257  2.423   -7.729  1.00 22.16 ? 131  ASN G CG  1 
ATOM   7666  O  OD1 . ASN G  1 131 ? 44.133  1.764   -7.186  1.00 23.77 ? 131  ASN G OD1 1 
ATOM   7667  N  ND2 . ASN G  1 131 ? 43.267  3.751   -7.741  1.00 22.91 ? 131  ASN G ND2 1 
ATOM   7668  N  N   . GLU G  1 132 ? 43.312  -0.428  -10.094 1.00 25.72 ? 132  GLU G N   1 
ATOM   7669  C  CA  . GLU G  1 132 ? 44.370  -1.126  -10.805 1.00 27.75 ? 132  GLU G CA  1 
ATOM   7670  C  C   . GLU G  1 132 ? 45.773  -0.620  -10.433 1.00 25.49 ? 132  GLU G C   1 
ATOM   7671  O  O   . GLU G  1 132 ? 46.706  -1.411  -10.340 1.00 25.77 ? 132  GLU G O   1 
ATOM   7672  C  CB  . GLU G  1 132 ? 44.142  -1.064  -12.318 1.00 29.64 ? 132  GLU G CB  1 
ATOM   7673  C  CG  . GLU G  1 132 ? 45.117  -1.936  -13.085 1.00 37.76 ? 132  GLU G CG  1 
ATOM   7674  C  CD  . GLU G  1 132 ? 44.858  -1.959  -14.582 1.00 48.54 ? 132  GLU G CD  1 
ATOM   7675  O  OE1 . GLU G  1 132 ? 45.768  -2.399  -15.326 1.00 47.54 ? 132  GLU G OE1 1 
ATOM   7676  O  OE2 . GLU G  1 132 ? 43.754  -1.546  -15.009 1.00 48.91 ? 132  GLU G OE2 1 
ATOM   7677  N  N   . GLU G  1 133 ? 45.921  0.687   -10.223 1.00 24.91 ? 133  GLU G N   1 
ATOM   7678  C  CA  . GLU G  1 133 ? 47.163  1.245   -9.681  1.00 25.57 ? 133  GLU G CA  1 
ATOM   7679  C  C   . GLU G  1 133 ? 47.631  0.542   -8.406  1.00 23.80 ? 133  GLU G C   1 
ATOM   7680  O  O   . GLU G  1 133 ? 48.807  0.255   -8.244  1.00 23.78 ? 133  GLU G O   1 
ATOM   7681  C  CB  . GLU G  1 133 ? 47.027  2.747   -9.406  1.00 24.55 ? 133  GLU G CB  1 
ATOM   7682  C  CG  . GLU G  1 133 ? 47.450  3.617   -10.561 1.00 32.73 ? 133  GLU G CG  1 
ATOM   7683  C  CD  . GLU G  1 133 ? 48.916  3.440   -10.902 1.00 35.92 ? 133  GLU G CD  1 
ATOM   7684  O  OE1 . GLU G  1 133 ? 49.728  3.314   -9.958  1.00 35.54 ? 133  GLU G OE1 1 
ATOM   7685  O  OE2 . GLU G  1 133 ? 49.258  3.425   -12.106 1.00 40.55 ? 133  GLU G OE2 1 
ATOM   7686  N  N   . SER G  1 134 ? 46.711  0.277   -7.494  1.00 23.01 ? 134  SER G N   1 
ATOM   7687  C  CA  . SER G  1 134 ? 47.076  -0.345  -6.241  1.00 21.60 ? 134  SER G CA  1 
ATOM   7688  C  C   . SER G  1 134 ? 47.710  -1.709  -6.471  1.00 23.97 ? 134  SER G C   1 
ATOM   7689  O  O   . SER G  1 134 ? 48.682  -2.067  -5.807  1.00 25.63 ? 134  SER G O   1 
ATOM   7690  C  CB  . SER G  1 134 ? 45.852  -0.489  -5.348  1.00 21.71 ? 134  SER G CB  1 
ATOM   7691  O  OG  . SER G  1 134 ? 46.223  -0.952  -4.063  1.00 21.88 ? 134  SER G OG  1 
ATOM   7692  N  N   . THR G  1 135 ? 47.153  -2.468  -7.414  1.00 26.43 ? 135  THR G N   1 
ATOM   7693  C  CA  . THR G  1 135 ? 47.608  -3.827  -7.689  1.00 23.76 ? 135  THR G CA  1 
ATOM   7694  C  C   . THR G  1 135 ? 48.975  -3.826  -8.381  1.00 23.96 ? 135  THR G C   1 
ATOM   7695  O  O   . THR G  1 135 ? 49.629  -4.861  -8.479  1.00 24.96 ? 135  THR G O   1 
ATOM   7696  C  CB  . THR G  1 135 ? 46.558  -4.621  -8.521  1.00 25.96 ? 135  THR G CB  1 
ATOM   7697  O  OG1 . THR G  1 135 ? 46.594  -4.207  -9.893  1.00 25.69 ? 135  THR G OG1 1 
ATOM   7698  C  CG2 . THR G  1 135 ? 45.153  -4.403  -7.971  1.00 25.80 ? 135  THR G CG2 1 
ATOM   7699  N  N   . LYS G  1 136 ? 49.410  -2.649  -8.825  1.00 23.37 ? 136  LYS G N   1 
ATOM   7700  C  CA  . LYS G  1 136 ? 50.685  -2.486  -9.530  1.00 23.38 ? 136  LYS G CA  1 
ATOM   7701  C  C   . LYS G  1 136 ? 51.776  -1.785  -8.709  1.00 22.78 ? 136  LYS G C   1 
ATOM   7702  O  O   . LYS G  1 136 ? 52.904  -2.254  -8.664  1.00 21.64 ? 136  LYS G O   1 
ATOM   7703  C  CB  . LYS G  1 136 ? 50.475  -1.726  -10.854 1.00 25.31 ? 136  LYS G CB  1 
ATOM   7704  C  CG  . LYS G  1 136 ? 50.083  -2.607  -12.053 1.00 26.63 ? 136  LYS G CG  1 
ATOM   7705  C  CD  . LYS G  1 136 ? 49.128  -1.886  -12.991 1.00 29.79 ? 136  LYS G CD  1 
ATOM   7706  C  CE  . LYS G  1 136 ? 49.554  -0.451  -13.232 1.00 32.52 ? 136  LYS G CE  1 
ATOM   7707  N  NZ  . LYS G  1 136 ? 50.701  -0.392  -14.182 1.00 41.86 ? 136  LYS G NZ  1 
ATOM   7708  N  N   . THR G  1 137 ? 51.440  -0.664  -8.070  1.00 22.22 ? 137  THR G N   1 
ATOM   7709  C  CA  . THR G  1 137 ? 52.445  0.202   -7.451  1.00 20.85 ? 137  THR G CA  1 
ATOM   7710  C  C   . THR G  1 137 ? 52.174  0.582   -5.986  1.00 20.78 ? 137  THR G C   1 
ATOM   7711  O  O   . THR G  1 137 ? 53.031  1.186   -5.329  1.00 19.51 ? 137  THR G O   1 
ATOM   7712  C  CB  . THR G  1 137 ? 52.615  1.507   -8.256  1.00 23.60 ? 137  THR G CB  1 
ATOM   7713  O  OG1 . THR G  1 137 ? 51.442  2.316   -8.108  1.00 22.86 ? 137  THR G OG1 1 
ATOM   7714  C  CG2 . THR G  1 137 ? 52.847  1.203   -9.744  1.00 22.19 ? 137  THR G CG2 1 
ATOM   7715  N  N   . GLY G  1 138 ? 50.991  0.220   -5.487  1.00 21.33 ? 138  GLY G N   1 
ATOM   7716  C  CA  . GLY G  1 138 ? 50.562  0.547   -4.137  1.00 19.11 ? 138  GLY G CA  1 
ATOM   7717  C  C   . GLY G  1 138 ? 50.127  1.996   -4.008  1.00 19.51 ? 138  GLY G C   1 
ATOM   7718  O  O   . GLY G  1 138 ? 49.936  2.505   -2.906  1.00 21.21 ? 138  GLY G O   1 
ATOM   7719  N  N   . ASN G  1 139 ? 49.954  2.659   -5.142  1.00 18.75 ? 139  ASN G N   1 
ATOM   7720  C  CA  . ASN G  1 139 ? 49.705  4.093   -5.169  1.00 22.01 ? 139  ASN G CA  1 
ATOM   7721  C  C   . ASN G  1 139 ? 50.761  4.808   -4.346  1.00 23.68 ? 139  ASN G C   1 
ATOM   7722  O  O   . ASN G  1 139 ? 50.441  5.647   -3.509  1.00 25.20 ? 139  ASN G O   1 
ATOM   7723  C  CB  . ASN G  1 139 ? 48.309  4.426   -4.638  1.00 22.79 ? 139  ASN G CB  1 
ATOM   7724  C  CG  . ASN G  1 139 ? 47.204  4.016   -5.590  1.00 22.38 ? 139  ASN G CG  1 
ATOM   7725  O  OD1 . ASN G  1 139 ? 47.099  4.542   -6.699  1.00 23.95 ? 139  ASN G OD1 1 
ATOM   7726  N  ND2 . ASN G  1 139 ? 46.359  3.078   -5.152  1.00 21.66 ? 139  ASN G ND2 1 
ATOM   7727  N  N   . ALA G  1 140 ? 52.024  4.463   -4.586  1.00 22.78 ? 140  ALA G N   1 
ATOM   7728  C  CA  . ALA G  1 140 ? 53.120  4.993   -3.790  1.00 23.16 ? 140  ALA G CA  1 
ATOM   7729  C  C   . ALA G  1 140 ? 53.727  6.259   -4.396  1.00 23.79 ? 140  ALA G C   1 
ATOM   7730  O  O   . ALA G  1 140 ? 54.550  6.913   -3.778  1.00 24.54 ? 140  ALA G O   1 
ATOM   7731  C  CB  . ALA G  1 140 ? 54.178  3.929   -3.562  1.00 20.87 ? 140  ALA G CB  1 
ATOM   7732  N  N   . GLY G  1 141 ? 53.307  6.614   -5.599  1.00 24.51 ? 141  GLY G N   1 
ATOM   7733  C  CA  . GLY G  1 141 ? 53.666  7.904   -6.143  1.00 25.04 ? 141  GLY G CA  1 
ATOM   7734  C  C   . GLY G  1 141 ? 55.022  7.891   -6.807  1.00 30.02 ? 141  GLY G C   1 
ATOM   7735  O  O   . GLY G  1 141 ? 55.568  6.825   -7.131  1.00 28.95 ? 141  GLY G O   1 
ATOM   7736  N  N   . SER G  1 142 ? 55.578  9.079   -7.016  1.00 29.77 ? 142  SER G N   1 
ATOM   7737  C  CA  . SER G  1 142 ? 56.803  9.188   -7.800  1.00 28.88 ? 142  SER G CA  1 
ATOM   7738  C  C   . SER G  1 142 ? 58.041  8.741   -7.026  1.00 26.71 ? 142  SER G C   1 
ATOM   7739  O  O   . SER G  1 142 ? 58.025  8.621   -5.794  1.00 23.70 ? 142  SER G O   1 
ATOM   7740  C  CB  . SER G  1 142 ? 56.981  10.608  -8.341  1.00 29.46 ? 142  SER G CB  1 
ATOM   7741  O  OG  . SER G  1 142 ? 57.121  11.522  -7.275  1.00 30.63 ? 142  SER G OG  1 
ATOM   7742  N  N   . ARG G  1 143 ? 59.108  8.487   -7.779  1.00 27.61 ? 143  ARG G N   1 
ATOM   7743  C  CA  . ARG G  1 143 ? 60.359  7.977   -7.230  1.00 25.94 ? 143  ARG G CA  1 
ATOM   7744  C  C   . ARG G  1 143 ? 61.245  9.132   -6.783  1.00 26.49 ? 143  ARG G C   1 
ATOM   7745  O  O   . ARG G  1 143 ? 61.675  9.956   -7.601  1.00 25.72 ? 143  ARG G O   1 
ATOM   7746  C  CB  . ARG G  1 143 ? 61.051  7.079   -8.265  1.00 23.66 ? 143  ARG G CB  1 
ATOM   7747  C  CG  . ARG G  1 143 ? 60.087  6.042   -8.819  1.00 19.37 ? 143  ARG G CG  1 
ATOM   7748  C  CD  . ARG G  1 143 ? 60.610  5.229   -9.976  1.00 20.13 ? 143  ARG G CD  1 
ATOM   7749  N  NE  . ARG G  1 143 ? 59.524  4.402   -10.504 1.00 23.34 ? 143  ARG G NE  1 
ATOM   7750  C  CZ  . ARG G  1 143 ? 59.655  3.430   -11.402 1.00 19.78 ? 143  ARG G CZ  1 
ATOM   7751  N  NH1 . ARG G  1 143 ? 60.842  3.125   -11.903 1.00 19.46 ? 143  ARG G NH1 1 
ATOM   7752  N  NH2 . ARG G  1 143 ? 58.585  2.757   -11.793 1.00 20.85 ? 143  ARG G NH2 1 
ATOM   7753  N  N   . LEU G  1 144 ? 61.486  9.187   -5.474  1.00 21.98 ? 144  LEU G N   1 
ATOM   7754  C  CA  . LEU G  1 144 ? 62.197  10.289  -4.839  1.00 22.18 ? 144  LEU G CA  1 
ATOM   7755  C  C   . LEU G  1 144 ? 63.686  10.074  -4.928  1.00 24.71 ? 144  LEU G C   1 
ATOM   7756  O  O   . LEU G  1 144 ? 64.437  11.014  -5.182  1.00 27.50 ? 144  LEU G O   1 
ATOM   7757  C  CB  . LEU G  1 144 ? 61.829  10.398  -3.352  1.00 22.05 ? 144  LEU G CB  1 
ATOM   7758  C  CG  . LEU G  1 144 ? 60.454  10.841  -2.850  1.00 20.91 ? 144  LEU G CG  1 
ATOM   7759  C  CD1 . LEU G  1 144 ? 60.509  10.966  -1.342  1.00 24.49 ? 144  LEU G CD1 1 
ATOM   7760  C  CD2 . LEU G  1 144 ? 60.030  12.146  -3.453  1.00 20.39 ? 144  LEU G CD2 1 
ATOM   7761  N  N   . ALA G  1 145 ? 64.112  8.836   -4.683  1.00 23.07 ? 145  ALA G N   1 
ATOM   7762  C  CA  . ALA G  1 145 ? 65.529  8.498   -4.648  1.00 23.12 ? 145  ALA G CA  1 
ATOM   7763  C  C   . ALA G  1 145 ? 65.733  7.005   -4.804  1.00 23.81 ? 145  ALA G C   1 
ATOM   7764  O  O   . ALA G  1 145 ? 64.873  6.211   -4.439  1.00 24.61 ? 145  ALA G O   1 
ATOM   7765  C  CB  . ALA G  1 145 ? 66.166  8.981   -3.365  1.00 21.60 ? 145  ALA G CB  1 
ATOM   7766  N  N   . CYS G  1 146 ? 66.886  6.636   -5.353  1.00 25.12 ? 146  CYS G N   1 
ATOM   7767  C  CA  . CYS G  1 146 ? 67.199  5.253   -5.672  1.00 23.31 ? 146  CYS G CA  1 
ATOM   7768  C  C   . CYS G  1 146 ? 68.697  5.013   -5.867  1.00 23.61 ? 146  CYS G C   1 
ATOM   7769  O  O   . CYS G  1 146 ? 69.482  5.937   -6.123  1.00 21.37 ? 146  CYS G O   1 
ATOM   7770  C  CB  . CYS G  1 146 ? 66.449  4.802   -6.928  1.00 23.10 ? 146  CYS G CB  1 
ATOM   7771  S  SG  . CYS G  1 146 ? 67.033  5.549   -8.452  1.00 26.92 ? 146  CYS G SG  1 
ATOM   7772  N  N   . GLY G  1 147 ? 69.076  3.750   -5.725  1.00 20.63 ? 147  GLY G N   1 
ATOM   7773  C  CA  . GLY G  1 147 ? 70.421  3.319   -6.007  1.00 22.17 ? 147  GLY G CA  1 
ATOM   7774  C  C   . GLY G  1 147 ? 70.348  1.903   -6.539  1.00 23.76 ? 147  GLY G C   1 
ATOM   7775  O  O   . GLY G  1 147 ? 69.362  1.194   -6.293  1.00 22.36 ? 147  GLY G O   1 
ATOM   7776  N  N   . VAL G  1 148 ? 71.378  1.503   -7.279  1.00 19.66 ? 148  VAL G N   1 
ATOM   7777  C  CA  . VAL G  1 148 ? 71.546  0.120   -7.705  1.00 17.15 ? 148  VAL G CA  1 
ATOM   7778  C  C   . VAL G  1 148 ? 72.113  -0.687  -6.544  1.00 18.89 ? 148  VAL G C   1 
ATOM   7779  O  O   . VAL G  1 148 ? 72.996  -0.210  -5.819  1.00 18.23 ? 148  VAL G O   1 
ATOM   7780  C  CB  . VAL G  1 148 ? 72.486  0.053   -8.908  1.00 14.48 ? 148  VAL G CB  1 
ATOM   7781  C  CG1 . VAL G  1 148 ? 72.557  -1.354  -9.460  1.00 15.30 ? 148  VAL G CG1 1 
ATOM   7782  C  CG2 . VAL G  1 148 ? 71.997  1.013   -9.960  1.00 17.29 ? 148  VAL G CG2 1 
ATOM   7783  N  N   . ILE G  1 149 ? 71.590  -1.895  -6.345  1.00 18.56 ? 149  ILE G N   1 
ATOM   7784  C  CA  . ILE G  1 149 ? 72.030  -2.746  -5.236  1.00 18.59 ? 149  ILE G CA  1 
ATOM   7785  C  C   . ILE G  1 149 ? 73.295  -3.482  -5.636  1.00 16.66 ? 149  ILE G C   1 
ATOM   7786  O  O   . ILE G  1 149 ? 73.275  -4.314  -6.549  1.00 17.25 ? 149  ILE G O   1 
ATOM   7787  C  CB  . ILE G  1 149 ? 70.938  -3.769  -4.813  1.00 17.65 ? 149  ILE G CB  1 
ATOM   7788  C  CG1 . ILE G  1 149 ? 69.619  -3.051  -4.529  1.00 16.63 ? 149  ILE G CG1 1 
ATOM   7789  C  CG2 . ILE G  1 149 ? 71.402  -4.604  -3.597  1.00 14.96 ? 149  ILE G CG2 1 
ATOM   7790  C  CD1 . ILE G  1 149 ? 68.435  -3.959  -4.505  1.00 15.31 ? 149  ILE G CD1 1 
ATOM   7791  N  N   . GLY G  1 150 ? 74.390  -3.166  -4.954  1.00 15.33 ? 150  GLY G N   1 
ATOM   7792  C  CA  . GLY G  1 150 ? 75.689  -3.735  -5.272  1.00 16.55 ? 150  GLY G CA  1 
ATOM   7793  C  C   . GLY G  1 150 ? 76.264  -4.648  -4.208  1.00 18.79 ? 150  GLY G C   1 
ATOM   7794  O  O   . GLY G  1 150 ? 75.758  -4.695  -3.078  1.00 18.94 ? 150  GLY G O   1 
ATOM   7795  N  N   . ILE G  1 151 ? 77.320  -5.376  -4.577  1.00 18.96 ? 151  ILE G N   1 
ATOM   7796  C  CA  . ILE G  1 151 ? 77.986  -6.312  -3.673  1.00 18.64 ? 151  ILE G CA  1 
ATOM   7797  C  C   . ILE G  1 151 ? 78.884  -5.551  -2.713  1.00 18.81 ? 151  ILE G C   1 
ATOM   7798  O  O   . ILE G  1 151 ? 79.629  -4.670  -3.125  1.00 21.18 ? 151  ILE G O   1 
ATOM   7799  C  CB  . ILE G  1 151 ? 78.821  -7.351  -4.444  1.00 18.88 ? 151  ILE G CB  1 
ATOM   7800  C  CG1 . ILE G  1 151 ? 77.934  -8.126  -5.413  1.00 19.61 ? 151  ILE G CG1 1 
ATOM   7801  C  CG2 . ILE G  1 151 ? 79.474  -8.304  -3.486  1.00 20.98 ? 151  ILE G CG2 1 
ATOM   7802  C  CD1 . ILE G  1 151 ? 78.691  -9.025  -6.348  1.00 17.71 ? 151  ILE G CD1 1 
ATOM   7803  N  N   . ALA G  1 152 ? 78.803  -5.896  -1.433  1.00 22.33 ? 152  ALA G N   1 
ATOM   7804  C  CA  . ALA G  1 152 ? 79.523  -5.196  -0.375  1.00 22.21 ? 152  ALA G CA  1 
ATOM   7805  C  C   . ALA G  1 152 ? 80.474  -6.177  0.300   1.00 26.24 ? 152  ALA G C   1 
ATOM   7806  O  O   . ALA G  1 152 ? 80.338  -7.392  0.132   1.00 27.87 ? 152  ALA G O   1 
ATOM   7807  C  CB  . ALA G  1 152 ? 78.540  -4.645  0.631   1.00 18.62 ? 152  ALA G CB  1 
ATOM   7808  N  N   . GLN G  1 153 ? 81.445  -5.679  1.055   1.00 25.05 ? 153  GLN G N   1 
ATOM   7809  C  CA  . GLN G  1 153 ? 82.340  -6.601  1.752   1.00 30.30 ? 153  GLN G CA  1 
ATOM   7810  C  C   . GLN G  1 153 ? 81.872  -6.940  3.159   1.00 33.74 ? 153  GLN G C   1 
ATOM   7811  O  O   . GLN G  1 153 ? 82.009  -8.095  3.569   1.00 36.82 ? 153  GLN G O   1 
ATOM   7812  C  CB  . GLN G  1 153 ? 83.793  -6.110  1.772   1.00 30.86 ? 153  GLN G CB  1 
ATOM   7813  C  CG  . GLN G  1 153 ? 84.044  -4.807  2.498   1.00 32.60 ? 153  GLN G CG  1 
ATOM   7814  C  CD  . GLN G  1 153 ? 85.534  -4.594  2.768   1.00 38.70 ? 153  GLN G CD  1 
ATOM   7815  O  OE1 . GLN G  1 153 ? 86.348  -5.515  2.613   1.00 35.83 ? 153  GLN G OE1 1 
ATOM   7816  N  NE2 . GLN G  1 153 ? 85.894  -3.380  3.170   1.00 40.07 ? 153  GLN G NE2 1 
ATOM   7817  O  OXT . GLN G  1 153 ? 81.357  -6.086  3.897   1.00 34.76 ? 153  GLN G OXT 1 
ATOM   7818  N  N   . ALA H  1 1   ? 71.325  -14.182 -22.903 1.00 38.99 ? 1    ALA H N   1 
ATOM   7819  C  CA  . ALA H  1 1   ? 71.424  -12.916 -23.630 1.00 41.12 ? 1    ALA H CA  1 
ATOM   7820  C  C   . ALA H  1 1   ? 71.453  -11.744 -22.662 1.00 39.77 ? 1    ALA H C   1 
ATOM   7821  O  O   . ALA H  1 1   ? 70.923  -10.670 -22.956 1.00 42.08 ? 1    ALA H O   1 
ATOM   7822  C  CB  . ALA H  1 1   ? 70.266  -12.760 -24.609 1.00 43.43 ? 1    ALA H CB  1 
ATOM   7823  N  N   . THR H  1 2   ? 72.083  -11.959 -21.513 1.00 35.48 ? 2    THR H N   1 
ATOM   7824  C  CA  . THR H  1 2   ? 72.120  -10.959 -20.452 1.00 34.53 ? 2    THR H CA  1 
ATOM   7825  C  C   . THR H  1 2   ? 72.660  -9.579  -20.902 1.00 31.64 ? 2    THR H C   1 
ATOM   7826  O  O   . THR H  1 2   ? 73.654  -9.476  -21.626 1.00 30.68 ? 2    THR H O   1 
ATOM   7827  C  CB  . THR H  1 2   ? 72.878  -11.483 -19.182 1.00 35.53 ? 2    THR H CB  1 
ATOM   7828  O  OG1 . THR H  1 2   ? 74.117  -12.099 -19.564 1.00 34.65 ? 2    THR H OG1 1 
ATOM   7829  C  CG2 . THR H  1 2   ? 72.029  -12.506 -18.424 1.00 34.58 ? 2    THR H CG2 1 
ATOM   7830  N  N   . LYS H  1 3   ? 71.965  -8.528  -20.471 1.00 30.25 ? 3    LYS H N   1 
ATOM   7831  C  CA  . LYS H  1 3   ? 72.418  -7.150  -20.619 1.00 26.39 ? 3    LYS H CA  1 
ATOM   7832  C  C   . LYS H  1 3   ? 72.620  -6.515  -19.233 1.00 23.99 ? 3    LYS H C   1 
ATOM   7833  O  O   . LYS H  1 3   ? 71.951  -6.878  -18.266 1.00 24.42 ? 3    LYS H O   1 
ATOM   7834  C  CB  . LYS H  1 3   ? 71.406  -6.347  -21.447 1.00 27.20 ? 3    LYS H CB  1 
ATOM   7835  C  CG  . LYS H  1 3   ? 71.176  -6.910  -22.841 1.00 32.05 ? 3    LYS H CG  1 
ATOM   7836  C  CD  . LYS H  1 3   ? 69.806  -6.546  -23.392 1.00 40.04 ? 3    LYS H CD  1 
ATOM   7837  C  CE  . LYS H  1 3   ? 69.771  -5.127  -23.959 1.00 47.19 ? 3    LYS H CE  1 
ATOM   7838  N  NZ  . LYS H  1 3   ? 70.423  -5.024  -25.309 1.00 51.80 ? 3    LYS H NZ  1 
ATOM   7839  N  N   . ALA H  1 4   ? 73.566  -5.592  -19.132 1.00 22.14 ? 4    ALA H N   1 
ATOM   7840  C  CA  . ALA H  1 4   ? 73.740  -4.806  -17.921 1.00 17.92 ? 4    ALA H CA  1 
ATOM   7841  C  C   . ALA H  1 4   ? 74.054  -3.372  -18.319 1.00 18.69 ? 4    ALA H C   1 
ATOM   7842  O  O   . ALA H  1 4   ? 74.432  -3.111  -19.450 1.00 17.16 ? 4    ALA H O   1 
ATOM   7843  C  CB  . ALA H  1 4   ? 74.848  -5.382  -17.074 1.00 18.41 ? 4    ALA H CB  1 
ATOM   7844  N  N   . VAL H  1 5   ? 73.884  -2.436  -17.392 1.00 21.83 ? 5    VAL H N   1 
ATOM   7845  C  CA  . VAL H  1 5   ? 74.203  -1.032  -17.654 1.00 19.63 ? 5    VAL H CA  1 
ATOM   7846  C  C   . VAL H  1 5   ? 74.882  -0.424  -16.429 1.00 20.28 ? 5    VAL H C   1 
ATOM   7847  O  O   . VAL H  1 5   ? 74.852  -0.996  -15.338 1.00 19.92 ? 5    VAL H O   1 
ATOM   7848  C  CB  . VAL H  1 5   ? 72.939  -0.217  -18.034 1.00 19.66 ? 5    VAL H CB  1 
ATOM   7849  C  CG1 . VAL H  1 5   ? 72.064  -0.010  -16.824 1.00 19.34 ? 5    VAL H CG1 1 
ATOM   7850  C  CG2 . VAL H  1 5   ? 73.318  1.121   -18.662 1.00 19.66 ? 5    VAL H CG2 1 
ATOM   7851  N  N   . CYS H  1 6   ? 75.507  0.730   -16.622 1.00 22.52 ? 6    CYS H N   1 
ATOM   7852  C  CA  . CYS H  1 6   ? 76.248  1.404   -15.566 1.00 20.82 ? 6    CYS H CA  1 
ATOM   7853  C  C   . CYS H  1 6   ? 76.253  2.914   -15.818 1.00 20.46 ? 6    CYS H C   1 
ATOM   7854  O  O   . CYS H  1 6   ? 76.686  3.357   -16.869 1.00 21.08 ? 6    CYS H O   1 
ATOM   7855  C  CB  . CYS H  1 6   ? 77.685  0.889   -15.561 1.00 19.89 ? 6    CYS H CB  1 
ATOM   7856  S  SG  . CYS H  1 6   ? 78.651  1.477   -14.192 1.00 23.08 ? 6    CYS H SG  1 
ATOM   7857  N  N   . VAL H  1 7   ? 75.769  3.705   -14.866 1.00 22.46 ? 7    VAL H N   1 
ATOM   7858  C  CA  . VAL H  1 7   ? 75.884  5.161   -14.975 1.00 21.02 ? 7    VAL H CA  1 
ATOM   7859  C  C   . VAL H  1 7   ? 77.059  5.656   -14.118 1.00 18.31 ? 7    VAL H C   1 
ATOM   7860  O  O   . VAL H  1 7   ? 77.085  5.449   -12.912 1.00 19.94 ? 7    VAL H O   1 
ATOM   7861  C  CB  . VAL H  1 7   ? 74.548  5.894   -14.624 1.00 21.99 ? 7    VAL H CB  1 
ATOM   7862  C  CG1 . VAL H  1 7   ? 74.718  7.413   -14.671 1.00 21.88 ? 7    VAL H CG1 1 
ATOM   7863  C  CG2 . VAL H  1 7   ? 73.457  5.481   -15.591 1.00 23.81 ? 7    VAL H CG2 1 
ATOM   7864  N  N   . LEU H  1 8   ? 78.047  6.283   -14.752 1.00 19.78 ? 8    LEU H N   1 
ATOM   7865  C  CA  . LEU H  1 8   ? 79.230  6.761   -14.036 1.00 18.58 ? 8    LEU H CA  1 
ATOM   7866  C  C   . LEU H  1 8   ? 79.054  8.209   -13.589 1.00 17.12 ? 8    LEU H C   1 
ATOM   7867  O  O   . LEU H  1 8   ? 78.768  9.081   -14.394 1.00 18.25 ? 8    LEU H O   1 
ATOM   7868  C  CB  . LEU H  1 8   ? 80.508  6.626   -14.885 1.00 15.89 ? 8    LEU H CB  1 
ATOM   7869  C  CG  . LEU H  1 8   ? 80.857  5.345   -15.656 1.00 16.78 ? 8    LEU H CG  1 
ATOM   7870  C  CD1 . LEU H  1 8   ? 82.253  5.465   -16.275 1.00 18.36 ? 8    LEU H CD1 1 
ATOM   7871  C  CD2 . LEU H  1 8   ? 80.795  4.131   -14.774 1.00 18.60 ? 8    LEU H CD2 1 
ATOM   7872  N  N   . LYS H  1 9   ? 79.227  8.442   -12.294 1.00 19.47 ? 9    LYS H N   1 
ATOM   7873  C  CA  . LYS H  1 9   ? 79.191  9.778   -11.713 1.00 18.93 ? 9    LYS H CA  1 
ATOM   7874  C  C   . LYS H  1 9   ? 80.360  9.880   -10.764 1.00 18.58 ? 9    LYS H C   1 
ATOM   7875  O  O   . LYS H  1 9   ? 80.854  8.871   -10.265 1.00 16.93 ? 9    LYS H O   1 
ATOM   7876  C  CB  . LYS H  1 9   ? 77.901  10.015  -10.926 1.00 19.27 ? 9    LYS H CB  1 
ATOM   7877  C  CG  . LYS H  1 9   ? 76.659  10.170  -11.779 1.00 20.75 ? 9    LYS H CG  1 
ATOM   7878  C  CD  . LYS H  1 9   ? 75.414  10.353  -10.911 1.00 25.74 ? 9    LYS H CD  1 
ATOM   7879  C  CE  . LYS H  1 9   ? 74.126  10.356  -11.741 1.00 27.14 ? 9    LYS H CE  1 
ATOM   7880  N  NZ  . LYS H  1 9   ? 74.320  11.071  -13.034 1.00 29.33 ? 9    LYS H NZ  1 
ATOM   7881  N  N   . GLY H  1 10  ? 80.809  11.103  -10.530 1.00 16.40 ? 10   GLY H N   1 
ATOM   7882  C  CA  . GLY H  1 10  ? 81.806  11.356  -9.519  1.00 19.14 ? 10   GLY H CA  1 
ATOM   7883  C  C   . GLY H  1 10  ? 81.602  12.727  -8.913  1.00 20.66 ? 10   GLY H C   1 
ATOM   7884  O  O   . GLY H  1 10  ? 80.488  13.268  -8.928  1.00 17.43 ? 10   GLY H O   1 
ATOM   7885  N  N   . ASP H  1 11  ? 82.690  13.286  -8.392  1.00 20.36 ? 11   ASP H N   1 
ATOM   7886  C  CA  . ASP H  1 11  ? 82.667  14.576  -7.706  1.00 22.32 ? 11   ASP H CA  1 
ATOM   7887  C  C   . ASP H  1 11  ? 83.039  15.725  -8.625  1.00 19.22 ? 11   ASP H C   1 
ATOM   7888  O  O   . ASP H  1 11  ? 82.936  16.887  -8.246  1.00 22.04 ? 11   ASP H O   1 
ATOM   7889  C  CB  . ASP H  1 11  ? 83.627  14.562  -6.514  1.00 21.58 ? 11   ASP H CB  1 
ATOM   7890  C  CG  . ASP H  1 11  ? 83.126  13.700  -5.380  1.00 27.30 ? 11   ASP H CG  1 
ATOM   7891  O  OD1 . ASP H  1 11  ? 81.914  13.771  -5.066  1.00 31.87 ? 11   ASP H OD1 1 
ATOM   7892  O  OD2 . ASP H  1 11  ? 83.941  12.953  -4.800  1.00 29.56 ? 11   ASP H OD2 1 
ATOM   7893  N  N   . GLY H  1 12  ? 83.493  15.389  -9.823  1.00 19.57 ? 12   GLY H N   1 
ATOM   7894  C  CA  . GLY H  1 12  ? 83.891  16.372  -10.814 1.00 17.36 ? 12   GLY H CA  1 
ATOM   7895  C  C   . GLY H  1 12  ? 82.959  16.312  -11.995 1.00 16.36 ? 12   GLY H C   1 
ATOM   7896  O  O   . GLY H  1 12  ? 81.783  15.982  -11.834 1.00 16.72 ? 12   GLY H O   1 
ATOM   7897  N  N   . PRO H  1 13  ? 83.484  16.610  -13.200 1.00 19.08 ? 13   PRO H N   1 
ATOM   7898  C  CA  . PRO H  1 13  ? 82.654  16.693  -14.408 1.00 14.70 ? 13   PRO H CA  1 
ATOM   7899  C  C   . PRO H  1 13  ? 82.458  15.367  -15.143 1.00 17.28 ? 13   PRO H C   1 
ATOM   7900  O  O   . PRO H  1 13  ? 81.719  15.337  -16.128 1.00 17.99 ? 13   PRO H O   1 
ATOM   7901  C  CB  . PRO H  1 13  ? 83.441  17.632  -15.311 1.00 15.70 ? 13   PRO H CB  1 
ATOM   7902  C  CG  . PRO H  1 13  ? 84.847  17.600  -14.816 1.00 15.12 ? 13   PRO H CG  1 
ATOM   7903  C  CD  . PRO H  1 13  ? 84.899  16.916  -13.481 1.00 17.38 ? 13   PRO H CD  1 
ATOM   7904  N  N   . VAL H  1 14  ? 83.106  14.296  -14.697 1.00 17.25 ? 14   VAL H N   1 
ATOM   7905  C  CA  . VAL H  1 14  ? 83.091  13.047  -15.456 1.00 16.82 ? 14   VAL H CA  1 
ATOM   7906  C  C   . VAL H  1 14  ? 81.799  12.267  -15.236 1.00 17.10 ? 14   VAL H C   1 
ATOM   7907  O  O   . VAL H  1 14  ? 81.435  11.958  -14.105 1.00 16.97 ? 14   VAL H O   1 
ATOM   7908  C  CB  . VAL H  1 14  ? 84.344  12.186  -15.158 1.00 14.57 ? 14   VAL H CB  1 
ATOM   7909  C  CG1 . VAL H  1 14  ? 84.297  10.891  -15.933 1.00 16.13 ? 14   VAL H CG1 1 
ATOM   7910  C  CG2 . VAL H  1 14  ? 85.607  12.968  -15.501 1.00 15.06 ? 14   VAL H CG2 1 
ATOM   7911  N  N   . GLN H  1 15  ? 81.099  11.983  -16.331 1.00 19.08 ? 15   GLN H N   1 
ATOM   7912  C  CA  . GLN H  1 15  ? 79.832  11.256  -16.301 1.00 19.06 ? 15   GLN H CA  1 
ATOM   7913  C  C   . GLN H  1 15  ? 79.653  10.459  -17.584 1.00 18.76 ? 15   GLN H C   1 
ATOM   7914  O  O   . GLN H  1 15  ? 80.117  10.865  -18.636 1.00 20.55 ? 15   GLN H O   1 
ATOM   7915  C  CB  . GLN H  1 15  ? 78.655  12.211  -16.092 1.00 20.76 ? 15   GLN H CB  1 
ATOM   7916  C  CG  . GLN H  1 15  ? 78.684  13.448  -16.956 1.00 22.84 ? 15   GLN H CG  1 
ATOM   7917  C  CD  . GLN H  1 15  ? 77.677  14.490  -16.505 1.00 25.19 ? 15   GLN H CD  1 
ATOM   7918  O  OE1 . GLN H  1 15  ? 77.709  15.643  -16.958 1.00 28.08 ? 15   GLN H OE1 1 
ATOM   7919  N  NE2 . GLN H  1 15  ? 76.772  14.090  -15.615 1.00 25.64 ? 15   GLN H NE2 1 
ATOM   7920  N  N   . GLY H  1 16  ? 78.985  9.318   -17.493 1.00 18.78 ? 16   GLY H N   1 
ATOM   7921  C  CA  . GLY H  1 16  ? 78.928  8.398   -18.609 1.00 17.32 ? 16   GLY H CA  1 
ATOM   7922  C  C   . GLY H  1 16  ? 77.982  7.235   -18.391 1.00 20.38 ? 16   GLY H C   1 
ATOM   7923  O  O   . GLY H  1 16  ? 77.570  6.954   -17.265 1.00 18.12 ? 16   GLY H O   1 
ATOM   7924  N  N   . ILE H  1 17  ? 77.621  6.581   -19.493 1.00 21.39 ? 17   ILE H N   1 
ATOM   7925  C  CA  . ILE H  1 17  ? 76.783  5.389   -19.477 1.00 21.10 ? 17   ILE H CA  1 
ATOM   7926  C  C   . ILE H  1 17  ? 77.492  4.280   -20.240 1.00 21.08 ? 17   ILE H C   1 
ATOM   7927  O  O   . ILE H  1 17  ? 77.829  4.443   -21.412 1.00 18.13 ? 17   ILE H O   1 
ATOM   7928  C  CB  . ILE H  1 17  ? 75.414  5.630   -20.144 1.00 21.95 ? 17   ILE H CB  1 
ATOM   7929  C  CG1 . ILE H  1 17  ? 74.642  6.724   -19.398 1.00 21.16 ? 17   ILE H CG1 1 
ATOM   7930  C  CG2 . ILE H  1 17  ? 74.631  4.325   -20.204 1.00 18.65 ? 17   ILE H CG2 1 
ATOM   7931  C  CD1 . ILE H  1 17  ? 73.478  7.275   -20.172 1.00 25.59 ? 17   ILE H CD1 1 
ATOM   7932  N  N   . ILE H  1 18  ? 77.735  3.165   -19.561 1.00 19.27 ? 18   ILE H N   1 
ATOM   7933  C  CA  . ILE H  1 18  ? 78.367  2.011   -20.180 1.00 20.09 ? 18   ILE H CA  1 
ATOM   7934  C  C   . ILE H  1 18  ? 77.386  0.850   -20.221 1.00 16.15 ? 18   ILE H C   1 
ATOM   7935  O  O   . ILE H  1 18  ? 76.748  0.530   -19.232 1.00 17.85 ? 18   ILE H O   1 
ATOM   7936  C  CB  . ILE H  1 18  ? 79.664  1.591   -19.435 1.00 17.43 ? 18   ILE H CB  1 
ATOM   7937  C  CG1 . ILE H  1 18  ? 80.645  2.768   -19.341 1.00 18.65 ? 18   ILE H CG1 1 
ATOM   7938  C  CG2 . ILE H  1 18  ? 80.315  0.389   -20.122 1.00 16.89 ? 18   ILE H CG2 1 
ATOM   7939  C  CD1 . ILE H  1 18  ? 81.129  3.304   -20.686 1.00 16.75 ? 18   ILE H CD1 1 
ATOM   7940  N  N   . ASN H  1 19  ? 77.265  0.233   -21.384 1.00 17.69 ? 19   ASN H N   1 
ATOM   7941  C  CA  . ASN H  1 19  ? 76.389  -0.909  -21.561 1.00 19.10 ? 19   ASN H CA  1 
ATOM   7942  C  C   . ASN H  1 19  ? 77.225  -2.168  -21.691 1.00 19.67 ? 19   ASN H C   1 
ATOM   7943  O  O   . ASN H  1 19  ? 78.371  -2.099  -22.115 1.00 20.61 ? 19   ASN H O   1 
ATOM   7944  C  CB  . ASN H  1 19  ? 75.540  -0.715  -22.811 1.00 21.17 ? 19   ASN H CB  1 
ATOM   7945  C  CG  . ASN H  1 19  ? 74.726  0.559   -22.764 1.00 21.31 ? 19   ASN H CG  1 
ATOM   7946  O  OD1 . ASN H  1 19  ? 73.758  0.659   -22.005 1.00 22.36 ? 19   ASN H OD1 1 
ATOM   7947  N  ND2 . ASN H  1 19  ? 75.105  1.539   -23.582 1.00 19.92 ? 19   ASN H ND2 1 
ATOM   7948  N  N   . PHE H  1 20  ? 76.660  -3.309  -21.304 1.00 21.25 ? 20   PHE H N   1 
ATOM   7949  C  CA  . PHE H  1 20  ? 77.329  -4.603  -21.430 1.00 20.34 ? 20   PHE H CA  1 
ATOM   7950  C  C   . PHE H  1 20  ? 76.357  -5.546  -22.107 1.00 23.40 ? 20   PHE H C   1 
ATOM   7951  O  O   . PHE H  1 20  ? 75.145  -5.397  -21.969 1.00 25.89 ? 20   PHE H O   1 
ATOM   7952  C  CB  . PHE H  1 20  ? 77.698  -5.178  -20.065 1.00 17.56 ? 20   PHE H CB  1 
ATOM   7953  C  CG  . PHE H  1 20  ? 78.380  -4.204  -19.156 1.00 18.27 ? 20   PHE H CG  1 
ATOM   7954  C  CD1 . PHE H  1 20  ? 77.666  -3.182  -18.543 1.00 19.93 ? 20   PHE H CD1 1 
ATOM   7955  C  CD2 . PHE H  1 20  ? 79.723  -4.316  -18.895 1.00 15.79 ? 20   PHE H CD2 1 
ATOM   7956  C  CE1 . PHE H  1 20  ? 78.296  -2.282  -17.695 1.00 19.55 ? 20   PHE H CE1 1 
ATOM   7957  C  CE2 . PHE H  1 20  ? 80.347  -3.417  -18.064 1.00 19.29 ? 20   PHE H CE2 1 
ATOM   7958  C  CZ  . PHE H  1 20  ? 79.633  -2.400  -17.466 1.00 17.63 ? 20   PHE H CZ  1 
ATOM   7959  N  N   . GLU H  1 21  ? 76.880  -6.507  -22.854 1.00 25.47 ? 21   GLU H N   1 
ATOM   7960  C  CA  . GLU H  1 21  ? 76.029  -7.483  -23.509 1.00 25.55 ? 21   GLU H CA  1 
ATOM   7961  C  C   . GLU H  1 21  ? 76.796  -8.774  -23.672 1.00 26.79 ? 21   GLU H C   1 
ATOM   7962  O  O   . GLU H  1 21  ? 77.895  -8.770  -24.225 1.00 26.42 ? 21   GLU H O   1 
ATOM   7963  C  CB  . GLU H  1 21  ? 75.554  -6.979  -24.869 1.00 27.72 ? 21   GLU H CB  1 
ATOM   7964  C  CG  . GLU H  1 21  ? 74.577  -7.929  -25.550 1.00 32.82 ? 21   GLU H CG  1 
ATOM   7965  C  CD  . GLU H  1 21  ? 73.961  -7.337  -26.797 1.00 44.32 ? 21   GLU H CD  1 
ATOM   7966  O  OE1 . GLU H  1 21  ? 74.004  -6.092  -26.950 1.00 47.08 ? 21   GLU H OE1 1 
ATOM   7967  O  OE2 . GLU H  1 21  ? 73.431  -8.117  -27.620 1.00 53.30 ? 21   GLU H OE2 1 
ATOM   7968  N  N   . GLN H  1 22  ? 76.223  -9.869  -23.166 1.00 26.76 ? 22   GLN H N   1 
ATOM   7969  C  CA  . GLN H  1 22  ? 76.850  -11.180 -23.251 1.00 25.42 ? 22   GLN H CA  1 
ATOM   7970  C  C   . GLN H  1 22  ? 75.863  -12.168 -23.829 1.00 26.27 ? 22   GLN H C   1 
ATOM   7971  O  O   . GLN H  1 22  ? 75.028  -12.689 -23.119 1.00 30.05 ? 22   GLN H O   1 
ATOM   7972  C  CB  . GLN H  1 22  ? 77.327  -11.645 -21.870 1.00 25.63 ? 22   GLN H CB  1 
ATOM   7973  C  CG  . GLN H  1 22  ? 78.247  -12.863 -21.901 1.00 23.43 ? 22   GLN H CG  1 
ATOM   7974  C  CD  . GLN H  1 22  ? 78.668  -13.304 -20.517 1.00 25.88 ? 22   GLN H CD  1 
ATOM   7975  O  OE1 . GLN H  1 22  ? 77.944  -13.109 -19.553 1.00 25.64 ? 22   GLN H OE1 1 
ATOM   7976  N  NE2 . GLN H  1 22  ? 79.842  -13.902 -20.413 1.00 23.78 ? 22   GLN H NE2 1 
ATOM   7977  N  N   . LYS H  1 23  ? 75.954  -12.415 -25.128 1.00 29.47 ? 23   LYS H N   1 
ATOM   7978  C  CA  . LYS H  1 23  ? 74.990  -13.275 -25.808 1.00 33.00 ? 23   LYS H CA  1 
ATOM   7979  C  C   . LYS H  1 23  ? 74.900  -14.680 -25.202 1.00 30.12 ? 23   LYS H C   1 
ATOM   7980  O  O   . LYS H  1 23  ? 73.822  -15.250 -25.096 1.00 33.31 ? 23   LYS H O   1 
ATOM   7981  C  CB  . LYS H  1 23  ? 75.313  -13.366 -27.305 1.00 34.62 ? 23   LYS H CB  1 
ATOM   7982  C  CG  . LYS H  1 23  ? 75.421  -12.020 -27.994 1.00 38.59 ? 23   LYS H CG  1 
ATOM   7983  C  CD  . LYS H  1 23  ? 74.074  -11.551 -28.535 1.00 47.61 ? 23   LYS H CD  1 
ATOM   7984  C  CE  . LYS H  1 23  ? 73.808  -12.100 -29.943 1.00 55.22 ? 23   LYS H CE  1 
ATOM   7985  N  NZ  . LYS H  1 23  ? 74.005  -13.586 -30.059 1.00 55.51 ? 23   LYS H NZ  1 
ATOM   7986  N  N   . GLU H  1 24  ? 76.031  -15.242 -24.806 1.00 28.77 ? 24   GLU H N   1 
ATOM   7987  C  CA  . GLU H  1 24  ? 76.049  -16.620 -24.354 1.00 27.64 ? 24   GLU H CA  1 
ATOM   7988  C  C   . GLU H  1 24  ? 76.595  -16.715 -22.949 1.00 29.40 ? 24   GLU H C   1 
ATOM   7989  O  O   . GLU H  1 24  ? 77.491  -15.970 -22.586 1.00 32.52 ? 24   GLU H O   1 
ATOM   7990  C  CB  . GLU H  1 24  ? 76.910  -17.463 -25.293 1.00 29.88 ? 24   GLU H CB  1 
ATOM   7991  C  CG  . GLU H  1 24  ? 76.371  -17.561 -26.722 1.00 34.87 ? 24   GLU H CG  1 
ATOM   7992  C  CD  . GLU H  1 24  ? 75.025  -18.289 -26.800 1.00 40.75 ? 24   GLU H CD  1 
ATOM   7993  O  OE1 . GLU H  1 24  ? 74.319  -18.126 -27.827 1.00 41.60 ? 24   GLU H OE1 1 
ATOM   7994  O  OE2 . GLU H  1 24  ? 74.676  -19.023 -25.836 1.00 37.14 ? 24   GLU H OE2 1 
ATOM   7995  N  N   . SER H  1 25  ? 76.047  -17.625 -22.156 1.00 28.89 ? 25   SER H N   1 
ATOM   7996  C  CA  . SER H  1 25  ? 76.605  -17.920 -20.851 1.00 30.34 ? 25   SER H CA  1 
ATOM   7997  C  C   . SER H  1 25  ? 78.115  -18.123 -20.999 1.00 32.73 ? 25   SER H C   1 
ATOM   7998  O  O   . SER H  1 25  ? 78.551  -18.985 -21.761 1.00 33.78 ? 25   SER H O   1 
ATOM   7999  C  CB  . SER H  1 25  ? 75.961  -19.186 -20.287 1.00 30.60 ? 25   SER H CB  1 
ATOM   8000  O  OG  . SER H  1 25  ? 76.798  -19.805 -19.316 1.00 34.77 ? 25   SER H OG  1 
ATOM   8001  N  N   . ASN H  1 26  ? 78.904  -17.314 -20.291 1.00 34.32 ? 26   ASN H N   1 
ATOM   8002  C  CA  . ASN H  1 26  ? 80.370  -17.435 -20.269 1.00 30.29 ? 26   ASN H CA  1 
ATOM   8003  C  C   . ASN H  1 26  ? 81.095  -17.100 -21.564 1.00 30.37 ? 26   ASN H C   1 
ATOM   8004  O  O   . ASN H  1 26  ? 82.285  -17.384 -21.709 1.00 30.35 ? 26   ASN H O   1 
ATOM   8005  C  CB  . ASN H  1 26  ? 80.808  -18.810 -19.760 1.00 34.55 ? 26   ASN H CB  1 
ATOM   8006  C  CG  . ASN H  1 26  ? 80.548  -18.982 -18.276 1.00 40.55 ? 26   ASN H CG  1 
ATOM   8007  O  OD1 . ASN H  1 26  ? 80.373  -17.996 -17.546 1.00 40.71 ? 26   ASN H OD1 1 
ATOM   8008  N  ND2 . ASN H  1 26  ? 80.509  -20.234 -17.819 1.00 40.43 ? 26   ASN H ND2 1 
ATOM   8009  N  N   . GLY H  1 27  ? 80.370  -16.491 -22.496 1.00 29.79 ? 27   GLY H N   1 
ATOM   8010  C  CA  . GLY H  1 27  ? 80.948  -16.024 -23.737 1.00 28.03 ? 27   GLY H CA  1 
ATOM   8011  C  C   . GLY H  1 27  ? 81.511  -14.621 -23.596 1.00 29.34 ? 27   GLY H C   1 
ATOM   8012  O  O   . GLY H  1 27  ? 81.643  -14.088 -22.485 1.00 27.28 ? 27   GLY H O   1 
ATOM   8013  N  N   . PRO H  1 28  ? 81.859  -14.012 -24.732 1.00 27.80 ? 28   PRO H N   1 
ATOM   8014  C  CA  . PRO H  1 28  ? 82.453  -12.675 -24.777 1.00 28.53 ? 28   PRO H CA  1 
ATOM   8015  C  C   . PRO H  1 28  ? 81.447  -11.606 -24.380 1.00 24.65 ? 28   PRO H C   1 
ATOM   8016  O  O   . PRO H  1 28  ? 80.293  -11.693 -24.763 1.00 25.01 ? 28   PRO H O   1 
ATOM   8017  C  CB  . PRO H  1 28  ? 82.827  -12.504 -26.258 1.00 31.56 ? 28   PRO H CB  1 
ATOM   8018  C  CG  . PRO H  1 28  ? 82.737  -13.875 -26.859 1.00 31.97 ? 28   PRO H CG  1 
ATOM   8019  C  CD  . PRO H  1 28  ? 81.721  -14.607 -26.070 1.00 29.19 ? 28   PRO H CD  1 
ATOM   8020  N  N   . VAL H  1 29  ? 81.894  -10.609 -23.630 1.00 22.62 ? 29   VAL H N   1 
ATOM   8021  C  CA  . VAL H  1 29  ? 81.057  -9.468  -23.291 1.00 26.96 ? 29   VAL H CA  1 
ATOM   8022  C  C   . VAL H  1 29  ? 81.428  -8.254  -24.163 1.00 25.18 ? 29   VAL H C   1 
ATOM   8023  O  O   . VAL H  1 29  ? 82.581  -7.836  -24.187 1.00 25.43 ? 29   VAL H O   1 
ATOM   8024  C  CB  . VAL H  1 29  ? 81.197  -9.081  -21.785 1.00 22.52 ? 29   VAL H CB  1 
ATOM   8025  C  CG1 . VAL H  1 29  ? 80.185  -8.004  -21.413 1.00 19.87 ? 29   VAL H CG1 1 
ATOM   8026  C  CG2 . VAL H  1 29  ? 81.055  -10.307 -20.879 1.00 19.12 ? 29   VAL H CG2 1 
ATOM   8027  N  N   . LYS H  1 30  ? 80.457  -7.697  -24.878 1.00 22.22 ? 30   LYS H N   1 
ATOM   8028  C  CA  . LYS H  1 30  ? 80.645  -6.407  -25.528 1.00 22.03 ? 30   LYS H CA  1 
ATOM   8029  C  C   . LYS H  1 30  ? 80.326  -5.271  -24.555 1.00 23.57 ? 30   LYS H C   1 
ATOM   8030  O  O   . LYS H  1 30  ? 79.239  -5.221  -23.972 1.00 24.15 ? 30   LYS H O   1 
ATOM   8031  C  CB  . LYS H  1 30  ? 79.765  -6.305  -26.774 1.00 28.03 ? 30   LYS H CB  1 
ATOM   8032  C  CG  . LYS H  1 30  ? 80.063  -5.112  -27.683 1.00 32.10 ? 30   LYS H CG  1 
ATOM   8033  C  CD  . LYS H  1 30  ? 79.646  -5.412  -29.127 1.00 41.14 ? 30   LYS H CD  1 
ATOM   8034  C  CE  . LYS H  1 30  ? 80.040  -4.284  -30.082 1.00 44.32 ? 30   LYS H CE  1 
ATOM   8035  N  NZ  . LYS H  1 30  ? 79.244  -3.038  -29.864 1.00 37.96 ? 30   LYS H NZ  1 
ATOM   8036  N  N   . VAL H  1 31  ? 81.283  -4.365  -24.381 1.00 21.26 ? 31   VAL H N   1 
ATOM   8037  C  CA  . VAL H  1 31  ? 81.163  -3.256  -23.437 1.00 21.87 ? 31   VAL H CA  1 
ATOM   8038  C  C   . VAL H  1 31  ? 81.278  -1.940  -24.211 1.00 22.23 ? 31   VAL H C   1 
ATOM   8039  O  O   . VAL H  1 31  ? 82.316  -1.653  -24.803 1.00 23.89 ? 31   VAL H O   1 
ATOM   8040  C  CB  . VAL H  1 31  ? 82.263  -3.337  -22.333 1.00 20.50 ? 31   VAL H CB  1 
ATOM   8041  C  CG1 . VAL H  1 31  ? 82.129  -2.205  -21.342 1.00 19.69 ? 31   VAL H CG1 1 
ATOM   8042  C  CG2 . VAL H  1 31  ? 82.230  -4.689  -21.622 1.00 17.43 ? 31   VAL H CG2 1 
ATOM   8043  N  N   . TRP H  1 32  ? 80.210  -1.149  -24.236 1.00 20.68 ? 32   TRP H N   1 
ATOM   8044  C  CA  . TRP H  1 32  ? 80.200  0.034   -25.081 1.00 19.84 ? 32   TRP H CA  1 
ATOM   8045  C  C   . TRP H  1 32  ? 79.414  1.161   -24.443 1.00 18.24 ? 32   TRP H C   1 
ATOM   8046  O  O   . TRP H  1 32  ? 78.508  0.920   -23.673 1.00 18.60 ? 32   TRP H O   1 
ATOM   8047  C  CB  . TRP H  1 32  ? 79.603  -0.296  -26.454 1.00 24.82 ? 32   TRP H CB  1 
ATOM   8048  C  CG  . TRP H  1 32  ? 78.086  -0.374  -26.466 1.00 24.52 ? 32   TRP H CG  1 
ATOM   8049  C  CD1 . TRP H  1 32  ? 77.211  0.629   -26.795 1.00 25.26 ? 32   TRP H CD1 1 
ATOM   8050  C  CD2 . TRP H  1 32  ? 77.284  -1.509  -26.138 1.00 21.21 ? 32   TRP H CD2 1 
ATOM   8051  N  NE1 . TRP H  1 32  ? 75.916  0.180   -26.689 1.00 26.20 ? 32   TRP H NE1 1 
ATOM   8052  C  CE2 . TRP H  1 32  ? 75.937  -1.130  -26.285 1.00 25.07 ? 32   TRP H CE2 1 
ATOM   8053  C  CE3 . TRP H  1 32  ? 77.574  -2.812  -25.731 1.00 24.33 ? 32   TRP H CE3 1 
ATOM   8054  C  CZ2 . TRP H  1 32  ? 74.882  -2.010  -26.039 1.00 27.85 ? 32   TRP H CZ2 1 
ATOM   8055  C  CZ3 . TRP H  1 32  ? 76.526  -3.682  -25.490 1.00 25.78 ? 32   TRP H CZ3 1 
ATOM   8056  C  CH2 . TRP H  1 32  ? 75.196  -3.278  -25.648 1.00 24.99 ? 32   TRP H CH2 1 
ATOM   8057  N  N   . GLY H  1 33  ? 79.761  2.394   -24.780 1.00 18.52 ? 33   GLY H N   1 
ATOM   8058  C  CA  . GLY H  1 33  ? 79.053  3.542   -24.255 1.00 18.53 ? 33   GLY H CA  1 
ATOM   8059  C  C   . GLY H  1 33  ? 79.830  4.816   -24.481 1.00 19.55 ? 33   GLY H C   1 
ATOM   8060  O  O   . GLY H  1 33  ? 80.613  4.904   -25.418 1.00 23.63 ? 33   GLY H O   1 
ATOM   8061  N  N   . SER H  1 34  ? 79.624  5.797   -23.611 1.00 20.50 ? 34   SER H N   1 
ATOM   8062  C  CA  . SER H  1 34  ? 80.241  7.111   -23.752 1.00 20.48 ? 34   SER H CA  1 
ATOM   8063  C  C   . SER H  1 34  ? 80.545  7.736   -22.387 1.00 21.35 ? 34   SER H C   1 
ATOM   8064  O  O   . SER H  1 34  ? 79.742  7.639   -21.460 1.00 19.69 ? 34   SER H O   1 
ATOM   8065  C  CB  . SER H  1 34  ? 79.328  8.035   -24.554 1.00 22.39 ? 34   SER H CB  1 
ATOM   8066  O  OG  . SER H  1 34  ? 79.748  9.383   -24.445 1.00 28.08 ? 34   SER H OG  1 
ATOM   8067  N  N   . ILE H  1 35  ? 81.721  8.354   -22.269 1.00 21.29 ? 35   ILE H N   1 
ATOM   8068  C  CA  . ILE H  1 35  ? 82.097  9.111   -21.082 1.00 17.68 ? 35   ILE H CA  1 
ATOM   8069  C  C   . ILE H  1 35  ? 82.438  10.539  -21.509 1.00 19.39 ? 35   ILE H C   1 
ATOM   8070  O  O   . ILE H  1 35  ? 83.077  10.752  -22.538 1.00 22.35 ? 35   ILE H O   1 
ATOM   8071  C  CB  . ILE H  1 35  ? 83.279  8.450   -20.331 1.00 17.45 ? 35   ILE H CB  1 
ATOM   8072  C  CG1 . ILE H  1 35  ? 83.018  6.947   -20.178 1.00 18.10 ? 35   ILE H CG1 1 
ATOM   8073  C  CG2 . ILE H  1 35  ? 83.493  9.105   -18.963 1.00 15.57 ? 35   ILE H CG2 1 
ATOM   8074  C  CD1 . ILE H  1 35  ? 84.131  6.174   -19.494 1.00 17.77 ? 35   ILE H CD1 1 
ATOM   8075  N  N   . LYS H  1 36  ? 81.978  11.523  -20.752 1.00 18.61 ? 36   LYS H N   1 
ATOM   8076  C  CA  . LYS H  1 36  ? 82.269  12.908  -21.090 1.00 19.86 ? 36   LYS H CA  1 
ATOM   8077  C  C   . LYS H  1 36  ? 82.910  13.569  -19.879 1.00 17.91 ? 36   LYS H C   1 
ATOM   8078  O  O   . LYS H  1 36  ? 82.945  12.972  -18.805 1.00 16.39 ? 36   LYS H O   1 
ATOM   8079  C  CB  . LYS H  1 36  ? 80.995  13.648  -21.542 1.00 24.73 ? 36   LYS H CB  1 
ATOM   8080  C  CG  . LYS H  1 36  ? 80.084  14.130  -20.411 1.00 23.84 ? 36   LYS H CG  1 
ATOM   8081  C  CD  . LYS H  1 36  ? 78.914  14.984  -20.922 1.00 24.26 ? 36   LYS H CD  1 
ATOM   8082  C  CE  . LYS H  1 36  ? 77.597  14.230  -20.857 1.00 30.15 ? 36   LYS H CE  1 
ATOM   8083  N  NZ  . LYS H  1 36  ? 76.406  15.143  -20.806 1.00 28.68 ? 36   LYS H NZ  1 
ATOM   8084  N  N   . GLY H  1 37  ? 83.431  14.782  -20.052 1.00 19.47 ? 37   GLY H N   1 
ATOM   8085  C  CA  . GLY H  1 37  ? 84.083  15.509  -18.965 1.00 18.12 ? 37   GLY H CA  1 
ATOM   8086  C  C   . GLY H  1 37  ? 85.531  15.122  -18.696 1.00 17.08 ? 37   GLY H C   1 
ATOM   8087  O  O   . GLY H  1 37  ? 86.118  15.563  -17.704 1.00 15.46 ? 37   GLY H O   1 
ATOM   8088  N  N   . LEU H  1 38  ? 86.106  14.316  -19.596 1.00 20.15 ? 38   LEU H N   1 
ATOM   8089  C  CA  . LEU H  1 38  ? 87.458  13.749  -19.443 1.00 17.28 ? 38   LEU H CA  1 
ATOM   8090  C  C   . LEU H  1 38  ? 88.543  14.595  -20.111 1.00 18.43 ? 38   LEU H C   1 
ATOM   8091  O  O   . LEU H  1 38  ? 88.280  15.312  -21.077 1.00 21.89 ? 38   LEU H O   1 
ATOM   8092  C  CB  . LEU H  1 38  ? 87.516  12.332  -20.041 1.00 15.93 ? 38   LEU H CB  1 
ATOM   8093  C  CG  . LEU H  1 38  ? 86.775  11.168  -19.379 1.00 13.88 ? 38   LEU H CG  1 
ATOM   8094  C  CD1 . LEU H  1 38  ? 86.706  10.001  -20.332 1.00 14.65 ? 38   LEU H CD1 1 
ATOM   8095  C  CD2 . LEU H  1 38  ? 87.454  10.764  -18.077 1.00 14.48 ? 38   LEU H CD2 1 
ATOM   8096  N  N   . THR H  1 39  ? 89.769  14.503  -19.612 1.00 18.00 ? 39   THR H N   1 
ATOM   8097  C  CA  . THR H  1 39  ? 90.882  15.153  -20.279 1.00 18.89 ? 39   THR H CA  1 
ATOM   8098  C  C   . THR H  1 39  ? 91.291  14.323  -21.499 1.00 21.18 ? 39   THR H C   1 
ATOM   8099  O  O   . THR H  1 39  ? 91.050  13.116  -21.558 1.00 19.96 ? 39   THR H O   1 
ATOM   8100  C  CB  . THR H  1 39  ? 92.078  15.383  -19.330 1.00 20.84 ? 39   THR H CB  1 
ATOM   8101  O  OG1 . THR H  1 39  ? 92.564  14.129  -18.842 1.00 21.64 ? 39   THR H OG1 1 
ATOM   8102  C  CG2 . THR H  1 39  ? 91.667  16.246  -18.150 1.00 20.34 ? 39   THR H CG2 1 
ATOM   8103  N  N   . GLU H  1 40  ? 91.879  14.985  -22.486 1.00 22.86 ? 40   GLU H N   1 
ATOM   8104  C  CA  . GLU H  1 40  ? 92.238  14.331  -23.727 1.00 22.97 ? 40   GLU H CA  1 
ATOM   8105  C  C   . GLU H  1 40  ? 93.248  13.233  -23.473 1.00 21.38 ? 40   GLU H C   1 
ATOM   8106  O  O   . GLU H  1 40  ? 94.220  13.450  -22.763 1.00 25.25 ? 40   GLU H O   1 
ATOM   8107  C  CB  . GLU H  1 40  ? 92.826  15.343  -24.700 1.00 24.16 ? 40   GLU H CB  1 
ATOM   8108  C  CG  . GLU H  1 40  ? 93.013  14.791  -26.101 1.00 28.09 ? 40   GLU H CG  1 
ATOM   8109  C  CD  . GLU H  1 40  ? 93.550  15.833  -27.062 1.00 33.01 ? 40   GLU H CD  1 
ATOM   8110  O  OE1 . GLU H  1 40  ? 93.927  16.930  -26.586 1.00 35.50 ? 40   GLU H OE1 1 
ATOM   8111  O  OE2 . GLU H  1 40  ? 93.595  15.556  -28.282 1.00 34.40 ? 40   GLU H OE2 1 
ATOM   8112  N  N   . GLY H  1 41  ? 93.011  12.050  -24.031 1.00 19.22 ? 41   GLY H N   1 
ATOM   8113  C  CA  . GLY H  1 41  ? 93.987  10.985  -23.953 1.00 17.71 ? 41   GLY H CA  1 
ATOM   8114  C  C   . GLY H  1 41  ? 93.505  9.713   -23.304 1.00 19.17 ? 41   GLY H C   1 
ATOM   8115  O  O   . GLY H  1 41  ? 92.328  9.407   -23.336 1.00 17.38 ? 41   GLY H O   1 
ATOM   8116  N  N   . LEU H  1 42  ? 94.442  8.978   -22.705 1.00 24.74 ? 42   LEU H N   1 
ATOM   8117  C  CA  . LEU H  1 42  ? 94.176  7.652   -22.138 1.00 22.87 ? 42   LEU H CA  1 
ATOM   8118  C  C   . LEU H  1 42  ? 93.859  7.682   -20.644 1.00 20.29 ? 42   LEU H C   1 
ATOM   8119  O  O   . LEU H  1 42  ? 94.517  8.367   -19.865 1.00 20.20 ? 42   LEU H O   1 
ATOM   8120  C  CB  . LEU H  1 42  ? 95.339  6.675   -22.399 1.00 22.12 ? 42   LEU H CB  1 
ATOM   8121  C  CG  . LEU H  1 42  ? 95.733  6.256   -23.822 1.00 22.03 ? 42   LEU H CG  1 
ATOM   8122  C  CD1 . LEU H  1 42  ? 96.967  5.382   -23.741 1.00 24.51 ? 42   LEU H CD1 1 
ATOM   8123  C  CD2 . LEU H  1 42  ? 94.628  5.526   -24.565 1.00 20.36 ? 42   LEU H CD2 1 
ATOM   8124  N  N   . HIS H  1 43  ? 92.829  6.922   -20.275 1.00 20.41 ? 43   HIS H N   1 
ATOM   8125  C  CA  . HIS H  1 43  ? 92.333  6.830   -18.918 1.00 17.83 ? 43   HIS H CA  1 
ATOM   8126  C  C   . HIS H  1 43  ? 92.070  5.365   -18.585 1.00 17.50 ? 43   HIS H C   1 
ATOM   8127  O  O   . HIS H  1 43  ? 91.377  4.678   -19.320 1.00 18.42 ? 43   HIS H O   1 
ATOM   8128  C  CB  . HIS H  1 43  ? 91.024  7.607   -18.806 1.00 18.89 ? 43   HIS H CB  1 
ATOM   8129  C  CG  . HIS H  1 43  ? 91.184  9.085   -18.964 1.00 18.29 ? 43   HIS H CG  1 
ATOM   8130  N  ND1 . HIS H  1 43  ? 91.492  9.915   -17.908 1.00 16.53 ? 43   HIS H ND1 1 
ATOM   8131  C  CD2 . HIS H  1 43  ? 91.068  9.883   -20.052 1.00 17.18 ? 43   HIS H CD2 1 
ATOM   8132  C  CE1 . HIS H  1 43  ? 91.573  11.159  -18.341 1.00 18.39 ? 43   HIS H CE1 1 
ATOM   8133  N  NE2 . HIS H  1 43  ? 91.319  11.169  -19.636 1.00 16.93 ? 43   HIS H NE2 1 
ATOM   8134  N  N   . GLY H  1 44  ? 92.608  4.886   -17.474 1.00 18.10 ? 44   GLY H N   1 
ATOM   8135  C  CA  . GLY H  1 44  ? 92.351  3.523   -17.057 1.00 16.74 ? 44   GLY H CA  1 
ATOM   8136  C  C   . GLY H  1 44  ? 90.868  3.259   -16.879 1.00 18.09 ? 44   GLY H C   1 
ATOM   8137  O  O   . GLY H  1 44  ? 90.127  4.118   -16.422 1.00 16.78 ? 44   GLY H O   1 
ATOM   8138  N  N   . PHE H  1 45  ? 90.444  2.053   -17.243 1.00 18.89 ? 45   PHE H N   1 
ATOM   8139  C  CA  . PHE H  1 45  ? 89.040  1.676   -17.279 1.00 16.75 ? 45   PHE H CA  1 
ATOM   8140  C  C   . PHE H  1 45  ? 88.904  0.275   -16.675 1.00 17.53 ? 45   PHE H C   1 
ATOM   8141  O  O   . PHE H  1 45  ? 89.238  -0.709  -17.318 1.00 16.89 ? 45   PHE H O   1 
ATOM   8142  C  CB  . PHE H  1 45  ? 88.560  1.698   -18.728 1.00 17.17 ? 45   PHE H CB  1 
ATOM   8143  C  CG  . PHE H  1 45  ? 87.061  1.600   -18.891 1.00 18.67 ? 45   PHE H CG  1 
ATOM   8144  C  CD1 . PHE H  1 45  ? 86.206  2.515   -18.270 1.00 20.00 ? 45   PHE H CD1 1 
ATOM   8145  C  CD2 . PHE H  1 45  ? 86.505  0.613   -19.705 1.00 19.94 ? 45   PHE H CD2 1 
ATOM   8146  C  CE1 . PHE H  1 45  ? 84.812  2.431   -18.438 1.00 20.72 ? 45   PHE H CE1 1 
ATOM   8147  C  CE2 . PHE H  1 45  ? 85.102  0.521   -19.887 1.00 21.40 ? 45   PHE H CE2 1 
ATOM   8148  C  CZ  . PHE H  1 45  ? 84.261  1.429   -19.256 1.00 19.60 ? 45   PHE H CZ  1 
ATOM   8149  N  N   . HIS H  1 46  ? 88.446  0.185   -15.425 1.00 18.17 ? 46   HIS H N   1 
ATOM   8150  C  CA  . HIS H  1 46  ? 88.535  -1.082  -14.697 1.00 18.24 ? 46   HIS H CA  1 
ATOM   8151  C  C   . HIS H  1 46  ? 87.269  -1.428  -13.937 1.00 19.70 ? 46   HIS H C   1 
ATOM   8152  O  O   . HIS H  1 46  ? 86.541  -0.544  -13.476 1.00 19.35 ? 46   HIS H O   1 
ATOM   8153  C  CB  . HIS H  1 46  ? 89.687  -1.077  -13.683 1.00 17.63 ? 46   HIS H CB  1 
ATOM   8154  C  CG  . HIS H  1 46  ? 90.975  -0.540  -14.214 1.00 16.07 ? 46   HIS H CG  1 
ATOM   8155  N  ND1 . HIS H  1 46  ? 91.607  0.547   -13.657 1.00 18.19 ? 46   HIS H ND1 1 
ATOM   8156  C  CD2 . HIS H  1 46  ? 91.753  -0.945  -15.243 1.00 17.79 ? 46   HIS H CD2 1 
ATOM   8157  C  CE1 . HIS H  1 46  ? 92.721  0.794   -14.323 1.00 19.19 ? 46   HIS H CE1 1 
ATOM   8158  N  NE2 . HIS H  1 46  ? 92.830  -0.097  -15.292 1.00 18.56 ? 46   HIS H NE2 1 
ATOM   8159  N  N   . VAL H  1 47  ? 87.036  -2.729  -13.798 1.00 17.86 ? 47   VAL H N   1 
ATOM   8160  C  CA  . VAL H  1 47  ? 86.011  -3.236  -12.906 1.00 19.39 ? 47   VAL H CA  1 
ATOM   8161  C  C   . VAL H  1 47  ? 86.587  -3.413  -11.500 1.00 20.03 ? 47   VAL H C   1 
ATOM   8162  O  O   . VAL H  1 47  ? 87.569  -4.143  -11.290 1.00 20.80 ? 47   VAL H O   1 
ATOM   8163  C  CB  . VAL H  1 47  ? 85.413  -4.560  -13.413 1.00 19.42 ? 47   VAL H CB  1 
ATOM   8164  C  CG1 . VAL H  1 47  ? 84.289  -5.022  -12.485 1.00 16.97 ? 47   VAL H CG1 1 
ATOM   8165  C  CG2 . VAL H  1 47  ? 84.922  -4.401  -14.857 1.00 16.53 ? 47   VAL H CG2 1 
ATOM   8166  N  N   . HIS H  1 48  ? 85.984  -2.718  -10.542 1.00 19.07 ? 48   HIS H N   1 
ATOM   8167  C  CA  . HIS H  1 48  ? 86.421  -2.783  -9.160  1.00 18.03 ? 48   HIS H CA  1 
ATOM   8168  C  C   . HIS H  1 48  ? 85.548  -3.752  -8.379  1.00 18.25 ? 48   HIS H C   1 
ATOM   8169  O  O   . HIS H  1 48  ? 84.425  -4.034  -8.767  1.00 17.72 ? 48   HIS H O   1 
ATOM   8170  C  CB  . HIS H  1 48  ? 86.438  -1.388  -8.528  1.00 18.21 ? 48   HIS H CB  1 
ATOM   8171  C  CG  . HIS H  1 48  ? 87.603  -0.545  -8.962  1.00 19.40 ? 48   HIS H CG  1 
ATOM   8172  N  ND1 . HIS H  1 48  ? 88.571  -0.097  -8.085  1.00 18.19 ? 48   HIS H ND1 1 
ATOM   8173  C  CD2 . HIS H  1 48  ? 87.959  -0.074  -10.182 1.00 17.80 ? 48   HIS H CD2 1 
ATOM   8174  C  CE1 . HIS H  1 48  ? 89.467  0.613   -8.750  1.00 19.25 ? 48   HIS H CE1 1 
ATOM   8175  N  NE2 . HIS H  1 48  ? 89.113  0.653   -10.020 1.00 15.93 ? 48   HIS H NE2 1 
ATOM   8176  N  N   . GLU H  1 49  ? 86.078  -4.252  -7.270  1.00 20.37 ? 49   GLU H N   1 
ATOM   8177  C  CA  . GLU H  1 49  ? 85.465  -5.365  -6.551  1.00 21.92 ? 49   GLU H CA  1 
ATOM   8178  C  C   . GLU H  1 49  ? 84.028  -5.137  -6.009  1.00 23.02 ? 49   GLU H C   1 
ATOM   8179  O  O   . GLU H  1 49  ? 83.129  -5.982  -6.195  1.00 20.55 ? 49   GLU H O   1 
ATOM   8180  C  CB  . GLU H  1 49  ? 86.400  -5.840  -5.426  1.00 20.79 ? 49   GLU H CB  1 
ATOM   8181  C  CG  . GLU H  1 49  ? 85.968  -7.176  -4.852  1.00 22.93 ? 49   GLU H CG  1 
ATOM   8182  C  CD  . GLU H  1 49  ? 86.874  -7.699  -3.763  1.00 25.83 ? 49   GLU H CD  1 
ATOM   8183  O  OE1 . GLU H  1 49  ? 87.950  -7.094  -3.512  1.00 28.31 ? 49   GLU H OE1 1 
ATOM   8184  O  OE2 . GLU H  1 49  ? 86.498  -8.729  -3.162  1.00 26.34 ? 49   GLU H OE2 1 
ATOM   8185  N  N   . PHE H  1 50  ? 83.811  -4.008  -5.336  1.00 19.44 ? 50   PHE H N   1 
ATOM   8186  C  CA  . PHE H  1 50  ? 82.564  -3.805  -4.604  1.00 20.44 ? 50   PHE H CA  1 
ATOM   8187  C  C   . PHE H  1 50  ? 81.608  -2.791  -5.253  1.00 21.24 ? 50   PHE H C   1 
ATOM   8188  O  O   . PHE H  1 50  ? 82.046  -1.766  -5.772  1.00 20.11 ? 50   PHE H O   1 
ATOM   8189  C  CB  . PHE H  1 50  ? 82.864  -3.406  -3.158  1.00 22.48 ? 50   PHE H CB  1 
ATOM   8190  C  CG  . PHE H  1 50  ? 83.773  -4.369  -2.434  1.00 23.41 ? 50   PHE H CG  1 
ATOM   8191  C  CD1 . PHE H  1 50  ? 83.432  -5.704  -2.307  1.00 23.31 ? 50   PHE H CD1 1 
ATOM   8192  C  CD2 . PHE H  1 50  ? 84.957  -3.932  -1.865  1.00 22.78 ? 50   PHE H CD2 1 
ATOM   8193  C  CE1 . PHE H  1 50  ? 84.259  -6.579  -1.640  1.00 24.94 ? 50   PHE H CE1 1 
ATOM   8194  C  CE2 . PHE H  1 50  ? 85.788  -4.806  -1.196  1.00 24.43 ? 50   PHE H CE2 1 
ATOM   8195  C  CZ  . PHE H  1 50  ? 85.438  -6.131  -1.084  1.00 24.22 ? 50   PHE H CZ  1 
ATOM   8196  N  N   . GLY H  1 51  ? 80.307  -3.095  -5.230  1.00 20.35 ? 51   GLY H N   1 
ATOM   8197  C  CA  . GLY H  1 51  ? 79.288  -2.160  -5.668  1.00 16.71 ? 51   GLY H CA  1 
ATOM   8198  C  C   . GLY H  1 51  ? 78.867  -1.288  -4.500  1.00 19.11 ? 51   GLY H C   1 
ATOM   8199  O  O   . GLY H  1 51  ? 77.675  -1.176  -4.176  1.00 17.66 ? 51   GLY H O   1 
ATOM   8200  N  N   . ASP H  1 52  ? 79.872  -0.677  -3.872  1.00 20.59 ? 52   ASP H N   1 
ATOM   8201  C  CA  . ASP H  1 52  ? 79.712  0.113   -2.661  1.00 19.59 ? 52   ASP H CA  1 
ATOM   8202  C  C   . ASP H  1 52  ? 80.116  1.561   -2.927  1.00 21.19 ? 52   ASP H C   1 
ATOM   8203  O  O   . ASP H  1 52  ? 81.292  1.852   -3.114  1.00 23.00 ? 52   ASP H O   1 
ATOM   8204  C  CB  . ASP H  1 52  ? 80.572  -0.489  -1.546  1.00 19.31 ? 52   ASP H CB  1 
ATOM   8205  C  CG  . ASP H  1 52  ? 80.311  0.145   -0.188  1.00 22.13 ? 52   ASP H CG  1 
ATOM   8206  O  OD1 . ASP H  1 52  ? 79.825  1.293   -0.166  1.00 21.45 ? 52   ASP H OD1 1 
ATOM   8207  O  OD2 . ASP H  1 52  ? 80.593  -0.499  0.855   1.00 20.79 ? 52   ASP H OD2 1 
ATOM   8208  N  N   . ASN H  1 53  ? 79.135  2.461   -2.952  1.00 20.18 ? 53   ASN H N   1 
ATOM   8209  C  CA  . ASN H  1 53  ? 79.376  3.885   -3.189  1.00 21.30 ? 53   ASN H CA  1 
ATOM   8210  C  C   . ASN H  1 53  ? 79.220  4.711   -1.907  1.00 22.17 ? 53   ASN H C   1 
ATOM   8211  O  O   . ASN H  1 53  ? 79.109  5.938   -1.960  1.00 20.83 ? 53   ASN H O   1 
ATOM   8212  C  CB  . ASN H  1 53  ? 78.408  4.412   -4.260  1.00 20.36 ? 53   ASN H CB  1 
ATOM   8213  C  CG  . ASN H  1 53  ? 78.881  5.709   -4.903  1.00 23.84 ? 53   ASN H CG  1 
ATOM   8214  O  OD1 . ASN H  1 53  ? 79.914  5.743   -5.568  1.00 26.53 ? 53   ASN H OD1 1 
ATOM   8215  N  ND2 . ASN H  1 53  ? 78.109  6.775   -4.732  1.00 22.99 ? 53   ASN H ND2 1 
ATOM   8216  N  N   . THR H  1 54  ? 79.215  4.033   -0.759  1.00 21.43 ? 54   THR H N   1 
ATOM   8217  C  CA  . THR H  1 54  ? 78.904  4.675   0.516   1.00 21.15 ? 54   THR H CA  1 
ATOM   8218  C  C   . THR H  1 54  ? 79.852  5.806   0.832   1.00 22.18 ? 54   THR H C   1 
ATOM   8219  O  O   . THR H  1 54  ? 79.460  6.790   1.436   1.00 26.37 ? 54   THR H O   1 
ATOM   8220  C  CB  . THR H  1 54  ? 78.891  3.683   1.692   1.00 20.57 ? 54   THR H CB  1 
ATOM   8221  O  OG1 . THR H  1 54  ? 80.129  2.972   1.739   1.00 24.61 ? 54   THR H OG1 1 
ATOM   8222  C  CG2 . THR H  1 54  ? 77.746  2.691   1.541   1.00 22.00 ? 54   THR H CG2 1 
ATOM   8223  N  N   . ALA H  1 55  ? 81.100  5.679   0.406   1.00 23.98 ? 55   ALA H N   1 
ATOM   8224  C  CA  . ALA H  1 55  ? 82.047  6.777   0.555   1.00 23.66 ? 55   ALA H CA  1 
ATOM   8225  C  C   . ALA H  1 55  ? 82.628  7.218   -0.796  1.00 24.54 ? 55   ALA H C   1 
ATOM   8226  O  O   . ALA H  1 55  ? 83.807  7.535   -0.888  1.00 32.26 ? 55   ALA H O   1 
ATOM   8227  C  CB  . ALA H  1 55  ? 83.159  6.382   1.523   1.00 23.71 ? 55   ALA H CB  1 
ATOM   8228  N  N   . GLY H  1 56  ? 81.811  7.244   -1.843  1.00 22.56 ? 56   GLY H N   1 
ATOM   8229  C  CA  . GLY H  1 56  ? 82.296  7.620   -3.163  1.00 21.35 ? 56   GLY H CA  1 
ATOM   8230  C  C   . GLY H  1 56  ? 82.979  6.461   -3.868  1.00 25.10 ? 56   GLY H C   1 
ATOM   8231  O  O   . GLY H  1 56  ? 82.762  5.305   -3.513  1.00 26.20 ? 56   GLY H O   1 
ATOM   8232  N  N   . CYS H  1 57  ? 83.816  6.757   -4.858  1.00 24.92 ? 57   CYS H N   1 
ATOM   8233  C  CA  . CYS H  1 57  ? 84.483  5.701   -5.619  1.00 24.56 ? 57   CYS H CA  1 
ATOM   8234  C  C   . CYS H  1 57  ? 85.462  4.872   -4.777  1.00 23.95 ? 57   CYS H C   1 
ATOM   8235  O  O   . CYS H  1 57  ? 85.755  3.723   -5.107  1.00 23.69 ? 57   CYS H O   1 
ATOM   8236  C  CB  . CYS H  1 57  ? 85.205  6.280   -6.842  1.00 25.58 ? 57   CYS H CB  1 
ATOM   8237  S  SG  . CYS H  1 57  ? 84.141  7.088   -8.071  1.00 28.58 ? 57   CYS H SG  1 
ATOM   8238  N  N   . THR H  1 58  ? 85.970  5.464   -3.703  1.00 22.25 ? 58   THR H N   1 
ATOM   8239  C  CA  . THR H  1 58  ? 86.907  4.795   -2.801  1.00 24.35 ? 58   THR H CA  1 
ATOM   8240  C  C   . THR H  1 58  ? 86.433  3.415   -2.305  1.00 25.49 ? 58   THR H C   1 
ATOM   8241  O  O   . THR H  1 58  ? 87.175  2.429   -2.373  1.00 23.48 ? 58   THR H O   1 
ATOM   8242  C  CB  . THR H  1 58  ? 87.225  5.709   -1.593  1.00 26.06 ? 58   THR H CB  1 
ATOM   8243  O  OG1 . THR H  1 58  ? 88.141  6.731   -2.006  1.00 32.05 ? 58   THR H OG1 1 
ATOM   8244  C  CG2 . THR H  1 58  ? 87.839  4.923   -0.449  1.00 26.78 ? 58   THR H CG2 1 
ATOM   8245  N  N   . SER H  1 59  ? 85.194  3.360   -1.814  1.00 24.36 ? 59   SER H N   1 
ATOM   8246  C  CA  . SER H  1 59  ? 84.623  2.151   -1.217  1.00 23.29 ? 59   SER H CA  1 
ATOM   8247  C  C   . SER H  1 59  ? 84.365  1.002   -2.198  1.00 22.33 ? 59   SER H C   1 
ATOM   8248  O  O   . SER H  1 59  ? 83.949  -0.087  -1.800  1.00 24.14 ? 59   SER H O   1 
ATOM   8249  C  CB  . SER H  1 59  ? 83.346  2.496   -0.450  1.00 24.08 ? 59   SER H CB  1 
ATOM   8250  O  OG  . SER H  1 59  ? 82.681  3.583   -1.065  1.00 24.59 ? 59   SER H OG  1 
ATOM   8251  N  N   . ALA H  1 60  ? 84.632  1.239   -3.474  1.00 22.04 ? 60   ALA H N   1 
ATOM   8252  C  CA  . ALA H  1 60  ? 84.522  0.187   -4.472  1.00 21.50 ? 60   ALA H CA  1 
ATOM   8253  C  C   . ALA H  1 60  ? 85.648  -0.841  -4.296  1.00 21.67 ? 60   ALA H C   1 
ATOM   8254  O  O   . ALA H  1 60  ? 85.594  -1.924  -4.863  1.00 21.78 ? 60   ALA H O   1 
ATOM   8255  C  CB  . ALA H  1 60  ? 84.541  0.774   -5.868  1.00 17.97 ? 60   ALA H CB  1 
ATOM   8256  N  N   . GLY H  1 61  ? 86.659  -0.501  -3.499  1.00 22.14 ? 61   GLY H N   1 
ATOM   8257  C  CA  . GLY H  1 61  ? 87.758  -1.407  -3.228  1.00 18.16 ? 61   GLY H CA  1 
ATOM   8258  C  C   . GLY H  1 61  ? 88.689  -1.549  -4.411  1.00 20.39 ? 61   GLY H C   1 
ATOM   8259  O  O   . GLY H  1 61  ? 88.736  -0.679  -5.282  1.00 18.95 ? 61   GLY H O   1 
ATOM   8260  N  N   . PRO H  1 62  ? 89.429  -2.668  -4.456  1.00 21.38 ? 62   PRO H N   1 
ATOM   8261  C  CA  . PRO H  1 62  ? 90.462  -2.935  -5.465  1.00 20.41 ? 62   PRO H CA  1 
ATOM   8262  C  C   . PRO H  1 62  ? 89.870  -3.334  -6.813  1.00 19.91 ? 62   PRO H C   1 
ATOM   8263  O  O   . PRO H  1 62  ? 88.652  -3.507  -6.939  1.00 19.70 ? 62   PRO H O   1 
ATOM   8264  C  CB  . PRO H  1 62  ? 91.219  -4.137  -4.885  1.00 23.96 ? 62   PRO H CB  1 
ATOM   8265  C  CG  . PRO H  1 62  ? 90.601  -4.433  -3.541  1.00 23.89 ? 62   PRO H CG  1 
ATOM   8266  C  CD  . PRO H  1 62  ? 89.266  -3.790  -3.516  1.00 22.22 ? 62   PRO H CD  1 
ATOM   8267  N  N   . HIS H  1 63  ? 90.719  -3.504  -7.818  1.00 18.70 ? 63   HIS H N   1 
ATOM   8268  C  CA  . HIS H  1 63  ? 90.225  -4.099  -9.050  1.00 20.27 ? 63   HIS H CA  1 
ATOM   8269  C  C   . HIS H  1 63  ? 89.689  -5.486  -8.723  1.00 22.29 ? 63   HIS H C   1 
ATOM   8270  O  O   . HIS H  1 63  ? 90.144  -6.134  -7.763  1.00 22.77 ? 63   HIS H O   1 
ATOM   8271  C  CB  . HIS H  1 63  ? 91.296  -4.174  -10.133 1.00 19.22 ? 63   HIS H CB  1 
ATOM   8272  C  CG  . HIS H  1 63  ? 91.894  -2.846  -10.485 1.00 19.91 ? 63   HIS H CG  1 
ATOM   8273  N  ND1 . HIS H  1 63  ? 93.008  -2.719  -11.287 1.00 18.00 ? 63   HIS H ND1 1 
ATOM   8274  C  CD2 . HIS H  1 63  ? 91.552  -1.591  -10.118 1.00 18.48 ? 63   HIS H CD2 1 
ATOM   8275  C  CE1 . HIS H  1 63  ? 93.307  -1.440  -11.421 1.00 18.27 ? 63   HIS H CE1 1 
ATOM   8276  N  NE2 . HIS H  1 63  ? 92.442  -0.736  -10.716 1.00 17.59 ? 63   HIS H NE2 1 
ATOM   8277  N  N   . PHE H  1 64  ? 88.717  -5.923  -9.519  1.00 21.24 ? 64   PHE H N   1 
ATOM   8278  C  CA  . PHE H  1 64  ? 88.046  -7.192  -9.305  1.00 20.50 ? 64   PHE H CA  1 
ATOM   8279  C  C   . PHE H  1 64  ? 89.027  -8.315  -9.602  1.00 20.24 ? 64   PHE H C   1 
ATOM   8280  O  O   . PHE H  1 64  ? 89.422  -8.524  -10.750 1.00 19.68 ? 64   PHE H O   1 
ATOM   8281  C  CB  . PHE H  1 64  ? 86.784  -7.296  -10.171 1.00 19.46 ? 64   PHE H CB  1 
ATOM   8282  C  CG  . PHE H  1 64  ? 86.048  -8.591  -10.008 1.00 17.81 ? 64   PHE H CG  1 
ATOM   8283  C  CD1 . PHE H  1 64  ? 85.808  -9.114  -8.746  1.00 17.69 ? 64   PHE H CD1 1 
ATOM   8284  C  CD2 . PHE H  1 64  ? 85.595  -9.285  -11.116 1.00 19.09 ? 64   PHE H CD2 1 
ATOM   8285  C  CE1 . PHE H  1 64  ? 85.146  -10.317 -8.597  1.00 18.99 ? 64   PHE H CE1 1 
ATOM   8286  C  CE2 . PHE H  1 64  ? 84.917  -10.484 -10.974 1.00 19.65 ? 64   PHE H CE2 1 
ATOM   8287  C  CZ  . PHE H  1 64  ? 84.697  -11.004 -9.717  1.00 18.10 ? 64   PHE H CZ  1 
ATOM   8288  N  N   . ASN H  1 65  ? 89.426  -9.025  -8.552  1.00 21.04 ? 65   ASN H N   1 
ATOM   8289  C  CA  . ASN H  1 65  ? 90.525  -9.975  -8.641  1.00 22.98 ? 65   ASN H CA  1 
ATOM   8290  C  C   . ASN H  1 65  ? 90.238  -11.288 -7.925  1.00 21.52 ? 65   ASN H C   1 
ATOM   8291  O  O   . ASN H  1 65  ? 90.835  -11.567 -6.892  1.00 24.72 ? 65   ASN H O   1 
ATOM   8292  C  CB  . ASN H  1 65  ? 91.779  -9.336  -8.048  1.00 20.83 ? 65   ASN H CB  1 
ATOM   8293  C  CG  . ASN H  1 65  ? 93.027  -10.119 -8.349  1.00 21.21 ? 65   ASN H CG  1 
ATOM   8294  O  OD1 . ASN H  1 65  ? 93.091  -10.866 -9.334  1.00 19.56 ? 65   ASN H OD1 1 
ATOM   8295  N  ND2 . ASN H  1 65  ? 94.043  -9.948  -7.503  1.00 21.60 ? 65   ASN H ND2 1 
ATOM   8296  N  N   . PRO H  1 66  ? 89.336  -12.106 -8.483  1.00 20.79 ? 66   PRO H N   1 
ATOM   8297  C  CA  . PRO H  1 66  ? 88.910  -13.365 -7.864  1.00 23.71 ? 66   PRO H CA  1 
ATOM   8298  C  C   . PRO H  1 66  ? 90.011  -14.425 -7.902  1.00 24.43 ? 66   PRO H C   1 
ATOM   8299  O  O   . PRO H  1 66  ? 90.007  -15.335 -7.074  1.00 23.96 ? 66   PRO H O   1 
ATOM   8300  C  CB  . PRO H  1 66  ? 87.733  -13.816 -8.744  1.00 21.82 ? 66   PRO H CB  1 
ATOM   8301  C  CG  . PRO H  1 66  ? 87.465  -12.702 -9.678  1.00 20.30 ? 66   PRO H CG  1 
ATOM   8302  C  CD  . PRO H  1 66  ? 88.712  -11.912 -9.796  1.00 20.12 ? 66   PRO H CD  1 
ATOM   8303  N  N   . LEU H  1 67  ? 90.935  -14.295 -8.856  1.00 27.53 ? 67   LEU H N   1 
ATOM   8304  C  CA  . LEU H  1 67  ? 92.023  -15.260 -9.050  1.00 25.93 ? 67   LEU H CA  1 
ATOM   8305  C  C   . LEU H  1 67  ? 93.331  -14.837 -8.380  1.00 26.19 ? 67   LEU H C   1 
ATOM   8306  O  O   . LEU H  1 67  ? 94.340  -15.516 -8.506  1.00 28.97 ? 67   LEU H O   1 
ATOM   8307  C  CB  . LEU H  1 67  ? 92.231  -15.554 -10.545 1.00 24.44 ? 67   LEU H CB  1 
ATOM   8308  C  CG  . LEU H  1 67  ? 90.966  -16.123 -11.207 1.00 25.04 ? 67   LEU H CG  1 
ATOM   8309  C  CD1 . LEU H  1 67  ? 91.210  -16.649 -12.604 1.00 23.92 ? 67   LEU H CD1 1 
ATOM   8310  C  CD2 . LEU H  1 67  ? 90.357  -17.209 -10.329 1.00 25.74 ? 67   LEU H CD2 1 
ATOM   8311  N  N   . SER H  1 68  ? 93.302  -13.716 -7.668  1.00 24.63 ? 68   SER H N   1 
ATOM   8312  C  CA  . SER H  1 68  ? 94.452  -13.251 -6.899  1.00 24.98 ? 68   SER H CA  1 
ATOM   8313  C  C   . SER H  1 68  ? 95.717  -13.074 -7.740  1.00 26.26 ? 68   SER H C   1 
ATOM   8314  O  O   . SER H  1 68  ? 96.811  -13.498 -7.351  1.00 28.24 ? 68   SER H O   1 
ATOM   8315  C  CB  . SER H  1 68  ? 94.711  -14.199 -5.733  1.00 28.70 ? 68   SER H CB  1 
ATOM   8316  O  OG  . SER H  1 68  ? 93.540  -14.307 -4.947  1.00 27.31 ? 68   SER H OG  1 
ATOM   8317  N  N   . ARG H  1 69  ? 95.560  -12.427 -8.887  1.00 24.58 ? 69   ARG H N   1 
ATOM   8318  C  CA  . ARG H  1 69  ? 96.660  -12.220 -9.809  1.00 25.22 ? 69   ARG H CA  1 
ATOM   8319  C  C   . ARG H  1 69  ? 97.081  -10.757 -9.820  1.00 24.58 ? 69   ARG H C   1 
ATOM   8320  O  O   . ARG H  1 69  ? 96.395  -9.919  -9.243  1.00 22.14 ? 69   ARG H O   1 
ATOM   8321  C  CB  . ARG H  1 69  ? 96.239  -12.666 -11.199 1.00 25.22 ? 69   ARG H CB  1 
ATOM   8322  C  CG  . ARG H  1 69  ? 96.168  -14.164 -11.312 1.00 28.70 ? 69   ARG H CG  1 
ATOM   8323  C  CD  . ARG H  1 69  ? 95.755  -14.617 -12.700 1.00 30.74 ? 69   ARG H CD  1 
ATOM   8324  N  NE  . ARG H  1 69  ? 95.714  -16.075 -12.737 1.00 37.91 ? 69   ARG H NE  1 
ATOM   8325  C  CZ  . ARG H  1 69  ? 95.145  -16.794 -13.698 1.00 38.67 ? 69   ARG H CZ  1 
ATOM   8326  N  NH1 . ARG H  1 69  ? 94.559  -16.193 -14.725 1.00 36.93 ? 69   ARG H NH1 1 
ATOM   8327  N  NH2 . ARG H  1 69  ? 95.164  -18.121 -13.629 1.00 40.53 ? 69   ARG H NH2 1 
ATOM   8328  N  N   . LYS H  1 70  ? 98.204  -10.453 -10.468 1.00 24.09 ? 70   LYS H N   1 
ATOM   8329  C  CA  . LYS H  1 70  ? 98.686  -9.081  -10.524 1.00 24.12 ? 70   LYS H CA  1 
ATOM   8330  C  C   . LYS H  1 70  ? 98.078  -8.320  -11.702 1.00 21.49 ? 70   LYS H C   1 
ATOM   8331  O  O   . LYS H  1 70  ? 97.536  -8.910  -12.626 1.00 20.81 ? 70   LYS H O   1 
ATOM   8332  C  CB  . LYS H  1 70  ? 100.217 -9.033  -10.571 1.00 27.34 ? 70   LYS H CB  1 
ATOM   8333  C  CG  . LYS H  1 70  ? 100.918 -9.607  -9.339  1.00 27.26 ? 70   LYS H CG  1 
ATOM   8334  C  CD  . LYS H  1 70  ? 102.416 -9.470  -9.479  1.00 30.58 ? 70   LYS H CD  1 
ATOM   8335  C  CE  . LYS H  1 70  ? 103.161 -10.487 -8.625  1.00 40.76 ? 70   LYS H CE  1 
ATOM   8336  N  NZ  . LYS H  1 70  ? 103.084 -11.881 -9.171  1.00 35.55 ? 70   LYS H NZ  1 
ATOM   8337  N  N   . HIS H  1 71  ? 98.165  -6.999  -11.650 1.00 21.03 ? 71   HIS H N   1 
ATOM   8338  C  CA  . HIS H  1 71  ? 97.534  -6.147  -12.648 1.00 19.24 ? 71   HIS H CA  1 
ATOM   8339  C  C   . HIS H  1 71  ? 98.127  -6.359  -14.028 1.00 21.79 ? 71   HIS H C   1 
ATOM   8340  O  O   . HIS H  1 71  ? 99.335  -6.528  -14.175 1.00 26.64 ? 71   HIS H O   1 
ATOM   8341  C  CB  . HIS H  1 71  ? 97.661  -4.673  -12.240 1.00 20.11 ? 71   HIS H CB  1 
ATOM   8342  C  CG  . HIS H  1 71  ? 97.049  -3.716  -13.219 1.00 22.50 ? 71   HIS H CG  1 
ATOM   8343  N  ND1 . HIS H  1 71  ? 95.703  -3.410  -13.224 1.00 20.64 ? 71   HIS H ND1 1 
ATOM   8344  C  CD2 . HIS H  1 71  ? 97.599  -3.001  -14.229 1.00 21.07 ? 71   HIS H CD2 1 
ATOM   8345  C  CE1 . HIS H  1 71  ? 95.453  -2.548  -14.194 1.00 19.47 ? 71   HIS H CE1 1 
ATOM   8346  N  NE2 . HIS H  1 71  ? 96.584  -2.289  -14.821 1.00 20.43 ? 71   HIS H NE2 1 
ATOM   8347  N  N   . GLY H  1 72  ? 97.276  -6.354  -15.045 1.00 20.35 ? 72   GLY H N   1 
ATOM   8348  C  CA  . GLY H  1 72  ? 97.753  -6.451  -16.412 1.00 21.90 ? 72   GLY H CA  1 
ATOM   8349  C  C   . GLY H  1 72  ? 96.838  -5.735  -17.384 1.00 22.77 ? 72   GLY H C   1 
ATOM   8350  O  O   . GLY H  1 72  ? 95.803  -5.193  -16.986 1.00 21.46 ? 72   GLY H O   1 
ATOM   8351  N  N   . GLY H  1 73  ? 97.227  -5.713  -18.656 1.00 23.16 ? 73   GLY H N   1 
ATOM   8352  C  CA  . GLY H  1 73  ? 96.364  -5.202  -19.705 1.00 22.77 ? 73   GLY H CA  1 
ATOM   8353  C  C   . GLY H  1 73  ? 95.336  -6.250  -20.086 1.00 22.37 ? 73   GLY H C   1 
ATOM   8354  O  O   . GLY H  1 73  ? 95.429  -7.400  -19.666 1.00 22.73 ? 73   GLY H O   1 
ATOM   8355  N  N   . PRO H  1 74  ? 94.352  -5.863  -20.899 1.00 24.62 ? 74   PRO H N   1 
ATOM   8356  C  CA  . PRO H  1 74  ? 93.248  -6.778  -21.237 1.00 26.94 ? 74   PRO H CA  1 
ATOM   8357  C  C   . PRO H  1 74  ? 93.724  -8.044  -21.955 1.00 26.12 ? 74   PRO H C   1 
ATOM   8358  O  O   . PRO H  1 74  ? 93.013  -9.046  -21.959 1.00 24.85 ? 74   PRO H O   1 
ATOM   8359  C  CB  . PRO H  1 74  ? 92.358  -5.949  -22.168 1.00 24.00 ? 74   PRO H CB  1 
ATOM   8360  C  CG  . PRO H  1 74  ? 92.869  -4.538  -22.079 1.00 23.40 ? 74   PRO H CG  1 
ATOM   8361  C  CD  . PRO H  1 74  ? 94.267  -4.571  -21.597 1.00 21.21 ? 74   PRO H CD  1 
ATOM   8362  N  N   . LYS H  1 75  ? 94.910  -7.987  -22.555 1.00 28.65 ? 75   LYS H N   1 
ATOM   8363  C  CA  . LYS H  1 75  ? 95.393  -9.062  -23.412 1.00 27.19 ? 75   LYS H CA  1 
ATOM   8364  C  C   . LYS H  1 75  ? 96.558  -9.806  -22.767 1.00 31.68 ? 75   LYS H C   1 
ATOM   8365  O  O   . LYS H  1 75  ? 97.126  -10.727 -23.363 1.00 35.31 ? 75   LYS H O   1 
ATOM   8366  C  CB  . LYS H  1 75  ? 95.813  -8.499  -24.770 1.00 30.44 ? 75   LYS H CB  1 
ATOM   8367  C  CG  . LYS H  1 75  ? 94.680  -7.886  -25.572 1.00 30.11 ? 75   LYS H CG  1 
ATOM   8368  C  CD  . LYS H  1 75  ? 93.917  -8.937  -26.371 1.00 37.36 ? 75   LYS H CD  1 
ATOM   8369  C  CE  . LYS H  1 75  ? 94.562  -9.192  -27.740 1.00 39.64 ? 75   LYS H CE  1 
ATOM   8370  N  NZ  . LYS H  1 75  ? 93.665  -9.967  -28.654 1.00 35.98 ? 75   LYS H NZ  1 
ATOM   8371  N  N   . ASP H  1 76  ? 96.912  -9.404  -21.549 1.00 30.21 ? 76   ASP H N   1 
ATOM   8372  C  CA  . ASP H  1 76  ? 98.015  -10.029 -20.836 1.00 29.37 ? 76   ASP H CA  1 
ATOM   8373  C  C   . ASP H  1 76  ? 97.595  -11.392 -20.281 1.00 32.27 ? 76   ASP H C   1 
ATOM   8374  O  O   . ASP H  1 76  ? 96.453  -11.584 -19.866 1.00 29.83 ? 76   ASP H O   1 
ATOM   8375  C  CB  . ASP H  1 76  ? 98.536  -9.114  -19.711 1.00 26.73 ? 76   ASP H CB  1 
ATOM   8376  C  CG  . ASP H  1 76  ? 99.623  -8.144  -20.184 1.00 30.05 ? 76   ASP H CG  1 
ATOM   8377  O  OD1 . ASP H  1 76  ? 100.657 -8.620  -20.698 1.00 40.65 ? 76   ASP H OD1 1 
ATOM   8378  O  OD2 . ASP H  1 76  ? 99.468  -6.910  -20.031 1.00 25.15 ? 76   ASP H OD2 1 
ATOM   8379  N  N   . GLU H  1 77  ? 98.528  -12.341 -20.308 1.00 36.04 ? 77   GLU H N   1 
ATOM   8380  C  CA  . GLU H  1 77  ? 98.366  -13.624 -19.635 1.00 35.72 ? 77   GLU H CA  1 
ATOM   8381  C  C   . GLU H  1 77  ? 97.944  -13.412 -18.177 1.00 32.99 ? 77   GLU H C   1 
ATOM   8382  O  O   . GLU H  1 77  ? 96.966  -13.988 -17.709 1.00 30.36 ? 77   GLU H O   1 
ATOM   8383  C  CB  . GLU H  1 77  ? 99.694  -14.392 -19.684 1.00 37.14 ? 77   GLU H CB  1 
ATOM   8384  C  CG  . GLU H  1 77  ? 99.749  -15.544 -20.679 1.00 43.13 ? 77   GLU H CG  1 
ATOM   8385  C  CD  . GLU H  1 77  ? 99.389  -16.883 -20.046 1.00 49.75 ? 77   GLU H CD  1 
ATOM   8386  O  OE1 . GLU H  1 77  ? 99.980  -17.909 -20.438 1.00 51.09 ? 77   GLU H OE1 1 
ATOM   8387  O  OE2 . GLU H  1 77  ? 98.521  -16.912 -19.146 1.00 54.35 ? 77   GLU H OE2 1 
ATOM   8388  N  N   . GLU H  1 78  ? 98.710  -12.592 -17.465 1.00 31.92 ? 78   GLU H N   1 
ATOM   8389  C  CA  . GLU H  1 78  ? 98.412  -12.232 -16.082 1.00 31.86 ? 78   GLU H CA  1 
ATOM   8390  C  C   . GLU H  1 78  ? 97.672  -10.904 -16.037 1.00 29.02 ? 78   GLU H C   1 
ATOM   8391  O  O   . GLU H  1 78  ? 98.142  -9.894  -16.577 1.00 25.50 ? 78   GLU H O   1 
ATOM   8392  C  CB  . GLU H  1 78  ? 99.695  -12.146 -15.240 1.00 28.49 ? 78   GLU H CB  1 
ATOM   8393  C  CG  . GLU H  1 78  ? 99.840  -13.240 -14.189 1.00 34.60 ? 78   GLU H CG  1 
ATOM   8394  C  CD  . GLU H  1 78  ? 99.860  -12.686 -12.765 1.00 35.76 ? 78   GLU H CD  1 
ATOM   8395  O  OE1 . GLU H  1 78  ? 100.244 -11.512 -12.604 1.00 36.28 ? 78   GLU H OE1 1 
ATOM   8396  O  OE2 . GLU H  1 78  ? 99.507  -13.420 -11.807 1.00 36.08 ? 78   GLU H OE2 1 
ATOM   8397  N  N   . ARG H  1 79  ? 96.514  -10.924 -15.385 1.00 25.44 ? 79   ARG H N   1 
ATOM   8398  C  CA  . ARG H  1 79  ? 95.684  -9.741  -15.227 1.00 24.33 ? 79   ARG H CA  1 
ATOM   8399  C  C   . ARG H  1 79  ? 94.664  -10.017 -14.152 1.00 21.74 ? 79   ARG H C   1 
ATOM   8400  O  O   . ARG H  1 79  ? 94.431  -11.174 -13.788 1.00 22.93 ? 79   ARG H O   1 
ATOM   8401  C  CB  . ARG H  1 79  ? 94.968  -9.361  -16.539 1.00 21.32 ? 79   ARG H CB  1 
ATOM   8402  C  CG  . ARG H  1 79  ? 94.133  -10.480 -17.167 1.00 19.92 ? 79   ARG H CG  1 
ATOM   8403  C  CD  . ARG H  1 79  ? 93.310  -9.994  -18.340 1.00 19.50 ? 79   ARG H CD  1 
ATOM   8404  N  NE  . ARG H  1 79  ? 92.008  -9.491  -17.899 1.00 20.98 ? 79   ARG H NE  1 
ATOM   8405  C  CZ  . ARG H  1 79  ? 91.003  -9.178  -18.715 1.00 20.74 ? 79   ARG H CZ  1 
ATOM   8406  N  NH1 . ARG H  1 79  ? 91.141  -9.301  -20.026 1.00 21.59 ? 79   ARG H NH1 1 
ATOM   8407  N  NH2 . ARG H  1 79  ? 89.849  -8.744  -18.217 1.00 22.93 ? 79   ARG H NH2 1 
ATOM   8408  N  N   . HIS H  1 80  ? 94.081  -8.939  -13.637 1.00 20.54 ? 80   HIS H N   1 
ATOM   8409  C  CA  . HIS H  1 80  ? 92.909  -9.010  -12.797 1.00 19.42 ? 80   HIS H CA  1 
ATOM   8410  C  C   . HIS H  1 80  ? 91.730  -9.200  -13.743 1.00 20.53 ? 80   HIS H C   1 
ATOM   8411  O  O   . HIS H  1 80  ? 91.749  -8.707  -14.867 1.00 22.20 ? 80   HIS H O   1 
ATOM   8412  C  CB  . HIS H  1 80  ? 92.712  -7.703  -12.031 1.00 21.35 ? 80   HIS H CB  1 
ATOM   8413  C  CG  . HIS H  1 80  ? 93.820  -7.357  -11.083 1.00 18.79 ? 80   HIS H CG  1 
ATOM   8414  N  ND1 . HIS H  1 80  ? 94.204  -6.054  -10.838 1.00 18.71 ? 80   HIS H ND1 1 
ATOM   8415  C  CD2 . HIS H  1 80  ? 94.599  -8.131  -10.296 1.00 20.68 ? 80   HIS H CD2 1 
ATOM   8416  C  CE1 . HIS H  1 80  ? 95.183  -6.041  -9.952  1.00 18.16 ? 80   HIS H CE1 1 
ATOM   8417  N  NE2 . HIS H  1 80  ? 95.447  -7.288  -9.610  1.00 20.39 ? 80   HIS H NE2 1 
ATOM   8418  N  N   . VAL H  1 81  ? 90.699  -9.906  -13.297 1.00 22.26 ? 81   VAL H N   1 
ATOM   8419  C  CA  . VAL H  1 81  ? 89.486  -10.063 -14.088 1.00 19.74 ? 81   VAL H CA  1 
ATOM   8420  C  C   . VAL H  1 81  ? 88.924  -8.702  -14.568 1.00 22.57 ? 81   VAL H C   1 
ATOM   8421  O  O   . VAL H  1 81  ? 88.415  -8.584  -15.702 1.00 20.65 ? 81   VAL H O   1 
ATOM   8422  C  CB  . VAL H  1 81  ? 88.427  -10.894 -13.295 1.00 20.28 ? 81   VAL H CB  1 
ATOM   8423  C  CG1 . VAL H  1 81  ? 87.009  -10.717 -13.858 1.00 18.04 ? 81   VAL H CG1 1 
ATOM   8424  C  CG2 . VAL H  1 81  ? 88.826  -12.371 -13.266 1.00 20.78 ? 81   VAL H CG2 1 
ATOM   8425  N  N   . GLY H  1 82  ? 89.031  -7.677  -13.720 1.00 18.73 ? 82   GLY H N   1 
ATOM   8426  C  CA  . GLY H  1 82  ? 88.485  -6.371  -14.050 1.00 20.25 ? 82   GLY H CA  1 
ATOM   8427  C  C   . GLY H  1 82  ? 89.381  -5.438  -14.857 1.00 20.08 ? 82   GLY H C   1 
ATOM   8428  O  O   . GLY H  1 82  ? 89.124  -4.240  -14.933 1.00 21.99 ? 82   GLY H O   1 
ATOM   8429  N  N   . ASP H  1 83  ? 90.428  -5.971  -15.467 1.00 19.20 ? 83   ASP H N   1 
ATOM   8430  C  CA  . ASP H  1 83  ? 91.365  -5.152  -16.229 1.00 19.79 ? 83   ASP H CA  1 
ATOM   8431  C  C   . ASP H  1 83  ? 90.949  -4.971  -17.702 1.00 21.21 ? 83   ASP H C   1 
ATOM   8432  O  O   . ASP H  1 83  ? 91.285  -5.784  -18.568 1.00 21.37 ? 83   ASP H O   1 
ATOM   8433  C  CB  . ASP H  1 83  ? 92.771  -5.747  -16.124 1.00 18.83 ? 83   ASP H CB  1 
ATOM   8434  C  CG  . ASP H  1 83  ? 93.325  -5.681  -14.710 1.00 19.56 ? 83   ASP H CG  1 
ATOM   8435  O  OD1 . ASP H  1 83  ? 92.863  -4.838  -13.930 1.00 19.48 ? 83   ASP H OD1 1 
ATOM   8436  O  OD2 . ASP H  1 83  ? 94.230  -6.460  -14.370 1.00 20.83 ? 83   ASP H OD2 1 
ATOM   8437  N  N   . LEU H  1 84  ? 90.220  -3.892  -17.973 1.00 20.77 ? 84   LEU H N   1 
ATOM   8438  C  CA  . LEU H  1 84  ? 89.759  -3.589  -19.329 1.00 20.02 ? 84   LEU H CA  1 
ATOM   8439  C  C   . LEU H  1 84  ? 90.621  -2.548  -20.044 1.00 18.13 ? 84   LEU H C   1 
ATOM   8440  O  O   . LEU H  1 84  ? 90.241  -2.038  -21.083 1.00 22.05 ? 84   LEU H O   1 
ATOM   8441  C  CB  . LEU H  1 84  ? 88.302  -3.142  -19.300 1.00 17.92 ? 84   LEU H CB  1 
ATOM   8442  C  CG  . LEU H  1 84  ? 87.414  -4.221  -18.698 1.00 18.92 ? 84   LEU H CG  1 
ATOM   8443  C  CD1 . LEU H  1 84  ? 85.976  -3.757  -18.618 1.00 21.41 ? 84   LEU H CD1 1 
ATOM   8444  C  CD2 . LEU H  1 84  ? 87.541  -5.501  -19.513 1.00 17.91 ? 84   LEU H CD2 1 
ATOM   8445  N  N   . GLY H  1 85  ? 91.785  -2.240  -19.484 1.00 22.07 ? 85   GLY H N   1 
ATOM   8446  C  CA  . GLY H  1 85  ? 92.740  -1.357  -20.135 1.00 21.37 ? 85   GLY H CA  1 
ATOM   8447  C  C   . GLY H  1 85  ? 92.435  0.124   -20.017 1.00 20.24 ? 85   GLY H C   1 
ATOM   8448  O  O   . GLY H  1 85  ? 92.147  0.629   -18.932 1.00 20.49 ? 85   GLY H O   1 
ATOM   8449  N  N   . ASN H  1 86  ? 92.517  0.811   -21.152 1.00 19.56 ? 86   ASN H N   1 
ATOM   8450  C  CA  . ASN H  1 86  ? 92.332  2.255   -21.255 1.00 19.66 ? 86   ASN H CA  1 
ATOM   8451  C  C   . ASN H  1 86  ? 91.209  2.582   -22.227 1.00 20.54 ? 86   ASN H C   1 
ATOM   8452  O  O   . ASN H  1 86  ? 90.960  1.840   -23.177 1.00 20.37 ? 86   ASN H O   1 
ATOM   8453  C  CB  . ASN H  1 86  ? 93.597  2.921   -21.824 1.00 19.74 ? 86   ASN H CB  1 
ATOM   8454  C  CG  . ASN H  1 86  ? 94.767  2.907   -20.866 1.00 19.52 ? 86   ASN H CG  1 
ATOM   8455  O  OD1 . ASN H  1 86  ? 94.710  3.492   -19.791 1.00 21.39 ? 86   ASN H OD1 1 
ATOM   8456  N  ND2 . ASN H  1 86  ? 95.851  2.261   -21.268 1.00 21.88 ? 86   ASN H ND2 1 
ATOM   8457  N  N   . VAL H  1 87  ? 90.557  3.716   -22.015 1.00 20.95 ? 87   VAL H N   1 
ATOM   8458  C  CA  . VAL H  1 87  ? 89.706  4.301   -23.049 1.00 21.33 ? 87   VAL H CA  1 
ATOM   8459  C  C   . VAL H  1 87  ? 90.356  5.606   -23.530 1.00 20.07 ? 87   VAL H C   1 
ATOM   8460  O  O   . VAL H  1 87  ? 91.264  6.125   -22.883 1.00 19.72 ? 87   VAL H O   1 
ATOM   8461  C  CB  . VAL H  1 87  ? 88.258  4.536   -22.561 1.00 18.40 ? 87   VAL H CB  1 
ATOM   8462  C  CG1 . VAL H  1 87  ? 87.551  3.204   -22.338 1.00 16.86 ? 87   VAL H CG1 1 
ATOM   8463  C  CG2 . VAL H  1 87  ? 88.257  5.365   -21.299 1.00 17.88 ? 87   VAL H CG2 1 
ATOM   8464  N  N   . THR H  1 88  ? 89.911  6.125   -24.669 1.00 19.18 ? 88   THR H N   1 
ATOM   8465  C  CA  . THR H  1 88  ? 90.532  7.326   -25.222 1.00 21.01 ? 88   THR H CA  1 
ATOM   8466  C  C   . THR H  1 88  ? 89.548  8.484   -25.274 1.00 17.88 ? 88   THR H C   1 
ATOM   8467  O  O   . THR H  1 88  ? 88.511  8.380   -25.902 1.00 21.88 ? 88   THR H O   1 
ATOM   8468  C  CB  . THR H  1 88  ? 91.102  7.079   -26.652 1.00 20.45 ? 88   THR H CB  1 
ATOM   8469  O  OG1 . THR H  1 88  ? 91.940  5.917   -26.651 1.00 19.87 ? 88   THR H OG1 1 
ATOM   8470  C  CG2 . THR H  1 88  ? 91.919  8.290   -27.143 1.00 18.40 ? 88   THR H CG2 1 
ATOM   8471  N  N   . ALA H  1 89  ? 89.873  9.586   -24.616 1.00 18.80 ? 89   ALA H N   1 
ATOM   8472  C  CA  . ALA H  1 89  ? 89.061  10.787  -24.719 1.00 17.80 ? 89   ALA H CA  1 
ATOM   8473  C  C   . ALA H  1 89  ? 89.612  11.670  -25.817 1.00 18.43 ? 89   ALA H C   1 
ATOM   8474  O  O   . ALA H  1 89  ? 90.809  11.890  -25.903 1.00 21.22 ? 89   ALA H O   1 
ATOM   8475  C  CB  . ALA H  1 89  ? 89.035  11.540  -23.398 1.00 17.88 ? 89   ALA H CB  1 
ATOM   8476  N  N   . GLY H  1 90  ? 88.730  12.157  -26.675 1.00 22.67 ? 90   GLY H N   1 
ATOM   8477  C  CA  . GLY H  1 90  ? 89.117  13.101  -27.702 1.00 24.88 ? 90   GLY H CA  1 
ATOM   8478  C  C   . GLY H  1 90  ? 89.387  14.471  -27.107 1.00 25.48 ? 90   GLY H C   1 
ATOM   8479  O  O   . GLY H  1 90  ? 89.336  14.669  -25.884 1.00 23.26 ? 90   GLY H O   1 
ATOM   8480  N  N   . LYS H  1 91  ? 89.684  15.425  -27.980 1.00 27.57 ? 91   LYS H N   1 
ATOM   8481  C  CA  . LYS H  1 91  ? 89.905  16.802  -27.565 1.00 30.94 ? 91   LYS H CA  1 
ATOM   8482  C  C   . LYS H  1 91  ? 88.584  17.338  -27.008 1.00 29.40 ? 91   LYS H C   1 
ATOM   8483  O  O   . LYS H  1 91  ? 88.559  18.305  -26.247 1.00 28.93 ? 91   LYS H O   1 
ATOM   8484  C  CB  . LYS H  1 91  ? 90.385  17.628  -28.763 1.00 29.06 ? 91   LYS H CB  1 
ATOM   8485  C  CG  . LYS H  1 91  ? 91.572  18.524  -28.473 1.00 33.51 ? 91   LYS H CG  1 
ATOM   8486  C  CD  . LYS H  1 91  ? 91.959  19.338  -29.697 1.00 39.56 ? 91   LYS H CD  1 
ATOM   8487  C  CE  . LYS H  1 91  ? 92.073  18.454  -30.946 1.00 44.46 ? 91   LYS H CE  1 
ATOM   8488  N  NZ  . LYS H  1 91  ? 93.291  17.584  -30.931 1.00 42.87 ? 91   LYS H NZ  1 
ATOM   8489  N  N   . ASP H  1 92  ? 87.502  16.679  -27.436 1.00 30.37 ? 92   ASP H N   1 
ATOM   8490  C  CA  . ASP H  1 92  ? 86.132  16.798  -26.925 1.00 29.01 ? 92   ASP H CA  1 
ATOM   8491  C  C   . ASP H  1 92  ? 86.021  16.585  -25.426 1.00 28.10 ? 92   ASP H C   1 
ATOM   8492  O  O   . ASP H  1 92  ? 85.097  17.077  -24.783 1.00 26.60 ? 92   ASP H O   1 
ATOM   8493  C  CB  . ASP H  1 92  ? 85.315  15.646  -27.511 1.00 30.53 ? 92   ASP H CB  1 
ATOM   8494  C  CG  . ASP H  1 92  ? 84.558  16.020  -28.750 1.00 39.03 ? 92   ASP H CG  1 
ATOM   8495  O  OD1 . ASP H  1 92  ? 84.636  17.193  -29.179 1.00 48.92 ? 92   ASP H OD1 1 
ATOM   8496  O  OD2 . ASP H  1 92  ? 83.874  15.118  -29.289 1.00 37.11 ? 92   ASP H OD2 1 
ATOM   8497  N  N   . GLY H  1 93  ? 86.927  15.774  -24.894 1.00 27.11 ? 93   GLY H N   1 
ATOM   8498  C  CA  . GLY H  1 93  ? 86.772  15.222  -23.564 1.00 23.16 ? 93   GLY H CA  1 
ATOM   8499  C  C   . GLY H  1 93  ? 85.815  14.039  -23.578 1.00 23.03 ? 93   GLY H C   1 
ATOM   8500  O  O   . GLY H  1 93  ? 85.454  13.518  -22.520 1.00 21.83 ? 93   GLY H O   1 
ATOM   8501  N  N   . VAL H  1 94  ? 85.402  13.615  -24.773 1.00 23.14 ? 94   VAL H N   1 
ATOM   8502  C  CA  . VAL H  1 94  ? 84.461  12.499  -24.910 1.00 22.63 ? 94   VAL H CA  1 
ATOM   8503  C  C   . VAL H  1 94  ? 85.167  11.197  -25.276 1.00 21.07 ? 94   VAL H C   1 
ATOM   8504  O  O   . VAL H  1 94  ? 85.943  11.155  -26.221 1.00 21.09 ? 94   VAL H O   1 
ATOM   8505  C  CB  . VAL H  1 94  ? 83.378  12.789  -25.971 1.00 26.31 ? 94   VAL H CB  1 
ATOM   8506  C  CG1 . VAL H  1 94  ? 82.415  11.612  -26.093 1.00 24.02 ? 94   VAL H CG1 1 
ATOM   8507  C  CG2 . VAL H  1 94  ? 82.627  14.074  -25.631 1.00 24.65 ? 94   VAL H CG2 1 
ATOM   8508  N  N   . ALA H  1 95  ? 84.901  10.145  -24.509 1.00 20.38 ? 95   ALA H N   1 
ATOM   8509  C  CA  . ALA H  1 95  ? 85.459  8.827   -24.778 1.00 19.69 ? 95   ALA H CA  1 
ATOM   8510  C  C   . ALA H  1 95  ? 84.363  7.900   -25.259 1.00 22.57 ? 95   ALA H C   1 
ATOM   8511  O  O   . ALA H  1 95  ? 83.486  7.516   -24.492 1.00 23.19 ? 95   ALA H O   1 
ATOM   8512  C  CB  . ALA H  1 95  ? 86.105  8.251   -23.532 1.00 18.91 ? 95   ALA H CB  1 
ATOM   8513  N  N   . ASN H  1 96  ? 84.416  7.549   -26.534 1.00 23.64 ? 96   ASN H N   1 
ATOM   8514  C  CA  . ASN H  1 96  ? 83.512  6.564   -27.089 1.00 24.31 ? 96   ASN H CA  1 
ATOM   8515  C  C   . ASN H  1 96  ? 84.073  5.183   -26.813 1.00 22.46 ? 96   ASN H C   1 
ATOM   8516  O  O   . ASN H  1 96  ? 85.034  4.759   -27.423 1.00 25.27 ? 96   ASN H O   1 
ATOM   8517  C  CB  . ASN H  1 96  ? 83.321  6.809   -28.585 1.00 27.32 ? 96   ASN H CB  1 
ATOM   8518  C  CG  . ASN H  1 96  ? 82.736  8.182   -28.863 1.00 34.66 ? 96   ASN H CG  1 
ATOM   8519  O  OD1 . ASN H  1 96  ? 81.690  8.556   -28.301 1.00 32.13 ? 96   ASN H OD1 1 
ATOM   8520  N  ND2 . ASN H  1 96  ? 83.413  8.953   -29.713 1.00 36.94 ? 96   ASN H ND2 1 
ATOM   8521  N  N   . VAL H  1 97  ? 83.475  4.494   -25.858 1.00 23.32 ? 97   VAL H N   1 
ATOM   8522  C  CA  . VAL H  1 97  ? 83.992  3.217   -25.398 1.00 21.47 ? 97   VAL H CA  1 
ATOM   8523  C  C   . VAL H  1 97  ? 83.416  2.079   -26.226 1.00 20.17 ? 97   VAL H C   1 
ATOM   8524  O  O   . VAL H  1 97  ? 82.207  2.002   -26.429 1.00 22.61 ? 97   VAL H O   1 
ATOM   8525  C  CB  . VAL H  1 97  ? 83.649  3.017   -23.903 1.00 20.23 ? 97   VAL H CB  1 
ATOM   8526  C  CG1 . VAL H  1 97  ? 84.109  1.640   -23.398 1.00 17.62 ? 97   VAL H CG1 1 
ATOM   8527  C  CG2 . VAL H  1 97  ? 84.244  4.153   -23.081 1.00 18.82 ? 97   VAL H CG2 1 
ATOM   8528  N  N   . SER H  1 98  ? 84.289  1.215   -26.727 1.00 20.33 ? 98   SER H N   1 
ATOM   8529  C  CA  . SER H  1 98  ? 83.865  -0.016  -27.381 1.00 20.97 ? 98   SER H CA  1 
ATOM   8530  C  C   . SER H  1 98  ? 84.936  -1.067  -27.154 1.00 22.19 ? 98   SER H C   1 
ATOM   8531  O  O   . SER H  1 98  ? 86.035  -0.962  -27.684 1.00 27.04 ? 98   SER H O   1 
ATOM   8532  C  CB  . SER H  1 98  ? 83.629  0.196   -28.875 1.00 23.23 ? 98   SER H CB  1 
ATOM   8533  O  OG  . SER H  1 98  ? 82.962  -0.924  -29.446 1.00 25.96 ? 98   SER H OG  1 
ATOM   8534  N  N   . ILE H  1 99  ? 84.629  -2.066  -26.342 1.00 19.99 ? 99   ILE H N   1 
ATOM   8535  C  CA  . ILE H  1 99  ? 85.615  -3.073  -25.980 1.00 21.37 ? 99   ILE H CA  1 
ATOM   8536  C  C   . ILE H  1 99  ? 84.944  -4.433  -26.044 1.00 23.12 ? 99   ILE H C   1 
ATOM   8537  O  O   . ILE H  1 99  ? 83.728  -4.538  -25.920 1.00 24.66 ? 99   ILE H O   1 
ATOM   8538  C  CB  . ILE H  1 99  ? 86.167  -2.815  -24.555 1.00 24.24 ? 99   ILE H CB  1 
ATOM   8539  C  CG1 . ILE H  1 99  ? 87.057  -1.568  -24.543 1.00 22.94 ? 99   ILE H CG1 1 
ATOM   8540  C  CG2 . ILE H  1 99  ? 86.929  -4.025  -24.022 1.00 24.85 ? 99   ILE H CG2 1 
ATOM   8541  C  CD1 . ILE H  1 99  ? 87.252  -0.961  -23.165 1.00 20.13 ? 99   ILE H CD1 1 
ATOM   8542  N  N   . GLU H  1 100 ? 85.718  -5.480  -26.269 1.00 23.56 ? 100  GLU H N   1 
ATOM   8543  C  CA  . GLU H  1 100 ? 85.141  -6.811  -26.254 1.00 24.34 ? 100  GLU H CA  1 
ATOM   8544  C  C   . GLU H  1 100 ? 86.065  -7.710  -25.465 1.00 23.09 ? 100  GLU H C   1 
ATOM   8545  O  O   . GLU H  1 100 ? 87.238  -7.843  -25.797 1.00 24.35 ? 100  GLU H O   1 
ATOM   8546  C  CB  . GLU H  1 100 ? 84.887  -7.330  -27.672 1.00 29.69 ? 100  GLU H CB  1 
ATOM   8547  C  CG  . GLU H  1 100 ? 84.879  -8.839  -27.764 1.00 33.39 ? 100  GLU H CG  1 
ATOM   8548  C  CD  . GLU H  1 100 ? 84.043  -9.353  -28.909 1.00 38.89 ? 100  GLU H CD  1 
ATOM   8549  O  OE1 . GLU H  1 100 ? 83.208  -8.580  -29.430 1.00 44.14 ? 100  GLU H OE1 1 
ATOM   8550  O  OE2 . GLU H  1 100 ? 84.215  -10.534 -29.277 1.00 40.56 ? 100  GLU H OE2 1 
ATOM   8551  N  N   . ASP H  1 101 ? 85.531  -8.294  -24.393 1.00 24.72 ? 101  ASP H N   1 
ATOM   8552  C  CA  . ASP H  1 101 ? 86.339  -9.018  -23.417 1.00 23.39 ? 101  ASP H CA  1 
ATOM   8553  C  C   . ASP H  1 101 ? 85.784  -10.401 -23.112 1.00 22.58 ? 101  ASP H C   1 
ATOM   8554  O  O   . ASP H  1 101 ? 84.586  -10.572 -22.964 1.00 22.20 ? 101  ASP H O   1 
ATOM   8555  C  CB  . ASP H  1 101 ? 86.460  -8.220  -22.117 1.00 19.50 ? 101  ASP H CB  1 
ATOM   8556  C  CG  . ASP H  1 101 ? 87.645  -8.659  -21.280 1.00 21.63 ? 101  ASP H CG  1 
ATOM   8557  O  OD1 . ASP H  1 101 ? 88.799  -8.401  -21.681 1.00 24.70 ? 101  ASP H OD1 1 
ATOM   8558  O  OD2 . ASP H  1 101 ? 87.433  -9.264  -20.217 1.00 21.64 ? 101  ASP H OD2 1 
ATOM   8559  N  N   . ARG H  1 102 ? 86.673  -11.377 -22.983 1.00 23.25 ? 102  ARG H N   1 
ATOM   8560  C  CA  . ARG H  1 102 ? 86.265  -12.752 -22.758 1.00 23.95 ? 102  ARG H CA  1 
ATOM   8561  C  C   . ARG H  1 102 ? 86.557  -13.211 -21.341 1.00 23.29 ? 102  ARG H C   1 
ATOM   8562  O  O   . ARG H  1 102 ? 86.251  -14.350 -20.990 1.00 25.07 ? 102  ARG H O   1 
ATOM   8563  C  CB  . ARG H  1 102 ? 86.958  -13.681 -23.758 1.00 28.56 ? 102  ARG H CB  1 
ATOM   8564  C  CG  . ARG H  1 102 ? 86.707  -13.294 -25.205 1.00 30.07 ? 102  ARG H CG  1 
ATOM   8565  C  CD  . ARG H  1 102 ? 86.726  -14.487 -26.137 1.00 35.32 ? 102  ARG H CD  1 
ATOM   8566  N  NE  . ARG H  1 102 ? 86.250  -14.105 -27.468 1.00 44.02 ? 102  ARG H NE  1 
ATOM   8567  C  CZ  . ARG H  1 102 ? 85.597  -14.916 -28.298 1.00 45.60 ? 102  ARG H CZ  1 
ATOM   8568  N  NH1 . ARG H  1 102 ? 85.331  -16.172 -27.934 1.00 43.19 ? 102  ARG H NH1 1 
ATOM   8569  N  NH2 . ARG H  1 102 ? 85.199  -14.465 -29.488 1.00 43.13 ? 102  ARG H NH2 1 
ATOM   8570  N  N   . VAL H  1 103 ? 87.143  -12.330 -20.529 1.00 23.87 ? 103  VAL H N   1 
ATOM   8571  C  CA  . VAL H  1 103 ? 87.452  -12.652 -19.122 1.00 24.40 ? 103  VAL H CA  1 
ATOM   8572  C  C   . VAL H  1 103 ? 86.356  -12.194 -18.127 1.00 25.13 ? 103  VAL H C   1 
ATOM   8573  O  O   . VAL H  1 103 ? 85.988  -12.937 -17.208 1.00 26.21 ? 103  VAL H O   1 
ATOM   8574  C  CB  . VAL H  1 103 ? 88.853  -12.131 -18.715 1.00 22.52 ? 103  VAL H CB  1 
ATOM   8575  C  CG1 . VAL H  1 103 ? 89.201  -12.553 -17.302 1.00 18.65 ? 103  VAL H CG1 1 
ATOM   8576  C  CG2 . VAL H  1 103 ? 89.890  -12.645 -19.696 1.00 22.27 ? 103  VAL H CG2 1 
ATOM   8577  N  N   . ILE H  1 104 ? 85.817  -10.992 -18.323 1.00 23.28 ? 104  ILE H N   1 
ATOM   8578  C  CA  . ILE H  1 104 ? 84.666  -10.575 -17.528 1.00 22.87 ? 104  ILE H CA  1 
ATOM   8579  C  C   . ILE H  1 104 ? 83.422  -11.376 -17.937 1.00 21.95 ? 104  ILE H C   1 
ATOM   8580  O  O   . ILE H  1 104 ? 83.408  -12.013 -18.981 1.00 23.62 ? 104  ILE H O   1 
ATOM   8581  C  CB  . ILE H  1 104 ? 84.390  -9.043  -17.597 1.00 22.64 ? 104  ILE H CB  1 
ATOM   8582  C  CG1 . ILE H  1 104 ? 84.128  -8.581  -19.039 1.00 17.37 ? 104  ILE H CG1 1 
ATOM   8583  C  CG2 . ILE H  1 104 ? 85.529  -8.259  -16.914 1.00 18.19 ? 104  ILE H CG2 1 
ATOM   8584  C  CD1 . ILE H  1 104 ? 83.432  -7.237  -19.122 1.00 17.02 ? 104  ILE H CD1 1 
ATOM   8585  N  N   . SER H  1 105 ? 82.391  -11.357 -17.097 1.00 21.97 ? 105  SER H N   1 
ATOM   8586  C  CA  . SER H  1 105 ? 81.163  -12.080 -17.371 1.00 22.53 ? 105  SER H CA  1 
ATOM   8587  C  C   . SER H  1 105 ? 79.987  -11.375 -16.706 1.00 22.64 ? 105  SER H C   1 
ATOM   8588  O  O   . SER H  1 105 ? 80.158  -10.634 -15.746 1.00 21.72 ? 105  SER H O   1 
ATOM   8589  C  CB  . SER H  1 105 ? 81.261  -13.529 -16.881 1.00 23.65 ? 105  SER H CB  1 
ATOM   8590  O  OG  . SER H  1 105 ? 80.193  -14.319 -17.376 1.00 26.25 ? 105  SER H OG  1 
ATOM   8591  N  N   . LEU H  1 106 ? 78.792  -11.596 -17.236 1.00 23.57 ? 106  LEU H N   1 
ATOM   8592  C  CA  . LEU H  1 106 ? 77.598  -11.011 -16.672 1.00 21.87 ? 106  LEU H CA  1 
ATOM   8593  C  C   . LEU H  1 106 ? 76.805  -12.118 -16.000 1.00 25.95 ? 106  LEU H C   1 
ATOM   8594  O  O   . LEU H  1 106 ? 75.617  -11.957 -15.702 1.00 27.25 ? 106  LEU H O   1 
ATOM   8595  C  CB  . LEU H  1 106 ? 76.778  -10.315 -17.758 1.00 25.08 ? 106  LEU H CB  1 
ATOM   8596  C  CG  . LEU H  1 106 ? 77.516  -9.221  -18.540 1.00 20.55 ? 106  LEU H CG  1 
ATOM   8597  C  CD1 . LEU H  1 106 ? 76.598  -8.587  -19.545 1.00 22.17 ? 106  LEU H CD1 1 
ATOM   8598  C  CD2 . LEU H  1 106 ? 78.065  -8.176  -17.591 1.00 20.78 ? 106  LEU H CD2 1 
ATOM   8599  N  N   . SER H  1 107 ? 77.488  -13.238 -15.754 1.00 26.36 ? 107  SER H N   1 
ATOM   8600  C  CA  . SER H  1 107 ? 76.906  -14.400 -15.079 1.00 30.57 ? 107  SER H CA  1 
ATOM   8601  C  C   . SER H  1 107 ? 77.985  -15.324 -14.523 1.00 30.60 ? 107  SER H C   1 
ATOM   8602  O  O   . SER H  1 107 ? 79.068  -15.422 -15.090 1.00 30.98 ? 107  SER H O   1 
ATOM   8603  C  CB  . SER H  1 107 ? 76.035  -15.195 -16.051 1.00 32.68 ? 107  SER H CB  1 
ATOM   8604  O  OG  . SER H  1 107 ? 76.841  -15.903 -16.982 1.00 35.25 ? 107  SER H OG  1 
ATOM   8605  N  N   . GLY H  1 108 ? 77.685  -16.016 -13.424 1.00 33.07 ? 108  GLY H N   1 
ATOM   8606  C  CA  . GLY H  1 108 ? 78.589  -17.021 -12.883 1.00 31.70 ? 108  GLY H CA  1 
ATOM   8607  C  C   . GLY H  1 108 ? 79.569  -16.455 -11.880 1.00 35.42 ? 108  GLY H C   1 
ATOM   8608  O  O   . GLY H  1 108 ? 79.329  -15.384 -11.337 1.00 37.30 ? 108  GLY H O   1 
ATOM   8609  N  N   . GLU H  1 109 ? 80.683  -17.156 -11.658 1.00 36.29 ? 109  GLU H N   1 
ATOM   8610  C  CA  . GLU H  1 109 ? 81.663  -16.805 -10.615 1.00 35.69 ? 109  GLU H CA  1 
ATOM   8611  C  C   . GLU H  1 109 ? 82.352  -15.456 -10.805 1.00 34.55 ? 109  GLU H C   1 
ATOM   8612  O  O   . GLU H  1 109 ? 82.743  -14.797 -9.833  1.00 37.33 ? 109  GLU H O   1 
ATOM   8613  C  CB  . GLU H  1 109 ? 82.768  -17.876 -10.498 1.00 40.59 ? 109  GLU H CB  1 
ATOM   8614  C  CG  . GLU H  1 109 ? 82.363  -19.310 -10.822 1.00 46.06 ? 109  GLU H CG  1 
ATOM   8615  C  CD  . GLU H  1 109 ? 82.415  -19.613 -12.319 1.00 53.85 ? 109  GLU H CD  1 
ATOM   8616  O  OE1 . GLU H  1 109 ? 81.341  -19.891 -12.925 1.00 48.02 ? 109  GLU H OE1 1 
ATOM   8617  O  OE2 . GLU H  1 109 ? 83.535  -19.566 -12.886 1.00 55.41 ? 109  GLU H OE2 1 
ATOM   8618  N  N   . HIS H  1 110 ? 82.546  -15.070 -12.058 1.00 34.77 ? 110  HIS H N   1 
ATOM   8619  C  CA  . HIS H  1 110 ? 83.279  -13.856 -12.375 1.00 29.75 ? 110  HIS H CA  1 
ATOM   8620  C  C   . HIS H  1 110 ? 82.341  -12.815 -12.951 1.00 25.52 ? 110  HIS H C   1 
ATOM   8621  O  O   . HIS H  1 110 ? 82.760  -11.981 -13.756 1.00 25.07 ? 110  HIS H O   1 
ATOM   8622  C  CB  . HIS H  1 110 ? 84.416  -14.146 -13.367 1.00 30.29 ? 110  HIS H CB  1 
ATOM   8623  C  CG  . HIS H  1 110 ? 85.437  -15.121 -12.851 1.00 33.94 ? 110  HIS H CG  1 
ATOM   8624  N  ND1 . HIS H  1 110 ? 86.451  -15.623 -13.640 1.00 31.20 ? 110  HIS H ND1 1 
ATOM   8625  C  CD2 . HIS H  1 110 ? 85.585  -15.698 -11.633 1.00 32.82 ? 110  HIS H CD2 1 
ATOM   8626  C  CE1 . HIS H  1 110 ? 87.186  -16.457 -12.925 1.00 34.56 ? 110  HIS H CE1 1 
ATOM   8627  N  NE2 . HIS H  1 110 ? 86.680  -16.524 -11.706 1.00 32.44 ? 110  HIS H NE2 1 
ATOM   8628  N  N   . SER H  1 111 ? 81.074  -12.884 -12.545 1.00 25.45 ? 111  SER H N   1 
ATOM   8629  C  CA  . SER H  1 111 ? 80.074  -11.910 -12.962 1.00 23.16 ? 111  SER H CA  1 
ATOM   8630  C  C   . SER H  1 111 ? 80.347  -10.544 -12.333 1.00 21.44 ? 111  SER H C   1 
ATOM   8631  O  O   . SER H  1 111 ? 80.668  -10.450 -11.139 1.00 20.68 ? 111  SER H O   1 
ATOM   8632  C  CB  . SER H  1 111 ? 78.685  -12.384 -12.577 1.00 22.97 ? 111  SER H CB  1 
ATOM   8633  O  OG  . SER H  1 111 ? 77.775  -11.312 -12.695 1.00 22.95 ? 111  SER H OG  1 
ATOM   8634  N  N   . ILE H  1 112 ? 80.240  -9.492  -13.142 1.00 19.08 ? 112  ILE H N   1 
ATOM   8635  C  CA  . ILE H  1 112 ? 80.572  -8.143  -12.692 1.00 18.64 ? 112  ILE H CA  1 
ATOM   8636  C  C   . ILE H  1 112 ? 79.313  -7.364  -12.352 1.00 18.36 ? 112  ILE H C   1 
ATOM   8637  O  O   . ILE H  1 112 ? 79.381  -6.182  -12.017 1.00 17.08 ? 112  ILE H O   1 
ATOM   8638  C  CB  . ILE H  1 112 ? 81.399  -7.369  -13.738 1.00 16.24 ? 112  ILE H CB  1 
ATOM   8639  C  CG1 . ILE H  1 112 ? 80.568  -7.125  -14.996 1.00 16.65 ? 112  ILE H CG1 1 
ATOM   8640  C  CG2 . ILE H  1 112 ? 82.653  -8.139  -14.077 1.00 17.42 ? 112  ILE H CG2 1 
ATOM   8641  C  CD1 . ILE H  1 112 ? 81.237  -6.221  -15.994 1.00 16.55 ? 112  ILE H CD1 1 
ATOM   8642  N  N   . ILE H  1 113 ? 78.166  -8.038  -12.451 1.00 20.29 ? 113  ILE H N   1 
ATOM   8643  C  CA  . ILE H  1 113 ? 76.895  -7.492  -11.973 1.00 19.92 ? 113  ILE H CA  1 
ATOM   8644  C  C   . ILE H  1 113 ? 76.975  -7.210  -10.450 1.00 20.30 ? 113  ILE H C   1 
ATOM   8645  O  O   . ILE H  1 113 ? 77.364  -8.074  -9.654  1.00 15.18 ? 113  ILE H O   1 
ATOM   8646  C  CB  . ILE H  1 113 ? 75.710  -8.445  -12.292 1.00 20.91 ? 113  ILE H CB  1 
ATOM   8647  C  CG1 . ILE H  1 113 ? 75.596  -8.683  -13.793 1.00 21.73 ? 113  ILE H CG1 1 
ATOM   8648  C  CG2 . ILE H  1 113 ? 74.391  -7.884  -11.775 1.00 20.03 ? 113  ILE H CG2 1 
ATOM   8649  C  CD1 . ILE H  1 113 ? 75.444  -7.441  -14.576 1.00 20.59 ? 113  ILE H CD1 1 
ATOM   8650  N  N   . GLY H  1 114 ? 76.617  -5.988  -10.058 1.00 18.41 ? 114  GLY H N   1 
ATOM   8651  C  CA  . GLY H  1 114 ? 76.641  -5.603  -8.666  1.00 15.54 ? 114  GLY H CA  1 
ATOM   8652  C  C   . GLY H  1 114 ? 77.991  -5.080  -8.238  1.00 16.43 ? 114  GLY H C   1 
ATOM   8653  O  O   . GLY H  1 114 ? 78.201  -4.772  -7.075  1.00 16.91 ? 114  GLY H O   1 
ATOM   8654  N  N   . ARG H  1 115 ? 78.925  -5.003  -9.175  1.00 18.74 ? 115  ARG H N   1 
ATOM   8655  C  CA  . ARG H  1 115 ? 80.239  -4.442  -8.876  1.00 18.96 ? 115  ARG H CA  1 
ATOM   8656  C  C   . ARG H  1 115 ? 80.339  -3.107  -9.597  1.00 17.41 ? 115  ARG H C   1 
ATOM   8657  O  O   . ARG H  1 115 ? 79.344  -2.627  -10.140 1.00 19.38 ? 115  ARG H O   1 
ATOM   8658  C  CB  . ARG H  1 115 ? 81.351  -5.416  -9.269  1.00 16.02 ? 115  ARG H CB  1 
ATOM   8659  C  CG  . ARG H  1 115 ? 81.111  -6.805  -8.724  1.00 16.47 ? 115  ARG H CG  1 
ATOM   8660  C  CD  . ARG H  1 115 ? 82.193  -7.777  -9.128  1.00 17.28 ? 115  ARG H CD  1 
ATOM   8661  N  NE  . ARG H  1 115 ? 81.887  -9.132  -8.693  1.00 17.71 ? 115  ARG H NE  1 
ATOM   8662  C  CZ  . ARG H  1 115 ? 82.155  -9.600  -7.477  1.00 20.73 ? 115  ARG H CZ  1 
ATOM   8663  N  NH1 . ARG H  1 115 ? 82.730  -8.817  -6.564  1.00 19.85 ? 115  ARG H NH1 1 
ATOM   8664  N  NH2 . ARG H  1 115 ? 81.857  -10.854 -7.168  1.00 19.07 ? 115  ARG H NH2 1 
ATOM   8665  N  N   . THR H  1 116 ? 81.525  -2.510  -9.620  1.00 18.35 ? 116  THR H N   1 
ATOM   8666  C  CA  . THR H  1 116 ? 81.659  -1.116  -10.057 1.00 19.58 ? 116  THR H CA  1 
ATOM   8667  C  C   . THR H  1 116 ? 82.538  -0.910  -11.294 1.00 19.43 ? 116  THR H C   1 
ATOM   8668  O  O   . THR H  1 116 ? 83.659  -1.434  -11.354 1.00 17.81 ? 116  THR H O   1 
ATOM   8669  C  CB  . THR H  1 116 ? 82.208  -0.253  -8.891  1.00 18.72 ? 116  THR H CB  1 
ATOM   8670  O  OG1 . THR H  1 116 ? 81.348  -0.394  -7.752  1.00 15.60 ? 116  THR H OG1 1 
ATOM   8671  C  CG2 . THR H  1 116 ? 82.323  1.234   -9.282  1.00 16.65 ? 116  THR H CG2 1 
ATOM   8672  N  N   . MET H  1 117 ? 82.026  -0.163  -12.278 1.00 17.40 ? 117  MET H N   1 
ATOM   8673  C  CA  . MET H  1 117 ? 82.871  0.373   -13.346 1.00 20.83 ? 117  MET H CA  1 
ATOM   8674  C  C   . MET H  1 117 ? 83.498  1.666   -12.852 1.00 19.78 ? 117  MET H C   1 
ATOM   8675  O  O   . MET H  1 117 ? 82.798  2.533   -12.325 1.00 17.39 ? 117  MET H O   1 
ATOM   8676  C  CB  . MET H  1 117 ? 82.084  0.696   -14.620 1.00 20.61 ? 117  MET H CB  1 
ATOM   8677  C  CG  . MET H  1 117 ? 82.011  -0.401  -15.669 1.00 22.70 ? 117  MET H CG  1 
ATOM   8678  S  SD  . MET H  1 117 ? 83.545  -1.257  -16.105 1.00 32.14 ? 117  MET H SD  1 
ATOM   8679  C  CE  . MET H  1 117 ? 84.703  0.088   -16.221 1.00 25.35 ? 117  MET H CE  1 
ATOM   8680  N  N   . VAL H  1 118 ? 84.813  1.798   -13.017 1.00 21.28 ? 118  VAL H N   1 
ATOM   8681  C  CA  . VAL H  1 118 ? 85.446  3.091   -12.779 1.00 19.47 ? 118  VAL H CA  1 
ATOM   8682  C  C   . VAL H  1 118 ? 86.458  3.507   -13.849 1.00 19.72 ? 118  VAL H C   1 
ATOM   8683  O  O   . VAL H  1 118 ? 87.219  2.686   -14.385 1.00 17.88 ? 118  VAL H O   1 
ATOM   8684  C  CB  . VAL H  1 118 ? 85.948  3.278   -11.315 1.00 18.90 ? 118  VAL H CB  1 
ATOM   8685  C  CG1 . VAL H  1 118 ? 86.065  1.957   -10.615 1.00 21.85 ? 118  VAL H CG1 1 
ATOM   8686  C  CG2 . VAL H  1 118 ? 87.230  4.108   -11.236 1.00 18.20 ? 118  VAL H CG2 1 
ATOM   8687  N  N   . VAL H  1 119 ? 86.376  4.793   -14.188 1.00 18.86 ? 119  VAL H N   1 
ATOM   8688  C  CA  . VAL H  1 119 ? 87.278  5.459   -15.102 1.00 16.85 ? 119  VAL H CA  1 
ATOM   8689  C  C   . VAL H  1 119 ? 88.238  6.274   -14.249 1.00 17.95 ? 119  VAL H C   1 
ATOM   8690  O  O   . VAL H  1 119 ? 87.828  6.970   -13.314 1.00 17.19 ? 119  VAL H O   1 
ATOM   8691  C  CB  . VAL H  1 119 ? 86.510  6.363   -16.113 1.00 17.68 ? 119  VAL H CB  1 
ATOM   8692  C  CG1 . VAL H  1 119 ? 85.849  7.531   -15.415 1.00 16.60 ? 119  VAL H CG1 1 
ATOM   8693  C  CG2 . VAL H  1 119 ? 87.437  6.865   -17.224 1.00 16.41 ? 119  VAL H CG2 1 
ATOM   8694  N  N   . HIS H  1 120 ? 89.521  6.184   -14.581 1.00 18.84 ? 120  HIS H N   1 
ATOM   8695  C  CA  . HIS H  1 120 ? 90.578  6.753   -13.755 1.00 19.40 ? 120  HIS H CA  1 
ATOM   8696  C  C   . HIS H  1 120 ? 91.188  8.030   -14.318 1.00 19.57 ? 120  HIS H C   1 
ATOM   8697  O  O   . HIS H  1 120 ? 91.051  8.353   -15.508 1.00 19.01 ? 120  HIS H O   1 
ATOM   8698  C  CB  . HIS H  1 120 ? 91.670  5.709   -13.524 1.00 17.73 ? 120  HIS H CB  1 
ATOM   8699  C  CG  . HIS H  1 120 ? 91.262  4.630   -12.579 1.00 16.43 ? 120  HIS H CG  1 
ATOM   8700  N  ND1 . HIS H  1 120 ? 91.437  4.738   -11.218 1.00 16.06 ? 120  HIS H ND1 1 
ATOM   8701  C  CD2 . HIS H  1 120 ? 90.648  3.446   -12.789 1.00 16.77 ? 120  HIS H CD2 1 
ATOM   8702  C  CE1 . HIS H  1 120 ? 90.967  3.655   -10.630 1.00 18.11 ? 120  HIS H CE1 1 
ATOM   8703  N  NE2 . HIS H  1 120 ? 90.473  2.858   -11.559 1.00 18.99 ? 120  HIS H NE2 1 
ATOM   8704  N  N   . GLU H  1 121 ? 91.864  8.740   -13.426 1.00 20.90 ? 121  GLU H N   1 
ATOM   8705  C  CA  . GLU H  1 121 ? 92.558  9.984   -13.722 1.00 21.54 ? 121  GLU H CA  1 
ATOM   8706  C  C   . GLU H  1 121 ? 93.442  9.913   -14.970 1.00 23.82 ? 121  GLU H C   1 
ATOM   8707  O  O   . GLU H  1 121 ? 93.298  10.728  -15.887 1.00 22.60 ? 121  GLU H O   1 
ATOM   8708  C  CB  . GLU H  1 121 ? 93.406  10.344  -12.514 1.00 19.04 ? 121  GLU H CB  1 
ATOM   8709  C  CG  . GLU H  1 121 ? 94.048  11.694  -12.557 1.00 23.88 ? 121  GLU H CG  1 
ATOM   8710  C  CD  . GLU H  1 121 ? 95.206  11.779  -11.580 1.00 26.64 ? 121  GLU H CD  1 
ATOM   8711  O  OE1 . GLU H  1 121 ? 95.151  11.070  -10.554 1.00 26.35 ? 121  GLU H OE1 1 
ATOM   8712  O  OE2 . GLU H  1 121 ? 96.175  12.528  -11.845 1.00 32.70 ? 121  GLU H OE2 1 
ATOM   8713  N  N   . LYS H  1 122 ? 94.360  8.945   -14.994 1.00 23.75 ? 122  LYS H N   1 
ATOM   8714  C  CA  . LYS H  1 122 ? 95.354  8.843   -16.065 1.00 22.09 ? 122  LYS H CA  1 
ATOM   8715  C  C   . LYS H  1 122 ? 95.538  7.441   -16.658 1.00 22.37 ? 122  LYS H C   1 
ATOM   8716  O  O   . LYS H  1 122 ? 94.766  6.511   -16.383 1.00 21.64 ? 122  LYS H O   1 
ATOM   8717  C  CB  . LYS H  1 122 ? 96.706  9.410   -15.608 1.00 22.41 ? 122  LYS H CB  1 
ATOM   8718  C  CG  . LYS H  1 122 ? 96.847  9.617   -14.105 1.00 22.73 ? 122  LYS H CG  1 
ATOM   8719  C  CD  . LYS H  1 122 ? 97.483  8.442   -13.419 1.00 22.74 ? 122  LYS H CD  1 
ATOM   8720  C  CE  . LYS H  1 122 ? 98.928  8.728   -13.076 1.00 22.32 ? 122  LYS H CE  1 
ATOM   8721  N  NZ  . LYS H  1 122 ? 99.052  10.057  -12.470 1.00 24.94 ? 122  LYS H NZ  1 
ATOM   8722  N  N   . GLN H  1 123 ? 96.580  7.310   -17.473 1.00 23.27 ? 123  GLN H N   1 
ATOM   8723  C  CA  . GLN H  1 123 ? 96.806  6.120   -18.278 1.00 20.57 ? 123  GLN H CA  1 
ATOM   8724  C  C   . GLN H  1 123 ? 97.137  4.917   -17.426 1.00 18.54 ? 123  GLN H C   1 
ATOM   8725  O  O   . GLN H  1 123 ? 97.940  4.995   -16.514 1.00 22.26 ? 123  GLN H O   1 
ATOM   8726  C  CB  . GLN H  1 123 ? 97.931  6.365   -19.280 1.00 21.39 ? 123  GLN H CB  1 
ATOM   8727  C  CG  . GLN H  1 123 ? 98.085  5.275   -20.334 1.00 22.09 ? 123  GLN H CG  1 
ATOM   8728  C  CD  . GLN H  1 123 ? 99.146  5.607   -21.370 1.00 22.64 ? 123  GLN H CD  1 
ATOM   8729  O  OE1 . GLN H  1 123 ? 99.474  6.776   -21.591 1.00 22.92 ? 123  GLN H OE1 1 
ATOM   8730  N  NE2 . GLN H  1 123 ? 99.688  4.579   -22.010 1.00 21.68 ? 123  GLN H NE2 1 
ATOM   8731  N  N   . ASP H  1 124 ? 96.503  3.800   -17.734 1.00 19.17 ? 124  ASP H N   1 
ATOM   8732  C  CA  . ASP H  1 124 ? 96.822  2.531   -17.110 1.00 18.33 ? 124  ASP H CA  1 
ATOM   8733  C  C   . ASP H  1 124 ? 98.098  1.977   -17.793 1.00 19.57 ? 124  ASP H C   1 
ATOM   8734  O  O   . ASP H  1 124 ? 98.149  1.825   -19.021 1.00 20.00 ? 124  ASP H O   1 
ATOM   8735  C  CB  . ASP H  1 124 ? 95.582  1.632   -17.225 1.00 17.75 ? 124  ASP H CB  1 
ATOM   8736  C  CG  . ASP H  1 124 ? 95.858  0.168   -16.955 1.00 20.16 ? 124  ASP H CG  1 
ATOM   8737  O  OD1 . ASP H  1 124 ? 96.985  -0.193  -16.577 1.00 20.98 ? 124  ASP H OD1 1 
ATOM   8738  O  OD2 . ASP H  1 124 ? 94.918  -0.635  -17.127 1.00 21.89 ? 124  ASP H OD2 1 
ATOM   8739  N  N   . ASP H  1 125 ? 99.143  1.735   -16.995 1.00 21.61 ? 125  ASP H N   1 
ATOM   8740  C  CA  . ASP H  1 125 ? 100.445 1.271   -17.511 1.00 22.79 ? 125  ASP H CA  1 
ATOM   8741  C  C   . ASP H  1 125 ? 100.523 -0.257  -17.682 1.00 23.22 ? 125  ASP H C   1 
ATOM   8742  O  O   . ASP H  1 125 ? 101.598 -0.808  -17.905 1.00 20.77 ? 125  ASP H O   1 
ATOM   8743  C  CB  . ASP H  1 125 ? 101.627 1.806   -16.665 1.00 20.60 ? 125  ASP H CB  1 
ATOM   8744  C  CG  . ASP H  1 125 ? 101.739 1.142   -15.292 1.00 23.05 ? 125  ASP H CG  1 
ATOM   8745  O  OD1 . ASP H  1 125 ? 101.301 -0.021  -15.143 1.00 22.67 ? 125  ASP H OD1 1 
ATOM   8746  O  OD2 . ASP H  1 125 ? 102.290 1.775   -14.353 1.00 21.28 ? 125  ASP H OD2 1 
ATOM   8747  N  N   . LEU H  1 126 ? 99.369  -0.915  -17.574 1.00 23.17 ? 126  LEU H N   1 
ATOM   8748  C  CA  . LEU H  1 126 ? 99.202  -2.346  -17.864 1.00 23.83 ? 126  LEU H CA  1 
ATOM   8749  C  C   . LEU H  1 126 ? 100.072 -3.278  -17.021 1.00 21.57 ? 126  LEU H C   1 
ATOM   8750  O  O   . LEU H  1 126 ? 100.372 -4.390  -17.435 1.00 22.88 ? 126  LEU H O   1 
ATOM   8751  C  CB  . LEU H  1 126 ? 99.404  -2.635  -19.355 1.00 22.31 ? 126  LEU H CB  1 
ATOM   8752  C  CG  . LEU H  1 126 ? 98.742  -1.693  -20.362 1.00 25.10 ? 126  LEU H CG  1 
ATOM   8753  C  CD1 . LEU H  1 126 ? 99.128  -2.112  -21.779 1.00 24.10 ? 126  LEU H CD1 1 
ATOM   8754  C  CD2 . LEU H  1 126 ? 97.213  -1.638  -20.195 1.00 20.89 ? 126  LEU H CD2 1 
ATOM   8755  N  N   . GLY H  1 127 ? 100.454 -2.823  -15.834 1.00 23.20 ? 127  GLY H N   1 
ATOM   8756  C  CA  . GLY H  1 127 ? 101.282 -3.610  -14.931 1.00 24.83 ? 127  GLY H CA  1 
ATOM   8757  C  C   . GLY H  1 127 ? 102.770 -3.622  -15.259 1.00 23.94 ? 127  GLY H C   1 
ATOM   8758  O  O   . GLY H  1 127 ? 103.512 -4.460  -14.748 1.00 24.55 ? 127  GLY H O   1 
ATOM   8759  N  N   . LYS H  1 128 ? 103.215 -2.686  -16.093 1.00 22.49 ? 128  LYS H N   1 
ATOM   8760  C  CA  . LYS H  1 128 ? 104.603 -2.669  -16.544 1.00 23.86 ? 128  LYS H CA  1 
ATOM   8761  C  C   . LYS H  1 128 ? 105.389 -1.405  -16.159 1.00 24.09 ? 128  LYS H C   1 
ATOM   8762  O  O   . LYS H  1 128 ? 106.307 -0.999  -16.881 1.00 24.76 ? 128  LYS H O   1 
ATOM   8763  C  CB  . LYS H  1 128 ? 104.665 -2.848  -18.068 1.00 23.34 ? 128  LYS H CB  1 
ATOM   8764  C  CG  . LYS H  1 128 ? 103.882 -4.034  -18.609 1.00 25.24 ? 128  LYS H CG  1 
ATOM   8765  C  CD  . LYS H  1 128 ? 103.972 -4.103  -20.127 1.00 24.88 ? 128  LYS H CD  1 
ATOM   8766  C  CE  . LYS H  1 128 ? 102.837 -4.935  -20.695 1.00 28.37 ? 128  LYS H CE  1 
ATOM   8767  N  NZ  . LYS H  1 128 ? 102.696 -6.232  -19.967 1.00 30.84 ? 128  LYS H NZ  1 
ATOM   8768  N  N   . GLY H  1 129 ? 105.044 -0.790  -15.033 1.00 23.34 ? 129  GLY H N   1 
ATOM   8769  C  CA  . GLY H  1 129 ? 105.658 0.467   -14.636 1.00 20.93 ? 129  GLY H CA  1 
ATOM   8770  C  C   . GLY H  1 129 ? 106.752 0.313   -13.594 1.00 21.23 ? 129  GLY H C   1 
ATOM   8771  O  O   . GLY H  1 129 ? 107.325 1.297   -13.118 1.00 20.30 ? 129  GLY H O   1 
ATOM   8772  N  N   . GLY H  1 130 ? 107.039 -0.928  -13.226 1.00 21.44 ? 130  GLY H N   1 
ATOM   8773  C  CA  . GLY H  1 130 ? 108.180 -1.220  -12.379 1.00 19.95 ? 130  GLY H CA  1 
ATOM   8774  C  C   . GLY H  1 130 ? 108.081 -0.706  -10.964 1.00 21.05 ? 130  GLY H C   1 
ATOM   8775  O  O   . GLY H  1 130 ? 109.050 -0.197  -10.416 1.00 22.30 ? 130  GLY H O   1 
ATOM   8776  N  N   . ASN H  1 131 ? 106.899 -0.826  -10.376 1.00 22.24 ? 131  ASN H N   1 
ATOM   8777  C  CA  . ASN H  1 131 ? 106.713 -0.596  -8.949  1.00 23.35 ? 131  ASN H CA  1 
ATOM   8778  C  C   . ASN H  1 131 ? 105.434 -1.269  -8.490  1.00 23.71 ? 131  ASN H C   1 
ATOM   8779  O  O   . ASN H  1 131 ? 104.670 -1.793  -9.299  1.00 23.71 ? 131  ASN H O   1 
ATOM   8780  C  CB  . ASN H  1 131 ? 106.718 0.898   -8.569  1.00 23.07 ? 131  ASN H CB  1 
ATOM   8781  C  CG  . ASN H  1 131 ? 105.694 1.732   -9.345  1.00 24.61 ? 131  ASN H CG  1 
ATOM   8782  O  OD1 . ASN H  1 131 ? 104.768 1.207   -9.970  1.00 21.88 ? 131  ASN H OD1 1 
ATOM   8783  N  ND2 . ASN H  1 131 ? 105.869 3.054   -9.301  1.00 23.82 ? 131  ASN H ND2 1 
ATOM   8784  N  N   . GLU H  1 132 ? 105.200 -1.252  -7.191  1.00 25.85 ? 132  GLU H N   1 
ATOM   8785  C  CA  . GLU H  1 132 ? 104.050 -1.942  -6.640  1.00 25.59 ? 132  GLU H CA  1 
ATOM   8786  C  C   . GLU H  1 132 ? 102.701 -1.343  -7.075  1.00 25.87 ? 132  GLU H C   1 
ATOM   8787  O  O   . GLU H  1 132 ? 101.745 -2.088  -7.299  1.00 23.88 ? 132  GLU H O   1 
ATOM   8788  C  CB  . GLU H  1 132 ? 104.166 -2.011  -5.123  1.00 29.39 ? 132  GLU H CB  1 
ATOM   8789  C  CG  . GLU H  1 132 ? 103.148 -2.926  -4.497  1.00 38.32 ? 132  GLU H CG  1 
ATOM   8790  C  CD  . GLU H  1 132 ? 103.310 -3.010  -3.006  1.00 46.88 ? 132  GLU H CD  1 
ATOM   8791  O  OE1 . GLU H  1 132 ? 102.280 -3.158  -2.307  1.00 45.71 ? 132  GLU H OE1 1 
ATOM   8792  O  OE2 . GLU H  1 132 ? 104.473 -2.918  -2.541  1.00 56.08 ? 132  GLU H OE2 1 
ATOM   8793  N  N   . GLU H  1 133 ? 102.615 -0.015  -7.199  1.00 23.51 ? 133  GLU H N   1 
ATOM   8794  C  CA  . GLU H  1 133 ? 101.368 0.607   -7.636  1.00 22.05 ? 133  GLU H CA  1 
ATOM   8795  C  C   . GLU H  1 133 ? 100.987 0.106   -9.008  1.00 21.83 ? 133  GLU H C   1 
ATOM   8796  O  O   . GLU H  1 133 ? 99.818  -0.016  -9.324  1.00 23.94 ? 133  GLU H O   1 
ATOM   8797  C  CB  . GLU H  1 133 ? 101.444 2.139   -7.668  1.00 23.32 ? 133  GLU H CB  1 
ATOM   8798  C  CG  . GLU H  1 133 ? 100.775 2.843   -6.480  1.00 28.76 ? 133  GLU H CG  1 
ATOM   8799  C  CD  . GLU H  1 133 ? 99.333  2.402   -6.226  1.00 31.98 ? 133  GLU H CD  1 
ATOM   8800  O  OE1 . GLU H  1 133 ? 98.518  2.399   -7.177  1.00 28.82 ? 133  GLU H OE1 1 
ATOM   8801  O  OE2 . GLU H  1 133 ? 99.008  2.076   -5.059  1.00 37.13 ? 133  GLU H OE2 1 
ATOM   8802  N  N   . SER H  1 134 ? 101.978 -0.171  -9.837  1.00 22.36 ? 134  SER H N   1 
ATOM   8803  C  CA  . SER H  1 134 ? 101.705 -0.639  -11.181 1.00 21.18 ? 134  SER H CA  1 
ATOM   8804  C  C   . SER H  1 134 ? 101.054 -2.019  -11.174 1.00 23.01 ? 134  SER H C   1 
ATOM   8805  O  O   . SER H  1 134 ? 100.190 -2.302  -12.000 1.00 21.89 ? 134  SER H O   1 
ATOM   8806  C  CB  . SER H  1 134 ? 102.988 -0.688  -11.997 1.00 20.88 ? 134  SER H CB  1 
ATOM   8807  O  OG  . SER H  1 134 ? 102.762 -1.418  -13.188 1.00 22.18 ? 134  SER H OG  1 
ATOM   8808  N  N   . THR H  1 135 ? 101.488 -2.879  -10.252 1.00 23.60 ? 135  THR H N   1 
ATOM   8809  C  CA  . THR H  1 135 ? 101.025 -4.266  -10.205 1.00 23.77 ? 135  THR H CA  1 
ATOM   8810  C  C   . THR H  1 135 ? 99.638  -4.382  -9.565  1.00 23.22 ? 135  THR H C   1 
ATOM   8811  O  O   . THR H  1 135 ? 99.077  -5.483  -9.451  1.00 23.65 ? 135  THR H O   1 
ATOM   8812  C  CB  . THR H  1 135 ? 102.018 -5.177  -9.427  1.00 24.62 ? 135  THR H CB  1 
ATOM   8813  O  OG1 . THR H  1 135 ? 101.962 -4.870  -8.030  1.00 25.55 ? 135  THR H OG1 1 
ATOM   8814  C  CG2 . THR H  1 135 ? 103.433 -4.995  -9.927  1.00 22.32 ? 135  THR H CG2 1 
ATOM   8815  N  N   . LYS H  1 136 ? 99.097  -3.237  -9.154  1.00 23.07 ? 136  LYS H N   1 
ATOM   8816  C  CA  . LYS H  1 136 ? 97.844  -3.176  -8.410  1.00 22.61 ? 136  LYS H CA  1 
ATOM   8817  C  C   . LYS H  1 136 ? 96.810  -2.371  -9.168  1.00 21.72 ? 136  LYS H C   1 
ATOM   8818  O  O   . LYS H  1 136 ? 95.695  -2.827  -9.370  1.00 21.37 ? 136  LYS H O   1 
ATOM   8819  C  CB  . LYS H  1 136 ? 98.061  -2.534  -7.032  1.00 23.21 ? 136  LYS H CB  1 
ATOM   8820  C  CG  . LYS H  1 136 ? 98.445  -3.514  -5.929  1.00 25.01 ? 136  LYS H CG  1 
ATOM   8821  C  CD  . LYS H  1 136 ? 99.281  -2.862  -4.845  1.00 25.69 ? 136  LYS H CD  1 
ATOM   8822  C  CE  . LYS H  1 136 ? 99.070  -1.360  -4.804  1.00 28.52 ? 136  LYS H CE  1 
ATOM   8823  N  NZ  . LYS H  1 136 ? 97.698  -0.975  -4.361  1.00 34.83 ? 136  LYS H NZ  1 
ATOM   8824  N  N   . THR H  1 137 ? 97.189  -1.163  -9.569  1.00 21.51 ? 137  THR H N   1 
ATOM   8825  C  CA  . THR H  1 137 ? 96.260  -0.219  -10.174 1.00 21.80 ? 137  THR H CA  1 
ATOM   8826  C  C   . THR H  1 137 ? 96.740  0.252   -11.552 1.00 23.41 ? 137  THR H C   1 
ATOM   8827  O  O   . THR H  1 137 ? 96.023  0.963   -12.261 1.00 24.09 ? 137  THR H O   1 
ATOM   8828  C  CB  . THR H  1 137 ? 96.054  1.008   -9.254  1.00 22.76 ? 137  THR H CB  1 
ATOM   8829  O  OG1 . THR H  1 137 ? 97.243  1.803   -9.238  1.00 21.93 ? 137  THR H OG1 1 
ATOM   8830  C  CG2 . THR H  1 137 ? 95.739  0.567   -7.830  1.00 21.71 ? 137  THR H CG2 1 
ATOM   8831  N  N   . GLY H  1 138 ? 97.953  -0.150  -11.928 1.00 22.00 ? 138  GLY H N   1 
ATOM   8832  C  CA  . GLY H  1 138 ? 98.543  0.263   -13.186 1.00 20.35 ? 138  GLY H CA  1 
ATOM   8833  C  C   . GLY H  1 138 ? 98.861  1.742   -13.181 1.00 20.15 ? 138  GLY H C   1 
ATOM   8834  O  O   . GLY H  1 138 ? 98.994  2.349   -14.237 1.00 22.43 ? 138  GLY H O   1 
ATOM   8835  N  N   . ASN H  1 139 ? 98.982  2.326   -11.996 1.00 20.90 ? 139  ASN H N   1 
ATOM   8836  C  CA  . ASN H  1 139 ? 99.276  3.756   -11.871 1.00 24.50 ? 139  ASN H CA  1 
ATOM   8837  C  C   . ASN H  1 139 ? 98.264  4.633   -12.602 1.00 24.24 ? 139  ASN H C   1 
ATOM   8838  O  O   . ASN H  1 139 ? 98.608  5.714   -13.104 1.00 24.51 ? 139  ASN H O   1 
ATOM   8839  C  CB  . ASN H  1 139 ? 100.690 4.075   -12.384 1.00 24.77 ? 139  ASN H CB  1 
ATOM   8840  C  CG  . ASN H  1 139 ? 101.765 3.636   -11.426 1.00 22.33 ? 139  ASN H CG  1 
ATOM   8841  O  OD1 . ASN H  1 139 ? 101.920 4.211   -10.344 1.00 24.13 ? 139  ASN H OD1 1 
ATOM   8842  N  ND2 . ASN H  1 139 ? 102.522 2.612   -11.815 1.00 20.86 ? 139  ASN H ND2 1 
ATOM   8843  N  N   . ALA H  1 140 ? 97.022  4.160   -12.662 1.00 22.94 ? 140  ALA H N   1 
ATOM   8844  C  CA  . ALA H  1 140 ? 95.948  4.874   -13.341 1.00 20.86 ? 140  ALA H CA  1 
ATOM   8845  C  C   . ALA H  1 140 ? 95.455  6.073   -12.533 1.00 21.27 ? 140  ALA H C   1 
ATOM   8846  O  O   . ALA H  1 140 ? 94.659  6.863   -13.019 1.00 20.65 ? 140  ALA H O   1 
ATOM   8847  C  CB  . ALA H  1 140 ? 94.801  3.925   -13.639 1.00 18.27 ? 140  ALA H CB  1 
ATOM   8848  N  N   . GLY H  1 141 ? 95.918  6.188   -11.291 1.00 24.24 ? 141  GLY H N   1 
ATOM   8849  C  CA  . GLY H  1 141 ? 95.635  7.350   -10.467 1.00 24.26 ? 141  GLY H CA  1 
ATOM   8850  C  C   . GLY H  1 141 ? 94.271  7.357   -9.813  1.00 23.12 ? 141  GLY H C   1 
ATOM   8851  O  O   . GLY H  1 141 ? 93.716  6.303   -9.527  1.00 23.19 ? 141  GLY H O   1 
ATOM   8852  N  N   . SER H  1 142 ? 93.734  8.557   -9.597  1.00 21.10 ? 142  SER H N   1 
ATOM   8853  C  CA  . SER H  1 142 ? 92.467  8.763   -8.879  1.00 24.60 ? 142  SER H CA  1 
ATOM   8854  C  C   . SER H  1 142 ? 91.215  8.233   -9.603  1.00 20.08 ? 142  SER H C   1 
ATOM   8855  O  O   . SER H  1 142 ? 91.214  8.056   -10.815 1.00 18.39 ? 142  SER H O   1 
ATOM   8856  C  CB  . SER H  1 142 ? 92.262  10.257  -8.597  1.00 24.15 ? 142  SER H CB  1 
ATOM   8857  O  OG  . SER H  1 142 ? 91.447  10.835  -9.607  1.00 23.82 ? 142  SER H OG  1 
ATOM   8858  N  N   . ARG H  1 143 ? 90.142  8.017   -8.846  1.00 20.35 ? 143  ARG H N   1 
ATOM   8859  C  CA  . ARG H  1 143 ? 88.876  7.537   -9.410  1.00 21.68 ? 143  ARG H CA  1 
ATOM   8860  C  C   . ARG H  1 143 ? 87.964  8.710   -9.788  1.00 21.27 ? 143  ARG H C   1 
ATOM   8861  O  O   . ARG H  1 143 ? 87.440  9.399   -8.911  1.00 21.61 ? 143  ARG H O   1 
ATOM   8862  C  CB  . ARG H  1 143 ? 88.181  6.577   -8.426  1.00 22.04 ? 143  ARG H CB  1 
ATOM   8863  C  CG  . ARG H  1 143 ? 89.160  5.584   -7.812  1.00 22.45 ? 143  ARG H CG  1 
ATOM   8864  C  CD  . ARG H  1 143 ? 88.578  4.562   -6.825  1.00 20.37 ? 143  ARG H CD  1 
ATOM   8865  N  NE  . ARG H  1 143 ? 89.672  3.678   -6.408  1.00 21.66 ? 143  ARG H NE  1 
ATOM   8866  C  CZ  . ARG H  1 143 ? 89.529  2.463   -5.889  1.00 19.39 ? 143  ARG H CZ  1 
ATOM   8867  N  NH1 . ARG H  1 143 ? 88.328  1.950   -5.687  1.00 18.36 ? 143  ARG H NH1 1 
ATOM   8868  N  NH2 . ARG H  1 143 ? 90.597  1.756   -5.573  1.00 20.73 ? 143  ARG H NH2 1 
ATOM   8869  N  N   . LEU H  1 144 ? 87.788  8.933   -11.092 1.00 17.50 ? 144  LEU H N   1 
ATOM   8870  C  CA  . LEU H  1 144 ? 87.088  10.116  -11.599 1.00 18.38 ? 144  LEU H CA  1 
ATOM   8871  C  C   . LEU H  1 144 ? 85.564  9.985   -11.547 1.00 19.53 ? 144  LEU H C   1 
ATOM   8872  O  O   . LEU H  1 144 ? 84.856  10.954  -11.266 1.00 16.71 ? 144  LEU H O   1 
ATOM   8873  C  CB  . LEU H  1 144 ? 87.519  10.421  -13.042 1.00 18.32 ? 144  LEU H CB  1 
ATOM   8874  C  CG  . LEU H  1 144 ? 88.978  10.787  -13.313 1.00 17.32 ? 144  LEU H CG  1 
ATOM   8875  C  CD1 . LEU H  1 144 ? 89.147  11.064  -14.791 1.00 17.93 ? 144  LEU H CD1 1 
ATOM   8876  C  CD2 . LEU H  1 144 ? 89.395  11.986  -12.495 1.00 15.69 ? 144  LEU H CD2 1 
ATOM   8877  N  N   . ALA H  1 145 ? 85.070  8.783   -11.833 1.00 17.47 ? 145  ALA H N   1 
ATOM   8878  C  CA  . ALA H  1 145 ? 83.640  8.512   -11.870 1.00 15.88 ? 145  ALA H CA  1 
ATOM   8879  C  C   . ALA H  1 145 ? 83.455  7.009   -11.773 1.00 17.40 ? 145  ALA H C   1 
ATOM   8880  O  O   . ALA H  1 145 ? 84.333  6.236   -12.160 1.00 18.56 ? 145  ALA H O   1 
ATOM   8881  C  CB  . ALA H  1 145 ? 83.022  9.041   -13.160 1.00 17.40 ? 145  ALA H CB  1 
ATOM   8882  N  N   . CYS H  1 146 ? 82.318  6.584   -11.249 1.00 16.74 ? 146  CYS H N   1 
ATOM   8883  C  CA  . CYS H  1 146 ? 82.062  5.162   -11.122 1.00 19.35 ? 146  CYS H CA  1 
ATOM   8884  C  C   . CYS H  1 146 ? 80.583  4.967   -10.993 1.00 20.02 ? 146  CYS H C   1 
ATOM   8885  O  O   . CYS H  1 146 ? 79.837  5.927   -10.746 1.00 19.17 ? 146  CYS H O   1 
ATOM   8886  C  CB  . CYS H  1 146 ? 82.753  4.580   -9.882  1.00 19.54 ? 146  CYS H CB  1 
ATOM   8887  S  SG  . CYS H  1 146 ? 82.148  5.261   -8.332  1.00 26.08 ? 146  CYS H SG  1 
ATOM   8888  N  N   . GLY H  1 147 ? 80.161  3.720   -11.159 1.00 16.88 ? 147  GLY H N   1 
ATOM   8889  C  CA  . GLY H  1 147 ? 78.776  3.376   -10.981 1.00 13.98 ? 147  GLY H CA  1 
ATOM   8890  C  C   . GLY H  1 147 ? 78.699  1.896   -10.734 1.00 16.84 ? 147  GLY H C   1 
ATOM   8891  O  O   . GLY H  1 147 ? 79.630  1.140   -11.045 1.00 15.66 ? 147  GLY H O   1 
ATOM   8892  N  N   . VAL H  1 148 ? 77.572  1.474   -10.180 1.00 16.60 ? 148  VAL H N   1 
ATOM   8893  C  CA  . VAL H  1 148 ? 77.349  0.063   -9.931  1.00 17.42 ? 148  VAL H CA  1 
ATOM   8894  C  C   . VAL H  1 148 ? 76.754  -0.581  -11.179 1.00 18.07 ? 148  VAL H C   1 
ATOM   8895  O  O   . VAL H  1 148 ? 75.867  -0.011  -11.823 1.00 16.45 ? 148  VAL H O   1 
ATOM   8896  C  CB  . VAL H  1 148 ? 76.463  -0.134  -8.695  1.00 15.05 ? 148  VAL H CB  1 
ATOM   8897  C  CG1 . VAL H  1 148 ? 76.357  -1.601  -8.357  1.00 15.11 ? 148  VAL H CG1 1 
ATOM   8898  C  CG2 . VAL H  1 148 ? 77.057  0.646   -7.539  1.00 15.71 ? 148  VAL H CG2 1 
ATOM   8899  N  N   . ILE H  1 149 ? 77.278  -1.750  -11.534 1.00 17.99 ? 149  ILE H N   1 
ATOM   8900  C  CA  . ILE H  1 149 ? 76.849  -2.449  -12.741 1.00 19.40 ? 149  ILE H CA  1 
ATOM   8901  C  C   . ILE H  1 149 ? 75.543  -3.188  -12.472 1.00 20.17 ? 149  ILE H C   1 
ATOM   8902  O  O   . ILE H  1 149 ? 75.484  -4.096  -11.632 1.00 19.88 ? 149  ILE H O   1 
ATOM   8903  C  CB  . ILE H  1 149 ? 77.954  -3.391  -13.285 1.00 19.82 ? 149  ILE H CB  1 
ATOM   8904  C  CG1 . ILE H  1 149 ? 79.220  -2.570  -13.569 1.00 16.55 ? 149  ILE H CG1 1 
ATOM   8905  C  CG2 . ILE H  1 149 ? 77.462  -4.126  -14.537 1.00 18.24 ? 149  ILE H CG2 1 
ATOM   8906  C  CD1 . ILE H  1 149 ? 80.432  -3.371  -13.882 1.00 17.96 ? 149  ILE H CD1 1 
ATOM   8907  N  N   . GLY H  1 150 ? 74.491  -2.766  -13.167 1.00 18.71 ? 150  GLY H N   1 
ATOM   8908  C  CA  . GLY H  1 150 ? 73.163  -3.269  -12.903 1.00 17.61 ? 150  GLY H CA  1 
ATOM   8909  C  C   . GLY H  1 150 ? 72.540  -4.027  -14.051 1.00 17.88 ? 150  GLY H C   1 
ATOM   8910  O  O   . GLY H  1 150 ? 72.952  -3.898  -15.192 1.00 20.24 ? 150  GLY H O   1 
ATOM   8911  N  N   . ILE H  1 151 ? 71.539  -4.832  -13.721 1.00 20.31 ? 151  ILE H N   1 
ATOM   8912  C  CA  . ILE H  1 151 ? 70.738  -5.571  -14.682 1.00 19.93 ? 151  ILE H CA  1 
ATOM   8913  C  C   . ILE H  1 151 ? 69.886  -4.618  -15.527 1.00 19.93 ? 151  ILE H C   1 
ATOM   8914  O  O   . ILE H  1 151 ? 69.164  -3.783  -14.981 1.00 21.12 ? 151  ILE H O   1 
ATOM   8915  C  CB  . ILE H  1 151 ? 69.836  -6.580  -13.926 1.00 21.16 ? 151  ILE H CB  1 
ATOM   8916  C  CG1 . ILE H  1 151 ? 70.689  -7.647  -13.241 1.00 16.74 ? 151  ILE H CG1 1 
ATOM   8917  C  CG2 . ILE H  1 151 ? 68.811  -7.221  -14.849 1.00 18.78 ? 151  ILE H CG2 1 
ATOM   8918  C  CD1 . ILE H  1 151 ? 69.882  -8.568  -12.346 1.00 18.79 ? 151  ILE H CD1 1 
ATOM   8919  N  N   . ALA H  1 152 ? 69.989  -4.737  -16.853 1.00 21.97 ? 152  ALA H N   1 
ATOM   8920  C  CA  . ALA H  1 152 ? 69.216  -3.929  -17.799 1.00 22.03 ? 152  ALA H CA  1 
ATOM   8921  C  C   . ALA H  1 152 ? 68.338  -4.847  -18.643 1.00 25.43 ? 152  ALA H C   1 
ATOM   8922  O  O   . ALA H  1 152 ? 68.535  -6.064  -18.642 1.00 25.77 ? 152  ALA H O   1 
ATOM   8923  C  CB  . ALA H  1 152 ? 70.148  -3.134  -18.698 1.00 21.67 ? 152  ALA H CB  1 
ATOM   8924  N  N   . GLN H  1 153 ? 67.367  -4.279  -19.360 1.00 27.97 ? 153  GLN H N   1 
ATOM   8925  C  CA  . GLN H  1 153 ? 66.527  -5.085  -20.267 1.00 32.50 ? 153  GLN H CA  1 
ATOM   8926  C  C   . GLN H  1 153 ? 66.912  -4.945  -21.742 1.00 37.10 ? 153  GLN H C   1 
ATOM   8927  O  O   . GLN H  1 153 ? 66.844  -5.927  -22.502 1.00 41.33 ? 153  GLN H O   1 
ATOM   8928  C  CB  . GLN H  1 153 ? 65.030  -4.791  -20.086 1.00 28.91 ? 153  GLN H CB  1 
ATOM   8929  C  CG  . GLN H  1 153 ? 64.600  -3.417  -20.541 1.00 30.19 ? 153  GLN H CG  1 
ATOM   8930  C  CD  . GLN H  1 153 ? 63.092  -3.292  -20.639 1.00 31.37 ? 153  GLN H CD  1 
ATOM   8931  O  OE1 . GLN H  1 153 ? 62.384  -4.294  -20.703 1.00 34.14 ? 153  GLN H OE1 1 
ATOM   8932  N  NE2 . GLN H  1 153 ? 62.594  -2.061  -20.649 1.00 29.47 ? 153  GLN H NE2 1 
ATOM   8933  O  OXT . GLN H  1 153 ? 67.303  -3.858  -22.199 1.00 37.52 ? 153  GLN H OXT 1 
ATOM   8934  N  N   . ALA I  1 1   ? 28.184  -15.840 -18.723 1.00 51.66 ? 1    ALA I N   1 
ATOM   8935  C  CA  . ALA I  1 1   ? 28.753  -14.685 -18.027 1.00 46.22 ? 1    ALA I CA  1 
ATOM   8936  C  C   . ALA I  1 1   ? 27.660  -13.733 -17.542 1.00 42.30 ? 1    ALA I C   1 
ATOM   8937  O  O   . ALA I  1 1   ? 27.086  -12.996 -18.342 1.00 44.61 ? 1    ALA I O   1 
ATOM   8938  C  CB  . ALA I  1 1   ? 29.750  -13.936 -18.941 1.00 43.02 ? 1    ALA I CB  1 
ATOM   8939  N  N   . THR I  1 2   ? 27.365  -13.742 -16.245 1.00 36.79 ? 2    THR I N   1 
ATOM   8940  C  CA  . THR I  1 2   ? 26.412  -12.777 -15.712 1.00 34.37 ? 2    THR I CA  1 
ATOM   8941  C  C   . THR I  1 2   ? 27.042  -11.379 -15.703 1.00 33.06 ? 2    THR I C   1 
ATOM   8942  O  O   . THR I  1 2   ? 28.207  -11.207 -15.337 1.00 31.76 ? 2    THR I O   1 
ATOM   8943  C  CB  . THR I  1 2   ? 25.938  -13.120 -14.270 1.00 35.92 ? 2    THR I CB  1 
ATOM   8944  O  OG1 . THR I  1 2   ? 25.778  -14.535 -14.106 1.00 38.64 ? 2    THR I OG1 1 
ATOM   8945  C  CG2 . THR I  1 2   ? 24.612  -12.432 -13.967 1.00 34.82 ? 2    THR I CG2 1 
ATOM   8946  N  N   . LYS I  1 3   ? 26.269  -10.383 -16.120 1.00 31.05 ? 3    LYS I N   1 
ATOM   8947  C  CA  . LYS I  1 3   ? 26.662  -8.989  -15.973 1.00 29.03 ? 3    LYS I CA  1 
ATOM   8948  C  C   . LYS I  1 3   ? 25.640  -8.249  -15.108 1.00 28.92 ? 3    LYS I C   1 
ATOM   8949  O  O   . LYS I  1 3   ? 24.440  -8.536  -15.151 1.00 29.85 ? 3    LYS I O   1 
ATOM   8950  C  CB  . LYS I  1 3   ? 26.773  -8.291  -17.331 1.00 29.50 ? 3    LYS I CB  1 
ATOM   8951  C  CG  . LYS I  1 3   ? 28.088  -8.477  -18.079 1.00 32.40 ? 3    LYS I CG  1 
ATOM   8952  C  CD  . LYS I  1 3   ? 27.906  -9.381  -19.284 1.00 39.77 ? 3    LYS I CD  1 
ATOM   8953  C  CE  . LYS I  1 3   ? 28.738  -8.910  -20.480 1.00 40.35 ? 3    LYS I CE  1 
ATOM   8954  N  NZ  . LYS I  1 3   ? 30.203  -9.096  -20.280 1.00 40.27 ? 3    LYS I NZ  1 
ATOM   8955  N  N   . ALA I  1 4   ? 26.122  -7.293  -14.325 1.00 24.68 ? 4    ALA I N   1 
ATOM   8956  C  CA  . ALA I  1 4   ? 25.252  -6.412  -13.569 1.00 22.13 ? 4    ALA I CA  1 
ATOM   8957  C  C   . ALA I  1 4   ? 25.787  -4.984  -13.652 1.00 22.88 ? 4    ALA I C   1 
ATOM   8958  O  O   . ALA I  1 4   ? 26.896  -4.751  -14.116 1.00 21.71 ? 4    ALA I O   1 
ATOM   8959  C  CB  . ALA I  1 4   ? 25.151  -6.869  -12.133 1.00 19.76 ? 4    ALA I CB  1 
ATOM   8960  N  N   . VAL I  1 5   ? 24.989  -4.022  -13.223 1.00 22.80 ? 5    VAL I N   1 
ATOM   8961  C  CA  . VAL I  1 5   ? 25.390  -2.637  -13.317 1.00 21.02 ? 5    VAL I CA  1 
ATOM   8962  C  C   . VAL I  1 5   ? 24.730  -1.883  -12.176 1.00 23.74 ? 5    VAL I C   1 
ATOM   8963  O  O   . VAL I  1 5   ? 23.780  -2.367  -11.562 1.00 23.99 ? 5    VAL I O   1 
ATOM   8964  C  CB  . VAL I  1 5   ? 25.008  -2.033  -14.681 1.00 23.94 ? 5    VAL I CB  1 
ATOM   8965  C  CG1 . VAL I  1 5   ? 23.502  -1.893  -14.783 1.00 23.48 ? 5    VAL I CG1 1 
ATOM   8966  C  CG2 . VAL I  1 5   ? 25.720  -0.681  -14.909 1.00 22.84 ? 5    VAL I CG2 1 
ATOM   8967  N  N   . CYS I  1 6   ? 25.253  -0.702  -11.884 1.00 23.55 ? 6    CYS I N   1 
ATOM   8968  C  CA  . CYS I  1 6   ? 24.817  0.066   -10.745 1.00 20.22 ? 6    CYS I CA  1 
ATOM   8969  C  C   . CYS I  1 6   ? 25.157  1.527   -10.991 1.00 20.02 ? 6    CYS I C   1 
ATOM   8970  O  O   . CYS I  1 6   ? 26.309  1.878   -11.154 1.00 20.25 ? 6    CYS I O   1 
ATOM   8971  C  CB  . CYS I  1 6   ? 25.548  -0.435  -9.502  1.00 21.27 ? 6    CYS I CB  1 
ATOM   8972  S  SG  . CYS I  1 6   ? 25.170  0.441   -7.979  1.00 31.33 ? 6    CYS I SG  1 
ATOM   8973  N  N   . VAL I  1 7   ? 24.150  2.378   -11.024 1.00 21.52 ? 7    VAL I N   1 
ATOM   8974  C  CA  . VAL I  1 7   ? 24.375  3.815   -11.067 1.00 21.20 ? 7    VAL I CA  1 
ATOM   8975  C  C   . VAL I  1 7   ? 24.250  4.377   -9.642  1.00 20.74 ? 7    VAL I C   1 
ATOM   8976  O  O   . VAL I  1 7   ? 23.235  4.195   -8.973  1.00 21.05 ? 7    VAL I O   1 
ATOM   8977  C  CB  . VAL I  1 7   ? 23.384  4.490   -12.043 1.00 22.42 ? 7    VAL I CB  1 
ATOM   8978  C  CG1 . VAL I  1 7   ? 23.522  6.006   -12.015 1.00 25.75 ? 7    VAL I CG1 1 
ATOM   8979  C  CG2 . VAL I  1 7   ? 23.598  3.960   -13.453 1.00 22.38 ? 7    VAL I CG2 1 
ATOM   8980  N  N   . LEU I  1 8   ? 25.303  5.028   -9.166  1.00 21.27 ? 8    LEU I N   1 
ATOM   8981  C  CA  . LEU I  1 8   ? 25.300  5.599   -7.824  1.00 21.02 ? 8    LEU I CA  1 
ATOM   8982  C  C   . LEU I  1 8   ? 24.882  7.072   -7.866  1.00 23.44 ? 8    LEU I C   1 
ATOM   8983  O  O   . LEU I  1 8   ? 25.365  7.839   -8.696  1.00 23.34 ? 8    LEU I O   1 
ATOM   8984  C  CB  . LEU I  1 8   ? 26.681  5.487   -7.158  1.00 20.32 ? 8    LEU I CB  1 
ATOM   8985  C  CG  . LEU I  1 8   ? 27.513  4.198   -7.095  1.00 22.24 ? 8    LEU I CG  1 
ATOM   8986  C  CD1 . LEU I  1 8   ? 28.759  4.404   -6.202  1.00 25.12 ? 8    LEU I CD1 1 
ATOM   8987  C  CD2 . LEU I  1 8   ? 26.715  3.045   -6.584  1.00 20.08 ? 8    LEU I CD2 1 
ATOM   8988  N  N   . LYS I  1 9   ? 23.986  7.454   -6.961  1.00 23.02 ? 9    LYS I N   1 
ATOM   8989  C  CA  . LYS I  1 9   ? 23.577  8.838   -6.808  1.00 22.49 ? 9    LYS I CA  1 
ATOM   8990  C  C   . LYS I  1 9   ? 23.304  9.062   -5.334  1.00 22.80 ? 9    LYS I C   1 
ATOM   8991  O  O   . LYS I  1 9   ? 23.045  8.122   -4.602  1.00 21.61 ? 9    LYS I O   1 
ATOM   8992  C  CB  . LYS I  1 9   ? 22.316  9.140   -7.631  1.00 26.80 ? 9    LYS I CB  1 
ATOM   8993  C  CG  . LYS I  1 9   ? 22.541  9.152   -9.136  1.00 30.99 ? 9    LYS I CG  1 
ATOM   8994  C  CD  . LYS I  1 9   ? 21.222  9.195   -9.889  1.00 38.44 ? 9    LYS I CD  1 
ATOM   8995  C  CE  . LYS I  1 9   ? 21.431  8.901   -11.377 1.00 39.66 ? 9    LYS I CE  1 
ATOM   8996  N  NZ  . LYS I  1 9   ? 22.521  9.748   -11.933 1.00 40.56 ? 9    LYS I NZ  1 
ATOM   8997  N  N   . GLY I  1 10  ? 23.365  10.314  -4.901  1.00 25.67 ? 10   GLY I N   1 
ATOM   8998  C  CA  . GLY I  1 10  ? 23.146  10.647  -3.511  1.00 27.47 ? 10   GLY I CA  1 
ATOM   8999  C  C   . GLY I  1 10  ? 22.790  12.108  -3.341  1.00 30.12 ? 10   GLY I C   1 
ATOM   9000  O  O   . GLY I  1 10  ? 22.550  12.811  -4.325  1.00 30.38 ? 10   GLY I O   1 
ATOM   9001  N  N   . ASP I  1 11  ? 22.766  12.557  -2.088  1.00 30.94 ? 11   ASP I N   1 
ATOM   9002  C  CA  . ASP I  1 11  ? 22.363  13.919  -1.730  1.00 33.90 ? 11   ASP I CA  1 
ATOM   9003  C  C   . ASP I  1 11  ? 23.264  15.016  -2.297  1.00 34.05 ? 11   ASP I C   1 
ATOM   9004  O  O   . ASP I  1 11  ? 22.885  16.184  -2.308  1.00 33.77 ? 11   ASP I O   1 
ATOM   9005  C  CB  . ASP I  1 11  ? 22.323  14.074  -0.210  1.00 33.12 ? 11   ASP I CB  1 
ATOM   9006  C  CG  . ASP I  1 11  ? 21.176  13.315  0.431   1.00 36.41 ? 11   ASP I CG  1 
ATOM   9007  O  OD1 . ASP I  1 11  ? 20.173  13.046  -0.263  1.00 37.93 ? 11   ASP I OD1 1 
ATOM   9008  O  OD2 . ASP I  1 11  ? 21.274  13.000  1.639   1.00 40.14 ? 11   ASP I OD2 1 
ATOM   9009  N  N   . GLY I  1 12  ? 24.454  14.643  -2.758  1.00 34.07 ? 12   GLY I N   1 
ATOM   9010  C  CA  . GLY I  1 12  ? 25.451  15.622  -3.141  1.00 30.46 ? 12   GLY I CA  1 
ATOM   9011  C  C   . GLY I  1 12  ? 26.092  15.417  -4.500  1.00 32.05 ? 12   GLY I C   1 
ATOM   9012  O  O   . GLY I  1 12  ? 25.429  15.025  -5.461  1.00 32.04 ? 12   GLY I O   1 
ATOM   9013  N  N   . PRO I  1 13  ? 27.408  15.683  -4.578  1.00 31.19 ? 13   PRO I N   1 
ATOM   9014  C  CA  . PRO I  1 13  ? 28.221  15.686  -5.800  1.00 26.90 ? 13   PRO I CA  1 
ATOM   9015  C  C   . PRO I  1 13  ? 28.586  14.287  -6.298  1.00 24.65 ? 13   PRO I C   1 
ATOM   9016  O  O   . PRO I  1 13  ? 28.897  14.129  -7.477  1.00 26.77 ? 13   PRO I O   1 
ATOM   9017  C  CB  . PRO I  1 13  ? 29.508  16.404  -5.364  1.00 26.22 ? 13   PRO I CB  1 
ATOM   9018  C  CG  . PRO I  1 13  ? 29.303  16.821  -3.933  1.00 31.45 ? 13   PRO I CG  1 
ATOM   9019  C  CD  . PRO I  1 13  ? 28.220  15.967  -3.386  1.00 29.14 ? 13   PRO I CD  1 
ATOM   9020  N  N   . VAL I  1 14  ? 28.572  13.294  -5.414  1.00 27.61 ? 14   VAL I N   1 
ATOM   9021  C  CA  . VAL I  1 14  ? 29.090  11.974  -5.759  1.00 24.58 ? 14   VAL I CA  1 
ATOM   9022  C  C   . VAL I  1 14  ? 28.115  11.211  -6.643  1.00 25.48 ? 14   VAL I C   1 
ATOM   9023  O  O   . VAL I  1 14  ? 26.936  11.075  -6.315  1.00 24.80 ? 14   VAL I O   1 
ATOM   9024  C  CB  . VAL I  1 14  ? 29.437  11.130  -4.510  1.00 25.10 ? 14   VAL I CB  1 
ATOM   9025  C  CG1 . VAL I  1 14  ? 30.211  9.887   -4.914  1.00 23.00 ? 14   VAL I CG1 1 
ATOM   9026  C  CG2 . VAL I  1 14  ? 30.235  11.949  -3.518  1.00 24.37 ? 14   VAL I CG2 1 
ATOM   9027  N  N   . GLN I  1 15  ? 28.623  10.740  -7.778  1.00 26.69 ? 15   GLN I N   1 
ATOM   9028  C  CA  . GLN I  1 15  ? 27.860  9.921   -8.700  1.00 27.23 ? 15   GLN I CA  1 
ATOM   9029  C  C   . GLN I  1 15  ? 28.815  9.039   -9.482  1.00 25.82 ? 15   GLN I C   1 
ATOM   9030  O  O   . GLN I  1 15  ? 29.950  9.424   -9.716  1.00 27.86 ? 15   GLN I O   1 
ATOM   9031  C  CB  . GLN I  1 15  ? 27.055  10.794  -9.659  1.00 29.85 ? 15   GLN I CB  1 
ATOM   9032  C  CG  . GLN I  1 15  ? 27.888  11.696  -10.538 1.00 30.04 ? 15   GLN I CG  1 
ATOM   9033  C  CD  . GLN I  1 15  ? 27.030  12.688  -11.293 1.00 39.82 ? 15   GLN I CD  1 
ATOM   9034  O  OE1 . GLN I  1 15  ? 25.809  12.742  -11.100 1.00 43.01 ? 15   GLN I OE1 1 
ATOM   9035  N  NE2 . GLN I  1 15  ? 27.658  13.481  -12.159 1.00 44.22 ? 15   GLN I NE2 1 
ATOM   9036  N  N   . GLY I  1 16  ? 28.356  7.858   -9.882  1.00 24.64 ? 16   GLY I N   1 
ATOM   9037  C  CA  . GLY I  1 16  ? 29.195  6.943   -10.625 1.00 23.57 ? 16   GLY I CA  1 
ATOM   9038  C  C   . GLY I  1 16  ? 28.466  5.779   -11.264 1.00 24.33 ? 16   GLY I C   1 
ATOM   9039  O  O   . GLY I  1 16  ? 27.264  5.602   -11.081 1.00 23.14 ? 16   GLY I O   1 
ATOM   9040  N  N   . ILE I  1 17  ? 29.219  4.989   -12.025 1.00 22.31 ? 17   ILE I N   1 
ATOM   9041  C  CA  . ILE I  1 17  ? 28.733  3.775   -12.656 1.00 20.28 ? 17   ILE I CA  1 
ATOM   9042  C  C   . ILE I  1 17  ? 29.700  2.641   -12.324 1.00 20.12 ? 17   ILE I C   1 
ATOM   9043  O  O   . ILE I  1 17  ? 30.877  2.685   -12.681 1.00 18.69 ? 17   ILE I O   1 
ATOM   9044  C  CB  . ILE I  1 17  ? 28.604  3.943   -14.197 1.00 20.72 ? 17   ILE I CB  1 
ATOM   9045  C  CG1 . ILE I  1 17  ? 27.763  5.173   -14.523 1.00 21.90 ? 17   ILE I CG1 1 
ATOM   9046  C  CG2 . ILE I  1 17  ? 27.968  2.720   -14.835 1.00 19.57 ? 17   ILE I CG2 1 
ATOM   9047  C  CD1 . ILE I  1 17  ? 27.473  5.339   -15.980 1.00 25.44 ? 17   ILE I CD1 1 
ATOM   9048  N  N   . ILE I  1 18  ? 29.202  1.635   -11.619 1.00 19.33 ? 18   ILE I N   1 
ATOM   9049  C  CA  . ILE I  1 18  ? 30.007  0.469   -11.278 1.00 19.27 ? 18   ILE I CA  1 
ATOM   9050  C  C   . ILE I  1 18  ? 29.482  -0.724  -12.055 1.00 18.58 ? 18   ILE I C   1 
ATOM   9051  O  O   . ILE I  1 18  ? 28.291  -0.971  -12.079 1.00 19.84 ? 18   ILE I O   1 
ATOM   9052  C  CB  . ILE I  1 18  ? 29.990  0.174   -9.746  1.00 18.84 ? 18   ILE I CB  1 
ATOM   9053  C  CG1 . ILE I  1 18  ? 30.533  1.369   -8.946  1.00 17.83 ? 18   ILE I CG1 1 
ATOM   9054  C  CG2 . ILE I  1 18  ? 30.755  -1.120  -9.425  1.00 16.48 ? 18   ILE I CG2 1 
ATOM   9055  C  CD1 . ILE I  1 18  ? 32.008  1.657   -9.185  1.00 16.90 ? 18   ILE I CD1 1 
ATOM   9056  N  N   . ASN I  1 19  ? 30.381  -1.444  -12.709 1.00 21.14 ? 19   ASN I N   1 
ATOM   9057  C  CA  . ASN I  1 19  ? 30.023  -2.604  -13.510 1.00 20.59 ? 19   ASN I CA  1 
ATOM   9058  C  C   . ASN I  1 19  ? 30.450  -3.883  -12.797 1.00 20.62 ? 19   ASN I C   1 
ATOM   9059  O  O   . ASN I  1 19  ? 31.466  -3.896  -12.120 1.00 21.54 ? 19   ASN I O   1 
ATOM   9060  C  CB  . ASN I  1 19  ? 30.719  -2.528  -14.870 1.00 22.83 ? 19   ASN I CB  1 
ATOM   9061  C  CG  . ASN I  1 19  ? 30.289  -1.314  -15.698 1.00 26.07 ? 19   ASN I CG  1 
ATOM   9062  O  OD1 . ASN I  1 19  ? 29.198  -1.301  -16.287 1.00 24.94 ? 19   ASN I OD1 1 
ATOM   9063  N  ND2 . ASN I  1 19  ? 31.162  -0.304  -15.774 1.00 22.59 ? 19   ASN I ND2 1 
ATOM   9064  N  N   . PHE I  1 20  ? 29.689  -4.957  -12.957 1.00 21.27 ? 20   PHE I N   1 
ATOM   9065  C  CA  . PHE I  1 20  ? 30.028  -6.232  -12.336 1.00 21.04 ? 20   PHE I CA  1 
ATOM   9066  C  C   . PHE I  1 20  ? 30.030  -7.300  -13.400 1.00 23.91 ? 20   PHE I C   1 
ATOM   9067  O  O   . PHE I  1 20  ? 29.210  -7.272  -14.309 1.00 26.13 ? 20   PHE I O   1 
ATOM   9068  C  CB  . PHE I  1 20  ? 29.005  -6.622  -11.273 1.00 19.42 ? 20   PHE I CB  1 
ATOM   9069  C  CG  . PHE I  1 20  ? 28.715  -5.543  -10.282 1.00 20.77 ? 20   PHE I CG  1 
ATOM   9070  C  CD1 . PHE I  1 20  ? 27.912  -4.467  -10.624 1.00 19.64 ? 20   PHE I CD1 1 
ATOM   9071  C  CD2 . PHE I  1 20  ? 29.231  -5.607  -8.998  1.00 19.21 ? 20   PHE I CD2 1 
ATOM   9072  C  CE1 . PHE I  1 20  ? 27.642  -3.473  -9.714  1.00 17.65 ? 20   PHE I CE1 1 
ATOM   9073  C  CE2 . PHE I  1 20  ? 28.961  -4.610  -8.084  1.00 18.71 ? 20   PHE I CE2 1 
ATOM   9074  C  CZ  . PHE I  1 20  ? 28.166  -3.547  -8.443  1.00 17.59 ? 20   PHE I CZ  1 
ATOM   9075  N  N   . GLU I  1 21  ? 30.941  -8.255  -13.289 1.00 24.78 ? 21   GLU I N   1 
ATOM   9076  C  CA  . GLU I  1 21  ? 30.956  -9.359  -14.236 1.00 30.44 ? 21   GLU I CA  1 
ATOM   9077  C  C   . GLU I  1 21  ? 31.432  -10.653 -13.612 1.00 28.17 ? 21   GLU I C   1 
ATOM   9078  O  O   . GLU I  1 21  ? 32.408  -10.676 -12.875 1.00 28.55 ? 21   GLU I O   1 
ATOM   9079  C  CB  . GLU I  1 21  ? 31.806  -9.034  -15.464 1.00 28.94 ? 21   GLU I CB  1 
ATOM   9080  C  CG  . GLU I  1 21  ? 31.725  -10.105 -16.531 1.00 34.35 ? 21   GLU I CG  1 
ATOM   9081  C  CD  . GLU I  1 21  ? 32.729  -9.899  -17.635 1.00 46.02 ? 21   GLU I CD  1 
ATOM   9082  O  OE1 . GLU I  1 21  ? 32.906  -10.832 -18.448 1.00 54.42 ? 21   GLU I OE1 1 
ATOM   9083  O  OE2 . GLU I  1 21  ? 33.341  -8.806  -17.684 1.00 46.49 ? 21   GLU I OE2 1 
ATOM   9084  N  N   . GLN I  1 22  ? 30.741  -11.736 -13.934 1.00 29.30 ? 22   GLN I N   1 
ATOM   9085  C  CA  . GLN I  1 22  ? 31.114  -13.045 -13.442 1.00 30.77 ? 22   GLN I CA  1 
ATOM   9086  C  C   . GLN I  1 22  ? 31.040  -14.048 -14.579 1.00 36.27 ? 22   GLN I C   1 
ATOM   9087  O  O   . GLN I  1 22  ? 29.957  -14.508 -14.917 1.00 39.34 ? 22   GLN I O   1 
ATOM   9088  C  CB  . GLN I  1 22  ? 30.173  -13.461 -12.327 1.00 29.86 ? 22   GLN I CB  1 
ATOM   9089  C  CG  . GLN I  1 22  ? 30.719  -14.558 -11.454 1.00 33.80 ? 22   GLN I CG  1 
ATOM   9090  C  CD  . GLN I  1 22  ? 29.791  -14.916 -10.315 1.00 32.56 ? 22   GLN I CD  1 
ATOM   9091  O  OE1 . GLN I  1 22  ? 28.575  -14.739 -10.407 1.00 30.89 ? 22   GLN I OE1 1 
ATOM   9092  N  NE2 . GLN I  1 22  ? 30.359  -15.432 -9.236  1.00 30.41 ? 22   GLN I NE2 1 
ATOM   9093  N  N   . LYS I  1 23  ? 32.191  -14.380 -15.165 1.00 38.52 ? 23   LYS I N   1 
ATOM   9094  C  CA  . LYS I  1 23  ? 32.255  -15.328 -16.282 1.00 44.21 ? 23   LYS I CA  1 
ATOM   9095  C  C   . LYS I  1 23  ? 31.750  -16.720 -15.891 1.00 45.41 ? 23   LYS I C   1 
ATOM   9096  O  O   . LYS I  1 23  ? 30.926  -17.307 -16.588 1.00 50.31 ? 23   LYS I O   1 
ATOM   9097  C  CB  . LYS I  1 23  ? 33.685  -15.438 -16.833 1.00 47.25 ? 23   LYS I CB  1 
ATOM   9098  C  CG  . LYS I  1 23  ? 34.356  -14.103 -17.150 1.00 50.99 ? 23   LYS I CG  1 
ATOM   9099  C  CD  . LYS I  1 23  ? 34.242  -13.735 -18.625 1.00 54.32 ? 23   LYS I CD  1 
ATOM   9100  C  CE  . LYS I  1 23  ? 35.473  -14.183 -19.431 1.00 58.14 ? 23   LYS I CE  1 
ATOM   9101  N  NZ  . LYS I  1 23  ? 35.607  -15.669 -19.560 1.00 48.71 ? 23   LYS I NZ  1 
ATOM   9102  N  N   . GLU I  1 24  ? 32.255  -17.245 -14.779 1.00 45.62 ? 24   GLU I N   1 
ATOM   9103  C  CA  . GLU I  1 24  ? 31.896  -18.588 -14.323 1.00 49.43 ? 24   GLU I CA  1 
ATOM   9104  C  C   . GLU I  1 24  ? 30.874  -18.451 -13.220 1.00 43.84 ? 24   GLU I C   1 
ATOM   9105  O  O   . GLU I  1 24  ? 30.814  -17.415 -12.577 1.00 43.65 ? 24   GLU I O   1 
ATOM   9106  C  CB  . GLU I  1 24  ? 33.126  -19.325 -13.774 1.00 53.71 ? 24   GLU I CB  1 
ATOM   9107  C  CG  . GLU I  1 24  ? 34.419  -19.116 -14.566 1.00 53.58 ? 24   GLU I CG  1 
ATOM   9108  C  CD  . GLU I  1 24  ? 34.496  -19.990 -15.806 1.00 57.71 ? 24   GLU I CD  1 
ATOM   9109  O  OE1 . GLU I  1 24  ? 35.615  -20.164 -16.334 1.00 56.66 ? 24   GLU I OE1 1 
ATOM   9110  O  OE2 . GLU I  1 24  ? 33.443  -20.508 -16.247 1.00 56.94 ? 24   GLU I OE2 1 
ATOM   9111  N  N   . SER I  1 25  ? 30.084  -19.495 -12.992 1.00 41.86 ? 25   SER I N   1 
ATOM   9112  C  CA  . SER I  1 25  ? 29.055  -19.462 -11.958 1.00 44.93 ? 25   SER I CA  1 
ATOM   9113  C  C   . SER I  1 25  ? 29.666  -19.407 -10.566 1.00 48.31 ? 25   SER I C   1 
ATOM   9114  O  O   . SER I  1 25  ? 29.089  -18.841 -9.636  1.00 48.04 ? 25   SER I O   1 
ATOM   9115  C  CB  . SER I  1 25  ? 28.154  -20.691 -12.060 1.00 51.33 ? 25   SER I CB  1 
ATOM   9116  O  OG  . SER I  1 25  ? 27.361  -20.826 -10.891 1.00 53.15 ? 25   SER I OG  1 
ATOM   9117  N  N   . ASN I  1 26  ? 30.835  -20.018 -10.428 1.00 51.09 ? 26   ASN I N   1 
ATOM   9118  C  CA  . ASN I  1 26  ? 31.542  -20.039 -9.164  1.00 48.55 ? 26   ASN I CA  1 
ATOM   9119  C  C   . ASN I  1 26  ? 32.857  -19.299 -9.309  1.00 46.33 ? 26   ASN I C   1 
ATOM   9120  O  O   . ASN I  1 26  ? 33.822  -19.551 -8.589  1.00 49.25 ? 26   ASN I O   1 
ATOM   9121  C  CB  . ASN I  1 26  ? 31.745  -21.479 -8.699  1.00 54.19 ? 26   ASN I CB  1 
ATOM   9122  C  CG  . ASN I  1 26  ? 30.517  -22.028 -7.983  1.00 64.38 ? 26   ASN I CG  1 
ATOM   9123  O  OD1 . ASN I  1 26  ? 30.132  -21.531 -6.916  1.00 68.37 ? 26   ASN I OD1 1 
ATOM   9124  N  ND2 . ASN I  1 26  ? 29.891  -23.050 -8.568  1.00 64.28 ? 26   ASN I ND2 1 
ATOM   9125  N  N   . GLY I  1 27  ? 32.872  -18.375 -10.263 1.00 46.28 ? 27   GLY I N   1 
ATOM   9126  C  CA  . GLY I  1 27  ? 34.037  -17.565 -10.541 1.00 44.82 ? 27   GLY I CA  1 
ATOM   9127  C  C   . GLY I  1 27  ? 34.055  -16.319 -9.684  1.00 42.25 ? 27   GLY I C   1 
ATOM   9128  O  O   . GLY I  1 27  ? 33.085  -16.028 -8.973  1.00 39.79 ? 27   GLY I O   1 
ATOM   9129  N  N   . PRO I  1 28  ? 35.174  -15.586 -9.726  1.00 40.62 ? 28   PRO I N   1 
ATOM   9130  C  CA  . PRO I  1 28  ? 35.253  -14.314 -9.014  1.00 36.32 ? 28   PRO I CA  1 
ATOM   9131  C  C   . PRO I  1 28  ? 34.398  -13.279 -9.730  1.00 33.14 ? 28   PRO I C   1 
ATOM   9132  O  O   . PRO I  1 28  ? 34.142  -13.400 -10.939 1.00 31.68 ? 28   PRO I O   1 
ATOM   9133  C  CB  . PRO I  1 28  ? 36.737  -13.936 -9.125  1.00 38.14 ? 28   PRO I CB  1 
ATOM   9134  C  CG  . PRO I  1 28  ? 37.438  -15.166 -9.578  1.00 42.62 ? 28   PRO I CG  1 
ATOM   9135  C  CD  . PRO I  1 28  ? 36.442  -15.921 -10.394 1.00 42.78 ? 28   PRO I CD  1 
ATOM   9136  N  N   . VAL I  1 29  ? 33.952  -12.269 -8.996  1.00 29.66 ? 29   VAL I N   1 
ATOM   9137  C  CA  . VAL I  1 29  ? 33.234  -11.174 -9.623  1.00 27.44 ? 29   VAL I CA  1 
ATOM   9138  C  C   . VAL I  1 29  ? 34.208  -10.015 -9.876  1.00 26.43 ? 29   VAL I C   1 
ATOM   9139  O  O   . VAL I  1 29  ? 34.931  -9.586  -8.973  1.00 23.82 ? 29   VAL I O   1 
ATOM   9140  C  CB  . VAL I  1 29  ? 31.985  -10.748 -8.796  1.00 24.76 ? 29   VAL I CB  1 
ATOM   9141  C  CG1 . VAL I  1 29  ? 31.287  -9.551  -9.427  1.00 20.48 ? 29   VAL I CG1 1 
ATOM   9142  C  CG2 . VAL I  1 29  ? 31.018  -11.913 -8.653  1.00 22.32 ? 29   VAL I CG2 1 
ATOM   9143  N  N   . LYS I  1 30  ? 34.240  -9.546  -11.124 1.00 24.48 ? 30   LYS I N   1 
ATOM   9144  C  CA  . LYS I  1 30  ? 35.047  -8.398  -11.511 1.00 25.84 ? 30   LYS I CA  1 
ATOM   9145  C  C   . LYS I  1 30  ? 34.215  -7.135  -11.336 1.00 24.58 ? 30   LYS I C   1 
ATOM   9146  O  O   . LYS I  1 30  ? 33.192  -6.971  -11.991 1.00 22.82 ? 30   LYS I O   1 
ATOM   9147  C  CB  . LYS I  1 30  ? 35.509  -8.537  -12.966 1.00 29.41 ? 30   LYS I CB  1 
ATOM   9148  C  CG  . LYS I  1 30  ? 36.690  -7.630  -13.366 1.00 37.61 ? 30   LYS I CG  1 
ATOM   9149  C  CD  . LYS I  1 30  ? 36.916  -7.611  -14.896 1.00 41.56 ? 30   LYS I CD  1 
ATOM   9150  C  CE  . LYS I  1 30  ? 37.838  -6.453  -15.319 1.00 36.94 ? 30   LYS I CE  1 
ATOM   9151  N  NZ  . LYS I  1 30  ? 37.634  -6.103  -16.756 1.00 39.97 ? 30   LYS I NZ  1 
ATOM   9152  N  N   . VAL I  1 31  ? 34.662  -6.259  -10.437 1.00 24.25 ? 31   VAL I N   1 
ATOM   9153  C  CA  . VAL I  1 31  ? 33.970  -5.007  -10.113 1.00 25.40 ? 31   VAL I CA  1 
ATOM   9154  C  C   . VAL I  1 31  ? 34.791  -3.821  -10.641 1.00 23.98 ? 31   VAL I C   1 
ATOM   9155  O  O   . VAL I  1 31  ? 35.934  -3.629  -10.229 1.00 25.15 ? 31   VAL I O   1 
ATOM   9156  C  CB  . VAL I  1 31  ? 33.747  -4.869  -8.567  1.00 20.23 ? 31   VAL I CB  1 
ATOM   9157  C  CG1 . VAL I  1 31  ? 32.914  -3.641  -8.237  1.00 18.49 ? 31   VAL I CG1 1 
ATOM   9158  C  CG2 . VAL I  1 31  ? 33.106  -6.126  -7.999  1.00 18.42 ? 31   VAL I CG2 1 
ATOM   9159  N  N   . TRP I  1 32  ? 34.230  -3.046  -11.570 1.00 22.94 ? 32   TRP I N   1 
ATOM   9160  C  CA  . TRP I  1 32  ? 34.966  -1.919  -12.139 1.00 22.83 ? 32   TRP I CA  1 
ATOM   9161  C  C   . TRP I  1 32  ? 34.085  -0.745  -12.551 1.00 22.77 ? 32   TRP I C   1 
ATOM   9162  O  O   . TRP I  1 32  ? 32.957  -0.928  -12.969 1.00 21.70 ? 32   TRP I O   1 
ATOM   9163  C  CB  . TRP I  1 32  ? 35.804  -2.374  -13.346 1.00 26.06 ? 32   TRP I CB  1 
ATOM   9164  C  CG  . TRP I  1 32  ? 35.068  -2.402  -14.689 1.00 26.73 ? 32   TRP I CG  1 
ATOM   9165  C  CD1 . TRP I  1 32  ? 34.997  -1.391  -15.622 1.00 27.39 ? 32   TRP I CD1 1 
ATOM   9166  C  CD2 . TRP I  1 32  ? 34.342  -3.506  -15.246 1.00 23.79 ? 32   TRP I CD2 1 
ATOM   9167  N  NE1 . TRP I  1 32  ? 34.259  -1.805  -16.715 1.00 27.35 ? 32   TRP I NE1 1 
ATOM   9168  C  CE2 . TRP I  1 32  ? 33.849  -3.094  -16.507 1.00 24.51 ? 32   TRP I CE2 1 
ATOM   9169  C  CE3 . TRP I  1 32  ? 34.055  -4.795  -14.799 1.00 26.95 ? 32   TRP I CE3 1 
ATOM   9170  C  CZ2 . TRP I  1 32  ? 33.087  -3.932  -17.315 1.00 24.57 ? 32   TRP I CZ2 1 
ATOM   9171  C  CZ3 . TRP I  1 32  ? 33.297  -5.624  -15.607 1.00 29.74 ? 32   TRP I CZ3 1 
ATOM   9172  C  CH2 . TRP I  1 32  ? 32.823  -5.189  -16.851 1.00 26.55 ? 32   TRP I CH2 1 
ATOM   9173  N  N   . GLY I  1 33  ? 34.621  0.465   -12.460 1.00 22.81 ? 33   GLY I N   1 
ATOM   9174  C  CA  . GLY I  1 33  ? 33.919  1.623   -12.973 1.00 21.34 ? 33   GLY I CA  1 
ATOM   9175  C  C   . GLY I  1 33  ? 34.520  2.903   -12.453 1.00 23.26 ? 33   GLY I C   1 
ATOM   9176  O  O   . GLY I  1 33  ? 35.665  2.926   -12.027 1.00 25.58 ? 33   GLY I O   1 
ATOM   9177  N  N   . SER I  1 34  ? 33.738  3.971   -12.478 1.00 25.13 ? 34   SER I N   1 
ATOM   9178  C  CA  . SER I  1 34  ? 34.224  5.279   -12.074 1.00 25.92 ? 34   SER I CA  1 
ATOM   9179  C  C   . SER I  1 34  ? 33.260  5.986   -11.123 1.00 24.43 ? 34   SER I C   1 
ATOM   9180  O  O   . SER I  1 34  ? 32.067  6.023   -11.376 1.00 29.81 ? 34   SER I O   1 
ATOM   9181  C  CB  . SER I  1 34  ? 34.437  6.141   -13.314 1.00 26.70 ? 34   SER I CB  1 
ATOM   9182  O  OG  . SER I  1 34  ? 34.670  7.484   -12.937 1.00 35.50 ? 34   SER I OG  1 
ATOM   9183  N  N   . ILE I  1 35  ? 33.774  6.551   -10.037 1.00 23.69 ? 35   ILE I N   1 
ATOM   9184  C  CA  . ILE I  1 35  ? 32.960  7.340   -9.118  1.00 22.45 ? 35   ILE I CA  1 
ATOM   9185  C  C   . ILE I  1 35  ? 33.532  8.747   -8.955  1.00 24.32 ? 35   ILE I C   1 
ATOM   9186  O  O   . ILE I  1 35  ? 34.567  8.934   -8.326  1.00 23.42 ? 35   ILE I O   1 
ATOM   9187  C  CB  . ILE I  1 35  ? 32.894  6.698   -7.731  1.00 23.42 ? 35   ILE I CB  1 
ATOM   9188  C  CG1 . ILE I  1 35  ? 32.597  5.198   -7.841  1.00 22.15 ? 35   ILE I CG1 1 
ATOM   9189  C  CG2 . ILE I  1 35  ? 31.862  7.425   -6.851  1.00 21.62 ? 35   ILE I CG2 1 
ATOM   9190  C  CD1 . ILE I  1 35  ? 32.501  4.510   -6.486  1.00 18.91 ? 35   ILE I CD1 1 
ATOM   9191  N  N   . LYS I  1 36  ? 32.856  9.739   -9.523  1.00 28.06 ? 36   LYS I N   1 
ATOM   9192  C  CA  . LYS I  1 36  ? 33.352  11.112  -9.483  1.00 27.64 ? 36   LYS I CA  1 
ATOM   9193  C  C   . LYS I  1 36  ? 32.785  11.905  -8.307  1.00 27.08 ? 36   LYS I C   1 
ATOM   9194  O  O   . LYS I  1 36  ? 31.810  11.491  -7.687  1.00 28.50 ? 36   LYS I O   1 
ATOM   9195  C  CB  . LYS I  1 36  ? 33.083  11.829  -10.816 1.00 27.26 ? 36   LYS I CB  1 
ATOM   9196  C  CG  . LYS I  1 36  ? 31.644  12.245  -11.050 1.00 32.92 ? 36   LYS I CG  1 
ATOM   9197  C  CD  . LYS I  1 36  ? 31.371  12.483  -12.540 1.00 36.57 ? 36   LYS I CD  1 
ATOM   9198  C  CE  . LYS I  1 36  ? 31.986  11.349  -13.381 1.00 46.49 ? 36   LYS I CE  1 
ATOM   9199  N  NZ  . LYS I  1 36  ? 31.788  11.505  -14.862 1.00 50.89 ? 36   LYS I NZ  1 
ATOM   9200  N  N   . GLY I  1 37  ? 33.417  13.032  -7.988  1.00 26.25 ? 37   GLY I N   1 
ATOM   9201  C  CA  . GLY I  1 37  ? 32.883  13.952  -7.000  1.00 24.87 ? 37   GLY I CA  1 
ATOM   9202  C  C   . GLY I  1 37  ? 33.319  13.693  -5.579  1.00 23.66 ? 37   GLY I C   1 
ATOM   9203  O  O   . GLY I  1 37  ? 32.795  14.309  -4.649  1.00 22.44 ? 37   GLY I O   1 
ATOM   9204  N  N   . LEU I  1 38  ? 34.286  12.789  -5.422  1.00 23.77 ? 38   LEU I N   1 
ATOM   9205  C  CA  . LEU I  1 38  ? 34.769  12.351  -4.111  1.00 22.32 ? 38   LEU I CA  1 
ATOM   9206  C  C   . LEU I  1 38  ? 35.912  13.223  -3.595  1.00 22.27 ? 38   LEU I C   1 
ATOM   9207  O  O   . LEU I  1 38  ? 36.598  13.890  -4.361  1.00 20.88 ? 38   LEU I O   1 
ATOM   9208  C  CB  . LEU I  1 38  ? 35.228  10.882  -4.167  1.00 20.69 ? 38   LEU I CB  1 
ATOM   9209  C  CG  . LEU I  1 38  ? 34.163  9.806   -4.421  1.00 21.42 ? 38   LEU I CG  1 
ATOM   9210  C  CD1 . LEU I  1 38  ? 34.794  8.465   -4.819  1.00 18.79 ? 38   LEU I CD1 1 
ATOM   9211  C  CD2 . LEU I  1 38  ? 33.268  9.649   -3.219  1.00 19.39 ? 38   LEU I CD2 1 
ATOM   9212  N  N   . THR I  1 39  ? 36.099  13.226  -2.279  1.00 24.52 ? 39   THR I N   1 
ATOM   9213  C  CA  . THR I  1 39  ? 37.260  13.871  -1.686  1.00 23.86 ? 39   THR I CA  1 
ATOM   9214  C  C   . THR I  1 39  ? 38.457  12.945  -1.913  1.00 26.42 ? 39   THR I C   1 
ATOM   9215  O  O   . THR I  1 39  ? 38.277  11.735  -2.109  1.00 25.32 ? 39   THR I O   1 
ATOM   9216  C  CB  . THR I  1 39  ? 37.050  14.136  -0.177  1.00 25.24 ? 39   THR I CB  1 
ATOM   9217  O  OG1 . THR I  1 39  ? 36.600  12.941  0.472   1.00 25.55 ? 39   THR I OG1 1 
ATOM   9218  C  CG2 . THR I  1 39  ? 36.015  15.225  0.043   1.00 24.72 ? 39   THR I CG2 1 
ATOM   9219  N  N   . GLU I  1 40  ? 39.669  13.498  -1.910  1.00 25.91 ? 40   GLU I N   1 
ATOM   9220  C  CA  . GLU I  1 40  ? 40.865  12.682  -2.143  1.00 26.44 ? 40   GLU I CA  1 
ATOM   9221  C  C   . GLU I  1 40  ? 41.098  11.720  -0.985  1.00 25.10 ? 40   GLU I C   1 
ATOM   9222  O  O   . GLU I  1 40  ? 40.975  12.102  0.181   1.00 23.83 ? 40   GLU I O   1 
ATOM   9223  C  CB  . GLU I  1 40  ? 42.120  13.550  -2.370  1.00 27.60 ? 40   GLU I CB  1 
ATOM   9224  C  CG  . GLU I  1 40  ? 43.379  12.743  -2.757  1.00 29.77 ? 40   GLU I CG  1 
ATOM   9225  C  CD  . GLU I  1 40  ? 44.646  13.590  -2.879  1.00 30.29 ? 40   GLU I CD  1 
ATOM   9226  O  OE1 . GLU I  1 40  ? 44.548  14.836  -2.805  1.00 32.58 ? 40   GLU I OE1 1 
ATOM   9227  O  OE2 . GLU I  1 40  ? 45.738  13.005  -3.061  1.00 29.19 ? 40   GLU I OE2 1 
ATOM   9228  N  N   . GLY I  1 41  ? 41.438  10.473  -1.306  1.00 23.63 ? 41   GLY I N   1 
ATOM   9229  C  CA  . GLY I  1 41  ? 41.725  9.490   -0.279  1.00 24.70 ? 41   GLY I CA  1 
ATOM   9230  C  C   . GLY I  1 41  ? 40.871  8.254   -0.409  1.00 21.51 ? 41   GLY I C   1 
ATOM   9231  O  O   . GLY I  1 41  ? 40.284  8.018   -1.457  1.00 23.08 ? 41   GLY I O   1 
ATOM   9232  N  N   . LEU I  1 42  ? 40.798  7.467   0.661   1.00 24.52 ? 42   LEU I N   1 
ATOM   9233  C  CA  . LEU I  1 42  ? 40.112  6.170   0.618   1.00 22.64 ? 42   LEU I CA  1 
ATOM   9234  C  C   . LEU I  1 42  ? 38.698  6.276   1.161   1.00 21.68 ? 42   LEU I C   1 
ATOM   9235  O  O   . LEU I  1 42  ? 38.477  6.909   2.197   1.00 24.52 ? 42   LEU I O   1 
ATOM   9236  C  CB  . LEU I  1 42  ? 40.869  5.109   1.424   1.00 19.49 ? 42   LEU I CB  1 
ATOM   9237  C  CG  . LEU I  1 42  ? 42.344  4.845   1.137   1.00 21.96 ? 42   LEU I CG  1 
ATOM   9238  C  CD1 . LEU I  1 42  ? 42.930  4.017   2.251   1.00 20.55 ? 42   LEU I CD1 1 
ATOM   9239  C  CD2 . LEU I  1 42  ? 42.532  4.156   -0.194  1.00 23.01 ? 42   LEU I CD2 1 
ATOM   9240  N  N   . HIS I  1 43  ? 37.756  5.634   0.470   1.00 20.27 ? 43   HIS I N   1 
ATOM   9241  C  CA  . HIS I  1 43  ? 36.343  5.665   0.835   1.00 19.33 ? 43   HIS I CA  1 
ATOM   9242  C  C   . HIS I  1 43  ? 35.791  4.246   0.895   1.00 17.56 ? 43   HIS I C   1 
ATOM   9243  O  O   . HIS I  1 43  ? 35.930  3.484   -0.044  1.00 18.38 ? 43   HIS I O   1 
ATOM   9244  C  CB  . HIS I  1 43  ? 35.540  6.470   -0.204  1.00 18.81 ? 43   HIS I CB  1 
ATOM   9245  C  CG  . HIS I  1 43  ? 35.922  7.917   -0.291  1.00 19.89 ? 43   HIS I CG  1 
ATOM   9246  N  ND1 . HIS I  1 43  ? 35.325  8.892   0.476   1.00 21.67 ? 43   HIS I ND1 1 
ATOM   9247  C  CD2 . HIS I  1 43  ? 36.828  8.558   -1.069  1.00 20.54 ? 43   HIS I CD2 1 
ATOM   9248  C  CE1 . HIS I  1 43  ? 35.853  10.067  0.187   1.00 20.15 ? 43   HIS I CE1 1 
ATOM   9249  N  NE2 . HIS I  1 43  ? 36.771  9.890   -0.744  1.00 20.98 ? 43   HIS I NE2 1 
ATOM   9250  N  N   . GLY I  1 44  ? 35.142  3.895   1.994   1.00 22.14 ? 44   GLY I N   1 
ATOM   9251  C  CA  . GLY I  1 44  ? 34.444  2.619   2.082   1.00 22.99 ? 44   GLY I CA  1 
ATOM   9252  C  C   . GLY I  1 44  ? 33.511  2.303   0.914   1.00 21.70 ? 44   GLY I C   1 
ATOM   9253  O  O   . GLY I  1 44  ? 32.803  3.164   0.389   1.00 19.84 ? 44   GLY I O   1 
ATOM   9254  N  N   . PHE I  1 45  ? 33.498  1.036   0.523   1.00 21.88 ? 45   PHE I N   1 
ATOM   9255  C  CA  . PHE I  1 45  ? 32.808  0.607   -0.683  1.00 19.07 ? 45   PHE I CA  1 
ATOM   9256  C  C   . PHE I  1 45  ? 32.190  -0.759  -0.390  1.00 20.84 ? 45   PHE I C   1 
ATOM   9257  O  O   . PHE I  1 45  ? 32.887  -1.781  -0.380  1.00 20.18 ? 45   PHE I O   1 
ATOM   9258  C  CB  . PHE I  1 45  ? 33.822  0.530   -1.825  1.00 18.18 ? 45   PHE I CB  1 
ATOM   9259  C  CG  . PHE I  1 45  ? 33.219  0.374   -3.183  1.00 17.38 ? 45   PHE I CG  1 
ATOM   9260  C  CD1 . PHE I  1 45  ? 32.400  1.356   -3.715  1.00 18.09 ? 45   PHE I CD1 1 
ATOM   9261  C  CD2 . PHE I  1 45  ? 33.490  -0.753  -3.943  1.00 17.95 ? 45   PHE I CD2 1 
ATOM   9262  C  CE1 . PHE I  1 45  ? 31.850  1.209   -4.966  1.00 15.93 ? 45   PHE I CE1 1 
ATOM   9263  C  CE2 . PHE I  1 45  ? 32.940  -0.901  -5.206  1.00 16.27 ? 45   PHE I CE2 1 
ATOM   9264  C  CZ  . PHE I  1 45  ? 32.125  0.081   -5.715  1.00 15.59 ? 45   PHE I CZ  1 
ATOM   9265  N  N   . HIS I  1 46  ? 30.884  -0.771  -0.135  1.00 18.46 ? 46   HIS I N   1 
ATOM   9266  C  CA  . HIS I  1 46  ? 30.226  -1.978  0.349   1.00 20.26 ? 46   HIS I CA  1 
ATOM   9267  C  C   . HIS I  1 46  ? 28.926  -2.274  -0.373  1.00 21.53 ? 46   HIS I C   1 
ATOM   9268  O  O   . HIS I  1 46  ? 28.239  -1.357  -0.855  1.00 21.65 ? 46   HIS I O   1 
ATOM   9269  C  CB  . HIS I  1 46  ? 29.935  -1.865  1.856   1.00 21.58 ? 46   HIS I CB  1 
ATOM   9270  C  CG  . HIS I  1 46  ? 31.067  -1.290  2.647   1.00 20.95 ? 46   HIS I CG  1 
ATOM   9271  N  ND1 . HIS I  1 46  ? 31.031  -0.024  3.187   1.00 19.88 ? 46   HIS I ND1 1 
ATOM   9272  C  CD2 . HIS I  1 46  ? 32.274  -1.806  2.979   1.00 18.97 ? 46   HIS I CD2 1 
ATOM   9273  C  CE1 . HIS I  1 46  ? 32.166  0.217   3.817   1.00 18.08 ? 46   HIS I CE1 1 
ATOM   9274  N  NE2 . HIS I  1 46  ? 32.936  -0.849  3.705   1.00 19.91 ? 46   HIS I NE2 1 
ATOM   9275  N  N   . VAL I  1 47  ? 28.593  -3.564  -0.432  1.00 20.67 ? 47   VAL I N   1 
ATOM   9276  C  CA  . VAL I  1 47  ? 27.256  -4.006  -0.818  1.00 20.02 ? 47   VAL I CA  1 
ATOM   9277  C  C   . VAL I  1 47  ? 26.377  -4.080  0.436   1.00 20.00 ? 47   VAL I C   1 
ATOM   9278  O  O   . VAL I  1 47  ? 26.688  -4.807  1.382   1.00 21.48 ? 47   VAL I O   1 
ATOM   9279  C  CB  . VAL I  1 47  ? 27.282  -5.374  -1.551  1.00 20.27 ? 47   VAL I CB  1 
ATOM   9280  C  CG1 . VAL I  1 47  ? 25.936  -5.669  -2.203  1.00 17.72 ? 47   VAL I CG1 1 
ATOM   9281  C  CG2 . VAL I  1 47  ? 28.381  -5.394  -2.603  1.00 18.78 ? 47   VAL I CG2 1 
ATOM   9282  N  N   . HIS I  1 48  ? 25.299  -3.295  0.439   1.00 19.68 ? 48   HIS I N   1 
ATOM   9283  C  CA  . HIS I  1 48  ? 24.326  -3.271  1.523   1.00 19.11 ? 48   HIS I CA  1 
ATOM   9284  C  C   . HIS I  1 48  ? 23.156  -4.207  1.251   1.00 19.70 ? 48   HIS I C   1 
ATOM   9285  O  O   . HIS I  1 48  ? 22.850  -4.515  0.103   1.00 18.84 ? 48   HIS I O   1 
ATOM   9286  C  CB  . HIS I  1 48  ? 23.847  -1.837  1.747   1.00 19.21 ? 48   HIS I CB  1 
ATOM   9287  C  CG  . HIS I  1 48  ? 24.870  -0.971  2.412   1.00 19.59 ? 48   HIS I CG  1 
ATOM   9288  N  ND1 . HIS I  1 48  ? 24.626  -0.288  3.582   1.00 19.52 ? 48   HIS I ND1 1 
ATOM   9289  C  CD2 . HIS I  1 48  ? 26.159  -0.707  2.088   1.00 20.19 ? 48   HIS I CD2 1 
ATOM   9290  C  CE1 . HIS I  1 48  ? 25.712  0.375   3.940   1.00 20.34 ? 48   HIS I CE1 1 
ATOM   9291  N  NE2 . HIS I  1 48  ? 26.656  0.139   3.048   1.00 17.89 ? 48   HIS I NE2 1 
ATOM   9292  N  N   . GLU I  1 49  ? 22.484  -4.641  2.310   1.00 21.23 ? 49   GLU I N   1 
ATOM   9293  C  CA  . GLU I  1 49  ? 21.534  -5.742  2.200   1.00 20.36 ? 49   GLU I CA  1 
ATOM   9294  C  C   . GLU I  1 49  ? 20.355  -5.500  1.240   1.00 21.98 ? 49   GLU I C   1 
ATOM   9295  O  O   . GLU I  1 49  ? 19.967  -6.390  0.481   1.00 22.66 ? 49   GLU I O   1 
ATOM   9296  C  CB  . GLU I  1 49  ? 21.028  -6.159  3.587   1.00 21.92 ? 49   GLU I CB  1 
ATOM   9297  C  CG  . GLU I  1 49  ? 20.464  -7.580  3.612   1.00 24.92 ? 49   GLU I CG  1 
ATOM   9298  C  CD  . GLU I  1 49  ? 19.726  -7.930  4.896   1.00 27.90 ? 49   GLU I CD  1 
ATOM   9299  O  OE1 . GLU I  1 49  ? 19.846  -7.186  5.897   1.00 29.10 ? 49   GLU I OE1 1 
ATOM   9300  O  OE2 . GLU I  1 49  ? 19.019  -8.961  4.898   1.00 27.97 ? 49   GLU I OE2 1 
ATOM   9301  N  N   . PHE I  1 50  ? 19.786  -4.300  1.262   1.00 22.27 ? 50   PHE I N   1 
ATOM   9302  C  CA  . PHE I  1 50  ? 18.502  -4.073  0.596   1.00 20.59 ? 50   PHE I CA  1 
ATOM   9303  C  C   . PHE I  1 50  ? 18.575  -3.139  -0.611  1.00 20.56 ? 50   PHE I C   1 
ATOM   9304  O  O   . PHE I  1 50  ? 19.215  -2.087  -0.557  1.00 20.07 ? 50   PHE I O   1 
ATOM   9305  C  CB  . PHE I  1 50  ? 17.457  -3.571  1.606   1.00 19.11 ? 50   PHE I CB  1 
ATOM   9306  C  CG  . PHE I  1 50  ? 17.253  -4.498  2.763   1.00 22.11 ? 50   PHE I CG  1 
ATOM   9307  C  CD1 . PHE I  1 50  ? 16.758  -5.775  2.559   1.00 23.44 ? 50   PHE I CD1 1 
ATOM   9308  C  CD2 . PHE I  1 50  ? 17.577  -4.106  4.048   1.00 22.78 ? 50   PHE I CD2 1 
ATOM   9309  C  CE1 . PHE I  1 50  ? 16.591  -6.631  3.608   1.00 23.81 ? 50   PHE I CE1 1 
ATOM   9310  C  CE2 . PHE I  1 50  ? 17.413  -4.960  5.091   1.00 24.91 ? 50   PHE I CE2 1 
ATOM   9311  C  CZ  . PHE I  1 50  ? 16.917  -6.226  4.873   1.00 24.89 ? 50   PHE I CZ  1 
ATOM   9312  N  N   . GLY I  1 51  ? 17.921  -3.543  -1.701  1.00 19.01 ? 51   GLY I N   1 
ATOM   9313  C  CA  . GLY I  1 51  ? 17.827  -2.717  -2.895  1.00 20.18 ? 51   GLY I CA  1 
ATOM   9314  C  C   . GLY I  1 51  ? 16.684  -1.728  -2.730  1.00 21.79 ? 51   GLY I C   1 
ATOM   9315  O  O   . GLY I  1 51  ? 15.857  -1.532  -3.618  1.00 20.75 ? 51   GLY I O   1 
ATOM   9316  N  N   . ASP I  1 52  ? 16.644  -1.108  -1.559  1.00 20.27 ? 52   ASP I N   1 
ATOM   9317  C  CA  . ASP I  1 52  ? 15.547  -0.245  -1.187  1.00 21.47 ? 52   ASP I CA  1 
ATOM   9318  C  C   . ASP I  1 52  ? 16.065  1.188   -1.017  1.00 23.18 ? 52   ASP I C   1 
ATOM   9319  O  O   . ASP I  1 52  ? 16.795  1.489   -0.079  1.00 23.84 ? 52   ASP I O   1 
ATOM   9320  C  CB  . ASP I  1 52  ? 14.892  -0.792  0.085   1.00 18.59 ? 52   ASP I CB  1 
ATOM   9321  C  CG  . ASP I  1 52  ? 13.840  0.116   0.637   1.00 22.69 ? 52   ASP I CG  1 
ATOM   9322  O  OD1 . ASP I  1 52  ? 13.782  1.284   0.220   1.00 21.76 ? 52   ASP I OD1 1 
ATOM   9323  O  OD2 . ASP I  1 52  ? 13.068  -0.337  1.509   1.00 28.70 ? 52   ASP I OD2 1 
ATOM   9324  N  N   . ASN I  1 53  ? 15.698  2.059   -1.953  1.00 23.35 ? 53   ASN I N   1 
ATOM   9325  C  CA  . ASN I  1 53  ? 16.103  3.459   -1.918  1.00 22.38 ? 53   ASN I CA  1 
ATOM   9326  C  C   . ASN I  1 53  ? 14.962  4.395   -1.530  1.00 24.53 ? 53   ASN I C   1 
ATOM   9327  O  O   . ASN I  1 53  ? 14.953  5.562   -1.927  1.00 26.00 ? 53   ASN I O   1 
ATOM   9328  C  CB  . ASN I  1 53  ? 16.642  3.877   -3.284  1.00 25.16 ? 53   ASN I CB  1 
ATOM   9329  C  CG  . ASN I  1 53  ? 17.279  5.259   -3.268  1.00 27.78 ? 53   ASN I CG  1 
ATOM   9330  O  OD1 . ASN I  1 53  ? 17.854  5.681   -2.262  1.00 27.04 ? 53   ASN I OD1 1 
ATOM   9331  N  ND2 . ASN I  1 53  ? 17.188  5.967   -4.399  1.00 30.83 ? 53   ASN I ND2 1 
ATOM   9332  N  N   . THR I  1 54  ? 14.006  3.894   -0.752  1.00 23.85 ? 54   THR I N   1 
ATOM   9333  C  CA  . THR I  1 54  ? 12.789  4.653   -0.478  1.00 27.22 ? 54   THR I CA  1 
ATOM   9334  C  C   . THR I  1 54  ? 13.024  5.766   0.540   1.00 26.36 ? 54   THR I C   1 
ATOM   9335  O  O   . THR I  1 54  ? 12.268  6.728   0.604   1.00 28.36 ? 54   THR I O   1 
ATOM   9336  C  CB  . THR I  1 54  ? 11.596  3.743   -0.058  1.00 24.00 ? 54   THR I CB  1 
ATOM   9337  O  OG1 . THR I  1 54  ? 11.923  3.032   1.140   1.00 26.29 ? 54   THR I OG1 1 
ATOM   9338  C  CG2 . THR I  1 54  ? 11.274  2.745   -1.170  1.00 24.63 ? 54   THR I CG2 1 
ATOM   9339  N  N   . ALA I  1 55  ? 14.093  5.644   1.313   1.00 27.21 ? 55   ALA I N   1 
ATOM   9340  C  CA  . ALA I  1 55  ? 14.437  6.656   2.299   1.00 26.92 ? 55   ALA I CA  1 
ATOM   9341  C  C   . ALA I  1 55  ? 15.857  7.160   2.077   1.00 28.07 ? 55   ALA I C   1 
ATOM   9342  O  O   . ALA I  1 55  ? 16.535  7.563   3.021   1.00 31.46 ? 55   ALA I O   1 
ATOM   9343  C  CB  . ALA I  1 55  ? 14.290  6.093   3.710   1.00 26.27 ? 55   ALA I CB  1 
ATOM   9344  N  N   . GLY I  1 56  ? 16.305  7.138   0.828   1.00 26.49 ? 56   GLY I N   1 
ATOM   9345  C  CA  . GLY I  1 56  ? 17.682  7.472   0.518   1.00 26.27 ? 56   GLY I CA  1 
ATOM   9346  C  C   . GLY I  1 56  ? 18.582  6.269   0.736   1.00 26.17 ? 56   GLY I C   1 
ATOM   9347  O  O   . GLY I  1 56  ? 18.134  5.121   0.666   1.00 24.68 ? 56   GLY I O   1 
ATOM   9348  N  N   . CYS I  1 57  ? 19.853  6.532   1.019   1.00 27.12 ? 57   CYS I N   1 
ATOM   9349  C  CA  . CYS I  1 57  ? 20.844  5.468   1.133   1.00 25.72 ? 57   CYS I CA  1 
ATOM   9350  C  C   . CYS I  1 57  ? 20.658  4.658   2.394   1.00 23.90 ? 57   CYS I C   1 
ATOM   9351  O  O   . CYS I  1 57  ? 21.121  3.522   2.480   1.00 24.94 ? 57   CYS I O   1 
ATOM   9352  C  CB  . CYS I  1 57  ? 22.253  6.049   1.081   1.00 26.63 ? 57   CYS I CB  1 
ATOM   9353  S  SG  . CYS I  1 57  ? 22.658  6.702   -0.558  1.00 32.93 ? 57   CYS I SG  1 
ATOM   9354  N  N   . THR I  1 58  ? 19.953  5.253   3.352   1.00 26.59 ? 58   THR I N   1 
ATOM   9355  C  CA  . THR I  1 58  ? 19.741  4.691   4.685   1.00 26.01 ? 58   THR I CA  1 
ATOM   9356  C  C   . THR I  1 58  ? 18.921  3.411   4.683   1.00 23.91 ? 58   THR I C   1 
ATOM   9357  O  O   . THR I  1 58  ? 19.176  2.499   5.471   1.00 23.88 ? 58   THR I O   1 
ATOM   9358  C  CB  . THR I  1 58  ? 19.019  5.713   5.571   1.00 28.01 ? 58   THR I CB  1 
ATOM   9359  O  OG1 . THR I  1 58  ? 19.682  6.982   5.473   1.00 32.53 ? 58   THR I OG1 1 
ATOM   9360  C  CG2 . THR I  1 58  ? 19.018  5.256   7.005   1.00 27.33 ? 58   THR I CG2 1 
ATOM   9361  N  N   . SER I  1 59  ? 17.925  3.354   3.805   1.00 22.61 ? 59   SER I N   1 
ATOM   9362  C  CA  . SER I  1 59  ? 17.038  2.200   3.732   1.00 22.08 ? 59   SER I CA  1 
ATOM   9363  C  C   . SER I  1 59  ? 17.690  0.991   3.066   1.00 22.58 ? 59   SER I C   1 
ATOM   9364  O  O   . SER I  1 59  ? 17.088  -0.078  2.975   1.00 22.13 ? 59   SER I O   1 
ATOM   9365  C  CB  . SER I  1 59  ? 15.729  2.573   3.037   1.00 21.82 ? 59   SER I CB  1 
ATOM   9366  O  OG  . SER I  1 59  ? 15.961  3.459   1.963   1.00 24.51 ? 59   SER I OG  1 
ATOM   9367  N  N   . ALA I  1 60  ? 18.931  1.177   2.623   1.00 24.13 ? 60   ALA I N   1 
ATOM   9368  C  CA  . ALA I  1 60  ? 19.752  0.120   2.036   1.00 23.11 ? 60   ALA I CA  1 
ATOM   9369  C  C   . ALA I  1 60  ? 20.082  -0.933  3.090   1.00 22.96 ? 60   ALA I C   1 
ATOM   9370  O  O   . ALA I  1 60  ? 20.479  -2.056  2.773   1.00 21.09 ? 60   ALA I O   1 
ATOM   9371  C  CB  . ALA I  1 60  ? 21.034  0.713   1.465   1.00 20.73 ? 60   ALA I CB  1 
ATOM   9372  N  N   . GLY I  1 61  ? 19.894  -0.562  4.349   1.00 22.13 ? 61   GLY I N   1 
ATOM   9373  C  CA  . GLY I  1 61  ? 20.201  -1.443  5.450   1.00 23.47 ? 61   GLY I CA  1 
ATOM   9374  C  C   . GLY I  1 61  ? 21.685  -1.528  5.744   1.00 22.36 ? 61   GLY I C   1 
ATOM   9375  O  O   . GLY I  1 61  ? 22.457  -0.637  5.397   1.00 22.43 ? 61   GLY I O   1 
ATOM   9376  N  N   . PRO I  1 62  ? 22.094  -2.616  6.394   1.00 23.11 ? 62   PRO I N   1 
ATOM   9377  C  CA  . PRO I  1 62  ? 23.476  -2.772  6.833   1.00 23.44 ? 62   PRO I CA  1 
ATOM   9378  C  C   . PRO I  1 62  ? 24.275  -3.404  5.713   1.00 21.16 ? 62   PRO I C   1 
ATOM   9379  O  O   . PRO I  1 62  ? 23.726  -3.713  4.656   1.00 22.78 ? 62   PRO I O   1 
ATOM   9380  C  CB  . PRO I  1 62  ? 23.355  -3.777  7.985   1.00 23.60 ? 62   PRO I CB  1 
ATOM   9381  C  CG  . PRO I  1 62  ? 21.955  -4.375  7.883   1.00 22.32 ? 62   PRO I CG  1 
ATOM   9382  C  CD  . PRO I  1 62  ? 21.309  -3.831  6.647   1.00 21.68 ? 62   PRO I CD  1 
ATOM   9383  N  N   . HIS I  1 63  ? 25.560  -3.610  5.944   1.00 20.44 ? 63   HIS I N   1 
ATOM   9384  C  CA  . HIS I  1 63  ? 26.354  -4.385  5.012   1.00 21.02 ? 63   HIS I CA  1 
ATOM   9385  C  C   . HIS I  1 63  ? 25.731  -5.766  4.800   1.00 20.91 ? 63   HIS I C   1 
ATOM   9386  O  O   . HIS I  1 63  ? 25.315  -6.423  5.755   1.00 20.87 ? 63   HIS I O   1 
ATOM   9387  C  CB  . HIS I  1 63  ? 27.799  -4.491  5.512   1.00 21.33 ? 63   HIS I CB  1 
ATOM   9388  C  CG  . HIS I  1 63  ? 28.466  -3.160  5.691   1.00 20.76 ? 63   HIS I CG  1 
ATOM   9389  N  ND1 . HIS I  1 63  ? 29.647  -3.001  6.380   1.00 20.83 ? 63   HIS I ND1 1 
ATOM   9390  C  CD2 . HIS I  1 63  ? 28.100  -1.923  5.286   1.00 20.47 ? 63   HIS I CD2 1 
ATOM   9391  C  CE1 . HIS I  1 63  ? 29.990  -1.726  6.379   1.00 22.79 ? 63   HIS I CE1 1 
ATOM   9392  N  NE2 . HIS I  1 63  ? 29.063  -1.048  5.724   1.00 22.24 ? 63   HIS I NE2 1 
ATOM   9393  N  N   . PHE I  1 64  ? 25.657  -6.187  3.539   1.00 21.69 ? 64   PHE I N   1 
ATOM   9394  C  CA  . PHE I  1 64  ? 25.116  -7.491  3.184   1.00 20.71 ? 64   PHE I CA  1 
ATOM   9395  C  C   . PHE I  1 64  ? 25.892  -8.568  3.946   1.00 23.53 ? 64   PHE I C   1 
ATOM   9396  O  O   . PHE I  1 64  ? 27.093  -8.736  3.743   1.00 24.86 ? 64   PHE I O   1 
ATOM   9397  C  CB  . PHE I  1 64  ? 25.190  -7.692  1.670   1.00 21.53 ? 64   PHE I CB  1 
ATOM   9398  C  CG  . PHE I  1 64  ? 24.647  -9.014  1.202   1.00 24.57 ? 64   PHE I CG  1 
ATOM   9399  C  CD1 . PHE I  1 64  ? 23.515  -9.564  1.790   1.00 25.09 ? 64   PHE I CD1 1 
ATOM   9400  C  CD2 . PHE I  1 64  ? 25.268  -9.706  0.170   1.00 22.21 ? 64   PHE I CD2 1 
ATOM   9401  C  CE1 . PHE I  1 64  ? 23.018  -10.786 1.353   1.00 24.57 ? 64   PHE I CE1 1 
ATOM   9402  C  CE2 . PHE I  1 64  ? 24.778  -10.923 -0.270  1.00 23.93 ? 64   PHE I CE2 1 
ATOM   9403  C  CZ  . PHE I  1 64  ? 23.652  -11.462 0.318   1.00 24.75 ? 64   PHE I CZ  1 
ATOM   9404  N  N   . ASN I  1 65  ? 25.205  -9.276  4.835   1.00 24.74 ? 65   ASN I N   1 
ATOM   9405  C  CA  . ASN I  1 65  ? 25.863  -10.164 5.795   1.00 25.14 ? 65   ASN I CA  1 
ATOM   9406  C  C   . ASN I  1 65  ? 25.114  -11.472 6.051   1.00 24.03 ? 65   ASN I C   1 
ATOM   9407  O  O   . ASN I  1 65  ? 24.699  -11.724 7.176   1.00 26.42 ? 65   ASN I O   1 
ATOM   9408  C  CB  . ASN I  1 65  ? 26.036  -9.437  7.128   1.00 23.77 ? 65   ASN I CB  1 
ATOM   9409  C  CG  . ASN I  1 65  ? 26.916  -10.194 8.090   1.00 24.36 ? 65   ASN I CG  1 
ATOM   9410  O  OD1 . ASN I  1 65  ? 27.608  -11.134 7.701   1.00 25.12 ? 65   ASN I OD1 1 
ATOM   9411  N  ND2 . ASN I  1 65  ? 26.913  -9.779  9.351   1.00 24.10 ? 65   ASN I ND2 1 
ATOM   9412  N  N   . PRO I  1 66  ? 24.956  -12.314 5.011   1.00 25.54 ? 66   PRO I N   1 
ATOM   9413  C  CA  . PRO I  1 66  ? 24.154  -13.541 5.106   1.00 27.08 ? 66   PRO I CA  1 
ATOM   9414  C  C   . PRO I  1 66  ? 24.693  -14.605 6.073   1.00 29.35 ? 66   PRO I C   1 
ATOM   9415  O  O   . PRO I  1 66  ? 23.937  -15.502 6.442   1.00 31.66 ? 66   PRO I O   1 
ATOM   9416  C  CB  . PRO I  1 66  ? 24.169  -14.081 3.670   1.00 26.66 ? 66   PRO I CB  1 
ATOM   9417  C  CG  . PRO I  1 66  ? 25.333  -13.470 3.034   1.00 24.52 ? 66   PRO I CG  1 
ATOM   9418  C  CD  . PRO I  1 66  ? 25.535  -12.140 3.668   1.00 23.08 ? 66   PRO I CD  1 
ATOM   9419  N  N   . LEU I  1 67  ? 25.963  -14.514 6.466   1.00 28.90 ? 67   LEU I N   1 
ATOM   9420  C  CA  . LEU I  1 67  ? 26.577  -15.517 7.340   1.00 28.53 ? 67   LEU I CA  1 
ATOM   9421  C  C   . LEU I  1 67  ? 26.755  -15.008 8.762   1.00 29.87 ? 67   LEU I C   1 
ATOM   9422  O  O   . LEU I  1 67  ? 27.147  -15.747 9.655   1.00 31.00 ? 67   LEU I O   1 
ATOM   9423  C  CB  . LEU I  1 67  ? 27.904  -16.014 6.756   1.00 30.88 ? 67   LEU I CB  1 
ATOM   9424  C  CG  . LEU I  1 67  ? 27.752  -16.700 5.394   1.00 28.42 ? 67   LEU I CG  1 
ATOM   9425  C  CD1 . LEU I  1 67  ? 29.061  -17.278 4.907   1.00 28.62 ? 67   LEU I CD1 1 
ATOM   9426  C  CD2 . LEU I  1 67  ? 26.677  -17.774 5.476   1.00 30.93 ? 67   LEU I CD2 1 
ATOM   9427  N  N   . SER I  1 68  ? 26.458  -13.733 8.964   1.00 29.44 ? 68   SER I N   1 
ATOM   9428  C  CA  . SER I  1 68  ? 26.373  -13.177 10.301  1.00 29.97 ? 68   SER I CA  1 
ATOM   9429  C  C   . SER I  1 68  ? 27.751  -13.046 10.911  1.00 32.52 ? 68   SER I C   1 
ATOM   9430  O  O   . SER I  1 68  ? 27.962  -13.320 12.100  1.00 32.97 ? 68   SER I O   1 
ATOM   9431  C  CB  . SER I  1 68  ? 25.439  -14.015 11.173  1.00 32.56 ? 68   SER I CB  1 
ATOM   9432  O  OG  . SER I  1 68  ? 24.120  -13.994 10.648  1.00 34.27 ? 68   SER I OG  1 
ATOM   9433  N  N   . ARG I  1 69  ? 28.675  -12.592 10.069  1.00 30.81 ? 69   ARG I N   1 
ATOM   9434  C  CA  . ARG I  1 69  ? 30.064  -12.384 10.439  1.00 29.21 ? 69   ARG I CA  1 
ATOM   9435  C  C   . ARG I  1 69  ? 30.268  -10.950 10.901  1.00 30.49 ? 69   ARG I C   1 
ATOM   9436  O  O   . ARG I  1 69  ? 29.360  -10.111 10.794  1.00 29.18 ? 69   ARG I O   1 
ATOM   9437  C  CB  . ARG I  1 69  ? 30.959  -12.642 9.232   1.00 26.90 ? 69   ARG I CB  1 
ATOM   9438  C  CG  . ARG I  1 69  ? 30.714  -13.968 8.544   1.00 32.24 ? 69   ARG I CG  1 
ATOM   9439  C  CD  . ARG I  1 69  ? 31.459  -15.090 9.245   1.00 37.10 ? 69   ARG I CD  1 
ATOM   9440  N  NE  . ARG I  1 69  ? 30.708  -15.647 10.360  1.00 38.02 ? 69   ARG I NE  1 
ATOM   9441  C  CZ  . ARG I  1 69  ? 31.179  -16.571 11.188  1.00 39.47 ? 69   ARG I CZ  1 
ATOM   9442  N  NH1 . ARG I  1 69  ? 32.416  -17.029 11.045  1.00 37.74 ? 69   ARG I NH1 1 
ATOM   9443  N  NH2 . ARG I  1 69  ? 30.411  -17.029 12.166  1.00 45.07 ? 69   ARG I NH2 1 
ATOM   9444  N  N   . LYS I  1 70  ? 31.469  -10.675 11.399  1.00 28.46 ? 70   LYS I N   1 
ATOM   9445  C  CA  . LYS I  1 70  ? 31.853  -9.324  11.784  1.00 29.65 ? 70   LYS I CA  1 
ATOM   9446  C  C   . LYS I  1 70  ? 32.526  -8.597  10.628  1.00 25.95 ? 70   LYS I C   1 
ATOM   9447  O  O   . LYS I  1 70  ? 33.046  -9.226  9.710   1.00 25.76 ? 70   LYS I O   1 
ATOM   9448  C  CB  . LYS I  1 70  ? 32.763  -9.350  13.013  1.00 31.14 ? 70   LYS I CB  1 
ATOM   9449  C  CG  . LYS I  1 70  ? 31.983  -9.301  14.310  1.00 34.91 ? 70   LYS I CG  1 
ATOM   9450  C  CD  . LYS I  1 70  ? 32.890  -9.253  15.516  1.00 38.15 ? 70   LYS I CD  1 
ATOM   9451  C  CE  . LYS I  1 70  ? 32.053  -9.007  16.754  1.00 44.79 ? 70   LYS I CE  1 
ATOM   9452  N  NZ  . LYS I  1 70  ? 30.725  -9.672  16.614  1.00 42.32 ? 70   LYS I NZ  1 
ATOM   9453  N  N   . HIS I  1 71  ? 32.505  -7.270  10.676  1.00 23.91 ? 71   HIS I N   1 
ATOM   9454  C  CA  . HIS I  1 71  ? 33.066  -6.463  9.600   1.00 23.42 ? 71   HIS I CA  1 
ATOM   9455  C  C   . HIS I  1 71  ? 34.563  -6.690  9.417   1.00 23.68 ? 71   HIS I C   1 
ATOM   9456  O  O   . HIS I  1 71  ? 35.305  -6.815  10.386  1.00 24.78 ? 71   HIS I O   1 
ATOM   9457  C  CB  . HIS I  1 71  ? 32.790  -4.969  9.826   1.00 22.79 ? 71   HIS I CB  1 
ATOM   9458  C  CG  . HIS I  1 71  ? 33.329  -4.089  8.740   1.00 23.50 ? 71   HIS I CG  1 
ATOM   9459  N  ND1 . HIS I  1 71  ? 32.709  -3.949  7.516   1.00 22.17 ? 71   HIS I ND1 1 
ATOM   9460  C  CD2 . HIS I  1 71  ? 34.441  -3.316  8.686   1.00 23.54 ? 71   HIS I CD2 1 
ATOM   9461  C  CE1 . HIS I  1 71  ? 33.413  -3.135  6.753   1.00 18.82 ? 71   HIS I CE1 1 
ATOM   9462  N  NE2 . HIS I  1 71  ? 34.466  -2.734  7.440   1.00 21.88 ? 71   HIS I NE2 1 
ATOM   9463  N  N   . GLY I  1 72  ? 34.994  -6.739  8.159   1.00 23.21 ? 72   GLY I N   1 
ATOM   9464  C  CA  . GLY I  1 72  ? 36.400  -6.819  7.824   1.00 23.17 ? 72   GLY I CA  1 
ATOM   9465  C  C   . GLY I  1 72  ? 36.696  -6.316  6.421   1.00 24.41 ? 72   GLY I C   1 
ATOM   9466  O  O   . GLY I  1 72  ? 35.819  -5.778  5.747   1.00 24.03 ? 72   GLY I O   1 
ATOM   9467  N  N   . GLY I  1 73  ? 37.940  -6.487  5.983   1.00 23.67 ? 73   GLY I N   1 
ATOM   9468  C  CA  . GLY I  1 73  ? 38.322  -6.173  4.623   1.00 24.50 ? 73   GLY I CA  1 
ATOM   9469  C  C   . GLY I  1 73  ? 38.002  -7.360  3.738   1.00 28.06 ? 73   GLY I C   1 
ATOM   9470  O  O   . GLY I  1 73  ? 37.679  -8.436  4.251   1.00 28.00 ? 73   GLY I O   1 
ATOM   9471  N  N   . PRO I  1 74  ? 38.089  -7.168  2.409   1.00 26.54 ? 74   PRO I N   1 
ATOM   9472  C  CA  . PRO I  1 74  ? 37.812  -8.174  1.377   1.00 25.39 ? 74   PRO I CA  1 
ATOM   9473  C  C   . PRO I  1 74  ? 38.780  -9.349  1.465   1.00 31.20 ? 74   PRO I C   1 
ATOM   9474  O  O   . PRO I  1 74  ? 38.447  -10.466 1.060   1.00 32.07 ? 74   PRO I O   1 
ATOM   9475  C  CB  . PRO I  1 74  ? 38.091  -7.430  0.063   1.00 27.86 ? 74   PRO I CB  1 
ATOM   9476  C  CG  . PRO I  1 74  ? 38.227  -6.008  0.396   1.00 24.39 ? 74   PRO I CG  1 
ATOM   9477  C  CD  . PRO I  1 74  ? 38.585  -5.904  1.840   1.00 27.01 ? 74   PRO I CD  1 
ATOM   9478  N  N   . LYS I  1 75  ? 39.983  -9.090  1.967   1.00 32.01 ? 75   LYS I N   1 
ATOM   9479  C  CA  . LYS I  1 75  ? 41.011  -10.122 2.018   1.00 31.66 ? 75   LYS I CA  1 
ATOM   9480  C  C   . LYS I  1 75  ? 41.075  -10.812 3.385   1.00 30.99 ? 75   LYS I C   1 
ATOM   9481  O  O   . LYS I  1 75  ? 41.882  -11.717 3.588   1.00 35.73 ? 75   LYS I O   1 
ATOM   9482  C  CB  . LYS I  1 75  ? 42.381  -9.550  1.643   1.00 30.48 ? 75   LYS I CB  1 
ATOM   9483  C  CG  . LYS I  1 75  ? 42.394  -8.681  0.388   1.00 35.06 ? 75   LYS I CG  1 
ATOM   9484  C  CD  . LYS I  1 75  ? 41.603  -9.302  -0.767  1.00 38.26 ? 75   LYS I CD  1 
ATOM   9485  C  CE  . LYS I  1 75  ? 42.439  -10.273 -1.603  1.00 38.78 ? 75   LYS I CE  1 
ATOM   9486  N  NZ  . LYS I  1 75  ? 41.895  -10.445 -2.988  1.00 38.39 ? 75   LYS I NZ  1 
ATOM   9487  N  N   . ASP I  1 76  ? 40.224  -10.391 4.315   1.00 30.05 ? 76   ASP I N   1 
ATOM   9488  C  CA  . ASP I  1 76  ? 40.149  -11.021 5.630   1.00 29.13 ? 76   ASP I CA  1 
ATOM   9489  C  C   . ASP I  1 76  ? 39.245  -12.255 5.615   1.00 32.89 ? 76   ASP I C   1 
ATOM   9490  O  O   . ASP I  1 76  ? 38.382  -12.395 4.741   1.00 32.13 ? 76   ASP I O   1 
ATOM   9491  C  CB  . ASP I  1 76  ? 39.613  -10.034 6.664   1.00 29.06 ? 76   ASP I CB  1 
ATOM   9492  C  CG  . ASP I  1 76  ? 40.574  -8.898  6.954   1.00 32.22 ? 76   ASP I CG  1 
ATOM   9493  O  OD1 . ASP I  1 76  ? 41.760  -8.983  6.575   1.00 37.76 ? 76   ASP I OD1 1 
ATOM   9494  O  OD2 . ASP I  1 76  ? 40.140  -7.912  7.576   1.00 30.30 ? 76   ASP I OD2 1 
ATOM   9495  N  N   . GLU I  1 77  ? 39.441  -13.140 6.593   1.00 32.53 ? 77   GLU I N   1 
ATOM   9496  C  CA  . GLU I  1 77  ? 38.588  -14.310 6.769   1.00 32.16 ? 77   GLU I CA  1 
ATOM   9497  C  C   . GLU I  1 77  ? 37.248  -13.892 7.381   1.00 33.73 ? 77   GLU I C   1 
ATOM   9498  O  O   . GLU I  1 77  ? 36.178  -14.276 6.890   1.00 35.59 ? 77   GLU I O   1 
ATOM   9499  C  CB  . GLU I  1 77  ? 39.282  -15.355 7.653   1.00 37.94 ? 77   GLU I CB  1 
ATOM   9500  C  CG  . GLU I  1 77  ? 40.117  -16.410 6.907   1.00 39.92 ? 77   GLU I CG  1 
ATOM   9501  C  CD  . GLU I  1 77  ? 39.386  -17.751 6.722   1.00 42.27 ? 77   GLU I CD  1 
ATOM   9502  O  OE1 . GLU I  1 77  ? 38.909  -18.327 7.728   1.00 37.01 ? 77   GLU I OE1 1 
ATOM   9503  O  OE2 . GLU I  1 77  ? 39.307  -18.236 5.567   1.00 43.18 ? 77   GLU I OE2 1 
ATOM   9504  N  N   . GLU I  1 78  ? 37.308  -13.115 8.462   1.00 34.17 ? 78   GLU I N   1 
ATOM   9505  C  CA  . GLU I  1 78  ? 36.110  -12.491 9.030   1.00 32.53 ? 78   GLU I CA  1 
ATOM   9506  C  C   . GLU I  1 78  ? 35.756  -11.232 8.249   1.00 29.09 ? 78   GLU I C   1 
ATOM   9507  O  O   . GLU I  1 78  ? 36.414  -10.200 8.393   1.00 28.33 ? 78   GLU I O   1 
ATOM   9508  C  CB  . GLU I  1 78  ? 36.299  -12.127 10.508  1.00 30.91 ? 78   GLU I CB  1 
ATOM   9509  C  CG  . GLU I  1 78  ? 35.774  -13.166 11.469  1.00 34.87 ? 78   GLU I CG  1 
ATOM   9510  C  CD  . GLU I  1 78  ? 34.272  -13.344 11.375  1.00 36.10 ? 78   GLU I CD  1 
ATOM   9511  O  OE1 . GLU I  1 78  ? 33.516  -12.437 11.791  1.00 34.07 ? 78   GLU I OE1 1 
ATOM   9512  O  OE2 . GLU I  1 78  ? 33.845  -14.415 10.902  1.00 40.96 ? 78   GLU I OE2 1 
ATOM   9513  N  N   . ARG I  1 79  ? 34.728  -11.339 7.410   1.00 29.64 ? 79   ARG I N   1 
ATOM   9514  C  CA  . ARG I  1 79  ? 34.160  -10.197 6.709   1.00 25.72 ? 79   ARG I CA  1 
ATOM   9515  C  C   . ARG I  1 79  ? 32.705  -10.488 6.392   1.00 27.17 ? 79   ARG I C   1 
ATOM   9516  O  O   . ARG I  1 79  ? 32.302  -11.651 6.307   1.00 26.83 ? 79   ARG I O   1 
ATOM   9517  C  CB  . ARG I  1 79  ? 34.918  -9.923  5.409   1.00 25.43 ? 79   ARG I CB  1 
ATOM   9518  C  CG  . ARG I  1 79  ? 35.053  -11.140 4.533   1.00 25.43 ? 79   ARG I CG  1 
ATOM   9519  C  CD  . ARG I  1 79  ? 35.496  -10.791 3.151   1.00 25.92 ? 79   ARG I CD  1 
ATOM   9520  N  NE  . ARG I  1 79  ? 34.376  -10.426 2.287   1.00 25.68 ? 79   ARG I NE  1 
ATOM   9521  C  CZ  . ARG I  1 79  ? 34.487  -10.248 0.974   1.00 26.06 ? 79   ARG I CZ  1 
ATOM   9522  N  NH1 . ARG I  1 79  ? 35.667  -10.400 0.390   1.00 26.17 ? 79   ARG I NH1 1 
ATOM   9523  N  NH2 . ARG I  1 79  ? 33.426  -9.929  0.242   1.00 22.84 ? 79   ARG I NH2 1 
ATOM   9524  N  N   . HIS I  1 80  ? 31.924  -9.421  6.245   1.00 26.30 ? 80   HIS I N   1 
ATOM   9525  C  CA  . HIS I  1 80  ? 30.593  -9.487  5.662   1.00 25.04 ? 80   HIS I CA  1 
ATOM   9526  C  C   . HIS I  1 80  ? 30.743  -9.791  4.178   1.00 24.27 ? 80   HIS I C   1 
ATOM   9527  O  O   . HIS I  1 80  ? 31.642  -9.265  3.526   1.00 22.97 ? 80   HIS I O   1 
ATOM   9528  C  CB  . HIS I  1 80  ? 29.920  -8.117  5.748   1.00 23.19 ? 80   HIS I CB  1 
ATOM   9529  C  CG  . HIS I  1 80  ? 29.777  -7.585  7.135   1.00 22.31 ? 80   HIS I CG  1 
ATOM   9530  N  ND1 . HIS I  1 80  ? 29.986  -6.260  7.442   1.00 22.08 ? 80   HIS I ND1 1 
ATOM   9531  C  CD2 . HIS I  1 80  ? 29.409  -8.184  8.288   1.00 24.95 ? 80   HIS I CD2 1 
ATOM   9532  C  CE1 . HIS I  1 80  ? 29.766  -6.064  8.728   1.00 22.95 ? 80   HIS I CE1 1 
ATOM   9533  N  NE2 . HIS I  1 80  ? 29.408  -7.216  9.266   1.00 27.42 ? 80   HIS I NE2 1 
ATOM   9534  N  N   . VAL I  1 81  ? 29.857  -10.602 3.617   1.00 25.46 ? 81   VAL I N   1 
ATOM   9535  C  CA  . VAL I  1 81  ? 29.867  -10.780 2.165   1.00 23.36 ? 81   VAL I CA  1 
ATOM   9536  C  C   . VAL I  1 81  ? 30.024  -9.416  1.473   1.00 24.57 ? 81   VAL I C   1 
ATOM   9537  O  O   . VAL I  1 81  ? 30.754  -9.292  0.493   1.00 26.16 ? 81   VAL I O   1 
ATOM   9538  C  CB  . VAL I  1 81  ? 28.598  -11.526 1.660   1.00 24.10 ? 81   VAL I CB  1 
ATOM   9539  C  CG1 . VAL I  1 81  ? 28.454  -11.424 0.137   1.00 22.88 ? 81   VAL I CG1 1 
ATOM   9540  C  CG2 . VAL I  1 81  ? 28.640  -12.975 2.090   1.00 26.47 ? 81   VAL I CG2 1 
ATOM   9541  N  N   . GLY I  1 82  ? 29.364  -8.389  2.007   1.00 24.64 ? 82   GLY I N   1 
ATOM   9542  C  CA  . GLY I  1 82  ? 29.342  -7.083  1.368   1.00 21.86 ? 82   GLY I CA  1 
ATOM   9543  C  C   . GLY I  1 82  ? 30.610  -6.243  1.424   1.00 21.93 ? 82   GLY I C   1 
ATOM   9544  O  O   . GLY I  1 82  ? 30.686  -5.203  0.775   1.00 21.62 ? 82   GLY I O   1 
ATOM   9545  N  N   . ASP I  1 83  ? 31.609  -6.696  2.177   1.00 22.01 ? 83   ASP I N   1 
ATOM   9546  C  CA  . ASP I  1 83  ? 32.817  -5.904  2.429   1.00 22.88 ? 83   ASP I CA  1 
ATOM   9547  C  C   . ASP I  1 83  ? 33.820  -5.870  1.286   1.00 21.00 ? 83   ASP I C   1 
ATOM   9548  O  O   . ASP I  1 83  ? 34.671  -6.745  1.192   1.00 22.52 ? 83   ASP I O   1 
ATOM   9549  C  CB  . ASP I  1 83  ? 33.540  -6.434  3.658   1.00 21.65 ? 83   ASP I CB  1 
ATOM   9550  C  CG  . ASP I  1 83  ? 32.754  -6.242  4.920   1.00 22.42 ? 83   ASP I CG  1 
ATOM   9551  O  OD1 . ASP I  1 83  ? 31.726  -5.540  4.866   1.00 20.80 ? 83   ASP I OD1 1 
ATOM   9552  O  OD2 . ASP I  1 83  ? 33.169  -6.797  5.962   1.00 22.81 ? 83   ASP I OD2 1 
ATOM   9553  N  N   . LEU I  1 84  ? 33.749  -4.846  0.443   1.00 19.33 ? 84   LEU I N   1 
ATOM   9554  C  CA  . LEU I  1 84  ? 34.686  -4.721  -0.666  1.00 20.50 ? 84   LEU I CA  1 
ATOM   9555  C  C   . LEU I  1 84  ? 35.822  -3.752  -0.345  1.00 22.82 ? 84   LEU I C   1 
ATOM   9556  O  O   . LEU I  1 84  ? 36.593  -3.362  -1.230  1.00 21.64 ? 84   LEU I O   1 
ATOM   9557  C  CB  . LEU I  1 84  ? 33.966  -4.336  -1.963  1.00 20.03 ? 84   LEU I CB  1 
ATOM   9558  C  CG  . LEU I  1 84  ? 33.119  -5.480  -2.529  1.00 21.78 ? 84   LEU I CG  1 
ATOM   9559  C  CD1 . LEU I  1 84  ? 32.475  -5.070  -3.832  1.00 21.05 ? 84   LEU I CD1 1 
ATOM   9560  C  CD2 . LEU I  1 84  ? 33.959  -6.758  -2.698  1.00 20.31 ? 84   LEU I CD2 1 
ATOM   9561  N  N   . GLY I  1 85  ? 35.928  -3.385  0.927   1.00 19.10 ? 85   GLY I N   1 
ATOM   9562  C  CA  . GLY I  1 85  ? 36.989  -2.509  1.376   1.00 21.69 ? 85   GLY I CA  1 
ATOM   9563  C  C   . GLY I  1 85  ? 36.884  -1.073  0.888   1.00 20.80 ? 85   GLY I C   1 
ATOM   9564  O  O   . GLY I  1 85  ? 35.827  -0.450  0.945   1.00 18.28 ? 85   GLY I O   1 
ATOM   9565  N  N   . ASN I  1 86  ? 38.007  -0.555  0.397   1.00 24.46 ? 86   ASN I N   1 
ATOM   9566  C  CA  . ASN I  1 86  ? 38.155  0.862   0.087   1.00 21.20 ? 86   ASN I CA  1 
ATOM   9567  C  C   . ASN I  1 86  ? 38.377  1.089   -1.387  1.00 18.68 ? 86   ASN I C   1 
ATOM   9568  O  O   . ASN I  1 86  ? 38.993  0.268   -2.057  1.00 20.40 ? 86   ASN I O   1 
ATOM   9569  C  CB  . ASN I  1 86  ? 39.349  1.438   0.861   1.00 20.42 ? 86   ASN I CB  1 
ATOM   9570  C  CG  . ASN I  1 86  ? 39.053  1.642   2.334   1.00 19.07 ? 86   ASN I CG  1 
ATOM   9571  O  OD1 . ASN I  1 86  ? 38.144  2.382   2.702   1.00 19.24 ? 86   ASN I OD1 1 
ATOM   9572  N  ND2 . ASN I  1 86  ? 39.833  1.000   3.186   1.00 22.09 ? 86   ASN I ND2 1 
ATOM   9573  N  N   . VAL I  1 87  ? 37.873  2.205   -1.895  1.00 18.83 ? 87   VAL I N   1 
ATOM   9574  C  CA  . VAL I  1 87  ? 38.275  2.680   -3.219  1.00 19.55 ? 87   VAL I CA  1 
ATOM   9575  C  C   . VAL I  1 87  ? 39.035  3.999   -3.032  1.00 19.91 ? 87   VAL I C   1 
ATOM   9576  O  O   . VAL I  1 87  ? 38.911  4.657   -1.994  1.00 18.56 ? 87   VAL I O   1 
ATOM   9577  C  CB  . VAL I  1 87  ? 37.099  2.773   -4.277  1.00 16.45 ? 87   VAL I CB  1 
ATOM   9578  C  CG1 . VAL I  1 87  ? 36.458  1.410   -4.495  1.00 16.35 ? 87   VAL I CG1 1 
ATOM   9579  C  CG2 . VAL I  1 87  ? 36.049  3.806   -3.890  1.00 16.81 ? 87   VAL I CG2 1 
ATOM   9580  N  N   . THR I  1 88  ? 39.838  4.356   -4.029  1.00 19.51 ? 88   THR I N   1 
ATOM   9581  C  CA  . THR I  1 88  ? 40.771  5.463   -3.918  1.00 20.97 ? 88   THR I CA  1 
ATOM   9582  C  C   . THR I  1 88  ? 40.448  6.534   -4.937  1.00 21.13 ? 88   THR I C   1 
ATOM   9583  O  O   . THR I  1 88  ? 40.444  6.264   -6.137  1.00 21.56 ? 88   THR I O   1 
ATOM   9584  C  CB  . THR I  1 88  ? 42.221  4.981   -4.147  1.00 21.00 ? 88   THR I CB  1 
ATOM   9585  O  OG1 . THR I  1 88  ? 42.519  3.921   -3.232  1.00 21.05 ? 88   THR I OG1 1 
ATOM   9586  C  CG2 . THR I  1 88  ? 43.207  6.117   -3.931  1.00 22.10 ? 88   THR I CG2 1 
ATOM   9587  N  N   . ALA I  1 89  ? 40.176  7.746   -4.455  1.00 21.62 ? 89   ALA I N   1 
ATOM   9588  C  CA  . ALA I  1 89  ? 39.927  8.888   -5.329  1.00 23.33 ? 89   ALA I CA  1 
ATOM   9589  C  C   . ALA I  1 89  ? 41.199  9.707   -5.471  1.00 24.44 ? 89   ALA I C   1 
ATOM   9590  O  O   . ALA I  1 89  ? 41.909  9.904   -4.489  1.00 24.64 ? 89   ALA I O   1 
ATOM   9591  C  CB  . ALA I  1 89  ? 38.804  9.749   -4.774  1.00 22.37 ? 89   ALA I CB  1 
ATOM   9592  N  N   . GLY I  1 90  ? 41.492  10.167  -6.689  1.00 25.86 ? 90   GLY I N   1 
ATOM   9593  C  CA  . GLY I  1 90  ? 42.643  11.019  -6.946  1.00 25.88 ? 90   GLY I CA  1 
ATOM   9594  C  C   . GLY I  1 90  ? 42.370  12.485  -6.637  1.00 28.60 ? 90   GLY I C   1 
ATOM   9595  O  O   . GLY I  1 90  ? 41.279  12.822  -6.176  1.00 27.40 ? 90   GLY I O   1 
ATOM   9596  N  N   . LYS I  1 91  ? 43.359  13.352  -6.878  1.00 29.99 ? 91   LYS I N   1 
ATOM   9597  C  CA  . LYS I  1 91  ? 43.200  14.803  -6.708  1.00 31.36 ? 91   LYS I CA  1 
ATOM   9598  C  C   . LYS I  1 91  ? 42.160  15.244  -7.710  1.00 30.88 ? 91   LYS I C   1 
ATOM   9599  O  O   . LYS I  1 91  ? 41.711  16.388  -7.740  1.00 31.18 ? 91   LYS I O   1 
ATOM   9600  C  CB  . LYS I  1 91  ? 44.506  15.528  -7.009  1.00 31.93 ? 91   LYS I CB  1 
ATOM   9601  C  CG  . LYS I  1 91  ? 45.700  14.987  -6.284  1.00 33.20 ? 91   LYS I CG  1 
ATOM   9602  C  CD  . LYS I  1 91  ? 46.966  15.667  -6.775  1.00 37.42 ? 91   LYS I CD  1 
ATOM   9603  C  CE  . LYS I  1 91  ? 48.156  15.312  -5.899  1.00 40.39 ? 91   LYS I CE  1 
ATOM   9604  N  NZ  . LYS I  1 91  ? 47.851  15.570  -4.460  1.00 31.72 ? 91   LYS I NZ  1 
ATOM   9605  N  N   . ASP I  1 92  ? 41.842  14.281  -8.559  1.00 34.28 ? 92   ASP I N   1 
ATOM   9606  C  CA  . ASP I  1 92  ? 40.790  14.301  -9.553  1.00 33.47 ? 92   ASP I CA  1 
ATOM   9607  C  C   . ASP I  1 92  ? 39.404  14.430  -8.910  1.00 29.58 ? 92   ASP I C   1 
ATOM   9608  O  O   . ASP I  1 92  ? 38.489  15.012  -9.477  1.00 29.25 ? 92   ASP I O   1 
ATOM   9609  C  CB  . ASP I  1 92  ? 40.866  12.936  -10.252 1.00 30.10 ? 92   ASP I CB  1 
ATOM   9610  C  CG  . ASP I  1 92  ? 40.556  13.010  -11.708 1.00 36.31 ? 92   ASP I CG  1 
ATOM   9611  O  OD1 . ASP I  1 92  ? 39.986  14.034  -12.139 1.00 45.65 ? 92   ASP I OD1 1 
ATOM   9612  O  OD2 . ASP I  1 92  ? 40.882  12.042  -12.423 1.00 38.25 ? 92   ASP I OD2 1 
ATOM   9613  N  N   . GLY I  1 93  ? 39.260  13.848  -7.726  1.00 29.26 ? 93   GLY I N   1 
ATOM   9614  C  CA  . GLY I  1 93  ? 37.956  13.581  -7.152  1.00 26.64 ? 93   GLY I CA  1 
ATOM   9615  C  C   . GLY I  1 93  ? 37.344  12.320  -7.753  1.00 27.09 ? 93   GLY I C   1 
ATOM   9616  O  O   . GLY I  1 93  ? 36.215  11.958  -7.433  1.00 27.37 ? 93   GLY I O   1 
ATOM   9617  N  N   . VAL I  1 94  ? 38.087  11.648  -8.628  1.00 27.41 ? 94   VAL I N   1 
ATOM   9618  C  CA  . VAL I  1 94  ? 37.596  10.442  -9.281  1.00 27.04 ? 94   VAL I CA  1 
ATOM   9619  C  C   . VAL I  1 94  ? 38.265  9.154   -8.781  1.00 26.64 ? 94   VAL I C   1 
ATOM   9620  O  O   . VAL I  1 94  ? 39.483  8.995   -8.887  1.00 27.08 ? 94   VAL I O   1 
ATOM   9621  C  CB  . VAL I  1 94  ? 37.754  10.526  -10.816 1.00 26.34 ? 94   VAL I CB  1 
ATOM   9622  C  CG1 . VAL I  1 94  ? 37.275  9.239   -11.472 1.00 24.08 ? 94   VAL I CG1 1 
ATOM   9623  C  CG2 . VAL I  1 94  ? 36.991  11.726  -11.365 1.00 25.55 ? 94   VAL I CG2 1 
ATOM   9624  N  N   . ALA I  1 95  ? 37.456  8.245   -8.236  1.00 25.94 ? 95   ALA I N   1 
ATOM   9625  C  CA  . ALA I  1 95  ? 37.884  6.870   -7.965  1.00 22.66 ? 95   ALA I CA  1 
ATOM   9626  C  C   . ALA I  1 95  ? 37.670  5.997   -9.198  1.00 25.27 ? 95   ALA I C   1 
ATOM   9627  O  O   . ALA I  1 95  ? 36.541  5.745   -9.593  1.00 26.39 ? 95   ALA I O   1 
ATOM   9628  C  CB  . ALA I  1 95  ? 37.110  6.299   -6.798  1.00 19.54 ? 95   ALA I CB  1 
ATOM   9629  N  N   . ASN I  1 96  ? 38.749  5.539   -9.820  1.00 27.82 ? 96   ASN I N   1 
ATOM   9630  C  CA  . ASN I  1 96  ? 38.618  4.533   -10.864 1.00 25.01 ? 96   ASN I CA  1 
ATOM   9631  C  C   . ASN I  1 96  ? 38.682  3.154   -10.239 1.00 24.33 ? 96   ASN I C   1 
ATOM   9632  O  O   . ASN I  1 96  ? 39.751  2.623   -9.983  1.00 26.27 ? 96   ASN I O   1 
ATOM   9633  C  CB  . ASN I  1 96  ? 39.713  4.687   -11.907 1.00 29.96 ? 96   ASN I CB  1 
ATOM   9634  C  CG  . ASN I  1 96  ? 39.620  6.001   -12.645 1.00 34.14 ? 96   ASN I CG  1 
ATOM   9635  O  OD1 . ASN I  1 96  ? 38.806  6.158   -13.563 1.00 31.44 ? 96   ASN I OD1 1 
ATOM   9636  N  ND2 . ASN I  1 96  ? 40.461  6.959   -12.250 1.00 34.47 ? 96   ASN I ND2 1 
ATOM   9637  N  N   . VAL I  1 97  ? 37.512  2.585   -10.012 1.00 22.99 ? 97   VAL I N   1 
ATOM   9638  C  CA  . VAL I  1 97  ? 37.349  1.380   -9.225  1.00 20.59 ? 97   VAL I CA  1 
ATOM   9639  C  C   . VAL I  1 97  ? 37.745  0.134   -10.005 1.00 21.00 ? 97   VAL I C   1 
ATOM   9640  O  O   . VAL I  1 97  ? 37.328  -0.049  -11.138 1.00 25.17 ? 97   VAL I O   1 
ATOM   9641  C  CB  . VAL I  1 97  ? 35.870  1.265   -8.781  1.00 20.07 ? 97   VAL I CB  1 
ATOM   9642  C  CG1 . VAL I  1 97  ? 35.627  -0.013  -8.009  1.00 21.44 ? 97   VAL I CG1 1 
ATOM   9643  C  CG2 . VAL I  1 97  ? 35.462  2.485   -7.964  1.00 18.26 ? 97   VAL I CG2 1 
ATOM   9644  N  N   . SER I  1 98  ? 38.550  -0.726  -9.398  1.00 22.05 ? 98   SER I N   1 
ATOM   9645  C  CA  . SER I  1 98  ? 38.863  -2.023  -9.993  1.00 23.08 ? 98   SER I CA  1 
ATOM   9646  C  C   . SER I  1 98  ? 39.139  -3.053  -8.908  1.00 24.35 ? 98   SER I C   1 
ATOM   9647  O  O   . SER I  1 98  ? 40.244  -3.110  -8.348  1.00 26.27 ? 98   SER I O   1 
ATOM   9648  C  CB  . SER I  1 98  ? 40.048  -1.925  -10.956 1.00 21.64 ? 98   SER I CB  1 
ATOM   9649  O  OG  . SER I  1 98  ? 40.388  -3.206  -11.463 1.00 23.86 ? 98   SER I OG  1 
ATOM   9650  N  N   . ILE I  1 99  ? 38.120  -3.847  -8.593  1.00 22.89 ? 99   ILE I N   1 
ATOM   9651  C  CA  . ILE I  1 99  ? 38.210  -4.855  -7.539  1.00 24.87 ? 99   ILE I CA  1 
ATOM   9652  C  C   . ILE I  1 99  ? 37.896  -6.220  -8.147  1.00 27.69 ? 99   ILE I C   1 
ATOM   9653  O  O   . ILE I  1 99  ? 37.267  -6.299  -9.208  1.00 27.75 ? 99   ILE I O   1 
ATOM   9654  C  CB  . ILE I  1 99  ? 37.223  -4.552  -6.377  1.00 23.98 ? 99   ILE I CB  1 
ATOM   9655  C  CG1 . ILE I  1 99  ? 37.632  -3.279  -5.634  1.00 21.74 ? 99   ILE I CG1 1 
ATOM   9656  C  CG2 . ILE I  1 99  ? 37.142  -5.718  -5.401  1.00 22.29 ? 99   ILE I CG2 1 
ATOM   9657  C  CD1 . ILE I  1 99  ? 36.507  -2.626  -4.883  1.00 16.73 ? 99   ILE I CD1 1 
ATOM   9658  N  N   . GLU I  1 100 ? 38.359  -7.286  -7.500  1.00 25.86 ? 100  GLU I N   1 
ATOM   9659  C  CA  . GLU I  1 100 ? 37.982  -8.639  -7.890  1.00 27.90 ? 100  GLU I CA  1 
ATOM   9660  C  C   . GLU I  1 100 ? 37.719  -9.428  -6.614  1.00 27.07 ? 100  GLU I C   1 
ATOM   9661  O  O   . GLU I  1 100 ? 38.571  -9.443  -5.736  1.00 27.47 ? 100  GLU I O   1 
ATOM   9662  C  CB  . GLU I  1 100 ? 39.091  -9.288  -8.719  1.00 31.94 ? 100  GLU I CB  1 
ATOM   9663  C  CG  . GLU I  1 100 ? 38.715  -10.621 -9.354  1.00 36.68 ? 100  GLU I CG  1 
ATOM   9664  C  CD  . GLU I  1 100 ? 39.776  -11.116 -10.326 1.00 49.46 ? 100  GLU I CD  1 
ATOM   9665  O  OE1 . GLU I  1 100 ? 40.299  -10.287 -11.109 1.00 52.02 ? 100  GLU I OE1 1 
ATOM   9666  O  OE2 . GLU I  1 100 ? 40.083  -12.330 -10.307 1.00 49.68 ? 100  GLU I OE2 1 
ATOM   9667  N  N   . ASP I  1 101 ? 36.547  -10.062 -6.505  1.00 25.86 ? 101  ASP I N   1 
ATOM   9668  C  CA  . ASP I  1 101 ? 36.130  -10.710 -5.260  1.00 27.48 ? 101  ASP I CA  1 
ATOM   9669  C  C   . ASP I  1 101 ? 35.561  -12.117 -5.484  1.00 28.13 ? 101  ASP I C   1 
ATOM   9670  O  O   . ASP I  1 101 ? 34.885  -12.359 -6.479  1.00 30.35 ? 101  ASP I O   1 
ATOM   9671  C  CB  . ASP I  1 101 ? 35.103  -9.832  -4.527  1.00 23.72 ? 101  ASP I CB  1 
ATOM   9672  C  CG  . ASP I  1 101 ? 35.107  -10.054 -3.017  1.00 27.03 ? 101  ASP I CG  1 
ATOM   9673  O  OD1 . ASP I  1 101 ? 36.124  -9.725  -2.361  1.00 27.21 ? 101  ASP I OD1 1 
ATOM   9674  O  OD2 . ASP I  1 101 ? 34.095  -10.557 -2.478  1.00 27.37 ? 101  ASP I OD2 1 
ATOM   9675  N  N   . ARG I  1 102 ? 35.825  -13.037 -4.557  1.00 28.88 ? 102  ARG I N   1 
ATOM   9676  C  CA  . ARG I  1 102 ? 35.346  -14.422 -4.678  1.00 30.49 ? 102  ARG I CA  1 
ATOM   9677  C  C   . ARG I  1 102 ? 34.194  -14.721 -3.728  1.00 29.31 ? 102  ARG I C   1 
ATOM   9678  O  O   . ARG I  1 102 ? 33.547  -15.769 -3.830  1.00 29.03 ? 102  ARG I O   1 
ATOM   9679  C  CB  . ARG I  1 102 ? 36.486  -15.414 -4.435  1.00 34.98 ? 102  ARG I CB  1 
ATOM   9680  C  CG  . ARG I  1 102 ? 37.611  -15.275 -5.446  1.00 44.48 ? 102  ARG I CG  1 
ATOM   9681  C  CD  . ARG I  1 102 ? 38.673  -16.368 -5.324  1.00 54.85 ? 102  ARG I CD  1 
ATOM   9682  N  NE  . ARG I  1 102 ? 39.720  -16.204 -6.339  1.00 58.25 ? 102  ARG I NE  1 
ATOM   9683  C  CZ  . ARG I  1 102 ? 39.754  -16.857 -7.504  1.00 62.33 ? 102  ARG I CZ  1 
ATOM   9684  N  NH1 . ARG I  1 102 ? 38.802  -17.739 -7.809  1.00 54.80 ? 102  ARG I NH1 1 
ATOM   9685  N  NH2 . ARG I  1 102 ? 40.745  -16.635 -8.366  1.00 60.03 ? 102  ARG I NH2 1 
ATOM   9686  N  N   . VAL I  1 103 ? 33.946  -13.786 -2.813  1.00 28.56 ? 103  VAL I N   1 
ATOM   9687  C  CA  . VAL I  1 103 ? 32.942  -13.947 -1.770  1.00 28.46 ? 103  VAL I CA  1 
ATOM   9688  C  C   . VAL I  1 103 ? 31.562  -13.465 -2.241  1.00 30.63 ? 103  VAL I C   1 
ATOM   9689  O  O   . VAL I  1 103 ? 30.553  -14.161 -2.061  1.00 26.73 ? 103  VAL I O   1 
ATOM   9690  C  CB  . VAL I  1 103 ? 33.394  -13.231 -0.480  1.00 27.32 ? 103  VAL I CB  1 
ATOM   9691  C  CG1 . VAL I  1 103 ? 32.343  -13.341 0.611   1.00 26.66 ? 103  VAL I CG1 1 
ATOM   9692  C  CG2 . VAL I  1 103 ? 34.714  -13.814 -0.011  1.00 26.66 ? 103  VAL I CG2 1 
ATOM   9693  N  N   . ILE I  1 104 ? 31.521  -12.279 -2.850  1.00 28.00 ? 104  ILE I N   1 
ATOM   9694  C  CA  . ILE I  1 104 ? 30.313  -11.827 -3.524  1.00 25.81 ? 104  ILE I CA  1 
ATOM   9695  C  C   . ILE I  1 104 ? 30.069  -12.672 -4.777  1.00 26.43 ? 104  ILE I C   1 
ATOM   9696  O  O   . ILE I  1 104 ? 30.978  -13.310 -5.292  1.00 25.99 ? 104  ILE I O   1 
ATOM   9697  C  CB  . ILE I  1 104 ? 30.353  -10.321 -3.927  1.00 24.23 ? 104  ILE I CB  1 
ATOM   9698  C  CG1 . ILE I  1 104 ? 31.520  -10.036 -4.875  1.00 21.61 ? 104  ILE I CG1 1 
ATOM   9699  C  CG2 . ILE I  1 104 ? 30.333  -9.412  -2.695  1.00 22.02 ? 104  ILE I CG2 1 
ATOM   9700  C  CD1 . ILE I  1 104 ? 31.407  -8.696  -5.596  1.00 22.46 ? 104  ILE I CD1 1 
ATOM   9701  N  N   . SER I  1 105 ? 28.828  -12.659 -5.257  1.00 28.34 ? 105  SER I N   1 
ATOM   9702  C  CA  . SER I  1 105 ? 28.440  -13.399 -6.452  1.00 29.17 ? 105  SER I CA  1 
ATOM   9703  C  C   . SER I  1 105 ? 27.264  -12.704 -7.172  1.00 26.28 ? 105  SER I C   1 
ATOM   9704  O  O   . SER I  1 105 ? 26.568  -11.878 -6.588  1.00 26.68 ? 105  SER I O   1 
ATOM   9705  C  CB  . SER I  1 105 ? 28.110  -14.854 -6.086  1.00 28.84 ? 105  SER I CB  1 
ATOM   9706  O  OG  . SER I  1 105 ? 27.775  -15.622 -7.230  1.00 28.91 ? 105  SER I OG  1 
ATOM   9707  N  N   . LEU I  1 106 ? 27.067  -13.024 -8.445  1.00 26.75 ? 106  LEU I N   1 
ATOM   9708  C  CA  . LEU I  1 106 ? 25.988  -12.456 -9.244  1.00 23.61 ? 106  LEU I CA  1 
ATOM   9709  C  C   . LEU I  1 106 ? 24.878  -13.490 -9.453  1.00 27.69 ? 106  LEU I C   1 
ATOM   9710  O  O   . LEU I  1 106 ? 24.009  -13.329 -10.316 1.00 30.76 ? 106  LEU I O   1 
ATOM   9711  C  CB  . LEU I  1 106 ? 26.530  -11.998 -10.604 1.00 25.96 ? 106  LEU I CB  1 
ATOM   9712  C  CG  . LEU I  1 106 ? 27.443  -10.770 -10.691 1.00 23.47 ? 106  LEU I CG  1 
ATOM   9713  C  CD1 . LEU I  1 106 ? 27.570  -10.316 -12.126 1.00 24.53 ? 106  LEU I CD1 1 
ATOM   9714  C  CD2 . LEU I  1 106 ? 26.898  -9.639  -9.832  1.00 22.72 ? 106  LEU I CD2 1 
ATOM   9715  N  N   . SER I  1 107 ? 24.930  -14.564 -8.675  1.00 29.28 ? 107  SER I N   1 
ATOM   9716  C  CA  . SER I  1 107 ? 23.927  -15.619 -8.724  1.00 30.89 ? 107  SER I CA  1 
ATOM   9717  C  C   . SER I  1 107 ? 24.066  -16.476 -7.479  1.00 31.00 ? 107  SER I C   1 
ATOM   9718  O  O   . SER I  1 107 ? 25.125  -16.501 -6.864  1.00 33.56 ? 107  SER I O   1 
ATOM   9719  C  CB  . SER I  1 107 ? 24.082  -16.476 -9.990  1.00 31.56 ? 107  SER I CB  1 
ATOM   9720  O  OG  . SER I  1 107 ? 25.183  -17.368 -9.904  1.00 33.36 ? 107  SER I OG  1 
ATOM   9721  N  N   . GLY I  1 108 ? 22.999  -17.171 -7.102  1.00 33.72 ? 108  GLY I N   1 
ATOM   9722  C  CA  . GLY I  1 108 ? 23.009  -17.992 -5.902  1.00 36.08 ? 108  GLY I CA  1 
ATOM   9723  C  C   . GLY I  1 108 ? 22.600  -17.216 -4.664  1.00 42.10 ? 108  GLY I C   1 
ATOM   9724  O  O   . GLY I  1 108 ? 21.830  -16.266 -4.764  1.00 41.76 ? 108  GLY I O   1 
ATOM   9725  N  N   . GLU I  1 109 ? 23.140  -17.606 -3.507  1.00 47.84 ? 109  GLU I N   1 
ATOM   9726  C  CA  . GLU I  1 109 ? 22.739  -17.066 -2.198  1.00 44.76 ? 109  GLU I CA  1 
ATOM   9727  C  C   . GLU I  1 109 ? 23.614  -15.895 -1.751  1.00 43.47 ? 109  GLU I C   1 
ATOM   9728  O  O   . GLU I  1 109 ? 23.269  -15.165 -0.818  1.00 41.59 ? 109  GLU I O   1 
ATOM   9729  C  CB  . GLU I  1 109 ? 22.788  -18.160 -1.124  1.00 46.52 ? 109  GLU I CB  1 
ATOM   9730  C  CG  . GLU I  1 109 ? 22.357  -19.549 -1.587  1.00 52.47 ? 109  GLU I CG  1 
ATOM   9731  C  CD  . GLU I  1 109 ? 23.537  -20.453 -1.968  1.00 61.10 ? 109  GLU I CD  1 
ATOM   9732  O  OE1 . GLU I  1 109 ? 24.444  -20.017 -2.727  1.00 54.14 ? 109  GLU I OE1 1 
ATOM   9733  O  OE2 . GLU I  1 109 ? 23.542  -21.619 -1.511  1.00 68.31 ? 109  GLU I OE2 1 
ATOM   9734  N  N   . HIS I  1 110 ? 24.765  -15.749 -2.395  1.00 43.09 ? 110  HIS I N   1 
ATOM   9735  C  CA  . HIS I  1 110 ? 25.638  -14.606 -2.153  1.00 41.39 ? 110  HIS I CA  1 
ATOM   9736  C  C   . HIS I  1 110 ? 25.417  -13.585 -3.268  1.00 36.23 ? 110  HIS I C   1 
ATOM   9737  O  O   . HIS I  1 110 ? 26.255  -12.688 -3.480  1.00 31.39 ? 110  HIS I O   1 
ATOM   9738  C  CB  . HIS I  1 110 ? 27.114  -15.042 -2.097  1.00 38.61 ? 110  HIS I CB  1 
ATOM   9739  C  CG  . HIS I  1 110 ? 27.544  -15.585 -0.765  1.00 40.21 ? 110  HIS I CG  1 
ATOM   9740  N  ND1 . HIS I  1 110 ? 28.860  -15.568 -0.344  1.00 40.11 ? 110  HIS I ND1 1 
ATOM   9741  C  CD2 . HIS I  1 110 ? 26.836  -16.150 0.244   1.00 38.81 ? 110  HIS I CD2 1 
ATOM   9742  C  CE1 . HIS I  1 110 ? 28.944  -16.107 0.861   1.00 34.34 ? 110  HIS I CE1 1 
ATOM   9743  N  NE2 . HIS I  1 110 ? 27.730  -16.466 1.240   1.00 37.90 ? 110  HIS I NE2 1 
ATOM   9744  N  N   . SER I  1 111 ? 24.285  -13.738 -3.969  1.00 32.41 ? 111  SER I N   1 
ATOM   9745  C  CA  . SER I  1 111 ? 23.934  -12.889 -5.108  1.00 29.21 ? 111  SER I CA  1 
ATOM   9746  C  C   . SER I  1 111 ? 23.665  -11.467 -4.656  1.00 25.24 ? 111  SER I C   1 
ATOM   9747  O  O   . SER I  1 111 ? 22.853  -11.238 -3.762  1.00 25.92 ? 111  SER I O   1 
ATOM   9748  C  CB  . SER I  1 111 ? 22.699  -13.426 -5.843  1.00 30.76 ? 111  SER I CB  1 
ATOM   9749  O  OG  . SER I  1 111 ? 22.388  -12.635 -6.981  1.00 27.23 ? 111  SER I OG  1 
ATOM   9750  N  N   . ILE I  1 112 ? 24.344  -10.511 -5.275  1.00 24.09 ? 112  ILE I N   1 
ATOM   9751  C  CA  . ILE I  1 112 ? 24.174  -9.120  -4.893  1.00 22.03 ? 112  ILE I CA  1 
ATOM   9752  C  C   . ILE I  1 112 ? 23.229  -8.384  -5.841  1.00 21.79 ? 112  ILE I C   1 
ATOM   9753  O  O   . ILE I  1 112 ? 22.936  -7.202  -5.642  1.00 18.97 ? 112  ILE I O   1 
ATOM   9754  C  CB  . ILE I  1 112 ? 25.530  -8.394  -4.780  1.00 22.32 ? 112  ILE I CB  1 
ATOM   9755  C  CG1 . ILE I  1 112 ? 26.265  -8.417  -6.115  1.00 17.89 ? 112  ILE I CG1 1 
ATOM   9756  C  CG2 . ILE I  1 112 ? 26.375  -9.038  -3.682  1.00 22.35 ? 112  ILE I CG2 1 
ATOM   9757  C  CD1 . ILE I  1 112 ? 27.452  -7.522  -6.147  1.00 19.40 ? 112  ILE I CD1 1 
ATOM   9758  N  N   . ILE I  1 113 ? 22.752  -9.095  -6.864  1.00 22.64 ? 113  ILE I N   1 
ATOM   9759  C  CA  . ILE I  1 113 ? 21.766  -8.545  -7.778  1.00 22.52 ? 113  ILE I CA  1 
ATOM   9760  C  C   . ILE I  1 113 ? 20.539  -8.173  -6.948  1.00 22.84 ? 113  ILE I C   1 
ATOM   9761  O  O   . ILE I  1 113 ? 20.048  -8.988  -6.167  1.00 22.49 ? 113  ILE I O   1 
ATOM   9762  C  CB  . ILE I  1 113 ? 21.377  -9.563  -8.870  1.00 23.80 ? 113  ILE I CB  1 
ATOM   9763  C  CG1 . ILE I  1 113 ? 22.618  -10.039 -9.629  1.00 23.32 ? 113  ILE I CG1 1 
ATOM   9764  C  CG2 . ILE I  1 113 ? 20.366  -8.960  -9.827  1.00 23.18 ? 113  ILE I CG2 1 
ATOM   9765  C  CD1 . ILE I  1 113 ? 22.728  -9.504  -11.034 1.00 23.60 ? 113  ILE I CD1 1 
ATOM   9766  N  N   . GLY I  1 114 ? 20.066  -6.934  -7.085  1.00 21.24 ? 114  GLY I N   1 
ATOM   9767  C  CA  . GLY I  1 114 ? 18.911  -6.475  -6.332  1.00 19.48 ? 114  GLY I CA  1 
ATOM   9768  C  C   . GLY I  1 114 ? 19.260  -5.870  -4.983  1.00 20.93 ? 114  GLY I C   1 
ATOM   9769  O  O   . GLY I  1 114 ? 18.364  -5.507  -4.214  1.00 19.33 ? 114  GLY I O   1 
ATOM   9770  N  N   . ARG I  1 115 ? 20.560  -5.774  -4.686  1.00 19.29 ? 115  ARG I N   1 
ATOM   9771  C  CA  . ARG I  1 115 ? 21.026  -5.145  -3.445  1.00 19.62 ? 115  ARG I CA  1 
ATOM   9772  C  C   . ARG I  1 115 ? 21.655  -3.791  -3.771  1.00 17.31 ? 115  ARG I C   1 
ATOM   9773  O  O   . ARG I  1 115 ? 21.479  -3.301  -4.872  1.00 18.93 ? 115  ARG I O   1 
ATOM   9774  C  CB  . ARG I  1 115 ? 21.953  -6.083  -2.662  1.00 18.03 ? 115  ARG I CB  1 
ATOM   9775  C  CG  . ARG I  1 115 ? 21.301  -7.456  -2.466  1.00 19.58 ? 115  ARG I CG  1 
ATOM   9776  C  CD  . ARG I  1 115 ? 22.028  -8.354  -1.498  1.00 21.80 ? 115  ARG I CD  1 
ATOM   9777  N  NE  . ARG I  1 115 ? 21.379  -9.668  -1.410  1.00 25.75 ? 115  ARG I NE  1 
ATOM   9778  C  CZ  . ARG I  1 115 ? 20.420  -9.990  -0.534  1.00 27.31 ? 115  ARG I CZ  1 
ATOM   9779  N  NH1 . ARG I  1 115 ? 19.954  -9.102  0.349   1.00 22.55 ? 115  ARG I NH1 1 
ATOM   9780  N  NH2 . ARG I  1 115 ? 19.916  -11.215 -0.540  1.00 28.77 ? 115  ARG I NH2 1 
ATOM   9781  N  N   . THR I  1 116 ? 22.360  -3.176  -2.829  1.00 18.43 ? 116  THR I N   1 
ATOM   9782  C  CA  . THR I  1 116 ? 22.832  -1.805  -3.032  1.00 19.61 ? 116  THR I CA  1 
ATOM   9783  C  C   . THR I  1 116 ? 24.356  -1.669  -2.886  1.00 18.71 ? 116  THR I C   1 
ATOM   9784  O  O   . THR I  1 116 ? 24.931  -2.133  -1.915  1.00 22.26 ? 116  THR I O   1 
ATOM   9785  C  CB  . THR I  1 116 ? 22.074  -0.817  -2.084  1.00 18.20 ? 116  THR I CB  1 
ATOM   9786  O  OG1 . THR I  1 116 ? 20.667  -0.938  -2.307  1.00 18.45 ? 116  THR I OG1 1 
ATOM   9787  C  CG2 . THR I  1 116 ? 22.478  0.636   -2.318  1.00 15.75 ? 116  THR I CG2 1 
ATOM   9788  N  N   . MET I  1 117 ? 25.000  -1.070  -3.881  1.00 18.92 ? 117  MET I N   1 
ATOM   9789  C  CA  . MET I  1 117 ? 26.375  -0.604  -3.749  1.00 19.22 ? 117  MET I CA  1 
ATOM   9790  C  C   . MET I  1 117 ? 26.308  0.760   -3.090  1.00 19.49 ? 117  MET I C   1 
ATOM   9791  O  O   . MET I  1 117 ? 25.550  1.625   -3.526  1.00 18.17 ? 117  MET I O   1 
ATOM   9792  C  CB  . MET I  1 117 ? 27.029  -0.396  -5.122  1.00 22.75 ? 117  MET I CB  1 
ATOM   9793  C  CG  . MET I  1 117 ? 27.789  -1.578  -5.735  1.00 25.25 ? 117  MET I CG  1 
ATOM   9794  S  SD  . MET I  1 117 ? 28.919  -2.490  -4.665  1.00 24.30 ? 117  MET I SD  1 
ATOM   9795  C  CE  . MET I  1 117 ? 29.814  -1.174  -3.879  1.00 20.64 ? 117  MET I CE  1 
ATOM   9796  N  N   . VAL I  1 118 ? 27.090  0.972   -2.047  1.00 18.86 ? 118  VAL I N   1 
ATOM   9797  C  CA  . VAL I  1 118 ? 27.221  2.332   -1.530  1.00 23.26 ? 118  VAL I CA  1 
ATOM   9798  C  C   . VAL I  1 118 ? 28.669  2.733   -1.283  1.00 21.50 ? 118  VAL I C   1 
ATOM   9799  O  O   . VAL I  1 118 ? 29.478  1.930   -0.799  1.00 21.17 ? 118  VAL I O   1 
ATOM   9800  C  CB  . VAL I  1 118 ? 26.274  2.654   -0.317  1.00 21.13 ? 118  VAL I CB  1 
ATOM   9801  C  CG1 . VAL I  1 118 ? 25.541  1.420   0.161   1.00 19.52 ? 118  VAL I CG1 1 
ATOM   9802  C  CG2 . VAL I  1 118 ? 27.014  3.356   0.787   1.00 19.85 ? 118  VAL I CG2 1 
ATOM   9803  N  N   . VAL I  1 119 ? 28.988  3.963   -1.683  1.00 20.27 ? 119  VAL I N   1 
ATOM   9804  C  CA  . VAL I  1 119 ? 30.300  4.543   -1.446  1.00 20.79 ? 119  VAL I CA  1 
ATOM   9805  C  C   . VAL I  1 119 ? 30.153  5.479   -0.268  1.00 22.21 ? 119  VAL I C   1 
ATOM   9806  O  O   . VAL I  1 119 ? 29.184  6.246   -0.192  1.00 20.14 ? 119  VAL I O   1 
ATOM   9807  C  CB  . VAL I  1 119 ? 30.867  5.289   -2.679  1.00 22.10 ? 119  VAL I CB  1 
ATOM   9808  C  CG1 . VAL I  1 119 ? 29.993  6.474   -3.037  1.00 21.90 ? 119  VAL I CG1 1 
ATOM   9809  C  CG2 . VAL I  1 119 ? 32.327  5.724   -2.433  1.00 17.93 ? 119  VAL I CG2 1 
ATOM   9810  N  N   . HIS I  1 120 ? 31.118  5.396   0.646   1.00 20.31 ? 120  HIS I N   1 
ATOM   9811  C  CA  . HIS I  1 120 ? 30.998  5.998   1.955   1.00 20.32 ? 120  HIS I CA  1 
ATOM   9812  C  C   . HIS I  1 120 ? 31.868  7.247   2.101   1.00 22.78 ? 120  HIS I C   1 
ATOM   9813  O  O   . HIS I  1 120 ? 32.695  7.550   1.244   1.00 23.46 ? 120  HIS I O   1 
ATOM   9814  C  CB  . HIS I  1 120 ? 31.315  4.966   3.049   1.00 21.58 ? 120  HIS I CB  1 
ATOM   9815  C  CG  . HIS I  1 120 ? 30.205  3.991   3.312   1.00 22.38 ? 120  HIS I CG  1 
ATOM   9816  N  ND1 . HIS I  1 120 ? 29.238  4.200   4.277   1.00 21.29 ? 120  HIS I ND1 1 
ATOM   9817  C  CD2 . HIS I  1 120 ? 29.911  2.793   2.751   1.00 21.58 ? 120  HIS I CD2 1 
ATOM   9818  C  CE1 . HIS I  1 120 ? 28.406  3.176   4.296   1.00 21.13 ? 120  HIS I CE1 1 
ATOM   9819  N  NE2 . HIS I  1 120 ? 28.788  2.309   3.375   1.00 18.98 ? 120  HIS I NE2 1 
ATOM   9820  N  N   . GLU I  1 121 ? 31.659  7.957   3.204   1.00 22.94 ? 121  GLU I N   1 
ATOM   9821  C  CA  . GLU I  1 121 ? 32.249  9.271   3.461   1.00 25.31 ? 121  GLU I CA  1 
ATOM   9822  C  C   . GLU I  1 121 ? 33.750  9.196   3.780   1.00 25.13 ? 121  GLU I C   1 
ATOM   9823  O  O   . GLU I  1 121 ? 34.564  9.889   3.167   1.00 23.74 ? 121  GLU I O   1 
ATOM   9824  C  CB  . GLU I  1 121 ? 31.463  9.936   4.608   1.00 23.71 ? 121  GLU I CB  1 
ATOM   9825  C  CG  . GLU I  1 121 ? 32.062  11.185  5.229   1.00 24.17 ? 121  GLU I CG  1 
ATOM   9826  C  CD  . GLU I  1 121 ? 31.434  11.485  6.597   1.00 27.86 ? 121  GLU I CD  1 
ATOM   9827  O  OE1 . GLU I  1 121 ? 30.975  10.520  7.263   1.00 24.55 ? 121  GLU I OE1 1 
ATOM   9828  O  OE2 . GLU I  1 121 ? 31.388  12.677  6.997   1.00 27.34 ? 121  GLU I OE2 1 
ATOM   9829  N  N   . LYS I  1 122 ? 34.095  8.353   4.751   1.00 24.83 ? 122  LYS I N   1 
ATOM   9830  C  CA  . LYS I  1 122 ? 35.468  8.203   5.194   1.00 21.87 ? 122  LYS I CA  1 
ATOM   9831  C  C   . LYS I  1 122 ? 36.002  6.827   4.843   1.00 20.31 ? 122  LYS I C   1 
ATOM   9832  O  O   . LYS I  1 122 ? 35.300  5.951   4.333   1.00 21.56 ? 122  LYS I O   1 
ATOM   9833  C  CB  . LYS I  1 122 ? 35.606  8.362   6.724   1.00 23.64 ? 122  LYS I CB  1 
ATOM   9834  C  CG  . LYS I  1 122 ? 34.513  9.112   7.467   1.00 24.95 ? 122  LYS I CG  1 
ATOM   9835  C  CD  . LYS I  1 122 ? 34.424  8.652   8.938   1.00 24.92 ? 122  LYS I CD  1 
ATOM   9836  C  CE  . LYS I  1 122 ? 34.991  9.681   9.906   1.00 35.63 ? 122  LYS I CE  1 
ATOM   9837  N  NZ  . LYS I  1 122 ? 34.214  10.970  9.926   1.00 35.72 ? 122  LYS I NZ  1 
ATOM   9838  N  N   . GLN I  1 123 ? 37.265  6.647   5.172   1.00 19.89 ? 123  GLN I N   1 
ATOM   9839  C  CA  . GLN I  1 123 ? 37.968  5.411   4.946   1.00 21.76 ? 123  GLN I CA  1 
ATOM   9840  C  C   . GLN I  1 123 ? 37.458  4.307   5.847   1.00 22.03 ? 123  GLN I C   1 
ATOM   9841  O  O   . GLN I  1 123 ? 37.318  4.487   7.068   1.00 22.97 ? 123  GLN I O   1 
ATOM   9842  C  CB  . GLN I  1 123 ? 39.461  5.610   5.217   1.00 21.94 ? 123  GLN I CB  1 
ATOM   9843  C  CG  . GLN I  1 123 ? 40.243  4.322   5.279   1.00 20.31 ? 123  GLN I CG  1 
ATOM   9844  C  CD  . GLN I  1 123 ? 41.701  4.558   5.545   1.00 22.03 ? 123  GLN I CD  1 
ATOM   9845  O  OE1 . GLN I  1 123 ? 42.175  5.694   5.510   1.00 22.41 ? 123  GLN I OE1 1 
ATOM   9846  N  NE2 . GLN I  1 123 ? 42.425  3.490   5.819   1.00 21.10 ? 123  GLN I NE2 1 
ATOM   9847  N  N   . ASP I  1 124 ? 37.205  3.163   5.221   1.00 18.72 ? 124  ASP I N   1 
ATOM   9848  C  CA  . ASP I  1 124 ? 36.891  1.919   5.899   1.00 19.82 ? 124  ASP I CA  1 
ATOM   9849  C  C   . ASP I  1 124 ? 38.117  1.435   6.722   1.00 21.00 ? 124  ASP I C   1 
ATOM   9850  O  O   . ASP I  1 124 ? 39.179  1.145   6.165   1.00 24.08 ? 124  ASP I O   1 
ATOM   9851  C  CB  . ASP I  1 124 ? 36.491  0.900   4.831   1.00 16.77 ? 124  ASP I CB  1 
ATOM   9852  C  CG  . ASP I  1 124 ? 36.006  -0.404  5.403   1.00 18.95 ? 124  ASP I CG  1 
ATOM   9853  O  OD1 . ASP I  1 124 ? 36.108  -0.613  6.623   1.00 21.77 ? 124  ASP I OD1 1 
ATOM   9854  O  OD2 . ASP I  1 124 ? 35.510  -1.239  4.624   1.00 21.42 ? 124  ASP I OD2 1 
ATOM   9855  N  N   . ASP I  1 125 ? 37.979  1.359   8.042   1.00 20.10 ? 125  ASP I N   1 
ATOM   9856  C  CA  . ASP I  1 125 ? 39.084  0.909   8.894   1.00 21.67 ? 125  ASP I CA  1 
ATOM   9857  C  C   . ASP I  1 125 ? 39.263  -0.619  8.939   1.00 23.87 ? 125  ASP I C   1 
ATOM   9858  O  O   . ASP I  1 125 ? 40.114  -1.126  9.668   1.00 26.67 ? 125  ASP I O   1 
ATOM   9859  C  CB  . ASP I  1 125 ? 38.999  1.520   10.313  1.00 21.60 ? 125  ASP I CB  1 
ATOM   9860  C  CG  . ASP I  1 125 ? 37.878  0.921   11.170  1.00 24.28 ? 125  ASP I CG  1 
ATOM   9861  O  OD1 . ASP I  1 125 ? 37.404  -0.203  10.879  1.00 22.80 ? 125  ASP I OD1 1 
ATOM   9862  O  OD2 . ASP I  1 125 ? 37.486  1.572   12.171  1.00 23.03 ? 125  ASP I OD2 1 
ATOM   9863  N  N   . LEU I  1 126 ? 38.465  -1.337  8.153   1.00 21.83 ? 126  LEU I N   1 
ATOM   9864  C  CA  . LEU I  1 126 ? 38.588  -2.796  7.983   1.00 22.52 ? 126  LEU I CA  1 
ATOM   9865  C  C   . LEU I  1 126 ? 38.411  -3.644  9.264   1.00 23.72 ? 126  LEU I C   1 
ATOM   9866  O  O   . LEU I  1 126 ? 38.917  -4.766  9.357   1.00 23.68 ? 126  LEU I O   1 
ATOM   9867  C  CB  . LEU I  1 126 ? 39.884  -3.169  7.237   1.00 22.06 ? 126  LEU I CB  1 
ATOM   9868  C  CG  . LEU I  1 126 ? 40.210  -2.460  5.904   1.00 21.11 ? 126  LEU I CG  1 
ATOM   9869  C  CD1 . LEU I  1 126 ? 41.468  -3.021  5.266   1.00 20.56 ? 126  LEU I CD1 1 
ATOM   9870  C  CD2 . LEU I  1 126 ? 39.061  -2.513  4.915   1.00 18.26 ? 126  LEU I CD2 1 
ATOM   9871  N  N   . GLY I  1 127 ? 37.676  -3.118  10.235  1.00 21.82 ? 127  GLY I N   1 
ATOM   9872  C  CA  . GLY I  1 127 ? 37.362  -3.879  11.428  1.00 23.55 ? 127  GLY I CA  1 
ATOM   9873  C  C   . GLY I  1 127 ? 38.329  -3.742  12.595  1.00 22.90 ? 127  GLY I C   1 
ATOM   9874  O  O   . GLY I  1 127 ? 38.227  -4.476  13.581  1.00 22.11 ? 127  GLY I O   1 
ATOM   9875  N  N   . LYS I  1 128 ? 39.263  -2.801  12.490  1.00 24.13 ? 128  LYS I N   1 
ATOM   9876  C  CA  . LYS I  1 128 ? 40.259  -2.593  13.540  1.00 25.49 ? 128  LYS I CA  1 
ATOM   9877  C  C   . LYS I  1 128 ? 40.332  -1.183  14.139  1.00 23.38 ? 128  LYS I C   1 
ATOM   9878  O  O   . LYS I  1 128 ? 41.416  -0.696  14.433  1.00 22.56 ? 128  LYS I O   1 
ATOM   9879  C  CB  . LYS I  1 128 ? 41.649  -3.011  13.054  1.00 26.75 ? 128  LYS I CB  1 
ATOM   9880  C  CG  . LYS I  1 128 ? 41.722  -3.467  11.612  1.00 24.50 ? 128  LYS I CG  1 
ATOM   9881  C  CD  . LYS I  1 128 ? 43.166  -3.702  11.212  1.00 29.61 ? 128  LYS I CD  1 
ATOM   9882  C  CE  . LYS I  1 128 ? 43.288  -4.740  10.098  1.00 36.17 ? 128  LYS I CE  1 
ATOM   9883  N  NZ  . LYS I  1 128 ? 43.184  -6.143  10.609  1.00 34.72 ? 128  LYS I NZ  1 
ATOM   9884  N  N   . GLY I  1 129 ? 39.184  -0.540  14.333  1.00 23.99 ? 129  GLY I N   1 
ATOM   9885  C  CA  . GLY I  1 129 ? 39.142  0.778   14.946  1.00 23.16 ? 129  GLY I CA  1 
ATOM   9886  C  C   . GLY I  1 129 ? 38.889  0.710   16.442  1.00 25.28 ? 129  GLY I C   1 
ATOM   9887  O  O   . GLY I  1 129 ? 38.716  1.742   17.094  1.00 26.15 ? 129  GLY I O   1 
ATOM   9888  N  N   . GLY I  1 130 ? 38.849  -0.508  16.983  1.00 23.19 ? 130  GLY I N   1 
ATOM   9889  C  CA  . GLY I  1 130 ? 38.745  -0.715  18.413  1.00 24.86 ? 130  GLY I CA  1 
ATOM   9890  C  C   . GLY I  1 130 ? 37.437  -0.275  19.055  1.00 28.00 ? 130  GLY I C   1 
ATOM   9891  O  O   . GLY I  1 130 ? 37.402  0.133   20.224  1.00 26.27 ? 130  GLY I O   1 
ATOM   9892  N  N   . ASN I  1 131 ? 36.356  -0.343  18.289  1.00 27.00 ? 131  ASN I N   1 
ATOM   9893  C  CA  . ASN I  1 131 ? 35.023  -0.145  18.840  1.00 26.10 ? 131  ASN I CA  1 
ATOM   9894  C  C   . ASN I  1 131 ? 33.991  -0.890  18.028  1.00 27.11 ? 131  ASN I C   1 
ATOM   9895  O  O   . ASN I  1 131 ? 34.308  -1.524  17.019  1.00 27.40 ? 131  ASN I O   1 
ATOM   9896  C  CB  . ASN I  1 131 ? 34.661  1.337   18.970  1.00 24.57 ? 131  ASN I CB  1 
ATOM   9897  C  CG  . ASN I  1 131 ? 34.643  2.049   17.649  1.00 24.94 ? 131  ASN I CG  1 
ATOM   9898  O  OD1 . ASN I  1 131 ? 34.611  1.413   16.597  1.00 24.47 ? 131  ASN I OD1 1 
ATOM   9899  N  ND2 . ASN I  1 131 ? 34.665  3.381   17.689  1.00 24.72 ? 131  ASN I ND2 1 
ATOM   9900  N  N   . GLU I  1 132 ? 32.753  -0.801  18.480  1.00 28.71 ? 132  GLU I N   1 
ATOM   9901  C  CA  . GLU I  1 132 ? 31.658  -1.551  17.892  1.00 29.21 ? 132  GLU I CA  1 
ATOM   9902  C  C   . GLU I  1 132 ? 31.348  -1.090  16.471  1.00 28.53 ? 132  GLU I C   1 
ATOM   9903  O  O   . GLU I  1 132 ? 31.125  -1.909  15.575  1.00 29.61 ? 132  GLU I O   1 
ATOM   9904  C  CB  . GLU I  1 132 ? 30.431  -1.384  18.768  1.00 33.00 ? 132  GLU I CB  1 
ATOM   9905  C  CG  . GLU I  1 132 ? 29.623  -2.640  18.942  1.00 39.42 ? 132  GLU I CG  1 
ATOM   9906  C  CD  . GLU I  1 132 ? 28.445  -2.406  19.857  1.00 51.11 ? 132  GLU I CD  1 
ATOM   9907  O  OE1 . GLU I  1 132 ? 27.429  -3.123  19.719  1.00 49.73 ? 132  GLU I OE1 1 
ATOM   9908  O  OE2 . GLU I  1 132 ? 28.541  -1.489  20.709  1.00 54.86 ? 132  GLU I OE2 1 
ATOM   9909  N  N   . GLU I  1 133 ? 31.311  0.226   16.280  1.00 28.15 ? 133  GLU I N   1 
ATOM   9910  C  CA  . GLU I  1 133 ? 31.206  0.810   14.954  1.00 26.76 ? 133  GLU I CA  1 
ATOM   9911  C  C   . GLU I  1 133 ? 32.074  0.036   13.989  1.00 24.57 ? 133  GLU I C   1 
ATOM   9912  O  O   . GLU I  1 133 ? 31.609  -0.422  12.953  1.00 26.77 ? 133  GLU I O   1 
ATOM   9913  C  CB  . GLU I  1 133 ? 31.695  2.262   14.973  1.00 29.26 ? 133  GLU I CB  1 
ATOM   9914  C  CG  . GLU I  1 133 ? 30.595  3.274   14.885  1.00 30.87 ? 133  GLU I CG  1 
ATOM   9915  C  CD  . GLU I  1 133 ? 29.577  2.886   13.846  1.00 34.76 ? 133  GLU I CD  1 
ATOM   9916  O  OE1 . GLU I  1 133 ? 29.962  2.790   12.663  1.00 34.83 ? 133  GLU I OE1 1 
ATOM   9917  O  OE2 . GLU I  1 133 ? 28.396  2.674   14.205  1.00 35.14 ? 133  GLU I OE2 1 
ATOM   9918  N  N   . SER I  1 134 ? 33.349  -0.081  14.343  1.00 22.74 ? 134  SER I N   1 
ATOM   9919  C  CA  . SER I  1 134 ? 34.356  -0.718  13.504  1.00 23.20 ? 134  SER I CA  1 
ATOM   9920  C  C   . SER I  1 134 ? 33.970  -2.141  13.085  1.00 23.18 ? 134  SER I C   1 
ATOM   9921  O  O   . SER I  1 134 ? 33.969  -2.470  11.900  1.00 24.62 ? 134  SER I O   1 
ATOM   9922  C  CB  . SER I  1 134 ? 35.710  -0.709  14.223  1.00 21.91 ? 134  SER I CB  1 
ATOM   9923  O  OG  . SER I  1 134 ? 36.712  -1.275  13.404  1.00 23.52 ? 134  SER I OG  1 
ATOM   9924  N  N   . THR I  1 135 ? 33.628  -2.975  14.062  1.00 28.06 ? 135  THR I N   1 
ATOM   9925  C  CA  . THR I  1 135 ? 33.251  -4.365  13.817  1.00 24.84 ? 135  THR I CA  1 
ATOM   9926  C  C   . THR I  1 135 ? 31.940  -4.475  13.047  1.00 26.68 ? 135  THR I C   1 
ATOM   9927  O  O   . THR I  1 135 ? 31.455  -5.577  12.813  1.00 28.33 ? 135  THR I O   1 
ATOM   9928  C  CB  . THR I  1 135 ? 33.098  -5.143  15.149  1.00 28.72 ? 135  THR I CB  1 
ATOM   9929  O  OG1 . THR I  1 135 ? 31.849  -4.799  15.770  1.00 31.12 ? 135  THR I OG1 1 
ATOM   9930  C  CG2 . THR I  1 135 ? 34.233  -4.813  16.100  1.00 25.18 ? 135  THR I CG2 1 
ATOM   9931  N  N   . LYS I  1 136 ? 31.388  -3.336  12.625  1.00 27.50 ? 136  LYS I N   1 
ATOM   9932  C  CA  . LYS I  1 136 ? 30.042  -3.280  12.046  1.00 25.86 ? 136  LYS I CA  1 
ATOM   9933  C  C   . LYS I  1 136 ? 30.011  -2.583  10.688  1.00 23.39 ? 136  LYS I C   1 
ATOM   9934  O  O   . LYS I  1 136 ? 29.576  -3.157  9.700   1.00 21.45 ? 136  LYS I O   1 
ATOM   9935  C  CB  . LYS I  1 136 ? 29.115  -2.543  13.016  1.00 28.43 ? 136  LYS I CB  1 
ATOM   9936  C  CG  . LYS I  1 136 ? 27.756  -3.172  13.207  1.00 30.75 ? 136  LYS I CG  1 
ATOM   9937  C  CD  . LYS I  1 136 ? 27.409  -3.283  14.706  1.00 37.69 ? 136  LYS I CD  1 
ATOM   9938  C  CE  . LYS I  1 136 ? 27.209  -1.921  15.378  1.00 41.21 ? 136  LYS I CE  1 
ATOM   9939  N  NZ  . LYS I  1 136 ? 25.988  -1.179  14.911  1.00 47.04 ? 136  LYS I NZ  1 
ATOM   9940  N  N   . THR I  1 137 ? 30.469  -1.335  10.654  1.00 25.83 ? 137  THR I N   1 
ATOM   9941  C  CA  . THR I  1 137 ? 30.421  -0.513  9.446   1.00 22.52 ? 137  THR I CA  1 
ATOM   9942  C  C   . THR I  1 137 ? 31.836  -0.115  9.026   1.00 24.08 ? 137  THR I C   1 
ATOM   9943  O  O   . THR I  1 137 ? 32.044  0.415   7.932   1.00 22.65 ? 137  THR I O   1 
ATOM   9944  C  CB  . THR I  1 137 ? 29.631  0.785   9.682   1.00 23.28 ? 137  THR I CB  1 
ATOM   9945  O  OG1 . THR I  1 137 ? 30.337  1.594   10.625  1.00 26.05 ? 137  THR I OG1 1 
ATOM   9946  C  CG2 . THR I  1 137 ? 28.231  0.500   10.214  1.00 21.10 ? 137  THR I CG2 1 
ATOM   9947  N  N   . GLY I  1 138 ? 32.804  -0.376  9.904   1.00 24.40 ? 138  GLY I N   1 
ATOM   9948  C  CA  . GLY I  1 138 ? 34.180  0.018   9.667   1.00 22.17 ? 138  GLY I CA  1 
ATOM   9949  C  C   . GLY I  1 138 ? 34.381  1.517   9.801   1.00 21.31 ? 138  GLY I C   1 
ATOM   9950  O  O   . GLY I  1 138 ? 35.292  2.076   9.210   1.00 20.46 ? 138  GLY I O   1 
ATOM   9951  N  N   . ASN I  1 139 ? 33.525  2.179   10.570  1.00 23.29 ? 139  ASN I N   1 
ATOM   9952  C  CA  . ASN I  1 139 ? 33.700  3.609   10.815  1.00 23.84 ? 139  ASN I CA  1 
ATOM   9953  C  C   . ASN I  1 139 ? 33.820  4.409   9.514   1.00 22.82 ? 139  ASN I C   1 
ATOM   9954  O  O   . ASN I  1 139 ? 34.439  5.477   9.483   1.00 23.12 ? 139  ASN I O   1 
ATOM   9955  C  CB  . ASN I  1 139 ? 34.937  3.839   11.700  1.00 26.59 ? 139  ASN I CB  1 
ATOM   9956  C  CG  . ASN I  1 139 ? 34.650  3.648   13.188  1.00 23.37 ? 139  ASN I CG  1 
ATOM   9957  O  OD1 . ASN I  1 139 ? 34.128  4.544   13.846  1.00 25.21 ? 139  ASN I OD1 1 
ATOM   9958  N  ND2 . ASN I  1 139 ? 35.009  2.488   13.720  1.00 24.21 ? 139  ASN I ND2 1 
ATOM   9959  N  N   . ALA I  1 140 ? 33.204  3.891   8.450   1.00 23.17 ? 140  ALA I N   1 
ATOM   9960  C  CA  . ALA I  1 140 ? 33.280  4.488   7.109   1.00 23.40 ? 140  ALA I CA  1 
ATOM   9961  C  C   . ALA I  1 140 ? 32.325  5.659   6.905   1.00 22.54 ? 140  ALA I C   1 
ATOM   9962  O  O   . ALA I  1 140 ? 32.368  6.325   5.881   1.00 23.72 ? 140  ALA I O   1 
ATOM   9963  C  CB  . ALA I  1 140 ? 33.068  3.420   6.010   1.00 21.57 ? 140  ALA I CB  1 
ATOM   9964  N  N   . GLY I  1 141 ? 31.451  5.892   7.869   1.00 22.98 ? 141  GLY I N   1 
ATOM   9965  C  CA  . GLY I  1 141 ? 30.693  7.122   7.899   1.00 22.27 ? 141  GLY I CA  1 
ATOM   9966  C  C   . GLY I  1 141 ? 29.404  7.104   7.113   1.00 26.18 ? 141  GLY I C   1 
ATOM   9967  O  O   . GLY I  1 141 ? 28.807  6.051   6.877   1.00 24.49 ? 141  GLY I O   1 
ATOM   9968  N  N   . SER I  1 142 ? 28.978  8.301   6.717   1.00 26.87 ? 142  SER I N   1 
ATOM   9969  C  CA  . SER I  1 142 ? 27.737  8.498   5.982   1.00 25.72 ? 142  SER I CA  1 
ATOM   9970  C  C   . SER I  1 142 ? 27.804  7.913   4.575   1.00 22.70 ? 142  SER I C   1 
ATOM   9971  O  O   . SER I  1 142 ? 28.879  7.672   4.032   1.00 21.42 ? 142  SER I O   1 
ATOM   9972  C  CB  . SER I  1 142 ? 27.405  9.987   5.900   1.00 24.35 ? 142  SER I CB  1 
ATOM   9973  O  OG  . SER I  1 142 ? 28.223  10.636  4.947   1.00 24.96 ? 142  SER I OG  1 
ATOM   9974  N  N   . ARG I  1 143 ? 26.633  7.695   3.993   1.00 24.38 ? 143  ARG I N   1 
ATOM   9975  C  CA  . ARG I  1 143 ? 26.517  7.125   2.663   1.00 21.76 ? 143  ARG I CA  1 
ATOM   9976  C  C   . ARG I  1 143 ? 26.403  8.264   1.645   1.00 24.38 ? 143  ARG I C   1 
ATOM   9977  O  O   . ARG I  1 143 ? 25.405  8.980   1.627   1.00 29.54 ? 143  ARG I O   1 
ATOM   9978  C  CB  . ARG I  1 143 ? 25.304  6.177   2.622   1.00 23.56 ? 143  ARG I CB  1 
ATOM   9979  C  CG  . ARG I  1 143 ? 25.386  5.044   3.670   1.00 21.14 ? 143  ARG I CG  1 
ATOM   9980  C  CD  . ARG I  1 143 ? 24.044  4.371   4.011   1.00 21.32 ? 143  ARG I CD  1 
ATOM   9981  N  NE  . ARG I  1 143 ? 24.201  3.431   5.124   1.00 22.79 ? 143  ARG I NE  1 
ATOM   9982  C  CZ  . ARG I  1 143 ? 23.402  2.393   5.365   1.00 21.56 ? 143  ARG I CZ  1 
ATOM   9983  N  NH1 . ARG I  1 143 ? 22.377  2.144   4.575   1.00 21.86 ? 143  ARG I NH1 1 
ATOM   9984  N  NH2 . ARG I  1 143 ? 23.638  1.591   6.392   1.00 21.79 ? 143  ARG I NH2 1 
ATOM   9985  N  N   . LEU I  1 144 ? 27.433  8.434   0.813   1.00 23.64 ? 144  LEU I N   1 
ATOM   9986  C  CA  . LEU I  1 144 ? 27.514  9.556   -0.135  1.00 23.26 ? 144  LEU I CA  1 
ATOM   9987  C  C   . LEU I  1 144 ? 26.721  9.343   -1.422  1.00 23.28 ? 144  LEU I C   1 
ATOM   9988  O  O   . LEU I  1 144 ? 26.175  10.289  -1.992  1.00 25.60 ? 144  LEU I O   1 
ATOM   9989  C  CB  . LEU I  1 144 ? 28.974  9.856   -0.505  1.00 21.77 ? 144  LEU I CB  1 
ATOM   9990  C  CG  . LEU I  1 144 ? 29.980  10.134  0.611   1.00 22.30 ? 144  LEU I CG  1 
ATOM   9991  C  CD1 . LEU I  1 144 ? 31.345  10.417  0.024   1.00 21.75 ? 144  LEU I CD1 1 
ATOM   9992  C  CD2 . LEU I  1 144 ? 29.508  11.278  1.476   1.00 22.33 ? 144  LEU I CD2 1 
ATOM   9993  N  N   . ALA I  1 145 ? 26.713  8.108   -1.903  1.00 20.33 ? 145  ALA I N   1 
ATOM   9994  C  CA  . ALA I  1 145 ? 25.932  7.737   -3.067  1.00 19.37 ? 145  ALA I CA  1 
ATOM   9995  C  C   . ALA I  1 145 ? 25.639  6.245   -2.985  1.00 20.20 ? 145  ALA I C   1 
ATOM   9996  O  O   . ALA I  1 145 ? 26.339  5.504   -2.306  1.00 20.17 ? 145  ALA I O   1 
ATOM   9997  C  CB  . ALA I  1 145 ? 26.672  8.069   -4.354  1.00 20.10 ? 145  ALA I CB  1 
ATOM   9998  N  N   . CYS I  1 146 ? 24.592  5.810   -3.668  1.00 20.49 ? 146  CYS I N   1 
ATOM   9999  C  CA  . CYS I  1 146 ? 24.265  4.398   -3.712  1.00 20.65 ? 146  CYS I CA  1 
ATOM   10000 C  C   . CYS I  1 146 ? 23.446  4.160   -4.955  1.00 20.80 ? 146  CYS I C   1 
ATOM   10001 O  O   . CYS I  1 146 ? 22.974  5.105   -5.585  1.00 20.01 ? 146  CYS I O   1 
ATOM   10002 C  CB  . CYS I  1 146 ? 23.478  3.967   -2.465  1.00 21.51 ? 146  CYS I CB  1 
ATOM   10003 S  SG  . CYS I  1 146 ? 21.850  4.759   -2.225  1.00 21.14 ? 146  CYS I SG  1 
ATOM   10004 N  N   . GLY I  1 147 ? 23.288  2.892   -5.310  1.00 19.51 ? 147  GLY I N   1 
ATOM   10005 C  CA  . GLY I  1 147 ? 22.403  2.512   -6.383  1.00 20.67 ? 147  GLY I CA  1 
ATOM   10006 C  C   . GLY I  1 147 ? 22.112  1.031   -6.284  1.00 22.38 ? 147  GLY I C   1 
ATOM   10007 O  O   . GLY I  1 147 ? 22.906  0.276   -5.708  1.00 19.82 ? 147  GLY I O   1 
ATOM   10008 N  N   . VAL I  1 148 ? 20.976  0.622   -6.843  1.00 19.54 ? 148  VAL I N   1 
ATOM   10009 C  CA  . VAL I  1 148 ? 20.567  -0.775  -6.833  1.00 19.97 ? 148  VAL I CA  1 
ATOM   10010 C  C   . VAL I  1 148 ? 21.325  -1.527  -7.913  1.00 20.17 ? 148  VAL I C   1 
ATOM   10011 O  O   . VAL I  1 148 ? 21.488  -1.020  -9.031  1.00 19.63 ? 148  VAL I O   1 
ATOM   10012 C  CB  . VAL I  1 148 ? 19.039  -0.923  -7.064  1.00 20.07 ? 148  VAL I CB  1 
ATOM   10013 C  CG1 . VAL I  1 148 ? 18.623  -2.383  -7.007  1.00 19.30 ? 148  VAL I CG1 1 
ATOM   10014 C  CG2 . VAL I  1 148 ? 18.260  -0.112  -6.038  1.00 18.68 ? 148  VAL I CG2 1 
ATOM   10015 N  N   . ILE I  1 149 ? 21.791  -2.730  -7.578  1.00 19.32 ? 149  ILE I N   1 
ATOM   10016 C  CA  . ILE I  1 149 ? 22.546  -3.556  -8.525  1.00 18.78 ? 149  ILE I CA  1 
ATOM   10017 C  C   . ILE I  1 149 ? 21.600  -4.289  -9.489  1.00 20.75 ? 149  ILE I C   1 
ATOM   10018 O  O   . ILE I  1 149 ? 20.843  -5.189  -9.109  1.00 19.36 ? 149  ILE I O   1 
ATOM   10019 C  CB  . ILE I  1 149 ? 23.533  -4.521  -7.800  1.00 18.95 ? 149  ILE I CB  1 
ATOM   10020 C  CG1 . ILE I  1 149 ? 24.549  -3.718  -6.981  1.00 18.48 ? 149  ILE I CG1 1 
ATOM   10021 C  CG2 . ILE I  1 149 ? 24.227  -5.471  -8.776  1.00 16.29 ? 149  ILE I CG2 1 
ATOM   10022 C  CD1 . ILE I  1 149 ? 25.307  -4.544  -5.954  1.00 16.21 ? 149  ILE I CD1 1 
ATOM   10023 N  N   . GLY I  1 150 ? 21.634  -3.878  -10.750 1.00 20.52 ? 150  GLY I N   1 
ATOM   10024 C  CA  . GLY I  1 150 ? 20.699  -4.402  -11.716 1.00 21.09 ? 150  GLY I CA  1 
ATOM   10025 C  C   . GLY I  1 150 ? 21.337  -5.353  -12.699 1.00 23.46 ? 150  GLY I C   1 
ATOM   10026 O  O   . GLY I  1 150 ? 22.546  -5.321  -12.906 1.00 25.37 ? 150  GLY I O   1 
ATOM   10027 N  N   . ILE I  1 151 ? 20.510  -6.203  -13.301 1.00 26.28 ? 151  ILE I N   1 
ATOM   10028 C  CA  . ILE I  1 151 ? 20.919  -7.071  -14.399 1.00 23.56 ? 151  ILE I CA  1 
ATOM   10029 C  C   . ILE I  1 151 ? 21.230  -6.219  -15.625 1.00 24.68 ? 151  ILE I C   1 
ATOM   10030 O  O   . ILE I  1 151 ? 20.442  -5.356  -16.000 1.00 24.58 ? 151  ILE I O   1 
ATOM   10031 C  CB  . ILE I  1 151 ? 19.799  -8.087  -14.726 1.00 21.97 ? 151  ILE I CB  1 
ATOM   10032 C  CG1 . ILE I  1 151 ? 19.504  -8.960  -13.495 1.00 22.81 ? 151  ILE I CG1 1 
ATOM   10033 C  CG2 . ILE I  1 151 ? 20.167  -8.933  -15.944 1.00 24.96 ? 151  ILE I CG2 1 
ATOM   10034 C  CD1 . ILE I  1 151 ? 18.232  -9.825  -13.597 1.00 23.59 ? 151  ILE I CD1 1 
ATOM   10035 N  N   . ALA I  1 152 ? 22.389  -6.452  -16.233 1.00 25.47 ? 152  ALA I N   1 
ATOM   10036 C  CA  . ALA I  1 152 ? 22.821  -5.696  -17.402 1.00 26.37 ? 152  ALA I CA  1 
ATOM   10037 C  C   . ALA I  1 152 ? 22.932  -6.632  -18.603 1.00 28.61 ? 152  ALA I C   1 
ATOM   10038 O  O   . ALA I  1 152 ? 22.972  -7.854  -18.441 1.00 26.64 ? 152  ALA I O   1 
ATOM   10039 C  CB  . ALA I  1 152 ? 24.165  -5.013  -17.125 1.00 26.82 ? 152  ALA I CB  1 
ATOM   10040 N  N   . GLN I  1 153 ? 22.977  -6.073  -19.809 1.00 30.24 ? 153  GLN I N   1 
ATOM   10041 C  CA  . GLN I  1 153 ? 23.095  -6.915  -21.000 1.00 33.67 ? 153  GLN I CA  1 
ATOM   10042 C  C   . GLN I  1 153 ? 24.552  -7.134  -21.371 1.00 39.17 ? 153  GLN I C   1 
ATOM   10043 O  O   . GLN I  1 153 ? 24.896  -8.179  -21.942 1.00 41.12 ? 153  GLN I O   1 
ATOM   10044 C  CB  . GLN I  1 153 ? 22.332  -6.334  -22.195 1.00 31.98 ? 153  GLN I CB  1 
ATOM   10045 C  CG  . GLN I  1 153 ? 23.026  -5.176  -22.878 1.00 36.71 ? 153  GLN I CG  1 
ATOM   10046 C  CD  . GLN I  1 153 ? 22.511  -4.937  -24.284 1.00 38.92 ? 153  GLN I CD  1 
ATOM   10047 O  OE1 . GLN I  1 153 ? 21.799  -5.771  -24.856 1.00 35.89 ? 153  GLN I OE1 1 
ATOM   10048 N  NE2 . GLN I  1 153 ? 22.874  -3.793  -24.855 1.00 43.57 ? 153  GLN I NE2 1 
ATOM   10049 O  OXT . GLN I  1 153 ? 25.398  -6.268  -21.096 1.00 37.50 ? 153  GLN I OXT 1 
ATOM   10050 N  N   . ALA J  1 1   ? 8.411   -16.023 1.495   1.00 46.99 ? 1    ALA J N   1 
ATOM   10051 C  CA  . ALA J  1 1   ? 7.605   -14.814 1.297   1.00 50.09 ? 1    ALA J CA  1 
ATOM   10052 C  C   . ALA J  1 1   ? 8.429   -13.629 0.787   1.00 46.10 ? 1    ALA J C   1 
ATOM   10053 O  O   . ALA J  1 1   ? 8.532   -12.601 1.458   1.00 48.40 ? 1    ALA J O   1 
ATOM   10054 C  CB  . ALA J  1 1   ? 6.855   -14.436 2.585   1.00 50.56 ? 1    ALA J CB  1 
ATOM   10055 N  N   . THR J  1 2   ? 8.994   -13.780 -0.410  1.00 42.83 ? 2    THR J N   1 
ATOM   10056 C  CA  . THR J  1 2   ? 9.816   -12.750 -1.047  1.00 37.49 ? 2    THR J CA  1 
ATOM   10057 C  C   . THR J  1 2   ? 9.157   -11.363 -1.108  1.00 37.94 ? 2    THR J C   1 
ATOM   10058 O  O   . THR J  1 2   ? 7.963   -11.232 -1.395  1.00 39.28 ? 2    THR J O   1 
ATOM   10059 C  CB  . THR J  1 2   ? 10.196  -13.171 -2.475  1.00 36.89 ? 2    THR J CB  1 
ATOM   10060 O  OG1 . THR J  1 2   ? 10.537  -14.560 -2.489  1.00 44.30 ? 2    THR J OG1 1 
ATOM   10061 C  CG2 . THR J  1 2   ? 11.373  -12.371 -2.970  1.00 37.45 ? 2    THR J CG2 1 
ATOM   10062 N  N   . LYS J  1 3   ? 9.954   -10.331 -0.836  1.00 37.94 ? 3    LYS J N   1 
ATOM   10063 C  CA  . LYS J  1 3   ? 9.519   -8.940  -0.947  1.00 34.94 ? 3    LYS J CA  1 
ATOM   10064 C  C   . LYS J  1 3   ? 10.478  -8.161  -1.856  1.00 30.55 ? 3    LYS J C   1 
ATOM   10065 O  O   . LYS J  1 3   ? 11.666  -8.491  -1.948  1.00 32.15 ? 3    LYS J O   1 
ATOM   10066 C  CB  . LYS J  1 3   ? 9.411   -8.285  0.445   1.00 32.18 ? 3    LYS J CB  1 
ATOM   10067 C  CG  . LYS J  1 3   ? 8.166   -8.697  1.222   1.00 35.16 ? 3    LYS J CG  1 
ATOM   10068 C  CD  . LYS J  1 3   ? 8.213   -8.318  2.708   1.00 44.59 ? 3    LYS J CD  1 
ATOM   10069 C  CE  . LYS J  1 3   ? 8.008   -6.820  2.963   1.00 46.63 ? 3    LYS J CE  1 
ATOM   10070 N  NZ  . LYS J  1 3   ? 6.654   -6.320  2.575   1.00 47.13 ? 3    LYS J NZ  1 
ATOM   10071 N  N   . ALA J  1 4   ? 9.959   -7.147  -2.543  1.00 25.53 ? 4    ALA J N   1 
ATOM   10072 C  CA  . ALA J  1 4   ? 10.789  -6.247  -3.339  1.00 23.18 ? 4    ALA J CA  1 
ATOM   10073 C  C   . ALA J  1 4   ? 10.203  -4.836  -3.345  1.00 22.61 ? 4    ALA J C   1 
ATOM   10074 O  O   . ALA J  1 4   ? 9.073   -4.625  -2.940  1.00 23.26 ? 4    ALA J O   1 
ATOM   10075 C  CB  . ALA J  1 4   ? 10.950  -6.773  -4.760  1.00 22.57 ? 4    ALA J CB  1 
ATOM   10076 N  N   . VAL J  1 5   ? 10.988  -3.868  -3.794  1.00 23.73 ? 5    VAL J N   1 
ATOM   10077 C  CA  . VAL J  1 5   ? 10.568  -2.469  -3.832  1.00 21.60 ? 5    VAL J CA  1 
ATOM   10078 C  C   . VAL J  1 5   ? 11.255  -1.781  -5.021  1.00 23.08 ? 5    VAL J C   1 
ATOM   10079 O  O   . VAL J  1 5   ? 12.240  -2.290  -5.569  1.00 21.72 ? 5    VAL J O   1 
ATOM   10080 C  CB  . VAL J  1 5   ? 10.899  -1.747  -2.499  1.00 21.25 ? 5    VAL J CB  1 
ATOM   10081 C  CG1 . VAL J  1 5   ? 12.387  -1.779  -2.238  1.00 21.54 ? 5    VAL J CG1 1 
ATOM   10082 C  CG2 . VAL J  1 5   ? 10.363  -0.317  -2.488  1.00 20.13 ? 5    VAL J CG2 1 
ATOM   10083 N  N   . CYS J  1 6   ? 10.722  -0.635  -5.423  1.00 21.21 ? 6    CYS J N   1 
ATOM   10084 C  CA  . CYS J  1 6   ? 11.219  0.089   -6.572  1.00 18.57 ? 6    CYS J CA  1 
ATOM   10085 C  C   . CYS J  1 6   ? 10.922  1.577   -6.401  1.00 21.37 ? 6    CYS J C   1 
ATOM   10086 O  O   . CYS J  1 6   ? 9.760   1.976   -6.258  1.00 20.72 ? 6    CYS J O   1 
ATOM   10087 C  CB  . CYS J  1 6   ? 10.522  -0.439  -7.819  1.00 20.15 ? 6    CYS J CB  1 
ATOM   10088 S  SG  . CYS J  1 6   ? 11.028  0.277   -9.378  1.00 27.58 ? 6    CYS J SG  1 
ATOM   10089 N  N   . VAL J  1 7   ? 11.966  2.397   -6.406  1.00 20.35 ? 7    VAL J N   1 
ATOM   10090 C  CA  . VAL J  1 7   ? 11.784  3.844   -6.454  1.00 22.10 ? 7    VAL J CA  1 
ATOM   10091 C  C   . VAL J  1 7   ? 11.859  4.321   -7.900  1.00 22.77 ? 7    VAL J C   1 
ATOM   10092 O  O   . VAL J  1 7   ? 12.870  4.135   -8.566  1.00 23.55 ? 7    VAL J O   1 
ATOM   10093 C  CB  . VAL J  1 7   ? 12.840  4.601   -5.620  1.00 23.11 ? 7    VAL J CB  1 
ATOM   10094 C  CG1 . VAL J  1 7   ? 12.666  6.109   -5.789  1.00 24.27 ? 7    VAL J CG1 1 
ATOM   10095 C  CG2 . VAL J  1 7   ? 12.747  4.204   -4.158  1.00 22.41 ? 7    VAL J CG2 1 
ATOM   10096 N  N   . LEU J  1 8   ? 10.782  4.928   -8.388  1.00 24.22 ? 8    LEU J N   1 
ATOM   10097 C  CA  . LEU J  1 8   ? 10.733  5.441   -9.756  1.00 20.54 ? 8    LEU J CA  1 
ATOM   10098 C  C   . LEU J  1 8   ? 11.091  6.926   -9.782  1.00 23.20 ? 8    LEU J C   1 
ATOM   10099 O  O   . LEU J  1 8   ? 10.510  7.722   -9.048  1.00 23.95 ? 8    LEU J O   1 
ATOM   10100 C  CB  . LEU J  1 8   ? 9.338   5.242   -10.352 1.00 20.46 ? 8    LEU J CB  1 
ATOM   10101 C  CG  . LEU J  1 8   ? 8.722   3.839   -10.379 1.00 19.42 ? 8    LEU J CG  1 
ATOM   10102 C  CD1 . LEU J  1 8   ? 7.236   3.986   -10.487 1.00 23.60 ? 8    LEU J CD1 1 
ATOM   10103 C  CD2 . LEU J  1 8   ? 9.228   3.031   -11.532 1.00 20.90 ? 8    LEU J CD2 1 
ATOM   10104 N  N   . LYS J  1 9   ? 12.058  7.289   -10.619 1.00 22.64 ? 9    LYS J N   1 
ATOM   10105 C  CA  . LYS J  1 9   ? 12.455  8.675   -10.808 1.00 21.22 ? 9    LYS J CA  1 
ATOM   10106 C  C   . LYS J  1 9   ? 12.661  8.903   -12.295 1.00 22.69 ? 9    LYS J C   1 
ATOM   10107 O  O   . LYS J  1 9   ? 12.927  7.961   -13.043 1.00 21.94 ? 9    LYS J O   1 
ATOM   10108 C  CB  . LYS J  1 9   ? 13.758  8.974   -10.056 1.00 25.14 ? 9    LYS J CB  1 
ATOM   10109 C  CG  . LYS J  1 9   ? 13.646  8.900   -8.529  1.00 28.90 ? 9    LYS J CG  1 
ATOM   10110 C  CD  . LYS J  1 9   ? 14.981  9.237   -7.857  1.00 42.48 ? 9    LYS J CD  1 
ATOM   10111 C  CE  . LYS J  1 9   ? 15.021  8.855   -6.366  1.00 42.10 ? 9    LYS J CE  1 
ATOM   10112 N  NZ  . LYS J  1 9   ? 14.255  9.806   -5.512  1.00 43.92 ? 9    LYS J NZ  1 
ATOM   10113 N  N   . GLY J  1 10  ? 12.536  10.152  -12.725 1.00 22.74 ? 10   GLY J N   1 
ATOM   10114 C  CA  . GLY J  1 10  ? 12.788  10.509  -14.106 1.00 24.50 ? 10   GLY J CA  1 
ATOM   10115 C  C   . GLY J  1 10  ? 13.280  11.941  -14.216 1.00 28.47 ? 10   GLY J C   1 
ATOM   10116 O  O   . GLY J  1 10  ? 13.684  12.549  -13.218 1.00 29.00 ? 10   GLY J O   1 
ATOM   10117 N  N   . ASP J  1 11  ? 13.234  12.479  -15.431 1.00 30.16 ? 11   ASP J N   1 
ATOM   10118 C  CA  . ASP J  1 11  ? 13.657  13.857  -15.704 1.00 33.28 ? 11   ASP J CA  1 
ATOM   10119 C  C   . ASP J  1 11  ? 12.560  14.902  -15.449 1.00 31.78 ? 11   ASP J C   1 
ATOM   10120 O  O   . ASP J  1 11  ? 12.852  16.081  -15.265 1.00 34.71 ? 11   ASP J O   1 
ATOM   10121 C  CB  . ASP J  1 11  ? 14.168  13.976  -17.143 1.00 32.95 ? 11   ASP J CB  1 
ATOM   10122 C  CG  . ASP J  1 11  ? 15.191  12.906  -17.485 1.00 37.97 ? 11   ASP J CG  1 
ATOM   10123 O  OD1 . ASP J  1 11  ? 15.913  12.457  -16.564 1.00 41.47 ? 11   ASP J OD1 1 
ATOM   10124 O  OD2 . ASP J  1 11  ? 15.271  12.513  -18.671 1.00 42.55 ? 11   ASP J OD2 1 
ATOM   10125 N  N   . GLY J  1 12  ? 11.304  14.464  -15.450 1.00 29.19 ? 12   GLY J N   1 
ATOM   10126 C  CA  . GLY J  1 12  ? 10.181  15.335  -15.166 1.00 25.75 ? 12   GLY J CA  1 
ATOM   10127 C  C   . GLY J  1 12  ? 9.735   15.136  -13.734 1.00 25.80 ? 12   GLY J C   1 
ATOM   10128 O  O   . GLY J  1 12  ? 10.507  14.639  -12.923 1.00 26.11 ? 12   GLY J O   1 
ATOM   10129 N  N   . PRO J  1 13  ? 8.475   15.498  -13.425 1.00 26.08 ? 13   PRO J N   1 
ATOM   10130 C  CA  . PRO J  1 13  ? 7.927   15.471  -12.063 1.00 21.63 ? 13   PRO J CA  1 
ATOM   10131 C  C   . PRO J  1 13  ? 7.512   14.074  -11.587 1.00 20.12 ? 13   PRO J C   1 
ATOM   10132 O  O   . PRO J  1 13  ? 7.223   13.925  -10.400 1.00 22.74 ? 13   PRO J O   1 
ATOM   10133 C  CB  . PRO J  1 13  ? 6.681   16.367  -12.161 1.00 21.43 ? 13   PRO J CB  1 
ATOM   10134 C  CG  . PRO J  1 13  ? 6.582   16.804  -13.608 1.00 22.23 ? 13   PRO J CG  1 
ATOM   10135 C  CD  . PRO J  1 13  ? 7.468   15.923  -14.412 1.00 24.19 ? 13   PRO J CD  1 
ATOM   10136 N  N   . VAL J  1 14  ? 7.489   13.081  -12.476 1.00 19.60 ? 14   VAL J N   1 
ATOM   10137 C  CA  . VAL J  1 14  ? 6.990   11.745  -12.133 1.00 19.16 ? 14   VAL J CA  1 
ATOM   10138 C  C   . VAL J  1 14  ? 7.893   10.989  -11.148 1.00 20.55 ? 14   VAL J C   1 
ATOM   10139 O  O   . VAL J  1 14  ? 9.068   10.758  -11.416 1.00 21.56 ? 14   VAL J O   1 
ATOM   10140 C  CB  . VAL J  1 14  ? 6.791   10.873  -13.386 1.00 16.55 ? 14   VAL J CB  1 
ATOM   10141 C  CG1 . VAL J  1 14  ? 6.309   9.479   -12.996 1.00 16.88 ? 14   VAL J CG1 1 
ATOM   10142 C  CG2 . VAL J  1 14  ? 5.822   11.534  -14.345 1.00 18.24 ? 14   VAL J CG2 1 
ATOM   10143 N  N   . GLN J  1 15  ? 7.337   10.605  -10.008 1.00 20.82 ? 15   GLN J N   1 
ATOM   10144 C  CA  . GLN J  1 15  ? 8.050   9.762   -9.059  1.00 23.24 ? 15   GLN J CA  1 
ATOM   10145 C  C   . GLN J  1 15  ? 7.085   8.926   -8.215  1.00 22.65 ? 15   GLN J C   1 
ATOM   10146 O  O   . GLN J  1 15  ? 5.930   9.289   -8.054  1.00 21.17 ? 15   GLN J O   1 
ATOM   10147 C  CB  . GLN J  1 15  ? 8.990   10.595  -8.175  1.00 26.62 ? 15   GLN J CB  1 
ATOM   10148 C  CG  . GLN J  1 15  ? 8.340   11.732  -7.410  1.00 28.50 ? 15   GLN J CG  1 
ATOM   10149 C  CD  . GLN J  1 15  ? 9.370   12.733  -6.871  1.00 37.41 ? 15   GLN J CD  1 
ATOM   10150 O  OE1 . GLN J  1 15  ? 10.559  12.417  -6.736  1.00 39.59 ? 15   GLN J OE1 1 
ATOM   10151 N  NE2 . GLN J  1 15  ? 8.914   13.946  -6.574  1.00 39.99 ? 15   GLN J NE2 1 
ATOM   10152 N  N   . GLY J  1 16  ? 7.571   7.806   -7.686  1.00 23.20 ? 16   GLY J N   1 
ATOM   10153 C  CA  . GLY J  1 16  ? 6.738   6.867   -6.955  1.00 21.81 ? 16   GLY J CA  1 
ATOM   10154 C  C   . GLY J  1 16  ? 7.495   5.729   -6.290  1.00 20.00 ? 16   GLY J C   1 
ATOM   10155 O  O   . GLY J  1 16  ? 8.701   5.607   -6.430  1.00 21.09 ? 16   GLY J O   1 
ATOM   10156 N  N   . ILE J  1 17  ? 6.773   4.900   -5.549  1.00 19.10 ? 17   ILE J N   1 
ATOM   10157 C  CA  . ILE J  1 17  ? 7.352   3.767   -4.848  1.00 19.54 ? 17   ILE J CA  1 
ATOM   10158 C  C   . ILE J  1 17  ? 6.418   2.597   -5.062  1.00 19.92 ? 17   ILE J C   1 
ATOM   10159 O  O   . ILE J  1 17  ? 5.237   2.669   -4.724  1.00 19.21 ? 17   ILE J O   1 
ATOM   10160 C  CB  . ILE J  1 17  ? 7.468   4.033   -3.329  1.00 21.76 ? 17   ILE J CB  1 
ATOM   10161 C  CG1 . ILE J  1 17  ? 8.431   5.187   -3.038  1.00 22.07 ? 17   ILE J CG1 1 
ATOM   10162 C  CG2 . ILE J  1 17  ? 7.896   2.778   -2.570  1.00 19.40 ? 17   ILE J CG2 1 
ATOM   10163 C  CD1 . ILE J  1 17  ? 8.437   5.572   -1.572  1.00 20.79 ? 17   ILE J CD1 1 
ATOM   10164 N  N   . ILE J  1 18  ? 6.947   1.526   -5.638  1.00 18.77 ? 18   ILE J N   1 
ATOM   10165 C  CA  . ILE J  1 18  ? 6.140   0.368   -5.968  1.00 19.25 ? 18   ILE J CA  1 
ATOM   10166 C  C   . ILE J  1 18  ? 6.650   -0.805  -5.154  1.00 19.36 ? 18   ILE J C   1 
ATOM   10167 O  O   . ILE J  1 18  ? 7.819   -1.140  -5.227  1.00 21.29 ? 18   ILE J O   1 
ATOM   10168 C  CB  . ILE J  1 18  ? 6.202   0.070   -7.499  1.00 18.07 ? 18   ILE J CB  1 
ATOM   10169 C  CG1 . ILE J  1 18  ? 5.663   1.265   -8.307  1.00 18.52 ? 18   ILE J CG1 1 
ATOM   10170 C  CG2 . ILE J  1 18  ? 5.479   -1.240  -7.864  1.00 16.33 ? 18   ILE J CG2 1 
ATOM   10171 C  CD1 . ILE J  1 18  ? 4.167   1.546   -8.131  1.00 16.88 ? 18   ILE J CD1 1 
ATOM   10172 N  N   . ASN J  1 19  ? 5.781   -1.407  -4.352  1.00 21.60 ? 19   ASN J N   1 
ATOM   10173 C  CA  . ASN J  1 19  ? 6.156   -2.563  -3.542  1.00 21.39 ? 19   ASN J CA  1 
ATOM   10174 C  C   . ASN J  1 19  ? 5.713   -3.836  -4.224  1.00 21.29 ? 19   ASN J C   1 
ATOM   10175 O  O   . ASN J  1 19  ? 4.703   -3.851  -4.911  1.00 22.87 ? 19   ASN J O   1 
ATOM   10176 C  CB  . ASN J  1 19  ? 5.497   -2.496  -2.165  1.00 24.58 ? 19   ASN J CB  1 
ATOM   10177 C  CG  . ASN J  1 19  ? 5.783   -1.204  -1.441  1.00 24.96 ? 19   ASN J CG  1 
ATOM   10178 O  OD1 . ASN J  1 19  ? 6.891   -0.987  -0.966  1.00 25.63 ? 19   ASN J OD1 1 
ATOM   10179 N  ND2 . ASN J  1 19  ? 4.777   -0.338  -1.346  1.00 26.56 ? 19   ASN J ND2 1 
ATOM   10180 N  N   . PHE J  1 20  ? 6.467   -4.908  -4.033  1.00 23.30 ? 20   PHE J N   1 
ATOM   10181 C  CA  . PHE J  1 20  ? 6.111   -6.213  -4.578  1.00 23.71 ? 20   PHE J CA  1 
ATOM   10182 C  C   . PHE J  1 20  ? 6.140   -7.219  -3.455  1.00 26.91 ? 20   PHE J C   1 
ATOM   10183 O  O   . PHE J  1 20  ? 6.970   -7.128  -2.548  1.00 28.24 ? 20   PHE J O   1 
ATOM   10184 C  CB  . PHE J  1 20  ? 7.106   -6.666  -5.646  1.00 21.46 ? 20   PHE J CB  1 
ATOM   10185 C  CG  . PHE J  1 20  ? 7.308   -5.681  -6.753  1.00 21.82 ? 20   PHE J CG  1 
ATOM   10186 C  CD1 . PHE J  1 20  ? 8.022   -4.512  -6.540  1.00 22.97 ? 20   PHE J CD1 1 
ATOM   10187 C  CD2 . PHE J  1 20  ? 6.807   -5.930  -8.014  1.00 21.42 ? 20   PHE J CD2 1 
ATOM   10188 C  CE1 . PHE J  1 20  ? 8.226   -3.607  -7.568  1.00 19.88 ? 20   PHE J CE1 1 
ATOM   10189 C  CE2 . PHE J  1 20  ? 7.006   -5.025  -9.049  1.00 22.86 ? 20   PHE J CE2 1 
ATOM   10190 C  CZ  . PHE J  1 20  ? 7.719   -3.864  -8.822  1.00 22.27 ? 20   PHE J CZ  1 
ATOM   10191 N  N   . GLU J  1 21  ? 5.238   -8.186  -3.511  1.00 28.78 ? 21   GLU J N   1 
ATOM   10192 C  CA  . GLU J  1 21  ? 5.217   -9.233  -2.505  1.00 32.56 ? 21   GLU J CA  1 
ATOM   10193 C  C   . GLU J  1 21  ? 4.806   -10.536 -3.167  1.00 33.70 ? 21   GLU J C   1 
ATOM   10194 O  O   . GLU J  1 21  ? 3.868   -10.563 -3.972  1.00 29.70 ? 21   GLU J O   1 
ATOM   10195 C  CB  . GLU J  1 21  ? 4.276   -8.866  -1.352  1.00 30.38 ? 21   GLU J CB  1 
ATOM   10196 C  CG  . GLU J  1 21  ? 4.408   -9.764  -0.124  1.00 41.11 ? 21   GLU J CG  1 
ATOM   10197 C  CD  . GLU J  1 21  ? 3.678   -9.208  1.094   1.00 47.74 ? 21   GLU J CD  1 
ATOM   10198 O  OE1 . GLU J  1 21  ? 4.185   -8.239  1.713   1.00 44.51 ? 21   GLU J OE1 1 
ATOM   10199 O  OE2 . GLU J  1 21  ? 2.597   -9.746  1.432   1.00 57.00 ? 21   GLU J OE2 1 
ATOM   10200 N  N   . GLN J  1 22  ? 5.531   -11.604 -2.855  1.00 30.04 ? 22   GLN J N   1 
ATOM   10201 C  CA  . GLN J  1 22  ? 5.182   -12.914 -3.371  1.00 33.14 ? 22   GLN J CA  1 
ATOM   10202 C  C   . GLN J  1 22  ? 5.243   -13.929 -2.253  1.00 40.49 ? 22   GLN J C   1 
ATOM   10203 O  O   . GLN J  1 22  ? 6.310   -14.460 -1.949  1.00 42.97 ? 22   GLN J O   1 
ATOM   10204 C  CB  . GLN J  1 22  ? 6.134   -13.319 -4.480  1.00 33.87 ? 22   GLN J CB  1 
ATOM   10205 C  CG  . GLN J  1 22  ? 5.732   -14.585 -5.180  1.00 33.88 ? 22   GLN J CG  1 
ATOM   10206 C  CD  . GLN J  1 22  ? 6.697   -14.942 -6.266  1.00 31.65 ? 22   GLN J CD  1 
ATOM   10207 O  OE1 . GLN J  1 22  ? 7.882   -14.668 -6.155  1.00 31.52 ? 22   GLN J OE1 1 
ATOM   10208 N  NE2 . GLN J  1 22  ? 6.200   -15.552 -7.329  1.00 33.84 ? 22   GLN J NE2 1 
ATOM   10209 N  N   . LYS J  1 23  ? 4.090   -14.202 -1.652  1.00 42.60 ? 23   LYS J N   1 
ATOM   10210 C  CA  . LYS J  1 23  ? 4.025   -15.035 -0.460  1.00 46.36 ? 23   LYS J CA  1 
ATOM   10211 C  C   . LYS J  1 23  ? 4.541   -16.456 -0.675  1.00 46.37 ? 23   LYS J C   1 
ATOM   10212 O  O   . LYS J  1 23  ? 5.162   -17.026 0.219   1.00 50.27 ? 23   LYS J O   1 
ATOM   10213 C  CB  . LYS J  1 23  ? 2.604   -15.050 0.112   1.00 49.15 ? 23   LYS J CB  1 
ATOM   10214 C  CG  . LYS J  1 23  ? 2.204   -13.754 0.817   1.00 51.19 ? 23   LYS J CG  1 
ATOM   10215 C  CD  . LYS J  1 23  ? 3.015   -13.540 2.092   1.00 56.52 ? 23   LYS J CD  1 
ATOM   10216 C  CE  . LYS J  1 23  ? 2.820   -14.700 3.080   1.00 65.22 ? 23   LYS J CE  1 
ATOM   10217 N  NZ  . LYS J  1 23  ? 3.478   -14.475 4.405   1.00 60.98 ? 23   LYS J NZ  1 
ATOM   10218 N  N   . GLU J  1 24  ? 4.296   -17.027 -1.850  1.00 44.36 ? 24   GLU J N   1 
ATOM   10219 C  CA  . GLU J  1 24  ? 4.729   -18.400 -2.113  1.00 49.32 ? 24   GLU J CA  1 
ATOM   10220 C  C   . GLU J  1 24  ? 5.523   -18.561 -3.395  1.00 49.49 ? 24   GLU J C   1 
ATOM   10221 O  O   . GLU J  1 24  ? 5.156   -18.022 -4.437  1.00 47.07 ? 24   GLU J O   1 
ATOM   10222 C  CB  . GLU J  1 24  ? 3.549   -19.385 -2.110  1.00 53.17 ? 24   GLU J CB  1 
ATOM   10223 C  CG  . GLU J  1 24  ? 3.210   -19.966 -0.726  1.00 59.46 ? 24   GLU J CG  1 
ATOM   10224 C  CD  . GLU J  1 24  ? 4.393   -20.683 -0.055  1.00 63.03 ? 24   GLU J CD  1 
ATOM   10225 O  OE1 . GLU J  1 24  ? 4.561   -20.529 1.183   1.00 56.76 ? 24   GLU J OE1 1 
ATOM   10226 O  OE2 . GLU J  1 24  ? 5.146   -21.403 -0.760  1.00 58.82 ? 24   GLU J OE2 1 
ATOM   10227 N  N   . SER J  1 25  ? 6.604   -19.330 -3.284  1.00 53.68 ? 25   SER J N   1 
ATOM   10228 C  CA  . SER J  1 25  ? 7.526   -19.650 -4.377  1.00 52.29 ? 25   SER J CA  1 
ATOM   10229 C  C   . SER J  1 25  ? 7.123   -19.119 -5.746  1.00 48.31 ? 25   SER J C   1 
ATOM   10230 O  O   . SER J  1 25  ? 7.572   -18.053 -6.154  1.00 51.16 ? 25   SER J O   1 
ATOM   10231 C  CB  . SER J  1 25  ? 7.762   -21.164 -4.446  1.00 53.38 ? 25   SER J CB  1 
ATOM   10232 O  OG  . SER J  1 25  ? 8.544   -21.507 -5.577  1.00 52.92 ? 25   SER J OG  1 
ATOM   10233 N  N   . ASN J  1 26  ? 6.295   -19.866 -6.464  1.00 48.15 ? 26   ASN J N   1 
ATOM   10234 C  CA  . ASN J  1 26  ? 5.860   -19.420 -7.785  1.00 51.62 ? 26   ASN J CA  1 
ATOM   10235 C  C   . ASN J  1 26  ? 4.393   -18.972 -7.813  1.00 49.94 ? 26   ASN J C   1 
ATOM   10236 O  O   . ASN J  1 26  ? 3.727   -19.057 -8.845  1.00 46.36 ? 26   ASN J O   1 
ATOM   10237 C  CB  . ASN J  1 26  ? 6.149   -20.487 -8.852  1.00 53.83 ? 26   ASN J CB  1 
ATOM   10238 C  CG  . ASN J  1 26  ? 7.643   -20.624 -9.161  1.00 59.81 ? 26   ASN J CG  1 
ATOM   10239 O  OD1 . ASN J  1 26  ? 8.380   -19.628 -9.230  1.00 56.38 ? 26   ASN J OD1 1 
ATOM   10240 N  ND2 . ASN J  1 26  ? 8.093   -21.863 -9.356  1.00 58.58 ? 26   ASN J ND2 1 
ATOM   10241 N  N   . GLY J  1 27  ? 3.910   -18.485 -6.670  1.00 48.11 ? 27   GLY J N   1 
ATOM   10242 C  CA  . GLY J  1 27  ? 2.563   -17.948 -6.550  1.00 43.42 ? 27   GLY J CA  1 
ATOM   10243 C  C   . GLY J  1 27  ? 2.427   -16.551 -7.134  1.00 41.68 ? 27   GLY J C   1 
ATOM   10244 O  O   . GLY J  1 27  ? 3.337   -16.062 -7.811  1.00 40.67 ? 27   GLY J O   1 
ATOM   10245 N  N   . PRO J  1 28  ? 1.282   -15.899 -6.885  1.00 42.26 ? 28   PRO J N   1 
ATOM   10246 C  CA  . PRO J  1 28  ? 1.032   -14.568 -7.447  1.00 38.60 ? 28   PRO J CA  1 
ATOM   10247 C  C   . PRO J  1 28  ? 1.835   -13.495 -6.727  1.00 31.26 ? 28   PRO J C   1 
ATOM   10248 O  O   . PRO J  1 28  ? 2.103   -13.596 -5.539  1.00 31.93 ? 28   PRO J O   1 
ATOM   10249 C  CB  . PRO J  1 28  ? -0.471  -14.345 -7.196  1.00 40.12 ? 28   PRO J CB  1 
ATOM   10250 C  CG  . PRO J  1 28  ? -1.021  -15.677 -6.771  1.00 46.63 ? 28   PRO J CG  1 
ATOM   10251 C  CD  . PRO J  1 28  ? 0.124   -16.403 -6.129  1.00 45.21 ? 28   PRO J CD  1 
ATOM   10252 N  N   . VAL J  1 29  ? 2.194   -12.461 -7.468  1.00 29.98 ? 29   VAL J N   1 
ATOM   10253 C  CA  . VAL J  1 29  ? 2.919   -11.319 -6.938  1.00 29.91 ? 29   VAL J CA  1 
ATOM   10254 C  C   . VAL J  1 29  ? 1.948   -10.145 -6.823  1.00 26.76 ? 29   VAL J C   1 
ATOM   10255 O  O   . VAL J  1 29  ? 1.322   -9.747  -7.797  1.00 27.76 ? 29   VAL J O   1 
ATOM   10256 C  CB  . VAL J  1 29  ? 4.092   -10.935 -7.880  1.00 28.08 ? 29   VAL J CB  1 
ATOM   10257 C  CG1 . VAL J  1 29  ? 4.760   -9.642  -7.442  1.00 25.20 ? 29   VAL J CG1 1 
ATOM   10258 C  CG2 . VAL J  1 29  ? 5.102   -12.075 -7.980  1.00 26.62 ? 29   VAL J CG2 1 
ATOM   10259 N  N   . LYS J  1 30  ? 1.801   -9.602  -5.630  1.00 24.86 ? 30   LYS J N   1 
ATOM   10260 C  CA  . LYS J  1 30  ? 1.012   -8.402  -5.478  1.00 25.01 ? 30   LYS J CA  1 
ATOM   10261 C  C   . LYS J  1 30  ? 1.892   -7.157  -5.627  1.00 26.30 ? 30   LYS J C   1 
ATOM   10262 O  O   . LYS J  1 30  ? 2.812   -6.935  -4.839  1.00 27.15 ? 30   LYS J O   1 
ATOM   10263 C  CB  . LYS J  1 30  ? 0.273   -8.383  -4.141  1.00 25.36 ? 30   LYS J CB  1 
ATOM   10264 C  CG  . LYS J  1 30  ? -0.095  -6.975  -3.730  1.00 27.39 ? 30   LYS J CG  1 
ATOM   10265 C  CD  . LYS J  1 30  ? -1.306  -6.904  -2.847  1.00 33.35 ? 30   LYS J CD  1 
ATOM   10266 C  CE  . LYS J  1 30  ? -2.061  -5.622  -3.159  1.00 35.56 ? 30   LYS J CE  1 
ATOM   10267 N  NZ  . LYS J  1 30  ? -2.305  -5.553  -4.640  1.00 30.20 ? 30   LYS J NZ  1 
ATOM   10268 N  N   . VAL J  1 31  ? 1.602   -6.362  -6.652  1.00 25.11 ? 31   VAL J N   1 
ATOM   10269 C  CA  . VAL J  1 31  ? 2.288   -5.104  -6.914  1.00 24.03 ? 31   VAL J CA  1 
ATOM   10270 C  C   . VAL J  1 31  ? 1.408   -3.936  -6.478  1.00 24.06 ? 31   VAL J C   1 
ATOM   10271 O  O   . VAL J  1 31  ? 0.320   -3.766  -7.000  1.00 26.59 ? 31   VAL J O   1 
ATOM   10272 C  CB  . VAL J  1 31  ? 2.552   -4.940  -8.420  1.00 22.55 ? 31   VAL J CB  1 
ATOM   10273 C  CG1 . VAL J  1 31  ? 3.323   -3.660  -8.695  1.00 19.53 ? 31   VAL J CG1 1 
ATOM   10274 C  CG2 . VAL J  1 31  ? 3.279   -6.161  -8.981  1.00 21.80 ? 31   VAL J CG2 1 
ATOM   10275 N  N   . TRP J  1 32  ? 1.853   -3.126  -5.530  1.00 22.02 ? 32   TRP J N   1 
ATOM   10276 C  CA  . TRP J  1 32  ? 1.034   -1.996  -5.117  1.00 21.99 ? 32   TRP J CA  1 
ATOM   10277 C  C   . TRP J  1 32  ? 1.916   -0.809  -4.797  1.00 20.99 ? 32   TRP J C   1 
ATOM   10278 O  O   . TRP J  1 32  ? 3.079   -0.971  -4.459  1.00 23.03 ? 32   TRP J O   1 
ATOM   10279 C  CB  . TRP J  1 32  ? 0.169   -2.361  -3.906  1.00 23.57 ? 32   TRP J CB  1 
ATOM   10280 C  CG  . TRP J  1 32  ? 0.901   -2.303  -2.600  1.00 22.00 ? 32   TRP J CG  1 
ATOM   10281 C  CD1 . TRP J  1 32  ? 0.932   -1.258  -1.724  1.00 24.95 ? 32   TRP J CD1 1 
ATOM   10282 C  CD2 . TRP J  1 32  ? 1.720   -3.330  -2.030  1.00 21.77 ? 32   TRP J CD2 1 
ATOM   10283 N  NE1 . TRP J  1 32  ? 1.719   -1.572  -0.638  1.00 27.08 ? 32   TRP J NE1 1 
ATOM   10284 C  CE2 . TRP J  1 32  ? 2.213   -2.838  -0.805  1.00 24.44 ? 32   TRP J CE2 1 
ATOM   10285 C  CE3 . TRP J  1 32  ? 2.086   -4.612  -2.439  1.00 24.89 ? 32   TRP J CE3 1 
ATOM   10286 C  CZ2 . TRP J  1 32  ? 3.049   -3.592  0.018   1.00 29.65 ? 32   TRP J CZ2 1 
ATOM   10287 C  CZ3 . TRP J  1 32  ? 2.919   -5.360  -1.621  1.00 27.00 ? 32   TRP J CZ3 1 
ATOM   10288 C  CH2 . TRP J  1 32  ? 3.392   -4.847  -0.406  1.00 29.26 ? 32   TRP J CH2 1 
ATOM   10289 N  N   . GLY J  1 33  ? 1.373   0.392   -4.887  1.00 20.55 ? 33   GLY J N   1 
ATOM   10290 C  CA  . GLY J  1 33  ? 2.182   1.557   -4.599  1.00 19.71 ? 33   GLY J CA  1 
ATOM   10291 C  C   . GLY J  1 33  ? 1.519   2.850   -4.992  1.00 20.55 ? 33   GLY J C   1 
ATOM   10292 O  O   . GLY J  1 33  ? 0.310   2.912   -5.183  1.00 23.28 ? 33   GLY J O   1 
ATOM   10293 N  N   . SER J  1 34  ? 2.319   3.895   -5.103  1.00 18.82 ? 34   SER J N   1 
ATOM   10294 C  CA  . SER J  1 34  ? 1.805   5.199   -5.464  1.00 21.58 ? 34   SER J CA  1 
ATOM   10295 C  C   . SER J  1 34  ? 2.797   5.879   -6.391  1.00 20.89 ? 34   SER J C   1 
ATOM   10296 O  O   . SER J  1 34  ? 3.991   5.750   -6.205  1.00 23.32 ? 34   SER J O   1 
ATOM   10297 C  CB  . SER J  1 34  ? 1.594   6.033   -4.208  1.00 25.26 ? 34   SER J CB  1 
ATOM   10298 O  OG  . SER J  1 34  ? 1.291   7.370   -4.542  1.00 32.74 ? 34   SER J OG  1 
ATOM   10299 N  N   . ILE J  1 35  ? 2.292   6.575   -7.403  1.00 21.17 ? 35   ILE J N   1 
ATOM   10300 C  CA  . ILE J  1 35  ? 3.101   7.361   -8.331  1.00 19.37 ? 35   ILE J CA  1 
ATOM   10301 C  C   . ILE J  1 35  ? 2.467   8.730   -8.443  1.00 19.15 ? 35   ILE J C   1 
ATOM   10302 O  O   . ILE J  1 35  ? 1.252   8.826   -8.598  1.00 19.04 ? 35   ILE J O   1 
ATOM   10303 C  CB  . ILE J  1 35  ? 3.103   6.761   -9.761  1.00 19.24 ? 35   ILE J CB  1 
ATOM   10304 C  CG1 . ILE J  1 35  ? 3.556   5.297   -9.756  1.00 18.00 ? 35   ILE J CG1 1 
ATOM   10305 C  CG2 . ILE J  1 35  ? 3.964   7.609   -10.693 1.00 16.59 ? 35   ILE J CG2 1 
ATOM   10306 C  CD1 . ILE J  1 35  ? 3.439   4.647   -11.109 1.00 16.49 ? 35   ILE J CD1 1 
ATOM   10307 N  N   . LYS J  1 36  ? 3.279   9.783   -8.389  1.00 20.24 ? 36   LYS J N   1 
ATOM   10308 C  CA  . LYS J  1 36  ? 2.783   11.151  -8.473  1.00 18.12 ? 36   LYS J CA  1 
ATOM   10309 C  C   . LYS J  1 36  ? 3.309   11.833  -9.727  1.00 19.00 ? 36   LYS J C   1 
ATOM   10310 O  O   . LYS J  1 36  ? 4.112   11.261  -10.463 1.00 18.43 ? 36   LYS J O   1 
ATOM   10311 C  CB  . LYS J  1 36  ? 3.199   11.945  -7.231  1.00 24.48 ? 36   LYS J CB  1 
ATOM   10312 C  CG  . LYS J  1 36  ? 4.651   12.439  -7.255  1.00 26.23 ? 36   LYS J CG  1 
ATOM   10313 C  CD  . LYS J  1 36  ? 5.041   13.136  -5.948  1.00 33.81 ? 36   LYS J CD  1 
ATOM   10314 C  CE  . LYS J  1 36  ? 4.847   12.206  -4.747  1.00 38.79 ? 36   LYS J CE  1 
ATOM   10315 N  NZ  . LYS J  1 36  ? 5.632   12.622  -3.541  1.00 40.52 ? 36   LYS J NZ  1 
ATOM   10316 N  N   . GLY J  1 37  ? 2.843   13.055  -9.974  1.00 21.25 ? 37   GLY J N   1 
ATOM   10317 C  CA  . GLY J  1 37  ? 3.325   13.871  -11.084 1.00 17.45 ? 37   GLY J CA  1 
ATOM   10318 C  C   . GLY J  1 37  ? 2.786   13.544  -12.459 1.00 17.63 ? 37   GLY J C   1 
ATOM   10319 O  O   . GLY J  1 37  ? 3.327   14.030  -13.452 1.00 19.96 ? 37   GLY J O   1 
ATOM   10320 N  N   . LEU J  1 38  ? 1.726   12.735  -12.529 1.00 18.17 ? 38   LEU J N   1 
ATOM   10321 C  CA  . LEU J  1 38  ? 1.200   12.228  -13.813 1.00 19.89 ? 38   LEU J CA  1 
ATOM   10322 C  C   . LEU J  1 38  ? 0.014   13.025  -14.384 1.00 19.88 ? 38   LEU J C   1 
ATOM   10323 O  O   . LEU J  1 38  ? -0.774  13.615  -13.651 1.00 19.63 ? 38   LEU J O   1 
ATOM   10324 C  CB  . LEU J  1 38  ? 0.795   10.748  -13.692 1.00 18.13 ? 38   LEU J CB  1 
ATOM   10325 C  CG  . LEU J  1 38  ? 1.898   9.694   -13.528 1.00 18.73 ? 38   LEU J CG  1 
ATOM   10326 C  CD1 . LEU J  1 38  ? 1.346   8.407   -12.958 1.00 17.77 ? 38   LEU J CD1 1 
ATOM   10327 C  CD2 . LEU J  1 38  ? 2.621   9.427   -14.853 1.00 18.01 ? 38   LEU J CD2 1 
ATOM   10328 N  N   . THR J  1 39  ? -0.112  13.043  -15.703 1.00 19.31 ? 39   THR J N   1 
ATOM   10329 C  CA  . THR J  1 39  ? -1.324  13.578  -16.300 1.00 21.49 ? 39   THR J CA  1 
ATOM   10330 C  C   . THR J  1 39  ? -2.470  12.600  -16.011 1.00 21.95 ? 39   THR J C   1 
ATOM   10331 O  O   . THR J  1 39  ? -2.247  11.384  -15.922 1.00 20.03 ? 39   THR J O   1 
ATOM   10332 C  CB  . THR J  1 39  ? -1.164  13.817  -17.811 1.00 21.61 ? 39   THR J CB  1 
ATOM   10333 O  OG1 . THR J  1 39  ? -0.760  12.602  -18.452 1.00 23.19 ? 39   THR J OG1 1 
ATOM   10334 C  CG2 . THR J  1 39  ? -0.122  14.902  -18.066 1.00 20.05 ? 39   THR J CG2 1 
ATOM   10335 N  N   . GLU J  1 40  ? -3.682  13.126  -15.834 1.00 21.37 ? 40   GLU J N   1 
ATOM   10336 C  CA  . GLU J  1 40  ? -4.811  12.285  -15.446 1.00 22.07 ? 40   GLU J CA  1 
ATOM   10337 C  C   . GLU J  1 40  ? -5.099  11.261  -16.519 1.00 19.15 ? 40   GLU J C   1 
ATOM   10338 O  O   . GLU J  1 40  ? -5.177  11.607  -17.677 1.00 20.12 ? 40   GLU J O   1 
ATOM   10339 C  CB  . GLU J  1 40  ? -6.071  13.117  -15.183 1.00 22.15 ? 40   GLU J CB  1 
ATOM   10340 C  CG  . GLU J  1 40  ? -7.286  12.262  -14.847 1.00 24.95 ? 40   GLU J CG  1 
ATOM   10341 C  CD  . GLU J  1 40  ? -8.513  13.070  -14.462 1.00 32.37 ? 40   GLU J CD  1 
ATOM   10342 O  OE1 . GLU J  1 40  ? -8.619  14.245  -14.898 1.00 34.35 ? 40   GLU J OE1 1 
ATOM   10343 O  OE2 . GLU J  1 40  ? -9.370  12.520  -13.728 1.00 35.39 ? 40   GLU J OE2 1 
ATOM   10344 N  N   . GLY J  1 41  ? -5.263  10.001  -16.129 1.00 20.19 ? 41   GLY J N   1 
ATOM   10345 C  CA  . GLY J  1 41  ? -5.610  8.953   -17.071 1.00 18.28 ? 41   GLY J CA  1 
ATOM   10346 C  C   . GLY J  1 41  ? -4.752  7.710   -16.985 1.00 17.58 ? 41   GLY J C   1 
ATOM   10347 O  O   . GLY J  1 41  ? -4.034  7.500   -16.021 1.00 18.52 ? 41   GLY J O   1 
ATOM   10348 N  N   . LEU J  1 42  ? -4.832  6.884   -18.021 1.00 23.05 ? 42   LEU J N   1 
ATOM   10349 C  CA  . LEU J  1 42  ? -4.100  5.616   -18.094 1.00 23.31 ? 42   LEU J CA  1 
ATOM   10350 C  C   . LEU J  1 42  ? -2.679  5.779   -18.654 1.00 19.24 ? 42   LEU J C   1 
ATOM   10351 O  O   . LEU J  1 42  ? -2.444  6.545   -19.592 1.00 17.09 ? 42   LEU J O   1 
ATOM   10352 C  CB  . LEU J  1 42  ? -4.891  4.583   -18.919 1.00 25.65 ? 42   LEU J CB  1 
ATOM   10353 C  CG  . LEU J  1 42  ? -6.287  4.157   -18.428 1.00 23.43 ? 42   LEU J CG  1 
ATOM   10354 C  CD1 . LEU J  1 42  ? -6.993  3.331   -19.496 1.00 25.14 ? 42   LEU J CD1 1 
ATOM   10355 C  CD2 . LEU J  1 42  ? -6.235  3.387   -17.104 1.00 20.90 ? 42   LEU J CD2 1 
ATOM   10356 N  N   . HIS J  1 43  ? -1.749  5.038   -18.059 1.00 19.53 ? 43   HIS J N   1 
ATOM   10357 C  CA  . HIS J  1 43  ? -0.318  5.159   -18.326 1.00 18.01 ? 43   HIS J CA  1 
ATOM   10358 C  C   . HIS J  1 43  ? 0.298   3.779   -18.309 1.00 18.57 ? 43   HIS J C   1 
ATOM   10359 O  O   . HIS J  1 43  ? 0.264   3.118   -17.283 1.00 19.62 ? 43   HIS J O   1 
ATOM   10360 C  CB  . HIS J  1 43  ? 0.356   5.948   -17.208 1.00 15.96 ? 43   HIS J CB  1 
ATOM   10361 C  CG  . HIS J  1 43  ? 0.066   7.412   -17.230 1.00 17.88 ? 43   HIS J CG  1 
ATOM   10362 N  ND1 . HIS J  1 43  ? 0.757   8.290   -18.032 1.00 17.14 ? 43   HIS J ND1 1 
ATOM   10363 C  CD2 . HIS J  1 43  ? -0.828  8.158   -16.537 1.00 16.68 ? 43   HIS J CD2 1 
ATOM   10364 C  CE1 . HIS J  1 43  ? 0.294   9.512   -17.845 1.00 18.26 ? 43   HIS J CE1 1 
ATOM   10365 N  NE2 . HIS J  1 43  ? -0.668  9.459   -16.940 1.00 17.61 ? 43   HIS J NE2 1 
ATOM   10366 N  N   . GLY J  1 44  ? 0.885   3.344   -19.414 1.00 18.92 ? 44   GLY J N   1 
ATOM   10367 C  CA  . GLY J  1 44  ? 1.557   2.055   -19.433 1.00 20.94 ? 44   GLY J CA  1 
ATOM   10368 C  C   . GLY J  1 44  ? 2.432   1.790   -18.213 1.00 20.53 ? 44   GLY J C   1 
ATOM   10369 O  O   . GLY J  1 44  ? 3.097   2.685   -17.697 1.00 19.13 ? 44   GLY J O   1 
ATOM   10370 N  N   . PHE J  1 45  ? 2.442   0.545   -17.756 1.00 19.00 ? 45   PHE J N   1 
ATOM   10371 C  CA  . PHE J  1 45  ? 3.199   0.173   -16.573 1.00 19.96 ? 45   PHE J CA  1 
ATOM   10372 C  C   . PHE J  1 45  ? 3.871   -1.182  -16.832 1.00 21.97 ? 45   PHE J C   1 
ATOM   10373 O  O   . PHE J  1 45  ? 3.199   -2.213  -16.822 1.00 21.66 ? 45   PHE J O   1 
ATOM   10374 C  CB  . PHE J  1 45  ? 2.249   0.096   -15.377 1.00 18.17 ? 45   PHE J CB  1 
ATOM   10375 C  CG  . PHE J  1 45  ? 2.935   -0.028  -14.057 1.00 20.04 ? 45   PHE J CG  1 
ATOM   10376 C  CD1 . PHE J  1 45  ? 3.920   0.887   -13.676 1.00 18.49 ? 45   PHE J CD1 1 
ATOM   10377 C  CD2 . PHE J  1 45  ? 2.569   -1.038  -13.164 1.00 21.53 ? 45   PHE J CD2 1 
ATOM   10378 C  CE1 . PHE J  1 45  ? 4.549   0.784   -12.438 1.00 17.89 ? 45   PHE J CE1 1 
ATOM   10379 C  CE2 . PHE J  1 45  ? 3.198   -1.149  -11.915 1.00 18.89 ? 45   PHE J CE2 1 
ATOM   10380 C  CZ  . PHE J  1 45  ? 4.188   -0.234  -11.557 1.00 19.50 ? 45   PHE J CZ  1 
ATOM   10381 N  N   . HIS J  1 46  ? 5.188   -1.176  -17.067 1.00 20.37 ? 46   HIS J N   1 
ATOM   10382 C  CA  . HIS J  1 46  ? 5.896   -2.375  -17.532 1.00 20.21 ? 46   HIS J CA  1 
ATOM   10383 C  C   . HIS J  1 46  ? 7.233   -2.652  -16.853 1.00 24.87 ? 46   HIS J C   1 
ATOM   10384 O  O   . HIS J  1 46  ? 7.967   -1.739  -16.469 1.00 22.70 ? 46   HIS J O   1 
ATOM   10385 C  CB  . HIS J  1 46  ? 6.148   -2.307  -19.034 1.00 22.59 ? 46   HIS J CB  1 
ATOM   10386 C  CG  . HIS J  1 46  ? 4.959   -1.867  -19.824 1.00 20.76 ? 46   HIS J CG  1 
ATOM   10387 N  ND1 . HIS J  1 46  ? 4.862   -0.608  -20.376 1.00 19.87 ? 46   HIS J ND1 1 
ATOM   10388 C  CD2 . HIS J  1 46  ? 3.812   -2.510  -20.140 1.00 20.19 ? 46   HIS J CD2 1 
ATOM   10389 C  CE1 . HIS J  1 46  ? 3.703   -0.495  -21.000 1.00 20.74 ? 46   HIS J CE1 1 
ATOM   10390 N  NE2 . HIS J  1 46  ? 3.046   -1.635  -20.869 1.00 21.74 ? 46   HIS J NE2 1 
ATOM   10391 N  N   . VAL J  1 47  ? 7.536   -3.938  -16.730 1.00 23.49 ? 47   VAL J N   1 
ATOM   10392 C  CA  . VAL J  1 47  ? 8.840   -4.389  -16.292 1.00 24.27 ? 47   VAL J CA  1 
ATOM   10393 C  C   . VAL J  1 47  ? 9.735   -4.445  -17.520 1.00 24.47 ? 47   VAL J C   1 
ATOM   10394 O  O   . VAL J  1 47  ? 9.446   -5.172  -18.472 1.00 24.67 ? 47   VAL J O   1 
ATOM   10395 C  CB  . VAL J  1 47  ? 8.760   -5.789  -15.650 1.00 23.47 ? 47   VAL J CB  1 
ATOM   10396 C  CG1 . VAL J  1 47  ? 10.144  -6.273  -15.255 1.00 23.98 ? 47   VAL J CG1 1 
ATOM   10397 C  CG2 . VAL J  1 47  ? 7.821   -5.770  -14.449 1.00 24.22 ? 47   VAL J CG2 1 
ATOM   10398 N  N   . HIS J  1 48  ? 10.804  -3.657  -17.511 1.00 23.71 ? 48   HIS J N   1 
ATOM   10399 C  CA  . HIS J  1 48  ? 11.751  -3.649  -18.615 1.00 22.96 ? 48   HIS J CA  1 
ATOM   10400 C  C   . HIS J  1 48  ? 12.945  -4.544  -18.326 1.00 23.60 ? 48   HIS J C   1 
ATOM   10401 O  O   . HIS J  1 48  ? 13.285  -4.788  -17.174 1.00 24.01 ? 48   HIS J O   1 
ATOM   10402 C  CB  . HIS J  1 48  ? 12.165  -2.220  -18.955 1.00 23.38 ? 48   HIS J CB  1 
ATOM   10403 C  CG  . HIS J  1 48  ? 11.118  -1.471  -19.723 1.00 24.81 ? 48   HIS J CG  1 
ATOM   10404 N  ND1 . HIS J  1 48  ? 11.256  -1.151  -21.060 1.00 25.14 ? 48   HIS J ND1 1 
ATOM   10405 C  CD2 . HIS J  1 48  ? 9.894   -1.022  -19.354 1.00 21.25 ? 48   HIS J CD2 1 
ATOM   10406 C  CE1 . HIS J  1 48  ? 10.175  -0.510  -21.471 1.00 23.95 ? 48   HIS J CE1 1 
ATOM   10407 N  NE2 . HIS J  1 48  ? 9.332   -0.421  -20.457 1.00 22.46 ? 48   HIS J NE2 1 
ATOM   10408 N  N   . GLU J  1 49  ? 13.583  -5.036  -19.380 1.00 26.68 ? 49   GLU J N   1 
ATOM   10409 C  CA  . GLU J  1 49  ? 14.543  -6.130  -19.241 1.00 25.55 ? 49   GLU J CA  1 
ATOM   10410 C  C   . GLU J  1 49  ? 15.753  -5.894  -18.319 1.00 23.98 ? 49   GLU J C   1 
ATOM   10411 O  O   . GLU J  1 49  ? 16.122  -6.762  -17.521 1.00 22.24 ? 49   GLU J O   1 
ATOM   10412 C  CB  . GLU J  1 49  ? 15.024  -6.591  -20.617 1.00 25.56 ? 49   GLU J CB  1 
ATOM   10413 C  CG  . GLU J  1 49  ? 15.457  -8.033  -20.601 1.00 26.03 ? 49   GLU J CG  1 
ATOM   10414 C  CD  . GLU J  1 49  ? 16.158  -8.418  -21.855 1.00 28.41 ? 49   GLU J CD  1 
ATOM   10415 O  OE1 . GLU J  1 49  ? 16.008  -7.680  -22.849 1.00 32.62 ? 49   GLU J OE1 1 
ATOM   10416 O  OE2 . GLU J  1 49  ? 16.861  -9.450  -21.846 1.00 30.93 ? 49   GLU J OE2 1 
ATOM   10417 N  N   . PHE J  1 50  ? 16.381  -4.731  -18.441 1.00 24.28 ? 50   PHE J N   1 
ATOM   10418 C  CA  . PHE J  1 50  ? 17.665  -4.502  -17.783 1.00 23.03 ? 50   PHE J CA  1 
ATOM   10419 C  C   . PHE J  1 50  ? 17.569  -3.522  -16.638 1.00 21.07 ? 50   PHE J C   1 
ATOM   10420 O  O   . PHE J  1 50  ? 16.939  -2.478  -16.759 1.00 22.75 ? 50   PHE J O   1 
ATOM   10421 C  CB  . PHE J  1 50  ? 18.704  -4.028  -18.807 1.00 23.77 ? 50   PHE J CB  1 
ATOM   10422 C  CG  . PHE J  1 50  ? 18.888  -4.983  -19.931 1.00 22.40 ? 50   PHE J CG  1 
ATOM   10423 C  CD1 . PHE J  1 50  ? 19.304  -6.279  -19.676 1.00 23.35 ? 50   PHE J CD1 1 
ATOM   10424 C  CD2 . PHE J  1 50  ? 18.603  -4.608  -21.228 1.00 24.74 ? 50   PHE J CD2 1 
ATOM   10425 C  CE1 . PHE J  1 50  ? 19.450  -7.187  -20.690 1.00 26.75 ? 50   PHE J CE1 1 
ATOM   10426 C  CE2 . PHE J  1 50  ? 18.747  -5.506  -22.267 1.00 28.62 ? 50   PHE J CE2 1 
ATOM   10427 C  CZ  . PHE J  1 50  ? 19.174  -6.806  -21.999 1.00 32.52 ? 50   PHE J CZ  1 
ATOM   10428 N  N   . GLY J  1 51  ? 18.200  -3.874  -15.525 1.00 21.72 ? 51   GLY J N   1 
ATOM   10429 C  CA  . GLY J  1 51  ? 18.257  -3.010  -14.357 1.00 22.45 ? 51   GLY J CA  1 
ATOM   10430 C  C   . GLY J  1 51  ? 19.402  -2.045  -14.548 1.00 24.81 ? 51   GLY J C   1 
ATOM   10431 O  O   . GLY J  1 51  ? 20.247  -1.867  -13.661 1.00 24.59 ? 51   GLY J O   1 
ATOM   10432 N  N   . ASP J  1 52  ? 19.419  -1.434  -15.728 1.00 19.48 ? 52   ASP J N   1 
ATOM   10433 C  CA  . ASP J  1 52  ? 20.485  -0.548  -16.151 1.00 22.81 ? 52   ASP J CA  1 
ATOM   10434 C  C   . ASP J  1 52  ? 19.942  0.877   -16.318 1.00 23.84 ? 52   ASP J C   1 
ATOM   10435 O  O   . ASP J  1 52  ? 19.065  1.122   -17.138 1.00 24.62 ? 52   ASP J O   1 
ATOM   10436 C  CB  . ASP J  1 52  ? 21.058  -1.084  -17.465 1.00 23.01 ? 52   ASP J CB  1 
ATOM   10437 C  CG  . ASP J  1 52  ? 22.213  -0.263  -17.992 1.00 24.98 ? 52   ASP J CG  1 
ATOM   10438 O  OD1 . ASP J  1 52  ? 22.444  0.849   -17.485 1.00 25.21 ? 52   ASP J OD1 1 
ATOM   10439 O  OD2 . ASP J  1 52  ? 22.894  -0.738  -18.927 1.00 27.48 ? 52   ASP J OD2 1 
ATOM   10440 N  N   . ASN J  1 53  ? 20.457  1.817   -15.537 1.00 23.01 ? 53   ASN J N   1 
ATOM   10441 C  CA  . ASN J  1 53  ? 19.988  3.197   -15.604 1.00 24.06 ? 53   ASN J CA  1 
ATOM   10442 C  C   . ASN J  1 53  ? 21.089  4.156   -16.049 1.00 25.72 ? 53   ASN J C   1 
ATOM   10443 O  O   . ASN J  1 53  ? 21.009  5.362   -15.825 1.00 26.96 ? 53   ASN J O   1 
ATOM   10444 C  CB  . ASN J  1 53  ? 19.445  3.631   -14.242 1.00 26.98 ? 53   ASN J CB  1 
ATOM   10445 C  CG  . ASN J  1 53  ? 18.941  5.071   -14.236 1.00 31.21 ? 53   ASN J CG  1 
ATOM   10446 O  OD1 . ASN J  1 53  ? 19.488  5.928   -13.538 1.00 34.68 ? 53   ASN J OD1 1 
ATOM   10447 N  ND2 . ASN J  1 53  ? 17.898  5.343   -15.018 1.00 32.40 ? 53   ASN J ND2 1 
ATOM   10448 N  N   . THR J  1 54  ? 22.119  3.618   -16.690 1.00 28.11 ? 54   THR J N   1 
ATOM   10449 C  CA  . THR J  1 54  ? 23.290  4.414   -17.055 1.00 27.66 ? 54   THR J CA  1 
ATOM   10450 C  C   . THR J  1 54  ? 22.959  5.553   -18.020 1.00 29.62 ? 54   THR J C   1 
ATOM   10451 O  O   . THR J  1 54  ? 23.450  6.670   -17.857 1.00 30.63 ? 54   THR J O   1 
ATOM   10452 C  CB  . THR J  1 54  ? 24.430  3.528   -17.602 1.00 26.32 ? 54   THR J CB  1 
ATOM   10453 O  OG1 . THR J  1 54  ? 23.946  2.729   -18.692 1.00 27.22 ? 54   THR J OG1 1 
ATOM   10454 C  CG2 . THR J  1 54  ? 24.969  2.617   -16.488 1.00 25.31 ? 54   THR J CG2 1 
ATOM   10455 N  N   . ALA J  1 55  ? 22.115  5.267   -19.010 1.00 30.56 ? 55   ALA J N   1 
ATOM   10456 C  CA  . ALA J  1 55  ? 21.614  6.291   -19.924 1.00 28.56 ? 55   ALA J CA  1 
ATOM   10457 C  C   . ALA J  1 55  ? 20.146  6.629   -19.644 1.00 29.40 ? 55   ALA J C   1 
ATOM   10458 O  O   . ALA J  1 55  ? 19.345  6.731   -20.566 1.00 31.90 ? 55   ALA J O   1 
ATOM   10459 C  CB  . ALA J  1 55  ? 21.780  5.836   -21.365 1.00 29.28 ? 55   ALA J CB  1 
ATOM   10460 N  N   . GLY J  1 56  ? 19.801  6.811   -18.372 1.00 32.00 ? 56   GLY J N   1 
ATOM   10461 C  CA  . GLY J  1 56  ? 18.427  7.061   -17.977 1.00 29.38 ? 56   GLY J CA  1 
ATOM   10462 C  C   . GLY J  1 56  ? 17.552  5.843   -18.200 1.00 30.50 ? 56   GLY J C   1 
ATOM   10463 O  O   . GLY J  1 56  ? 18.022  4.712   -18.131 1.00 30.78 ? 56   GLY J O   1 
ATOM   10464 N  N   . CYS J  1 57  ? 16.275  6.073   -18.485 1.00 31.16 ? 57   CYS J N   1 
ATOM   10465 C  CA  . CYS J  1 57  ? 15.328  4.986   -18.692 1.00 27.19 ? 57   CYS J CA  1 
ATOM   10466 C  C   . CYS J  1 57  ? 15.597  4.182   -19.962 1.00 26.24 ? 57   CYS J C   1 
ATOM   10467 O  O   . CYS J  1 57  ? 15.280  2.995   -20.026 1.00 25.93 ? 57   CYS J O   1 
ATOM   10468 C  CB  . CYS J  1 57  ? 13.893  5.524   -18.697 1.00 29.23 ? 57   CYS J CB  1 
ATOM   10469 S  SG  . CYS J  1 57  ? 13.352  6.260   -17.130 1.00 33.26 ? 57   CYS J SG  1 
ATOM   10470 N  N   . THR J  1 58  ? 16.175  4.823   -20.971 1.00 28.68 ? 58   THR J N   1 
ATOM   10471 C  CA  . THR J  1 58  ? 16.428  4.149   -22.243 1.00 28.19 ? 58   THR J CA  1 
ATOM   10472 C  C   . THR J  1 58  ? 17.254  2.867   -22.094 1.00 27.47 ? 58   THR J C   1 
ATOM   10473 O  O   . THR J  1 58  ? 17.089  1.922   -22.886 1.00 24.00 ? 58   THR J O   1 
ATOM   10474 C  CB  . THR J  1 58  ? 17.121  5.092   -23.252 1.00 28.45 ? 58   THR J CB  1 
ATOM   10475 O  OG1 . THR J  1 58  ? 16.327  6.270   -23.426 1.00 34.21 ? 58   THR J OG1 1 
ATOM   10476 C  CG2 . THR J  1 58  ? 17.300  4.412   -24.607 1.00 26.34 ? 58   THR J CG2 1 
ATOM   10477 N  N   . SER J  1 59  ? 18.130  2.844   -21.080 1.00 27.41 ? 59   SER J N   1 
ATOM   10478 C  CA  . SER J  1 59  ? 19.064  1.728   -20.858 1.00 24.02 ? 59   SER J CA  1 
ATOM   10479 C  C   . SER J  1 59  ? 18.358  0.495   -20.332 1.00 22.75 ? 59   SER J C   1 
ATOM   10480 O  O   . SER J  1 59  ? 18.969  -0.554  -20.172 1.00 24.22 ? 59   SER J O   1 
ATOM   10481 C  CB  . SER J  1 59  ? 20.167  2.117   -19.879 1.00 25.16 ? 59   SER J CB  1 
ATOM   10482 O  OG  . SER J  1 59  ? 20.393  3.508   -19.921 1.00 27.06 ? 59   SER J OG  1 
ATOM   10483 N  N   . ALA J  1 60  ? 17.063  0.608   -20.080 1.00 24.05 ? 60   ALA J N   1 
ATOM   10484 C  CA  . ALA J  1 60  ? 16.323  -0.517  -19.539 1.00 24.01 ? 60   ALA J CA  1 
ATOM   10485 C  C   . ALA J  1 60  ? 16.019  -1.564  -20.607 1.00 23.97 ? 60   ALA J C   1 
ATOM   10486 O  O   . ALA J  1 60  ? 15.743  -2.714  -20.289 1.00 25.75 ? 60   ALA J O   1 
ATOM   10487 C  CB  . ALA J  1 60  ? 15.048  -0.038  -18.866 1.00 22.78 ? 60   ALA J CB  1 
ATOM   10488 N  N   . GLY J  1 61  ? 16.086  -1.178  -21.874 1.00 24.96 ? 61   GLY J N   1 
ATOM   10489 C  CA  . GLY J  1 61  ? 15.747  -2.099  -22.947 1.00 25.38 ? 61   GLY J CA  1 
ATOM   10490 C  C   . GLY J  1 61  ? 14.241  -2.286  -23.116 1.00 27.08 ? 61   GLY J C   1 
ATOM   10491 O  O   . GLY J  1 61  ? 13.448  -1.523  -22.562 1.00 27.53 ? 61   GLY J O   1 
ATOM   10492 N  N   . PRO J  1 62  ? 13.834  -3.311  -23.884 1.00 28.81 ? 62   PRO J N   1 
ATOM   10493 C  CA  . PRO J  1 62  ? 12.410  -3.543  -24.145 1.00 27.52 ? 62   PRO J CA  1 
ATOM   10494 C  C   . PRO J  1 62  ? 11.699  -4.109  -22.927 1.00 25.97 ? 62   PRO J C   1 
ATOM   10495 O  O   . PRO J  1 62  ? 12.338  -4.359  -21.904 1.00 26.51 ? 62   PRO J O   1 
ATOM   10496 C  CB  . PRO J  1 62  ? 12.415  -4.601  -25.266 1.00 27.61 ? 62   PRO J CB  1 
ATOM   10497 C  CG  . PRO J  1 62  ? 13.844  -4.782  -25.675 1.00 24.81 ? 62   PRO J CG  1 
ATOM   10498 C  CD  . PRO J  1 62  ? 14.684  -4.325  -24.533 1.00 28.74 ? 62   PRO J CD  1 
ATOM   10499 N  N   . HIS J  1 63  ? 10.392  -4.323  -23.044 1.00 24.04 ? 63   HIS J N   1 
ATOM   10500 C  CA  . HIS J  1 63  ? 9.659   -5.002  -21.994 1.00 25.78 ? 63   HIS J CA  1 
ATOM   10501 C  C   . HIS J  1 63  ? 10.293  -6.366  -21.794 1.00 26.94 ? 63   HIS J C   1 
ATOM   10502 O  O   . HIS J  1 63  ? 10.634  -7.045  -22.756 1.00 27.78 ? 63   HIS J O   1 
ATOM   10503 C  CB  . HIS J  1 63  ? 8.170   -5.159  -22.337 1.00 26.10 ? 63   HIS J CB  1 
ATOM   10504 C  CG  . HIS J  1 63  ? 7.473   -3.869  -22.646 1.00 23.17 ? 63   HIS J CG  1 
ATOM   10505 N  ND1 . HIS J  1 63  ? 6.272   -3.817  -23.323 1.00 24.56 ? 63   HIS J ND1 1 
ATOM   10506 C  CD2 . HIS J  1 63  ? 7.816   -2.586  -22.392 1.00 22.48 ? 63   HIS J CD2 1 
ATOM   10507 C  CE1 . HIS J  1 63  ? 5.901   -2.558  -23.468 1.00 24.69 ? 63   HIS J CE1 1 
ATOM   10508 N  NE2 . HIS J  1 63  ? 6.823   -1.790  -22.916 1.00 25.27 ? 63   HIS J NE2 1 
ATOM   10509 N  N   . PHE J  1 64  ? 10.452  -6.753  -20.535 1.00 26.07 ? 64   PHE J N   1 
ATOM   10510 C  CA  . PHE J  1 64  ? 10.996  -8.055  -20.178 1.00 28.00 ? 64   PHE J CA  1 
ATOM   10511 C  C   . PHE J  1 64  ? 10.234  -9.164  -20.921 1.00 30.84 ? 64   PHE J C   1 
ATOM   10512 O  O   . PHE J  1 64  ? 9.023   -9.332  -20.733 1.00 28.81 ? 64   PHE J O   1 
ATOM   10513 C  CB  . PHE J  1 64  ? 10.920  -8.225  -18.661 1.00 23.82 ? 64   PHE J CB  1 
ATOM   10514 C  CG  . PHE J  1 64  ? 11.425  -9.535  -18.165 1.00 25.31 ? 64   PHE J CG  1 
ATOM   10515 C  CD1 . PHE J  1 64  ? 12.530  -10.131 -18.736 1.00 29.30 ? 64   PHE J CD1 1 
ATOM   10516 C  CD2 . PHE J  1 64  ? 10.810  -10.160 -17.098 1.00 25.53 ? 64   PHE J CD2 1 
ATOM   10517 C  CE1 . PHE J  1 64  ? 12.998  -11.351 -18.263 1.00 28.19 ? 64   PHE J CE1 1 
ATOM   10518 C  CE2 . PHE J  1 64  ? 11.272  -11.366 -16.623 1.00 29.20 ? 64   PHE J CE2 1 
ATOM   10519 C  CZ  . PHE J  1 64  ? 12.369  -11.963 -17.204 1.00 27.89 ? 64   PHE J CZ  1 
ATOM   10520 N  N   . ASN J  1 65  ? 10.943  -9.902  -21.776 1.00 31.25 ? 65   ASN J N   1 
ATOM   10521 C  CA  . ASN J  1 65  ? 10.306  -10.894 -22.641 1.00 32.84 ? 65   ASN J CA  1 
ATOM   10522 C  C   . ASN J  1 65  ? 11.078  -12.222 -22.735 1.00 32.76 ? 65   ASN J C   1 
ATOM   10523 O  O   . ASN J  1 65  ? 11.581  -12.581 -23.799 1.00 34.28 ? 65   ASN J O   1 
ATOM   10524 C  CB  . ASN J  1 65  ? 10.083  -10.294 -24.031 1.00 30.06 ? 65   ASN J CB  1 
ATOM   10525 C  CG  . ASN J  1 65  ? 9.113   -11.104 -24.881 1.00 32.43 ? 65   ASN J CG  1 
ATOM   10526 O  OD1 . ASN J  1 65  ? 8.366   -11.955 -24.377 1.00 29.60 ? 65   ASN J OD1 1 
ATOM   10527 N  ND2 . ASN J  1 65  ? 9.117   -10.833 -26.186 1.00 28.09 ? 65   ASN J ND2 1 
ATOM   10528 N  N   . PRO J  1 66  ? 11.134  -12.969 -21.622 1.00 31.05 ? 66   PRO J N   1 
ATOM   10529 C  CA  . PRO J  1 66  ? 11.875  -14.229 -21.492 1.00 34.00 ? 66   PRO J CA  1 
ATOM   10530 C  C   . PRO J  1 66  ? 11.403  -15.294 -22.486 1.00 38.74 ? 66   PRO J C   1 
ATOM   10531 O  O   . PRO J  1 66  ? 12.227  -16.055 -22.997 1.00 39.23 ? 66   PRO J O   1 
ATOM   10532 C  CB  . PRO J  1 66  ? 11.536  -14.706 -20.071 1.00 36.20 ? 66   PRO J CB  1 
ATOM   10533 C  CG  . PRO J  1 66  ? 10.809  -13.592 -19.413 1.00 33.29 ? 66   PRO J CG  1 
ATOM   10534 C  CD  . PRO J  1 66  ? 10.242  -12.728 -20.477 1.00 31.03 ? 66   PRO J CD  1 
ATOM   10535 N  N   . LEU J  1 67  ? 10.095  -15.349 -22.741 1.00 38.55 ? 67   LEU J N   1 
ATOM   10536 C  CA  . LEU J  1 67  ? 9.505   -16.394 -23.580 1.00 36.07 ? 67   LEU J CA  1 
ATOM   10537 C  C   . LEU J  1 67  ? 9.302   -15.962 -25.041 1.00 35.63 ? 67   LEU J C   1 
ATOM   10538 O  O   . LEU J  1 67  ? 8.582   -16.613 -25.794 1.00 39.02 ? 67   LEU J O   1 
ATOM   10539 C  CB  . LEU J  1 67  ? 8.191   -16.898 -22.960 1.00 35.92 ? 67   LEU J CB  1 
ATOM   10540 C  CG  . LEU J  1 67  ? 8.295   -17.487 -21.544 1.00 32.98 ? 67   LEU J CG  1 
ATOM   10541 C  CD1 . LEU J  1 67  ? 6.942   -17.859 -20.966 1.00 33.65 ? 67   LEU J CD1 1 
ATOM   10542 C  CD2 . LEU J  1 67  ? 9.211   -18.692 -21.531 1.00 37.88 ? 67   LEU J CD2 1 
ATOM   10543 N  N   . SER J  1 68  ? 9.952   -14.867 -25.429 1.00 34.46 ? 68   SER J N   1 
ATOM   10544 C  CA  . SER J  1 68  ? 9.915   -14.347 -26.802 1.00 36.50 ? 68   SER J CA  1 
ATOM   10545 C  C   . SER J  1 68  ? 8.533   -14.385 -27.463 1.00 37.34 ? 68   SER J C   1 
ATOM   10546 O  O   . SER J  1 68  ? 8.215   -15.294 -28.230 1.00 41.46 ? 68   SER J O   1 
ATOM   10547 C  CB  . SER J  1 68  ? 10.967  -15.046 -27.670 1.00 44.03 ? 68   SER J CB  1 
ATOM   10548 O  OG  . SER J  1 68  ? 12.284  -14.730 -27.234 1.00 43.61 ? 68   SER J OG  1 
ATOM   10549 N  N   . ARG J  1 69  ? 7.730   -13.367 -27.163 1.00 39.73 ? 69   ARG J N   1 
ATOM   10550 C  CA  . ARG J  1 69  ? 6.318   -13.306 -27.533 1.00 35.83 ? 69   ARG J CA  1 
ATOM   10551 C  C   . ARG J  1 69  ? 5.931   -11.881 -27.882 1.00 35.48 ? 69   ARG J C   1 
ATOM   10552 O  O   . ARG J  1 69  ? 6.776   -10.981 -27.857 1.00 34.20 ? 69   ARG J O   1 
ATOM   10553 C  CB  . ARG J  1 69  ? 5.441   -13.793 -26.381 1.00 36.33 ? 69   ARG J CB  1 
ATOM   10554 C  CG  . ARG J  1 69  ? 5.384   -15.302 -26.241 1.00 40.62 ? 69   ARG J CG  1 
ATOM   10555 C  CD  . ARG J  1 69  ? 4.405   -15.714 -25.166 1.00 43.97 ? 69   ARG J CD  1 
ATOM   10556 N  NE  . ARG J  1 69  ? 4.195   -17.159 -25.147 1.00 53.30 ? 69   ARG J NE  1 
ATOM   10557 C  CZ  . ARG J  1 69  ? 3.663   -17.824 -24.125 1.00 50.52 ? 69   ARG J CZ  1 
ATOM   10558 N  NH1 . ARG J  1 69  ? 3.287   -17.175 -23.030 1.00 50.73 ? 69   ARG J NH1 1 
ATOM   10559 N  NH2 . ARG J  1 69  ? 3.514   -19.140 -24.195 1.00 55.94 ? 69   ARG J NH2 1 
ATOM   10560 N  N   . LYS J  1 70  ? 4.655   -11.684 -28.208 1.00 34.74 ? 70   LYS J N   1 
ATOM   10561 C  CA  . LYS J  1 70  ? 4.152   -10.374 -28.610 1.00 35.31 ? 70   LYS J CA  1 
ATOM   10562 C  C   . LYS J  1 70  ? 3.522   -9.607  -27.441 1.00 32.40 ? 70   LYS J C   1 
ATOM   10563 O  O   . LYS J  1 70  ? 3.211   -10.182 -26.399 1.00 32.68 ? 70   LYS J O   1 
ATOM   10564 C  CB  . LYS J  1 70  ? 3.136   -10.505 -29.750 1.00 37.86 ? 70   LYS J CB  1 
ATOM   10565 C  CG  . LYS J  1 70  ? 3.711   -10.875 -31.118 1.00 39.90 ? 70   LYS J CG  1 
ATOM   10566 C  CD  . LYS J  1 70  ? 2.745   -10.432 -32.226 1.00 43.13 ? 70   LYS J CD  1 
ATOM   10567 C  CE  . LYS J  1 70  ? 2.994   -11.138 -33.553 1.00 51.35 ? 70   LYS J CE  1 
ATOM   10568 N  NZ  . LYS J  1 70  ? 2.448   -12.534 -33.580 1.00 55.15 ? 70   LYS J NZ  1 
ATOM   10569 N  N   . HIS J  1 71  ? 3.322   -8.306  -27.627 1.00 32.67 ? 71   HIS J N   1 
ATOM   10570 C  CA  . HIS J  1 71  ? 2.759   -7.471  -26.570 1.00 29.59 ? 71   HIS J CA  1 
ATOM   10571 C  C   . HIS J  1 71  ? 1.271   -7.718  -26.365 1.00 30.34 ? 71   HIS J C   1 
ATOM   10572 O  O   . HIS J  1 71  ? 0.503   -7.886  -27.317 1.00 31.14 ? 71   HIS J O   1 
ATOM   10573 C  CB  . HIS J  1 71  ? 3.003   -5.981  -26.841 1.00 29.84 ? 71   HIS J CB  1 
ATOM   10574 C  CG  . HIS J  1 71  ? 2.474   -5.079  -25.768 1.00 28.66 ? 71   HIS J CG  1 
ATOM   10575 N  ND1 . HIS J  1 71  ? 3.181   -4.793  -24.621 1.00 30.40 ? 71   HIS J ND1 1 
ATOM   10576 C  CD2 . HIS J  1 71  ? 1.303   -4.406  -25.663 1.00 31.16 ? 71   HIS J CD2 1 
ATOM   10577 C  CE1 . HIS J  1 71  ? 2.470   -3.983  -23.853 1.00 27.33 ? 71   HIS J CE1 1 
ATOM   10578 N  NE2 . HIS J  1 71  ? 1.326   -3.735  -24.462 1.00 29.33 ? 71   HIS J NE2 1 
ATOM   10579 N  N   . GLY J  1 72  ? 0.873   -7.731  -25.100 1.00 31.63 ? 72   GLY J N   1 
ATOM   10580 C  CA  . GLY J  1 72  ? -0.519  -7.874  -24.723 1.00 30.70 ? 72   GLY J CA  1 
ATOM   10581 C  C   . GLY J  1 72  ? -0.704  -7.230  -23.371 1.00 28.53 ? 72   GLY J C   1 
ATOM   10582 O  O   . GLY J  1 72  ? 0.193   -6.546  -22.874 1.00 28.57 ? 72   GLY J O   1 
ATOM   10583 N  N   . GLY J  1 73  ? -1.867  -7.443  -22.773 1.00 28.50 ? 73   GLY J N   1 
ATOM   10584 C  CA  . GLY J  1 73  ? -2.120  -6.963  -21.430 1.00 27.61 ? 73   GLY J CA  1 
ATOM   10585 C  C   . GLY J  1 73  ? -1.911  -8.079  -20.431 1.00 27.76 ? 73   GLY J C   1 
ATOM   10586 O  O   . GLY J  1 73  ? -1.680  -9.229  -20.805 1.00 28.46 ? 73   GLY J O   1 
ATOM   10587 N  N   . PRO J  1 74  ? -1.999  -7.743  -19.146 1.00 26.89 ? 74   PRO J N   1 
ATOM   10588 C  CA  . PRO J  1 74  ? -1.837  -8.684  -18.038 1.00 28.71 ? 74   PRO J CA  1 
ATOM   10589 C  C   . PRO J  1 74  ? -2.682  -9.958  -18.203 1.00 32.34 ? 74   PRO J C   1 
ATOM   10590 O  O   . PRO J  1 74  ? -2.203  -11.057 -17.908 1.00 32.76 ? 74   PRO J O   1 
ATOM   10591 C  CB  . PRO J  1 74  ? -2.333  -7.879  -16.840 1.00 26.50 ? 74   PRO J CB  1 
ATOM   10592 C  CG  . PRO J  1 74  ? -2.104  -6.480  -17.214 1.00 24.13 ? 74   PRO J CG  1 
ATOM   10593 C  CD  . PRO J  1 74  ? -2.320  -6.388  -18.682 1.00 24.72 ? 74   PRO J CD  1 
ATOM   10594 N  N   . LYS J  1 75  ? -3.916  -9.812  -18.682 1.00 34.48 ? 75   LYS J N   1 
ATOM   10595 C  CA  . LYS J  1 75  ? -4.869  -10.926 -18.724 1.00 33.63 ? 75   LYS J CA  1 
ATOM   10596 C  C   . LYS J  1 75  ? -4.896  -11.690 -20.055 1.00 33.46 ? 75   LYS J C   1 
ATOM   10597 O  O   . LYS J  1 75  ? -5.730  -12.572 -20.266 1.00 34.81 ? 75   LYS J O   1 
ATOM   10598 C  CB  . LYS J  1 75  ? -6.265  -10.415 -18.386 1.00 33.72 ? 75   LYS J CB  1 
ATOM   10599 C  CG  . LYS J  1 75  ? -6.367  -9.770  -17.005 1.00 33.79 ? 75   LYS J CG  1 
ATOM   10600 C  CD  . LYS J  1 75  ? -6.876  -10.750 -15.956 1.00 40.90 ? 75   LYS J CD  1 
ATOM   10601 C  CE  . LYS J  1 75  ? -8.410  -10.813 -15.945 1.00 44.48 ? 75   LYS J CE  1 
ATOM   10602 N  NZ  . LYS J  1 75  ? -8.936  -11.930 -15.098 1.00 42.04 ? 75   LYS J NZ  1 
ATOM   10603 N  N   . ASP J  1 76  ? -3.982  -11.345 -20.952 1.00 34.96 ? 76   ASP J N   1 
ATOM   10604 C  CA  . ASP J  1 76  ? -3.846  -12.052 -22.221 1.00 35.84 ? 76   ASP J CA  1 
ATOM   10605 C  C   . ASP J  1 76  ? -2.893  -13.227 -22.053 1.00 37.87 ? 76   ASP J C   1 
ATOM   10606 O  O   . ASP J  1 76  ? -2.071  -13.241 -21.134 1.00 39.23 ? 76   ASP J O   1 
ATOM   10607 C  CB  . ASP J  1 76  ? -3.348  -11.095 -23.305 1.00 32.42 ? 76   ASP J CB  1 
ATOM   10608 C  CG  . ASP J  1 76  ? -4.348  -10.005 -23.607 1.00 33.37 ? 76   ASP J CG  1 
ATOM   10609 O  OD1 . ASP J  1 76  ? -5.555  -10.308 -23.601 1.00 42.63 ? 76   ASP J OD1 1 
ATOM   10610 O  OD2 . ASP J  1 76  ? -3.951  -8.848  -23.844 1.00 35.09 ? 76   ASP J OD2 1 
ATOM   10611 N  N   . GLU J  1 77  ? -3.014  -14.229 -22.913 1.00 40.17 ? 77   GLU J N   1 
ATOM   10612 C  CA  . GLU J  1 77  ? -2.086  -15.347 -22.855 1.00 41.63 ? 77   GLU J CA  1 
ATOM   10613 C  C   . GLU J  1 77  ? -0.815  -14.962 -23.591 1.00 42.35 ? 77   GLU J C   1 
ATOM   10614 O  O   . GLU J  1 77  ? 0.293   -15.132 -23.064 1.00 43.43 ? 77   GLU J O   1 
ATOM   10615 C  CB  . GLU J  1 77  ? -2.698  -16.611 -23.446 1.00 47.53 ? 77   GLU J CB  1 
ATOM   10616 C  CG  . GLU J  1 77  ? -3.745  -17.254 -22.562 1.00 52.84 ? 77   GLU J CG  1 
ATOM   10617 C  CD  . GLU J  1 77  ? -3.571  -18.756 -22.475 1.00 66.51 ? 77   GLU J CD  1 
ATOM   10618 O  OE1 . GLU J  1 77  ? -4.591  -19.467 -22.321 1.00 67.85 ? 77   GLU J OE1 1 
ATOM   10619 O  OE2 . GLU J  1 77  ? -2.407  -19.219 -22.561 1.00 67.18 ? 77   GLU J OE2 1 
ATOM   10620 N  N   . GLU J  1 78  ? -0.982  -14.452 -24.813 1.00 40.96 ? 78   GLU J N   1 
ATOM   10621 C  CA  . GLU J  1 78  ? 0.104   -13.785 -25.515 1.00 38.69 ? 78   GLU J CA  1 
ATOM   10622 C  C   . GLU J  1 78  ? 0.389   -12.462 -24.819 1.00 38.23 ? 78   GLU J C   1 
ATOM   10623 O  O   . GLU J  1 78  ? -0.378  -11.501 -24.940 1.00 35.35 ? 78   GLU J O   1 
ATOM   10624 C  CB  . GLU J  1 78  ? -0.224  -13.533 -26.996 1.00 38.85 ? 78   GLU J CB  1 
ATOM   10625 C  CG  . GLU J  1 78  ? 0.283   -14.613 -27.957 1.00 46.26 ? 78   GLU J CG  1 
ATOM   10626 C  CD  . GLU J  1 78  ? 1.788   -14.523 -28.259 1.00 51.18 ? 78   GLU J CD  1 
ATOM   10627 O  OE1 . GLU J  1 78  ? 2.221   -13.528 -28.889 1.00 49.02 ? 78   GLU J OE1 1 
ATOM   10628 O  OE2 . GLU J  1 78  ? 2.533   -15.468 -27.896 1.00 50.13 ? 78   GLU J OE2 1 
ATOM   10629 N  N   . ARG J  1 79  ? 1.486   -12.430 -24.072 1.00 35.19 ? 79   ARG J N   1 
ATOM   10630 C  CA  . ARG J  1 79  ? 1.999   -11.187 -23.524 1.00 32.35 ? 79   ARG J CA  1 
ATOM   10631 C  C   . ARG J  1 79  ? 3.499   -11.345 -23.329 1.00 33.72 ? 79   ARG J C   1 
ATOM   10632 O  O   . ARG J  1 79  ? 4.023   -12.461 -23.401 1.00 32.33 ? 79   ARG J O   1 
ATOM   10633 C  CB  . ARG J  1 79  ? 1.307   -10.847 -22.193 1.00 30.30 ? 79   ARG J CB  1 
ATOM   10634 C  CG  . ARG J  1 79  ? 1.261   -12.006 -21.211 1.00 30.62 ? 79   ARG J CG  1 
ATOM   10635 C  CD  . ARG J  1 79  ? 0.745   -11.592 -19.863 1.00 30.02 ? 79   ARG J CD  1 
ATOM   10636 N  NE  . ARG J  1 79  ? 1.781   -11.024 -19.000 1.00 29.44 ? 79   ARG J NE  1 
ATOM   10637 C  CZ  . ARG J  1 79  ? 1.638   -10.869 -17.686 1.00 28.21 ? 79   ARG J CZ  1 
ATOM   10638 N  NH1 . ARG J  1 79  ? 0.511   -11.243 -17.102 1.00 28.95 ? 79   ARG J NH1 1 
ATOM   10639 N  NH2 . ARG J  1 79  ? 2.619   -10.355 -16.953 1.00 28.42 ? 79   ARG J NH2 1 
ATOM   10640 N  N   . HIS J  1 80  ? 4.180   -10.220 -23.125 1.00 29.93 ? 80   HIS J N   1 
ATOM   10641 C  CA  . HIS J  1 80  ? 5.503   -10.215 -22.530 1.00 27.98 ? 80   HIS J CA  1 
ATOM   10642 C  C   . HIS J  1 80  ? 5.324   -10.488 -21.038 1.00 29.31 ? 80   HIS J C   1 
ATOM   10643 O  O   . HIS J  1 80  ? 4.245   -10.254 -20.493 1.00 30.18 ? 80   HIS J O   1 
ATOM   10644 C  CB  . HIS J  1 80  ? 6.149   -8.846  -22.729 1.00 28.53 ? 80   HIS J CB  1 
ATOM   10645 C  CG  . HIS J  1 80  ? 6.318   -8.457  -24.165 1.00 28.80 ? 80   HIS J CG  1 
ATOM   10646 N  ND1 . HIS J  1 80  ? 6.090   -7.178  -24.622 1.00 27.44 ? 80   HIS J ND1 1 
ATOM   10647 C  CD2 . HIS J  1 80  ? 6.703   -9.176  -25.245 1.00 30.50 ? 80   HIS J CD2 1 
ATOM   10648 C  CE1 . HIS J  1 80  ? 6.324   -7.124  -25.921 1.00 29.18 ? 80   HIS J CE1 1 
ATOM   10649 N  NE2 . HIS J  1 80  ? 6.696   -8.325  -26.325 1.00 31.14 ? 80   HIS J NE2 1 
ATOM   10650 N  N   . VAL J  1 81  ? 6.358   -10.989 -20.367 1.00 32.47 ? 81   VAL J N   1 
ATOM   10651 C  CA  . VAL J  1 81  ? 6.263   -11.233 -18.925 1.00 27.79 ? 81   VAL J CA  1 
ATOM   10652 C  C   . VAL J  1 81  ? 6.108   -9.923  -18.142 1.00 26.73 ? 81   VAL J C   1 
ATOM   10653 O  O   . VAL J  1 81  ? 5.413   -9.877  -17.121 1.00 29.01 ? 81   VAL J O   1 
ATOM   10654 C  CB  . VAL J  1 81  ? 7.448   -12.087 -18.398 1.00 29.34 ? 81   VAL J CB  1 
ATOM   10655 C  CG1 . VAL J  1 81  ? 7.620   -11.944 -16.885 1.00 24.98 ? 81   VAL J CG1 1 
ATOM   10656 C  CG2 . VAL J  1 81  ? 7.251   -13.552 -18.780 1.00 32.93 ? 81   VAL J CG2 1 
ATOM   10657 N  N   . GLY J  1 82  ? 6.719   -8.855  -18.645 1.00 24.80 ? 82   GLY J N   1 
ATOM   10658 C  CA  . GLY J  1 82  ? 6.683   -7.573  -17.971 1.00 24.61 ? 82   GLY J CA  1 
ATOM   10659 C  C   . GLY J  1 82  ? 5.480   -6.707  -18.293 1.00 25.34 ? 82   GLY J C   1 
ATOM   10660 O  O   . GLY J  1 82  ? 5.460   -5.525  -17.953 1.00 22.66 ? 82   GLY J O   1 
ATOM   10661 N  N   . ASP J  1 83  ? 4.476   -7.299  -18.937 1.00 27.49 ? 83   ASP J N   1 
ATOM   10662 C  CA  . ASP J  1 83  ? 3.244   -6.598  -19.318 1.00 24.13 ? 83   ASP J CA  1 
ATOM   10663 C  C   . ASP J  1 83  ? 2.226   -6.468  -18.197 1.00 25.42 ? 83   ASP J C   1 
ATOM   10664 O  O   . ASP J  1 83  ? 1.379   -7.340  -18.007 1.00 26.54 ? 83   ASP J O   1 
ATOM   10665 C  CB  . ASP J  1 83  ? 2.591   -7.296  -20.495 1.00 24.59 ? 83   ASP J CB  1 
ATOM   10666 C  CG  . ASP J  1 83  ? 3.358   -7.094  -21.763 1.00 28.46 ? 83   ASP J CG  1 
ATOM   10667 O  OD1 . ASP J  1 83  ? 4.309   -6.292  -21.727 1.00 24.63 ? 83   ASP J OD1 1 
ATOM   10668 O  OD2 . ASP J  1 83  ? 3.017   -7.727  -22.787 1.00 32.78 ? 83   ASP J OD2 1 
ATOM   10669 N  N   . LEU J  1 84  ? 2.296   -5.362  -17.468 1.00 22.87 ? 84   LEU J N   1 
ATOM   10670 C  CA  . LEU J  1 84  ? 1.429   -5.172  -16.326 1.00 24.48 ? 84   LEU J CA  1 
ATOM   10671 C  C   . LEU J  1 84  ? 0.282   -4.216  -16.647 1.00 25.91 ? 84   LEU J C   1 
ATOM   10672 O  O   . LEU J  1 84  ? -0.484  -3.822  -15.753 1.00 26.87 ? 84   LEU J O   1 
ATOM   10673 C  CB  . LEU J  1 84  ? 2.238   -4.707  -15.110 1.00 25.58 ? 84   LEU J CB  1 
ATOM   10674 C  CG  . LEU J  1 84  ? 3.372   -5.658  -14.703 1.00 24.13 ? 84   LEU J CG  1 
ATOM   10675 C  CD1 . LEU J  1 84  ? 3.990   -5.198  -13.403 1.00 24.47 ? 84   LEU J CD1 1 
ATOM   10676 C  CD2 . LEU J  1 84  ? 2.868   -7.088  -14.577 1.00 25.83 ? 84   LEU J CD2 1 
ATOM   10677 N  N   . GLY J  1 85  ? 0.166   -3.867  -17.926 1.00 20.68 ? 85   GLY J N   1 
ATOM   10678 C  CA  . GLY J  1 85  ? -0.939  -3.067  -18.414 1.00 20.41 ? 85   GLY J CA  1 
ATOM   10679 C  C   . GLY J  1 85  ? -0.803  -1.592  -18.097 1.00 22.29 ? 85   GLY J C   1 
ATOM   10680 O  O   . GLY J  1 85  ? 0.245   -0.983  -18.339 1.00 21.24 ? 85   GLY J O   1 
ATOM   10681 N  N   . ASN J  1 86  ? -1.880  -1.024  -17.553 1.00 23.44 ? 86   ASN J N   1 
ATOM   10682 C  CA  . ASN J  1 86  ? -1.938  0.386   -17.190 1.00 20.59 ? 86   ASN J CA  1 
ATOM   10683 C  C   . ASN J  1 86  ? -2.134  0.647   -15.707 1.00 19.21 ? 86   ASN J C   1 
ATOM   10684 O  O   . ASN J  1 86  ? -2.633  -0.195  -14.958 1.00 17.45 ? 86   ASN J O   1 
ATOM   10685 C  CB  . ASN J  1 86  ? -3.084  1.080   -17.901 1.00 20.24 ? 86   ASN J CB  1 
ATOM   10686 C  CG  . ASN J  1 86  ? -2.830  1.282   -19.345 1.00 18.71 ? 86   ASN J CG  1 
ATOM   10687 O  OD1 . ASN J  1 86  ? -2.012  2.109   -19.735 1.00 18.98 ? 86   ASN J OD1 1 
ATOM   10688 N  ND2 . ASN J  1 86  ? -3.560  0.549   -20.170 1.00 22.46 ? 86   ASN J ND2 1 
ATOM   10689 N  N   . VAL J  1 87  ? -1.745  1.852   -15.317 1.00 17.45 ? 87   VAL J N   1 
ATOM   10690 C  CA  . VAL J  1 87  ? -2.065  2.393   -14.024 1.00 18.70 ? 87   VAL J CA  1 
ATOM   10691 C  C   . VAL J  1 87  ? -2.913  3.639   -14.268 1.00 18.36 ? 87   VAL J C   1 
ATOM   10692 O  O   . VAL J  1 87  ? -2.839  4.244   -15.327 1.00 16.90 ? 87   VAL J O   1 
ATOM   10693 C  CB  . VAL J  1 87  ? -0.789  2.731   -13.213 1.00 19.94 ? 87   VAL J CB  1 
ATOM   10694 C  CG1 . VAL J  1 87  ? -0.108  1.442   -12.725 1.00 18.41 ? 87   VAL J CG1 1 
ATOM   10695 C  CG2 . VAL J  1 87  ? 0.176   3.582   -14.033 1.00 16.86 ? 87   VAL J CG2 1 
ATOM   10696 N  N   . THR J  1 88  ? -3.742  4.001   -13.295 1.00 19.11 ? 88   THR J N   1 
ATOM   10697 C  CA  . THR J  1 88  ? -4.634  5.140   -13.444 1.00 21.77 ? 88   THR J CA  1 
ATOM   10698 C  C   . THR J  1 88  ? -4.240  6.262   -12.501 1.00 20.61 ? 88   THR J C   1 
ATOM   10699 O  O   . THR J  1 88  ? -4.139  6.053   -11.294 1.00 18.95 ? 88   THR J O   1 
ATOM   10700 C  CB  . THR J  1 88  ? -6.114  4.765   -13.148 1.00 22.70 ? 88   THR J CB  1 
ATOM   10701 O  OG1 . THR J  1 88  ? -6.493  3.620   -13.922 1.00 21.78 ? 88   THR J OG1 1 
ATOM   10702 C  CG2 . THR J  1 88  ? -7.035  5.924   -13.490 1.00 20.41 ? 88   THR J CG2 1 
ATOM   10703 N  N   . ALA J  1 89  ? -4.031  7.448   -13.065 1.00 18.90 ? 89   ALA J N   1 
ATOM   10704 C  CA  . ALA J  1 89  ? -3.749  8.643   -12.286 1.00 20.19 ? 89   ALA J CA  1 
ATOM   10705 C  C   . ALA J  1 89  ? -5.011  9.478   -12.144 1.00 19.95 ? 89   ALA J C   1 
ATOM   10706 O  O   . ALA J  1 89  ? -5.708  9.716   -13.126 1.00 22.24 ? 89   ALA J O   1 
ATOM   10707 C  CB  . ALA J  1 89  ? -2.646  9.457   -12.952 1.00 19.31 ? 89   ALA J CB  1 
ATOM   10708 N  N   . GLY J  1 90  ? -5.313  9.918   -10.927 1.00 21.46 ? 90   GLY J N   1 
ATOM   10709 C  CA  . GLY J  1 90  ? -6.467  10.770  -10.703 1.00 22.09 ? 90   GLY J CA  1 
ATOM   10710 C  C   . GLY J  1 90  ? -6.220  12.174  -11.221 1.00 22.52 ? 90   GLY J C   1 
ATOM   10711 O  O   . GLY J  1 90  ? -5.124  12.471  -11.690 1.00 20.81 ? 90   GLY J O   1 
ATOM   10712 N  N   . LYS J  1 91  ? -7.242  13.030  -11.160 1.00 25.62 ? 91   LYS J N   1 
ATOM   10713 C  CA  . LYS J  1 91  ? -7.117  14.444  -11.551 1.00 28.45 ? 91   LYS J CA  1 
ATOM   10714 C  C   . LYS J  1 91  ? -5.990  15.080  -10.743 1.00 28.87 ? 91   LYS J C   1 
ATOM   10715 O  O   . LYS J  1 91  ? -5.406  16.102  -11.109 1.00 29.50 ? 91   LYS J O   1 
ATOM   10716 C  CB  . LYS J  1 91  ? -8.437  15.178  -11.303 1.00 27.16 ? 91   LYS J CB  1 
ATOM   10717 C  CG  . LYS J  1 91  ? -8.315  16.684  -11.344 1.00 31.91 ? 91   LYS J CG  1 
ATOM   10718 C  CD  . LYS J  1 91  ? -9.589  17.354  -11.858 1.00 34.90 ? 91   LYS J CD  1 
ATOM   10719 C  CE  . LYS J  1 91  ? -10.840 16.748  -11.246 1.00 40.41 ? 91   LYS J CE  1 
ATOM   10720 N  NZ  . LYS J  1 91  ? -11.285 15.494  -11.946 1.00 42.99 ? 91   LYS J NZ  1 
ATOM   10721 N  N   . ASP J  1 92  ? -5.732  14.415  -9.624  1.00 30.10 ? 92   ASP J N   1 
ATOM   10722 C  CA  . ASP J  1 92  ? -4.646  14.613  -8.678  1.00 28.93 ? 92   ASP J CA  1 
ATOM   10723 C  C   . ASP J  1 92  ? -3.240  14.634  -9.303  1.00 26.52 ? 92   ASP J C   1 
ATOM   10724 O  O   . ASP J  1 92  ? -2.377  15.417  -8.912  1.00 25.49 ? 92   ASP J O   1 
ATOM   10725 C  CB  . ASP J  1 92  ? -4.717  13.398  -7.747  1.00 28.18 ? 92   ASP J CB  1 
ATOM   10726 C  CG  . ASP J  1 92  ? -4.360  13.724  -6.346  1.00 32.27 ? 92   ASP J CG  1 
ATOM   10727 O  OD1 . ASP J  1 92  ? -3.993  14.889  -6.095  1.00 38.42 ? 92   ASP J OD1 1 
ATOM   10728 O  OD2 . ASP J  1 92  ? -4.455  12.813  -5.500  1.00 32.64 ? 92   ASP J OD2 1 
ATOM   10729 N  N   . GLY J  1 93  ? -3.014  13.738  -10.259 1.00 24.06 ? 93   GLY J N   1 
ATOM   10730 C  CA  . GLY J  1 93  ? -1.686  13.476  -10.772 1.00 20.61 ? 93   GLY J CA  1 
ATOM   10731 C  C   . GLY J  1 93  ? -1.169  12.183  -10.173 1.00 19.13 ? 93   GLY J C   1 
ATOM   10732 O  O   . GLY J  1 93  ? -0.153  11.642  -10.613 1.00 18.90 ? 93   GLY J O   1 
ATOM   10733 N  N   . VAL J  1 94  ? -1.897  11.686  -9.176  1.00 20.97 ? 94   VAL J N   1 
ATOM   10734 C  CA  . VAL J  1 94  ? -1.470  10.560  -8.351  1.00 20.90 ? 94   VAL J CA  1 
ATOM   10735 C  C   . VAL J  1 94  ? -2.138  9.233   -8.718  1.00 22.13 ? 94   VAL J C   1 
ATOM   10736 O  O   . VAL J  1 94  ? -3.367  9.128   -8.745  1.00 23.93 ? 94   VAL J O   1 
ATOM   10737 C  CB  . VAL J  1 94  ? -1.729  10.838  -6.860  1.00 20.32 ? 94   VAL J CB  1 
ATOM   10738 C  CG1 . VAL J  1 94  ? -1.457  9.584   -6.035  1.00 22.07 ? 94   VAL J CG1 1 
ATOM   10739 C  CG2 . VAL J  1 94  ? -0.872  11.987  -6.392  1.00 20.87 ? 94   VAL J CG2 1 
ATOM   10740 N  N   . ALA J  1 95  ? -1.321  8.218   -8.984  1.00 21.78 ? 95   ALA J N   1 
ATOM   10741 C  CA  . ALA J  1 95  ? -1.841  6.907   -9.341  1.00 21.43 ? 95   ALA J CA  1 
ATOM   10742 C  C   . ALA J  1 95  ? -1.724  5.942   -8.184  1.00 22.29 ? 95   ALA J C   1 
ATOM   10743 O  O   . ALA J  1 95  ? -0.634  5.632   -7.736  1.00 21.42 ? 95   ALA J O   1 
ATOM   10744 C  CB  . ALA J  1 95  ? -1.116  6.343   -10.573 1.00 19.63 ? 95   ALA J CB  1 
ATOM   10745 N  N   . ASN J  1 96  ? -2.852  5.442   -7.710  1.00 23.88 ? 96   ASN J N   1 
ATOM   10746 C  CA  . ASN J  1 96  ? -2.799  4.374   -6.737  1.00 22.07 ? 96   ASN J CA  1 
ATOM   10747 C  C   . ASN J  1 96  ? -2.838  3.053   -7.451  1.00 21.21 ? 96   ASN J C   1 
ATOM   10748 O  O   . ASN J  1 96  ? -3.752  2.768   -8.210  1.00 23.89 ? 96   ASN J O   1 
ATOM   10749 C  CB  . ASN J  1 96  ? -3.876  4.559   -5.685  1.00 24.85 ? 96   ASN J CB  1 
ATOM   10750 C  CG  . ASN J  1 96  ? -3.700  5.878   -4.954  1.00 33.30 ? 96   ASN J CG  1 
ATOM   10751 O  OD1 . ASN J  1 96  ? -2.719  6.067   -4.210  1.00 32.13 ? 96   ASN J OD1 1 
ATOM   10752 N  ND2 . ASN J  1 96  ? -4.603  6.825   -5.214  1.00 37.22 ? 96   ASN J ND2 1 
ATOM   10753 N  N   . VAL J  1 97  ? -1.776  2.290   -7.252  1.00 20.41 ? 97   VAL J N   1 
ATOM   10754 C  CA  . VAL J  1 97  ? -1.526  1.083   -8.005  1.00 20.10 ? 97   VAL J CA  1 
ATOM   10755 C  C   . VAL J  1 97  ? -1.772  -0.089  -7.098  1.00 20.25 ? 97   VAL J C   1 
ATOM   10756 O  O   . VAL J  1 97  ? -1.280  -0.124  -5.975  1.00 22.74 ? 97   VAL J O   1 
ATOM   10757 C  CB  . VAL J  1 97  ? -0.061  1.032   -8.472  1.00 18.78 ? 97   VAL J CB  1 
ATOM   10758 C  CG1 . VAL J  1 97  ? 0.219   -0.264  -9.208  1.00 17.84 ? 97   VAL J CG1 1 
ATOM   10759 C  CG2 . VAL J  1 97  ? 0.276   2.260   -9.324  1.00 15.16 ? 97   VAL J CG2 1 
ATOM   10760 N  N   . SER J  1 98  ? -2.556  -1.041  -7.578  1.00 20.72 ? 98   SER J N   1 
ATOM   10761 C  CA  . SER J  1 98  ? -2.766  -2.284  -6.861  1.00 22.23 ? 98   SER J CA  1 
ATOM   10762 C  C   . SER J  1 98  ? -3.137  -3.364  -7.857  1.00 24.25 ? 98   SER J C   1 
ATOM   10763 O  O   . SER J  1 98  ? -4.292  -3.490  -8.261  1.00 25.65 ? 98   SER J O   1 
ATOM   10764 C  CB  . SER J  1 98  ? -3.843  -2.136  -5.790  1.00 27.11 ? 98   SER J CB  1 
ATOM   10765 O  OG  . SER J  1 98  ? -3.861  -3.284  -4.962  1.00 31.77 ? 98   SER J OG  1 
ATOM   10766 N  N   . ILE J  1 99  ? -2.127  -4.135  -8.245  1.00 23.57 ? 99   ILE J N   1 
ATOM   10767 C  CA  . ILE J  1 99  ? -2.229  -5.148  -9.282  1.00 25.19 ? 99   ILE J CA  1 
ATOM   10768 C  C   . ILE J  1 99  ? -1.832  -6.500  -8.699  1.00 27.48 ? 99   ILE J C   1 
ATOM   10769 O  O   . ILE J  1 99  ? -0.978  -6.568  -7.822  1.00 27.89 ? 99   ILE J O   1 
ATOM   10770 C  CB  . ILE J  1 99  ? -1.284  -4.812  -10.459 1.00 21.27 ? 99   ILE J CB  1 
ATOM   10771 C  CG1 . ILE J  1 99  ? -1.759  -3.546  -11.168 1.00 20.54 ? 99   ILE J CG1 1 
ATOM   10772 C  CG2 . ILE J  1 99  ? -1.177  -5.979  -11.421 1.00 24.14 ? 99   ILE J CG2 1 
ATOM   10773 C  CD1 . ILE J  1 99  ? -0.673  -2.835  -11.912 1.00 22.28 ? 99   ILE J CD1 1 
ATOM   10774 N  N   . GLU J  1 100 ? -2.463  -7.570  -9.173  1.00 30.22 ? 100  GLU J N   1 
ATOM   10775 C  CA  . GLU J  1 100 ? -2.051  -8.929  -8.824  1.00 30.90 ? 100  GLU J CA  1 
ATOM   10776 C  C   . GLU J  1 100 ? -1.750  -9.686  -10.127 1.00 30.35 ? 100  GLU J C   1 
ATOM   10777 O  O   . GLU J  1 100 ? -2.597  -9.736  -11.027 1.00 30.38 ? 100  GLU J O   1 
ATOM   10778 C  CB  . GLU J  1 100 ? -3.134  -9.627  -7.987  1.00 31.25 ? 100  GLU J CB  1 
ATOM   10779 C  CG  . GLU J  1 100 ? -2.818  -11.064 -7.591  1.00 34.89 ? 100  GLU J CG  1 
ATOM   10780 C  CD  . GLU J  1 100 ? -4.052  -11.819 -7.108  1.00 46.55 ? 100  GLU J CD  1 
ATOM   10781 O  OE1 . GLU J  1 100 ? -4.946  -11.179 -6.505  1.00 51.11 ? 100  GLU J OE1 1 
ATOM   10782 O  OE2 . GLU J  1 100 ? -4.132  -13.051 -7.337  1.00 47.88 ? 100  GLU J OE2 1 
ATOM   10783 N  N   . ASP J  1 101 ? -0.543  -10.243 -10.241 1.00 27.46 ? 101  ASP J N   1 
ATOM   10784 C  CA  . ASP J  1 101 ? -0.108  -10.888 -11.480 1.00 29.96 ? 101  ASP J CA  1 
ATOM   10785 C  C   . ASP J  1 101 ? 0.570   -12.235 -11.218 1.00 31.97 ? 101  ASP J C   1 
ATOM   10786 O  O   . ASP J  1 101 ? 1.307   -12.378 -10.255 1.00 34.18 ? 101  ASP J O   1 
ATOM   10787 C  CB  . ASP J  1 101 ? 0.831   -9.961  -12.261 1.00 27.33 ? 101  ASP J CB  1 
ATOM   10788 C  CG  . ASP J  1 101 ? 0.943   -10.340 -13.734 1.00 28.85 ? 101  ASP J CG  1 
ATOM   10789 O  OD1 . ASP J  1 101 ? -0.008  -10.085 -14.511 1.00 28.45 ? 101  ASP J OD1 1 
ATOM   10790 O  OD2 . ASP J  1 101 ? 1.996   -10.884 -14.123 1.00 30.18 ? 101  ASP J OD2 1 
ATOM   10791 N  N   . ARG J  1 102 ? 0.336   -13.221 -12.080 1.00 34.05 ? 102  ARG J N   1 
ATOM   10792 C  CA  . ARG J  1 102 ? 0.888   -14.558 -11.861 1.00 34.10 ? 102  ARG J CA  1 
ATOM   10793 C  C   . ARG J  1 102 ? 1.999   -14.909 -12.847 1.00 36.19 ? 102  ARG J C   1 
ATOM   10794 O  O   . ARG J  1 102 ? 2.620   -15.968 -12.733 1.00 39.57 ? 102  ARG J O   1 
ATOM   10795 C  CB  . ARG J  1 102 ? -0.222  -15.611 -11.917 1.00 39.60 ? 102  ARG J CB  1 
ATOM   10796 C  CG  . ARG J  1 102 ? -1.327  -15.373 -10.889 1.00 47.26 ? 102  ARG J CG  1 
ATOM   10797 C  CD  . ARG J  1 102 ? -2.610  -16.139 -11.203 1.00 48.03 ? 102  ARG J CD  1 
ATOM   10798 N  NE  . ARG J  1 102 ? -3.654  -15.839 -10.226 1.00 53.12 ? 102  ARG J NE  1 
ATOM   10799 C  CZ  . ARG J  1 102 ? -3.829  -16.506 -9.089  1.00 55.93 ? 102  ARG J CZ  1 
ATOM   10800 N  NH1 . ARG J  1 102 ? -3.030  -17.524 -8.784  1.00 55.24 ? 102  ARG J NH1 1 
ATOM   10801 N  NH2 . ARG J  1 102 ? -4.804  -16.159 -8.256  1.00 56.86 ? 102  ARG J NH2 1 
ATOM   10802 N  N   . VAL J  1 103 ? 2.250   -14.017 -13.804 1.00 32.47 ? 103  VAL J N   1 
ATOM   10803 C  CA  . VAL J  1 103 ? 3.265   -14.255 -14.830 1.00 33.10 ? 103  VAL J CA  1 
ATOM   10804 C  C   . VAL J  1 103 ? 4.667   -13.737 -14.425 1.00 34.08 ? 103  VAL J C   1 
ATOM   10805 O  O   . VAL J  1 103 ? 5.672   -14.420 -14.649 1.00 34.72 ? 103  VAL J O   1 
ATOM   10806 C  CB  . VAL J  1 103 ? 2.804   -13.724 -16.209 1.00 31.99 ? 103  VAL J CB  1 
ATOM   10807 C  CG1 . VAL J  1 103 ? 3.904   -13.866 -17.245 1.00 30.51 ? 103  VAL J CG1 1 
ATOM   10808 C  CG2 . VAL J  1 103 ? 1.543   -14.465 -16.656 1.00 30.17 ? 103  VAL J CG2 1 
ATOM   10809 N  N   . ILE J  1 104 ? 4.735   -12.554 -13.812 1.00 33.27 ? 104  ILE J N   1 
ATOM   10810 C  CA  . ILE J  1 104 ? 5.987   -12.097 -13.203 1.00 32.20 ? 104  ILE J CA  1 
ATOM   10811 C  C   . ILE J  1 104 ? 6.270   -12.899 -11.930 1.00 31.28 ? 104  ILE J C   1 
ATOM   10812 O  O   . ILE J  1 104 ? 5.345   -13.383 -11.282 1.00 32.06 ? 104  ILE J O   1 
ATOM   10813 C  CB  . ILE J  1 104 ? 5.986   -10.576 -12.858 1.00 28.25 ? 104  ILE J CB  1 
ATOM   10814 C  CG1 . ILE J  1 104 ? 4.946   -10.265 -11.775 1.00 28.35 ? 104  ILE J CG1 1 
ATOM   10815 C  CG2 . ILE J  1 104 ? 5.787   -9.725  -14.114 1.00 26.30 ? 104  ILE J CG2 1 
ATOM   10816 C  CD1 . ILE J  1 104 ? 4.983   -8.834  -11.264 1.00 25.06 ? 104  ILE J CD1 1 
ATOM   10817 N  N   . SER J  1 105 ? 7.548   -13.038 -11.582 1.00 31.02 ? 105  SER J N   1 
ATOM   10818 C  CA  . SER J  1 105 ? 7.955   -13.691 -10.334 1.00 32.39 ? 105  SER J CA  1 
ATOM   10819 C  C   . SER J  1 105 ? 9.088   -12.926 -9.651  1.00 29.89 ? 105  SER J C   1 
ATOM   10820 O  O   . SER J  1 105 ? 9.842   -12.214 -10.312 1.00 32.35 ? 105  SER J O   1 
ATOM   10821 C  CB  . SER J  1 105 ? 8.400   -15.135 -10.601 1.00 32.27 ? 105  SER J CB  1 
ATOM   10822 O  OG  . SER J  1 105 ? 8.798   -15.768 -9.397  1.00 34.08 ? 105  SER J OG  1 
ATOM   10823 N  N   . LEU J  1 106 ? 9.207   -13.074 -8.335  1.00 28.58 ? 106  LEU J N   1 
ATOM   10824 C  CA  . LEU J  1 106 ? 10.343  -12.513 -7.597  1.00 28.67 ? 106  LEU J CA  1 
ATOM   10825 C  C   . LEU J  1 106 ? 11.436  -13.570 -7.366  1.00 31.21 ? 106  LEU J C   1 
ATOM   10826 O  O   . LEU J  1 106 ? 12.388  -13.342 -6.625  1.00 29.74 ? 106  LEU J O   1 
ATOM   10827 C  CB  . LEU J  1 106 ? 9.891   -11.915 -6.262  1.00 29.30 ? 106  LEU J CB  1 
ATOM   10828 C  CG  . LEU J  1 106 ? 8.767   -10.876 -6.305  1.00 27.85 ? 106  LEU J CG  1 
ATOM   10829 C  CD1 . LEU J  1 106 ? 8.557   -10.256 -4.951  1.00 25.20 ? 106  LEU J CD1 1 
ATOM   10830 C  CD2 . LEU J  1 106 ? 9.060   -9.799  -7.356  1.00 26.35 ? 106  LEU J CD2 1 
ATOM   10831 N  N   . SER J  1 107 ? 11.276  -14.730 -7.998  1.00 31.78 ? 107  SER J N   1 
ATOM   10832 C  CA  . SER J  1 107 ? 12.269  -15.796 -7.936  1.00 33.77 ? 107  SER J CA  1 
ATOM   10833 C  C   . SER J  1 107 ? 12.280  -16.577 -9.255  1.00 36.52 ? 107  SER J C   1 
ATOM   10834 O  O   . SER J  1 107 ? 11.420  -16.377 -10.117 1.00 35.20 ? 107  SER J O   1 
ATOM   10835 C  CB  . SER J  1 107 ? 11.988  -16.739 -6.759  1.00 31.94 ? 107  SER J CB  1 
ATOM   10836 O  OG  . SER J  1 107 ? 10.826  -17.522 -6.986  1.00 36.23 ? 107  SER J OG  1 
ATOM   10837 N  N   . GLY J  1 108 ? 13.263  -17.454 -9.417  1.00 33.30 ? 108  GLY J N   1 
ATOM   10838 C  CA  . GLY J  1 108 ? 13.266  -18.349 -10.549 1.00 34.02 ? 108  GLY J CA  1 
ATOM   10839 C  C   . GLY J  1 108 ? 13.558  -17.641 -11.849 1.00 41.55 ? 108  GLY J C   1 
ATOM   10840 O  O   . GLY J  1 108 ? 13.975  -16.484 -11.851 1.00 40.05 ? 108  GLY J O   1 
ATOM   10841 N  N   . GLU J  1 109 ? 13.330  -18.337 -12.961 1.00 44.58 ? 109  GLU J N   1 
ATOM   10842 C  CA  . GLU J  1 109 ? 13.788  -17.862 -14.260 1.00 41.48 ? 109  GLU J CA  1 
ATOM   10843 C  C   . GLU J  1 109 ? 13.182  -16.516 -14.653 1.00 40.30 ? 109  GLU J C   1 
ATOM   10844 O  O   . GLU J  1 109 ? 13.859  -15.674 -15.243 1.00 37.47 ? 109  GLU J O   1 
ATOM   10845 C  CB  . GLU J  1 109 ? 13.536  -18.911 -15.352 1.00 47.85 ? 109  GLU J CB  1 
ATOM   10846 C  CG  . GLU J  1 109 ? 14.160  -20.282 -15.078 1.00 54.73 ? 109  GLU J CG  1 
ATOM   10847 C  CD  . GLU J  1 109 ? 13.209  -21.220 -14.338 1.00 63.91 ? 109  GLU J CD  1 
ATOM   10848 O  OE1 . GLU J  1 109 ? 12.074  -20.790 -14.023 1.00 62.34 ? 109  GLU J OE1 1 
ATOM   10849 O  OE2 . GLU J  1 109 ? 13.591  -22.388 -14.082 1.00 64.80 ? 109  GLU J OE2 1 
ATOM   10850 N  N   . HIS J  1 110 ? 11.908  -16.316 -14.328 1.00 41.26 ? 110  HIS J N   1 
ATOM   10851 C  CA  . HIS J  1 110 ? 11.211  -15.096 -14.726 1.00 41.11 ? 110  HIS J CA  1 
ATOM   10852 C  C   . HIS J  1 110 ? 11.236  -14.046 -13.633 1.00 36.56 ? 110  HIS J C   1 
ATOM   10853 O  O   . HIS J  1 110 ? 10.323  -13.223 -13.536 1.00 35.79 ? 110  HIS J O   1 
ATOM   10854 C  CB  . HIS J  1 110 ? 9.760   -15.391 -15.134 1.00 41.50 ? 110  HIS J CB  1 
ATOM   10855 C  CG  . HIS J  1 110 ? 9.644   -16.254 -16.353 1.00 44.63 ? 110  HIS J CG  1 
ATOM   10856 N  ND1 . HIS J  1 110 ? 8.526   -17.012 -16.628 1.00 42.80 ? 110  HIS J ND1 1 
ATOM   10857 C  CD2 . HIS J  1 110 ? 10.522  -16.494 -17.360 1.00 42.15 ? 110  HIS J CD2 1 
ATOM   10858 C  CE1 . HIS J  1 110 ? 8.716   -17.673 -17.757 1.00 44.72 ? 110  HIS J CE1 1 
ATOM   10859 N  NE2 . HIS J  1 110 ? 9.919   -17.376 -18.220 1.00 42.59 ? 110  HIS J NE2 1 
ATOM   10860 N  N   . SER J  1 111 ? 12.277  -14.086 -12.807 1.00 36.47 ? 111  SER J N   1 
ATOM   10861 C  CA  . SER J  1 111 ? 12.414  -13.122 -11.727 1.00 31.27 ? 111  SER J CA  1 
ATOM   10862 C  C   . SER J  1 111 ? 12.609  -11.738 -12.320 1.00 29.49 ? 111  SER J C   1 
ATOM   10863 O  O   . SER J  1 111 ? 13.143  -11.579 -13.421 1.00 27.80 ? 111  SER J O   1 
ATOM   10864 C  CB  . SER J  1 111 ? 13.582  -13.470 -10.818 1.00 28.15 ? 111  SER J CB  1 
ATOM   10865 O  OG  . SER J  1 111 ? 13.755  -12.466 -9.833  1.00 28.08 ? 111  SER J OG  1 
ATOM   10866 N  N   . ILE J  1 112 ? 12.149  -10.742 -11.581 1.00 29.36 ? 112  ILE J N   1 
ATOM   10867 C  CA  . ILE J  1 112 ? 12.194  -9.362  -12.017 1.00 24.96 ? 112  ILE J CA  1 
ATOM   10868 C  C   . ILE J  1 112 ? 13.069  -8.577  -11.054 1.00 23.38 ? 112  ILE J C   1 
ATOM   10869 O  O   . ILE J  1 112 ? 13.233  -7.370  -11.206 1.00 25.10 ? 112  ILE J O   1 
ATOM   10870 C  CB  . ILE J  1 112 ? 10.779  -8.747  -12.049 1.00 25.55 ? 112  ILE J CB  1 
ATOM   10871 C  CG1 . ILE J  1 112 ? 10.111  -8.880  -10.680 1.00 23.17 ? 112  ILE J CG1 1 
ATOM   10872 C  CG2 . ILE J  1 112 ? 9.918   -9.437  -13.096 1.00 25.30 ? 112  ILE J CG2 1 
ATOM   10873 C  CD1 . ILE J  1 112 ? 8.924   -7.972  -10.494 1.00 25.38 ? 112  ILE J CD1 1 
ATOM   10874 N  N   . ILE J  1 113 ? 13.620  -9.255  -10.049 1.00 24.01 ? 113  ILE J N   1 
ATOM   10875 C  CA  . ILE J  1 113 ? 14.562  -8.605  -9.141  1.00 23.81 ? 113  ILE J CA  1 
ATOM   10876 C  C   . ILE J  1 113 ? 15.772  -8.195  -9.966  1.00 21.96 ? 113  ILE J C   1 
ATOM   10877 O  O   . ILE J  1 113 ? 16.338  -9.017  -10.682 1.00 23.81 ? 113  ILE J O   1 
ATOM   10878 C  CB  . ILE J  1 113 ? 14.990  -9.536  -7.966  1.00 24.37 ? 113  ILE J CB  1 
ATOM   10879 C  CG1 . ILE J  1 113 ? 13.768  -10.089 -7.219  1.00 23.32 ? 113  ILE J CG1 1 
ATOM   10880 C  CG2 . ILE J  1 113 ? 15.936  -8.819  -6.997  1.00 22.51 ? 113  ILE J CG2 1 
ATOM   10881 C  CD1 . ILE J  1 113 ? 12.884  -9.057  -6.589  1.00 23.46 ? 113  ILE J CD1 1 
ATOM   10882 N  N   . GLY J  1 114 ? 16.147  -6.920  -9.905  1.00 22.09 ? 114  GLY J N   1 
ATOM   10883 C  CA  . GLY J  1 114 ? 17.283  -6.438  -10.683 1.00 22.38 ? 114  GLY J CA  1 
ATOM   10884 C  C   . GLY J  1 114 ? 16.959  -5.972  -12.101 1.00 22.27 ? 114  GLY J C   1 
ATOM   10885 O  O   . GLY J  1 114 ? 17.850  -5.666  -12.895 1.00 20.38 ? 114  GLY J O   1 
ATOM   10886 N  N   . ARG J  1 115 ? 15.671  -5.923  -12.418 1.00 21.69 ? 115  ARG J N   1 
ATOM   10887 C  CA  . ARG J  1 115 ? 15.204  -5.375  -13.680 1.00 20.72 ? 115  ARG J CA  1 
ATOM   10888 C  C   . ARG J  1 115 ? 14.601  -3.998  -13.401 1.00 19.07 ? 115  ARG J C   1 
ATOM   10889 O  O   . ARG J  1 115 ? 14.841  -3.433  -12.344 1.00 22.32 ? 115  ARG J O   1 
ATOM   10890 C  CB  . ARG J  1 115 ? 14.215  -6.339  -14.321 1.00 21.57 ? 115  ARG J CB  1 
ATOM   10891 C  CG  . ARG J  1 115 ? 14.746  -7.782  -14.304 1.00 23.42 ? 115  ARG J CG  1 
ATOM   10892 C  CD  . ARG J  1 115 ? 14.227  -8.603  -15.473 1.00 25.89 ? 115  ARG J CD  1 
ATOM   10893 N  NE  . ARG J  1 115 ? 14.804  -9.947  -15.519 1.00 26.60 ? 115  ARG J NE  1 
ATOM   10894 C  CZ  . ARG J  1 115 ? 15.692  -10.359 -16.424 1.00 26.56 ? 115  ARG J CZ  1 
ATOM   10895 N  NH1 . ARG J  1 115 ? 16.125  -9.533  -17.370 1.00 25.40 ? 115  ARG J NH1 1 
ATOM   10896 N  NH2 . ARG J  1 115 ? 16.152  -11.603 -16.384 1.00 29.36 ? 115  ARG J NH2 1 
ATOM   10897 N  N   . THR J  1 116 ? 13.843  -3.442  -14.334 1.00 20.19 ? 116  THR J N   1 
ATOM   10898 C  CA  . THR J  1 116 ? 13.414  -2.045  -14.216 1.00 22.32 ? 116  THR J CA  1 
ATOM   10899 C  C   . THR J  1 116 ? 11.911  -1.894  -14.424 1.00 21.35 ? 116  THR J C   1 
ATOM   10900 O  O   . THR J  1 116 ? 11.381  -2.419  -15.396 1.00 20.43 ? 116  THR J O   1 
ATOM   10901 C  CB  . THR J  1 116 ? 14.169  -1.157  -15.244 1.00 21.07 ? 116  THR J CB  1 
ATOM   10902 O  OG1 . THR J  1 116 ? 15.553  -1.126  -14.904 1.00 19.59 ? 116  THR J OG1 1 
ATOM   10903 C  CG2 . THR J  1 116 ? 13.633  0.272   -15.263 1.00 20.50 ? 116  THR J CG2 1 
ATOM   10904 N  N   . MET J  1 117 ? 11.233  -1.204  -13.503 1.00 19.21 ? 117  MET J N   1 
ATOM   10905 C  CA  . MET J  1 117 ? 9.834   -0.831  -13.699 1.00 19.49 ? 117  MET J CA  1 
ATOM   10906 C  C   . MET J  1 117 ? 9.803   0.500   -14.406 1.00 20.60 ? 117  MET J C   1 
ATOM   10907 O  O   . MET J  1 117 ? 10.463  1.439   -13.971 1.00 19.04 ? 117  MET J O   1 
ATOM   10908 C  CB  . MET J  1 117 ? 9.117   -0.617  -12.366 1.00 21.65 ? 117  MET J CB  1 
ATOM   10909 C  CG  . MET J  1 117 ? 8.400   -1.815  -11.750 1.00 25.18 ? 117  MET J CG  1 
ATOM   10910 S  SD  . MET J  1 117 ? 7.248   -2.715  -12.795 1.00 29.82 ? 117  MET J SD  1 
ATOM   10911 C  CE  . MET J  1 117 ? 6.421   -1.402  -13.663 1.00 24.56 ? 117  MET J CE  1 
ATOM   10912 N  N   . VAL J  1 118 ? 9.023   0.615   -15.473 1.00 19.57 ? 118  VAL J N   1 
ATOM   10913 C  CA  . VAL J  1 118 ? 8.804   1.940   -16.021 1.00 17.25 ? 118  VAL J CA  1 
ATOM   10914 C  C   . VAL J  1 118 ? 7.349   2.304   -16.154 1.00 20.77 ? 118  VAL J C   1 
ATOM   10915 O  O   . VAL J  1 118 ? 6.503   1.457   -16.457 1.00 19.91 ? 118  VAL J O   1 
ATOM   10916 C  CB  . VAL J  1 118 ? 9.637   2.248   -17.302 1.00 20.04 ? 118  VAL J CB  1 
ATOM   10917 C  CG1 . VAL J  1 118 ? 10.482  1.060   -17.717 1.00 21.18 ? 118  VAL J CG1 1 
ATOM   10918 C  CG2 . VAL J  1 118 ? 8.773   2.770   -18.419 1.00 19.87 ? 118  VAL J CG2 1 
ATOM   10919 N  N   . VAL J  1 119 ? 7.069   3.573   -15.853 1.00 21.32 ? 119  VAL J N   1 
ATOM   10920 C  CA  . VAL J  1 119 ? 5.756   4.163   -16.078 1.00 19.94 ? 119  VAL J CA  1 
ATOM   10921 C  C   . VAL J  1 119 ? 5.872   5.034   -17.331 1.00 19.59 ? 119  VAL J C   1 
ATOM   10922 O  O   . VAL J  1 119 ? 6.847   5.773   -17.501 1.00 17.56 ? 119  VAL J O   1 
ATOM   10923 C  CB  . VAL J  1 119 ? 5.209   4.937   -14.823 1.00 19.16 ? 119  VAL J CB  1 
ATOM   10924 C  CG1 . VAL J  1 119 ? 6.024   6.185   -14.531 1.00 17.55 ? 119  VAL J CG1 1 
ATOM   10925 C  CG2 . VAL J  1 119 ? 3.730   5.289   -14.992 1.00 17.61 ? 119  VAL J CG2 1 
ATOM   10926 N  N   . HIS J  1 120 ? 4.887   4.916   -18.219 1.00 17.90 ? 120  HIS J N   1 
ATOM   10927 C  CA  . HIS J  1 120 ? 4.970   5.532   -19.538 1.00 20.03 ? 120  HIS J CA  1 
ATOM   10928 C  C   . HIS J  1 120 ? 4.105   6.770   -19.709 1.00 20.38 ? 120  HIS J C   1 
ATOM   10929 O  O   . HIS J  1 120 ? 3.226   7.072   -18.893 1.00 19.28 ? 120  HIS J O   1 
ATOM   10930 C  CB  . HIS J  1 120 ? 4.650   4.517   -20.643 1.00 18.62 ? 120  HIS J CB  1 
ATOM   10931 C  CG  . HIS J  1 120 ? 5.640   3.397   -20.736 1.00 20.29 ? 120  HIS J CG  1 
ATOM   10932 N  ND1 . HIS J  1 120 ? 6.729   3.431   -21.582 1.00 21.59 ? 120  HIS J ND1 1 
ATOM   10933 C  CD2 . HIS J  1 120 ? 5.711   2.212   -20.085 1.00 19.68 ? 120  HIS J CD2 1 
ATOM   10934 C  CE1 . HIS J  1 120 ? 7.423   2.318   -21.449 1.00 20.18 ? 120  HIS J CE1 1 
ATOM   10935 N  NE2 . HIS J  1 120 ? 6.829   1.561   -20.545 1.00 19.27 ? 120  HIS J NE2 1 
ATOM   10936 N  N   . GLU J  1 121 ? 4.373   7.470   -20.802 1.00 19.89 ? 121  GLU J N   1 
ATOM   10937 C  CA  . GLU J  1 121 ? 3.713   8.725   -21.147 1.00 23.37 ? 121  GLU J CA  1 
ATOM   10938 C  C   . GLU J  1 121 ? 2.227   8.573   -21.527 1.00 21.15 ? 121  GLU J C   1 
ATOM   10939 O  O   . GLU J  1 121 ? 1.409   9.415   -21.183 1.00 19.09 ? 121  GLU J O   1 
ATOM   10940 C  CB  . GLU J  1 121 ? 4.502   9.385   -22.281 1.00 22.76 ? 121  GLU J CB  1 
ATOM   10941 C  CG  . GLU J  1 121 ? 3.748   10.364  -23.153 1.00 26.74 ? 121  GLU J CG  1 
ATOM   10942 C  CD  . GLU J  1 121 ? 4.404   10.519  -24.523 1.00 27.94 ? 121  GLU J CD  1 
ATOM   10943 O  OE1 . GLU J  1 121 ? 4.926   9.505   -25.050 1.00 23.94 ? 121  GLU J OE1 1 
ATOM   10944 O  OE2 . GLU J  1 121 ? 4.390   11.644  -25.071 1.00 30.72 ? 121  GLU J OE2 1 
ATOM   10945 N  N   . LYS J  1 122 ? 1.889   7.494   -22.227 1.00 21.96 ? 122  LYS J N   1 
ATOM   10946 C  CA  . LYS J  1 122 ? 0.540   7.309   -22.755 1.00 23.65 ? 122  LYS J CA  1 
ATOM   10947 C  C   . LYS J  1 122 ? -0.057  5.968   -22.331 1.00 21.56 ? 122  LYS J C   1 
ATOM   10948 O  O   . LYS J  1 122 ? 0.606   5.140   -21.712 1.00 18.65 ? 122  LYS J O   1 
ATOM   10949 C  CB  . LYS J  1 122 ? 0.526   7.399   -24.298 1.00 23.83 ? 122  LYS J CB  1 
ATOM   10950 C  CG  . LYS J  1 122 ? 1.061   8.706   -24.907 1.00 27.95 ? 122  LYS J CG  1 
ATOM   10951 C  CD  . LYS J  1 122 ? 1.412   8.553   -26.406 1.00 24.35 ? 122  LYS J CD  1 
ATOM   10952 C  CE  . LYS J  1 122 ? 0.322   9.129   -27.306 1.00 37.00 ? 122  LYS J CE  1 
ATOM   10953 N  NZ  . LYS J  1 122 ? -0.033  10.555  -26.988 1.00 39.03 ? 122  LYS J NZ  1 
ATOM   10954 N  N   . GLN J  1 123 ? -1.316  5.767   -22.701 1.00 19.66 ? 123  GLN J N   1 
ATOM   10955 C  CA  . GLN J  1 123 ? -2.040  4.537   -22.412 1.00 21.53 ? 123  GLN J CA  1 
ATOM   10956 C  C   . GLN J  1 123 ? -1.525  3.341   -23.206 1.00 21.94 ? 123  GLN J C   1 
ATOM   10957 O  O   . GLN J  1 123 ? -1.302  3.431   -24.409 1.00 24.33 ? 123  GLN J O   1 
ATOM   10958 C  CB  . GLN J  1 123 ? -3.526  4.735   -22.730 1.00 23.11 ? 123  GLN J CB  1 
ATOM   10959 C  CG  . GLN J  1 123 ? -4.386  3.508   -22.521 1.00 23.12 ? 123  GLN J CG  1 
ATOM   10960 C  CD  . GLN J  1 123 ? -5.852  3.801   -22.743 1.00 27.09 ? 123  GLN J CD  1 
ATOM   10961 O  OE1 . GLN J  1 123 ? -6.243  4.957   -22.926 1.00 30.99 ? 123  GLN J OE1 1 
ATOM   10962 N  NE2 . GLN J  1 123 ? -6.674  2.762   -22.730 1.00 25.31 ? 123  GLN J NE2 1 
ATOM   10963 N  N   . ASP J  1 124 ? -1.367  2.210   -22.533 1.00 22.09 ? 124  ASP J N   1 
ATOM   10964 C  CA  . ASP J  1 124 ? -0.982  0.971   -23.195 1.00 23.69 ? 124  ASP J CA  1 
ATOM   10965 C  C   . ASP J  1 124 ? -2.234  0.335   -23.800 1.00 25.12 ? 124  ASP J C   1 
ATOM   10966 O  O   . ASP J  1 124 ? -3.165  -0.023  -23.076 1.00 28.27 ? 124  ASP J O   1 
ATOM   10967 C  CB  . ASP J  1 124 ? -0.320  0.036   -22.176 1.00 22.58 ? 124  ASP J CB  1 
ATOM   10968 C  CG  . ASP J  1 124 ? 0.155   -1.263  -22.786 1.00 24.91 ? 124  ASP J CG  1 
ATOM   10969 O  OD1 . ASP J  1 124 ? -0.070  -1.483  -23.988 1.00 26.19 ? 124  ASP J OD1 1 
ATOM   10970 O  OD2 . ASP J  1 124 ? 0.757   -2.075  -22.056 1.00 27.11 ? 124  ASP J OD2 1 
ATOM   10971 N  N   . ASP J  1 125 ? -2.263  0.203   -25.124 1.00 25.10 ? 125  ASP J N   1 
ATOM   10972 C  CA  . ASP J  1 125 ? -3.426  -0.369  -25.811 1.00 26.60 ? 125  ASP J CA  1 
ATOM   10973 C  C   . ASP J  1 125 ? -3.566  -1.887  -25.633 1.00 27.85 ? 125  ASP J C   1 
ATOM   10974 O  O   . ASP J  1 125 ? -4.504  -2.494  -26.141 1.00 28.24 ? 125  ASP J O   1 
ATOM   10975 C  CB  . ASP J  1 125 ? -3.460  0.025   -27.300 1.00 27.55 ? 125  ASP J CB  1 
ATOM   10976 C  CG  . ASP J  1 125 ? -2.309  -0.573  -28.112 1.00 30.13 ? 125  ASP J CG  1 
ATOM   10977 O  OD1 . ASP J  1 125 ? -1.813  -1.672  -27.768 1.00 29.65 ? 125  ASP J OD1 1 
ATOM   10978 O  OD2 . ASP J  1 125 ? -1.912  0.060   -29.117 1.00 30.48 ? 125  ASP J OD2 1 
ATOM   10979 N  N   . LEU J  1 126 ? -2.635  -2.484  -24.901 1.00 27.27 ? 126  LEU J N   1 
ATOM   10980 C  CA  . LEU J  1 126 ? -2.704  -3.896  -24.542 1.00 26.15 ? 126  LEU J CA  1 
ATOM   10981 C  C   . LEU J  1 126 ? -2.580  -4.823  -25.742 1.00 28.96 ? 126  LEU J C   1 
ATOM   10982 O  O   . LEU J  1 126 ? -3.043  -5.967  -25.703 1.00 32.19 ? 126  LEU J O   1 
ATOM   10983 C  CB  . LEU J  1 126 ? -3.978  -4.194  -23.751 1.00 25.87 ? 126  LEU J CB  1 
ATOM   10984 C  CG  . LEU J  1 126 ? -4.236  -3.277  -22.550 1.00 25.46 ? 126  LEU J CG  1 
ATOM   10985 C  CD1 . LEU J  1 126 ? -5.568  -3.636  -21.913 1.00 26.70 ? 126  LEU J CD1 1 
ATOM   10986 C  CD2 . LEU J  1 126 ? -3.120  -3.358  -21.526 1.00 23.65 ? 126  LEU J CD2 1 
ATOM   10987 N  N   . GLY J  1 127 ? -1.942  -4.330  -26.801 1.00 30.97 ? 127  GLY J N   1 
ATOM   10988 C  CA  . GLY J  1 127 ? -1.674  -5.139  -27.976 1.00 30.76 ? 127  GLY J CA  1 
ATOM   10989 C  C   . GLY J  1 127 ? -2.867  -5.257  -28.907 1.00 34.76 ? 127  GLY J C   1 
ATOM   10990 O  O   . GLY J  1 127 ? -2.942  -6.182  -29.717 1.00 36.36 ? 127  GLY J O   1 
ATOM   10991 N  N   . LYS J  1 128 ? -3.799  -4.313  -28.795 1.00 34.30 ? 128  LYS J N   1 
ATOM   10992 C  CA  . LYS J  1 128 ? -5.029  -4.343  -29.578 1.00 35.25 ? 128  LYS J CA  1 
ATOM   10993 C  C   . LYS J  1 128 ? -5.136  -3.146  -30.522 1.00 35.70 ? 128  LYS J C   1 
ATOM   10994 O  O   . LYS J  1 128 ? -6.205  -2.879  -31.086 1.00 40.27 ? 128  LYS J O   1 
ATOM   10995 C  CB  . LYS J  1 128 ? -6.254  -4.404  -28.654 1.00 34.79 ? 128  LYS J CB  1 
ATOM   10996 C  CG  . LYS J  1 128 ? -6.109  -5.384  -27.510 1.00 33.78 ? 128  LYS J CG  1 
ATOM   10997 C  CD  . LYS J  1 128 ? -7.445  -5.859  -26.995 1.00 35.19 ? 128  LYS J CD  1 
ATOM   10998 C  CE  . LYS J  1 128 ? -7.253  -7.073  -26.101 1.00 41.61 ? 128  LYS J CE  1 
ATOM   10999 N  NZ  . LYS J  1 128 ? -6.254  -8.020  -26.685 1.00 43.38 ? 128  LYS J NZ  1 
ATOM   11000 N  N   . GLY J  1 129 ? -4.019  -2.449  -30.710 1.00 33.27 ? 129  GLY J N   1 
ATOM   11001 C  CA  . GLY J  1 129 ? -3.980  -1.247  -31.530 1.00 38.17 ? 129  GLY J CA  1 
ATOM   11002 C  C   . GLY J  1 129 ? -4.073  -1.437  -33.040 1.00 45.36 ? 129  GLY J C   1 
ATOM   11003 O  O   . GLY J  1 129 ? -4.554  -0.539  -33.748 1.00 48.80 ? 129  GLY J O   1 
ATOM   11004 N  N   . GLY J  1 130 ? -3.610  -2.579  -33.548 1.00 39.80 ? 130  GLY J N   1 
ATOM   11005 C  CA  . GLY J  1 130 ? -3.692  -2.840  -34.975 1.00 41.22 ? 130  GLY J CA  1 
ATOM   11006 C  C   . GLY J  1 130 ? -2.396  -2.580  -35.720 1.00 43.51 ? 130  GLY J C   1 
ATOM   11007 O  O   . GLY J  1 130 ? -1.989  -3.379  -36.568 1.00 44.28 ? 130  GLY J O   1 
ATOM   11008 N  N   . ASN J  1 131 ? -1.736  -1.465  -35.420 1.00 42.92 ? 131  ASN J N   1 
ATOM   11009 C  CA  . ASN J  1 131 ? -0.448  -1.193  -36.051 1.00 39.19 ? 131  ASN J CA  1 
ATOM   11010 C  C   . ASN J  1 131 ? 0.625   -2.132  -35.513 1.00 39.48 ? 131  ASN J C   1 
ATOM   11011 O  O   . ASN J  1 131 ? 0.308   -3.134  -34.872 1.00 41.68 ? 131  ASN J O   1 
ATOM   11012 C  CB  . ASN J  1 131 ? -0.062  0.295   -35.976 1.00 40.24 ? 131  ASN J CB  1 
ATOM   11013 C  CG  . ASN J  1 131 ? 0.408   0.731   -34.607 1.00 40.15 ? 131  ASN J CG  1 
ATOM   11014 O  OD1 . ASN J  1 131 ? 0.050   0.142   -33.581 1.00 37.89 ? 131  ASN J OD1 1 
ATOM   11015 N  ND2 . ASN J  1 131 ? 1.206   1.802   -34.584 1.00 40.89 ? 131  ASN J ND2 1 
ATOM   11016 N  N   . GLU J  1 132 ? 1.889   -1.850  -35.785 1.00 40.55 ? 132  GLU J N   1 
ATOM   11017 C  CA  . GLU J  1 132 ? 2.913   -2.805  -35.392 1.00 41.51 ? 132  GLU J CA  1 
ATOM   11018 C  C   . GLU J  1 132 ? 3.575   -2.454  -34.051 1.00 39.72 ? 132  GLU J C   1 
ATOM   11019 O  O   . GLU J  1 132 ? 4.058   -3.343  -33.353 1.00 38.05 ? 132  GLU J O   1 
ATOM   11020 C  CB  . GLU J  1 132 ? 3.944   -2.996  -36.504 1.00 45.72 ? 132  GLU J CB  1 
ATOM   11021 C  CG  . GLU J  1 132 ? 4.451   -4.424  -36.608 1.00 48.86 ? 132  GLU J CG  1 
ATOM   11022 C  CD  . GLU J  1 132 ? 5.858   -4.502  -37.173 1.00 56.82 ? 132  GLU J CD  1 
ATOM   11023 O  OE1 . GLU J  1 132 ? 6.390   -3.448  -37.592 1.00 53.74 ? 132  GLU J OE1 1 
ATOM   11024 O  OE2 . GLU J  1 132 ? 6.430   -5.617  -37.193 1.00 57.99 ? 132  GLU J OE2 1 
ATOM   11025 N  N   . GLU J  1 133 ? 3.593   -1.166  -33.703 1.00 38.02 ? 133  GLU J N   1 
ATOM   11026 C  CA  . GLU J  1 133 ? 4.029   -0.717  -32.376 1.00 38.80 ? 133  GLU J CA  1 
ATOM   11027 C  C   . GLU J  1 133 ? 3.256   -1.430  -31.273 1.00 36.30 ? 133  GLU J C   1 
ATOM   11028 O  O   . GLU J  1 133 ? 3.824   -1.863  -30.273 1.00 34.95 ? 133  GLU J O   1 
ATOM   11029 C  CB  . GLU J  1 133 ? 3.817   0.791   -32.216 1.00 37.97 ? 133  GLU J CB  1 
ATOM   11030 C  CG  . GLU J  1 133 ? 4.985   1.635   -32.652 1.00 41.36 ? 133  GLU J CG  1 
ATOM   11031 C  CD  . GLU J  1 133 ? 6.256   1.267   -31.921 1.00 42.71 ? 133  GLU J CD  1 
ATOM   11032 O  OE1 . GLU J  1 133 ? 6.169   0.783   -30.769 1.00 36.92 ? 133  GLU J OE1 1 
ATOM   11033 O  OE2 . GLU J  1 133 ? 7.343   1.459   -32.507 1.00 48.93 ? 133  GLU J OE2 1 
ATOM   11034 N  N   . SER J  1 134 ? 1.947   -1.521  -31.469 1.00 35.47 ? 134  SER J N   1 
ATOM   11035 C  CA  . SER J  1 134 ? 1.061   -2.208  -30.555 1.00 33.17 ? 134  SER J CA  1 
ATOM   11036 C  C   . SER J  1 134 ? 1.616   -3.577  -30.158 1.00 33.94 ? 134  SER J C   1 
ATOM   11037 O  O   . SER J  1 134 ? 1.594   -3.935  -28.981 1.00 34.39 ? 134  SER J O   1 
ATOM   11038 C  CB  . SER J  1 134 ? -0.330  -2.338  -31.184 1.00 33.91 ? 134  SER J CB  1 
ATOM   11039 O  OG  . SER J  1 134 ? -1.237  -2.965  -30.299 1.00 34.26 ? 134  SER J OG  1 
ATOM   11040 N  N   . THR J  1 135 ? 2.129   -4.333  -31.127 1.00 33.58 ? 135  THR J N   1 
ATOM   11041 C  CA  . THR J  1 135 ? 2.647   -5.678  -30.847 1.00 34.98 ? 135  THR J CA  1 
ATOM   11042 C  C   . THR J  1 135 ? 3.975   -5.675  -30.076 1.00 34.48 ? 135  THR J C   1 
ATOM   11043 O  O   . THR J  1 135 ? 4.479   -6.735  -29.686 1.00 33.62 ? 135  THR J O   1 
ATOM   11044 C  CB  . THR J  1 135 ? 2.814   -6.530  -32.135 1.00 37.20 ? 135  THR J CB  1 
ATOM   11045 O  OG1 . THR J  1 135 ? 3.699   -5.870  -33.048 1.00 38.71 ? 135  THR J OG1 1 
ATOM   11046 C  CG2 . THR J  1 135 ? 1.476   -6.761  -32.810 1.00 41.51 ? 135  THR J CG2 1 
ATOM   11047 N  N   . LYS J  1 136 ? 4.520   -4.485  -29.844 1.00 33.58 ? 136  LYS J N   1 
ATOM   11048 C  CA  . LYS J  1 136 ? 5.834   -4.333  -29.219 1.00 34.70 ? 136  LYS J CA  1 
ATOM   11049 C  C   . LYS J  1 136 ? 5.799   -3.572  -27.890 1.00 29.40 ? 136  LYS J C   1 
ATOM   11050 O  O   . LYS J  1 136 ? 6.235   -4.075  -26.859 1.00 27.93 ? 136  LYS J O   1 
ATOM   11051 C  CB  . LYS J  1 136 ? 6.779   -3.608  -30.183 1.00 34.86 ? 136  LYS J CB  1 
ATOM   11052 C  CG  . LYS J  1 136 ? 7.316   -4.482  -31.301 1.00 38.74 ? 136  LYS J CG  1 
ATOM   11053 C  CD  . LYS J  1 136 ? 7.486   -3.677  -32.580 1.00 46.36 ? 136  LYS J CD  1 
ATOM   11054 C  CE  . LYS J  1 136 ? 8.146   -2.335  -32.311 1.00 45.10 ? 136  LYS J CE  1 
ATOM   11055 N  NZ  . LYS J  1 136 ? 9.553   -2.483  -31.841 1.00 45.88 ? 136  LYS J NZ  1 
ATOM   11056 N  N   . THR J  1 137 ? 5.293   -2.345  -27.944 1.00 30.23 ? 137  THR J N   1 
ATOM   11057 C  CA  . THR J  1 137 ? 5.310   -1.436  -26.812 1.00 28.49 ? 137  THR J CA  1 
ATOM   11058 C  C   . THR J  1 137 ? 3.900   -1.083  -26.349 1.00 28.31 ? 137  THR J C   1 
ATOM   11059 O  O   . THR J  1 137 ? 3.728   -0.505  -25.279 1.00 26.98 ? 137  THR J O   1 
ATOM   11060 C  CB  . THR J  1 137 ? 6.065   -0.131  -27.155 1.00 29.36 ? 137  THR J CB  1 
ATOM   11061 O  OG1 . THR J  1 137 ? 5.332   0.618   -28.133 1.00 29.20 ? 137  THR J OG1 1 
ATOM   11062 C  CG2 . THR J  1 137 ? 7.455   -0.441  -27.701 1.00 29.41 ? 137  THR J CG2 1 
ATOM   11063 N  N   . GLY J  1 138 ? 2.897   -1.443  -27.150 1.00 30.46 ? 138  GLY J N   1 
ATOM   11064 C  CA  . GLY J  1 138 ? 1.515   -1.097  -26.859 1.00 27.71 ? 138  GLY J CA  1 
ATOM   11065 C  C   . GLY J  1 138 ? 1.253   0.386   -27.085 1.00 27.50 ? 138  GLY J C   1 
ATOM   11066 O  O   . GLY J  1 138 ? 0.260   0.943   -26.629 1.00 25.32 ? 138  GLY J O   1 
ATOM   11067 N  N   . ASN J  1 139 ? 2.155   1.036   -27.804 1.00 30.24 ? 139  ASN J N   1 
ATOM   11068 C  CA  . ASN J  1 139 ? 1.980   2.442   -28.127 1.00 29.12 ? 139  ASN J CA  1 
ATOM   11069 C  C   . ASN J  1 139 ? 1.898   3.266   -26.849 1.00 25.61 ? 139  ASN J C   1 
ATOM   11070 O  O   . ASN J  1 139 ? 1.258   4.316   -26.819 1.00 25.70 ? 139  ASN J O   1 
ATOM   11071 C  CB  . ASN J  1 139 ? 0.732   2.645   -29.004 1.00 29.94 ? 139  ASN J CB  1 
ATOM   11072 C  CG  . ASN J  1 139 ? 0.923   2.138   -30.437 1.00 32.70 ? 139  ASN J CG  1 
ATOM   11073 O  OD1 . ASN J  1 139 ? 1.712   2.692   -31.204 1.00 32.69 ? 139  ASN J OD1 1 
ATOM   11074 N  ND2 . ASN J  1 139 ? 0.183   1.092   -30.801 1.00 31.10 ? 139  ASN J ND2 1 
ATOM   11075 N  N   . ALA J  1 140 ? 2.573   2.788   -25.804 1.00 25.93 ? 140  ALA J N   1 
ATOM   11076 C  CA  . ALA J  1 140 ? 2.537   3.429   -24.485 1.00 22.56 ? 140  ALA J CA  1 
ATOM   11077 C  C   . ALA J  1 140 ? 3.396   4.687   -24.398 1.00 21.92 ? 140  ALA J C   1 
ATOM   11078 O  O   . ALA J  1 140 ? 3.288   5.446   -23.446 1.00 22.12 ? 140  ALA J O   1 
ATOM   11079 C  CB  . ALA J  1 140 ? 2.917   2.445   -23.397 1.00 19.28 ? 140  ALA J CB  1 
ATOM   11080 N  N   . GLY J  1 141 ? 4.241   4.912   -25.395 1.00 22.19 ? 141  GLY J N   1 
ATOM   11081 C  CA  . GLY J  1 141 ? 4.953   6.170   -25.504 1.00 22.63 ? 141  GLY J CA  1 
ATOM   11082 C  C   . GLY J  1 141 ? 6.247   6.195   -24.731 1.00 24.72 ? 141  GLY J C   1 
ATOM   11083 O  O   . GLY J  1 141 ? 6.812   5.148   -24.420 1.00 26.57 ? 141  GLY J O   1 
ATOM   11084 N  N   . SER J  1 142 ? 6.715   7.395   -24.410 1.00 25.02 ? 142  SER J N   1 
ATOM   11085 C  CA  . SER J  1 142 ? 8.012   7.554   -23.770 1.00 23.01 ? 142  SER J CA  1 
ATOM   11086 C  C   . SER J  1 142 ? 7.997   7.087   -22.317 1.00 23.32 ? 142  SER J C   1 
ATOM   11087 O  O   . SER J  1 142 ? 6.950   6.804   -21.762 1.00 20.89 ? 142  SER J O   1 
ATOM   11088 C  CB  . SER J  1 142 ? 8.505   9.004   -23.878 1.00 24.12 ? 142  SER J CB  1 
ATOM   11089 O  OG  . SER J  1 142 ? 7.908   9.839   -22.899 1.00 26.17 ? 142  SER J OG  1 
ATOM   11090 N  N   . ARG J  1 143 ? 9.181   7.013   -21.718 1.00 25.93 ? 143  ARG J N   1 
ATOM   11091 C  CA  . ARG J  1 143 ? 9.357   6.546   -20.349 1.00 24.42 ? 143  ARG J CA  1 
ATOM   11092 C  C   . ARG J  1 143 ? 9.488   7.744   -19.419 1.00 23.12 ? 143  ARG J C   1 
ATOM   11093 O  O   . ARG J  1 143 ? 10.467  8.478   -19.500 1.00 25.15 ? 143  ARG J O   1 
ATOM   11094 C  CB  . ARG J  1 143 ? 10.604  5.641   -20.263 1.00 24.30 ? 143  ARG J CB  1 
ATOM   11095 C  CG  . ARG J  1 143 ? 10.732  4.681   -21.463 1.00 25.32 ? 143  ARG J CG  1 
ATOM   11096 C  CD  . ARG J  1 143 ? 11.970  3.775   -21.410 1.00 22.85 ? 143  ARG J CD  1 
ATOM   11097 N  NE  . ARG J  1 143 ? 11.946  2.815   -22.511 1.00 23.77 ? 143  ARG J NE  1 
ATOM   11098 C  CZ  . ARG J  1 143 ? 12.698  1.719   -22.586 1.00 22.57 ? 143  ARG J CZ  1 
ATOM   11099 N  NH1 . ARG J  1 143 ? 13.552  1.414   -21.629 1.00 24.24 ? 143  ARG J NH1 1 
ATOM   11100 N  NH2 . ARG J  1 143 ? 12.589  0.920   -23.627 1.00 24.69 ? 143  ARG J NH2 1 
ATOM   11101 N  N   . LEU J  1 144 ? 8.503   7.934   -18.540 1.00 21.25 ? 144  LEU J N   1 
ATOM   11102 C  CA  . LEU J  1 144 ? 8.439   9.107   -17.671 1.00 20.46 ? 144  LEU J CA  1 
ATOM   11103 C  C   . LEU J  1 144 ? 9.287   8.960   -16.414 1.00 20.93 ? 144  LEU J C   1 
ATOM   11104 O  O   . LEU J  1 144 ? 9.855   9.935   -15.917 1.00 20.55 ? 144  LEU J O   1 
ATOM   11105 C  CB  . LEU J  1 144 ? 6.994   9.376   -17.255 1.00 20.45 ? 144  LEU J CB  1 
ATOM   11106 C  CG  . LEU J  1 144 ? 5.982   9.670   -18.353 1.00 21.55 ? 144  LEU J CG  1 
ATOM   11107 C  CD1 . LEU J  1 144 ? 4.653   10.068  -17.723 1.00 19.35 ? 144  LEU J CD1 1 
ATOM   11108 C  CD2 . LEU J  1 144 ? 6.522   10.755  -19.280 1.00 21.80 ? 144  LEU J CD2 1 
ATOM   11109 N  N   . ALA J  1 145 ? 9.342   7.742   -15.883 1.00 20.01 ? 145  ALA J N   1 
ATOM   11110 C  CA  . ALA J  1 145 ? 10.161  7.451   -14.713 1.00 19.46 ? 145  ALA J CA  1 
ATOM   11111 C  C   . ALA J  1 145 ? 10.427  5.960   -14.619 1.00 18.76 ? 145  ALA J C   1 
ATOM   11112 O  O   . ALA J  1 145 ? 9.640   5.153   -15.089 1.00 20.61 ? 145  ALA J O   1 
ATOM   11113 C  CB  . ALA J  1 145 ? 9.490   7.946   -13.445 1.00 16.38 ? 145  ALA J CB  1 
ATOM   11114 N  N   . CYS J  1 146 ? 11.542  5.603   -13.999 1.00 20.36 ? 146  CYS J N   1 
ATOM   11115 C  CA  . CYS J  1 146 ? 11.902  4.211   -13.821 1.00 20.82 ? 146  CYS J CA  1 
ATOM   11116 C  C   . CYS J  1 146 ? 12.757  4.051   -12.574 1.00 19.24 ? 146  CYS J C   1 
ATOM   11117 O  O   . CYS J  1 146 ? 13.279  5.017   -12.032 1.00 19.65 ? 146  CYS J O   1 
ATOM   11118 C  CB  . CYS J  1 146 ? 12.657  3.679   -15.045 1.00 22.76 ? 146  CYS J CB  1 
ATOM   11119 S  SG  . CYS J  1 146 ? 14.295  4.419   -15.322 1.00 27.69 ? 146  CYS J SG  1 
ATOM   11120 N  N   . GLY J  1 147 ? 12.877  2.816   -12.123 1.00 16.64 ? 147  GLY J N   1 
ATOM   11121 C  CA  . GLY J  1 147 ? 13.727  2.489   -11.007 1.00 18.46 ? 147  GLY J CA  1 
ATOM   11122 C  C   . GLY J  1 147 ? 14.060  1.022   -11.133 1.00 20.30 ? 147  GLY J C   1 
ATOM   11123 O  O   . GLY J  1 147 ? 13.365  0.276   -11.824 1.00 19.22 ? 147  GLY J O   1 
ATOM   11124 N  N   . VAL J  1 148 ? 15.138  0.615   -10.477 1.00 20.94 ? 148  VAL J N   1 
ATOM   11125 C  CA  . VAL J  1 148 ? 15.583  -0.768  -10.493 1.00 20.62 ? 148  VAL J CA  1 
ATOM   11126 C  C   . VAL J  1 148 ? 14.849  -1.495  -9.384  1.00 18.57 ? 148  VAL J C   1 
ATOM   11127 O  O   . VAL J  1 148 ? 14.714  -0.974  -8.280  1.00 16.00 ? 148  VAL J O   1 
ATOM   11128 C  CB  . VAL J  1 148 ? 17.126  -0.871  -10.283 1.00 20.31 ? 148  VAL J CB  1 
ATOM   11129 C  CG1 . VAL J  1 148 ? 17.594  -2.327  -10.328 1.00 19.32 ? 148  VAL J CG1 1 
ATOM   11130 C  CG2 . VAL J  1 148 ? 17.858  -0.039  -11.325 1.00 19.19 ? 148  VAL J CG2 1 
ATOM   11131 N  N   . ILE J  1 149 ? 14.368  -2.695  -9.692  1.00 19.84 ? 149  ILE J N   1 
ATOM   11132 C  CA  . ILE J  1 149 ? 13.646  -3.512  -8.724  1.00 20.80 ? 149  ILE J CA  1 
ATOM   11133 C  C   . ILE J  1 149 ? 14.618  -4.206  -7.763  1.00 21.78 ? 149  ILE J C   1 
ATOM   11134 O  O   . ILE J  1 149 ? 15.419  -5.059  -8.168  1.00 22.66 ? 149  ILE J O   1 
ATOM   11135 C  CB  . ILE J  1 149 ? 12.730  -4.546  -9.427  1.00 21.23 ? 149  ILE J CB  1 
ATOM   11136 C  CG1 . ILE J  1 149 ? 11.706  -3.824  -10.306 1.00 18.67 ? 149  ILE J CG1 1 
ATOM   11137 C  CG2 . ILE J  1 149 ? 12.029  -5.440  -8.395  1.00 20.21 ? 149  ILE J CG2 1 
ATOM   11138 C  CD1 . ILE J  1 149 ? 10.942  -4.736  -11.228 1.00 21.07 ? 149  ILE J CD1 1 
ATOM   11139 N  N   . GLY J  1 150 ? 14.552  -3.831  -6.489  1.00 21.15 ? 150  GLY J N   1 
ATOM   11140 C  CA  . GLY J  1 150 ? 15.478  -4.366  -5.514  1.00 20.07 ? 150  GLY J CA  1 
ATOM   11141 C  C   . GLY J  1 150 ? 14.823  -5.197  -4.430  1.00 21.33 ? 150  GLY J C   1 
ATOM   11142 O  O   . GLY J  1 150 ? 13.633  -5.083  -4.177  1.00 21.52 ? 150  GLY J O   1 
ATOM   11143 N  N   . ILE J  1 151 ? 15.627  -6.041  -3.790  1.00 24.82 ? 151  ILE J N   1 
ATOM   11144 C  CA  . ILE J  1 151 ? 15.214  -6.819  -2.623  1.00 24.33 ? 151  ILE J CA  1 
ATOM   11145 C  C   . ILE J  1 151 ? 14.868  -5.910  -1.433  1.00 23.08 ? 151  ILE J C   1 
ATOM   11146 O  O   . ILE J  1 151 ? 15.607  -4.973  -1.133  1.00 21.97 ? 151  ILE J O   1 
ATOM   11147 C  CB  . ILE J  1 151 ? 16.340  -7.819  -2.226  1.00 24.40 ? 151  ILE J CB  1 
ATOM   11148 C  CG1 . ILE J  1 151 ? 16.676  -8.739  -3.405  1.00 21.77 ? 151  ILE J CG1 1 
ATOM   11149 C  CG2 . ILE J  1 151 ? 15.953  -8.614  -0.983  1.00 27.13 ? 151  ILE J CG2 1 
ATOM   11150 C  CD1 . ILE J  1 151 ? 17.845  -9.682  -3.142  1.00 24.01 ? 151  ILE J CD1 1 
ATOM   11151 N  N   . ALA J  1 152 ? 13.742  -6.192  -0.773  1.00 23.81 ? 152  ALA J N   1 
ATOM   11152 C  CA  . ALA J  1 152 ? 13.276  -5.427  0.384   1.00 23.72 ? 152  ALA J CA  1 
ATOM   11153 C  C   . ALA J  1 152 ? 13.109  -6.374  1.564   1.00 30.35 ? 152  ALA J C   1 
ATOM   11154 O  O   . ALA J  1 152 ? 13.078  -7.592  1.382   1.00 33.34 ? 152  ALA J O   1 
ATOM   11155 C  CB  . ALA J  1 152 ? 11.943  -4.760  0.078   1.00 23.76 ? 152  ALA J CB  1 
ATOM   11156 N  N   . GLN J  1 153 ? 13.001  -5.833  2.775   1.00 31.42 ? 153  GLN J N   1 
ATOM   11157 C  CA  . GLN J  1 153 ? 12.677  -6.678  3.919   1.00 33.95 ? 153  GLN J CA  1 
ATOM   11158 C  C   . GLN J  1 153 ? 11.180  -6.619  4.223   1.00 43.74 ? 153  GLN J C   1 
ATOM   11159 O  O   . GLN J  1 153 ? 10.574  -7.638  4.577   1.00 51.06 ? 153  GLN J O   1 
ATOM   11160 C  CB  . GLN J  1 153 ? 13.481  -6.278  5.152   1.00 36.16 ? 153  GLN J CB  1 
ATOM   11161 C  CG  . GLN J  1 153 ? 13.051  -4.969  5.793   1.00 37.60 ? 153  GLN J CG  1 
ATOM   11162 C  CD  . GLN J  1 153 ? 13.872  -4.641  7.023   1.00 39.31 ? 153  GLN J CD  1 
ATOM   11163 O  OE1 . GLN J  1 153 ? 14.395  -5.539  7.699   1.00 34.39 ? 153  GLN J OE1 1 
ATOM   11164 N  NE2 . GLN J  1 153 ? 14.005  -3.347  7.315   1.00 43.66 ? 153  GLN J NE2 1 
ATOM   11165 O  OXT . GLN J  1 153 ? 10.541  -5.561  4.110   1.00 43.20 ? 153  GLN J OXT 1 
ATOM   11166 N  N   . ALA K  1 1   ? 33.316  -14.429 37.287  1.00 46.10 ? 1    ALA K N   1 
ATOM   11167 C  CA  . ALA K  1 1   ? 32.996  -13.111 36.744  1.00 44.13 ? 1    ALA K CA  1 
ATOM   11168 C  C   . ALA K  1 1   ? 33.947  -12.012 37.239  1.00 41.11 ? 1    ALA K C   1 
ATOM   11169 O  O   . ALA K  1 1   ? 33.512  -11.067 37.906  1.00 41.44 ? 1    ALA K O   1 
ATOM   11170 C  CB  . ALA K  1 1   ? 31.539  -12.748 37.060  1.00 43.51 ? 1    ALA K CB  1 
ATOM   11171 N  N   . THR K  1 2   ? 35.237  -12.136 36.908  1.00 42.44 ? 2    THR K N   1 
ATOM   11172 C  CA  . THR K  1 2   ? 36.235  -11.128 37.295  1.00 35.58 ? 2    THR K CA  1 
ATOM   11173 C  C   . THR K  1 2   ? 36.008  -9.844  36.506  1.00 33.19 ? 2    THR K C   1 
ATOM   11174 O  O   . THR K  1 2   ? 35.674  -9.869  35.318  1.00 35.50 ? 2    THR K O   1 
ATOM   11175 C  CB  . THR K  1 2   ? 37.696  -11.613 37.105  1.00 34.08 ? 2    THR K CB  1 
ATOM   11176 O  OG1 . THR K  1 2   ? 37.776  -13.030 37.305  1.00 40.13 ? 2    THR K OG1 1 
ATOM   11177 C  CG2 . THR K  1 2   ? 38.625  -10.922 38.086  1.00 30.66 ? 2    THR K CG2 1 
ATOM   11178 N  N   . LYS K  1 3   ? 36.165  -8.718  37.187  1.00 33.52 ? 3    LYS K N   1 
ATOM   11179 C  CA  . LYS K  1 3   ? 35.902  -7.417  36.597  1.00 32.62 ? 3    LYS K CA  1 
ATOM   11180 C  C   . LYS K  1 3   ? 37.042  -6.510  37.017  1.00 30.79 ? 3    LYS K C   1 
ATOM   11181 O  O   . LYS K  1 3   ? 37.578  -6.656  38.114  1.00 31.40 ? 3    LYS K O   1 
ATOM   11182 C  CB  . LYS K  1 3   ? 34.567  -6.869  37.112  1.00 34.81 ? 3    LYS K CB  1 
ATOM   11183 C  CG  . LYS K  1 3   ? 33.634  -6.356  36.029  1.00 38.44 ? 3    LYS K CG  1 
ATOM   11184 C  CD  . LYS K  1 3   ? 32.203  -6.225  36.537  1.00 43.34 ? 3    LYS K CD  1 
ATOM   11185 C  CE  . LYS K  1 3   ? 31.855  -4.777  36.874  1.00 47.27 ? 3    LYS K CE  1 
ATOM   11186 N  NZ  . LYS K  1 3   ? 31.627  -3.929  35.658  1.00 53.42 ? 3    LYS K NZ  1 
ATOM   11187 N  N   . ALA K  1 4   ? 37.424  -5.591  36.141  1.00 27.40 ? 4    ALA K N   1 
ATOM   11188 C  CA  . ALA K  1 4   ? 38.506  -4.665  36.426  1.00 27.95 ? 4    ALA K CA  1 
ATOM   11189 C  C   . ALA K  1 4   ? 38.157  -3.312  35.838  1.00 26.88 ? 4    ALA K C   1 
ATOM   11190 O  O   . ALA K  1 4   ? 37.191  -3.184  35.100  1.00 26.15 ? 4    ALA K O   1 
ATOM   11191 C  CB  . ALA K  1 4   ? 39.810  -5.176  35.850  1.00 26.68 ? 4    ALA K CB  1 
ATOM   11192 N  N   . VAL K  1 5   ? 38.929  -2.292  36.180  1.00 26.42 ? 5    VAL K N   1 
ATOM   11193 C  CA  . VAL K  1 5   ? 38.655  -0.955  35.673  1.00 26.83 ? 5    VAL K CA  1 
ATOM   11194 C  C   . VAL K  1 5   ? 39.940  -0.143  35.705  1.00 29.33 ? 5    VAL K C   1 
ATOM   11195 O  O   . VAL K  1 5   ? 40.883  -0.465  36.433  1.00 30.65 ? 5    VAL K O   1 
ATOM   11196 C  CB  . VAL K  1 5   ? 37.483  -0.240  36.438  1.00 26.37 ? 5    VAL K CB  1 
ATOM   11197 C  CG1 . VAL K  1 5   ? 37.836  -0.003  37.901  1.00 27.42 ? 5    VAL K CG1 1 
ATOM   11198 C  CG2 . VAL K  1 5   ? 37.096  1.065   35.761  1.00 23.76 ? 5    VAL K CG2 1 
ATOM   11199 N  N   . CYS K  1 6   ? 39.987  0.900   34.892  1.00 30.18 ? 6    CYS K N   1 
ATOM   11200 C  CA  . CYS K  1 6   ? 41.181  1.710   34.791  1.00 30.87 ? 6    CYS K CA  1 
ATOM   11201 C  C   . CYS K  1 6   ? 40.775  3.145   34.489  1.00 32.17 ? 6    CYS K C   1 
ATOM   11202 O  O   . CYS K  1 6   ? 39.937  3.389   33.617  1.00 28.93 ? 6    CYS K O   1 
ATOM   11203 C  CB  . CYS K  1 6   ? 42.069  1.159   33.678  1.00 32.17 ? 6    CYS K CB  1 
ATOM   11204 S  SG  . CYS K  1 6   ? 43.697  1.895   33.560  1.00 38.03 ? 6    CYS K SG  1 
ATOM   11205 N  N   . VAL K  1 7   ? 41.355  4.084   35.236  1.00 33.91 ? 7    VAL K N   1 
ATOM   11206 C  CA  . VAL K  1 7   ? 41.145  5.507   34.995  1.00 33.28 ? 7    VAL K CA  1 
ATOM   11207 C  C   . VAL K  1 7   ? 42.412  6.064   34.348  1.00 32.86 ? 7    VAL K C   1 
ATOM   11208 O  O   . VAL K  1 7   ? 43.510  5.870   34.858  1.00 33.89 ? 7    VAL K O   1 
ATOM   11209 C  CB  . VAL K  1 7   ? 40.824  6.268   36.310  1.00 36.94 ? 7    VAL K CB  1 
ATOM   11210 C  CG1 . VAL K  1 7   ? 40.615  7.758   36.044  1.00 34.93 ? 7    VAL K CG1 1 
ATOM   11211 C  CG2 . VAL K  1 7   ? 39.607  5.660   36.997  1.00 33.34 ? 7    VAL K CG2 1 
ATOM   11212 N  N   . LEU K  1 8   ? 42.268  6.725   33.208  1.00 33.00 ? 8    LEU K N   1 
ATOM   11213 C  CA  . LEU K  1 8   ? 43.425  7.258   32.505  1.00 33.20 ? 8    LEU K CA  1 
ATOM   11214 C  C   . LEU K  1 8   ? 43.552  8.768   32.747  1.00 35.73 ? 8    LEU K C   1 
ATOM   11215 O  O   . LEU K  1 8   ? 42.630  9.526   32.426  1.00 33.40 ? 8    LEU K O   1 
ATOM   11216 C  CB  . LEU K  1 8   ? 43.336  6.961   30.998  1.00 32.38 ? 8    LEU K CB  1 
ATOM   11217 C  CG  . LEU K  1 8   ? 43.083  5.540   30.457  1.00 35.03 ? 8    LEU K CG  1 
ATOM   11218 C  CD1 . LEU K  1 8   ? 43.344  5.479   28.945  1.00 33.26 ? 8    LEU K CD1 1 
ATOM   11219 C  CD2 . LEU K  1 8   ? 43.906  4.485   31.173  1.00 32.54 ? 8    LEU K CD2 1 
ATOM   11220 N  N   . LYS K  1 9   ? 44.690  9.188   33.317  1.00 37.12 ? 9    LYS K N   1 
ATOM   11221 C  CA  . LYS K  1 9   ? 44.980  10.602  33.589  1.00 37.55 ? 9    LYS K CA  1 
ATOM   11222 C  C   . LYS K  1 9   ? 46.338  11.016  32.994  1.00 38.88 ? 9    LYS K C   1 
ATOM   11223 O  O   . LYS K  1 9   ? 47.305  10.241  33.030  1.00 37.12 ? 9    LYS K O   1 
ATOM   11224 C  CB  . LYS K  1 9   ? 44.986  10.889  35.105  1.00 36.94 ? 9    LYS K CB  1 
ATOM   11225 C  CG  . LYS K  1 9   ? 43.756  10.418  35.901  1.00 43.75 ? 9    LYS K CG  1 
ATOM   11226 C  CD  . LYS K  1 9   ? 44.086  10.298  37.412  1.00 44.53 ? 9    LYS K CD  1 
ATOM   11227 C  CE  . LYS K  1 9   ? 42.942  9.698   38.263  1.00 43.60 ? 9    LYS K CE  1 
ATOM   11228 N  NZ  . LYS K  1 9   ? 42.066  10.717  38.939  1.00 41.06 ? 9    LYS K NZ  1 
ATOM   11229 N  N   . GLY K  1 10  ? 46.412  12.241  32.472  1.00 39.40 ? 10   GLY K N   1 
ATOM   11230 C  CA  . GLY K  1 10  ? 47.659  12.777  31.943  1.00 42.84 ? 10   GLY K CA  1 
ATOM   11231 C  C   . GLY K  1 10  ? 47.802  14.294  32.023  1.00 44.31 ? 10   GLY K C   1 
ATOM   11232 O  O   . GLY K  1 10  ? 47.025  14.969  32.688  1.00 45.68 ? 10   GLY K O   1 
ATOM   11233 N  N   . ASP K  1 11  ? 48.795  14.834  31.324  1.00 44.64 ? 11   ASP K N   1 
ATOM   11234 C  CA  . ASP K  1 11  ? 49.135  16.251  31.432  1.00 45.06 ? 11   ASP K CA  1 
ATOM   11235 C  C   . ASP K  1 11  ? 48.429  17.118  30.388  1.00 48.22 ? 11   ASP K C   1 
ATOM   11236 O  O   . ASP K  1 11  ? 48.594  18.347  30.371  1.00 50.41 ? 11   ASP K O   1 
ATOM   11237 C  CB  . ASP K  1 11  ? 50.654  16.439  31.316  1.00 48.03 ? 11   ASP K CB  1 
ATOM   11238 C  CG  . ASP K  1 11  ? 51.434  15.488  32.210  1.00 52.49 ? 11   ASP K CG  1 
ATOM   11239 O  OD1 . ASP K  1 11  ? 51.072  15.358  33.398  1.00 54.99 ? 11   ASP K OD1 1 
ATOM   11240 O  OD2 . ASP K  1 11  ? 52.410  14.873  31.727  1.00 54.86 ? 11   ASP K OD2 1 
ATOM   11241 N  N   . GLY K  1 12  ? 47.645  16.486  29.518  1.00 45.83 ? 12   GLY K N   1 
ATOM   11242 C  CA  . GLY K  1 12  ? 46.948  17.206  28.464  1.00 41.03 ? 12   GLY K CA  1 
ATOM   11243 C  C   . GLY K  1 12  ? 45.437  17.093  28.552  1.00 39.71 ? 12   GLY K C   1 
ATOM   11244 O  O   . GLY K  1 12  ? 44.879  16.874  29.631  1.00 40.53 ? 12   GLY K O   1 
ATOM   11245 N  N   . PRO K  1 13  ? 44.754  17.242  27.411  1.00 38.58 ? 13   PRO K N   1 
ATOM   11246 C  CA  . PRO K  1 13  ? 43.292  17.115  27.419  1.00 40.67 ? 13   PRO K CA  1 
ATOM   11247 C  C   . PRO K  1 13  ? 42.796  15.650  27.441  1.00 42.57 ? 13   PRO K C   1 
ATOM   11248 O  O   . PRO K  1 13  ? 41.593  15.427  27.258  1.00 43.33 ? 13   PRO K O   1 
ATOM   11249 C  CB  . PRO K  1 13  ? 42.866  17.808  26.107  1.00 41.21 ? 13   PRO K CB  1 
ATOM   11250 C  CG  . PRO K  1 13  ? 44.143  18.362  25.470  1.00 38.03 ? 13   PRO K CG  1 
ATOM   11251 C  CD  . PRO K  1 13  ? 45.279  17.606  26.083  1.00 40.88 ? 13   PRO K CD  1 
ATOM   11252 N  N   . VAL K  1 14  ? 43.688  14.684  27.680  1.00 42.43 ? 14   VAL K N   1 
ATOM   11253 C  CA  . VAL K  1 14  ? 43.350  13.258  27.532  1.00 40.66 ? 14   VAL K CA  1 
ATOM   11254 C  C   . VAL K  1 14  ? 43.025  12.505  28.849  1.00 39.88 ? 14   VAL K C   1 
ATOM   11255 O  O   . VAL K  1 14  ? 43.886  12.332  29.720  1.00 34.14 ? 14   VAL K O   1 
ATOM   11256 C  CB  . VAL K  1 14  ? 44.443  12.489  26.716  1.00 38.51 ? 14   VAL K CB  1 
ATOM   11257 C  CG1 . VAL K  1 14  ? 44.036  11.038  26.499  1.00 36.79 ? 14   VAL K CG1 1 
ATOM   11258 C  CG2 . VAL K  1 14  ? 44.700  13.176  25.375  1.00 37.36 ? 14   VAL K CG2 1 
ATOM   11259 N  N   . GLN K  1 15  ? 41.777  12.037  28.951  1.00 40.81 ? 15   GLN K N   1 
ATOM   11260 C  CA  . GLN K  1 15  ? 41.261  11.318  30.122  1.00 37.33 ? 15   GLN K CA  1 
ATOM   11261 C  C   . GLN K  1 15  ? 40.170  10.307  29.723  1.00 33.16 ? 15   GLN K C   1 
ATOM   11262 O  O   . GLN K  1 15  ? 39.346  10.593  28.857  1.00 37.57 ? 15   GLN K O   1 
ATOM   11263 C  CB  . GLN K  1 15  ? 40.697  12.317  31.144  1.00 39.75 ? 15   GLN K CB  1 
ATOM   11264 C  CG  . GLN K  1 15  ? 39.955  13.493  30.501  1.00 40.54 ? 15   GLN K CG  1 
ATOM   11265 C  CD  . GLN K  1 15  ? 39.176  14.345  31.497  1.00 47.33 ? 15   GLN K CD  1 
ATOM   11266 O  OE1 . GLN K  1 15  ? 39.429  15.545  31.631  1.00 45.16 ? 15   GLN K OE1 1 
ATOM   11267 N  NE2 . GLN K  1 15  ? 38.217  13.729  32.190  1.00 46.99 ? 15   GLN K NE2 1 
ATOM   11268 N  N   . GLY K  1 16  ? 40.161  9.137   30.355  1.00 27.76 ? 16   GLY K N   1 
ATOM   11269 C  CA  . GLY K  1 16  ? 39.158  8.124   30.073  1.00 28.43 ? 16   GLY K CA  1 
ATOM   11270 C  C   . GLY K  1 16  ? 38.937  7.124   31.205  1.00 31.98 ? 16   GLY K C   1 
ATOM   11271 O  O   . GLY K  1 16  ? 39.665  7.108   32.197  1.00 31.23 ? 16   GLY K O   1 
ATOM   11272 N  N   . ILE K  1 17  ? 37.907  6.296   31.060  1.00 31.65 ? 17   ILE K N   1 
ATOM   11273 C  CA  . ILE K  1 17  ? 37.647  5.201   31.985  1.00 30.04 ? 17   ILE K CA  1 
ATOM   11274 C  C   . ILE K  1 17  ? 37.471  3.966   31.129  1.00 28.06 ? 17   ILE K C   1 
ATOM   11275 O  O   . ILE K  1 17  ? 36.779  4.008   30.129  1.00 27.55 ? 17   ILE K O   1 
ATOM   11276 C  CB  . ILE K  1 17  ? 36.364  5.429   32.815  1.00 31.96 ? 17   ILE K CB  1 
ATOM   11277 C  CG1 . ILE K  1 17  ? 36.529  6.641   33.741  1.00 35.01 ? 17   ILE K CG1 1 
ATOM   11278 C  CG2 . ILE K  1 17  ? 36.000  4.174   33.623  1.00 28.22 ? 17   ILE K CG2 1 
ATOM   11279 C  CD1 . ILE K  1 17  ? 35.303  6.924   34.607  1.00 30.70 ? 17   ILE K CD1 1 
ATOM   11280 N  N   . ILE K  1 18  ? 38.113  2.870   31.502  1.00 28.56 ? 18   ILE K N   1 
ATOM   11281 C  CA  . ILE K  1 18  ? 38.047  1.665   30.693  1.00 25.92 ? 18   ILE K CA  1 
ATOM   11282 C  C   . ILE K  1 18  ? 37.724  0.513   31.612  1.00 23.99 ? 18   ILE K C   1 
ATOM   11283 O  O   . ILE K  1 18  ? 38.365  0.336   32.632  1.00 25.63 ? 18   ILE K O   1 
ATOM   11284 C  CB  . ILE K  1 18  ? 39.370  1.417   29.905  1.00 26.07 ? 18   ILE K CB  1 
ATOM   11285 C  CG1 . ILE K  1 18  ? 39.587  2.509   28.854  1.00 21.82 ? 18   ILE K CG1 1 
ATOM   11286 C  CG2 . ILE K  1 18  ? 39.370  0.041   29.224  1.00 22.67 ? 18   ILE K CG2 1 
ATOM   11287 C  CD1 . ILE K  1 18  ? 38.785  2.309   27.591  1.00 23.29 ? 18   ILE K CD1 1 
ATOM   11288 N  N   . ASN K  1 19  ? 36.705  -0.252  31.253  1.00 22.20 ? 19   ASN K N   1 
ATOM   11289 C  CA  . ASN K  1 19  ? 36.247  -1.363  32.062  1.00 24.68 ? 19   ASN K CA  1 
ATOM   11290 C  C   . ASN K  1 19  ? 36.708  -2.649  31.427  1.00 24.38 ? 19   ASN K C   1 
ATOM   11291 O  O   . ASN K  1 19  ? 36.932  -2.702  30.226  1.00 24.41 ? 19   ASN K O   1 
ATOM   11292 C  CB  . ASN K  1 19  ? 34.719  -1.341  32.175  1.00 26.51 ? 19   ASN K CB  1 
ATOM   11293 C  CG  . ASN K  1 19  ? 34.196  -0.025  32.741  1.00 27.29 ? 19   ASN K CG  1 
ATOM   11294 O  OD1 . ASN K  1 19  ? 34.322  0.240   33.937  1.00 28.67 ? 19   ASN K OD1 1 
ATOM   11295 N  ND2 . ASN K  1 19  ? 33.612  0.806   31.880  1.00 25.47 ? 19   ASN K ND2 1 
ATOM   11296 N  N   . PHE K  1 20  ? 36.858  -3.684  32.233  1.00 23.96 ? 20   PHE K N   1 
ATOM   11297 C  CA  . PHE K  1 20  ? 37.255  -4.988  31.735  1.00 25.19 ? 20   PHE K CA  1 
ATOM   11298 C  C   . PHE K  1 20  ? 36.289  -5.974  32.320  1.00 29.45 ? 20   PHE K C   1 
ATOM   11299 O  O   . PHE K  1 20  ? 35.820  -5.798  33.439  1.00 31.49 ? 20   PHE K O   1 
ATOM   11300 C  CB  . PHE K  1 20  ? 38.671  -5.346  32.184  1.00 25.35 ? 20   PHE K CB  1 
ATOM   11301 C  CG  . PHE K  1 20  ? 39.698  -4.347  31.771  1.00 25.53 ? 20   PHE K CG  1 
ATOM   11302 C  CD1 . PHE K  1 20  ? 39.822  -3.142  32.444  1.00 25.99 ? 20   PHE K CD1 1 
ATOM   11303 C  CD2 . PHE K  1 20  ? 40.527  -4.595  30.694  1.00 26.40 ? 20   PHE K CD2 1 
ATOM   11304 C  CE1 . PHE K  1 20  ? 40.763  -2.201  32.050  1.00 27.03 ? 20   PHE K CE1 1 
ATOM   11305 C  CE2 . PHE K  1 20  ? 41.472  -3.662  30.300  1.00 28.49 ? 20   PHE K CE2 1 
ATOM   11306 C  CZ  . PHE K  1 20  ? 41.588  -2.462  30.979  1.00 26.09 ? 20   PHE K CZ  1 
ATOM   11307 N  N   . GLU K  1 21  ? 35.987  -7.016  31.566  1.00 31.76 ? 21   GLU K N   1 
ATOM   11308 C  CA  . GLU K  1 21  ? 35.048  -8.019  32.022  1.00 36.14 ? 21   GLU K CA  1 
ATOM   11309 C  C   . GLU K  1 21  ? 35.519  -9.355  31.491  1.00 34.93 ? 21   GLU K C   1 
ATOM   11310 O  O   . GLU K  1 21  ? 35.726  -9.514  30.297  1.00 35.25 ? 21   GLU K O   1 
ATOM   11311 C  CB  . GLU K  1 21  ? 33.637  -7.690  31.514  1.00 38.65 ? 21   GLU K CB  1 
ATOM   11312 C  CG  . GLU K  1 21  ? 32.544  -8.663  31.942  1.00 43.94 ? 21   GLU K CG  1 
ATOM   11313 C  CD  . GLU K  1 21  ? 31.161  -8.222  31.474  1.00 53.42 ? 21   GLU K CD  1 
ATOM   11314 O  OE1 . GLU K  1 21  ? 30.520  -7.420  32.192  1.00 55.52 ? 21   GLU K OE1 1 
ATOM   11315 O  OE2 . GLU K  1 21  ? 30.720  -8.676  30.392  1.00 53.26 ? 21   GLU K OE2 1 
ATOM   11316 N  N   . GLN K  1 22  ? 35.711  -10.314 32.382  1.00 35.18 ? 22   GLN K N   1 
ATOM   11317 C  CA  . GLN K  1 22  ? 36.054  -11.652 31.950  1.00 37.04 ? 22   GLN K CA  1 
ATOM   11318 C  C   . GLN K  1 22  ? 35.124  -12.659 32.607  1.00 40.68 ? 22   GLN K C   1 
ATOM   11319 O  O   . GLN K  1 22  ? 35.393  -13.161 33.692  1.00 39.17 ? 22   GLN K O   1 
ATOM   11320 C  CB  . GLN K  1 22  ? 37.506  -11.971 32.267  1.00 35.25 ? 22   GLN K CB  1 
ATOM   11321 C  CG  . GLN K  1 22  ? 38.025  -13.183 31.530  1.00 35.92 ? 22   GLN K CG  1 
ATOM   11322 C  CD  . GLN K  1 22  ? 39.447  -13.492 31.901  1.00 36.48 ? 22   GLN K CD  1 
ATOM   11323 O  OE1 . GLN K  1 22  ? 39.944  -13.035 32.935  1.00 33.21 ? 22   GLN K OE1 1 
ATOM   11324 N  NE2 . GLN K  1 22  ? 40.117  -14.271 31.065  1.00 37.68 ? 22   GLN K NE2 1 
ATOM   11325 N  N   . LYS K  1 23  ? 34.018  -12.930 31.923  1.00 47.90 ? 23   LYS K N   1 
ATOM   11326 C  CA  . LYS K  1 23  ? 33.013  -13.891 32.367  1.00 49.52 ? 23   LYS K CA  1 
ATOM   11327 C  C   . LYS K  1 23  ? 33.644  -15.221 32.788  1.00 48.52 ? 23   LYS K C   1 
ATOM   11328 O  O   . LYS K  1 23  ? 33.279  -15.790 33.816  1.00 47.80 ? 23   LYS K O   1 
ATOM   11329 C  CB  . LYS K  1 23  ? 31.976  -14.123 31.253  1.00 49.42 ? 23   LYS K CB  1 
ATOM   11330 C  CG  . LYS K  1 23  ? 31.054  -12.927 30.953  1.00 54.38 ? 23   LYS K CG  1 
ATOM   11331 C  CD  . LYS K  1 23  ? 31.813  -11.631 30.575  1.00 52.43 ? 23   LYS K CD  1 
ATOM   11332 C  CE  . LYS K  1 23  ? 32.272  -11.588 29.108  1.00 49.18 ? 23   LYS K CE  1 
ATOM   11333 N  NZ  . LYS K  1 23  ? 33.577  -12.275 28.855  1.00 42.88 ? 23   LYS K NZ  1 
ATOM   11334 N  N   . GLU K  1 24  ? 34.602  -15.702 32.000  1.00 46.20 ? 24   GLU K N   1 
ATOM   11335 C  CA  . GLU K  1 24  ? 35.153  -17.041 32.194  1.00 45.98 ? 24   GLU K CA  1 
ATOM   11336 C  C   . GLU K  1 24  ? 36.672  -17.056 32.387  1.00 46.54 ? 24   GLU K C   1 
ATOM   11337 O  O   . GLU K  1 24  ? 37.400  -16.289 31.757  1.00 46.96 ? 24   GLU K O   1 
ATOM   11338 C  CB  . GLU K  1 24  ? 34.762  -17.946 31.019  1.00 49.36 ? 24   GLU K CB  1 
ATOM   11339 C  CG  . GLU K  1 24  ? 33.253  -18.110 30.823  1.00 49.50 ? 24   GLU K CG  1 
ATOM   11340 C  CD  . GLU K  1 24  ? 32.623  -19.025 31.864  1.00 56.83 ? 24   GLU K CD  1 
ATOM   11341 O  OE1 . GLU K  1 24  ? 31.378  -19.023 31.993  1.00 58.85 ? 24   GLU K OE1 1 
ATOM   11342 O  OE2 . GLU K  1 24  ? 33.375  -19.747 32.558  1.00 56.49 ? 24   GLU K OE2 1 
ATOM   11343 N  N   . SER K  1 25  ? 37.132  -17.952 33.257  1.00 48.19 ? 25   SER K N   1 
ATOM   11344 C  CA  . SER K  1 25  ? 38.549  -18.104 33.593  1.00 47.94 ? 25   SER K CA  1 
ATOM   11345 C  C   . SER K  1 25  ? 39.458  -18.151 32.360  1.00 50.71 ? 25   SER K C   1 
ATOM   11346 O  O   . SER K  1 25  ? 40.537  -17.546 32.340  1.00 48.51 ? 25   SER K O   1 
ATOM   11347 C  CB  . SER K  1 25  ? 38.742  -19.368 34.442  1.00 45.39 ? 25   SER K CB  1 
ATOM   11348 O  OG  . SER K  1 25  ? 40.115  -19.696 34.585  1.00 49.68 ? 25   SER K OG  1 
ATOM   11349 N  N   . ASN K  1 26  ? 39.015  -18.876 31.337  1.00 53.00 ? 26   ASN K N   1 
ATOM   11350 C  CA  . ASN K  1 26  ? 39.785  -19.032 30.109  1.00 51.97 ? 26   ASN K CA  1 
ATOM   11351 C  C   . ASN K  1 26  ? 39.038  -18.502 28.896  1.00 49.49 ? 26   ASN K C   1 
ATOM   11352 O  O   . ASN K  1 26  ? 39.245  -18.969 27.771  1.00 47.68 ? 26   ASN K O   1 
ATOM   11353 C  CB  . ASN K  1 26  ? 40.185  -20.496 29.905  1.00 49.97 ? 26   ASN K CB  1 
ATOM   11354 C  CG  . ASN K  1 26  ? 41.325  -20.911 30.817  1.00 54.84 ? 26   ASN K CG  1 
ATOM   11355 O  OD1 . ASN K  1 26  ? 42.313  -20.187 30.966  1.00 54.79 ? 26   ASN K OD1 1 
ATOM   11356 N  ND2 . ASN K  1 26  ? 41.192  -22.078 31.436  1.00 56.91 ? 26   ASN K ND2 1 
ATOM   11357 N  N   . GLY K  1 27  ? 38.166  -17.528 29.142  1.00 47.37 ? 27   GLY K N   1 
ATOM   11358 C  CA  . GLY K  1 27  ? 37.416  -16.882 28.085  1.00 44.79 ? 27   GLY K CA  1 
ATOM   11359 C  C   . GLY K  1 27  ? 38.079  -15.569 27.730  1.00 40.29 ? 27   GLY K C   1 
ATOM   11360 O  O   . GLY K  1 27  ? 39.120  -15.231 28.293  1.00 41.46 ? 27   GLY K O   1 
ATOM   11361 N  N   . PRO K  1 28  ? 37.482  -14.824 26.790  1.00 40.86 ? 28   PRO K N   1 
ATOM   11362 C  CA  . PRO K  1 28  ? 37.976  -13.512 26.371  1.00 37.20 ? 28   PRO K CA  1 
ATOM   11363 C  C   . PRO K  1 28  ? 37.687  -12.445 27.421  1.00 34.47 ? 28   PRO K C   1 
ATOM   11364 O  O   . PRO K  1 28  ? 36.862  -12.653 28.315  1.00 35.75 ? 28   PRO K O   1 
ATOM   11365 C  CB  . PRO K  1 28  ? 37.154  -13.209 25.108  1.00 35.75 ? 28   PRO K CB  1 
ATOM   11366 C  CG  . PRO K  1 28  ? 36.436  -14.466 24.779  1.00 39.13 ? 28   PRO K CG  1 
ATOM   11367 C  CD  . PRO K  1 28  ? 36.271  -15.206 26.051  1.00 40.44 ? 28   PRO K CD  1 
ATOM   11368 N  N   . VAL K  1 29  ? 38.371  -11.314 27.302  1.00 30.89 ? 29   VAL K N   1 
ATOM   11369 C  CA  . VAL K  1 29  ? 38.135  -10.166 28.155  1.00 29.44 ? 29   VAL K CA  1 
ATOM   11370 C  C   . VAL K  1 29  ? 37.440  -9.115  27.306  1.00 29.07 ? 29   VAL K C   1 
ATOM   11371 O  O   . VAL K  1 29  ? 37.877  -8.829  26.193  1.00 27.81 ? 29   VAL K O   1 
ATOM   11372 C  CB  . VAL K  1 29  ? 39.462  -9.586  28.714  1.00 30.63 ? 29   VAL K CB  1 
ATOM   11373 C  CG1 . VAL K  1 29  ? 39.199  -8.412  29.683  1.00 26.49 ? 29   VAL K CG1 1 
ATOM   11374 C  CG2 . VAL K  1 29  ? 40.275  -10.668 29.387  1.00 27.67 ? 29   VAL K CG2 1 
ATOM   11375 N  N   . LYS K  1 30  ? 36.347  -8.552  27.818  1.00 29.40 ? 30   LYS K N   1 
ATOM   11376 C  CA  . LYS K  1 30  ? 35.673  -7.469  27.120  1.00 30.98 ? 30   LYS K CA  1 
ATOM   11377 C  C   . LYS K  1 30  ? 36.159  -6.121  27.640  1.00 28.43 ? 30   LYS K C   1 
ATOM   11378 O  O   . LYS K  1 30  ? 35.921  -5.764  28.778  1.00 29.59 ? 30   LYS K O   1 
ATOM   11379 C  CB  . LYS K  1 30  ? 34.148  -7.587  27.212  1.00 34.75 ? 30   LYS K CB  1 
ATOM   11380 C  CG  . LYS K  1 30  ? 33.430  -6.694  26.200  1.00 38.14 ? 30   LYS K CG  1 
ATOM   11381 C  CD  . LYS K  1 30  ? 31.906  -6.749  26.324  1.00 48.16 ? 30   LYS K CD  1 
ATOM   11382 C  CE  . LYS K  1 30  ? 31.259  -5.573  25.575  1.00 47.79 ? 30   LYS K CE  1 
ATOM   11383 N  NZ  . LYS K  1 30  ? 29.774  -5.696  25.456  1.00 50.28 ? 30   LYS K NZ  1 
ATOM   11384 N  N   . VAL K  1 31  ? 36.855  -5.390  26.782  1.00 26.79 ? 31   VAL K N   1 
ATOM   11385 C  CA  . VAL K  1 31  ? 37.462  -4.119  27.135  1.00 26.69 ? 31   VAL K CA  1 
ATOM   11386 C  C   . VAL K  1 31  ? 36.634  -2.978  26.566  1.00 26.71 ? 31   VAL K C   1 
ATOM   11387 O  O   . VAL K  1 31  ? 36.649  -2.752  25.356  1.00 29.40 ? 31   VAL K O   1 
ATOM   11388 C  CB  . VAL K  1 31  ? 38.884  -4.025  26.543  1.00 26.72 ? 31   VAL K CB  1 
ATOM   11389 C  CG1 . VAL K  1 31  ? 39.515  -2.666  26.863  1.00 25.21 ? 31   VAL K CG1 1 
ATOM   11390 C  CG2 . VAL K  1 31  ? 39.743  -5.180  27.043  1.00 26.39 ? 31   VAL K CG2 1 
ATOM   11391 N  N   . TRP K  1 32  ? 35.907  -2.261  27.417  1.00 26.04 ? 32   TRP K N   1 
ATOM   11392 C  CA  . TRP K  1 32  ? 35.053  -1.197  26.918  1.00 24.93 ? 32   TRP K CA  1 
ATOM   11393 C  C   . TRP K  1 32  ? 35.140  0.068   27.753  1.00 22.21 ? 32   TRP K C   1 
ATOM   11394 O  O   . TRP K  1 32  ? 35.370  0.018   28.944  1.00 25.84 ? 32   TRP K O   1 
ATOM   11395 C  CB  . TRP K  1 32  ? 33.597  -1.682  26.799  1.00 28.42 ? 32   TRP K CB  1 
ATOM   11396 C  CG  . TRP K  1 32  ? 32.792  -1.644  28.082  1.00 28.61 ? 32   TRP K CG  1 
ATOM   11397 C  CD1 . TRP K  1 32  ? 31.952  -0.645  28.503  1.00 27.78 ? 32   TRP K CD1 1 
ATOM   11398 C  CD2 . TRP K  1 32  ? 32.747  -2.658  29.090  1.00 26.71 ? 32   TRP K CD2 1 
ATOM   11399 N  NE1 . TRP K  1 32  ? 31.396  -0.977  29.718  1.00 28.68 ? 32   TRP K NE1 1 
ATOM   11400 C  CE2 . TRP K  1 32  ? 31.867  -2.207  30.098  1.00 31.17 ? 32   TRP K CE2 1 
ATOM   11401 C  CE3 . TRP K  1 32  ? 33.369  -3.900  29.243  1.00 27.68 ? 32   TRP K CE3 1 
ATOM   11402 C  CZ2 . TRP K  1 32  ? 31.597  -2.958  31.244  1.00 35.47 ? 32   TRP K CZ2 1 
ATOM   11403 C  CZ3 . TRP K  1 32  ? 33.098  -4.645  30.375  1.00 33.87 ? 32   TRP K CZ3 1 
ATOM   11404 C  CH2 . TRP K  1 32  ? 32.220  -4.172  31.366  1.00 35.39 ? 32   TRP K CH2 1 
ATOM   11405 N  N   . GLY K  1 33  ? 34.947  1.211   27.122  1.00 21.78 ? 33   GLY K N   1 
ATOM   11406 C  CA  . GLY K  1 33  ? 34.959  2.455   27.848  1.00 22.50 ? 33   GLY K CA  1 
ATOM   11407 C  C   . GLY K  1 33  ? 34.950  3.627   26.907  1.00 27.41 ? 33   GLY K C   1 
ATOM   11408 O  O   . GLY K  1 33  ? 34.453  3.533   25.785  1.00 27.41 ? 33   GLY K O   1 
ATOM   11409 N  N   . SER K  1 34  ? 35.506  4.738   27.368  1.00 27.66 ? 34   SER K N   1 
ATOM   11410 C  CA  . SER K  1 34  ? 35.548  5.958   26.584  1.00 30.66 ? 34   SER K CA  1 
ATOM   11411 C  C   . SER K  1 34  ? 36.840  6.706   26.889  1.00 32.25 ? 34   SER K C   1 
ATOM   11412 O  O   . SER K  1 34  ? 37.384  6.600   27.990  1.00 32.16 ? 34   SER K O   1 
ATOM   11413 C  CB  . SER K  1 34  ? 34.338  6.836   26.916  1.00 32.70 ? 34   SER K CB  1 
ATOM   11414 O  OG  . SER K  1 34  ? 34.175  7.883   25.971  1.00 37.59 ? 34   SER K OG  1 
ATOM   11415 N  N   . ILE K  1 35  ? 37.337  7.446   25.902  1.00 33.90 ? 35   ILE K N   1 
ATOM   11416 C  CA  . ILE K  1 35  ? 38.457  8.355   26.108  1.00 32.30 ? 35   ILE K CA  1 
ATOM   11417 C  C   . ILE K  1 35  ? 38.133  9.672   25.413  1.00 34.42 ? 35   ILE K C   1 
ATOM   11418 O  O   . ILE K  1 35  ? 37.497  9.680   24.360  1.00 34.50 ? 35   ILE K O   1 
ATOM   11419 C  CB  . ILE K  1 35  ? 39.765  7.768   25.568  1.00 29.59 ? 35   ILE K CB  1 
ATOM   11420 C  CG1 . ILE K  1 35  ? 39.889  6.303   26.001  1.00 28.07 ? 35   ILE K CG1 1 
ATOM   11421 C  CG2 . ILE K  1 35  ? 40.952  8.606   26.032  1.00 29.68 ? 35   ILE K CG2 1 
ATOM   11422 C  CD1 . ILE K  1 35  ? 41.250  5.688   25.767  1.00 27.20 ? 35   ILE K CD1 1 
ATOM   11423 N  N   . LYS K  1 36  ? 38.552  10.782  26.013  1.00 35.82 ? 36   LYS K N   1 
ATOM   11424 C  CA  . LYS K  1 36  ? 38.224  12.108  25.494  1.00 35.58 ? 36   LYS K CA  1 
ATOM   11425 C  C   . LYS K  1 36  ? 39.469  12.984  25.394  1.00 36.34 ? 36   LYS K C   1 
ATOM   11426 O  O   . LYS K  1 36  ? 40.507  12.677  25.987  1.00 35.78 ? 36   LYS K O   1 
ATOM   11427 C  CB  . LYS K  1 36  ? 37.188  12.791  26.395  1.00 39.78 ? 36   LYS K CB  1 
ATOM   11428 C  CG  . LYS K  1 36  ? 37.739  13.233  27.749  1.00 39.72 ? 36   LYS K CG  1 
ATOM   11429 C  CD  . LYS K  1 36  ? 36.802  14.182  28.474  1.00 39.79 ? 36   LYS K CD  1 
ATOM   11430 C  CE  . LYS K  1 36  ? 35.525  13.482  28.909  1.00 47.57 ? 36   LYS K CE  1 
ATOM   11431 N  NZ  . LYS K  1 36  ? 34.749  14.272  29.913  1.00 55.08 ? 36   LYS K NZ  1 
ATOM   11432 N  N   . GLY K  1 37  ? 39.359  14.079  24.646  1.00 36.40 ? 37   GLY K N   1 
ATOM   11433 C  CA  . GLY K  1 37  ? 40.471  15.000  24.478  1.00 37.16 ? 37   GLY K CA  1 
ATOM   11434 C  C   . GLY K  1 37  ? 41.501  14.534  23.465  1.00 38.26 ? 37   GLY K C   1 
ATOM   11435 O  O   . GLY K  1 37  ? 42.503  15.210  23.235  1.00 41.93 ? 37   GLY K O   1 
ATOM   11436 N  N   . LEU K  1 38  ? 41.256  13.371  22.867  1.00 38.44 ? 38   LEU K N   1 
ATOM   11437 C  CA  . LEU K  1 38  ? 42.098  12.835  21.801  1.00 35.25 ? 38   LEU K CA  1 
ATOM   11438 C  C   . LEU K  1 38  ? 41.991  13.692  20.554  1.00 32.14 ? 38   LEU K C   1 
ATOM   11439 O  O   . LEU K  1 38  ? 41.017  14.414  20.387  1.00 32.11 ? 38   LEU K O   1 
ATOM   11440 C  CB  . LEU K  1 38  ? 41.637  11.417  21.473  1.00 32.50 ? 38   LEU K CB  1 
ATOM   11441 C  CG  . LEU K  1 38  ? 42.353  10.260  22.161  1.00 30.52 ? 38   LEU K CG  1 
ATOM   11442 C  CD1 . LEU K  1 38  ? 43.410  10.737  23.144  1.00 31.31 ? 38   LEU K CD1 1 
ATOM   11443 C  CD2 . LEU K  1 38  ? 41.336  9.335   22.800  1.00 30.64 ? 38   LEU K CD2 1 
ATOM   11444 N  N   . THR K  1 39  ? 43.001  13.623  19.689  1.00 36.74 ? 39   THR K N   1 
ATOM   11445 C  CA  . THR K  1 39  ? 42.885  14.173  18.333  1.00 37.19 ? 39   THR K CA  1 
ATOM   11446 C  C   . THR K  1 39  ? 42.112  13.193  17.462  1.00 36.39 ? 39   THR K C   1 
ATOM   11447 O  O   . THR K  1 39  ? 42.273  11.979  17.606  1.00 36.75 ? 39   THR K O   1 
ATOM   11448 C  CB  . THR K  1 39  ? 44.257  14.416  17.664  1.00 34.60 ? 39   THR K CB  1 
ATOM   11449 O  OG1 . THR K  1 39  ? 45.111  13.289  17.892  1.00 36.16 ? 39   THR K OG1 1 
ATOM   11450 C  CG2 . THR K  1 39  ? 44.911  15.663  18.217  1.00 36.04 ? 39   THR K CG2 1 
ATOM   11451 N  N   . GLU K  1 40  ? 41.270  13.707  16.569  1.00 37.13 ? 40   GLU K N   1 
ATOM   11452 C  CA  . GLU K  1 40  ? 40.542  12.831  15.657  1.00 38.38 ? 40   GLU K CA  1 
ATOM   11453 C  C   . GLU K  1 40  ? 41.524  11.869  14.992  1.00 35.94 ? 40   GLU K C   1 
ATOM   11454 O  O   . GLU K  1 40  ? 42.613  12.274  14.594  1.00 36.78 ? 40   GLU K O   1 
ATOM   11455 C  CB  . GLU K  1 40  ? 39.780  13.632  14.598  1.00 39.74 ? 40   GLU K CB  1 
ATOM   11456 C  CG  . GLU K  1 40  ? 38.769  12.788  13.825  1.00 41.52 ? 40   GLU K CG  1 
ATOM   11457 C  CD  . GLU K  1 40  ? 38.030  13.561  12.748  1.00 44.94 ? 40   GLU K CD  1 
ATOM   11458 O  OE1 . GLU K  1 40  ? 38.353  14.754  12.522  1.00 45.52 ? 40   GLU K OE1 1 
ATOM   11459 O  OE2 . GLU K  1 40  ? 37.122  12.961  12.126  1.00 46.16 ? 40   GLU K OE2 1 
ATOM   11460 N  N   . GLY K  1 41  ? 41.155  10.595  14.896  1.00 34.25 ? 41   GLY K N   1 
ATOM   11461 C  CA  . GLY K  1 41  ? 42.016  9.611   14.263  1.00 32.66 ? 41   GLY K CA  1 
ATOM   11462 C  C   . GLY K  1 41  ? 42.313  8.405   15.128  1.00 29.87 ? 41   GLY K C   1 
ATOM   11463 O  O   . GLY K  1 41  ? 41.652  8.193   16.139  1.00 28.77 ? 41   GLY K O   1 
ATOM   11464 N  N   . LEU K  1 42  ? 43.314  7.621   14.729  1.00 30.11 ? 42   LEU K N   1 
ATOM   11465 C  CA  . LEU K  1 42  ? 43.686  6.397   15.446  1.00 29.15 ? 42   LEU K CA  1 
ATOM   11466 C  C   . LEU K  1 42  ? 44.768  6.634   16.515  1.00 30.33 ? 42   LEU K C   1 
ATOM   11467 O  O   . LEU K  1 42  ? 45.633  7.496   16.354  1.00 33.01 ? 42   LEU K O   1 
ATOM   11468 C  CB  . LEU K  1 42  ? 44.123  5.302   14.462  1.00 28.23 ? 42   LEU K CB  1 
ATOM   11469 C  CG  . LEU K  1 42  ? 43.072  4.751   13.478  1.00 30.18 ? 42   LEU K CG  1 
ATOM   11470 C  CD1 . LEU K  1 42  ? 43.690  3.861   12.397  1.00 31.44 ? 42   LEU K CD1 1 
ATOM   11471 C  CD2 . LEU K  1 42  ? 41.969  3.995   14.212  1.00 30.41 ? 42   LEU K CD2 1 
ATOM   11472 N  N   . HIS K  1 43  ? 44.709  5.867   17.604  1.00 27.47 ? 43   HIS K N   1 
ATOM   11473 C  CA  . HIS K  1 43  ? 45.658  5.995   18.707  1.00 26.80 ? 43   HIS K CA  1 
ATOM   11474 C  C   . HIS K  1 43  ? 45.978  4.631   19.304  1.00 25.87 ? 43   HIS K C   1 
ATOM   11475 O  O   . HIS K  1 43  ? 45.077  3.901   19.696  1.00 24.78 ? 43   HIS K O   1 
ATOM   11476 C  CB  . HIS K  1 43  ? 45.081  6.893   19.809  1.00 28.86 ? 43   HIS K CB  1 
ATOM   11477 C  CG  . HIS K  1 43  ? 44.896  8.320   19.395  1.00 30.82 ? 43   HIS K CG  1 
ATOM   11478 N  ND1 . HIS K  1 43  ? 45.827  9.298   19.670  1.00 31.63 ? 43   HIS K ND1 1 
ATOM   11479 C  CD2 . HIS K  1 43  ? 43.887  8.933   18.728  1.00 30.65 ? 43   HIS K CD2 1 
ATOM   11480 C  CE1 . HIS K  1 43  ? 45.400  10.453  19.186  1.00 34.47 ? 43   HIS K CE1 1 
ATOM   11481 N  NE2 . HIS K  1 43  ? 44.228  10.257  18.607  1.00 31.55 ? 43   HIS K NE2 1 
ATOM   11482 N  N   . GLY K  1 44  ? 47.260  4.292   19.390  1.00 26.64 ? 44   GLY K N   1 
ATOM   11483 C  CA  . GLY K  1 44  ? 47.666  3.026   19.975  1.00 24.04 ? 44   GLY K CA  1 
ATOM   11484 C  C   . GLY K  1 44  ? 47.172  2.877   21.403  1.00 27.95 ? 44   GLY K C   1 
ATOM   11485 O  O   . GLY K  1 44  ? 47.131  3.855   22.153  1.00 28.13 ? 44   GLY K O   1 
ATOM   11486 N  N   . PHE K  1 45  ? 46.824  1.645   21.779  1.00 25.75 ? 45   PHE K N   1 
ATOM   11487 C  CA  . PHE K  1 45  ? 46.139  1.341   23.038  1.00 24.37 ? 45   PHE K CA  1 
ATOM   11488 C  C   . PHE K  1 45  ? 46.692  0.018   23.576  1.00 25.98 ? 45   PHE K C   1 
ATOM   11489 O  O   . PHE K  1 45  ? 46.328  -1.054  23.082  1.00 24.20 ? 45   PHE K O   1 
ATOM   11490 C  CB  . PHE K  1 45  ? 44.634  1.244   22.752  1.00 26.69 ? 45   PHE K CB  1 
ATOM   11491 C  CG  . PHE K  1 45  ? 43.760  1.055   23.967  1.00 29.74 ? 45   PHE K CG  1 
ATOM   11492 C  CD1 . PHE K  1 45  ? 43.643  2.049   24.928  1.00 29.57 ? 45   PHE K CD1 1 
ATOM   11493 C  CD2 . PHE K  1 45  ? 42.993  -0.096  24.108  1.00 29.31 ? 45   PHE K CD2 1 
ATOM   11494 C  CE1 . PHE K  1 45  ? 42.809  1.878   26.029  1.00 29.38 ? 45   PHE K CE1 1 
ATOM   11495 C  CE2 . PHE K  1 45  ? 42.154  -0.275  25.209  1.00 29.31 ? 45   PHE K CE2 1 
ATOM   11496 C  CZ  . PHE K  1 45  ? 42.062  0.715   26.167  1.00 27.48 ? 45   PHE K CZ  1 
ATOM   11497 N  N   . HIS K  1 46  ? 47.584  0.098   24.570  1.00 26.62 ? 46   HIS K N   1 
ATOM   11498 C  CA  . HIS K  1 46  ? 48.344  -1.071  25.022  1.00 25.99 ? 46   HIS K CA  1 
ATOM   11499 C  C   . HIS K  1 46  ? 48.424  -1.201  26.534  1.00 29.42 ? 46   HIS K C   1 
ATOM   11500 O  O   . HIS K  1 46  ? 48.437  -0.209  27.262  1.00 30.45 ? 46   HIS K O   1 
ATOM   11501 C  CB  . HIS K  1 46  ? 49.777  -1.062  24.453  1.00 25.67 ? 46   HIS K CB  1 
ATOM   11502 C  CG  . HIS K  1 46  ? 49.852  -0.664  23.013  1.00 27.06 ? 46   HIS K CG  1 
ATOM   11503 N  ND1 . HIS K  1 46  ? 50.384  0.541   22.600  1.00 27.57 ? 46   HIS K ND1 1 
ATOM   11504 C  CD2 . HIS K  1 46  ? 49.441  -1.296  21.887  1.00 24.72 ? 46   HIS K CD2 1 
ATOM   11505 C  CE1 . HIS K  1 46  ? 50.293  0.633   21.286  1.00 24.68 ? 46   HIS K CE1 1 
ATOM   11506 N  NE2 . HIS K  1 46  ? 49.726  -0.469  20.829  1.00 24.38 ? 46   HIS K NE2 1 
ATOM   11507 N  N   . VAL K  1 47  ? 48.490  -2.446  26.991  1.00 30.23 ? 47   VAL K N   1 
ATOM   11508 C  CA  . VAL K  1 47  ? 48.772  -2.758  28.384  1.00 30.41 ? 47   VAL K CA  1 
ATOM   11509 C  C   . VAL K  1 47  ? 50.277  -2.860  28.596  1.00 30.15 ? 47   VAL K C   1 
ATOM   11510 O  O   . VAL K  1 47  ? 50.884  -3.867  28.220  1.00 30.26 ? 47   VAL K O   1 
ATOM   11511 C  CB  . VAL K  1 47  ? 48.170  -4.122  28.766  1.00 27.63 ? 47   VAL K CB  1 
ATOM   11512 C  CG1 . VAL K  1 47  ? 48.379  -4.397  30.249  1.00 26.19 ? 47   VAL K CG1 1 
ATOM   11513 C  CG2 . VAL K  1 47  ? 46.699  -4.173  28.394  1.00 27.20 ? 47   VAL K CG2 1 
ATOM   11514 N  N   . HIS K  1 48  ? 50.881  -1.832  29.190  1.00 31.08 ? 48   HIS K N   1 
ATOM   11515 C  CA  . HIS K  1 48  ? 52.304  -1.884  29.561  1.00 30.55 ? 48   HIS K CA  1 
ATOM   11516 C  C   . HIS K  1 48  ? 52.541  -2.716  30.840  1.00 28.42 ? 48   HIS K C   1 
ATOM   11517 O  O   . HIS K  1 48  ? 51.619  -3.008  31.590  1.00 29.03 ? 48   HIS K O   1 
ATOM   11518 C  CB  . HIS K  1 48  ? 52.895  -0.477  29.683  1.00 28.76 ? 48   HIS K CB  1 
ATOM   11519 C  CG  . HIS K  1 48  ? 52.872  0.306   28.402  1.00 27.43 ? 48   HIS K CG  1 
ATOM   11520 N  ND1 . HIS K  1 48  ? 54.000  0.897   27.868  1.00 27.45 ? 48   HIS K ND1 1 
ATOM   11521 C  CD2 . HIS K  1 48  ? 51.862  0.597   27.552  1.00 25.81 ? 48   HIS K CD2 1 
ATOM   11522 C  CE1 . HIS K  1 48  ? 53.681  1.520   26.748  1.00 27.04 ? 48   HIS K CE1 1 
ATOM   11523 N  NE2 . HIS K  1 48  ? 52.388  1.356   26.532  1.00 26.30 ? 48   HIS K NE2 1 
ATOM   11524 N  N   . GLU K  1 49  ? 53.784  -3.096  31.082  1.00 29.23 ? 49   GLU K N   1 
ATOM   11525 C  CA  . GLU K  1 49  ? 54.091  -4.157  32.041  1.00 30.76 ? 49   GLU K CA  1 
ATOM   11526 C  C   . GLU K  1 49  ? 53.925  -3.819  33.524  1.00 30.19 ? 49   GLU K C   1 
ATOM   11527 O  O   . GLU K  1 49  ? 53.600  -4.686  34.339  1.00 26.75 ? 49   GLU K O   1 
ATOM   11528 C  CB  . GLU K  1 49  ? 55.518  -4.641  31.808  1.00 28.41 ? 49   GLU K CB  1 
ATOM   11529 C  CG  . GLU K  1 49  ? 55.880  -5.883  32.568  1.00 28.89 ? 49   GLU K CG  1 
ATOM   11530 C  CD  . GLU K  1 49  ? 57.332  -6.229  32.374  1.00 32.01 ? 49   GLU K CD  1 
ATOM   11531 O  OE1 . GLU K  1 49  ? 57.983  -5.529  31.568  1.00 34.50 ? 49   GLU K OE1 1 
ATOM   11532 O  OE2 . GLU K  1 49  ? 57.820  -7.183  33.017  1.00 33.07 ? 49   GLU K OE2 1 
ATOM   11533 N  N   . PHE K  1 50  ? 54.185  -2.572  33.886  1.00 32.27 ? 50   PHE K N   1 
ATOM   11534 C  CA  . PHE K  1 50  ? 54.220  -2.220  35.301  1.00 32.86 ? 50   PHE K CA  1 
ATOM   11535 C  C   . PHE K  1 50  ? 53.092  -1.292  35.710  1.00 31.58 ? 50   PHE K C   1 
ATOM   11536 O  O   . PHE K  1 50  ? 52.728  -0.381  34.967  1.00 30.22 ? 50   PHE K O   1 
ATOM   11537 C  CB  . PHE K  1 50  ? 55.586  -1.629  35.672  1.00 32.50 ? 50   PHE K CB  1 
ATOM   11538 C  CG  . PHE K  1 50  ? 56.725  -2.516  35.292  1.00 31.94 ? 50   PHE K CG  1 
ATOM   11539 C  CD1 . PHE K  1 50  ? 56.786  -3.817  35.778  1.00 32.09 ? 50   PHE K CD1 1 
ATOM   11540 C  CD2 . PHE K  1 50  ? 57.708  -2.076  34.419  1.00 30.66 ? 50   PHE K CD2 1 
ATOM   11541 C  CE1 . PHE K  1 50  ? 57.820  -4.658  35.418  1.00 30.45 ? 50   PHE K CE1 1 
ATOM   11542 C  CE2 . PHE K  1 50  ? 58.741  -2.910  34.051  1.00 30.62 ? 50   PHE K CE2 1 
ATOM   11543 C  CZ  . PHE K  1 50  ? 58.798  -4.204  34.550  1.00 29.80 ? 50   PHE K CZ  1 
ATOM   11544 N  N   . GLY K  1 51  ? 52.528  -1.550  36.889  1.00 33.54 ? 51   GLY K N   1 
ATOM   11545 C  CA  . GLY K  1 51  ? 51.571  -0.642  37.494  1.00 32.56 ? 51   GLY K CA  1 
ATOM   11546 C  C   . GLY K  1 51  ? 52.360  0.317   38.355  1.00 33.55 ? 51   GLY K C   1 
ATOM   11547 O  O   . GLY K  1 51  ? 52.316  0.267   39.590  1.00 36.34 ? 51   GLY K O   1 
ATOM   11548 N  N   . ASP K  1 52  ? 53.103  1.191   37.689  1.00 35.51 ? 52   ASP K N   1 
ATOM   11549 C  CA  . ASP K  1 52  ? 54.062  2.052   38.359  1.00 31.85 ? 52   ASP K CA  1 
ATOM   11550 C  C   . ASP K  1 52  ? 53.915  3.453   37.791  1.00 33.42 ? 52   ASP K C   1 
ATOM   11551 O  O   . ASP K  1 52  ? 54.294  3.713   36.649  1.00 34.65 ? 52   ASP K O   1 
ATOM   11552 C  CB  . ASP K  1 52  ? 55.475  1.500   38.154  1.00 31.08 ? 52   ASP K CB  1 
ATOM   11553 C  CG  . ASP K  1 52  ? 56.520  2.233   38.973  1.00 34.84 ? 52   ASP K CG  1 
ATOM   11554 O  OD1 . ASP K  1 52  ? 56.459  3.482   39.060  1.00 33.44 ? 52   ASP K OD1 1 
ATOM   11555 O  OD2 . ASP K  1 52  ? 57.415  1.553   39.521  1.00 36.41 ? 52   ASP K OD2 1 
ATOM   11556 N  N   . ASN K  1 53  ? 53.340  4.350   38.586  1.00 33.68 ? 53   ASN K N   1 
ATOM   11557 C  CA  . ASN K  1 53  ? 53.031  5.699   38.126  1.00 36.37 ? 53   ASN K CA  1 
ATOM   11558 C  C   . ASN K  1 53  ? 54.009  6.727   38.673  1.00 37.12 ? 53   ASN K C   1 
ATOM   11559 O  O   . ASN K  1 53  ? 53.785  7.937   38.546  1.00 36.03 ? 53   ASN K O   1 
ATOM   11560 C  CB  . ASN K  1 53  ? 51.602  6.087   38.529  1.00 37.49 ? 53   ASN K CB  1 
ATOM   11561 C  CG  . ASN K  1 53  ? 51.067  7.284   37.738  1.00 42.61 ? 53   ASN K CG  1 
ATOM   11562 O  OD1 . ASN K  1 53  ? 51.188  7.344   36.510  1.00 42.25 ? 53   ASN K OD1 1 
ATOM   11563 N  ND2 . ASN K  1 53  ? 50.456  8.233   38.441  1.00 45.25 ? 53   ASN K ND2 1 
ATOM   11564 N  N   . THR K  1 54  ? 55.099  6.245   39.271  1.00 38.33 ? 54   THR K N   1 
ATOM   11565 C  CA  . THR K  1 54  ? 56.001  7.120   40.026  1.00 36.80 ? 54   THR K CA  1 
ATOM   11566 C  C   . THR K  1 54  ? 56.681  8.168   39.156  1.00 40.57 ? 54   THR K C   1 
ATOM   11567 O  O   . THR K  1 54  ? 57.098  9.218   39.656  1.00 38.14 ? 54   THR K O   1 
ATOM   11568 C  CB  . THR K  1 54  ? 57.063  6.333   40.810  1.00 37.13 ? 54   THR K CB  1 
ATOM   11569 O  OG1 . THR K  1 54  ? 57.955  5.688   39.899  1.00 42.26 ? 54   THR K OG1 1 
ATOM   11570 C  CG2 . THR K  1 54  ? 56.407  5.294   41.704  1.00 36.37 ? 54   THR K CG2 1 
ATOM   11571 N  N   . ALA K  1 55  ? 56.778  7.880   37.859  1.00 39.05 ? 55   ALA K N   1 
ATOM   11572 C  CA  . ALA K  1 55  ? 57.362  8.805   36.902  1.00 36.24 ? 55   ALA K CA  1 
ATOM   11573 C  C   . ALA K  1 55  ? 56.385  9.081   35.766  1.00 41.82 ? 55   ALA K C   1 
ATOM   11574 O  O   . ALA K  1 55  ? 56.784  9.193   34.600  1.00 44.41 ? 55   ALA K O   1 
ATOM   11575 C  CB  . ALA K  1 55  ? 58.657  8.238   36.354  1.00 39.56 ? 55   ALA K CB  1 
ATOM   11576 N  N   . GLY K  1 56  ? 55.104  9.194   36.102  1.00 39.82 ? 56   GLY K N   1 
ATOM   11577 C  CA  . GLY K  1 56  ? 54.079  9.373   35.090  1.00 39.11 ? 56   GLY K CA  1 
ATOM   11578 C  C   . GLY K  1 56  ? 53.916  8.109   34.263  1.00 39.10 ? 56   GLY K C   1 
ATOM   11579 O  O   . GLY K  1 56  ? 54.253  7.011   34.716  1.00 38.58 ? 56   GLY K O   1 
ATOM   11580 N  N   . CYS K  1 57  ? 53.409  8.255   33.044  1.00 39.68 ? 57   CYS K N   1 
ATOM   11581 C  CA  . CYS K  1 57  ? 53.244  7.105   32.158  1.00 40.11 ? 57   CYS K CA  1 
ATOM   11582 C  C   . CYS K  1 57  ? 54.571  6.408   31.835  1.00 37.95 ? 57   CYS K C   1 
ATOM   11583 O  O   . CYS K  1 57  ? 54.585  5.219   31.499  1.00 36.88 ? 57   CYS K O   1 
ATOM   11584 C  CB  . CYS K  1 57  ? 52.555  7.536   30.865  1.00 41.37 ? 57   CYS K CB  1 
ATOM   11585 S  SG  . CYS K  1 57  ? 51.105  8.559   31.130  1.00 38.77 ? 57   CYS K SG  1 
ATOM   11586 N  N   . THR K  1 58  ? 55.675  7.150   31.950  1.00 42.20 ? 58   THR K N   1 
ATOM   11587 C  CA  . THR K  1 58  ? 57.015  6.644   31.610  1.00 38.93 ? 58   THR K CA  1 
ATOM   11588 C  C   . THR K  1 58  ? 57.457  5.409   32.397  1.00 35.59 ? 58   THR K C   1 
ATOM   11589 O  O   . THR K  1 58  ? 58.201  4.573   31.872  1.00 31.26 ? 58   THR K O   1 
ATOM   11590 C  CB  . THR K  1 58  ? 58.100  7.731   31.784  1.00 37.67 ? 58   THR K CB  1 
ATOM   11591 O  OG1 . THR K  1 58  ? 57.850  8.824   30.888  1.00 40.43 ? 58   THR K OG1 1 
ATOM   11592 C  CG2 . THR K  1 58  ? 59.468  7.154   31.496  1.00 34.57 ? 58   THR K CG2 1 
ATOM   11593 N  N   . SER K  1 59  ? 57.013  5.299   33.650  1.00 32.89 ? 59   SER K N   1 
ATOM   11594 C  CA  . SER K  1 59  ? 57.446  4.197   34.517  1.00 29.40 ? 59   SER K CA  1 
ATOM   11595 C  C   . SER K  1 59  ? 56.660  2.912   34.289  1.00 30.89 ? 59   SER K C   1 
ATOM   11596 O  O   . SER K  1 59  ? 56.972  1.865   34.863  1.00 29.32 ? 59   SER K O   1 
ATOM   11597 C  CB  . SER K  1 59  ? 57.413  4.609   35.995  1.00 34.80 ? 59   SER K CB  1 
ATOM   11598 O  OG  . SER K  1 59  ? 56.447  5.620   36.230  1.00 37.65 ? 59   SER K OG  1 
ATOM   11599 N  N   . ALA K  1 60  ? 55.648  3.002   33.429  1.00 32.95 ? 60   ALA K N   1 
ATOM   11600 C  CA  . ALA K  1 60  ? 54.829  1.856   33.060  1.00 32.87 ? 60   ALA K CA  1 
ATOM   11601 C  C   . ALA K  1 60  ? 55.687  0.754   32.446  1.00 32.97 ? 60   ALA K C   1 
ATOM   11602 O  O   . ALA K  1 60  ? 55.361  -0.432  32.534  1.00 33.37 ? 60   ALA K O   1 
ATOM   11603 C  CB  . ALA K  1 60  ? 53.733  2.286   32.088  1.00 28.69 ? 60   ALA K CB  1 
ATOM   11604 N  N   . GLY K  1 61  ? 56.791  1.153   31.825  1.00 33.34 ? 61   GLY K N   1 
ATOM   11605 C  CA  . GLY K  1 61  ? 57.671  0.200   31.182  1.00 30.41 ? 61   GLY K CA  1 
ATOM   11606 C  C   . GLY K  1 61  ? 57.239  -0.011  29.752  1.00 30.06 ? 61   GLY K C   1 
ATOM   11607 O  O   . GLY K  1 61  ? 56.655  0.891   29.142  1.00 30.26 ? 61   GLY K O   1 
ATOM   11608 N  N   . PRO K  1 62  ? 57.498  -1.213  29.217  1.00 29.66 ? 62   PRO K N   1 
ATOM   11609 C  CA  . PRO K  1 62  ? 57.243  -1.506  27.811  1.00 32.96 ? 62   PRO K CA  1 
ATOM   11610 C  C   . PRO K  1 62  ? 55.880  -2.180  27.667  1.00 31.63 ? 62   PRO K C   1 
ATOM   11611 O  O   . PRO K  1 62  ? 55.223  -2.416  28.684  1.00 31.43 ? 62   PRO K O   1 
ATOM   11612 C  CB  . PRO K  1 62  ? 58.360  -2.508  27.473  1.00 34.16 ? 62   PRO K CB  1 
ATOM   11613 C  CG  . PRO K  1 62  ? 58.960  -2.944  28.828  1.00 30.60 ? 62   PRO K CG  1 
ATOM   11614 C  CD  . PRO K  1 62  ? 58.048  -2.393  29.893  1.00 30.37 ? 62   PRO K CD  1 
ATOM   11615 N  N   . HIS K  1 63  ? 55.454  -2.486  26.443  1.00 30.09 ? 63   HIS K N   1 
ATOM   11616 C  CA  . HIS K  1 63  ? 54.225  -3.255  26.279  1.00 28.92 ? 63   HIS K CA  1 
ATOM   11617 C  C   . HIS K  1 63  ? 54.374  -4.565  27.054  1.00 29.51 ? 63   HIS K C   1 
ATOM   11618 O  O   . HIS K  1 63  ? 55.442  -5.171  27.045  1.00 29.25 ? 63   HIS K O   1 
ATOM   11619 C  CB  . HIS K  1 63  ? 53.910  -3.519  24.798  1.00 28.79 ? 63   HIS K CB  1 
ATOM   11620 C  CG  . HIS K  1 63  ? 53.699  -2.273  23.991  1.00 26.50 ? 63   HIS K CG  1 
ATOM   11621 N  ND1 . HIS K  1 63  ? 53.864  -2.235  22.624  1.00 25.08 ? 63   HIS K ND1 1 
ATOM   11622 C  CD2 . HIS K  1 63  ? 53.350  -1.019  24.361  1.00 26.95 ? 63   HIS K CD2 1 
ATOM   11623 C  CE1 . HIS K  1 63  ? 53.621  -1.014  22.184  1.00 24.70 ? 63   HIS K CE1 1 
ATOM   11624 N  NE2 . HIS K  1 63  ? 53.313  -0.254  23.217  1.00 26.42 ? 63   HIS K NE2 1 
ATOM   11625 N  N   . PHE K  1 64  ? 53.318  -4.984  27.748  1.00 27.58 ? 64   PHE K N   1 
ATOM   11626 C  CA  . PHE K  1 64  ? 53.358  -6.226  28.509  1.00 27.59 ? 64   PHE K CA  1 
ATOM   11627 C  C   . PHE K  1 64  ? 53.660  -7.405  27.577  1.00 30.20 ? 64   PHE K C   1 
ATOM   11628 O  O   . PHE K  1 64  ? 52.884  -7.711  26.668  1.00 26.80 ? 64   PHE K O   1 
ATOM   11629 C  CB  . PHE K  1 64  ? 52.042  -6.422  29.264  1.00 29.44 ? 64   PHE K CB  1 
ATOM   11630 C  CG  . PHE K  1 64  ? 51.952  -7.722  30.004  1.00 28.27 ? 64   PHE K CG  1 
ATOM   11631 C  CD1 . PHE K  1 64  ? 52.976  -8.134  30.839  1.00 28.25 ? 64   PHE K CD1 1 
ATOM   11632 C  CD2 . PHE K  1 64  ? 50.829  -8.523  29.879  1.00 26.81 ? 64   PHE K CD2 1 
ATOM   11633 C  CE1 . PHE K  1 64  ? 52.890  -9.334  31.515  1.00 28.41 ? 64   PHE K CE1 1 
ATOM   11634 C  CE2 . PHE K  1 64  ? 50.739  -9.718  30.547  1.00 27.27 ? 64   PHE K CE2 1 
ATOM   11635 C  CZ  . PHE K  1 64  ? 51.768  -10.124 31.368  1.00 29.73 ? 64   PHE K CZ  1 
ATOM   11636 N  N   . ASN K  1 65  ? 54.795  -8.063  27.810  1.00 32.03 ? 65   ASN K N   1 
ATOM   11637 C  CA  . ASN K  1 65  ? 55.340  -9.035  26.852  1.00 33.10 ? 65   ASN K CA  1 
ATOM   11638 C  C   . ASN K  1 65  ? 55.937  -10.313 27.455  1.00 35.85 ? 65   ASN K C   1 
ATOM   11639 O  O   . ASN K  1 65  ? 57.093  -10.640 27.180  1.00 39.27 ? 65   ASN K O   1 
ATOM   11640 C  CB  . ASN K  1 65  ? 56.420  -8.359  25.996  1.00 31.18 ? 65   ASN K CB  1 
ATOM   11641 C  CG  . ASN K  1 65  ? 56.885  -9.234  24.848  1.00 33.03 ? 65   ASN K CG  1 
ATOM   11642 O  OD1 . ASN K  1 65  ? 56.141  -10.085 24.365  1.00 33.28 ? 65   ASN K OD1 1 
ATOM   11643 N  ND2 . ASN K  1 65  ? 58.114  -9.021  24.400  1.00 32.76 ? 65   ASN K ND2 1 
ATOM   11644 N  N   . PRO K  1 66  ? 55.144  -11.061 28.238  1.00 32.35 ? 66   PRO K N   1 
ATOM   11645 C  CA  . PRO K  1 66  ? 55.607  -12.247 28.976  1.00 34.38 ? 66   PRO K CA  1 
ATOM   11646 C  C   . PRO K  1 66  ? 56.244  -13.328 28.088  1.00 40.17 ? 66   PRO K C   1 
ATOM   11647 O  O   . PRO K  1 66  ? 56.904  -14.230 28.613  1.00 40.15 ? 66   PRO K O   1 
ATOM   11648 C  CB  . PRO K  1 66  ? 54.318  -12.825 29.578  1.00 36.23 ? 66   PRO K CB  1 
ATOM   11649 C  CG  . PRO K  1 66  ? 53.274  -11.804 29.382  1.00 34.41 ? 66   PRO K CG  1 
ATOM   11650 C  CD  . PRO K  1 66  ? 53.681  -10.937 28.247  1.00 31.13 ? 66   PRO K CD  1 
ATOM   11651 N  N   . LEU K  1 67  ? 56.032  -13.247 26.774  1.00 40.76 ? 67   LEU K N   1 
ATOM   11652 C  CA  . LEU K  1 67  ? 56.478  -14.293 25.849  1.00 39.67 ? 67   LEU K CA  1 
ATOM   11653 C  C   . LEU K  1 67  ? 57.654  -13.862 24.964  1.00 37.86 ? 67   LEU K C   1 
ATOM   11654 O  O   . LEU K  1 67  ? 58.060  -14.595 24.063  1.00 39.96 ? 67   LEU K O   1 
ATOM   11655 C  CB  . LEU K  1 67  ? 55.303  -14.796 24.989  1.00 38.46 ? 67   LEU K CB  1 
ATOM   11656 C  CG  . LEU K  1 67  ? 54.326  -15.759 25.681  1.00 35.71 ? 67   LEU K CG  1 
ATOM   11657 C  CD1 . LEU K  1 67  ? 53.605  -15.077 26.829  1.00 37.34 ? 67   LEU K CD1 1 
ATOM   11658 C  CD2 . LEU K  1 67  ? 53.326  -16.331 24.712  1.00 38.94 ? 67   LEU K CD2 1 
ATOM   11659 N  N   . SER K  1 68  ? 58.205  -12.683 25.239  1.00 36.82 ? 68   SER K N   1 
ATOM   11660 C  CA  . SER K  1 68  ? 59.289  -12.123 24.431  1.00 39.65 ? 68   SER K CA  1 
ATOM   11661 C  C   . SER K  1 68  ? 59.009  -12.282 22.940  1.00 41.39 ? 68   SER K C   1 
ATOM   11662 O  O   . SER K  1 68  ? 59.613  -13.118 22.267  1.00 45.31 ? 68   SER K O   1 
ATOM   11663 C  CB  . SER K  1 68  ? 60.636  -12.756 24.795  1.00 42.99 ? 68   SER K CB  1 
ATOM   11664 O  OG  . SER K  1 68  ? 61.035  -12.401 26.112  1.00 45.16 ? 68   SER K OG  1 
ATOM   11665 N  N   . ARG K  1 69  ? 58.072  -11.482 22.439  1.00 39.09 ? 69   ARG K N   1 
ATOM   11666 C  CA  . ARG K  1 69  ? 57.698  -11.510 21.038  1.00 33.58 ? 69   ARG K CA  1 
ATOM   11667 C  C   . ARG K  1 69  ? 57.795  -10.106 20.485  1.00 33.60 ? 69   ARG K C   1 
ATOM   11668 O  O   . ARG K  1 69  ? 57.999  -9.159  21.245  1.00 32.18 ? 69   ARG K O   1 
ATOM   11669 C  CB  . ARG K  1 69  ? 56.286  -12.060 20.879  1.00 32.17 ? 69   ARG K CB  1 
ATOM   11670 C  CG  . ARG K  1 69  ? 56.223  -13.546 21.093  1.00 35.63 ? 69   ARG K CG  1 
ATOM   11671 C  CD  . ARG K  1 69  ? 54.873  -14.101 20.729  1.00 39.45 ? 69   ARG K CD  1 
ATOM   11672 N  NE  . ARG K  1 69  ? 54.826  -15.545 20.932  1.00 43.94 ? 69   ARG K NE  1 
ATOM   11673 C  CZ  . ARG K  1 69  ? 53.791  -16.314 20.606  1.00 44.17 ? 69   ARG K CZ  1 
ATOM   11674 N  NH1 . ARG K  1 69  ? 52.711  -15.778 20.051  1.00 45.33 ? 69   ARG K NH1 1 
ATOM   11675 N  NH2 . ARG K  1 69  ? 53.838  -17.620 20.835  1.00 48.39 ? 69   ARG K NH2 1 
ATOM   11676 N  N   . LYS K  1 70  ? 57.673  -9.980  19.162  1.00 34.49 ? 70   LYS K N   1 
ATOM   11677 C  CA  . LYS K  1 70  ? 57.719  -8.677  18.500  1.00 31.45 ? 70   LYS K CA  1 
ATOM   11678 C  C   . LYS K  1 70  ? 56.331  -8.055  18.481  1.00 28.07 ? 70   LYS K C   1 
ATOM   11679 O  O   . LYS K  1 70  ? 55.327  -8.763  18.473  1.00 28.01 ? 70   LYS K O   1 
ATOM   11680 C  CB  . LYS K  1 70  ? 58.247  -8.796  17.068  1.00 29.42 ? 70   LYS K CB  1 
ATOM   11681 C  CG  . LYS K  1 70  ? 59.747  -9.004  16.941  1.00 33.35 ? 70   LYS K CG  1 
ATOM   11682 C  CD  . LYS K  1 70  ? 60.181  -8.942  15.473  1.00 35.86 ? 70   LYS K CD  1 
ATOM   11683 C  CE  . LYS K  1 70  ? 61.348  -9.873  15.197  1.00 42.97 ? 70   LYS K CE  1 
ATOM   11684 N  NZ  . LYS K  1 70  ? 60.982  -11.314 15.416  1.00 49.10 ? 70   LYS K NZ  1 
ATOM   11685 N  N   . HIS K  1 71  ? 56.294  -6.727  18.466  1.00 27.21 ? 71   HIS K N   1 
ATOM   11686 C  CA  . HIS K  1 71  ? 55.046  -5.970  18.444  1.00 26.73 ? 71   HIS K CA  1 
ATOM   11687 C  C   . HIS K  1 71  ? 54.180  -6.329  17.262  1.00 25.44 ? 71   HIS K C   1 
ATOM   11688 O  O   . HIS K  1 71  ? 54.669  -6.419  16.141  1.00 27.57 ? 71   HIS K O   1 
ATOM   11689 C  CB  . HIS K  1 71  ? 55.342  -4.468  18.387  1.00 27.02 ? 71   HIS K CB  1 
ATOM   11690 C  CG  . HIS K  1 71  ? 54.117  -3.611  18.361  1.00 24.37 ? 71   HIS K CG  1 
ATOM   11691 N  ND1 . HIS K  1 71  ? 53.307  -3.435  19.463  1.00 24.10 ? 71   HIS K ND1 1 
ATOM   11692 C  CD2 . HIS K  1 71  ? 53.570  -2.868  17.372  1.00 23.93 ? 71   HIS K CD2 1 
ATOM   11693 C  CE1 . HIS K  1 71  ? 52.311  -2.626  19.153  1.00 24.90 ? 71   HIS K CE1 1 
ATOM   11694 N  NE2 . HIS K  1 71  ? 52.446  -2.270  17.890  1.00 24.92 ? 71   HIS K NE2 1 
ATOM   11695 N  N   . GLY K  1 72  ? 52.886  -6.505  17.512  1.00 26.36 ? 72   GLY K N   1 
ATOM   11696 C  CA  . GLY K  1 72  ? 51.933  -6.762  16.450  1.00 26.36 ? 72   GLY K CA  1 
ATOM   11697 C  C   . GLY K  1 72  ? 50.596  -6.103  16.706  1.00 25.28 ? 72   GLY K C   1 
ATOM   11698 O  O   . GLY K  1 72  ? 50.447  -5.338  17.652  1.00 23.32 ? 72   GLY K O   1 
ATOM   11699 N  N   . GLY K  1 73  ? 49.629  -6.383  15.838  1.00 27.41 ? 73   GLY K N   1 
ATOM   11700 C  CA  . GLY K  1 73  ? 48.257  -5.964  16.060  1.00 24.95 ? 73   GLY K CA  1 
ATOM   11701 C  C   . GLY K  1 73  ? 47.515  -7.052  16.819  1.00 26.81 ? 73   GLY K C   1 
ATOM   11702 O  O   . GLY K  1 73  ? 47.959  -8.200  16.848  1.00 26.20 ? 73   GLY K O   1 
ATOM   11703 N  N   . PRO K  1 74  ? 46.370  -6.710  17.432  1.00 27.43 ? 74   PRO K N   1 
ATOM   11704 C  CA  . PRO K  1 74  ? 45.709  -7.742  18.234  1.00 28.42 ? 74   PRO K CA  1 
ATOM   11705 C  C   . PRO K  1 74  ? 45.453  -8.999  17.411  1.00 29.40 ? 74   PRO K C   1 
ATOM   11706 O  O   . PRO K  1 74  ? 45.519  -10.105 17.950  1.00 29.34 ? 74   PRO K O   1 
ATOM   11707 C  CB  . PRO K  1 74  ? 44.376  -7.091  18.640  1.00 25.79 ? 74   PRO K CB  1 
ATOM   11708 C  CG  . PRO K  1 74  ? 44.544  -5.644  18.404  1.00 25.21 ? 74   PRO K CG  1 
ATOM   11709 C  CD  . PRO K  1 74  ? 45.562  -5.484  17.315  1.00 25.22 ? 74   PRO K CD  1 
ATOM   11710 N  N   . LYS K  1 75  ? 45.167  -8.835  16.121  1.00 31.97 ? 75   LYS K N   1 
ATOM   11711 C  CA  . LYS K  1 75  ? 44.769  -9.977  15.297  1.00 33.84 ? 75   LYS K CA  1 
ATOM   11712 C  C   . LYS K  1 75  ? 45.953  -10.831 14.841  1.00 34.68 ? 75   LYS K C   1 
ATOM   11713 O  O   . LYS K  1 75  ? 45.764  -11.956 14.367  1.00 36.12 ? 75   LYS K O   1 
ATOM   11714 C  CB  . LYS K  1 75  ? 43.957  -9.525  14.078  1.00 36.51 ? 75   LYS K CB  1 
ATOM   11715 C  CG  . LYS K  1 75  ? 42.819  -8.543  14.358  1.00 36.67 ? 75   LYS K CG  1 
ATOM   11716 C  CD  . LYS K  1 75  ? 42.005  -8.911  15.594  1.00 40.64 ? 75   LYS K CD  1 
ATOM   11717 C  CE  . LYS K  1 75  ? 41.340  -10.274 15.492  1.00 43.21 ? 75   LYS K CE  1 
ATOM   11718 N  NZ  . LYS K  1 75  ? 40.861  -10.697 16.846  1.00 47.27 ? 75   LYS K NZ  1 
ATOM   11719 N  N   . ASP K  1 76  ? 47.166  -10.292 14.985  1.00 35.10 ? 76   ASP K N   1 
ATOM   11720 C  CA  . ASP K  1 76  ? 48.390  -10.954 14.523  1.00 31.58 ? 76   ASP K CA  1 
ATOM   11721 C  C   . ASP K  1 76  ? 48.795  -12.089 15.462  1.00 31.89 ? 76   ASP K C   1 
ATOM   11722 O  O   . ASP K  1 76  ? 48.446  -12.072 16.632  1.00 31.33 ? 76   ASP K O   1 
ATOM   11723 C  CB  . ASP K  1 76  ? 49.542  -9.942  14.402  1.00 29.58 ? 76   ASP K CB  1 
ATOM   11724 C  CG  . ASP K  1 76  ? 49.309  -8.894  13.312  1.00 32.90 ? 76   ASP K CG  1 
ATOM   11725 O  OD1 . ASP K  1 76  ? 48.628  -9.193  12.302  1.00 36.30 ? 76   ASP K OD1 1 
ATOM   11726 O  OD2 . ASP K  1 76  ? 49.819  -7.763  13.461  1.00 33.24 ? 76   ASP K OD2 1 
ATOM   11727 N  N   . GLU K  1 77  ? 49.522  -13.074 14.938  1.00 37.50 ? 77   GLU K N   1 
ATOM   11728 C  CA  . GLU K  1 77  ? 50.088  -14.162 15.744  1.00 39.12 ? 77   GLU K CA  1 
ATOM   11729 C  C   . GLU K  1 77  ? 51.264  -13.656 16.577  1.00 37.85 ? 77   GLU K C   1 
ATOM   11730 O  O   . GLU K  1 77  ? 51.334  -13.885 17.794  1.00 38.51 ? 77   GLU K O   1 
ATOM   11731 C  CB  . GLU K  1 77  ? 50.565  -15.304 14.840  1.00 41.79 ? 77   GLU K CB  1 
ATOM   11732 C  CG  . GLU K  1 77  ? 49.484  -16.278 14.400  1.00 48.99 ? 77   GLU K CG  1 
ATOM   11733 C  CD  . GLU K  1 77  ? 49.366  -17.482 15.320  1.00 53.96 ? 77   GLU K CD  1 
ATOM   11734 O  OE1 . GLU K  1 77  ? 48.391  -18.254 15.169  1.00 50.70 ? 77   GLU K OE1 1 
ATOM   11735 O  OE2 . GLU K  1 77  ? 50.255  -17.656 16.188  1.00 57.28 ? 77   GLU K OE2 1 
ATOM   11736 N  N   . GLU K  1 78  ? 52.193  -12.986 15.899  1.00 34.26 ? 78   GLU K N   1 
ATOM   11737 C  CA  . GLU K  1 78  ? 53.328  -12.353 16.549  1.00 34.51 ? 78   GLU K CA  1 
ATOM   11738 C  C   . GLU K  1 78  ? 52.913  -11.014 17.139  1.00 32.91 ? 78   GLU K C   1 
ATOM   11739 O  O   . GLU K  1 78  ? 52.864  -9.998  16.442  1.00 30.77 ? 78   GLU K O   1 
ATOM   11740 C  CB  . GLU K  1 78  ? 54.483  -12.152 15.565  1.00 35.32 ? 78   GLU K CB  1 
ATOM   11741 C  CG  . GLU K  1 78  ? 55.560  -13.213 15.647  1.00 39.47 ? 78   GLU K CG  1 
ATOM   11742 C  CD  . GLU K  1 78  ? 56.315  -13.177 16.959  1.00 40.16 ? 78   GLU K CD  1 
ATOM   11743 O  OE1 . GLU K  1 78  ? 57.067  -12.206 17.195  1.00 36.64 ? 78   GLU K OE1 1 
ATOM   11744 O  OE2 . GLU K  1 78  ? 56.166  -14.134 17.750  1.00 44.96 ? 78   GLU K OE2 1 
ATOM   11745 N  N   . ARG K  1 79  ? 52.615  -11.022 18.432  1.00 33.19 ? 79   ARG K N   1 
ATOM   11746 C  CA  . ARG K  1 79  ? 52.205  -9.817  19.130  1.00 29.78 ? 79   ARG K CA  1 
ATOM   11747 C  C   . ARG K  1 79  ? 52.624  -9.928  20.573  1.00 30.02 ? 79   ARG K C   1 
ATOM   11748 O  O   . ARG K  1 79  ? 52.888  -11.026 21.067  1.00 31.77 ? 79   ARG K O   1 
ATOM   11749 C  CB  . ARG K  1 79  ? 50.691  -9.653  19.068  1.00 28.16 ? 79   ARG K CB  1 
ATOM   11750 C  CG  . ARG K  1 79  ? 49.939  -10.809 19.692  1.00 28.48 ? 79   ARG K CG  1 
ATOM   11751 C  CD  . ARG K  1 79  ? 48.465  -10.514 19.832  1.00 25.69 ? 79   ARG K CD  1 
ATOM   11752 N  NE  . ARG K  1 79  ? 48.157  -9.839  21.086  1.00 27.73 ? 79   ARG K NE  1 
ATOM   11753 C  CZ  . ARG K  1 79  ? 46.923  -9.591  21.510  1.00 27.72 ? 79   ARG K CZ  1 
ATOM   11754 N  NH1 . ARG K  1 79  ? 45.884  -9.964  20.776  1.00 26.56 ? 79   ARG K NH1 1 
ATOM   11755 N  NH2 . ARG K  1 79  ? 46.723  -8.976  22.669  1.00 27.46 ? 79   ARG K NH2 1 
ATOM   11756 N  N   . HIS K  1 80  ? 52.692  -8.788  21.246  1.00 29.15 ? 80   HIS K N   1 
ATOM   11757 C  CA  . HIS K  1 80  ? 52.845  -8.782  22.689  1.00 29.71 ? 80   HIS K CA  1 
ATOM   11758 C  C   . HIS K  1 80  ? 51.471  -9.041  23.289  1.00 28.12 ? 80   HIS K C   1 
ATOM   11759 O  O   . HIS K  1 80  ? 50.458  -8.666  22.708  1.00 27.59 ? 80   HIS K O   1 
ATOM   11760 C  CB  . HIS K  1 80  ? 53.357  -7.431  23.176  1.00 30.38 ? 80   HIS K CB  1 
ATOM   11761 C  CG  . HIS K  1 80  ? 54.634  -6.994  22.535  1.00 28.25 ? 80   HIS K CG  1 
ATOM   11762 N  ND1 . HIS K  1 80  ? 54.849  -5.697  22.123  1.00 25.54 ? 80   HIS K ND1 1 
ATOM   11763 C  CD2 . HIS K  1 80  ? 55.767  -7.674  22.245  1.00 30.08 ? 80   HIS K CD2 1 
ATOM   11764 C  CE1 . HIS K  1 80  ? 56.060  -5.595  21.606  1.00 27.48 ? 80   HIS K CE1 1 
ATOM   11765 N  NE2 . HIS K  1 80  ? 56.640  -6.782  21.668  1.00 30.30 ? 80   HIS K NE2 1 
ATOM   11766 N  N   . VAL K  1 81  ? 51.424  -9.679  24.450  1.00 30.16 ? 81   VAL K N   1 
ATOM   11767 C  CA  . VAL K  1 81  ? 50.140  -9.911  25.103  1.00 30.18 ? 81   VAL K CA  1 
ATOM   11768 C  C   . VAL K  1 81  ? 49.336  -8.603  25.224  1.00 29.66 ? 81   VAL K C   1 
ATOM   11769 O  O   . VAL K  1 81  ? 48.131  -8.598  24.980  1.00 28.83 ? 81   VAL K O   1 
ATOM   11770 C  CB  . VAL K  1 81  ? 50.313  -10.628 26.471  1.00 31.09 ? 81   VAL K CB  1 
ATOM   11771 C  CG1 . VAL K  1 81  ? 49.059  -10.482 27.333  1.00 27.39 ? 81   VAL K CG1 1 
ATOM   11772 C  CG2 . VAL K  1 81  ? 50.666  -12.098 26.250  1.00 28.23 ? 81   VAL K CG2 1 
ATOM   11773 N  N   . GLY K  1 82  ? 50.012  -7.496  25.554  1.00 29.07 ? 82   GLY K N   1 
ATOM   11774 C  CA  . GLY K  1 82  ? 49.356  -6.210  25.757  1.00 26.48 ? 82   GLY K CA  1 
ATOM   11775 C  C   . GLY K  1 82  ? 49.109  -5.387  24.500  1.00 28.27 ? 82   GLY K C   1 
ATOM   11776 O  O   . GLY K  1 82  ? 48.825  -4.188  24.582  1.00 27.96 ? 82   GLY K O   1 
ATOM   11777 N  N   . ASP K  1 83  ? 49.214  -6.031  23.338  1.00 26.61 ? 83   ASP K N   1 
ATOM   11778 C  CA  . ASP K  1 83  ? 48.996  -5.382  22.037  1.00 26.82 ? 83   ASP K CA  1 
ATOM   11779 C  C   . ASP K  1 83  ? 47.527  -5.338  21.658  1.00 25.72 ? 83   ASP K C   1 
ATOM   11780 O  O   . ASP K  1 83  ? 47.002  -6.313  21.128  1.00 25.93 ? 83   ASP K O   1 
ATOM   11781 C  CB  . ASP K  1 83  ? 49.748  -6.136  20.935  1.00 26.32 ? 83   ASP K CB  1 
ATOM   11782 C  CG  . ASP K  1 83  ? 51.210  -5.762  20.868  1.00 26.65 ? 83   ASP K CG  1 
ATOM   11783 O  OD1 . ASP K  1 83  ? 51.524  -4.610  21.210  1.00 26.75 ? 83   ASP K OD1 1 
ATOM   11784 O  OD2 . ASP K  1 83  ? 52.042  -6.605  20.473  1.00 27.05 ? 83   ASP K OD2 1 
ATOM   11785 N  N   . LEU K  1 84  ? 46.865  -4.212  21.922  1.00 26.83 ? 84   LEU K N   1 
ATOM   11786 C  CA  . LEU K  1 84  ? 45.425  -4.102  21.672  1.00 26.93 ? 84   LEU K CA  1 
ATOM   11787 C  C   . LEU K  1 84  ? 45.144  -3.228  20.448  1.00 26.82 ? 84   LEU K C   1 
ATOM   11788 O  O   . LEU K  1 84  ? 43.999  -3.018  20.058  1.00 27.16 ? 84   LEU K O   1 
ATOM   11789 C  CB  . LEU K  1 84  ? 44.659  -3.626  22.924  1.00 23.01 ? 84   LEU K CB  1 
ATOM   11790 C  CG  . LEU K  1 84  ? 44.647  -4.576  24.132  1.00 20.04 ? 84   LEU K CG  1 
ATOM   11791 C  CD1 . LEU K  1 84  ? 43.817  -4.007  25.246  1.00 20.89 ? 84   LEU K CD1 1 
ATOM   11792 C  CD2 . LEU K  1 84  ? 44.135  -5.956  23.781  1.00 20.13 ? 84   LEU K CD2 1 
ATOM   11793 N  N   . GLY K  1 85  ? 46.211  -2.750  19.823  1.00 27.56 ? 85   GLY K N   1 
ATOM   11794 C  CA  . GLY K  1 85  ? 46.088  -1.998  18.598  1.00 22.65 ? 85   GLY K CA  1 
ATOM   11795 C  C   . GLY K  1 85  ? 45.685  -0.554  18.787  1.00 24.30 ? 85   GLY K C   1 
ATOM   11796 O  O   . GLY K  1 85  ? 46.342  0.221   19.481  1.00 25.20 ? 85   GLY K O   1 
ATOM   11797 N  N   . ASN K  1 86  ? 44.578  -0.205  18.153  1.00 25.41 ? 86   ASN K N   1 
ATOM   11798 C  CA  . ASN K  1 86  ? 44.156  1.170   18.004  1.00 25.76 ? 86   ASN K CA  1 
ATOM   11799 C  C   . ASN K  1 86  ? 42.754  1.398   18.566  1.00 25.88 ? 86   ASN K C   1 
ATOM   11800 O  O   . ASN K  1 86  ? 41.935  0.473   18.622  1.00 20.14 ? 86   ASN K O   1 
ATOM   11801 C  CB  . ASN K  1 86  ? 44.161  1.549   16.518  1.00 25.95 ? 86   ASN K CB  1 
ATOM   11802 C  CG  . ASN K  1 86  ? 45.551  1.804   15.982  1.00 27.12 ? 86   ASN K CG  1 
ATOM   11803 O  OD1 . ASN K  1 86  ? 46.211  2.757   16.381  1.00 29.41 ? 86   ASN K OD1 1 
ATOM   11804 N  ND2 . ASN K  1 86  ? 45.998  0.962   15.059  1.00 27.21 ? 86   ASN K ND2 1 
ATOM   11805 N  N   . VAL K  1 87  ? 42.497  2.638   18.980  1.00 24.72 ? 87   VAL K N   1 
ATOM   11806 C  CA  . VAL K  1 87  ? 41.169  3.086   19.354  1.00 24.38 ? 87   VAL K CA  1 
ATOM   11807 C  C   . VAL K  1 87  ? 40.890  4.289   18.458  1.00 25.07 ? 87   VAL K C   1 
ATOM   11808 O  O   . VAL K  1 87  ? 41.832  4.920   17.991  1.00 24.90 ? 87   VAL K O   1 
ATOM   11809 C  CB  . VAL K  1 87  ? 41.106  3.465   20.858  1.00 26.51 ? 87   VAL K CB  1 
ATOM   11810 C  CG1 . VAL K  1 87  ? 41.248  2.216   21.729  1.00 23.64 ? 87   VAL K CG1 1 
ATOM   11811 C  CG2 . VAL K  1 87  ? 42.179  4.492   21.205  1.00 20.97 ? 87   VAL K CG2 1 
ATOM   11812 N  N   . THR K  1 88  ? 39.620  4.601   18.194  1.00 25.04 ? 88   THR K N   1 
ATOM   11813 C  CA  . THR K  1 88  ? 39.297  5.664   17.242  1.00 27.66 ? 88   THR K CA  1 
ATOM   11814 C  C   . THR K  1 88  ? 38.634  6.896   17.873  1.00 29.56 ? 88   THR K C   1 
ATOM   11815 O  O   . THR K  1 88  ? 37.566  6.796   18.479  1.00 31.56 ? 88   THR K O   1 
ATOM   11816 C  CB  . THR K  1 88  ? 38.379  5.146   16.097  1.00 29.49 ? 88   THR K CB  1 
ATOM   11817 O  OG1 . THR K  1 88  ? 38.885  3.907   15.582  1.00 29.33 ? 88   THR K OG1 1 
ATOM   11818 C  CG2 . THR K  1 88  ? 38.280  6.176   14.968  1.00 27.45 ? 88   THR K CG2 1 
ATOM   11819 N  N   . ALA K  1 89  ? 39.257  8.058   17.693  1.00 28.98 ? 89   ALA K N   1 
ATOM   11820 C  CA  . ALA K  1 89  ? 38.686  9.327   18.139  1.00 31.06 ? 89   ALA K CA  1 
ATOM   11821 C  C   . ALA K  1 89  ? 37.891  10.024  17.032  1.00 35.17 ? 89   ALA K C   1 
ATOM   11822 O  O   . ALA K  1 89  ? 38.357  10.140  15.896  1.00 36.60 ? 89   ALA K O   1 
ATOM   11823 C  CB  . ALA K  1 89  ? 39.782  10.240  18.643  1.00 30.14 ? 89   ALA K CB  1 
ATOM   11824 N  N   . GLY K  1 90  ? 36.693  10.498  17.360  1.00 37.84 ? 90   GLY K N   1 
ATOM   11825 C  CA  . GLY K  1 90  ? 35.898  11.256  16.405  1.00 38.05 ? 90   GLY K CA  1 
ATOM   11826 C  C   . GLY K  1 90  ? 36.359  12.705  16.348  1.00 42.49 ? 90   GLY K C   1 
ATOM   11827 O  O   . GLY K  1 90  ? 37.302  13.082  17.052  1.00 39.98 ? 90   GLY K O   1 
ATOM   11828 N  N   . LYS K  1 91  ? 35.705  13.512  15.507  1.00 45.24 ? 91   LYS K N   1 
ATOM   11829 C  CA  . LYS K  1 91  ? 35.963  14.955  15.442  1.00 45.08 ? 91   LYS K CA  1 
ATOM   11830 C  C   . LYS K  1 91  ? 35.785  15.582  16.819  1.00 44.30 ? 91   LYS K C   1 
ATOM   11831 O  O   . LYS K  1 91  ? 36.394  16.601  17.139  1.00 43.91 ? 91   LYS K O   1 
ATOM   11832 C  CB  . LYS K  1 91  ? 35.024  15.632  14.436  1.00 47.91 ? 91   LYS K CB  1 
ATOM   11833 C  CG  . LYS K  1 91  ? 35.584  15.739  13.020  1.00 53.62 ? 91   LYS K CG  1 
ATOM   11834 C  CD  . LYS K  1 91  ? 34.510  16.131  12.002  1.00 57.98 ? 91   LYS K CD  1 
ATOM   11835 C  CE  . LYS K  1 91  ? 33.570  14.964  11.686  1.00 58.48 ? 91   LYS K CE  1 
ATOM   11836 N  NZ  . LYS K  1 91  ? 34.243  13.868  10.922  1.00 55.93 ? 91   LYS K NZ  1 
ATOM   11837 N  N   . ASP K  1 92  ? 34.940  14.944  17.623  1.00 46.95 ? 92   ASP K N   1 
ATOM   11838 C  CA  . ASP K  1 92  ? 34.647  15.354  18.990  1.00 44.49 ? 92   ASP K CA  1 
ATOM   11839 C  C   . ASP K  1 92  ? 35.874  15.247  19.898  1.00 43.95 ? 92   ASP K C   1 
ATOM   11840 O  O   . ASP K  1 92  ? 35.954  15.900  20.934  1.00 43.54 ? 92   ASP K O   1 
ATOM   11841 C  CB  . ASP K  1 92  ? 33.530  14.457  19.532  1.00 46.65 ? 92   ASP K CB  1 
ATOM   11842 C  CG  . ASP K  1 92  ? 32.765  15.093  20.681  1.00 60.82 ? 92   ASP K CG  1 
ATOM   11843 O  OD1 . ASP K  1 92  ? 33.116  16.226  21.089  1.00 64.57 ? 92   ASP K OD1 1 
ATOM   11844 O  OD2 . ASP K  1 92  ? 31.806  14.454  21.176  1.00 62.42 ? 92   ASP K OD2 1 
ATOM   11845 N  N   . GLY K  1 93  ? 36.833  14.417  19.499  1.00 42.96 ? 93   GLY K N   1 
ATOM   11846 C  CA  . GLY K  1 93  ? 37.952  14.073  20.355  1.00 35.95 ? 93   GLY K CA  1 
ATOM   11847 C  C   . GLY K  1 93  ? 37.602  12.870  21.208  1.00 33.98 ? 93   GLY K C   1 
ATOM   11848 O  O   . GLY K  1 93  ? 38.345  12.486  22.093  1.00 34.77 ? 93   GLY K O   1 
ATOM   11849 N  N   . VAL K  1 94  ? 36.458  12.262  20.933  1.00 36.96 ? 94   VAL K N   1 
ATOM   11850 C  CA  . VAL K  1 94  ? 35.988  11.140  21.739  1.00 38.89 ? 94   VAL K CA  1 
ATOM   11851 C  C   . VAL K  1 94  ? 36.298  9.785   21.110  1.00 31.42 ? 94   VAL K C   1 
ATOM   11852 O  O   . VAL K  1 94  ? 35.910  9.510   19.987  1.00 33.10 ? 94   VAL K O   1 
ATOM   11853 C  CB  . VAL K  1 94  ? 34.452  11.226  21.997  1.00 43.66 ? 94   VAL K CB  1 
ATOM   11854 C  CG1 . VAL K  1 94  ? 34.023  10.248  23.099  1.00 37.37 ? 94   VAL K CG1 1 
ATOM   11855 C  CG2 . VAL K  1 94  ? 34.041  12.642  22.359  1.00 44.32 ? 94   VAL K CG2 1 
ATOM   11856 N  N   . ALA K  1 95  ? 36.983  8.930   21.851  1.00 30.78 ? 95   ALA K N   1 
ATOM   11857 C  CA  . ALA K  1 95  ? 37.131  7.539   21.439  1.00 31.25 ? 95   ALA K CA  1 
ATOM   11858 C  C   . ALA K  1 95  ? 36.241  6.614   22.268  1.00 32.32 ? 95   ALA K C   1 
ATOM   11859 O  O   . ALA K  1 95  ? 36.434  6.466   23.477  1.00 29.52 ? 95   ALA K O   1 
ATOM   11860 C  CB  . ALA K  1 95  ? 38.594  7.092   21.533  1.00 29.20 ? 95   ALA K CB  1 
ATOM   11861 N  N   . ASN K  1 96  ? 35.254  6.005   21.614  1.00 34.39 ? 96   ASN K N   1 
ATOM   11862 C  CA  . ASN K  1 96  ? 34.522  4.895   22.217  1.00 31.78 ? 96   ASN K CA  1 
ATOM   11863 C  C   . ASN K  1 96  ? 35.305  3.620   22.008  1.00 29.66 ? 96   ASN K C   1 
ATOM   11864 O  O   . ASN K  1 96  ? 35.708  3.305   20.875  1.00 28.48 ? 96   ASN K O   1 
ATOM   11865 C  CB  . ASN K  1 96  ? 33.132  4.739   21.608  1.00 31.47 ? 96   ASN K CB  1 
ATOM   11866 C  CG  . ASN K  1 96  ? 32.276  5.952   21.824  1.00 38.18 ? 96   ASN K CG  1 
ATOM   11867 O  OD1 . ASN K  1 96  ? 32.283  6.541   22.908  1.00 41.84 ? 96   ASN K OD1 1 
ATOM   11868 N  ND2 . ASN K  1 96  ? 31.545  6.356   20.787  1.00 40.56 ? 96   ASN K ND2 1 
ATOM   11869 N  N   . VAL K  1 97  ? 35.530  2.901   23.101  1.00 23.36 ? 97   VAL K N   1 
ATOM   11870 C  CA  . VAL K  1 97  ? 36.321  1.689   23.058  1.00 24.27 ? 97   VAL K CA  1 
ATOM   11871 C  C   . VAL K  1 97  ? 35.428  0.479   23.261  1.00 26.27 ? 97   VAL K C   1 
ATOM   11872 O  O   . VAL K  1 97  ? 34.484  0.508   24.048  1.00 26.35 ? 97   VAL K O   1 
ATOM   11873 C  CB  . VAL K  1 97  ? 37.405  1.694   24.148  1.00 24.61 ? 97   VAL K CB  1 
ATOM   11874 C  CG1 . VAL K  1 97  ? 38.242  0.440   24.062  1.00 24.37 ? 97   VAL K CG1 1 
ATOM   11875 C  CG2 . VAL K  1 97  ? 38.275  2.954   24.048  1.00 25.19 ? 97   VAL K CG2 1 
ATOM   11876 N  N   . SER K  1 98  ? 35.726  -0.590  22.542  1.00 25.51 ? 98   SER K N   1 
ATOM   11877 C  CA  . SER K  1 98  ? 35.031  -1.853  22.724  1.00 25.25 ? 98   SER K CA  1 
ATOM   11878 C  C   . SER K  1 98  ? 35.830  -2.872  21.935  1.00 27.37 ? 98   SER K C   1 
ATOM   11879 O  O   . SER K  1 98  ? 35.863  -2.863  20.699  1.00 27.06 ? 98   SER K O   1 
ATOM   11880 C  CB  . SER K  1 98  ? 33.569  -1.774  22.255  1.00 30.73 ? 98   SER K CB  1 
ATOM   11881 O  OG  . SER K  1 98  ? 32.860  -2.989  22.495  1.00 33.94 ? 98   SER K OG  1 
ATOM   11882 N  N   . ILE K  1 99  ? 36.516  -3.727  22.672  1.00 26.42 ? 99   ILE K N   1 
ATOM   11883 C  CA  . ILE K  1 99  ? 37.443  -4.666  22.091  1.00 25.83 ? 99   ILE K CA  1 
ATOM   11884 C  C   . ILE K  1 99  ? 37.202  -5.969  22.837  1.00 27.18 ? 99   ILE K C   1 
ATOM   11885 O  O   . ILE K  1 99  ? 37.005  -5.960  24.045  1.00 27.87 ? 99   ILE K O   1 
ATOM   11886 C  CB  . ILE K  1 99  ? 38.906  -4.160  22.287  1.00 24.21 ? 99   ILE K CB  1 
ATOM   11887 C  CG1 . ILE K  1 99  ? 39.136  -2.860  21.504  1.00 24.90 ? 99   ILE K CG1 1 
ATOM   11888 C  CG2 . ILE K  1 99  ? 39.926  -5.195  21.874  1.00 25.42 ? 99   ILE K CG2 1 
ATOM   11889 C  CD1 . ILE K  1 99  ? 40.468  -2.181  21.779  1.00 22.99 ? 99   ILE K CD1 1 
ATOM   11890 N  N   . GLU K  1 100 ? 37.178  -7.085  22.123  1.00 27.60 ? 100  GLU K N   1 
ATOM   11891 C  CA  . GLU K  1 100 ? 37.220  -8.380  22.776  1.00 27.39 ? 100  GLU K CA  1 
ATOM   11892 C  C   . GLU K  1 100 ? 38.562  -9.047  22.453  1.00 29.11 ? 100  GLU K C   1 
ATOM   11893 O  O   . GLU K  1 100 ? 39.003  -9.006  21.309  1.00 30.07 ? 100  GLU K O   1 
ATOM   11894 C  CB  . GLU K  1 100 ? 36.050  -9.250  22.325  1.00 30.04 ? 100  GLU K CB  1 
ATOM   11895 C  CG  . GLU K  1 100 ? 36.252  -10.716 22.668  1.00 35.68 ? 100  GLU K CG  1 
ATOM   11896 C  CD  . GLU K  1 100 ? 35.084  -11.592 22.260  1.00 41.45 ? 100  GLU K CD  1 
ATOM   11897 O  OE1 . GLU K  1 100 ? 33.927  -11.184 22.518  1.00 40.98 ? 100  GLU K OE1 1 
ATOM   11898 O  OE2 . GLU K  1 100 ? 35.332  -12.692 21.704  1.00 41.78 ? 100  GLU K OE2 1 
ATOM   11899 N  N   . ASP K  1 101 ? 39.211  -9.640  23.463  1.00 31.51 ? 101  ASP K N   1 
ATOM   11900 C  CA  . ASP K  1 101 ? 40.558  -10.221 23.325  1.00 32.05 ? 101  ASP K CA  1 
ATOM   11901 C  C   . ASP K  1 101 ? 40.720  -11.521 24.124  1.00 31.60 ? 101  ASP K C   1 
ATOM   11902 O  O   . ASP K  1 101 ? 40.320  -11.592 25.276  1.00 31.53 ? 101  ASP K O   1 
ATOM   11903 C  CB  . ASP K  1 101 ? 41.631  -9.217  23.781  1.00 27.85 ? 101  ASP K CB  1 
ATOM   11904 C  CG  . ASP K  1 101 ? 43.028  -9.581  23.283  1.00 28.77 ? 101  ASP K CG  1 
ATOM   11905 O  OD1 . ASP K  1 101 ? 43.299  -9.423  22.075  1.00 33.23 ? 101  ASP K OD1 1 
ATOM   11906 O  OD2 . ASP K  1 101 ? 43.867  -10.020 24.091  1.00 29.23 ? 101  ASP K OD2 1 
ATOM   11907 N  N   . ARG K  1 102 ? 41.329  -12.533 23.511  1.00 32.42 ? 102  ARG K N   1 
ATOM   11908 C  CA  . ARG K  1 102 ? 41.571  -13.824 24.156  1.00 31.84 ? 102  ARG K CA  1 
ATOM   11909 C  C   . ARG K  1 102 ? 43.017  -13.997 24.633  1.00 31.92 ? 102  ARG K C   1 
ATOM   11910 O  O   . ARG K  1 102 ? 43.375  -15.037 25.199  1.00 30.26 ? 102  ARG K O   1 
ATOM   11911 C  CB  . ARG K  1 102 ? 41.214  -14.964 23.198  1.00 33.51 ? 102  ARG K CB  1 
ATOM   11912 C  CG  . ARG K  1 102 ? 39.749  -14.978 22.793  1.00 40.68 ? 102  ARG K CG  1 
ATOM   11913 C  CD  . ARG K  1 102 ? 39.417  -16.102 21.797  1.00 46.73 ? 102  ARG K CD  1 
ATOM   11914 N  NE  . ARG K  1 102 ? 37.995  -16.460 21.857  1.00 49.91 ? 102  ARG K NE  1 
ATOM   11915 C  CZ  . ARG K  1 102 ? 37.006  -15.732 21.331  1.00 51.33 ? 102  ARG K CZ  1 
ATOM   11916 N  NH1 . ARG K  1 102 ? 37.272  -14.592 20.694  1.00 51.49 ? 102  ARG K NH1 1 
ATOM   11917 N  NH2 . ARG K  1 102 ? 35.743  -16.136 21.447  1.00 44.33 ? 102  ARG K NH2 1 
ATOM   11918 N  N   . VAL K  1 103 ? 43.844  -12.981 24.396  1.00 33.00 ? 103  VAL K N   1 
ATOM   11919 C  CA  . VAL K  1 103 ? 45.261  -13.033 24.756  1.00 30.24 ? 103  VAL K CA  1 
ATOM   11920 C  C   . VAL K  1 103 ? 45.516  -12.411 26.132  1.00 31.30 ? 103  VAL K C   1 
ATOM   11921 O  O   . VAL K  1 103 ? 46.156  -13.028 26.987  1.00 33.32 ? 103  VAL K O   1 
ATOM   11922 C  CB  . VAL K  1 103 ? 46.158  -12.383 23.673  1.00 29.99 ? 103  VAL K CB  1 
ATOM   11923 C  CG1 . VAL K  1 103 ? 47.617  -12.393 24.106  1.00 28.89 ? 103  VAL K CG1 1 
ATOM   11924 C  CG2 . VAL K  1 103 ? 45.997  -13.111 22.338  1.00 30.41 ? 103  VAL K CG2 1 
ATOM   11925 N  N   . ILE K  1 104 ? 45.010  -11.200 26.359  1.00 30.09 ? 104  ILE K N   1 
ATOM   11926 C  CA  . ILE K  1 104 ? 45.021  -10.652 27.714  1.00 29.88 ? 104  ILE K CA  1 
ATOM   11927 C  C   . ILE K  1 104 ? 44.079  -11.488 28.558  1.00 30.65 ? 104  ILE K C   1 
ATOM   11928 O  O   . ILE K  1 104 ? 43.184  -12.162 28.041  1.00 30.59 ? 104  ILE K O   1 
ATOM   11929 C  CB  . ILE K  1 104 ? 44.583  -9.160  27.809  1.00 29.05 ? 104  ILE K CB  1 
ATOM   11930 C  CG1 . ILE K  1 104 ? 43.087  -8.998  27.505  1.00 26.01 ? 104  ILE K CG1 1 
ATOM   11931 C  CG2 . ILE K  1 104 ? 45.443  -8.269  26.926  1.00 24.74 ? 104  ILE K CG2 1 
ATOM   11932 C  CD1 . ILE K  1 104 ? 42.609  -7.569  27.598  1.00 22.15 ? 104  ILE K CD1 1 
ATOM   11933 N  N   . SER K  1 105 ? 44.296  -11.447 29.866  1.00 34.75 ? 105  SER K N   1 
ATOM   11934 C  CA  . SER K  1 105 ? 43.427  -12.122 30.820  1.00 33.93 ? 105  SER K CA  1 
ATOM   11935 C  C   . SER K  1 105 ? 43.351  -11.279 32.091  1.00 31.93 ? 105  SER K C   1 
ATOM   11936 O  O   . SER K  1 105 ? 44.149  -10.362 32.285  1.00 29.58 ? 105  SER K O   1 
ATOM   11937 C  CB  . SER K  1 105 ? 43.961  -13.522 31.132  1.00 32.69 ? 105  SER K CB  1 
ATOM   11938 O  OG  . SER K  1 105 ? 43.000  -14.295 31.831  1.00 33.31 ? 105  SER K OG  1 
ATOM   11939 N  N   . LEU K  1 106 ? 42.378  -11.577 32.943  1.00 32.94 ? 106  LEU K N   1 
ATOM   11940 C  CA  . LEU K  1 106 ? 42.264  -10.899 34.228  1.00 34.23 ? 106  LEU K CA  1 
ATOM   11941 C  C   . LEU K  1 106 ? 42.795  -11.791 35.355  1.00 32.60 ? 106  LEU K C   1 
ATOM   11942 O  O   . LEU K  1 106 ? 42.668  -11.463 36.531  1.00 32.56 ? 106  LEU K O   1 
ATOM   11943 C  CB  . LEU K  1 106 ? 40.814  -10.465 34.496  1.00 32.38 ? 106  LEU K CB  1 
ATOM   11944 C  CG  . LEU K  1 106 ? 40.183  -9.446  33.539  1.00 31.28 ? 106  LEU K CG  1 
ATOM   11945 C  CD1 . LEU K  1 106 ? 38.891  -8.918  34.122  1.00 29.83 ? 106  LEU K CD1 1 
ATOM   11946 C  CD2 . LEU K  1 106 ? 41.139  -8.293  33.228  1.00 27.06 ? 106  LEU K CD2 1 
ATOM   11947 N  N   . SER K  1 107 ? 43.389  -12.922 34.975  1.00 34.04 ? 107  SER K N   1 
ATOM   11948 C  CA  . SER K  1 107 ? 44.008  -13.848 35.920  1.00 34.51 ? 107  SER K CA  1 
ATOM   11949 C  C   . SER K  1 107 ? 44.948  -14.795 35.176  1.00 36.70 ? 107  SER K C   1 
ATOM   11950 O  O   . SER K  1 107 ? 44.843  -14.943 33.961  1.00 36.73 ? 107  SER K O   1 
ATOM   11951 C  CB  . SER K  1 107 ? 42.945  -14.647 36.678  1.00 34.97 ? 107  SER K CB  1 
ATOM   11952 O  OG  . SER K  1 107 ? 42.352  -15.629 35.851  1.00 35.58 ? 107  SER K OG  1 
ATOM   11953 N  N   . GLY K  1 108 ? 45.863  -15.434 35.904  1.00 36.66 ? 108  GLY K N   1 
ATOM   11954 C  CA  . GLY K  1 108 ? 46.827  -16.344 35.303  1.00 36.42 ? 108  GLY K CA  1 
ATOM   11955 C  C   . GLY K  1 108 ? 48.190  -15.695 35.135  1.00 40.91 ? 108  GLY K C   1 
ATOM   11956 O  O   . GLY K  1 108 ? 48.475  -14.675 35.764  1.00 39.23 ? 108  GLY K O   1 
ATOM   11957 N  N   . GLU K  1 109 ? 49.043  -16.269 34.288  1.00 44.60 ? 109  GLU K N   1 
ATOM   11958 C  CA  . GLU K  1 109 ? 50.347  -15.655 34.048  1.00 43.46 ? 109  GLU K CA  1 
ATOM   11959 C  C   . GLU K  1 109 ? 50.209  -14.397 33.198  1.00 40.49 ? 109  GLU K C   1 
ATOM   11960 O  O   . GLU K  1 109 ? 51.077  -13.521 33.243  1.00 39.11 ? 109  GLU K O   1 
ATOM   11961 C  CB  . GLU K  1 109 ? 51.343  -16.617 33.389  1.00 45.69 ? 109  GLU K CB  1 
ATOM   11962 C  CG  . GLU K  1 109 ? 51.278  -18.052 33.856  1.00 49.43 ? 109  GLU K CG  1 
ATOM   11963 C  CD  . GLU K  1 109 ? 50.564  -18.939 32.850  1.00 62.04 ? 109  GLU K CD  1 
ATOM   11964 O  OE1 . GLU K  1 109 ? 49.307  -18.930 32.825  1.00 57.67 ? 109  GLU K OE1 1 
ATOM   11965 O  OE2 . GLU K  1 109 ? 51.269  -19.641 32.085  1.00 62.46 ? 109  GLU K OE2 1 
ATOM   11966 N  N   . HIS K  1 110 ? 49.122  -14.312 32.430  1.00 38.72 ? 110  HIS K N   1 
ATOM   11967 C  CA  . HIS K  1 110 ? 48.913  -13.175 31.530  1.00 39.66 ? 110  HIS K CA  1 
ATOM   11968 C  C   . HIS K  1 110 ? 47.877  -12.185 32.036  1.00 35.21 ? 110  HIS K C   1 
ATOM   11969 O  O   . HIS K  1 110 ? 47.332  -11.394 31.265  1.00 33.92 ? 110  HIS K O   1 
ATOM   11970 C  CB  . HIS K  1 110 ? 48.561  -13.637 30.116  1.00 36.72 ? 110  HIS K CB  1 
ATOM   11971 C  CG  . HIS K  1 110 ? 49.580  -14.555 29.522  1.00 38.74 ? 110  HIS K CG  1 
ATOM   11972 N  ND1 . HIS K  1 110 ? 49.271  -15.486 28.554  1.00 42.15 ? 110  HIS K ND1 1 
ATOM   11973 C  CD2 . HIS K  1 110 ? 50.899  -14.708 29.786  1.00 41.08 ? 110  HIS K CD2 1 
ATOM   11974 C  CE1 . HIS K  1 110 ? 50.361  -16.161 28.236  1.00 41.29 ? 110  HIS K CE1 1 
ATOM   11975 N  NE2 . HIS K  1 110 ? 51.362  -15.711 28.970  1.00 39.80 ? 110  HIS K NE2 1 
ATOM   11976 N  N   . SER K  1 111 ? 47.628  -12.227 33.339  1.00 32.77 ? 111  SER K N   1 
ATOM   11977 C  CA  . SER K  1 111 ? 46.744  -11.275 33.983  1.00 32.15 ? 111  SER K CA  1 
ATOM   11978 C  C   . SER K  1 111 ? 47.286  -9.867  33.812  1.00 30.53 ? 111  SER K C   1 
ATOM   11979 O  O   . SER K  1 111 ? 48.481  -9.625  34.007  1.00 30.96 ? 111  SER K O   1 
ATOM   11980 C  CB  . SER K  1 111 ? 46.619  -11.604 35.472  1.00 33.49 ? 111  SER K CB  1 
ATOM   11981 O  OG  . SER K  1 111 ? 45.816  -10.648 36.137  1.00 35.55 ? 111  SER K OG  1 
ATOM   11982 N  N   . ILE K  1 112 ? 46.411  -8.936  33.449  1.00 29.60 ? 112  ILE K N   1 
ATOM   11983 C  CA  . ILE K  1 112 ? 46.819  -7.543  33.308  1.00 30.16 ? 112  ILE K CA  1 
ATOM   11984 C  C   . ILE K  1 112 ? 46.410  -6.696  34.519  1.00 29.37 ? 112  ILE K C   1 
ATOM   11985 O  O   . ILE K  1 112 ? 46.446  -5.464  34.471  1.00 28.16 ? 112  ILE K O   1 
ATOM   11986 C  CB  . ILE K  1 112 ? 46.291  -6.925  31.995  1.00 28.90 ? 112  ILE K CB  1 
ATOM   11987 C  CG1 . ILE K  1 112 ? 44.760  -6.969  31.941  1.00 27.07 ? 112  ILE K CG1 1 
ATOM   11988 C  CG2 . ILE K  1 112 ? 46.906  -7.635  30.783  1.00 29.59 ? 112  ILE K CG2 1 
ATOM   11989 C  CD1 . ILE K  1 112 ? 44.168  -6.135  30.806  1.00 24.94 ? 112  ILE K CD1 1 
ATOM   11990 N  N   . ILE K  1 113 ? 46.024  -7.373  35.601  1.00 31.12 ? 113  ILE K N   1 
ATOM   11991 C  CA  . ILE K  1 113 ? 45.649  -6.717  36.857  1.00 33.08 ? 113  ILE K CA  1 
ATOM   11992 C  C   . ILE K  1 113 ? 46.898  -6.218  37.618  1.00 32.35 ? 113  ILE K C   1 
ATOM   11993 O  O   . ILE K  1 113 ? 47.810  -7.001  37.938  1.00 28.38 ? 113  ILE K O   1 
ATOM   11994 C  CB  . ILE K  1 113 ? 44.800  -7.664  37.761  1.00 33.58 ? 113  ILE K CB  1 
ATOM   11995 C  CG1 . ILE K  1 113 ? 43.611  -8.255  36.983  1.00 31.62 ? 113  ILE K CG1 1 
ATOM   11996 C  CG2 . ILE K  1 113 ? 44.315  -6.936  39.015  1.00 32.31 ? 113  ILE K CG2 1 
ATOM   11997 C  CD1 . ILE K  1 113 ? 42.360  -7.386  36.982  1.00 29.61 ? 113  ILE K CD1 1 
ATOM   11998 N  N   . GLY K  1 114 ? 46.939  -4.912  37.891  1.00 29.63 ? 114  GLY K N   1 
ATOM   11999 C  CA  . GLY K  1 114 ? 48.097  -4.301  38.518  1.00 28.79 ? 114  GLY K CA  1 
ATOM   12000 C  C   . GLY K  1 114 ? 49.080  -3.760  37.499  1.00 28.46 ? 114  GLY K C   1 
ATOM   12001 O  O   . GLY K  1 114 ? 50.175  -3.332  37.842  1.00 31.39 ? 114  GLY K O   1 
ATOM   12002 N  N   . ARG K  1 115 ? 48.687  -3.787  36.231  1.00 31.80 ? 115  ARG K N   1 
ATOM   12003 C  CA  . ARG K  1 115 ? 49.525  -3.298  35.138  1.00 27.52 ? 115  ARG K CA  1 
ATOM   12004 C  C   . ARG K  1 115 ? 48.938  -1.999  34.613  1.00 27.09 ? 115  ARG K C   1 
ATOM   12005 O  O   . ARG K  1 115 ? 48.020  -1.465  35.211  1.00 30.36 ? 115  ARG K O   1 
ATOM   12006 C  CB  . ARG K  1 115 ? 49.654  -4.361  34.051  1.00 27.96 ? 115  ARG K CB  1 
ATOM   12007 C  CG  . ARG K  1 115 ? 50.108  -5.707  34.619  1.00 26.86 ? 115  ARG K CG  1 
ATOM   12008 C  CD  . ARG K  1 115 ? 50.726  -6.571  33.558  1.00 28.14 ? 115  ARG K CD  1 
ATOM   12009 N  NE  . ARG K  1 115 ? 51.192  -7.850  34.081  1.00 26.92 ? 115  ARG K NE  1 
ATOM   12010 C  CZ  . ARG K  1 115 ? 52.430  -8.067  34.506  1.00 27.40 ? 115  ARG K CZ  1 
ATOM   12011 N  NH1 . ARG K  1 115 ? 53.314  -7.080  34.480  1.00 25.92 ? 115  ARG K NH1 1 
ATOM   12012 N  NH2 . ARG K  1 115 ? 52.781  -9.268  34.950  1.00 24.93 ? 115  ARG K NH2 1 
ATOM   12013 N  N   . THR K  1 116 ? 49.458  -1.470  33.518  1.00 27.91 ? 116  THR K N   1 
ATOM   12014 C  CA  . THR K  1 116 ? 49.041  -0.135  33.095  1.00 29.44 ? 116  THR K CA  1 
ATOM   12015 C  C   . THR K  1 116 ? 48.422  -0.093  31.688  1.00 29.79 ? 116  THR K C   1 
ATOM   12016 O  O   . THR K  1 116 ? 48.975  -0.640  30.747  1.00 30.80 ? 116  THR K O   1 
ATOM   12017 C  CB  . THR K  1 116 ? 50.225  0.864   33.206  1.00 28.46 ? 116  THR K CB  1 
ATOM   12018 O  OG1 . THR K  1 116 ? 50.626  0.969   34.574  1.00 31.82 ? 116  THR K OG1 1 
ATOM   12019 C  CG2 . THR K  1 116 ? 49.849  2.246   32.703  1.00 29.00 ? 116  THR K CG2 1 
ATOM   12020 N  N   . MET K  1 117 ? 47.260  0.539   31.558  1.00 28.74 ? 117  MET K N   1 
ATOM   12021 C  CA  . MET K  1 117 ? 46.721  0.861   30.241  1.00 33.52 ? 117  MET K CA  1 
ATOM   12022 C  C   . MET K  1 117 ? 47.263  2.226   29.865  1.00 33.66 ? 117  MET K C   1 
ATOM   12023 O  O   . MET K  1 117 ? 47.280  3.137   30.703  1.00 31.10 ? 117  MET K O   1 
ATOM   12024 C  CB  . MET K  1 117 ? 45.179  0.938   30.241  1.00 34.20 ? 117  MET K CB  1 
ATOM   12025 C  CG  . MET K  1 117 ? 44.433  -0.396  30.265  1.00 35.69 ? 117  MET K CG  1 
ATOM   12026 S  SD  . MET K  1 117 ? 44.704  -1.426  28.803  1.00 38.09 ? 117  MET K SD  1 
ATOM   12027 C  CE  . MET K  1 117 ? 44.875  -0.166  27.545  1.00 31.65 ? 117  MET K CE  1 
ATOM   12028 N  N   . VAL K  1 118 ? 47.708  2.372   28.619  1.00 32.23 ? 118  VAL K N   1 
ATOM   12029 C  CA  . VAL K  1 118 ? 48.041  3.693   28.102  1.00 30.96 ? 118  VAL K CA  1 
ATOM   12030 C  C   . VAL K  1 118 ? 47.528  3.905   26.672  1.00 30.27 ? 118  VAL K C   1 
ATOM   12031 O  O   . VAL K  1 118 ? 47.410  2.964   25.890  1.00 30.15 ? 118  VAL K O   1 
ATOM   12032 C  CB  . VAL K  1 118 ? 49.553  4.071   28.317  1.00 29.65 ? 118  VAL K CB  1 
ATOM   12033 C  CG1 . VAL K  1 118 ? 50.383  2.859   28.629  1.00 25.91 ? 118  VAL K CG1 1 
ATOM   12034 C  CG2 . VAL K  1 118 ? 50.105  4.858   27.150  1.00 30.12 ? 118  VAL K CG2 1 
ATOM   12035 N  N   . VAL K  1 119 ? 47.150  5.143   26.375  1.00 30.74 ? 119  VAL K N   1 
ATOM   12036 C  CA  . VAL K  1 119 ? 46.724  5.539   25.044  1.00 27.42 ? 119  VAL K CA  1 
ATOM   12037 C  C   . VAL K  1 119 ? 47.831  6.441   24.521  1.00 30.64 ? 119  VAL K C   1 
ATOM   12038 O  O   . VAL K  1 119 ? 48.360  7.277   25.259  1.00 30.01 ? 119  VAL K O   1 
ATOM   12039 C  CB  . VAL K  1 119 ? 45.360  6.278   25.067  1.00 28.86 ? 119  VAL K CB  1 
ATOM   12040 C  CG1 . VAL K  1 119 ? 45.414  7.492   25.978  1.00 27.42 ? 119  VAL K CG1 1 
ATOM   12041 C  CG2 . VAL K  1 119 ? 44.922  6.673   23.653  1.00 25.27 ? 119  VAL K CG2 1 
ATOM   12042 N  N   . HIS K  1 120 ? 48.199  6.258   23.257  1.00 31.67 ? 120  HIS K N   1 
ATOM   12043 C  CA  . HIS K  1 120 ? 49.407  6.883   22.726  1.00 31.24 ? 120  HIS K CA  1 
ATOM   12044 C  C   . HIS K  1 120 ? 49.121  8.010   21.730  1.00 30.85 ? 120  HIS K C   1 
ATOM   12045 O  O   . HIS K  1 120 ? 48.061  8.060   21.099  1.00 30.91 ? 120  HIS K O   1 
ATOM   12046 C  CB  . HIS K  1 120 ? 50.333  5.826   22.108  1.00 29.67 ? 120  HIS K CB  1 
ATOM   12047 C  CG  . HIS K  1 120 ? 50.946  4.884   23.105  1.00 27.93 ? 120  HIS K CG  1 
ATOM   12048 N  ND1 . HIS K  1 120 ? 52.243  5.017   23.553  1.00 25.16 ? 120  HIS K ND1 1 
ATOM   12049 C  CD2 . HIS K  1 120 ? 50.453  3.776   23.712  1.00 27.08 ? 120  HIS K CD2 1 
ATOM   12050 C  CE1 . HIS K  1 120 ? 52.516  4.043   24.402  1.00 27.43 ? 120  HIS K CE1 1 
ATOM   12051 N  NE2 . HIS K  1 120 ? 51.448  3.275   24.518  1.00 25.56 ? 120  HIS K NE2 1 
ATOM   12052 N  N   . GLU K  1 121 ? 50.083  8.917   21.615  1.00 30.28 ? 121  GLU K N   1 
ATOM   12053 C  CA  . GLU K  1 121 ? 49.965  10.092  20.765  1.00 32.83 ? 121  GLU K CA  1 
ATOM   12054 C  C   . GLU K  1 121 ? 49.577  9.746   19.338  1.00 34.63 ? 121  GLU K C   1 
ATOM   12055 O  O   . GLU K  1 121 ? 48.788  10.452  18.714  1.00 34.20 ? 121  GLU K O   1 
ATOM   12056 C  CB  . GLU K  1 121 ? 51.300  10.837  20.763  1.00 35.91 ? 121  GLU K CB  1 
ATOM   12057 C  CG  . GLU K  1 121 ? 51.549  11.752  19.578  1.00 36.52 ? 121  GLU K CG  1 
ATOM   12058 C  CD  . GLU K  1 121 ? 52.999  12.235  19.521  1.00 40.59 ? 121  GLU K CD  1 
ATOM   12059 O  OE1 . GLU K  1 121 ? 53.907  11.499  19.982  1.00 39.61 ? 121  GLU K OE1 1 
ATOM   12060 O  OE2 . GLU K  1 121 ? 53.229  13.354  19.017  1.00 42.42 ? 121  GLU K OE2 1 
ATOM   12061 N  N   . LYS K  1 122 ? 50.135  8.651   18.833  1.00 33.10 ? 122  LYS K N   1 
ATOM   12062 C  CA  . LYS K  1 122 ? 50.056  8.328   17.416  1.00 32.06 ? 122  LYS K CA  1 
ATOM   12063 C  C   . LYS K  1 122 ? 49.441  6.953   17.128  1.00 29.67 ? 122  LYS K C   1 
ATOM   12064 O  O   . LYS K  1 122 ? 49.476  6.046   17.956  1.00 29.36 ? 122  LYS K O   1 
ATOM   12065 C  CB  . LYS K  1 122 ? 51.462  8.379   16.797  1.00 33.41 ? 122  LYS K CB  1 
ATOM   12066 C  CG  . LYS K  1 122 ? 52.273  9.640   17.102  1.00 36.68 ? 122  LYS K CG  1 
ATOM   12067 C  CD  . LYS K  1 122 ? 53.686  9.580   16.505  1.00 36.62 ? 122  LYS K CD  1 
ATOM   12068 C  CE  . LYS K  1 122 ? 53.643  9.592   14.981  1.00 42.80 ? 122  LYS K CE  1 
ATOM   12069 N  NZ  . LYS K  1 122 ? 52.953  10.807  14.430  1.00 46.01 ? 122  LYS K NZ  1 
ATOM   12070 N  N   . GLN K  1 123 ? 48.901  6.811   15.924  1.00 29.69 ? 123  GLN K N   1 
ATOM   12071 C  CA  . GLN K  1 123 ? 48.440  5.527   15.413  1.00 29.68 ? 123  GLN K CA  1 
ATOM   12072 C  C   . GLN K  1 123 ? 49.501  4.427   15.538  1.00 28.84 ? 123  GLN K C   1 
ATOM   12073 O  O   . GLN K  1 123 ? 50.582  4.546   14.964  1.00 32.15 ? 123  GLN K O   1 
ATOM   12074 C  CB  . GLN K  1 123 ? 48.037  5.675   13.936  1.00 28.33 ? 123  GLN K CB  1 
ATOM   12075 C  CG  . GLN K  1 123 ? 47.887  4.349   13.196  1.00 30.28 ? 123  GLN K CG  1 
ATOM   12076 C  CD  . GLN K  1 123 ? 47.087  4.460   11.897  1.00 30.12 ? 123  GLN K CD  1 
ATOM   12077 O  OE1 . GLN K  1 123 ? 46.680  5.546   11.489  1.00 29.62 ? 123  GLN K OE1 1 
ATOM   12078 N  NE2 . GLN K  1 123 ? 46.862  3.326   11.248  1.00 29.55 ? 123  GLN K NE2 1 
ATOM   12079 N  N   . ASP K  1 124 ? 49.192  3.367   16.284  1.00 23.78 ? 124  ASP K N   1 
ATOM   12080 C  CA  . ASP K  1 124 ? 49.974  2.133   16.248  1.00 22.61 ? 124  ASP K CA  1 
ATOM   12081 C  C   . ASP K  1 124 ? 49.995  1.555   14.807  1.00 26.92 ? 124  ASP K C   1 
ATOM   12082 O  O   . ASP K  1 124 ? 48.945  1.368   14.175  1.00 26.97 ? 124  ASP K O   1 
ATOM   12083 C  CB  . ASP K  1 124 ? 49.379  1.128   17.231  1.00 23.02 ? 124  ASP K CB  1 
ATOM   12084 C  CG  . ASP K  1 124 ? 50.179  -0.154  17.333  1.00 23.07 ? 124  ASP K CG  1 
ATOM   12085 O  OD1 . ASP K  1 124 ? 51.055  -0.390  16.501  1.00 24.43 ? 124  ASP K OD1 1 
ATOM   12086 O  OD2 . ASP K  1 124 ? 49.932  -0.946  18.257  1.00 25.87 ? 124  ASP K OD2 1 
ATOM   12087 N  N   . ASP K  1 125 ? 51.195  1.295   14.288  1.00 26.38 ? 125  ASP K N   1 
ATOM   12088 C  CA  . ASP K  1 125 ? 51.373  0.785   12.929  1.00 24.71 ? 125  ASP K CA  1 
ATOM   12089 C  C   . ASP K  1 125 ? 51.355  -0.743  12.871  1.00 23.91 ? 125  ASP K C   1 
ATOM   12090 O  O   . ASP K  1 125 ? 51.493  -1.329  11.805  1.00 27.37 ? 125  ASP K O   1 
ATOM   12091 C  CB  . ASP K  1 125 ? 52.653  1.358   12.277  1.00 25.74 ? 125  ASP K CB  1 
ATOM   12092 C  CG  . ASP K  1 125 ? 53.956  0.781   12.867  1.00 24.25 ? 125  ASP K CG  1 
ATOM   12093 O  OD1 . ASP K  1 125 ? 53.925  -0.271  13.540  1.00 22.24 ? 125  ASP K OD1 1 
ATOM   12094 O  OD2 . ASP K  1 125 ? 55.032  1.378   12.627  1.00 23.31 ? 125  ASP K OD2 1 
ATOM   12095 N  N   . LEU K  1 126 ? 51.178  -1.370  14.026  1.00 23.80 ? 126  LEU K N   1 
ATOM   12096 C  CA  . LEU K  1 126 ? 51.023  -2.822  14.154  1.00 23.19 ? 126  LEU K CA  1 
ATOM   12097 C  C   . LEU K  1 126 ? 52.217  -3.635  13.647  1.00 23.96 ? 126  LEU K C   1 
ATOM   12098 O  O   . LEU K  1 126 ? 52.065  -4.794  13.273  1.00 25.73 ? 126  LEU K O   1 
ATOM   12099 C  CB  . LEU K  1 126 ? 49.709  -3.309  13.513  1.00 24.29 ? 126  LEU K CB  1 
ATOM   12100 C  CG  . LEU K  1 126 ? 48.416  -2.498  13.699  1.00 24.44 ? 126  LEU K CG  1 
ATOM   12101 C  CD1 . LEU K  1 126 ? 47.268  -3.084  12.860  1.00 24.30 ? 126  LEU K CD1 1 
ATOM   12102 C  CD2 . LEU K  1 126 ? 48.000  -2.349  15.153  1.00 22.05 ? 126  LEU K CD2 1 
ATOM   12103 N  N   . GLY K  1 127 ? 53.401  -3.029  13.649  1.00 25.26 ? 127  GLY K N   1 
ATOM   12104 C  CA  . GLY K  1 127 ? 54.628  -3.715  13.255  1.00 25.15 ? 127  GLY K CA  1 
ATOM   12105 C  C   . GLY K  1 127 ? 54.983  -3.637  11.780  1.00 24.66 ? 127  GLY K C   1 
ATOM   12106 O  O   . GLY K  1 127 ? 55.763  -4.444  11.279  1.00 26.57 ? 127  GLY K O   1 
ATOM   12107 N  N   . LYS K  1 128 ? 54.411  -2.649  11.096  1.00 24.18 ? 128  LYS K N   1 
ATOM   12108 C  CA  . LYS K  1 128 ? 54.494  -2.521  9.646   1.00 23.64 ? 128  LYS K CA  1 
ATOM   12109 C  C   . LYS K  1 128 ? 55.164  -1.219  9.216   1.00 21.46 ? 128  LYS K C   1 
ATOM   12110 O  O   . LYS K  1 128 ? 55.101  -0.831  8.047   1.00 23.19 ? 128  LYS K O   1 
ATOM   12111 C  CB  . LYS K  1 128 ? 53.082  -2.584  9.042   1.00 25.44 ? 128  LYS K CB  1 
ATOM   12112 C  CG  . LYS K  1 128 ? 52.278  -3.776  9.525   1.00 25.01 ? 128  LYS K CG  1 
ATOM   12113 C  CD  . LYS K  1 128 ? 51.031  -3.994  8.730   1.00 30.59 ? 128  LYS K CD  1 
ATOM   12114 C  CE  . LYS K  1 128 ? 50.035  -4.800  9.570   1.00 43.82 ? 128  LYS K CE  1 
ATOM   12115 N  NZ  . LYS K  1 128 ? 50.705  -5.845  10.427  1.00 42.86 ? 128  LYS K NZ  1 
ATOM   12116 N  N   . GLY K  1 129 ? 55.797  -0.538  10.162  1.00 23.41 ? 129  GLY K N   1 
ATOM   12117 C  CA  . GLY K  1 129 ? 56.441  0.736   9.882   1.00 22.90 ? 129  GLY K CA  1 
ATOM   12118 C  C   . GLY K  1 129 ? 57.853  0.612   9.347   1.00 21.99 ? 129  GLY K C   1 
ATOM   12119 O  O   . GLY K  1 129 ? 58.443  1.608   8.907   1.00 23.22 ? 129  GLY K O   1 
ATOM   12120 N  N   . GLY K  1 130 ? 58.396  -0.606  9.407   1.00 20.58 ? 130  GLY K N   1 
ATOM   12121 C  CA  . GLY K  1 130 ? 59.634  -0.951  8.732   1.00 22.67 ? 130  GLY K CA  1 
ATOM   12122 C  C   . GLY K  1 130 ? 60.920  -0.609  9.455   1.00 22.65 ? 130  GLY K C   1 
ATOM   12123 O  O   . GLY K  1 130 ? 61.932  -0.335  8.829   1.00 25.67 ? 130  GLY K O   1 
ATOM   12124 N  N   . ASN K  1 131 ? 60.880  -0.620  10.777  1.00 24.96 ? 131  ASN K N   1 
ATOM   12125 C  CA  . ASN K  1 131 ? 62.062  -0.381  11.593  1.00 23.58 ? 131  ASN K CA  1 
ATOM   12126 C  C   . ASN K  1 131 ? 61.930  -1.093  12.929  1.00 25.83 ? 131  ASN K C   1 
ATOM   12127 O  O   . ASN K  1 131 ? 60.917  -1.758  13.182  1.00 26.19 ? 131  ASN K O   1 
ATOM   12128 C  CB  . ASN K  1 131 ? 62.339  1.120   11.776  1.00 24.50 ? 131  ASN K CB  1 
ATOM   12129 C  CG  . ASN K  1 131 ? 61.120  1.918   12.238  1.00 24.14 ? 131  ASN K CG  1 
ATOM   12130 O  OD1 . ASN K  1 131 ? 60.205  1.399   12.891  1.00 23.82 ? 131  ASN K OD1 1 
ATOM   12131 N  ND2 . ASN K  1 131 ? 61.121  3.207   11.915  1.00 22.51 ? 131  ASN K ND2 1 
ATOM   12132 N  N   . GLU K  1 132 ? 62.948  -0.981  13.777  1.00 26.69 ? 132  GLU K N   1 
ATOM   12133 C  CA  . GLU K  1 132 ? 62.894  -1.629  15.091  1.00 30.08 ? 132  GLU K CA  1 
ATOM   12134 C  C   . GLU K  1 132 ? 61.861  -1.010  16.043  1.00 26.47 ? 132  GLU K C   1 
ATOM   12135 O  O   . GLU K  1 132 ? 61.283  -1.705  16.876  1.00 28.67 ? 132  GLU K O   1 
ATOM   12136 C  CB  . GLU K  1 132 ? 64.271  -1.661  15.743  1.00 36.00 ? 132  GLU K CB  1 
ATOM   12137 C  CG  . GLU K  1 132 ? 65.100  -2.862  15.355  1.00 37.12 ? 132  GLU K CG  1 
ATOM   12138 C  CD  . GLU K  1 132 ? 66.552  -2.678  15.737  1.00 49.21 ? 132  GLU K CD  1 
ATOM   12139 O  OE1 . GLU K  1 132 ? 66.998  -1.505  15.818  1.00 49.17 ? 132  GLU K OE1 1 
ATOM   12140 O  OE2 . GLU K  1 132 ? 67.245  -3.700  15.950  1.00 53.79 ? 132  GLU K OE2 1 
ATOM   12141 N  N   . GLU K  1 133 ? 61.647  0.294   15.924  1.00 26.22 ? 133  GLU K N   1 
ATOM   12142 C  CA  . GLU K  1 133 ? 60.568  0.971   16.629  1.00 27.13 ? 133  GLU K CA  1 
ATOM   12143 C  C   . GLU K  1 133 ? 59.228  0.280   16.420  1.00 26.34 ? 133  GLU K C   1 
ATOM   12144 O  O   . GLU K  1 133 ? 58.477  0.067   17.365  1.00 27.66 ? 133  GLU K O   1 
ATOM   12145 C  CB  . GLU K  1 133 ? 60.457  2.410   16.143  1.00 29.43 ? 133  GLU K CB  1 
ATOM   12146 C  CG  . GLU K  1 133 ? 61.240  3.363   16.964  1.00 35.42 ? 133  GLU K CG  1 
ATOM   12147 C  CD  . GLU K  1 133 ? 60.754  3.359   18.386  1.00 38.15 ? 133  GLU K CD  1 
ATOM   12148 O  OE1 . GLU K  1 133 ? 59.533  3.153   18.557  1.00 37.35 ? 133  GLU K OE1 1 
ATOM   12149 O  OE2 . GLU K  1 133 ? 61.578  3.548   19.316  1.00 39.99 ? 133  GLU K OE2 1 
ATOM   12150 N  N   . SER K  1 134 ? 58.934  -0.052  15.169  1.00 26.12 ? 134  SER K N   1 
ATOM   12151 C  CA  . SER K  1 134 ? 57.682  -0.701  14.812  1.00 23.48 ? 134  SER K CA  1 
ATOM   12152 C  C   . SER K  1 134 ? 57.486  -2.036  15.548  1.00 24.64 ? 134  SER K C   1 
ATOM   12153 O  O   . SER K  1 134 ? 56.385  -2.351  16.007  1.00 23.74 ? 134  SER K O   1 
ATOM   12154 C  CB  . SER K  1 134 ? 57.609  -0.896  13.296  1.00 21.56 ? 134  SER K CB  1 
ATOM   12155 O  OG  . SER K  1 134 ? 56.282  -1.182  12.887  1.00 22.97 ? 134  SER K OG  1 
ATOM   12156 N  N   . THR K  1 135 ? 58.561  -2.811  15.661  1.00 26.71 ? 135  THR K N   1 
ATOM   12157 C  CA  . THR K  1 135 ? 58.510  -4.141  16.255  1.00 24.34 ? 135  THR K CA  1 
ATOM   12158 C  C   . THR K  1 135 ? 58.564  -4.043  17.765  1.00 27.42 ? 135  THR K C   1 
ATOM   12159 O  O   . THR K  1 135 ? 58.659  -5.058  18.468  1.00 28.73 ? 135  THR K O   1 
ATOM   12160 C  CB  . THR K  1 135 ? 59.711  -4.982  15.815  1.00 26.21 ? 135  THR K CB  1 
ATOM   12161 O  OG1 . THR K  1 135 ? 60.895  -4.463  16.434  1.00 27.39 ? 135  THR K OG1 1 
ATOM   12162 C  CG2 . THR K  1 135 ? 59.867  -4.945  14.300  1.00 23.91 ? 135  THR K CG2 1 
ATOM   12163 N  N   . LYS K  1 136 ? 58.496  -2.813  18.263  1.00 26.85 ? 136  LYS K N   1 
ATOM   12164 C  CA  . LYS K  1 136 ? 58.638  -2.561  19.686  1.00 29.84 ? 136  LYS K CA  1 
ATOM   12165 C  C   . LYS K  1 136 ? 57.437  -1.816  20.278  1.00 25.66 ? 136  LYS K C   1 
ATOM   12166 O  O   . LYS K  1 136 ? 56.831  -2.264  21.245  1.00 27.86 ? 136  LYS K O   1 
ATOM   12167 C  CB  . LYS K  1 136 ? 59.920  -1.756  19.937  1.00 33.05 ? 136  LYS K CB  1 
ATOM   12168 C  CG  . LYS K  1 136 ? 60.662  -2.155  21.196  1.00 37.92 ? 136  LYS K CG  1 
ATOM   12169 C  CD  . LYS K  1 136 ? 61.796  -3.123  20.875  1.00 42.68 ? 136  LYS K CD  1 
ATOM   12170 C  CE  . LYS K  1 136 ? 63.025  -2.351  20.437  1.00 44.71 ? 136  LYS K CE  1 
ATOM   12171 N  NZ  . LYS K  1 136 ? 63.231  -1.153  21.320  1.00 49.99 ? 136  LYS K NZ  1 
ATOM   12172 N  N   . THR K  1 137 ? 57.124  -0.665  19.697  1.00 25.10 ? 137  THR K N   1 
ATOM   12173 C  CA  . THR K  1 137 ? 56.068  0.206   20.190  1.00 25.90 ? 137  THR K CA  1 
ATOM   12174 C  C   . THR K  1 137 ? 54.974  0.455   19.117  1.00 28.44 ? 137  THR K C   1 
ATOM   12175 O  O   . THR K  1 137 ? 53.900  0.991   19.418  1.00 26.04 ? 137  THR K O   1 
ATOM   12176 C  CB  . THR K  1 137 ? 56.662  1.553   20.684  1.00 24.91 ? 137  THR K CB  1 
ATOM   12177 O  OG1 . THR K  1 137 ? 57.205  2.282   19.579  1.00 24.41 ? 137  THR K OG1 1 
ATOM   12178 C  CG2 . THR K  1 137 ? 57.774  1.309   21.684  1.00 26.02 ? 137  THR K CG2 1 
ATOM   12179 N  N   . GLY K  1 138 ? 55.257  0.052   17.877  1.00 25.46 ? 138  GLY K N   1 
ATOM   12180 C  CA  . GLY K  1 138 ? 54.372  0.300   16.760  1.00 21.45 ? 138  GLY K CA  1 
ATOM   12181 C  C   . GLY K  1 138 ? 54.465  1.734   16.296  1.00 22.62 ? 138  GLY K C   1 
ATOM   12182 O  O   . GLY K  1 138 ? 53.631  2.193   15.540  1.00 24.63 ? 138  GLY K O   1 
ATOM   12183 N  N   . ASN K  1 139 ? 55.488  2.446   16.746  1.00 25.23 ? 139  ASN K N   1 
ATOM   12184 C  CA  . ASN K  1 139 ? 55.683  3.848   16.368  1.00 26.40 ? 139  ASN K CA  1 
ATOM   12185 C  C   . ASN K  1 139 ? 54.514  4.724   16.829  1.00 27.50 ? 139  ASN K C   1 
ATOM   12186 O  O   . ASN K  1 139 ? 54.184  5.728   16.187  1.00 26.18 ? 139  ASN K O   1 
ATOM   12187 C  CB  . ASN K  1 139 ? 55.907  3.990   14.849  1.00 27.52 ? 139  ASN K CB  1 
ATOM   12188 C  CG  . ASN K  1 139 ? 57.365  3.751   14.430  1.00 25.02 ? 139  ASN K CG  1 
ATOM   12189 O  OD1 . ASN K  1 139 ? 58.277  4.387   14.941  1.00 31.00 ? 139  ASN K OD1 1 
ATOM   12190 N  ND2 . ASN K  1 139 ? 57.575  2.847   13.481  1.00 25.68 ? 139  ASN K ND2 1 
ATOM   12191 N  N   . ALA K  1 140 ? 53.899  4.330   17.947  1.00 28.61 ? 140  ALA K N   1 
ATOM   12192 C  CA  . ALA K  1 140 ? 52.689  4.982   18.465  1.00 30.13 ? 140  ALA K CA  1 
ATOM   12193 C  C   . ALA K  1 140 ? 52.982  6.286   19.211  1.00 33.56 ? 140  ALA K C   1 
ATOM   12194 O  O   . ALA K  1 140 ? 52.066  6.978   19.656  1.00 34.74 ? 140  ALA K O   1 
ATOM   12195 C  CB  . ALA K  1 140 ? 51.892  4.023   19.358  1.00 25.90 ? 140  ALA K CB  1 
ATOM   12196 N  N   . GLY K  1 141 ? 54.260  6.619   19.347  1.00 33.64 ? 141  GLY K N   1 
ATOM   12197 C  CA  . GLY K  1 141 ? 54.647  7.907   19.882  1.00 32.71 ? 141  GLY K CA  1 
ATOM   12198 C  C   . GLY K  1 141 ? 54.490  8.008   21.380  1.00 35.49 ? 141  GLY K C   1 
ATOM   12199 O  O   . GLY K  1 141 ? 54.627  7.015   22.102  1.00 34.74 ? 141  GLY K O   1 
ATOM   12200 N  N   . SER K  1 142 ? 54.189  9.214   21.849  1.00 34.49 ? 142  SER K N   1 
ATOM   12201 C  CA  . SER K  1 142 ? 54.181  9.498   23.282  1.00 36.12 ? 142  SER K CA  1 
ATOM   12202 C  C   . SER K  1 142 ? 52.986  8.897   24.016  1.00 34.82 ? 142  SER K C   1 
ATOM   12203 O  O   . SER K  1 142 ? 51.950  8.631   23.412  1.00 33.22 ? 142  SER K O   1 
ATOM   12204 C  CB  . SER K  1 142 ? 54.235  11.009  23.527  1.00 39.08 ? 142  SER K CB  1 
ATOM   12205 O  OG  . SER K  1 142 ? 53.100  11.667  22.989  1.00 38.37 ? 142  SER K OG  1 
ATOM   12206 N  N   . ARG K  1 143 ? 53.149  8.690   25.326  1.00 37.06 ? 143  ARG K N   1 
ATOM   12207 C  CA  . ARG K  1 143 ? 52.072  8.207   26.190  1.00 34.39 ? 143  ARG K CA  1 
ATOM   12208 C  C   . ARG K  1 143 ? 51.239  9.394   26.681  1.00 34.81 ? 143  ARG K C   1 
ATOM   12209 O  O   . ARG K  1 143 ? 51.712  10.199  27.478  1.00 36.80 ? 143  ARG K O   1 
ATOM   12210 C  CB  . ARG K  1 143 ? 52.650  7.425   27.370  1.00 35.43 ? 143  ARG K CB  1 
ATOM   12211 C  CG  . ARG K  1 143 ? 53.768  6.487   26.969  1.00 30.69 ? 143  ARG K CG  1 
ATOM   12212 C  CD  . ARG K  1 143 ? 54.375  5.735   28.143  1.00 31.86 ? 143  ARG K CD  1 
ATOM   12213 N  NE  . ARG K  1 143 ? 55.442  4.858   27.666  1.00 33.78 ? 143  ARG K NE  1 
ATOM   12214 C  CZ  . ARG K  1 143 ? 55.932  3.806   28.320  1.00 31.69 ? 143  ARG K CZ  1 
ATOM   12215 N  NH1 . ARG K  1 143 ? 55.458  3.461   29.503  1.00 32.95 ? 143  ARG K NH1 1 
ATOM   12216 N  NH2 . ARG K  1 143 ? 56.900  3.083   27.774  1.00 32.23 ? 143  ARG K NH2 1 
ATOM   12217 N  N   . LEU K  1 144 ? 50.006  9.497   26.189  1.00 33.31 ? 144  LEU K N   1 
ATOM   12218 C  CA  . LEU K  1 144 ? 49.149  10.650  26.443  1.00 32.26 ? 144  LEU K CA  1 
ATOM   12219 C  C   . LEU K  1 144 ? 48.446  10.589  27.792  1.00 34.26 ? 144  LEU K C   1 
ATOM   12220 O  O   . LEU K  1 144 ? 48.225  11.618  28.436  1.00 33.67 ? 144  LEU K O   1 
ATOM   12221 C  CB  . LEU K  1 144 ? 48.082  10.758  25.362  1.00 34.02 ? 144  LEU K CB  1 
ATOM   12222 C  CG  . LEU K  1 144 ? 48.479  11.092  23.930  1.00 32.42 ? 144  LEU K CG  1 
ATOM   12223 C  CD1 . LEU K  1 144 ? 47.203  11.301  23.133  1.00 33.02 ? 144  LEU K CD1 1 
ATOM   12224 C  CD2 . LEU K  1 144 ? 49.369  12.321  23.880  1.00 31.78 ? 144  LEU K CD2 1 
ATOM   12225 N  N   . ALA K  1 145 ? 48.073  9.382   28.198  1.00 29.84 ? 145  ALA K N   1 
ATOM   12226 C  CA  . ALA K  1 145 ? 47.384  9.174   29.461  1.00 32.70 ? 145  ALA K CA  1 
ATOM   12227 C  C   . ALA K  1 145 ? 47.494  7.713   29.843  1.00 29.30 ? 145  ALA K C   1 
ATOM   12228 O  O   . ALA K  1 145 ? 47.621  6.855   28.983  1.00 29.90 ? 145  ALA K O   1 
ATOM   12229 C  CB  . ALA K  1 145 ? 45.908  9.595   29.355  1.00 35.05 ? 145  ALA K CB  1 
ATOM   12230 N  N   . CYS K  1 146 ? 47.451  7.432   31.137  1.00 28.35 ? 146  CYS K N   1 
ATOM   12231 C  CA  . CYS K  1 146 ? 47.566  6.064   31.606  1.00 29.93 ? 146  CYS K CA  1 
ATOM   12232 C  C   . CYS K  1 146 ? 46.944  5.901   32.988  1.00 30.68 ? 146  CYS K C   1 
ATOM   12233 O  O   . CYS K  1 146 ? 46.509  6.874   33.606  1.00 30.01 ? 146  CYS K O   1 
ATOM   12234 C  CB  . CYS K  1 146 ? 49.031  5.630   31.636  1.00 33.14 ? 146  CYS K CB  1 
ATOM   12235 S  SG  . CYS K  1 146 ? 49.998  6.327   33.000  1.00 38.58 ? 146  CYS K SG  1 
ATOM   12236 N  N   . GLY K  1 147 ? 46.904  4.659   33.456  1.00 28.87 ? 147  GLY K N   1 
ATOM   12237 C  CA  . GLY K  1 147 ? 46.326  4.338   34.740  1.00 29.11 ? 147  GLY K CA  1 
ATOM   12238 C  C   . GLY K  1 147 ? 46.543  2.876   35.045  1.00 28.73 ? 147  GLY K C   1 
ATOM   12239 O  O   . GLY K  1 147 ? 46.698  2.076   34.134  1.00 27.73 ? 147  GLY K O   1 
ATOM   12240 N  N   . VAL K  1 148 ? 46.571  2.531   36.331  1.00 31.17 ? 148  VAL K N   1 
ATOM   12241 C  CA  . VAL K  1 148 ? 46.786  1.154   36.747  1.00 27.74 ? 148  VAL K CA  1 
ATOM   12242 C  C   . VAL K  1 148 ? 45.453  0.428   36.688  1.00 29.23 ? 148  VAL K C   1 
ATOM   12243 O  O   . VAL K  1 148 ? 44.399  1.036   36.877  1.00 30.45 ? 148  VAL K O   1 
ATOM   12244 C  CB  . VAL K  1 148 ? 47.422  1.080   38.154  1.00 25.68 ? 148  VAL K CB  1 
ATOM   12245 C  CG1 . VAL K  1 148 ? 47.756  -0.361  38.525  1.00 23.91 ? 148  VAL K CG1 1 
ATOM   12246 C  CG2 . VAL K  1 148 ? 48.670  1.938   38.190  1.00 24.93 ? 148  VAL K CG2 1 
ATOM   12247 N  N   . ILE K  1 149 ? 45.500  -0.865  36.392  1.00 29.59 ? 149  ILE K N   1 
ATOM   12248 C  CA  . ILE K  1 149 ? 44.289  -1.663  36.219  1.00 29.25 ? 149  ILE K CA  1 
ATOM   12249 C  C   . ILE K  1 149 ? 43.987  -2.380  37.521  1.00 28.77 ? 149  ILE K C   1 
ATOM   12250 O  O   . ILE K  1 149 ? 44.775  -3.219  37.965  1.00 29.46 ? 149  ILE K O   1 
ATOM   12251 C  CB  . ILE K  1 149 ? 44.449  -2.706  35.071  1.00 29.77 ? 149  ILE K CB  1 
ATOM   12252 C  CG1 . ILE K  1 149 ? 44.824  -2.016  33.760  1.00 27.77 ? 149  ILE K CG1 1 
ATOM   12253 C  CG2 . ILE K  1 149 ? 43.170  -3.517  34.882  1.00 29.63 ? 149  ILE K CG2 1 
ATOM   12254 C  CD1 . ILE K  1 149 ? 45.396  -2.958  32.749  1.00 28.66 ? 149  ILE K CD1 1 
ATOM   12255 N  N   . GLY K  1 150 ? 42.851  -2.048  38.134  1.00 28.60 ? 150  GLY K N   1 
ATOM   12256 C  CA  . GLY K  1 150 ? 42.479  -2.644  39.404  1.00 25.37 ? 150  GLY K CA  1 
ATOM   12257 C  C   . GLY K  1 150 ? 41.150  -3.368  39.410  1.00 26.31 ? 150  GLY K C   1 
ATOM   12258 O  O   . GLY K  1 150 ? 40.226  -3.002  38.685  1.00 28.83 ? 150  GLY K O   1 
ATOM   12259 N  N   . ILE K  1 151 ? 41.082  -4.420  40.224  1.00 29.41 ? 151  ILE K N   1 
ATOM   12260 C  CA  . ILE K  1 151 ? 39.841  -5.103  40.603  1.00 29.45 ? 151  ILE K CA  1 
ATOM   12261 C  C   . ILE K  1 151 ? 38.662  -4.147  40.837  1.00 28.91 ? 151  ILE K C   1 
ATOM   12262 O  O   . ILE K  1 151 ? 38.768  -3.186  41.600  1.00 27.70 ? 151  ILE K O   1 
ATOM   12263 C  CB  . ILE K  1 151 ? 40.051  -5.915  41.909  1.00 29.59 ? 151  ILE K CB  1 
ATOM   12264 C  CG1 . ILE K  1 151 ? 41.351  -6.724  41.851  1.00 31.13 ? 151  ILE K CG1 1 
ATOM   12265 C  CG2 . ILE K  1 151 ? 38.870  -6.822  42.175  1.00 29.78 ? 151  ILE K CG2 1 
ATOM   12266 C  CD1 . ILE K  1 151 ? 41.491  -7.747  42.973  1.00 32.15 ? 151  ILE K CD1 1 
ATOM   12267 N  N   . ALA K  1 152 ? 37.541  -4.418  40.173  1.00 28.05 ? 152  ALA K N   1 
ATOM   12268 C  CA  . ALA K  1 152 ? 36.320  -3.638  40.344  1.00 30.54 ? 152  ALA K CA  1 
ATOM   12269 C  C   . ALA K  1 152 ? 35.211  -4.557  40.872  1.00 32.30 ? 152  ALA K C   1 
ATOM   12270 O  O   . ALA K  1 152 ? 35.346  -5.785  40.843  1.00 29.48 ? 152  ALA K O   1 
ATOM   12271 C  CB  . ALA K  1 152 ? 35.908  -2.998  39.013  1.00 28.38 ? 152  ALA K CB  1 
ATOM   12272 N  N   . GLN K  1 153 ? 34.120  -3.986  41.372  1.00 33.24 ? 153  GLN K N   1 
ATOM   12273 C  CA  . GLN K  1 153 ? 32.990  -4.841  41.727  1.00 37.35 ? 153  GLN K CA  1 
ATOM   12274 C  C   . GLN K  1 153 ? 32.022  -5.006  40.555  1.00 42.74 ? 153  GLN K C   1 
ATOM   12275 O  O   . GLN K  1 153 ? 31.426  -6.073  40.372  1.00 45.50 ? 153  GLN K O   1 
ATOM   12276 C  CB  . GLN K  1 153 ? 32.263  -4.356  42.985  1.00 37.39 ? 153  GLN K CB  1 
ATOM   12277 C  CG  . GLN K  1 153 ? 31.468  -3.080  42.833  1.00 40.56 ? 153  GLN K CG  1 
ATOM   12278 C  CD  . GLN K  1 153 ? 30.533  -2.846  44.010  1.00 39.86 ? 153  GLN K CD  1 
ATOM   12279 O  OE1 . GLN K  1 153 ? 30.415  -3.688  44.909  1.00 40.79 ? 153  GLN K OE1 1 
ATOM   12280 N  NE2 . GLN K  1 153 ? 29.868  -1.694  44.012  1.00 41.67 ? 153  GLN K NE2 1 
ATOM   12281 O  OXT . GLN K  1 153 ? 31.831  -4.085  39.753  1.00 46.92 ? 153  GLN K OXT 1 
ATOM   12282 N  N   . ALA L  1 1   ? 59.872  -13.581 44.295  1.00 46.52 ? 1    ALA L N   1 
ATOM   12283 C  CA  . ALA L  1 1   ? 60.079  -12.304 44.971  1.00 48.73 ? 1    ALA L CA  1 
ATOM   12284 C  C   . ALA L  1 1   ? 59.265  -11.178 44.325  1.00 48.10 ? 1    ALA L C   1 
ATOM   12285 O  O   . ALA L  1 1   ? 59.823  -10.225 43.784  1.00 50.62 ? 1    ALA L O   1 
ATOM   12286 C  CB  . ALA L  1 1   ? 61.568  -11.947 45.005  1.00 48.69 ? 1    ALA L CB  1 
ATOM   12287 N  N   . THR L  1 2   ? 57.943  -11.291 44.394  1.00 46.88 ? 2    THR L N   1 
ATOM   12288 C  CA  . THR L  1 2   ? 57.051  -10.285 43.829  1.00 44.47 ? 2    THR L CA  1 
ATOM   12289 C  C   . THR L  1 2   ? 57.303  -8.888  44.415  1.00 42.14 ? 2    THR L C   1 
ATOM   12290 O  O   . THR L  1 2   ? 57.729  -8.738  45.556  1.00 41.44 ? 2    THR L O   1 
ATOM   12291 C  CB  . THR L  1 2   ? 55.560  -10.679 44.007  1.00 46.53 ? 2    THR L CB  1 
ATOM   12292 O  OG1 . THR L  1 2   ? 55.421  -12.105 43.942  1.00 48.47 ? 2    THR L OG1 1 
ATOM   12293 C  CG2 . THR L  1 2   ? 54.691  -10.035 42.919  1.00 44.91 ? 2    THR L CG2 1 
ATOM   12294 N  N   . LYS L  1 3   ? 57.013  -7.868  43.617  1.00 43.66 ? 3    LYS L N   1 
ATOM   12295 C  CA  . LYS L  1 3   ? 57.320  -6.487  43.952  1.00 39.74 ? 3    LYS L CA  1 
ATOM   12296 C  C   . LYS L  1 3   ? 56.161  -5.612  43.464  1.00 38.64 ? 3    LYS L C   1 
ATOM   12297 O  O   . LYS L  1 3   ? 55.647  -5.815  42.359  1.00 37.77 ? 3    LYS L O   1 
ATOM   12298 C  CB  . LYS L  1 3   ? 58.624  -6.100  43.248  1.00 42.72 ? 3    LYS L CB  1 
ATOM   12299 C  CG  . LYS L  1 3   ? 59.438  -4.986  43.891  1.00 47.21 ? 3    LYS L CG  1 
ATOM   12300 C  CD  . LYS L  1 3   ? 60.851  -4.959  43.285  1.00 52.11 ? 3    LYS L CD  1 
ATOM   12301 C  CE  . LYS L  1 3   ? 61.481  -3.562  43.319  1.00 58.33 ? 3    LYS L CE  1 
ATOM   12302 N  NZ  . LYS L  1 3   ? 61.771  -3.078  44.704  1.00 63.17 ? 3    LYS L NZ  1 
ATOM   12303 N  N   . ALA L  1 4   ? 55.732  -4.657  44.287  1.00 38.21 ? 4    ALA L N   1 
ATOM   12304 C  CA  . ALA L  1 4   ? 54.643  -3.758  43.902  1.00 35.12 ? 4    ALA L CA  1 
ATOM   12305 C  C   . ALA L  1 4   ? 54.895  -2.331  44.357  1.00 32.37 ? 4    ALA L C   1 
ATOM   12306 O  O   . ALA L  1 4   ? 55.801  -2.064  45.125  1.00 33.58 ? 4    ALA L O   1 
ATOM   12307 C  CB  . ALA L  1 4   ? 53.301  -4.259  44.432  1.00 33.78 ? 4    ALA L CB  1 
ATOM   12308 N  N   . VAL L  1 5   ? 54.086  -1.414  43.853  1.00 32.78 ? 5    VAL L N   1 
ATOM   12309 C  CA  . VAL L  1 5   ? 54.212  -0.006  44.178  1.00 32.35 ? 5    VAL L CA  1 
ATOM   12310 C  C   . VAL L  1 5   ? 52.808  0.616   44.207  1.00 34.31 ? 5    VAL L C   1 
ATOM   12311 O  O   . VAL L  1 5   ? 51.821  -0.042  43.878  1.00 33.36 ? 5    VAL L O   1 
ATOM   12312 C  CB  . VAL L  1 5   ? 55.141  0.723   43.172  1.00 32.67 ? 5    VAL L CB  1 
ATOM   12313 C  CG1 . VAL L  1 5   ? 54.419  0.994   41.875  1.00 32.66 ? 5    VAL L CG1 1 
ATOM   12314 C  CG2 . VAL L  1 5   ? 55.685  2.021   43.767  1.00 32.74 ? 5    VAL L CG2 1 
ATOM   12315 N  N   . CYS L  1 6   ? 52.718  1.873   44.620  1.00 32.93 ? 6    CYS L N   1 
ATOM   12316 C  CA  . CYS L  1 6   ? 51.444  2.558   44.718  1.00 29.68 ? 6    CYS L CA  1 
ATOM   12317 C  C   . CYS L  1 6   ? 51.715  4.050   44.869  1.00 30.48 ? 6    CYS L C   1 
ATOM   12318 O  O   . CYS L  1 6   ? 52.469  4.468   45.741  1.00 34.03 ? 6    CYS L O   1 
ATOM   12319 C  CB  . CYS L  1 6   ? 50.666  2.031   45.931  1.00 33.51 ? 6    CYS L CB  1 
ATOM   12320 S  SG  . CYS L  1 6   ? 49.059  2.822   46.250  1.00 36.43 ? 6    CYS L SG  1 
ATOM   12321 N  N   . VAL L  1 7   ? 51.117  4.860   44.014  1.00 29.60 ? 7    VAL L N   1 
ATOM   12322 C  CA  . VAL L  1 7   ? 51.273  6.302   44.132  1.00 33.10 ? 7    VAL L CA  1 
ATOM   12323 C  C   . VAL L  1 7   ? 49.980  6.911   44.676  1.00 34.99 ? 7    VAL L C   1 
ATOM   12324 O  O   . VAL L  1 7   ? 48.949  6.884   44.007  1.00 33.96 ? 7    VAL L O   1 
ATOM   12325 C  CB  . VAL L  1 7   ? 51.672  6.940   42.775  1.00 36.40 ? 7    VAL L CB  1 
ATOM   12326 C  CG1 . VAL L  1 7   ? 51.696  8.466   42.866  1.00 34.74 ? 7    VAL L CG1 1 
ATOM   12327 C  CG2 . VAL L  1 7   ? 53.023  6.387   42.305  1.00 33.11 ? 7    VAL L CG2 1 
ATOM   12328 N  N   . LEU L  1 8   ? 50.039  7.430   45.905  1.00 37.89 ? 8    LEU L N   1 
ATOM   12329 C  CA  . LEU L  1 8   ? 48.873  8.016   46.565  1.00 34.35 ? 8    LEU L CA  1 
ATOM   12330 C  C   . LEU L  1 8   ? 48.613  9.454   46.120  1.00 34.98 ? 8    LEU L C   1 
ATOM   12331 O  O   . LEU L  1 8   ? 49.472  10.316  46.239  1.00 38.33 ? 8    LEU L O   1 
ATOM   12332 C  CB  . LEU L  1 8   ? 49.023  7.968   48.084  1.00 33.68 ? 8    LEU L CB  1 
ATOM   12333 C  CG  . LEU L  1 8   ? 49.475  6.661   48.744  1.00 36.61 ? 8    LEU L CG  1 
ATOM   12334 C  CD1 . LEU L  1 8   ? 49.388  6.768   50.271  1.00 38.14 ? 8    LEU L CD1 1 
ATOM   12335 C  CD2 . LEU L  1 8   ? 48.660  5.491   48.257  1.00 33.88 ? 8    LEU L CD2 1 
ATOM   12336 N  N   . LYS L  1 9   ? 47.417  9.703   45.602  1.00 37.33 ? 9    LYS L N   1 
ATOM   12337 C  CA  . LYS L  1 9   ? 47.013  11.039  45.191  1.00 39.11 ? 9    LYS L CA  1 
ATOM   12338 C  C   . LYS L  1 9   ? 45.594  11.268  45.675  1.00 41.08 ? 9    LYS L C   1 
ATOM   12339 O  O   . LYS L  1 9   ? 44.823  10.315  45.831  1.00 41.01 ? 9    LYS L O   1 
ATOM   12340 C  CB  . LYS L  1 9   ? 47.059  11.182  43.664  1.00 42.42 ? 9    LYS L CB  1 
ATOM   12341 C  CG  . LYS L  1 9   ? 48.442  11.455  43.071  1.00 47.28 ? 9    LYS L CG  1 
ATOM   12342 C  CD  . LYS L  1 9   ? 48.403  11.340  41.538  1.00 51.02 ? 9    LYS L CD  1 
ATOM   12343 C  CE  . LYS L  1 9   ? 49.639  11.938  40.875  1.00 51.13 ? 9    LYS L CE  1 
ATOM   12344 N  NZ  . LYS L  1 9   ? 49.587  13.436  40.819  1.00 54.34 ? 9    LYS L NZ  1 
ATOM   12345 N  N   . GLY L  1 10  ? 45.243  12.525  45.913  1.00 40.39 ? 10   GLY L N   1 
ATOM   12346 C  CA  . GLY L  1 10  ? 43.901  12.852  46.353  1.00 44.31 ? 10   GLY L CA  1 
ATOM   12347 C  C   . GLY L  1 10  ? 43.450  14.170  45.762  1.00 50.61 ? 10   GLY L C   1 
ATOM   12348 O  O   . GLY L  1 10  ? 44.132  14.726  44.899  1.00 50.89 ? 10   GLY L O   1 
ATOM   12349 N  N   . ASP L  1 11  ? 42.302  14.668  46.215  1.00 49.90 ? 11   ASP L N   1 
ATOM   12350 C  CA  . ASP L  1 11  ? 41.828  15.980  45.788  1.00 51.52 ? 11   ASP L CA  1 
ATOM   12351 C  C   . ASP L  1 11  ? 42.440  17.086  46.666  1.00 51.17 ? 11   ASP L C   1 
ATOM   12352 O  O   . ASP L  1 11  ? 41.976  18.228  46.649  1.00 52.58 ? 11   ASP L O   1 
ATOM   12353 C  CB  . ASP L  1 11  ? 40.291  16.046  45.820  1.00 54.68 ? 11   ASP L CB  1 
ATOM   12354 C  CG  . ASP L  1 11  ? 39.628  15.132  44.782  1.00 54.87 ? 11   ASP L CG  1 
ATOM   12355 O  OD1 . ASP L  1 11  ? 40.225  14.102  44.398  1.00 55.68 ? 11   ASP L OD1 1 
ATOM   12356 O  OD2 . ASP L  1 11  ? 38.494  15.444  44.356  1.00 53.17 ? 11   ASP L OD2 1 
ATOM   12357 N  N   . GLY L  1 12  ? 43.488  16.742  47.420  1.00 48.51 ? 12   GLY L N   1 
ATOM   12358 C  CA  . GLY L  1 12  ? 44.117  17.666  48.355  1.00 46.72 ? 12   GLY L CA  1 
ATOM   12359 C  C   . GLY L  1 12  ? 45.638  17.664  48.299  1.00 47.16 ? 12   GLY L C   1 
ATOM   12360 O  O   . GLY L  1 12  ? 46.213  17.193  47.320  1.00 47.63 ? 12   GLY L O   1 
ATOM   12361 N  N   . PRO L  1 13  ? 46.297  18.194  49.352  1.00 46.81 ? 13   PRO L N   1 
ATOM   12362 C  CA  . PRO L  1 13  ? 47.764  18.318  49.436  1.00 44.85 ? 13   PRO L CA  1 
ATOM   12363 C  C   . PRO L  1 13  ? 48.498  16.997  49.679  1.00 42.76 ? 13   PRO L C   1 
ATOM   12364 O  O   . PRO L  1 13  ? 49.715  16.939  49.481  1.00 42.74 ? 13   PRO L O   1 
ATOM   12365 C  CB  . PRO L  1 13  ? 47.979  19.241  50.648  1.00 41.07 ? 13   PRO L CB  1 
ATOM   12366 C  CG  . PRO L  1 13  ? 46.642  19.823  50.965  1.00 44.05 ? 13   PRO L CG  1 
ATOM   12367 C  CD  . PRO L  1 13  ? 45.635  18.812  50.513  1.00 46.18 ? 13   PRO L CD  1 
ATOM   12368 N  N   . VAL L  1 14  ? 47.772  15.967  50.113  1.00 43.12 ? 14   VAL L N   1 
ATOM   12369 C  CA  . VAL L  1 14  ? 48.375  14.681  50.464  1.00 40.36 ? 14   VAL L CA  1 
ATOM   12370 C  C   . VAL L  1 14  ? 48.773  13.860  49.236  1.00 41.98 ? 14   VAL L C   1 
ATOM   12371 O  O   . VAL L  1 14  ? 47.969  13.664  48.318  1.00 39.29 ? 14   VAL L O   1 
ATOM   12372 C  CB  . VAL L  1 14  ? 47.431  13.843  51.335  1.00 34.84 ? 14   VAL L CB  1 
ATOM   12373 C  CG1 . VAL L  1 14  ? 48.150  12.597  51.828  1.00 34.32 ? 14   VAL L CG1 1 
ATOM   12374 C  CG2 . VAL L  1 14  ? 46.928  14.677  52.488  1.00 32.82 ? 14   VAL L CG2 1 
ATOM   12375 N  N   . GLN L  1 15  ? 50.017  13.383  49.236  1.00 44.15 ? 15   GLN L N   1 
ATOM   12376 C  CA  . GLN L  1 15  ? 50.557  12.578  48.141  1.00 40.99 ? 15   GLN L CA  1 
ATOM   12377 C  C   . GLN L  1 15  ? 51.708  11.738  48.677  1.00 37.73 ? 15   GLN L C   1 
ATOM   12378 O  O   . GLN L  1 15  ? 52.458  12.193  49.527  1.00 38.16 ? 15   GLN L O   1 
ATOM   12379 C  CB  . GLN L  1 15  ? 51.061  13.481  47.018  1.00 40.83 ? 15   GLN L CB  1 
ATOM   12380 C  CG  . GLN L  1 15  ? 52.353  14.210  47.371  1.00 47.56 ? 15   GLN L CG  1 
ATOM   12381 C  CD  . GLN L  1 15  ? 52.930  15.000  46.208  1.00 54.71 ? 15   GLN L CD  1 
ATOM   12382 O  OE1 . GLN L  1 15  ? 52.321  15.962  45.727  1.00 54.49 ? 15   GLN L OE1 1 
ATOM   12383 N  NE2 . GLN L  1 15  ? 54.120  14.601  45.756  1.00 54.23 ? 15   GLN L NE2 1 
ATOM   12384 N  N   . GLY L  1 16  ? 51.848  10.514  48.186  1.00 36.37 ? 16   GLY L N   1 
ATOM   12385 C  CA  . GLY L  1 16  ? 52.917  9.641   48.643  1.00 35.03 ? 16   GLY L CA  1 
ATOM   12386 C  C   . GLY L  1 16  ? 53.301  8.593   47.615  1.00 37.08 ? 16   GLY L C   1 
ATOM   12387 O  O   . GLY L  1 16  ? 52.669  8.472   46.563  1.00 37.18 ? 16   GLY L O   1 
ATOM   12388 N  N   . ILE L  1 17  ? 54.356  7.844   47.908  1.00 36.05 ? 17   ILE L N   1 
ATOM   12389 C  CA  . ILE L  1 17  ? 54.738  6.705   47.087  1.00 35.81 ? 17   ILE L CA  1 
ATOM   12390 C  C   . ILE L  1 17  ? 55.057  5.533   47.995  1.00 33.32 ? 17   ILE L C   1 
ATOM   12391 O  O   . ILE L  1 17  ? 55.975  5.596   48.806  1.00 34.80 ? 17   ILE L O   1 
ATOM   12392 C  CB  . ILE L  1 17  ? 55.952  6.995   46.176  1.00 37.40 ? 17   ILE L CB  1 
ATOM   12393 C  CG1 . ILE L  1 17  ? 55.549  7.928   45.025  1.00 37.48 ? 17   ILE L CG1 1 
ATOM   12394 C  CG2 . ILE L  1 17  ? 56.547  5.675   45.642  1.00 33.73 ? 17   ILE L CG2 1 
ATOM   12395 C  CD1 . ILE L  1 17  ? 56.612  8.084   43.942  1.00 36.97 ? 17   ILE L CD1 1 
ATOM   12396 N  N   . ILE L  1 18  ? 54.297  4.460   47.853  1.00 31.49 ? 18   ILE L N   1 
ATOM   12397 C  CA  . ILE L  1 18  ? 54.451  3.317   48.736  1.00 34.87 ? 18   ILE L CA  1 
ATOM   12398 C  C   . ILE L  1 18  ? 54.981  2.119   47.964  1.00 34.23 ? 18   ILE L C   1 
ATOM   12399 O  O   . ILE L  1 18  ? 54.514  1.834   46.863  1.00 34.65 ? 18   ILE L O   1 
ATOM   12400 C  CB  . ILE L  1 18  ? 53.113  2.961   49.444  1.00 31.53 ? 18   ILE L CB  1 
ATOM   12401 C  CG1 . ILE L  1 18  ? 52.592  4.165   50.249  1.00 33.39 ? 18   ILE L CG1 1 
ATOM   12402 C  CG2 . ILE L  1 18  ? 53.273  1.719   50.312  1.00 30.61 ? 18   ILE L CG2 1 
ATOM   12403 C  CD1 . ILE L  1 18  ? 53.503  4.607   51.423  1.00 34.38 ? 18   ILE L CD1 1 
ATOM   12404 N  N   . ASN L  1 19  ? 55.958  1.430   48.549  1.00 32.47 ? 19   ASN L N   1 
ATOM   12405 C  CA  . ASN L  1 19  ? 56.586  0.281   47.913  1.00 34.06 ? 19   ASN L CA  1 
ATOM   12406 C  C   . ASN L  1 19  ? 56.224  -0.981  48.664  1.00 33.45 ? 19   ASN L C   1 
ATOM   12407 O  O   . ASN L  1 19  ? 55.984  -0.936  49.859  1.00 33.40 ? 19   ASN L O   1 
ATOM   12408 C  CB  . ASN L  1 19  ? 58.108  0.451   47.858  1.00 32.08 ? 19   ASN L CB  1 
ATOM   12409 C  CG  . ASN L  1 19  ? 58.533  1.675   47.061  1.00 36.14 ? 19   ASN L CG  1 
ATOM   12410 O  OD1 . ASN L  1 19  ? 58.666  1.616   45.831  1.00 43.24 ? 19   ASN L OD1 1 
ATOM   12411 N  ND2 . ASN L  1 19  ? 58.759  2.790   47.754  1.00 30.87 ? 19   ASN L ND2 1 
ATOM   12412 N  N   . PHE L  1 20  ? 56.161  -2.101  47.951  1.00 33.49 ? 20   PHE L N   1 
ATOM   12413 C  CA  . PHE L  1 20  ? 55.860  -3.394  48.553  1.00 34.66 ? 20   PHE L CA  1 
ATOM   12414 C  C   . PHE L  1 20  ? 56.937  -4.356  48.082  1.00 35.82 ? 20   PHE L C   1 
ATOM   12415 O  O   . PHE L  1 20  ? 57.724  -4.019  47.208  1.00 40.18 ? 20   PHE L O   1 
ATOM   12416 C  CB  . PHE L  1 20  ? 54.471  -3.907  48.135  1.00 32.49 ? 20   PHE L CB  1 
ATOM   12417 C  CG  . PHE L  1 20  ? 53.338  -2.937  48.415  1.00 33.13 ? 20   PHE L CG  1 
ATOM   12418 C  CD1 . PHE L  1 20  ? 53.035  -1.916  47.517  1.00 32.01 ? 20   PHE L CD1 1 
ATOM   12419 C  CD2 . PHE L  1 20  ? 52.569  -3.055  49.571  1.00 32.25 ? 20   PHE L CD2 1 
ATOM   12420 C  CE1 . PHE L  1 20  ? 51.991  -1.021  47.763  1.00 31.37 ? 20   PHE L CE1 1 
ATOM   12421 C  CE2 . PHE L  1 20  ? 51.528  -2.169  49.829  1.00 30.18 ? 20   PHE L CE2 1 
ATOM   12422 C  CZ  . PHE L  1 20  ? 51.236  -1.149  48.918  1.00 32.36 ? 20   PHE L CZ  1 
ATOM   12423 N  N   . GLU L  1 21  ? 56.980  -5.548  48.658  1.00 37.08 ? 21   GLU L N   1 
ATOM   12424 C  CA  . GLU L  1 21  ? 58.000  -6.514  48.287  1.00 39.51 ? 21   GLU L CA  1 
ATOM   12425 C  C   . GLU L  1 21  ? 57.794  -7.782  49.091  1.00 41.51 ? 21   GLU L C   1 
ATOM   12426 O  O   . GLU L  1 21  ? 57.683  -7.741  50.312  1.00 42.16 ? 21   GLU L O   1 
ATOM   12427 C  CB  . GLU L  1 21  ? 59.392  -5.926  48.538  1.00 45.40 ? 21   GLU L CB  1 
ATOM   12428 C  CG  . GLU L  1 21  ? 60.566  -6.874  48.330  1.00 49.84 ? 21   GLU L CG  1 
ATOM   12429 C  CD  . GLU L  1 21  ? 61.894  -6.227  48.711  1.00 58.19 ? 21   GLU L CD  1 
ATOM   12430 O  OE1 . GLU L  1 21  ? 62.333  -5.301  47.985  1.00 56.26 ? 21   GLU L OE1 1 
ATOM   12431 O  OE2 . GLU L  1 21  ? 62.493  -6.644  49.736  1.00 57.90 ? 21   GLU L OE2 1 
ATOM   12432 N  N   . GLN L  1 22  ? 57.727  -8.912  48.403  1.00 41.47 ? 22   GLN L N   1 
ATOM   12433 C  CA  . GLN L  1 22  ? 57.490  -10.175 49.078  1.00 44.04 ? 22   GLN L CA  1 
ATOM   12434 C  C   . GLN L  1 22  ? 58.427  -11.247 48.547  1.00 48.89 ? 22   GLN L C   1 
ATOM   12435 O  O   . GLN L  1 22  ? 58.137  -11.886 47.539  1.00 48.03 ? 22   GLN L O   1 
ATOM   12436 C  CB  . GLN L  1 22  ? 56.044  -10.606 48.873  1.00 44.21 ? 22   GLN L CB  1 
ATOM   12437 C  CG  . GLN L  1 22  ? 55.629  -11.801 49.697  1.00 46.06 ? 22   GLN L CG  1 
ATOM   12438 C  CD  . GLN L  1 22  ? 54.178  -12.158 49.478  1.00 46.61 ? 22   GLN L CD  1 
ATOM   12439 O  OE1 . GLN L  1 22  ? 53.653  -12.003 48.376  1.00 46.21 ? 22   GLN L OE1 1 
ATOM   12440 N  NE2 . GLN L  1 22  ? 53.519  -12.635 50.526  1.00 47.57 ? 22   GLN L NE2 1 
ATOM   12441 N  N   . LYS L  1 23  ? 59.555  -11.433 49.229  1.00 53.59 ? 23   LYS L N   1 
ATOM   12442 C  CA  . LYS L  1 23  ? 60.536  -12.446 48.843  1.00 55.58 ? 23   LYS L CA  1 
ATOM   12443 C  C   . LYS L  1 23  ? 59.905  -13.836 48.753  1.00 59.22 ? 23   LYS L C   1 
ATOM   12444 O  O   . LYS L  1 23  ? 59.805  -14.414 47.665  1.00 60.59 ? 23   LYS L O   1 
ATOM   12445 C  CB  . LYS L  1 23  ? 61.721  -12.458 49.818  1.00 53.80 ? 23   LYS L CB  1 
ATOM   12446 C  CG  . LYS L  1 23  ? 62.888  -11.576 49.395  1.00 56.30 ? 23   LYS L CG  1 
ATOM   12447 C  CD  . LYS L  1 23  ? 62.514  -10.092 49.345  1.00 56.14 ? 23   LYS L CD  1 
ATOM   12448 C  CE  . LYS L  1 23  ? 63.488  -9.293  48.468  1.00 59.61 ? 23   LYS L CE  1 
ATOM   12449 N  NZ  . LYS L  1 23  ? 64.937  -9.522  48.779  1.00 60.55 ? 23   LYS L NZ  1 
ATOM   12450 N  N   . GLU L  1 24  ? 59.483  -14.364 49.898  1.00 57.84 ? 24   GLU L N   1 
ATOM   12451 C  CA  . GLU L  1 24  ? 58.856  -15.683 49.957  1.00 62.48 ? 24   GLU L CA  1 
ATOM   12452 C  C   . GLU L  1 24  ? 57.365  -15.591 49.624  1.00 61.22 ? 24   GLU L C   1 
ATOM   12453 O  O   . GLU L  1 24  ? 56.716  -14.589 49.934  1.00 59.01 ? 24   GLU L O   1 
ATOM   12454 C  CB  . GLU L  1 24  ? 59.046  -16.298 51.351  1.00 62.71 ? 24   GLU L CB  1 
ATOM   12455 C  CG  . GLU L  1 24  ? 60.503  -16.435 51.786  1.00 61.59 ? 24   GLU L CG  1 
ATOM   12456 C  CD  . GLU L  1 24  ? 61.182  -17.666 51.204  1.00 64.74 ? 24   GLU L CD  1 
ATOM   12457 O  OE1 . GLU L  1 24  ? 60.534  -18.739 51.164  1.00 61.01 ? 24   GLU L OE1 1 
ATOM   12458 O  OE2 . GLU L  1 24  ? 62.365  -17.560 50.800  1.00 60.81 ? 24   GLU L OE2 1 
ATOM   12459 N  N   . SER L  1 25  ? 56.819  -16.628 48.991  1.00 63.17 ? 25   SER L N   1 
ATOM   12460 C  CA  . SER L  1 25  ? 55.381  -16.650 48.728  1.00 66.13 ? 25   SER L CA  1 
ATOM   12461 C  C   . SER L  1 25  ? 54.658  -16.916 50.043  1.00 63.38 ? 25   SER L C   1 
ATOM   12462 O  O   . SER L  1 25  ? 55.029  -17.823 50.794  1.00 64.15 ? 25   SER L O   1 
ATOM   12463 C  CB  . SER L  1 25  ? 55.003  -17.710 47.683  1.00 65.45 ? 25   SER L CB  1 
ATOM   12464 O  OG  . SER L  1 25  ? 54.427  -18.857 48.292  1.00 62.73 ? 25   SER L OG  1 
ATOM   12465 N  N   . ASN L  1 26  ? 53.636  -16.118 50.329  1.00 59.67 ? 26   ASN L N   1 
ATOM   12466 C  CA  . ASN L  1 26  ? 52.929  -16.237 51.601  1.00 63.25 ? 26   ASN L CA  1 
ATOM   12467 C  C   . ASN L  1 26  ? 53.834  -15.939 52.810  1.00 60.71 ? 26   ASN L C   1 
ATOM   12468 O  O   . ASN L  1 26  ? 53.594  -16.424 53.919  1.00 59.80 ? 26   ASN L O   1 
ATOM   12469 C  CB  . ASN L  1 26  ? 52.271  -17.619 51.733  1.00 66.19 ? 26   ASN L CB  1 
ATOM   12470 C  CG  . ASN L  1 26  ? 51.103  -17.812 50.770  1.00 69.05 ? 26   ASN L CG  1 
ATOM   12471 O  OD1 . ASN L  1 26  ? 50.317  -16.886 50.528  1.00 67.17 ? 26   ASN L OD1 1 
ATOM   12472 N  ND2 . ASN L  1 26  ? 50.980  -19.022 50.223  1.00 68.35 ? 26   ASN L ND2 1 
ATOM   12473 N  N   . GLY L  1 27  ? 54.875  -15.143 52.577  1.00 56.97 ? 27   GLY L N   1 
ATOM   12474 C  CA  . GLY L  1 27  ? 55.720  -14.638 53.643  1.00 52.18 ? 27   GLY L CA  1 
ATOM   12475 C  C   . GLY L  1 27  ? 55.433  -13.162 53.852  1.00 51.24 ? 27   GLY L C   1 
ATOM   12476 O  O   . GLY L  1 27  ? 54.588  -12.599 53.154  1.00 52.15 ? 27   GLY L O   1 
ATOM   12477 N  N   . PRO L  1 28  ? 56.125  -12.528 54.816  1.00 50.68 ? 28   PRO L N   1 
ATOM   12478 C  CA  . PRO L  1 28  ? 55.938  -11.104 55.127  1.00 46.85 ? 28   PRO L CA  1 
ATOM   12479 C  C   . PRO L  1 28  ? 56.066  -10.202 53.907  1.00 43.76 ? 28   PRO L C   1 
ATOM   12480 O  O   . PRO L  1 28  ? 56.758  -10.544 52.950  1.00 47.67 ? 28   PRO L O   1 
ATOM   12481 C  CB  . PRO L  1 28  ? 57.072  -10.810 56.118  1.00 48.07 ? 28   PRO L CB  1 
ATOM   12482 C  CG  . PRO L  1 28  ? 57.315  -12.107 56.790  1.00 51.13 ? 28   PRO L CG  1 
ATOM   12483 C  CD  . PRO L  1 28  ? 57.060  -13.176 55.754  1.00 53.54 ? 28   PRO L CD  1 
ATOM   12484 N  N   . VAL L  1 29  ? 55.410  -9.049  53.955  1.00 40.26 ? 29   VAL L N   1 
ATOM   12485 C  CA  . VAL L  1 29  ? 55.450  -8.097  52.855  1.00 42.31 ? 29   VAL L CA  1 
ATOM   12486 C  C   . VAL L  1 29  ? 56.007  -6.761  53.349  1.00 40.37 ? 29   VAL L C   1 
ATOM   12487 O  O   . VAL L  1 29  ? 55.304  -6.004  54.013  1.00 42.59 ? 29   VAL L O   1 
ATOM   12488 C  CB  . VAL L  1 29  ? 54.037  -7.916  52.222  1.00 37.97 ? 29   VAL L CB  1 
ATOM   12489 C  CG1 . VAL L  1 29  ? 54.004  -6.731  51.277  1.00 35.79 ? 29   VAL L CG1 1 
ATOM   12490 C  CG2 . VAL L  1 29  ? 53.599  -9.192  51.511  1.00 36.60 ? 29   VAL L CG2 1 
ATOM   12491 N  N   . LYS L  1 30  ? 57.273  -6.482  53.041  1.00 37.84 ? 30   LYS L N   1 
ATOM   12492 C  CA  . LYS L  1 30  ? 57.909  -5.234  53.465  1.00 39.70 ? 30   LYS L CA  1 
ATOM   12493 C  C   . LYS L  1 30  ? 57.234  -4.059  52.773  1.00 39.19 ? 30   LYS L C   1 
ATOM   12494 O  O   . LYS L  1 30  ? 57.215  -3.986  51.545  1.00 41.17 ? 30   LYS L O   1 
ATOM   12495 C  CB  . LYS L  1 30  ? 59.421  -5.242  53.157  1.00 42.53 ? 30   LYS L CB  1 
ATOM   12496 C  CG  . LYS L  1 30  ? 60.210  -4.001  53.663  1.00 45.83 ? 30   LYS L CG  1 
ATOM   12497 C  CD  . LYS L  1 30  ? 61.660  -3.927  53.102  1.00 54.14 ? 30   LYS L CD  1 
ATOM   12498 C  CE  . LYS L  1 30  ? 62.390  -2.610  53.470  1.00 47.59 ? 30   LYS L CE  1 
ATOM   12499 N  NZ  . LYS L  1 30  ? 63.506  -2.262  52.514  1.00 40.16 ? 30   LYS L NZ  1 
ATOM   12500 N  N   . VAL L  1 31  ? 56.666  -3.144  53.552  1.00 36.34 ? 31   VAL L N   1 
ATOM   12501 C  CA  . VAL L  1 31  ? 56.041  -1.957  52.970  1.00 37.82 ? 31   VAL L CA  1 
ATOM   12502 C  C   . VAL L  1 31  ? 56.765  -0.692  53.422  1.00 37.41 ? 31   VAL L C   1 
ATOM   12503 O  O   . VAL L  1 31  ? 56.713  -0.332  54.600  1.00 36.97 ? 31   VAL L O   1 
ATOM   12504 C  CB  . VAL L  1 31  ? 54.529  -1.852  53.323  1.00 36.24 ? 31   VAL L CB  1 
ATOM   12505 C  CG1 . VAL L  1 31  ? 53.924  -0.583  52.730  1.00 32.91 ? 31   VAL L CG1 1 
ATOM   12506 C  CG2 . VAL L  1 31  ? 53.765  -3.084  52.843  1.00 35.20 ? 31   VAL L CG2 1 
ATOM   12507 N  N   . TRP L  1 32  ? 57.458  -0.029  52.497  1.00 34.22 ? 32   TRP L N   1 
ATOM   12508 C  CA  . TRP L  1 32  ? 58.139  1.216   52.832  1.00 33.19 ? 32   TRP L CA  1 
ATOM   12509 C  C   . TRP L  1 32  ? 57.732  2.342   51.915  1.00 33.44 ? 32   TRP L C   1 
ATOM   12510 O  O   . TRP L  1 32  ? 57.167  2.099   50.860  1.00 37.44 ? 32   TRP L O   1 
ATOM   12511 C  CB  . TRP L  1 32  ? 59.654  1.036   52.824  1.00 38.46 ? 32   TRP L CB  1 
ATOM   12512 C  CG  . TRP L  1 32  ? 60.275  0.855   51.481  1.00 38.05 ? 32   TRP L CG  1 
ATOM   12513 C  CD1 . TRP L  1 32  ? 60.924  1.807   50.736  1.00 36.06 ? 32   TRP L CD1 1 
ATOM   12514 C  CD2 . TRP L  1 32  ? 60.351  -0.363  50.733  1.00 37.27 ? 32   TRP L CD2 1 
ATOM   12515 N  NE1 . TRP L  1 32  ? 61.383  1.252   49.563  1.00 36.37 ? 32   TRP L NE1 1 
ATOM   12516 C  CE2 . TRP L  1 32  ? 61.045  -0.076  49.537  1.00 38.71 ? 32   TRP L CE2 1 
ATOM   12517 C  CE3 . TRP L  1 32  ? 59.897  -1.666  50.956  1.00 40.07 ? 32   TRP L CE3 1 
ATOM   12518 C  CZ2 . TRP L  1 32  ? 61.289  -1.049  48.566  1.00 41.23 ? 32   TRP L CZ2 1 
ATOM   12519 C  CZ3 . TRP L  1 32  ? 60.146  -2.632  49.988  1.00 41.79 ? 32   TRP L CZ3 1 
ATOM   12520 C  CH2 . TRP L  1 32  ? 60.833  -2.317  48.809  1.00 41.78 ? 32   TRP L CH2 1 
ATOM   12521 N  N   . GLY L  1 33  ? 57.995  3.580   52.318  1.00 31.87 ? 33   GLY L N   1 
ATOM   12522 C  CA  . GLY L  1 33  ? 57.570  4.709   51.516  1.00 31.49 ? 33   GLY L CA  1 
ATOM   12523 C  C   . GLY L  1 33  ? 57.475  6.009   52.275  1.00 30.74 ? 33   GLY L C   1 
ATOM   12524 O  O   . GLY L  1 33  ? 57.987  6.127   53.373  1.00 33.82 ? 33   GLY L O   1 
ATOM   12525 N  N   . SER L  1 34  ? 56.799  6.989   51.691  1.00 31.74 ? 34   SER L N   1 
ATOM   12526 C  CA  . SER L  1 34  ? 56.750  8.319   52.280  1.00 35.22 ? 34   SER L CA  1 
ATOM   12527 C  C   . SER L  1 34  ? 55.495  9.074   51.849  1.00 35.93 ? 34   SER L C   1 
ATOM   12528 O  O   . SER L  1 34  ? 55.033  8.940   50.718  1.00 37.95 ? 34   SER L O   1 
ATOM   12529 C  CB  . SER L  1 34  ? 58.026  9.100   51.921  1.00 37.13 ? 34   SER L CB  1 
ATOM   12530 O  OG  . SER L  1 34  ? 57.872  10.499  52.106  1.00 40.84 ? 34   SER L OG  1 
ATOM   12531 N  N   . ILE L  1 35  ? 54.943  9.857   52.768  1.00 33.74 ? 35   ILE L N   1 
ATOM   12532 C  CA  . ILE L  1 35  ? 53.732  10.617  52.514  1.00 33.81 ? 35   ILE L CA  1 
ATOM   12533 C  C   . ILE L  1 35  ? 53.937  12.039  53.029  1.00 37.33 ? 35   ILE L C   1 
ATOM   12534 O  O   . ILE L  1 35  ? 54.538  12.239  54.078  1.00 37.52 ? 35   ILE L O   1 
ATOM   12535 C  CB  . ILE L  1 35  ? 52.525  9.973   53.227  1.00 33.85 ? 35   ILE L CB  1 
ATOM   12536 C  CG1 . ILE L  1 35  ? 52.490  8.463   52.957  1.00 32.16 ? 35   ILE L CG1 1 
ATOM   12537 C  CG2 . ILE L  1 35  ? 51.211  10.657  52.825  1.00 34.70 ? 35   ILE L CG2 1 
ATOM   12538 C  CD1 . ILE L  1 35  ? 51.195  7.790   53.389  1.00 30.84 ? 35   ILE L CD1 1 
ATOM   12539 N  N   . LYS L  1 36  ? 53.445  13.026  52.289  1.00 38.08 ? 36   LYS L N   1 
ATOM   12540 C  CA  . LYS L  1 36  ? 53.619  14.424  52.659  1.00 37.43 ? 36   LYS L CA  1 
ATOM   12541 C  C   . LYS L  1 36  ? 52.267  15.124  52.654  1.00 38.62 ? 36   LYS L C   1 
ATOM   12542 O  O   . LYS L  1 36  ? 51.296  14.583  52.126  1.00 40.56 ? 36   LYS L O   1 
ATOM   12543 C  CB  . LYS L  1 36  ? 54.578  15.117  51.684  1.00 40.59 ? 36   LYS L CB  1 
ATOM   12544 C  CG  . LYS L  1 36  ? 53.965  15.492  50.337  1.00 43.02 ? 36   LYS L CG  1 
ATOM   12545 C  CD  . LYS L  1 36  ? 54.932  16.313  49.483  1.00 48.50 ? 36   LYS L CD  1 
ATOM   12546 C  CE  . LYS L  1 36  ? 56.221  15.539  49.181  1.00 55.96 ? 36   LYS L CE  1 
ATOM   12547 N  NZ  . LYS L  1 36  ? 57.195  16.301  48.325  1.00 50.12 ? 36   LYS L NZ  1 
ATOM   12548 N  N   . GLY L  1 37  ? 52.201  16.317  53.242  1.00 36.04 ? 37   GLY L N   1 
ATOM   12549 C  CA  . GLY L  1 37  ? 50.974  17.100  53.240  1.00 37.08 ? 37   GLY L CA  1 
ATOM   12550 C  C   . GLY L  1 37  ? 49.935  16.639  54.256  1.00 40.23 ? 37   GLY L C   1 
ATOM   12551 O  O   . GLY L  1 37  ? 48.782  17.088  54.230  1.00 37.87 ? 37   GLY L O   1 
ATOM   12552 N  N   . LEU L  1 38  ? 50.352  15.736  55.145  1.00 39.98 ? 38   LEU L N   1 
ATOM   12553 C  CA  . LEU L  1 38  ? 49.523  15.212  56.232  1.00 35.14 ? 38   LEU L CA  1 
ATOM   12554 C  C   . LEU L  1 38  ? 49.455  16.190  57.415  1.00 38.50 ? 38   LEU L C   1 
ATOM   12555 O  O   . LEU L  1 38  ? 50.345  17.021  57.594  1.00 41.25 ? 38   LEU L O   1 
ATOM   12556 C  CB  . LEU L  1 38  ? 50.129  13.893  56.718  1.00 34.80 ? 38   LEU L CB  1 
ATOM   12557 C  CG  . LEU L  1 38  ? 49.558  12.518  56.346  1.00 35.34 ? 38   LEU L CG  1 
ATOM   12558 C  CD1 . LEU L  1 38  ? 48.627  12.552  55.142  1.00 31.41 ? 38   LEU L CD1 1 
ATOM   12559 C  CD2 . LEU L  1 38  ? 50.689  11.498  56.170  1.00 31.54 ? 38   LEU L CD2 1 
ATOM   12560 N  N   . THR L  1 39  ? 48.409  16.094  58.230  1.00 36.56 ? 39   THR L N   1 
ATOM   12561 C  CA  . THR L  1 39  ? 48.402  16.796  59.513  1.00 35.11 ? 39   THR L CA  1 
ATOM   12562 C  C   . THR L  1 39  ? 49.270  16.018  60.499  1.00 35.60 ? 39   THR L C   1 
ATOM   12563 O  O   . THR L  1 39  ? 49.298  14.787  60.470  1.00 36.14 ? 39   THR L O   1 
ATOM   12564 C  CB  . THR L  1 39  ? 46.979  16.944  60.104  1.00 32.59 ? 39   THR L CB  1 
ATOM   12565 O  OG1 . THR L  1 39  ? 46.325  15.670  60.116  1.00 33.52 ? 39   THR L OG1 1 
ATOM   12566 C  CG2 . THR L  1 39  ? 46.138  17.943  59.304  1.00 30.63 ? 39   THR L CG2 1 
ATOM   12567 N  N   . GLU L  1 40  ? 49.985  16.737  61.359  1.00 35.06 ? 40   GLU L N   1 
ATOM   12568 C  CA  . GLU L  1 40  ? 50.843  16.113  62.367  1.00 39.36 ? 40   GLU L CA  1 
ATOM   12569 C  C   . GLU L  1 40  ? 50.044  15.128  63.228  1.00 36.43 ? 40   GLU L C   1 
ATOM   12570 O  O   . GLU L  1 40  ? 48.979  15.462  63.746  1.00 35.17 ? 40   GLU L O   1 
ATOM   12571 C  CB  . GLU L  1 40  ? 51.494  17.187  63.253  1.00 38.03 ? 40   GLU L CB  1 
ATOM   12572 C  CG  . GLU L  1 40  ? 52.678  16.692  64.104  1.00 36.50 ? 40   GLU L CG  1 
ATOM   12573 C  CD  . GLU L  1 40  ? 53.211  17.762  65.067  1.00 37.86 ? 40   GLU L CD  1 
ATOM   12574 O  OE1 . GLU L  1 40  ? 52.897  18.958  64.865  1.00 33.91 ? 40   GLU L OE1 1 
ATOM   12575 O  OE2 . GLU L  1 40  ? 53.947  17.407  66.024  1.00 38.46 ? 40   GLU L OE2 1 
ATOM   12576 N  N   . GLY L  1 41  ? 50.558  13.913  63.377  1.00 36.21 ? 41   GLY L N   1 
ATOM   12577 C  CA  . GLY L  1 41  ? 49.866  12.904  64.159  1.00 36.06 ? 41   GLY L CA  1 
ATOM   12578 C  C   . GLY L  1 41  ? 49.612  11.604  63.413  1.00 35.47 ? 41   GLY L C   1 
ATOM   12579 O  O   . GLY L  1 41  ? 50.241  11.321  62.375  1.00 34.00 ? 41   GLY L O   1 
ATOM   12580 N  N   . LEU L  1 42  ? 48.678  10.815  63.946  1.00 34.10 ? 42   LEU L N   1 
ATOM   12581 C  CA  . LEU L  1 42  ? 48.401  9.478   63.422  1.00 32.13 ? 42   LEU L CA  1 
ATOM   12582 C  C   . LEU L  1 42  ? 47.298  9.469   62.364  1.00 30.55 ? 42   LEU L C   1 
ATOM   12583 O  O   . LEU L  1 42  ? 46.254  10.107  62.535  1.00 28.85 ? 42   LEU L O   1 
ATOM   12584 C  CB  . LEU L  1 42  ? 48.053  8.506   64.553  1.00 33.26 ? 42   LEU L CB  1 
ATOM   12585 C  CG  . LEU L  1 42  ? 49.149  8.000   65.491  1.00 29.33 ? 42   LEU L CG  1 
ATOM   12586 C  CD1 . LEU L  1 42  ? 48.597  6.847   66.304  1.00 31.10 ? 42   LEU L CD1 1 
ATOM   12587 C  CD2 . LEU L  1 42  ? 50.345  7.540   64.719  1.00 32.98 ? 42   LEU L CD2 1 
ATOM   12588 N  N   . HIS L  1 43  ? 47.552  8.743   61.274  1.00 30.18 ? 43   HIS L N   1 
ATOM   12589 C  CA  . HIS L  1 43  ? 46.611  8.624   60.156  1.00 30.30 ? 43   HIS L CA  1 
ATOM   12590 C  C   . HIS L  1 43  ? 46.429  7.170   59.761  1.00 28.26 ? 43   HIS L C   1 
ATOM   12591 O  O   . HIS L  1 43  ? 47.409  6.462   59.564  1.00 30.38 ? 43   HIS L O   1 
ATOM   12592 C  CB  . HIS L  1 43  ? 47.126  9.391   58.943  1.00 29.37 ? 43   HIS L CB  1 
ATOM   12593 C  CG  . HIS L  1 43  ? 47.285  10.855  59.185  1.00 31.76 ? 43   HIS L CG  1 
ATOM   12594 N  ND1 . HIS L  1 43  ? 46.263  11.754  58.975  1.00 31.42 ? 43   HIS L ND1 1 
ATOM   12595 C  CD2 . HIS L  1 43  ? 48.337  11.576  59.637  1.00 30.87 ? 43   HIS L CD2 1 
ATOM   12596 C  CE1 . HIS L  1 43  ? 46.681  12.968  59.278  1.00 33.82 ? 43   HIS L CE1 1 
ATOM   12597 N  NE2 . HIS L  1 43  ? 47.936  12.888  59.683  1.00 34.25 ? 43   HIS L NE2 1 
ATOM   12598 N  N   . GLY L  1 44  ? 45.181  6.732   59.635  1.00 30.01 ? 44   GLY L N   1 
ATOM   12599 C  CA  . GLY L  1 44  ? 44.880  5.360   59.257  1.00 27.75 ? 44   GLY L CA  1 
ATOM   12600 C  C   . GLY L  1 44  ? 45.415  5.007   57.880  1.00 29.53 ? 44   GLY L C   1 
ATOM   12601 O  O   . GLY L  1 44  ? 45.389  5.832   56.959  1.00 29.20 ? 44   GLY L O   1 
ATOM   12602 N  N   . PHE L  1 45  ? 45.882  3.768   57.744  1.00 27.24 ? 45   PHE L N   1 
ATOM   12603 C  CA  . PHE L  1 45  ? 46.537  3.296   56.535  1.00 25.16 ? 45   PHE L CA  1 
ATOM   12604 C  C   . PHE L  1 45  ? 46.008  1.910   56.206  1.00 25.36 ? 45   PHE L C   1 
ATOM   12605 O  O   . PHE L  1 45  ? 46.387  0.934   56.850  1.00 24.02 ? 45   PHE L O   1 
ATOM   12606 C  CB  . PHE L  1 45  ? 48.035  3.216   56.799  1.00 28.25 ? 45   PHE L CB  1 
ATOM   12607 C  CG  . PHE L  1 45  ? 48.882  3.122   55.563  1.00 27.19 ? 45   PHE L CG  1 
ATOM   12608 C  CD1 . PHE L  1 45  ? 48.805  4.093   54.574  1.00 30.75 ? 45   PHE L CD1 1 
ATOM   12609 C  CD2 . PHE L  1 45  ? 49.795  2.084   55.416  1.00 28.28 ? 45   PHE L CD2 1 
ATOM   12610 C  CE1 . PHE L  1 45  ? 49.605  4.011   53.442  1.00 33.27 ? 45   PHE L CE1 1 
ATOM   12611 C  CE2 . PHE L  1 45  ? 50.602  2.001   54.298  1.00 29.77 ? 45   PHE L CE2 1 
ATOM   12612 C  CZ  . PHE L  1 45  ? 50.509  2.965   53.309  1.00 32.66 ? 45   PHE L CZ  1 
ATOM   12613 N  N   . HIS L  1 46  ? 45.123  1.813   55.217  1.00 27.80 ? 46   HIS L N   1 
ATOM   12614 C  CA  . HIS L  1 46  ? 44.539  0.515   54.891  1.00 26.56 ? 46   HIS L CA  1 
ATOM   12615 C  C   . HIS L  1 46  ? 44.504  0.184   53.398  1.00 30.10 ? 46   HIS L C   1 
ATOM   12616 O  O   . HIS L  1 46  ? 44.473  1.073   52.534  1.00 25.28 ? 46   HIS L O   1 
ATOM   12617 C  CB  . HIS L  1 46  ? 43.116  0.378   55.452  1.00 29.02 ? 46   HIS L CB  1 
ATOM   12618 C  CG  . HIS L  1 46  ? 42.894  1.081   56.755  1.00 26.76 ? 46   HIS L CG  1 
ATOM   12619 N  ND1 . HIS L  1 46  ? 42.284  2.315   56.839  1.00 25.84 ? 46   HIS L ND1 1 
ATOM   12620 C  CD2 . HIS L  1 46  ? 43.179  0.714   58.027  1.00 27.08 ? 46   HIS L CD2 1 
ATOM   12621 C  CE1 . HIS L  1 46  ? 42.216  2.684   58.105  1.00 28.29 ? 46   HIS L CE1 1 
ATOM   12622 N  NE2 . HIS L  1 46  ? 42.757  1.733   58.846  1.00 28.29 ? 46   HIS L NE2 1 
ATOM   12623 N  N   . VAL L  1 47  ? 44.498  -1.122  53.126  1.00 30.82 ? 47   VAL L N   1 
ATOM   12624 C  CA  . VAL L  1 47  ? 44.199  -1.654  51.807  1.00 29.89 ? 47   VAL L CA  1 
ATOM   12625 C  C   . VAL L  1 47  ? 42.689  -1.794  51.687  1.00 29.97 ? 47   VAL L C   1 
ATOM   12626 O  O   . VAL L  1 47  ? 42.060  -2.529  52.456  1.00 29.97 ? 47   VAL L O   1 
ATOM   12627 C  CB  . VAL L  1 47  ? 44.849  -3.048  51.572  1.00 30.22 ? 47   VAL L CB  1 
ATOM   12628 C  CG1 . VAL L  1 47  ? 44.751  -3.446  50.101  1.00 29.99 ? 47   VAL L CG1 1 
ATOM   12629 C  CG2 . VAL L  1 47  ? 46.300  -3.050  52.017  1.00 31.45 ? 47   VAL L CG2 1 
ATOM   12630 N  N   . HIS L  1 48  ? 42.113  -1.072  50.727  1.00 31.86 ? 48   HIS L N   1 
ATOM   12631 C  CA  . HIS L  1 48  ? 40.686  -1.164  50.427  1.00 30.13 ? 48   HIS L CA  1 
ATOM   12632 C  C   . HIS L  1 48  ? 40.436  -2.104  49.241  1.00 29.44 ? 48   HIS L C   1 
ATOM   12633 O  O   . HIS L  1 48  ? 41.346  -2.412  48.472  1.00 26.82 ? 48   HIS L O   1 
ATOM   12634 C  CB  . HIS L  1 48  ? 40.098  0.226   50.178  1.00 28.91 ? 48   HIS L CB  1 
ATOM   12635 C  CG  . HIS L  1 48  ? 40.014  1.072   51.412  1.00 28.89 ? 48   HIS L CG  1 
ATOM   12636 N  ND1 . HIS L  1 48  ? 38.832  1.628   51.856  1.00 29.40 ? 48   HIS L ND1 1 
ATOM   12637 C  CD2 . HIS L  1 48  ? 40.963  1.449   52.303  1.00 28.75 ? 48   HIS L CD2 1 
ATOM   12638 C  CE1 . HIS L  1 48  ? 39.060  2.314   52.961  1.00 28.01 ? 48   HIS L CE1 1 
ATOM   12639 N  NE2 . HIS L  1 48  ? 40.343  2.221   53.256  1.00 25.40 ? 48   HIS L NE2 1 
ATOM   12640 N  N   . GLU L  1 49  ? 39.192  -2.542  49.089  1.00 30.43 ? 49   GLU L N   1 
ATOM   12641 C  CA  . GLU L  1 49  ? 38.894  -3.701  48.254  1.00 28.98 ? 49   GLU L CA  1 
ATOM   12642 C  C   . GLU L  1 49  ? 39.061  -3.487  46.745  1.00 32.24 ? 49   GLU L C   1 
ATOM   12643 O  O   . GLU L  1 49  ? 39.537  -4.374  46.029  1.00 32.29 ? 49   GLU L O   1 
ATOM   12644 C  CB  . GLU L  1 49  ? 37.492  -4.213  48.550  1.00 25.46 ? 49   GLU L CB  1 
ATOM   12645 C  CG  . GLU L  1 49  ? 37.275  -5.601  48.035  1.00 28.12 ? 49   GLU L CG  1 
ATOM   12646 C  CD  . GLU L  1 49  ? 35.866  -6.086  48.260  1.00 33.11 ? 49   GLU L CD  1 
ATOM   12647 O  OE1 . GLU L  1 49  ? 35.196  -5.540  49.164  1.00 30.70 ? 49   GLU L OE1 1 
ATOM   12648 O  OE2 . GLU L  1 49  ? 35.436  -7.013  47.532  1.00 34.10 ? 49   GLU L OE2 1 
ATOM   12649 N  N   . PHE L  1 50  ? 38.672  -2.314  46.261  1.00 31.45 ? 50   PHE L N   1 
ATOM   12650 C  CA  . PHE L  1 50  ? 38.566  -2.103  44.827  1.00 28.20 ? 50   PHE L CA  1 
ATOM   12651 C  C   . PHE L  1 50  ? 39.598  -1.126  44.276  1.00 30.15 ? 50   PHE L C   1 
ATOM   12652 O  O   . PHE L  1 50  ? 39.794  -0.036  44.817  1.00 30.15 ? 50   PHE L O   1 
ATOM   12653 C  CB  . PHE L  1 50  ? 37.139  -1.665  44.464  1.00 29.78 ? 50   PHE L CB  1 
ATOM   12654 C  CG  . PHE L  1 50  ? 36.083  -2.661  44.872  1.00 29.42 ? 50   PHE L CG  1 
ATOM   12655 C  CD1 . PHE L  1 50  ? 36.194  -3.997  44.506  1.00 30.15 ? 50   PHE L CD1 1 
ATOM   12656 C  CD2 . PHE L  1 50  ? 34.981  -2.266  45.600  1.00 28.12 ? 50   PHE L CD2 1 
ATOM   12657 C  CE1 . PHE L  1 50  ? 35.233  -4.916  44.872  1.00 29.13 ? 50   PHE L CE1 1 
ATOM   12658 C  CE2 . PHE L  1 50  ? 34.019  -3.178  45.967  1.00 29.34 ? 50   PHE L CE2 1 
ATOM   12659 C  CZ  . PHE L  1 50  ? 34.147  -4.506  45.606  1.00 29.22 ? 50   PHE L CZ  1 
ATOM   12660 N  N   . GLY L  1 51  ? 40.256  -1.536  43.193  1.00 28.78 ? 51   GLY L N   1 
ATOM   12661 C  CA  . GLY L  1 51  ? 41.203  -0.694  42.487  1.00 28.44 ? 51   GLY L CA  1 
ATOM   12662 C  C   . GLY L  1 51  ? 40.458  0.159   41.483  1.00 30.22 ? 51   GLY L C   1 
ATOM   12663 O  O   . GLY L  1 51  ? 40.777  0.213   40.285  1.00 30.91 ? 51   GLY L O   1 
ATOM   12664 N  N   . ASP L  1 52  ? 39.447  0.836   42.000  1.00 28.12 ? 52   ASP L N   1 
ATOM   12665 C  CA  . ASP L  1 52  ? 38.531  1.611   41.194  1.00 29.73 ? 52   ASP L CA  1 
ATOM   12666 C  C   . ASP L  1 52  ? 38.641  3.047   41.698  1.00 31.73 ? 52   ASP L C   1 
ATOM   12667 O  O   . ASP L  1 52  ? 38.464  3.320   42.884  1.00 34.16 ? 52   ASP L O   1 
ATOM   12668 C  CB  . ASP L  1 52  ? 37.113  1.035   41.362  1.00 28.17 ? 52   ASP L CB  1 
ATOM   12669 C  CG  . ASP L  1 52  ? 36.066  1.803   40.601  1.00 28.64 ? 52   ASP L CG  1 
ATOM   12670 O  OD1 . ASP L  1 52  ? 36.314  2.977   40.262  1.00 29.84 ? 52   ASP L OD1 1 
ATOM   12671 O  OD2 . ASP L  1 52  ? 34.984  1.228   40.346  1.00 30.25 ? 52   ASP L OD2 1 
ATOM   12672 N  N   . ASN L  1 53  ? 38.962  3.962   40.798  1.00 32.33 ? 53   ASN L N   1 
ATOM   12673 C  CA  . ASN L  1 53  ? 39.228  5.335   41.180  1.00 32.08 ? 53   ASN L CA  1 
ATOM   12674 C  C   . ASN L  1 53  ? 38.274  6.228   40.422  1.00 32.96 ? 53   ASN L C   1 
ATOM   12675 O  O   . ASN L  1 53  ? 38.491  7.432   40.283  1.00 34.80 ? 53   ASN L O   1 
ATOM   12676 C  CB  . ASN L  1 53  ? 40.676  5.685   40.836  1.00 37.96 ? 53   ASN L CB  1 
ATOM   12677 C  CG  . ASN L  1 53  ? 41.041  7.111   41.201  1.00 42.15 ? 53   ASN L CG  1 
ATOM   12678 O  OD1 . ASN L  1 53  ? 40.448  7.706   42.107  1.00 43.14 ? 53   ASN L OD1 1 
ATOM   12679 N  ND2 . ASN L  1 53  ? 42.032  7.667   40.498  1.00 46.34 ? 53   ASN L ND2 1 
ATOM   12680 N  N   . THR L  1 54  ? 37.204  5.622   39.924  1.00 32.96 ? 54   THR L N   1 
ATOM   12681 C  CA  . THR L  1 54  ? 36.299  6.318   39.031  1.00 33.19 ? 54   THR L CA  1 
ATOM   12682 C  C   . THR L  1 54  ? 35.601  7.473   39.751  1.00 36.36 ? 54   THR L C   1 
ATOM   12683 O  O   . THR L  1 54  ? 35.319  8.514   39.148  1.00 35.22 ? 54   THR L O   1 
ATOM   12684 C  CB  . THR L  1 54  ? 35.314  5.338   38.364  1.00 32.67 ? 54   THR L CB  1 
ATOM   12685 O  OG1 . THR L  1 54  ? 34.524  4.683   39.363  1.00 37.39 ? 54   THR L OG1 1 
ATOM   12686 C  CG2 . THR L  1 54  ? 36.088  4.282   37.583  1.00 29.71 ? 54   THR L CG2 1 
ATOM   12687 N  N   . ALA L  1 55  ? 35.358  7.298   41.049  1.00 37.23 ? 55   ALA L N   1 
ATOM   12688 C  CA  . ALA L  1 55  ? 34.766  8.354   41.874  1.00 38.79 ? 55   ALA L CA  1 
ATOM   12689 C  C   . ALA L  1 55  ? 35.673  8.722   43.048  1.00 37.26 ? 55   ALA L C   1 
ATOM   12690 O  O   . ALA L  1 55  ? 35.232  8.760   44.196  1.00 38.94 ? 55   ALA L O   1 
ATOM   12691 C  CB  . ALA L  1 55  ? 33.388  7.934   42.373  1.00 35.61 ? 55   ALA L CB  1 
ATOM   12692 N  N   . GLY L  1 56  ? 36.939  8.995   42.749  1.00 37.86 ? 56   GLY L N   1 
ATOM   12693 C  CA  . GLY L  1 56  ? 37.936  9.239   43.775  1.00 34.82 ? 56   GLY L CA  1 
ATOM   12694 C  C   . GLY L  1 56  ? 38.174  8.030   44.664  1.00 37.23 ? 56   GLY L C   1 
ATOM   12695 O  O   . GLY L  1 56  ? 37.922  6.887   44.278  1.00 33.40 ? 56   GLY L O   1 
ATOM   12696 N  N   . CYS L  1 57  ? 38.653  8.298   45.874  1.00 39.72 ? 57   CYS L N   1 
ATOM   12697 C  CA  . CYS L  1 57  ? 38.955  7.265   46.866  1.00 37.91 ? 57   CYS L CA  1 
ATOM   12698 C  C   . CYS L  1 57  ? 37.709  6.524   47.346  1.00 33.77 ? 57   CYS L C   1 
ATOM   12699 O  O   . CYS L  1 57  ? 37.812  5.443   47.940  1.00 30.42 ? 57   CYS L O   1 
ATOM   12700 C  CB  . CYS L  1 57  ? 39.679  7.890   48.063  1.00 37.18 ? 57   CYS L CB  1 
ATOM   12701 S  SG  . CYS L  1 57  ? 41.086  8.950   47.603  1.00 48.60 ? 57   CYS L SG  1 
ATOM   12702 N  N   . THR L  1 58  ? 36.548  7.128   47.085  1.00 33.12 ? 58   THR L N   1 
ATOM   12703 C  CA  . THR L  1 58  ? 35.240  6.591   47.460  1.00 32.38 ? 58   THR L CA  1 
ATOM   12704 C  C   . THR L  1 58  ? 34.985  5.212   46.875  1.00 31.53 ? 58   THR L C   1 
ATOM   12705 O  O   . THR L  1 58  ? 34.509  4.313   47.572  1.00 31.17 ? 58   THR L O   1 
ATOM   12706 C  CB  . THR L  1 58  ? 34.092  7.515   46.966  1.00 36.68 ? 58   THR L CB  1 
ATOM   12707 O  OG1 . THR L  1 58  ? 34.400  8.886   47.254  1.00 42.21 ? 58   THR L OG1 1 
ATOM   12708 C  CG2 . THR L  1 58  ? 32.769  7.147   47.618  1.00 35.93 ? 58   THR L CG2 1 
ATOM   12709 N  N   . SER L  1 59  ? 35.288  5.059   45.586  1.00 31.66 ? 59   SER L N   1 
ATOM   12710 C  CA  . SER L  1 59  ? 34.968  3.842   44.843  1.00 28.63 ? 59   SER L CA  1 
ATOM   12711 C  C   . SER L  1 59  ? 35.911  2.688   45.137  1.00 30.51 ? 59   SER L C   1 
ATOM   12712 O  O   . SER L  1 59  ? 35.836  1.638   44.504  1.00 29.72 ? 59   SER L O   1 
ATOM   12713 C  CB  . SER L  1 59  ? 34.920  4.129   43.347  1.00 30.68 ? 59   SER L CB  1 
ATOM   12714 O  OG  . SER L  1 59  ? 35.641  5.304   43.039  1.00 31.26 ? 59   SER L OG  1 
ATOM   12715 N  N   . ALA L  1 60  ? 36.778  2.888   46.124  1.00 29.65 ? 60   ALA L N   1 
ATOM   12716 C  CA  . ALA L  1 60  ? 37.710  1.862   46.570  1.00 30.88 ? 60   ALA L CA  1 
ATOM   12717 C  C   . ALA L  1 60  ? 37.010  0.848   47.460  1.00 29.36 ? 60   ALA L C   1 
ATOM   12718 O  O   . ALA L  1 60  ? 37.542  -0.235  47.731  1.00 28.69 ? 60   ALA L O   1 
ATOM   12719 C  CB  . ALA L  1 60  ? 38.878  2.500   47.318  1.00 29.98 ? 60   ALA L CB  1 
ATOM   12720 N  N   . GLY L  1 61  ? 35.818  1.206   47.922  1.00 28.30 ? 61   GLY L N   1 
ATOM   12721 C  CA  . GLY L  1 61  ? 35.046  0.323   48.771  1.00 27.85 ? 61   GLY L CA  1 
ATOM   12722 C  C   . GLY L  1 61  ? 35.509  0.289   50.218  1.00 30.77 ? 61   GLY L C   1 
ATOM   12723 O  O   . GLY L  1 61  ? 36.137  1.229   50.716  1.00 31.05 ? 61   GLY L O   1 
ATOM   12724 N  N   . PRO L  1 62  ? 35.197  -0.810  50.910  1.00 30.04 ? 62   PRO L N   1 
ATOM   12725 C  CA  . PRO L  1 62  ? 35.555  -1.012  52.312  1.00 28.70 ? 62   PRO L CA  1 
ATOM   12726 C  C   . PRO L  1 62  ? 37.024  -1.385  52.459  1.00 30.11 ? 62   PRO L C   1 
ATOM   12727 O  O   . PRO L  1 62  ? 37.757  -1.455  51.479  1.00 31.64 ? 62   PRO L O   1 
ATOM   12728 C  CB  . PRO L  1 62  ? 34.709  -2.226  52.719  1.00 29.42 ? 62   PRO L CB  1 
ATOM   12729 C  CG  . PRO L  1 62  ? 33.887  -2.600  51.514  1.00 29.14 ? 62   PRO L CG  1 
ATOM   12730 C  CD  . PRO L  1 62  ? 34.544  -1.995  50.336  1.00 29.80 ? 62   PRO L CD  1 
ATOM   12731 N  N   . HIS L  1 63  ? 37.452  -1.629  53.687  1.00 29.19 ? 63   HIS L N   1 
ATOM   12732 C  CA  . HIS L  1 63  ? 38.733  -2.258  53.903  1.00 30.18 ? 63   HIS L CA  1 
ATOM   12733 C  C   . HIS L  1 63  ? 38.642  -3.668  53.317  1.00 33.70 ? 63   HIS L C   1 
ATOM   12734 O  O   . HIS L  1 63  ? 37.630  -4.360  53.488  1.00 32.76 ? 63   HIS L O   1 
ATOM   12735 C  CB  . HIS L  1 63  ? 39.040  -2.291  55.396  1.00 30.87 ? 63   HIS L CB  1 
ATOM   12736 C  CG  . HIS L  1 63  ? 39.138  -0.928  56.014  1.00 27.59 ? 63   HIS L CG  1 
ATOM   12737 N  ND1 . HIS L  1 63  ? 39.479  -0.729  57.335  1.00 25.72 ? 63   HIS L ND1 1 
ATOM   12738 C  CD2 . HIS L  1 63  ? 38.965  0.304   55.483  1.00 27.45 ? 63   HIS L CD2 1 
ATOM   12739 C  CE1 . HIS L  1 63  ? 39.493  0.566   57.593  1.00 28.67 ? 63   HIS L CE1 1 
ATOM   12740 N  NE2 . HIS L  1 63  ? 39.184  1.216   56.485  1.00 26.79 ? 63   HIS L NE2 1 
ATOM   12741 N  N   . PHE L  1 64  ? 39.683  -4.076  52.598  1.00 32.42 ? 64   PHE L N   1 
ATOM   12742 C  CA  . PHE L  1 64  ? 39.738  -5.415  52.025  1.00 29.87 ? 64   PHE L CA  1 
ATOM   12743 C  C   . PHE L  1 64  ? 39.431  -6.438  53.113  1.00 29.88 ? 64   PHE L C   1 
ATOM   12744 O  O   . PHE L  1 64  ? 40.164  -6.543  54.088  1.00 32.41 ? 64   PHE L O   1 
ATOM   12745 C  CB  . PHE L  1 64  ? 41.116  -5.657  51.394  1.00 32.51 ? 64   PHE L CB  1 
ATOM   12746 C  CG  . PHE L  1 64  ? 41.250  -6.994  50.715  1.00 35.01 ? 64   PHE L CG  1 
ATOM   12747 C  CD1 . PHE L  1 64  ? 40.276  -7.439  49.824  1.00 35.64 ? 64   PHE L CD1 1 
ATOM   12748 C  CD2 . PHE L  1 64  ? 42.353  -7.802  50.959  1.00 34.07 ? 64   PHE L CD2 1 
ATOM   12749 C  CE1 . PHE L  1 64  ? 40.393  -8.677  49.201  1.00 35.86 ? 64   PHE L CE1 1 
ATOM   12750 C  CE2 . PHE L  1 64  ? 42.480  -9.039  50.342  1.00 35.24 ? 64   PHE L CE2 1 
ATOM   12751 C  CZ  . PHE L  1 64  ? 41.499  -9.477  49.459  1.00 35.95 ? 64   PHE L CZ  1 
ATOM   12752 N  N   . ASN L  1 65  ? 38.333  -7.174  52.960  1.00 33.13 ? 65   ASN L N   1 
ATOM   12753 C  CA  . ASN L  1 65  ? 37.843  -8.037  54.036  1.00 31.82 ? 65   ASN L CA  1 
ATOM   12754 C  C   . ASN L  1 65  ? 37.421  -9.435  53.566  1.00 31.91 ? 65   ASN L C   1 
ATOM   12755 O  O   . ASN L  1 65  ? 36.306  -9.871  53.843  1.00 30.91 ? 65   ASN L O   1 
ATOM   12756 C  CB  . ASN L  1 65  ? 36.685  -7.337  54.764  1.00 29.76 ? 65   ASN L CB  1 
ATOM   12757 C  CG  . ASN L  1 65  ? 36.225  -8.074  56.027  1.00 30.51 ? 65   ASN L CG  1 
ATOM   12758 O  OD1 . ASN L  1 65  ? 36.996  -8.783  56.684  1.00 32.17 ? 65   ASN L OD1 1 
ATOM   12759 N  ND2 . ASN L  1 65  ? 34.960  -7.886  56.379  1.00 29.25 ? 65   ASN L ND2 1 
ATOM   12760 N  N   . PRO L  1 66  ? 38.330  -10.152 52.877  1.00 32.20 ? 66   PRO L N   1 
ATOM   12761 C  CA  . PRO L  1 66  ? 38.072  -11.485 52.310  1.00 32.23 ? 66   PRO L CA  1 
ATOM   12762 C  C   . PRO L  1 66  ? 37.379  -12.426 53.294  1.00 34.56 ? 66   PRO L C   1 
ATOM   12763 O  O   . PRO L  1 66  ? 36.466  -13.152 52.896  1.00 37.81 ? 66   PRO L O   1 
ATOM   12764 C  CB  . PRO L  1 66  ? 39.476  -12.039 52.035  1.00 37.54 ? 66   PRO L CB  1 
ATOM   12765 C  CG  . PRO L  1 66  ? 40.389  -10.883 52.014  1.00 35.82 ? 66   PRO L CG  1 
ATOM   12766 C  CD  . PRO L  1 66  ? 39.737  -9.737  52.729  1.00 34.16 ? 66   PRO L CD  1 
ATOM   12767 N  N   . LEU L  1 67  ? 37.824  -12.416 54.553  1.00 34.10 ? 67   LEU L N   1 
ATOM   12768 C  CA  . LEU L  1 67  ? 37.389  -13.385 55.563  1.00 33.20 ? 67   LEU L CA  1 
ATOM   12769 C  C   . LEU L  1 67  ? 36.222  -12.881 56.400  1.00 36.14 ? 67   LEU L C   1 
ATOM   12770 O  O   . LEU L  1 67  ? 35.786  -13.546 57.341  1.00 37.21 ? 67   LEU L O   1 
ATOM   12771 C  CB  . LEU L  1 67  ? 38.552  -13.750 56.480  1.00 32.88 ? 67   LEU L CB  1 
ATOM   12772 C  CG  . LEU L  1 67  ? 39.620  -14.596 55.795  1.00 34.71 ? 67   LEU L CG  1 
ATOM   12773 C  CD1 . LEU L  1 67  ? 40.963  -14.375 56.428  1.00 34.59 ? 67   LEU L CD1 1 
ATOM   12774 C  CD2 . LEU L  1 67  ? 39.228  -16.052 55.842  1.00 33.95 ? 67   LEU L CD2 1 
ATOM   12775 N  N   . SER L  1 68  ? 35.726  -11.698 56.055  1.00 34.40 ? 68   SER L N   1 
ATOM   12776 C  CA  . SER L  1 68  ? 34.541  -11.160 56.694  1.00 32.59 ? 68   SER L CA  1 
ATOM   12777 C  C   . SER L  1 68  ? 34.694  -11.138 58.209  1.00 36.62 ? 68   SER L C   1 
ATOM   12778 O  O   . SER L  1 68  ? 33.858  -11.678 58.931  1.00 38.07 ? 68   SER L O   1 
ATOM   12779 C  CB  . SER L  1 68  ? 33.316  -11.984 56.292  1.00 36.12 ? 68   SER L CB  1 
ATOM   12780 O  OG  . SER L  1 68  ? 33.032  -11.837 54.906  1.00 40.38 ? 68   SER L OG  1 
ATOM   12781 N  N   . ARG L  1 69  ? 35.773  -10.522 58.687  1.00 36.49 ? 69   ARG L N   1 
ATOM   12782 C  CA  . ARG L  1 69  ? 35.978  -10.348 60.120  1.00 35.28 ? 69   ARG L CA  1 
ATOM   12783 C  C   . ARG L  1 69  ? 35.794  -8.878  60.493  1.00 35.25 ? 69   ARG L C   1 
ATOM   12784 O  O   . ARG L  1 69  ? 35.476  -8.059  59.634  1.00 36.78 ? 69   ARG L O   1 
ATOM   12785 C  CB  . ARG L  1 69  ? 37.355  -10.864 60.541  1.00 35.87 ? 69   ARG L CB  1 
ATOM   12786 C  CG  . ARG L  1 69  ? 37.456  -12.385 60.577  1.00 36.33 ? 69   ARG L CG  1 
ATOM   12787 C  CD  . ARG L  1 69  ? 38.864  -12.813 60.937  1.00 43.76 ? 69   ARG L CD  1 
ATOM   12788 N  NE  . ARG L  1 69  ? 39.089  -14.243 60.730  1.00 48.06 ? 69   ARG L NE  1 
ATOM   12789 C  CZ  . ARG L  1 69  ? 40.249  -14.769 60.338  1.00 45.77 ? 69   ARG L CZ  1 
ATOM   12790 N  NH1 . ARG L  1 69  ? 41.294  -13.980 60.094  1.00 44.50 ? 69   ARG L NH1 1 
ATOM   12791 N  NH2 . ARG L  1 69  ? 40.359  -16.084 60.175  1.00 40.96 ? 69   ARG L NH2 1 
ATOM   12792 N  N   . LYS L  1 70  ? 35.981  -8.546  61.767  1.00 34.88 ? 70   LYS L N   1 
ATOM   12793 C  CA  . LYS L  1 70  ? 35.825  -7.166  62.228  1.00 32.87 ? 70   LYS L CA  1 
ATOM   12794 C  C   . LYS L  1 70  ? 37.119  -6.363  62.101  1.00 30.03 ? 70   LYS L C   1 
ATOM   12795 O  O   . LYS L  1 70  ? 38.208  -6.932  62.080  1.00 31.28 ? 70   LYS L O   1 
ATOM   12796 C  CB  . LYS L  1 70  ? 35.314  -7.139  63.677  1.00 34.10 ? 70   LYS L CB  1 
ATOM   12797 C  CG  . LYS L  1 70  ? 33.807  -6.988  63.791  1.00 36.97 ? 70   LYS L CG  1 
ATOM   12798 C  CD  . LYS L  1 70  ? 33.221  -7.915  64.837  1.00 42.05 ? 70   LYS L CD  1 
ATOM   12799 C  CE  . LYS L  1 70  ? 31.693  -7.780  64.907  1.00 50.97 ? 70   LYS L CE  1 
ATOM   12800 N  NZ  . LYS L  1 70  ? 31.008  -7.952  63.581  1.00 46.41 ? 70   LYS L NZ  1 
ATOM   12801 N  N   . HIS L  1 71  ? 36.990  -5.039  62.012  1.00 28.26 ? 71   HIS L N   1 
ATOM   12802 C  CA  . HIS L  1 71  ? 38.153  -4.149  61.985  1.00 27.71 ? 71   HIS L CA  1 
ATOM   12803 C  C   . HIS L  1 71  ? 39.067  -4.361  63.171  1.00 28.50 ? 71   HIS L C   1 
ATOM   12804 O  O   . HIS L  1 71  ? 38.606  -4.515  64.308  1.00 30.50 ? 71   HIS L O   1 
ATOM   12805 C  CB  . HIS L  1 71  ? 37.731  -2.684  61.972  1.00 27.34 ? 71   HIS L CB  1 
ATOM   12806 C  CG  . HIS L  1 71  ? 38.884  -1.731  61.888  1.00 28.44 ? 71   HIS L CG  1 
ATOM   12807 N  ND1 . HIS L  1 71  ? 39.691  -1.637  60.775  1.00 28.23 ? 71   HIS L ND1 1 
ATOM   12808 C  CD2 . HIS L  1 71  ? 39.357  -0.823  62.772  1.00 27.38 ? 71   HIS L CD2 1 
ATOM   12809 C  CE1 . HIS L  1 71  ? 40.613  -0.713  60.976  1.00 27.64 ? 71   HIS L CE1 1 
ATOM   12810 N  NE2 . HIS L  1 71  ? 40.436  -0.210  62.183  1.00 28.82 ? 71   HIS L NE2 1 
ATOM   12811 N  N   . GLY L  1 72  ? 40.371  -4.349  62.911  1.00 29.63 ? 72   GLY L N   1 
ATOM   12812 C  CA  . GLY L  1 72  ? 41.342  -4.518  63.973  1.00 28.32 ? 72   GLY L CA  1 
ATOM   12813 C  C   . GLY L  1 72  ? 42.649  -3.817  63.689  1.00 29.11 ? 72   GLY L C   1 
ATOM   12814 O  O   . GLY L  1 72  ? 42.819  -3.194  62.641  1.00 27.48 ? 72   GLY L O   1 
ATOM   12815 N  N   . GLY L  1 73  ? 43.571  -3.910  64.642  1.00 32.69 ? 73   GLY L N   1 
ATOM   12816 C  CA  . GLY L  1 73  ? 44.938  -3.475  64.421  1.00 34.77 ? 73   GLY L CA  1 
ATOM   12817 C  C   . GLY L  1 73  ? 45.682  -4.530  63.619  1.00 33.78 ? 73   GLY L C   1 
ATOM   12818 O  O   . GLY L  1 73  ? 45.184  -5.650  63.450  1.00 33.93 ? 73   GLY L O   1 
ATOM   12819 N  N   . PRO L  1 74  ? 46.877  -4.183  63.117  1.00 32.00 ? 74   PRO L N   1 
ATOM   12820 C  CA  . PRO L  1 74  ? 47.642  -5.146  62.319  1.00 31.10 ? 74   PRO L CA  1 
ATOM   12821 C  C   . PRO L  1 74  ? 47.919  -6.425  63.109  1.00 31.72 ? 74   PRO L C   1 
ATOM   12822 O  O   . PRO L  1 74  ? 47.920  -7.512  62.526  1.00 32.06 ? 74   PRO L O   1 
ATOM   12823 C  CB  . PRO L  1 74  ? 48.952  -4.404  62.031  1.00 32.36 ? 74   PRO L CB  1 
ATOM   12824 C  CG  . PRO L  1 74  ? 48.631  -2.961  62.192  1.00 34.33 ? 74   PRO L CG  1 
ATOM   12825 C  CD  . PRO L  1 74  ? 47.557  -2.880  63.232  1.00 31.67 ? 74   PRO L CD  1 
ATOM   12826 N  N   . LYS L  1 75  ? 48.135  -6.292  64.419  1.00 33.70 ? 75   LYS L N   1 
ATOM   12827 C  CA  . LYS L  1 75  ? 48.569  -7.418  65.256  1.00 32.42 ? 75   LYS L CA  1 
ATOM   12828 C  C   . LYS L  1 75  ? 47.461  -8.024  66.123  1.00 32.91 ? 75   LYS L C   1 
ATOM   12829 O  O   . LYS L  1 75  ? 47.741  -8.818  67.025  1.00 32.60 ? 75   LYS L O   1 
ATOM   12830 C  CB  . LYS L  1 75  ? 49.774  -7.022  66.113  1.00 33.26 ? 75   LYS L CB  1 
ATOM   12831 C  CG  . LYS L  1 75  ? 51.021  -6.681  65.299  1.00 35.52 ? 75   LYS L CG  1 
ATOM   12832 C  CD  . LYS L  1 75  ? 51.924  -7.908  65.035  1.00 41.85 ? 75   LYS L CD  1 
ATOM   12833 C  CE  . LYS L  1 75  ? 52.535  -8.472  66.341  1.00 44.98 ? 75   LYS L CE  1 
ATOM   12834 N  NZ  . LYS L  1 75  ? 53.963  -8.935  66.214  1.00 43.20 ? 75   LYS L NZ  1 
ATOM   12835 N  N   . ASP L  1 76  ? 46.213  -7.655  65.833  1.00 32.60 ? 76   ASP L N   1 
ATOM   12836 C  CA  . ASP L  1 76  ? 45.040  -8.271  66.455  1.00 32.21 ? 76   ASP L CA  1 
ATOM   12837 C  C   . ASP L  1 76  ? 44.670  -9.537  65.699  1.00 34.81 ? 76   ASP L C   1 
ATOM   12838 O  O   . ASP L  1 76  ? 44.893  -9.625  64.491  1.00 35.80 ? 76   ASP L O   1 
ATOM   12839 C  CB  . ASP L  1 76  ? 43.856  -7.309  66.422  1.00 31.07 ? 76   ASP L CB  1 
ATOM   12840 C  CG  . ASP L  1 76  ? 43.994  -6.185  67.414  1.00 31.25 ? 76   ASP L CG  1 
ATOM   12841 O  OD1 . ASP L  1 76  ? 44.349  -6.475  68.574  1.00 35.18 ? 76   ASP L OD1 1 
ATOM   12842 O  OD2 . ASP L  1 76  ? 43.755  -5.016  67.036  1.00 30.16 ? 76   ASP L OD2 1 
ATOM   12843 N  N   . GLU L  1 77  ? 44.108  -10.518 66.400  1.00 37.85 ? 77   GLU L N   1 
ATOM   12844 C  CA  . GLU L  1 77  ? 43.681  -11.750 65.746  1.00 40.40 ? 77   GLU L CA  1 
ATOM   12845 C  C   . GLU L  1 77  ? 42.501  -11.432 64.840  1.00 37.74 ? 77   GLU L C   1 
ATOM   12846 O  O   . GLU L  1 77  ? 42.414  -11.922 63.712  1.00 41.70 ? 77   GLU L O   1 
ATOM   12847 C  CB  . GLU L  1 77  ? 43.293  -12.811 66.776  1.00 48.59 ? 77   GLU L CB  1 
ATOM   12848 C  CG  . GLU L  1 77  ? 43.561  -14.253 66.324  1.00 59.15 ? 77   GLU L CG  1 
ATOM   12849 C  CD  . GLU L  1 77  ? 42.746  -14.685 65.099  1.00 58.24 ? 77   GLU L CD  1 
ATOM   12850 O  OE1 . GLU L  1 77  ? 43.135  -15.684 64.451  1.00 61.41 ? 77   GLU L OE1 1 
ATOM   12851 O  OE2 . GLU L  1 77  ? 41.716  -14.043 64.789  1.00 53.32 ? 77   GLU L OE2 1 
ATOM   12852 N  N   . GLU L  1 78  ? 41.599  -10.601 65.350  1.00 36.24 ? 78   GLU L N   1 
ATOM   12853 C  CA  . GLU L  1 78  ? 40.484  -10.081 64.569  1.00 37.45 ? 78   GLU L CA  1 
ATOM   12854 C  C   . GLU L  1 78  ? 40.879  -8.795  63.842  1.00 36.15 ? 78   GLU L C   1 
ATOM   12855 O  O   . GLU L  1 78  ? 41.045  -7.742  64.466  1.00 34.95 ? 78   GLU L O   1 
ATOM   12856 C  CB  . GLU L  1 78  ? 39.275  -9.812  65.465  1.00 37.23 ? 78   GLU L CB  1 
ATOM   12857 C  CG  . GLU L  1 78  ? 38.360  -11.001 65.645  1.00 41.70 ? 78   GLU L CG  1 
ATOM   12858 C  CD  . GLU L  1 78  ? 37.368  -11.143 64.508  1.00 42.87 ? 78   GLU L CD  1 
ATOM   12859 O  OE1 . GLU L  1 78  ? 36.616  -10.180 64.246  1.00 38.53 ? 78   GLU L OE1 1 
ATOM   12860 O  OE2 . GLU L  1 78  ? 37.337  -12.229 63.883  1.00 51.68 ? 78   GLU L OE2 1 
ATOM   12861 N  N   . ARG L  1 79  ? 41.027  -8.897  62.524  1.00 31.70 ? 79   ARG L N   1 
ATOM   12862 C  CA  . ARG L  1 79  ? 41.316  -7.754  61.671  1.00 33.28 ? 79   ARG L CA  1 
ATOM   12863 C  C   . ARG L  1 79  ? 40.902  -8.086  60.245  1.00 31.26 ? 79   ARG L C   1 
ATOM   12864 O  O   . ARG L  1 79  ? 40.816  -9.261  59.878  1.00 33.14 ? 79   ARG L O   1 
ATOM   12865 C  CB  . ARG L  1 79  ? 42.809  -7.413  61.701  1.00 31.78 ? 79   ARG L CB  1 
ATOM   12866 C  CG  . ARG L  1 79  ? 43.703  -8.571  61.295  1.00 31.96 ? 79   ARG L CG  1 
ATOM   12867 C  CD  . ARG L  1 79  ? 45.116  -8.111  60.964  1.00 31.30 ? 79   ARG L CD  1 
ATOM   12868 N  NE  . ARG L  1 79  ? 45.241  -7.614  59.591  1.00 32.14 ? 79   ARG L NE  1 
ATOM   12869 C  CZ  . ARG L  1 79  ? 46.403  -7.354  58.993  1.00 31.37 ? 79   ARG L CZ  1 
ATOM   12870 N  NH1 . ARG L  1 79  ? 47.545  -7.542  59.643  1.00 31.86 ? 79   ARG L NH1 1 
ATOM   12871 N  NH2 . ARG L  1 79  ? 46.428  -6.908  57.748  1.00 30.15 ? 79   ARG L NH2 1 
ATOM   12872 N  N   . HIS L  1 80  ? 40.629  -7.054  59.454  1.00 28.56 ? 80   HIS L N   1 
ATOM   12873 C  CA  . HIS L  1 80  ? 40.456  -7.219  58.021  1.00 30.27 ? 80   HIS L CA  1 
ATOM   12874 C  C   . HIS L  1 80  ? 41.847  -7.462  57.437  1.00 33.17 ? 80   HIS L C   1 
ATOM   12875 O  O   . HIS L  1 80  ? 42.856  -7.191  58.105  1.00 30.78 ? 80   HIS L O   1 
ATOM   12876 C  CB  . HIS L  1 80  ? 39.839  -5.963  57.397  1.00 28.13 ? 80   HIS L CB  1 
ATOM   12877 C  CG  . HIS L  1 80  ? 38.526  -5.563  57.998  1.00 28.93 ? 80   HIS L CG  1 
ATOM   12878 N  ND1 . HIS L  1 80  ? 38.167  -4.246  58.195  1.00 28.65 ? 80   HIS L ND1 1 
ATOM   12879 C  CD2 . HIS L  1 80  ? 37.485  -6.303  58.445  1.00 27.03 ? 80   HIS L CD2 1 
ATOM   12880 C  CE1 . HIS L  1 80  ? 36.961  -4.190  58.728  1.00 25.62 ? 80   HIS L CE1 1 
ATOM   12881 N  NE2 . HIS L  1 80  ? 36.528  -5.425  58.898  1.00 27.01 ? 80   HIS L NE2 1 
ATOM   12882 N  N   . VAL L  1 81  ? 41.917  -7.965  56.204  1.00 32.71 ? 81   VAL L N   1 
ATOM   12883 C  CA  . VAL L  1 81  ? 43.221  -8.166  55.556  1.00 31.63 ? 81   VAL L CA  1 
ATOM   12884 C  C   . VAL L  1 81  ? 43.923  -6.829  55.277  1.00 28.81 ? 81   VAL L C   1 
ATOM   12885 O  O   . VAL L  1 81  ? 45.139  -6.726  55.393  1.00 29.39 ? 81   VAL L O   1 
ATOM   12886 C  CB  . VAL L  1 81  ? 43.122  -9.030  54.257  1.00 33.95 ? 81   VAL L CB  1 
ATOM   12887 C  CG1 . VAL L  1 81  ? 44.387  -8.889  53.395  1.00 32.67 ? 81   VAL L CG1 1 
ATOM   12888 C  CG2 . VAL L  1 81  ? 42.873  -10.499 54.598  1.00 33.14 ? 81   VAL L CG2 1 
ATOM   12889 N  N   . GLY L  1 82  ? 43.153  -5.802  54.933  1.00 28.54 ? 82   GLY L N   1 
ATOM   12890 C  CA  . GLY L  1 82  ? 43.722  -4.503  54.615  1.00 29.53 ? 82   GLY L CA  1 
ATOM   12891 C  C   . GLY L  1 82  ? 43.997  -3.596  55.803  1.00 26.59 ? 82   GLY L C   1 
ATOM   12892 O  O   . GLY L  1 82  ? 44.259  -2.407  55.630  1.00 26.02 ? 82   GLY L O   1 
ATOM   12893 N  N   . ASP L  1 83  ? 43.933  -4.159  57.008  1.00 29.13 ? 83   ASP L N   1 
ATOM   12894 C  CA  . ASP L  1 83  ? 44.126  -3.406  58.252  1.00 29.83 ? 83   ASP L CA  1 
ATOM   12895 C  C   . ASP L  1 83  ? 45.592  -3.205  58.576  1.00 27.90 ? 83   ASP L C   1 
ATOM   12896 O  O   . ASP L  1 83  ? 46.196  -4.047  59.229  1.00 29.56 ? 83   ASP L O   1 
ATOM   12897 C  CB  . ASP L  1 83  ? 43.476  -4.137  59.430  1.00 28.72 ? 83   ASP L CB  1 
ATOM   12898 C  CG  . ASP L  1 83  ? 41.974  -3.998  59.442  1.00 29.02 ? 83   ASP L CG  1 
ATOM   12899 O  OD1 . ASP L  1 83  ? 41.468  -3.171  58.664  1.00 25.60 ? 83   ASP L OD1 1 
ATOM   12900 O  OD2 . ASP L  1 83  ? 41.311  -4.709  60.229  1.00 29.26 ? 83   ASP L OD2 1 
ATOM   12901 N  N   . LEU L  1 84  ? 46.162  -2.089  58.137  1.00 29.10 ? 84   LEU L N   1 
ATOM   12902 C  CA  . LEU L  1 84  ? 47.581  -1.842  58.377  1.00 30.21 ? 84   LEU L CA  1 
ATOM   12903 C  C   . LEU L  1 84  ? 47.842  -0.825  59.500  1.00 31.23 ? 84   LEU L C   1 
ATOM   12904 O  O   . LEU L  1 84  ? 48.957  -0.327  59.645  1.00 36.05 ? 84   LEU L O   1 
ATOM   12905 C  CB  . LEU L  1 84  ? 48.309  -1.461  57.073  1.00 29.04 ? 84   LEU L CB  1 
ATOM   12906 C  CG  . LEU L  1 84  ? 48.393  -2.530  55.967  1.00 29.23 ? 84   LEU L CG  1 
ATOM   12907 C  CD1 . LEU L  1 84  ? 49.255  -2.062  54.790  1.00 26.30 ? 84   LEU L CD1 1 
ATOM   12908 C  CD2 . LEU L  1 84  ? 48.891  -3.877  56.505  1.00 28.20 ? 84   LEU L CD2 1 
ATOM   12909 N  N   . GLY L  1 85  ? 46.820  -0.532  60.300  1.00 29.32 ? 85   GLY L N   1 
ATOM   12910 C  CA  . GLY L  1 85  ? 46.988  0.344   61.444  1.00 27.48 ? 85   GLY L CA  1 
ATOM   12911 C  C   . GLY L  1 85  ? 47.127  1.802   61.062  1.00 26.56 ? 85   GLY L C   1 
ATOM   12912 O  O   . GLY L  1 85  ? 46.353  2.311   60.260  1.00 28.84 ? 85   GLY L O   1 
ATOM   12913 N  N   . ASN L  1 86  ? 48.127  2.470   61.630  1.00 30.72 ? 86   ASN L N   1 
ATOM   12914 C  CA  . ASN L  1 86  ? 48.355  3.899   61.394  1.00 30.53 ? 86   ASN L CA  1 
ATOM   12915 C  C   . ASN L  1 86  ? 49.728  4.200   60.818  1.00 30.43 ? 86   ASN L C   1 
ATOM   12916 O  O   . ASN L  1 86  ? 50.682  3.448   61.025  1.00 27.79 ? 86   ASN L O   1 
ATOM   12917 C  CB  . ASN L  1 86  ? 48.261  4.685   62.709  1.00 30.10 ? 86   ASN L CB  1 
ATOM   12918 C  CG  . ASN L  1 86  ? 46.891  4.645   63.322  1.00 27.10 ? 86   ASN L CG  1 
ATOM   12919 O  OD1 . ASN L  1 86  ? 46.004  5.384   62.923  1.00 28.12 ? 86   ASN L OD1 1 
ATOM   12920 N  ND2 . ASN L  1 86  ? 46.715  3.790   64.318  1.00 28.28 ? 86   ASN L ND2 1 
ATOM   12921 N  N   . VAL L  1 87  ? 49.828  5.331   60.126  1.00 31.13 ? 87   VAL L N   1 
ATOM   12922 C  CA  . VAL L  1 87  ? 51.131  5.947   59.889  1.00 34.15 ? 87   VAL L CA  1 
ATOM   12923 C  C   . VAL L  1 87  ? 51.265  7.278   60.676  1.00 34.96 ? 87   VAL L C   1 
ATOM   12924 O  O   . VAL L  1 87  ? 50.266  7.966   60.932  1.00 29.91 ? 87   VAL L O   1 
ATOM   12925 C  CB  . VAL L  1 87  ? 51.497  6.083   58.365  1.00 29.59 ? 87   VAL L CB  1 
ATOM   12926 C  CG1 . VAL L  1 87  ? 51.633  4.707   57.719  1.00 27.86 ? 87   VAL L CG1 1 
ATOM   12927 C  CG2 . VAL L  1 87  ? 50.499  6.957   57.608  1.00 28.85 ? 87   VAL L CG2 1 
ATOM   12928 N  N   . THR L  1 88  ? 52.499  7.609   61.072  1.00 35.43 ? 88   THR L N   1 
ATOM   12929 C  CA  . THR L  1 88  ? 52.782  8.822   61.843  1.00 37.11 ? 88   THR L CA  1 
ATOM   12930 C  C   . THR L  1 88  ? 53.419  9.942   61.017  1.00 37.34 ? 88   THR L C   1 
ATOM   12931 O  O   . THR L  1 88  ? 54.527  9.791   60.492  1.00 36.24 ? 88   THR L O   1 
ATOM   12932 C  CB  . THR L  1 88  ? 53.726  8.532   63.023  1.00 38.60 ? 88   THR L CB  1 
ATOM   12933 O  OG1 . THR L  1 88  ? 53.331  7.314   63.669  1.00 39.71 ? 88   THR L OG1 1 
ATOM   12934 C  CG2 . THR L  1 88  ? 53.706  9.694   64.026  1.00 35.57 ? 88   THR L CG2 1 
ATOM   12935 N  N   . ALA L  1 89  ? 52.719  11.072  60.932  1.00 37.34 ? 89   ALA L N   1 
ATOM   12936 C  CA  . ALA L  1 89  ? 53.232  12.267  60.262  1.00 37.77 ? 89   ALA L CA  1 
ATOM   12937 C  C   . ALA L  1 89  ? 53.951  13.202  61.245  1.00 40.08 ? 89   ALA L C   1 
ATOM   12938 O  O   . ALA L  1 89  ? 53.340  13.676  62.207  1.00 40.87 ? 89   ALA L O   1 
ATOM   12939 C  CB  . ALA L  1 89  ? 52.092  13.009  59.578  1.00 36.29 ? 89   ALA L CB  1 
ATOM   12940 N  N   . GLY L  1 90  ? 55.236  13.475  61.000  1.00 39.80 ? 90   GLY L N   1 
ATOM   12941 C  CA  . GLY L  1 90  ? 56.009  14.378  61.840  1.00 35.60 ? 90   GLY L CA  1 
ATOM   12942 C  C   . GLY L  1 90  ? 55.510  15.806  61.732  1.00 36.81 ? 90   GLY L C   1 
ATOM   12943 O  O   . GLY L  1 90  ? 54.557  16.078  61.012  1.00 37.76 ? 90   GLY L O   1 
ATOM   12944 N  N   . LYS L  1 91  ? 56.159  16.725  62.442  1.00 40.72 ? 91   LYS L N   1 
ATOM   12945 C  CA  . LYS L  1 91  ? 55.723  18.124  62.491  1.00 38.94 ? 91   LYS L CA  1 
ATOM   12946 C  C   . LYS L  1 91  ? 55.585  18.743  61.095  1.00 41.20 ? 91   LYS L C   1 
ATOM   12947 O  O   . LYS L  1 91  ? 54.833  19.698  60.903  1.00 42.27 ? 91   LYS L O   1 
ATOM   12948 C  CB  . LYS L  1 91  ? 56.694  18.952  63.347  1.00 42.19 ? 91   LYS L CB  1 
ATOM   12949 C  CG  . LYS L  1 91  ? 56.134  20.300  63.828  1.00 46.10 ? 91   LYS L CG  1 
ATOM   12950 C  CD  . LYS L  1 91  ? 57.065  20.986  64.845  1.00 44.77 ? 91   LYS L CD  1 
ATOM   12951 C  CE  . LYS L  1 91  ? 57.762  19.986  65.781  1.00 42.59 ? 91   LYS L CE  1 
ATOM   12952 N  NZ  . LYS L  1 91  ? 56.842  19.179  66.637  1.00 36.67 ? 91   LYS L NZ  1 
ATOM   12953 N  N   . ASP L  1 92  ? 56.305  18.169  60.131  1.00 42.25 ? 92   ASP L N   1 
ATOM   12954 C  CA  . ASP L  1 92  ? 56.441  18.710  58.774  1.00 44.18 ? 92   ASP L CA  1 
ATOM   12955 C  C   . ASP L  1 92  ? 55.338  18.284  57.794  1.00 43.00 ? 92   ASP L C   1 
ATOM   12956 O  O   . ASP L  1 92  ? 55.371  18.651  56.615  1.00 43.59 ? 92   ASP L O   1 
ATOM   12957 C  CB  . ASP L  1 92  ? 57.810  18.315  58.190  1.00 39.50 ? 92   ASP L CB  1 
ATOM   12958 C  CG  . ASP L  1 92  ? 58.134  16.835  58.387  1.00 39.35 ? 92   ASP L CG  1 
ATOM   12959 O  OD1 . ASP L  1 92  ? 57.249  16.060  58.811  1.00 37.46 ? 92   ASP L OD1 1 
ATOM   12960 O  OD2 . ASP L  1 92  ? 59.287  16.442  58.120  1.00 43.66 ? 92   ASP L OD2 1 
ATOM   12961 N  N   . GLY L  1 93  ? 54.368  17.517  58.280  1.00 43.26 ? 93   GLY L N   1 
ATOM   12962 C  CA  . GLY L  1 93  ? 53.351  16.943  57.419  1.00 36.72 ? 93   GLY L CA  1 
ATOM   12963 C  C   . GLY L  1 93  ? 53.785  15.597  56.861  1.00 38.39 ? 93   GLY L C   1 
ATOM   12964 O  O   . GLY L  1 93  ? 52.990  14.902  56.228  1.00 39.72 ? 93   GLY L O   1 
ATOM   12965 N  N   . VAL L  1 94  ? 55.037  15.214  57.115  1.00 37.16 ? 94   VAL L N   1 
ATOM   12966 C  CA  . VAL L  1 94  ? 55.633  14.051  56.453  1.00 36.55 ? 94   VAL L CA  1 
ATOM   12967 C  C   . VAL L  1 94  ? 55.731  12.767  57.286  1.00 36.37 ? 94   VAL L C   1 
ATOM   12968 O  O   . VAL L  1 94  ? 56.445  12.701  58.294  1.00 37.57 ? 94   VAL L O   1 
ATOM   12969 C  CB  . VAL L  1 94  ? 57.017  14.384  55.844  1.00 36.01 ? 94   VAL L CB  1 
ATOM   12970 C  CG1 . VAL L  1 94  ? 57.678  13.128  55.300  1.00 32.93 ? 94   VAL L CG1 1 
ATOM   12971 C  CG2 . VAL L  1 94  ? 56.864  15.430  54.757  1.00 36.13 ? 94   VAL L CG2 1 
ATOM   12972 N  N   . ALA L  1 95  ? 55.022  11.746  56.808  1.00 35.35 ? 95   ALA L N   1 
ATOM   12973 C  CA  . ALA L  1 95  ? 54.987  10.419  57.410  1.00 35.20 ? 95   ALA L CA  1 
ATOM   12974 C  C   . ALA L  1 95  ? 55.938  9.476   56.700  1.00 34.93 ? 95   ALA L C   1 
ATOM   12975 O  O   . ALA L  1 95  ? 55.805  9.231   55.504  1.00 35.57 ? 95   ALA L O   1 
ATOM   12976 C  CB  . ALA L  1 95  ? 53.568  9.853   57.348  1.00 33.66 ? 95   ALA L CB  1 
ATOM   12977 N  N   . ASN L  1 96  ? 56.898  8.937   57.433  1.00 36.32 ? 96   ASN L N   1 
ATOM   12978 C  CA  . ASN L  1 96  ? 57.754  7.916   56.863  1.00 37.49 ? 96   ASN L CA  1 
ATOM   12979 C  C   . ASN L  1 96  ? 57.179  6.562   57.205  1.00 38.85 ? 96   ASN L C   1 
ATOM   12980 O  O   . ASN L  1 96  ? 56.881  6.269   58.364  1.00 39.58 ? 96   ASN L O   1 
ATOM   12981 C  CB  . ASN L  1 96  ? 59.197  8.058   57.346  1.00 41.71 ? 96   ASN L CB  1 
ATOM   12982 C  CG  . ASN L  1 96  ? 59.763  9.444   57.077  1.00 46.55 ? 96   ASN L CG  1 
ATOM   12983 O  OD1 . ASN L  1 96  ? 59.883  9.873   55.923  1.00 44.63 ? 96   ASN L OD1 1 
ATOM   12984 N  ND2 . ASN L  1 96  ? 60.096  10.161  58.149  1.00 49.66 ? 96   ASN L ND2 1 
ATOM   12985 N  N   . VAL L  1 97  ? 57.004  5.748   56.175  1.00 37.87 ? 97   VAL L N   1 
ATOM   12986 C  CA  . VAL L  1 97  ? 56.327  4.477   56.317  1.00 37.35 ? 97   VAL L CA  1 
ATOM   12987 C  C   . VAL L  1 97  ? 57.312  3.323   56.294  1.00 37.55 ? 97   VAL L C   1 
ATOM   12988 O  O   . VAL L  1 97  ? 58.072  3.166   55.341  1.00 39.53 ? 97   VAL L O   1 
ATOM   12989 C  CB  . VAL L  1 97  ? 55.320  4.276   55.180  1.00 35.26 ? 97   VAL L CB  1 
ATOM   12990 C  CG1 . VAL L  1 97  ? 54.773  2.851   55.199  1.00 33.83 ? 97   VAL L CG1 1 
ATOM   12991 C  CG2 . VAL L  1 97  ? 54.210  5.324   55.264  1.00 33.94 ? 97   VAL L CG2 1 
ATOM   12992 N  N   . SER L  1 98  ? 57.303  2.526   57.352  1.00 32.12 ? 98   SER L N   1 
ATOM   12993 C  CA  . SER L  1 98  ? 58.015  1.263   57.354  1.00 36.40 ? 98   SER L CA  1 
ATOM   12994 C  C   . SER L  1 98  ? 57.106  0.281   58.055  1.00 38.63 ? 98   SER L C   1 
ATOM   12995 O  O   . SER L  1 98  ? 56.560  0.588   59.109  1.00 41.08 ? 98   SER L O   1 
ATOM   12996 C  CB  . SER L  1 98  ? 59.359  1.386   58.078  1.00 45.04 ? 98   SER L CB  1 
ATOM   12997 O  OG  . SER L  1 98  ? 59.897  0.113   58.400  1.00 46.54 ? 98   SER L OG  1 
ATOM   12998 N  N   . ILE L  1 99  ? 56.917  -0.888  57.454  1.00 40.73 ? 99   ILE L N   1 
ATOM   12999 C  CA  . ILE L  1 99  ? 55.945  -1.867  57.937  1.00 39.24 ? 99   ILE L CA  1 
ATOM   13000 C  C   . ILE L  1 99  ? 56.406  -3.224  57.438  1.00 37.70 ? 99   ILE L C   1 
ATOM   13001 O  O   . ILE L  1 99  ? 57.117  -3.307  56.443  1.00 40.83 ? 99   ILE L O   1 
ATOM   13002 C  CB  . ILE L  1 99  ? 54.498  -1.565  57.400  1.00 39.47 ? 99   ILE L CB  1 
ATOM   13003 C  CG1 . ILE L  1 99  ? 53.926  -0.277  58.010  1.00 37.84 ? 99   ILE L CG1 1 
ATOM   13004 C  CG2 . ILE L  1 99  ? 53.542  -2.734  57.645  1.00 36.10 ? 99   ILE L CG2 1 
ATOM   13005 C  CD1 . ILE L  1 99  ? 52.759  0.332   57.227  1.00 30.48 ? 99   ILE L CD1 1 
ATOM   13006 N  N   . GLU L  1 100 ? 56.033  -4.282  58.143  1.00 37.68 ? 100  GLU L N   1 
ATOM   13007 C  CA  . GLU L  1 100 ? 56.244  -5.634  57.653  1.00 39.89 ? 100  GLU L CA  1 
ATOM   13008 C  C   . GLU L  1 100 ? 55.080  -6.479  58.126  1.00 41.02 ? 100  GLU L C   1 
ATOM   13009 O  O   . GLU L  1 100 ? 54.954  -6.768  59.315  1.00 44.14 ? 100  GLU L O   1 
ATOM   13010 C  CB  . GLU L  1 100 ? 57.570  -6.208  58.146  1.00 44.62 ? 100  GLU L CB  1 
ATOM   13011 C  CG  . GLU L  1 100 ? 57.797  -7.661  57.746  1.00 46.63 ? 100  GLU L CG  1 
ATOM   13012 C  CD  . GLU L  1 100 ? 59.252  -7.951  57.396  1.00 56.56 ? 100  GLU L CD  1 
ATOM   13013 O  OE1 . GLU L  1 100 ? 60.043  -6.987  57.256  1.00 53.93 ? 100  GLU L OE1 1 
ATOM   13014 O  OE2 . GLU L  1 100 ? 59.601  -9.145  57.245  1.00 61.13 ? 100  GLU L OE2 1 
ATOM   13015 N  N   . ASP L  1 101 ? 54.222  -6.864  57.185  1.00 43.45 ? 101  ASP L N   1 
ATOM   13016 C  CA  . ASP L  1 101 ? 52.947  -7.503  57.509  1.00 40.31 ? 101  ASP L CA  1 
ATOM   13017 C  C   . ASP L  1 101 ? 52.850  -8.906  56.905  1.00 37.68 ? 101  ASP L C   1 
ATOM   13018 O  O   . ASP L  1 101 ? 53.295  -9.137  55.791  1.00 37.18 ? 101  ASP L O   1 
ATOM   13019 C  CB  . ASP L  1 101 ? 51.792  -6.611  57.035  1.00 37.24 ? 101  ASP L CB  1 
ATOM   13020 C  CG  . ASP L  1 101 ? 50.445  -7.021  57.617  1.00 37.47 ? 101  ASP L CG  1 
ATOM   13021 O  OD1 . ASP L  1 101 ? 49.931  -6.297  58.495  1.00 39.21 ? 101  ASP L OD1 1 
ATOM   13022 O  OD2 . ASP L  1 101 ? 49.895  -8.060  57.196  1.00 36.99 ? 101  ASP L OD2 1 
ATOM   13023 N  N   . ARG L  1 102 ? 52.262  -9.836  57.649  1.00 39.70 ? 102  ARG L N   1 
ATOM   13024 C  CA  . ARG L  1 102 ? 52.186  -11.233 57.226  1.00 39.20 ? 102  ARG L CA  1 
ATOM   13025 C  C   . ARG L  1 102 ? 50.753  -11.691 56.962  1.00 35.70 ? 102  ARG L C   1 
ATOM   13026 O  O   . ARG L  1 102 ? 50.510  -12.889 56.793  1.00 37.15 ? 102  ARG L O   1 
ATOM   13027 C  CB  . ARG L  1 102 ? 52.832  -12.136 58.283  1.00 40.34 ? 102  ARG L CB  1 
ATOM   13028 C  CG  . ARG L  1 102 ? 53.815  -11.395 59.175  1.00 48.60 ? 102  ARG L CG  1 
ATOM   13029 C  CD  . ARG L  1 102 ? 55.052  -12.220 59.492  1.00 55.68 ? 102  ARG L CD  1 
ATOM   13030 N  NE  . ARG L  1 102 ? 56.181  -11.373 59.882  1.00 57.55 ? 102  ARG L NE  1 
ATOM   13031 C  CZ  . ARG L  1 102 ? 57.417  -11.820 60.075  1.00 61.15 ? 102  ARG L CZ  1 
ATOM   13032 N  NH1 . ARG L  1 102 ? 57.686  -13.113 59.914  1.00 63.44 ? 102  ARG L NH1 1 
ATOM   13033 N  NH2 . ARG L  1 102 ? 58.384  -10.979 60.427  1.00 62.38 ? 102  ARG L NH2 1 
ATOM   13034 N  N   . VAL L  1 103 ? 49.807  -10.749 56.945  1.00 33.51 ? 103  VAL L N   1 
ATOM   13035 C  CA  . VAL L  1 103 ? 48.418  -11.056 56.579  1.00 35.49 ? 103  VAL L CA  1 
ATOM   13036 C  C   . VAL L  1 103 ? 48.101  -10.683 55.120  1.00 36.08 ? 103  VAL L C   1 
ATOM   13037 O  O   . VAL L  1 103 ? 47.538  -11.493 54.371  1.00 35.89 ? 103  VAL L O   1 
ATOM   13038 C  CB  . VAL L  1 103 ? 47.401  -10.406 57.543  1.00 32.32 ? 103  VAL L CB  1 
ATOM   13039 C  CG1 . VAL L  1 103 ? 46.013  -10.414 56.945  1.00 30.46 ? 103  VAL L CG1 1 
ATOM   13040 C  CG2 . VAL L  1 103 ? 47.401  -11.133 58.867  1.00 32.47 ? 103  VAL L CG2 1 
ATOM   13041 N  N   . ILE L  1 104 ? 48.461  -9.463  54.724  1.00 33.25 ? 104  ILE L N   1 
ATOM   13042 C  CA  . ILE L  1 104 ? 48.397  -9.083  53.323  1.00 33.53 ? 104  ILE L CA  1 
ATOM   13043 C  C   . ILE L  1 104 ? 49.385  -9.940  52.530  1.00 39.93 ? 104  ILE L C   1 
ATOM   13044 O  O   . ILE L  1 104 ? 50.365  -10.446 53.091  1.00 37.36 ? 104  ILE L O   1 
ATOM   13045 C  CB  . ILE L  1 104 ? 48.769  -7.593  53.083  1.00 35.24 ? 104  ILE L CB  1 
ATOM   13046 C  CG1 . ILE L  1 104 ? 50.202  -7.312  53.547  1.00 33.14 ? 104  ILE L CG1 1 
ATOM   13047 C  CG2 . ILE L  1 104 ? 47.761  -6.646  53.727  1.00 29.85 ? 104  ILE L CG2 1 
ATOM   13048 C  CD1 . ILE L  1 104 ? 50.730  -5.991  53.075  1.00 30.55 ? 104  ILE L CD1 1 
ATOM   13049 N  N   . SER L  1 105 ? 49.126  -10.084 51.229  1.00 39.38 ? 105  SER L N   1 
ATOM   13050 C  CA  . SER L  1 105 ? 50.004  -10.820 50.320  1.00 40.74 ? 105  SER L CA  1 
ATOM   13051 C  C   . SER L  1 105 ? 50.124  -10.084 48.988  1.00 39.67 ? 105  SER L C   1 
ATOM   13052 O  O   . SER L  1 105 ? 49.270  -9.271  48.645  1.00 40.06 ? 105  SER L O   1 
ATOM   13053 C  CB  . SER L  1 105 ? 49.469  -12.240 50.087  1.00 42.45 ? 105  SER L CB  1 
ATOM   13054 O  OG  . SER L  1 105 ? 50.350  -13.000 49.272  1.00 43.36 ? 105  SER L OG  1 
ATOM   13055 N  N   . LEU L  1 106 ? 51.186  -10.368 48.239  1.00 43.51 ? 106  LEU L N   1 
ATOM   13056 C  CA  . LEU L  1 106 ? 51.352  -9.802  46.894  1.00 41.46 ? 106  LEU L CA  1 
ATOM   13057 C  C   . LEU L  1 106 ? 50.971  -10.816 45.805  1.00 42.68 ? 106  LEU L C   1 
ATOM   13058 O  O   . LEU L  1 106 ? 51.086  -10.534 44.607  1.00 43.56 ? 106  LEU L O   1 
ATOM   13059 C  CB  . LEU L  1 106 ? 52.778  -9.279  46.682  1.00 40.32 ? 106  LEU L CB  1 
ATOM   13060 C  CG  . LEU L  1 106 ? 53.126  -7.957  47.379  1.00 38.15 ? 106  LEU L CG  1 
ATOM   13061 C  CD1 . LEU L  1 106 ? 54.439  -7.392  46.864  1.00 37.09 ? 106  LEU L CD1 1 
ATOM   13062 C  CD2 . LEU L  1 106 ? 52.008  -6.940  47.191  1.00 36.32 ? 106  LEU L CD2 1 
ATOM   13063 N  N   . SER L  1 107 ? 50.508  -11.990 46.241  1.00 44.15 ? 107  SER L N   1 
ATOM   13064 C  CA  . SER L  1 107 ? 50.007  -13.030 45.345  1.00 43.66 ? 107  SER L CA  1 
ATOM   13065 C  C   . SER L  1 107 ? 48.958  -13.902 46.044  1.00 41.34 ? 107  SER L C   1 
ATOM   13066 O  O   . SER L  1 107 ? 48.881  -13.947 47.272  1.00 44.99 ? 107  SER L O   1 
ATOM   13067 C  CB  . SER L  1 107 ? 51.160  -13.902 44.821  1.00 42.58 ? 107  SER L CB  1 
ATOM   13068 O  OG  . SER L  1 107 ? 51.443  -14.969 45.710  1.00 42.24 ? 107  SER L OG  1 
ATOM   13069 N  N   . GLY L  1 108 ? 48.145  -14.593 45.257  1.00 42.10 ? 108  GLY L N   1 
ATOM   13070 C  CA  . GLY L  1 108 ? 47.199  -15.545 45.806  1.00 45.98 ? 108  GLY L CA  1 
ATOM   13071 C  C   . GLY L  1 108 ? 45.841  -14.980 46.177  1.00 47.17 ? 108  GLY L C   1 
ATOM   13072 O  O   . GLY L  1 108 ? 45.432  -13.920 45.709  1.00 46.82 ? 108  GLY L O   1 
ATOM   13073 N  N   . GLU L  1 109 ? 45.148  -15.713 47.039  1.00 49.12 ? 109  GLU L N   1 
ATOM   13074 C  CA  . GLU L  1 109 ? 43.785  -15.407 47.458  1.00 47.96 ? 109  GLU L CA  1 
ATOM   13075 C  C   . GLU L  1 109 ? 43.678  -14.060 48.166  1.00 47.48 ? 109  GLU L C   1 
ATOM   13076 O  O   . GLU L  1 109 ? 42.619  -13.429 48.167  1.00 48.27 ? 109  GLU L O   1 
ATOM   13077 C  CB  . GLU L  1 109 ? 43.283  -16.508 48.402  1.00 51.91 ? 109  GLU L CB  1 
ATOM   13078 C  CG  . GLU L  1 109 ? 43.811  -17.920 48.090  1.00 60.86 ? 109  GLU L CG  1 
ATOM   13079 C  CD  . GLU L  1 109 ? 45.267  -18.173 48.539  1.00 62.10 ? 109  GLU L CD  1 
ATOM   13080 O  OE1 . GLU L  1 109 ? 46.023  -17.206 48.801  1.00 56.82 ? 109  GLU L OE1 1 
ATOM   13081 O  OE2 . GLU L  1 109 ? 45.657  -19.362 48.622  1.00 65.13 ? 109  GLU L OE2 1 
ATOM   13082 N  N   . HIS L  1 110 ? 44.771  -13.633 48.791  1.00 47.78 ? 110  HIS L N   1 
ATOM   13083 C  CA  . HIS L  1 110 ? 44.755  -12.410 49.587  1.00 42.76 ? 110  HIS L CA  1 
ATOM   13084 C  C   . HIS L  1 110 ? 45.583  -11.309 48.958  1.00 42.00 ? 110  HIS L C   1 
ATOM   13085 O  O   . HIS L  1 110 ? 45.824  -10.274 49.586  1.00 42.32 ? 110  HIS L O   1 
ATOM   13086 C  CB  . HIS L  1 110 ? 45.225  -12.681 51.022  1.00 42.56 ? 110  HIS L CB  1 
ATOM   13087 C  CG  . HIS L  1 110 ? 44.206  -13.387 51.866  1.00 45.95 ? 110  HIS L CG  1 
ATOM   13088 N  ND1 . HIS L  1 110 ? 44.534  -14.063 53.021  1.00 47.47 ? 110  HIS L ND1 1 
ATOM   13089 C  CD2 . HIS L  1 110 ? 42.866  -13.530 51.714  1.00 45.74 ? 110  HIS L CD2 1 
ATOM   13090 C  CE1 . HIS L  1 110 ? 43.439  -14.584 53.549  1.00 47.79 ? 110  HIS L CE1 1 
ATOM   13091 N  NE2 . HIS L  1 110 ? 42.413  -14.277 52.773  1.00 45.23 ? 110  HIS L NE2 1 
ATOM   13092 N  N   . SER L  1 111 ? 46.013  -11.541 47.717  1.00 42.03 ? 111  SER L N   1 
ATOM   13093 C  CA  . SER L  1 111 ? 46.857  -10.594 47.001  1.00 41.08 ? 111  SER L CA  1 
ATOM   13094 C  C   . SER L  1 111 ? 46.237  -9.208  47.022  1.00 38.23 ? 111  SER L C   1 
ATOM   13095 O  O   . SER L  1 111 ? 45.028  -9.059  46.831  1.00 36.70 ? 111  SER L O   1 
ATOM   13096 C  CB  . SER L  1 111 ? 47.069  -11.039 45.550  1.00 40.30 ? 111  SER L CB  1 
ATOM   13097 O  OG  . SER L  1 111 ? 47.688  -10.008 44.795  1.00 37.01 ? 111  SER L OG  1 
ATOM   13098 N  N   . ILE L  1 112 ? 47.063  -8.194  47.259  1.00 37.57 ? 112  ILE L N   1 
ATOM   13099 C  CA  . ILE L  1 112 ? 46.575  -6.824  47.252  1.00 33.65 ? 112  ILE L CA  1 
ATOM   13100 C  C   . ILE L  1 112 ? 46.926  -6.117  45.959  1.00 32.73 ? 112  ILE L C   1 
ATOM   13101 O  O   . ILE L  1 112 ? 46.718  -4.909  45.837  1.00 33.28 ? 112  ILE L O   1 
ATOM   13102 C  CB  . ILE L  1 112 ? 47.095  -6.021  48.447  1.00 34.53 ? 112  ILE L CB  1 
ATOM   13103 C  CG1 . ILE L  1 112 ? 48.630  -6.025  48.457  1.00 37.39 ? 112  ILE L CG1 1 
ATOM   13104 C  CG2 . ILE L  1 112 ? 46.514  -6.587  49.741  1.00 33.00 ? 112  ILE L CG2 1 
ATOM   13105 C  CD1 . ILE L  1 112 ? 49.255  -5.017  49.405  1.00 33.10 ? 112  ILE L CD1 1 
ATOM   13106 N  N   . ILE L  1 113 ? 47.454  -6.867  44.990  1.00 33.65 ? 113  ILE L N   1 
ATOM   13107 C  CA  . ILE L  1 113 ? 47.726  -6.301  43.670  1.00 32.51 ? 113  ILE L CA  1 
ATOM   13108 C  C   . ILE L  1 113 ? 46.381  -6.004  43.035  1.00 32.28 ? 113  ILE L C   1 
ATOM   13109 O  O   . ILE L  1 113 ? 45.504  -6.871  42.988  1.00 31.61 ? 113  ILE L O   1 
ATOM   13110 C  CB  . ILE L  1 113 ? 48.548  -7.261  42.739  1.00 34.51 ? 113  ILE L CB  1 
ATOM   13111 C  CG1 . ILE L  1 113 ? 49.893  -7.665  43.369  1.00 33.81 ? 113  ILE L CG1 1 
ATOM   13112 C  CG2 . ILE L  1 113 ? 48.754  -6.634  41.355  1.00 30.22 ? 113  ILE L CG2 1 
ATOM   13113 C  CD1 . ILE L  1 113 ? 50.962  -6.600  43.330  1.00 31.79 ? 113  ILE L CD1 1 
ATOM   13114 N  N   . GLY L  1 114 ? 46.209  -4.776  42.559  1.00 32.40 ? 114  GLY L N   1 
ATOM   13115 C  CA  . GLY L  1 114 ? 44.967  -4.400  41.913  1.00 30.05 ? 114  GLY L CA  1 
ATOM   13116 C  C   . GLY L  1 114 ? 43.959  -3.822  42.887  1.00 33.32 ? 114  GLY L C   1 
ATOM   13117 O  O   . GLY L  1 114 ? 42.825  -3.516  42.517  1.00 30.64 ? 114  GLY L O   1 
ATOM   13118 N  N   . ARG L  1 115 ? 44.357  -3.672  44.146  1.00 32.37 ? 115  ARG L N   1 
ATOM   13119 C  CA  . ARG L  1 115 ? 43.466  -3.038  45.106  1.00 31.33 ? 115  ARG L CA  1 
ATOM   13120 C  C   . ARG L  1 115 ? 43.951  -1.631  45.433  1.00 32.04 ? 115  ARG L C   1 
ATOM   13121 O  O   . ARG L  1 115 ? 44.842  -1.112  44.760  1.00 34.47 ? 115  ARG L O   1 
ATOM   13122 C  CB  . ARG L  1 115 ? 43.289  -3.914  46.339  1.00 31.15 ? 115  ARG L CB  1 
ATOM   13123 C  CG  . ARG L  1 115 ? 42.873  -5.316  45.953  1.00 31.83 ? 115  ARG L CG  1 
ATOM   13124 C  CD  . ARG L  1 115 ? 42.409  -6.129  47.129  1.00 31.15 ? 115  ARG L CD  1 
ATOM   13125 N  NE  . ARG L  1 115 ? 42.154  -7.504  46.720  1.00 33.33 ? 115  ARG L NE  1 
ATOM   13126 C  CZ  . ARG L  1 115 ? 40.996  -7.941  46.234  1.00 33.65 ? 115  ARG L CZ  1 
ATOM   13127 N  NH1 . ARG L  1 115 ? 39.972  -7.109  46.100  1.00 30.78 ? 115  ARG L NH1 1 
ATOM   13128 N  NH2 . ARG L  1 115 ? 40.860  -9.215  45.884  1.00 35.36 ? 115  ARG L NH2 1 
ATOM   13129 N  N   . THR L  1 116 ? 43.355  -0.998  46.434  1.00 32.04 ? 116  THR L N   1 
ATOM   13130 C  CA  . THR L  1 116 ? 43.669  0.398   46.702  1.00 31.84 ? 116  THR L CA  1 
ATOM   13131 C  C   . THR L  1 116 ? 44.314  0.611   48.071  1.00 30.27 ? 116  THR L C   1 
ATOM   13132 O  O   . THR L  1 116 ? 43.899  0.030   49.066  1.00 31.28 ? 116  THR L O   1 
ATOM   13133 C  CB  . THR L  1 116 ? 42.431  1.304   46.503  1.00 29.39 ? 116  THR L CB  1 
ATOM   13134 O  OG1 . THR L  1 116 ? 42.114  1.363   45.105  1.00 33.95 ? 116  THR L OG1 1 
ATOM   13135 C  CG2 . THR L  1 116 ? 42.697  2.713   46.997  1.00 28.61 ? 116  THR L CG2 1 
ATOM   13136 N  N   . MET L  1 117 ? 45.363  1.420   48.096  1.00 30.09 ? 117  MET L N   1 
ATOM   13137 C  CA  . MET L  1 117 ? 45.956  1.860   49.341  1.00 29.77 ? 117  MET L CA  1 
ATOM   13138 C  C   . MET L  1 117 ? 45.373  3.248   49.610  1.00 28.99 ? 117  MET L C   1 
ATOM   13139 O  O   . MET L  1 117 ? 45.485  4.139   48.771  1.00 30.57 ? 117  MET L O   1 
ATOM   13140 C  CB  . MET L  1 117 ? 47.485  1.914   49.182  1.00 32.91 ? 117  MET L CB  1 
ATOM   13141 C  CG  . MET L  1 117 ? 48.328  1.990   50.467  1.00 31.67 ? 117  MET L CG  1 
ATOM   13142 S  SD  . MET L  1 117 ? 48.173  0.594   51.601  1.00 38.23 ? 117  MET L SD  1 
ATOM   13143 C  CE  . MET L  1 117 ? 48.049  -0.777  50.469  1.00 29.22 ? 117  MET L CE  1 
ATOM   13144 N  N   . VAL L  1 118 ? 44.706  3.430   50.748  1.00 30.21 ? 118  VAL L N   1 
ATOM   13145 C  CA  . VAL L  1 118 ? 44.332  4.786   51.149  1.00 31.42 ? 118  VAL L CA  1 
ATOM   13146 C  C   . VAL L  1 118 ? 44.917  5.189   52.509  1.00 32.92 ? 118  VAL L C   1 
ATOM   13147 O  O   . VAL L  1 118 ? 45.097  4.360   53.412  1.00 31.33 ? 118  VAL L O   1 
ATOM   13148 C  CB  . VAL L  1 118 ? 42.788  5.091   51.083  1.00 31.61 ? 118  VAL L CB  1 
ATOM   13149 C  CG1 . VAL L  1 118 ? 42.043  4.096   50.202  1.00 27.70 ? 118  VAL L CG1 1 
ATOM   13150 C  CG2 . VAL L  1 118 ? 42.179  5.160   52.469  1.00 33.26 ? 118  VAL L CG2 1 
ATOM   13151 N  N   . VAL L  1 119 ? 45.253  6.471   52.612  1.00 32.89 ? 119  VAL L N   1 
ATOM   13152 C  CA  . VAL L  1 119 ? 45.663  7.086   53.866  1.00 32.83 ? 119  VAL L CA  1 
ATOM   13153 C  C   . VAL L  1 119 ? 44.478  7.937   54.347  1.00 33.02 ? 119  VAL L C   1 
ATOM   13154 O  O   . VAL L  1 119 ? 43.888  8.688   53.558  1.00 29.51 ? 119  VAL L O   1 
ATOM   13155 C  CB  . VAL L  1 119 ? 46.963  7.933   53.693  1.00 32.96 ? 119  VAL L CB  1 
ATOM   13156 C  CG1 . VAL L  1 119 ? 46.771  9.038   52.652  1.00 30.84 ? 119  VAL L CG1 1 
ATOM   13157 C  CG2 . VAL L  1 119 ? 47.425  8.513   55.032  1.00 32.43 ? 119  VAL L CG2 1 
ATOM   13158 N  N   . HIS L  1 120 ? 44.115  7.795   55.624  1.00 31.56 ? 120  HIS L N   1 
ATOM   13159 C  CA  . HIS L  1 120 ? 42.898  8.419   56.150  1.00 31.16 ? 120  HIS L CA  1 
ATOM   13160 C  C   . HIS L  1 120 ? 43.122  9.745   56.895  1.00 31.60 ? 120  HIS L C   1 
ATOM   13161 O  O   . HIS L  1 120 ? 44.238  10.077  57.286  1.00 30.66 ? 120  HIS L O   1 
ATOM   13162 C  CB  . HIS L  1 120 ? 42.128  7.436   57.041  1.00 28.08 ? 120  HIS L CB  1 
ATOM   13163 C  CG  . HIS L  1 120 ? 41.227  6.507   56.284  1.00 29.86 ? 120  HIS L CG  1 
ATOM   13164 N  ND1 . HIS L  1 120 ? 41.612  5.239   55.902  1.00 28.67 ? 120  HIS L ND1 1 
ATOM   13165 C  CD2 . HIS L  1 120 ? 39.955  6.659   55.845  1.00 28.71 ? 120  HIS L CD2 1 
ATOM   13166 C  CE1 . HIS L  1 120 ? 40.621  4.654   55.258  1.00 26.74 ? 120  HIS L CE1 1 
ATOM   13167 N  NE2 . HIS L  1 120 ? 39.603  5.494   55.211  1.00 30.25 ? 120  HIS L NE2 1 
ATOM   13168 N  N   . GLU L  1 121 ? 42.027  10.480  57.082  1.00 31.97 ? 121  GLU L N   1 
ATOM   13169 C  CA  . GLU L  1 121 ? 42.002  11.785  57.744  1.00 31.98 ? 121  GLU L CA  1 
ATOM   13170 C  C   . GLU L  1 121 ? 42.509  11.725  59.188  1.00 31.16 ? 121  GLU L C   1 
ATOM   13171 O  O   . GLU L  1 121 ? 43.495  12.374  59.552  1.00 30.55 ? 121  GLU L O   1 
ATOM   13172 C  CB  . GLU L  1 121 ? 40.560  12.327  57.710  1.00 30.53 ? 121  GLU L CB  1 
ATOM   13173 C  CG  . GLU L  1 121 ? 40.295  13.628  58.476  1.00 29.81 ? 121  GLU L CG  1 
ATOM   13174 C  CD  . GLU L  1 121 ? 38.796  13.913  58.664  1.00 38.58 ? 121  GLU L CD  1 
ATOM   13175 O  OE1 . GLU L  1 121 ? 37.970  12.969  58.582  1.00 38.54 ? 121  GLU L OE1 1 
ATOM   13176 O  OE2 . GLU L  1 121 ? 38.435  15.086  58.906  1.00 43.74 ? 121  GLU L OE2 1 
ATOM   13177 N  N   . LYS L  1 122 ? 41.815  10.944  60.007  1.00 33.91 ? 122  LYS L N   1 
ATOM   13178 C  CA  . LYS L  1 122 ? 42.120  10.843  61.429  1.00 31.18 ? 122  LYS L CA  1 
ATOM   13179 C  C   . LYS L  1 122 ? 42.841  9.535   61.728  1.00 30.53 ? 122  LYS L C   1 
ATOM   13180 O  O   . LYS L  1 122 ? 43.092  8.729   60.832  1.00 29.68 ? 122  LYS L O   1 
ATOM   13181 C  CB  . LYS L  1 122 ? 40.830  10.905  62.262  1.00 31.09 ? 122  LYS L CB  1 
ATOM   13182 C  CG  . LYS L  1 122 ? 39.678  11.669  61.614  1.00 32.01 ? 122  LYS L CG  1 
ATOM   13183 C  CD  . LYS L  1 122 ? 38.325  11.236  62.180  1.00 33.97 ? 122  LYS L CD  1 
ATOM   13184 C  CE  . LYS L  1 122 ? 37.739  12.274  63.113  1.00 39.38 ? 122  LYS L CE  1 
ATOM   13185 N  NZ  . LYS L  1 122 ? 37.423  13.548  62.401  1.00 43.67 ? 122  LYS L NZ  1 
ATOM   13186 N  N   . GLN L  1 123 ? 43.136  9.331   63.008  1.00 28.25 ? 123  GLN L N   1 
ATOM   13187 C  CA  . GLN L  1 123 ? 43.788  8.135   63.515  1.00 27.89 ? 123  GLN L CA  1 
ATOM   13188 C  C   . GLN L  1 123 ? 42.833  6.935   63.612  1.00 29.31 ? 123  GLN L C   1 
ATOM   13189 O  O   . GLN L  1 123 ? 41.672  7.079   63.996  1.00 29.27 ? 123  GLN L O   1 
ATOM   13190 C  CB  . GLN L  1 123 ? 44.365  8.463   64.895  1.00 29.21 ? 123  GLN L CB  1 
ATOM   13191 C  CG  . GLN L  1 123 ? 44.858  7.294   65.715  1.00 29.50 ? 123  GLN L CG  1 
ATOM   13192 C  CD  . GLN L  1 123 ? 45.361  7.732   67.088  1.00 31.96 ? 123  GLN L CD  1 
ATOM   13193 O  OE1 . GLN L  1 123 ? 45.530  8.928   67.362  1.00 29.52 ? 123  GLN L OE1 1 
ATOM   13194 N  NE2 . GLN L  1 123 ? 45.596  6.761   67.958  1.00 30.09 ? 123  GLN L NE2 1 
ATOM   13195 N  N   . ASP L  1 124 ? 43.337  5.754   63.260  1.00 28.63 ? 124  ASP L N   1 
ATOM   13196 C  CA  . ASP L  1 124 ? 42.589  4.496   63.353  1.00 26.67 ? 124  ASP L CA  1 
ATOM   13197 C  C   . ASP L  1 124 ? 42.625  3.967   64.793  1.00 26.64 ? 124  ASP L C   1 
ATOM   13198 O  O   . ASP L  1 124 ? 43.696  3.728   65.349  1.00 25.44 ? 124  ASP L O   1 
ATOM   13199 C  CB  . ASP L  1 124 ? 43.196  3.489   62.358  1.00 25.83 ? 124  ASP L CB  1 
ATOM   13200 C  CG  . ASP L  1 124 ? 42.655  2.069   62.514  1.00 27.37 ? 124  ASP L CG  1 
ATOM   13201 O  OD1 . ASP L  1 124 ? 41.874  1.797   63.446  1.00 25.39 ? 124  ASP L OD1 1 
ATOM   13202 O  OD2 . ASP L  1 124 ? 43.030  1.208   61.685  1.00 27.07 ? 124  ASP L OD2 1 
ATOM   13203 N  N   . ASP L  1 125 ? 41.452  3.784   65.398  1.00 27.69 ? 125  ASP L N   1 
ATOM   13204 C  CA  . ASP L  1 125 ? 41.370  3.375   66.807  1.00 26.24 ? 125  ASP L CA  1 
ATOM   13205 C  C   . ASP L  1 125 ? 41.516  1.858   67.029  1.00 25.82 ? 125  ASP L C   1 
ATOM   13206 O  O   . ASP L  1 125 ? 41.289  1.360   68.133  1.00 24.66 ? 125  ASP L O   1 
ATOM   13207 C  CB  . ASP L  1 125 ? 40.092  3.921   67.466  1.00 23.70 ? 125  ASP L CB  1 
ATOM   13208 C  CG  . ASP L  1 125 ? 38.818  3.247   66.958  1.00 26.02 ? 125  ASP L CG  1 
ATOM   13209 O  OD1 . ASP L  1 125 ? 38.883  2.072   66.532  1.00 26.37 ? 125  ASP L OD1 1 
ATOM   13210 O  OD2 . ASP L  1 125 ? 37.744  3.890   67.012  1.00 24.64 ? 125  ASP L OD2 1 
ATOM   13211 N  N   . LEU L  1 126 ? 41.915  1.150   65.970  1.00 27.23 ? 126  LEU L N   1 
ATOM   13212 C  CA  . LEU L  1 126 ? 42.161  -0.299  65.977  1.00 27.46 ? 126  LEU L CA  1 
ATOM   13213 C  C   . LEU L  1 126 ? 40.977  -1.197  66.430  1.00 26.32 ? 126  LEU L C   1 
ATOM   13214 O  O   . LEU L  1 126 ? 41.187  -2.308  66.914  1.00 27.67 ? 126  LEU L O   1 
ATOM   13215 C  CB  . LEU L  1 126 ? 43.456  -0.630  66.740  1.00 28.13 ? 126  LEU L CB  1 
ATOM   13216 C  CG  . LEU L  1 126 ? 44.636  0.325   66.505  1.00 25.57 ? 126  LEU L CG  1 
ATOM   13217 C  CD1 . LEU L  1 126 ? 45.870  -0.110  67.278  1.00 28.56 ? 126  LEU L CD1 1 
ATOM   13218 C  CD2 . LEU L  1 126 ? 44.960  0.449   65.031  1.00 28.54 ? 126  LEU L CD2 1 
ATOM   13219 N  N   . GLY L  1 127 ? 39.745  -0.723  66.248  1.00 24.54 ? 127  GLY L N   1 
ATOM   13220 C  CA  . GLY L  1 127 ? 38.564  -1.518  66.556  1.00 25.30 ? 127  GLY L CA  1 
ATOM   13221 C  C   . GLY L  1 127 ? 38.174  -1.502  68.028  1.00 27.72 ? 127  GLY L C   1 
ATOM   13222 O  O   . GLY L  1 127 ? 37.227  -2.180  68.447  1.00 27.84 ? 127  GLY L O   1 
ATOM   13223 N  N   . LYS L  1 128 ? 38.903  -0.704  68.805  1.00 27.13 ? 128  LYS L N   1 
ATOM   13224 C  CA  . LYS L  1 128 ? 38.779  -0.655  70.256  1.00 25.04 ? 128  LYS L CA  1 
ATOM   13225 C  C   . LYS L  1 128 ? 38.070  0.628   70.715  1.00 27.01 ? 128  LYS L C   1 
ATOM   13226 O  O   . LYS L  1 128 ? 38.177  1.042   71.882  1.00 24.18 ? 128  LYS L O   1 
ATOM   13227 C  CB  . LYS L  1 128 ? 40.180  -0.726  70.864  1.00 23.95 ? 128  LYS L CB  1 
ATOM   13228 C  CG  . LYS L  1 128 ? 40.954  -1.943  70.409  1.00 25.70 ? 128  LYS L CG  1 
ATOM   13229 C  CD  . LYS L  1 128 ? 42.421  -1.863  70.764  1.00 27.15 ? 128  LYS L CD  1 
ATOM   13230 C  CE  . LYS L  1 128 ? 43.081  -3.195  70.476  1.00 31.81 ? 128  LYS L CE  1 
ATOM   13231 N  NZ  . LYS L  1 128 ? 42.528  -4.268  71.370  1.00 40.55 ? 128  LYS L NZ  1 
ATOM   13232 N  N   . GLY L  1 129 ? 37.344  1.246   69.786  1.00 26.21 ? 129  GLY L N   1 
ATOM   13233 C  CA  . GLY L  1 129 ? 36.738  2.546   70.013  1.00 24.80 ? 129  GLY L CA  1 
ATOM   13234 C  C   . GLY L  1 129 ? 35.384  2.457   70.672  1.00 22.14 ? 129  GLY L C   1 
ATOM   13235 O  O   . GLY L  1 129 ? 34.857  3.464   71.133  1.00 22.66 ? 129  GLY L O   1 
ATOM   13236 N  N   . GLY L  1 130 ? 34.811  1.257   70.705  1.00 21.47 ? 130  GLY L N   1 
ATOM   13237 C  CA  . GLY L  1 130 ? 33.578  1.032   71.440  1.00 22.55 ? 130  GLY L CA  1 
ATOM   13238 C  C   . GLY L  1 130 ? 32.317  1.563   70.783  1.00 22.41 ? 130  GLY L C   1 
ATOM   13239 O  O   . GLY L  1 130 ? 31.329  1.837   71.462  1.00 20.18 ? 130  GLY L O   1 
ATOM   13240 N  N   . ASN L  1 131 ? 32.357  1.737   69.465  1.00 22.16 ? 131  ASN L N   1 
ATOM   13241 C  CA  . ASN L  1 131 ? 31.146  1.972   68.687  1.00 22.93 ? 131  ASN L CA  1 
ATOM   13242 C  C   . ASN L  1 131 ? 31.182  1.160   67.412  1.00 23.77 ? 131  ASN L C   1 
ATOM   13243 O  O   . ASN L  1 131 ? 32.164  0.477   67.146  1.00 24.77 ? 131  ASN L O   1 
ATOM   13244 C  CB  . ASN L  1 131 ? 30.911  3.454   68.397  1.00 23.32 ? 131  ASN L CB  1 
ATOM   13245 C  CG  . ASN L  1 131 ? 32.119  4.134   67.871  1.00 23.49 ? 131  ASN L CG  1 
ATOM   13246 O  OD1 . ASN L  1 131 ? 32.783  3.629   66.976  1.00 28.34 ? 131  ASN L OD1 1 
ATOM   13247 N  ND2 . ASN L  1 131 ? 32.425  5.292   68.419  1.00 24.76 ? 131  ASN L ND2 1 
ATOM   13248 N  N   . GLU L  1 132 ? 30.107  1.207   66.635  1.00 25.38 ? 132  GLU L N   1 
ATOM   13249 C  CA  . GLU L  1 132 ? 30.025  0.367   65.439  1.00 28.24 ? 132  GLU L CA  1 
ATOM   13250 C  C   . GLU L  1 132 ? 31.024  0.784   64.361  1.00 30.45 ? 132  GLU L C   1 
ATOM   13251 O  O   . GLU L  1 132 ? 31.667  -0.060  63.736  1.00 31.11 ? 132  GLU L O   1 
ATOM   13252 C  CB  . GLU L  1 132 ? 28.625  0.377   64.848  1.00 29.39 ? 132  GLU L CB  1 
ATOM   13253 C  CG  . GLU L  1 132 ? 28.480  -0.683  63.786  1.00 35.26 ? 132  GLU L CG  1 
ATOM   13254 C  CD  . GLU L  1 132 ? 27.086  -0.756  63.225  1.00 48.11 ? 132  GLU L CD  1 
ATOM   13255 O  OE1 . GLU L  1 132 ? 26.298  0.194   63.459  1.00 47.33 ? 132  GLU L OE1 1 
ATOM   13256 O  OE2 . GLU L  1 132 ? 26.788  -1.766  62.546  1.00 47.21 ? 132  GLU L OE2 1 
ATOM   13257 N  N   . GLU L  1 133 ? 31.119  2.089   64.129  1.00 28.69 ? 133  GLU L N   1 
ATOM   13258 C  CA  . GLU L  1 133 ? 32.149  2.654   63.277  1.00 29.14 ? 133  GLU L CA  1 
ATOM   13259 C  C   . GLU L  1 133 ? 33.523  2.054   63.553  1.00 30.18 ? 133  GLU L C   1 
ATOM   13260 O  O   . GLU L  1 133 ? 34.267  1.735   62.622  1.00 32.88 ? 133  GLU L O   1 
ATOM   13261 C  CB  . GLU L  1 133 ? 32.213  4.170   63.464  1.00 30.31 ? 133  GLU L CB  1 
ATOM   13262 C  CG  . GLU L  1 133 ? 31.611  4.929   62.331  1.00 35.54 ? 133  GLU L CG  1 
ATOM   13263 C  CD  . GLU L  1 133 ? 32.194  4.496   61.010  1.00 40.13 ? 133  GLU L CD  1 
ATOM   13264 O  OE1 . GLU L  1 133 ? 33.427  4.623   60.840  1.00 37.04 ? 133  GLU L OE1 1 
ATOM   13265 O  OE2 . GLU L  1 133 ? 31.417  4.027   60.147  1.00 43.19 ? 133  GLU L OE2 1 
ATOM   13266 N  N   . SER L  1 134 ? 33.863  1.911   64.829  1.00 26.95 ? 134  SER L N   1 
ATOM   13267 C  CA  . SER L  1 134 ? 35.178  1.427   65.198  1.00 24.87 ? 134  SER L CA  1 
ATOM   13268 C  C   . SER L  1 134 ? 35.419  0.001   64.714  1.00 28.85 ? 134  SER L C   1 
ATOM   13269 O  O   . SER L  1 134 ? 36.531  -0.349  64.311  1.00 30.40 ? 134  SER L O   1 
ATOM   13270 C  CB  . SER L  1 134 ? 35.376  1.505   66.701  1.00 23.03 ? 134  SER L CB  1 
ATOM   13271 O  OG  . SER L  1 134 ? 36.618  0.937   67.043  1.00 26.33 ? 134  SER L OG  1 
ATOM   13272 N  N   . THR L  1 135 ? 34.376  -0.820  64.739  1.00 27.80 ? 135  THR L N   1 
ATOM   13273 C  CA  . THR L  1 135 ? 34.499  -2.208  64.313  1.00 27.91 ? 135  THR L CA  1 
ATOM   13274 C  C   . THR L  1 135 ? 34.514  -2.356  62.779  1.00 30.46 ? 135  THR L C   1 
ATOM   13275 O  O   . THR L  1 135 ? 34.566  -3.470  62.261  1.00 32.32 ? 135  THR L O   1 
ATOM   13276 C  CB  . THR L  1 135 ? 33.346  -3.033  64.881  1.00 28.22 ? 135  THR L CB  1 
ATOM   13277 O  OG1 . THR L  1 135 ? 32.114  -2.518  64.375  1.00 28.07 ? 135  THR L OG1 1 
ATOM   13278 C  CG2 . THR L  1 135 ? 33.314  -2.911  66.383  1.00 30.63 ? 135  THR L CG2 1 
ATOM   13279 N  N   . LYS L  1 136 ? 34.479  -1.234  62.062  1.00 28.88 ? 136  LYS L N   1 
ATOM   13280 C  CA  . LYS L  1 136 ? 34.350  -1.236  60.608  1.00 27.43 ? 136  LYS L CA  1 
ATOM   13281 C  C   . LYS L  1 136 ? 35.457  -0.457  59.894  1.00 29.80 ? 136  LYS L C   1 
ATOM   13282 O  O   . LYS L  1 136 ? 36.066  -0.964  58.938  1.00 29.20 ? 136  LYS L O   1 
ATOM   13283 C  CB  . LYS L  1 136 ? 32.980  -0.676  60.204  1.00 28.29 ? 136  LYS L CB  1 
ATOM   13284 C  CG  . LYS L  1 136 ? 31.860  -1.706  60.239  1.00 32.29 ? 136  LYS L CG  1 
ATOM   13285 C  CD  . LYS L  1 136 ? 30.494  -1.093  60.558  1.00 36.44 ? 136  LYS L CD  1 
ATOM   13286 C  CE  . LYS L  1 136 ? 29.929  -0.260  59.416  1.00 39.49 ? 136  LYS L CE  1 
ATOM   13287 N  NZ  . LYS L  1 136 ? 30.735  0.970   59.161  1.00 40.93 ? 136  LYS L NZ  1 
ATOM   13288 N  N   . THR L  1 137 ? 35.699  0.776   60.340  1.00 27.41 ? 137  THR L N   1 
ATOM   13289 C  CA  . THR L  1 137 ? 36.699  1.634   59.707  1.00 28.49 ? 137  THR L CA  1 
ATOM   13290 C  C   . THR L  1 137 ? 37.769  2.090   60.691  1.00 28.67 ? 137  THR L C   1 
ATOM   13291 O  O   . THR L  1 137 ? 38.766  2.703   60.299  1.00 28.10 ? 137  THR L O   1 
ATOM   13292 C  CB  . THR L  1 137 ? 36.063  2.894   59.080  1.00 30.05 ? 137  THR L CB  1 
ATOM   13293 O  OG1 . THR L  1 137 ? 35.465  3.690   60.107  1.00 27.63 ? 137  THR L OG1 1 
ATOM   13294 C  CG2 . THR L  1 137 ? 35.012  2.521   58.057  1.00 27.78 ? 137  THR L CG2 1 
ATOM   13295 N  N   . GLY L  1 138 ? 37.551  1.803   61.973  1.00 30.46 ? 138  GLY L N   1 
ATOM   13296 C  CA  . GLY L  1 138 ? 38.446  2.249   63.020  1.00 25.83 ? 138  GLY L CA  1 
ATOM   13297 C  C   . GLY L  1 138 ? 38.342  3.745   63.244  1.00 25.61 ? 138  GLY L C   1 
ATOM   13298 O  O   . GLY L  1 138 ? 39.268  4.366   63.750  1.00 28.20 ? 138  GLY L O   1 
ATOM   13299 N  N   . ASN L  1 139 ? 37.212  4.331   62.871  1.00 26.22 ? 139  ASN L N   1 
ATOM   13300 C  CA  . ASN L  1 139 ? 37.018  5.771   63.037  1.00 29.05 ? 139  ASN L CA  1 
ATOM   13301 C  C   . ASN L  1 139 ? 38.149  6.613   62.418  1.00 27.78 ? 139  ASN L C   1 
ATOM   13302 O  O   . ASN L  1 139 ? 38.493  7.681   62.932  1.00 26.05 ? 139  ASN L O   1 
ATOM   13303 C  CB  . ASN L  1 139 ? 36.832  6.129   64.526  1.00 29.69 ? 139  ASN L CB  1 
ATOM   13304 C  CG  . ASN L  1 139 ? 35.460  5.731   65.068  1.00 27.41 ? 139  ASN L CG  1 
ATOM   13305 O  OD1 . ASN L  1 139 ? 34.428  6.135   64.536  1.00 29.15 ? 139  ASN L OD1 1 
ATOM   13306 N  ND2 . ASN L  1 139 ? 35.449  4.949   66.136  1.00 25.20 ? 139  ASN L ND2 1 
ATOM   13307 N  N   . ALA L  1 140 ? 38.709  6.139   61.307  1.00 28.90 ? 140  ALA L N   1 
ATOM   13308 C  CA  . ALA L  1 140 ? 39.781  6.861   60.613  1.00 28.84 ? 140  ALA L CA  1 
ATOM   13309 C  C   . ALA L  1 140 ? 39.299  8.027   59.732  1.00 29.48 ? 140  ALA L C   1 
ATOM   13310 O  O   . ALA L  1 140 ? 40.105  8.786   59.195  1.00 28.41 ? 140  ALA L O   1 
ATOM   13311 C  CB  . ALA L  1 140 ? 40.645  5.893   59.808  1.00 25.59 ? 140  ALA L CB  1 
ATOM   13312 N  N   . GLY L  1 141 ? 37.989  8.173   59.580  1.00 28.31 ? 141  GLY L N   1 
ATOM   13313 C  CA  . GLY L  1 141 ? 37.456  9.324   58.875  1.00 29.72 ? 141  GLY L CA  1 
ATOM   13314 C  C   . GLY L  1 141 ? 37.648  9.311   57.369  1.00 33.07 ? 141  GLY L C   1 
ATOM   13315 O  O   . GLY L  1 141 ? 37.752  8.251   56.747  1.00 34.20 ? 141  GLY L O   1 
ATOM   13316 N  N   . SER L  1 142 ? 37.693  10.500  56.774  1.00 32.85 ? 142  SER L N   1 
ATOM   13317 C  CA  . SER L  1 142 ? 37.695  10.624  55.315  1.00 31.89 ? 142  SER L CA  1 
ATOM   13318 C  C   . SER L  1 142 ? 38.949  10.055  54.660  1.00 30.12 ? 142  SER L C   1 
ATOM   13319 O  O   . SER L  1 142 ? 39.920  9.721   55.333  1.00 30.55 ? 142  SER L O   1 
ATOM   13320 C  CB  . SER L  1 142 ? 37.481  12.079  54.877  1.00 31.41 ? 142  SER L CB  1 
ATOM   13321 O  OG  . SER L  1 142 ? 38.703  12.790  54.843  1.00 32.23 ? 142  SER L OG  1 
ATOM   13322 N  N   . ARG L  1 143 ? 38.911  9.955   53.335  1.00 31.30 ? 143  ARG L N   1 
ATOM   13323 C  CA  . ARG L  1 143 ? 39.998  9.367   52.560  1.00 29.59 ? 143  ARG L CA  1 
ATOM   13324 C  C   . ARG L  1 143 ? 40.814  10.479  51.905  1.00 31.22 ? 143  ARG L C   1 
ATOM   13325 O  O   . ARG L  1 143 ? 40.320  11.172  51.023  1.00 31.82 ? 143  ARG L O   1 
ATOM   13326 C  CB  . ARG L  1 143 ? 39.422  8.401   51.513  1.00 29.68 ? 143  ARG L CB  1 
ATOM   13327 C  CG  . ARG L  1 143 ? 38.899  7.096   52.109  1.00 29.12 ? 143  ARG L CG  1 
ATOM   13328 C  CD  . ARG L  1 143 ? 37.786  6.445   51.289  1.00 28.33 ? 143  ARG L CD  1 
ATOM   13329 N  NE  . ARG L  1 143 ? 37.111  5.405   52.072  1.00 30.18 ? 143  ARG L NE  1 
ATOM   13330 C  CZ  . ARG L  1 143 ? 36.486  4.348   51.557  1.00 29.88 ? 143  ARG L CZ  1 
ATOM   13331 N  NH1 . ARG L  1 143 ? 36.451  4.166   50.247  1.00 30.55 ? 143  ARG L NH1 1 
ATOM   13332 N  NH2 . ARG L  1 143 ? 35.909  3.460   52.356  1.00 28.27 ? 143  ARG L NH2 1 
ATOM   13333 N  N   . LEU L  1 144 ? 42.060  10.652  52.349  1.00 32.78 ? 144  LEU L N   1 
ATOM   13334 C  CA  . LEU L  1 144 ? 42.879  11.806  51.955  1.00 31.44 ? 144  LEU L CA  1 
ATOM   13335 C  C   . LEU L  1 144 ? 43.543  11.622  50.604  1.00 34.49 ? 144  LEU L C   1 
ATOM   13336 O  O   . LEU L  1 144 ? 43.555  12.535  49.778  1.00 34.79 ? 144  LEU L O   1 
ATOM   13337 C  CB  . LEU L  1 144 ? 43.951  12.109  53.004  1.00 34.34 ? 144  LEU L CB  1 
ATOM   13338 C  CG  . LEU L  1 144 ? 43.534  12.514  54.420  1.00 31.32 ? 144  LEU L CG  1 
ATOM   13339 C  CD1 . LEU L  1 144 ? 44.776  12.806  55.244  1.00 28.54 ? 144  LEU L CD1 1 
ATOM   13340 C  CD2 . LEU L  1 144 ? 42.593  13.710  54.385  1.00 27.62 ? 144  LEU L CD2 1 
ATOM   13341 N  N   . ALA L  1 145 ? 44.116  10.443  50.397  1.00 35.27 ? 145  ALA L N   1 
ATOM   13342 C  CA  . ALA L  1 145 ? 44.702  10.090  49.112  1.00 34.38 ? 145  ALA L CA  1 
ATOM   13343 C  C   . ALA L  1 145 ? 44.711  8.570   48.915  1.00 34.84 ? 145  ALA L C   1 
ATOM   13344 O  O   . ALA L  1 145 ? 44.698  7.804   49.878  1.00 33.30 ? 145  ALA L O   1 
ATOM   13345 C  CB  . ALA L  1 145 ? 46.107  10.664  48.990  1.00 35.58 ? 145  ALA L CB  1 
ATOM   13346 N  N   . CYS L  1 146 ? 44.725  8.141   47.658  1.00 37.47 ? 146  CYS L N   1 
ATOM   13347 C  CA  . CYS L  1 146 ? 44.678  6.720   47.332  1.00 35.69 ? 146  CYS L CA  1 
ATOM   13348 C  C   . CYS L  1 146 ? 45.409  6.436   46.024  1.00 34.13 ? 146  CYS L C   1 
ATOM   13349 O  O   . CYS L  1 146 ? 45.768  7.350   45.277  1.00 33.56 ? 146  CYS L O   1 
ATOM   13350 C  CB  . CYS L  1 146 ? 43.224  6.230   47.230  1.00 32.60 ? 146  CYS L CB  1 
ATOM   13351 S  SG  . CYS L  1 146 ? 42.263  6.956   45.870  1.00 40.74 ? 146  CYS L SG  1 
ATOM   13352 N  N   . GLY L  1 147 ? 45.618  5.154   45.759  1.00 30.86 ? 147  GLY L N   1 
ATOM   13353 C  CA  . GLY L  1 147 ? 46.271  4.717   44.550  1.00 30.93 ? 147  GLY L CA  1 
ATOM   13354 C  C   . GLY L  1 147 ? 46.083  3.224   44.417  1.00 30.88 ? 147  GLY L C   1 
ATOM   13355 O  O   . GLY L  1 147 ? 45.997  2.512   45.418  1.00 30.05 ? 147  GLY L O   1 
ATOM   13356 N  N   . VAL L  1 148 ? 46.007  2.747   43.180  1.00 31.35 ? 148  VAL L N   1 
ATOM   13357 C  CA  . VAL L  1 148 ? 45.889  1.321   42.932  1.00 31.24 ? 148  VAL L CA  1 
ATOM   13358 C  C   . VAL L  1 148 ? 47.256  0.682   43.087  1.00 29.49 ? 148  VAL L C   1 
ATOM   13359 O  O   . VAL L  1 148 ? 48.274  1.245   42.669  1.00 29.56 ? 148  VAL L O   1 
ATOM   13360 C  CB  . VAL L  1 148 ? 45.346  1.029   41.516  1.00 31.74 ? 148  VAL L CB  1 
ATOM   13361 C  CG1 . VAL L  1 148 ? 45.102  -0.469  41.331  1.00 28.72 ? 148  VAL L CG1 1 
ATOM   13362 C  CG2 . VAL L  1 148 ? 44.080  1.823   41.256  1.00 30.24 ? 148  VAL L CG2 1 
ATOM   13363 N  N   . ILE L  1 149 ? 47.275  -0.502  43.685  1.00 31.81 ? 149  ILE L N   1 
ATOM   13364 C  CA  . ILE L  1 149 ? 48.516  -1.228  43.911  1.00 32.87 ? 149  ILE L CA  1 
ATOM   13365 C  C   . ILE L  1 149 ? 48.958  -1.992  42.651  1.00 34.03 ? 149  ILE L C   1 
ATOM   13366 O  O   . ILE L  1 149 ? 48.406  -3.054  42.328  1.00 32.35 ? 149  ILE L O   1 
ATOM   13367 C  CB  . ILE L  1 149 ? 48.393  -2.188  45.126  1.00 34.58 ? 149  ILE L CB  1 
ATOM   13368 C  CG1 . ILE L  1 149 ? 47.991  -1.422  46.391  1.00 29.86 ? 149  ILE L CG1 1 
ATOM   13369 C  CG2 . ILE L  1 149 ? 49.704  -2.962  45.352  1.00 32.09 ? 149  ILE L CG2 1 
ATOM   13370 C  CD1 . ILE L  1 149 ? 47.723  -2.330  47.569  1.00 28.23 ? 149  ILE L CD1 1 
ATOM   13371 N  N   . GLY L  1 150 ? 49.957  -1.447  41.953  1.00 31.78 ? 150  GLY L N   1 
ATOM   13372 C  CA  . GLY L  1 150 ? 50.446  -2.036  40.717  1.00 33.79 ? 150  GLY L CA  1 
ATOM   13373 C  C   . GLY L  1 150 ? 51.770  -2.787  40.793  1.00 34.47 ? 150  GLY L C   1 
ATOM   13374 O  O   . GLY L  1 150 ? 52.618  -2.485  41.626  1.00 36.44 ? 150  GLY L O   1 
ATOM   13375 N  N   . ILE L  1 151 ? 51.943  -3.773  39.913  1.00 34.24 ? 151  ILE L N   1 
ATOM   13376 C  CA  . ILE L  1 151 ? 53.180  -4.547  39.826  1.00 36.15 ? 151  ILE L CA  1 
ATOM   13377 C  C   . ILE L  1 151 ? 54.345  -3.639  39.410  1.00 36.36 ? 151  ILE L C   1 
ATOM   13378 O  O   . ILE L  1 151 ? 54.242  -2.896  38.430  1.00 35.56 ? 151  ILE L O   1 
ATOM   13379 C  CB  . ILE L  1 151 ? 53.037  -5.716  38.816  1.00 31.63 ? 151  ILE L CB  1 
ATOM   13380 C  CG1 . ILE L  1 151 ? 52.005  -6.730  39.308  1.00 29.64 ? 151  ILE L CG1 1 
ATOM   13381 C  CG2 . ILE L  1 151 ? 54.355  -6.413  38.600  1.00 32.10 ? 151  ILE L CG2 1 
ATOM   13382 C  CD1 . ILE L  1 151 ? 51.585  -7.723  38.247  1.00 29.98 ? 151  ILE L CD1 1 
ATOM   13383 N  N   . ALA L  1 152 ? 55.439  -3.680  40.166  1.00 35.61 ? 152  ALA L N   1 
ATOM   13384 C  CA  . ALA L  1 152 ? 56.613  -2.878  39.838  1.00 36.27 ? 152  ALA L CA  1 
ATOM   13385 C  C   . ALA L  1 152 ? 57.781  -3.783  39.453  1.00 38.24 ? 152  ALA L C   1 
ATOM   13386 O  O   . ALA L  1 152 ? 57.813  -4.967  39.820  1.00 36.62 ? 152  ALA L O   1 
ATOM   13387 C  CB  . ALA L  1 152 ? 56.988  -1.991  41.002  1.00 36.99 ? 152  ALA L CB  1 
ATOM   13388 N  N   . GLN L  1 153 ? 58.735  -3.239  38.703  1.00 36.74 ? 153  GLN L N   1 
ATOM   13389 C  CA  . GLN L  1 153 ? 59.856  -4.059  38.262  1.00 42.01 ? 153  GLN L CA  1 
ATOM   13390 C  C   . GLN L  1 153 ? 60.874  -4.239  39.369  1.00 49.07 ? 153  GLN L C   1 
ATOM   13391 O  O   . GLN L  1 153 ? 61.361  -5.359  39.584  1.00 49.59 ? 153  GLN L O   1 
ATOM   13392 C  CB  . GLN L  1 153 ? 60.513  -3.509  36.987  1.00 46.62 ? 153  GLN L CB  1 
ATOM   13393 C  CG  . GLN L  1 153 ? 61.422  -2.291  37.128  1.00 46.72 ? 153  GLN L CG  1 
ATOM   13394 C  CD  . GLN L  1 153 ? 62.143  -1.973  35.812  1.00 47.57 ? 153  GLN L CD  1 
ATOM   13395 O  OE1 . GLN L  1 153 ? 62.657  -2.876  35.137  1.00 42.59 ? 153  GLN L OE1 1 
ATOM   13396 N  NE2 . GLN L  1 153 ? 62.171  -0.691  35.440  1.00 45.17 ? 153  GLN L NE2 1 
ATOM   13397 O  OXT . GLN L  1 153 ? 61.197  -3.269  40.065  1.00 53.18 ? 153  GLN L OXT 1 
HETATM 13398 ZN ZN  . ZN  M  2 .   ? 33.169  -32.386 22.742  1.00 23.23 ? 155  ZN  A ZN  1 
HETATM 13399 ZN ZN  . ZN  N  2 .   ? 58.259  -33.127 -7.910  1.00 23.66 ? 155  ZN  B ZN  1 
HETATM 13400 ZN ZN  . ZN  O  2 .   ? 8.930   -33.754 11.272  1.00 22.73 ? 155  ZN  C ZN  1 
HETATM 13401 ZN ZN  . ZN  P  2 .   ? -30.039 -33.509 4.249   1.00 23.44 ? 155  ZN  D ZN  1 
HETATM 13402 ZN ZN  . ZN  Q  2 .   ? 11.722  -29.835 38.083  1.00 31.78 ? 155  ZN  E ZN  1 
HETATM 13403 ZN ZN  . ZN  R  2 .   ? 25.262  -32.667 75.297  1.00 24.11 ? 155  ZN  F ZN  1 
HETATM 13404 ZN ZN  . ZN  S  2 .   ? 54.842  -4.139  -5.774  1.00 22.61 ? 155  ZN  G ZN  1 
HETATM 13405 ZN ZN  . ZN  T  2 .   ? 93.904  -4.470  -12.289 1.00 21.71 ? 155  ZN  H ZN  1 
HETATM 13406 ZN ZN  . ZN  U  2 .   ? 30.967  -4.809  6.557   1.00 24.75 ? 155  ZN  I ZN  1 
HETATM 13407 ZN ZN  . ZN  V  2 .   ? 4.998   -5.649  -23.499 1.00 27.41 ? 155  ZN  J ZN  1 
HETATM 13408 ZN ZN  . ZN  W  2 .   ? 53.494  -4.118  21.483  1.00 29.93 ? 155  ZN  K ZN  1 
HETATM 13409 ZN ZN  . ZN  X  2 .   ? 39.621  -2.524  58.698  1.00 28.32 ? 155  ZN  L ZN  1 
HETATM 13410 O  O   . HOH Y  3 .   ? 24.258  -41.032 10.561  1.00 19.69 ? 154  HOH A O   1 
HETATM 13411 O  O   . HOH Y  3 .   ? 42.423  -39.923 5.941   1.00 17.15 ? 156  HOH A O   1 
HETATM 13412 O  O   . HOH Y  3 .   ? 35.834  -24.716 21.221  1.00 22.61 ? 157  HOH A O   1 
HETATM 13413 O  O   . HOH Y  3 .   ? 33.714  -38.409 22.956  1.00 22.37 ? 158  HOH A O   1 
HETATM 13414 O  O   . HOH Y  3 .   ? 21.815  -37.934 22.916  1.00 20.18 ? 159  HOH A O   1 
HETATM 13415 O  O   . HOH Y  3 .   ? 36.853  -50.759 14.592  1.00 23.59 ? 160  HOH A O   1 
HETATM 13416 O  O   . HOH Y  3 .   ? 28.734  -33.495 20.292  1.00 20.44 ? 161  HOH A O   1 
HETATM 13417 O  O   . HOH Y  3 .   ? 49.406  -38.687 12.062  1.00 17.92 ? 162  HOH A O   1 
HETATM 13418 O  O   . HOH Y  3 .   ? 30.125  -50.489 17.049  1.00 17.23 ? 163  HOH A O   1 
HETATM 13419 O  O   . HOH Y  3 .   ? 39.784  -45.714 22.804  1.00 17.17 ? 164  HOH A O   1 
HETATM 13420 O  O   . HOH Y  3 .   ? 37.228  -33.784 24.786  1.00 24.96 ? 165  HOH A O   1 
HETATM 13421 O  O   . HOH Y  3 .   ? 22.467  -30.673 19.605  1.00 25.88 ? 166  HOH A O   1 
HETATM 13422 O  O   . HOH Y  3 .   ? 39.194  -50.799 10.720  1.00 27.36 ? 167  HOH A O   1 
HETATM 13423 O  O   . HOH Y  3 .   ? 22.633  -36.703 18.739  1.00 23.94 ? 168  HOH A O   1 
HETATM 13424 O  O   . HOH Y  3 .   ? 50.401  -34.863 18.735  1.00 23.69 ? 169  HOH A O   1 
HETATM 13425 O  O   . HOH Y  3 .   ? 37.441  -20.512 11.323  1.00 29.73 ? 170  HOH A O   1 
HETATM 13426 O  O   . HOH Y  3 .   ? 40.875  -35.678 -3.897  1.00 17.85 ? 171  HOH A O   1 
HETATM 13427 O  O   . HOH Y  3 .   ? 32.032  -22.329 9.047   1.00 27.27 ? 181  HOH A O   1 
HETATM 13428 O  O   . HOH Y  3 .   ? 29.649  -23.084 2.479   1.00 32.04 ? 196  HOH A O   1 
HETATM 13429 O  O   . HOH Y  3 .   ? 33.071  -38.804 35.334  1.00 30.82 ? 202  HOH A O   1 
HETATM 13430 O  O   . HOH Y  3 .   ? 32.792  -17.103 0.432   1.00 29.05 ? 214  HOH A O   1 
HETATM 13431 O  O   . HOH Y  3 .   ? 39.864  -37.165 26.172  1.00 24.06 ? 219  HOH A O   1 
HETATM 13432 O  O   . HOH Y  3 .   ? 43.527  -44.399 11.395  1.00 23.58 ? 241  HOH A O   1 
HETATM 13433 O  O   . HOH Y  3 .   ? 35.484  -39.838 -1.004  1.00 22.61 ? 243  HOH A O   1 
HETATM 13434 O  O   . HOH Y  3 .   ? 26.216  -33.689 -1.204  1.00 31.63 ? 266  HOH A O   1 
HETATM 13435 O  O   . HOH Y  3 .   ? 24.988  -45.993 23.554  1.00 25.87 ? 280  HOH A O   1 
HETATM 13436 O  O   . HOH Y  3 .   ? 36.202  -29.925 28.082  1.00 28.37 ? 291  HOH A O   1 
HETATM 13437 O  O   . HOH Y  3 .   ? 25.519  -39.704 2.662   1.00 24.50 ? 294  HOH A O   1 
HETATM 13438 O  O   . HOH Y  3 .   ? 30.061  -49.832 19.836  1.00 19.53 ? 296  HOH A O   1 
HETATM 13439 O  O   . HOH Y  3 .   ? 29.944  -41.880 33.368  1.00 27.36 ? 308  HOH A O   1 
HETATM 13440 O  O   . HOH Y  3 .   ? 38.399  -17.141 10.708  1.00 33.45 ? 328  HOH A O   1 
HETATM 13441 O  O   . HOH Y  3 .   ? 27.298  -27.933 26.748  1.00 28.24 ? 345  HOH A O   1 
HETATM 13442 O  O   . HOH Y  3 .   ? 25.855  -42.196 2.396   1.00 24.88 ? 352  HOH A O   1 
HETATM 13443 O  O   . HOH Y  3 .   ? 47.538  -44.461 9.928   1.00 32.10 ? 393  HOH A O   1 
HETATM 13444 O  O   . HOH Y  3 .   ? 26.540  -35.897 -2.721  1.00 34.98 ? 395  HOH A O   1 
HETATM 13445 O  O   . HOH Y  3 .   ? 26.629  -42.918 26.443  1.00 25.57 ? 401  HOH A O   1 
HETATM 13446 O  O   . HOH Y  3 .   ? 38.079  -36.594 24.192  1.00 26.54 ? 403  HOH A O   1 
HETATM 13447 O  O   . HOH Y  3 .   ? 21.212  -57.326 11.110  1.00 28.89 ? 412  HOH A O   1 
HETATM 13448 O  O   . HOH Y  3 .   ? 32.931  -36.801 37.172  1.00 29.85 ? 418  HOH A O   1 
HETATM 13449 O  O   . HOH Y  3 .   ? 43.473  -39.541 24.123  1.00 27.50 ? 427  HOH A O   1 
HETATM 13450 O  O   . HOH Y  3 .   ? 25.443  -29.290 13.258  1.00 26.10 ? 429  HOH A O   1 
HETATM 13451 O  O   . HOH Y  3 .   ? 25.671  -40.092 29.968  1.00 28.99 ? 441  HOH A O   1 
HETATM 13452 O  O   . HOH Y  3 .   ? 21.913  -36.316 27.342  1.00 27.17 ? 443  HOH A O   1 
HETATM 13453 O  O   . HOH Y  3 .   ? 35.452  -35.109 -0.413  1.00 24.09 ? 445  HOH A O   1 
HETATM 13454 O  O   . HOH Y  3 .   ? 31.751  -52.215 16.111  1.00 16.19 ? 447  HOH A O   1 
HETATM 13455 O  O   . HOH Y  3 .   ? 51.304  -37.616 21.532  1.00 38.64 ? 471  HOH A O   1 
HETATM 13456 O  O   . HOH Y  3 .   ? 35.827  -14.604 3.713   1.00 29.37 ? 480  HOH A O   1 
HETATM 13457 O  O   . HOH Y  3 .   ? 30.013  -38.238 -1.915  1.00 31.40 ? 502  HOH A O   1 
HETATM 13458 O  O   . HOH Y  3 .   ? 22.801  -47.166 4.571   1.00 25.32 ? 510  HOH A O   1 
HETATM 13459 O  O   . HOH Y  3 .   ? 22.219  -33.886 9.860   1.00 18.77 ? 517  HOH A O   1 
HETATM 13460 O  O   . HOH Y  3 .   ? 35.127  -40.586 24.501  1.00 24.37 ? 526  HOH A O   1 
HETATM 13461 O  O   . HOH Y  3 .   ? 33.096  -23.535 20.502  1.00 24.89 ? 531  HOH A O   1 
HETATM 13462 O  O   . HOH Y  3 .   ? 42.422  -37.124 25.287  1.00 33.06 ? 540  HOH A O   1 
HETATM 13463 O  O   . HOH Y  3 .   ? 18.095  -50.207 9.416   1.00 28.53 ? 545  HOH A O   1 
HETATM 13464 O  O   . HOH Y  3 .   ? 20.725  -54.495 15.170  1.00 24.42 ? 546  HOH A O   1 
HETATM 13465 O  O   . HOH Y  3 .   ? 21.897  -48.656 7.347   1.00 24.24 ? 555  HOH A O   1 
HETATM 13466 O  O   . HOH Y  3 .   ? 37.218  -39.339 23.764  1.00 25.83 ? 569  HOH A O   1 
HETATM 13467 O  O   . HOH Y  3 .   ? 20.748  -33.628 31.820  1.00 28.75 ? 579  HOH A O   1 
HETATM 13468 O  O   . HOH Y  3 .   ? 43.040  -43.588 7.781   1.00 25.47 ? 591  HOH A O   1 
HETATM 13469 O  O   . HOH Y  3 .   ? 46.144  -27.444 17.810  1.00 27.03 ? 629  HOH A O   1 
HETATM 13470 O  O   . HOH Y  3 .   ? 24.824  -35.184 14.574  1.00 20.17 ? 632  HOH A O   1 
HETATM 13471 O  O   . HOH Y  3 .   ? 21.769  -33.069 5.938   1.00 28.40 ? 635  HOH A O   1 
HETATM 13472 O  O   . HOH Y  3 .   ? 43.094  -25.037 6.986   1.00 27.74 ? 651  HOH A O   1 
HETATM 13473 O  O   . HOH Y  3 .   ? 19.585  -51.620 7.561   1.00 24.88 ? 655  HOH A O   1 
HETATM 13474 O  O   . HOH Y  3 .   ? 32.984  -23.449 29.917  1.00 36.92 ? 673  HOH A O   1 
HETATM 13475 O  O   . HOH Y  3 .   ? 30.627  -33.029 -4.763  1.00 35.64 ? 674  HOH A O   1 
HETATM 13476 O  O   . HOH Y  3 .   ? 44.506  -40.923 8.225   1.00 20.23 ? 682  HOH A O   1 
HETATM 13477 O  O   . HOH Y  3 .   ? 33.250  -53.401 8.765   1.00 26.72 ? 685  HOH A O   1 
HETATM 13478 O  O   . HOH Y  3 .   ? 22.736  -31.446 10.203  1.00 20.21 ? 699  HOH A O   1 
HETATM 13479 O  O   . HOH Y  3 .   ? 24.807  -46.618 20.601  1.00 22.58 ? 712  HOH A O   1 
HETATM 13480 O  O   . HOH Y  3 .   ? 23.496  -54.028 16.738  1.00 20.12 ? 730  HOH A O   1 
HETATM 13481 O  O   . HOH Y  3 .   ? 28.143  -28.113 0.557   1.00 33.35 ? 740  HOH A O   1 
HETATM 13482 O  O   . HOH Y  3 .   ? 27.869  -33.487 -3.053  1.00 35.18 ? 750  HOH A O   1 
HETATM 13483 O  O   . HOH Y  3 .   ? 16.978  -47.598 15.065  1.00 36.07 ? 755  HOH A O   1 
HETATM 13484 O  O   . HOH Y  3 .   ? 45.145  -26.192 6.669   1.00 28.68 ? 772  HOH A O   1 
HETATM 13485 O  O   . HOH Y  3 .   ? 44.498  -41.647 11.048  1.00 26.04 ? 775  HOH A O   1 
HETATM 13486 O  O   . HOH Y  3 .   ? 28.317  -26.144 1.850   1.00 28.32 ? 789  HOH A O   1 
HETATM 13487 O  O   . HOH Y  3 .   ? 41.792  -25.331 24.395  1.00 29.32 ? 800  HOH A O   1 
HETATM 13488 O  O   . HOH Y  3 .   ? 20.731  -36.805 20.912  1.00 28.46 ? 801  HOH A O   1 
HETATM 13489 O  O   . HOH Y  3 .   ? 24.764  -48.985 19.578  1.00 21.87 ? 817  HOH A O   1 
HETATM 13490 O  O   . HOH Y  3 .   ? 42.179  -41.976 24.546  1.00 29.86 ? 821  HOH A O   1 
HETATM 13491 O  O   . HOH Y  3 .   ? 22.579  -22.885 23.277  1.00 34.99 ? 824  HOH A O   1 
HETATM 13492 O  O   . HOH Y  3 .   ? 26.241  -40.637 -1.346  1.00 38.42 ? 835  HOH A O   1 
HETATM 13493 O  O   . HOH Y  3 .   ? 50.121  -46.160 13.549  1.00 31.60 ? 847  HOH A O   1 
HETATM 13494 O  O   . HOH Y  3 .   ? 24.069  -36.391 1.791   1.00 30.77 ? 849  HOH A O   1 
HETATM 13495 O  O   . HOH Y  3 .   ? 43.966  -46.148 13.815  1.00 31.81 ? 855  HOH A O   1 
HETATM 13496 O  O   . HOH Y  3 .   ? 24.269  -56.402 16.504  1.00 22.59 ? 862  HOH A O   1 
HETATM 13497 O  O   . HOH Y  3 .   ? 51.192  -40.408 21.545  1.00 37.40 ? 870  HOH A O   1 
HETATM 13498 O  O   . HOH Y  3 .   ? 46.167  -47.665 12.985  1.00 37.10 ? 876  HOH A O   1 
HETATM 13499 O  O   . HOH Y  3 .   ? 18.623  -46.098 16.724  1.00 29.52 ? 908  HOH A O   1 
HETATM 13500 O  O   . HOH Y  3 .   ? 19.377  -54.516 7.316   1.00 29.55 ? 911  HOH A O   1 
HETATM 13501 O  O   . HOH Y  3 .   ? 48.503  -47.356 15.292  1.00 32.73 ? 912  HOH A O   1 
HETATM 13502 O  O   . HOH Y  3 .   ? 22.106  -44.440 8.746   1.00 21.25 ? 924  HOH A O   1 
HETATM 13503 O  O   . HOH Y  3 .   ? 24.442  -53.451 13.204  1.00 20.67 ? 933  HOH A O   1 
HETATM 13504 O  O   . HOH Y  3 .   ? 33.345  -20.921 12.548  1.00 33.61 ? 936  HOH A O   1 
HETATM 13505 O  O   . HOH Y  3 .   ? 24.315  -56.038 13.454  1.00 20.93 ? 948  HOH A O   1 
HETATM 13506 O  O   . HOH Y  3 .   ? 23.530  -31.221 13.000  1.00 25.30 ? 955  HOH A O   1 
HETATM 13507 O  O   . HOH Y  3 .   ? 33.504  -41.333 27.180  1.00 28.75 ? 965  HOH A O   1 
HETATM 13508 O  O   . HOH Y  3 .   ? 40.547  -43.662 23.534  1.00 33.67 ? 978  HOH A O   1 
HETATM 13509 O  O   . HOH Y  3 .   ? 44.414  -39.636 13.783  1.00 23.67 ? 990  HOH A O   1 
HETATM 13510 O  O   . HOH Y  3 .   ? 37.561  -49.017 20.909  1.00 26.02 ? 1013 HOH A O   1 
HETATM 13511 O  O   . HOH Y  3 .   ? 25.715  -25.708 13.372  1.00 26.25 ? 1018 HOH A O   1 
HETATM 13512 O  O   . HOH Y  3 .   ? 44.381  -26.630 9.427   1.00 23.44 ? 1024 HOH A O   1 
HETATM 13513 O  O   . HOH Y  3 .   ? 48.827  -41.029 22.609  1.00 29.33 ? 1026 HOH A O   1 
HETATM 13514 O  O   . HOH Y  3 .   ? 22.320  -32.817 16.817  1.00 30.86 ? 1037 HOH A O   1 
HETATM 13515 O  O   . HOH Y  3 .   ? 18.604  -51.977 5.124   1.00 31.77 ? 1054 HOH A O   1 
HETATM 13516 O  O   . HOH Y  3 .   ? 35.840  -20.181 -1.619  1.00 38.02 ? 1062 HOH A O   1 
HETATM 13517 O  O   . HOH Y  3 .   ? 27.550  -20.752 26.324  1.00 44.89 ? 1063 HOH A O   1 
HETATM 13518 O  O   . HOH Y  3 .   ? 42.395  -28.264 -3.339  1.00 29.84 ? 1071 HOH A O   1 
HETATM 13519 O  O   . HOH Y  3 .   ? 31.672  -43.339 29.385  1.00 31.26 ? 1074 HOH A O   1 
HETATM 13520 O  O   . HOH Y  3 .   ? 42.787  -24.781 13.184  1.00 26.52 ? 1087 HOH A O   1 
HETATM 13521 O  O   . HOH Y  3 .   ? 30.052  -44.481 33.103  1.00 32.38 ? 1099 HOH A O   1 
HETATM 13522 O  O   . HOH Y  3 .   ? 41.602  -27.854 20.830  1.00 25.34 ? 1110 HOH A O   1 
HETATM 13523 O  O   . HOH Y  3 .   ? 31.425  -42.303 1.158   1.00 23.88 ? 1111 HOH A O   1 
HETATM 13524 O  O   . HOH Y  3 .   ? 45.669  -46.042 9.009   1.00 34.02 ? 1121 HOH A O   1 
HETATM 13525 O  O   . HOH Y  3 .   ? 44.910  -24.781 11.640  1.00 29.59 ? 1127 HOH A O   1 
HETATM 13526 O  O   . HOH Y  3 .   ? 25.518  -36.827 -0.813  1.00 33.43 ? 1132 HOH A O   1 
HETATM 13527 O  O   . HOH Y  3 .   ? 17.102  -46.269 21.923  1.00 35.69 ? 1147 HOH A O   1 
HETATM 13528 O  O   . HOH Y  3 .   ? 46.989  -51.795 16.546  1.00 44.78 ? 1161 HOH A O   1 
HETATM 13529 O  O   . HOH Y  3 .   ? 17.900  -43.969 21.949  1.00 30.24 ? 1164 HOH A O   1 
HETATM 13530 O  O   . HOH Y  3 .   ? 21.393  -56.068 7.447   1.00 31.71 ? 1182 HOH A O   1 
HETATM 13531 O  O   . HOH Y  3 .   ? 52.948  -41.617 20.215  1.00 30.09 ? 1199 HOH A O   1 
HETATM 13532 O  O   . HOH Y  3 .   ? 25.830  -56.158 7.270   1.00 25.60 ? 1219 HOH A O   1 
HETATM 13533 O  O   . HOH Y  3 .   ? 35.451  -20.100 27.769  1.00 37.29 ? 1222 HOH A O   1 
HETATM 13534 O  O   . HOH Y  3 .   ? 25.402  -28.362 1.451   1.00 35.40 ? 1236 HOH A O   1 
HETATM 13535 O  O   . HOH Y  3 .   ? 39.480  -28.451 -2.486  1.00 27.49 ? 1241 HOH A O   1 
HETATM 13536 O  O   . HOH Y  3 .   ? 32.660  -41.159 -0.743  1.00 31.23 ? 1242 HOH A O   1 
HETATM 13537 O  O   . HOH Y  3 .   ? 21.214  -30.446 6.318   1.00 38.29 ? 1257 HOH A O   1 
HETATM 13538 O  O   . HOH Y  3 .   ? 21.418  -30.438 21.973  1.00 31.49 ? 1262 HOH A O   1 
HETATM 13539 O  O   . HOH Y  3 .   ? 27.595  -41.546 0.759   1.00 32.10 ? 1276 HOH A O   1 
HETATM 13540 O  O   . HOH Y  3 .   ? 24.572  -20.559 3.286   1.00 38.73 ? 1289 HOH A O   1 
HETATM 13541 O  O   . HOH Y  3 .   ? 21.553  -45.791 20.533  1.00 20.96 ? 1303 HOH A O   1 
HETATM 13542 O  O   . HOH Y  3 .   ? 19.750  -43.166 6.617   1.00 23.26 ? 1308 HOH A O   1 
HETATM 13543 O  O   . HOH Y  3 .   ? 18.003  -41.255 22.831  1.00 20.67 ? 1321 HOH A O   1 
HETATM 13544 O  O   . HOH Y  3 .   ? 38.117  -56.741 12.448  1.00 27.61 ? 1322 HOH A O   1 
HETATM 13545 O  O   . HOH Y  3 .   ? 23.376  -34.460 18.408  1.00 25.44 ? 1323 HOH A O   1 
HETATM 13546 O  O   . HOH Y  3 .   ? 37.664  -34.680 -9.082  1.00 40.37 ? 1326 HOH A O   1 
HETATM 13547 O  O   . HOH Y  3 .   ? 35.961  -20.131 7.844   1.00 34.06 ? 1328 HOH A O   1 
HETATM 13548 O  O   . HOH Y  3 .   ? 31.941  -44.949 1.626   1.00 24.91 ? 1348 HOH A O   1 
HETATM 13549 O  O   . HOH Y  3 .   ? 41.888  -28.666 -6.206  1.00 30.36 ? 1359 HOH A O   1 
HETATM 13550 O  O   . HOH Y  3 .   ? 43.711  -35.617 26.690  1.00 33.10 ? 1386 HOH A O   1 
HETATM 13551 O  O   . HOH Y  3 .   ? 37.798  -34.362 -11.650 1.00 38.89 ? 1396 HOH A O   1 
HETATM 13552 O  O   . HOH Y  3 .   ? 38.236  -41.826 24.367  1.00 30.71 ? 1398 HOH A O   1 
HETATM 13553 O  O   . HOH Y  3 .   ? 41.338  -38.409 -9.067  1.00 39.87 ? 1401 HOH A O   1 
HETATM 13554 O  O   . HOH Y  3 .   ? 40.150  -48.629 23.051  1.00 32.32 ? 1413 HOH A O   1 
HETATM 13555 O  O   . HOH Y  3 .   ? 30.815  -55.073 4.979   1.00 30.08 ? 1420 HOH A O   1 
HETATM 13556 O  O   . HOH Y  3 .   ? 37.402  -47.142 4.385   1.00 23.97 ? 1429 HOH A O   1 
HETATM 13557 O  O   . HOH Y  3 .   ? 25.075  -24.183 16.679  1.00 32.98 ? 1442 HOH A O   1 
HETATM 13558 O  O   . HOH Y  3 .   ? 31.883  -22.337 18.383  1.00 34.52 ? 1443 HOH A O   1 
HETATM 13559 O  O   . HOH Y  3 .   ? 38.823  -37.962 29.799  1.00 43.14 ? 1474 HOH A O   1 
HETATM 13560 O  O   . HOH Y  3 .   ? 40.277  -56.138 11.257  1.00 38.69 ? 1485 HOH A O   1 
HETATM 13561 O  O   . HOH Y  3 .   ? 29.544  -50.703 24.134  1.00 31.01 ? 1490 HOH A O   1 
HETATM 13562 O  O   . HOH Y  3 .   ? 26.576  -32.606 32.616  1.00 30.83 ? 1540 HOH A O   1 
HETATM 13563 O  O   . HOH Y  3 .   ? 29.048  -30.423 29.667  1.00 33.18 ? 1542 HOH A O   1 
HETATM 13564 O  O   . HOH Y  3 .   ? 22.220  -39.196 26.596  1.00 34.48 ? 1550 HOH A O   1 
HETATM 13565 O  O   . HOH Y  3 .   ? 23.066  -49.622 3.750   1.00 28.28 ? 1561 HOH A O   1 
HETATM 13566 O  O   . HOH Y  3 .   ? 29.562  -20.351 24.908  1.00 43.68 ? 1566 HOH A O   1 
HETATM 13567 O  O   . HOH Y  3 .   ? 39.261  -40.343 26.389  1.00 36.91 ? 1577 HOH A O   1 
HETATM 13568 O  O   . HOH Y  3 .   ? 30.166  -30.540 -4.782  1.00 39.67 ? 1582 HOH A O   1 
HETATM 13569 O  O   . HOH Y  3 .   ? 25.512  -49.838 2.198   1.00 34.14 ? 1604 HOH A O   1 
HETATM 13570 O  O   . HOH Y  3 .   ? 35.622  -50.668 22.541  1.00 37.48 ? 1616 HOH A O   1 
HETATM 13571 O  O   . HOH Y  3 .   ? 39.778  -49.922 3.373   1.00 36.22 ? 1657 HOH A O   1 
HETATM 13572 O  O   . HOH Y  3 .   ? 53.737  -44.199 20.705  1.00 40.64 ? 1660 HOH A O   1 
HETATM 13573 O  O   . HOH Y  3 .   ? 36.786  -38.024 33.801  1.00 44.88 ? 1663 HOH A O   1 
HETATM 13574 O  O   . HOH Y  3 .   ? 19.891  -26.637 5.234   1.00 37.80 ? 1674 HOH A O   1 
HETATM 13575 O  O   . HOH Y  3 .   ? 36.790  -22.296 3.556   1.00 31.90 ? 1677 HOH A O   1 
HETATM 13576 O  O   . HOH Y  3 .   ? 40.905  -53.698 11.004  1.00 33.05 ? 1679 HOH A O   1 
HETATM 13577 O  O   . HOH Y  3 .   ? 37.982  -27.935 -4.602  1.00 32.42 ? 1705 HOH A O   1 
HETATM 13578 O  O   . HOH Y  3 .   ? 44.170  -46.277 20.440  1.00 30.68 ? 1714 HOH A O   1 
HETATM 13579 O  O   . HOH Y  3 .   ? 24.282  -31.763 33.080  1.00 34.66 ? 1718 HOH A O   1 
HETATM 13580 O  O   . HOH Y  3 .   ? 46.002  -48.038 10.422  1.00 40.09 ? 1729 HOH A O   1 
HETATM 13581 O  O   . HOH Y  3 .   ? 19.151  -46.759 13.871  1.00 28.52 ? 1734 HOH A O   1 
HETATM 13582 O  O   . HOH Y  3 .   ? 30.550  -41.167 -2.400  1.00 37.26 ? 1751 HOH A O   1 
HETATM 13583 O  O   . HOH Z  3 .   ? 62.651  -34.037 -5.486  1.00 16.05 ? 154  HOH B O   1 
HETATM 13584 O  O   . HOH Z  3 .   ? 57.621  -39.260 -7.867  1.00 16.81 ? 156  HOH B O   1 
HETATM 13585 O  O   . HOH Z  3 .   ? 49.316  -39.627 9.227   1.00 16.29 ? 157  HOH B O   1 
HETATM 13586 O  O   . HOH Z  3 .   ? 67.356  -40.632 4.566   1.00 19.41 ? 158  HOH B O   1 
HETATM 13587 O  O   . HOH Z  3 .   ? 55.352  -25.514 -6.929  1.00 22.76 ? 159  HOH B O   1 
HETATM 13588 O  O   . HOH Z  3 .   ? 45.432  -28.429 -3.175  1.00 25.74 ? 160  HOH B O   1 
HETATM 13589 O  O   . HOH Z  3 .   ? 66.012  -33.997 -17.637 1.00 20.34 ? 161  HOH B O   1 
HETATM 13590 O  O   . HOH Z  3 .   ? 69.599  -43.821 6.815   1.00 23.55 ? 162  HOH B O   1 
HETATM 13591 O  O   . HOH Z  3 .   ? 66.745  -35.315 0.115   1.00 19.42 ? 163  HOH B O   1 
HETATM 13592 O  O   . HOH Z  3 .   ? 66.434  -41.361 -14.402 1.00 21.82 ? 164  HOH B O   1 
HETATM 13593 O  O   . HOH Z  3 .   ? 66.358  -16.860 -5.143  1.00 27.31 ? 165  HOH B O   1 
HETATM 13594 O  O   . HOH Z  3 .   ? 66.195  -38.857 11.892  1.00 26.96 ? 166  HOH B O   1 
HETATM 13595 O  O   . HOH Z  3 .   ? 66.800  -47.081 -4.142  1.00 26.01 ? 167  HOH B O   1 
HETATM 13596 O  O   . HOH Z  3 .   ? 65.033  -43.766 -10.980 1.00 23.66 ? 168  HOH B O   1 
HETATM 13597 O  O   . HOH Z  3 .   ? 63.865  -31.334 16.587  1.00 34.38 ? 169  HOH B O   1 
HETATM 13598 O  O   . HOH Z  3 .   ? 42.245  -39.189 3.257   1.00 15.82 ? 175  HOH B O   1 
HETATM 13599 O  O   . HOH Z  3 .   ? 56.019  -31.027 -13.453 1.00 25.72 ? 180  HOH B O   1 
HETATM 13600 O  O   . HOH Z  3 .   ? 55.944  -34.493 15.279  1.00 23.46 ? 184  HOH B O   1 
HETATM 13601 O  O   . HOH Z  3 .   ? 65.406  -25.112 0.984   1.00 25.82 ? 190  HOH B O   1 
HETATM 13602 O  O   . HOH Z  3 .   ? 54.143  -21.128 9.687   1.00 26.56 ? 200  HOH B O   1 
HETATM 13603 O  O   . HOH Z  3 .   ? 49.710  -29.222 -7.151  1.00 23.43 ? 204  HOH B O   1 
HETATM 13604 O  O   . HOH Z  3 .   ? 54.745  -50.589 1.361   1.00 25.86 ? 212  HOH B O   1 
HETATM 13605 O  O   . HOH Z  3 .   ? 67.030  -49.340 -3.889  1.00 24.12 ? 225  HOH B O   1 
HETATM 13606 O  O   . HOH Z  3 .   ? 46.967  -26.919 4.512   1.00 23.57 ? 230  HOH B O   1 
HETATM 13607 O  O   . HOH Z  3 .   ? 52.905  -50.753 5.047   1.00 22.85 ? 232  HOH B O   1 
HETATM 13608 O  O   . HOH Z  3 .   ? 61.603  -22.121 11.402  1.00 27.11 ? 237  HOH B O   1 
HETATM 13609 O  O   . HOH Z  3 .   ? 48.594  -43.364 7.761   1.00 25.10 ? 245  HOH B O   1 
HETATM 13610 O  O   . HOH Z  3 .   ? 47.953  -44.333 5.023   1.00 26.95 ? 246  HOH B O   1 
HETATM 13611 O  O   . HOH Z  3 .   ? 69.978  -47.495 8.100   1.00 27.72 ? 262  HOH B O   1 
HETATM 13612 O  O   . HOH Z  3 .   ? 48.726  -25.423 1.263   1.00 26.52 ? 269  HOH B O   1 
HETATM 13613 O  O   . HOH Z  3 .   ? 68.292  -33.215 0.792   1.00 20.25 ? 270  HOH B O   1 
HETATM 13614 O  O   . HOH Z  3 .   ? 69.451  -33.383 5.029   1.00 25.69 ? 293  HOH B O   1 
HETATM 13615 O  O   . HOH Z  3 .   ? 67.649  -54.171 0.029   1.00 25.37 ? 304  HOH B O   1 
HETATM 13616 O  O   . HOH Z  3 .   ? 51.479  -56.424 -0.974  1.00 29.99 ? 319  HOH B O   1 
HETATM 13617 O  O   . HOH Z  3 .   ? 70.037  -37.565 -10.137 1.00 22.27 ? 331  HOH B O   1 
HETATM 13618 O  O   . HOH Z  3 .   ? 61.298  -20.301 4.731   1.00 19.08 ? 333  HOH B O   1 
HETATM 13619 O  O   . HOH Z  3 .   ? 66.668  -30.241 -14.957 1.00 32.23 ? 335  HOH B O   1 
HETATM 13620 O  O   . HOH Z  3 .   ? 56.187  -47.769 11.677  1.00 31.89 ? 360  HOH B O   1 
HETATM 13621 O  O   . HOH Z  3 .   ? 47.593  -25.219 7.012   1.00 25.42 ? 376  HOH B O   1 
HETATM 13622 O  O   . HOH Z  3 .   ? 66.497  -45.822 -10.490 1.00 32.25 ? 381  HOH B O   1 
HETATM 13623 O  O   . HOH Z  3 .   ? 68.113  -30.820 4.325   1.00 20.06 ? 394  HOH B O   1 
HETATM 13624 O  O   . HOH Z  3 .   ? 57.844  -24.358 -6.600  1.00 26.61 ? 397  HOH B O   1 
HETATM 13625 O  O   . HOH Z  3 .   ? 65.465  -23.219 -1.061  1.00 36.11 ? 404  HOH B O   1 
HETATM 13626 O  O   . HOH Z  3 .   ? 63.748  -20.958 12.184  1.00 33.17 ? 409  HOH B O   1 
HETATM 13627 O  O   . HOH Z  3 .   ? 46.689  -25.198 2.985   1.00 22.26 ? 411  HOH B O   1 
HETATM 13628 O  O   . HOH Z  3 .   ? 67.482  -30.764 1.542   1.00 26.85 ? 416  HOH B O   1 
HETATM 13629 O  O   . HOH Z  3 .   ? 44.552  -45.468 5.787   1.00 40.93 ? 417  HOH B O   1 
HETATM 13630 O  O   . HOH Z  3 .   ? 52.846  -20.756 2.878   1.00 24.47 ? 424  HOH B O   1 
HETATM 13631 O  O   . HOH Z  3 .   ? 69.827  -25.985 -9.873  1.00 31.90 ? 444  HOH B O   1 
HETATM 13632 O  O   . HOH Z  3 .   ? 66.863  -24.741 -10.431 1.00 31.98 ? 465  HOH B O   1 
HETATM 13633 O  O   . HOH Z  3 .   ? 66.447  -46.595 -7.773  1.00 23.40 ? 472  HOH B O   1 
HETATM 13634 O  O   . HOH Z  3 .   ? 68.306  -25.060 5.266   1.00 38.68 ? 473  HOH B O   1 
HETATM 13635 O  O   . HOH Z  3 .   ? 71.323  -32.555 -15.561 1.00 25.31 ? 474  HOH B O   1 
HETATM 13636 O  O   . HOH Z  3 .   ? 73.121  -30.847 -14.600 1.00 24.07 ? 475  HOH B O   1 
HETATM 13637 O  O   . HOH Z  3 .   ? 56.731  -32.110 15.236  1.00 25.35 ? 501  HOH B O   1 
HETATM 13638 O  O   . HOH Z  3 .   ? 51.267  -27.243 16.726  1.00 34.77 ? 508  HOH B O   1 
HETATM 13639 O  O   . HOH Z  3 .   ? 54.216  -28.563 -14.244 1.00 37.07 ? 511  HOH B O   1 
HETATM 13640 O  O   . HOH Z  3 .   ? 53.522  -27.868 20.725  1.00 35.42 ? 528  HOH B O   1 
HETATM 13641 O  O   . HOH Z  3 .   ? 59.603  -22.474 -5.913  1.00 30.95 ? 548  HOH B O   1 
HETATM 13642 O  O   . HOH Z  3 .   ? 63.454  -52.633 7.931   1.00 30.47 ? 558  HOH B O   1 
HETATM 13643 O  O   . HOH Z  3 .   ? 56.726  -41.554 -9.415  1.00 23.98 ? 560  HOH B O   1 
HETATM 13644 O  O   . HOH Z  3 .   ? 67.089  -25.337 3.173   1.00 29.41 ? 572  HOH B O   1 
HETATM 13645 O  O   . HOH Z  3 .   ? 64.365  -54.201 3.406   1.00 27.97 ? 576  HOH B O   1 
HETATM 13646 O  O   . HOH Z  3 .   ? 55.762  -51.613 -0.530  1.00 26.96 ? 582  HOH B O   1 
HETATM 13647 O  O   . HOH Z  3 .   ? 69.102  -38.717 -8.001  1.00 23.16 ? 604  HOH B O   1 
HETATM 13648 O  O   . HOH Z  3 .   ? 59.332  -40.001 15.583  1.00 27.60 ? 625  HOH B O   1 
HETATM 13649 O  O   . HOH Z  3 .   ? 60.464  -52.732 0.089   1.00 25.95 ? 630  HOH B O   1 
HETATM 13650 O  O   . HOH Z  3 .   ? 68.860  -23.740 -8.802  1.00 27.96 ? 633  HOH B O   1 
HETATM 13651 O  O   . HOH Z  3 .   ? 47.082  -40.954 7.666   1.00 24.63 ? 634  HOH B O   1 
HETATM 13652 O  O   . HOH Z  3 .   ? 57.121  -30.820 -17.527 1.00 33.04 ? 636  HOH B O   1 
HETATM 13653 O  O   . HOH Z  3 .   ? 54.198  -17.798 -1.270  1.00 31.46 ? 643  HOH B O   1 
HETATM 13654 O  O   . HOH Z  3 .   ? 69.186  -31.117 -16.373 1.00 27.92 ? 645  HOH B O   1 
HETATM 13655 O  O   . HOH Z  3 .   ? 55.699  -38.621 16.570  1.00 27.52 ? 652  HOH B O   1 
HETATM 13656 O  O   . HOH Z  3 .   ? 48.411  -27.046 -6.503  1.00 27.78 ? 670  HOH B O   1 
HETATM 13657 O  O   . HOH Z  3 .   ? 68.240  -47.608 11.884  1.00 35.77 ? 672  HOH B O   1 
HETATM 13658 O  O   . HOH Z  3 .   ? 48.599  -23.519 10.431  1.00 37.36 ? 675  HOH B O   1 
HETATM 13659 O  O   . HOH Z  3 .   ? 72.602  -47.236 1.733   1.00 34.66 ? 677  HOH B O   1 
HETATM 13660 O  O   . HOH Z  3 .   ? 59.518  -44.386 13.977  1.00 25.16 ? 680  HOH B O   1 
HETATM 13661 O  O   . HOH Z  3 .   ? 54.075  -34.778 -10.201 1.00 21.18 ? 696  HOH B O   1 
HETATM 13662 O  O   . HOH Z  3 .   ? 58.032  -42.486 -12.283 1.00 21.60 ? 697  HOH B O   1 
HETATM 13663 O  O   . HOH Z  3 .   ? 53.355  -37.039 -9.292  1.00 21.31 ? 714  HOH B O   1 
HETATM 13664 O  O   . HOH Z  3 .   ? 53.091  -42.664 -8.850  1.00 31.31 ? 715  HOH B O   1 
HETATM 13665 O  O   . HOH Z  3 .   ? 53.051  -58.919 -1.263  1.00 27.86 ? 747  HOH B O   1 
HETATM 13666 O  O   . HOH Z  3 .   ? 53.058  -31.839 -10.176 1.00 25.29 ? 761  HOH B O   1 
HETATM 13667 O  O   . HOH Z  3 .   ? 56.426  -41.145 17.194  1.00 30.45 ? 764  HOH B O   1 
HETATM 13668 O  O   . HOH Z  3 .   ? 54.183  -39.779 -8.288  1.00 21.95 ? 767  HOH B O   1 
HETATM 13669 O  O   . HOH Z  3 .   ? 46.453  -22.633 3.895   1.00 26.74 ? 784  HOH B O   1 
HETATM 13670 O  O   . HOH Z  3 .   ? 57.897  -52.639 -0.977  1.00 31.38 ? 792  HOH B O   1 
HETATM 13671 O  O   . HOH Z  3 .   ? 55.662  -20.980 13.576  1.00 32.57 ? 804  HOH B O   1 
HETATM 13672 O  O   . HOH Z  3 .   ? 39.312  -42.041 -5.065  1.00 31.99 ? 805  HOH B O   1 
HETATM 13673 O  O   . HOH Z  3 .   ? 67.898  -35.554 -2.729  1.00 28.24 ? 806  HOH B O   1 
HETATM 13674 O  O   . HOH Z  3 .   ? 61.298  -37.060 16.929  1.00 31.96 ? 808  HOH B O   1 
HETATM 13675 O  O   . HOH Z  3 .   ? 68.218  -32.625 -18.585 1.00 26.37 ? 825  HOH B O   1 
HETATM 13676 O  O   . HOH Z  3 .   ? 46.657  -47.309 5.226   1.00 38.72 ? 828  HOH B O   1 
HETATM 13677 O  O   . HOH Z  3 .   ? 59.816  -41.718 13.946  1.00 20.26 ? 838  HOH B O   1 
HETATM 13678 O  O   . HOH Z  3 .   ? 61.469  -50.236 -1.235  1.00 22.53 ? 839  HOH B O   1 
HETATM 13679 O  O   . HOH Z  3 .   ? 70.474  -32.387 7.583   1.00 32.28 ? 860  HOH B O   1 
HETATM 13680 O  O   . HOH Z  3 .   ? 56.272  -43.882 17.600  1.00 34.32 ? 893  HOH B O   1 
HETATM 13681 O  O   . HOH Z  3 .   ? 57.267  -54.966 -1.411  1.00 38.51 ? 899  HOH B O   1 
HETATM 13682 O  O   . HOH Z  3 .   ? 43.811  -47.494 -6.389  1.00 35.24 ? 901  HOH B O   1 
HETATM 13683 O  O   . HOH Z  3 .   ? 68.492  -30.975 9.171   1.00 31.23 ? 922  HOH B O   1 
HETATM 13684 O  O   . HOH Z  3 .   ? 61.892  -50.407 -3.476  1.00 24.30 ? 928  HOH B O   1 
HETATM 13685 O  O   . HOH Z  3 .   ? 58.487  -22.031 4.940   1.00 21.47 ? 942  HOH B O   1 
HETATM 13686 O  O   . HOH Z  3 .   ? 48.935  -38.343 -9.870  1.00 23.42 ? 950  HOH B O   1 
HETATM 13687 O  O   . HOH Z  3 .   ? 46.777  -40.099 2.035   1.00 18.14 ? 951  HOH B O   1 
HETATM 13688 O  O   . HOH Z  3 .   ? 54.341  -56.900 2.648   1.00 26.39 ? 952  HOH B O   1 
HETATM 13689 O  O   . HOH Z  3 .   ? 53.340  -33.030 -12.522 1.00 29.65 ? 963  HOH B O   1 
HETATM 13690 O  O   . HOH Z  3 .   ? 62.244  -25.286 12.343  1.00 26.24 ? 988  HOH B O   1 
HETATM 13691 O  O   . HOH Z  3 .   ? 64.547  -28.948 -12.294 1.00 26.12 ? 989  HOH B O   1 
HETATM 13692 O  O   . HOH Z  3 .   ? 46.636  -40.944 -0.074  1.00 21.66 ? 993  HOH B O   1 
HETATM 13693 O  O   . HOH Z  3 .   ? 59.857  -52.443 -4.046  1.00 29.71 ? 1008 HOH B O   1 
HETATM 13694 O  O   . HOH Z  3 .   ? 52.196  -30.582 -12.001 1.00 33.00 ? 1012 HOH B O   1 
HETATM 13695 O  O   . HOH Z  3 .   ? 51.565  -56.937 1.485   1.00 31.40 ? 1025 HOH B O   1 
HETATM 13696 O  O   . HOH Z  3 .   ? 61.447  -55.128 -0.698  1.00 33.43 ? 1028 HOH B O   1 
HETATM 13697 O  O   . HOH Z  3 .   ? 70.064  -46.376 -4.705  1.00 27.02 ? 1030 HOH B O   1 
HETATM 13698 O  O   . HOH Z  3 .   ? 58.977  -39.755 -20.106 1.00 29.98 ? 1050 HOH B O   1 
HETATM 13699 O  O   . HOH Z  3 .   ? 45.789  -32.049 -9.507  1.00 31.65 ? 1066 HOH B O   1 
HETATM 13700 O  O   . HOH Z  3 .   ? 68.515  -20.835 -9.763  1.00 34.19 ? 1069 HOH B O   1 
HETATM 13701 O  O   . HOH Z  3 .   ? 39.305  -39.508 -4.438  1.00 34.78 ? 1076 HOH B O   1 
HETATM 13702 O  O   . HOH Z  3 .   ? 71.081  -37.483 -5.956  1.00 27.86 ? 1084 HOH B O   1 
HETATM 13703 O  O   . HOH Z  3 .   ? 59.431  -43.819 -13.990 1.00 26.78 ? 1086 HOH B O   1 
HETATM 13704 O  O   . HOH Z  3 .   ? 61.349  -55.076 3.544   1.00 27.79 ? 1106 HOH B O   1 
HETATM 13705 O  O   . HOH Z  3 .   ? 51.442  -38.353 -10.924 1.00 22.28 ? 1107 HOH B O   1 
HETATM 13706 O  O   . HOH Z  3 .   ? 49.637  -27.117 -10.932 1.00 32.03 ? 1137 HOH B O   1 
HETATM 13707 O  O   . HOH Z  3 .   ? 52.822  -20.158 12.270  1.00 37.46 ? 1142 HOH B O   1 
HETATM 13708 O  O   . HOH Z  3 .   ? 47.504  -36.373 -11.261 1.00 28.88 ? 1154 HOH B O   1 
HETATM 13709 O  O   . HOH Z  3 .   ? 45.259  -34.813 -10.277 1.00 36.66 ? 1166 HOH B O   1 
HETATM 13710 O  O   . HOH Z  3 .   ? 47.937  -26.209 -8.720  1.00 30.33 ? 1167 HOH B O   1 
HETATM 13711 O  O   . HOH Z  3 .   ? 51.239  -48.449 12.875  1.00 42.00 ? 1178 HOH B O   1 
HETATM 13712 O  O   . HOH Z  3 .   ? 59.521  -15.940 10.434  1.00 37.11 ? 1179 HOH B O   1 
HETATM 13713 O  O   . HOH Z  3 .   ? 37.502  -37.147 -2.312  1.00 28.08 ? 1183 HOH B O   1 
HETATM 13714 O  O   . HOH Z  3 .   ? 46.512  -41.931 4.576   1.00 30.27 ? 1187 HOH B O   1 
HETATM 13715 O  O   . HOH Z  3 .   ? 70.098  -32.261 -1.349  1.00 30.78 ? 1189 HOH B O   1 
HETATM 13716 O  O   . HOH Z  3 .   ? 54.573  -48.636 17.941  1.00 47.27 ? 1194 HOH B O   1 
HETATM 13717 O  O   . HOH Z  3 .   ? 47.358  -25.938 9.513   1.00 29.42 ? 1220 HOH B O   1 
HETATM 13718 O  O   . HOH Z  3 .   ? 55.667  -46.291 17.445  1.00 45.98 ? 1227 HOH B O   1 
HETATM 13719 O  O   . HOH Z  3 .   ? 47.455  -22.193 7.005   1.00 30.29 ? 1235 HOH B O   1 
HETATM 13720 O  O   . HOH Z  3 .   ? 63.960  -55.411 1.213   1.00 29.41 ? 1247 HOH B O   1 
HETATM 13721 O  O   . HOH Z  3 .   ? 57.907  -33.990 18.410  1.00 40.28 ? 1264 HOH B O   1 
HETATM 13722 O  O   . HOH Z  3 .   ? 57.170  -15.695 13.277  1.00 39.93 ? 1278 HOH B O   1 
HETATM 13723 O  O   . HOH Z  3 .   ? 57.339  -56.776 0.430   1.00 33.91 ? 1297 HOH B O   1 
HETATM 13724 O  O   . HOH Z  3 .   ? 57.515  -46.847 14.594  1.00 44.99 ? 1298 HOH B O   1 
HETATM 13725 O  O   . HOH Z  3 .   ? 56.638  -25.631 -15.486 1.00 29.01 ? 1307 HOH B O   1 
HETATM 13726 O  O   . HOH Z  3 .   ? 73.931  -49.499 5.320   1.00 31.07 ? 1312 HOH B O   1 
HETATM 13727 O  O   . HOH Z  3 .   ? 68.181  -56.033 10.409  1.00 34.66 ? 1318 HOH B O   1 
HETATM 13728 O  O   . HOH Z  3 .   ? 53.764  -46.827 10.925  1.00 31.89 ? 1319 HOH B O   1 
HETATM 13729 O  O   . HOH Z  3 .   ? 58.718  -24.023 -15.124 1.00 32.45 ? 1340 HOH B O   1 
HETATM 13730 O  O   . HOH Z  3 .   ? 62.002  -22.903 -5.462  1.00 28.70 ? 1352 HOH B O   1 
HETATM 13731 O  O   . HOH Z  3 .   ? 50.890  -21.860 -11.129 1.00 33.18 ? 1353 HOH B O   1 
HETATM 13732 O  O   . HOH Z  3 .   ? 53.171  -50.237 13.191  1.00 41.85 ? 1377 HOH B O   1 
HETATM 13733 O  O   . HOH Z  3 .   ? 54.736  -47.642 14.419  1.00 44.76 ? 1380 HOH B O   1 
HETATM 13734 O  O   . HOH Z  3 .   ? 51.696  -49.371 -1.535  1.00 30.11 ? 1389 HOH B O   1 
HETATM 13735 O  O   . HOH Z  3 .   ? 53.702  -52.409 -2.639  1.00 32.93 ? 1400 HOH B O   1 
HETATM 13736 O  O   . HOH Z  3 .   ? 58.457  -45.621 17.192  1.00 49.52 ? 1407 HOH B O   1 
HETATM 13737 O  O   . HOH Z  3 .   ? 48.547  -47.266 -0.514  1.00 32.18 ? 1415 HOH B O   1 
HETATM 13738 O  O   . HOH Z  3 .   ? 58.895  -54.349 14.203  1.00 38.27 ? 1417 HOH B O   1 
HETATM 13739 O  O   . HOH Z  3 .   ? 47.889  -22.944 -8.117  1.00 32.17 ? 1428 HOH B O   1 
HETATM 13740 O  O   . HOH Z  3 .   ? 57.752  -36.509 18.730  1.00 37.44 ? 1436 HOH B O   1 
HETATM 13741 O  O   . HOH Z  3 .   ? 47.854  -23.788 -2.251  1.00 33.72 ? 1444 HOH B O   1 
HETATM 13742 O  O   . HOH Z  3 .   ? 56.538  -28.565 -17.005 1.00 34.94 ? 1445 HOH B O   1 
HETATM 13743 O  O   . HOH Z  3 .   ? 67.254  -26.644 -12.961 1.00 42.94 ? 1457 HOH B O   1 
HETATM 13744 O  O   . HOH Z  3 .   ? 72.151  -46.612 10.025  1.00 36.78 ? 1463 HOH B O   1 
HETATM 13745 O  O   . HOH Z  3 .   ? 60.313  -52.369 13.985  1.00 41.91 ? 1470 HOH B O   1 
HETATM 13746 O  O   . HOH Z  3 .   ? 42.986  -34.886 -12.384 1.00 36.16 ? 1500 HOH B O   1 
HETATM 13747 O  O   . HOH Z  3 .   ? 48.579  -25.741 12.126  1.00 32.36 ? 1509 HOH B O   1 
HETATM 13748 O  O   . HOH Z  3 .   ? 70.450  -54.497 11.759  1.00 33.17 ? 1516 HOH B O   1 
HETATM 13749 O  O   . HOH Z  3 .   ? 70.120  -29.500 -10.801 1.00 35.64 ? 1543 HOH B O   1 
HETATM 13750 O  O   . HOH Z  3 .   ? 46.119  -47.848 2.302   1.00 31.38 ? 1546 HOH B O   1 
HETATM 13751 O  O   . HOH Z  3 .   ? 68.292  -58.773 10.970  1.00 29.79 ? 1549 HOH B O   1 
HETATM 13752 O  O   . HOH Z  3 .   ? 51.156  -28.140 -12.895 1.00 33.37 ? 1559 HOH B O   1 
HETATM 13753 O  O   . HOH Z  3 .   ? 66.217  -54.434 10.179  1.00 33.95 ? 1562 HOH B O   1 
HETATM 13754 O  O   . HOH Z  3 .   ? 61.248  -19.916 0.737   1.00 28.00 ? 1570 HOH B O   1 
HETATM 13755 O  O   . HOH Z  3 .   ? 74.603  -45.755 1.565   1.00 38.92 ? 1585 HOH B O   1 
HETATM 13756 O  O   . HOH Z  3 .   ? 47.507  -25.587 -4.436  1.00 30.18 ? 1598 HOH B O   1 
HETATM 13757 O  O   . HOH Z  3 .   ? 70.115  -40.068 -11.415 1.00 31.58 ? 1614 HOH B O   1 
HETATM 13758 O  O   . HOH Z  3 .   ? 64.351  -56.650 9.397   1.00 37.97 ? 1617 HOH B O   1 
HETATM 13759 O  O   . HOH Z  3 .   ? 59.561  -56.514 13.339  1.00 49.14 ? 1624 HOH B O   1 
HETATM 13760 O  O   . HOH Z  3 .   ? 63.125  -45.159 -15.248 1.00 31.87 ? 1634 HOH B O   1 
HETATM 13761 O  O   . HOH Z  3 .   ? 60.539  -46.018 -13.280 1.00 34.25 ? 1646 HOH B O   1 
HETATM 13762 O  O   . HOH Z  3 .   ? 44.631  -26.203 -1.940  1.00 32.30 ? 1650 HOH B O   1 
HETATM 13763 O  O   . HOH Z  3 .   ? 68.272  -22.665 9.631   1.00 37.69 ? 1661 HOH B O   1 
HETATM 13764 O  O   . HOH Z  3 .   ? 65.355  -23.941 -3.484  1.00 28.23 ? 1699 HOH B O   1 
HETATM 13765 O  O   . HOH Z  3 .   ? 57.099  -33.091 -17.198 1.00 33.02 ? 1708 HOH B O   1 
HETATM 13766 O  O   . HOH Z  3 .   ? 47.987  -46.718 1.874   1.00 33.08 ? 1724 HOH B O   1 
HETATM 13767 O  O   . HOH Z  3 .   ? 54.539  -35.149 17.712  1.00 36.33 ? 1762 HOH B O   1 
HETATM 13768 O  O   . HOH Z  3 .   ? 62.208  -54.876 7.532   1.00 36.50 ? 1765 HOH B O   1 
HETATM 13769 O  O   . HOH Z  3 .   ? 50.353  -23.092 13.822  1.00 41.90 ? 1769 HOH B O   1 
HETATM 13770 O  O   . HOH Z  3 .   ? 54.099  -52.536 12.464  1.00 48.55 ? 1777 HOH B O   1 
HETATM 13771 O  O   . HOH Z  3 .   ? 54.346  -56.818 5.513   1.00 29.58 ? 1802 HOH B O   1 
HETATM 13772 O  O   . HOH AA 3 .   ? 17.081  -31.920 11.500  1.00 22.28 ? 154  HOH C O   1 
HETATM 13773 O  O   . HOH AA 3 .   ? -10.196 -40.545 11.145  1.00 15.62 ? 156  HOH C O   1 
HETATM 13774 O  O   . HOH AA 3 .   ? -8.315  -39.461 2.179   1.00 18.21 ? 157  HOH C O   1 
HETATM 13775 O  O   . HOH AA 3 .   ? 8.570   -39.893 10.464  1.00 21.59 ? 158  HOH C O   1 
HETATM 13776 O  O   . HOH AA 3 .   ? 9.063   -34.859 16.434  1.00 19.05 ? 159  HOH C O   1 
HETATM 13777 O  O   . HOH AA 3 .   ? 4.769   -51.552 16.634  1.00 17.12 ? 160  HOH C O   1 
HETATM 13778 O  O   . HOH AA 3 .   ? -1.008  -57.522 8.111   1.00 20.15 ? 161  HOH C O   1 
HETATM 13779 O  O   . HOH AA 3 .   ? 5.421   -46.870 5.648   1.00 22.39 ? 162  HOH C O   1 
HETATM 13780 O  O   . HOH AA 3 .   ? 12.671  -43.166 8.762   1.00 23.71 ? 163  HOH C O   1 
HETATM 13781 O  O   . HOH AA 3 .   ? -3.226  -41.559 4.728   1.00 21.85 ? 164  HOH C O   1 
HETATM 13782 O  O   . HOH AA 3 .   ? 2.809   -41.794 25.388  1.00 22.35 ? 165  HOH C O   1 
HETATM 13783 O  O   . HOH AA 3 .   ? -12.740 -36.089 20.087  1.00 23.97 ? 166  HOH C O   1 
HETATM 13784 O  O   . HOH AA 3 .   ? 20.860  -34.673 12.776  1.00 19.63 ? 167  HOH C O   1 
HETATM 13785 O  O   . HOH AA 3 .   ? 8.511   -23.996 16.492  1.00 36.03 ? 168  HOH C O   1 
HETATM 13786 O  O   . HOH AA 3 .   ? -6.805  -45.228 7.854   1.00 23.51 ? 169  HOH C O   1 
HETATM 13787 O  O   . HOH AA 3 .   ? 15.709  -29.369 14.473  1.00 24.18 ? 173  HOH C O   1 
HETATM 13788 O  O   . HOH AA 3 .   ? 4.581   -51.467 30.450  1.00 30.82 ? 179  HOH C O   1 
HETATM 13789 O  O   . HOH AA 3 .   ? 1.956   -45.035 27.365  1.00 25.06 ? 187  HOH C O   1 
HETATM 13790 O  O   . HOH AA 3 .   ? 12.259  -31.539 6.368   1.00 21.60 ? 198  HOH C O   1 
HETATM 13791 O  O   . HOH AA 3 .   ? 1.667   -52.655 11.326  1.00 20.97 ? 208  HOH C O   1 
HETATM 13792 O  O   . HOH AA 3 .   ? 6.811   -25.811 9.509   1.00 22.26 ? 210  HOH C O   1 
HETATM 13793 O  O   . HOH AA 3 .   ? 7.347   -51.360 15.218  1.00 19.58 ? 216  HOH C O   1 
HETATM 13794 O  O   . HOH AA 3 .   ? -0.703  -51.835 11.591  1.00 16.35 ? 218  HOH C O   1 
HETATM 13795 O  O   . HOH AA 3 .   ? -0.449  -36.969 -1.807  1.00 27.65 ? 220  HOH C O   1 
HETATM 13796 O  O   . HOH AA 3 .   ? 7.434   -51.858 9.392   1.00 28.37 ? 221  HOH C O   1 
HETATM 13797 O  O   . HOH AA 3 .   ? 18.725  -42.070 14.519  1.00 24.39 ? 252  HOH C O   1 
HETATM 13798 O  O   . HOH AA 3 .   ? -2.073  -53.839 22.482  1.00 24.54 ? 267  HOH C O   1 
HETATM 13799 O  O   . HOH AA 3 .   ? -4.852  -51.660 11.911  1.00 19.19 ? 274  HOH C O   1 
HETATM 13800 O  O   . HOH AA 3 .   ? -2.822  -21.790 12.912  1.00 31.38 ? 275  HOH C O   1 
HETATM 13801 O  O   . HOH AA 3 .   ? 9.508   -50.381 20.102  1.00 25.79 ? 290  HOH C O   1 
HETATM 13802 O  O   . HOH AA 3 .   ? 10.901  -48.430 19.569  1.00 22.45 ? 292  HOH C O   1 
HETATM 13803 O  O   . HOH AA 3 .   ? -6.815  -42.253 6.986   1.00 20.77 ? 302  HOH C O   1 
HETATM 13804 O  O   . HOH AA 3 .   ? 7.586   -25.022 11.645  1.00 21.74 ? 310  HOH C O   1 
HETATM 13805 O  O   . HOH AA 3 .   ? -1.005  -55.841 21.185  1.00 23.60 ? 312  HOH C O   1 
HETATM 13806 O  O   . HOH AA 3 .   ? 14.476  -39.814 20.752  1.00 20.81 ? 323  HOH C O   1 
HETATM 13807 O  O   . HOH AA 3 .   ? 14.589  -44.868 9.104   1.00 27.43 ? 334  HOH C O   1 
HETATM 13808 O  O   . HOH AA 3 .   ? 2.925   -53.832 13.457  1.00 21.11 ? 370  HOH C O   1 
HETATM 13809 O  O   . HOH AA 3 .   ? -3.749  -25.883 7.772   1.00 24.69 ? 372  HOH C O   1 
HETATM 13810 O  O   . HOH AA 3 .   ? 5.641   -36.105 22.803  1.00 24.87 ? 374  HOH C O   1 
HETATM 13811 O  O   . HOH AA 3 .   ? 6.606   -55.567 22.344  1.00 26.78 ? 390  HOH C O   1 
HETATM 13812 O  O   . HOH AA 3 .   ? 6.281   -27.126 2.498   1.00 37.56 ? 391  HOH C O   1 
HETATM 13813 O  O   . HOH AA 3 .   ? 3.126   -53.668 16.234  1.00 16.82 ? 413  HOH C O   1 
HETATM 13814 O  O   . HOH AA 3 .   ? -4.845  -54.096 9.588   1.00 24.44 ? 426  HOH C O   1 
HETATM 13815 O  O   . HOH AA 3 .   ? 19.867  -30.929 14.392  1.00 32.24 ? 434  HOH C O   1 
HETATM 13816 O  O   . HOH AA 3 .   ? 2.091   -29.006 -1.177  1.00 28.67 ? 455  HOH C O   1 
HETATM 13817 O  O   . HOH AA 3 .   ? 4.355   -30.314 22.673  1.00 28.97 ? 470  HOH C O   1 
HETATM 13818 O  O   . HOH AA 3 .   ? -4.760  -47.399 5.685   1.00 23.21 ? 482  HOH C O   1 
HETATM 13819 O  O   . HOH AA 3 .   ? -9.120  -41.590 8.002   1.00 23.18 ? 498  HOH C O   1 
HETATM 13820 O  O   . HOH AA 3 .   ? 16.700  -30.772 16.444  1.00 28.20 ? 522  HOH C O   1 
HETATM 13821 O  O   . HOH AA 3 .   ? -4.906  -40.706 6.189   1.00 21.65 ? 524  HOH C O   1 
HETATM 13822 O  O   . HOH AA 3 .   ? 2.153   -55.666 21.027  1.00 25.02 ? 530  HOH C O   1 
HETATM 13823 O  O   . HOH AA 3 .   ? -7.330  -51.633 11.652  1.00 22.31 ? 534  HOH C O   1 
HETATM 13824 O  O   . HOH AA 3 .   ? 0.312   -49.547 28.525  1.00 33.79 ? 539  HOH C O   1 
HETATM 13825 O  O   . HOH AA 3 .   ? -12.178 -33.851 21.335  1.00 28.25 ? 559  HOH C O   1 
HETATM 13826 O  O   . HOH AA 3 .   ? -7.405  -48.645 6.545   1.00 30.04 ? 561  HOH C O   1 
HETATM 13827 O  O   . HOH AA 3 .   ? 18.121  -47.493 11.997  1.00 31.79 ? 565  HOH C O   1 
HETATM 13828 O  O   . HOH AA 3 .   ? -2.715  -31.778 28.715  1.00 36.01 ? 567  HOH C O   1 
HETATM 13829 O  O   . HOH AA 3 .   ? 4.214   -50.274 7.943   1.00 23.26 ? 577  HOH C O   1 
HETATM 13830 O  O   . HOH AA 3 .   ? -8.948  -48.279 19.756  1.00 28.50 ? 578  HOH C O   1 
HETATM 13831 O  O   . HOH AA 3 .   ? -7.211  -48.279 21.378  1.00 26.82 ? 593  HOH C O   1 
HETATM 13832 O  O   . HOH AA 3 .   ? -9.219  -26.036 9.938   1.00 27.66 ? 602  HOH C O   1 
HETATM 13833 O  O   . HOH AA 3 .   ? 15.130  -44.512 15.226  1.00 27.48 ? 609  HOH C O   1 
HETATM 13834 O  O   . HOH AA 3 .   ? 3.010   -56.661 13.314  1.00 21.44 ? 610  HOH C O   1 
HETATM 13835 O  O   . HOH AA 3 .   ? -8.986  -48.407 14.650  1.00 27.14 ? 611  HOH C O   1 
HETATM 13836 O  O   . HOH AA 3 .   ? 4.344   -56.167 16.404  1.00 17.54 ? 614  HOH C O   1 
HETATM 13837 O  O   . HOH AA 3 .   ? 1.714   -22.284 14.778  1.00 29.93 ? 620  HOH C O   1 
HETATM 13838 O  O   . HOH AA 3 .   ? -7.899  -27.366 7.616   1.00 23.22 ? 657  HOH C O   1 
HETATM 13839 O  O   . HOH AA 3 .   ? 8.694   -35.331 6.555   1.00 16.12 ? 701  HOH C O   1 
HETATM 13840 O  O   . HOH AA 3 .   ? 8.046   -37.667 5.921   1.00 23.66 ? 709  HOH C O   1 
HETATM 13841 O  O   . HOH AA 3 .   ? 7.619   -40.447 7.488   1.00 22.63 ? 718  HOH C O   1 
HETATM 13842 O  O   . HOH AA 3 .   ? -8.118  -46.154 21.262  1.00 25.92 ? 719  HOH C O   1 
HETATM 13843 O  O   . HOH AA 3 .   ? 6.845   -25.195 21.053  1.00 26.37 ? 735  HOH C O   1 
HETATM 13844 O  O   . HOH AA 3 .   ? 6.190   -40.284 25.919  1.00 29.42 ? 737  HOH C O   1 
HETATM 13845 O  O   . HOH AA 3 .   ? -9.705  -44.075 10.192  1.00 28.30 ? 739  HOH C O   1 
HETATM 13846 O  O   . HOH AA 3 .   ? 2.693   -52.766 8.747   1.00 28.29 ? 745  HOH C O   1 
HETATM 13847 O  O   . HOH AA 3 .   ? 4.603   -26.573 22.162  1.00 30.42 ? 752  HOH C O   1 
HETATM 13848 O  O   . HOH AA 3 .   ? 4.135   -56.881 20.622  1.00 29.65 ? 763  HOH C O   1 
HETATM 13849 O  O   . HOH AA 3 .   ? -5.126  -18.009 12.628  1.00 45.66 ? 765  HOH C O   1 
HETATM 13850 O  O   . HOH AA 3 .   ? 0.713   -40.736 28.874  1.00 27.65 ? 776  HOH C O   1 
HETATM 13851 O  O   . HOH AA 3 .   ? -1.658  -48.153 5.134   1.00 33.37 ? 782  HOH C O   1 
HETATM 13852 O  O   . HOH AA 3 .   ? -5.282  -37.943 -4.365  1.00 29.06 ? 787  HOH C O   1 
HETATM 13853 O  O   . HOH AA 3 .   ? -9.829  -48.320 17.115  1.00 27.88 ? 796  HOH C O   1 
HETATM 13854 O  O   . HOH AA 3 .   ? 6.105   -22.970 21.026  1.00 37.61 ? 797  HOH C O   1 
HETATM 13855 O  O   . HOH AA 3 .   ? 16.482  -45.793 13.198  1.00 34.72 ? 819  HOH C O   1 
HETATM 13856 O  O   . HOH AA 3 .   ? 7.692   -42.986 6.000   1.00 28.69 ? 822  HOH C O   1 
HETATM 13857 O  O   . HOH AA 3 .   ? 7.511   -50.981 29.554  1.00 32.54 ? 830  HOH C O   1 
HETATM 13858 O  O   . HOH AA 3 .   ? -1.133  -28.608 1.810   1.00 31.14 ? 841  HOH C O   1 
HETATM 13859 O  O   . HOH AA 3 .   ? 2.455   -39.207 25.239  1.00 24.37 ? 850  HOH C O   1 
HETATM 13860 O  O   . HOH AA 3 .   ? 6.780   -23.466 14.323  1.00 33.34 ? 859  HOH C O   1 
HETATM 13861 O  O   . HOH AA 3 .   ? 4.124   -37.420 24.664  1.00 30.61 ? 864  HOH C O   1 
HETATM 13862 O  O   . HOH AA 3 .   ? 18.967  -30.142 11.665  1.00 27.72 ? 880  HOH C O   1 
HETATM 13863 O  O   . HOH AA 3 .   ? -15.026 -37.288 20.133  1.00 30.88 ? 885  HOH C O   1 
HETATM 13864 O  O   . HOH AA 3 .   ? 15.046  -28.108 22.748  1.00 40.65 ? 894  HOH C O   1 
HETATM 13865 O  O   . HOH AA 3 .   ? -7.876  -18.838 13.425  1.00 39.23 ? 902  HOH C O   1 
HETATM 13866 O  O   . HOH AA 3 .   ? -9.238  -23.148 9.840   1.00 31.71 ? 903  HOH C O   1 
HETATM 13867 O  O   . HOH AA 3 .   ? 8.510   -38.751 3.724   1.00 27.98 ? 913  HOH C O   1 
HETATM 13868 O  O   . HOH AA 3 .   ? -1.757  -23.156 18.308  1.00 30.83 ? 915  HOH C O   1 
HETATM 13869 O  O   . HOH AA 3 .   ? 7.278   -48.737 27.904  1.00 26.56 ? 917  HOH C O   1 
HETATM 13870 O  O   . HOH AA 3 .   ? 0.117   -50.390 8.226   1.00 19.82 ? 930  HOH C O   1 
HETATM 13871 O  O   . HOH AA 3 .   ? -4.339  -55.634 17.631  1.00 22.41 ? 944  HOH C O   1 
HETATM 13872 O  O   . HOH AA 3 .   ? 9.233   -42.048 8.855   1.00 25.63 ? 954  HOH C O   1 
HETATM 13873 O  O   . HOH AA 3 .   ? 10.851  -38.766 23.071  1.00 21.94 ? 961  HOH C O   1 
HETATM 13874 O  O   . HOH AA 3 .   ? 17.113  -43.161 16.721  1.00 27.34 ? 982  HOH C O   1 
HETATM 13875 O  O   . HOH AA 3 .   ? -6.491  -23.800 23.986  1.00 36.86 ? 992  HOH C O   1 
HETATM 13876 O  O   . HOH AA 3 .   ? -8.930  -35.559 29.025  1.00 34.15 ? 1001 HOH C O   1 
HETATM 13877 O  O   . HOH AA 3 .   ? 14.509  -32.014 21.523  1.00 34.48 ? 1004 HOH C O   1 
HETATM 13878 O  O   . HOH AA 3 .   ? -11.917 -26.832 10.602  1.00 28.03 ? 1016 HOH C O   1 
HETATM 13879 O  O   . HOH AA 3 .   ? -13.581 -39.863 20.577  1.00 31.44 ? 1017 HOH C O   1 
HETATM 13880 O  O   . HOH AA 3 .   ? 13.621  -39.085 23.306  1.00 29.65 ? 1019 HOH C O   1 
HETATM 13881 O  O   . HOH AA 3 .   ? 9.916   -53.414 21.313  1.00 27.57 ? 1043 HOH C O   1 
HETATM 13882 O  O   . HOH AA 3 .   ? 20.494  -30.021 9.070   1.00 30.74 ? 1044 HOH C O   1 
HETATM 13883 O  O   . HOH AA 3 .   ? -3.404  -56.107 19.791  1.00 26.94 ? 1051 HOH C O   1 
HETATM 13884 O  O   . HOH AA 3 .   ? 4.713   -29.929 3.642   1.00 31.85 ? 1060 HOH C O   1 
HETATM 13885 O  O   . HOH AA 3 .   ? -6.327  -51.848 24.842  1.00 30.39 ? 1077 HOH C O   1 
HETATM 13886 O  O   . HOH AA 3 .   ? -13.130 -24.121 29.756  1.00 35.40 ? 1090 HOH C O   1 
HETATM 13887 O  O   . HOH AA 3 .   ? -4.933  -54.225 23.950  1.00 28.50 ? 1091 HOH C O   1 
HETATM 13888 O  O   . HOH AA 3 .   ? 22.725  -33.452 14.313  1.00 26.67 ? 1101 HOH C O   1 
HETATM 13889 O  O   . HOH AA 3 .   ? -5.429  -49.480 5.159   1.00 29.39 ? 1114 HOH C O   1 
HETATM 13890 O  O   . HOH AA 3 .   ? -9.363  -42.714 23.448  1.00 31.16 ? 1124 HOH C O   1 
HETATM 13891 O  O   . HOH AA 3 .   ? 5.915   -46.934 29.310  1.00 34.21 ? 1128 HOH C O   1 
HETATM 13892 O  O   . HOH AA 3 .   ? -24.008 -37.690 20.655  1.00 39.24 ? 1134 HOH C O   1 
HETATM 13893 O  O   . HOH AA 3 .   ? -4.501  -40.512 27.670  1.00 25.35 ? 1135 HOH C O   1 
HETATM 13894 O  O   . HOH AA 3 .   ? 17.113  -40.094 20.276  1.00 30.44 ? 1139 HOH C O   1 
HETATM 13895 O  O   . HOH AA 3 .   ? 14.612  -47.244 8.498   1.00 35.27 ? 1144 HOH C O   1 
HETATM 13896 O  O   . HOH AA 3 .   ? 8.991   -41.207 4.497   1.00 30.85 ? 1170 HOH C O   1 
HETATM 13897 O  O   . HOH AA 3 .   ? -10.284 -32.898 28.052  1.00 40.95 ? 1172 HOH C O   1 
HETATM 13898 O  O   . HOH AA 3 .   ? 13.348  -52.264 11.115  1.00 39.25 ? 1177 HOH C O   1 
HETATM 13899 O  O   . HOH AA 3 .   ? -3.180  -26.717 2.413   1.00 35.82 ? 1195 HOH C O   1 
HETATM 13900 O  O   . HOH AA 3 .   ? 0.384   -25.523 26.939  1.00 47.07 ? 1196 HOH C O   1 
HETATM 13901 O  O   . HOH AA 3 .   ? -7.323  -51.365 7.657   1.00 25.92 ? 1204 HOH C O   1 
HETATM 13902 O  O   . HOH AA 3 .   ? 0.690   -20.608 23.191  1.00 37.91 ? 1208 HOH C O   1 
HETATM 13903 O  O   . HOH AA 3 .   ? 1.101   -46.884 2.985   1.00 32.73 ? 1214 HOH C O   1 
HETATM 13904 O  O   . HOH AA 3 .   ? 17.681  -27.974 12.662  1.00 32.26 ? 1218 HOH C O   1 
HETATM 13905 O  O   . HOH AA 3 .   ? 14.130  -40.873 24.948  1.00 32.35 ? 1229 HOH C O   1 
HETATM 13906 O  O   . HOH AA 3 .   ? -1.235  -38.814 -3.424  1.00 29.14 ? 1246 HOH C O   1 
HETATM 13907 O  O   . HOH AA 3 .   ? -3.534  -41.803 -4.876  1.00 28.19 ? 1268 HOH C O   1 
HETATM 13908 O  O   . HOH AA 3 .   ? -6.666  -49.470 23.823  1.00 31.02 ? 1280 HOH C O   1 
HETATM 13909 O  O   . HOH AA 3 .   ? -13.700 -26.429 12.457  1.00 33.55 ? 1282 HOH C O   1 
HETATM 13910 O  O   . HOH AA 3 .   ? 20.020  -40.490 5.678   1.00 21.78 ? 1309 HOH C O   1 
HETATM 13911 O  O   . HOH AA 3 .   ? -2.295  -56.399 25.880  1.00 30.77 ? 1310 HOH C O   1 
HETATM 13912 O  O   . HOH AA 3 .   ? -15.420 -28.927 17.086  1.00 28.44 ? 1325 HOH C O   1 
HETATM 13913 O  O   . HOH AA 3 .   ? 17.240  -42.565 18.977  1.00 26.83 ? 1331 HOH C O   1 
HETATM 13914 O  O   . HOH AA 3 .   ? 8.529   -39.672 24.677  1.00 26.11 ? 1383 HOH C O   1 
HETATM 13915 O  O   . HOH AA 3 .   ? -15.336 -36.056 23.511  1.00 30.34 ? 1392 HOH C O   1 
HETATM 13916 O  O   . HOH AA 3 .   ? 0.521   -18.622 10.634  1.00 43.09 ? 1394 HOH C O   1 
HETATM 13917 O  O   . HOH AA 3 .   ? -14.984 -38.528 23.661  1.00 29.40 ? 1405 HOH C O   1 
HETATM 13918 O  O   . HOH AA 3 .   ? 7.083   -22.533 25.702  1.00 44.59 ? 1440 HOH C O   1 
HETATM 13919 O  O   . HOH AA 3 .   ? 7.347   -29.977 3.115   1.00 38.35 ? 1455 HOH C O   1 
HETATM 13920 O  O   . HOH AA 3 .   ? -8.550  -41.686 26.042  1.00 33.77 ? 1456 HOH C O   1 
HETATM 13921 O  O   . HOH AA 3 .   ? -3.901  -58.299 20.540  1.00 29.98 ? 1458 HOH C O   1 
HETATM 13922 O  O   . HOH AA 3 .   ? -0.328  -28.846 -2.494  1.00 36.26 ? 1466 HOH C O   1 
HETATM 13923 O  O   . HOH AA 3 .   ? 12.410  -39.756 3.808   1.00 36.46 ? 1475 HOH C O   1 
HETATM 13924 O  O   . HOH AA 3 .   ? 6.328   -25.205 25.993  1.00 40.77 ? 1478 HOH C O   1 
HETATM 13925 O  O   . HOH AA 3 .   ? -6.922  -25.711 5.435   1.00 36.21 ? 1482 HOH C O   1 
HETATM 13926 O  O   . HOH AA 3 .   ? -0.820  -21.020 16.892  1.00 34.26 ? 1494 HOH C O   1 
HETATM 13927 O  O   . HOH AA 3 .   ? 1.861   -46.666 29.328  1.00 35.73 ? 1511 HOH C O   1 
HETATM 13928 O  O   . HOH AA 3 .   ? 21.818  -38.196 2.259   1.00 37.06 ? 1514 HOH C O   1 
HETATM 13929 O  O   . HOH AA 3 .   ? 14.016  -47.150 17.619  1.00 26.35 ? 1517 HOH C O   1 
HETATM 13930 O  O   . HOH AA 3 .   ? -6.062  -22.464 26.334  1.00 38.02 ? 1518 HOH C O   1 
HETATM 13931 O  O   . HOH AA 3 .   ? 8.784   -24.991 18.961  1.00 31.75 ? 1535 HOH C O   1 
HETATM 13932 O  O   . HOH AA 3 .   ? -17.296 -36.190 20.199  1.00 33.98 ? 1545 HOH C O   1 
HETATM 13933 O  O   . HOH AA 3 .   ? -7.730  -23.962 7.875   1.00 37.22 ? 1560 HOH C O   1 
HETATM 13934 O  O   . HOH AA 3 .   ? 22.309  -39.719 4.896   1.00 25.23 ? 1565 HOH C O   1 
HETATM 13935 O  O   . HOH AA 3 .   ? -0.183  -57.777 27.084  1.00 31.04 ? 1576 HOH C O   1 
HETATM 13936 O  O   . HOH AA 3 .   ? -10.687 -22.765 19.761  1.00 37.64 ? 1594 HOH C O   1 
HETATM 13937 O  O   . HOH AA 3 .   ? 7.901   -19.194 4.215   1.00 43.65 ? 1599 HOH C O   1 
HETATM 13938 O  O   . HOH AA 3 .   ? -8.679  -29.001 26.486  1.00 42.15 ? 1626 HOH C O   1 
HETATM 13939 O  O   . HOH AA 3 .   ? 9.076   -43.085 27.883  1.00 32.52 ? 1630 HOH C O   1 
HETATM 13940 O  O   . HOH AA 3 .   ? -12.198 -37.783 25.969  1.00 35.38 ? 1643 HOH C O   1 
HETATM 13941 O  O   . HOH AA 3 .   ? 7.372   -21.681 3.820   1.00 32.11 ? 1678 HOH C O   1 
HETATM 13942 O  O   . HOH AA 3 .   ? -7.973  -38.224 29.349  1.00 33.62 ? 1696 HOH C O   1 
HETATM 13943 O  O   . HOH AA 3 .   ? -11.623 -41.797 22.947  1.00 36.06 ? 1715 HOH C O   1 
HETATM 13944 O  O   . HOH AA 3 .   ? 4.831   -34.191 -0.760  1.00 32.30 ? 1723 HOH C O   1 
HETATM 13945 O  O   . HOH AA 3 .   ? 9.326   -57.236 27.797  1.00 33.83 ? 1725 HOH C O   1 
HETATM 13946 O  O   . HOH AA 3 .   ? -3.603  -33.902 26.922  1.00 35.62 ? 1753 HOH C O   1 
HETATM 13947 O  O   . HOH AA 3 .   ? 16.987  -36.093 22.187  1.00 33.15 ? 1763 HOH C O   1 
HETATM 13948 O  O   . HOH AA 3 .   ? 18.805  -25.057 8.807   1.00 37.99 ? 1770 HOH C O   1 
HETATM 13949 O  O   . HOH AA 3 .   ? -5.204  -37.277 29.544  1.00 39.76 ? 1772 HOH C O   1 
HETATM 13950 O  O   . HOH AA 3 .   ? -2.360  -58.667 23.995  1.00 28.41 ? 1780 HOH C O   1 
HETATM 13951 O  O   . HOH AA 3 .   ? 4.553   -31.382 -0.195  1.00 33.92 ? 1789 HOH C O   1 
HETATM 13952 O  O   . HOH AA 3 .   ? -4.401  -55.092 26.370  1.00 37.26 ? 1790 HOH C O   1 
HETATM 13953 O  O   . HOH AA 3 .   ? 15.901  -37.581 23.894  1.00 34.57 ? 1791 HOH C O   1 
HETATM 13954 O  O   . HOH AA 3 .   ? 0.614   -19.431 14.107  1.00 39.31 ? 1800 HOH C O   1 
HETATM 13955 O  O   . HOH AA 3 .   ? 14.392  -49.766 17.430  1.00 33.26 ? 1808 HOH C O   1 
HETATM 13956 O  O   . HOH BA 3 .   ? -33.548 -31.334 8.898   1.00 21.40 ? 154  HOH D O   1 
HETATM 13957 O  O   . HOH BA 3 .   ? -10.742 -40.266 3.782   1.00 15.93 ? 156  HOH D O   1 
HETATM 13958 O  O   . HOH BA 3 .   ? -7.034  -47.211 1.521   1.00 27.48 ? 157  HOH D O   1 
HETATM 13959 O  O   . HOH BA 3 .   ? -29.905 -34.494 -1.043  1.00 16.20 ? 158  HOH D O   1 
HETATM 13960 O  O   . HOH BA 3 .   ? -15.788 -40.825 8.890   1.00 21.99 ? 159  HOH D O   1 
HETATM 13961 O  O   . HOH BA 3 .   ? -27.565 -25.974 6.283   1.00 21.70 ? 160  HOH D O   1 
HETATM 13962 O  O   . HOH BA 3 .   ? -12.597 -39.972 12.874  1.00 20.70 ? 161  HOH D O   1 
HETATM 13963 O  O   . HOH BA 3 .   ? -30.027 -35.243 8.740   1.00 17.84 ? 162  HOH D O   1 
HETATM 13964 O  O   . HOH BA 3 .   ? -30.136 -42.053 6.375   1.00 24.69 ? 163  HOH D O   1 
HETATM 13965 O  O   . HOH BA 3 .   ? -29.649 -39.889 4.954   1.00 19.33 ? 164  HOH D O   1 
HETATM 13966 O  O   . HOH BA 3 .   ? -39.978 -41.359 0.172   1.00 19.53 ? 165  HOH D O   1 
HETATM 13967 O  O   . HOH BA 3 .   ? -3.162  -35.580 -2.154  1.00 27.00 ? 166  HOH D O   1 
HETATM 13968 O  O   . HOH BA 3 .   ? -20.860 -37.759 16.632  1.00 27.20 ? 167  HOH D O   1 
HETATM 13969 O  O   . HOH BA 3 .   ? -16.200 -51.157 2.049   1.00 29.07 ? 168  HOH D O   1 
HETATM 13970 O  O   . HOH BA 3 .   ? -26.097 -46.816 9.297   1.00 22.81 ? 169  HOH D O   1 
HETATM 13971 O  O   . HOH BA 3 .   ? -26.880 -35.888 -7.075  1.00 24.61 ? 170  HOH D O   1 
HETATM 13972 O  O   . HOH BA 3 .   ? -36.710 -25.270 -1.376  1.00 31.18 ? 171  HOH D O   1 
HETATM 13973 O  O   . HOH BA 3 .   ? -20.414 -51.400 3.015   1.00 26.86 ? 172  HOH D O   1 
HETATM 13974 O  O   . HOH BA 3 .   ? -35.395 -38.961 -5.583  1.00 25.93 ? 173  HOH D O   1 
HETATM 13975 O  O   . HOH BA 3 .   ? -17.698 -41.520 10.489  1.00 21.37 ? 188  HOH D O   1 
HETATM 13976 O  O   . HOH BA 3 .   ? -17.667 -21.333 3.412   1.00 30.87 ? 238  HOH D O   1 
HETATM 13977 O  O   . HOH BA 3 .   ? -33.658 -42.838 6.344   1.00 26.96 ? 239  HOH D O   1 
HETATM 13978 O  O   . HOH BA 3 .   ? -40.286 -43.266 6.106   1.00 25.29 ? 254  HOH D O   1 
HETATM 13979 O  O   . HOH BA 3 .   ? -27.980 -50.734 -0.756  1.00 23.22 ? 257  HOH D O   1 
HETATM 13980 O  O   . HOH BA 3 .   ? -13.056 -27.420 7.734   1.00 24.16 ? 300  HOH D O   1 
HETATM 13981 O  O   . HOH BA 3 .   ? -11.498 -41.582 6.741   1.00 20.73 ? 311  HOH D O   1 
HETATM 13982 O  O   . HOH BA 3 .   ? -25.606 -25.877 -6.114  1.00 23.43 ? 329  HOH D O   1 
HETATM 13983 O  O   . HOH BA 3 .   ? -24.839 -29.664 11.178  1.00 25.80 ? 341  HOH D O   1 
HETATM 13984 O  O   . HOH BA 3 .   ? -15.961 -20.524 0.664   1.00 30.99 ? 342  HOH D O   1 
HETATM 13985 O  O   . HOH BA 3 .   ? -14.156 -45.205 7.226   1.00 25.40 ? 362  HOH D O   1 
HETATM 13986 O  O   . HOH BA 3 .   ? -22.970 -43.670 -12.796 1.00 26.45 ? 364  HOH D O   1 
HETATM 13987 O  O   . HOH BA 3 .   ? -24.431 -31.274 -10.361 1.00 23.70 ? 377  HOH D O   1 
HETATM 13988 O  O   . HOH BA 3 .   ? -8.634  -20.599 -3.690  1.00 41.27 ? 406  HOH D O   1 
HETATM 13989 O  O   . HOH BA 3 .   ? -35.631 -50.999 3.013   1.00 37.01 ? 420  HOH D O   1 
HETATM 13990 O  O   . HOH BA 3 .   ? -35.780 -31.446 -5.514  1.00 32.46 ? 421  HOH D O   1 
HETATM 13991 O  O   . HOH BA 3 .   ? -15.315 -42.054 -12.284 1.00 26.52 ? 425  HOH D O   1 
HETATM 13992 O  O   . HOH BA 3 .   ? -22.724 -52.553 2.752   1.00 26.83 ? 449  HOH D O   1 
HETATM 13993 O  O   . HOH BA 3 .   ? -14.646 -22.694 -7.718  1.00 30.79 ? 462  HOH D O   1 
HETATM 13994 O  O   . HOH BA 3 .   ? -17.318 -25.978 8.135   1.00 25.20 ? 469  HOH D O   1 
HETATM 13995 O  O   . HOH BA 3 .   ? -43.237 -38.458 10.409  1.00 25.84 ? 481  HOH D O   1 
HETATM 13996 O  O   . HOH BA 3 .   ? -19.059 -53.136 -8.071  1.00 27.67 ? 487  HOH D O   1 
HETATM 13997 O  O   . HOH BA 3 .   ? -17.951 -36.139 17.209  1.00 22.15 ? 490  HOH D O   1 
HETATM 13998 O  O   . HOH BA 3 .   ? -28.939 -42.586 8.694   1.00 28.89 ? 505  HOH D O   1 
HETATM 13999 O  O   . HOH BA 3 .   ? -28.280 -25.139 3.967   1.00 25.03 ? 507  HOH D O   1 
HETATM 14000 O  O   . HOH BA 3 .   ? -13.417 -43.013 8.252   1.00 23.17 ? 516  HOH D O   1 
HETATM 14001 O  O   . HOH BA 3 .   ? -5.158  -28.341 -1.466  1.00 20.69 ? 523  HOH D O   1 
HETATM 14002 O  O   . HOH BA 3 .   ? -40.578 -45.598 5.605   1.00 28.47 ? 537  HOH D O   1 
HETATM 14003 O  O   . HOH BA 3 .   ? -14.593 -25.737 9.199   1.00 26.39 ? 552  HOH D O   1 
HETATM 14004 O  O   . HOH BA 3 .   ? -32.295 -52.235 5.513   1.00 33.37 ? 554  HOH D O   1 
HETATM 14005 O  O   . HOH BA 3 .   ? -15.637 -53.928 -3.257  1.00 35.34 ? 586  HOH D O   1 
HETATM 14006 O  O   . HOH BA 3 .   ? -11.456 -25.693 6.367   1.00 22.82 ? 598  HOH D O   1 
HETATM 14007 O  O   . HOH BA 3 .   ? -26.782 -31.113 -8.874  1.00 32.98 ? 600  HOH D O   1 
HETATM 14008 O  O   . HOH BA 3 .   ? -25.825 -32.061 15.577  1.00 28.00 ? 601  HOH D O   1 
HETATM 14009 O  O   . HOH BA 3 .   ? -27.132 -33.512 -8.874  1.00 25.74 ? 617  HOH D O   1 
HETATM 14010 O  O   . HOH BA 3 .   ? -16.125 -39.536 -12.500 1.00 26.12 ? 638  HOH D O   1 
HETATM 14011 O  O   . HOH BA 3 .   ? -28.021 -24.936 -5.690  1.00 27.90 ? 658  HOH D O   1 
HETATM 14012 O  O   . HOH BA 3 .   ? -38.140 -23.460 0.257   1.00 38.25 ? 661  HOH D O   1 
HETATM 14013 O  O   . HOH BA 3 .   ? -31.612 -53.079 1.824   1.00 36.22 ? 678  HOH D O   1 
HETATM 14014 O  O   . HOH BA 3 .   ? -25.538 -51.008 -1.999  1.00 24.55 ? 679  HOH D O   1 
HETATM 14015 O  O   . HOH BA 3 .   ? -8.793  -32.887 -6.182  1.00 26.01 ? 691  HOH D O   1 
HETATM 14016 O  O   . HOH BA 3 .   ? -29.039 -37.820 9.047   1.00 23.96 ? 702  HOH D O   1 
HETATM 14017 O  O   . HOH BA 3 .   ? -28.785 -40.190 7.714   1.00 25.84 ? 704  HOH D O   1 
HETATM 14018 O  O   . HOH BA 3 .   ? -36.130 -44.260 -0.213  1.00 21.96 ? 705  HOH D O   1 
HETATM 14019 O  O   . HOH BA 3 .   ? -11.404 -33.939 -13.610 1.00 28.79 ? 706  HOH D O   1 
HETATM 14020 O  O   . HOH BA 3 .   ? -18.905 -22.616 -2.188  1.00 27.18 ? 711  HOH D O   1 
HETATM 14021 O  O   . HOH BA 3 .   ? -33.452 -54.936 1.543   1.00 24.24 ? 722  HOH D O   1 
HETATM 14022 O  O   . HOH BA 3 .   ? -19.487 -20.353 -1.476  1.00 34.45 ? 724  HOH D O   1 
HETATM 14023 O  O   . HOH BA 3 .   ? -13.845 -47.599 13.429  1.00 27.71 ? 731  HOH D O   1 
HETATM 14024 O  O   . HOH BA 3 .   ? -24.549 -53.239 -0.565  1.00 30.12 ? 734  HOH D O   1 
HETATM 14025 O  O   . HOH BA 3 .   ? -20.421 -20.924 1.157   1.00 32.25 ? 738  HOH D O   1 
HETATM 14026 O  O   . HOH BA 3 .   ? -21.873 -48.350 -13.675 1.00 29.54 ? 751  HOH D O   1 
HETATM 14027 O  O   . HOH BA 3 .   ? -13.033 -47.430 15.841  1.00 31.69 ? 758  HOH D O   1 
HETATM 14028 O  O   . HOH BA 3 .   ? -32.641 -48.747 6.262   1.00 31.40 ? 760  HOH D O   1 
HETATM 14029 O  O   . HOH BA 3 .   ? -11.990 -42.471 -8.576  1.00 27.82 ? 771  HOH D O   1 
HETATM 14030 O  O   . HOH BA 3 .   ? -36.123 -46.467 -1.569  1.00 27.60 ? 773  HOH D O   1 
HETATM 14031 O  O   . HOH BA 3 .   ? -22.767 -42.643 17.464  1.00 22.69 ? 779  HOH D O   1 
HETATM 14032 O  O   . HOH BA 3 .   ? -33.374 -54.753 5.248   1.00 34.72 ? 791  HOH D O   1 
HETATM 14033 O  O   . HOH BA 3 .   ? -10.168 -40.717 -8.442  1.00 29.04 ? 812  HOH D O   1 
HETATM 14034 O  O   . HOH BA 3 .   ? -22.746 -45.377 17.667  1.00 31.39 ? 814  HOH D O   1 
HETATM 14035 O  O   . HOH BA 3 .   ? -7.531  -23.707 0.726   1.00 40.24 ? 818  HOH D O   1 
HETATM 14036 O  O   . HOH BA 3 .   ? -22.852 -56.447 -14.172 1.00 31.16 ? 820  HOH D O   1 
HETATM 14037 O  O   . HOH BA 3 .   ? -29.781 -22.740 -5.110  1.00 33.84 ? 823  HOH D O   1 
HETATM 14038 O  O   . HOH BA 3 .   ? -33.726 -47.083 -3.756  1.00 31.49 ? 829  HOH D O   1 
HETATM 14039 O  O   . HOH BA 3 .   ? -11.749 -23.022 6.707   1.00 34.17 ? 831  HOH D O   1 
HETATM 14040 O  O   . HOH BA 3 .   ? -36.389 -24.712 7.550   1.00 32.64 ? 833  HOH D O   1 
HETATM 14041 O  O   . HOH BA 3 .   ? -32.096 -31.785 -6.807  1.00 23.00 ? 837  HOH D O   1 
HETATM 14042 O  O   . HOH BA 3 .   ? -26.396 -45.435 11.126  1.00 34.14 ? 853  HOH D O   1 
HETATM 14043 O  O   . HOH BA 3 .   ? -19.660 -39.397 19.005  1.00 29.95 ? 858  HOH D O   1 
HETATM 14044 O  O   . HOH BA 3 .   ? -11.448 -31.711 -12.843 1.00 36.15 ? 874  HOH D O   1 
HETATM 14045 O  O   . HOH BA 3 .   ? -35.644 -26.260 10.284  1.00 29.44 ? 878  HOH D O   1 
HETATM 14046 O  O   . HOH BA 3 .   ? -26.945 -38.644 13.682  1.00 21.74 ? 881  HOH D O   1 
HETATM 14047 O  O   . HOH BA 3 .   ? -13.462 -23.408 8.750   1.00 26.50 ? 884  HOH D O   1 
HETATM 14048 O  O   . HOH BA 3 .   ? -25.206 -29.803 -6.515  1.00 26.08 ? 891  HOH D O   1 
HETATM 14049 O  O   . HOH BA 3 .   ? -23.503 -40.024 17.104  1.00 25.50 ? 892  HOH D O   1 
HETATM 14050 O  O   . HOH BA 3 .   ? -38.463 -43.379 -0.356  1.00 31.59 ? 906  HOH D O   1 
HETATM 14051 O  O   . HOH BA 3 .   ? -29.284 -38.674 11.354  1.00 25.75 ? 914  HOH D O   1 
HETATM 14052 O  O   . HOH BA 3 .   ? -30.668 -33.831 -6.971  1.00 24.89 ? 923  HOH D O   1 
HETATM 14053 O  O   . HOH BA 3 .   ? -41.159 -40.033 9.881   1.00 18.65 ? 925  HOH D O   1 
HETATM 14054 O  O   . HOH BA 3 .   ? -7.260  -39.433 -5.774  1.00 28.47 ? 932  HOH D O   1 
HETATM 14055 O  O   . HOH BA 3 .   ? -42.755 -37.561 -3.881  1.00 25.49 ? 949  HOH D O   1 
HETATM 14056 O  O   . HOH BA 3 .   ? -42.229 -34.345 2.155   1.00 24.84 ? 953  HOH D O   1 
HETATM 14057 O  O   . HOH BA 3 .   ? -36.960 -28.928 1.447   1.00 30.62 ? 957  HOH D O   1 
HETATM 14058 O  O   . HOH BA 3 .   ? -25.980 -41.006 13.584  1.00 22.96 ? 964  HOH D O   1 
HETATM 14059 O  O   . HOH BA 3 .   ? -41.048 -42.306 9.357   1.00 23.25 ? 977  HOH D O   1 
HETATM 14060 O  O   . HOH BA 3 .   ? -24.979 -50.366 6.171   1.00 27.12 ? 979  HOH D O   1 
HETATM 14061 O  O   . HOH BA 3 .   ? -29.490 -24.725 -3.586  1.00 32.13 ? 994  HOH D O   1 
HETATM 14062 O  O   . HOH BA 3 .   ? -28.477 -54.916 -11.227 1.00 35.31 ? 998  HOH D O   1 
HETATM 14063 O  O   . HOH BA 3 .   ? -24.586 -33.884 -11.315 1.00 26.77 ? 1011 HOH D O   1 
HETATM 14064 O  O   . HOH BA 3 .   ? -19.714 -41.944 18.649  1.00 32.10 ? 1023 HOH D O   1 
HETATM 14065 O  O   . HOH BA 3 .   ? -39.164 -40.211 -4.645  1.00 31.21 ? 1027 HOH D O   1 
HETATM 14066 O  O   . HOH BA 3 .   ? -37.762 -37.695 -4.873  1.00 26.59 ? 1036 HOH D O   1 
HETATM 14067 O  O   . HOH BA 3 .   ? -19.863 -28.859 13.476  1.00 26.80 ? 1040 HOH D O   1 
HETATM 14068 O  O   . HOH BA 3 .   ? -38.585 -27.915 -2.518  1.00 36.82 ? 1065 HOH D O   1 
HETATM 14069 O  O   . HOH BA 3 .   ? -8.310  -34.928 -4.898  1.00 26.23 ? 1067 HOH D O   1 
HETATM 14070 O  O   . HOH BA 3 .   ? -11.528 -22.779 -0.754  1.00 33.86 ? 1095 HOH D O   1 
HETATM 14071 O  O   . HOH BA 3 .   ? -22.299 -20.681 -1.250  1.00 36.76 ? 1126 HOH D O   1 
HETATM 14072 O  O   . HOH BA 3 .   ? -23.335 -27.033 11.850  1.00 28.29 ? 1138 HOH D O   1 
HETATM 14073 O  O   . HOH BA 3 .   ? -24.033 -22.824 12.458  1.00 36.49 ? 1141 HOH D O   1 
HETATM 14074 O  O   . HOH BA 3 .   ? -20.716 -50.179 6.774   1.00 30.45 ? 1152 HOH D O   1 
HETATM 14075 O  O   . HOH BA 3 .   ? -11.351 -20.801 -12.010 1.00 44.61 ? 1153 HOH D O   1 
HETATM 14076 O  O   . HOH BA 3 .   ? -18.016 -43.110 19.956  1.00 33.03 ? 1186 HOH D O   1 
HETATM 14077 O  O   . HOH BA 3 .   ? -27.548 -43.450 12.241  1.00 30.70 ? 1188 HOH D O   1 
HETATM 14078 O  O   . HOH BA 3 .   ? -18.603 -28.839 15.772  1.00 34.76 ? 1191 HOH D O   1 
HETATM 14079 O  O   . HOH BA 3 .   ? -32.928 -37.577 -7.307  1.00 28.56 ? 1206 HOH D O   1 
HETATM 14080 O  O   . HOH BA 3 .   ? -24.978 -29.729 -12.604 1.00 36.17 ? 1228 HOH D O   1 
HETATM 14081 O  O   . HOH BA 3 .   ? -5.272  -49.168 1.693   1.00 31.44 ? 1256 HOH D O   1 
HETATM 14082 O  O   . HOH BA 3 .   ? -21.071 -25.731 11.663  1.00 32.52 ? 1263 HOH D O   1 
HETATM 14083 O  O   . HOH BA 3 .   ? -34.552 -51.509 5.182   1.00 34.31 ? 1269 HOH D O   1 
HETATM 14084 O  O   . HOH BA 3 .   ? -26.864 -30.242 12.656  1.00 30.17 ? 1271 HOH D O   1 
HETATM 14085 O  O   . HOH BA 3 .   ? -2.919  -49.458 1.142   1.00 35.39 ? 1292 HOH D O   1 
HETATM 14086 O  O   . HOH BA 3 .   ? -41.795 -24.648 8.896   1.00 45.65 ? 1293 HOH D O   1 
HETATM 14087 O  O   . HOH BA 3 .   ? -27.603 -23.382 2.177   1.00 26.73 ? 1296 HOH D O   1 
HETATM 14088 O  O   . HOH BA 3 .   ? -35.411 -46.943 5.481   1.00 35.10 ? 1316 HOH D O   1 
HETATM 14089 O  O   . HOH BA 3 .   ? -31.361 -34.117 11.067  1.00 30.25 ? 1320 HOH D O   1 
HETATM 14090 O  O   . HOH BA 3 .   ? -39.325 -41.656 -6.960  1.00 27.02 ? 1327 HOH D O   1 
HETATM 14091 O  O   . HOH BA 3 .   ? -22.342 -30.701 -13.794 1.00 26.62 ? 1330 HOH D O   1 
HETATM 14092 O  O   . HOH BA 3 .   ? -36.854 -33.389 -6.731  1.00 37.16 ? 1342 HOH D O   1 
HETATM 14093 O  O   . HOH BA 3 .   ? -2.720  -28.585 -0.175  1.00 35.41 ? 1343 HOH D O   1 
HETATM 14094 O  O   . HOH BA 3 .   ? -29.783 -30.599 11.691  1.00 26.73 ? 1350 HOH D O   1 
HETATM 14095 O  O   . HOH BA 3 .   ? -23.375 -41.005 -9.848  1.00 21.08 ? 1356 HOH D O   1 
HETATM 14096 O  O   . HOH BA 3 .   ? -37.434 -29.589 -0.869  1.00 33.59 ? 1367 HOH D O   1 
HETATM 14097 O  O   . HOH BA 3 .   ? -0.327  -49.515 0.883   1.00 40.64 ? 1384 HOH D O   1 
HETATM 14098 O  O   . HOH BA 3 .   ? -34.543 -21.816 3.118   1.00 34.89 ? 1385 HOH D O   1 
HETATM 14099 O  O   . HOH BA 3 .   ? -27.413 -27.352 13.595  1.00 29.41 ? 1390 HOH D O   1 
HETATM 14100 O  O   . HOH BA 3 .   ? -25.226 -26.391 13.444  1.00 35.96 ? 1402 HOH D O   1 
HETATM 14101 O  O   . HOH BA 3 .   ? -23.595 -52.612 5.697   1.00 34.09 ? 1409 HOH D O   1 
HETATM 14102 O  O   . HOH BA 3 .   ? -32.665 -28.216 12.527  1.00 34.50 ? 1414 HOH D O   1 
HETATM 14103 O  O   . HOH BA 3 .   ? -24.701 -27.664 -10.856 1.00 34.28 ? 1451 HOH D O   1 
HETATM 14104 O  O   . HOH BA 3 .   ? -20.371 -56.623 -13.528 1.00 30.73 ? 1465 HOH D O   1 
HETATM 14105 O  O   . HOH BA 3 .   ? -14.520 -13.922 -4.233  1.00 37.81 ? 1467 HOH D O   1 
HETATM 14106 O  O   . HOH BA 3 .   ? -34.681 -28.895 10.239  1.00 32.47 ? 1502 HOH D O   1 
HETATM 14107 O  O   . HOH BA 3 .   ? -30.694 -36.576 -6.668  1.00 26.32 ? 1519 HOH D O   1 
HETATM 14108 O  O   . HOH BA 3 .   ? -18.487 -19.091 -10.586 1.00 35.42 ? 1525 HOH D O   1 
HETATM 14109 O  O   . HOH BA 3 .   ? -24.834 -20.077 -10.998 1.00 34.64 ? 1530 HOH D O   1 
HETATM 14110 O  O   . HOH BA 3 .   ? -21.705 -47.165 12.381  1.00 30.30 ? 1544 HOH D O   1 
HETATM 14111 O  O   . HOH BA 3 .   ? -11.740 -44.410 4.778   1.00 31.07 ? 1552 HOH D O   1 
HETATM 14112 O  O   . HOH BA 3 .   ? -23.070 -51.321 -16.147 1.00 31.67 ? 1555 HOH D O   1 
HETATM 14113 O  O   . HOH BA 3 .   ? -37.337 -36.117 -7.569  1.00 33.16 ? 1556 HOH D O   1 
HETATM 14114 O  O   . HOH BA 3 .   ? -40.266 -30.642 2.549   1.00 40.85 ? 1558 HOH D O   1 
HETATM 14115 O  O   . HOH BA 3 .   ? -37.591 -42.255 -3.152  1.00 26.43 ? 1571 HOH D O   1 
HETATM 14116 O  O   . HOH BA 3 .   ? -18.120 -56.984 -9.619  1.00 34.82 ? 1578 HOH D O   1 
HETATM 14117 O  O   . HOH BA 3 .   ? -24.546 -29.595 16.153  1.00 32.49 ? 1591 HOH D O   1 
HETATM 14118 O  O   . HOH BA 3 .   ? -21.494 -21.848 11.080  1.00 35.47 ? 1632 HOH D O   1 
HETATM 14119 O  O   . HOH BA 3 .   ? -33.955 -26.020 13.491  1.00 37.33 ? 1633 HOH D O   1 
HETATM 14120 O  O   . HOH BA 3 .   ? -22.924 -47.384 16.317  1.00 29.64 ? 1639 HOH D O   1 
HETATM 14121 O  O   . HOH BA 3 .   ? -20.915 -49.362 11.689  1.00 41.46 ? 1655 HOH D O   1 
HETATM 14122 O  O   . HOH BA 3 .   ? -20.665 -49.949 -16.666 1.00 46.46 ? 1668 HOH D O   1 
HETATM 14123 O  O   . HOH BA 3 .   ? -17.924 -54.821 -10.988 1.00 38.28 ? 1686 HOH D O   1 
HETATM 14124 O  O   . HOH BA 3 .   ? -44.935 -34.892 13.308  1.00 30.26 ? 1695 HOH D O   1 
HETATM 14125 O  O   . HOH BA 3 .   ? -21.424 -48.320 7.774   1.00 30.18 ? 1707 HOH D O   1 
HETATM 14126 O  O   . HOH BA 3 .   ? -41.194 -30.508 0.134   1.00 34.45 ? 1711 HOH D O   1 
HETATM 14127 O  O   . HOH BA 3 .   ? -14.156 -25.716 -9.148  1.00 28.33 ? 1713 HOH D O   1 
HETATM 14128 O  O   . HOH BA 3 .   ? -31.108 -47.903 -4.479  1.00 22.97 ? 1717 HOH D O   1 
HETATM 14129 O  O   . HOH BA 3 .   ? -36.032 -44.196 6.952   1.00 32.55 ? 1731 HOH D O   1 
HETATM 14130 O  O   . HOH BA 3 .   ? -19.509 -18.403 -7.856  1.00 33.31 ? 1736 HOH D O   1 
HETATM 14131 O  O   . HOH BA 3 .   ? -19.349 -48.459 9.190   1.00 37.17 ? 1740 HOH D O   1 
HETATM 14132 O  O   . HOH BA 3 .   ? -29.048 -47.373 -12.412 1.00 31.81 ? 1801 HOH D O   1 
HETATM 14133 O  O   . HOH CA 3 .   ? 21.036  -37.498 54.234  1.00 17.80 ? 154  HOH E O   1 
HETATM 14134 O  O   . HOH CA 3 .   ? 11.861  -22.040 41.022  1.00 36.40 ? 156  HOH E O   1 
HETATM 14135 O  O   . HOH CA 3 .   ? 16.044  -31.153 35.536  1.00 26.44 ? 157  HOH E O   1 
HETATM 14136 O  O   . HOH CA 3 .   ? 26.439  -38.738 36.794  1.00 24.76 ? 158  HOH E O   1 
HETATM 14137 O  O   . HOH CA 3 .   ? 22.975  -32.884 35.255  1.00 26.34 ? 159  HOH E O   1 
HETATM 14138 O  O   . HOH CA 3 .   ? 19.539  -18.569 48.459  1.00 38.98 ? 160  HOH E O   1 
HETATM 14139 O  O   . HOH CA 3 .   ? 11.501  -31.640 22.102  1.00 28.37 ? 161  HOH E O   1 
HETATM 14140 O  O   . HOH CA 3 .   ? 7.215   -38.252 36.031  1.00 33.15 ? 162  HOH E O   1 
HETATM 14141 O  O   . HOH CA 3 .   ? 29.111  -42.499 35.642  1.00 33.54 ? 165  HOH E O   1 
HETATM 14142 O  O   . HOH CA 3 .   ? 7.778   -31.014 40.344  1.00 26.67 ? 171  HOH E O   1 
HETATM 14143 O  O   . HOH CA 3 .   ? 16.934  -35.857 28.362  1.00 33.09 ? 176  HOH E O   1 
HETATM 14144 O  O   . HOH CA 3 .   ? 18.456  -41.243 53.915  1.00 28.82 ? 222  HOH E O   1 
HETATM 14145 O  O   . HOH CA 3 .   ? 17.086  -48.083 38.800  1.00 32.77 ? 227  HOH E O   1 
HETATM 14146 O  O   . HOH CA 3 .   ? 10.840  -36.152 38.678  1.00 32.14 ? 249  HOH E O   1 
HETATM 14147 O  O   . HOH CA 3 .   ? 6.297   -26.867 37.187  1.00 30.53 ? 272  HOH E O   1 
HETATM 14148 O  O   . HOH CA 3 .   ? 30.313  -33.547 52.085  1.00 29.35 ? 273  HOH E O   1 
HETATM 14149 O  O   . HOH CA 3 .   ? 12.185  -45.713 47.778  1.00 35.69 ? 338  HOH E O   1 
HETATM 14150 O  O   . HOH CA 3 .   ? 13.849  -37.152 52.712  1.00 28.96 ? 361  HOH E O   1 
HETATM 14151 O  O   . HOH CA 3 .   ? -0.175  -33.376 28.295  1.00 35.40 ? 392  HOH E O   1 
HETATM 14152 O  O   . HOH CA 3 .   ? 16.017  -48.224 45.740  1.00 39.39 ? 400  HOH E O   1 
HETATM 14153 O  O   . HOH CA 3 .   ? 30.574  -20.853 45.535  1.00 41.20 ? 408  HOH E O   1 
HETATM 14154 O  O   . HOH CA 3 .   ? 32.533  -41.220 35.277  1.00 30.66 ? 438  HOH E O   1 
HETATM 14155 O  O   . HOH CA 3 .   ? 11.893  -25.468 30.336  1.00 42.39 ? 448  HOH E O   1 
HETATM 14156 O  O   . HOH CA 3 .   ? 23.817  -26.896 36.453  1.00 28.44 ? 450  HOH E O   1 
HETATM 14157 O  O   . HOH CA 3 .   ? 32.864  -33.896 56.353  1.00 28.00 ? 453  HOH E O   1 
HETATM 14158 O  O   . HOH CA 3 .   ? 24.193  -20.286 44.355  1.00 38.23 ? 467  HOH E O   1 
HETATM 14159 O  O   . HOH CA 3 .   ? 18.032  -38.591 55.002  1.00 23.43 ? 491  HOH E O   1 
HETATM 14160 O  O   . HOH CA 3 .   ? 12.480  -36.464 57.438  1.00 20.75 ? 525  HOH E O   1 
HETATM 14161 O  O   . HOH CA 3 .   ? 8.600   -43.178 46.891  1.00 38.07 ? 556  HOH E O   1 
HETATM 14162 O  O   . HOH CA 3 .   ? 20.326  -22.985 55.077  1.00 30.62 ? 562  HOH E O   1 
HETATM 14163 O  O   . HOH CA 3 .   ? 16.117  -34.045 26.573  1.00 33.99 ? 573  HOH E O   1 
HETATM 14164 O  O   . HOH CA 3 .   ? 5.122   -24.056 37.494  1.00 37.94 ? 588  HOH E O   1 
HETATM 14165 O  O   . HOH CA 3 .   ? 30.945  -31.277 51.257  1.00 32.09 ? 592  HOH E O   1 
HETATM 14166 O  O   . HOH CA 3 .   ? 25.414  -28.898 34.737  1.00 35.53 ? 608  HOH E O   1 
HETATM 14167 O  O   . HOH CA 3 .   ? 13.399  -21.143 39.305  1.00 30.78 ? 618  HOH E O   1 
HETATM 14168 O  O   . HOH CA 3 .   ? 23.353  -51.670 46.303  1.00 42.74 ? 639  HOH E O   1 
HETATM 14169 O  O   . HOH CA 3 .   ? 10.413  -44.344 49.148  1.00 43.47 ? 642  HOH E O   1 
HETATM 14170 O  O   . HOH CA 3 .   ? 8.334   -43.081 44.047  1.00 35.99 ? 644  HOH E O   1 
HETATM 14171 O  O   . HOH CA 3 .   ? 4.804   -33.146 52.678  1.00 38.27 ? 665  HOH E O   1 
HETATM 14172 O  O   . HOH CA 3 .   ? 25.596  -51.862 28.322  1.00 38.46 ? 683  HOH E O   1 
HETATM 14173 O  O   . HOH CA 3 .   ? 5.624   -22.574 44.009  1.00 33.47 ? 686  HOH E O   1 
HETATM 14174 O  O   . HOH CA 3 .   ? 9.677   -26.514 26.678  1.00 36.48 ? 687  HOH E O   1 
HETATM 14175 O  O   . HOH CA 3 .   ? 20.174  -28.701 30.724  1.00 33.90 ? 703  HOH E O   1 
HETATM 14176 O  O   . HOH CA 3 .   ? 16.212  -42.025 53.046  1.00 32.59 ? 733  HOH E O   1 
HETATM 14177 O  O   . HOH CA 3 .   ? 21.248  -52.233 34.144  1.00 35.78 ? 746  HOH E O   1 
HETATM 14178 O  O   . HOH CA 3 .   ? 9.625   -25.057 51.663  1.00 33.07 ? 768  HOH E O   1 
HETATM 14179 O  O   . HOH CA 3 .   ? 15.127  -39.135 53.600  1.00 27.83 ? 774  HOH E O   1 
HETATM 14180 O  O   . HOH CA 3 .   ? 21.626  -30.853 31.865  1.00 31.27 ? 836  HOH E O   1 
HETATM 14181 O  O   . HOH CA 3 .   ? 15.221  -22.544 51.595  1.00 31.89 ? 863  HOH E O   1 
HETATM 14182 O  O   . HOH CA 3 .   ? 9.372   -24.467 29.921  1.00 44.88 ? 920  HOH E O   1 
HETATM 14183 O  O   . HOH CA 3 .   ? 29.369  -26.383 56.535  1.00 27.57 ? 929  HOH E O   1 
HETATM 14184 O  O   . HOH CA 3 .   ? 2.104   -38.303 28.288  1.00 37.86 ? 958  HOH E O   1 
HETATM 14185 O  O   . HOH CA 3 .   ? 7.848   -33.353 41.174  1.00 28.68 ? 970  HOH E O   1 
HETATM 14186 O  O   . HOH CA 3 .   ? 4.915   -34.428 45.040  1.00 29.45 ? 973  HOH E O   1 
HETATM 14187 O  O   . HOH CA 3 .   ? 30.811  -37.496 52.270  1.00 30.19 ? 975  HOH E O   1 
HETATM 14188 O  O   . HOH CA 3 .   ? 35.871  -29.895 46.315  1.00 42.06 ? 985  HOH E O   1 
HETATM 14189 O  O   . HOH CA 3 .   ? 6.420   -37.253 26.411  1.00 35.46 ? 997  HOH E O   1 
HETATM 14190 O  O   . HOH CA 3 .   ? 8.622   -36.027 40.924  1.00 31.62 ? 1002 HOH E O   1 
HETATM 14191 O  O   . HOH CA 3 .   ? 9.974   -37.448 27.745  1.00 36.63 ? 1005 HOH E O   1 
HETATM 14192 O  O   . HOH CA 3 .   ? 31.614  -30.408 35.665  1.00 34.72 ? 1009 HOH E O   1 
HETATM 14193 O  O   . HOH CA 3 .   ? 20.429  -21.898 34.603  1.00 33.82 ? 1015 HOH E O   1 
HETATM 14194 O  O   . HOH CA 3 .   ? 29.212  -31.326 34.860  1.00 34.12 ? 1034 HOH E O   1 
HETATM 14195 O  O   . HOH CA 3 .   ? 31.845  -25.652 56.947  1.00 32.27 ? 1057 HOH E O   1 
HETATM 14196 O  O   . HOH CA 3 .   ? 17.860  -24.360 55.117  1.00 30.65 ? 1105 HOH E O   1 
HETATM 14197 O  O   . HOH CA 3 .   ? 15.959  -22.538 54.073  1.00 32.10 ? 1169 HOH E O   1 
HETATM 14198 O  O   . HOH CA 3 .   ? 7.885   -28.419 41.193  1.00 34.44 ? 1175 HOH E O   1 
HETATM 14199 O  O   . HOH CA 3 .   ? 17.376  -50.132 40.327  1.00 38.27 ? 1181 HOH E O   1 
HETATM 14200 O  O   . HOH CA 3 .   ? 17.275  -31.740 26.685  1.00 39.58 ? 1184 HOH E O   1 
HETATM 14201 O  O   . HOH CA 3 .   ? 11.768  -40.396 30.690  1.00 33.41 ? 1210 HOH E O   1 
HETATM 14202 O  O   . HOH CA 3 .   ? 4.683   -36.764 45.994  1.00 28.67 ? 1212 HOH E O   1 
HETATM 14203 O  O   . HOH CA 3 .   ? 10.758  -23.226 53.114  1.00 29.66 ? 1248 HOH E O   1 
HETATM 14204 O  O   . HOH CA 3 .   ? 34.096  -29.258 63.864  1.00 30.63 ? 1306 HOH E O   1 
HETATM 14205 O  O   . HOH CA 3 .   ? 11.143  -48.083 34.433  1.00 37.23 ? 1332 HOH E O   1 
HETATM 14206 O  O   . HOH CA 3 .   ? 23.901  -45.482 51.428  1.00 40.30 ? 1355 HOH E O   1 
HETATM 14207 O  O   . HOH CA 3 .   ? 20.090  -35.453 29.924  1.00 36.60 ? 1360 HOH E O   1 
HETATM 14208 O  O   . HOH CA 3 .   ? 22.111  -18.307 44.550  1.00 38.09 ? 1411 HOH E O   1 
HETATM 14209 O  O   . HOH CA 3 .   ? 4.818   -34.868 57.945  1.00 35.65 ? 1416 HOH E O   1 
HETATM 14210 O  O   . HOH CA 3 .   ? 24.155  -50.867 26.421  1.00 36.68 ? 1461 HOH E O   1 
HETATM 14211 O  O   . HOH CA 3 .   ? 6.808   -40.793 32.154  1.00 42.56 ? 1472 HOH E O   1 
HETATM 14212 O  O   . HOH CA 3 .   ? 34.265  -16.665 51.071  1.00 48.20 ? 1476 HOH E O   1 
HETATM 14213 O  O   . HOH CA 3 .   ? 7.966   -24.841 53.544  1.00 41.38 ? 1493 HOH E O   1 
HETATM 14214 O  O   . HOH CA 3 .   ? 8.682   -25.376 45.794  1.00 35.82 ? 1495 HOH E O   1 
HETATM 14215 O  O   . HOH CA 3 .   ? 36.036  -31.385 48.465  1.00 34.21 ? 1498 HOH E O   1 
HETATM 14216 O  O   . HOH CA 3 .   ? 25.875  -51.226 42.280  1.00 35.45 ? 1522 HOH E O   1 
HETATM 14217 O  O   . HOH CA 3 .   ? 18.887  -12.339 52.032  1.00 50.67 ? 1583 HOH E O   1 
HETATM 14218 O  O   . HOH CA 3 .   ? 6.697   -19.012 34.704  1.00 47.08 ? 1606 HOH E O   1 
HETATM 14219 O  O   . HOH CA 3 .   ? 30.109  -28.815 34.365  1.00 36.57 ? 1638 HOH E O   1 
HETATM 14220 O  O   . HOH CA 3 .   ? 31.974  -23.868 45.324  1.00 37.15 ? 1720 HOH E O   1 
HETATM 14221 O  O   . HOH CA 3 .   ? 26.652  -26.206 56.107  1.00 35.26 ? 1741 HOH E O   1 
HETATM 14222 O  O   . HOH CA 3 .   ? 26.465  -11.146 45.287  1.00 44.00 ? 1773 HOH E O   1 
HETATM 14223 O  O   . HOH CA 3 .   ? 18.092  -47.991 49.319  1.00 37.02 ? 1779 HOH E O   1 
HETATM 14224 O  O   . HOH DA 3 .   ? 20.751  -33.749 77.630  1.00 19.92 ? 154  HOH F O   1 
HETATM 14225 O  O   . HOH DA 3 .   ? 25.929  -24.677 72.983  1.00 22.87 ? 156  HOH F O   1 
HETATM 14226 O  O   . HOH DA 3 .   ? 30.229  -33.907 57.829  1.00 22.36 ? 157  HOH F O   1 
HETATM 14227 O  O   . HOH DA 3 .   ? 23.514  -37.200 55.673  1.00 18.77 ? 158  HOH F O   1 
HETATM 14228 O  O   . HOH DA 3 .   ? 22.302  -31.755 84.701  1.00 28.64 ? 159  HOH F O   1 
HETATM 14229 O  O   . HOH DA 3 .   ? 26.932  -40.989 73.271  1.00 26.61 ? 160  HOH F O   1 
HETATM 14230 O  O   . HOH DA 3 .   ? 17.626  -47.011 79.373  1.00 25.17 ? 161  HOH F O   1 
HETATM 14231 O  O   . HOH DA 3 .   ? 13.682  -34.797 78.150  1.00 20.30 ? 162  HOH F O   1 
HETATM 14232 O  O   . HOH DA 3 .   ? 17.960  -38.919 57.434  1.00 21.90 ? 163  HOH F O   1 
HETATM 14233 O  O   . HOH DA 3 .   ? 17.989  -23.758 79.436  1.00 32.96 ? 164  HOH F O   1 
HETATM 14234 O  O   . HOH DA 3 .   ? 14.682  -37.418 58.340  1.00 17.49 ? 165  HOH F O   1 
HETATM 14235 O  O   . HOH DA 3 .   ? 8.252   -32.667 78.393  1.00 29.16 ? 166  HOH F O   1 
HETATM 14236 O  O   . HOH DA 3 .   ? 29.363  -34.386 72.409  1.00 22.34 ? 167  HOH F O   1 
HETATM 14237 O  O   . HOH DA 3 .   ? 18.469  -49.500 66.362  1.00 28.12 ? 168  HOH F O   1 
HETATM 14238 O  O   . HOH DA 3 .   ? 16.235  -49.080 62.260  1.00 30.44 ? 169  HOH F O   1 
HETATM 14239 O  O   . HOH DA 3 .   ? 24.413  -23.892 74.993  1.00 23.39 ? 174  HOH F O   1 
HETATM 14240 O  O   . HOH DA 3 .   ? 25.617  -29.313 82.769  1.00 27.85 ? 182  HOH F O   1 
HETATM 14241 O  O   . HOH DA 3 .   ? 6.595   -42.401 76.657  1.00 24.60 ? 194  HOH F O   1 
HETATM 14242 O  O   . HOH DA 3 .   ? 20.611  -37.012 86.196  1.00 28.32 ? 207  HOH F O   1 
HETATM 14243 O  O   . HOH DA 3 .   ? 24.541  -43.778 81.911  1.00 30.22 ? 213  HOH F O   1 
HETATM 14244 O  O   . HOH DA 3 .   ? 11.403  -20.333 63.382  1.00 34.65 ? 226  HOH F O   1 
HETATM 14245 O  O   . HOH DA 3 .   ? 27.104  -45.714 68.483  1.00 22.96 ? 233  HOH F O   1 
HETATM 14246 O  O   . HOH DA 3 .   ? 19.554  -38.804 84.476  1.00 22.28 ? 256  HOH F O   1 
HETATM 14247 O  O   . HOH DA 3 .   ? 14.102  -24.922 77.111  1.00 29.13 ? 258  HOH F O   1 
HETATM 14248 O  O   . HOH DA 3 .   ? 28.906  -36.626 71.531  1.00 22.97 ? 264  HOH F O   1 
HETATM 14249 O  O   . HOH DA 3 .   ? 16.509  -46.278 82.844  1.00 28.43 ? 289  HOH F O   1 
HETATM 14250 O  O   . HOH DA 3 .   ? 22.149  -22.982 76.469  1.00 25.32 ? 318  HOH F O   1 
HETATM 14251 O  O   . HOH DA 3 .   ? 8.407   -51.498 69.672  1.00 30.73 ? 324  HOH F O   1 
HETATM 14252 O  O   . HOH DA 3 .   ? 30.988  -39.362 66.529  1.00 25.43 ? 332  HOH F O   1 
HETATM 14253 O  O   . HOH DA 3 .   ? 28.721  -31.274 82.784  1.00 30.58 ? 340  HOH F O   1 
HETATM 14254 O  O   . HOH DA 3 .   ? 26.764  -41.892 84.868  1.00 32.62 ? 363  HOH F O   1 
HETATM 14255 O  O   . HOH DA 3 .   ? 19.127  -49.639 74.792  1.00 27.32 ? 365  HOH F O   1 
HETATM 14256 O  O   . HOH DA 3 .   ? 28.847  -28.085 67.777  1.00 27.63 ? 375  HOH F O   1 
HETATM 14257 O  O   . HOH DA 3 .   ? 20.028  -40.071 58.594  1.00 22.93 ? 402  HOH F O   1 
HETATM 14258 O  O   . HOH DA 3 .   ? 14.451  -20.260 70.383  1.00 32.42 ? 428  HOH F O   1 
HETATM 14259 O  O   . HOH DA 3 .   ? 31.232  -30.620 75.916  1.00 24.45 ? 435  HOH F O   1 
HETATM 14260 O  O   . HOH DA 3 .   ? 14.496  -21.702 58.682  1.00 31.82 ? 436  HOH F O   1 
HETATM 14261 O  O   . HOH DA 3 .   ? 17.999  -23.237 59.054  1.00 35.73 ? 456  HOH F O   1 
HETATM 14262 O  O   . HOH DA 3 .   ? 24.018  -21.622 77.647  1.00 34.38 ? 488  HOH F O   1 
HETATM 14263 O  O   . HOH DA 3 .   ? 5.940   -31.991 54.983  1.00 30.96 ? 496  HOH F O   1 
HETATM 14264 O  O   . HOH DA 3 .   ? 16.810  -49.612 78.922  1.00 33.43 ? 515  HOH F O   1 
HETATM 14265 O  O   . HOH DA 3 .   ? 19.324  -42.732 59.124  1.00 28.64 ? 519  HOH F O   1 
HETATM 14266 O  O   . HOH DA 3 .   ? 29.466  -31.464 71.811  1.00 22.96 ? 532  HOH F O   1 
HETATM 14267 O  O   . HOH DA 3 .   ? 20.087  -42.574 55.697  1.00 33.97 ? 533  HOH F O   1 
HETATM 14268 O  O   . HOH DA 3 .   ? 31.347  -37.462 67.905  1.00 23.64 ? 535  HOH F O   1 
HETATM 14269 O  O   . HOH DA 3 .   ? 20.121  -24.889 58.958  1.00 22.26 ? 543  HOH F O   1 
HETATM 14270 O  O   . HOH DA 3 .   ? 6.017   -51.003 68.602  1.00 37.95 ? 571  HOH F O   1 
HETATM 14271 O  O   . HOH DA 3 .   ? 9.579   -46.844 81.210  1.00 28.87 ? 583  HOH F O   1 
HETATM 14272 O  O   . HOH DA 3 .   ? 31.453  -20.959 70.815  1.00 30.77 ? 597  HOH F O   1 
HETATM 14273 O  O   . HOH DA 3 .   ? 28.611  -43.968 69.288  1.00 28.19 ? 640  HOH F O   1 
HETATM 14274 O  O   . HOH DA 3 .   ? 30.452  -19.336 75.236  1.00 32.93 ? 671  HOH F O   1 
HETATM 14275 O  O   . HOH DA 3 .   ? 33.617  -26.412 77.600  1.00 30.82 ? 725  HOH F O   1 
HETATM 14276 O  O   . HOH DA 3 .   ? 33.287  -28.030 75.708  1.00 29.86 ? 777  HOH F O   1 
HETATM 14277 O  O   . HOH DA 3 .   ? 22.655  -23.580 63.003  1.00 26.15 ? 803  HOH F O   1 
HETATM 14278 O  O   . HOH DA 3 .   ? 16.232  -20.294 57.835  1.00 41.85 ? 813  HOH F O   1 
HETATM 14279 O  O   . HOH DA 3 .   ? 27.559  -38.970 71.480  1.00 24.01 ? 851  HOH F O   1 
HETATM 14280 O  O   . HOH DA 3 .   ? 16.768  -41.812 58.646  1.00 28.15 ? 869  HOH F O   1 
HETATM 14281 O  O   . HOH DA 3 .   ? 20.361  -46.935 81.094  1.00 29.03 ? 927  HOH F O   1 
HETATM 14282 O  O   . HOH DA 3 .   ? 16.865  -51.253 71.198  1.00 33.67 ? 972  HOH F O   1 
HETATM 14283 O  O   . HOH DA 3 .   ? 31.009  -29.638 71.736  1.00 24.20 ? 999  HOH F O   1 
HETATM 14284 O  O   . HOH DA 3 .   ? 31.592  -36.006 60.596  1.00 25.36 ? 1021 HOH F O   1 
HETATM 14285 O  O   . HOH DA 3 .   ? 17.116  -49.604 73.169  1.00 26.47 ? 1022 HOH F O   1 
HETATM 14286 O  O   . HOH DA 3 .   ? 31.189  -37.677 70.648  1.00 32.71 ? 1032 HOH F O   1 
HETATM 14287 O  O   . HOH DA 3 .   ? 27.987  -27.073 62.288  1.00 23.90 ? 1052 HOH F O   1 
HETATM 14288 O  O   . HOH DA 3 .   ? 6.051   -30.168 62.620  1.00 32.84 ? 1059 HOH F O   1 
HETATM 14289 O  O   . HOH DA 3 .   ? 9.634   -39.861 76.591  1.00 23.87 ? 1098 HOH F O   1 
HETATM 14290 O  O   . HOH DA 3 .   ? 4.881   -39.923 65.231  1.00 27.18 ? 1112 HOH F O   1 
HETATM 14291 O  O   . HOH DA 3 .   ? 15.748  -23.877 57.729  1.00 31.34 ? 1115 HOH F O   1 
HETATM 14292 O  O   . HOH DA 3 .   ? 3.964   -38.213 63.927  1.00 35.93 ? 1140 HOH F O   1 
HETATM 14293 O  O   . HOH DA 3 .   ? 13.668  -28.410 77.153  1.00 26.36 ? 1155 HOH F O   1 
HETATM 14294 O  O   . HOH DA 3 .   ? 4.136   -46.307 76.223  1.00 32.72 ? 1180 HOH F O   1 
HETATM 14295 O  O   . HOH DA 3 .   ? 22.332  -23.339 60.564  1.00 33.08 ? 1202 HOH F O   1 
HETATM 14296 O  O   . HOH DA 3 .   ? 22.251  -38.766 87.751  1.00 31.02 ? 1211 HOH F O   1 
HETATM 14297 O  O   . HOH DA 3 .   ? 22.115  -24.091 57.217  1.00 32.25 ? 1232 HOH F O   1 
HETATM 14298 O  O   . HOH DA 3 .   ? 6.289   -32.113 60.985  1.00 30.07 ? 1273 HOH F O   1 
HETATM 14299 O  O   . HOH DA 3 .   ? 10.440  -44.053 56.101  1.00 37.21 ? 1294 HOH F O   1 
HETATM 14300 O  O   . HOH DA 3 .   ? 1.429   -46.352 75.624  1.00 37.37 ? 1295 HOH F O   1 
HETATM 14301 O  O   . HOH DA 3 .   ? 28.777  -42.238 76.233  1.00 29.04 ? 1302 HOH F O   1 
HETATM 14302 O  O   . HOH DA 3 .   ? 2.622   -32.255 61.071  1.00 37.95 ? 1314 HOH F O   1 
HETATM 14303 O  O   . HOH DA 3 .   ? 18.937  -19.151 67.295  1.00 35.37 ? 1315 HOH F O   1 
HETATM 14304 O  O   . HOH DA 3 .   ? 21.452  -24.173 85.953  1.00 35.96 ? 1324 HOH F O   1 
HETATM 14305 O  O   . HOH DA 3 .   ? 1.121   -33.175 62.836  1.00 40.42 ? 1334 HOH F O   1 
HETATM 14306 O  O   . HOH DA 3 .   ? 18.127  -43.604 56.842  1.00 38.77 ? 1335 HOH F O   1 
HETATM 14307 O  O   . HOH DA 3 .   ? 5.733   -23.344 68.927  1.00 34.32 ? 1358 HOH F O   1 
HETATM 14308 O  O   . HOH DA 3 .   ? 18.922  -46.189 83.508  1.00 32.78 ? 1362 HOH F O   1 
HETATM 14309 O  O   . HOH DA 3 .   ? 30.243  -42.608 67.672  1.00 35.07 ? 1364 HOH F O   1 
HETATM 14310 O  O   . HOH DA 3 .   ? 27.833  -30.900 85.971  1.00 36.74 ? 1365 HOH F O   1 
HETATM 14311 O  O   . HOH DA 3 .   ? 31.573  -32.652 73.227  1.00 30.12 ? 1371 HOH F O   1 
HETATM 14312 O  O   . HOH DA 3 .   ? 19.969  -20.982 59.746  1.00 34.26 ? 1381 HOH F O   1 
HETATM 14313 O  O   . HOH DA 3 .   ? 35.155  -40.600 81.432  1.00 28.19 ? 1388 HOH F O   1 
HETATM 14314 O  O   . HOH DA 3 .   ? 32.752  -30.352 65.667  1.00 32.36 ? 1403 HOH F O   1 
HETATM 14315 O  O   . HOH DA 3 .   ? 35.544  -38.789 77.044  1.00 39.40 ? 1404 HOH F O   1 
HETATM 14316 O  O   . HOH DA 3 .   ? 2.003   -35.064 60.681  1.00 36.72 ? 1406 HOH F O   1 
HETATM 14317 O  O   . HOH DA 3 .   ? 10.520  -51.309 64.474  1.00 43.73 ? 1422 HOH F O   1 
HETATM 14318 O  O   . HOH DA 3 .   ? 27.229  -45.094 82.727  1.00 36.08 ? 1423 HOH F O   1 
HETATM 14319 O  O   . HOH DA 3 .   ? 8.304   -13.118 65.948  1.00 43.91 ? 1424 HOH F O   1 
HETATM 14320 O  O   . HOH DA 3 .   ? 8.528   -16.693 74.532  1.00 50.23 ? 1433 HOH F O   1 
HETATM 14321 O  O   . HOH DA 3 .   ? 34.321  -43.041 81.268  1.00 35.23 ? 1480 HOH F O   1 
HETATM 14322 O  O   . HOH DA 3 .   ? 31.260  -24.758 80.161  1.00 36.78 ? 1481 HOH F O   1 
HETATM 14323 O  O   . HOH DA 3 .   ? 20.385  -26.371 86.469  1.00 35.82 ? 1496 HOH F O   1 
HETATM 14324 O  O   . HOH DA 3 .   ? 3.029   -32.365 76.553  1.00 34.05 ? 1497 HOH F O   1 
HETATM 14325 O  O   . HOH DA 3 .   ? 20.330  -45.346 58.985  1.00 32.98 ? 1501 HOH F O   1 
HETATM 14326 O  O   . HOH DA 3 .   ? 16.304  -18.276 67.118  1.00 41.13 ? 1506 HOH F O   1 
HETATM 14327 O  O   . HOH DA 3 .   ? 23.215  -29.217 87.157  1.00 35.98 ? 1507 HOH F O   1 
HETATM 14328 O  O   . HOH DA 3 .   ? 10.791  -44.997 61.130  1.00 34.30 ? 1508 HOH F O   1 
HETATM 14329 O  O   . HOH DA 3 .   ? 3.676   -37.757 75.110  1.00 28.29 ? 1521 HOH F O   1 
HETATM 14330 O  O   . HOH DA 3 .   ? 3.774   -31.773 49.134  1.00 41.98 ? 1523 HOH F O   1 
HETATM 14331 O  O   . HOH DA 3 .   ? 28.188  -41.457 71.156  1.00 30.11 ? 1537 HOH F O   1 
HETATM 14332 O  O   . HOH DA 3 .   ? 8.545   -24.833 57.540  1.00 33.19 ? 1541 HOH F O   1 
HETATM 14333 O  O   . HOH DA 3 .   ? 18.384  -21.343 80.059  1.00 36.35 ? 1574 HOH F O   1 
HETATM 14334 O  O   . HOH DA 3 .   ? 4.675   -36.717 60.288  1.00 34.31 ? 1592 HOH F O   1 
HETATM 14335 O  O   . HOH DA 3 .   ? 7.425   -20.485 69.268  1.00 38.97 ? 1608 HOH F O   1 
HETATM 14336 O  O   . HOH DA 3 .   ? 4.572   -32.227 58.687  1.00 35.88 ? 1631 HOH F O   1 
HETATM 14337 O  O   . HOH DA 3 .   ? 24.613  -24.144 56.418  1.00 34.51 ? 1644 HOH F O   1 
HETATM 14338 O  O   . HOH DA 3 .   ? 8.708   -53.213 63.444  1.00 39.84 ? 1658 HOH F O   1 
HETATM 14339 O  O   . HOH DA 3 .   ? -1.851  -36.181 60.062  1.00 34.31 ? 1672 HOH F O   1 
HETATM 14340 O  O   . HOH DA 3 .   ? 0.677   -37.348 59.583  1.00 47.26 ? 1675 HOH F O   1 
HETATM 14341 O  O   . HOH DA 3 .   ? 32.716  -37.527 56.505  1.00 26.97 ? 1682 HOH F O   1 
HETATM 14342 O  O   . HOH DA 3 .   ? 29.633  -44.237 78.912  1.00 30.73 ? 1689 HOH F O   1 
HETATM 14343 O  O   . HOH DA 3 .   ? 28.266  -46.273 78.564  1.00 36.73 ? 1709 HOH F O   1 
HETATM 14344 O  O   . HOH DA 3 .   ? 25.752  -29.478 86.052  1.00 39.67 ? 1712 HOH F O   1 
HETATM 14345 O  O   . HOH DA 3 .   ? 8.819   -23.107 76.062  1.00 43.21 ? 1727 HOH F O   1 
HETATM 14346 O  O   . HOH DA 3 .   ? 32.522  -40.449 55.802  1.00 32.48 ? 1733 HOH F O   1 
HETATM 14347 O  O   . HOH DA 3 .   ? 1.207   -28.854 68.649  1.00 33.76 ? 1750 HOH F O   1 
HETATM 14348 O  O   . HOH DA 3 .   ? 7.367   -48.716 82.445  1.00 36.30 ? 1754 HOH F O   1 
HETATM 14349 O  O   . HOH DA 3 .   ? 4.783   -51.384 65.993  1.00 41.30 ? 1771 HOH F O   1 
HETATM 14350 O  O   . HOH DA 3 .   ? 2.496   -46.765 73.344  1.00 43.24 ? 1783 HOH F O   1 
HETATM 14351 O  O   . HOH DA 3 .   ? 6.404   -49.325 61.210  1.00 37.12 ? 1785 HOH F O   1 
HETATM 14352 O  O   . HOH DA 3 .   ? 11.499  -17.746 60.812  1.00 38.19 ? 1796 HOH F O   1 
HETATM 14353 O  O   . HOH DA 3 .   ? 9.643   -27.807 79.210  1.00 46.72 ? 1803 HOH F O   1 
HETATM 14354 O  O   . HOH EA 3 .   ? 56.955  -11.689 -7.878  1.00 16.36 ? 154  HOH G O   1 
HETATM 14355 O  O   . HOH EA 3 .   ? 55.012  -2.047  -10.492 1.00 19.90 ? 156  HOH G O   1 
HETATM 14356 O  O   . HOH EA 3 .   ? 55.364  2.166   -6.183  1.00 17.66 ? 157  HOH G O   1 
HETATM 14357 O  O   . HOH EA 3 .   ? 72.390  2.002   -13.868 1.00 20.20 ? 158  HOH G O   1 
HETATM 14358 O  O   . HOH EA 3 .   ? 74.247  1.933   -4.906  1.00 19.92 ? 159  HOH G O   1 
HETATM 14359 O  O   . HOH EA 3 .   ? 60.871  2.816   8.260   1.00 24.53 ? 160  HOH G O   1 
HETATM 14360 O  O   . HOH EA 3 .   ? 55.016  -3.315  -0.565  1.00 17.44 ? 161  HOH G O   1 
HETATM 14361 O  O   . HOH EA 3 .   ? 46.840  -6.051  -4.932  1.00 27.24 ? 162  HOH G O   1 
HETATM 14362 O  O   . HOH EA 3 .   ? 69.754  -15.829 6.410   1.00 26.59 ? 163  HOH G O   1 
HETATM 14363 O  O   . HOH EA 3 .   ? 42.768  -3.254  -4.006  1.00 21.83 ? 164  HOH G O   1 
HETATM 14364 O  O   . HOH EA 3 .   ? 63.207  -18.755 4.892   1.00 18.01 ? 165  HOH G O   1 
HETATM 14365 O  O   . HOH EA 3 .   ? 58.114  -1.962  5.537   1.00 19.26 ? 166  HOH G O   1 
HETATM 14366 O  O   . HOH EA 3 .   ? 67.274  -12.039 -9.828  1.00 22.69 ? 167  HOH G O   1 
HETATM 14367 O  O   . HOH EA 3 .   ? 60.352  -6.799  9.091   1.00 23.10 ? 168  HOH G O   1 
HETATM 14368 O  O   . HOH EA 3 .   ? 59.715  -7.939  -12.661 1.00 24.07 ? 169  HOH G O   1 
HETATM 14369 O  O   . HOH EA 3 .   ? 65.693  -15.350 0.362   1.00 21.40 ? 170  HOH G O   1 
HETATM 14370 O  O   . HOH EA 3 .   ? 56.370  -12.729 -5.168  1.00 20.87 ? 171  HOH G O   1 
HETATM 14371 O  O   . HOH EA 3 .   ? 64.889  -8.745  -14.812 1.00 26.38 ? 172  HOH G O   1 
HETATM 14372 O  O   . HOH EA 3 .   ? 69.440  3.311   -9.980  1.00 24.92 ? 173  HOH G O   1 
HETATM 14373 O  O   . HOH EA 3 .   ? 67.650  3.588   -11.591 1.00 27.73 ? 177  HOH G O   1 
HETATM 14374 O  O   . HOH EA 3 .   ? 49.579  1.450   4.080   1.00 27.19 ? 189  HOH G O   1 
HETATM 14375 O  O   . HOH EA 3 .   ? 76.167  -15.653 -2.633  1.00 34.64 ? 192  HOH G O   1 
HETATM 14376 O  O   . HOH EA 3 .   ? 45.435  4.049   -1.989  1.00 26.22 ? 193  HOH G O   1 
HETATM 14377 O  O   . HOH EA 3 .   ? 57.476  -1.056  -16.751 1.00 32.60 ? 197  HOH G O   1 
HETATM 14378 O  O   . HOH EA 3 .   ? 61.674  5.908   11.642  1.00 24.47 ? 205  HOH G O   1 
HETATM 14379 O  O   . HOH EA 3 .   ? 48.704  -13.135 -8.637  1.00 27.73 ? 224  HOH G O   1 
HETATM 14380 O  O   . HOH EA 3 .   ? 41.490  5.566   -8.482  1.00 25.72 ? 234  HOH G O   1 
HETATM 14381 O  O   . HOH EA 3 .   ? 69.588  -12.394 -10.757 1.00 24.17 ? 235  HOH G O   1 
HETATM 14382 O  O   . HOH EA 3 .   ? 40.646  -2.258  1.020   1.00 26.23 ? 240  HOH G O   1 
HETATM 14383 O  O   . HOH EA 3 .   ? 41.102  -4.436  -2.571  1.00 23.77 ? 251  HOH G O   1 
HETATM 14384 O  O   . HOH EA 3 .   ? 75.448  -17.961 -2.282  1.00 32.86 ? 265  HOH G O   1 
HETATM 14385 O  O   . HOH EA 3 .   ? 76.456  -3.242  3.856   1.00 23.32 ? 283  HOH G O   1 
HETATM 14386 O  O   . HOH EA 3 .   ? 72.734  -12.789 -7.849  1.00 29.61 ? 285  HOH G O   1 
HETATM 14387 O  O   . HOH EA 3 .   ? 61.931  -16.094 -2.667  1.00 25.00 ? 288  HOH G O   1 
HETATM 14388 O  O   . HOH EA 3 .   ? 57.914  1.241   -14.670 1.00 25.24 ? 306  HOH G O   1 
HETATM 14389 O  O   . HOH EA 3 .   ? 69.189  1.801   -20.757 1.00 27.44 ? 307  HOH G O   1 
HETATM 14390 O  O   . HOH EA 3 .   ? 51.261  -6.436  -10.764 1.00 22.24 ? 309  HOH G O   1 
HETATM 14391 O  O   . HOH EA 3 .   ? 67.297  -1.499  -18.764 1.00 22.59 ? 320  HOH G O   1 
HETATM 14392 O  O   . HOH EA 3 .   ? 48.049  -8.534  -2.429  1.00 26.06 ? 325  HOH G O   1 
HETATM 14393 O  O   . HOH EA 3 .   ? 79.339  -10.253 -0.090  1.00 29.28 ? 355  HOH G O   1 
HETATM 14394 O  O   . HOH EA 3 .   ? 59.464  -17.879 -12.266 1.00 38.15 ? 387  HOH G O   1 
HETATM 14395 O  O   . HOH EA 3 .   ? 48.209  -12.287 0.591   1.00 29.15 ? 415  HOH G O   1 
HETATM 14396 O  O   . HOH EA 3 .   ? 70.454  9.562   7.233   1.00 30.50 ? 423  HOH G O   1 
HETATM 14397 O  O   . HOH EA 3 .   ? 77.603  0.749   4.554   1.00 24.59 ? 430  HOH G O   1 
HETATM 14398 O  O   . HOH EA 3 .   ? 81.758  -9.561  -0.633  1.00 34.39 ? 437  HOH G O   1 
HETATM 14399 O  O   . HOH EA 3 .   ? 62.918  4.881   14.803  1.00 32.51 ? 454  HOH G O   1 
HETATM 14400 O  O   . HOH EA 3 .   ? 46.981  -7.175  -0.744  1.00 25.11 ? 457  HOH G O   1 
HETATM 14401 O  O   . HOH EA 3 .   ? 64.443  -13.797 -11.871 1.00 30.63 ? 458  HOH G O   1 
HETATM 14402 O  O   . HOH EA 3 .   ? 51.625  2.175   -12.679 1.00 34.41 ? 466  HOH G O   1 
HETATM 14403 O  O   . HOH EA 3 .   ? 54.255  -4.493  6.048   1.00 19.42 ? 476  HOH G O   1 
HETATM 14404 O  O   . HOH EA 3 .   ? 64.634  -17.168 -0.716  1.00 26.14 ? 503  HOH G O   1 
HETATM 14405 O  O   . HOH EA 3 .   ? 60.515  -4.407  10.350  1.00 26.79 ? 509  HOH G O   1 
HETATM 14406 O  O   . HOH EA 3 .   ? 59.387  -12.527 4.740   1.00 21.20 ? 541  HOH G O   1 
HETATM 14407 O  O   . HOH EA 3 .   ? 54.715  -14.413 -1.462  1.00 28.84 ? 544  HOH G O   1 
HETATM 14408 O  O   . HOH EA 3 .   ? 52.532  -5.794  4.908   1.00 26.04 ? 659  HOH G O   1 
HETATM 14409 O  O   . HOH EA 3 .   ? 71.942  9.751   -16.960 1.00 30.04 ? 708  HOH G O   1 
HETATM 14410 O  O   . HOH EA 3 .   ? 51.672  5.382   -7.975  1.00 23.03 ? 713  HOH G O   1 
HETATM 14411 O  O   . HOH EA 3 .   ? 56.160  0.270   -10.991 1.00 27.06 ? 720  HOH G O   1 
HETATM 14412 O  O   . HOH EA 3 .   ? 53.552  -12.814 6.959   1.00 32.95 ? 749  HOH G O   1 
HETATM 14413 O  O   . HOH EA 3 .   ? 75.879  -5.623  4.300   1.00 27.85 ? 754  HOH G O   1 
HETATM 14414 O  O   . HOH EA 3 .   ? 69.233  -17.160 8.563   1.00 30.19 ? 756  HOH G O   1 
HETATM 14415 O  O   . HOH EA 3 .   ? 73.217  3.440   -8.582  1.00 25.90 ? 757  HOH G O   1 
HETATM 14416 O  O   . HOH EA 3 .   ? 57.289  17.079  6.371   1.00 37.49 ? 781  HOH G O   1 
HETATM 14417 O  O   . HOH EA 3 .   ? 63.537  -12.050 -13.692 1.00 29.79 ? 795  HOH G O   1 
HETATM 14418 O  O   . HOH EA 3 .   ? 62.667  -15.756 -12.692 1.00 33.49 ? 799  HOH G O   1 
HETATM 14419 O  O   . HOH EA 3 .   ? 59.449  -8.556  5.272   1.00 21.90 ? 810  HOH G O   1 
HETATM 14420 O  O   . HOH EA 3 .   ? 46.454  -0.270  2.854   1.00 25.80 ? 811  HOH G O   1 
HETATM 14421 O  O   . HOH EA 3 .   ? 71.087  -14.404 -10.541 1.00 31.44 ? 816  HOH G O   1 
HETATM 14422 O  O   . HOH EA 3 .   ? 65.932  14.978  7.245   1.00 29.64 ? 832  HOH G O   1 
HETATM 14423 O  O   . HOH EA 3 .   ? 71.362  5.001   -9.124  1.00 27.72 ? 848  HOH G O   1 
HETATM 14424 O  O   . HOH EA 3 .   ? 74.887  4.248   -6.167  1.00 22.47 ? 861  HOH G O   1 
HETATM 14425 O  O   . HOH EA 3 .   ? 55.646  -6.253  -13.552 1.00 34.13 ? 871  HOH G O   1 
HETATM 14426 O  O   . HOH EA 3 .   ? 78.216  -18.672 4.081   1.00 34.97 ? 886  HOH G O   1 
HETATM 14427 O  O   . HOH EA 3 .   ? 56.906  18.777  4.544   1.00 36.88 ? 921  HOH G O   1 
HETATM 14428 O  O   . HOH EA 3 .   ? 77.986  8.849   -1.528  1.00 23.28 ? 940  HOH G O   1 
HETATM 14429 O  O   . HOH EA 3 .   ? 69.775  -3.287  12.899  1.00 39.01 ? 943  HOH G O   1 
HETATM 14430 O  O   . HOH EA 3 .   ? 69.373  13.075  -3.500  1.00 30.04 ? 947  HOH G O   1 
HETATM 14431 O  O   . HOH EA 3 .   ? 67.130  -11.077 -14.683 1.00 22.75 ? 962  HOH G O   1 
HETATM 14432 O  O   . HOH EA 3 .   ? 56.686  -14.658 -3.689  1.00 25.41 ? 971  HOH G O   1 
HETATM 14433 O  O   . HOH EA 3 .   ? 64.128  -17.377 3.012   1.00 25.83 ? 974  HOH G O   1 
HETATM 14434 O  O   . HOH EA 3 .   ? 48.466  -5.479  2.386   1.00 28.57 ? 980  HOH G O   1 
HETATM 14435 O  O   . HOH EA 3 .   ? 55.741  -5.490  -10.900 1.00 26.07 ? 987  HOH G O   1 
HETATM 14436 O  O   . HOH EA 3 .   ? 46.456  2.303   2.269   1.00 28.80 ? 991  HOH G O   1 
HETATM 14437 O  O   . HOH EA 3 .   ? 70.143  -0.327  -21.361 1.00 29.74 ? 1053 HOH G O   1 
HETATM 14438 O  O   . HOH EA 3 .   ? 65.417  10.738  -10.397 1.00 37.53 ? 1070 HOH G O   1 
HETATM 14439 O  O   . HOH EA 3 .   ? 52.500  0.462   6.321   1.00 31.39 ? 1079 HOH G O   1 
HETATM 14440 O  O   . HOH EA 3 .   ? 77.931  -14.008 -2.572  1.00 38.15 ? 1080 HOH G O   1 
HETATM 14441 O  O   . HOH EA 3 .   ? 57.754  -18.651 -4.383  1.00 34.71 ? 1093 HOH G O   1 
HETATM 14442 O  O   . HOH EA 3 .   ? 69.006  -21.729 1.563   1.00 36.62 ? 1097 HOH G O   1 
HETATM 14443 O  O   . HOH EA 3 .   ? 43.992  2.441   -11.319 1.00 22.46 ? 1109 HOH G O   1 
HETATM 14444 O  O   . HOH EA 3 .   ? 75.330  -13.657 -4.650  1.00 27.34 ? 1122 HOH G O   1 
HETATM 14445 O  O   . HOH EA 3 .   ? 69.477  -12.072 -13.815 1.00 26.49 ? 1143 HOH G O   1 
HETATM 14446 O  O   . HOH EA 3 .   ? 58.877  3.982   -17.750 1.00 39.26 ? 1173 HOH G O   1 
HETATM 14447 O  O   . HOH EA 3 .   ? 59.133  3.399   -15.154 1.00 26.33 ? 1185 HOH G O   1 
HETATM 14448 O  O   . HOH EA 3 .   ? 69.480  -14.668 9.464   1.00 39.72 ? 1200 HOH G O   1 
HETATM 14449 O  O   . HOH EA 3 .   ? 78.799  -18.276 6.403   1.00 41.55 ? 1215 HOH G O   1 
HETATM 14450 O  O   . HOH EA 3 .   ? 59.536  -8.424  10.761  1.00 35.37 ? 1223 HOH G O   1 
HETATM 14451 O  O   . HOH EA 3 .   ? 76.465  12.340  -3.554  1.00 38.44 ? 1225 HOH G O   1 
HETATM 14452 O  O   . HOH EA 3 .   ? 62.892  10.429  -10.519 1.00 35.65 ? 1231 HOH G O   1 
HETATM 14453 O  O   . HOH EA 3 .   ? 60.779  16.821  6.620   1.00 38.59 ? 1238 HOH G O   1 
HETATM 14454 O  O   . HOH EA 3 .   ? 45.612  -9.510  -4.181  1.00 33.39 ? 1240 HOH G O   1 
HETATM 14455 O  O   . HOH EA 3 .   ? 52.002  -14.183 5.302   1.00 34.58 ? 1254 HOH G O   1 
HETATM 14456 O  O   . HOH EA 3 .   ? 64.092  12.258  -7.530  1.00 33.42 ? 1258 HOH G O   1 
HETATM 14457 O  O   . HOH EA 3 .   ? 66.667  -6.617  11.220  1.00 33.93 ? 1265 HOH G O   1 
HETATM 14458 O  O   . HOH EA 3 .   ? 58.273  -16.649 -2.886  1.00 25.84 ? 1266 HOH G O   1 
HETATM 14459 O  O   . HOH EA 3 .   ? 48.766  -13.557 3.326   1.00 35.55 ? 1279 HOH G O   1 
HETATM 14460 O  O   . HOH EA 3 .   ? 71.718  -11.169 -14.807 1.00 29.46 ? 1288 HOH G O   1 
HETATM 14461 O  O   . HOH EA 3 .   ? 58.936  11.740  -5.796  1.00 30.54 ? 1337 HOH G O   1 
HETATM 14462 O  O   . HOH EA 3 .   ? 60.654  -16.974 -10.229 1.00 33.34 ? 1339 HOH G O   1 
HETATM 14463 O  O   . HOH EA 3 .   ? 48.881  -16.605 -7.731  1.00 40.05 ? 1346 HOH G O   1 
HETATM 14464 O  O   . HOH EA 3 .   ? 50.441  -18.851 -6.601  1.00 38.42 ? 1351 HOH G O   1 
HETATM 14465 O  O   . HOH EA 3 .   ? 44.654  -7.492  -4.730  1.00 35.34 ? 1361 HOH G O   1 
HETATM 14466 O  O   . HOH EA 3 .   ? 64.258  -16.944 -3.213  1.00 32.79 ? 1375 HOH G O   1 
HETATM 14467 O  O   . HOH EA 3 .   ? 72.225  12.046  -16.350 1.00 39.37 ? 1395 HOH G O   1 
HETATM 14468 O  O   . HOH EA 3 .   ? 80.266  -16.113 6.101   1.00 40.09 ? 1397 HOH G O   1 
HETATM 14469 O  O   . HOH EA 3 .   ? 68.343  -10.505 11.451  1.00 44.59 ? 1410 HOH G O   1 
HETATM 14470 O  O   . HOH EA 3 .   ? 44.374  4.923   -10.950 1.00 30.65 ? 1421 HOH G O   1 
HETATM 14471 O  O   . HOH EA 3 .   ? 60.624  -17.471 1.323   1.00 23.64 ? 1425 HOH G O   1 
HETATM 14472 O  O   . HOH EA 3 .   ? 71.507  13.863  -3.550  1.00 28.28 ? 1427 HOH G O   1 
HETATM 14473 O  O   . HOH EA 3 .   ? 48.378  3.201   7.607   1.00 30.69 ? 1438 HOH G O   1 
HETATM 14474 O  O   . HOH EA 3 .   ? 57.333  -7.741  -14.579 1.00 35.68 ? 1449 HOH G O   1 
HETATM 14475 O  O   . HOH EA 3 .   ? 58.945  13.595  18.054  1.00 48.19 ? 1479 HOH G O   1 
HETATM 14476 O  O   . HOH EA 3 .   ? 50.194  2.441   9.182   1.00 35.86 ? 1484 HOH G O   1 
HETATM 14477 O  O   . HOH EA 3 .   ? 64.067  10.959  -13.130 1.00 39.55 ? 1492 HOH G O   1 
HETATM 14478 O  O   . HOH EA 3 .   ? 69.226  15.556  2.728   1.00 37.73 ? 1499 HOH G O   1 
HETATM 14479 O  O   . HOH EA 3 .   ? 78.968  -20.948 7.036   1.00 34.32 ? 1505 HOH G O   1 
HETATM 14480 O  O   . HOH EA 3 .   ? 61.139  -10.757 -14.172 1.00 30.93 ? 1515 HOH G O   1 
HETATM 14481 O  O   . HOH EA 3 .   ? 58.587  -21.232 -2.796  1.00 28.16 ? 1520 HOH G O   1 
HETATM 14482 O  O   . HOH EA 3 .   ? 71.585  16.312  -0.524  1.00 38.66 ? 1524 HOH G O   1 
HETATM 14483 O  O   . HOH EA 3 .   ? 55.362  -13.367 2.444   1.00 26.34 ? 1526 HOH G O   1 
HETATM 14484 O  O   . HOH EA 3 .   ? 71.585  -10.499 -10.074 1.00 22.94 ? 1529 HOH G O   1 
HETATM 14485 O  O   . HOH EA 3 .   ? 59.291  12.252  14.545  1.00 40.02 ? 1531 HOH G O   1 
HETATM 14486 O  O   . HOH EA 3 .   ? 51.359  9.314   5.304   1.00 26.18 ? 1533 HOH G O   1 
HETATM 14487 O  O   . HOH EA 3 .   ? 72.770  -11.162 -12.154 1.00 26.61 ? 1534 HOH G O   1 
HETATM 14488 O  O   . HOH EA 3 .   ? 46.620  5.493   -0.451  1.00 30.81 ? 1538 HOH G O   1 
HETATM 14489 O  O   . HOH EA 3 .   ? 59.091  -17.382 -0.890  1.00 30.45 ? 1547 HOH G O   1 
HETATM 14490 O  O   . HOH EA 3 .   ? 57.200  -14.872 4.298   1.00 33.46 ? 1551 HOH G O   1 
HETATM 14491 O  O   . HOH EA 3 .   ? 47.151  4.676   1.793   1.00 26.67 ? 1590 HOH G O   1 
HETATM 14492 O  O   . HOH EA 3 .   ? 76.485  -20.993 7.696   1.00 46.69 ? 1596 HOH G O   1 
HETATM 14493 O  O   . HOH EA 3 .   ? 54.664  -3.495  -15.439 1.00 39.70 ? 1601 HOH G O   1 
HETATM 14494 O  O   . HOH EA 3 .   ? 64.520  -20.266 -0.227  1.00 34.52 ? 1602 HOH G O   1 
HETATM 14495 O  O   . HOH EA 3 .   ? 74.432  12.316  -1.964  1.00 36.22 ? 1603 HOH G O   1 
HETATM 14496 O  O   . HOH EA 3 .   ? 52.983  -5.275  -12.403 1.00 27.69 ? 1605 HOH G O   1 
HETATM 14497 O  O   . HOH EA 3 .   ? 53.645  0.104   -13.770 1.00 35.68 ? 1607 HOH G O   1 
HETATM 14498 O  O   . HOH EA 3 .   ? 67.928  -23.198 -3.011  1.00 39.45 ? 1609 HOH G O   1 
HETATM 14499 O  O   . HOH EA 3 .   ? 57.015  -10.424 -15.264 1.00 40.60 ? 1613 HOH G O   1 
HETATM 14500 O  O   . HOH EA 3 .   ? 70.906  16.264  -3.647  1.00 39.19 ? 1618 HOH G O   1 
HETATM 14501 O  O   . HOH EA 3 .   ? 72.470  14.009  -14.227 1.00 40.71 ? 1628 HOH G O   1 
HETATM 14502 O  O   . HOH EA 3 .   ? 73.265  10.108  -1.018  1.00 34.50 ? 1645 HOH G O   1 
HETATM 14503 O  O   . HOH EA 3 .   ? 53.526  -2.585  -13.158 1.00 30.89 ? 1659 HOH G O   1 
HETATM 14504 O  O   . HOH EA 3 .   ? 49.826  -6.007  5.888   1.00 31.07 ? 1664 HOH G O   1 
HETATM 14505 O  O   . HOH EA 3 .   ? 72.347  -2.528  13.611  1.00 45.70 ? 1665 HOH G O   1 
HETATM 14506 O  O   . HOH EA 3 .   ? 51.712  8.599   7.795   1.00 34.94 ? 1683 HOH G O   1 
HETATM 14507 O  O   . HOH EA 3 .   ? 45.980  2.244   -14.137 1.00 33.50 ? 1688 HOH G O   1 
HETATM 14508 O  O   . HOH EA 3 .   ? 75.096  -0.832  9.757   1.00 40.45 ? 1710 HOH G O   1 
HETATM 14509 O  O   . HOH EA 3 .   ? 74.709  2.077   7.336   1.00 31.67 ? 1728 HOH G O   1 
HETATM 14510 O  O   . HOH EA 3 .   ? 59.902  -12.686 7.649   1.00 31.40 ? 1732 HOH G O   1 
HETATM 14511 O  O   . HOH EA 3 .   ? 72.769  6.237   -6.233  1.00 30.13 ? 1739 HOH G O   1 
HETATM 14512 O  O   . HOH EA 3 .   ? 61.762  -12.904 9.108   1.00 32.50 ? 1744 HOH G O   1 
HETATM 14513 O  O   . HOH EA 3 .   ? 44.064  3.008   -18.105 1.00 41.44 ? 1746 HOH G O   1 
HETATM 14514 O  O   . HOH EA 3 .   ? 70.898  -3.990  15.291  1.00 51.20 ? 1758 HOH G O   1 
HETATM 14515 O  O   . HOH EA 3 .   ? 49.068  7.924   8.146   1.00 34.52 ? 1774 HOH G O   1 
HETATM 14516 O  O   . HOH EA 3 .   ? 48.207  5.696   7.448   1.00 36.32 ? 1775 HOH G O   1 
HETATM 14517 O  O   . HOH EA 3 .   ? 68.491  0.379   11.850  1.00 29.63 ? 1784 HOH G O   1 
HETATM 14518 O  O   . HOH EA 3 .   ? 74.735  -21.725 4.558   1.00 43.89 ? 1799 HOH G O   1 
HETATM 14519 O  O   . HOH EA 3 .   ? 44.099  1.311   -16.170 1.00 39.01 ? 1806 HOH G O   1 
HETATM 14520 O  O   . HOH FA 3 .   ? 74.763  2.508   -12.373 1.00 14.61 ? 154  HOH H O   1 
HETATM 14521 O  O   . HOH FA 3 .   ? 81.783  -2.908  0.967   1.00 21.27 ? 156  HOH H O   1 
HETATM 14522 O  O   . HOH FA 3 .   ? 96.641  -5.313  -23.541 1.00 25.39 ? 157  HOH H O   1 
HETATM 14523 O  O   . HOH FA 3 .   ? 84.639  13.574  -11.804 1.00 16.92 ? 158  HOH H O   1 
HETATM 14524 O  O   . HOH FA 3 .   ? 93.411  1.595   -11.599 1.00 18.23 ? 159  HOH H O   1 
HETATM 14525 O  O   . HOH FA 3 .   ? 97.755  4.760   -9.060  1.00 24.31 ? 160  HOH H O   1 
HETATM 14526 O  O   . HOH FA 3 .   ? 80.432  13.675  -12.135 1.00 18.55 ? 161  HOH H O   1 
HETATM 14527 O  O   . HOH FA 3 .   ? 87.185  17.871  -21.307 1.00 23.81 ? 162  HOH H O   1 
HETATM 14528 O  O   . HOH FA 3 .   ? 93.987  -3.043  -17.520 1.00 18.67 ? 163  HOH H O   1 
HETATM 14529 O  O   . HOH FA 3 .   ? 83.014  -14.448 -20.016 1.00 23.86 ? 164  HOH H O   1 
HETATM 14530 O  O   . HOH FA 3 .   ? 91.876  -12.226 -10.966 1.00 21.52 ? 165  HOH H O   1 
HETATM 14531 O  O   . HOH FA 3 .   ? 93.678  -3.057  -7.332  1.00 21.48 ? 166  HOH H O   1 
HETATM 14532 O  O   . HOH FA 3 .   ? 81.898  -16.479 -14.783 1.00 29.49 ? 167  HOH H O   1 
HETATM 14533 O  O   . HOH FA 3 .   ? 94.544  3.789   -9.104  1.00 26.22 ? 168  HOH H O   1 
HETATM 14534 O  O   . HOH FA 3 .   ? 80.748  17.364  -17.607 1.00 19.41 ? 169  HOH H O   1 
HETATM 14535 O  O   . HOH FA 3 .   ? 87.260  7.825   -28.288 1.00 24.59 ? 170  HOH H O   1 
HETATM 14536 O  O   . HOH FA 3 .   ? 90.615  -0.941  -23.520 1.00 19.66 ? 171  HOH H O   1 
HETATM 14537 O  O   . HOH FA 3 .   ? 80.408  3.322   -28.383 1.00 24.20 ? 172  HOH H O   1 
HETATM 14538 O  O   . HOH FA 3 .   ? 108.376 -2.747  -18.486 1.00 26.40 ? 173  HOH H O   1 
HETATM 14539 O  O   . HOH FA 3 .   ? 102.004 -6.284  -12.794 1.00 19.67 ? 174  HOH H O   1 
HETATM 14540 O  O   . HOH FA 3 .   ? 92.427  -13.100 -13.275 1.00 20.83 ? 175  HOH H O   1 
HETATM 14541 O  O   . HOH FA 3 .   ? 84.087  19.210  -8.557  1.00 18.42 ? 176  HOH H O   1 
HETATM 14542 O  O   . HOH FA 3 .   ? 97.251  -7.022  -7.590  1.00 18.68 ? 177  HOH H O   1 
HETATM 14543 O  O   . HOH FA 3 .   ? 90.363  8.224   -5.895  1.00 19.32 ? 178  HOH H O   1 
HETATM 14544 O  O   . HOH FA 3 .   ? 104.679 1.792   -5.696  1.00 22.98 ? 195  HOH H O   1 
HETATM 14545 O  O   . HOH FA 3 .   ? 103.764 3.831   -14.755 1.00 26.71 ? 209  HOH H O   1 
HETATM 14546 O  O   . HOH FA 3 .   ? 88.410  -2.340  -28.382 1.00 19.25 ? 215  HOH H O   1 
HETATM 14547 O  O   . HOH FA 3 .   ? 76.658  1.159   -3.532  1.00 17.66 ? 217  HOH H O   1 
HETATM 14548 O  O   . HOH FA 3 .   ? 73.179  -3.764  -22.907 1.00 29.14 ? 242  HOH H O   1 
HETATM 14549 O  O   . HOH FA 3 .   ? 76.810  -10.545 -9.317  1.00 24.32 ? 244  HOH H O   1 
HETATM 14550 O  O   . HOH FA 3 .   ? 96.026  10.751  -18.947 1.00 29.11 ? 253  HOH H O   1 
HETATM 14551 O  O   . HOH FA 3 .   ? 94.680  12.606  -20.102 1.00 23.10 ? 259  HOH H O   1 
HETATM 14552 O  O   . HOH FA 3 .   ? 73.145  -20.563 -26.837 1.00 32.20 ? 263  HOH H O   1 
HETATM 14553 O  O   . HOH FA 3 .   ? 88.418  -4.692  -27.691 1.00 27.63 ? 268  HOH H O   1 
HETATM 14554 O  O   . HOH FA 3 .   ? 100.126 6.610   -15.575 1.00 23.06 ? 295  HOH H O   1 
HETATM 14555 O  O   . HOH FA 3 .   ? 83.219  16.345  -22.651 1.00 23.50 ? 301  HOH H O   1 
HETATM 14556 O  O   . HOH FA 3 .   ? 92.839  -6.926  -6.524  1.00 23.68 ? 326  HOH H O   1 
HETATM 14557 O  O   . HOH FA 3 .   ? 75.935  6.221   -10.688 1.00 23.93 ? 337  HOH H O   1 
HETATM 14558 O  O   . HOH FA 3 .   ? 92.770  -0.389  -7.022  1.00 24.06 ? 346  HOH H O   1 
HETATM 14559 O  O   . HOH FA 3 .   ? 74.917  -19.866 -23.288 1.00 29.42 ? 350  HOH H O   1 
HETATM 14560 O  O   . HOH FA 3 .   ? 99.526  1.729   -21.546 1.00 22.03 ? 358  HOH H O   1 
HETATM 14561 O  O   . HOH FA 3 .   ? 82.084  3.156   -5.402  1.00 21.03 ? 371  HOH H O   1 
HETATM 14562 O  O   . HOH FA 3 .   ? 80.721  -12.597 -8.854  1.00 27.87 ? 379  HOH H O   1 
HETATM 14563 O  O   . HOH FA 3 .   ? 85.275  11.610  -8.618  1.00 24.01 ? 380  HOH H O   1 
HETATM 14564 O  O   . HOH FA 3 .   ? 78.559  -13.925 -25.580 1.00 22.10 ? 386  HOH H O   1 
HETATM 14565 O  O   . HOH FA 3 .   ? 79.727  5.913   -28.320 1.00 28.62 ? 396  HOH H O   1 
HETATM 14566 O  O   . HOH FA 3 .   ? 83.793  -10.077 -3.914  1.00 22.77 ? 398  HOH H O   1 
HETATM 14567 O  O   . HOH FA 3 .   ? 100.614 -8.576  -15.818 1.00 23.84 ? 410  HOH H O   1 
HETATM 14568 O  O   . HOH FA 3 .   ? 102.280 5.438   -16.747 1.00 19.96 ? 431  HOH H O   1 
HETATM 14569 O  O   . HOH FA 3 .   ? 102.199 2.517   -20.933 1.00 25.78 ? 432  HOH H O   1 
HETATM 14570 O  O   . HOH FA 3 .   ? 92.730  4.848   -6.740  1.00 29.23 ? 463  HOH H O   1 
HETATM 14571 O  O   . HOH FA 3 .   ? 79.874  2.157   -7.135  1.00 21.75 ? 478  HOH H O   1 
HETATM 14572 O  O   . HOH FA 3 .   ? 89.765  13.497  -16.780 1.00 15.83 ? 483  HOH H O   1 
HETATM 14573 O  O   . HOH FA 3 .   ? 107.223 -5.243  -17.906 1.00 29.27 ? 492  HOH H O   1 
HETATM 14574 O  O   . HOH FA 3 .   ? 75.165  3.425   -9.919  1.00 19.57 ? 493  HOH H O   1 
HETATM 14575 O  O   . HOH FA 3 .   ? 101.582 -6.904  -17.286 1.00 27.95 ? 494  HOH H O   1 
HETATM 14576 O  O   . HOH FA 3 .   ? 103.210 0.474   -20.154 1.00 21.89 ? 495  HOH H O   1 
HETATM 14577 O  O   . HOH FA 3 .   ? 105.937 -3.698  -13.207 1.00 22.61 ? 499  HOH H O   1 
HETATM 14578 O  O   . HOH FA 3 .   ? 101.528 4.822   -19.143 1.00 20.72 ? 500  HOH H O   1 
HETATM 14579 O  O   . HOH FA 3 .   ? 81.264  -11.746 -4.256  1.00 27.72 ? 506  HOH H O   1 
HETATM 14580 O  O   . HOH FA 3 .   ? 86.926  14.580  -11.760 1.00 18.54 ? 512  HOH H O   1 
HETATM 14581 O  O   . HOH FA 3 .   ? 73.999  7.543   -10.415 1.00 31.06 ? 514  HOH H O   1 
HETATM 14582 O  O   . HOH FA 3 .   ? 91.487  -2.638  -25.336 1.00 31.48 ? 521  HOH H O   1 
HETATM 14583 O  O   . HOH FA 3 .   ? 77.666  13.481  -11.793 1.00 23.68 ? 529  HOH H O   1 
HETATM 14584 O  O   . HOH FA 3 .   ? 87.046  -5.741  -30.488 1.00 35.92 ? 550  HOH H O   1 
HETATM 14585 O  O   . HOH FA 3 .   ? 97.297  10.036  -22.891 1.00 23.42 ? 566  HOH H O   1 
HETATM 14586 O  O   . HOH FA 3 .   ? 92.483  13.320  -15.903 1.00 23.10 ? 575  HOH H O   1 
HETATM 14587 O  O   . HOH FA 3 .   ? 104.635 4.403   -6.527  1.00 26.95 ? 587  HOH H O   1 
HETATM 14588 O  O   . HOH FA 3 .   ? 95.514  15.905  -21.620 1.00 32.08 ? 594  HOH H O   1 
HETATM 14589 O  O   . HOH FA 3 .   ? 91.510  17.959  -22.552 1.00 25.09 ? 606  HOH H O   1 
HETATM 14590 O  O   . HOH FA 3 .   ? 92.784  11.233  -27.665 1.00 21.90 ? 615  HOH H O   1 
HETATM 14591 O  O   . HOH FA 3 .   ? 79.870  16.049  -9.228  1.00 21.88 ? 619  HOH H O   1 
HETATM 14592 O  O   . HOH FA 3 .   ? 69.224  -8.723  -18.783 1.00 32.05 ? 622  HOH H O   1 
HETATM 14593 O  O   . HOH FA 3 .   ? 77.347  -20.979 -23.222 1.00 29.12 ? 624  HOH H O   1 
HETATM 14594 O  O   . HOH FA 3 .   ? 78.237  -12.795 -8.152  1.00 27.72 ? 626  HOH H O   1 
HETATM 14595 O  O   . HOH FA 3 .   ? 71.744  5.163   -23.100 1.00 33.58 ? 648  HOH H O   1 
HETATM 14596 O  O   . HOH FA 3 .   ? 88.104  -9.325  -6.218  1.00 23.72 ? 666  HOH H O   1 
HETATM 14597 O  O   . HOH FA 3 .   ? 76.301  -14.527 -10.087 1.00 29.35 ? 676  HOH H O   1 
HETATM 14598 O  O   . HOH FA 3 .   ? 71.235  2.499   -22.131 1.00 29.25 ? 684  HOH H O   1 
HETATM 14599 O  O   . HOH FA 3 .   ? 66.822  -1.303  -21.803 1.00 32.50 ? 689  HOH H O   1 
HETATM 14600 O  O   . HOH FA 3 .   ? 107.201 -7.222  -19.721 1.00 23.62 ? 698  HOH H O   1 
HETATM 14601 O  O   . HOH FA 3 .   ? 107.084 0.751   -5.182  1.00 27.89 ? 707  HOH H O   1 
HETATM 14602 O  O   . HOH FA 3 .   ? 99.390  8.994   -17.501 1.00 23.04 ? 717  HOH H O   1 
HETATM 14603 O  O   . HOH FA 3 .   ? 86.394  -11.678 -28.532 1.00 43.44 ? 721  HOH H O   1 
HETATM 14604 O  O   . HOH FA 3 .   ? 71.512  -9.148  -16.755 1.00 26.64 ? 729  HOH H O   1 
HETATM 14605 O  O   . HOH FA 3 .   ? 91.201  -11.476 -4.180  1.00 29.90 ? 742  HOH H O   1 
HETATM 14606 O  O   . HOH FA 3 .   ? 99.068  9.304   -21.317 1.00 28.34 ? 744  HOH H O   1 
HETATM 14607 O  O   . HOH FA 3 .   ? 83.122  9.689   -6.277  1.00 31.55 ? 748  HOH H O   1 
HETATM 14608 O  O   . HOH FA 3 .   ? 104.235 5.123   -9.321  1.00 26.15 ? 753  HOH H O   1 
HETATM 14609 O  O   . HOH FA 3 .   ? 106.936 -4.599  -10.969 1.00 21.45 ? 762  HOH H O   1 
HETATM 14610 O  O   . HOH FA 3 .   ? 101.382 0.897   -3.867  1.00 29.35 ? 780  HOH H O   1 
HETATM 14611 O  O   . HOH FA 3 .   ? 79.091  -20.778 -11.920 1.00 43.26 ? 788  HOH H O   1 
HETATM 14612 O  O   . HOH FA 3 .   ? 71.496  10.010  -14.121 1.00 32.09 ? 793  HOH H O   1 
HETATM 14613 O  O   . HOH FA 3 .   ? 78.260  6.628   -8.677  1.00 20.41 ? 794  HOH H O   1 
HETATM 14614 O  O   . HOH FA 3 .   ? 83.516  11.850  -29.485 1.00 35.86 ? 815  HOH H O   1 
HETATM 14615 O  O   . HOH FA 3 .   ? 78.257  4.147   -7.912  1.00 22.34 ? 842  HOH H O   1 
HETATM 14616 O  O   . HOH FA 3 .   ? 85.919  12.406  -28.962 1.00 30.45 ? 843  HOH H O   1 
HETATM 14617 O  O   . HOH FA 3 .   ? 78.652  12.437  -24.319 1.00 29.39 ? 846  HOH H O   1 
HETATM 14618 O  O   . HOH FA 3 .   ? 96.946  1.124   -23.712 1.00 29.19 ? 854  HOH H O   1 
HETATM 14619 O  O   . HOH FA 3 .   ? 104.453 7.772   -9.409  1.00 31.85 ? 866  HOH H O   1 
HETATM 14620 O  O   . HOH FA 3 .   ? 75.443  -12.105 -11.603 1.00 32.06 ? 877  HOH H O   1 
HETATM 14621 O  O   . HOH FA 3 .   ? 78.985  -12.728 -4.727  1.00 30.07 ? 879  HOH H O   1 
HETATM 14622 O  O   . HOH FA 3 .   ? 75.118  16.858  -17.874 1.00 30.43 ? 887  HOH H O   1 
HETATM 14623 O  O   . HOH FA 3 .   ? 80.807  16.898  -24.006 1.00 28.65 ? 890  HOH H O   1 
HETATM 14624 O  O   . HOH FA 3 .   ? 95.275  10.012  -27.435 1.00 26.98 ? 896  HOH H O   1 
HETATM 14625 O  O   . HOH FA 3 .   ? 81.094  19.155  -20.327 1.00 30.95 ? 905  HOH H O   1 
HETATM 14626 O  O   . HOH FA 3 .   ? 71.476  -2.972  -26.460 1.00 34.93 ? 907  HOH H O   1 
HETATM 14627 O  O   . HOH FA 3 .   ? 92.777  13.201  -29.653 1.00 30.08 ? 916  HOH H O   1 
HETATM 14628 O  O   . HOH FA 3 .   ? 84.877  -1.040  0.406   1.00 26.01 ? 937  HOH H O   1 
HETATM 14629 O  O   . HOH FA 3 .   ? 72.569  -1.654  -21.689 1.00 25.01 ? 939  HOH H O   1 
HETATM 14630 O  O   . HOH FA 3 .   ? 92.362  2.417   -7.937  1.00 23.18 ? 946  HOH H O   1 
HETATM 14631 O  O   . HOH FA 3 .   ? 74.113  4.146   -24.210 1.00 26.08 ? 956  HOH H O   1 
HETATM 14632 O  O   . HOH FA 3 .   ? 89.245  11.964  -8.067  1.00 28.17 ? 968  HOH H O   1 
HETATM 14633 O  O   . HOH FA 3 .   ? 75.676  -11.442 -7.069  1.00 31.04 ? 996  HOH H O   1 
HETATM 14634 O  O   . HOH FA 3 .   ? 84.435  -16.017 -22.960 1.00 29.48 ? 1003 HOH H O   1 
HETATM 14635 O  O   . HOH FA 3 .   ? 89.352  -6.983  -1.370  1.00 34.08 ? 1029 HOH H O   1 
HETATM 14636 O  O   . HOH FA 3 .   ? 84.216  18.333  -21.329 1.00 27.55 ? 1033 HOH H O   1 
HETATM 14637 O  O   . HOH FA 3 .   ? 93.040  0.211   -4.618  1.00 22.71 ? 1041 HOH H O   1 
HETATM 14638 O  O   . HOH FA 3 .   ? 89.945  1.866   -2.035  1.00 24.03 ? 1047 HOH H O   1 
HETATM 14639 O  O   . HOH FA 3 .   ? 71.726  -18.316 -25.458 1.00 39.67 ? 1064 HOH H O   1 
HETATM 14640 O  O   . HOH FA 3 .   ? 92.488  -16.652 -5.452  1.00 35.19 ? 1073 HOH H O   1 
HETATM 14641 O  O   . HOH FA 3 .   ? 103.414 -8.435  -12.721 1.00 29.89 ? 1075 HOH H O   1 
HETATM 14642 O  O   . HOH FA 3 .   ? 91.089  -0.297  -2.765  1.00 21.87 ? 1081 HOH H O   1 
HETATM 14643 O  O   . HOH FA 3 .   ? 80.284  8.761   -6.343  1.00 26.72 ? 1082 HOH H O   1 
HETATM 14644 O  O   . HOH FA 3 .   ? 89.794  -7.173  -23.932 1.00 29.45 ? 1085 HOH H O   1 
HETATM 14645 O  O   . HOH FA 3 .   ? 91.561  -14.233 -15.848 1.00 29.13 ? 1088 HOH H O   1 
HETATM 14646 O  O   . HOH FA 3 .   ? 99.362  -6.017  -22.778 1.00 30.93 ? 1096 HOH H O   1 
HETATM 14647 O  O   . HOH FA 3 .   ? 71.879  -16.287 -21.688 1.00 33.81 ? 1118 HOH H O   1 
HETATM 14648 O  O   . HOH FA 3 .   ? 101.634 7.436   -13.715 1.00 28.28 ? 1129 HOH H O   1 
HETATM 14649 O  O   . HOH FA 3 .   ? 87.817  14.208  -8.744  1.00 26.07 ? 1151 HOH H O   1 
HETATM 14650 O  O   . HOH FA 3 .   ? 70.308  -17.616 -23.417 1.00 43.25 ? 1157 HOH H O   1 
HETATM 14651 O  O   . HOH FA 3 .   ? 87.439  -9.121  -30.050 1.00 38.61 ? 1158 HOH H O   1 
HETATM 14652 O  O   . HOH FA 3 .   ? 73.146  0.764   -27.628 1.00 39.48 ? 1198 HOH H O   1 
HETATM 14653 O  O   . HOH FA 3 .   ? 69.517  11.268  -12.771 1.00 35.59 ? 1201 HOH H O   1 
HETATM 14654 O  O   . HOH FA 3 .   ? 94.852  -0.420  -23.199 1.00 29.35 ? 1213 HOH H O   1 
HETATM 14655 O  O   . HOH FA 3 .   ? 76.725  -2.814  -29.711 1.00 33.78 ? 1216 HOH H O   1 
HETATM 14656 O  O   . HOH FA 3 .   ? 93.166  18.879  -25.057 1.00 26.55 ? 1224 HOH H O   1 
HETATM 14657 O  O   . HOH FA 3 .   ? 74.708  10.486  -17.533 1.00 33.23 ? 1261 HOH H O   1 
HETATM 14658 O  O   . HOH FA 3 .   ? 66.955  12.083  -13.106 1.00 40.49 ? 1272 HOH H O   1 
HETATM 14659 O  O   . HOH FA 3 .   ? 82.822  -17.213 -28.892 1.00 36.02 ? 1299 HOH H O   1 
HETATM 14660 O  O   . HOH FA 3 .   ? 85.763  -17.140 -25.040 1.00 28.97 ? 1304 HOH H O   1 
HETATM 14661 O  O   . HOH FA 3 .   ? 75.964  10.911  -15.101 1.00 25.51 ? 1336 HOH H O   1 
HETATM 14662 O  O   . HOH FA 3 .   ? 90.480  -8.846  -3.960  1.00 30.02 ? 1345 HOH H O   1 
HETATM 14663 O  O   . HOH FA 3 .   ? 95.484  -13.794 -15.647 1.00 31.61 ? 1368 HOH H O   1 
HETATM 14664 O  O   . HOH FA 3 .   ? 94.079  18.293  -21.221 1.00 31.30 ? 1370 HOH H O   1 
HETATM 14665 O  O   . HOH FA 3 .   ? 106.051 -0.360  -19.679 1.00 26.27 ? 1372 HOH H O   1 
HETATM 14666 O  O   . HOH FA 3 .   ? 75.091  -14.719 -20.507 1.00 30.56 ? 1391 HOH H O   1 
HETATM 14667 O  O   . HOH FA 3 .   ? 93.217  -7.770  -30.456 1.00 36.66 ? 1393 HOH H O   1 
HETATM 14668 O  O   . HOH FA 3 .   ? 82.692  0.199   2.822   1.00 32.54 ? 1412 HOH H O   1 
HETATM 14669 O  O   . HOH FA 3 .   ? 66.946  -9.011  -17.059 1.00 34.37 ? 1426 HOH H O   1 
HETATM 14670 O  O   . HOH FA 3 .   ? 90.047  -5.178  -25.620 1.00 31.02 ? 1431 HOH H O   1 
HETATM 14671 O  O   . HOH FA 3 .   ? 83.130  19.111  -25.750 1.00 31.48 ? 1432 HOH H O   1 
HETATM 14672 O  O   . HOH FA 3 .   ? 94.021  -12.446 -28.527 1.00 42.28 ? 1437 HOH H O   1 
HETATM 14673 O  O   . HOH FA 3 .   ? 74.154  -3.158  -29.832 1.00 35.48 ? 1459 HOH H O   1 
HETATM 14674 O  O   . HOH FA 3 .   ? 89.111  9.369   -29.425 1.00 34.23 ? 1462 HOH H O   1 
HETATM 14675 O  O   . HOH FA 3 .   ? 87.293  -1.057  0.669   1.00 24.82 ? 1464 HOH H O   1 
HETATM 14676 O  O   . HOH FA 3 .   ? 102.498 -10.551 -20.934 1.00 40.44 ? 1503 HOH H O   1 
HETATM 14677 O  O   . HOH FA 3 .   ? 89.715  -10.945 -23.588 1.00 28.71 ? 1553 HOH H O   1 
HETATM 14678 O  O   . HOH FA 3 .   ? 75.324  6.935   -5.464  1.00 28.48 ? 1563 HOH H O   1 
HETATM 14679 O  O   . HOH FA 3 .   ? 78.880  19.413  -21.256 1.00 41.04 ? 1567 HOH H O   1 
HETATM 14680 O  O   . HOH FA 3 .   ? 87.972  0.716   4.133   1.00 31.17 ? 1568 HOH H O   1 
HETATM 14681 O  O   . HOH FA 3 .   ? 89.176  18.374  -23.575 1.00 33.06 ? 1579 HOH H O   1 
HETATM 14682 O  O   . HOH FA 3 .   ? 95.160  -1.529  -4.208  1.00 34.73 ? 1587 HOH H O   1 
HETATM 14683 O  O   . HOH FA 3 .   ? 87.388  1.752   1.558   1.00 30.96 ? 1593 HOH H O   1 
HETATM 14684 O  O   . HOH FA 3 .   ? 95.530  -12.523 -25.138 1.00 43.65 ? 1595 HOH H O   1 
HETATM 14685 O  O   . HOH FA 3 .   ? 104.720 -7.590  -15.690 1.00 35.61 ? 1619 HOH H O   1 
HETATM 14686 O  O   . HOH FA 3 .   ? 102.362 -14.245 -10.002 1.00 43.96 ? 1637 HOH H O   1 
HETATM 14687 O  O   . HOH FA 3 .   ? 101.798 -7.689  -23.832 1.00 44.31 ? 1642 HOH H O   1 
HETATM 14688 O  O   . HOH FA 3 .   ? 82.429  -11.963 -30.059 1.00 44.78 ? 1670 HOH H O   1 
HETATM 14689 O  O   . HOH FA 3 .   ? 97.041  10.335  -8.301  1.00 35.21 ? 1671 HOH H O   1 
HETATM 14690 O  O   . HOH FA 3 .   ? 78.102  -0.544  -30.159 1.00 36.51 ? 1680 HOH H O   1 
HETATM 14691 O  O   . HOH FA 3 .   ? 98.712  8.559   -9.417  1.00 31.27 ? 1681 HOH H O   1 
HETATM 14692 O  O   . HOH FA 3 .   ? 78.249  -11.423 -26.045 1.00 30.80 ? 1697 HOH H O   1 
HETATM 14693 O  O   . HOH FA 3 .   ? 103.551 9.021   -13.448 1.00 31.11 ? 1698 HOH H O   1 
HETATM 14694 O  O   . HOH FA 3 .   ? 81.281  -10.483 -32.884 1.00 35.48 ? 1745 HOH H O   1 
HETATM 14695 O  O   . HOH FA 3 .   ? 100.350 5.034   -25.268 1.00 30.85 ? 1752 HOH H O   1 
HETATM 14696 O  O   . HOH FA 3 .   ? 80.698  -0.700  -30.430 1.00 38.77 ? 1755 HOH H O   1 
HETATM 14697 O  O   . HOH FA 3 .   ? 106.780 -0.579  -2.454  1.00 37.90 ? 1756 HOH H O   1 
HETATM 14698 O  O   . HOH FA 3 .   ? 79.588  -0.871  3.581   1.00 32.53 ? 1757 HOH H O   1 
HETATM 14699 O  O   . HOH FA 3 .   ? 84.139  -11.687 -32.404 1.00 46.64 ? 1759 HOH H O   1 
HETATM 14700 O  O   . HOH FA 3 .   ? 96.132  15.704  -18.060 1.00 29.27 ? 1760 HOH H O   1 
HETATM 14701 O  O   . HOH FA 3 .   ? 91.592  -12.688 -23.190 1.00 37.66 ? 1787 HOH H O   1 
HETATM 14702 O  O   . HOH FA 3 .   ? 96.565  -17.432 -17.750 1.00 42.07 ? 1792 HOH H O   1 
HETATM 14703 O  O   . HOH FA 3 .   ? 96.300  12.874  -17.022 1.00 31.27 ? 1804 HOH H O   1 
HETATM 14704 O  O   . HOH FA 3 .   ? 98.699  2.948   -26.562 1.00 34.17 ? 1805 HOH H O   1 
HETATM 14705 O  O   . HOH GA 3 .   ? 39.108  -2.530  -1.959  1.00 23.87 ? 154  HOH I O   1 
HETATM 14706 O  O   . HOH GA 3 .   ? 21.300  1.258   -10.468 1.00 20.16 ? 156  HOH I O   1 
HETATM 14707 O  O   . HOH GA 3 .   ? 24.200  8.360   5.749   1.00 21.06 ? 157  HOH I O   1 
HETATM 14708 O  O   . HOH GA 3 .   ? 35.255  14.665  -9.280  1.00 25.97 ? 158  HOH I O   1 
HETATM 14709 O  O   . HOH GA 3 .   ? 14.584  0.692   -4.202  1.00 20.44 ? 159  HOH I O   1 
HETATM 14710 O  O   . HOH GA 3 .   ? 28.473  -12.488 5.651   1.00 25.45 ? 160  HOH I O   1 
HETATM 14711 O  O   . HOH GA 3 .   ? 27.973  -3.559  -16.756 1.00 23.37 ? 161  HOH I O   1 
HETATM 14712 O  O   . HOH GA 3 .   ? 28.230  -6.796  11.918  1.00 30.46 ? 162  HOH I O   1 
HETATM 14713 O  O   . HOH GA 3 .   ? 35.279  -3.664  3.794   1.00 21.27 ? 163  HOH I O   1 
HETATM 14714 O  O   . HOH GA 3 .   ? 24.461  12.083  -6.853  1.00 31.56 ? 164  HOH I O   1 
HETATM 14715 O  O   . HOH GA 3 .   ? 32.317  14.586  -2.020  1.00 20.51 ? 165  HOH I O   1 
HETATM 14716 O  O   . HOH GA 3 .   ? 41.930  1.220   6.087   1.00 22.97 ? 166  HOH I O   1 
HETATM 14717 O  O   . HOH GA 3 .   ? 34.592  6.262   17.919  1.00 30.11 ? 167  HOH I O   1 
HETATM 14718 O  O   . HOH GA 3 .   ? 25.787  -0.410  7.880   1.00 25.99 ? 199  HOH I O   1 
HETATM 14719 O  O   . HOH GA 3 .   ? 42.018  -3.882  -6.642  1.00 25.75 ? 201  HOH I O   1 
HETATM 14720 O  O   . HOH GA 3 .   ? 39.763  16.521  -1.153  1.00 29.40 ? 203  HOH I O   1 
HETATM 14721 O  O   . HOH GA 3 .   ? 39.589  3.118   -6.523  1.00 22.19 ? 229  HOH I O   1 
HETATM 14722 O  O   . HOH GA 3 .   ? 41.236  1.444   -12.091 1.00 26.13 ? 231  HOH I O   1 
HETATM 14723 O  O   . HOH GA 3 .   ? 29.054  -5.874  -16.882 1.00 29.84 ? 236  HOH I O   1 
HETATM 14724 O  O   . HOH GA 3 .   ? 14.328  8.388   -2.779  1.00 29.85 ? 248  HOH I O   1 
HETATM 14725 O  O   . HOH GA 3 .   ? 36.263  -18.127 -6.764  1.00 44.99 ? 255  HOH I O   1 
HETATM 14726 O  O   . HOH GA 3 .   ? 19.222  3.578   -5.315  1.00 25.38 ? 277  HOH I O   1 
HETATM 14727 O  O   . HOH GA 3 .   ? 26.770  -3.202  8.686   1.00 24.16 ? 287  HOH I O   1 
HETATM 14728 O  O   . HOH GA 3 .   ? 32.237  -15.806 -6.371  1.00 30.60 ? 305  HOH I O   1 
HETATM 14729 O  O   . HOH GA 3 .   ? 30.238  1.356   6.631   1.00 21.69 ? 322  HOH I O   1 
HETATM 14730 O  O   . HOH GA 3 .   ? 30.658  4.652   10.654  1.00 26.81 ? 344  HOH I O   1 
HETATM 14731 O  O   . HOH GA 3 .   ? 19.620  1.763   -3.707  1.00 22.70 ? 347  HOH I O   1 
HETATM 14732 O  O   . HOH GA 3 .   ? 33.472  12.647  -1.030  1.00 19.46 ? 348  HOH I O   1 
HETATM 14733 O  O   . HOH GA 3 .   ? 20.753  5.252   -8.723  1.00 24.40 ? 351  HOH I O   1 
HETATM 14734 O  O   . HOH GA 3 .   ? 37.383  -8.671  10.708  1.00 25.00 ? 354  HOH I O   1 
HETATM 14735 O  O   . HOH GA 3 .   ? 38.442  -9.151  -3.147  1.00 28.14 ? 366  HOH I O   1 
HETATM 14736 O  O   . HOH GA 3 .   ? 19.784  2.653   -8.445  1.00 25.98 ? 368  HOH I O   1 
HETATM 14737 O  O   . HOH GA 3 .   ? 19.442  -11.673 -6.465  1.00 23.76 ? 373  HOH I O   1 
HETATM 14738 O  O   . HOH GA 3 .   ? 42.524  8.799   2.550   1.00 30.88 ? 384  HOH I O   1 
HETATM 14739 O  O   . HOH GA 3 .   ? 27.079  13.022  -2.359  1.00 29.66 ? 388  HOH I O   1 
HETATM 14740 O  O   . HOH GA 3 .   ? 39.893  17.858  -8.661  1.00 29.86 ? 399  HOH I O   1 
HETATM 14741 O  O   . HOH GA 3 .   ? 42.166  -13.530 7.450   1.00 36.64 ? 405  HOH I O   1 
HETATM 14742 O  O   . HOH GA 3 .   ? 21.007  -15.556 6.400   1.00 37.35 ? 433  HOH I O   1 
HETATM 14743 O  O   . HOH GA 3 .   ? 22.761  -8.909  5.616   1.00 31.84 ? 460  HOH I O   1 
HETATM 14744 O  O   . HOH GA 3 .   ? 37.760  -13.976 2.650   1.00 30.42 ? 479  HOH I O   1 
HETATM 14745 O  O   . HOH GA 3 .   ? 19.063  2.690   -0.810  1.00 21.87 ? 513  HOH I O   1 
HETATM 14746 O  O   . HOH GA 3 .   ? 44.115  -1.403  14.935  1.00 24.71 ? 520  HOH I O   1 
HETATM 14747 O  O   . HOH GA 3 .   ? 31.253  2.149   18.694  1.00 27.05 ? 542  HOH I O   1 
HETATM 14748 O  O   . HOH GA 3 .   ? 45.485  3.435   5.008   1.00 25.72 ? 557  HOH I O   1 
HETATM 14749 O  O   . HOH GA 3 .   ? 40.317  20.836  -8.004  1.00 28.44 ? 580  HOH I O   1 
HETATM 14750 O  O   . HOH GA 3 .   ? 43.902  -3.869  15.058  1.00 25.04 ? 585  HOH I O   1 
HETATM 14751 O  O   . HOH GA 3 .   ? 40.656  -14.957 2.568   1.00 36.01 ? 599  HOH I O   1 
HETATM 14752 O  O   . HOH GA 3 .   ? 18.188  -10.279 2.254   1.00 31.72 ? 603  HOH I O   1 
HETATM 14753 O  O   . HOH GA 3 .   ? 33.874  12.483  1.782   1.00 27.55 ? 612  HOH I O   1 
HETATM 14754 O  O   . HOH GA 3 .   ? 21.260  -11.581 4.569   1.00 31.35 ? 621  HOH I O   1 
HETATM 14755 O  O   . HOH GA 3 .   ? 26.496  -17.619 -3.842  1.00 41.60 ? 637  HOH I O   1 
HETATM 14756 O  O   . HOH GA 3 .   ? 30.746  -17.179 -4.217  1.00 37.66 ? 641  HOH I O   1 
HETATM 14757 O  O   . HOH GA 3 .   ? 21.078  -12.908 -2.050  1.00 30.22 ? 646  HOH I O   1 
HETATM 14758 O  O   . HOH GA 3 .   ? 28.135  -16.509 -14.006 1.00 41.10 ? 649  HOH I O   1 
HETATM 14759 O  O   . HOH GA 3 .   ? 45.387  5.957   4.856   1.00 29.67 ? 656  HOH I O   1 
HETATM 14760 O  O   . HOH GA 3 .   ? 15.211  -1.162  4.998   1.00 33.24 ? 668  HOH I O   1 
HETATM 14761 O  O   . HOH GA 3 .   ? 20.079  6.081   -5.716  1.00 28.11 ? 688  HOH I O   1 
HETATM 14762 O  O   . HOH GA 3 .   ? 38.473  -12.098 -3.059  1.00 29.13 ? 692  HOH I O   1 
HETATM 14763 O  O   . HOH GA 3 .   ? 27.152  -16.419 -11.788 1.00 38.04 ? 694  HOH I O   1 
HETATM 14764 O  O   . HOH GA 3 .   ? 30.875  -13.701 5.170   1.00 28.09 ? 710  HOH I O   1 
HETATM 14765 O  O   . HOH GA 3 .   ? 37.660  18.503  -1.444  1.00 29.68 ? 741  HOH I O   1 
HETATM 14766 O  O   . HOH GA 3 .   ? 35.811  -6.549  -19.067 1.00 31.55 ? 743  HOH I O   1 
HETATM 14767 O  O   . HOH GA 3 .   ? 17.313  -12.430 0.893   1.00 35.90 ? 759  HOH I O   1 
HETATM 14768 O  O   . HOH GA 3 .   ? 22.201  -11.092 8.704   1.00 31.95 ? 770  HOH I O   1 
HETATM 14769 O  O   . HOH GA 3 .   ? 37.666  16.710  -11.927 1.00 30.79 ? 790  HOH I O   1 
HETATM 14770 O  O   . HOH GA 3 .   ? 38.845  9.454   2.905   1.00 22.43 ? 844  HOH I O   1 
HETATM 14771 O  O   . HOH GA 3 .   ? 34.130  6.979   15.602  1.00 33.91 ? 875  HOH I O   1 
HETATM 14772 O  O   . HOH GA 3 .   ? 34.794  -19.483 -4.895  1.00 42.35 ? 889  HOH I O   1 
HETATM 14773 O  O   . HOH GA 3 .   ? 20.211  2.139   7.658   1.00 28.63 ? 898  HOH I O   1 
HETATM 14774 O  O   . HOH GA 3 .   ? 34.841  -12.691 -13.813 1.00 30.59 ? 934  HOH I O   1 
HETATM 14775 O  O   . HOH GA 3 .   ? 41.229  -6.286  3.053   1.00 26.80 ? 935  HOH I O   1 
HETATM 14776 O  O   . HOH GA 3 .   ? 26.831  1.970   7.207   1.00 26.45 ? 941  HOH I O   1 
HETATM 14777 O  O   . HOH GA 3 .   ? 25.999  4.355   7.413   1.00 27.89 ? 960  HOH I O   1 
HETATM 14778 O  O   . HOH GA 3 .   ? 35.632  17.729  -2.438  1.00 28.92 ? 967  HOH I O   1 
HETATM 14779 O  O   . HOH GA 3 .   ? 21.900  0.043   8.840   1.00 32.28 ? 976  HOH I O   1 
HETATM 14780 O  O   . HOH GA 3 .   ? 20.315  -13.348 -8.540  1.00 30.64 ? 984  HOH I O   1 
HETATM 14781 O  O   . HOH GA 3 .   ? 22.244  -8.518  8.258   1.00 29.90 ? 995  HOH I O   1 
HETATM 14782 O  O   . HOH GA 3 .   ? 42.365  -0.195  2.536   1.00 25.97 ? 1010 HOH I O   1 
HETATM 14783 O  O   . HOH GA 3 .   ? 32.224  6.636   11.844  1.00 28.46 ? 1014 HOH I O   1 
HETATM 14784 O  O   . HOH GA 3 .   ? 29.178  -18.334 -6.933  1.00 45.42 ? 1042 HOH I O   1 
HETATM 14785 O  O   . HOH GA 3 .   ? 23.552  -10.506 -17.973 1.00 32.93 ? 1049 HOH I O   1 
HETATM 14786 O  O   . HOH GA 3 .   ? 21.693  8.834   2.019   1.00 33.63 ? 1056 HOH I O   1 
HETATM 14787 O  O   . HOH GA 3 .   ? 41.584  -4.986  0.661   1.00 31.03 ? 1072 HOH I O   1 
HETATM 14788 O  O   . HOH GA 3 .   ? 27.838  9.532   -13.447 1.00 35.55 ? 1078 HOH I O   1 
HETATM 14789 O  O   . HOH GA 3 .   ? 45.004  9.836   -3.779  1.00 33.04 ? 1089 HOH I O   1 
HETATM 14790 O  O   . HOH GA 3 .   ? 20.868  -13.097 7.921   1.00 42.48 ? 1094 HOH I O   1 
HETATM 14791 O  O   . HOH GA 3 .   ? 41.047  14.870  0.798   1.00 27.20 ? 1102 HOH I O   1 
HETATM 14792 O  O   . HOH GA 3 .   ? 18.744  -13.305 -3.809  1.00 27.65 ? 1108 HOH I O   1 
HETATM 14793 O  O   . HOH GA 3 .   ? 27.445  0.955   16.124  1.00 30.41 ? 1123 HOH I O   1 
HETATM 14794 O  O   . HOH GA 3 .   ? 37.941  -7.429  14.460  1.00 30.59 ? 1125 HOH I O   1 
HETATM 14795 O  O   . HOH GA 3 .   ? 19.914  7.938   -3.250  1.00 34.71 ? 1130 HOH I O   1 
HETATM 14796 O  O   . HOH GA 3 .   ? 17.725  2.580   9.202   1.00 32.69 ? 1131 HOH I O   1 
HETATM 14797 O  O   . HOH GA 3 .   ? 42.647  7.411   -10.324 1.00 32.88 ? 1133 HOH I O   1 
HETATM 14798 O  O   . HOH GA 3 .   ? 38.371  1.181   -13.856 1.00 27.35 ? 1146 HOH I O   1 
HETATM 14799 O  O   . HOH GA 3 .   ? 19.353  -6.549  8.354   1.00 38.12 ? 1156 HOH I O   1 
HETATM 14800 O  O   . HOH GA 3 .   ? 34.618  15.006  -11.786 1.00 32.89 ? 1159 HOH I O   1 
HETATM 14801 O  O   . HOH GA 3 .   ? 23.687  -16.672 9.310   1.00 33.46 ? 1162 HOH I O   1 
HETATM 14802 O  O   . HOH GA 3 .   ? 37.412  6.090   9.272   1.00 26.66 ? 1165 HOH I O   1 
HETATM 14803 O  O   . HOH GA 3 .   ? 22.698  6.721   5.715   1.00 24.76 ? 1192 HOH I O   1 
HETATM 14804 O  O   . HOH GA 3 .   ? 21.926  -14.293 -11.669 1.00 29.94 ? 1197 HOH I O   1 
HETATM 14805 O  O   . HOH GA 3 .   ? 18.667  10.102  -3.041  1.00 35.04 ? 1203 HOH I O   1 
HETATM 14806 O  O   . HOH GA 3 .   ? 19.388  8.908   3.341   1.00 37.56 ? 1207 HOH I O   1 
HETATM 14807 O  O   . HOH GA 3 .   ? 19.956  -13.414 3.143   1.00 36.48 ? 1209 HOH I O   1 
HETATM 14808 O  O   . HOH GA 3 .   ? 40.784  9.419   -13.218 1.00 33.45 ? 1217 HOH I O   1 
HETATM 14809 O  O   . HOH GA 3 .   ? 30.965  8.017   -14.008 1.00 32.33 ? 1221 HOH I O   1 
HETATM 14810 O  O   . HOH GA 3 .   ? 18.519  -10.622 6.564   1.00 35.05 ? 1237 HOH I O   1 
HETATM 14811 O  O   . HOH GA 3 .   ? 40.979  -6.685  -6.010  1.00 23.57 ? 1255 HOH I O   1 
HETATM 14812 O  O   . HOH GA 3 .   ? 19.768  -12.435 -10.873 1.00 32.61 ? 1259 HOH I O   1 
HETATM 14813 O  O   . HOH GA 3 .   ? 16.776  -0.769  6.973   1.00 35.67 ? 1277 HOH I O   1 
HETATM 14814 O  O   . HOH GA 3 .   ? 41.252  8.139   5.750   1.00 33.29 ? 1300 HOH I O   1 
HETATM 14815 O  O   . HOH GA 3 .   ? 38.211  -3.366  -16.822 1.00 38.86 ? 1311 HOH I O   1 
HETATM 14816 O  O   . HOH GA 3 .   ? 26.900  -18.402 10.144  1.00 32.97 ? 1333 HOH I O   1 
HETATM 14817 O  O   . HOH GA 3 .   ? 21.756  15.408  -5.572  1.00 33.97 ? 1344 HOH I O   1 
HETATM 14818 O  O   . HOH GA 3 .   ? 43.135  -7.442  -2.588  1.00 34.10 ? 1347 HOH I O   1 
HETATM 14819 O  O   . HOH GA 3 .   ? 40.218  -6.650  -3.608  1.00 27.27 ? 1354 HOH I O   1 
HETATM 14820 O  O   . HOH GA 3 .   ? 20.244  -1.588  9.857   1.00 34.05 ? 1363 HOH I O   1 
HETATM 14821 O  O   . HOH GA 3 .   ? 41.980  10.166  -9.856  1.00 34.61 ? 1366 HOH I O   1 
HETATM 14822 O  O   . HOH GA 3 .   ? 42.951  2.410   9.408   1.00 27.31 ? 1374 HOH I O   1 
HETATM 14823 O  O   . HOH GA 3 .   ? 34.226  -19.606 10.870  1.00 36.24 ? 1378 HOH I O   1 
HETATM 14824 O  O   . HOH GA 3 .   ? 22.979  16.901  -7.203  1.00 40.28 ? 1419 HOH I O   1 
HETATM 14825 O  O   . HOH GA 3 .   ? 29.226  3.531   7.831   1.00 31.21 ? 1430 HOH I O   1 
HETATM 14826 O  O   . HOH GA 3 .   ? 38.194  -0.709  -17.100 1.00 36.59 ? 1435 HOH I O   1 
HETATM 14827 O  O   . HOH GA 3 .   ? 21.574  -14.684 1.478   1.00 36.77 ? 1447 HOH I O   1 
HETATM 14828 O  O   . HOH GA 3 .   ? 42.721  -0.337  9.273   1.00 29.66 ? 1450 HOH I O   1 
HETATM 14829 O  O   . HOH GA 3 .   ? 31.673  2.260   -17.080 1.00 33.38 ? 1452 HOH I O   1 
HETATM 14830 O  O   . HOH GA 3 .   ? 38.346  -13.791 0.193   1.00 34.10 ? 1454 HOH I O   1 
HETATM 14831 O  O   . HOH GA 3 .   ? 23.061  14.563  2.996   1.00 39.80 ? 1468 HOH I O   1 
HETATM 14832 O  O   . HOH GA 3 .   ? 18.580  5.210   10.687  1.00 46.64 ? 1488 HOH I O   1 
HETATM 14833 O  O   . HOH GA 3 .   ? 27.960  -16.219 13.345  1.00 39.56 ? 1489 HOH I O   1 
HETATM 14834 O  O   . HOH GA 3 .   ? 19.554  -10.654 9.455   1.00 39.58 ? 1491 HOH I O   1 
HETATM 14835 O  O   . HOH GA 3 .   ? 35.072  16.767  -7.610  1.00 31.09 ? 1512 HOH I O   1 
HETATM 14836 O  O   . HOH GA 3 .   ? 38.760  3.851   12.808  1.00 29.28 ? 1548 HOH I O   1 
HETATM 14837 O  O   . HOH GA 3 .   ? 18.020  1.963   11.779  1.00 44.85 ? 1554 HOH I O   1 
HETATM 14838 O  O   . HOH GA 3 .   ? 24.991  16.076  3.679   1.00 32.64 ? 1557 HOH I O   1 
HETATM 14839 O  O   . HOH GA 3 .   ? 46.337  11.287  -6.815  1.00 40.22 ? 1572 HOH I O   1 
HETATM 14840 O  O   . HOH GA 3 .   ? 11.561  8.333   -2.373  1.00 32.33 ? 1600 HOH I O   1 
HETATM 14841 O  O   . HOH GA 3 .   ? 29.300  10.402  9.806   1.00 29.75 ? 1610 HOH I O   1 
HETATM 14842 O  O   . HOH GA 3 .   ? 40.894  -5.980  8.475   1.00 31.60 ? 1611 HOH I O   1 
HETATM 14843 O  O   . HOH GA 3 .   ? 39.285  5.193   10.994  1.00 30.87 ? 1629 HOH I O   1 
HETATM 14844 O  O   . HOH GA 3 .   ? 43.789  0.015   4.601   1.00 35.12 ? 1640 HOH I O   1 
HETATM 14845 O  O   . HOH GA 3 .   ? 45.497  12.181  -9.359  1.00 34.20 ? 1647 HOH I O   1 
HETATM 14846 O  O   . HOH GA 3 .   ? 43.039  -6.614  4.696   1.00 31.83 ? 1656 HOH I O   1 
HETATM 14847 O  O   . HOH GA 3 .   ? 29.703  -15.710 15.259  1.00 44.19 ? 1685 HOH I O   1 
HETATM 14848 O  O   . HOH GA 3 .   ? 38.885  11.693  2.044   1.00 26.52 ? 1687 HOH I O   1 
HETATM 14849 O  O   . HOH GA 3 .   ? 9.203   0.760   3.627   1.00 38.90 ? 1694 HOH I O   1 
HETATM 14850 O  O   . HOH GA 3 .   ? 10.122  -0.377  1.738   1.00 28.19 ? 1704 HOH I O   1 
HETATM 14851 O  O   . HOH GA 3 .   ? 21.416  9.621   -0.364  1.00 41.05 ? 1737 HOH I O   1 
HETATM 14852 O  O   . HOH GA 3 .   ? 29.408  9.600   -15.200 1.00 43.05 ? 1742 HOH I O   1 
HETATM 14853 O  O   . HOH GA 3 .   ? 9.384   -2.680  1.734   1.00 33.98 ? 1743 HOH I O   1 
HETATM 14854 O  O   . HOH GA 3 .   ? 21.540  12.253  -12.325 1.00 39.32 ? 1747 HOH I O   1 
HETATM 14855 O  O   . HOH GA 3 .   ? 25.567  15.949  1.018   1.00 35.82 ? 1748 HOH I O   1 
HETATM 14856 O  O   . HOH GA 3 .   ? 18.907  11.958  2.437   1.00 42.42 ? 1749 HOH I O   1 
HETATM 14857 O  O   . HOH GA 3 .   ? 39.598  -1.884  -15.085 1.00 37.65 ? 1768 HOH I O   1 
HETATM 14858 O  O   . HOH GA 3 .   ? 19.211  -0.241  11.616  1.00 48.67 ? 1786 HOH I O   1 
HETATM 14859 O  O   . HOH GA 3 .   ? 35.927  -22.875 -15.982 1.00 55.89 ? 1788 HOH I O   1 
HETATM 14860 O  O   . HOH GA 3 .   ? 26.525  13.786  -15.020 1.00 42.80 ? 1797 HOH I O   1 
HETATM 14861 O  O   . HOH HA 3 .   ? -3.095  -2.835  -15.216 1.00 18.26 ? 154  HOH J O   1 
HETATM 14862 O  O   . HOH HA 3 .   ? 0.829   -4.536  -21.178 1.00 23.56 ? 156  HOH J O   1 
HETATM 14863 O  O   . HOH HA 3 .   ? 14.615  1.172   -6.987  1.00 17.99 ? 157  HOH J O   1 
HETATM 14864 O  O   . HOH HA 3 .   ? 9.156   12.468  -15.060 1.00 23.75 ? 158  HOH J O   1 
HETATM 14865 O  O   . HOH HA 3 .   ? 14.964  -13.318 -14.292 1.00 30.13 ? 159  HOH J O   1 
HETATM 14866 O  O   . HOH HA 3 .   ? 4.969   3.538   -28.248 1.00 22.44 ? 160  HOH J O   1 
HETATM 14867 O  O   . HOH HA 3 .   ? 7.813   -13.383 -22.229 1.00 33.37 ? 161  HOH J O   1 
HETATM 14868 O  O   . HOH HA 3 .   ? -3.545  2.658   -11.078 1.00 18.26 ? 162  HOH J O   1 
HETATM 14869 O  O   . HOH HA 3 .   ? -5.572  5.945   -8.870  1.00 24.22 ? 163  HOH J O   1 
HETATM 14870 O  O   . HOH HA 3 .   ? 13.668  -2.940  2.845   1.00 27.07 ? 164  HOH J O   1 
HETATM 14871 O  O   . HOH HA 3 .   ? 15.827  6.081   -11.796 1.00 26.15 ? 183  HOH J O   1 
HETATM 14872 O  O   . HOH HA 3 .   ? 9.004   -4.023  -26.078 1.00 28.50 ? 186  HOH J O   1 
HETATM 14873 O  O   . HOH HA 3 .   ? 1.369   -12.739 -2.686  1.00 35.84 ? 211  HOH J O   1 
HETATM 14874 O  O   . HOH HA 3 .   ? 2.321   12.261  -17.101 1.00 19.23 ? 223  HOH J O   1 
HETATM 14875 O  O   . HOH HA 3 .   ? 11.680  7.471   -23.494 1.00 22.62 ? 250  HOH J O   1 
HETATM 14876 O  O   . HOH HA 3 .   ? 9.839   -1.616  -25.443 1.00 24.05 ? 276  HOH J O   1 
HETATM 14877 O  O   . HOH HA 3 .   ? 16.902  2.313   -16.469 1.00 25.25 ? 298  HOH J O   1 
HETATM 14878 O  O   . HOH HA 3 .   ? 6.554   -5.887  -0.180  1.00 32.30 ? 314  HOH J O   1 
HETATM 14879 O  O   . HOH HA 3 .   ? -2.886  8.060   -23.793 1.00 22.97 ? 316  HOH J O   1 
HETATM 14880 O  O   . HOH HA 3 .   ? -6.656  16.527  -15.176 1.00 21.82 ? 321  HOH J O   1 
HETATM 14881 O  O   . HOH HA 3 .   ? 4.333   -15.928 -10.096 1.00 36.10 ? 336  HOH J O   1 
HETATM 14882 O  O   . HOH HA 3 .   ? 17.798  -10.684 -19.544 1.00 29.49 ? 343  HOH J O   1 
HETATM 14883 O  O   . HOH HA 3 .   ? 7.297   -8.061  -28.817 1.00 34.21 ? 356  HOH J O   1 
HETATM 14884 O  O   . HOH HA 3 .   ? 4.154   13.970  -16.252 1.00 20.34 ? 357  HOH J O   1 
HETATM 14885 O  O   . HOH HA 3 .   ? 0.807   -10.704 -0.915  1.00 40.83 ? 359  HOH J O   1 
HETATM 14886 O  O   . HOH HA 3 .   ? 19.824  6.014   -11.045 1.00 31.53 ? 369  HOH J O   1 
HETATM 14887 O  O   . HOH HA 3 .   ? 6.905   2.245   -25.127 1.00 25.41 ? 383  HOH J O   1 
HETATM 14888 O  O   . HOH HA 3 .   ? -1.802  1.096   -3.305  1.00 23.83 ? 385  HOH J O   1 
HETATM 14889 O  O   . HOH HA 3 .   ? 2.172   11.890  -20.240 1.00 22.01 ? 389  HOH J O   1 
HETATM 14890 O  O   . HOH HA 3 .   ? 3.552   -15.829 -20.259 1.00 34.90 ? 407  HOH J O   1 
HETATM 14891 O  O   . HOH HA 3 .   ? -6.044  0.230   -22.867 1.00 27.24 ? 419  HOH J O   1 
HETATM 14892 O  O   . HOH HA 3 .   ? -6.462  7.648   -20.158 1.00 28.05 ? 439  HOH J O   1 
HETATM 14893 O  O   . HOH HA 3 .   ? 8.228   -16.930 -2.742  1.00 44.56 ? 446  HOH J O   1 
HETATM 14894 O  O   . HOH HA 3 .   ? -7.130  -1.892  -25.508 1.00 29.88 ? 461  HOH J O   1 
HETATM 14895 O  O   . HOH HA 3 .   ? -1.752  4.749   -26.561 1.00 27.34 ? 464  HOH J O   1 
HETATM 14896 O  O   . HOH HA 3 .   ? 9.856   10.837  -21.216 1.00 28.52 ? 468  HOH J O   1 
HETATM 14897 O  O   . HOH HA 3 .   ? 21.659  0.694   -12.789 1.00 22.83 ? 484  HOH J O   1 
HETATM 14898 O  O   . HOH HA 3 .   ? 5.273   -14.279 -21.807 1.00 36.60 ? 489  HOH J O   1 
HETATM 14899 O  O   . HOH HA 3 .   ? 16.410  1.749   -14.185 1.00 23.01 ? 518  HOH J O   1 
HETATM 14900 O  O   . HOH HA 3 .   ? 22.496  -3.089  -19.893 1.00 27.86 ? 538  HOH J O   1 
HETATM 14901 O  O   . HOH HA 3 .   ? -7.716  0.056   -32.661 1.00 35.32 ? 551  HOH J O   1 
HETATM 14902 O  O   . HOH HA 3 .   ? 17.092  -11.719 -10.734 1.00 23.02 ? 553  HOH J O   1 
HETATM 14903 O  O   . HOH HA 3 .   ? 9.357   0.798   -24.691 1.00 27.14 ? 563  HOH J O   1 
HETATM 14904 O  O   . HOH HA 3 .   ? 14.050  -0.753  -25.966 1.00 26.43 ? 568  HOH J O   1 
HETATM 14905 O  O   . HOH HA 3 .   ? 7.106   13.471  -17.134 1.00 30.19 ? 570  HOH J O   1 
HETATM 14906 O  O   . HOH HA 3 .   ? 7.433   3.590   1.478   1.00 28.61 ? 581  HOH J O   1 
HETATM 14907 O  O   . HOH HA 3 .   ? 16.860  2.575   -9.387  1.00 23.55 ? 596  HOH J O   1 
HETATM 14908 O  O   . HOH HA 3 .   ? -5.032  -6.875  -11.143 1.00 24.25 ? 607  HOH J O   1 
HETATM 14909 O  O   . HOH HA 3 .   ? 7.871   1.058   0.913   1.00 32.10 ? 616  HOH J O   1 
HETATM 14910 O  O   . HOH HA 3 .   ? 17.198  -7.459  -25.156 1.00 31.03 ? 660  HOH J O   1 
HETATM 14911 O  O   . HOH HA 3 .   ? 17.010  3.308   -12.176 1.00 24.86 ? 663  HOH J O   1 
HETATM 14912 O  O   . HOH HA 3 .   ? 11.706  -0.613  -26.532 1.00 30.67 ? 664  HOH J O   1 
HETATM 14913 O  O   . HOH HA 3 .   ? -1.089  -10.196 -27.422 1.00 32.55 ? 669  HOH J O   1 
HETATM 14914 O  O   . HOH HA 3 .   ? -4.310  -7.163  -13.900 1.00 30.15 ? 690  HOH J O   1 
HETATM 14915 O  O   . HOH HA 3 .   ? 21.247  8.013   -15.353 1.00 32.73 ? 693  HOH J O   1 
HETATM 14916 O  O   . HOH HA 3 .   ? 5.752   0.525   -23.798 1.00 23.81 ? 695  HOH J O   1 
HETATM 14917 O  O   . HOH HA 3 .   ? -4.734  -4.662  -14.599 1.00 27.84 ? 723  HOH J O   1 
HETATM 14918 O  O   . HOH HA 3 .   ? -1.572  3.639   -2.974  1.00 27.12 ? 726  HOH J O   1 
HETATM 14919 O  O   . HOH HA 3 .   ? 11.268  -2.048  -29.123 1.00 34.87 ? 766  HOH J O   1 
HETATM 14920 O  O   . HOH HA 3 .   ? 5.112   8.757   -4.170  1.00 27.36 ? 778  HOH J O   1 
HETATM 14921 O  O   . HOH HA 3 .   ? 2.672   9.619   -4.582  1.00 25.29 ? 809  HOH J O   1 
HETATM 14922 O  O   . HOH HA 3 .   ? 15.044  1.385   -25.406 1.00 28.96 ? 827  HOH J O   1 
HETATM 14923 O  O   . HOH HA 3 .   ? 11.310  12.144  -11.004 1.00 23.22 ? 840  HOH J O   1 
HETATM 14924 O  O   . HOH HA 3 .   ? 20.787  -2.041  -22.049 1.00 27.02 ? 852  HOH J O   1 
HETATM 14925 O  O   . HOH HA 3 .   ? -5.597  10.279  -4.280  1.00 41.30 ? 872  HOH J O   1 
HETATM 14926 O  O   . HOH HA 3 .   ? -2.513  -9.130  -13.795 1.00 28.60 ? 873  HOH J O   1 
HETATM 14927 O  O   . HOH HA 3 .   ? 10.589  -4.745  -28.758 1.00 38.67 ? 888  HOH J O   1 
HETATM 14928 O  O   . HOH HA 3 .   ? 5.558   -17.345 -14.362 1.00 45.72 ? 895  HOH J O   1 
HETATM 14929 O  O   . HOH HA 3 .   ? 14.822  -9.954  1.560   1.00 36.56 ? 904  HOH J O   1 
HETATM 14930 O  O   . HOH HA 3 .   ? 10.684  -20.433 -11.524 1.00 48.79 ? 909  HOH J O   1 
HETATM 14931 O  O   . HOH HA 3 .   ? 16.503  3.503   -7.232  1.00 23.29 ? 959  HOH J O   1 
HETATM 14932 O  O   . HOH HA 3 .   ? 10.758  13.083  -18.694 1.00 33.67 ? 986  HOH J O   1 
HETATM 14933 O  O   . HOH HA 3 .   ? -8.007  13.238  -7.585  1.00 33.32 ? 1039 HOH J O   1 
HETATM 14934 O  O   . HOH HA 3 .   ? 3.692   3.542   -1.732  1.00 28.58 ? 1045 HOH J O   1 
HETATM 14935 O  O   . HOH HA 3 .   ? 9.877   8.709   -5.011  1.00 30.54 ? 1048 HOH J O   1 
HETATM 14936 O  O   . HOH HA 3 .   ? 12.161  10.996  -17.697 1.00 28.95 ? 1058 HOH J O   1 
HETATM 14937 O  O   . HOH HA 3 .   ? -3.286  -2.896  -2.156  1.00 31.02 ? 1113 HOH J O   1 
HETATM 14938 O  O   . HOH HA 3 .   ? 4.624   2.289   0.041   1.00 29.17 ? 1120 HOH J O   1 
HETATM 14939 O  O   . HOH HA 3 .   ? 0.023   -7.250  -0.055  1.00 35.70 ? 1136 HOH J O   1 
HETATM 14940 O  O   . HOH HA 3 .   ? 15.824  -12.380 -4.342  1.00 34.08 ? 1149 HOH J O   1 
HETATM 14941 O  O   . HOH HA 3 .   ? 11.604  9.181   -6.666  1.00 32.16 ? 1150 HOH J O   1 
HETATM 14942 O  O   . HOH HA 3 .   ? -1.935  17.612  -7.081  1.00 28.90 ? 1163 HOH J O   1 
HETATM 14943 O  O   . HOH HA 3 .   ? 12.284  -10.301 1.383   1.00 34.92 ? 1176 HOH J O   1 
HETATM 14944 O  O   . HOH HA 3 .   ? 13.539  7.254   -21.752 1.00 32.21 ? 1230 HOH J O   1 
HETATM 14945 O  O   . HOH HA 3 .   ? 7.254   16.497  -5.938  1.00 42.07 ? 1249 HOH J O   1 
HETATM 14946 O  O   . HOH HA 3 .   ? 17.545  -13.492 -12.970 1.00 30.97 ? 1251 HOH J O   1 
HETATM 14947 O  O   . HOH HA 3 .   ? 14.466  -14.290 -4.666  1.00 35.53 ? 1252 HOH J O   1 
HETATM 14948 O  O   . HOH HA 3 .   ? 14.490  -17.082 -22.039 1.00 39.82 ? 1284 HOH J O   1 
HETATM 14949 O  O   . HOH HA 3 .   ? 19.439  -2.046  -24.934 1.00 36.59 ? 1287 HOH J O   1 
HETATM 14950 O  O   . HOH HA 3 .   ? 0.179   -5.213  1.750   1.00 35.55 ? 1290 HOH J O   1 
HETATM 14951 O  O   . HOH HA 3 .   ? 3.114   5.011   -30.759 1.00 34.53 ? 1301 HOH J O   1 
HETATM 14952 O  O   . HOH HA 3 .   ? 15.296  9.084   -17.373 1.00 31.58 ? 1305 HOH J O   1 
HETATM 14953 O  O   . HOH HA 3 .   ? -2.012  15.456  -3.802  1.00 40.28 ? 1313 HOH J O   1 
HETATM 14954 O  O   . HOH HA 3 .   ? -9.667  11.537  -9.467  1.00 25.94 ? 1329 HOH J O   1 
HETATM 14955 O  O   . HOH HA 3 .   ? 13.426  -10.752 -1.676  1.00 34.50 ? 1338 HOH J O   1 
HETATM 14956 O  O   . HOH HA 3 .   ? 21.832  10.508  -15.285 1.00 46.97 ? 1369 HOH J O   1 
HETATM 14957 O  O   . HOH HA 3 .   ? 8.438   -16.322 4.469   1.00 44.80 ? 1379 HOH J O   1 
HETATM 14958 O  O   . HOH HA 3 .   ? -6.293  15.966  -4.169  1.00 39.01 ? 1439 HOH J O   1 
HETATM 14959 O  O   . HOH HA 3 .   ? -2.464  -3.366  0.476   1.00 26.63 ? 1441 HOH J O   1 
HETATM 14960 O  O   . HOH HA 3 .   ? -6.893  -8.203  -9.758  1.00 34.70 ? 1453 HOH J O   1 
HETATM 14961 O  O   . HOH HA 3 .   ? 16.330  8.001   -14.905 1.00 38.46 ? 1469 HOH J O   1 
HETATM 14962 O  O   . HOH HA 3 .   ? -1.764  -14.355 -18.587 1.00 35.71 ? 1471 HOH J O   1 
HETATM 14963 O  O   . HOH HA 3 .   ? 6.042   -0.587  2.972   1.00 36.38 ? 1473 HOH J O   1 
HETATM 14964 O  O   . HOH HA 3 .   ? 6.410   -3.202  2.727   1.00 35.05 ? 1477 HOH J O   1 
HETATM 14965 O  O   . HOH HA 3 .   ? 16.524  8.697   -12.420 1.00 29.12 ? 1483 HOH J O   1 
HETATM 14966 O  O   . HOH HA 3 .   ? 16.226  11.256  -11.705 1.00 29.52 ? 1504 HOH J O   1 
HETATM 14967 O  O   . HOH HA 3 .   ? 13.501  -9.499  -22.991 1.00 32.02 ? 1581 HOH J O   1 
HETATM 14968 O  O   . HOH HA 3 .   ? 9.687   13.252  -21.535 1.00 41.35 ? 1584 HOH J O   1 
HETATM 14969 O  O   . HOH HA 3 .   ? -2.291  -0.830  0.615   1.00 32.48 ? 1586 HOH J O   1 
HETATM 14970 O  O   . HOH HA 3 .   ? 18.435  10.481  -15.045 1.00 40.52 ? 1588 HOH J O   1 
HETATM 14971 O  O   . HOH HA 3 .   ? 25.694  -0.817  -19.059 1.00 29.92 ? 1589 HOH J O   1 
HETATM 14972 O  O   . HOH HA 3 .   ? -10.961 15.919  -14.520 1.00 40.96 ? 1597 HOH J O   1 
HETATM 14973 O  O   . HOH HA 3 .   ? -4.457  -18.823 -6.526  1.00 55.44 ? 1620 HOH J O   1 
HETATM 14974 O  O   . HOH HA 3 .   ? 18.953  -12.768 -16.952 1.00 36.19 ? 1621 HOH J O   1 
HETATM 14975 O  O   . HOH HA 3 .   ? -6.276  -12.706 -25.274 1.00 37.43 ? 1622 HOH J O   1 
HETATM 14976 O  O   . HOH HA 3 .   ? 24.634  3.038   -21.383 1.00 31.87 ? 1623 HOH J O   1 
HETATM 14977 O  O   . HOH HA 3 .   ? 16.676  7.931   -21.438 1.00 34.02 ? 1627 HOH J O   1 
HETATM 14978 O  O   . HOH HA 3 .   ? -3.792  -13.463 -26.408 1.00 39.38 ? 1649 HOH J O   1 
HETATM 14979 O  O   . HOH HA 3 .   ? 8.147   -3.468  -0.321  1.00 29.71 ? 1651 HOH J O   1 
HETATM 14980 O  O   . HOH HA 3 .   ? 1.742   -5.449  3.668   1.00 43.74 ? 1652 HOH J O   1 
HETATM 14981 O  O   . HOH HA 3 .   ? 5.329   7.408   -1.454  1.00 38.96 ? 1653 HOH J O   1 
HETATM 14982 O  O   . HOH HA 3 .   ? -4.706  -6.902  -4.121  1.00 42.75 ? 1666 HOH J O   1 
HETATM 14983 O  O   . HOH HA 3 .   ? 3.153   -0.815  1.618   1.00 36.02 ? 1669 HOH J O   1 
HETATM 14984 O  O   . HOH HA 3 .   ? 4.279   -17.856 -16.611 1.00 48.26 ? 1684 HOH J O   1 
HETATM 14985 O  O   . HOH HA 3 .   ? 10.815  18.423  -12.265 1.00 30.15 ? 1690 HOH J O   1 
HETATM 14986 O  O   . HOH HA 3 .   ? 13.097  16.948  -12.196 1.00 34.49 ? 1693 HOH J O   1 
HETATM 14987 O  O   . HOH HA 3 .   ? 7.541   9.726   -3.963  1.00 32.35 ? 1701 HOH J O   1 
HETATM 14988 O  O   . HOH HA 3 .   ? 13.811  3.953   -25.631 1.00 22.70 ? 1703 HOH J O   1 
HETATM 14989 O  O   . HOH HA 3 .   ? -5.668  10.285  -7.200  1.00 31.33 ? 1706 HOH J O   1 
HETATM 14990 O  O   . HOH HA 3 .   ? 9.790   3.412   -25.197 1.00 25.20 ? 1719 HOH J O   1 
HETATM 14991 O  O   . HOH HA 3 .   ? -2.815  9.310   -20.289 1.00 22.35 ? 1722 HOH J O   1 
HETATM 14992 O  O   . HOH HA 3 .   ? 4.555   -4.970  2.286   1.00 41.18 ? 1726 HOH J O   1 
HETATM 14993 O  O   . HOH HA 3 .   ? -2.897  -17.562 -3.783  1.00 48.84 ? 1735 HOH J O   1 
HETATM 14994 O  O   . HOH HA 3 .   ? 27.067  0.222   -21.867 1.00 43.24 ? 1761 HOH J O   1 
HETATM 14995 O  O   . HOH HA 3 .   ? 1.346   -1.470  3.738   1.00 44.69 ? 1778 HOH J O   1 
HETATM 14996 O  O   . HOH HA 3 .   ? 16.031  -8.384  7.602   1.00 38.13 ? 1781 HOH J O   1 
HETATM 14997 O  O   . HOH HA 3 .   ? -4.219  18.047  -5.861  1.00 34.97 ? 1794 HOH J O   1 
HETATM 14998 O  O   . HOH IA 3 .   ? 37.724  3.203   19.621  1.00 24.27 ? 154  HOH K O   1 
HETATM 14999 O  O   . HOH IA 3 .   ? 48.233  -9.492  38.258  1.00 27.86 ? 156  HOH K O   1 
HETATM 15000 O  O   . HOH IA 3 .   ? 57.117  4.887   19.004  1.00 31.70 ? 157  HOH K O   1 
HETATM 15001 O  O   . HOH IA 3 .   ? 52.397  -12.827 22.838  1.00 33.85 ? 158  HOH K O   1 
HETATM 15002 O  O   . HOH IA 3 .   ? 54.192  -11.485 24.910  1.00 31.65 ? 160  HOH K O   1 
HETATM 15003 O  O   . HOH IA 3 .   ? 57.745  -4.138  7.365   1.00 19.98 ? 178  HOH K O   1 
HETATM 15004 O  O   . HOH IA 3 .   ? 63.805  2.437   14.943  1.00 25.99 ? 185  HOH K O   1 
HETATM 15005 O  O   . HOH IA 3 .   ? 48.835  -3.437  18.928  1.00 25.69 ? 191  HOH K O   1 
HETATM 15006 O  O   . HOH IA 3 .   ? 47.571  0.826   11.617  1.00 29.35 ? 206  HOH K O   1 
HETATM 15007 O  O   . HOH IA 3 .   ? 46.634  -15.653 31.806  1.00 35.41 ? 261  HOH K O   1 
HETATM 15008 O  O   . HOH IA 3 .   ? 56.513  9.353   26.332  1.00 39.02 ? 279  HOH K O   1 
HETATM 15009 O  O   . HOH IA 3 .   ? 44.989  -6.293  14.187  1.00 23.40 ? 281  HOH K O   1 
HETATM 15010 O  O   . HOH IA 3 .   ? 46.287  9.902   15.412  1.00 35.84 ? 282  HOH K O   1 
HETATM 15011 O  O   . HOH IA 3 .   ? 43.234  3.519   37.216  1.00 31.54 ? 286  HOH K O   1 
HETATM 15012 O  O   . HOH IA 3 .   ? 53.612  1.938   21.838  1.00 24.39 ? 299  HOH K O   1 
HETATM 15013 O  O   . HOH IA 3 .   ? 50.210  3.977   35.669  1.00 33.98 ? 303  HOH K O   1 
HETATM 15014 O  O   . HOH IA 3 .   ? 59.330  0.842   36.138  1.00 38.15 ? 315  HOH K O   1 
HETATM 15015 O  O   . HOH IA 3 .   ? 64.799  0.289   19.700  1.00 47.02 ? 339  HOH K O   1 
HETATM 15016 O  O   . HOH IA 3 .   ? 51.758  3.297   40.449  1.00 32.34 ? 349  HOH K O   1 
HETATM 15017 O  O   . HOH IA 3 .   ? 52.648  6.150   14.009  1.00 28.49 ? 353  HOH K O   1 
HETATM 15018 O  O   . HOH IA 3 .   ? 29.714  -5.045  27.985  1.00 39.97 ? 367  HOH K O   1 
HETATM 15019 O  O   . HOH IA 3 .   ? 45.366  -16.741 25.245  1.00 38.69 ? 414  HOH K O   1 
HETATM 15020 O  O   . HOH IA 3 .   ? 46.706  -7.148  12.305  1.00 32.52 ? 451  HOH K O   1 
HETATM 15021 O  O   . HOH IA 3 .   ? 54.635  -1.911  5.750   1.00 22.41 ? 477  HOH K O   1 
HETATM 15022 O  O   . HOH IA 3 .   ? 50.735  -10.914 34.675  1.00 28.21 ? 485  HOH K O   1 
HETATM 15023 O  O   . HOH IA 3 .   ? 41.998  -2.166  18.571  1.00 27.27 ? 486  HOH K O   1 
HETATM 15024 O  O   . HOH IA 3 .   ? 48.165  7.785   36.227  1.00 37.91 ? 497  HOH K O   1 
HETATM 15025 O  O   . HOH IA 3 .   ? 40.865  -4.293  17.220  1.00 24.89 ? 504  HOH K O   1 
HETATM 15026 O  O   . HOH IA 3 .   ? 37.318  15.222  23.656  1.00 31.62 ? 547  HOH K O   1 
HETATM 15027 O  O   . HOH IA 3 .   ? 36.855  -4.008  18.406  1.00 27.45 ? 564  HOH K O   1 
HETATM 15028 O  O   . HOH IA 3 .   ? 59.217  -6.309  20.997  1.00 32.10 ? 574  HOH K O   1 
HETATM 15029 O  O   . HOH IA 3 .   ? 37.599  -6.392  19.044  1.00 25.26 ? 589  HOH K O   1 
HETATM 15030 O  O   . HOH IA 3 .   ? 59.212  2.077   41.771  1.00 34.41 ? 595  HOH K O   1 
HETATM 15031 O  O   . HOH IA 3 .   ? 58.147  -3.529  9.695   1.00 26.53 ? 623  HOH K O   1 
HETATM 15032 O  O   . HOH IA 3 .   ? 58.416  -6.526  7.077   1.00 24.05 ? 627  HOH K O   1 
HETATM 15033 O  O   . HOH IA 3 .   ? 36.922  -20.674 29.954  1.00 44.48 ? 628  HOH K O   1 
HETATM 15034 O  O   . HOH IA 3 .   ? 47.970  13.133  19.523  1.00 32.72 ? 631  HOH K O   1 
HETATM 15035 O  O   . HOH IA 3 .   ? 39.767  -14.581 35.078  1.00 35.41 ? 647  HOH K O   1 
HETATM 15036 O  O   . HOH IA 3 .   ? 45.940  1.928   7.731   1.00 30.38 ? 650  HOH K O   1 
HETATM 15037 O  O   . HOH IA 3 .   ? 45.922  4.596   38.304  1.00 38.40 ? 653  HOH K O   1 
HETATM 15038 O  O   . HOH IA 3 .   ? 57.091  7.692   28.409  1.00 41.55 ? 654  HOH K O   1 
HETATM 15039 O  O   . HOH IA 3 .   ? 49.509  -0.300  10.104  1.00 32.15 ? 662  HOH K O   1 
HETATM 15040 O  O   . HOH IA 3 .   ? 46.151  -13.726 17.600  1.00 34.10 ? 681  HOH K O   1 
HETATM 15041 O  O   . HOH IA 3 .   ? 45.621  13.218  20.865  1.00 32.57 ? 700  HOH K O   1 
HETATM 15042 O  O   . HOH IA 3 .   ? 55.963  2.093   24.573  1.00 28.99 ? 716  HOH K O   1 
HETATM 15043 O  O   . HOH IA 3 .   ? 54.901  3.453   11.244  1.00 24.13 ? 732  HOH K O   1 
HETATM 15044 O  O   . HOH IA 3 .   ? 45.019  -0.381  11.855  1.00 30.92 ? 736  HOH K O   1 
HETATM 15045 O  O   . HOH IA 3 .   ? 61.198  -4.371  31.340  1.00 33.89 ? 783  HOH K O   1 
HETATM 15046 O  O   . HOH IA 3 .   ? 31.522  4.527   17.972  1.00 34.25 ? 785  HOH K O   1 
HETATM 15047 O  O   . HOH IA 3 .   ? 34.407  -1.938  35.268  1.00 32.11 ? 786  HOH K O   1 
HETATM 15048 O  O   . HOH IA 3 .   ? 56.854  -6.989  11.692  1.00 29.27 ? 798  HOH K O   1 
HETATM 15049 O  O   . HOH IA 3 .   ? 52.531  4.470   34.803  1.00 34.92 ? 802  HOH K O   1 
HETATM 15050 O  O   . HOH IA 3 .   ? 28.806  -4.818  30.157  1.00 38.43 ? 807  HOH K O   1 
HETATM 15051 O  O   . HOH IA 3 .   ? 50.199  -14.449 22.898  1.00 36.44 ? 826  HOH K O   1 
HETATM 15052 O  O   . HOH IA 3 .   ? 36.530  -8.613  40.590  1.00 36.13 ? 834  HOH K O   1 
HETATM 15053 O  O   . HOH IA 3 .   ? 57.173  0.323   25.200  1.00 29.55 ? 845  HOH K O   1 
HETATM 15054 O  O   . HOH IA 3 .   ? 48.695  5.291   37.546  1.00 38.42 ? 857  HOH K O   1 
HETATM 15055 O  O   . HOH IA 3 .   ? 57.483  -5.437  25.450  1.00 31.79 ? 865  HOH K O   1 
HETATM 15056 O  O   . HOH IA 3 .   ? 56.213  4.414   24.597  1.00 32.67 ? 867  HOH K O   1 
HETATM 15057 O  O   . HOH IA 3 .   ? 40.889  17.031  20.723  1.00 32.04 ? 882  HOH K O   1 
HETATM 15058 O  O   . HOH IA 3 .   ? 45.399  4.227   8.235   1.00 32.22 ? 900  HOH K O   1 
HETATM 15059 O  O   . HOH IA 3 .   ? 56.598  -7.880  29.764  1.00 27.24 ? 910  HOH K O   1 
HETATM 15060 O  O   . HOH IA 3 .   ? 53.547  5.289   11.768  1.00 27.44 ? 918  HOH K O   1 
HETATM 15061 O  O   . HOH IA 3 .   ? 46.914  14.033  28.028  1.00 40.30 ? 969  HOH K O   1 
HETATM 15062 O  O   . HOH IA 3 .   ? 55.545  -7.072  9.530   1.00 33.30 ? 1000 HOH K O   1 
HETATM 15063 O  O   . HOH IA 3 .   ? 55.191  4.522   21.950  1.00 28.79 ? 1006 HOH K O   1 
HETATM 15064 O  O   . HOH IA 3 .   ? 62.975  -14.656 26.686  1.00 32.94 ? 1020 HOH K O   1 
HETATM 15065 O  O   . HOH IA 3 .   ? 38.993  17.062  27.665  1.00 39.55 ? 1046 HOH K O   1 
HETATM 15066 O  O   . HOH IA 3 .   ? 47.738  -14.841 26.219  1.00 33.12 ? 1061 HOH K O   1 
HETATM 15067 O  O   . HOH IA 3 .   ? 56.554  6.841   24.652  1.00 37.81 ? 1068 HOH K O   1 
HETATM 15068 O  O   . HOH IA 3 .   ? 61.618  -9.716  25.994  1.00 44.11 ? 1100 HOH K O   1 
HETATM 15069 O  O   . HOH IA 3 .   ? 61.603  -1.510  31.267  1.00 35.46 ? 1104 HOH K O   1 
HETATM 15070 O  O   . HOH IA 3 .   ? 37.968  17.786  15.650  1.00 39.73 ? 1148 HOH K O   1 
HETATM 15071 O  O   . HOH IA 3 .   ? 56.422  -7.892  35.708  1.00 33.71 ? 1160 HOH K O   1 
HETATM 15072 O  O   . HOH IA 3 .   ? 40.375  -6.569  17.910  1.00 34.74 ? 1168 HOH K O   1 
HETATM 15073 O  O   . HOH IA 3 .   ? 50.175  13.255  29.514  1.00 40.82 ? 1190 HOH K O   1 
HETATM 15074 O  O   . HOH IA 3 .   ? 54.399  -16.383 16.898  1.00 39.10 ? 1193 HOH K O   1 
HETATM 15075 O  O   . HOH IA 3 .   ? 55.434  -9.971  36.355  1.00 27.26 ? 1233 HOH K O   1 
HETATM 15076 O  O   . HOH IA 3 .   ? 43.161  -17.176 32.024  1.00 44.52 ? 1243 HOH K O   1 
HETATM 15077 O  O   . HOH IA 3 .   ? 59.822  -8.780  28.441  1.00 35.86 ? 1253 HOH K O   1 
HETATM 15078 O  O   . HOH IA 3 .   ? 32.965  1.627   36.106  1.00 33.92 ? 1267 HOH K O   1 
HETATM 15079 O  O   . HOH IA 3 .   ? 32.258  3.699   32.329  1.00 33.79 ? 1270 HOH K O   1 
HETATM 15080 O  O   . HOH IA 3 .   ? 42.987  17.975  20.026  1.00 32.31 ? 1274 HOH K O   1 
HETATM 15081 O  O   . HOH IA 3 .   ? 40.582  16.659  17.054  1.00 35.83 ? 1317 HOH K O   1 
HETATM 15082 O  O   . HOH IA 3 .   ? 44.902  6.857   37.037  1.00 34.20 ? 1341 HOH K O   1 
HETATM 15083 O  O   . HOH IA 3 .   ? 59.718  1.568   28.239  1.00 28.39 ? 1349 HOH K O   1 
HETATM 15084 O  O   . HOH IA 3 .   ? 34.116  16.945  29.384  1.00 37.30 ? 1373 HOH K O   1 
HETATM 15085 O  O   . HOH IA 3 .   ? 41.508  -8.567  20.050  1.00 33.02 ? 1408 HOH K O   1 
HETATM 15086 O  O   . HOH IA 3 .   ? 55.262  -12.669 35.853  1.00 43.50 ? 1418 HOH K O   1 
HETATM 15087 O  O   . HOH IA 3 .   ? 30.627  -0.608  35.390  1.00 39.31 ? 1434 HOH K O   1 
HETATM 15088 O  O   . HOH IA 3 .   ? 51.892  11.808  30.458  1.00 39.53 ? 1446 HOH K O   1 
HETATM 15089 O  O   . HOH IA 3 .   ? 35.276  -14.683 29.251  1.00 43.06 ? 1460 HOH K O   1 
HETATM 15090 O  O   . HOH IA 3 .   ? 38.201  -10.082 18.294  1.00 33.13 ? 1486 HOH K O   1 
HETATM 15091 O  O   . HOH IA 3 .   ? 60.286  4.215   39.100  1.00 40.32 ? 1510 HOH K O   1 
HETATM 15092 O  O   . HOH IA 3 .   ? 49.561  8.881   13.892  1.00 36.86 ? 1539 HOH K O   1 
HETATM 15093 O  O   . HOH IA 3 .   ? 29.905  -1.069  40.994  1.00 41.67 ? 1573 HOH K O   1 
HETATM 15094 O  O   . HOH IA 3 .   ? 54.368  -17.433 13.876  1.00 44.01 ? 1575 HOH K O   1 
HETATM 15095 O  O   . HOH IA 3 .   ? 38.588  -16.325 18.870  1.00 41.11 ? 1612 HOH K O   1 
HETATM 15096 O  O   . HOH IA 3 .   ? 54.179  -16.319 30.246  1.00 40.14 ? 1615 HOH K O   1 
HETATM 15097 O  O   . HOH IA 3 .   ? 37.281  18.152  19.901  1.00 37.84 ? 1625 HOH K O   1 
HETATM 15098 O  O   . HOH IA 3 .   ? 38.701  -12.293 19.990  1.00 34.58 ? 1673 HOH K O   1 
HETATM 15099 O  O   . HOH IA 3 .   ? 65.503  0.815   12.792  1.00 25.35 ? 1691 HOH K O   1 
HETATM 15100 O  O   . HOH IA 3 .   ? 48.916  -21.631 16.516  1.00 51.58 ? 1692 HOH K O   1 
HETATM 15101 O  O   . HOH IA 3 .   ? 57.103  -6.144  14.397  1.00 27.95 ? 1702 HOH K O   1 
HETATM 15102 O  O   . HOH IA 3 .   ? 57.080  -2.058  24.096  1.00 31.72 ? 1716 HOH K O   1 
HETATM 15103 O  O   . HOH IA 3 .   ? 33.181  -0.982  37.965  1.00 35.24 ? 1721 HOH K O   1 
HETATM 15104 O  O   . HOH IA 3 .   ? 37.807  17.743  23.829  1.00 29.55 ? 1738 HOH K O   1 
HETATM 15105 O  O   . HOH IA 3 .   ? 33.914  -8.590  41.107  1.00 43.82 ? 1766 HOH K O   1 
HETATM 15106 O  O   . HOH IA 3 .   ? 29.489  0.307   31.095  1.00 37.86 ? 1767 HOH K O   1 
HETATM 15107 O  O   . HOH IA 3 .   ? 64.788  1.942   17.202  1.00 38.89 ? 1793 HOH K O   1 
HETATM 15108 O  O   . HOH IA 3 .   ? 54.746  -16.521 33.556  1.00 49.16 ? 1798 HOH K O   1 
HETATM 15109 O  O   . HOH IA 3 .   ? 48.443  -21.540 14.139  1.00 45.40 ? 1807 HOH K O   1 
HETATM 15110 O  O   . HOH JA 3 .   ? 39.193  3.576   57.886  1.00 27.76 ? 154  HOH L O   1 
HETATM 15111 O  O   . HOH JA 3 .   ? 35.675  -4.074  55.164  1.00 27.63 ? 156  HOH L O   1 
HETATM 15112 O  O   . HOH JA 3 .   ? 33.969  -1.131  41.628  1.00 32.42 ? 157  HOH L O   1 
HETATM 15113 O  O   . HOH JA 3 .   ? 58.881  -0.732  38.374  1.00 38.20 ? 158  HOH L O   1 
HETATM 15114 O  O   . HOH JA 3 .   ? 31.759  4.898   71.889  1.00 20.50 ? 159  HOH L O   1 
HETATM 15115 O  O   . HOH JA 3 .   ? 43.649  15.159  58.203  1.00 24.79 ? 160  HOH L O   1 
HETATM 15116 O  O   . HOH JA 3 .   ? 39.619  -10.257 56.271  1.00 28.19 ? 161  HOH L O   1 
HETATM 15117 O  O   . HOH JA 3 .   ? 43.929  -1.192  61.361  1.00 27.13 ? 162  HOH L O   1 
HETATM 15118 O  O   . HOH JA 3 .   ? 49.473  3.535   41.769  1.00 25.40 ? 163  HOH L O   1 
HETATM 15119 O  O   . HOH JA 3 .   ? 40.902  2.358   38.794  1.00 28.61 ? 164  HOH L O   1 
HETATM 15120 O  O   . HOH JA 3 .   ? 39.456  -6.621  66.233  1.00 30.10 ? 228  HOH L O   1 
HETATM 15121 O  O   . HOH JA 3 .   ? 46.986  -10.684 62.781  1.00 29.93 ? 247  HOH L O   1 
HETATM 15122 O  O   . HOH JA 3 .   ? 59.948  -9.545  51.902  1.00 42.88 ? 260  HOH L O   1 
HETATM 15123 O  O   . HOH JA 3 .   ? 43.120  -10.930 46.235  1.00 36.77 ? 271  HOH L O   1 
HETATM 15124 O  O   . HOH JA 3 .   ? 36.204  10.602  46.429  1.00 36.63 ? 278  HOH L O   1 
HETATM 15125 O  O   . HOH JA 3 .   ? 36.648  3.787   55.218  1.00 30.50 ? 284  HOH L O   1 
HETATM 15126 O  O   . HOH JA 3 .   ? 37.258  -8.251  45.520  1.00 29.29 ? 297  HOH L O   1 
HETATM 15127 O  O   . HOH JA 3 .   ? 38.461  9.837   39.127  1.00 43.15 ? 313  HOH L O   1 
HETATM 15128 O  O   . HOH JA 3 .   ? 40.028  4.763   44.624  1.00 35.21 ? 317  HOH L O   1 
HETATM 15129 O  O   . HOH JA 3 .   ? 44.345  -12.202 61.005  1.00 38.62 ? 327  HOH L O   1 
HETATM 15130 O  O   . HOH JA 3 .   ? 33.874  -5.136  59.749  1.00 29.72 ? 330  HOH L O   1 
HETATM 15131 O  O   . HOH JA 3 .   ? 45.307  -9.499  42.884  1.00 31.66 ? 378  HOH L O   1 
HETATM 15132 O  O   . HOH JA 3 .   ? 45.502  15.446  56.681  1.00 31.55 ? 382  HOH L O   1 
HETATM 15133 O  O   . HOH JA 3 .   ? 36.952  5.821   57.286  1.00 32.85 ? 422  HOH L O   1 
HETATM 15134 O  O   . HOH JA 3 .   ? 54.449  19.602  67.783  1.00 28.24 ? 440  HOH L O   1 
HETATM 15135 O  O   . HOH JA 3 .   ? 43.560  -11.371 43.390  1.00 38.41 ? 442  HOH L O   1 
HETATM 15136 O  O   . HOH JA 3 .   ? 54.829  6.468   60.620  1.00 39.22 ? 452  HOH L O   1 
HETATM 15137 O  O   . HOH JA 3 .   ? 35.068  -1.378  70.025  1.00 23.88 ? 459  HOH L O   1 
HETATM 15138 O  O   . HOH JA 3 .   ? 35.647  6.734   60.083  1.00 34.67 ? 527  HOH L O   1 
HETATM 15139 O  O   . HOH JA 3 .   ? 27.781  3.013   67.428  1.00 26.28 ? 536  HOH L O   1 
HETATM 15140 O  O   . HOH JA 3 .   ? 55.273  12.219  46.664  1.00 40.91 ? 549  HOH L O   1 
HETATM 15141 O  O   . HOH JA 3 .   ? 55.329  15.299  66.771  1.00 36.20 ? 584  HOH L O   1 
HETATM 15142 O  O   . HOH JA 3 .   ? 58.731  -11.970 51.981  1.00 47.12 ? 590  HOH L O   1 
HETATM 15143 O  O   . HOH JA 3 .   ? 35.879  -14.693 64.835  1.00 43.80 ? 605  HOH L O   1 
HETATM 15144 O  O   . HOH JA 3 .   ? 58.456  -7.688  39.485  1.00 42.32 ? 613  HOH L O   1 
HETATM 15145 O  O   . HOH JA 3 .   ? 59.259  3.766   43.765  1.00 39.25 ? 667  HOH L O   1 
HETATM 15146 O  O   . HOH JA 3 .   ? 59.864  -0.428  42.410  1.00 40.49 ? 727  HOH L O   1 
HETATM 15147 O  O   . HOH JA 3 .   ? 45.518  12.335  63.622  1.00 35.70 ? 728  HOH L O   1 
HETATM 15148 O  O   . HOH JA 3 .   ? 56.921  8.877   61.074  1.00 42.56 ? 769  HOH L O   1 
HETATM 15149 O  O   . HOH JA 3 .   ? 33.436  0.142   44.854  1.00 37.81 ? 856  HOH L O   1 
HETATM 15150 O  O   . HOH JA 3 .   ? 25.509  1.866   65.409  1.00 33.43 ? 868  HOH L O   1 
HETATM 15151 O  O   . HOH JA 3 .   ? 42.016  -11.545 58.465  1.00 37.46 ? 883  HOH L O   1 
HETATM 15152 O  O   . HOH JA 3 .   ? 37.864  -10.621 45.017  1.00 38.32 ? 897  HOH L O   1 
HETATM 15153 O  O   . HOH JA 3 .   ? 32.659  1.078   42.716  1.00 37.50 ? 919  HOH L O   1 
HETATM 15154 O  O   . HOH JA 3 .   ? 47.917  -4.122  66.263  1.00 28.64 ? 926  HOH L O   1 
HETATM 15155 O  O   . HOH JA 3 .   ? 35.758  -1.219  56.154  1.00 27.70 ? 931  HOH L O   1 
HETATM 15156 O  O   . HOH JA 3 .   ? 56.076  -6.294  61.897  1.00 44.33 ? 938  HOH L O   1 
HETATM 15157 O  O   . HOH JA 3 .   ? 59.043  16.686  62.291  1.00 39.26 ? 945  HOH L O   1 
HETATM 15158 O  O   . HOH JA 3 .   ? 39.662  8.580   65.506  1.00 27.73 ? 966  HOH L O   1 
HETATM 15159 O  O   . HOH JA 3 .   ? 32.910  1.776   51.410  1.00 26.62 ? 981  HOH L O   1 
HETATM 15160 O  O   . HOH JA 3 .   ? 35.537  1.140   55.105  1.00 29.19 ? 983  HOH L O   1 
HETATM 15161 O  O   . HOH JA 3 .   ? 46.076  14.408  62.486  1.00 34.97 ? 1007 HOH L O   1 
HETATM 15162 O  O   . HOH JA 3 .   ? 58.587  -1.319  44.324  1.00 40.67 ? 1031 HOH L O   1 
HETATM 15163 O  O   . HOH JA 3 .   ? 34.113  -14.554 54.215  1.00 37.95 ? 1035 HOH L O   1 
HETATM 15164 O  O   . HOH JA 3 .   ? 58.976  13.809  59.549  1.00 40.99 ? 1038 HOH L O   1 
HETATM 15165 O  O   . HOH JA 3 .   ? 49.787  19.620  61.529  1.00 35.10 ? 1055 HOH L O   1 
HETATM 15166 O  O   . HOH JA 3 .   ? 55.918  14.576  43.247  1.00 47.14 ? 1083 HOH L O   1 
HETATM 15167 O  O   . HOH JA 3 .   ? 33.087  3.916   50.114  1.00 30.70 ? 1092 HOH L O   1 
HETATM 15168 O  O   . HOH JA 3 .   ? 46.345  17.346  54.831  1.00 37.48 ? 1103 HOH L O   1 
HETATM 15169 O  O   . HOH JA 3 .   ? 57.337  15.751  64.565  1.00 44.43 ? 1116 HOH L O   1 
HETATM 15170 O  O   . HOH JA 3 .   ? 44.975  3.951   67.760  1.00 26.89 ? 1117 HOH L O   1 
HETATM 15171 O  O   . HOH JA 3 .   ? 35.793  6.110   54.410  1.00 34.14 ? 1119 HOH L O   1 
HETATM 15172 O  O   . HOH JA 3 .   ? 37.904  8.151   67.105  1.00 28.74 ? 1145 HOH L O   1 
HETATM 15173 O  O   . HOH JA 3 .   ? 33.232  2.633   54.216  1.00 32.37 ? 1171 HOH L O   1 
HETATM 15174 O  O   . HOH JA 3 .   ? 46.252  -3.507  67.953  1.00 37.29 ? 1174 HOH L O   1 
HETATM 15175 O  O   . HOH JA 3 .   ? 53.510  13.284  64.553  1.00 39.04 ? 1205 HOH L O   1 
HETATM 15176 O  O   . HOH JA 3 .   ? 31.847  0.366   46.829  1.00 32.39 ? 1226 HOH L O   1 
HETATM 15177 O  O   . HOH JA 3 .   ? 31.549  2.875   57.395  1.00 39.34 ? 1234 HOH L O   1 
HETATM 15178 O  O   . HOH JA 3 .   ? 46.349  4.625   41.000  1.00 35.71 ? 1239 HOH L O   1 
HETATM 15179 O  O   . HOH JA 3 .   ? 49.219  -19.551 52.408  1.00 53.33 ? 1244 HOH L O   1 
HETATM 15180 O  O   . HOH JA 3 .   ? 46.687  -21.819 50.043  1.00 50.67 ? 1245 HOH L O   1 
HETATM 15181 O  O   . HOH JA 3 .   ? 31.579  0.018   50.382  1.00 30.76 ? 1250 HOH L O   1 
HETATM 15182 O  O   . HOH JA 3 .   ? 40.941  -11.135 42.371  1.00 41.95 ? 1260 HOH L O   1 
HETATM 15183 O  O   . HOH JA 3 .   ? 59.842  -2.096  56.161  1.00 42.17 ? 1275 HOH L O   1 
HETATM 15184 O  O   . HOH JA 3 .   ? 33.481  -5.404  55.399  1.00 31.88 ? 1281 HOH L O   1 
HETATM 15185 O  O   . HOH JA 3 .   ? 60.323  8.732   60.673  1.00 44.45 ? 1283 HOH L O   1 
HETATM 15186 O  O   . HOH JA 3 .   ? 38.883  -14.760 64.899  1.00 47.51 ? 1285 HOH L O   1 
HETATM 15187 O  O   . HOH JA 3 .   ? 43.994  -15.511 61.046  1.00 46.19 ? 1286 HOH L O   1 
HETATM 15188 O  O   . HOH JA 3 .   ? 33.271  6.577   51.442  1.00 33.88 ? 1291 HOH L O   1 
HETATM 15189 O  O   . HOH JA 3 .   ? 48.610  2.444   65.859  1.00 28.59 ? 1357 HOH L O   1 
HETATM 15190 O  O   . HOH JA 3 .   ? 55.536  4.787   62.357  1.00 40.77 ? 1376 HOH L O   1 
HETATM 15191 O  O   . HOH JA 3 .   ? 60.230  -4.362  57.134  1.00 44.78 ? 1382 HOH L O   1 
HETATM 15192 O  O   . HOH JA 3 .   ? 52.833  1.440   61.200  1.00 37.87 ? 1387 HOH L O   1 
HETATM 15193 O  O   . HOH JA 3 .   ? 49.532  20.207  58.067  1.00 41.37 ? 1399 HOH L O   1 
HETATM 15194 O  O   . HOH JA 3 .   ? 44.265  8.460   42.902  1.00 38.15 ? 1448 HOH L O   1 
HETATM 15195 O  O   . HOH JA 3 .   ? 30.986  2.910   46.504  1.00 43.38 ? 1487 HOH L O   1 
HETATM 15196 O  O   . HOH JA 3 .   ? 47.590  -11.343 42.248  1.00 37.75 ? 1513 HOH L O   1 
HETATM 15197 O  O   . HOH JA 3 .   ? 32.255  -4.260  49.244  1.00 35.21 ? 1527 HOH L O   1 
HETATM 15198 O  O   . HOH JA 3 .   ? 44.452  -21.074 46.799  1.00 49.90 ? 1528 HOH L O   1 
HETATM 15199 O  O   . HOH JA 3 .   ? 56.205  -8.579  40.736  1.00 36.90 ? 1532 HOH L O   1 
HETATM 15200 O  O   . HOH JA 3 .   ? 47.184  11.987  66.062  1.00 33.08 ? 1536 HOH L O   1 
HETATM 15201 O  O   . HOH JA 3 .   ? 31.293  -1.664  48.383  1.00 37.65 ? 1564 HOH L O   1 
HETATM 15202 O  O   . HOH JA 3 .   ? 31.922  -7.160  47.515  1.00 41.51 ? 1569 HOH L O   1 
HETATM 15203 O  O   . HOH JA 3 .   ? 59.479  11.696  61.084  1.00 45.98 ? 1580 HOH L O   1 
HETATM 15204 O  O   . HOH JA 3 .   ? 31.762  4.530   44.290  1.00 38.37 ? 1635 HOH L O   1 
HETATM 15205 O  O   . HOH JA 3 .   ? 50.791  -13.843 53.140  1.00 47.06 ? 1636 HOH L O   1 
HETATM 15206 O  O   . HOH JA 3 .   ? 31.300  8.828   51.742  1.00 34.64 ? 1641 HOH L O   1 
HETATM 15207 O  O   . HOH JA 3 .   ? 48.185  -14.777 53.205  1.00 44.40 ? 1648 HOH L O   1 
HETATM 15208 O  O   . HOH JA 3 .   ? 31.414  7.519   66.294  1.00 37.85 ? 1654 HOH L O   1 
HETATM 15209 O  O   . HOH JA 3 .   ? 43.767  5.638   42.529  1.00 34.58 ? 1662 HOH L O   1 
HETATM 15210 O  O   . HOH JA 3 .   ? 34.300  -11.037 63.329  1.00 43.60 ? 1667 HOH L O   1 
HETATM 15211 O  O   . HOH JA 3 .   ? 56.062  -10.976 67.066  1.00 44.82 ? 1676 HOH L O   1 
HETATM 15212 O  O   . HOH JA 3 .   ? 54.581  17.582  54.009  1.00 39.79 ? 1700 HOH L O   1 
HETATM 15213 O  O   . HOH JA 3 .   ? 37.213  -15.793 59.736  1.00 43.78 ? 1730 HOH L O   1 
HETATM 15214 O  O   . HOH JA 3 .   ? 35.485  -16.679 55.499  1.00 42.16 ? 1764 HOH L O   1 
HETATM 15215 O  O   . HOH JA 3 .   ? 42.353  3.892   43.692  1.00 34.97 ? 1776 HOH L O   1 
HETATM 15216 O  O   . HOH JA 3 .   ? 55.385  -9.805  63.183  1.00 55.53 ? 1782 HOH L O   1 
HETATM 15217 O  O   . HOH JA 3 .   ? 50.542  0.483   62.201  1.00 40.43 ? 1795 HOH L O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   1   1   ALA ALA A . n 
A 1 2   THR 2   2   2   THR THR A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   ALA 4   4   4   ALA ALA A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   CYS 6   6   6   CYS CYS A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  TRP 32  32  32  TRP TRP A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  HIS 43  43  43  HIS HIS A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  HIS 46  46  46  HIS HIS A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  HIS 48  48  48  HIS HIS A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  PHE 50  50  50  PHE PHE A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  CYS 57  57  57  CYS CYS A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  PRO 62  62  62  PRO PRO A . n 
A 1 63  HIS 63  63  63  HIS HIS A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  GLY 90  90  90  GLY GLY A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ASN 96  96  96  ASN ASN A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 ARG 102 102 102 ARG ARG A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 GLU 109 109 109 GLU GLU A . n 
A 1 110 HIS 110 110 110 HIS HIS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 MET 117 117 117 MET MET A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 GLN 123 123 123 GLN GLN A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 CYS 146 146 146 CYS CYS A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 GLN 153 153 153 GLN GLN A . n 
B 1 1   ALA 1   1   1   ALA ALA B . n 
B 1 2   THR 2   2   2   THR THR B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   ALA 4   4   4   ALA ALA B . n 
B 1 5   VAL 5   5   5   VAL VAL B . n 
B 1 6   CYS 6   6   6   CYS CYS B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   LEU 8   8   8   LEU LEU B . n 
B 1 9   LYS 9   9   9   LYS LYS B . n 
B 1 10  GLY 10  10  10  GLY GLY B . n 
B 1 11  ASP 11  11  11  ASP ASP B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  PRO 13  13  13  PRO PRO B . n 
B 1 14  VAL 14  14  14  VAL VAL B . n 
B 1 15  GLN 15  15  15  GLN GLN B . n 
B 1 16  GLY 16  16  16  GLY GLY B . n 
B 1 17  ILE 17  17  17  ILE ILE B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  ASN 19  19  19  ASN ASN B . n 
B 1 20  PHE 20  20  20  PHE PHE B . n 
B 1 21  GLU 21  21  21  GLU GLU B . n 
B 1 22  GLN 22  22  22  GLN GLN B . n 
B 1 23  LYS 23  23  23  LYS LYS B . n 
B 1 24  GLU 24  24  24  GLU GLU B . n 
B 1 25  SER 25  25  25  SER SER B . n 
B 1 26  ASN 26  26  26  ASN ASN B . n 
B 1 27  GLY 27  27  27  GLY GLY B . n 
B 1 28  PRO 28  28  28  PRO PRO B . n 
B 1 29  VAL 29  29  29  VAL VAL B . n 
B 1 30  LYS 30  30  30  LYS LYS B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  TRP 32  32  32  TRP TRP B . n 
B 1 33  GLY 33  33  33  GLY GLY B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  ILE 35  35  35  ILE ILE B . n 
B 1 36  LYS 36  36  36  LYS LYS B . n 
B 1 37  GLY 37  37  37  GLY GLY B . n 
B 1 38  LEU 38  38  38  LEU LEU B . n 
B 1 39  THR 39  39  39  THR THR B . n 
B 1 40  GLU 40  40  40  GLU GLU B . n 
B 1 41  GLY 41  41  41  GLY GLY B . n 
B 1 42  LEU 42  42  42  LEU LEU B . n 
B 1 43  HIS 43  43  43  HIS HIS B . n 
B 1 44  GLY 44  44  44  GLY GLY B . n 
B 1 45  PHE 45  45  45  PHE PHE B . n 
B 1 46  HIS 46  46  46  HIS HIS B . n 
B 1 47  VAL 47  47  47  VAL VAL B . n 
B 1 48  HIS 48  48  48  HIS HIS B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  PHE 50  50  50  PHE PHE B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  THR 54  54  54  THR THR B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  GLY 56  56  56  GLY GLY B . n 
B 1 57  CYS 57  57  57  CYS CYS B . n 
B 1 58  THR 58  58  58  THR THR B . n 
B 1 59  SER 59  59  59  SER SER B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  PRO 62  62  62  PRO PRO B . n 
B 1 63  HIS 63  63  63  HIS HIS B . n 
B 1 64  PHE 64  64  64  PHE PHE B . n 
B 1 65  ASN 65  65  65  ASN ASN B . n 
B 1 66  PRO 66  66  66  PRO PRO B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  SER 68  68  68  SER SER B . n 
B 1 69  ARG 69  69  69  ARG ARG B . n 
B 1 70  LYS 70  70  70  LYS LYS B . n 
B 1 71  HIS 71  71  71  HIS HIS B . n 
B 1 72  GLY 72  72  72  GLY GLY B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LYS 75  75  75  LYS LYS B . n 
B 1 76  ASP 76  76  76  ASP ASP B . n 
B 1 77  GLU 77  77  77  GLU GLU B . n 
B 1 78  GLU 78  78  78  GLU GLU B . n 
B 1 79  ARG 79  79  79  ARG ARG B . n 
B 1 80  HIS 80  80  80  HIS HIS B . n 
B 1 81  VAL 81  81  81  VAL VAL B . n 
B 1 82  GLY 82  82  82  GLY GLY B . n 
B 1 83  ASP 83  83  83  ASP ASP B . n 
B 1 84  LEU 84  84  84  LEU LEU B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  ASN 86  86  86  ASN ASN B . n 
B 1 87  VAL 87  87  87  VAL VAL B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  GLY 90  90  90  GLY GLY B . n 
B 1 91  LYS 91  91  91  LYS LYS B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  GLY 93  93  93  GLY GLY B . n 
B 1 94  VAL 94  94  94  VAL VAL B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  ASN 96  96  96  ASN ASN B . n 
B 1 97  VAL 97  97  97  VAL VAL B . n 
B 1 98  SER 98  98  98  SER SER B . n 
B 1 99  ILE 99  99  99  ILE ILE B . n 
B 1 100 GLU 100 100 100 GLU GLU B . n 
B 1 101 ASP 101 101 101 ASP ASP B . n 
B 1 102 ARG 102 102 102 ARG ARG B . n 
B 1 103 VAL 103 103 103 VAL VAL B . n 
B 1 104 ILE 104 104 104 ILE ILE B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 SER 107 107 107 SER SER B . n 
B 1 108 GLY 108 108 108 GLY GLY B . n 
B 1 109 GLU 109 109 109 GLU GLU B . n 
B 1 110 HIS 110 110 110 HIS HIS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ILE 112 112 112 ILE ILE B . n 
B 1 113 ILE 113 113 113 ILE ILE B . n 
B 1 114 GLY 114 114 114 GLY GLY B . n 
B 1 115 ARG 115 115 115 ARG ARG B . n 
B 1 116 THR 116 116 116 THR THR B . n 
B 1 117 MET 117 117 117 MET MET B . n 
B 1 118 VAL 118 118 118 VAL VAL B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 HIS 120 120 120 HIS HIS B . n 
B 1 121 GLU 121 121 121 GLU GLU B . n 
B 1 122 LYS 122 122 122 LYS LYS B . n 
B 1 123 GLN 123 123 123 GLN GLN B . n 
B 1 124 ASP 124 124 124 ASP ASP B . n 
B 1 125 ASP 125 125 125 ASP ASP B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 GLY 127 127 127 GLY GLY B . n 
B 1 128 LYS 128 128 128 LYS LYS B . n 
B 1 129 GLY 129 129 129 GLY GLY B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ASN 131 131 131 ASN ASN B . n 
B 1 132 GLU 132 132 132 GLU GLU B . n 
B 1 133 GLU 133 133 133 GLU GLU B . n 
B 1 134 SER 134 134 134 SER SER B . n 
B 1 135 THR 135 135 135 THR THR B . n 
B 1 136 LYS 136 136 136 LYS LYS B . n 
B 1 137 THR 137 137 137 THR THR B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 ASN 139 139 139 ASN ASN B . n 
B 1 140 ALA 140 140 140 ALA ALA B . n 
B 1 141 GLY 141 141 141 GLY GLY B . n 
B 1 142 SER 142 142 142 SER SER B . n 
B 1 143 ARG 143 143 143 ARG ARG B . n 
B 1 144 LEU 144 144 144 LEU LEU B . n 
B 1 145 ALA 145 145 145 ALA ALA B . n 
B 1 146 CYS 146 146 146 CYS CYS B . n 
B 1 147 GLY 147 147 147 GLY GLY B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 ILE 149 149 149 ILE ILE B . n 
B 1 150 GLY 150 150 150 GLY GLY B . n 
B 1 151 ILE 151 151 151 ILE ILE B . n 
B 1 152 ALA 152 152 152 ALA ALA B . n 
B 1 153 GLN 153 153 153 GLN GLN B . n 
C 1 1   ALA 1   1   1   ALA ALA C . n 
C 1 2   THR 2   2   2   THR THR C . n 
C 1 3   LYS 3   3   3   LYS LYS C . n 
C 1 4   ALA 4   4   4   ALA ALA C . n 
C 1 5   VAL 5   5   5   VAL VAL C . n 
C 1 6   CYS 6   6   6   CYS CYS C . n 
C 1 7   VAL 7   7   7   VAL VAL C . n 
C 1 8   LEU 8   8   8   LEU LEU C . n 
C 1 9   LYS 9   9   9   LYS LYS C . n 
C 1 10  GLY 10  10  10  GLY GLY C . n 
C 1 11  ASP 11  11  11  ASP ASP C . n 
C 1 12  GLY 12  12  12  GLY GLY C . n 
C 1 13  PRO 13  13  13  PRO PRO C . n 
C 1 14  VAL 14  14  14  VAL VAL C . n 
C 1 15  GLN 15  15  15  GLN GLN C . n 
C 1 16  GLY 16  16  16  GLY GLY C . n 
C 1 17  ILE 17  17  17  ILE ILE C . n 
C 1 18  ILE 18  18  18  ILE ILE C . n 
C 1 19  ASN 19  19  19  ASN ASN C . n 
C 1 20  PHE 20  20  20  PHE PHE C . n 
C 1 21  GLU 21  21  21  GLU GLU C . n 
C 1 22  GLN 22  22  22  GLN GLN C . n 
C 1 23  LYS 23  23  23  LYS LYS C . n 
C 1 24  GLU 24  24  24  GLU GLU C . n 
C 1 25  SER 25  25  25  SER SER C . n 
C 1 26  ASN 26  26  26  ASN ASN C . n 
C 1 27  GLY 27  27  27  GLY GLY C . n 
C 1 28  PRO 28  28  28  PRO PRO C . n 
C 1 29  VAL 29  29  29  VAL VAL C . n 
C 1 30  LYS 30  30  30  LYS LYS C . n 
C 1 31  VAL 31  31  31  VAL VAL C . n 
C 1 32  TRP 32  32  32  TRP TRP C . n 
C 1 33  GLY 33  33  33  GLY GLY C . n 
C 1 34  SER 34  34  34  SER SER C . n 
C 1 35  ILE 35  35  35  ILE ILE C . n 
C 1 36  LYS 36  36  36  LYS LYS C . n 
C 1 37  GLY 37  37  37  GLY GLY C . n 
C 1 38  LEU 38  38  38  LEU LEU C . n 
C 1 39  THR 39  39  39  THR THR C . n 
C 1 40  GLU 40  40  40  GLU GLU C . n 
C 1 41  GLY 41  41  41  GLY GLY C . n 
C 1 42  LEU 42  42  42  LEU LEU C . n 
C 1 43  HIS 43  43  43  HIS HIS C . n 
C 1 44  GLY 44  44  44  GLY GLY C . n 
C 1 45  PHE 45  45  45  PHE PHE C . n 
C 1 46  HIS 46  46  46  HIS HIS C . n 
C 1 47  VAL 47  47  47  VAL VAL C . n 
C 1 48  HIS 48  48  48  HIS HIS C . n 
C 1 49  GLU 49  49  49  GLU GLU C . n 
C 1 50  PHE 50  50  50  PHE PHE C . n 
C 1 51  GLY 51  51  51  GLY GLY C . n 
C 1 52  ASP 52  52  52  ASP ASP C . n 
C 1 53  ASN 53  53  53  ASN ASN C . n 
C 1 54  THR 54  54  54  THR THR C . n 
C 1 55  ALA 55  55  55  ALA ALA C . n 
C 1 56  GLY 56  56  56  GLY GLY C . n 
C 1 57  CYS 57  57  57  CYS CYS C . n 
C 1 58  THR 58  58  58  THR THR C . n 
C 1 59  SER 59  59  59  SER SER C . n 
C 1 60  ALA 60  60  60  ALA ALA C . n 
C 1 61  GLY 61  61  61  GLY GLY C . n 
C 1 62  PRO 62  62  62  PRO PRO C . n 
C 1 63  HIS 63  63  63  HIS HIS C . n 
C 1 64  PHE 64  64  64  PHE PHE C . n 
C 1 65  ASN 65  65  65  ASN ASN C . n 
C 1 66  PRO 66  66  66  PRO PRO C . n 
C 1 67  LEU 67  67  67  LEU LEU C . n 
C 1 68  SER 68  68  68  SER SER C . n 
C 1 69  ARG 69  69  69  ARG ARG C . n 
C 1 70  LYS 70  70  70  LYS LYS C . n 
C 1 71  HIS 71  71  71  HIS HIS C . n 
C 1 72  GLY 72  72  72  GLY GLY C . n 
C 1 73  GLY 73  73  73  GLY GLY C . n 
C 1 74  PRO 74  74  74  PRO PRO C . n 
C 1 75  LYS 75  75  75  LYS LYS C . n 
C 1 76  ASP 76  76  76  ASP ASP C . n 
C 1 77  GLU 77  77  77  GLU GLU C . n 
C 1 78  GLU 78  78  78  GLU GLU C . n 
C 1 79  ARG 79  79  79  ARG ARG C . n 
C 1 80  HIS 80  80  80  HIS HIS C . n 
C 1 81  VAL 81  81  81  VAL VAL C . n 
C 1 82  GLY 82  82  82  GLY GLY C . n 
C 1 83  ASP 83  83  83  ASP ASP C . n 
C 1 84  LEU 84  84  84  LEU LEU C . n 
C 1 85  GLY 85  85  85  GLY GLY C . n 
C 1 86  ASN 86  86  86  ASN ASN C . n 
C 1 87  VAL 87  87  87  VAL VAL C . n 
C 1 88  THR 88  88  88  THR THR C . n 
C 1 89  ALA 89  89  89  ALA ALA C . n 
C 1 90  GLY 90  90  90  GLY GLY C . n 
C 1 91  LYS 91  91  91  LYS LYS C . n 
C 1 92  ASP 92  92  92  ASP ASP C . n 
C 1 93  GLY 93  93  93  GLY GLY C . n 
C 1 94  VAL 94  94  94  VAL VAL C . n 
C 1 95  ALA 95  95  95  ALA ALA C . n 
C 1 96  ASN 96  96  96  ASN ASN C . n 
C 1 97  VAL 97  97  97  VAL VAL C . n 
C 1 98  SER 98  98  98  SER SER C . n 
C 1 99  ILE 99  99  99  ILE ILE C . n 
C 1 100 GLU 100 100 100 GLU GLU C . n 
C 1 101 ASP 101 101 101 ASP ASP C . n 
C 1 102 ARG 102 102 102 ARG ARG C . n 
C 1 103 VAL 103 103 103 VAL VAL C . n 
C 1 104 ILE 104 104 104 ILE ILE C . n 
C 1 105 SER 105 105 105 SER SER C . n 
C 1 106 LEU 106 106 106 LEU LEU C . n 
C 1 107 SER 107 107 107 SER SER C . n 
C 1 108 GLY 108 108 108 GLY GLY C . n 
C 1 109 GLU 109 109 109 GLU GLU C . n 
C 1 110 HIS 110 110 110 HIS HIS C . n 
C 1 111 SER 111 111 111 SER SER C . n 
C 1 112 ILE 112 112 112 ILE ILE C . n 
C 1 113 ILE 113 113 113 ILE ILE C . n 
C 1 114 GLY 114 114 114 GLY GLY C . n 
C 1 115 ARG 115 115 115 ARG ARG C . n 
C 1 116 THR 116 116 116 THR THR C . n 
C 1 117 MET 117 117 117 MET MET C . n 
C 1 118 VAL 118 118 118 VAL VAL C . n 
C 1 119 VAL 119 119 119 VAL VAL C . n 
C 1 120 HIS 120 120 120 HIS HIS C . n 
C 1 121 GLU 121 121 121 GLU GLU C . n 
C 1 122 LYS 122 122 122 LYS LYS C . n 
C 1 123 GLN 123 123 123 GLN GLN C . n 
C 1 124 ASP 124 124 124 ASP ASP C . n 
C 1 125 ASP 125 125 125 ASP ASP C . n 
C 1 126 LEU 126 126 126 LEU LEU C . n 
C 1 127 GLY 127 127 127 GLY GLY C . n 
C 1 128 LYS 128 128 128 LYS LYS C . n 
C 1 129 GLY 129 129 129 GLY GLY C . n 
C 1 130 GLY 130 130 130 GLY GLY C . n 
C 1 131 ASN 131 131 131 ASN ASN C . n 
C 1 132 GLU 132 132 132 GLU GLU C . n 
C 1 133 GLU 133 133 133 GLU GLU C . n 
C 1 134 SER 134 134 134 SER SER C . n 
C 1 135 THR 135 135 135 THR THR C . n 
C 1 136 LYS 136 136 136 LYS LYS C . n 
C 1 137 THR 137 137 137 THR THR C . n 
C 1 138 GLY 138 138 138 GLY GLY C . n 
C 1 139 ASN 139 139 139 ASN ASN C . n 
C 1 140 ALA 140 140 140 ALA ALA C . n 
C 1 141 GLY 141 141 141 GLY GLY C . n 
C 1 142 SER 142 142 142 SER SER C . n 
C 1 143 ARG 143 143 143 ARG ARG C . n 
C 1 144 LEU 144 144 144 LEU LEU C . n 
C 1 145 ALA 145 145 145 ALA ALA C . n 
C 1 146 CYS 146 146 146 CYS CYS C . n 
C 1 147 GLY 147 147 147 GLY GLY C . n 
C 1 148 VAL 148 148 148 VAL VAL C . n 
C 1 149 ILE 149 149 149 ILE ILE C . n 
C 1 150 GLY 150 150 150 GLY GLY C . n 
C 1 151 ILE 151 151 151 ILE ILE C . n 
C 1 152 ALA 152 152 152 ALA ALA C . n 
C 1 153 GLN 153 153 153 GLN GLN C . n 
D 1 1   ALA 1   1   1   ALA ALA D . n 
D 1 2   THR 2   2   2   THR THR D . n 
D 1 3   LYS 3   3   3   LYS LYS D . n 
D 1 4   ALA 4   4   4   ALA ALA D . n 
D 1 5   VAL 5   5   5   VAL VAL D . n 
D 1 6   CYS 6   6   6   CYS CYS D . n 
D 1 7   VAL 7   7   7   VAL VAL D . n 
D 1 8   LEU 8   8   8   LEU LEU D . n 
D 1 9   LYS 9   9   9   LYS LYS D . n 
D 1 10  GLY 10  10  10  GLY GLY D . n 
D 1 11  ASP 11  11  11  ASP ASP D . n 
D 1 12  GLY 12  12  12  GLY GLY D . n 
D 1 13  PRO 13  13  13  PRO PRO D . n 
D 1 14  VAL 14  14  14  VAL VAL D . n 
D 1 15  GLN 15  15  15  GLN GLN D . n 
D 1 16  GLY 16  16  16  GLY GLY D . n 
D 1 17  ILE 17  17  17  ILE ILE D . n 
D 1 18  ILE 18  18  18  ILE ILE D . n 
D 1 19  ASN 19  19  19  ASN ASN D . n 
D 1 20  PHE 20  20  20  PHE PHE D . n 
D 1 21  GLU 21  21  21  GLU GLU D . n 
D 1 22  GLN 22  22  22  GLN GLN D . n 
D 1 23  LYS 23  23  23  LYS LYS D . n 
D 1 24  GLU 24  24  24  GLU GLU D . n 
D 1 25  SER 25  25  25  SER SER D . n 
D 1 26  ASN 26  26  26  ASN ASN D . n 
D 1 27  GLY 27  27  27  GLY GLY D . n 
D 1 28  PRO 28  28  28  PRO PRO D . n 
D 1 29  VAL 29  29  29  VAL VAL D . n 
D 1 30  LYS 30  30  30  LYS LYS D . n 
D 1 31  VAL 31  31  31  VAL VAL D . n 
D 1 32  TRP 32  32  32  TRP TRP D . n 
D 1 33  GLY 33  33  33  GLY GLY D . n 
D 1 34  SER 34  34  34  SER SER D . n 
D 1 35  ILE 35  35  35  ILE ILE D . n 
D 1 36  LYS 36  36  36  LYS LYS D . n 
D 1 37  GLY 37  37  37  GLY GLY D . n 
D 1 38  LEU 38  38  38  LEU LEU D . n 
D 1 39  THR 39  39  39  THR THR D . n 
D 1 40  GLU 40  40  40  GLU GLU D . n 
D 1 41  GLY 41  41  41  GLY GLY D . n 
D 1 42  LEU 42  42  42  LEU LEU D . n 
D 1 43  HIS 43  43  43  HIS HIS D . n 
D 1 44  GLY 44  44  44  GLY GLY D . n 
D 1 45  PHE 45  45  45  PHE PHE D . n 
D 1 46  HIS 46  46  46  HIS HIS D . n 
D 1 47  VAL 47  47  47  VAL VAL D . n 
D 1 48  HIS 48  48  48  HIS HIS D . n 
D 1 49  GLU 49  49  49  GLU GLU D . n 
D 1 50  PHE 50  50  50  PHE PHE D . n 
D 1 51  GLY 51  51  51  GLY GLY D . n 
D 1 52  ASP 52  52  52  ASP ASP D . n 
D 1 53  ASN 53  53  53  ASN ASN D . n 
D 1 54  THR 54  54  54  THR THR D . n 
D 1 55  ALA 55  55  55  ALA ALA D . n 
D 1 56  GLY 56  56  56  GLY GLY D . n 
D 1 57  CYS 57  57  57  CYS CYS D . n 
D 1 58  THR 58  58  58  THR THR D . n 
D 1 59  SER 59  59  59  SER SER D . n 
D 1 60  ALA 60  60  60  ALA ALA D . n 
D 1 61  GLY 61  61  61  GLY GLY D . n 
D 1 62  PRO 62  62  62  PRO PRO D . n 
D 1 63  HIS 63  63  63  HIS HIS D . n 
D 1 64  PHE 64  64  64  PHE PHE D . n 
D 1 65  ASN 65  65  65  ASN ASN D . n 
D 1 66  PRO 66  66  66  PRO PRO D . n 
D 1 67  LEU 67  67  67  LEU LEU D . n 
D 1 68  SER 68  68  68  SER SER D . n 
D 1 69  ARG 69  69  69  ARG ARG D . n 
D 1 70  LYS 70  70  70  LYS LYS D . n 
D 1 71  HIS 71  71  71  HIS HIS D . n 
D 1 72  GLY 72  72  72  GLY GLY D . n 
D 1 73  GLY 73  73  73  GLY GLY D . n 
D 1 74  PRO 74  74  74  PRO PRO D . n 
D 1 75  LYS 75  75  75  LYS LYS D . n 
D 1 76  ASP 76  76  76  ASP ASP D . n 
D 1 77  GLU 77  77  77  GLU GLU D . n 
D 1 78  GLU 78  78  78  GLU GLU D . n 
D 1 79  ARG 79  79  79  ARG ARG D . n 
D 1 80  HIS 80  80  80  HIS HIS D . n 
D 1 81  VAL 81  81  81  VAL VAL D . n 
D 1 82  GLY 82  82  82  GLY GLY D . n 
D 1 83  ASP 83  83  83  ASP ASP D . n 
D 1 84  LEU 84  84  84  LEU LEU D . n 
D 1 85  GLY 85  85  85  GLY GLY D . n 
D 1 86  ASN 86  86  86  ASN ASN D . n 
D 1 87  VAL 87  87  87  VAL VAL D . n 
D 1 88  THR 88  88  88  THR THR D . n 
D 1 89  ALA 89  89  89  ALA ALA D . n 
D 1 90  GLY 90  90  90  GLY GLY D . n 
D 1 91  LYS 91  91  91  LYS LYS D . n 
D 1 92  ASP 92  92  92  ASP ASP D . n 
D 1 93  GLY 93  93  93  GLY GLY D . n 
D 1 94  VAL 94  94  94  VAL VAL D . n 
D 1 95  ALA 95  95  95  ALA ALA D . n 
D 1 96  ASN 96  96  96  ASN ASN D . n 
D 1 97  VAL 97  97  97  VAL VAL D . n 
D 1 98  SER 98  98  98  SER SER D . n 
D 1 99  ILE 99  99  99  ILE ILE D . n 
D 1 100 GLU 100 100 100 GLU GLU D . n 
D 1 101 ASP 101 101 101 ASP ASP D . n 
D 1 102 ARG 102 102 102 ARG ARG D . n 
D 1 103 VAL 103 103 103 VAL VAL D . n 
D 1 104 ILE 104 104 104 ILE ILE D . n 
D 1 105 SER 105 105 105 SER SER D . n 
D 1 106 LEU 106 106 106 LEU LEU D . n 
D 1 107 SER 107 107 107 SER SER D . n 
D 1 108 GLY 108 108 108 GLY GLY D . n 
D 1 109 GLU 109 109 109 GLU GLU D . n 
D 1 110 HIS 110 110 110 HIS HIS D . n 
D 1 111 SER 111 111 111 SER SER D . n 
D 1 112 ILE 112 112 112 ILE ILE D . n 
D 1 113 ILE 113 113 113 ILE ILE D . n 
D 1 114 GLY 114 114 114 GLY GLY D . n 
D 1 115 ARG 115 115 115 ARG ARG D . n 
D 1 116 THR 116 116 116 THR THR D . n 
D 1 117 MET 117 117 117 MET MET D . n 
D 1 118 VAL 118 118 118 VAL VAL D . n 
D 1 119 VAL 119 119 119 VAL VAL D . n 
D 1 120 HIS 120 120 120 HIS HIS D . n 
D 1 121 GLU 121 121 121 GLU GLU D . n 
D 1 122 LYS 122 122 122 LYS LYS D . n 
D 1 123 GLN 123 123 123 GLN GLN D . n 
D 1 124 ASP 124 124 124 ASP ASP D . n 
D 1 125 ASP 125 125 125 ASP ASP D . n 
D 1 126 LEU 126 126 126 LEU LEU D . n 
D 1 127 GLY 127 127 127 GLY GLY D . n 
D 1 128 LYS 128 128 128 LYS LYS D . n 
D 1 129 GLY 129 129 129 GLY GLY D . n 
D 1 130 GLY 130 130 130 GLY GLY D . n 
D 1 131 ASN 131 131 131 ASN ASN D . n 
D 1 132 GLU 132 132 132 GLU GLU D . n 
D 1 133 GLU 133 133 133 GLU GLU D . n 
D 1 134 SER 134 134 134 SER SER D . n 
D 1 135 THR 135 135 135 THR THR D . n 
D 1 136 LYS 136 136 136 LYS LYS D . n 
D 1 137 THR 137 137 137 THR THR D . n 
D 1 138 GLY 138 138 138 GLY GLY D . n 
D 1 139 ASN 139 139 139 ASN ASN D . n 
D 1 140 ALA 140 140 140 ALA ALA D . n 
D 1 141 GLY 141 141 141 GLY GLY D . n 
D 1 142 SER 142 142 142 SER SER D . n 
D 1 143 ARG 143 143 143 ARG ARG D . n 
D 1 144 LEU 144 144 144 LEU LEU D . n 
D 1 145 ALA 145 145 145 ALA ALA D . n 
D 1 146 CYS 146 146 146 CYS CYS D . n 
D 1 147 GLY 147 147 147 GLY GLY D . n 
D 1 148 VAL 148 148 148 VAL VAL D . n 
D 1 149 ILE 149 149 149 ILE ILE D . n 
D 1 150 GLY 150 150 150 GLY GLY D . n 
D 1 151 ILE 151 151 151 ILE ILE D . n 
D 1 152 ALA 152 152 152 ALA ALA D . n 
D 1 153 GLN 153 153 153 GLN GLN D . n 
E 1 1   ALA 1   1   1   ALA ALA E . n 
E 1 2   THR 2   2   2   THR THR E . n 
E 1 3   LYS 3   3   3   LYS LYS E . n 
E 1 4   ALA 4   4   4   ALA ALA E . n 
E 1 5   VAL 5   5   5   VAL VAL E . n 
E 1 6   CYS 6   6   6   CYS CYS E . n 
E 1 7   VAL 7   7   7   VAL VAL E . n 
E 1 8   LEU 8   8   8   LEU LEU E . n 
E 1 9   LYS 9   9   9   LYS LYS E . n 
E 1 10  GLY 10  10  10  GLY GLY E . n 
E 1 11  ASP 11  11  11  ASP ASP E . n 
E 1 12  GLY 12  12  12  GLY GLY E . n 
E 1 13  PRO 13  13  13  PRO PRO E . n 
E 1 14  VAL 14  14  14  VAL VAL E . n 
E 1 15  GLN 15  15  15  GLN GLN E . n 
E 1 16  GLY 16  16  16  GLY GLY E . n 
E 1 17  ILE 17  17  17  ILE ILE E . n 
E 1 18  ILE 18  18  18  ILE ILE E . n 
E 1 19  ASN 19  19  19  ASN ASN E . n 
E 1 20  PHE 20  20  20  PHE PHE E . n 
E 1 21  GLU 21  21  21  GLU GLU E . n 
E 1 22  GLN 22  22  22  GLN GLN E . n 
E 1 23  LYS 23  23  23  LYS LYS E . n 
E 1 24  GLU 24  24  24  GLU GLU E . n 
E 1 25  SER 25  25  25  SER SER E . n 
E 1 26  ASN 26  26  26  ASN ASN E . n 
E 1 27  GLY 27  27  27  GLY GLY E . n 
E 1 28  PRO 28  28  28  PRO PRO E . n 
E 1 29  VAL 29  29  29  VAL VAL E . n 
E 1 30  LYS 30  30  30  LYS LYS E . n 
E 1 31  VAL 31  31  31  VAL VAL E . n 
E 1 32  TRP 32  32  32  TRP TRP E . n 
E 1 33  GLY 33  33  33  GLY GLY E . n 
E 1 34  SER 34  34  34  SER SER E . n 
E 1 35  ILE 35  35  35  ILE ILE E . n 
E 1 36  LYS 36  36  36  LYS LYS E . n 
E 1 37  GLY 37  37  37  GLY GLY E . n 
E 1 38  LEU 38  38  38  LEU LEU E . n 
E 1 39  THR 39  39  39  THR THR E . n 
E 1 40  GLU 40  40  40  GLU GLU E . n 
E 1 41  GLY 41  41  41  GLY GLY E . n 
E 1 42  LEU 42  42  42  LEU LEU E . n 
E 1 43  HIS 43  43  43  HIS HIS E . n 
E 1 44  GLY 44  44  44  GLY GLY E . n 
E 1 45  PHE 45  45  45  PHE PHE E . n 
E 1 46  HIS 46  46  46  HIS HIS E . n 
E 1 47  VAL 47  47  47  VAL VAL E . n 
E 1 48  HIS 48  48  48  HIS HIS E . n 
E 1 49  GLU 49  49  49  GLU GLU E . n 
E 1 50  PHE 50  50  50  PHE PHE E . n 
E 1 51  GLY 51  51  51  GLY GLY E . n 
E 1 52  ASP 52  52  52  ASP ASP E . n 
E 1 53  ASN 53  53  53  ASN ASN E . n 
E 1 54  THR 54  54  54  THR THR E . n 
E 1 55  ALA 55  55  55  ALA ALA E . n 
E 1 56  GLY 56  56  56  GLY GLY E . n 
E 1 57  CYS 57  57  57  CYS CYS E . n 
E 1 58  THR 58  58  58  THR THR E . n 
E 1 59  SER 59  59  59  SER SER E . n 
E 1 60  ALA 60  60  60  ALA ALA E . n 
E 1 61  GLY 61  61  61  GLY GLY E . n 
E 1 62  PRO 62  62  62  PRO PRO E . n 
E 1 63  HIS 63  63  63  HIS HIS E . n 
E 1 64  PHE 64  64  64  PHE PHE E . n 
E 1 65  ASN 65  65  65  ASN ASN E . n 
E 1 66  PRO 66  66  66  PRO PRO E . n 
E 1 67  LEU 67  67  67  LEU LEU E . n 
E 1 68  SER 68  68  68  SER SER E . n 
E 1 69  ARG 69  69  69  ARG ARG E . n 
E 1 70  LYS 70  70  70  LYS LYS E . n 
E 1 71  HIS 71  71  71  HIS HIS E . n 
E 1 72  GLY 72  72  72  GLY GLY E . n 
E 1 73  GLY 73  73  73  GLY GLY E . n 
E 1 74  PRO 74  74  74  PRO PRO E . n 
E 1 75  LYS 75  75  75  LYS LYS E . n 
E 1 76  ASP 76  76  76  ASP ASP E . n 
E 1 77  GLU 77  77  77  GLU GLU E . n 
E 1 78  GLU 78  78  78  GLU GLU E . n 
E 1 79  ARG 79  79  79  ARG ARG E . n 
E 1 80  HIS 80  80  80  HIS HIS E . n 
E 1 81  VAL 81  81  81  VAL VAL E . n 
E 1 82  GLY 82  82  82  GLY GLY E . n 
E 1 83  ASP 83  83  83  ASP ASP E . n 
E 1 84  LEU 84  84  84  LEU LEU E . n 
E 1 85  GLY 85  85  85  GLY GLY E . n 
E 1 86  ASN 86  86  86  ASN ASN E . n 
E 1 87  VAL 87  87  87  VAL VAL E . n 
E 1 88  THR 88  88  88  THR THR E . n 
E 1 89  ALA 89  89  89  ALA ALA E . n 
E 1 90  GLY 90  90  90  GLY GLY E . n 
E 1 91  LYS 91  91  91  LYS LYS E . n 
E 1 92  ASP 92  92  92  ASP ASP E . n 
E 1 93  GLY 93  93  93  GLY GLY E . n 
E 1 94  VAL 94  94  94  VAL VAL E . n 
E 1 95  ALA 95  95  95  ALA ALA E . n 
E 1 96  ASN 96  96  96  ASN ASN E . n 
E 1 97  VAL 97  97  97  VAL VAL E . n 
E 1 98  SER 98  98  98  SER SER E . n 
E 1 99  ILE 99  99  99  ILE ILE E . n 
E 1 100 GLU 100 100 100 GLU GLU E . n 
E 1 101 ASP 101 101 101 ASP ASP E . n 
E 1 102 ARG 102 102 102 ARG ARG E . n 
E 1 103 VAL 103 103 103 VAL VAL E . n 
E 1 104 ILE 104 104 104 ILE ILE E . n 
E 1 105 SER 105 105 105 SER SER E . n 
E 1 106 LEU 106 106 106 LEU LEU E . n 
E 1 107 SER 107 107 107 SER SER E . n 
E 1 108 GLY 108 108 108 GLY GLY E . n 
E 1 109 GLU 109 109 109 GLU GLU E . n 
E 1 110 HIS 110 110 110 HIS HIS E . n 
E 1 111 SER 111 111 111 SER SER E . n 
E 1 112 ILE 112 112 112 ILE ILE E . n 
E 1 113 ILE 113 113 113 ILE ILE E . n 
E 1 114 GLY 114 114 114 GLY GLY E . n 
E 1 115 ARG 115 115 115 ARG ARG E . n 
E 1 116 THR 116 116 116 THR THR E . n 
E 1 117 MET 117 117 117 MET MET E . n 
E 1 118 VAL 118 118 118 VAL VAL E . n 
E 1 119 VAL 119 119 119 VAL VAL E . n 
E 1 120 HIS 120 120 120 HIS HIS E . n 
E 1 121 GLU 121 121 121 GLU GLU E . n 
E 1 122 LYS 122 122 122 LYS LYS E . n 
E 1 123 GLN 123 123 123 GLN GLN E . n 
E 1 124 ASP 124 124 124 ASP ASP E . n 
E 1 125 ASP 125 125 125 ASP ASP E . n 
E 1 126 LEU 126 126 126 LEU LEU E . n 
E 1 127 GLY 127 127 127 GLY GLY E . n 
E 1 128 LYS 128 128 128 LYS LYS E . n 
E 1 129 GLY 129 129 129 GLY GLY E . n 
E 1 130 GLY 130 130 130 GLY GLY E . n 
E 1 131 ASN 131 131 131 ASN ASN E . n 
E 1 132 GLU 132 132 132 GLU GLU E . n 
E 1 133 GLU 133 133 133 GLU GLU E . n 
E 1 134 SER 134 134 134 SER SER E . n 
E 1 135 THR 135 135 135 THR THR E . n 
E 1 136 LYS 136 136 136 LYS LYS E . n 
E 1 137 THR 137 137 137 THR THR E . n 
E 1 138 GLY 138 138 138 GLY GLY E . n 
E 1 139 ASN 139 139 139 ASN ASN E . n 
E 1 140 ALA 140 140 140 ALA ALA E . n 
E 1 141 GLY 141 141 141 GLY GLY E . n 
E 1 142 SER 142 142 142 SER SER E . n 
E 1 143 ARG 143 143 143 ARG ARG E . n 
E 1 144 LEU 144 144 144 LEU LEU E . n 
E 1 145 ALA 145 145 145 ALA ALA E . n 
E 1 146 CYS 146 146 146 CYS CYS E . n 
E 1 147 GLY 147 147 147 GLY GLY E . n 
E 1 148 VAL 148 148 148 VAL VAL E . n 
E 1 149 ILE 149 149 149 ILE ILE E . n 
E 1 150 GLY 150 150 150 GLY GLY E . n 
E 1 151 ILE 151 151 151 ILE ILE E . n 
E 1 152 ALA 152 152 152 ALA ALA E . n 
E 1 153 GLN 153 153 153 GLN GLN E . n 
F 1 1   ALA 1   1   1   ALA ALA F . n 
F 1 2   THR 2   2   2   THR THR F . n 
F 1 3   LYS 3   3   3   LYS LYS F . n 
F 1 4   ALA 4   4   4   ALA ALA F . n 
F 1 5   VAL 5   5   5   VAL VAL F . n 
F 1 6   CYS 6   6   6   CYS CYS F . n 
F 1 7   VAL 7   7   7   VAL VAL F . n 
F 1 8   LEU 8   8   8   LEU LEU F . n 
F 1 9   LYS 9   9   9   LYS LYS F . n 
F 1 10  GLY 10  10  10  GLY GLY F . n 
F 1 11  ASP 11  11  11  ASP ASP F . n 
F 1 12  GLY 12  12  12  GLY GLY F . n 
F 1 13  PRO 13  13  13  PRO PRO F . n 
F 1 14  VAL 14  14  14  VAL VAL F . n 
F 1 15  GLN 15  15  15  GLN GLN F . n 
F 1 16  GLY 16  16  16  GLY GLY F . n 
F 1 17  ILE 17  17  17  ILE ILE F . n 
F 1 18  ILE 18  18  18  ILE ILE F . n 
F 1 19  ASN 19  19  19  ASN ASN F . n 
F 1 20  PHE 20  20  20  PHE PHE F . n 
F 1 21  GLU 21  21  21  GLU GLU F . n 
F 1 22  GLN 22  22  22  GLN GLN F . n 
F 1 23  LYS 23  23  23  LYS LYS F . n 
F 1 24  GLU 24  24  24  GLU GLU F . n 
F 1 25  SER 25  25  25  SER SER F . n 
F 1 26  ASN 26  26  26  ASN ASN F . n 
F 1 27  GLY 27  27  27  GLY GLY F . n 
F 1 28  PRO 28  28  28  PRO PRO F . n 
F 1 29  VAL 29  29  29  VAL VAL F . n 
F 1 30  LYS 30  30  30  LYS LYS F . n 
F 1 31  VAL 31  31  31  VAL VAL F . n 
F 1 32  TRP 32  32  32  TRP TRP F . n 
F 1 33  GLY 33  33  33  GLY GLY F . n 
F 1 34  SER 34  34  34  SER SER F . n 
F 1 35  ILE 35  35  35  ILE ILE F . n 
F 1 36  LYS 36  36  36  LYS LYS F . n 
F 1 37  GLY 37  37  37  GLY GLY F . n 
F 1 38  LEU 38  38  38  LEU LEU F . n 
F 1 39  THR 39  39  39  THR THR F . n 
F 1 40  GLU 40  40  40  GLU GLU F . n 
F 1 41  GLY 41  41  41  GLY GLY F . n 
F 1 42  LEU 42  42  42  LEU LEU F . n 
F 1 43  HIS 43  43  43  HIS HIS F . n 
F 1 44  GLY 44  44  44  GLY GLY F . n 
F 1 45  PHE 45  45  45  PHE PHE F . n 
F 1 46  HIS 46  46  46  HIS HIS F . n 
F 1 47  VAL 47  47  47  VAL VAL F . n 
F 1 48  HIS 48  48  48  HIS HIS F . n 
F 1 49  GLU 49  49  49  GLU GLU F . n 
F 1 50  PHE 50  50  50  PHE PHE F . n 
F 1 51  GLY 51  51  51  GLY GLY F . n 
F 1 52  ASP 52  52  52  ASP ASP F . n 
F 1 53  ASN 53  53  53  ASN ASN F . n 
F 1 54  THR 54  54  54  THR THR F . n 
F 1 55  ALA 55  55  55  ALA ALA F . n 
F 1 56  GLY 56  56  56  GLY GLY F . n 
F 1 57  CYS 57  57  57  CYS CYS F . n 
F 1 58  THR 58  58  58  THR THR F . n 
F 1 59  SER 59  59  59  SER SER F . n 
F 1 60  ALA 60  60  60  ALA ALA F . n 
F 1 61  GLY 61  61  61  GLY GLY F . n 
F 1 62  PRO 62  62  62  PRO PRO F . n 
F 1 63  HIS 63  63  63  HIS HIS F . n 
F 1 64  PHE 64  64  64  PHE PHE F . n 
F 1 65  ASN 65  65  65  ASN ASN F . n 
F 1 66  PRO 66  66  66  PRO PRO F . n 
F 1 67  LEU 67  67  67  LEU LEU F . n 
F 1 68  SER 68  68  68  SER SER F . n 
F 1 69  ARG 69  69  69  ARG ARG F . n 
F 1 70  LYS 70  70  70  LYS LYS F . n 
F 1 71  HIS 71  71  71  HIS HIS F . n 
F 1 72  GLY 72  72  72  GLY GLY F . n 
F 1 73  GLY 73  73  73  GLY GLY F . n 
F 1 74  PRO 74  74  74  PRO PRO F . n 
F 1 75  LYS 75  75  75  LYS LYS F . n 
F 1 76  ASP 76  76  76  ASP ASP F . n 
F 1 77  GLU 77  77  77  GLU GLU F . n 
F 1 78  GLU 78  78  78  GLU GLU F . n 
F 1 79  ARG 79  79  79  ARG ARG F . n 
F 1 80  HIS 80  80  80  HIS HIS F . n 
F 1 81  VAL 81  81  81  VAL VAL F . n 
F 1 82  GLY 82  82  82  GLY GLY F . n 
F 1 83  ASP 83  83  83  ASP ASP F . n 
F 1 84  LEU 84  84  84  LEU LEU F . n 
F 1 85  GLY 85  85  85  GLY GLY F . n 
F 1 86  ASN 86  86  86  ASN ASN F . n 
F 1 87  VAL 87  87  87  VAL VAL F . n 
F 1 88  THR 88  88  88  THR THR F . n 
F 1 89  ALA 89  89  89  ALA ALA F . n 
F 1 90  GLY 90  90  90  GLY GLY F . n 
F 1 91  LYS 91  91  91  LYS LYS F . n 
F 1 92  ASP 92  92  92  ASP ASP F . n 
F 1 93  GLY 93  93  93  GLY GLY F . n 
F 1 94  VAL 94  94  94  VAL VAL F . n 
F 1 95  ALA 95  95  95  ALA ALA F . n 
F 1 96  ASN 96  96  96  ASN ASN F . n 
F 1 97  VAL 97  97  97  VAL VAL F . n 
F 1 98  SER 98  98  98  SER SER F . n 
F 1 99  ILE 99  99  99  ILE ILE F . n 
F 1 100 GLU 100 100 100 GLU GLU F . n 
F 1 101 ASP 101 101 101 ASP ASP F . n 
F 1 102 ARG 102 102 102 ARG ARG F . n 
F 1 103 VAL 103 103 103 VAL VAL F . n 
F 1 104 ILE 104 104 104 ILE ILE F . n 
F 1 105 SER 105 105 105 SER SER F . n 
F 1 106 LEU 106 106 106 LEU LEU F . n 
F 1 107 SER 107 107 107 SER SER F . n 
F 1 108 GLY 108 108 108 GLY GLY F . n 
F 1 109 GLU 109 109 109 GLU GLU F . n 
F 1 110 HIS 110 110 110 HIS HIS F . n 
F 1 111 SER 111 111 111 SER SER F . n 
F 1 112 ILE 112 112 112 ILE ILE F . n 
F 1 113 ILE 113 113 113 ILE ILE F . n 
F 1 114 GLY 114 114 114 GLY GLY F . n 
F 1 115 ARG 115 115 115 ARG ARG F . n 
F 1 116 THR 116 116 116 THR THR F . n 
F 1 117 MET 117 117 117 MET MET F . n 
F 1 118 VAL 118 118 118 VAL VAL F . n 
F 1 119 VAL 119 119 119 VAL VAL F . n 
F 1 120 HIS 120 120 120 HIS HIS F . n 
F 1 121 GLU 121 121 121 GLU GLU F . n 
F 1 122 LYS 122 122 122 LYS LYS F . n 
F 1 123 GLN 123 123 123 GLN GLN F . n 
F 1 124 ASP 124 124 124 ASP ASP F . n 
F 1 125 ASP 125 125 125 ASP ASP F . n 
F 1 126 LEU 126 126 126 LEU LEU F . n 
F 1 127 GLY 127 127 127 GLY GLY F . n 
F 1 128 LYS 128 128 128 LYS LYS F . n 
F 1 129 GLY 129 129 129 GLY GLY F . n 
F 1 130 GLY 130 130 130 GLY GLY F . n 
F 1 131 ASN 131 131 131 ASN ASN F . n 
F 1 132 GLU 132 132 132 GLU GLU F . n 
F 1 133 GLU 133 133 133 GLU GLU F . n 
F 1 134 SER 134 134 134 SER SER F . n 
F 1 135 THR 135 135 135 THR THR F . n 
F 1 136 LYS 136 136 136 LYS LYS F . n 
F 1 137 THR 137 137 137 THR THR F . n 
F 1 138 GLY 138 138 138 GLY GLY F . n 
F 1 139 ASN 139 139 139 ASN ASN F . n 
F 1 140 ALA 140 140 140 ALA ALA F . n 
F 1 141 GLY 141 141 141 GLY GLY F . n 
F 1 142 SER 142 142 142 SER SER F . n 
F 1 143 ARG 143 143 143 ARG ARG F . n 
F 1 144 LEU 144 144 144 LEU LEU F . n 
F 1 145 ALA 145 145 145 ALA ALA F . n 
F 1 146 CYS 146 146 146 CYS CYS F . n 
F 1 147 GLY 147 147 147 GLY GLY F . n 
F 1 148 VAL 148 148 148 VAL VAL F . n 
F 1 149 ILE 149 149 149 ILE ILE F . n 
F 1 150 GLY 150 150 150 GLY GLY F . n 
F 1 151 ILE 151 151 151 ILE ILE F . n 
F 1 152 ALA 152 152 152 ALA ALA F . n 
F 1 153 GLN 153 153 153 GLN GLN F . n 
G 1 1   ALA 1   1   1   ALA ALA G . n 
G 1 2   THR 2   2   2   THR THR G . n 
G 1 3   LYS 3   3   3   LYS LYS G . n 
G 1 4   ALA 4   4   4   ALA ALA G . n 
G 1 5   VAL 5   5   5   VAL VAL G . n 
G 1 6   CYS 6   6   6   CYS CYS G . n 
G 1 7   VAL 7   7   7   VAL VAL G . n 
G 1 8   LEU 8   8   8   LEU LEU G . n 
G 1 9   LYS 9   9   9   LYS LYS G . n 
G 1 10  GLY 10  10  10  GLY GLY G . n 
G 1 11  ASP 11  11  11  ASP ASP G . n 
G 1 12  GLY 12  12  12  GLY GLY G . n 
G 1 13  PRO 13  13  13  PRO PRO G . n 
G 1 14  VAL 14  14  14  VAL VAL G . n 
G 1 15  GLN 15  15  15  GLN GLN G . n 
G 1 16  GLY 16  16  16  GLY GLY G . n 
G 1 17  ILE 17  17  17  ILE ILE G . n 
G 1 18  ILE 18  18  18  ILE ILE G . n 
G 1 19  ASN 19  19  19  ASN ASN G . n 
G 1 20  PHE 20  20  20  PHE PHE G . n 
G 1 21  GLU 21  21  21  GLU GLU G . n 
G 1 22  GLN 22  22  22  GLN GLN G . n 
G 1 23  LYS 23  23  23  LYS LYS G . n 
G 1 24  GLU 24  24  24  GLU GLU G . n 
G 1 25  SER 25  25  25  SER SER G . n 
G 1 26  ASN 26  26  26  ASN ASN G . n 
G 1 27  GLY 27  27  27  GLY GLY G . n 
G 1 28  PRO 28  28  28  PRO PRO G . n 
G 1 29  VAL 29  29  29  VAL VAL G . n 
G 1 30  LYS 30  30  30  LYS LYS G . n 
G 1 31  VAL 31  31  31  VAL VAL G . n 
G 1 32  TRP 32  32  32  TRP TRP G . n 
G 1 33  GLY 33  33  33  GLY GLY G . n 
G 1 34  SER 34  34  34  SER SER G . n 
G 1 35  ILE 35  35  35  ILE ILE G . n 
G 1 36  LYS 36  36  36  LYS LYS G . n 
G 1 37  GLY 37  37  37  GLY GLY G . n 
G 1 38  LEU 38  38  38  LEU LEU G . n 
G 1 39  THR 39  39  39  THR THR G . n 
G 1 40  GLU 40  40  40  GLU GLU G . n 
G 1 41  GLY 41  41  41  GLY GLY G . n 
G 1 42  LEU 42  42  42  LEU LEU G . n 
G 1 43  HIS 43  43  43  HIS HIS G . n 
G 1 44  GLY 44  44  44  GLY GLY G . n 
G 1 45  PHE 45  45  45  PHE PHE G . n 
G 1 46  HIS 46  46  46  HIS HIS G . n 
G 1 47  VAL 47  47  47  VAL VAL G . n 
G 1 48  HIS 48  48  48  HIS HIS G . n 
G 1 49  GLU 49  49  49  GLU GLU G . n 
G 1 50  PHE 50  50  50  PHE PHE G . n 
G 1 51  GLY 51  51  51  GLY GLY G . n 
G 1 52  ASP 52  52  52  ASP ASP G . n 
G 1 53  ASN 53  53  53  ASN ASN G . n 
G 1 54  THR 54  54  54  THR THR G . n 
G 1 55  ALA 55  55  55  ALA ALA G . n 
G 1 56  GLY 56  56  56  GLY GLY G . n 
G 1 57  CYS 57  57  57  CYS CYS G . n 
G 1 58  THR 58  58  58  THR THR G . n 
G 1 59  SER 59  59  59  SER SER G . n 
G 1 60  ALA 60  60  60  ALA ALA G . n 
G 1 61  GLY 61  61  61  GLY GLY G . n 
G 1 62  PRO 62  62  62  PRO PRO G . n 
G 1 63  HIS 63  63  63  HIS HIS G . n 
G 1 64  PHE 64  64  64  PHE PHE G . n 
G 1 65  ASN 65  65  65  ASN ASN G . n 
G 1 66  PRO 66  66  66  PRO PRO G . n 
G 1 67  LEU 67  67  67  LEU LEU G . n 
G 1 68  SER 68  68  68  SER SER G . n 
G 1 69  ARG 69  69  69  ARG ARG G . n 
G 1 70  LYS 70  70  70  LYS LYS G . n 
G 1 71  HIS 71  71  71  HIS HIS G . n 
G 1 72  GLY 72  72  72  GLY GLY G . n 
G 1 73  GLY 73  73  73  GLY GLY G . n 
G 1 74  PRO 74  74  74  PRO PRO G . n 
G 1 75  LYS 75  75  75  LYS LYS G . n 
G 1 76  ASP 76  76  76  ASP ASP G . n 
G 1 77  GLU 77  77  77  GLU GLU G . n 
G 1 78  GLU 78  78  78  GLU GLU G . n 
G 1 79  ARG 79  79  79  ARG ARG G . n 
G 1 80  HIS 80  80  80  HIS HIS G . n 
G 1 81  VAL 81  81  81  VAL VAL G . n 
G 1 82  GLY 82  82  82  GLY GLY G . n 
G 1 83  ASP 83  83  83  ASP ASP G . n 
G 1 84  LEU 84  84  84  LEU LEU G . n 
G 1 85  GLY 85  85  85  GLY GLY G . n 
G 1 86  ASN 86  86  86  ASN ASN G . n 
G 1 87  VAL 87  87  87  VAL VAL G . n 
G 1 88  THR 88  88  88  THR THR G . n 
G 1 89  ALA 89  89  89  ALA ALA G . n 
G 1 90  GLY 90  90  90  GLY GLY G . n 
G 1 91  LYS 91  91  91  LYS LYS G . n 
G 1 92  ASP 92  92  92  ASP ASP G . n 
G 1 93  GLY 93  93  93  GLY GLY G . n 
G 1 94  VAL 94  94  94  VAL VAL G . n 
G 1 95  ALA 95  95  95  ALA ALA G . n 
G 1 96  ASN 96  96  96  ASN ASN G . n 
G 1 97  VAL 97  97  97  VAL VAL G . n 
G 1 98  SER 98  98  98  SER SER G . n 
G 1 99  ILE 99  99  99  ILE ILE G . n 
G 1 100 GLU 100 100 100 GLU GLU G . n 
G 1 101 ASP 101 101 101 ASP ASP G . n 
G 1 102 ARG 102 102 102 ARG ARG G . n 
G 1 103 VAL 103 103 103 VAL VAL G . n 
G 1 104 ILE 104 104 104 ILE ILE G . n 
G 1 105 SER 105 105 105 SER SER G . n 
G 1 106 LEU 106 106 106 LEU LEU G . n 
G 1 107 SER 107 107 107 SER SER G . n 
G 1 108 GLY 108 108 108 GLY GLY G . n 
G 1 109 GLU 109 109 109 GLU GLU G . n 
G 1 110 HIS 110 110 110 HIS HIS G . n 
G 1 111 SER 111 111 111 SER SER G . n 
G 1 112 ILE 112 112 112 ILE ILE G . n 
G 1 113 ILE 113 113 113 ILE ILE G . n 
G 1 114 GLY 114 114 114 GLY GLY G . n 
G 1 115 ARG 115 115 115 ARG ARG G . n 
G 1 116 THR 116 116 116 THR THR G . n 
G 1 117 MET 117 117 117 MET MET G . n 
G 1 118 VAL 118 118 118 VAL VAL G . n 
G 1 119 VAL 119 119 119 VAL VAL G . n 
G 1 120 HIS 120 120 120 HIS HIS G . n 
G 1 121 GLU 121 121 121 GLU GLU G . n 
G 1 122 LYS 122 122 122 LYS LYS G . n 
G 1 123 GLN 123 123 123 GLN GLN G . n 
G 1 124 ASP 124 124 124 ASP ASP G . n 
G 1 125 ASP 125 125 125 ASP ASP G . n 
G 1 126 LEU 126 126 126 LEU LEU G . n 
G 1 127 GLY 127 127 127 GLY GLY G . n 
G 1 128 LYS 128 128 128 LYS LYS G . n 
G 1 129 GLY 129 129 129 GLY GLY G . n 
G 1 130 GLY 130 130 130 GLY GLY G . n 
G 1 131 ASN 131 131 131 ASN ASN G . n 
G 1 132 GLU 132 132 132 GLU GLU G . n 
G 1 133 GLU 133 133 133 GLU GLU G . n 
G 1 134 SER 134 134 134 SER SER G . n 
G 1 135 THR 135 135 135 THR THR G . n 
G 1 136 LYS 136 136 136 LYS LYS G . n 
G 1 137 THR 137 137 137 THR THR G . n 
G 1 138 GLY 138 138 138 GLY GLY G . n 
G 1 139 ASN 139 139 139 ASN ASN G . n 
G 1 140 ALA 140 140 140 ALA ALA G . n 
G 1 141 GLY 141 141 141 GLY GLY G . n 
G 1 142 SER 142 142 142 SER SER G . n 
G 1 143 ARG 143 143 143 ARG ARG G . n 
G 1 144 LEU 144 144 144 LEU LEU G . n 
G 1 145 ALA 145 145 145 ALA ALA G . n 
G 1 146 CYS 146 146 146 CYS CYS G . n 
G 1 147 GLY 147 147 147 GLY GLY G . n 
G 1 148 VAL 148 148 148 VAL VAL G . n 
G 1 149 ILE 149 149 149 ILE ILE G . n 
G 1 150 GLY 150 150 150 GLY GLY G . n 
G 1 151 ILE 151 151 151 ILE ILE G . n 
G 1 152 ALA 152 152 152 ALA ALA G . n 
G 1 153 GLN 153 153 153 GLN GLN G . n 
H 1 1   ALA 1   1   1   ALA ALA H . n 
H 1 2   THR 2   2   2   THR THR H . n 
H 1 3   LYS 3   3   3   LYS LYS H . n 
H 1 4   ALA 4   4   4   ALA ALA H . n 
H 1 5   VAL 5   5   5   VAL VAL H . n 
H 1 6   CYS 6   6   6   CYS CYS H . n 
H 1 7   VAL 7   7   7   VAL VAL H . n 
H 1 8   LEU 8   8   8   LEU LEU H . n 
H 1 9   LYS 9   9   9   LYS LYS H . n 
H 1 10  GLY 10  10  10  GLY GLY H . n 
H 1 11  ASP 11  11  11  ASP ASP H . n 
H 1 12  GLY 12  12  12  GLY GLY H . n 
H 1 13  PRO 13  13  13  PRO PRO H . n 
H 1 14  VAL 14  14  14  VAL VAL H . n 
H 1 15  GLN 15  15  15  GLN GLN H . n 
H 1 16  GLY 16  16  16  GLY GLY H . n 
H 1 17  ILE 17  17  17  ILE ILE H . n 
H 1 18  ILE 18  18  18  ILE ILE H . n 
H 1 19  ASN 19  19  19  ASN ASN H . n 
H 1 20  PHE 20  20  20  PHE PHE H . n 
H 1 21  GLU 21  21  21  GLU GLU H . n 
H 1 22  GLN 22  22  22  GLN GLN H . n 
H 1 23  LYS 23  23  23  LYS LYS H . n 
H 1 24  GLU 24  24  24  GLU GLU H . n 
H 1 25  SER 25  25  25  SER SER H . n 
H 1 26  ASN 26  26  26  ASN ASN H . n 
H 1 27  GLY 27  27  27  GLY GLY H . n 
H 1 28  PRO 28  28  28  PRO PRO H . n 
H 1 29  VAL 29  29  29  VAL VAL H . n 
H 1 30  LYS 30  30  30  LYS LYS H . n 
H 1 31  VAL 31  31  31  VAL VAL H . n 
H 1 32  TRP 32  32  32  TRP TRP H . n 
H 1 33  GLY 33  33  33  GLY GLY H . n 
H 1 34  SER 34  34  34  SER SER H . n 
H 1 35  ILE 35  35  35  ILE ILE H . n 
H 1 36  LYS 36  36  36  LYS LYS H . n 
H 1 37  GLY 37  37  37  GLY GLY H . n 
H 1 38  LEU 38  38  38  LEU LEU H . n 
H 1 39  THR 39  39  39  THR THR H . n 
H 1 40  GLU 40  40  40  GLU GLU H . n 
H 1 41  GLY 41  41  41  GLY GLY H . n 
H 1 42  LEU 42  42  42  LEU LEU H . n 
H 1 43  HIS 43  43  43  HIS HIS H . n 
H 1 44  GLY 44  44  44  GLY GLY H . n 
H 1 45  PHE 45  45  45  PHE PHE H . n 
H 1 46  HIS 46  46  46  HIS HIS H . n 
H 1 47  VAL 47  47  47  VAL VAL H . n 
H 1 48  HIS 48  48  48  HIS HIS H . n 
H 1 49  GLU 49  49  49  GLU GLU H . n 
H 1 50  PHE 50  50  50  PHE PHE H . n 
H 1 51  GLY 51  51  51  GLY GLY H . n 
H 1 52  ASP 52  52  52  ASP ASP H . n 
H 1 53  ASN 53  53  53  ASN ASN H . n 
H 1 54  THR 54  54  54  THR THR H . n 
H 1 55  ALA 55  55  55  ALA ALA H . n 
H 1 56  GLY 56  56  56  GLY GLY H . n 
H 1 57  CYS 57  57  57  CYS CYS H . n 
H 1 58  THR 58  58  58  THR THR H . n 
H 1 59  SER 59  59  59  SER SER H . n 
H 1 60  ALA 60  60  60  ALA ALA H . n 
H 1 61  GLY 61  61  61  GLY GLY H . n 
H 1 62  PRO 62  62  62  PRO PRO H . n 
H 1 63  HIS 63  63  63  HIS HIS H . n 
H 1 64  PHE 64  64  64  PHE PHE H . n 
H 1 65  ASN 65  65  65  ASN ASN H . n 
H 1 66  PRO 66  66  66  PRO PRO H . n 
H 1 67  LEU 67  67  67  LEU LEU H . n 
H 1 68  SER 68  68  68  SER SER H . n 
H 1 69  ARG 69  69  69  ARG ARG H . n 
H 1 70  LYS 70  70  70  LYS LYS H . n 
H 1 71  HIS 71  71  71  HIS HIS H . n 
H 1 72  GLY 72  72  72  GLY GLY H . n 
H 1 73  GLY 73  73  73  GLY GLY H . n 
H 1 74  PRO 74  74  74  PRO PRO H . n 
H 1 75  LYS 75  75  75  LYS LYS H . n 
H 1 76  ASP 76  76  76  ASP ASP H . n 
H 1 77  GLU 77  77  77  GLU GLU H . n 
H 1 78  GLU 78  78  78  GLU GLU H . n 
H 1 79  ARG 79  79  79  ARG ARG H . n 
H 1 80  HIS 80  80  80  HIS HIS H . n 
H 1 81  VAL 81  81  81  VAL VAL H . n 
H 1 82  GLY 82  82  82  GLY GLY H . n 
H 1 83  ASP 83  83  83  ASP ASP H . n 
H 1 84  LEU 84  84  84  LEU LEU H . n 
H 1 85  GLY 85  85  85  GLY GLY H . n 
H 1 86  ASN 86  86  86  ASN ASN H . n 
H 1 87  VAL 87  87  87  VAL VAL H . n 
H 1 88  THR 88  88  88  THR THR H . n 
H 1 89  ALA 89  89  89  ALA ALA H . n 
H 1 90  GLY 90  90  90  GLY GLY H . n 
H 1 91  LYS 91  91  91  LYS LYS H . n 
H 1 92  ASP 92  92  92  ASP ASP H . n 
H 1 93  GLY 93  93  93  GLY GLY H . n 
H 1 94  VAL 94  94  94  VAL VAL H . n 
H 1 95  ALA 95  95  95  ALA ALA H . n 
H 1 96  ASN 96  96  96  ASN ASN H . n 
H 1 97  VAL 97  97  97  VAL VAL H . n 
H 1 98  SER 98  98  98  SER SER H . n 
H 1 99  ILE 99  99  99  ILE ILE H . n 
H 1 100 GLU 100 100 100 GLU GLU H . n 
H 1 101 ASP 101 101 101 ASP ASP H . n 
H 1 102 ARG 102 102 102 ARG ARG H . n 
H 1 103 VAL 103 103 103 VAL VAL H . n 
H 1 104 ILE 104 104 104 ILE ILE H . n 
H 1 105 SER 105 105 105 SER SER H . n 
H 1 106 LEU 106 106 106 LEU LEU H . n 
H 1 107 SER 107 107 107 SER SER H . n 
H 1 108 GLY 108 108 108 GLY GLY H . n 
H 1 109 GLU 109 109 109 GLU GLU H . n 
H 1 110 HIS 110 110 110 HIS HIS H . n 
H 1 111 SER 111 111 111 SER SER H . n 
H 1 112 ILE 112 112 112 ILE ILE H . n 
H 1 113 ILE 113 113 113 ILE ILE H . n 
H 1 114 GLY 114 114 114 GLY GLY H . n 
H 1 115 ARG 115 115 115 ARG ARG H . n 
H 1 116 THR 116 116 116 THR THR H . n 
H 1 117 MET 117 117 117 MET MET H . n 
H 1 118 VAL 118 118 118 VAL VAL H . n 
H 1 119 VAL 119 119 119 VAL VAL H . n 
H 1 120 HIS 120 120 120 HIS HIS H . n 
H 1 121 GLU 121 121 121 GLU GLU H . n 
H 1 122 LYS 122 122 122 LYS LYS H . n 
H 1 123 GLN 123 123 123 GLN GLN H . n 
H 1 124 ASP 124 124 124 ASP ASP H . n 
H 1 125 ASP 125 125 125 ASP ASP H . n 
H 1 126 LEU 126 126 126 LEU LEU H . n 
H 1 127 GLY 127 127 127 GLY GLY H . n 
H 1 128 LYS 128 128 128 LYS LYS H . n 
H 1 129 GLY 129 129 129 GLY GLY H . n 
H 1 130 GLY 130 130 130 GLY GLY H . n 
H 1 131 ASN 131 131 131 ASN ASN H . n 
H 1 132 GLU 132 132 132 GLU GLU H . n 
H 1 133 GLU 133 133 133 GLU GLU H . n 
H 1 134 SER 134 134 134 SER SER H . n 
H 1 135 THR 135 135 135 THR THR H . n 
H 1 136 LYS 136 136 136 LYS LYS H . n 
H 1 137 THR 137 137 137 THR THR H . n 
H 1 138 GLY 138 138 138 GLY GLY H . n 
H 1 139 ASN 139 139 139 ASN ASN H . n 
H 1 140 ALA 140 140 140 ALA ALA H . n 
H 1 141 GLY 141 141 141 GLY GLY H . n 
H 1 142 SER 142 142 142 SER SER H . n 
H 1 143 ARG 143 143 143 ARG ARG H . n 
H 1 144 LEU 144 144 144 LEU LEU H . n 
H 1 145 ALA 145 145 145 ALA ALA H . n 
H 1 146 CYS 146 146 146 CYS CYS H . n 
H 1 147 GLY 147 147 147 GLY GLY H . n 
H 1 148 VAL 148 148 148 VAL VAL H . n 
H 1 149 ILE 149 149 149 ILE ILE H . n 
H 1 150 GLY 150 150 150 GLY GLY H . n 
H 1 151 ILE 151 151 151 ILE ILE H . n 
H 1 152 ALA 152 152 152 ALA ALA H . n 
H 1 153 GLN 153 153 153 GLN GLN H . n 
I 1 1   ALA 1   1   1   ALA ALA I . n 
I 1 2   THR 2   2   2   THR THR I . n 
I 1 3   LYS 3   3   3   LYS LYS I . n 
I 1 4   ALA 4   4   4   ALA ALA I . n 
I 1 5   VAL 5   5   5   VAL VAL I . n 
I 1 6   CYS 6   6   6   CYS CYS I . n 
I 1 7   VAL 7   7   7   VAL VAL I . n 
I 1 8   LEU 8   8   8   LEU LEU I . n 
I 1 9   LYS 9   9   9   LYS LYS I . n 
I 1 10  GLY 10  10  10  GLY GLY I . n 
I 1 11  ASP 11  11  11  ASP ASP I . n 
I 1 12  GLY 12  12  12  GLY GLY I . n 
I 1 13  PRO 13  13  13  PRO PRO I . n 
I 1 14  VAL 14  14  14  VAL VAL I . n 
I 1 15  GLN 15  15  15  GLN GLN I . n 
I 1 16  GLY 16  16  16  GLY GLY I . n 
I 1 17  ILE 17  17  17  ILE ILE I . n 
I 1 18  ILE 18  18  18  ILE ILE I . n 
I 1 19  ASN 19  19  19  ASN ASN I . n 
I 1 20  PHE 20  20  20  PHE PHE I . n 
I 1 21  GLU 21  21  21  GLU GLU I . n 
I 1 22  GLN 22  22  22  GLN GLN I . n 
I 1 23  LYS 23  23  23  LYS LYS I . n 
I 1 24  GLU 24  24  24  GLU GLU I . n 
I 1 25  SER 25  25  25  SER SER I . n 
I 1 26  ASN 26  26  26  ASN ASN I . n 
I 1 27  GLY 27  27  27  GLY GLY I . n 
I 1 28  PRO 28  28  28  PRO PRO I . n 
I 1 29  VAL 29  29  29  VAL VAL I . n 
I 1 30  LYS 30  30  30  LYS LYS I . n 
I 1 31  VAL 31  31  31  VAL VAL I . n 
I 1 32  TRP 32  32  32  TRP TRP I . n 
I 1 33  GLY 33  33  33  GLY GLY I . n 
I 1 34  SER 34  34  34  SER SER I . n 
I 1 35  ILE 35  35  35  ILE ILE I . n 
I 1 36  LYS 36  36  36  LYS LYS I . n 
I 1 37  GLY 37  37  37  GLY GLY I . n 
I 1 38  LEU 38  38  38  LEU LEU I . n 
I 1 39  THR 39  39  39  THR THR I . n 
I 1 40  GLU 40  40  40  GLU GLU I . n 
I 1 41  GLY 41  41  41  GLY GLY I . n 
I 1 42  LEU 42  42  42  LEU LEU I . n 
I 1 43  HIS 43  43  43  HIS HIS I . n 
I 1 44  GLY 44  44  44  GLY GLY I . n 
I 1 45  PHE 45  45  45  PHE PHE I . n 
I 1 46  HIS 46  46  46  HIS HIS I . n 
I 1 47  VAL 47  47  47  VAL VAL I . n 
I 1 48  HIS 48  48  48  HIS HIS I . n 
I 1 49  GLU 49  49  49  GLU GLU I . n 
I 1 50  PHE 50  50  50  PHE PHE I . n 
I 1 51  GLY 51  51  51  GLY GLY I . n 
I 1 52  ASP 52  52  52  ASP ASP I . n 
I 1 53  ASN 53  53  53  ASN ASN I . n 
I 1 54  THR 54  54  54  THR THR I . n 
I 1 55  ALA 55  55  55  ALA ALA I . n 
I 1 56  GLY 56  56  56  GLY GLY I . n 
I 1 57  CYS 57  57  57  CYS CYS I . n 
I 1 58  THR 58  58  58  THR THR I . n 
I 1 59  SER 59  59  59  SER SER I . n 
I 1 60  ALA 60  60  60  ALA ALA I . n 
I 1 61  GLY 61  61  61  GLY GLY I . n 
I 1 62  PRO 62  62  62  PRO PRO I . n 
I 1 63  HIS 63  63  63  HIS HIS I . n 
I 1 64  PHE 64  64  64  PHE PHE I . n 
I 1 65  ASN 65  65  65  ASN ASN I . n 
I 1 66  PRO 66  66  66  PRO PRO I . n 
I 1 67  LEU 67  67  67  LEU LEU I . n 
I 1 68  SER 68  68  68  SER SER I . n 
I 1 69  ARG 69  69  69  ARG ARG I . n 
I 1 70  LYS 70  70  70  LYS LYS I . n 
I 1 71  HIS 71  71  71  HIS HIS I . n 
I 1 72  GLY 72  72  72  GLY GLY I . n 
I 1 73  GLY 73  73  73  GLY GLY I . n 
I 1 74  PRO 74  74  74  PRO PRO I . n 
I 1 75  LYS 75  75  75  LYS LYS I . n 
I 1 76  ASP 76  76  76  ASP ASP I . n 
I 1 77  GLU 77  77  77  GLU GLU I . n 
I 1 78  GLU 78  78  78  GLU GLU I . n 
I 1 79  ARG 79  79  79  ARG ARG I . n 
I 1 80  HIS 80  80  80  HIS HIS I . n 
I 1 81  VAL 81  81  81  VAL VAL I . n 
I 1 82  GLY 82  82  82  GLY GLY I . n 
I 1 83  ASP 83  83  83  ASP ASP I . n 
I 1 84  LEU 84  84  84  LEU LEU I . n 
I 1 85  GLY 85  85  85  GLY GLY I . n 
I 1 86  ASN 86  86  86  ASN ASN I . n 
I 1 87  VAL 87  87  87  VAL VAL I . n 
I 1 88  THR 88  88  88  THR THR I . n 
I 1 89  ALA 89  89  89  ALA ALA I . n 
I 1 90  GLY 90  90  90  GLY GLY I . n 
I 1 91  LYS 91  91  91  LYS LYS I . n 
I 1 92  ASP 92  92  92  ASP ASP I . n 
I 1 93  GLY 93  93  93  GLY GLY I . n 
I 1 94  VAL 94  94  94  VAL VAL I . n 
I 1 95  ALA 95  95  95  ALA ALA I . n 
I 1 96  ASN 96  96  96  ASN ASN I . n 
I 1 97  VAL 97  97  97  VAL VAL I . n 
I 1 98  SER 98  98  98  SER SER I . n 
I 1 99  ILE 99  99  99  ILE ILE I . n 
I 1 100 GLU 100 100 100 GLU GLU I . n 
I 1 101 ASP 101 101 101 ASP ASP I . n 
I 1 102 ARG 102 102 102 ARG ARG I . n 
I 1 103 VAL 103 103 103 VAL VAL I . n 
I 1 104 ILE 104 104 104 ILE ILE I . n 
I 1 105 SER 105 105 105 SER SER I . n 
I 1 106 LEU 106 106 106 LEU LEU I . n 
I 1 107 SER 107 107 107 SER SER I . n 
I 1 108 GLY 108 108 108 GLY GLY I . n 
I 1 109 GLU 109 109 109 GLU GLU I . n 
I 1 110 HIS 110 110 110 HIS HIS I . n 
I 1 111 SER 111 111 111 SER SER I . n 
I 1 112 ILE 112 112 112 ILE ILE I . n 
I 1 113 ILE 113 113 113 ILE ILE I . n 
I 1 114 GLY 114 114 114 GLY GLY I . n 
I 1 115 ARG 115 115 115 ARG ARG I . n 
I 1 116 THR 116 116 116 THR THR I . n 
I 1 117 MET 117 117 117 MET MET I . n 
I 1 118 VAL 118 118 118 VAL VAL I . n 
I 1 119 VAL 119 119 119 VAL VAL I . n 
I 1 120 HIS 120 120 120 HIS HIS I . n 
I 1 121 GLU 121 121 121 GLU GLU I . n 
I 1 122 LYS 122 122 122 LYS LYS I . n 
I 1 123 GLN 123 123 123 GLN GLN I . n 
I 1 124 ASP 124 124 124 ASP ASP I . n 
I 1 125 ASP 125 125 125 ASP ASP I . n 
I 1 126 LEU 126 126 126 LEU LEU I . n 
I 1 127 GLY 127 127 127 GLY GLY I . n 
I 1 128 LYS 128 128 128 LYS LYS I . n 
I 1 129 GLY 129 129 129 GLY GLY I . n 
I 1 130 GLY 130 130 130 GLY GLY I . n 
I 1 131 ASN 131 131 131 ASN ASN I . n 
I 1 132 GLU 132 132 132 GLU GLU I . n 
I 1 133 GLU 133 133 133 GLU GLU I . n 
I 1 134 SER 134 134 134 SER SER I . n 
I 1 135 THR 135 135 135 THR THR I . n 
I 1 136 LYS 136 136 136 LYS LYS I . n 
I 1 137 THR 137 137 137 THR THR I . n 
I 1 138 GLY 138 138 138 GLY GLY I . n 
I 1 139 ASN 139 139 139 ASN ASN I . n 
I 1 140 ALA 140 140 140 ALA ALA I . n 
I 1 141 GLY 141 141 141 GLY GLY I . n 
I 1 142 SER 142 142 142 SER SER I . n 
I 1 143 ARG 143 143 143 ARG ARG I . n 
I 1 144 LEU 144 144 144 LEU LEU I . n 
I 1 145 ALA 145 145 145 ALA ALA I . n 
I 1 146 CYS 146 146 146 CYS CYS I . n 
I 1 147 GLY 147 147 147 GLY GLY I . n 
I 1 148 VAL 148 148 148 VAL VAL I . n 
I 1 149 ILE 149 149 149 ILE ILE I . n 
I 1 150 GLY 150 150 150 GLY GLY I . n 
I 1 151 ILE 151 151 151 ILE ILE I . n 
I 1 152 ALA 152 152 152 ALA ALA I . n 
I 1 153 GLN 153 153 153 GLN GLN I . n 
J 1 1   ALA 1   1   1   ALA ALA J . n 
J 1 2   THR 2   2   2   THR THR J . n 
J 1 3   LYS 3   3   3   LYS LYS J . n 
J 1 4   ALA 4   4   4   ALA ALA J . n 
J 1 5   VAL 5   5   5   VAL VAL J . n 
J 1 6   CYS 6   6   6   CYS CYS J . n 
J 1 7   VAL 7   7   7   VAL VAL J . n 
J 1 8   LEU 8   8   8   LEU LEU J . n 
J 1 9   LYS 9   9   9   LYS LYS J . n 
J 1 10  GLY 10  10  10  GLY GLY J . n 
J 1 11  ASP 11  11  11  ASP ASP J . n 
J 1 12  GLY 12  12  12  GLY GLY J . n 
J 1 13  PRO 13  13  13  PRO PRO J . n 
J 1 14  VAL 14  14  14  VAL VAL J . n 
J 1 15  GLN 15  15  15  GLN GLN J . n 
J 1 16  GLY 16  16  16  GLY GLY J . n 
J 1 17  ILE 17  17  17  ILE ILE J . n 
J 1 18  ILE 18  18  18  ILE ILE J . n 
J 1 19  ASN 19  19  19  ASN ASN J . n 
J 1 20  PHE 20  20  20  PHE PHE J . n 
J 1 21  GLU 21  21  21  GLU GLU J . n 
J 1 22  GLN 22  22  22  GLN GLN J . n 
J 1 23  LYS 23  23  23  LYS LYS J . n 
J 1 24  GLU 24  24  24  GLU GLU J . n 
J 1 25  SER 25  25  25  SER SER J . n 
J 1 26  ASN 26  26  26  ASN ASN J . n 
J 1 27  GLY 27  27  27  GLY GLY J . n 
J 1 28  PRO 28  28  28  PRO PRO J . n 
J 1 29  VAL 29  29  29  VAL VAL J . n 
J 1 30  LYS 30  30  30  LYS LYS J . n 
J 1 31  VAL 31  31  31  VAL VAL J . n 
J 1 32  TRP 32  32  32  TRP TRP J . n 
J 1 33  GLY 33  33  33  GLY GLY J . n 
J 1 34  SER 34  34  34  SER SER J . n 
J 1 35  ILE 35  35  35  ILE ILE J . n 
J 1 36  LYS 36  36  36  LYS LYS J . n 
J 1 37  GLY 37  37  37  GLY GLY J . n 
J 1 38  LEU 38  38  38  LEU LEU J . n 
J 1 39  THR 39  39  39  THR THR J . n 
J 1 40  GLU 40  40  40  GLU GLU J . n 
J 1 41  GLY 41  41  41  GLY GLY J . n 
J 1 42  LEU 42  42  42  LEU LEU J . n 
J 1 43  HIS 43  43  43  HIS HIS J . n 
J 1 44  GLY 44  44  44  GLY GLY J . n 
J 1 45  PHE 45  45  45  PHE PHE J . n 
J 1 46  HIS 46  46  46  HIS HIS J . n 
J 1 47  VAL 47  47  47  VAL VAL J . n 
J 1 48  HIS 48  48  48  HIS HIS J . n 
J 1 49  GLU 49  49  49  GLU GLU J . n 
J 1 50  PHE 50  50  50  PHE PHE J . n 
J 1 51  GLY 51  51  51  GLY GLY J . n 
J 1 52  ASP 52  52  52  ASP ASP J . n 
J 1 53  ASN 53  53  53  ASN ASN J . n 
J 1 54  THR 54  54  54  THR THR J . n 
J 1 55  ALA 55  55  55  ALA ALA J . n 
J 1 56  GLY 56  56  56  GLY GLY J . n 
J 1 57  CYS 57  57  57  CYS CYS J . n 
J 1 58  THR 58  58  58  THR THR J . n 
J 1 59  SER 59  59  59  SER SER J . n 
J 1 60  ALA 60  60  60  ALA ALA J . n 
J 1 61  GLY 61  61  61  GLY GLY J . n 
J 1 62  PRO 62  62  62  PRO PRO J . n 
J 1 63  HIS 63  63  63  HIS HIS J . n 
J 1 64  PHE 64  64  64  PHE PHE J . n 
J 1 65  ASN 65  65  65  ASN ASN J . n 
J 1 66  PRO 66  66  66  PRO PRO J . n 
J 1 67  LEU 67  67  67  LEU LEU J . n 
J 1 68  SER 68  68  68  SER SER J . n 
J 1 69  ARG 69  69  69  ARG ARG J . n 
J 1 70  LYS 70  70  70  LYS LYS J . n 
J 1 71  HIS 71  71  71  HIS HIS J . n 
J 1 72  GLY 72  72  72  GLY GLY J . n 
J 1 73  GLY 73  73  73  GLY GLY J . n 
J 1 74  PRO 74  74  74  PRO PRO J . n 
J 1 75  LYS 75  75  75  LYS LYS J . n 
J 1 76  ASP 76  76  76  ASP ASP J . n 
J 1 77  GLU 77  77  77  GLU GLU J . n 
J 1 78  GLU 78  78  78  GLU GLU J . n 
J 1 79  ARG 79  79  79  ARG ARG J . n 
J 1 80  HIS 80  80  80  HIS HIS J . n 
J 1 81  VAL 81  81  81  VAL VAL J . n 
J 1 82  GLY 82  82  82  GLY GLY J . n 
J 1 83  ASP 83  83  83  ASP ASP J . n 
J 1 84  LEU 84  84  84  LEU LEU J . n 
J 1 85  GLY 85  85  85  GLY GLY J . n 
J 1 86  ASN 86  86  86  ASN ASN J . n 
J 1 87  VAL 87  87  87  VAL VAL J . n 
J 1 88  THR 88  88  88  THR THR J . n 
J 1 89  ALA 89  89  89  ALA ALA J . n 
J 1 90  GLY 90  90  90  GLY GLY J . n 
J 1 91  LYS 91  91  91  LYS LYS J . n 
J 1 92  ASP 92  92  92  ASP ASP J . n 
J 1 93  GLY 93  93  93  GLY GLY J . n 
J 1 94  VAL 94  94  94  VAL VAL J . n 
J 1 95  ALA 95  95  95  ALA ALA J . n 
J 1 96  ASN 96  96  96  ASN ASN J . n 
J 1 97  VAL 97  97  97  VAL VAL J . n 
J 1 98  SER 98  98  98  SER SER J . n 
J 1 99  ILE 99  99  99  ILE ILE J . n 
J 1 100 GLU 100 100 100 GLU GLU J . n 
J 1 101 ASP 101 101 101 ASP ASP J . n 
J 1 102 ARG 102 102 102 ARG ARG J . n 
J 1 103 VAL 103 103 103 VAL VAL J . n 
J 1 104 ILE 104 104 104 ILE ILE J . n 
J 1 105 SER 105 105 105 SER SER J . n 
J 1 106 LEU 106 106 106 LEU LEU J . n 
J 1 107 SER 107 107 107 SER SER J . n 
J 1 108 GLY 108 108 108 GLY GLY J . n 
J 1 109 GLU 109 109 109 GLU GLU J . n 
J 1 110 HIS 110 110 110 HIS HIS J . n 
J 1 111 SER 111 111 111 SER SER J . n 
J 1 112 ILE 112 112 112 ILE ILE J . n 
J 1 113 ILE 113 113 113 ILE ILE J . n 
J 1 114 GLY 114 114 114 GLY GLY J . n 
J 1 115 ARG 115 115 115 ARG ARG J . n 
J 1 116 THR 116 116 116 THR THR J . n 
J 1 117 MET 117 117 117 MET MET J . n 
J 1 118 VAL 118 118 118 VAL VAL J . n 
J 1 119 VAL 119 119 119 VAL VAL J . n 
J 1 120 HIS 120 120 120 HIS HIS J . n 
J 1 121 GLU 121 121 121 GLU GLU J . n 
J 1 122 LYS 122 122 122 LYS LYS J . n 
J 1 123 GLN 123 123 123 GLN GLN J . n 
J 1 124 ASP 124 124 124 ASP ASP J . n 
J 1 125 ASP 125 125 125 ASP ASP J . n 
J 1 126 LEU 126 126 126 LEU LEU J . n 
J 1 127 GLY 127 127 127 GLY GLY J . n 
J 1 128 LYS 128 128 128 LYS LYS J . n 
J 1 129 GLY 129 129 129 GLY GLY J . n 
J 1 130 GLY 130 130 130 GLY GLY J . n 
J 1 131 ASN 131 131 131 ASN ASN J . n 
J 1 132 GLU 132 132 132 GLU GLU J . n 
J 1 133 GLU 133 133 133 GLU GLU J . n 
J 1 134 SER 134 134 134 SER SER J . n 
J 1 135 THR 135 135 135 THR THR J . n 
J 1 136 LYS 136 136 136 LYS LYS J . n 
J 1 137 THR 137 137 137 THR THR J . n 
J 1 138 GLY 138 138 138 GLY GLY J . n 
J 1 139 ASN 139 139 139 ASN ASN J . n 
J 1 140 ALA 140 140 140 ALA ALA J . n 
J 1 141 GLY 141 141 141 GLY GLY J . n 
J 1 142 SER 142 142 142 SER SER J . n 
J 1 143 ARG 143 143 143 ARG ARG J . n 
J 1 144 LEU 144 144 144 LEU LEU J . n 
J 1 145 ALA 145 145 145 ALA ALA J . n 
J 1 146 CYS 146 146 146 CYS CYS J . n 
J 1 147 GLY 147 147 147 GLY GLY J . n 
J 1 148 VAL 148 148 148 VAL VAL J . n 
J 1 149 ILE 149 149 149 ILE ILE J . n 
J 1 150 GLY 150 150 150 GLY GLY J . n 
J 1 151 ILE 151 151 151 ILE ILE J . n 
J 1 152 ALA 152 152 152 ALA ALA J . n 
J 1 153 GLN 153 153 153 GLN GLN J . n 
K 1 1   ALA 1   1   1   ALA ALA K . n 
K 1 2   THR 2   2   2   THR THR K . n 
K 1 3   LYS 3   3   3   LYS LYS K . n 
K 1 4   ALA 4   4   4   ALA ALA K . n 
K 1 5   VAL 5   5   5   VAL VAL K . n 
K 1 6   CYS 6   6   6   CYS CYS K . n 
K 1 7   VAL 7   7   7   VAL VAL K . n 
K 1 8   LEU 8   8   8   LEU LEU K . n 
K 1 9   LYS 9   9   9   LYS LYS K . n 
K 1 10  GLY 10  10  10  GLY GLY K . n 
K 1 11  ASP 11  11  11  ASP ASP K . n 
K 1 12  GLY 12  12  12  GLY GLY K . n 
K 1 13  PRO 13  13  13  PRO PRO K . n 
K 1 14  VAL 14  14  14  VAL VAL K . n 
K 1 15  GLN 15  15  15  GLN GLN K . n 
K 1 16  GLY 16  16  16  GLY GLY K . n 
K 1 17  ILE 17  17  17  ILE ILE K . n 
K 1 18  ILE 18  18  18  ILE ILE K . n 
K 1 19  ASN 19  19  19  ASN ASN K . n 
K 1 20  PHE 20  20  20  PHE PHE K . n 
K 1 21  GLU 21  21  21  GLU GLU K . n 
K 1 22  GLN 22  22  22  GLN GLN K . n 
K 1 23  LYS 23  23  23  LYS LYS K . n 
K 1 24  GLU 24  24  24  GLU GLU K . n 
K 1 25  SER 25  25  25  SER SER K . n 
K 1 26  ASN 26  26  26  ASN ASN K . n 
K 1 27  GLY 27  27  27  GLY GLY K . n 
K 1 28  PRO 28  28  28  PRO PRO K . n 
K 1 29  VAL 29  29  29  VAL VAL K . n 
K 1 30  LYS 30  30  30  LYS LYS K . n 
K 1 31  VAL 31  31  31  VAL VAL K . n 
K 1 32  TRP 32  32  32  TRP TRP K . n 
K 1 33  GLY 33  33  33  GLY GLY K . n 
K 1 34  SER 34  34  34  SER SER K . n 
K 1 35  ILE 35  35  35  ILE ILE K . n 
K 1 36  LYS 36  36  36  LYS LYS K . n 
K 1 37  GLY 37  37  37  GLY GLY K . n 
K 1 38  LEU 38  38  38  LEU LEU K . n 
K 1 39  THR 39  39  39  THR THR K . n 
K 1 40  GLU 40  40  40  GLU GLU K . n 
K 1 41  GLY 41  41  41  GLY GLY K . n 
K 1 42  LEU 42  42  42  LEU LEU K . n 
K 1 43  HIS 43  43  43  HIS HIS K . n 
K 1 44  GLY 44  44  44  GLY GLY K . n 
K 1 45  PHE 45  45  45  PHE PHE K . n 
K 1 46  HIS 46  46  46  HIS HIS K . n 
K 1 47  VAL 47  47  47  VAL VAL K . n 
K 1 48  HIS 48  48  48  HIS HIS K . n 
K 1 49  GLU 49  49  49  GLU GLU K . n 
K 1 50  PHE 50  50  50  PHE PHE K . n 
K 1 51  GLY 51  51  51  GLY GLY K . n 
K 1 52  ASP 52  52  52  ASP ASP K . n 
K 1 53  ASN 53  53  53  ASN ASN K . n 
K 1 54  THR 54  54  54  THR THR K . n 
K 1 55  ALA 55  55  55  ALA ALA K . n 
K 1 56  GLY 56  56  56  GLY GLY K . n 
K 1 57  CYS 57  57  57  CYS CYS K . n 
K 1 58  THR 58  58  58  THR THR K . n 
K 1 59  SER 59  59  59  SER SER K . n 
K 1 60  ALA 60  60  60  ALA ALA K . n 
K 1 61  GLY 61  61  61  GLY GLY K . n 
K 1 62  PRO 62  62  62  PRO PRO K . n 
K 1 63  HIS 63  63  63  HIS HIS K . n 
K 1 64  PHE 64  64  64  PHE PHE K . n 
K 1 65  ASN 65  65  65  ASN ASN K . n 
K 1 66  PRO 66  66  66  PRO PRO K . n 
K 1 67  LEU 67  67  67  LEU LEU K . n 
K 1 68  SER 68  68  68  SER SER K . n 
K 1 69  ARG 69  69  69  ARG ARG K . n 
K 1 70  LYS 70  70  70  LYS LYS K . n 
K 1 71  HIS 71  71  71  HIS HIS K . n 
K 1 72  GLY 72  72  72  GLY GLY K . n 
K 1 73  GLY 73  73  73  GLY GLY K . n 
K 1 74  PRO 74  74  74  PRO PRO K . n 
K 1 75  LYS 75  75  75  LYS LYS K . n 
K 1 76  ASP 76  76  76  ASP ASP K . n 
K 1 77  GLU 77  77  77  GLU GLU K . n 
K 1 78  GLU 78  78  78  GLU GLU K . n 
K 1 79  ARG 79  79  79  ARG ARG K . n 
K 1 80  HIS 80  80  80  HIS HIS K . n 
K 1 81  VAL 81  81  81  VAL VAL K . n 
K 1 82  GLY 82  82  82  GLY GLY K . n 
K 1 83  ASP 83  83  83  ASP ASP K . n 
K 1 84  LEU 84  84  84  LEU LEU K . n 
K 1 85  GLY 85  85  85  GLY GLY K . n 
K 1 86  ASN 86  86  86  ASN ASN K . n 
K 1 87  VAL 87  87  87  VAL VAL K . n 
K 1 88  THR 88  88  88  THR THR K . n 
K 1 89  ALA 89  89  89  ALA ALA K . n 
K 1 90  GLY 90  90  90  GLY GLY K . n 
K 1 91  LYS 91  91  91  LYS LYS K . n 
K 1 92  ASP 92  92  92  ASP ASP K . n 
K 1 93  GLY 93  93  93  GLY GLY K . n 
K 1 94  VAL 94  94  94  VAL VAL K . n 
K 1 95  ALA 95  95  95  ALA ALA K . n 
K 1 96  ASN 96  96  96  ASN ASN K . n 
K 1 97  VAL 97  97  97  VAL VAL K . n 
K 1 98  SER 98  98  98  SER SER K . n 
K 1 99  ILE 99  99  99  ILE ILE K . n 
K 1 100 GLU 100 100 100 GLU GLU K . n 
K 1 101 ASP 101 101 101 ASP ASP K . n 
K 1 102 ARG 102 102 102 ARG ARG K . n 
K 1 103 VAL 103 103 103 VAL VAL K . n 
K 1 104 ILE 104 104 104 ILE ILE K . n 
K 1 105 SER 105 105 105 SER SER K . n 
K 1 106 LEU 106 106 106 LEU LEU K . n 
K 1 107 SER 107 107 107 SER SER K . n 
K 1 108 GLY 108 108 108 GLY GLY K . n 
K 1 109 GLU 109 109 109 GLU GLU K . n 
K 1 110 HIS 110 110 110 HIS HIS K . n 
K 1 111 SER 111 111 111 SER SER K . n 
K 1 112 ILE 112 112 112 ILE ILE K . n 
K 1 113 ILE 113 113 113 ILE ILE K . n 
K 1 114 GLY 114 114 114 GLY GLY K . n 
K 1 115 ARG 115 115 115 ARG ARG K . n 
K 1 116 THR 116 116 116 THR THR K . n 
K 1 117 MET 117 117 117 MET MET K . n 
K 1 118 VAL 118 118 118 VAL VAL K . n 
K 1 119 VAL 119 119 119 VAL VAL K . n 
K 1 120 HIS 120 120 120 HIS HIS K . n 
K 1 121 GLU 121 121 121 GLU GLU K . n 
K 1 122 LYS 122 122 122 LYS LYS K . n 
K 1 123 GLN 123 123 123 GLN GLN K . n 
K 1 124 ASP 124 124 124 ASP ASP K . n 
K 1 125 ASP 125 125 125 ASP ASP K . n 
K 1 126 LEU 126 126 126 LEU LEU K . n 
K 1 127 GLY 127 127 127 GLY GLY K . n 
K 1 128 LYS 128 128 128 LYS LYS K . n 
K 1 129 GLY 129 129 129 GLY GLY K . n 
K 1 130 GLY 130 130 130 GLY GLY K . n 
K 1 131 ASN 131 131 131 ASN ASN K . n 
K 1 132 GLU 132 132 132 GLU GLU K . n 
K 1 133 GLU 133 133 133 GLU GLU K . n 
K 1 134 SER 134 134 134 SER SER K . n 
K 1 135 THR 135 135 135 THR THR K . n 
K 1 136 LYS 136 136 136 LYS LYS K . n 
K 1 137 THR 137 137 137 THR THR K . n 
K 1 138 GLY 138 138 138 GLY GLY K . n 
K 1 139 ASN 139 139 139 ASN ASN K . n 
K 1 140 ALA 140 140 140 ALA ALA K . n 
K 1 141 GLY 141 141 141 GLY GLY K . n 
K 1 142 SER 142 142 142 SER SER K . n 
K 1 143 ARG 143 143 143 ARG ARG K . n 
K 1 144 LEU 144 144 144 LEU LEU K . n 
K 1 145 ALA 145 145 145 ALA ALA K . n 
K 1 146 CYS 146 146 146 CYS CYS K . n 
K 1 147 GLY 147 147 147 GLY GLY K . n 
K 1 148 VAL 148 148 148 VAL VAL K . n 
K 1 149 ILE 149 149 149 ILE ILE K . n 
K 1 150 GLY 150 150 150 GLY GLY K . n 
K 1 151 ILE 151 151 151 ILE ILE K . n 
K 1 152 ALA 152 152 152 ALA ALA K . n 
K 1 153 GLN 153 153 153 GLN GLN K . n 
L 1 1   ALA 1   1   1   ALA ALA L . n 
L 1 2   THR 2   2   2   THR THR L . n 
L 1 3   LYS 3   3   3   LYS LYS L . n 
L 1 4   ALA 4   4   4   ALA ALA L . n 
L 1 5   VAL 5   5   5   VAL VAL L . n 
L 1 6   CYS 6   6   6   CYS CYS L . n 
L 1 7   VAL 7   7   7   VAL VAL L . n 
L 1 8   LEU 8   8   8   LEU LEU L . n 
L 1 9   LYS 9   9   9   LYS LYS L . n 
L 1 10  GLY 10  10  10  GLY GLY L . n 
L 1 11  ASP 11  11  11  ASP ASP L . n 
L 1 12  GLY 12  12  12  GLY GLY L . n 
L 1 13  PRO 13  13  13  PRO PRO L . n 
L 1 14  VAL 14  14  14  VAL VAL L . n 
L 1 15  GLN 15  15  15  GLN GLN L . n 
L 1 16  GLY 16  16  16  GLY GLY L . n 
L 1 17  ILE 17  17  17  ILE ILE L . n 
L 1 18  ILE 18  18  18  ILE ILE L . n 
L 1 19  ASN 19  19  19  ASN ASN L . n 
L 1 20  PHE 20  20  20  PHE PHE L . n 
L 1 21  GLU 21  21  21  GLU GLU L . n 
L 1 22  GLN 22  22  22  GLN GLN L . n 
L 1 23  LYS 23  23  23  LYS LYS L . n 
L 1 24  GLU 24  24  24  GLU GLU L . n 
L 1 25  SER 25  25  25  SER SER L . n 
L 1 26  ASN 26  26  26  ASN ASN L . n 
L 1 27  GLY 27  27  27  GLY GLY L . n 
L 1 28  PRO 28  28  28  PRO PRO L . n 
L 1 29  VAL 29  29  29  VAL VAL L . n 
L 1 30  LYS 30  30  30  LYS LYS L . n 
L 1 31  VAL 31  31  31  VAL VAL L . n 
L 1 32  TRP 32  32  32  TRP TRP L . n 
L 1 33  GLY 33  33  33  GLY GLY L . n 
L 1 34  SER 34  34  34  SER SER L . n 
L 1 35  ILE 35  35  35  ILE ILE L . n 
L 1 36  LYS 36  36  36  LYS LYS L . n 
L 1 37  GLY 37  37  37  GLY GLY L . n 
L 1 38  LEU 38  38  38  LEU LEU L . n 
L 1 39  THR 39  39  39  THR THR L . n 
L 1 40  GLU 40  40  40  GLU GLU L . n 
L 1 41  GLY 41  41  41  GLY GLY L . n 
L 1 42  LEU 42  42  42  LEU LEU L . n 
L 1 43  HIS 43  43  43  HIS HIS L . n 
L 1 44  GLY 44  44  44  GLY GLY L . n 
L 1 45  PHE 45  45  45  PHE PHE L . n 
L 1 46  HIS 46  46  46  HIS HIS L . n 
L 1 47  VAL 47  47  47  VAL VAL L . n 
L 1 48  HIS 48  48  48  HIS HIS L . n 
L 1 49  GLU 49  49  49  GLU GLU L . n 
L 1 50  PHE 50  50  50  PHE PHE L . n 
L 1 51  GLY 51  51  51  GLY GLY L . n 
L 1 52  ASP 52  52  52  ASP ASP L . n 
L 1 53  ASN 53  53  53  ASN ASN L . n 
L 1 54  THR 54  54  54  THR THR L . n 
L 1 55  ALA 55  55  55  ALA ALA L . n 
L 1 56  GLY 56  56  56  GLY GLY L . n 
L 1 57  CYS 57  57  57  CYS CYS L . n 
L 1 58  THR 58  58  58  THR THR L . n 
L 1 59  SER 59  59  59  SER SER L . n 
L 1 60  ALA 60  60  60  ALA ALA L . n 
L 1 61  GLY 61  61  61  GLY GLY L . n 
L 1 62  PRO 62  62  62  PRO PRO L . n 
L 1 63  HIS 63  63  63  HIS HIS L . n 
L 1 64  PHE 64  64  64  PHE PHE L . n 
L 1 65  ASN 65  65  65  ASN ASN L . n 
L 1 66  PRO 66  66  66  PRO PRO L . n 
L 1 67  LEU 67  67  67  LEU LEU L . n 
L 1 68  SER 68  68  68  SER SER L . n 
L 1 69  ARG 69  69  69  ARG ARG L . n 
L 1 70  LYS 70  70  70  LYS LYS L . n 
L 1 71  HIS 71  71  71  HIS HIS L . n 
L 1 72  GLY 72  72  72  GLY GLY L . n 
L 1 73  GLY 73  73  73  GLY GLY L . n 
L 1 74  PRO 74  74  74  PRO PRO L . n 
L 1 75  LYS 75  75  75  LYS LYS L . n 
L 1 76  ASP 76  76  76  ASP ASP L . n 
L 1 77  GLU 77  77  77  GLU GLU L . n 
L 1 78  GLU 78  78  78  GLU GLU L . n 
L 1 79  ARG 79  79  79  ARG ARG L . n 
L 1 80  HIS 80  80  80  HIS HIS L . n 
L 1 81  VAL 81  81  81  VAL VAL L . n 
L 1 82  GLY 82  82  82  GLY GLY L . n 
L 1 83  ASP 83  83  83  ASP ASP L . n 
L 1 84  LEU 84  84  84  LEU LEU L . n 
L 1 85  GLY 85  85  85  GLY GLY L . n 
L 1 86  ASN 86  86  86  ASN ASN L . n 
L 1 87  VAL 87  87  87  VAL VAL L . n 
L 1 88  THR 88  88  88  THR THR L . n 
L 1 89  ALA 89  89  89  ALA ALA L . n 
L 1 90  GLY 90  90  90  GLY GLY L . n 
L 1 91  LYS 91  91  91  LYS LYS L . n 
L 1 92  ASP 92  92  92  ASP ASP L . n 
L 1 93  GLY 93  93  93  GLY GLY L . n 
L 1 94  VAL 94  94  94  VAL VAL L . n 
L 1 95  ALA 95  95  95  ALA ALA L . n 
L 1 96  ASN 96  96  96  ASN ASN L . n 
L 1 97  VAL 97  97  97  VAL VAL L . n 
L 1 98  SER 98  98  98  SER SER L . n 
L 1 99  ILE 99  99  99  ILE ILE L . n 
L 1 100 GLU 100 100 100 GLU GLU L . n 
L 1 101 ASP 101 101 101 ASP ASP L . n 
L 1 102 ARG 102 102 102 ARG ARG L . n 
L 1 103 VAL 103 103 103 VAL VAL L . n 
L 1 104 ILE 104 104 104 ILE ILE L . n 
L 1 105 SER 105 105 105 SER SER L . n 
L 1 106 LEU 106 106 106 LEU LEU L . n 
L 1 107 SER 107 107 107 SER SER L . n 
L 1 108 GLY 108 108 108 GLY GLY L . n 
L 1 109 GLU 109 109 109 GLU GLU L . n 
L 1 110 HIS 110 110 110 HIS HIS L . n 
L 1 111 SER 111 111 111 SER SER L . n 
L 1 112 ILE 112 112 112 ILE ILE L . n 
L 1 113 ILE 113 113 113 ILE ILE L . n 
L 1 114 GLY 114 114 114 GLY GLY L . n 
L 1 115 ARG 115 115 115 ARG ARG L . n 
L 1 116 THR 116 116 116 THR THR L . n 
L 1 117 MET 117 117 117 MET MET L . n 
L 1 118 VAL 118 118 118 VAL VAL L . n 
L 1 119 VAL 119 119 119 VAL VAL L . n 
L 1 120 HIS 120 120 120 HIS HIS L . n 
L 1 121 GLU 121 121 121 GLU GLU L . n 
L 1 122 LYS 122 122 122 LYS LYS L . n 
L 1 123 GLN 123 123 123 GLN GLN L . n 
L 1 124 ASP 124 124 124 ASP ASP L . n 
L 1 125 ASP 125 125 125 ASP ASP L . n 
L 1 126 LEU 126 126 126 LEU LEU L . n 
L 1 127 GLY 127 127 127 GLY GLY L . n 
L 1 128 LYS 128 128 128 LYS LYS L . n 
L 1 129 GLY 129 129 129 GLY GLY L . n 
L 1 130 GLY 130 130 130 GLY GLY L . n 
L 1 131 ASN 131 131 131 ASN ASN L . n 
L 1 132 GLU 132 132 132 GLU GLU L . n 
L 1 133 GLU 133 133 133 GLU GLU L . n 
L 1 134 SER 134 134 134 SER SER L . n 
L 1 135 THR 135 135 135 THR THR L . n 
L 1 136 LYS 136 136 136 LYS LYS L . n 
L 1 137 THR 137 137 137 THR THR L . n 
L 1 138 GLY 138 138 138 GLY GLY L . n 
L 1 139 ASN 139 139 139 ASN ASN L . n 
L 1 140 ALA 140 140 140 ALA ALA L . n 
L 1 141 GLY 141 141 141 GLY GLY L . n 
L 1 142 SER 142 142 142 SER SER L . n 
L 1 143 ARG 143 143 143 ARG ARG L . n 
L 1 144 LEU 144 144 144 LEU LEU L . n 
L 1 145 ALA 145 145 145 ALA ALA L . n 
L 1 146 CYS 146 146 146 CYS CYS L . n 
L 1 147 GLY 147 147 147 GLY GLY L . n 
L 1 148 VAL 148 148 148 VAL VAL L . n 
L 1 149 ILE 149 149 149 ILE ILE L . n 
L 1 150 GLY 150 150 150 GLY GLY L . n 
L 1 151 ILE 151 151 151 ILE ILE L . n 
L 1 152 ALA 152 152 152 ALA ALA L . n 
L 1 153 GLN 153 153 153 GLN GLN L . n 
# 
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 ZN  1   155  155  ZN  ZN  A . 
N  2 ZN  1   155  155  ZN  ZN  B . 
O  2 ZN  1   155  155  ZN  ZN  C . 
P  2 ZN  1   155  155  ZN  ZN  D . 
Q  2 ZN  1   155  155  ZN  ZN  E . 
R  2 ZN  1   155  155  ZN  ZN  F . 
S  2 ZN  1   155  155  ZN  ZN  G . 
T  2 ZN  1   155  155  ZN  ZN  H . 
U  2 ZN  1   155  155  ZN  ZN  I . 
V  2 ZN  1   155  155  ZN  ZN  J . 
W  2 ZN  1   155  155  ZN  ZN  K . 
X  2 ZN  1   155  155  ZN  ZN  L . 
Y  3 HOH 1   154  6    HOH HOH A . 
Y  3 HOH 2   156  8    HOH HOH A . 
Y  3 HOH 3   157  25   HOH HOH A . 
Y  3 HOH 4   158  27   HOH HOH A . 
Y  3 HOH 5   159  45   HOH HOH A . 
Y  3 HOH 6   160  47   HOH HOH A . 
Y  3 HOH 7   161  50   HOH HOH A . 
Y  3 HOH 8   162  63   HOH HOH A . 
Y  3 HOH 9   163  163  HOH HOH A . 
Y  3 HOH 10  164  80   HOH HOH A . 
Y  3 HOH 11  165  94   HOH HOH A . 
Y  3 HOH 12  166  102  HOH HOH A . 
Y  3 HOH 13  167  108  HOH HOH A . 
Y  3 HOH 14  168  120  HOH HOH A . 
Y  3 HOH 15  169  121  HOH HOH A . 
Y  3 HOH 16  170  124  HOH HOH A . 
Y  3 HOH 17  171  133  HOH HOH A . 
Y  3 HOH 18  181  181  HOH HOH A . 
Y  3 HOH 19  196  196  HOH HOH A . 
Y  3 HOH 20  202  202  HOH HOH A . 
Y  3 HOH 21  214  214  HOH HOH A . 
Y  3 HOH 22  219  219  HOH HOH A . 
Y  3 HOH 23  241  241  HOH HOH A . 
Y  3 HOH 24  243  243  HOH HOH A . 
Y  3 HOH 25  266  266  HOH HOH A . 
Y  3 HOH 26  280  280  HOH HOH A . 
Y  3 HOH 27  291  291  HOH HOH A . 
Y  3 HOH 28  294  294  HOH HOH A . 
Y  3 HOH 29  296  296  HOH HOH A . 
Y  3 HOH 30  308  308  HOH HOH A . 
Y  3 HOH 31  328  328  HOH HOH A . 
Y  3 HOH 32  345  345  HOH HOH A . 
Y  3 HOH 33  352  352  HOH HOH A . 
Y  3 HOH 34  393  393  HOH HOH A . 
Y  3 HOH 35  395  395  HOH HOH A . 
Y  3 HOH 36  401  401  HOH HOH A . 
Y  3 HOH 37  403  403  HOH HOH A . 
Y  3 HOH 38  412  412  HOH HOH A . 
Y  3 HOH 39  418  418  HOH HOH A . 
Y  3 HOH 40  427  427  HOH HOH A . 
Y  3 HOH 41  429  429  HOH HOH A . 
Y  3 HOH 42  441  441  HOH HOH A . 
Y  3 HOH 43  443  443  HOH HOH A . 
Y  3 HOH 44  445  445  HOH HOH A . 
Y  3 HOH 45  447  447  HOH HOH A . 
Y  3 HOH 46  471  471  HOH HOH A . 
Y  3 HOH 47  480  480  HOH HOH A . 
Y  3 HOH 48  502  502  HOH HOH A . 
Y  3 HOH 49  510  510  HOH HOH A . 
Y  3 HOH 50  517  517  HOH HOH A . 
Y  3 HOH 51  526  526  HOH HOH A . 
Y  3 HOH 52  531  531  HOH HOH A . 
Y  3 HOH 53  540  540  HOH HOH A . 
Y  3 HOH 54  545  545  HOH HOH A . 
Y  3 HOH 55  546  546  HOH HOH A . 
Y  3 HOH 56  555  555  HOH HOH A . 
Y  3 HOH 57  569  569  HOH HOH A . 
Y  3 HOH 58  579  579  HOH HOH A . 
Y  3 HOH 59  591  591  HOH HOH A . 
Y  3 HOH 60  629  629  HOH HOH A . 
Y  3 HOH 61  632  632  HOH HOH A . 
Y  3 HOH 62  635  635  HOH HOH A . 
Y  3 HOH 63  651  651  HOH HOH A . 
Y  3 HOH 64  655  655  HOH HOH A . 
Y  3 HOH 65  673  673  HOH HOH A . 
Y  3 HOH 66  674  674  HOH HOH A . 
Y  3 HOH 67  682  682  HOH HOH A . 
Y  3 HOH 68  685  685  HOH HOH A . 
Y  3 HOH 69  699  699  HOH HOH A . 
Y  3 HOH 70  712  712  HOH HOH A . 
Y  3 HOH 71  730  730  HOH HOH A . 
Y  3 HOH 72  740  740  HOH HOH A . 
Y  3 HOH 73  750  750  HOH HOH A . 
Y  3 HOH 74  755  755  HOH HOH A . 
Y  3 HOH 75  772  772  HOH HOH A . 
Y  3 HOH 76  775  775  HOH HOH A . 
Y  3 HOH 77  789  789  HOH HOH A . 
Y  3 HOH 78  800  800  HOH HOH A . 
Y  3 HOH 79  801  801  HOH HOH A . 
Y  3 HOH 80  817  817  HOH HOH A . 
Y  3 HOH 81  821  821  HOH HOH A . 
Y  3 HOH 82  824  824  HOH HOH A . 
Y  3 HOH 83  835  835  HOH HOH A . 
Y  3 HOH 84  847  847  HOH HOH A . 
Y  3 HOH 85  849  849  HOH HOH A . 
Y  3 HOH 86  855  855  HOH HOH A . 
Y  3 HOH 87  862  862  HOH HOH A . 
Y  3 HOH 88  870  870  HOH HOH A . 
Y  3 HOH 89  876  876  HOH HOH A . 
Y  3 HOH 90  908  908  HOH HOH A . 
Y  3 HOH 91  911  911  HOH HOH A . 
Y  3 HOH 92  912  912  HOH HOH A . 
Y  3 HOH 93  924  924  HOH HOH A . 
Y  3 HOH 94  933  933  HOH HOH A . 
Y  3 HOH 95  936  936  HOH HOH A . 
Y  3 HOH 96  948  948  HOH HOH A . 
Y  3 HOH 97  955  955  HOH HOH A . 
Y  3 HOH 98  965  965  HOH HOH A . 
Y  3 HOH 99  978  978  HOH HOH A . 
Y  3 HOH 100 990  990  HOH HOH A . 
Y  3 HOH 101 1013 1013 HOH HOH A . 
Y  3 HOH 102 1018 1018 HOH HOH A . 
Y  3 HOH 103 1024 1024 HOH HOH A . 
Y  3 HOH 104 1026 1026 HOH HOH A . 
Y  3 HOH 105 1037 1037 HOH HOH A . 
Y  3 HOH 106 1054 1054 HOH HOH A . 
Y  3 HOH 107 1062 1062 HOH HOH A . 
Y  3 HOH 108 1063 1063 HOH HOH A . 
Y  3 HOH 109 1071 1071 HOH HOH A . 
Y  3 HOH 110 1074 1074 HOH HOH A . 
Y  3 HOH 111 1087 1087 HOH HOH A . 
Y  3 HOH 112 1099 1099 HOH HOH A . 
Y  3 HOH 113 1110 1110 HOH HOH A . 
Y  3 HOH 114 1111 1111 HOH HOH A . 
Y  3 HOH 115 1121 1121 HOH HOH A . 
Y  3 HOH 116 1127 1127 HOH HOH A . 
Y  3 HOH 117 1132 1132 HOH HOH A . 
Y  3 HOH 118 1147 1147 HOH HOH A . 
Y  3 HOH 119 1161 1161 HOH HOH A . 
Y  3 HOH 120 1164 1164 HOH HOH A . 
Y  3 HOH 121 1182 1182 HOH HOH A . 
Y  3 HOH 122 1199 1199 HOH HOH A . 
Y  3 HOH 123 1219 1219 HOH HOH A . 
Y  3 HOH 124 1222 1222 HOH HOH A . 
Y  3 HOH 125 1236 1236 HOH HOH A . 
Y  3 HOH 126 1241 1241 HOH HOH A . 
Y  3 HOH 127 1242 1242 HOH HOH A . 
Y  3 HOH 128 1257 1257 HOH HOH A . 
Y  3 HOH 129 1262 1262 HOH HOH A . 
Y  3 HOH 130 1276 1276 HOH HOH A . 
Y  3 HOH 131 1289 1289 HOH HOH A . 
Y  3 HOH 132 1303 1303 HOH HOH A . 
Y  3 HOH 133 1308 1308 HOH HOH A . 
Y  3 HOH 134 1321 1321 HOH HOH A . 
Y  3 HOH 135 1322 1322 HOH HOH A . 
Y  3 HOH 136 1323 1323 HOH HOH A . 
Y  3 HOH 137 1326 1326 HOH HOH A . 
Y  3 HOH 138 1328 1328 HOH HOH A . 
Y  3 HOH 139 1348 1348 HOH HOH A . 
Y  3 HOH 140 1359 1359 HOH HOH A . 
Y  3 HOH 141 1386 1386 HOH HOH A . 
Y  3 HOH 142 1396 1396 HOH HOH A . 
Y  3 HOH 143 1398 1398 HOH HOH A . 
Y  3 HOH 144 1401 1401 HOH HOH A . 
Y  3 HOH 145 1413 1413 HOH HOH A . 
Y  3 HOH 146 1420 1420 HOH HOH A . 
Y  3 HOH 147 1429 1429 HOH HOH A . 
Y  3 HOH 148 1442 1442 HOH HOH A . 
Y  3 HOH 149 1443 1443 HOH HOH A . 
Y  3 HOH 150 1474 1474 HOH HOH A . 
Y  3 HOH 151 1485 1485 HOH HOH A . 
Y  3 HOH 152 1490 1490 HOH HOH A . 
Y  3 HOH 153 1540 1540 HOH HOH A . 
Y  3 HOH 154 1542 1542 HOH HOH A . 
Y  3 HOH 155 1550 1550 HOH HOH A . 
Y  3 HOH 156 1561 1561 HOH HOH A . 
Y  3 HOH 157 1566 1566 HOH HOH A . 
Y  3 HOH 158 1577 1577 HOH HOH A . 
Y  3 HOH 159 1582 1582 HOH HOH A . 
Y  3 HOH 160 1604 1604 HOH HOH A . 
Y  3 HOH 161 1616 1616 HOH HOH A . 
Y  3 HOH 162 1657 1657 HOH HOH A . 
Y  3 HOH 163 1660 1660 HOH HOH A . 
Y  3 HOH 164 1663 1663 HOH HOH A . 
Y  3 HOH 165 1674 1674 HOH HOH A . 
Y  3 HOH 166 1677 1677 HOH HOH A . 
Y  3 HOH 167 1679 1679 HOH HOH A . 
Y  3 HOH 168 1705 1705 HOH HOH A . 
Y  3 HOH 169 1714 1714 HOH HOH A . 
Y  3 HOH 170 1718 1718 HOH HOH A . 
Y  3 HOH 171 1729 1729 HOH HOH A . 
Y  3 HOH 172 1734 1734 HOH HOH A . 
Y  3 HOH 173 1751 1751 HOH HOH A . 
Z  3 HOH 1   154  1    HOH HOH B . 
Z  3 HOH 2   156  3    HOH HOH B . 
Z  3 HOH 3   157  9    HOH HOH B . 
Z  3 HOH 4   158  13   HOH HOH B . 
Z  3 HOH 5   159  21   HOH HOH B . 
Z  3 HOH 6   160  22   HOH HOH B . 
Z  3 HOH 7   161  32   HOH HOH B . 
Z  3 HOH 8   162  60   HOH HOH B . 
Z  3 HOH 9   163  61   HOH HOH B . 
Z  3 HOH 10  164  92   HOH HOH B . 
Z  3 HOH 11  165  113  HOH HOH B . 
Z  3 HOH 12  166  118  HOH HOH B . 
Z  3 HOH 13  167  138  HOH HOH B . 
Z  3 HOH 14  168  147  HOH HOH B . 
Z  3 HOH 15  169  152  HOH HOH B . 
Z  3 HOH 16  175  175  HOH HOH B . 
Z  3 HOH 17  180  180  HOH HOH B . 
Z  3 HOH 18  184  184  HOH HOH B . 
Z  3 HOH 19  190  190  HOH HOH B . 
Z  3 HOH 20  200  200  HOH HOH B . 
Z  3 HOH 21  204  204  HOH HOH B . 
Z  3 HOH 22  212  212  HOH HOH B . 
Z  3 HOH 23  225  225  HOH HOH B . 
Z  3 HOH 24  230  230  HOH HOH B . 
Z  3 HOH 25  232  232  HOH HOH B . 
Z  3 HOH 26  237  237  HOH HOH B . 
Z  3 HOH 27  245  245  HOH HOH B . 
Z  3 HOH 28  246  246  HOH HOH B . 
Z  3 HOH 29  262  262  HOH HOH B . 
Z  3 HOH 30  269  269  HOH HOH B . 
Z  3 HOH 31  270  270  HOH HOH B . 
Z  3 HOH 32  293  293  HOH HOH B . 
Z  3 HOH 33  304  304  HOH HOH B . 
Z  3 HOH 34  319  319  HOH HOH B . 
Z  3 HOH 35  331  331  HOH HOH B . 
Z  3 HOH 36  333  333  HOH HOH B . 
Z  3 HOH 37  335  335  HOH HOH B . 
Z  3 HOH 38  360  360  HOH HOH B . 
Z  3 HOH 39  376  376  HOH HOH B . 
Z  3 HOH 40  381  381  HOH HOH B . 
Z  3 HOH 41  394  394  HOH HOH B . 
Z  3 HOH 42  397  397  HOH HOH B . 
Z  3 HOH 43  404  404  HOH HOH B . 
Z  3 HOH 44  409  409  HOH HOH B . 
Z  3 HOH 45  411  411  HOH HOH B . 
Z  3 HOH 46  416  416  HOH HOH B . 
Z  3 HOH 47  417  417  HOH HOH B . 
Z  3 HOH 48  424  424  HOH HOH B . 
Z  3 HOH 49  444  444  HOH HOH B . 
Z  3 HOH 50  465  465  HOH HOH B . 
Z  3 HOH 51  472  472  HOH HOH B . 
Z  3 HOH 52  473  473  HOH HOH B . 
Z  3 HOH 53  474  474  HOH HOH B . 
Z  3 HOH 54  475  475  HOH HOH B . 
Z  3 HOH 55  501  501  HOH HOH B . 
Z  3 HOH 56  508  508  HOH HOH B . 
Z  3 HOH 57  511  511  HOH HOH B . 
Z  3 HOH 58  528  528  HOH HOH B . 
Z  3 HOH 59  548  548  HOH HOH B . 
Z  3 HOH 60  558  558  HOH HOH B . 
Z  3 HOH 61  560  560  HOH HOH B . 
Z  3 HOH 62  572  572  HOH HOH B . 
Z  3 HOH 63  576  576  HOH HOH B . 
Z  3 HOH 64  582  582  HOH HOH B . 
Z  3 HOH 65  604  604  HOH HOH B . 
Z  3 HOH 66  625  625  HOH HOH B . 
Z  3 HOH 67  630  630  HOH HOH B . 
Z  3 HOH 68  633  633  HOH HOH B . 
Z  3 HOH 69  634  634  HOH HOH B . 
Z  3 HOH 70  636  636  HOH HOH B . 
Z  3 HOH 71  643  643  HOH HOH B . 
Z  3 HOH 72  645  645  HOH HOH B . 
Z  3 HOH 73  652  652  HOH HOH B . 
Z  3 HOH 74  670  670  HOH HOH B . 
Z  3 HOH 75  672  672  HOH HOH B . 
Z  3 HOH 76  675  675  HOH HOH B . 
Z  3 HOH 77  677  677  HOH HOH B . 
Z  3 HOH 78  680  680  HOH HOH B . 
Z  3 HOH 79  696  696  HOH HOH B . 
Z  3 HOH 80  697  697  HOH HOH B . 
Z  3 HOH 81  714  714  HOH HOH B . 
Z  3 HOH 82  715  715  HOH HOH B . 
Z  3 HOH 83  747  747  HOH HOH B . 
Z  3 HOH 84  761  761  HOH HOH B . 
Z  3 HOH 85  764  764  HOH HOH B . 
Z  3 HOH 86  767  767  HOH HOH B . 
Z  3 HOH 87  784  784  HOH HOH B . 
Z  3 HOH 88  792  792  HOH HOH B . 
Z  3 HOH 89  804  804  HOH HOH B . 
Z  3 HOH 90  805  805  HOH HOH B . 
Z  3 HOH 91  806  806  HOH HOH B . 
Z  3 HOH 92  808  808  HOH HOH B . 
Z  3 HOH 93  825  825  HOH HOH B . 
Z  3 HOH 94  828  828  HOH HOH B . 
Z  3 HOH 95  838  838  HOH HOH B . 
Z  3 HOH 96  839  839  HOH HOH B . 
Z  3 HOH 97  860  860  HOH HOH B . 
Z  3 HOH 98  893  893  HOH HOH B . 
Z  3 HOH 99  899  899  HOH HOH B . 
Z  3 HOH 100 901  901  HOH HOH B . 
Z  3 HOH 101 922  922  HOH HOH B . 
Z  3 HOH 102 928  928  HOH HOH B . 
Z  3 HOH 103 942  942  HOH HOH B . 
Z  3 HOH 104 950  950  HOH HOH B . 
Z  3 HOH 105 951  951  HOH HOH B . 
Z  3 HOH 106 952  952  HOH HOH B . 
Z  3 HOH 107 963  963  HOH HOH B . 
Z  3 HOH 108 988  988  HOH HOH B . 
Z  3 HOH 109 989  989  HOH HOH B . 
Z  3 HOH 110 993  993  HOH HOH B . 
Z  3 HOH 111 1008 1008 HOH HOH B . 
Z  3 HOH 112 1012 1012 HOH HOH B . 
Z  3 HOH 113 1025 1025 HOH HOH B . 
Z  3 HOH 114 1028 1028 HOH HOH B . 
Z  3 HOH 115 1030 1030 HOH HOH B . 
Z  3 HOH 116 1050 1050 HOH HOH B . 
Z  3 HOH 117 1066 1066 HOH HOH B . 
Z  3 HOH 118 1069 1069 HOH HOH B . 
Z  3 HOH 119 1076 1076 HOH HOH B . 
Z  3 HOH 120 1084 1084 HOH HOH B . 
Z  3 HOH 121 1086 1086 HOH HOH B . 
Z  3 HOH 122 1106 1106 HOH HOH B . 
Z  3 HOH 123 1107 1107 HOH HOH B . 
Z  3 HOH 124 1137 1137 HOH HOH B . 
Z  3 HOH 125 1142 1142 HOH HOH B . 
Z  3 HOH 126 1154 1154 HOH HOH B . 
Z  3 HOH 127 1166 1166 HOH HOH B . 
Z  3 HOH 128 1167 1167 HOH HOH B . 
Z  3 HOH 129 1178 1178 HOH HOH B . 
Z  3 HOH 130 1179 1179 HOH HOH B . 
Z  3 HOH 131 1183 1183 HOH HOH B . 
Z  3 HOH 132 1187 1187 HOH HOH B . 
Z  3 HOH 133 1189 1189 HOH HOH B . 
Z  3 HOH 134 1194 1194 HOH HOH B . 
Z  3 HOH 135 1220 1220 HOH HOH B . 
Z  3 HOH 136 1227 1227 HOH HOH B . 
Z  3 HOH 137 1235 1235 HOH HOH B . 
Z  3 HOH 138 1247 1247 HOH HOH B . 
Z  3 HOH 139 1264 1264 HOH HOH B . 
Z  3 HOH 140 1278 1278 HOH HOH B . 
Z  3 HOH 141 1297 1297 HOH HOH B . 
Z  3 HOH 142 1298 1298 HOH HOH B . 
Z  3 HOH 143 1307 1307 HOH HOH B . 
Z  3 HOH 144 1312 1312 HOH HOH B . 
Z  3 HOH 145 1318 1318 HOH HOH B . 
Z  3 HOH 146 1319 1319 HOH HOH B . 
Z  3 HOH 147 1340 1340 HOH HOH B . 
Z  3 HOH 148 1352 1352 HOH HOH B . 
Z  3 HOH 149 1353 1353 HOH HOH B . 
Z  3 HOH 150 1377 1377 HOH HOH B . 
Z  3 HOH 151 1380 1380 HOH HOH B . 
Z  3 HOH 152 1389 1389 HOH HOH B . 
Z  3 HOH 153 1400 1400 HOH HOH B . 
Z  3 HOH 154 1407 1407 HOH HOH B . 
Z  3 HOH 155 1415 1415 HOH HOH B . 
Z  3 HOH 156 1417 1417 HOH HOH B . 
Z  3 HOH 157 1428 1428 HOH HOH B . 
Z  3 HOH 158 1436 1436 HOH HOH B . 
Z  3 HOH 159 1444 1444 HOH HOH B . 
Z  3 HOH 160 1445 1445 HOH HOH B . 
Z  3 HOH 161 1457 1457 HOH HOH B . 
Z  3 HOH 162 1463 1463 HOH HOH B . 
Z  3 HOH 163 1470 1470 HOH HOH B . 
Z  3 HOH 164 1500 1500 HOH HOH B . 
Z  3 HOH 165 1509 1509 HOH HOH B . 
Z  3 HOH 166 1516 1516 HOH HOH B . 
Z  3 HOH 167 1543 1543 HOH HOH B . 
Z  3 HOH 168 1546 1546 HOH HOH B . 
Z  3 HOH 169 1549 1549 HOH HOH B . 
Z  3 HOH 170 1559 1559 HOH HOH B . 
Z  3 HOH 171 1562 1562 HOH HOH B . 
Z  3 HOH 172 1570 1570 HOH HOH B . 
Z  3 HOH 173 1585 1585 HOH HOH B . 
Z  3 HOH 174 1598 1598 HOH HOH B . 
Z  3 HOH 175 1614 1614 HOH HOH B . 
Z  3 HOH 176 1617 1617 HOH HOH B . 
Z  3 HOH 177 1624 1624 HOH HOH B . 
Z  3 HOH 178 1634 1634 HOH HOH B . 
Z  3 HOH 179 1646 1646 HOH HOH B . 
Z  3 HOH 180 1650 1650 HOH HOH B . 
Z  3 HOH 181 1661 1661 HOH HOH B . 
Z  3 HOH 182 1699 1699 HOH HOH B . 
Z  3 HOH 183 1708 1708 HOH HOH B . 
Z  3 HOH 184 1724 1724 HOH HOH B . 
Z  3 HOH 185 1762 1762 HOH HOH B . 
Z  3 HOH 186 1765 1765 HOH HOH B . 
Z  3 HOH 187 1769 1769 HOH HOH B . 
Z  3 HOH 188 1777 1777 HOH HOH B . 
Z  3 HOH 189 1802 1802 HOH HOH B . 
AA 3 HOH 1   154  16   HOH HOH C . 
AA 3 HOH 2   156  24   HOH HOH C . 
AA 3 HOH 3   157  35   HOH HOH C . 
AA 3 HOH 4   158  54   HOH HOH C . 
AA 3 HOH 5   159  59   HOH HOH C . 
AA 3 HOH 6   160  67   HOH HOH C . 
AA 3 HOH 7   161  91   HOH HOH C . 
AA 3 HOH 8   162  99   HOH HOH C . 
AA 3 HOH 9   163  107  HOH HOH C . 
AA 3 HOH 10  164  115  HOH HOH C . 
AA 3 HOH 11  165  130  HOH HOH C . 
AA 3 HOH 12  166  166  HOH HOH C . 
AA 3 HOH 13  167  150  HOH HOH C . 
AA 3 HOH 14  168  168  HOH HOH C . 
AA 3 HOH 15  169  155  HOH HOH C . 
AA 3 HOH 16  173  173  HOH HOH C . 
AA 3 HOH 17  179  179  HOH HOH C . 
AA 3 HOH 18  187  187  HOH HOH C . 
AA 3 HOH 19  198  198  HOH HOH C . 
AA 3 HOH 20  208  208  HOH HOH C . 
AA 3 HOH 21  210  210  HOH HOH C . 
AA 3 HOH 22  216  216  HOH HOH C . 
AA 3 HOH 23  218  218  HOH HOH C . 
AA 3 HOH 24  220  220  HOH HOH C . 
AA 3 HOH 25  221  221  HOH HOH C . 
AA 3 HOH 26  252  252  HOH HOH C . 
AA 3 HOH 27  267  267  HOH HOH C . 
AA 3 HOH 28  274  274  HOH HOH C . 
AA 3 HOH 29  275  275  HOH HOH C . 
AA 3 HOH 30  290  290  HOH HOH C . 
AA 3 HOH 31  292  292  HOH HOH C . 
AA 3 HOH 32  302  302  HOH HOH C . 
AA 3 HOH 33  310  310  HOH HOH C . 
AA 3 HOH 34  312  312  HOH HOH C . 
AA 3 HOH 35  323  323  HOH HOH C . 
AA 3 HOH 36  334  334  HOH HOH C . 
AA 3 HOH 37  370  370  HOH HOH C . 
AA 3 HOH 38  372  372  HOH HOH C . 
AA 3 HOH 39  374  374  HOH HOH C . 
AA 3 HOH 40  390  390  HOH HOH C . 
AA 3 HOH 41  391  391  HOH HOH C . 
AA 3 HOH 42  413  413  HOH HOH C . 
AA 3 HOH 43  426  426  HOH HOH C . 
AA 3 HOH 44  434  434  HOH HOH C . 
AA 3 HOH 45  455  455  HOH HOH C . 
AA 3 HOH 46  470  470  HOH HOH C . 
AA 3 HOH 47  482  482  HOH HOH C . 
AA 3 HOH 48  498  498  HOH HOH C . 
AA 3 HOH 49  522  522  HOH HOH C . 
AA 3 HOH 50  524  524  HOH HOH C . 
AA 3 HOH 51  530  530  HOH HOH C . 
AA 3 HOH 52  534  534  HOH HOH C . 
AA 3 HOH 53  539  539  HOH HOH C . 
AA 3 HOH 54  559  559  HOH HOH C . 
AA 3 HOH 55  561  561  HOH HOH C . 
AA 3 HOH 56  565  565  HOH HOH C . 
AA 3 HOH 57  567  567  HOH HOH C . 
AA 3 HOH 58  577  577  HOH HOH C . 
AA 3 HOH 59  578  578  HOH HOH C . 
AA 3 HOH 60  593  593  HOH HOH C . 
AA 3 HOH 61  602  602  HOH HOH C . 
AA 3 HOH 62  609  609  HOH HOH C . 
AA 3 HOH 63  610  610  HOH HOH C . 
AA 3 HOH 64  611  611  HOH HOH C . 
AA 3 HOH 65  614  614  HOH HOH C . 
AA 3 HOH 66  620  620  HOH HOH C . 
AA 3 HOH 67  657  657  HOH HOH C . 
AA 3 HOH 68  701  701  HOH HOH C . 
AA 3 HOH 69  709  709  HOH HOH C . 
AA 3 HOH 70  718  718  HOH HOH C . 
AA 3 HOH 71  719  719  HOH HOH C . 
AA 3 HOH 72  735  735  HOH HOH C . 
AA 3 HOH 73  737  737  HOH HOH C . 
AA 3 HOH 74  739  739  HOH HOH C . 
AA 3 HOH 75  745  745  HOH HOH C . 
AA 3 HOH 76  752  752  HOH HOH C . 
AA 3 HOH 77  763  763  HOH HOH C . 
AA 3 HOH 78  765  765  HOH HOH C . 
AA 3 HOH 79  776  776  HOH HOH C . 
AA 3 HOH 80  782  782  HOH HOH C . 
AA 3 HOH 81  787  787  HOH HOH C . 
AA 3 HOH 82  796  796  HOH HOH C . 
AA 3 HOH 83  797  797  HOH HOH C . 
AA 3 HOH 84  819  819  HOH HOH C . 
AA 3 HOH 85  822  822  HOH HOH C . 
AA 3 HOH 86  830  830  HOH HOH C . 
AA 3 HOH 87  841  841  HOH HOH C . 
AA 3 HOH 88  850  850  HOH HOH C . 
AA 3 HOH 89  859  859  HOH HOH C . 
AA 3 HOH 90  864  864  HOH HOH C . 
AA 3 HOH 91  880  880  HOH HOH C . 
AA 3 HOH 92  885  885  HOH HOH C . 
AA 3 HOH 93  894  894  HOH HOH C . 
AA 3 HOH 94  902  902  HOH HOH C . 
AA 3 HOH 95  903  903  HOH HOH C . 
AA 3 HOH 96  913  913  HOH HOH C . 
AA 3 HOH 97  915  915  HOH HOH C . 
AA 3 HOH 98  917  917  HOH HOH C . 
AA 3 HOH 99  930  930  HOH HOH C . 
AA 3 HOH 100 944  944  HOH HOH C . 
AA 3 HOH 101 954  954  HOH HOH C . 
AA 3 HOH 102 961  961  HOH HOH C . 
AA 3 HOH 103 982  982  HOH HOH C . 
AA 3 HOH 104 992  992  HOH HOH C . 
AA 3 HOH 105 1001 1001 HOH HOH C . 
AA 3 HOH 106 1004 1004 HOH HOH C . 
AA 3 HOH 107 1016 1016 HOH HOH C . 
AA 3 HOH 108 1017 1017 HOH HOH C . 
AA 3 HOH 109 1019 1019 HOH HOH C . 
AA 3 HOH 110 1043 1043 HOH HOH C . 
AA 3 HOH 111 1044 1044 HOH HOH C . 
AA 3 HOH 112 1051 1051 HOH HOH C . 
AA 3 HOH 113 1060 1060 HOH HOH C . 
AA 3 HOH 114 1077 1077 HOH HOH C . 
AA 3 HOH 115 1090 1090 HOH HOH C . 
AA 3 HOH 116 1091 1091 HOH HOH C . 
AA 3 HOH 117 1101 1101 HOH HOH C . 
AA 3 HOH 118 1114 1114 HOH HOH C . 
AA 3 HOH 119 1124 1124 HOH HOH C . 
AA 3 HOH 120 1128 1128 HOH HOH C . 
AA 3 HOH 121 1134 1134 HOH HOH C . 
AA 3 HOH 122 1135 1135 HOH HOH C . 
AA 3 HOH 123 1139 1139 HOH HOH C . 
AA 3 HOH 124 1144 1144 HOH HOH C . 
AA 3 HOH 125 1170 1170 HOH HOH C . 
AA 3 HOH 126 1172 1172 HOH HOH C . 
AA 3 HOH 127 1177 1177 HOH HOH C . 
AA 3 HOH 128 1195 1195 HOH HOH C . 
AA 3 HOH 129 1196 1196 HOH HOH C . 
AA 3 HOH 130 1204 1204 HOH HOH C . 
AA 3 HOH 131 1208 1208 HOH HOH C . 
AA 3 HOH 132 1214 1214 HOH HOH C . 
AA 3 HOH 133 1218 1218 HOH HOH C . 
AA 3 HOH 134 1229 1229 HOH HOH C . 
AA 3 HOH 135 1246 1246 HOH HOH C . 
AA 3 HOH 136 1268 1268 HOH HOH C . 
AA 3 HOH 137 1280 1280 HOH HOH C . 
AA 3 HOH 138 1282 1282 HOH HOH C . 
AA 3 HOH 139 1309 1309 HOH HOH C . 
AA 3 HOH 140 1310 1310 HOH HOH C . 
AA 3 HOH 141 1325 1325 HOH HOH C . 
AA 3 HOH 142 1331 1331 HOH HOH C . 
AA 3 HOH 143 1383 1383 HOH HOH C . 
AA 3 HOH 144 1392 1392 HOH HOH C . 
AA 3 HOH 145 1394 1394 HOH HOH C . 
AA 3 HOH 146 1405 1405 HOH HOH C . 
AA 3 HOH 147 1440 1440 HOH HOH C . 
AA 3 HOH 148 1455 1455 HOH HOH C . 
AA 3 HOH 149 1456 1456 HOH HOH C . 
AA 3 HOH 150 1458 1458 HOH HOH C . 
AA 3 HOH 151 1466 1466 HOH HOH C . 
AA 3 HOH 152 1475 1475 HOH HOH C . 
AA 3 HOH 153 1478 1478 HOH HOH C . 
AA 3 HOH 154 1482 1482 HOH HOH C . 
AA 3 HOH 155 1494 1494 HOH HOH C . 
AA 3 HOH 156 1511 1511 HOH HOH C . 
AA 3 HOH 157 1514 1514 HOH HOH C . 
AA 3 HOH 158 1517 1517 HOH HOH C . 
AA 3 HOH 159 1518 1518 HOH HOH C . 
AA 3 HOH 160 1535 1535 HOH HOH C . 
AA 3 HOH 161 1545 1545 HOH HOH C . 
AA 3 HOH 162 1560 1560 HOH HOH C . 
AA 3 HOH 163 1565 1565 HOH HOH C . 
AA 3 HOH 164 1576 1576 HOH HOH C . 
AA 3 HOH 165 1594 1594 HOH HOH C . 
AA 3 HOH 166 1599 1599 HOH HOH C . 
AA 3 HOH 167 1626 1626 HOH HOH C . 
AA 3 HOH 168 1630 1630 HOH HOH C . 
AA 3 HOH 169 1643 1643 HOH HOH C . 
AA 3 HOH 170 1678 1678 HOH HOH C . 
AA 3 HOH 171 1696 1696 HOH HOH C . 
AA 3 HOH 172 1715 1715 HOH HOH C . 
AA 3 HOH 173 1723 1723 HOH HOH C . 
AA 3 HOH 174 1725 1725 HOH HOH C . 
AA 3 HOH 175 1753 1753 HOH HOH C . 
AA 3 HOH 176 1763 1763 HOH HOH C . 
AA 3 HOH 177 1770 1770 HOH HOH C . 
AA 3 HOH 178 1772 1772 HOH HOH C . 
AA 3 HOH 179 1780 1780 HOH HOH C . 
AA 3 HOH 180 1789 1789 HOH HOH C . 
AA 3 HOH 181 1790 1790 HOH HOH C . 
AA 3 HOH 182 1791 1791 HOH HOH C . 
AA 3 HOH 183 1800 1800 HOH HOH C . 
AA 3 HOH 184 1808 1808 HOH HOH C . 
BA 3 HOH 1   154  154  HOH HOH D . 
BA 3 HOH 2   156  12   HOH HOH D . 
BA 3 HOH 3   157  42   HOH HOH D . 
BA 3 HOH 4   158  46   HOH HOH D . 
BA 3 HOH 5   159  48   HOH HOH D . 
BA 3 HOH 6   160  66   HOH HOH D . 
BA 3 HOH 7   161  69   HOH HOH D . 
BA 3 HOH 8   162  76   HOH HOH D . 
BA 3 HOH 9   163  83   HOH HOH D . 
BA 3 HOH 10  164  95   HOH HOH D . 
BA 3 HOH 11  165  96   HOH HOH D . 
BA 3 HOH 12  166  97   HOH HOH D . 
BA 3 HOH 13  167  98   HOH HOH D . 
BA 3 HOH 14  168  111  HOH HOH D . 
BA 3 HOH 15  169  119  HOH HOH D . 
BA 3 HOH 16  170  135  HOH HOH D . 
BA 3 HOH 17  171  139  HOH HOH D . 
BA 3 HOH 18  172  146  HOH HOH D . 
BA 3 HOH 19  173  153  HOH HOH D . 
BA 3 HOH 20  188  188  HOH HOH D . 
BA 3 HOH 21  238  238  HOH HOH D . 
BA 3 HOH 22  239  239  HOH HOH D . 
BA 3 HOH 23  254  254  HOH HOH D . 
BA 3 HOH 24  257  257  HOH HOH D . 
BA 3 HOH 25  300  300  HOH HOH D . 
BA 3 HOH 26  311  311  HOH HOH D . 
BA 3 HOH 27  329  329  HOH HOH D . 
BA 3 HOH 28  341  341  HOH HOH D . 
BA 3 HOH 29  342  342  HOH HOH D . 
BA 3 HOH 30  362  362  HOH HOH D . 
BA 3 HOH 31  364  364  HOH HOH D . 
BA 3 HOH 32  377  377  HOH HOH D . 
BA 3 HOH 33  406  406  HOH HOH D . 
BA 3 HOH 34  420  420  HOH HOH D . 
BA 3 HOH 35  421  421  HOH HOH D . 
BA 3 HOH 36  425  425  HOH HOH D . 
BA 3 HOH 37  449  449  HOH HOH D . 
BA 3 HOH 38  462  462  HOH HOH D . 
BA 3 HOH 39  469  469  HOH HOH D . 
BA 3 HOH 40  481  481  HOH HOH D . 
BA 3 HOH 41  487  487  HOH HOH D . 
BA 3 HOH 42  490  490  HOH HOH D . 
BA 3 HOH 43  505  505  HOH HOH D . 
BA 3 HOH 44  507  507  HOH HOH D . 
BA 3 HOH 45  516  516  HOH HOH D . 
BA 3 HOH 46  523  523  HOH HOH D . 
BA 3 HOH 47  537  537  HOH HOH D . 
BA 3 HOH 48  552  552  HOH HOH D . 
BA 3 HOH 49  554  554  HOH HOH D . 
BA 3 HOH 50  586  586  HOH HOH D . 
BA 3 HOH 51  598  598  HOH HOH D . 
BA 3 HOH 52  600  600  HOH HOH D . 
BA 3 HOH 53  601  601  HOH HOH D . 
BA 3 HOH 54  617  617  HOH HOH D . 
BA 3 HOH 55  638  638  HOH HOH D . 
BA 3 HOH 56  658  658  HOH HOH D . 
BA 3 HOH 57  661  661  HOH HOH D . 
BA 3 HOH 58  678  678  HOH HOH D . 
BA 3 HOH 59  679  679  HOH HOH D . 
BA 3 HOH 60  691  691  HOH HOH D . 
BA 3 HOH 61  702  702  HOH HOH D . 
BA 3 HOH 62  704  704  HOH HOH D . 
BA 3 HOH 63  705  705  HOH HOH D . 
BA 3 HOH 64  706  706  HOH HOH D . 
BA 3 HOH 65  711  711  HOH HOH D . 
BA 3 HOH 66  722  722  HOH HOH D . 
BA 3 HOH 67  724  724  HOH HOH D . 
BA 3 HOH 68  731  731  HOH HOH D . 
BA 3 HOH 69  734  734  HOH HOH D . 
BA 3 HOH 70  738  738  HOH HOH D . 
BA 3 HOH 71  751  751  HOH HOH D . 
BA 3 HOH 72  758  758  HOH HOH D . 
BA 3 HOH 73  760  760  HOH HOH D . 
BA 3 HOH 74  771  771  HOH HOH D . 
BA 3 HOH 75  773  773  HOH HOH D . 
BA 3 HOH 76  779  779  HOH HOH D . 
BA 3 HOH 77  791  791  HOH HOH D . 
BA 3 HOH 78  812  812  HOH HOH D . 
BA 3 HOH 79  814  814  HOH HOH D . 
BA 3 HOH 80  818  818  HOH HOH D . 
BA 3 HOH 81  820  820  HOH HOH D . 
BA 3 HOH 82  823  823  HOH HOH D . 
BA 3 HOH 83  829  829  HOH HOH D . 
BA 3 HOH 84  831  831  HOH HOH D . 
BA 3 HOH 85  833  833  HOH HOH D . 
BA 3 HOH 86  837  837  HOH HOH D . 
BA 3 HOH 87  853  853  HOH HOH D . 
BA 3 HOH 88  858  858  HOH HOH D . 
BA 3 HOH 89  874  874  HOH HOH D . 
BA 3 HOH 90  878  878  HOH HOH D . 
BA 3 HOH 91  881  881  HOH HOH D . 
BA 3 HOH 92  884  884  HOH HOH D . 
BA 3 HOH 93  891  891  HOH HOH D . 
BA 3 HOH 94  892  892  HOH HOH D . 
BA 3 HOH 95  906  906  HOH HOH D . 
BA 3 HOH 96  914  914  HOH HOH D . 
BA 3 HOH 97  923  923  HOH HOH D . 
BA 3 HOH 98  925  925  HOH HOH D . 
BA 3 HOH 99  932  932  HOH HOH D . 
BA 3 HOH 100 949  949  HOH HOH D . 
BA 3 HOH 101 953  953  HOH HOH D . 
BA 3 HOH 102 957  957  HOH HOH D . 
BA 3 HOH 103 964  964  HOH HOH D . 
BA 3 HOH 104 977  977  HOH HOH D . 
BA 3 HOH 105 979  979  HOH HOH D . 
BA 3 HOH 106 994  994  HOH HOH D . 
BA 3 HOH 107 998  998  HOH HOH D . 
BA 3 HOH 108 1011 1011 HOH HOH D . 
BA 3 HOH 109 1023 1023 HOH HOH D . 
BA 3 HOH 110 1027 1027 HOH HOH D . 
BA 3 HOH 111 1036 1036 HOH HOH D . 
BA 3 HOH 112 1040 1040 HOH HOH D . 
BA 3 HOH 113 1065 1065 HOH HOH D . 
BA 3 HOH 114 1067 1067 HOH HOH D . 
BA 3 HOH 115 1095 1095 HOH HOH D . 
BA 3 HOH 116 1126 1126 HOH HOH D . 
BA 3 HOH 117 1138 1138 HOH HOH D . 
BA 3 HOH 118 1141 1141 HOH HOH D . 
BA 3 HOH 119 1152 1152 HOH HOH D . 
BA 3 HOH 120 1153 1153 HOH HOH D . 
BA 3 HOH 121 1186 1186 HOH HOH D . 
BA 3 HOH 122 1188 1188 HOH HOH D . 
BA 3 HOH 123 1191 1191 HOH HOH D . 
BA 3 HOH 124 1206 1206 HOH HOH D . 
BA 3 HOH 125 1228 1228 HOH HOH D . 
BA 3 HOH 126 1256 1256 HOH HOH D . 
BA 3 HOH 127 1263 1263 HOH HOH D . 
BA 3 HOH 128 1269 1269 HOH HOH D . 
BA 3 HOH 129 1271 1271 HOH HOH D . 
BA 3 HOH 130 1292 1292 HOH HOH D . 
BA 3 HOH 131 1293 1293 HOH HOH D . 
BA 3 HOH 132 1296 1296 HOH HOH D . 
BA 3 HOH 133 1316 1316 HOH HOH D . 
BA 3 HOH 134 1320 1320 HOH HOH D . 
BA 3 HOH 135 1327 1327 HOH HOH D . 
BA 3 HOH 136 1330 1330 HOH HOH D . 
BA 3 HOH 137 1342 1342 HOH HOH D . 
BA 3 HOH 138 1343 1343 HOH HOH D . 
BA 3 HOH 139 1350 1350 HOH HOH D . 
BA 3 HOH 140 1356 1356 HOH HOH D . 
BA 3 HOH 141 1367 1367 HOH HOH D . 
BA 3 HOH 142 1384 1384 HOH HOH D . 
BA 3 HOH 143 1385 1385 HOH HOH D . 
BA 3 HOH 144 1390 1390 HOH HOH D . 
BA 3 HOH 145 1402 1402 HOH HOH D . 
BA 3 HOH 146 1409 1409 HOH HOH D . 
BA 3 HOH 147 1414 1414 HOH HOH D . 
BA 3 HOH 148 1451 1451 HOH HOH D . 
BA 3 HOH 149 1465 1465 HOH HOH D . 
BA 3 HOH 150 1467 1467 HOH HOH D . 
BA 3 HOH 151 1502 1502 HOH HOH D . 
BA 3 HOH 152 1519 1519 HOH HOH D . 
BA 3 HOH 153 1525 1525 HOH HOH D . 
BA 3 HOH 154 1530 1530 HOH HOH D . 
BA 3 HOH 155 1544 1544 HOH HOH D . 
BA 3 HOH 156 1552 1552 HOH HOH D . 
BA 3 HOH 157 1555 1555 HOH HOH D . 
BA 3 HOH 158 1556 1556 HOH HOH D . 
BA 3 HOH 159 1558 1558 HOH HOH D . 
BA 3 HOH 160 1571 1571 HOH HOH D . 
BA 3 HOH 161 1578 1578 HOH HOH D . 
BA 3 HOH 162 1591 1591 HOH HOH D . 
BA 3 HOH 163 1632 1632 HOH HOH D . 
BA 3 HOH 164 1633 1633 HOH HOH D . 
BA 3 HOH 165 1639 1639 HOH HOH D . 
BA 3 HOH 166 1655 1655 HOH HOH D . 
BA 3 HOH 167 1668 1668 HOH HOH D . 
BA 3 HOH 168 1686 1686 HOH HOH D . 
BA 3 HOH 169 1695 1695 HOH HOH D . 
BA 3 HOH 170 1707 1707 HOH HOH D . 
BA 3 HOH 171 1711 1711 HOH HOH D . 
BA 3 HOH 172 1713 1713 HOH HOH D . 
BA 3 HOH 173 1717 1717 HOH HOH D . 
BA 3 HOH 174 1731 1731 HOH HOH D . 
BA 3 HOH 175 1736 1736 HOH HOH D . 
BA 3 HOH 176 1740 1740 HOH HOH D . 
BA 3 HOH 177 1801 1801 HOH HOH D . 
CA 3 HOH 1   154  11   HOH HOH E . 
CA 3 HOH 2   156  156  HOH HOH E . 
CA 3 HOH 3   157  20   HOH HOH E . 
CA 3 HOH 4   158  36   HOH HOH E . 
CA 3 HOH 5   159  55   HOH HOH E . 
CA 3 HOH 6   160  122  HOH HOH E . 
CA 3 HOH 7   161  125  HOH HOH E . 
CA 3 HOH 8   162  129  HOH HOH E . 
CA 3 HOH 9   165  165  HOH HOH E . 
CA 3 HOH 10  171  171  HOH HOH E . 
CA 3 HOH 11  176  176  HOH HOH E . 
CA 3 HOH 12  222  222  HOH HOH E . 
CA 3 HOH 13  227  227  HOH HOH E . 
CA 3 HOH 14  249  249  HOH HOH E . 
CA 3 HOH 15  272  272  HOH HOH E . 
CA 3 HOH 16  273  273  HOH HOH E . 
CA 3 HOH 17  338  338  HOH HOH E . 
CA 3 HOH 18  361  361  HOH HOH E . 
CA 3 HOH 19  392  392  HOH HOH E . 
CA 3 HOH 20  400  400  HOH HOH E . 
CA 3 HOH 21  408  408  HOH HOH E . 
CA 3 HOH 22  438  438  HOH HOH E . 
CA 3 HOH 23  448  448  HOH HOH E . 
CA 3 HOH 24  450  450  HOH HOH E . 
CA 3 HOH 25  453  453  HOH HOH E . 
CA 3 HOH 26  467  467  HOH HOH E . 
CA 3 HOH 27  491  491  HOH HOH E . 
CA 3 HOH 28  525  525  HOH HOH E . 
CA 3 HOH 29  556  556  HOH HOH E . 
CA 3 HOH 30  562  562  HOH HOH E . 
CA 3 HOH 31  573  573  HOH HOH E . 
CA 3 HOH 32  588  588  HOH HOH E . 
CA 3 HOH 33  592  592  HOH HOH E . 
CA 3 HOH 34  608  608  HOH HOH E . 
CA 3 HOH 35  618  618  HOH HOH E . 
CA 3 HOH 36  639  639  HOH HOH E . 
CA 3 HOH 37  642  642  HOH HOH E . 
CA 3 HOH 38  644  644  HOH HOH E . 
CA 3 HOH 39  665  665  HOH HOH E . 
CA 3 HOH 40  683  683  HOH HOH E . 
CA 3 HOH 41  686  686  HOH HOH E . 
CA 3 HOH 42  687  687  HOH HOH E . 
CA 3 HOH 43  703  703  HOH HOH E . 
CA 3 HOH 44  733  733  HOH HOH E . 
CA 3 HOH 45  746  746  HOH HOH E . 
CA 3 HOH 46  768  768  HOH HOH E . 
CA 3 HOH 47  774  774  HOH HOH E . 
CA 3 HOH 48  836  836  HOH HOH E . 
CA 3 HOH 49  863  863  HOH HOH E . 
CA 3 HOH 50  920  920  HOH HOH E . 
CA 3 HOH 51  929  929  HOH HOH E . 
CA 3 HOH 52  958  958  HOH HOH E . 
CA 3 HOH 53  970  970  HOH HOH E . 
CA 3 HOH 54  973  973  HOH HOH E . 
CA 3 HOH 55  975  975  HOH HOH E . 
CA 3 HOH 56  985  985  HOH HOH E . 
CA 3 HOH 57  997  997  HOH HOH E . 
CA 3 HOH 58  1002 1002 HOH HOH E . 
CA 3 HOH 59  1005 1005 HOH HOH E . 
CA 3 HOH 60  1009 1009 HOH HOH E . 
CA 3 HOH 61  1015 1015 HOH HOH E . 
CA 3 HOH 62  1034 1034 HOH HOH E . 
CA 3 HOH 63  1057 1057 HOH HOH E . 
CA 3 HOH 64  1105 1105 HOH HOH E . 
CA 3 HOH 65  1169 1169 HOH HOH E . 
CA 3 HOH 66  1175 1175 HOH HOH E . 
CA 3 HOH 67  1181 1181 HOH HOH E . 
CA 3 HOH 68  1184 1184 HOH HOH E . 
CA 3 HOH 69  1210 1210 HOH HOH E . 
CA 3 HOH 70  1212 1212 HOH HOH E . 
CA 3 HOH 71  1248 1248 HOH HOH E . 
CA 3 HOH 72  1306 1306 HOH HOH E . 
CA 3 HOH 73  1332 1332 HOH HOH E . 
CA 3 HOH 74  1355 1355 HOH HOH E . 
CA 3 HOH 75  1360 1360 HOH HOH E . 
CA 3 HOH 76  1411 1411 HOH HOH E . 
CA 3 HOH 77  1416 1416 HOH HOH E . 
CA 3 HOH 78  1461 1461 HOH HOH E . 
CA 3 HOH 79  1472 1472 HOH HOH E . 
CA 3 HOH 80  1476 1476 HOH HOH E . 
CA 3 HOH 81  1493 1493 HOH HOH E . 
CA 3 HOH 82  1495 1495 HOH HOH E . 
CA 3 HOH 83  1498 1498 HOH HOH E . 
CA 3 HOH 84  1522 1522 HOH HOH E . 
CA 3 HOH 85  1583 1583 HOH HOH E . 
CA 3 HOH 86  1606 1606 HOH HOH E . 
CA 3 HOH 87  1638 1638 HOH HOH E . 
CA 3 HOH 88  1720 1720 HOH HOH E . 
CA 3 HOH 89  1741 1741 HOH HOH E . 
CA 3 HOH 90  1773 1773 HOH HOH E . 
CA 3 HOH 91  1779 1779 HOH HOH E . 
DA 3 HOH 1   154  7    HOH HOH F . 
DA 3 HOH 2   156  19   HOH HOH F . 
DA 3 HOH 3   157  37   HOH HOH F . 
DA 3 HOH 4   158  43   HOH HOH F . 
DA 3 HOH 5   159  159  HOH HOH F . 
DA 3 HOH 6   160  73   HOH HOH F . 
DA 3 HOH 7   161  87   HOH HOH F . 
DA 3 HOH 8   162  101  HOH HOH F . 
DA 3 HOH 9   163  106  HOH HOH F . 
DA 3 HOH 10  164  110  HOH HOH F . 
DA 3 HOH 11  165  127  HOH HOH F . 
DA 3 HOH 12  166  131  HOH HOH F . 
DA 3 HOH 13  167  144  HOH HOH F . 
DA 3 HOH 14  168  151  HOH HOH F . 
DA 3 HOH 15  169  169  HOH HOH F . 
DA 3 HOH 16  174  174  HOH HOH F . 
DA 3 HOH 17  182  182  HOH HOH F . 
DA 3 HOH 18  194  194  HOH HOH F . 
DA 3 HOH 19  207  207  HOH HOH F . 
DA 3 HOH 20  213  213  HOH HOH F . 
DA 3 HOH 21  226  226  HOH HOH F . 
DA 3 HOH 22  233  233  HOH HOH F . 
DA 3 HOH 23  256  256  HOH HOH F . 
DA 3 HOH 24  258  258  HOH HOH F . 
DA 3 HOH 25  264  264  HOH HOH F . 
DA 3 HOH 26  289  289  HOH HOH F . 
DA 3 HOH 27  318  318  HOH HOH F . 
DA 3 HOH 28  324  324  HOH HOH F . 
DA 3 HOH 29  332  332  HOH HOH F . 
DA 3 HOH 30  340  340  HOH HOH F . 
DA 3 HOH 31  363  363  HOH HOH F . 
DA 3 HOH 32  365  365  HOH HOH F . 
DA 3 HOH 33  375  375  HOH HOH F . 
DA 3 HOH 34  402  402  HOH HOH F . 
DA 3 HOH 35  428  428  HOH HOH F . 
DA 3 HOH 36  435  435  HOH HOH F . 
DA 3 HOH 37  436  436  HOH HOH F . 
DA 3 HOH 38  456  456  HOH HOH F . 
DA 3 HOH 39  488  488  HOH HOH F . 
DA 3 HOH 40  496  496  HOH HOH F . 
DA 3 HOH 41  515  515  HOH HOH F . 
DA 3 HOH 42  519  519  HOH HOH F . 
DA 3 HOH 43  532  532  HOH HOH F . 
DA 3 HOH 44  533  533  HOH HOH F . 
DA 3 HOH 45  535  535  HOH HOH F . 
DA 3 HOH 46  543  543  HOH HOH F . 
DA 3 HOH 47  571  571  HOH HOH F . 
DA 3 HOH 48  583  583  HOH HOH F . 
DA 3 HOH 49  597  597  HOH HOH F . 
DA 3 HOH 50  640  640  HOH HOH F . 
DA 3 HOH 51  671  671  HOH HOH F . 
DA 3 HOH 52  725  725  HOH HOH F . 
DA 3 HOH 53  777  777  HOH HOH F . 
DA 3 HOH 54  803  803  HOH HOH F . 
DA 3 HOH 55  813  813  HOH HOH F . 
DA 3 HOH 56  851  851  HOH HOH F . 
DA 3 HOH 57  869  869  HOH HOH F . 
DA 3 HOH 58  927  927  HOH HOH F . 
DA 3 HOH 59  972  972  HOH HOH F . 
DA 3 HOH 60  999  999  HOH HOH F . 
DA 3 HOH 61  1021 1021 HOH HOH F . 
DA 3 HOH 62  1022 1022 HOH HOH F . 
DA 3 HOH 63  1032 1032 HOH HOH F . 
DA 3 HOH 64  1052 1052 HOH HOH F . 
DA 3 HOH 65  1059 1059 HOH HOH F . 
DA 3 HOH 66  1098 1098 HOH HOH F . 
DA 3 HOH 67  1112 1112 HOH HOH F . 
DA 3 HOH 68  1115 1115 HOH HOH F . 
DA 3 HOH 69  1140 1140 HOH HOH F . 
DA 3 HOH 70  1155 1155 HOH HOH F . 
DA 3 HOH 71  1180 1180 HOH HOH F . 
DA 3 HOH 72  1202 1202 HOH HOH F . 
DA 3 HOH 73  1211 1211 HOH HOH F . 
DA 3 HOH 74  1232 1232 HOH HOH F . 
DA 3 HOH 75  1273 1273 HOH HOH F . 
DA 3 HOH 76  1294 1294 HOH HOH F . 
DA 3 HOH 77  1295 1295 HOH HOH F . 
DA 3 HOH 78  1302 1302 HOH HOH F . 
DA 3 HOH 79  1314 1314 HOH HOH F . 
DA 3 HOH 80  1315 1315 HOH HOH F . 
DA 3 HOH 81  1324 1324 HOH HOH F . 
DA 3 HOH 82  1334 1334 HOH HOH F . 
DA 3 HOH 83  1335 1335 HOH HOH F . 
DA 3 HOH 84  1358 1358 HOH HOH F . 
DA 3 HOH 85  1362 1362 HOH HOH F . 
DA 3 HOH 86  1364 1364 HOH HOH F . 
DA 3 HOH 87  1365 1365 HOH HOH F . 
DA 3 HOH 88  1371 1371 HOH HOH F . 
DA 3 HOH 89  1381 1381 HOH HOH F . 
DA 3 HOH 90  1388 1388 HOH HOH F . 
DA 3 HOH 91  1403 1403 HOH HOH F . 
DA 3 HOH 92  1404 1404 HOH HOH F . 
DA 3 HOH 93  1406 1406 HOH HOH F . 
DA 3 HOH 94  1422 1422 HOH HOH F . 
DA 3 HOH 95  1423 1423 HOH HOH F . 
DA 3 HOH 96  1424 1424 HOH HOH F . 
DA 3 HOH 97  1433 1433 HOH HOH F . 
DA 3 HOH 98  1480 1480 HOH HOH F . 
DA 3 HOH 99  1481 1481 HOH HOH F . 
DA 3 HOH 100 1496 1496 HOH HOH F . 
DA 3 HOH 101 1497 1497 HOH HOH F . 
DA 3 HOH 102 1501 1501 HOH HOH F . 
DA 3 HOH 103 1506 1506 HOH HOH F . 
DA 3 HOH 104 1507 1507 HOH HOH F . 
DA 3 HOH 105 1508 1508 HOH HOH F . 
DA 3 HOH 106 1521 1521 HOH HOH F . 
DA 3 HOH 107 1523 1523 HOH HOH F . 
DA 3 HOH 108 1537 1537 HOH HOH F . 
DA 3 HOH 109 1541 1541 HOH HOH F . 
DA 3 HOH 110 1574 1574 HOH HOH F . 
DA 3 HOH 111 1592 1592 HOH HOH F . 
DA 3 HOH 112 1608 1608 HOH HOH F . 
DA 3 HOH 113 1631 1631 HOH HOH F . 
DA 3 HOH 114 1644 1644 HOH HOH F . 
DA 3 HOH 115 1658 1658 HOH HOH F . 
DA 3 HOH 116 1672 1672 HOH HOH F . 
DA 3 HOH 117 1675 1675 HOH HOH F . 
DA 3 HOH 118 1682 1682 HOH HOH F . 
DA 3 HOH 119 1689 1689 HOH HOH F . 
DA 3 HOH 120 1709 1709 HOH HOH F . 
DA 3 HOH 121 1712 1712 HOH HOH F . 
DA 3 HOH 122 1727 1727 HOH HOH F . 
DA 3 HOH 123 1733 1733 HOH HOH F . 
DA 3 HOH 124 1750 1750 HOH HOH F . 
DA 3 HOH 125 1754 1754 HOH HOH F . 
DA 3 HOH 126 1771 1771 HOH HOH F . 
DA 3 HOH 127 1783 1783 HOH HOH F . 
DA 3 HOH 128 1785 1785 HOH HOH F . 
DA 3 HOH 129 1796 1796 HOH HOH F . 
DA 3 HOH 130 1803 1803 HOH HOH F . 
EA 3 HOH 1   154  10   HOH HOH G . 
EA 3 HOH 2   156  14   HOH HOH G . 
EA 3 HOH 3   157  28   HOH HOH G . 
EA 3 HOH 4   158  30   HOH HOH G . 
EA 3 HOH 5   159  33   HOH HOH G . 
EA 3 HOH 6   160  51   HOH HOH G . 
EA 3 HOH 7   161  58   HOH HOH G . 
EA 3 HOH 8   162  70   HOH HOH G . 
EA 3 HOH 9   163  85   HOH HOH G . 
EA 3 HOH 10  164  164  HOH HOH G . 
EA 3 HOH 11  165  88   HOH HOH G . 
EA 3 HOH 12  166  93   HOH HOH G . 
EA 3 HOH 13  167  104  HOH HOH G . 
EA 3 HOH 14  168  105  HOH HOH G . 
EA 3 HOH 15  169  114  HOH HOH G . 
EA 3 HOH 16  170  117  HOH HOH G . 
EA 3 HOH 17  171  128  HOH HOH G . 
EA 3 HOH 18  172  141  HOH HOH G . 
EA 3 HOH 19  173  149  HOH HOH G . 
EA 3 HOH 20  177  177  HOH HOH G . 
EA 3 HOH 21  189  189  HOH HOH G . 
EA 3 HOH 22  192  192  HOH HOH G . 
EA 3 HOH 23  193  193  HOH HOH G . 
EA 3 HOH 24  197  197  HOH HOH G . 
EA 3 HOH 25  205  205  HOH HOH G . 
EA 3 HOH 26  224  224  HOH HOH G . 
EA 3 HOH 27  234  234  HOH HOH G . 
EA 3 HOH 28  235  235  HOH HOH G . 
EA 3 HOH 29  240  240  HOH HOH G . 
EA 3 HOH 30  251  251  HOH HOH G . 
EA 3 HOH 31  265  265  HOH HOH G . 
EA 3 HOH 32  283  283  HOH HOH G . 
EA 3 HOH 33  285  285  HOH HOH G . 
EA 3 HOH 34  288  288  HOH HOH G . 
EA 3 HOH 35  306  306  HOH HOH G . 
EA 3 HOH 36  307  307  HOH HOH G . 
EA 3 HOH 37  309  309  HOH HOH G . 
EA 3 HOH 38  320  320  HOH HOH G . 
EA 3 HOH 39  325  325  HOH HOH G . 
EA 3 HOH 40  355  355  HOH HOH G . 
EA 3 HOH 41  387  387  HOH HOH G . 
EA 3 HOH 42  415  415  HOH HOH G . 
EA 3 HOH 43  423  423  HOH HOH G . 
EA 3 HOH 44  430  430  HOH HOH G . 
EA 3 HOH 45  437  437  HOH HOH G . 
EA 3 HOH 46  454  454  HOH HOH G . 
EA 3 HOH 47  457  457  HOH HOH G . 
EA 3 HOH 48  458  458  HOH HOH G . 
EA 3 HOH 49  466  466  HOH HOH G . 
EA 3 HOH 50  476  476  HOH HOH G . 
EA 3 HOH 51  503  503  HOH HOH G . 
EA 3 HOH 52  509  509  HOH HOH G . 
EA 3 HOH 53  541  541  HOH HOH G . 
EA 3 HOH 54  544  544  HOH HOH G . 
EA 3 HOH 55  659  659  HOH HOH G . 
EA 3 HOH 56  708  708  HOH HOH G . 
EA 3 HOH 57  713  713  HOH HOH G . 
EA 3 HOH 58  720  720  HOH HOH G . 
EA 3 HOH 59  749  749  HOH HOH G . 
EA 3 HOH 60  754  754  HOH HOH G . 
EA 3 HOH 61  756  756  HOH HOH G . 
EA 3 HOH 62  757  757  HOH HOH G . 
EA 3 HOH 63  781  781  HOH HOH G . 
EA 3 HOH 64  795  795  HOH HOH G . 
EA 3 HOH 65  799  799  HOH HOH G . 
EA 3 HOH 66  810  810  HOH HOH G . 
EA 3 HOH 67  811  811  HOH HOH G . 
EA 3 HOH 68  816  816  HOH HOH G . 
EA 3 HOH 69  832  832  HOH HOH G . 
EA 3 HOH 70  848  848  HOH HOH G . 
EA 3 HOH 71  861  861  HOH HOH G . 
EA 3 HOH 72  871  871  HOH HOH G . 
EA 3 HOH 73  886  886  HOH HOH G . 
EA 3 HOH 74  921  921  HOH HOH G . 
EA 3 HOH 75  940  940  HOH HOH G . 
EA 3 HOH 76  943  943  HOH HOH G . 
EA 3 HOH 77  947  947  HOH HOH G . 
EA 3 HOH 78  962  962  HOH HOH G . 
EA 3 HOH 79  971  971  HOH HOH G . 
EA 3 HOH 80  974  974  HOH HOH G . 
EA 3 HOH 81  980  980  HOH HOH G . 
EA 3 HOH 82  987  987  HOH HOH G . 
EA 3 HOH 83  991  991  HOH HOH G . 
EA 3 HOH 84  1053 1053 HOH HOH G . 
EA 3 HOH 85  1070 1070 HOH HOH G . 
EA 3 HOH 86  1079 1079 HOH HOH G . 
EA 3 HOH 87  1080 1080 HOH HOH G . 
EA 3 HOH 88  1093 1093 HOH HOH G . 
EA 3 HOH 89  1097 1097 HOH HOH G . 
EA 3 HOH 90  1109 1109 HOH HOH G . 
EA 3 HOH 91  1122 1122 HOH HOH G . 
EA 3 HOH 92  1143 1143 HOH HOH G . 
EA 3 HOH 93  1173 1173 HOH HOH G . 
EA 3 HOH 94  1185 1185 HOH HOH G . 
EA 3 HOH 95  1200 1200 HOH HOH G . 
EA 3 HOH 96  1215 1215 HOH HOH G . 
EA 3 HOH 97  1223 1223 HOH HOH G . 
EA 3 HOH 98  1225 1225 HOH HOH G . 
EA 3 HOH 99  1231 1231 HOH HOH G . 
EA 3 HOH 100 1238 1238 HOH HOH G . 
EA 3 HOH 101 1240 1240 HOH HOH G . 
EA 3 HOH 102 1254 1254 HOH HOH G . 
EA 3 HOH 103 1258 1258 HOH HOH G . 
EA 3 HOH 104 1265 1265 HOH HOH G . 
EA 3 HOH 105 1266 1266 HOH HOH G . 
EA 3 HOH 106 1279 1279 HOH HOH G . 
EA 3 HOH 107 1288 1288 HOH HOH G . 
EA 3 HOH 108 1337 1337 HOH HOH G . 
EA 3 HOH 109 1339 1339 HOH HOH G . 
EA 3 HOH 110 1346 1346 HOH HOH G . 
EA 3 HOH 111 1351 1351 HOH HOH G . 
EA 3 HOH 112 1361 1361 HOH HOH G . 
EA 3 HOH 113 1375 1375 HOH HOH G . 
EA 3 HOH 114 1395 1395 HOH HOH G . 
EA 3 HOH 115 1397 1397 HOH HOH G . 
EA 3 HOH 116 1410 1410 HOH HOH G . 
EA 3 HOH 117 1421 1421 HOH HOH G . 
EA 3 HOH 118 1425 1425 HOH HOH G . 
EA 3 HOH 119 1427 1427 HOH HOH G . 
EA 3 HOH 120 1438 1438 HOH HOH G . 
EA 3 HOH 121 1449 1449 HOH HOH G . 
EA 3 HOH 122 1479 1479 HOH HOH G . 
EA 3 HOH 123 1484 1484 HOH HOH G . 
EA 3 HOH 124 1492 1492 HOH HOH G . 
EA 3 HOH 125 1499 1499 HOH HOH G . 
EA 3 HOH 126 1505 1505 HOH HOH G . 
EA 3 HOH 127 1515 1515 HOH HOH G . 
EA 3 HOH 128 1520 1520 HOH HOH G . 
EA 3 HOH 129 1524 1524 HOH HOH G . 
EA 3 HOH 130 1526 1526 HOH HOH G . 
EA 3 HOH 131 1529 1529 HOH HOH G . 
EA 3 HOH 132 1531 1531 HOH HOH G . 
EA 3 HOH 133 1533 1533 HOH HOH G . 
EA 3 HOH 134 1534 1534 HOH HOH G . 
EA 3 HOH 135 1538 1538 HOH HOH G . 
EA 3 HOH 136 1547 1547 HOH HOH G . 
EA 3 HOH 137 1551 1551 HOH HOH G . 
EA 3 HOH 138 1590 1590 HOH HOH G . 
EA 3 HOH 139 1596 1596 HOH HOH G . 
EA 3 HOH 140 1601 1601 HOH HOH G . 
EA 3 HOH 141 1602 1602 HOH HOH G . 
EA 3 HOH 142 1603 1603 HOH HOH G . 
EA 3 HOH 143 1605 1605 HOH HOH G . 
EA 3 HOH 144 1607 1607 HOH HOH G . 
EA 3 HOH 145 1609 1609 HOH HOH G . 
EA 3 HOH 146 1613 1613 HOH HOH G . 
EA 3 HOH 147 1618 1618 HOH HOH G . 
EA 3 HOH 148 1628 1628 HOH HOH G . 
EA 3 HOH 149 1645 1645 HOH HOH G . 
EA 3 HOH 150 1659 1659 HOH HOH G . 
EA 3 HOH 151 1664 1664 HOH HOH G . 
EA 3 HOH 152 1665 1665 HOH HOH G . 
EA 3 HOH 153 1683 1683 HOH HOH G . 
EA 3 HOH 154 1688 1688 HOH HOH G . 
EA 3 HOH 155 1710 1710 HOH HOH G . 
EA 3 HOH 156 1728 1728 HOH HOH G . 
EA 3 HOH 157 1732 1732 HOH HOH G . 
EA 3 HOH 158 1739 1739 HOH HOH G . 
EA 3 HOH 159 1744 1744 HOH HOH G . 
EA 3 HOH 160 1746 1746 HOH HOH G . 
EA 3 HOH 161 1758 1758 HOH HOH G . 
EA 3 HOH 162 1774 1774 HOH HOH G . 
EA 3 HOH 163 1775 1775 HOH HOH G . 
EA 3 HOH 164 1784 1784 HOH HOH G . 
EA 3 HOH 165 1799 1799 HOH HOH G . 
EA 3 HOH 166 1806 1806 HOH HOH G . 
FA 3 HOH 1   154  2    HOH HOH H . 
FA 3 HOH 2   156  5    HOH HOH H . 
FA 3 HOH 3   157  157  HOH HOH H . 
FA 3 HOH 4   158  15   HOH HOH H . 
FA 3 HOH 5   159  17   HOH HOH H . 
FA 3 HOH 6   160  18   HOH HOH H . 
FA 3 HOH 7   161  23   HOH HOH H . 
FA 3 HOH 8   162  162  HOH HOH H . 
FA 3 HOH 9   163  26   HOH HOH H . 
FA 3 HOH 10  164  41   HOH HOH H . 
FA 3 HOH 11  165  44   HOH HOH H . 
FA 3 HOH 12  166  49   HOH HOH H . 
FA 3 HOH 13  167  62   HOH HOH H . 
FA 3 HOH 14  168  65   HOH HOH H . 
FA 3 HOH 15  169  71   HOH HOH H . 
FA 3 HOH 16  170  170  HOH HOH H . 
FA 3 HOH 17  171  72   HOH HOH H . 
FA 3 HOH 18  172  172  HOH HOH H . 
FA 3 HOH 19  173  77   HOH HOH H . 
FA 3 HOH 20  174  116  HOH HOH H . 
FA 3 HOH 21  175  123  HOH HOH H . 
FA 3 HOH 22  176  134  HOH HOH H . 
FA 3 HOH 23  177  137  HOH HOH H . 
FA 3 HOH 24  178  142  HOH HOH H . 
FA 3 HOH 25  195  195  HOH HOH H . 
FA 3 HOH 26  209  209  HOH HOH H . 
FA 3 HOH 27  215  215  HOH HOH H . 
FA 3 HOH 28  217  217  HOH HOH H . 
FA 3 HOH 29  242  242  HOH HOH H . 
FA 3 HOH 30  244  244  HOH HOH H . 
FA 3 HOH 31  253  253  HOH HOH H . 
FA 3 HOH 32  259  259  HOH HOH H . 
FA 3 HOH 33  263  263  HOH HOH H . 
FA 3 HOH 34  268  268  HOH HOH H . 
FA 3 HOH 35  295  295  HOH HOH H . 
FA 3 HOH 36  301  301  HOH HOH H . 
FA 3 HOH 37  326  326  HOH HOH H . 
FA 3 HOH 38  337  337  HOH HOH H . 
FA 3 HOH 39  346  346  HOH HOH H . 
FA 3 HOH 40  350  350  HOH HOH H . 
FA 3 HOH 41  358  358  HOH HOH H . 
FA 3 HOH 42  371  371  HOH HOH H . 
FA 3 HOH 43  379  379  HOH HOH H . 
FA 3 HOH 44  380  380  HOH HOH H . 
FA 3 HOH 45  386  386  HOH HOH H . 
FA 3 HOH 46  396  396  HOH HOH H . 
FA 3 HOH 47  398  398  HOH HOH H . 
FA 3 HOH 48  410  410  HOH HOH H . 
FA 3 HOH 49  431  431  HOH HOH H . 
FA 3 HOH 50  432  432  HOH HOH H . 
FA 3 HOH 51  463  463  HOH HOH H . 
FA 3 HOH 52  478  478  HOH HOH H . 
FA 3 HOH 53  483  483  HOH HOH H . 
FA 3 HOH 54  492  492  HOH HOH H . 
FA 3 HOH 55  493  493  HOH HOH H . 
FA 3 HOH 56  494  494  HOH HOH H . 
FA 3 HOH 57  495  495  HOH HOH H . 
FA 3 HOH 58  499  499  HOH HOH H . 
FA 3 HOH 59  500  500  HOH HOH H . 
FA 3 HOH 60  506  506  HOH HOH H . 
FA 3 HOH 61  512  512  HOH HOH H . 
FA 3 HOH 62  514  514  HOH HOH H . 
FA 3 HOH 63  521  521  HOH HOH H . 
FA 3 HOH 64  529  529  HOH HOH H . 
FA 3 HOH 65  550  550  HOH HOH H . 
FA 3 HOH 66  566  566  HOH HOH H . 
FA 3 HOH 67  575  575  HOH HOH H . 
FA 3 HOH 68  587  587  HOH HOH H . 
FA 3 HOH 69  594  594  HOH HOH H . 
FA 3 HOH 70  606  606  HOH HOH H . 
FA 3 HOH 71  615  615  HOH HOH H . 
FA 3 HOH 72  619  619  HOH HOH H . 
FA 3 HOH 73  622  622  HOH HOH H . 
FA 3 HOH 74  624  624  HOH HOH H . 
FA 3 HOH 75  626  626  HOH HOH H . 
FA 3 HOH 76  648  648  HOH HOH H . 
FA 3 HOH 77  666  666  HOH HOH H . 
FA 3 HOH 78  676  676  HOH HOH H . 
FA 3 HOH 79  684  684  HOH HOH H . 
FA 3 HOH 80  689  689  HOH HOH H . 
FA 3 HOH 81  698  698  HOH HOH H . 
FA 3 HOH 82  707  707  HOH HOH H . 
FA 3 HOH 83  717  717  HOH HOH H . 
FA 3 HOH 84  721  721  HOH HOH H . 
FA 3 HOH 85  729  729  HOH HOH H . 
FA 3 HOH 86  742  742  HOH HOH H . 
FA 3 HOH 87  744  744  HOH HOH H . 
FA 3 HOH 88  748  748  HOH HOH H . 
FA 3 HOH 89  753  753  HOH HOH H . 
FA 3 HOH 90  762  762  HOH HOH H . 
FA 3 HOH 91  780  780  HOH HOH H . 
FA 3 HOH 92  788  788  HOH HOH H . 
FA 3 HOH 93  793  793  HOH HOH H . 
FA 3 HOH 94  794  794  HOH HOH H . 
FA 3 HOH 95  815  815  HOH HOH H . 
FA 3 HOH 96  842  842  HOH HOH H . 
FA 3 HOH 97  843  843  HOH HOH H . 
FA 3 HOH 98  846  846  HOH HOH H . 
FA 3 HOH 99  854  854  HOH HOH H . 
FA 3 HOH 100 866  866  HOH HOH H . 
FA 3 HOH 101 877  877  HOH HOH H . 
FA 3 HOH 102 879  879  HOH HOH H . 
FA 3 HOH 103 887  887  HOH HOH H . 
FA 3 HOH 104 890  890  HOH HOH H . 
FA 3 HOH 105 896  896  HOH HOH H . 
FA 3 HOH 106 905  905  HOH HOH H . 
FA 3 HOH 107 907  907  HOH HOH H . 
FA 3 HOH 108 916  916  HOH HOH H . 
FA 3 HOH 109 937  937  HOH HOH H . 
FA 3 HOH 110 939  939  HOH HOH H . 
FA 3 HOH 111 946  946  HOH HOH H . 
FA 3 HOH 112 956  956  HOH HOH H . 
FA 3 HOH 113 968  968  HOH HOH H . 
FA 3 HOH 114 996  996  HOH HOH H . 
FA 3 HOH 115 1003 1003 HOH HOH H . 
FA 3 HOH 116 1029 1029 HOH HOH H . 
FA 3 HOH 117 1033 1033 HOH HOH H . 
FA 3 HOH 118 1041 1041 HOH HOH H . 
FA 3 HOH 119 1047 1047 HOH HOH H . 
FA 3 HOH 120 1064 1064 HOH HOH H . 
FA 3 HOH 121 1073 1073 HOH HOH H . 
FA 3 HOH 122 1075 1075 HOH HOH H . 
FA 3 HOH 123 1081 1081 HOH HOH H . 
FA 3 HOH 124 1082 1082 HOH HOH H . 
FA 3 HOH 125 1085 1085 HOH HOH H . 
FA 3 HOH 126 1088 1088 HOH HOH H . 
FA 3 HOH 127 1096 1096 HOH HOH H . 
FA 3 HOH 128 1118 1118 HOH HOH H . 
FA 3 HOH 129 1129 1129 HOH HOH H . 
FA 3 HOH 130 1151 1151 HOH HOH H . 
FA 3 HOH 131 1157 1157 HOH HOH H . 
FA 3 HOH 132 1158 1158 HOH HOH H . 
FA 3 HOH 133 1198 1198 HOH HOH H . 
FA 3 HOH 134 1201 1201 HOH HOH H . 
FA 3 HOH 135 1213 1213 HOH HOH H . 
FA 3 HOH 136 1216 1216 HOH HOH H . 
FA 3 HOH 137 1224 1224 HOH HOH H . 
FA 3 HOH 138 1261 1261 HOH HOH H . 
FA 3 HOH 139 1272 1272 HOH HOH H . 
FA 3 HOH 140 1299 1299 HOH HOH H . 
FA 3 HOH 141 1304 1304 HOH HOH H . 
FA 3 HOH 142 1336 1336 HOH HOH H . 
FA 3 HOH 143 1345 1345 HOH HOH H . 
FA 3 HOH 144 1368 1368 HOH HOH H . 
FA 3 HOH 145 1370 1370 HOH HOH H . 
FA 3 HOH 146 1372 1372 HOH HOH H . 
FA 3 HOH 147 1391 1391 HOH HOH H . 
FA 3 HOH 148 1393 1393 HOH HOH H . 
FA 3 HOH 149 1412 1412 HOH HOH H . 
FA 3 HOH 150 1426 1426 HOH HOH H . 
FA 3 HOH 151 1431 1431 HOH HOH H . 
FA 3 HOH 152 1432 1432 HOH HOH H . 
FA 3 HOH 153 1437 1437 HOH HOH H . 
FA 3 HOH 154 1459 1459 HOH HOH H . 
FA 3 HOH 155 1462 1462 HOH HOH H . 
FA 3 HOH 156 1464 1464 HOH HOH H . 
FA 3 HOH 157 1503 1503 HOH HOH H . 
FA 3 HOH 158 1553 1553 HOH HOH H . 
FA 3 HOH 159 1563 1563 HOH HOH H . 
FA 3 HOH 160 1567 1567 HOH HOH H . 
FA 3 HOH 161 1568 1568 HOH HOH H . 
FA 3 HOH 162 1579 1579 HOH HOH H . 
FA 3 HOH 163 1587 1587 HOH HOH H . 
FA 3 HOH 164 1593 1593 HOH HOH H . 
FA 3 HOH 165 1595 1595 HOH HOH H . 
FA 3 HOH 166 1619 1619 HOH HOH H . 
FA 3 HOH 167 1637 1637 HOH HOH H . 
FA 3 HOH 168 1642 1642 HOH HOH H . 
FA 3 HOH 169 1670 1670 HOH HOH H . 
FA 3 HOH 170 1671 1671 HOH HOH H . 
FA 3 HOH 171 1680 1680 HOH HOH H . 
FA 3 HOH 172 1681 1681 HOH HOH H . 
FA 3 HOH 173 1697 1697 HOH HOH H . 
FA 3 HOH 174 1698 1698 HOH HOH H . 
FA 3 HOH 175 1745 1745 HOH HOH H . 
FA 3 HOH 176 1752 1752 HOH HOH H . 
FA 3 HOH 177 1755 1755 HOH HOH H . 
FA 3 HOH 178 1756 1756 HOH HOH H . 
FA 3 HOH 179 1757 1757 HOH HOH H . 
FA 3 HOH 180 1759 1759 HOH HOH H . 
FA 3 HOH 181 1760 1760 HOH HOH H . 
FA 3 HOH 182 1787 1787 HOH HOH H . 
FA 3 HOH 183 1792 1792 HOH HOH H . 
FA 3 HOH 184 1804 1804 HOH HOH H . 
FA 3 HOH 185 1805 1805 HOH HOH H . 
GA 3 HOH 1   154  29   HOH HOH I . 
GA 3 HOH 2   156  38   HOH HOH I . 
GA 3 HOH 3   157  39   HOH HOH I . 
GA 3 HOH 4   158  158  HOH HOH I . 
GA 3 HOH 5   159  40   HOH HOH I . 
GA 3 HOH 6   160  53   HOH HOH I . 
GA 3 HOH 7   161  161  HOH HOH I . 
GA 3 HOH 8   162  57   HOH HOH I . 
GA 3 HOH 9   163  84   HOH HOH I . 
GA 3 HOH 10  164  89   HOH HOH I . 
GA 3 HOH 11  165  109  HOH HOH I . 
GA 3 HOH 12  166  145  HOH HOH I . 
GA 3 HOH 13  167  167  HOH HOH I . 
GA 3 HOH 14  199  199  HOH HOH I . 
GA 3 HOH 15  201  201  HOH HOH I . 
GA 3 HOH 16  203  203  HOH HOH I . 
GA 3 HOH 17  229  229  HOH HOH I . 
GA 3 HOH 18  231  231  HOH HOH I . 
GA 3 HOH 19  236  236  HOH HOH I . 
GA 3 HOH 20  248  248  HOH HOH I . 
GA 3 HOH 21  255  255  HOH HOH I . 
GA 3 HOH 22  277  277  HOH HOH I . 
GA 3 HOH 23  287  287  HOH HOH I . 
GA 3 HOH 24  305  305  HOH HOH I . 
GA 3 HOH 25  322  322  HOH HOH I . 
GA 3 HOH 26  344  344  HOH HOH I . 
GA 3 HOH 27  347  347  HOH HOH I . 
GA 3 HOH 28  348  348  HOH HOH I . 
GA 3 HOH 29  351  351  HOH HOH I . 
GA 3 HOH 30  354  354  HOH HOH I . 
GA 3 HOH 31  366  366  HOH HOH I . 
GA 3 HOH 32  368  368  HOH HOH I . 
GA 3 HOH 33  373  373  HOH HOH I . 
GA 3 HOH 34  384  384  HOH HOH I . 
GA 3 HOH 35  388  388  HOH HOH I . 
GA 3 HOH 36  399  399  HOH HOH I . 
GA 3 HOH 37  405  405  HOH HOH I . 
GA 3 HOH 38  433  433  HOH HOH I . 
GA 3 HOH 39  460  460  HOH HOH I . 
GA 3 HOH 40  479  479  HOH HOH I . 
GA 3 HOH 41  513  513  HOH HOH I . 
GA 3 HOH 42  520  520  HOH HOH I . 
GA 3 HOH 43  542  542  HOH HOH I . 
GA 3 HOH 44  557  557  HOH HOH I . 
GA 3 HOH 45  580  580  HOH HOH I . 
GA 3 HOH 46  585  585  HOH HOH I . 
GA 3 HOH 47  599  599  HOH HOH I . 
GA 3 HOH 48  603  603  HOH HOH I . 
GA 3 HOH 49  612  612  HOH HOH I . 
GA 3 HOH 50  621  621  HOH HOH I . 
GA 3 HOH 51  637  637  HOH HOH I . 
GA 3 HOH 52  641  641  HOH HOH I . 
GA 3 HOH 53  646  646  HOH HOH I . 
GA 3 HOH 54  649  649  HOH HOH I . 
GA 3 HOH 55  656  656  HOH HOH I . 
GA 3 HOH 56  668  668  HOH HOH I . 
GA 3 HOH 57  688  688  HOH HOH I . 
GA 3 HOH 58  692  692  HOH HOH I . 
GA 3 HOH 59  694  694  HOH HOH I . 
GA 3 HOH 60  710  710  HOH HOH I . 
GA 3 HOH 61  741  741  HOH HOH I . 
GA 3 HOH 62  743  743  HOH HOH I . 
GA 3 HOH 63  759  759  HOH HOH I . 
GA 3 HOH 64  770  770  HOH HOH I . 
GA 3 HOH 65  790  790  HOH HOH I . 
GA 3 HOH 66  844  844  HOH HOH I . 
GA 3 HOH 67  875  875  HOH HOH I . 
GA 3 HOH 68  889  889  HOH HOH I . 
GA 3 HOH 69  898  898  HOH HOH I . 
GA 3 HOH 70  934  934  HOH HOH I . 
GA 3 HOH 71  935  935  HOH HOH I . 
GA 3 HOH 72  941  941  HOH HOH I . 
GA 3 HOH 73  960  960  HOH HOH I . 
GA 3 HOH 74  967  967  HOH HOH I . 
GA 3 HOH 75  976  976  HOH HOH I . 
GA 3 HOH 76  984  984  HOH HOH I . 
GA 3 HOH 77  995  995  HOH HOH I . 
GA 3 HOH 78  1010 1010 HOH HOH I . 
GA 3 HOH 79  1014 1014 HOH HOH I . 
GA 3 HOH 80  1042 1042 HOH HOH I . 
GA 3 HOH 81  1049 1049 HOH HOH I . 
GA 3 HOH 82  1056 1056 HOH HOH I . 
GA 3 HOH 83  1072 1072 HOH HOH I . 
GA 3 HOH 84  1078 1078 HOH HOH I . 
GA 3 HOH 85  1089 1089 HOH HOH I . 
GA 3 HOH 86  1094 1094 HOH HOH I . 
GA 3 HOH 87  1102 1102 HOH HOH I . 
GA 3 HOH 88  1108 1108 HOH HOH I . 
GA 3 HOH 89  1123 1123 HOH HOH I . 
GA 3 HOH 90  1125 1125 HOH HOH I . 
GA 3 HOH 91  1130 1130 HOH HOH I . 
GA 3 HOH 92  1131 1131 HOH HOH I . 
GA 3 HOH 93  1133 1133 HOH HOH I . 
GA 3 HOH 94  1146 1146 HOH HOH I . 
GA 3 HOH 95  1156 1156 HOH HOH I . 
GA 3 HOH 96  1159 1159 HOH HOH I . 
GA 3 HOH 97  1162 1162 HOH HOH I . 
GA 3 HOH 98  1165 1165 HOH HOH I . 
GA 3 HOH 99  1192 1192 HOH HOH I . 
GA 3 HOH 100 1197 1197 HOH HOH I . 
GA 3 HOH 101 1203 1203 HOH HOH I . 
GA 3 HOH 102 1207 1207 HOH HOH I . 
GA 3 HOH 103 1209 1209 HOH HOH I . 
GA 3 HOH 104 1217 1217 HOH HOH I . 
GA 3 HOH 105 1221 1221 HOH HOH I . 
GA 3 HOH 106 1237 1237 HOH HOH I . 
GA 3 HOH 107 1255 1255 HOH HOH I . 
GA 3 HOH 108 1259 1259 HOH HOH I . 
GA 3 HOH 109 1277 1277 HOH HOH I . 
GA 3 HOH 110 1300 1300 HOH HOH I . 
GA 3 HOH 111 1311 1311 HOH HOH I . 
GA 3 HOH 112 1333 1333 HOH HOH I . 
GA 3 HOH 113 1344 1344 HOH HOH I . 
GA 3 HOH 114 1347 1347 HOH HOH I . 
GA 3 HOH 115 1354 1354 HOH HOH I . 
GA 3 HOH 116 1363 1363 HOH HOH I . 
GA 3 HOH 117 1366 1366 HOH HOH I . 
GA 3 HOH 118 1374 1374 HOH HOH I . 
GA 3 HOH 119 1378 1378 HOH HOH I . 
GA 3 HOH 120 1419 1419 HOH HOH I . 
GA 3 HOH 121 1430 1430 HOH HOH I . 
GA 3 HOH 122 1435 1435 HOH HOH I . 
GA 3 HOH 123 1447 1447 HOH HOH I . 
GA 3 HOH 124 1450 1450 HOH HOH I . 
GA 3 HOH 125 1452 1452 HOH HOH I . 
GA 3 HOH 126 1454 1454 HOH HOH I . 
GA 3 HOH 127 1468 1468 HOH HOH I . 
GA 3 HOH 128 1488 1488 HOH HOH I . 
GA 3 HOH 129 1489 1489 HOH HOH I . 
GA 3 HOH 130 1491 1491 HOH HOH I . 
GA 3 HOH 131 1512 1512 HOH HOH I . 
GA 3 HOH 132 1548 1548 HOH HOH I . 
GA 3 HOH 133 1554 1554 HOH HOH I . 
GA 3 HOH 134 1557 1557 HOH HOH I . 
GA 3 HOH 135 1572 1572 HOH HOH I . 
GA 3 HOH 136 1600 1600 HOH HOH I . 
GA 3 HOH 137 1610 1610 HOH HOH I . 
GA 3 HOH 138 1611 1611 HOH HOH I . 
GA 3 HOH 139 1629 1629 HOH HOH I . 
GA 3 HOH 140 1640 1640 HOH HOH I . 
GA 3 HOH 141 1647 1647 HOH HOH I . 
GA 3 HOH 142 1656 1656 HOH HOH I . 
GA 3 HOH 143 1685 1685 HOH HOH I . 
GA 3 HOH 144 1687 1687 HOH HOH I . 
GA 3 HOH 145 1694 1694 HOH HOH I . 
GA 3 HOH 146 1704 1704 HOH HOH I . 
GA 3 HOH 147 1737 1737 HOH HOH I . 
GA 3 HOH 148 1742 1742 HOH HOH I . 
GA 3 HOH 149 1743 1743 HOH HOH I . 
GA 3 HOH 150 1747 1747 HOH HOH I . 
GA 3 HOH 151 1748 1748 HOH HOH I . 
GA 3 HOH 152 1749 1749 HOH HOH I . 
GA 3 HOH 153 1768 1768 HOH HOH I . 
GA 3 HOH 154 1786 1786 HOH HOH I . 
GA 3 HOH 155 1788 1788 HOH HOH I . 
GA 3 HOH 156 1797 1797 HOH HOH I . 
HA 3 HOH 1   154  4    HOH HOH J . 
HA 3 HOH 2   156  34   HOH HOH J . 
HA 3 HOH 3   157  52   HOH HOH J . 
HA 3 HOH 4   158  78   HOH HOH J . 
HA 3 HOH 5   159  79   HOH HOH J . 
HA 3 HOH 6   160  82   HOH HOH J . 
HA 3 HOH 7   161  100  HOH HOH J . 
HA 3 HOH 8   162  103  HOH HOH J . 
HA 3 HOH 9   163  112  HOH HOH J . 
HA 3 HOH 10  164  148  HOH HOH J . 
HA 3 HOH 11  183  183  HOH HOH J . 
HA 3 HOH 12  186  186  HOH HOH J . 
HA 3 HOH 13  211  211  HOH HOH J . 
HA 3 HOH 14  223  223  HOH HOH J . 
HA 3 HOH 15  250  250  HOH HOH J . 
HA 3 HOH 16  276  276  HOH HOH J . 
HA 3 HOH 17  298  298  HOH HOH J . 
HA 3 HOH 18  314  314  HOH HOH J . 
HA 3 HOH 19  316  316  HOH HOH J . 
HA 3 HOH 20  321  321  HOH HOH J . 
HA 3 HOH 21  336  336  HOH HOH J . 
HA 3 HOH 22  343  343  HOH HOH J . 
HA 3 HOH 23  356  356  HOH HOH J . 
HA 3 HOH 24  357  357  HOH HOH J . 
HA 3 HOH 25  359  359  HOH HOH J . 
HA 3 HOH 26  369  369  HOH HOH J . 
HA 3 HOH 27  383  383  HOH HOH J . 
HA 3 HOH 28  385  385  HOH HOH J . 
HA 3 HOH 29  389  389  HOH HOH J . 
HA 3 HOH 30  407  407  HOH HOH J . 
HA 3 HOH 31  419  419  HOH HOH J . 
HA 3 HOH 32  439  439  HOH HOH J . 
HA 3 HOH 33  446  446  HOH HOH J . 
HA 3 HOH 34  461  461  HOH HOH J . 
HA 3 HOH 35  464  464  HOH HOH J . 
HA 3 HOH 36  468  468  HOH HOH J . 
HA 3 HOH 37  484  484  HOH HOH J . 
HA 3 HOH 38  489  489  HOH HOH J . 
HA 3 HOH 39  518  518  HOH HOH J . 
HA 3 HOH 40  538  538  HOH HOH J . 
HA 3 HOH 41  551  551  HOH HOH J . 
HA 3 HOH 42  553  553  HOH HOH J . 
HA 3 HOH 43  563  563  HOH HOH J . 
HA 3 HOH 44  568  568  HOH HOH J . 
HA 3 HOH 45  570  570  HOH HOH J . 
HA 3 HOH 46  581  581  HOH HOH J . 
HA 3 HOH 47  596  596  HOH HOH J . 
HA 3 HOH 48  607  607  HOH HOH J . 
HA 3 HOH 49  616  616  HOH HOH J . 
HA 3 HOH 50  660  660  HOH HOH J . 
HA 3 HOH 51  663  663  HOH HOH J . 
HA 3 HOH 52  664  664  HOH HOH J . 
HA 3 HOH 53  669  669  HOH HOH J . 
HA 3 HOH 54  690  690  HOH HOH J . 
HA 3 HOH 55  693  693  HOH HOH J . 
HA 3 HOH 56  695  695  HOH HOH J . 
HA 3 HOH 57  723  723  HOH HOH J . 
HA 3 HOH 58  726  726  HOH HOH J . 
HA 3 HOH 59  766  766  HOH HOH J . 
HA 3 HOH 60  778  778  HOH HOH J . 
HA 3 HOH 61  809  809  HOH HOH J . 
HA 3 HOH 62  827  827  HOH HOH J . 
HA 3 HOH 63  840  840  HOH HOH J . 
HA 3 HOH 64  852  852  HOH HOH J . 
HA 3 HOH 65  872  872  HOH HOH J . 
HA 3 HOH 66  873  873  HOH HOH J . 
HA 3 HOH 67  888  888  HOH HOH J . 
HA 3 HOH 68  895  895  HOH HOH J . 
HA 3 HOH 69  904  904  HOH HOH J . 
HA 3 HOH 70  909  909  HOH HOH J . 
HA 3 HOH 71  959  959  HOH HOH J . 
HA 3 HOH 72  986  986  HOH HOH J . 
HA 3 HOH 73  1039 1039 HOH HOH J . 
HA 3 HOH 74  1045 1045 HOH HOH J . 
HA 3 HOH 75  1048 1048 HOH HOH J . 
HA 3 HOH 76  1058 1058 HOH HOH J . 
HA 3 HOH 77  1113 1113 HOH HOH J . 
HA 3 HOH 78  1120 1120 HOH HOH J . 
HA 3 HOH 79  1136 1136 HOH HOH J . 
HA 3 HOH 80  1149 1149 HOH HOH J . 
HA 3 HOH 81  1150 1150 HOH HOH J . 
HA 3 HOH 82  1163 1163 HOH HOH J . 
HA 3 HOH 83  1176 1176 HOH HOH J . 
HA 3 HOH 84  1230 1230 HOH HOH J . 
HA 3 HOH 85  1249 1249 HOH HOH J . 
HA 3 HOH 86  1251 1251 HOH HOH J . 
HA 3 HOH 87  1252 1252 HOH HOH J . 
HA 3 HOH 88  1284 1284 HOH HOH J . 
HA 3 HOH 89  1287 1287 HOH HOH J . 
HA 3 HOH 90  1290 1290 HOH HOH J . 
HA 3 HOH 91  1301 1301 HOH HOH J . 
HA 3 HOH 92  1305 1305 HOH HOH J . 
HA 3 HOH 93  1313 1313 HOH HOH J . 
HA 3 HOH 94  1329 1329 HOH HOH J . 
HA 3 HOH 95  1338 1338 HOH HOH J . 
HA 3 HOH 96  1369 1369 HOH HOH J . 
HA 3 HOH 97  1379 1379 HOH HOH J . 
HA 3 HOH 98  1439 1439 HOH HOH J . 
HA 3 HOH 99  1441 1441 HOH HOH J . 
HA 3 HOH 100 1453 1453 HOH HOH J . 
HA 3 HOH 101 1469 1469 HOH HOH J . 
HA 3 HOH 102 1471 1471 HOH HOH J . 
HA 3 HOH 103 1473 1473 HOH HOH J . 
HA 3 HOH 104 1477 1477 HOH HOH J . 
HA 3 HOH 105 1483 1483 HOH HOH J . 
HA 3 HOH 106 1504 1504 HOH HOH J . 
HA 3 HOH 107 1581 1581 HOH HOH J . 
HA 3 HOH 108 1584 1584 HOH HOH J . 
HA 3 HOH 109 1586 1586 HOH HOH J . 
HA 3 HOH 110 1588 1588 HOH HOH J . 
HA 3 HOH 111 1589 1589 HOH HOH J . 
HA 3 HOH 112 1597 1597 HOH HOH J . 
HA 3 HOH 113 1620 1620 HOH HOH J . 
HA 3 HOH 114 1621 1621 HOH HOH J . 
HA 3 HOH 115 1622 1622 HOH HOH J . 
HA 3 HOH 116 1623 1623 HOH HOH J . 
HA 3 HOH 117 1627 1627 HOH HOH J . 
HA 3 HOH 118 1649 1649 HOH HOH J . 
HA 3 HOH 119 1651 1651 HOH HOH J . 
HA 3 HOH 120 1652 1652 HOH HOH J . 
HA 3 HOH 121 1653 1653 HOH HOH J . 
HA 3 HOH 122 1666 1666 HOH HOH J . 
HA 3 HOH 123 1669 1669 HOH HOH J . 
HA 3 HOH 124 1684 1684 HOH HOH J . 
HA 3 HOH 125 1690 1690 HOH HOH J . 
HA 3 HOH 126 1693 1693 HOH HOH J . 
HA 3 HOH 127 1701 1701 HOH HOH J . 
HA 3 HOH 128 1703 1703 HOH HOH J . 
HA 3 HOH 129 1706 1706 HOH HOH J . 
HA 3 HOH 130 1719 1719 HOH HOH J . 
HA 3 HOH 131 1722 1722 HOH HOH J . 
HA 3 HOH 132 1726 1726 HOH HOH J . 
HA 3 HOH 133 1735 1735 HOH HOH J . 
HA 3 HOH 134 1761 1761 HOH HOH J . 
HA 3 HOH 135 1778 1778 HOH HOH J . 
HA 3 HOH 136 1781 1781 HOH HOH J . 
HA 3 HOH 137 1794 1794 HOH HOH J . 
IA 3 HOH 1   154  56   HOH HOH K . 
IA 3 HOH 2   156  68   HOH HOH K . 
IA 3 HOH 3   157  74   HOH HOH K . 
IA 3 HOH 4   158  140  HOH HOH K . 
IA 3 HOH 5   160  160  HOH HOH K . 
IA 3 HOH 6   178  178  HOH HOH K . 
IA 3 HOH 7   185  185  HOH HOH K . 
IA 3 HOH 8   191  191  HOH HOH K . 
IA 3 HOH 9   206  206  HOH HOH K . 
IA 3 HOH 10  261  261  HOH HOH K . 
IA 3 HOH 11  279  279  HOH HOH K . 
IA 3 HOH 12  281  281  HOH HOH K . 
IA 3 HOH 13  282  282  HOH HOH K . 
IA 3 HOH 14  286  286  HOH HOH K . 
IA 3 HOH 15  299  299  HOH HOH K . 
IA 3 HOH 16  303  303  HOH HOH K . 
IA 3 HOH 17  315  315  HOH HOH K . 
IA 3 HOH 18  339  339  HOH HOH K . 
IA 3 HOH 19  349  349  HOH HOH K . 
IA 3 HOH 20  353  353  HOH HOH K . 
IA 3 HOH 21  367  367  HOH HOH K . 
IA 3 HOH 22  414  414  HOH HOH K . 
IA 3 HOH 23  451  451  HOH HOH K . 
IA 3 HOH 24  477  477  HOH HOH K . 
IA 3 HOH 25  485  485  HOH HOH K . 
IA 3 HOH 26  486  486  HOH HOH K . 
IA 3 HOH 27  497  497  HOH HOH K . 
IA 3 HOH 28  504  504  HOH HOH K . 
IA 3 HOH 29  547  547  HOH HOH K . 
IA 3 HOH 30  564  564  HOH HOH K . 
IA 3 HOH 31  574  574  HOH HOH K . 
IA 3 HOH 32  589  589  HOH HOH K . 
IA 3 HOH 33  595  595  HOH HOH K . 
IA 3 HOH 34  623  623  HOH HOH K . 
IA 3 HOH 35  627  627  HOH HOH K . 
IA 3 HOH 36  628  628  HOH HOH K . 
IA 3 HOH 37  631  631  HOH HOH K . 
IA 3 HOH 38  647  647  HOH HOH K . 
IA 3 HOH 39  650  650  HOH HOH K . 
IA 3 HOH 40  653  653  HOH HOH K . 
IA 3 HOH 41  654  654  HOH HOH K . 
IA 3 HOH 42  662  662  HOH HOH K . 
IA 3 HOH 43  681  681  HOH HOH K . 
IA 3 HOH 44  700  700  HOH HOH K . 
IA 3 HOH 45  716  716  HOH HOH K . 
IA 3 HOH 46  732  732  HOH HOH K . 
IA 3 HOH 47  736  736  HOH HOH K . 
IA 3 HOH 48  783  783  HOH HOH K . 
IA 3 HOH 49  785  785  HOH HOH K . 
IA 3 HOH 50  786  786  HOH HOH K . 
IA 3 HOH 51  798  798  HOH HOH K . 
IA 3 HOH 52  802  802  HOH HOH K . 
IA 3 HOH 53  807  807  HOH HOH K . 
IA 3 HOH 54  826  826  HOH HOH K . 
IA 3 HOH 55  834  834  HOH HOH K . 
IA 3 HOH 56  845  845  HOH HOH K . 
IA 3 HOH 57  857  857  HOH HOH K . 
IA 3 HOH 58  865  865  HOH HOH K . 
IA 3 HOH 59  867  867  HOH HOH K . 
IA 3 HOH 60  882  882  HOH HOH K . 
IA 3 HOH 61  900  900  HOH HOH K . 
IA 3 HOH 62  910  910  HOH HOH K . 
IA 3 HOH 63  918  918  HOH HOH K . 
IA 3 HOH 64  969  969  HOH HOH K . 
IA 3 HOH 65  1000 1000 HOH HOH K . 
IA 3 HOH 66  1006 1006 HOH HOH K . 
IA 3 HOH 67  1020 1020 HOH HOH K . 
IA 3 HOH 68  1046 1046 HOH HOH K . 
IA 3 HOH 69  1061 1061 HOH HOH K . 
IA 3 HOH 70  1068 1068 HOH HOH K . 
IA 3 HOH 71  1100 1100 HOH HOH K . 
IA 3 HOH 72  1104 1104 HOH HOH K . 
IA 3 HOH 73  1148 1148 HOH HOH K . 
IA 3 HOH 74  1160 1160 HOH HOH K . 
IA 3 HOH 75  1168 1168 HOH HOH K . 
IA 3 HOH 76  1190 1190 HOH HOH K . 
IA 3 HOH 77  1193 1193 HOH HOH K . 
IA 3 HOH 78  1233 1233 HOH HOH K . 
IA 3 HOH 79  1243 1243 HOH HOH K . 
IA 3 HOH 80  1253 1253 HOH HOH K . 
IA 3 HOH 81  1267 1267 HOH HOH K . 
IA 3 HOH 82  1270 1270 HOH HOH K . 
IA 3 HOH 83  1274 1274 HOH HOH K . 
IA 3 HOH 84  1317 1317 HOH HOH K . 
IA 3 HOH 85  1341 1341 HOH HOH K . 
IA 3 HOH 86  1349 1349 HOH HOH K . 
IA 3 HOH 87  1373 1373 HOH HOH K . 
IA 3 HOH 88  1408 1408 HOH HOH K . 
IA 3 HOH 89  1418 1418 HOH HOH K . 
IA 3 HOH 90  1434 1434 HOH HOH K . 
IA 3 HOH 91  1446 1446 HOH HOH K . 
IA 3 HOH 92  1460 1460 HOH HOH K . 
IA 3 HOH 93  1486 1486 HOH HOH K . 
IA 3 HOH 94  1510 1510 HOH HOH K . 
IA 3 HOH 95  1539 1539 HOH HOH K . 
IA 3 HOH 96  1573 1573 HOH HOH K . 
IA 3 HOH 97  1575 1575 HOH HOH K . 
IA 3 HOH 98  1612 1612 HOH HOH K . 
IA 3 HOH 99  1615 1615 HOH HOH K . 
IA 3 HOH 100 1625 1625 HOH HOH K . 
IA 3 HOH 101 1673 1673 HOH HOH K . 
IA 3 HOH 102 1691 1691 HOH HOH K . 
IA 3 HOH 103 1692 1692 HOH HOH K . 
IA 3 HOH 104 1702 1702 HOH HOH K . 
IA 3 HOH 105 1716 1716 HOH HOH K . 
IA 3 HOH 106 1721 1721 HOH HOH K . 
IA 3 HOH 107 1738 1738 HOH HOH K . 
IA 3 HOH 108 1766 1766 HOH HOH K . 
IA 3 HOH 109 1767 1767 HOH HOH K . 
IA 3 HOH 110 1793 1793 HOH HOH K . 
IA 3 HOH 111 1798 1798 HOH HOH K . 
IA 3 HOH 112 1807 1807 HOH HOH K . 
JA 3 HOH 1   154  31   HOH HOH L . 
JA 3 HOH 2   156  64   HOH HOH L . 
JA 3 HOH 3   157  75   HOH HOH L . 
JA 3 HOH 4   158  81   HOH HOH L . 
JA 3 HOH 5   159  86   HOH HOH L . 
JA 3 HOH 6   160  90   HOH HOH L . 
JA 3 HOH 7   161  126  HOH HOH L . 
JA 3 HOH 8   162  132  HOH HOH L . 
JA 3 HOH 9   163  136  HOH HOH L . 
JA 3 HOH 10  164  143  HOH HOH L . 
JA 3 HOH 11  228  228  HOH HOH L . 
JA 3 HOH 12  247  247  HOH HOH L . 
JA 3 HOH 13  260  260  HOH HOH L . 
JA 3 HOH 14  271  271  HOH HOH L . 
JA 3 HOH 15  278  278  HOH HOH L . 
JA 3 HOH 16  284  284  HOH HOH L . 
JA 3 HOH 17  297  297  HOH HOH L . 
JA 3 HOH 18  313  313  HOH HOH L . 
JA 3 HOH 19  317  317  HOH HOH L . 
JA 3 HOH 20  327  327  HOH HOH L . 
JA 3 HOH 21  330  330  HOH HOH L . 
JA 3 HOH 22  378  378  HOH HOH L . 
JA 3 HOH 23  382  382  HOH HOH L . 
JA 3 HOH 24  422  422  HOH HOH L . 
JA 3 HOH 25  440  440  HOH HOH L . 
JA 3 HOH 26  442  442  HOH HOH L . 
JA 3 HOH 27  452  452  HOH HOH L . 
JA 3 HOH 28  459  459  HOH HOH L . 
JA 3 HOH 29  527  527  HOH HOH L . 
JA 3 HOH 30  536  536  HOH HOH L . 
JA 3 HOH 31  549  549  HOH HOH L . 
JA 3 HOH 32  584  584  HOH HOH L . 
JA 3 HOH 33  590  590  HOH HOH L . 
JA 3 HOH 34  605  605  HOH HOH L . 
JA 3 HOH 35  613  613  HOH HOH L . 
JA 3 HOH 36  667  667  HOH HOH L . 
JA 3 HOH 37  727  727  HOH HOH L . 
JA 3 HOH 38  728  728  HOH HOH L . 
JA 3 HOH 39  769  769  HOH HOH L . 
JA 3 HOH 40  856  856  HOH HOH L . 
JA 3 HOH 41  868  868  HOH HOH L . 
JA 3 HOH 42  883  883  HOH HOH L . 
JA 3 HOH 43  897  897  HOH HOH L . 
JA 3 HOH 44  919  919  HOH HOH L . 
JA 3 HOH 45  926  926  HOH HOH L . 
JA 3 HOH 46  931  931  HOH HOH L . 
JA 3 HOH 47  938  938  HOH HOH L . 
JA 3 HOH 48  945  945  HOH HOH L . 
JA 3 HOH 49  966  966  HOH HOH L . 
JA 3 HOH 50  981  981  HOH HOH L . 
JA 3 HOH 51  983  983  HOH HOH L . 
JA 3 HOH 52  1007 1007 HOH HOH L . 
JA 3 HOH 53  1031 1031 HOH HOH L . 
JA 3 HOH 54  1035 1035 HOH HOH L . 
JA 3 HOH 55  1038 1038 HOH HOH L . 
JA 3 HOH 56  1055 1055 HOH HOH L . 
JA 3 HOH 57  1083 1083 HOH HOH L . 
JA 3 HOH 58  1092 1092 HOH HOH L . 
JA 3 HOH 59  1103 1103 HOH HOH L . 
JA 3 HOH 60  1116 1116 HOH HOH L . 
JA 3 HOH 61  1117 1117 HOH HOH L . 
JA 3 HOH 62  1119 1119 HOH HOH L . 
JA 3 HOH 63  1145 1145 HOH HOH L . 
JA 3 HOH 64  1171 1171 HOH HOH L . 
JA 3 HOH 65  1174 1174 HOH HOH L . 
JA 3 HOH 66  1205 1205 HOH HOH L . 
JA 3 HOH 67  1226 1226 HOH HOH L . 
JA 3 HOH 68  1234 1234 HOH HOH L . 
JA 3 HOH 69  1239 1239 HOH HOH L . 
JA 3 HOH 70  1244 1244 HOH HOH L . 
JA 3 HOH 71  1245 1245 HOH HOH L . 
JA 3 HOH 72  1250 1250 HOH HOH L . 
JA 3 HOH 73  1260 1260 HOH HOH L . 
JA 3 HOH 74  1275 1275 HOH HOH L . 
JA 3 HOH 75  1281 1281 HOH HOH L . 
JA 3 HOH 76  1283 1283 HOH HOH L . 
JA 3 HOH 77  1285 1285 HOH HOH L . 
JA 3 HOH 78  1286 1286 HOH HOH L . 
JA 3 HOH 79  1291 1291 HOH HOH L . 
JA 3 HOH 80  1357 1357 HOH HOH L . 
JA 3 HOH 81  1376 1376 HOH HOH L . 
JA 3 HOH 82  1382 1382 HOH HOH L . 
JA 3 HOH 83  1387 1387 HOH HOH L . 
JA 3 HOH 84  1399 1399 HOH HOH L . 
JA 3 HOH 85  1448 1448 HOH HOH L . 
JA 3 HOH 86  1487 1487 HOH HOH L . 
JA 3 HOH 87  1513 1513 HOH HOH L . 
JA 3 HOH 88  1527 1527 HOH HOH L . 
JA 3 HOH 89  1528 1528 HOH HOH L . 
JA 3 HOH 90  1532 1532 HOH HOH L . 
JA 3 HOH 91  1536 1536 HOH HOH L . 
JA 3 HOH 92  1564 1564 HOH HOH L . 
JA 3 HOH 93  1569 1569 HOH HOH L . 
JA 3 HOH 94  1580 1580 HOH HOH L . 
JA 3 HOH 95  1635 1635 HOH HOH L . 
JA 3 HOH 96  1636 1636 HOH HOH L . 
JA 3 HOH 97  1641 1641 HOH HOH L . 
JA 3 HOH 98  1648 1648 HOH HOH L . 
JA 3 HOH 99  1654 1654 HOH HOH L . 
JA 3 HOH 100 1662 1662 HOH HOH L . 
JA 3 HOH 101 1667 1667 HOH HOH L . 
JA 3 HOH 102 1676 1676 HOH HOH L . 
JA 3 HOH 103 1700 1700 HOH HOH L . 
JA 3 HOH 104 1730 1730 HOH HOH L . 
JA 3 HOH 105 1764 1764 HOH HOH L . 
JA 3 HOH 106 1776 1776 HOH HOH L . 
JA 3 HOH 107 1782 1782 HOH HOH L . 
JA 3 HOH 108 1795 1795 HOH HOH L . 
# 
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,Y,Z   
2 1 C,D,O,P,AA,BA 
3 1 E,F,Q,R,CA,DA 
4 1 G,H,S,T,EA,FA 
5 1 I,J,U,V,GA,HA 
6 1 K,L,W,X,IA,JA 
# 
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)' 1400  ? 
1 MORE         -12   ? 
1 'SSA (A^2)'  13950 ? 
2 'ABSA (A^2)' 1470  ? 
2 MORE         -12   ? 
2 'SSA (A^2)'  13890 ? 
3 'ABSA (A^2)' 1440  ? 
3 MORE         -12   ? 
3 'SSA (A^2)'  14010 ? 
4 'ABSA (A^2)' 1440  ? 
4 MORE         -12   ? 
4 'SSA (A^2)'  13910 ? 
5 'ABSA (A^2)' 1420  ? 
5 MORE         -12   ? 
5 'SSA (A^2)'  14030 ? 
6 'ABSA (A^2)' 1460  ? 
6 MORE         -11   ? 
6 'SSA (A^2)'  13960 ? 
# 
_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  ND1 ? A HIS 63 ? A HIS 63 ? 1_555 ZN ? M ZN . ? A ZN 155 ? 1_555 ND1 ? A HIS 71 ? A HIS 71 ? 1_555 104.7 ? 
2  ND1 ? A HIS 63 ? A HIS 63 ? 1_555 ZN ? M ZN . ? A ZN 155 ? 1_555 ND1 ? A HIS 80 ? A HIS 80 ? 1_555 118.0 ? 
3  ND1 ? A HIS 71 ? A HIS 71 ? 1_555 ZN ? M ZN . ? A ZN 155 ? 1_555 ND1 ? A HIS 80 ? A HIS 80 ? 1_555 118.5 ? 
4  ND1 ? A HIS 63 ? A HIS 63 ? 1_555 ZN ? M ZN . ? A ZN 155 ? 1_555 OD1 ? A ASP 83 ? A ASP 83 ? 1_555 109.3 ? 
5  ND1 ? A HIS 71 ? A HIS 71 ? 1_555 ZN ? M ZN . ? A ZN 155 ? 1_555 OD1 ? A ASP 83 ? A ASP 83 ? 1_555 98.3  ? 
6  ND1 ? A HIS 80 ? A HIS 80 ? 1_555 ZN ? M ZN . ? A ZN 155 ? 1_555 OD1 ? A ASP 83 ? A ASP 83 ? 1_555 106.1 ? 
7  ND1 ? B HIS 63 ? B HIS 63 ? 1_555 ZN ? N ZN . ? B ZN 155 ? 1_555 ND1 ? B HIS 71 ? B HIS 71 ? 1_555 99.4  ? 
8  ND1 ? B HIS 63 ? B HIS 63 ? 1_555 ZN ? N ZN . ? B ZN 155 ? 1_555 ND1 ? B HIS 80 ? B HIS 80 ? 1_555 117.4 ? 
9  ND1 ? B HIS 71 ? B HIS 71 ? 1_555 ZN ? N ZN . ? B ZN 155 ? 1_555 ND1 ? B HIS 80 ? B HIS 80 ? 1_555 120.5 ? 
10 ND1 ? B HIS 63 ? B HIS 63 ? 1_555 ZN ? N ZN . ? B ZN 155 ? 1_555 OD1 ? B ASP 83 ? B ASP 83 ? 1_555 99.4  ? 
11 ND1 ? B HIS 71 ? B HIS 71 ? 1_555 ZN ? N ZN . ? B ZN 155 ? 1_555 OD1 ? B ASP 83 ? B ASP 83 ? 1_555 96.6  ? 
12 ND1 ? B HIS 80 ? B HIS 80 ? 1_555 ZN ? N ZN . ? B ZN 155 ? 1_555 OD1 ? B ASP 83 ? B ASP 83 ? 1_555 119.0 ? 
13 ND1 ? C HIS 63 ? C HIS 63 ? 1_555 ZN ? O ZN . ? C ZN 155 ? 1_555 ND1 ? C HIS 71 ? C HIS 71 ? 1_555 100.9 ? 
14 ND1 ? C HIS 63 ? C HIS 63 ? 1_555 ZN ? O ZN . ? C ZN 155 ? 1_555 ND1 ? C HIS 80 ? C HIS 80 ? 1_555 107.0 ? 
15 ND1 ? C HIS 71 ? C HIS 71 ? 1_555 ZN ? O ZN . ? C ZN 155 ? 1_555 ND1 ? C HIS 80 ? C HIS 80 ? 1_555 119.9 ? 
16 ND1 ? C HIS 63 ? C HIS 63 ? 1_555 ZN ? O ZN . ? C ZN 155 ? 1_555 OD1 ? C ASP 83 ? C ASP 83 ? 1_555 110.9 ? 
17 ND1 ? C HIS 71 ? C HIS 71 ? 1_555 ZN ? O ZN . ? C ZN 155 ? 1_555 OD1 ? C ASP 83 ? C ASP 83 ? 1_555 100.0 ? 
18 ND1 ? C HIS 80 ? C HIS 80 ? 1_555 ZN ? O ZN . ? C ZN 155 ? 1_555 OD1 ? C ASP 83 ? C ASP 83 ? 1_555 117.0 ? 
19 ND1 ? D HIS 63 ? D HIS 63 ? 1_555 ZN ? P ZN . ? D ZN 155 ? 1_555 ND1 ? D HIS 71 ? D HIS 71 ? 1_555 104.6 ? 
20 ND1 ? D HIS 63 ? D HIS 63 ? 1_555 ZN ? P ZN . ? D ZN 155 ? 1_555 ND1 ? D HIS 80 ? D HIS 80 ? 1_555 111.2 ? 
21 ND1 ? D HIS 71 ? D HIS 71 ? 1_555 ZN ? P ZN . ? D ZN 155 ? 1_555 ND1 ? D HIS 80 ? D HIS 80 ? 1_555 124.5 ? 
22 ND1 ? D HIS 63 ? D HIS 63 ? 1_555 ZN ? P ZN . ? D ZN 155 ? 1_555 OD1 ? D ASP 83 ? D ASP 83 ? 1_555 98.3  ? 
23 ND1 ? D HIS 71 ? D HIS 71 ? 1_555 ZN ? P ZN . ? D ZN 155 ? 1_555 OD1 ? D ASP 83 ? D ASP 83 ? 1_555 99.2  ? 
24 ND1 ? D HIS 80 ? D HIS 80 ? 1_555 ZN ? P ZN . ? D ZN 155 ? 1_555 OD1 ? D ASP 83 ? D ASP 83 ? 1_555 115.4 ? 
25 ND1 ? E HIS 63 ? E HIS 63 ? 1_555 ZN ? Q ZN . ? E ZN 155 ? 1_555 ND1 ? E HIS 80 ? E HIS 80 ? 1_555 121.6 ? 
26 ND1 ? E HIS 63 ? E HIS 63 ? 1_555 ZN ? Q ZN . ? E ZN 155 ? 1_555 OD1 ? E ASP 83 ? E ASP 83 ? 1_555 109.8 ? 
27 ND1 ? E HIS 80 ? E HIS 80 ? 1_555 ZN ? Q ZN . ? E ZN 155 ? 1_555 OD1 ? E ASP 83 ? E ASP 83 ? 1_555 102.6 ? 
28 ND1 ? E HIS 63 ? E HIS 63 ? 1_555 ZN ? Q ZN . ? E ZN 155 ? 1_555 ND1 ? E HIS 71 ? E HIS 71 ? 1_555 104.5 ? 
29 ND1 ? E HIS 80 ? E HIS 80 ? 1_555 ZN ? Q ZN . ? E ZN 155 ? 1_555 ND1 ? E HIS 71 ? E HIS 71 ? 1_555 120.2 ? 
30 OD1 ? E ASP 83 ? E ASP 83 ? 1_555 ZN ? Q ZN . ? E ZN 155 ? 1_555 ND1 ? E HIS 71 ? E HIS 71 ? 1_555 94.4  ? 
31 ND1 ? F HIS 63 ? F HIS 63 ? 1_555 ZN ? R ZN . ? F ZN 155 ? 1_555 ND1 ? F HIS 80 ? F HIS 80 ? 1_555 114.6 ? 
32 ND1 ? F HIS 63 ? F HIS 63 ? 1_555 ZN ? R ZN . ? F ZN 155 ? 1_555 OD1 ? F ASP 83 ? F ASP 83 ? 1_555 108.3 ? 
33 ND1 ? F HIS 80 ? F HIS 80 ? 1_555 ZN ? R ZN . ? F ZN 155 ? 1_555 OD1 ? F ASP 83 ? F ASP 83 ? 1_555 115.8 ? 
34 ND1 ? F HIS 63 ? F HIS 63 ? 1_555 ZN ? R ZN . ? F ZN 155 ? 1_555 ND1 ? F HIS 71 ? F HIS 71 ? 1_555 104.5 ? 
35 ND1 ? F HIS 80 ? F HIS 80 ? 1_555 ZN ? R ZN . ? F ZN 155 ? 1_555 ND1 ? F HIS 71 ? F HIS 71 ? 1_555 118.0 ? 
36 OD1 ? F ASP 83 ? F ASP 83 ? 1_555 ZN ? R ZN . ? F ZN 155 ? 1_555 ND1 ? F HIS 71 ? F HIS 71 ? 1_555 93.2  ? 
37 ND1 ? G HIS 63 ? G HIS 63 ? 1_555 ZN ? S ZN . ? G ZN 155 ? 1_555 ND1 ? G HIS 71 ? G HIS 71 ? 1_555 99.2  ? 
38 ND1 ? G HIS 63 ? G HIS 63 ? 1_555 ZN ? S ZN . ? G ZN 155 ? 1_555 ND1 ? G HIS 80 ? G HIS 80 ? 1_555 112.5 ? 
39 ND1 ? G HIS 71 ? G HIS 71 ? 1_555 ZN ? S ZN . ? G ZN 155 ? 1_555 ND1 ? G HIS 80 ? G HIS 80 ? 1_555 121.5 ? 
40 ND1 ? G HIS 63 ? G HIS 63 ? 1_555 ZN ? S ZN . ? G ZN 155 ? 1_555 OD1 ? G ASP 83 ? G ASP 83 ? 1_555 107.0 ? 
41 ND1 ? G HIS 71 ? G HIS 71 ? 1_555 ZN ? S ZN . ? G ZN 155 ? 1_555 OD1 ? G ASP 83 ? G ASP 83 ? 1_555 95.9  ? 
42 ND1 ? G HIS 80 ? G HIS 80 ? 1_555 ZN ? S ZN . ? G ZN 155 ? 1_555 OD1 ? G ASP 83 ? G ASP 83 ? 1_555 118.0 ? 
43 ND1 ? H HIS 63 ? H HIS 63 ? 1_555 ZN ? T ZN . ? H ZN 155 ? 1_555 ND1 ? H HIS 71 ? H HIS 71 ? 1_555 97.9  ? 
44 ND1 ? H HIS 63 ? H HIS 63 ? 1_555 ZN ? T ZN . ? H ZN 155 ? 1_555 ND1 ? H HIS 80 ? H HIS 80 ? 1_555 109.4 ? 
45 ND1 ? H HIS 71 ? H HIS 71 ? 1_555 ZN ? T ZN . ? H ZN 155 ? 1_555 ND1 ? H HIS 80 ? H HIS 80 ? 1_555 120.2 ? 
46 ND1 ? H HIS 63 ? H HIS 63 ? 1_555 ZN ? T ZN . ? H ZN 155 ? 1_555 OD1 ? H ASP 83 ? H ASP 83 ? 1_555 108.1 ? 
47 ND1 ? H HIS 71 ? H HIS 71 ? 1_555 ZN ? T ZN . ? H ZN 155 ? 1_555 OD1 ? H ASP 83 ? H ASP 83 ? 1_555 99.3  ? 
48 ND1 ? H HIS 80 ? H HIS 80 ? 1_555 ZN ? T ZN . ? H ZN 155 ? 1_555 OD1 ? H ASP 83 ? H ASP 83 ? 1_555 119.5 ? 
49 ND1 ? I HIS 63 ? I HIS 63 ? 1_555 ZN ? U ZN . ? I ZN 155 ? 1_555 ND1 ? I HIS 71 ? I HIS 71 ? 1_555 100.8 ? 
50 ND1 ? I HIS 63 ? I HIS 63 ? 1_555 ZN ? U ZN . ? I ZN 155 ? 1_555 ND1 ? I HIS 80 ? I HIS 80 ? 1_555 109.7 ? 
51 ND1 ? I HIS 71 ? I HIS 71 ? 1_555 ZN ? U ZN . ? I ZN 155 ? 1_555 ND1 ? I HIS 80 ? I HIS 80 ? 1_555 119.7 ? 
52 ND1 ? I HIS 63 ? I HIS 63 ? 1_555 ZN ? U ZN . ? I ZN 155 ? 1_555 OD1 ? I ASP 83 ? I ASP 83 ? 1_555 116.9 ? 
53 ND1 ? I HIS 71 ? I HIS 71 ? 1_555 ZN ? U ZN . ? I ZN 155 ? 1_555 OD1 ? I ASP 83 ? I ASP 83 ? 1_555 102.4 ? 
54 ND1 ? I HIS 80 ? I HIS 80 ? 1_555 ZN ? U ZN . ? I ZN 155 ? 1_555 OD1 ? I ASP 83 ? I ASP 83 ? 1_555 107.6 ? 
55 ND1 ? J HIS 63 ? J HIS 63 ? 1_555 ZN ? V ZN . ? J ZN 155 ? 1_555 ND1 ? J HIS 71 ? J HIS 71 ? 1_555 100.6 ? 
56 ND1 ? J HIS 63 ? J HIS 63 ? 1_555 ZN ? V ZN . ? J ZN 155 ? 1_555 ND1 ? J HIS 80 ? J HIS 80 ? 1_555 109.2 ? 
57 ND1 ? J HIS 71 ? J HIS 71 ? 1_555 ZN ? V ZN . ? J ZN 155 ? 1_555 ND1 ? J HIS 80 ? J HIS 80 ? 1_555 113.8 ? 
58 ND1 ? J HIS 63 ? J HIS 63 ? 1_555 ZN ? V ZN . ? J ZN 155 ? 1_555 OD1 ? J ASP 83 ? J ASP 83 ? 1_555 112.8 ? 
59 ND1 ? J HIS 71 ? J HIS 71 ? 1_555 ZN ? V ZN . ? J ZN 155 ? 1_555 OD1 ? J ASP 83 ? J ASP 83 ? 1_555 106.2 ? 
60 ND1 ? J HIS 80 ? J HIS 80 ? 1_555 ZN ? V ZN . ? J ZN 155 ? 1_555 OD1 ? J ASP 83 ? J ASP 83 ? 1_555 113.6 ? 
61 ND1 ? K HIS 63 ? K HIS 63 ? 1_555 ZN ? W ZN . ? K ZN 155 ? 1_555 ND1 ? K HIS 71 ? K HIS 71 ? 1_555 103.2 ? 
62 ND1 ? K HIS 63 ? K HIS 63 ? 1_555 ZN ? W ZN . ? K ZN 155 ? 1_555 ND1 ? K HIS 80 ? K HIS 80 ? 1_555 111.0 ? 
63 ND1 ? K HIS 71 ? K HIS 71 ? 1_555 ZN ? W ZN . ? K ZN 155 ? 1_555 ND1 ? K HIS 80 ? K HIS 80 ? 1_555 124.3 ? 
64 ND1 ? K HIS 63 ? K HIS 63 ? 1_555 ZN ? W ZN . ? K ZN 155 ? 1_555 OD1 ? K ASP 83 ? K ASP 83 ? 1_555 115.5 ? 
65 ND1 ? K HIS 71 ? K HIS 71 ? 1_555 ZN ? W ZN . ? K ZN 155 ? 1_555 OD1 ? K ASP 83 ? K ASP 83 ? 1_555 82.3  ? 
66 ND1 ? K HIS 80 ? K HIS 80 ? 1_555 ZN ? W ZN . ? K ZN 155 ? 1_555 OD1 ? K ASP 83 ? K ASP 83 ? 1_555 117.6 ? 
67 ND1 ? L HIS 63 ? L HIS 63 ? 1_555 ZN ? X ZN . ? L ZN 155 ? 1_555 ND1 ? L HIS 71 ? L HIS 71 ? 1_555 104.2 ? 
68 ND1 ? L HIS 63 ? L HIS 63 ? 1_555 ZN ? X ZN . ? L ZN 155 ? 1_555 ND1 ? L HIS 80 ? L HIS 80 ? 1_555 114.9 ? 
69 ND1 ? L HIS 71 ? L HIS 71 ? 1_555 ZN ? X ZN . ? L ZN 155 ? 1_555 ND1 ? L HIS 80 ? L HIS 80 ? 1_555 120.8 ? 
70 ND1 ? L HIS 63 ? L HIS 63 ? 1_555 ZN ? X ZN . ? L ZN 155 ? 1_555 OD1 ? L ASP 83 ? L ASP 83 ? 1_555 108.2 ? 
71 ND1 ? L HIS 71 ? L HIS 71 ? 1_555 ZN ? X ZN . ? L ZN 155 ? 1_555 OD1 ? L ASP 83 ? L ASP 83 ? 1_555 96.7  ? 
72 ND1 ? L HIS 80 ? L HIS 80 ? 1_555 ZN ? X ZN . ? L ZN 155 ? 1_555 OD1 ? L ASP 83 ? L ASP 83 ? 1_555 110.1 ? 
# 
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 2010-09-08 
2 'Structure model' 1 1 2011-07-13 
3 'Structure model' 1 2 2017-07-26 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Refinement description'    
3 3 'Structure model' 'Source and taxonomy'       
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 3 'Structure model' entity_src_gen 
2 3 'Structure model' software       
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
CrystalClear 'data collection' . ? 1 
PHASER       phasing           . ? 2 
PHENIX       refinement        . ? 3 
HKL-2000     'data reduction'  . ? 4 
HKL-2000     'data scaling'    . ? 5 
# 
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 SER C 98  ? ? -152.07 82.98   
2  1 ARG C 115 ? ? -106.60 -166.94 
3  1 LYS D 136 ? ? -122.56 -58.92  
4  1 ALA E 55  ? ? -111.35 56.02   
5  1 LYS E 91  ? ? -52.98  -8.57   
6  1 SER E 98  ? ? -162.85 95.70   
7  1 ARG E 115 ? ? -116.30 -169.25 
8  1 LYS E 136 ? ? -128.01 -63.28  
9  1 SER G 25  ? ? -30.57  -75.78  
10 1 LYS G 128 ? ? -97.39  34.18   
11 1 SER I 68  ? ? 72.26   41.89   
12 1 ARG I 115 ? ? -107.59 -167.51 
13 1 THR I 135 ? ? -66.79  4.93    
14 1 LYS I 136 ? ? -127.32 -57.63  
15 1 SER J 25  ? ? -4.40   -85.65  
16 1 ALA J 55  ? ? -106.82 45.53   
17 1 SER J 68  ? ? 41.81   82.78   
18 1 ARG J 115 ? ? -104.99 -164.80 
19 1 ASN J 131 ? ? -71.08  -167.13 
20 1 SER K 68  ? ? 44.35   73.24   
21 1 SER K 98  ? ? -169.09 108.13  
22 1 LYS K 136 ? ? -123.42 -55.42  
23 1 ILE K 151 ? ? -38.93  127.63  
24 1 GLU L 21  ? ? -179.35 127.84  
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION' ZN  
3 water      HOH 
# 
_pdbx_reflns_twin.domain_id    1 
_pdbx_reflns_twin.crystal_id   1 
_pdbx_reflns_twin.diffrn_id    1 
_pdbx_reflns_twin.type         ? 
_pdbx_reflns_twin.operator     l,-k,h 
_pdbx_reflns_twin.fraction     0.124 
# 
