data_9B7A
# 
_entry.id   9B7A 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.401 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9B7A         pdb_00009b7a 10.2210/pdb9b7a/pdb 
WWPDB D_1000282791 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-22 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9B7A 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              cluo@simm.ac.cn 
_pdbx_contact_author.name_first         CHENG 
_pdbx_contact_author.name_last          Luo 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-3864-8382 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wu, Y.'  1 ? 
'Xu, H.'  2 ? 
'Luo, C.' 3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                598 
_citation.page_last                 598 
_citation.title                     
'Inhibited peroxidase activity of peroxiredoxin 1 by palmitic acid exacerbates nonalcoholic steatohepatitis in male mice.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-55939-2 
_citation.pdbx_database_id_PubMed   39799115 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Yin, W.'     1  ?                   
primary 'Xu, H.'      2  ?                   
primary 'Bai, Z.'     3  ?                   
primary 'Wu, Y.'      4  0009-0006-7759-9551 
primary 'Zhang, Y.'   5  ?                   
primary 'Liu, R.'     6  ?                   
primary 'Wang, Z.'    7  ?                   
primary 'Zhang, B.'   8  ?                   
primary 'Shen, J.'    9  ?                   
primary 'Zhang, H.'   10 0000-0002-6166-2089 
primary 'Chen, X.'    11 ?                   
primary 'Ma, D.'      12 ?                   
primary 'Shi, X.'     13 ?                   
primary 'Yan, L.'     14 ?                   
primary 'Zhang, C.'   15 ?                   
primary 'Jiang, H.'   16 0000-0003-0656-6315 
primary 'Chen, K.'    17 ?                   
primary 'Guo, D.'     18 ?                   
primary 'Niu, W.'     19 ?                   
primary 'Yin, H.'     20 0000-0001-7049-1560 
primary 'Zhang, W.J.' 21 0000-0003-4727-2380 
primary 'Luo, C.'     22 0000-0003-3864-8382 
primary 'Xie, X.'     23 0000-0003-4317-7327 
# 
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 Peroxiredoxin-1                                                                                19337.066 2   
1.11.1.24 ? ? ? 
2 non-polymer syn '(2R)-3-(3,4-dihydroxyphenyl)-2-{[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]oxy}propanoic acid' 360.315   1   ? ? 
? ? 
3 water       nat water                                                                                          18.015    392 ? ? 
? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;Natural killer cell-enhancing factor A,NKEF-A,Proliferation-associated gene protein,PAG,Thioredoxin peroxidase 2,Thioredoxin-dependent peroxide reductase 2,Thioredoxin-dependent peroxiredoxin 1
;
# 
_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       
;MSSGNAKIGHPAPNFKATAVMPDGQFKDISLSDYKGKYVVFFFYPLDFTFVSPTEIIAFSDRAEEFKKLNCQVIGASVDS
HFSHLAWVNTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLV
QAFQFTDKHGEVCPA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSSGNAKIGHPAPNFKATAVMPDGQFKDISLSDYKGKYVVFFFYPLDFTFVSPTEIIAFSDRAEEFKKLNCQVIGASVDS
HFSHLAWVNTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLV
QAFQFTDKHGEVCPA
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(2R)-3-(3,4-dihydroxyphenyl)-2-{[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]oxy}propanoic acid' ROA 
3 water                                                                                          HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   SER n 
1 4   GLY n 
1 5   ASN n 
1 6   ALA n 
1 7   LYS n 
1 8   ILE n 
1 9   GLY n 
1 10  HIS n 
1 11  PRO n 
1 12  ALA n 
1 13  PRO n 
1 14  ASN n 
1 15  PHE n 
1 16  LYS n 
1 17  ALA n 
1 18  THR n 
1 19  ALA n 
1 20  VAL n 
1 21  MET n 
1 22  PRO n 
1 23  ASP n 
1 24  GLY n 
1 25  GLN n 
1 26  PHE n 
1 27  LYS n 
1 28  ASP n 
1 29  ILE n 
1 30  SER n 
1 31  LEU n 
1 32  SER n 
1 33  ASP n 
1 34  TYR n 
1 35  LYS n 
1 36  GLY n 
1 37  LYS n 
1 38  TYR n 
1 39  VAL n 
1 40  VAL n 
1 41  PHE n 
1 42  PHE n 
1 43  PHE n 
1 44  TYR n 
1 45  PRO n 
1 46  LEU n 
1 47  ASP n 
1 48  PHE n 
1 49  THR n 
1 50  PHE n 
1 51  VAL n 
1 52  SER n 
1 53  PRO n 
1 54  THR n 
1 55  GLU n 
1 56  ILE n 
1 57  ILE n 
1 58  ALA n 
1 59  PHE n 
1 60  SER n 
1 61  ASP n 
1 62  ARG n 
1 63  ALA n 
1 64  GLU n 
1 65  GLU n 
1 66  PHE n 
1 67  LYS n 
1 68  LYS n 
1 69  LEU n 
1 70  ASN n 
1 71  CYS n 
1 72  GLN n 
1 73  VAL n 
1 74  ILE n 
1 75  GLY n 
1 76  ALA n 
1 77  SER n 
1 78  VAL n 
1 79  ASP n 
1 80  SER n 
1 81  HIS n 
1 82  PHE n 
1 83  SER n 
1 84  HIS n 
1 85  LEU n 
1 86  ALA n 
1 87  TRP n 
1 88  VAL n 
1 89  ASN n 
1 90  THR n 
1 91  PRO n 
1 92  LYS n 
1 93  LYS n 
1 94  GLN n 
1 95  GLY n 
1 96  GLY n 
1 97  LEU n 
1 98  GLY n 
1 99  PRO n 
1 100 MET n 
1 101 ASN n 
1 102 ILE n 
1 103 PRO n 
1 104 LEU n 
1 105 VAL n 
1 106 SER n 
1 107 ASP n 
1 108 PRO n 
1 109 LYS n 
1 110 ARG n 
1 111 THR n 
1 112 ILE n 
1 113 ALA n 
1 114 GLN n 
1 115 ASP n 
1 116 TYR n 
1 117 GLY n 
1 118 VAL n 
1 119 LEU n 
1 120 LYS n 
1 121 ALA n 
1 122 ASP n 
1 123 GLU n 
1 124 GLY n 
1 125 ILE n 
1 126 SER n 
1 127 PHE n 
1 128 ARG n 
1 129 GLY n 
1 130 LEU n 
1 131 PHE n 
1 132 ILE n 
1 133 ILE n 
1 134 ASP n 
1 135 ASP n 
1 136 LYS n 
1 137 GLY n 
1 138 ILE n 
1 139 LEU n 
1 140 ARG n 
1 141 GLN n 
1 142 ILE n 
1 143 THR n 
1 144 VAL n 
1 145 ASN n 
1 146 ASP n 
1 147 LEU n 
1 148 PRO n 
1 149 VAL n 
1 150 GLY n 
1 151 ARG n 
1 152 SER n 
1 153 VAL n 
1 154 ASP n 
1 155 GLU n 
1 156 THR n 
1 157 LEU n 
1 158 ARG n 
1 159 LEU n 
1 160 VAL n 
1 161 GLN n 
1 162 ALA n 
1 163 PHE n 
1 164 GLN n 
1 165 PHE n 
1 166 THR n 
1 167 ASP n 
1 168 LYS n 
1 169 HIS n 
1 170 GLY n 
1 171 GLU n 
1 172 VAL n 
1 173 CYS n 
1 174 PRO n 
1 175 ALA n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   175 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'PRDX1, PAGA, PAGB, TDPX2' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_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                   ? 
# 
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 
ROA non-polymer         . '(2R)-3-(3,4-dihydroxyphenyl)-2-{[(2E)-3-(3,4-dihydroxyphenyl)prop-2-enoyl]oxy}propanoic acid' 
'Rosmarinic acid' 'C18 H16 O8'     360.315 
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 
TYR 'L-peptide linking' y TYROSINE                                                                                       ? 
'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                                                                         ? 
'C5 H11 N O2'    117.146 
# 
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   SER 3   3   3   SER SER A . n 
A 1 4   GLY 4   4   4   GLY GLY A . n 
A 1 5   ASN 5   5   5   ASN ASN A . n 
A 1 6   ALA 6   6   6   ALA ALA A . n 
A 1 7   LYS 7   7   7   LYS LYS A . n 
A 1 8   ILE 8   8   8   ILE ILE A . n 
A 1 9   GLY 9   9   9   GLY GLY A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  PRO 11  11  11  PRO PRO A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  ASN 14  14  14  ASN ASN A . n 
A 1 15  PHE 15  15  15  PHE PHE A . n 
A 1 16  LYS 16  16  16  LYS LYS A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  THR 18  18  18  THR THR A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  MET 21  21  21  MET MET A . n 
A 1 22  PRO 22  22  22  PRO PRO A . n 
A 1 23  ASP 23  23  23  ASP ASP A . n 
A 1 24  GLY 24  24  24  GLY GLY A . n 
A 1 25  GLN 25  25  25  GLN GLN A . n 
A 1 26  PHE 26  26  26  PHE PHE A . n 
A 1 27  LYS 27  27  27  LYS LYS A . n 
A 1 28  ASP 28  28  28  ASP ASP A . n 
A 1 29  ILE 29  29  29  ILE ILE A . n 
A 1 30  SER 30  30  30  SER SER A . n 
A 1 31  LEU 31  31  31  LEU LEU A . n 
A 1 32  SER 32  32  32  SER SER A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  TYR 34  34  34  TYR TYR A . n 
A 1 35  LYS 35  35  35  LYS LYS A . n 
A 1 36  GLY 36  36  36  GLY GLY A . n 
A 1 37  LYS 37  37  37  LYS LYS A . n 
A 1 38  TYR 38  38  38  TYR TYR A . n 
A 1 39  VAL 39  39  39  VAL VAL A . n 
A 1 40  VAL 40  40  40  VAL VAL A . n 
A 1 41  PHE 41  41  41  PHE PHE A . n 
A 1 42  PHE 42  42  42  PHE PHE A . n 
A 1 43  PHE 43  43  43  PHE PHE A . n 
A 1 44  TYR 44  44  44  TYR TYR A . n 
A 1 45  PRO 45  45  45  PRO PRO A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  THR 49  49  49  THR THR A . n 
A 1 50  PHE 50  50  50  PHE PHE A . n 
A 1 51  VAL 51  51  51  VAL VAL A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  PRO 53  53  53  PRO PRO A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ILE 56  56  56  ILE ILE A . n 
A 1 57  ILE 57  57  57  ILE ILE A . n 
A 1 58  ALA 58  58  58  ALA ALA A . n 
A 1 59  PHE 59  59  59  PHE PHE A . n 
A 1 60  SER 60  60  60  SER SER A . n 
A 1 61  ASP 61  61  61  ASP ASP A . n 
A 1 62  ARG 62  62  62  ARG ARG A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  GLU 65  65  65  GLU GLU A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LYS 67  67  67  LYS LYS A . n 
A 1 68  LYS 68  68  68  LYS LYS A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  ASN 70  70  70  ASN ASN A . n 
A 1 71  CYS 71  71  71  CYS CYS A . n 
A 1 72  GLN 72  72  72  GLN GLN A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  ILE 74  74  74  ILE ILE A . n 
A 1 75  GLY 75  75  75  GLY GLY A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  SER 77  77  77  SER SER A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  ASP 79  79  79  ASP ASP A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  HIS 81  81  81  HIS HIS A . n 
A 1 82  PHE 82  82  82  PHE PHE A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  HIS 84  84  84  HIS HIS A . n 
A 1 85  LEU 85  85  85  LEU LEU A . n 
A 1 86  ALA 86  86  86  ALA ALA A . n 
A 1 87  TRP 87  87  87  TRP TRP A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  ASN 89  89  89  ASN ASN A . n 
A 1 90  THR 90  90  90  THR THR A . n 
A 1 91  PRO 91  91  91  PRO PRO A . n 
A 1 92  LYS 92  92  92  LYS LYS A . n 
A 1 93  LYS 93  93  93  LYS LYS A . n 
A 1 94  GLN 94  94  94  GLN GLN A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  GLY 96  96  96  GLY GLY A . n 
A 1 97  LEU 97  97  97  LEU LEU A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  PRO 99  99  99  PRO PRO A . n 
A 1 100 MET 100 100 100 MET MET A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 ILE 102 102 102 ILE ILE A . n 
A 1 103 PRO 103 103 103 PRO PRO A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 VAL 105 105 105 VAL VAL A . n 
A 1 106 SER 106 106 106 SER SER A . n 
A 1 107 ASP 107 107 107 ASP ASP A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 LYS 109 109 109 LYS LYS A . n 
A 1 110 ARG 110 110 110 ARG ARG A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 GLN 114 114 114 GLN GLN A . n 
A 1 115 ASP 115 115 115 ASP ASP A . n 
A 1 116 TYR 116 116 116 TYR TYR A . n 
A 1 117 GLY 117 117 117 GLY GLY A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 LYS 120 120 120 LYS LYS A . n 
A 1 121 ALA 121 121 121 ALA ALA A . n 
A 1 122 ASP 122 122 122 ASP ASP A . n 
A 1 123 GLU 123 123 123 GLU GLU A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 ILE 125 125 125 ILE ILE A . n 
A 1 126 SER 126 126 126 SER SER A . n 
A 1 127 PHE 127 127 127 PHE PHE A . n 
A 1 128 ARG 128 128 128 ARG ARG A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 PHE 131 131 131 PHE PHE A . n 
A 1 132 ILE 132 132 132 ILE ILE A . n 
A 1 133 ILE 133 133 133 ILE ILE A . n 
A 1 134 ASP 134 134 134 ASP ASP A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 GLY 137 137 137 GLY GLY A . n 
A 1 138 ILE 138 138 138 ILE ILE A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 ARG 140 140 140 ARG ARG A . n 
A 1 141 GLN 141 141 141 GLN GLN A . n 
A 1 142 ILE 142 142 142 ILE ILE A . n 
A 1 143 THR 143 143 143 THR THR A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASN 145 145 145 ASN ASN A . n 
A 1 146 ASP 146 146 146 ASP ASP A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 PRO 148 148 148 PRO PRO A . n 
A 1 149 VAL 149 149 149 VAL VAL A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ARG 151 151 151 ARG ARG A . n 
A 1 152 SER 152 152 152 SER SER A . n 
A 1 153 VAL 153 153 153 VAL VAL A . n 
A 1 154 ASP 154 154 154 ASP ASP A . n 
A 1 155 GLU 155 155 155 GLU GLU A . n 
A 1 156 THR 156 156 156 THR THR A . n 
A 1 157 LEU 157 157 157 LEU LEU A . n 
A 1 158 ARG 158 158 158 ARG ARG A . n 
A 1 159 LEU 159 159 159 LEU LEU A . n 
A 1 160 VAL 160 160 160 VAL VAL A . n 
A 1 161 GLN 161 161 161 GLN GLN A . n 
A 1 162 ALA 162 162 162 ALA ALA A . n 
A 1 163 PHE 163 163 163 PHE PHE A . n 
A 1 164 GLN 164 164 164 GLN GLN A . n 
A 1 165 PHE 165 165 165 PHE PHE A . n 
A 1 166 THR 166 166 166 THR THR A . n 
A 1 167 ASP 167 167 167 ASP ASP A . n 
A 1 168 LYS 168 168 168 LYS LYS A . n 
A 1 169 HIS 169 169 169 HIS HIS A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 GLU 171 171 ?   ?   ?   A . n 
A 1 172 VAL 172 172 ?   ?   ?   A . n 
A 1 173 CYS 173 173 ?   ?   ?   A . n 
A 1 174 PRO 174 174 ?   ?   ?   A . n 
A 1 175 ALA 175 175 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   SER 3   3   3   SER SER B . n 
B 1 4   GLY 4   4   4   GLY GLY B . n 
B 1 5   ASN 5   5   5   ASN ASN B . n 
B 1 6   ALA 6   6   6   ALA ALA B . n 
B 1 7   LYS 7   7   7   LYS LYS B . n 
B 1 8   ILE 8   8   8   ILE ILE B . n 
B 1 9   GLY 9   9   9   GLY GLY B . n 
B 1 10  HIS 10  10  10  HIS HIS B . n 
B 1 11  PRO 11  11  11  PRO PRO B . n 
B 1 12  ALA 12  12  12  ALA ALA B . n 
B 1 13  PRO 13  13  13  PRO PRO B . n 
B 1 14  ASN 14  14  14  ASN ASN B . n 
B 1 15  PHE 15  15  15  PHE PHE B . n 
B 1 16  LYS 16  16  16  LYS LYS B . n 
B 1 17  ALA 17  17  17  ALA ALA B . n 
B 1 18  THR 18  18  18  THR THR B . n 
B 1 19  ALA 19  19  19  ALA ALA B . n 
B 1 20  VAL 20  20  20  VAL VAL B . n 
B 1 21  MET 21  21  21  MET MET B . n 
B 1 22  PRO 22  22  22  PRO PRO B . n 
B 1 23  ASP 23  23  23  ASP ASP B . n 
B 1 24  GLY 24  24  24  GLY GLY B . n 
B 1 25  GLN 25  25  25  GLN GLN B . n 
B 1 26  PHE 26  26  26  PHE PHE B . n 
B 1 27  LYS 27  27  27  LYS LYS B . n 
B 1 28  ASP 28  28  28  ASP ASP B . n 
B 1 29  ILE 29  29  29  ILE ILE B . n 
B 1 30  SER 30  30  30  SER SER B . n 
B 1 31  LEU 31  31  31  LEU LEU B . n 
B 1 32  SER 32  32  32  SER SER B . n 
B 1 33  ASP 33  33  33  ASP ASP B . n 
B 1 34  TYR 34  34  34  TYR TYR B . n 
B 1 35  LYS 35  35  35  LYS LYS B . n 
B 1 36  GLY 36  36  36  GLY GLY B . n 
B 1 37  LYS 37  37  37  LYS LYS B . n 
B 1 38  TYR 38  38  38  TYR TYR B . n 
B 1 39  VAL 39  39  39  VAL VAL B . n 
B 1 40  VAL 40  40  40  VAL VAL B . n 
B 1 41  PHE 41  41  41  PHE PHE B . n 
B 1 42  PHE 42  42  42  PHE PHE B . n 
B 1 43  PHE 43  43  43  PHE PHE B . n 
B 1 44  TYR 44  44  44  TYR TYR B . n 
B 1 45  PRO 45  45  45  PRO PRO B . n 
B 1 46  LEU 46  46  46  LEU LEU B . n 
B 1 47  ASP 47  47  47  ASP ASP B . n 
B 1 48  PHE 48  48  48  PHE PHE B . n 
B 1 49  THR 49  49  49  THR THR B . n 
B 1 50  PHE 50  50  50  PHE PHE B . n 
B 1 51  VAL 51  51  51  VAL VAL B . n 
B 1 52  SER 52  52  52  SER SER B . n 
B 1 53  PRO 53  53  53  PRO PRO B . n 
B 1 54  THR 54  54  54  THR THR B . n 
B 1 55  GLU 55  55  55  GLU GLU B . n 
B 1 56  ILE 56  56  56  ILE ILE B . n 
B 1 57  ILE 57  57  57  ILE ILE B . n 
B 1 58  ALA 58  58  58  ALA ALA B . n 
B 1 59  PHE 59  59  59  PHE PHE B . n 
B 1 60  SER 60  60  60  SER SER B . n 
B 1 61  ASP 61  61  61  ASP ASP B . n 
B 1 62  ARG 62  62  62  ARG ARG B . n 
B 1 63  ALA 63  63  63  ALA ALA B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  GLU 65  65  65  GLU GLU B . n 
B 1 66  PHE 66  66  66  PHE PHE B . n 
B 1 67  LYS 67  67  67  LYS LYS B . n 
B 1 68  LYS 68  68  68  LYS LYS B . n 
B 1 69  LEU 69  69  69  LEU LEU B . n 
B 1 70  ASN 70  70  70  ASN ASN B . n 
B 1 71  CYS 71  71  71  CYS CYS B . n 
B 1 72  GLN 72  72  72  GLN GLN B . n 
B 1 73  VAL 73  73  73  VAL VAL B . n 
B 1 74  ILE 74  74  74  ILE ILE B . n 
B 1 75  GLY 75  75  75  GLY GLY B . n 
B 1 76  ALA 76  76  76  ALA ALA B . n 
B 1 77  SER 77  77  77  SER SER B . n 
B 1 78  VAL 78  78  78  VAL VAL B . n 
B 1 79  ASP 79  79  79  ASP ASP B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  HIS 81  81  81  HIS HIS B . n 
B 1 82  PHE 82  82  82  PHE PHE B . n 
B 1 83  SER 83  83  83  SER SER B . n 
B 1 84  HIS 84  84  84  HIS HIS B . n 
B 1 85  LEU 85  85  85  LEU LEU B . n 
B 1 86  ALA 86  86  86  ALA ALA B . n 
B 1 87  TRP 87  87  87  TRP TRP B . n 
B 1 88  VAL 88  88  88  VAL VAL B . n 
B 1 89  ASN 89  89  89  ASN ASN B . n 
B 1 90  THR 90  90  90  THR THR B . n 
B 1 91  PRO 91  91  91  PRO PRO B . n 
B 1 92  LYS 92  92  92  LYS LYS B . n 
B 1 93  LYS 93  93  93  LYS LYS B . n 
B 1 94  GLN 94  94  94  GLN GLN B . n 
B 1 95  GLY 95  95  95  GLY GLY B . n 
B 1 96  GLY 96  96  96  GLY GLY B . n 
B 1 97  LEU 97  97  97  LEU LEU B . n 
B 1 98  GLY 98  98  98  GLY GLY B . n 
B 1 99  PRO 99  99  99  PRO PRO B . n 
B 1 100 MET 100 100 100 MET MET B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 ILE 102 102 102 ILE ILE B . n 
B 1 103 PRO 103 103 103 PRO PRO B . n 
B 1 104 LEU 104 104 104 LEU LEU B . n 
B 1 105 VAL 105 105 105 VAL VAL B . n 
B 1 106 SER 106 106 106 SER SER B . n 
B 1 107 ASP 107 107 107 ASP ASP B . n 
B 1 108 PRO 108 108 108 PRO PRO B . n 
B 1 109 LYS 109 109 109 LYS LYS B . n 
B 1 110 ARG 110 110 110 ARG ARG B . n 
B 1 111 THR 111 111 111 THR THR B . n 
B 1 112 ILE 112 112 112 ILE ILE B . n 
B 1 113 ALA 113 113 113 ALA ALA B . n 
B 1 114 GLN 114 114 114 GLN GLN B . n 
B 1 115 ASP 115 115 115 ASP ASP B . n 
B 1 116 TYR 116 116 116 TYR TYR B . n 
B 1 117 GLY 117 117 117 GLY GLY B . n 
B 1 118 VAL 118 118 118 VAL VAL B . n 
B 1 119 LEU 119 119 119 LEU LEU B . n 
B 1 120 LYS 120 120 120 LYS LYS B . n 
B 1 121 ALA 121 121 121 ALA ALA B . n 
B 1 122 ASP 122 122 122 ASP ASP B . n 
B 1 123 GLU 123 123 123 GLU GLU B . n 
B 1 124 GLY 124 124 124 GLY GLY B . n 
B 1 125 ILE 125 125 125 ILE ILE B . n 
B 1 126 SER 126 126 126 SER SER B . n 
B 1 127 PHE 127 127 127 PHE PHE B . n 
B 1 128 ARG 128 128 128 ARG ARG B . n 
B 1 129 GLY 129 129 129 GLY GLY B . n 
B 1 130 LEU 130 130 130 LEU LEU B . n 
B 1 131 PHE 131 131 131 PHE PHE B . n 
B 1 132 ILE 132 132 132 ILE ILE B . n 
B 1 133 ILE 133 133 133 ILE ILE B . n 
B 1 134 ASP 134 134 134 ASP ASP B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 LYS 136 136 136 LYS LYS B . n 
B 1 137 GLY 137 137 137 GLY GLY B . n 
B 1 138 ILE 138 138 138 ILE ILE B . n 
B 1 139 LEU 139 139 139 LEU LEU B . n 
B 1 140 ARG 140 140 140 ARG ARG B . n 
B 1 141 GLN 141 141 141 GLN GLN B . n 
B 1 142 ILE 142 142 142 ILE ILE B . n 
B 1 143 THR 143 143 143 THR THR B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASN 145 145 145 ASN ASN B . n 
B 1 146 ASP 146 146 146 ASP ASP B . n 
B 1 147 LEU 147 147 147 LEU LEU B . n 
B 1 148 PRO 148 148 148 PRO PRO B . n 
B 1 149 VAL 149 149 149 VAL VAL B . n 
B 1 150 GLY 150 150 150 GLY GLY B . n 
B 1 151 ARG 151 151 151 ARG ARG B . n 
B 1 152 SER 152 152 152 SER SER B . n 
B 1 153 VAL 153 153 153 VAL VAL B . n 
B 1 154 ASP 154 154 154 ASP ASP B . n 
B 1 155 GLU 155 155 155 GLU GLU B . n 
B 1 156 THR 156 156 156 THR THR B . n 
B 1 157 LEU 157 157 157 LEU LEU B . n 
B 1 158 ARG 158 158 158 ARG ARG B . n 
B 1 159 LEU 159 159 159 LEU LEU B . n 
B 1 160 VAL 160 160 160 VAL VAL B . n 
B 1 161 GLN 161 161 161 GLN GLN B . n 
B 1 162 ALA 162 162 162 ALA ALA B . n 
B 1 163 PHE 163 163 163 PHE PHE B . n 
B 1 164 GLN 164 164 164 GLN GLN B . n 
B 1 165 PHE 165 165 165 PHE PHE B . n 
B 1 166 THR 166 166 166 THR THR B . n 
B 1 167 ASP 167 167 167 ASP ASP B . n 
B 1 168 LYS 168 168 168 LYS LYS B . n 
B 1 169 HIS 169 169 169 HIS HIS B . n 
B 1 170 GLY 170 170 170 GLY GLY B . n 
B 1 171 GLU 171 171 ?   ?   ?   B . n 
B 1 172 VAL 172 172 ?   ?   ?   B . n 
B 1 173 CYS 173 173 ?   ?   ?   B . n 
B 1 174 PRO 174 174 ?   ?   ?   B . n 
B 1 175 ALA 175 175 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        ROA 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ROA 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 
C 2 ROA 1   201 201 ROA ROA A . 
D 3 HOH 1   301 301 HOH HOH A . 
D 3 HOH 2   302 302 HOH HOH A . 
D 3 HOH 3   303 303 HOH HOH A . 
D 3 HOH 4   304 304 HOH HOH A . 
D 3 HOH 5   305 305 HOH HOH A . 
D 3 HOH 6   306 306 HOH HOH A . 
D 3 HOH 7   307 307 HOH HOH A . 
D 3 HOH 8   308 308 HOH HOH A . 
D 3 HOH 9   309 309 HOH HOH A . 
D 3 HOH 10  310 310 HOH HOH A . 
D 3 HOH 11  311 311 HOH HOH A . 
D 3 HOH 12  312 312 HOH HOH A . 
D 3 HOH 13  313 313 HOH HOH A . 
D 3 HOH 14  314 314 HOH HOH A . 
D 3 HOH 15  315 315 HOH HOH A . 
D 3 HOH 16  316 316 HOH HOH A . 
D 3 HOH 17  317 317 HOH HOH A . 
D 3 HOH 18  318 318 HOH HOH A . 
D 3 HOH 19  319 319 HOH HOH A . 
D 3 HOH 20  320 320 HOH HOH A . 
D 3 HOH 21  321 321 HOH HOH A . 
D 3 HOH 22  322 322 HOH HOH A . 
D 3 HOH 23  323 323 HOH HOH A . 
D 3 HOH 24  324 324 HOH HOH A . 
D 3 HOH 25  325 325 HOH HOH A . 
D 3 HOH 26  326 326 HOH HOH A . 
D 3 HOH 27  327 327 HOH HOH A . 
D 3 HOH 28  328 328 HOH HOH A . 
D 3 HOH 29  329 329 HOH HOH A . 
D 3 HOH 30  330 330 HOH HOH A . 
D 3 HOH 31  331 331 HOH HOH A . 
D 3 HOH 32  332 332 HOH HOH A . 
D 3 HOH 33  333 333 HOH HOH A . 
D 3 HOH 34  334 334 HOH HOH A . 
D 3 HOH 35  335 335 HOH HOH A . 
D 3 HOH 36  336 336 HOH HOH A . 
D 3 HOH 37  337 337 HOH HOH A . 
D 3 HOH 38  338 338 HOH HOH A . 
D 3 HOH 39  339 339 HOH HOH A . 
D 3 HOH 40  340 340 HOH HOH A . 
D 3 HOH 41  341 341 HOH HOH A . 
D 3 HOH 42  342 342 HOH HOH A . 
D 3 HOH 43  343 343 HOH HOH A . 
D 3 HOH 44  344 344 HOH HOH A . 
D 3 HOH 45  345 345 HOH HOH A . 
D 3 HOH 46  346 346 HOH HOH A . 
D 3 HOH 47  347 347 HOH HOH A . 
D 3 HOH 48  348 348 HOH HOH A . 
D 3 HOH 49  349 349 HOH HOH A . 
D 3 HOH 50  350 350 HOH HOH A . 
D 3 HOH 51  351 351 HOH HOH A . 
D 3 HOH 52  352 352 HOH HOH A . 
D 3 HOH 53  353 353 HOH HOH A . 
D 3 HOH 54  354 354 HOH HOH A . 
D 3 HOH 55  355 355 HOH HOH A . 
D 3 HOH 56  356 356 HOH HOH A . 
D 3 HOH 57  357 357 HOH HOH A . 
D 3 HOH 58  358 358 HOH HOH A . 
D 3 HOH 59  359 359 HOH HOH A . 
D 3 HOH 60  360 360 HOH HOH A . 
D 3 HOH 61  361 361 HOH HOH A . 
D 3 HOH 62  362 362 HOH HOH A . 
D 3 HOH 63  363 363 HOH HOH A . 
D 3 HOH 64  364 364 HOH HOH A . 
D 3 HOH 65  365 365 HOH HOH A . 
D 3 HOH 66  366 366 HOH HOH A . 
D 3 HOH 67  367 367 HOH HOH A . 
D 3 HOH 68  368 368 HOH HOH A . 
D 3 HOH 69  369 369 HOH HOH A . 
D 3 HOH 70  370 370 HOH HOH A . 
D 3 HOH 71  371 371 HOH HOH A . 
D 3 HOH 72  372 372 HOH HOH A . 
D 3 HOH 73  373 373 HOH HOH A . 
D 3 HOH 74  374 374 HOH HOH A . 
D 3 HOH 75  375 375 HOH HOH A . 
D 3 HOH 76  376 376 HOH HOH A . 
D 3 HOH 77  377 377 HOH HOH A . 
D 3 HOH 78  378 378 HOH HOH A . 
D 3 HOH 79  379 379 HOH HOH A . 
D 3 HOH 80  380 380 HOH HOH A . 
D 3 HOH 81  381 381 HOH HOH A . 
D 3 HOH 82  382 382 HOH HOH A . 
D 3 HOH 83  383 383 HOH HOH A . 
D 3 HOH 84  384 384 HOH HOH A . 
D 3 HOH 85  385 385 HOH HOH A . 
D 3 HOH 86  386 386 HOH HOH A . 
D 3 HOH 87  387 387 HOH HOH A . 
D 3 HOH 88  388 388 HOH HOH A . 
D 3 HOH 89  389 389 HOH HOH A . 
D 3 HOH 90  390 390 HOH HOH A . 
D 3 HOH 91  391 391 HOH HOH A . 
D 3 HOH 92  392 392 HOH HOH A . 
D 3 HOH 93  393 393 HOH HOH A . 
D 3 HOH 94  394 394 HOH HOH A . 
D 3 HOH 95  395 395 HOH HOH A . 
D 3 HOH 96  396 396 HOH HOH A . 
D 3 HOH 97  397 397 HOH HOH A . 
D 3 HOH 98  398 398 HOH HOH A . 
D 3 HOH 99  399 399 HOH HOH A . 
D 3 HOH 100 400 400 HOH HOH A . 
D 3 HOH 101 401 401 HOH HOH A . 
D 3 HOH 102 402 402 HOH HOH A . 
D 3 HOH 103 403 403 HOH HOH A . 
D 3 HOH 104 404 404 HOH HOH A . 
D 3 HOH 105 405 405 HOH HOH A . 
D 3 HOH 106 406 406 HOH HOH A . 
D 3 HOH 107 407 407 HOH HOH A . 
D 3 HOH 108 408 408 HOH HOH A . 
D 3 HOH 109 409 409 HOH HOH A . 
D 3 HOH 110 410 410 HOH HOH A . 
D 3 HOH 111 411 411 HOH HOH A . 
D 3 HOH 112 412 412 HOH HOH A . 
D 3 HOH 113 413 413 HOH HOH A . 
D 3 HOH 114 414 414 HOH HOH A . 
D 3 HOH 115 415 415 HOH HOH A . 
D 3 HOH 116 416 416 HOH HOH A . 
D 3 HOH 117 417 417 HOH HOH A . 
D 3 HOH 118 418 418 HOH HOH A . 
D 3 HOH 119 419 419 HOH HOH A . 
D 3 HOH 120 420 420 HOH HOH A . 
D 3 HOH 121 421 421 HOH HOH A . 
D 3 HOH 122 422 422 HOH HOH A . 
D 3 HOH 123 423 423 HOH HOH A . 
D 3 HOH 124 424 424 HOH HOH A . 
D 3 HOH 125 425 425 HOH HOH A . 
D 3 HOH 126 426 426 HOH HOH A . 
D 3 HOH 127 427 427 HOH HOH A . 
D 3 HOH 128 428 428 HOH HOH A . 
D 3 HOH 129 429 429 HOH HOH A . 
D 3 HOH 130 430 430 HOH HOH A . 
D 3 HOH 131 431 431 HOH HOH A . 
D 3 HOH 132 432 432 HOH HOH A . 
D 3 HOH 133 433 433 HOH HOH A . 
D 3 HOH 134 434 434 HOH HOH A . 
D 3 HOH 135 435 435 HOH HOH A . 
D 3 HOH 136 436 436 HOH HOH A . 
D 3 HOH 137 437 437 HOH HOH A . 
D 3 HOH 138 438 438 HOH HOH A . 
D 3 HOH 139 439 439 HOH HOH A . 
D 3 HOH 140 440 440 HOH HOH A . 
D 3 HOH 141 441 441 HOH HOH A . 
D 3 HOH 142 442 442 HOH HOH A . 
D 3 HOH 143 443 443 HOH HOH A . 
D 3 HOH 144 444 444 HOH HOH A . 
D 3 HOH 145 445 445 HOH HOH A . 
D 3 HOH 146 446 446 HOH HOH A . 
D 3 HOH 147 447 447 HOH HOH A . 
D 3 HOH 148 448 448 HOH HOH A . 
D 3 HOH 149 449 449 HOH HOH A . 
D 3 HOH 150 450 450 HOH HOH A . 
D 3 HOH 151 451 451 HOH HOH A . 
D 3 HOH 152 452 452 HOH HOH A . 
D 3 HOH 153 453 453 HOH HOH A . 
D 3 HOH 154 454 454 HOH HOH A . 
D 3 HOH 155 455 455 HOH HOH A . 
D 3 HOH 156 456 456 HOH HOH A . 
D 3 HOH 157 457 457 HOH HOH A . 
D 3 HOH 158 458 458 HOH HOH A . 
D 3 HOH 159 459 459 HOH HOH A . 
D 3 HOH 160 460 460 HOH HOH A . 
D 3 HOH 161 461 461 HOH HOH A . 
D 3 HOH 162 462 462 HOH HOH A . 
D 3 HOH 163 463 463 HOH HOH A . 
D 3 HOH 164 464 464 HOH HOH A . 
D 3 HOH 165 465 465 HOH HOH A . 
D 3 HOH 166 466 466 HOH HOH A . 
D 3 HOH 167 467 467 HOH HOH A . 
D 3 HOH 168 468 468 HOH HOH A . 
D 3 HOH 169 469 469 HOH HOH A . 
D 3 HOH 170 470 470 HOH HOH A . 
D 3 HOH 171 471 471 HOH HOH A . 
D 3 HOH 172 472 472 HOH HOH A . 
D 3 HOH 173 473 473 HOH HOH A . 
D 3 HOH 174 474 474 HOH HOH A . 
D 3 HOH 175 475 475 HOH HOH A . 
D 3 HOH 176 476 476 HOH HOH A . 
D 3 HOH 177 477 477 HOH HOH A . 
D 3 HOH 178 478 478 HOH HOH A . 
D 3 HOH 179 479 479 HOH HOH A . 
D 3 HOH 180 480 480 HOH HOH A . 
D 3 HOH 181 481 481 HOH HOH A . 
D 3 HOH 182 482 482 HOH HOH A . 
D 3 HOH 183 483 483 HOH HOH A . 
D 3 HOH 184 484 484 HOH HOH A . 
D 3 HOH 185 485 486 HOH HOH A . 
D 3 HOH 186 486 487 HOH HOH A . 
D 3 HOH 187 487 488 HOH HOH A . 
D 3 HOH 188 488 489 HOH HOH A . 
D 3 HOH 189 489 490 HOH HOH A . 
D 3 HOH 190 490 491 HOH HOH A . 
D 3 HOH 191 491 492 HOH HOH A . 
D 3 HOH 192 492 493 HOH HOH A . 
D 3 HOH 193 493 494 HOH HOH A . 
D 3 HOH 194 494 495 HOH HOH A . 
D 3 HOH 195 495 496 HOH HOH A . 
D 3 HOH 196 496 497 HOH HOH A . 
D 3 HOH 197 497 498 HOH HOH A . 
D 3 HOH 198 498 499 HOH HOH A . 
D 3 HOH 199 499 500 HOH HOH A . 
D 3 HOH 200 500 501 HOH HOH A . 
D 3 HOH 201 501 502 HOH HOH A . 
D 3 HOH 202 502 503 HOH HOH A . 
D 3 HOH 203 503 504 HOH HOH A . 
D 3 HOH 204 504 505 HOH HOH A . 
D 3 HOH 205 505 506 HOH HOH A . 
D 3 HOH 206 506 507 HOH HOH A . 
D 3 HOH 207 507 508 HOH HOH A . 
D 3 HOH 208 508 509 HOH HOH A . 
E 3 HOH 1   201 201 HOH HOH B . 
E 3 HOH 2   202 202 HOH HOH B . 
E 3 HOH 3   203 203 HOH HOH B . 
E 3 HOH 4   204 204 HOH HOH B . 
E 3 HOH 5   205 205 HOH HOH B . 
E 3 HOH 6   206 206 HOH HOH B . 
E 3 HOH 7   207 207 HOH HOH B . 
E 3 HOH 8   208 208 HOH HOH B . 
E 3 HOH 9   209 209 HOH HOH B . 
E 3 HOH 10  210 210 HOH HOH B . 
E 3 HOH 11  211 211 HOH HOH B . 
E 3 HOH 12  212 212 HOH HOH B . 
E 3 HOH 13  213 213 HOH HOH B . 
E 3 HOH 14  214 214 HOH HOH B . 
E 3 HOH 15  215 215 HOH HOH B . 
E 3 HOH 16  216 216 HOH HOH B . 
E 3 HOH 17  217 217 HOH HOH B . 
E 3 HOH 18  218 218 HOH HOH B . 
E 3 HOH 19  219 219 HOH HOH B . 
E 3 HOH 20  220 220 HOH HOH B . 
E 3 HOH 21  221 221 HOH HOH B . 
E 3 HOH 22  222 222 HOH HOH B . 
E 3 HOH 23  223 223 HOH HOH B . 
E 3 HOH 24  224 224 HOH HOH B . 
E 3 HOH 25  225 225 HOH HOH B . 
E 3 HOH 26  226 226 HOH HOH B . 
E 3 HOH 27  227 227 HOH HOH B . 
E 3 HOH 28  228 228 HOH HOH B . 
E 3 HOH 29  229 229 HOH HOH B . 
E 3 HOH 30  230 230 HOH HOH B . 
E 3 HOH 31  231 231 HOH HOH B . 
E 3 HOH 32  232 232 HOH HOH B . 
E 3 HOH 33  233 233 HOH HOH B . 
E 3 HOH 34  234 234 HOH HOH B . 
E 3 HOH 35  235 235 HOH HOH B . 
E 3 HOH 36  236 236 HOH HOH B . 
E 3 HOH 37  237 237 HOH HOH B . 
E 3 HOH 38  238 238 HOH HOH B . 
E 3 HOH 39  239 239 HOH HOH B . 
E 3 HOH 40  240 240 HOH HOH B . 
E 3 HOH 41  241 241 HOH HOH B . 
E 3 HOH 42  242 242 HOH HOH B . 
E 3 HOH 43  243 243 HOH HOH B . 
E 3 HOH 44  244 244 HOH HOH B . 
E 3 HOH 45  245 245 HOH HOH B . 
E 3 HOH 46  246 246 HOH HOH B . 
E 3 HOH 47  247 247 HOH HOH B . 
E 3 HOH 48  248 248 HOH HOH B . 
E 3 HOH 49  249 249 HOH HOH B . 
E 3 HOH 50  250 250 HOH HOH B . 
E 3 HOH 51  251 251 HOH HOH B . 
E 3 HOH 52  252 252 HOH HOH B . 
E 3 HOH 53  253 253 HOH HOH B . 
E 3 HOH 54  254 254 HOH HOH B . 
E 3 HOH 55  255 255 HOH HOH B . 
E 3 HOH 56  256 256 HOH HOH B . 
E 3 HOH 57  257 257 HOH HOH B . 
E 3 HOH 58  258 258 HOH HOH B . 
E 3 HOH 59  259 259 HOH HOH B . 
E 3 HOH 60  260 260 HOH HOH B . 
E 3 HOH 61  261 261 HOH HOH B . 
E 3 HOH 62  262 262 HOH HOH B . 
E 3 HOH 63  263 263 HOH HOH B . 
E 3 HOH 64  264 264 HOH HOH B . 
E 3 HOH 65  265 265 HOH HOH B . 
E 3 HOH 66  266 266 HOH HOH B . 
E 3 HOH 67  267 267 HOH HOH B . 
E 3 HOH 68  268 268 HOH HOH B . 
E 3 HOH 69  269 269 HOH HOH B . 
E 3 HOH 70  270 270 HOH HOH B . 
E 3 HOH 71  271 271 HOH HOH B . 
E 3 HOH 72  272 272 HOH HOH B . 
E 3 HOH 73  273 273 HOH HOH B . 
E 3 HOH 74  274 274 HOH HOH B . 
E 3 HOH 75  275 275 HOH HOH B . 
E 3 HOH 76  276 276 HOH HOH B . 
E 3 HOH 77  277 277 HOH HOH B . 
E 3 HOH 78  278 278 HOH HOH B . 
E 3 HOH 79  279 279 HOH HOH B . 
E 3 HOH 80  280 280 HOH HOH B . 
E 3 HOH 81  281 281 HOH HOH B . 
E 3 HOH 82  282 282 HOH HOH B . 
E 3 HOH 83  283 283 HOH HOH B . 
E 3 HOH 84  284 284 HOH HOH B . 
E 3 HOH 85  285 285 HOH HOH B . 
E 3 HOH 86  286 286 HOH HOH B . 
E 3 HOH 87  287 287 HOH HOH B . 
E 3 HOH 88  288 288 HOH HOH B . 
E 3 HOH 89  289 289 HOH HOH B . 
E 3 HOH 90  290 290 HOH HOH B . 
E 3 HOH 91  291 291 HOH HOH B . 
E 3 HOH 92  292 292 HOH HOH B . 
E 3 HOH 93  293 293 HOH HOH B . 
E 3 HOH 94  294 294 HOH HOH B . 
E 3 HOH 95  295 295 HOH HOH B . 
E 3 HOH 96  296 296 HOH HOH B . 
E 3 HOH 97  297 297 HOH HOH B . 
E 3 HOH 98  298 298 HOH HOH B . 
E 3 HOH 99  299 299 HOH HOH B . 
E 3 HOH 100 300 300 HOH HOH B . 
E 3 HOH 101 301 301 HOH HOH B . 
E 3 HOH 102 302 302 HOH HOH B . 
E 3 HOH 103 303 303 HOH HOH B . 
E 3 HOH 104 304 304 HOH HOH B . 
E 3 HOH 105 305 305 HOH HOH B . 
E 3 HOH 106 306 306 HOH HOH B . 
E 3 HOH 107 307 307 HOH HOH B . 
E 3 HOH 108 308 308 HOH HOH B . 
E 3 HOH 109 309 309 HOH HOH B . 
E 3 HOH 110 310 310 HOH HOH B . 
E 3 HOH 111 311 311 HOH HOH B . 
E 3 HOH 112 312 312 HOH HOH B . 
E 3 HOH 113 313 313 HOH HOH B . 
E 3 HOH 114 314 314 HOH HOH B . 
E 3 HOH 115 315 315 HOH HOH B . 
E 3 HOH 116 316 316 HOH HOH B . 
E 3 HOH 117 317 317 HOH HOH B . 
E 3 HOH 118 318 318 HOH HOH B . 
E 3 HOH 119 319 319 HOH HOH B . 
E 3 HOH 120 320 320 HOH HOH B . 
E 3 HOH 121 321 321 HOH HOH B . 
E 3 HOH 122 322 322 HOH HOH B . 
E 3 HOH 123 323 323 HOH HOH B . 
E 3 HOH 124 324 324 HOH HOH B . 
E 3 HOH 125 325 325 HOH HOH B . 
E 3 HOH 126 326 326 HOH HOH B . 
E 3 HOH 127 327 327 HOH HOH B . 
E 3 HOH 128 328 328 HOH HOH B . 
E 3 HOH 129 329 329 HOH HOH B . 
E 3 HOH 130 330 330 HOH HOH B . 
E 3 HOH 131 331 331 HOH HOH B . 
E 3 HOH 132 332 332 HOH HOH B . 
E 3 HOH 133 333 333 HOH HOH B . 
E 3 HOH 134 334 334 HOH HOH B . 
E 3 HOH 135 335 335 HOH HOH B . 
E 3 HOH 136 336 336 HOH HOH B . 
E 3 HOH 137 337 337 HOH HOH B . 
E 3 HOH 138 338 338 HOH HOH B . 
E 3 HOH 139 339 339 HOH HOH B . 
E 3 HOH 140 340 340 HOH HOH B . 
E 3 HOH 141 341 341 HOH HOH B . 
E 3 HOH 142 342 342 HOH HOH B . 
E 3 HOH 143 343 343 HOH HOH B . 
E 3 HOH 144 344 344 HOH HOH B . 
E 3 HOH 145 345 345 HOH HOH B . 
E 3 HOH 146 346 346 HOH HOH B . 
E 3 HOH 147 347 347 HOH HOH B . 
E 3 HOH 148 348 348 HOH HOH B . 
E 3 HOH 149 349 349 HOH HOH B . 
E 3 HOH 150 350 350 HOH HOH B . 
E 3 HOH 151 351 351 HOH HOH B . 
E 3 HOH 152 352 352 HOH HOH B . 
E 3 HOH 153 353 353 HOH HOH B . 
E 3 HOH 154 354 354 HOH HOH B . 
E 3 HOH 155 355 355 HOH HOH B . 
E 3 HOH 156 356 356 HOH HOH B . 
E 3 HOH 157 357 357 HOH HOH B . 
E 3 HOH 158 358 358 HOH HOH B . 
E 3 HOH 159 359 359 HOH HOH B . 
E 3 HOH 160 360 360 HOH HOH B . 
E 3 HOH 161 361 361 HOH HOH B . 
E 3 HOH 162 362 362 HOH HOH B . 
E 3 HOH 163 363 363 HOH HOH B . 
E 3 HOH 164 364 364 HOH HOH B . 
E 3 HOH 165 365 365 HOH HOH B . 
E 3 HOH 166 366 366 HOH HOH B . 
E 3 HOH 167 367 367 HOH HOH B . 
E 3 HOH 168 368 368 HOH HOH B . 
E 3 HOH 169 369 369 HOH HOH B . 
E 3 HOH 170 370 370 HOH HOH B . 
E 3 HOH 171 371 371 HOH HOH B . 
E 3 HOH 172 372 372 HOH HOH B . 
E 3 HOH 173 373 373 HOH HOH B . 
E 3 HOH 174 374 374 HOH HOH B . 
E 3 HOH 175 375 375 HOH HOH B . 
E 3 HOH 176 376 376 HOH HOH B . 
E 3 HOH 177 377 377 HOH HOH B . 
E 3 HOH 178 378 378 HOH HOH B . 
E 3 HOH 179 379 379 HOH HOH B . 
E 3 HOH 180 380 380 HOH HOH B . 
E 3 HOH 181 381 381 HOH HOH B . 
E 3 HOH 182 382 382 HOH HOH B . 
E 3 HOH 183 383 383 HOH HOH B . 
E 3 HOH 184 384 384 HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A SER 3   ? CB ? A SER 3   CB 
2 1 Y 1 A SER 3   ? OG ? A SER 3   OG 
3 1 Y 1 A LYS 93  ? CE ? A LYS 93  CE 
4 1 Y 1 B SER 3   ? CB ? B SER 3   CB 
5 1 Y 1 B SER 3   ? OG ? B SER 3   OG 
6 1 Y 1 B LYS 109 ? CD ? B LYS 109 CD 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.15.2_3472 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9B7A 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     66.762 
_cell.length_a_esd                 ? 
_cell.length_b                     78.573 
_cell.length_b_esd                 ? 
_cell.length_c                     82.689 
_cell.length_c_esd                 ? 
_cell.volume                       433760.912 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9B7A 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            'P 2ac 2ab' 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9B7A 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.80 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          56.13 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '10% v/v Tacsimate pH 7.5, 0.1M MES pH 6.5, and 25% PEG4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-05-23 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9785 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL19U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9785 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL19U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          27.75 
_reflns.entry_id                                       9B7A 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.71 
_reflns.d_resolution_low                               43.33 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     47617 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.86 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          18.64 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.994 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.713 
_reflns_shell.d_res_low                                     1.774 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4637 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.939 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               30.73 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9B7A 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.71 
_refine.ls_d_res_low                             43.33 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     47398 
_refine.ls_number_reflns_R_free                  2377 
_refine.ls_number_reflns_R_work                  45021 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.87 
_refine.ls_percent_reflns_R_free                 5.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1662 
_refine.ls_R_factor_R_free                       0.1919 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1648 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 19.7142 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.1718 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.71 
_refine_hist.d_res_low                        43.33 
_refine_hist.number_atoms_solvent             393 
_refine_hist.number_atoms_total               3045 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2626 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         26 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0059 ? 2719 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.8054 ? 3679 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0614 ? 397  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0066 ? 481  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 3.1681 ? 1597 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.71 1.75  . . 139 2585 98.66  . . . . 0.2285 . . . . . . . . . . . 0.2634 
'X-RAY DIFFRACTION' 1.75 1.79  . . 148 2583 99.71  . . . . 0.2104 . . . . . . . . . . . 0.2685 
'X-RAY DIFFRACTION' 1.79 1.83  . . 155 2598 99.82  . . . . 0.2016 . . . . . . . . . . . 0.2869 
'X-RAY DIFFRACTION' 1.83 1.87  . . 130 2637 99.86  . . . . 0.1849 . . . . . . . . . . . 0.2035 
'X-RAY DIFFRACTION' 1.87 1.92  . . 155 2569 100.00 . . . . 0.1899 . . . . . . . . . . . 0.2132 
'X-RAY DIFFRACTION' 1.92 1.98  . . 158 2597 100.00 . . . . 0.1830 . . . . . . . . . . . 0.2268 
'X-RAY DIFFRACTION' 1.98 2.04  . . 138 2630 99.93  . . . . 0.1840 . . . . . . . . . . . 0.2412 
'X-RAY DIFFRACTION' 2.04 2.12  . . 136 2653 100.00 . . . . 0.1803 . . . . . . . . . . . 0.2322 
'X-RAY DIFFRACTION' 2.12 2.20  . . 137 2619 100.00 . . . . 0.1755 . . . . . . . . . . . 0.2147 
'X-RAY DIFFRACTION' 2.20 2.30  . . 136 2642 100.00 . . . . 0.1865 . . . . . . . . . . . 0.2120 
'X-RAY DIFFRACTION' 2.30 2.42  . . 124 2649 100.00 . . . . 0.1768 . . . . . . . . . . . 0.2072 
'X-RAY DIFFRACTION' 2.42 2.58  . . 129 2673 100.00 . . . . 0.1750 . . . . . . . . . . . 0.2203 
'X-RAY DIFFRACTION' 2.58 2.77  . . 148 2633 100.00 . . . . 0.1753 . . . . . . . . . . . 0.1954 
'X-RAY DIFFRACTION' 2.77 3.05  . . 126 2694 100.00 . . . . 0.1723 . . . . . . . . . . . 0.2017 
'X-RAY DIFFRACTION' 3.05 3.50  . . 121 2702 100.00 . . . . 0.1651 . . . . . . . . . . . 0.2089 
'X-RAY DIFFRACTION' 3.50 4.40  . . 154 2718 100.00 . . . . 0.1364 . . . . . . . . . . . 0.1473 
'X-RAY DIFFRACTION' 4.40 43.33 . . 143 2839 99.90  . . . . 0.1471 . . . . . . . . . . . 0.1615 
# 
_struct.entry_id                     9B7A 
_struct.title                        'Crystal structure of peroxiredoxin 1 with RA' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9B7A 
_struct_keywords.text            OXIDOREDUCTASE 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PRDX1_HUMAN 
_struct_ref.pdbx_db_accession          Q06830 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSSGNAKIGHPAPNFKATAVMPDGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDS
HFCHLAWVNTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLV
QAFQFTDKHGEVCPA
;
_struct_ref.pdbx_align_begin           1 
# 
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 9B7A A 1 ? 175 ? Q06830 1 ? 175 ? 1 175 
2 1 9B7A B 1 ? 175 ? Q06830 1 ? 175 ? 1 175 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9B7A SER A 52 ? UNP Q06830 CYS 52 conflict 52 1 
1 9B7A SER A 83 ? UNP Q06830 CYS 83 conflict 83 2 
2 9B7A SER B 52 ? UNP Q06830 CYS 52 conflict 52 3 
2 9B7A SER B 83 ? UNP Q06830 CYS 83 conflict 83 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
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)' 1820  ? 
1 MORE         -9    ? 
1 'SSA (A^2)'  14690 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_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]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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  AA1 SER A 32  ? LYS A 35  ? SER A 32  LYS A 35  5 ? 4  
HELX_P HELX_P2  AA2 VAL A 51  ? ARG A 62  ? VAL A 51  ARG A 62  1 ? 12 
HELX_P HELX_P3  AA3 ARG A 62  ? LEU A 69  ? ARG A 62  LEU A 69  1 ? 8  
HELX_P HELX_P4  AA4 SER A 80  ? THR A 90  ? SER A 80  THR A 90  1 ? 11 
HELX_P HELX_P5  AA5 PRO A 91  ? GLY A 95  ? PRO A 91  GLY A 95  5 ? 5  
HELX_P HELX_P6  AA6 ARG A 110 ? TYR A 116 ? ARG A 110 TYR A 116 1 ? 7  
HELX_P HELX_P7  AA7 SER A 152 ? HIS A 169 ? SER A 152 HIS A 169 1 ? 18 
HELX_P HELX_P8  AA8 SER B 32  ? LYS B 35  ? SER B 32  LYS B 35  5 ? 4  
HELX_P HELX_P9  AA9 VAL B 51  ? ARG B 62  ? VAL B 51  ARG B 62  1 ? 12 
HELX_P HELX_P10 AB1 ARG B 62  ? LYS B 68  ? ARG B 62  LYS B 68  1 ? 7  
HELX_P HELX_P11 AB2 SER B 80  ? ASN B 89  ? SER B 80  ASN B 89  1 ? 10 
HELX_P HELX_P12 AB3 PRO B 91  ? GLY B 95  ? PRO B 91  GLY B 95  5 ? 5  
HELX_P HELX_P13 AB4 ARG B 110 ? TYR B 116 ? ARG B 110 TYR B 116 1 ? 7  
HELX_P HELX_P14 AB5 SER B 152 ? LYS B 168 ? SER B 152 LYS B 168 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   14 
_struct_sheet.details          ? 
# 
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 
AA1 1  2  ? anti-parallel 
AA1 2  3  ? anti-parallel 
AA1 3  4  ? parallel      
AA1 4  5  ? parallel      
AA1 5  6  ? anti-parallel 
AA1 6  7  ? anti-parallel 
AA1 7  8  ? anti-parallel 
AA1 8  9  ? anti-parallel 
AA1 9  10 ? anti-parallel 
AA1 10 11 ? parallel      
AA1 11 12 ? parallel      
AA1 12 13 ? anti-parallel 
AA1 13 14 ? 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 
AA1 1  PHE A 26  ? SER A 30  ? PHE A 26  SER A 30  
AA1 2  LYS A 16  ? VAL A 20  ? LYS A 16  VAL A 20  
AA1 3  LEU A 104 ? SER A 106 ? LEU A 104 SER A 106 
AA1 4  CYS A 71  ? SER A 77  ? CYS A 71  SER A 77  
AA1 5  TYR A 38  ? PHE A 43  ? TYR A 38  PHE A 43  
AA1 6  ARG A 128 ? ILE A 133 ? ARG A 128 ILE A 133 
AA1 7  LEU A 139 ? ASN A 145 ? LEU A 139 ASN A 145 
AA1 8  LEU B 139 ? ASN B 145 ? LEU B 139 ASN B 145 
AA1 9  ARG B 128 ? ILE B 133 ? ARG B 128 ILE B 133 
AA1 10 TYR B 38  ? PHE B 43  ? TYR B 38  PHE B 43  
AA1 11 CYS B 71  ? SER B 77  ? CYS B 71  SER B 77  
AA1 12 LEU B 104 ? SER B 106 ? LEU B 104 SER B 106 
AA1 13 LYS B 16  ? VAL B 20  ? LYS B 16  VAL B 20  
AA1 14 PHE B 26  ? SER B 30  ? PHE B 26  SER B 30  
# 
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 
AA1 1  2  O LYS A 27  ? O LYS A 27  N ALA A 19  ? N ALA A 19  
AA1 2  3  N THR A 18  ? N THR A 18  O SER A 106 ? O SER A 106 
AA1 3  4  O VAL A 105 ? O VAL A 105 N GLY A 75  ? N GLY A 75  
AA1 4  5  O ILE A 74  ? O ILE A 74  N VAL A 40  ? N VAL A 40  
AA1 5  6  N PHE A 43  ? N PHE A 43  O GLY A 129 ? O GLY A 129 
AA1 6  7  N LEU A 130 ? N LEU A 130 O THR A 143 ? O THR A 143 
AA1 7  8  N VAL A 144 ? N VAL A 144 O ILE B 142 ? O ILE B 142 
AA1 8  9  O ARG B 140 ? O ARG B 140 N ILE B 132 ? N ILE B 132 
AA1 9  10 O GLY B 129 ? O GLY B 129 N PHE B 43  ? N PHE B 43  
AA1 10 11 N VAL B 40  ? N VAL B 40  O ILE B 74  ? O ILE B 74  
AA1 11 12 N GLY B 75  ? N GLY B 75  O VAL B 105 ? O VAL B 105 
AA1 12 13 O SER B 106 ? O SER B 106 N THR B 18  ? N THR B 18  
AA1 13 14 N ALA B 17  ? N ALA B 17  O ILE B 29  ? O ILE B 29  
# 
_pdbx_entry_details.entry_id                   9B7A 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    THR 
_pdbx_validate_torsion.auth_asym_id    B 
_pdbx_validate_torsion.auth_seq_id     49 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -113.73 
_pdbx_validate_torsion.psi             -169.17 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 x+1/2,-y+1/2,-z 
3 -x,y+1/2,-z+1/2 
4 -x+1/2,-y,z+1/2 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A SER 2   ? A SER 2   
3  1 Y 1 A GLU 171 ? A GLU 171 
4  1 Y 1 A VAL 172 ? A VAL 172 
5  1 Y 1 A CYS 173 ? A CYS 173 
6  1 Y 1 A PRO 174 ? A PRO 174 
7  1 Y 1 A ALA 175 ? A ALA 175 
8  1 Y 1 B MET 1   ? B MET 1   
9  1 Y 1 B SER 2   ? B SER 2   
10 1 Y 1 B GLU 171 ? B GLU 171 
11 1 Y 1 B VAL 172 ? B VAL 172 
12 1 Y 1 B CYS 173 ? B CYS 173 
13 1 Y 1 B PRO 174 ? B PRO 174 
14 1 Y 1 B ALA 175 ? B ALA 175 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
ROA CAU  C Y N 290 
ROA CAV  C Y N 291 
ROA OAY  O N N 292 
ROA CAW  C Y N 293 
ROA OAZ  O N N 294 
ROA CAX  C Y N 295 
ROA CAT  C Y N 296 
ROA CAS  C Y N 297 
ROA CAO  C N N 298 
ROA CAN  C N R 299 
ROA CAP  C N N 300 
ROA OAR  O N N 301 
ROA OAQ  O N N 302 
ROA OAM  O N N 303 
ROA CAK  C N N 304 
ROA OAL  O N N 305 
ROA CAJ  C N N 306 
ROA CAI  C N N 307 
ROA CAC  C Y N 308 
ROA CAD  C Y N 309 
ROA CAE  C Y N 310 
ROA OAG  O N N 311 
ROA CAF  C Y N 312 
ROA OAH  O N N 313 
ROA CAB  C Y N 314 
ROA CAA  C Y N 315 
ROA HAU  H N N 316 
ROA HOAY H N N 317 
ROA HOAZ H N N 318 
ROA HAX  H N N 319 
ROA HAT  H N N 320 
ROA HAO  H N N 321 
ROA HAOA H N N 322 
ROA HAN  H N N 323 
ROA HAJ  H N N 324 
ROA HAI  H N N 325 
ROA HAD  H N N 326 
ROA HOAG H N N 327 
ROA HOAH H N N 328 
ROA HAB  H N N 329 
ROA HAA  H N N 330 
ROA H18  H N N 331 
SER N    N N N 332 
SER CA   C N S 333 
SER C    C N N 334 
SER O    O N N 335 
SER CB   C N N 336 
SER OG   O N N 337 
SER OXT  O N N 338 
SER H    H N N 339 
SER H2   H N N 340 
SER HA   H N N 341 
SER HB2  H N N 342 
SER HB3  H N N 343 
SER HG   H N N 344 
SER HXT  H N N 345 
THR N    N N N 346 
THR CA   C N S 347 
THR C    C N N 348 
THR O    O N N 349 
THR CB   C N R 350 
THR OG1  O N N 351 
THR CG2  C N N 352 
THR OXT  O N N 353 
THR H    H N N 354 
THR H2   H N N 355 
THR HA   H N N 356 
THR HB   H N N 357 
THR HG1  H N N 358 
THR HG21 H N N 359 
THR HG22 H N N 360 
THR HG23 H N N 361 
THR HXT  H N N 362 
TRP N    N N N 363 
TRP CA   C N S 364 
TRP C    C N N 365 
TRP O    O N N 366 
TRP CB   C N N 367 
TRP CG   C Y N 368 
TRP CD1  C Y N 369 
TRP CD2  C Y N 370 
TRP NE1  N Y N 371 
TRP CE2  C Y N 372 
TRP CE3  C Y N 373 
TRP CZ2  C Y N 374 
TRP CZ3  C Y N 375 
TRP CH2  C Y N 376 
TRP OXT  O N N 377 
TRP H    H N N 378 
TRP H2   H N N 379 
TRP HA   H N N 380 
TRP HB2  H N N 381 
TRP HB3  H N N 382 
TRP HD1  H N N 383 
TRP HE1  H N N 384 
TRP HE3  H N N 385 
TRP HZ2  H N N 386 
TRP HZ3  H N N 387 
TRP HH2  H N N 388 
TRP HXT  H N N 389 
TYR N    N N N 390 
TYR CA   C N S 391 
TYR C    C N N 392 
TYR O    O N N 393 
TYR CB   C N N 394 
TYR CG   C Y N 395 
TYR CD1  C Y N 396 
TYR CD2  C Y N 397 
TYR CE1  C Y N 398 
TYR CE2  C Y N 399 
TYR CZ   C Y N 400 
TYR OH   O N N 401 
TYR OXT  O N N 402 
TYR H    H N N 403 
TYR H2   H N N 404 
TYR HA   H N N 405 
TYR HB2  H N N 406 
TYR HB3  H N N 407 
TYR HD1  H N N 408 
TYR HD2  H N N 409 
TYR HE1  H N N 410 
TYR HE2  H N N 411 
TYR HH   H N N 412 
TYR HXT  H N N 413 
VAL N    N N N 414 
VAL CA   C N S 415 
VAL C    C N N 416 
VAL O    O N N 417 
VAL CB   C N N 418 
VAL CG1  C N N 419 
VAL CG2  C N N 420 
VAL OXT  O N N 421 
VAL H    H N N 422 
VAL H2   H N N 423 
VAL HA   H N N 424 
VAL HB   H N N 425 
VAL HG11 H N N 426 
VAL HG12 H N N 427 
VAL HG13 H N N 428 
VAL HG21 H N N 429 
VAL HG22 H N N 430 
VAL HG23 H N N 431 
VAL HXT  H N N 432 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
ROA CAU CAV  doub Y N 277 
ROA CAU CAS  sing Y N 278 
ROA CAU HAU  sing N N 279 
ROA CAV OAY  sing N N 280 
ROA CAV CAW  sing Y N 281 
ROA OAY HOAY sing N N 282 
ROA CAW OAZ  sing N N 283 
ROA CAW CAX  doub Y N 284 
ROA OAZ HOAZ sing N N 285 
ROA CAX CAT  sing Y N 286 
ROA CAX HAX  sing N N 287 
ROA CAT CAS  doub Y N 288 
ROA CAT HAT  sing N N 289 
ROA CAS CAO  sing N N 290 
ROA CAO CAN  sing N N 291 
ROA CAO HAO  sing N N 292 
ROA CAO HAOA sing N N 293 
ROA CAN CAP  sing N N 294 
ROA CAN OAM  sing N N 295 
ROA CAN HAN  sing N N 296 
ROA CAP OAR  doub N N 297 
ROA CAP OAQ  sing N N 298 
ROA OAQ H18  sing N N 299 
ROA OAM CAK  sing N N 300 
ROA CAK OAL  doub N N 301 
ROA CAK CAJ  sing N N 302 
ROA CAJ CAI  doub N E 303 
ROA CAJ HAJ  sing N N 304 
ROA CAI CAC  sing N N 305 
ROA CAI HAI  sing N N 306 
ROA CAC CAD  doub Y N 307 
ROA CAC CAA  sing Y N 308 
ROA CAD CAE  sing Y N 309 
ROA CAD HAD  sing N N 310 
ROA CAE OAG  sing N N 311 
ROA CAE CAF  doub Y N 312 
ROA OAG HOAG sing N N 313 
ROA CAF OAH  sing N N 314 
ROA CAF CAB  sing Y N 315 
ROA OAH HOAH sing N N 316 
ROA CAB CAA  doub Y N 317 
ROA CAB HAB  sing N N 318 
ROA CAA HAA  sing N N 319 
SER N   CA   sing N N 320 
SER N   H    sing N N 321 
SER N   H2   sing N N 322 
SER CA  C    sing N N 323 
SER CA  CB   sing N N 324 
SER CA  HA   sing N N 325 
SER C   O    doub N N 326 
SER C   OXT  sing N N 327 
SER CB  OG   sing N N 328 
SER CB  HB2  sing N N 329 
SER CB  HB3  sing N N 330 
SER OG  HG   sing N N 331 
SER OXT HXT  sing N N 332 
THR N   CA   sing N N 333 
THR N   H    sing N N 334 
THR N   H2   sing N N 335 
THR CA  C    sing N N 336 
THR CA  CB   sing N N 337 
THR CA  HA   sing N N 338 
THR C   O    doub N N 339 
THR C   OXT  sing N N 340 
THR CB  OG1  sing N N 341 
THR CB  CG2  sing N N 342 
THR CB  HB   sing N N 343 
THR OG1 HG1  sing N N 344 
THR CG2 HG21 sing N N 345 
THR CG2 HG22 sing N N 346 
THR CG2 HG23 sing N N 347 
THR OXT HXT  sing N N 348 
TRP N   CA   sing N N 349 
TRP N   H    sing N N 350 
TRP N   H2   sing N N 351 
TRP CA  C    sing N N 352 
TRP CA  CB   sing N N 353 
TRP CA  HA   sing N N 354 
TRP C   O    doub N N 355 
TRP C   OXT  sing N N 356 
TRP CB  CG   sing N N 357 
TRP CB  HB2  sing N N 358 
TRP CB  HB3  sing N N 359 
TRP CG  CD1  doub Y N 360 
TRP CG  CD2  sing Y N 361 
TRP CD1 NE1  sing Y N 362 
TRP CD1 HD1  sing N N 363 
TRP CD2 CE2  doub Y N 364 
TRP CD2 CE3  sing Y N 365 
TRP NE1 CE2  sing Y N 366 
TRP NE1 HE1  sing N N 367 
TRP CE2 CZ2  sing Y N 368 
TRP CE3 CZ3  doub Y N 369 
TRP CE3 HE3  sing N N 370 
TRP CZ2 CH2  doub Y N 371 
TRP CZ2 HZ2  sing N N 372 
TRP CZ3 CH2  sing Y N 373 
TRP CZ3 HZ3  sing N N 374 
TRP CH2 HH2  sing N N 375 
TRP OXT HXT  sing N N 376 
TYR N   CA   sing N N 377 
TYR N   H    sing N N 378 
TYR N   H2   sing N N 379 
TYR CA  C    sing N N 380 
TYR CA  CB   sing N N 381 
TYR CA  HA   sing N N 382 
TYR C   O    doub N N 383 
TYR C   OXT  sing N N 384 
TYR CB  CG   sing N N 385 
TYR CB  HB2  sing N N 386 
TYR CB  HB3  sing N N 387 
TYR CG  CD1  doub Y N 388 
TYR CG  CD2  sing Y N 389 
TYR CD1 CE1  sing Y N 390 
TYR CD1 HD1  sing N N 391 
TYR CD2 CE2  doub Y N 392 
TYR CD2 HD2  sing N N 393 
TYR CE1 CZ   doub Y N 394 
TYR CE1 HE1  sing N N 395 
TYR CE2 CZ   sing Y N 396 
TYR CE2 HE2  sing N N 397 
TYR CZ  OH   sing N N 398 
TYR OH  HH   sing N N 399 
TYR OXT HXT  sing N N 400 
VAL N   CA   sing N N 401 
VAL N   H    sing N N 402 
VAL N   H2   sing N N 403 
VAL CA  C    sing N N 404 
VAL CA  CB   sing N N 405 
VAL CA  HA   sing N N 406 
VAL C   O    doub N N 407 
VAL C   OXT  sing N N 408 
VAL CB  CG1  sing N N 409 
VAL CB  CG2  sing N N 410 
VAL CB  HB   sing N N 411 
VAL CG1 HG11 sing N N 412 
VAL CG1 HG12 sing N N 413 
VAL CG1 HG13 sing N N 414 
VAL CG2 HG21 sing N N 415 
VAL CG2 HG22 sing N N 416 
VAL CG2 HG23 sing N N 417 
VAL OXT HXT  sing N N 418 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           82104064 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4XCS 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 21 21 21' 
_space_group.name_Hall        'P 2ac 2ab' 
_space_group.IT_number        19 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9B7A 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.014979 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012727 
_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]   0.012094 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . SER A 1 3   ? 7.44766   21.35121 14.06796 1.000 53.36906 ? 3   SER A N   1 
ATOM   2    C CA  . SER A 1 3   ? 7.70353   22.73145 13.66842 0.868 51.98209 ? 3   SER A CA  1 
ATOM   3    C C   . SER A 1 3   ? 6.43968   23.58943 13.75384 1.000 49.19882 ? 3   SER A C   1 
ATOM   4    O O   . SER A 1 3   ? 6.49312   24.74910 14.16907 1.000 47.56077 ? 3   SER A O   1 
ATOM   5    N N   . GLY A 1 4   ? 5.30439   23.02221 13.34471 1.000 47.15955 ? 4   GLY A N   1 
ATOM   6    C CA  . GLY A 1 4   ? 4.04305   23.73645 13.40090 1.000 40.29034 ? 4   GLY A CA  1 
ATOM   7    C C   . GLY A 1 4   ? 3.69827   24.46213 12.11280 1.000 42.67264 ? 4   GLY A C   1 
ATOM   8    O O   . GLY A 1 4   ? 4.45059   24.48320 11.13330 1.000 43.02086 ? 4   GLY A O   1 
ATOM   9    N N   . ASN A 1 5   ? 2.51588   25.08362 12.13053 1.000 35.76810 ? 5   ASN A N   1 
ATOM   10   C CA  . ASN A 1 5   ? 1.96589   25.77598 10.97073 1.000 36.92111 ? 5   ASN A CA  1 
ATOM   11   C C   . ASN A 1 5   ? 1.74206   27.26048 11.22753 1.000 33.20209 ? 5   ASN A C   1 
ATOM   12   O O   . ASN A 1 5   ? 1.05419   27.91980 10.43877 1.000 34.23690 ? 5   ASN A O   1 
ATOM   13   C CB  . ASN A 1 5   ? 0.65242   25.12490 10.53792 1.000 39.10399 ? 5   ASN A CB  1 
ATOM   14   C CG  . ASN A 1 5   ? 0.84224   23.68855 10.09270 1.000 46.31365 ? 5   ASN A CG  1 
ATOM   15   O OD1 . ASN A 1 5   ? 1.22111   23.42972 8.95130  1.000 51.81948 ? 5   ASN A OD1 1 
ATOM   16   N ND2 . ASN A 1 5   ? 0.58673   22.74595 10.99665 1.000 47.69313 ? 5   ASN A ND2 1 
ATOM   17   N N   . ALA A 1 6   ? 2.28593   27.79737 12.31337 1.000 30.77092 ? 6   ALA A N   1 
ATOM   18   C CA  . ALA A 1 6   ? 2.16469   29.22317 12.60457 1.000 31.39544 ? 6   ALA A CA  1 
ATOM   19   C C   . ALA A 1 6   ? 3.24969   29.96832 11.83722 1.000 32.71793 ? 6   ALA A C   1 
ATOM   20   O O   . ALA A 1 6   ? 4.43579   29.84746 12.15578 1.000 36.63855 ? 6   ALA A O   1 
ATOM   21   C CB  . ALA A 1 6   ? 2.27734   29.46416 14.10640 1.000 30.51389 ? 6   ALA A CB  1 
ATOM   22   N N   . LYS A 1 7   ? 2.85136   30.74502 10.82880 1.000 28.80192 ? 7   LYS A N   1 
ATOM   23   C CA  . LYS A 1 7   ? 3.77901   31.49104 9.98716  1.000 27.55676 ? 7   LYS A CA  1 
ATOM   24   C C   . LYS A 1 7   ? 3.34381   32.95103 9.93178  1.000 28.08089 ? 7   LYS A C   1 
ATOM   25   O O   . LYS A 1 7   ? 2.16472   33.23511 9.69023  1.000 26.97685 ? 7   LYS A O   1 
ATOM   26   C CB  . LYS A 1 7   ? 3.81993   30.92296 8.56208  1.000 32.59263 ? 7   LYS A CB  1 
ATOM   27   C CG  . LYS A 1 7   ? 4.13527   29.42864 8.46174  1.000 37.50818 ? 7   LYS A CG  1 
ATOM   28   C CD  . LYS A 1 7   ? 5.06748   29.15182 7.28443  1.000 46.28608 ? 7   LYS A CD  1 
ATOM   29   C CE  . LYS A 1 7   ? 4.62412   27.93122 6.48073  1.000 55.50041 ? 7   LYS A CE  1 
ATOM   30   N NZ  . LYS A 1 7   ? 4.32212   26.75084 7.34151  1.000 54.52776 ? 7   LYS A NZ  1 
ATOM   31   N N   . ILE A 1 8   ? 4.29325   33.86827 10.14515 1.000 28.86454 ? 8   ILE A N   1 
ATOM   32   C CA  . ILE A 1 8   ? 3.99898   35.29541 10.00052 1.000 28.10207 ? 8   ILE A CA  1 
ATOM   33   C C   . ILE A 1 8   ? 3.48133   35.56331 8.59676  1.000 29.62072 ? 8   ILE A C   1 
ATOM   34   O O   . ILE A 1 8   ? 4.05537   35.09357 7.60742  1.000 30.04886 ? 8   ILE A O   1 
ATOM   35   C CB  . ILE A 1 8   ? 5.24506   36.15241 10.28687 1.000 28.17559 ? 8   ILE A CB  1 
ATOM   36   C CG1 . ILE A 1 8   ? 5.82447   35.86637 11.68129 1.000 30.74955 ? 8   ILE A CG1 1 
ATOM   37   C CG2 . ILE A 1 8   ? 4.92447   37.64771 10.12068 1.000 28.48482 ? 8   ILE A CG2 1 
ATOM   38   C CD1 . ILE A 1 8   ? 4.96164   36.35404 12.80745 1.000 27.60906 ? 8   ILE A CD1 1 
ATOM   39   N N   . GLY A 1 9   ? 2.40203   36.33853 8.50164  1.000 28.47655 ? 9   GLY A N   1 
ATOM   40   C CA  . GLY A 1 9   ? 1.84642   36.71619 7.21957  1.000 31.40201 ? 9   GLY A CA  1 
ATOM   41   C C   . GLY A 1 9   ? 0.88580   35.71251 6.62322  1.000 32.38849 ? 9   GLY A C   1 
ATOM   42   O O   . GLY A 1 9   ? 0.29292   35.99299 5.57219  1.000 32.57369 ? 9   GLY A O   1 
ATOM   43   N N   . HIS A 1 10  ? 0.71330   34.56370 7.25643  1.000 30.90141 ? 10  HIS A N   1 
ATOM   44   C CA  . HIS A 1 10  ? -0.21465  33.52313 6.85252  1.000 32.40284 ? 10  HIS A CA  1 
ATOM   45   C C   . HIS A 1 10  ? -1.36875  33.43748 7.84040  1.000 31.13200 ? 10  HIS A C   1 
ATOM   46   O O   . HIS A 1 10  ? -1.23055  33.82983 9.00327  1.000 29.16853 ? 10  HIS A O   1 
ATOM   47   C CB  . HIS A 1 10  ? 0.50574   32.16745 6.78672  1.000 33.80732 ? 10  HIS A CB  1 
ATOM   48   C CG  . HIS A 1 10  ? 1.45510   32.04490 5.63668  1.000 40.22944 ? 10  HIS A CG  1 
ATOM   49   N ND1 . HIS A 1 10  ? 2.60435   32.79847 5.53589  1.000 43.71392 ? 10  HIS A ND1 1 
ATOM   50   C CD2 . HIS A 1 10  ? 1.42117   31.26073 4.53263  1.000 43.48984 ? 10  HIS A CD2 1 
ATOM   51   C CE1 . HIS A 1 10  ? 3.23774   32.48536 4.41898  1.000 46.94399 ? 10  HIS A CE1 1 
ATOM   52   N NE2 . HIS A 1 10  ? 2.54145   31.55364 3.79284  1.000 50.53025 ? 10  HIS A NE2 1 
ATOM   53   N N   . PRO A 1 11  ? -2.51690  32.90656 7.42332  1.000 29.95843 ? 11  PRO A N   1 
ATOM   54   C CA  . PRO A 1 11  ? -3.61014  32.67491 8.37496  1.000 28.03438 ? 11  PRO A CA  1 
ATOM   55   C C   . PRO A 1 11  ? -3.13518  31.86446 9.57159  1.000 28.69395 ? 11  PRO A C   1 
ATOM   56   O O   . PRO A 1 11  ? -2.47950  30.82979 9.42078  1.000 29.08679 ? 11  PRO A O   1 
ATOM   57   C CB  . PRO A 1 11  ? -4.63783  31.89190 7.54696  1.000 30.79845 ? 11  PRO A CB  1 
ATOM   58   C CG  . PRO A 1 11  ? -4.37626  32.30437 6.14902  1.000 32.25896 ? 11  PRO A CG  1 
ATOM   59   C CD  . PRO A 1 11  ? -2.88745  32.51795 6.04905  1.000 34.73169 ? 11  PRO A CD  1 
ATOM   60   N N   . ALA A 1 12  ? -3.45946  32.34856 10.76641 1.000 28.57647 ? 12  ALA A N   1 
ATOM   61   C CA  . ALA A 1 12  ? -3.14188  31.60078 11.97302 1.000 27.89039 ? 12  ALA A CA  1 
ATOM   62   C C   . ALA A 1 12  ? -3.96067  30.31472 11.99671 1.000 27.45316 ? 12  ALA A C   1 
ATOM   63   O O   . ALA A 1 12  ? -5.14068  30.33555 11.63863 1.000 29.29772 ? 12  ALA A O   1 
ATOM   64   C CB  . ALA A 1 12  ? -3.44686  32.41888 13.22378 1.000 27.86869 ? 12  ALA A CB  1 
ATOM   65   N N   . PRO A 1 13  ? -3.36989  29.19278 12.40978 1.000 28.30591 ? 13  PRO A N   1 
ATOM   66   C CA  . PRO A 1 13  ? -4.11182  27.92278 12.43841 1.000 31.30341 ? 13  PRO A CA  1 
ATOM   67   C C   . PRO A 1 13  ? -5.41612  28.02960 13.21752 1.000 29.22507 ? 13  PRO A C   1 
ATOM   68   O O   . PRO A 1 13  ? -5.44626  28.50574 14.35501 1.000 29.61852 ? 13  PRO A O   1 
ATOM   69   C CB  . PRO A 1 13  ? -3.13176  26.95904 13.12037 1.000 31.71179 ? 13  PRO A CB  1 
ATOM   70   C CG  . PRO A 1 13  ? -1.78086  27.52385 12.82367 1.000 31.42090 ? 13  PRO A CG  1 
ATOM   71   C CD  . PRO A 1 13  ? -1.96443  29.02915 12.82398 1.000 29.12841 ? 13  PRO A CD  1 
ATOM   72   N N   . ASN A 1 14  ? -6.50827  27.58334 12.59854 1.000 29.59512 ? 14  ASN A N   1 
ATOM   73   C CA  . ASN A 1 14  ? -7.76927  27.55969 13.31808 1.000 29.61689 ? 14  ASN A CA  1 
ATOM   74   C C   . ASN A 1 14  ? -7.75670  26.43486 14.34810 1.000 33.32735 ? 14  ASN A C   1 
ATOM   75   O O   . ASN A 1 14  ? -6.95668  25.49328 14.28170 1.000 33.73307 ? 14  ASN A O   1 
ATOM   76   C CB  . ASN A 1 14  ? -8.94898  27.39267 12.35035 1.000 35.63313 ? 14  ASN A CB  1 
ATOM   77   C CG  . ASN A 1 14  ? -10.27439 27.92756 12.91579 1.000 36.78275 ? 14  ASN A CG  1 
ATOM   78   O OD1 . ASN A 1 14  ? -10.32319 28.52729 13.98744 1.000 34.88510 ? 14  ASN A OD1 1 
ATOM   79   N ND2 . ASN A 1 14  ? -11.35420 27.71721 12.17327 1.000 41.22213 ? 14  ASN A ND2 1 
ATOM   80   N N   . PHE A 1 15  ? -8.64458  26.55953 15.32505 1.000 29.60783 ? 15  PHE A N   1 
ATOM   81   C CA  . PHE A 1 15  ? -8.86147  25.52088 16.31481 1.000 31.18483 ? 15  PHE A CA  1 
ATOM   82   C C   . PHE A 1 15  ? -10.31155 25.59950 16.74932 1.000 30.70428 ? 15  PHE A C   1 
ATOM   83   O O   . PHE A 1 15  ? -10.95444 26.64316 16.63394 1.000 32.18810 ? 15  PHE A O   1 
ATOM   84   C CB  . PHE A 1 15  ? -7.91234  25.65141 17.52215 1.000 29.90759 ? 15  PHE A CB  1 
ATOM   85   C CG  . PHE A 1 15  ? -8.10728  26.91478 18.33366 1.000 30.44212 ? 15  PHE A CG  1 
ATOM   86   C CD1 . PHE A 1 15  ? -9.15842  27.03361 19.23447 1.000 31.17926 ? 15  PHE A CD1 1 
ATOM   87   C CD2 . PHE A 1 15  ? -7.22032  27.97065 18.20791 1.000 27.33437 ? 15  PHE A CD2 1 
ATOM   88   C CE1 . PHE A 1 15  ? -9.33957  28.20150 19.97425 1.000 31.87760 ? 15  PHE A CE1 1 
ATOM   89   C CE2 . PHE A 1 15  ? -7.38861  29.13657 18.95304 1.000 32.66787 ? 15  PHE A CE2 1 
ATOM   90   C CZ  . PHE A 1 15  ? -8.44856  29.24704 19.83444 1.000 29.83544 ? 15  PHE A CZ  1 
ATOM   91   N N   . LYS A 1 16  ? -10.82250 24.47577 17.23327 1.000 31.41345 ? 16  LYS A N   1 
ATOM   92   C CA  . LYS A 1 16  ? -12.11313 24.40456 17.90402 1.000 29.13981 ? 16  LYS A CA  1 
ATOM   93   C C   . LYS A 1 16  ? -11.90825 23.57851 19.15954 1.000 33.49249 ? 16  LYS A C   1 
ATOM   94   O O   . LYS A 1 16  ? -11.46604 22.42522 19.08343 1.000 33.43084 ? 16  LYS A O   1 
ATOM   95   C CB  . LYS A 1 16  ? -13.19188 23.77576 17.00990 1.000 36.13669 ? 16  LYS A CB  1 
ATOM   96   C CG  . LYS A 1 16  ? -14.61493 23.93638 17.54375 1.000 37.67578 ? 16  LYS A CG  1 
ATOM   97   C CD  . LYS A 1 16  ? -15.56595 22.89482 16.94226 1.000 48.68389 ? 16  LYS A CD  1 
ATOM   98   C CE  . LYS A 1 16  ? -16.84842 22.76422 17.75525 1.000 49.41140 ? 16  LYS A CE  1 
ATOM   99   N NZ  . LYS A 1 16  ? -17.85122 23.81018 17.37955 1.000 53.59783 ? 16  LYS A NZ  1 
ATOM   100  N N   . ALA A 1 17  ? -12.21411 24.16278 20.31047 1.000 26.50448 ? 17  ALA A N   1 
ATOM   101  C CA  . ALA A 1 17  ? -11.87337 23.53535 21.57498 1.000 28.10779 ? 17  ALA A CA  1 
ATOM   102  C C   . ALA A 1 17  ? -12.85620 23.98124 22.63700 1.000 26.27253 ? 17  ALA A C   1 
ATOM   103  O O   . ALA A 1 17  ? -13.46764 25.05216 22.54054 1.000 28.95459 ? 17  ALA A O   1 
ATOM   104  C CB  . ALA A 1 17  ? -10.44076 23.87871 22.00055 1.000 26.85481 ? 17  ALA A CB  1 
ATOM   105  N N   . THR A 1 18  ? -12.98057 23.16263 23.67415 1.000 25.00524 ? 18  THR A N   1 
ATOM   106  C CA  . THR A 1 18  ? -13.79255 23.53024 24.82062 1.000 22.83452 ? 18  THR A CA  1 
ATOM   107  C C   . THR A 1 18  ? -13.01892 24.50234 25.69482 1.000 27.31998 ? 18  THR A C   1 
ATOM   108  O O   . THR A 1 18  ? -11.85492 24.25438 26.02825 1.000 25.70282 ? 18  THR A O   1 
ATOM   109  C CB  . THR A 1 18  ? -14.16813 22.29752 25.63899 1.000 28.45313 ? 18  THR A CB  1 
ATOM   110  O OG1 . THR A 1 18  ? -14.87738 21.37595 24.80119 1.000 29.82661 ? 18  THR A OG1 1 
ATOM   111  C CG2 . THR A 1 18  ? -15.03016 22.69312 26.83040 1.000 26.84746 ? 18  THR A CG2 1 
ATOM   112  N N   . ALA A 1 19  ? -13.66636 25.60466 26.06203 1.000 27.15661 ? 19  ALA A N   1 
ATOM   113  C CA  . ALA A 1 19  ? -13.09413 26.58437 26.97304 1.000 25.24648 ? 19  ALA A CA  1 
ATOM   114  C C   . ALA A 1 19  ? -14.02077 26.80073 28.15709 1.000 26.14192 ? 19  ALA A C   1 
ATOM   115  O O   . ALA A 1 19  ? -15.23371 26.58224 28.05961 1.000 27.14750 ? 19  ALA A O   1 
ATOM   116  C CB  . ALA A 1 19  ? -12.85189 27.92773 26.25163 1.000 26.28501 ? 19  ALA A CB  1 
ATOM   117  N N   . VAL A 1 20  ? -13.44956 27.23513 29.27955 1.000 25.34050 ? 20  VAL A N   1 
ATOM   118  C CA  . VAL A 1 20  ? -14.24868 27.78055 30.37002 1.000 25.28341 ? 20  VAL A CA  1 
ATOM   119  C C   . VAL A 1 20  ? -14.35780 29.28239 30.13538 1.000 26.99231 ? 20  VAL A C   1 
ATOM   120  O O   . VAL A 1 20  ? -13.33890 29.97588 29.98460 1.000 26.59024 ? 20  VAL A O   1 
ATOM   121  C CB  . VAL A 1 20  ? -13.64171 27.46066 31.74710 1.000 33.69450 ? 20  VAL A CB  1 
ATOM   122  C CG1 . VAL A 1 20  ? -12.22636 28.00030 31.87086 1.000 32.95528 ? 20  VAL A CG1 1 
ATOM   123  C CG2 . VAL A 1 20  ? -14.54033 27.98454 32.87198 1.000 28.20267 ? 20  VAL A CG2 1 
ATOM   124  N N   . MET A 1 21  ? -15.58615 29.77531 30.04813 1.000 25.61071 ? 21  MET A N   1 
ATOM   125  C CA  . MET A 1 21  ? -15.82940 31.16945 29.70531 1.000 26.07987 ? 21  MET A CA  1 
ATOM   126  C C   . MET A 1 21  ? -15.82669 32.03307 30.95358 1.000 26.54887 ? 21  MET A C   1 
ATOM   127  O O   . MET A 1 21  ? -15.89926 31.53485 32.07272 1.000 27.44698 ? 21  MET A O   1 
ATOM   128  C CB  . MET A 1 21  ? -17.15276 31.27798 28.96172 1.000 28.86549 ? 21  MET A CB  1 
ATOM   129  C CG  . MET A 1 21  ? -17.24338 30.33425 27.77883 1.000 25.56249 ? 21  MET A CG  1 
ATOM   130  S SD  . MET A 1 21  ? -15.94517 30.65454 26.56990 1.000 29.65077 ? 21  MET A SD  1 
ATOM   131  C CE  . MET A 1 21  ? -16.48113 32.22141 25.88668 1.000 32.28778 ? 21  MET A CE  1 
ATOM   132  N N   . PRO A 1 22  ? -15.74468 33.36156 30.79276 1.000 25.49740 ? 22  PRO A N   1 
ATOM   133  C CA  . PRO A 1 22  ? -15.78459 34.24508 31.97173 1.000 28.13219 ? 22  PRO A CA  1 
ATOM   134  C C   . PRO A 1 22  ? -16.95882 33.99455 32.90562 1.000 28.60211 ? 22  PRO A C   1 
ATOM   135  O O   . PRO A 1 22  ? -16.82744 34.22659 34.11365 1.000 29.63859 ? 22  PRO A O   1 
ATOM   136  C CB  . PRO A 1 22  ? -15.85094 35.64534 31.34523 1.000 27.90557 ? 22  PRO A CB  1 
ATOM   137  C CG  . PRO A 1 22  ? -15.08364 35.50166 30.07041 1.000 25.56166 ? 22  PRO A CG  1 
ATOM   138  C CD  . PRO A 1 22  ? -15.39652 34.09467 29.56107 1.000 24.92088 ? 22  PRO A CD  1 
ATOM   139  N N   . ASP A 1 23  ? -18.09773 33.51293 32.39988 1.000 28.31362 ? 23  ASP A N   1 
ATOM   140  C CA  . ASP A 1 23  ? -19.23324 33.26355 33.27679 1.000 32.26879 ? 23  ASP A CA  1 
ATOM   141  C C   . ASP A 1 23  ? -19.12231 31.94294 34.02623 1.000 34.67594 ? 23  ASP A C   1 
ATOM   142  O O   . ASP A 1 23  ? -20.03365 31.60716 34.78759 1.000 35.62254 ? 23  ASP A O   1 
ATOM   143  C CB  . ASP A 1 23  ? -20.55335 33.32587 32.48611 1.000 35.27469 ? 23  ASP A CB  1 
ATOM   144  C CG  . ASP A 1 23  ? -20.69488 32.21179 31.45439 1.000 38.25995 ? 23  ASP A CG  1 
ATOM   145  O OD1 . ASP A 1 23  ? -19.77234 31.38284 31.29707 1.000 33.16981 ? 23  ASP A OD1 1 
ATOM   146  O OD2 . ASP A 1 23  ? -21.75605 32.16352 30.79509 1.000 42.15125 ? 23  ASP A OD2 1 
ATOM   147  N N   . GLY A 1 24  ? -18.03073 31.20013 33.84461 1.000 29.48750 ? 24  GLY A N   1 
ATOM   148  C CA  . GLY A 1 24  ? -17.82218 29.96771 34.57052 1.000 31.04520 ? 24  GLY A CA  1 
ATOM   149  C C   . GLY A 1 24  ? -18.41523 28.74797 33.91044 1.000 33.09490 ? 24  GLY A C   1 
ATOM   150  O O   . GLY A 1 24  ? -18.33852 27.65440 34.48288 1.000 32.84877 ? 24  GLY A O   1 
ATOM   151  N N   . GLN A 1 25  ? -18.99891 28.89706 32.73078 1.000 32.60471 ? 25  GLN A N   1 
ATOM   152  C CA  . GLN A 1 25  ? -19.57892 27.78476 31.99801 1.000 32.63497 ? 25  GLN A CA  1 
ATOM   153  C C   . GLN A 1 25  ? -18.65287 27.34534 30.87203 1.000 30.39431 ? 25  GLN A C   1 
ATOM   154  O O   . GLN A 1 25  ? -17.76378 28.07926 30.43115 1.000 28.67434 ? 25  GLN A O   1 
ATOM   155  C CB  . GLN A 1 25  ? -20.95108 28.16758 31.43694 1.000 36.01677 ? 25  GLN A CB  1 
ATOM   156  C CG  . GLN A 1 25  ? -21.94687 28.59677 32.50623 1.000 41.30377 ? 25  GLN A CG  1 
ATOM   157  C CD  . GLN A 1 25  ? -23.38090 28.55067 32.01453 1.000 45.11240 ? 25  GLN A CD  1 
ATOM   158  O OE1 . GLN A 1 25  ? -24.16964 27.71572 32.45229 1.000 49.17732 ? 25  GLN A OE1 1 
ATOM   159  N NE2 . GLN A 1 25  ? -23.72406 29.45243 31.10070 1.000 48.06079 ? 25  GLN A NE2 1 
ATOM   160  N N   . PHE A 1 26  ? -18.87108 26.12505 30.40507 1.000 25.64360 ? 26  PHE A N   1 
ATOM   161  C CA  . PHE A 1 26  ? -18.07718 25.58687 29.31822 1.000 23.62983 ? 26  PHE A CA  1 
ATOM   162  C C   . PHE A 1 26  ? -18.73228 25.92140 27.98823 1.000 28.32745 ? 26  PHE A C   1 
ATOM   163  O O   . PHE A 1 26  ? -19.95920 25.89598 27.86289 1.000 32.31505 ? 26  PHE A O   1 
ATOM   164  C CB  . PHE A 1 26  ? -17.92058 24.06845 29.44876 1.000 28.18677 ? 26  PHE A CB  1 
ATOM   165  C CG  . PHE A 1 26  ? -17.30258 23.62973 30.74298 1.000 29.53135 ? 26  PHE A CG  1 
ATOM   166  C CD1 . PHE A 1 26  ? -16.07758 24.13595 31.14807 1.000 27.77482 ? 26  PHE A CD1 1 
ATOM   167  C CD2 . PHE A 1 26  ? -17.93389 22.68254 31.54546 1.000 30.15207 ? 26  PHE A CD2 1 
ATOM   168  C CE1 . PHE A 1 26  ? -15.49700 23.72220 32.34146 1.000 28.29234 ? 26  PHE A CE1 1 
ATOM   169  C CE2 . PHE A 1 26  ? -17.36805 22.26563 32.73645 1.000 33.52249 ? 26  PHE A CE2 1 
ATOM   170  C CZ  . PHE A 1 26  ? -16.14118 22.79213 33.14169 1.000 30.58063 ? 26  PHE A CZ  1 
ATOM   171  N N   . LYS A 1 27  ? -17.90411 26.22328 26.99376 1.000 28.00125 ? 27  LYS A N   1 
ATOM   172  C CA  . LYS A 1 27  ? -18.38661 26.48676 25.64968 1.000 28.06346 ? 27  LYS A CA  1 
ATOM   173  C C   . LYS A 1 27  ? -17.30747 26.07908 24.66271 1.000 27.67864 ? 27  LYS A C   1 
ATOM   174  O O   . LYS A 1 27  ? -16.12173 26.30461 24.91043 1.000 27.86937 ? 27  LYS A O   1 
ATOM   175  C CB  . LYS A 1 27  ? -18.74492 27.97084 25.47952 1.000 29.36433 ? 27  LYS A CB  1 
ATOM   176  C CG  . LYS A 1 27  ? -19.25849 28.34384 24.09411 1.000 30.61790 ? 27  LYS A CG  1 
ATOM   177  C CD  . LYS A 1 27  ? -19.56671 29.83401 24.01932 1.000 33.97030 ? 27  LYS A CD  1 
ATOM   178  C CE  . LYS A 1 27  ? -20.01047 30.25136 22.62245 1.000 37.59494 ? 27  LYS A CE  1 
ATOM   179  N NZ  . LYS A 1 27  ? -19.90829 31.74762 22.46865 1.000 47.01546 ? 27  LYS A NZ  1 
ATOM   180  N N   . ASP A 1 28  ? -17.71583 25.48485 23.54271 1.000 25.79857 ? 28  ASP A N   1 
ATOM   181  C CA  . ASP A 1 28  ? -16.77524 25.18382 22.47182 1.000 27.48531 ? 28  ASP A CA  1 
ATOM   182  C C   . ASP A 1 28  ? -16.60934 26.41499 21.59274 1.000 30.88337 ? 28  ASP A C   1 
ATOM   183  O O   . ASP A 1 28  ? -17.58560 26.90991 21.01871 1.000 31.87903 ? 28  ASP A O   1 
ATOM   184  C CB  . ASP A 1 28  ? -17.25038 23.99548 21.64301 1.000 31.26212 ? 28  ASP A CB  1 
ATOM   185  C CG  . ASP A 1 28  ? -17.20291 22.69549 22.41393 1.000 35.76996 ? 28  ASP A CG  1 
ATOM   186  O OD1 . ASP A 1 28  ? -16.79022 22.70432 23.59224 1.000 31.81206 ? 28  ASP A OD1 1 
ATOM   187  O OD2 . ASP A 1 28  ? -17.59630 21.66329 21.84122 1.000 40.20892 ? 28  ASP A OD2 1 
ATOM   188  N N   . ILE A 1 29  ? -15.38107 26.92003 21.49847 1.000 26.70299 ? 29  ILE A N   1 
ATOM   189  C CA  . ILE A 1 29  ? -15.10129 28.12479 20.73442 1.000 27.17712 ? 29  ILE A CA  1 
ATOM   190  C C   . ILE A 1 29  ? -14.04342 27.82486 19.68115 1.000 29.14401 ? 29  ILE A C   1 
ATOM   191  O O   . ILE A 1 29  ? -13.28101 26.85833 19.78162 1.000 30.37738 ? 29  ILE A O   1 
ATOM   192  C CB  . ILE A 1 29  ? -14.65670 29.28217 21.65349 1.000 27.55727 ? 29  ILE A CB  1 
ATOM   193  C CG1 . ILE A 1 29  ? -13.26606 29.01374 22.23400 1.000 26.03536 ? 29  ILE A CG1 1 
ATOM   194  C CG2 . ILE A 1 29  ? -15.67379 29.47316 22.78988 1.000 28.61938 ? 29  ILE A CG2 1 
ATOM   195  C CD1 . ILE A 1 29  ? -12.71662 30.18893 23.08168 1.000 26.11120 ? 29  ILE A CD1 1 
ATOM   196  N N   . SER A 1 30  ? -14.00401 28.68087 18.65857 1.000 27.73568 ? 30  SER A N   1 
ATOM   197  C CA  . SER A 1 30  ? -13.04962 28.57899 17.56499 1.000 28.36162 ? 30  SER A CA  1 
ATOM   198  C C   . SER A 1 30  ? -12.36776 29.91913 17.34892 1.000 28.61854 ? 30  SER A C   1 
ATOM   199  O O   . SER A 1 30  ? -12.97546 30.97318 17.53288 1.000 26.74455 ? 30  SER A O   1 
ATOM   200  C CB  . SER A 1 30  ? -13.70791 28.15125 16.24323 1.000 31.74938 ? 30  SER A CB  1 
ATOM   201  O OG  . SER A 1 30  ? -14.34384 26.89562 16.36755 1.000 32.74578 ? 30  SER A OG  1 
ATOM   202  N N   . LEU A 1 31  ? -11.10287 29.86369 16.92826 1.000 27.84322 ? 31  LEU A N   1 
ATOM   203  C CA  . LEU A 1 31  ? -10.38484 31.09039 16.59381 1.000 28.36800 ? 31  LEU A CA  1 
ATOM   204  C C   . LEU A 1 31  ? -11.15599 31.90958 15.56757 1.000 30.26015 ? 31  LEU A C   1 
ATOM   205  O O   . LEU A 1 31  ? -11.19706 33.14477 15.64359 1.000 29.97681 ? 31  LEU A O   1 
ATOM   206  C CB  . LEU A 1 31  ? -8.99132  30.75994 16.06578 1.000 28.36458 ? 31  LEU A CB  1 
ATOM   207  C CG  . LEU A 1 31  ? -8.18750  31.98611 15.62414 1.000 31.17706 ? 31  LEU A CG  1 
ATOM   208  C CD1 . LEU A 1 31  ? -7.91727  32.92525 16.81711 1.000 33.34263 ? 31  LEU A CD1 1 
ATOM   209  C CD2 . LEU A 1 31  ? -6.89836  31.57817 14.93228 1.000 30.79434 ? 31  LEU A CD2 1 
ATOM   210  N N   . SER A 1 32  ? -11.79374 31.23073 14.61134 1.000 29.59709 ? 32  SER A N   1 
ATOM   211  C CA  . SER A 1 32  ? -12.54296 31.91150 13.56583 1.000 30.79019 ? 32  SER A CA  1 
ATOM   212  C C   . SER A 1 32  ? -13.77165 32.63126 14.09977 1.000 29.92057 ? 32  SER A C   1 
ATOM   213  O O   . SER A 1 32  ? -14.33503 33.46188 13.37972 1.000 30.27818 ? 32  SER A O   1 
ATOM   214  C CB  . SER A 1 32  ? -12.95055 30.90960 12.48363 1.000 31.26096 ? 32  SER A CB  1 
ATOM   215  O OG  . SER A 1 32  ? -13.61444 29.80043 13.06396 1.000 34.09157 ? 32  SER A OG  1 
ATOM   216  N N   . ASP A 1 33  ? -14.20174 32.33817 15.33399 1.000 28.92603 ? 33  ASP A N   1 
ATOM   217  C CA  . ASP A 1 33  ? -15.30854 33.07986 15.93399 1.000 28.69701 ? 33  ASP A CA  1 
ATOM   218  C C   . ASP A 1 33  ? -14.97515 34.55014 16.09041 1.000 28.61429 ? 33  ASP A C   1 
ATOM   219  O O   . ASP A 1 33  ? -15.88346 35.37991 16.19919 1.000 30.05270 ? 33  ASP A O   1 
ATOM   220  C CB  . ASP A 1 33  ? -15.66590 32.55464 17.32661 1.000 29.45285 ? 33  ASP A CB  1 
ATOM   221  C CG  . ASP A 1 33  ? -16.25214 31.15944 17.31087 1.000 30.19741 ? 33  ASP A CG  1 
ATOM   222  O OD1 . ASP A 1 33  ? -16.58005 30.64341 16.22246 1.000 32.87122 ? 33  ASP A OD1 1 
ATOM   223  O OD2 . ASP A 1 33  ? -16.38548 30.58933 18.41208 1.000 32.64431 ? 33  ASP A OD2 1 
ATOM   224  N N   . TYR A 1 34  ? -13.69210 34.88611 16.13702 1.000 28.37858 ? 34  TYR A N   1 
ATOM   225  C CA  . TYR A 1 34  ? -13.26342 36.23696 16.45855 1.000 30.37795 ? 34  TYR A CA  1 
ATOM   226  C C   . TYR A 1 34  ? -12.76656 36.99737 15.23718 1.000 30.55497 ? 34  TYR A C   1 
ATOM   227  O O   . TYR A 1 34  ? -12.13576 38.04940 15.38941 1.000 28.87156 ? 34  TYR A O   1 
ATOM   228  C CB  . TYR A 1 34  ? -12.20569 36.17220 17.57191 1.000 27.46932 ? 34  TYR A CB  1 
ATOM   229  C CG  . TYR A 1 34  ? -12.75950 35.46743 18.79800 1.000 28.06852 ? 34  TYR A CG  1 
ATOM   230  C CD1 . TYR A 1 34  ? -13.54055 36.15239 19.72336 1.000 27.45218 ? 34  TYR A CD1 1 
ATOM   231  C CD2 . TYR A 1 34  ? -12.55406 34.10121 19.00005 1.000 28.43754 ? 34  TYR A CD2 1 
ATOM   232  C CE1 . TYR A 1 34  ? -14.06677 35.51883 20.83760 1.000 27.93537 ? 34  TYR A CE1 1 
ATOM   233  C CE2 . TYR A 1 34  ? -13.07950 33.46024 20.10512 1.000 28.30972 ? 34  TYR A CE2 1 
ATOM   234  C CZ  . TYR A 1 34  ? -13.83905 34.16899 21.02083 1.000 28.26432 ? 34  TYR A CZ  1 
ATOM   235  O OH  . TYR A 1 34  ? -14.37130 33.52626 22.11275 1.000 31.26783 ? 34  TYR A OH  1 
ATOM   236  N N   . LYS A 1 35  ? -13.04738 36.50938 14.02747 1.000 29.92121 ? 35  LYS A N   1 
ATOM   237  C CA  . LYS A 1 35  ? -12.67056 37.27747 12.85016 1.000 32.06033 ? 35  LYS A CA  1 
ATOM   238  C C   . LYS A 1 35  ? -13.34923 38.63864 12.90164 1.000 29.11926 ? 35  LYS A C   1 
ATOM   239  O O   . LYS A 1 35  ? -14.47479 38.77061 13.39533 1.000 33.22727 ? 35  LYS A O   1 
ATOM   240  C CB  . LYS A 1 35  ? -13.02464 36.52686 11.56585 1.000 35.13921 ? 35  LYS A CB  1 
ATOM   241  C CG  . LYS A 1 35  ? -11.91189 35.56513 11.15440 1.000 38.35481 ? 35  LYS A CG  1 
ATOM   242  C CD  . LYS A 1 35  ? -12.14742 34.88276 9.82287  0.402 41.37665 ? 35  LYS A CD  1 
ATOM   243  C CE  . LYS A 1 35  ? -10.83677 34.31417 9.29243  0.668 40.42828 ? 35  LYS A CE  1 
ATOM   244  N NZ  . LYS A 1 35  ? -10.83847 34.10368 7.82220  1.000 50.25698 ? 35  LYS A NZ  1 
ATOM   245  N N   . GLY A 1 36  ? -12.62771 39.66419 12.44631 1.000 30.70866 ? 36  GLY A N   1 
ATOM   246  C CA  . GLY A 1 36  ? -13.06088 41.03323 12.60735 1.000 33.57354 ? 36  GLY A CA  1 
ATOM   247  C C   . GLY A 1 36  ? -12.49375 41.73774 13.82174 1.000 33.58088 ? 36  GLY A C   1 
ATOM   248  O O   . GLY A 1 36  ? -12.67654 42.95604 13.95711 1.000 31.18976 ? 36  GLY A O   1 
ATOM   249  N N   . LYS A 1 37  ? -11.83667 41.00924 14.72057 1.000 30.69379 ? 37  LYS A N   1 
ATOM   250  C CA  . LYS A 1 37  ? -11.13568 41.57566 15.86316 1.000 30.37022 ? 37  LYS A CA  1 
ATOM   251  C C   . LYS A 1 37  ? -9.71108  41.04320 15.87537 1.000 28.54759 ? 37  LYS A C   1 
ATOM   252  O O   . LYS A 1 37  ? -9.44165  39.94452 15.38132 1.000 25.94678 ? 37  LYS A O   1 
ATOM   253  C CB  . LYS A 1 37  ? -11.80007 41.20557 17.20411 1.000 34.18090 ? 37  LYS A CB  1 
ATOM   254  C CG  . LYS A 1 37  ? -13.31584 41.12885 17.17508 1.000 37.91807 ? 37  LYS A CG  1 
ATOM   255  C CD  . LYS A 1 37  ? -13.86687 40.79433 18.55097 1.000 39.47283 ? 37  LYS A CD  1 
ATOM   256  C CE  . LYS A 1 37  ? -13.63525 41.93916 19.52699 1.000 46.01277 ? 37  LYS A CE  1 
ATOM   257  N NZ  . LYS A 1 37  ? -14.45577 41.80059 20.76585 1.000 50.09154 ? 37  LYS A NZ  1 
ATOM   258  N N   . TYR A 1 38  ? -8.79725  41.83508 16.42937 1.000 25.80654 ? 38  TYR A N   1 
ATOM   259  C CA  . TYR A 1 38  ? -7.49665  41.29258 16.78684 1.000 26.05152 ? 38  TYR A CA  1 
ATOM   260  C C   . TYR A 1 38  ? -7.68001  40.24743 17.87887 1.000 23.59251 ? 38  TYR A C   1 
ATOM   261  O O   . TYR A 1 38  ? -8.64098  40.29201 18.65629 1.000 24.15697 ? 38  TYR A O   1 
ATOM   262  C CB  . TYR A 1 38  ? -6.55518  42.41359 17.25775 1.000 24.97760 ? 38  TYR A CB  1 
ATOM   263  C CG  . TYR A 1 38  ? -5.62567  42.89845 16.16924 1.000 23.90134 ? 38  TYR A CG  1 
ATOM   264  C CD1 . TYR A 1 38  ? -6.10991  43.61222 15.06825 1.000 24.24461 ? 38  TYR A CD1 1 
ATOM   265  C CD2 . TYR A 1 38  ? -4.26216  42.64960 16.23453 1.000 22.23303 ? 38  TYR A CD2 1 
ATOM   266  C CE1 . TYR A 1 38  ? -5.25035  44.06837 14.07317 1.000 24.39477 ? 38  TYR A CE1 1 
ATOM   267  C CE2 . TYR A 1 38  ? -3.40270  43.08651 15.24018 1.000 26.11876 ? 38  TYR A CE2 1 
ATOM   268  C CZ  . TYR A 1 38  ? -3.90190  43.81001 14.16598 1.000 25.97590 ? 38  TYR A CZ  1 
ATOM   269  O OH  . TYR A 1 38  ? -3.03818  44.22146 13.17844 1.000 25.67010 ? 38  TYR A OH  1 
ATOM   270  N N   . VAL A 1 39  ? -6.76763  39.27526 17.91444 1.000 21.91500 ? 39  VAL A N   1 
ATOM   271  C CA  . VAL A 1 39  ? -6.76189  38.23818 18.93774 1.000 21.61342 ? 39  VAL A CA  1 
ATOM   272  C C   . VAL A 1 39  ? -5.35419  38.11838 19.49602 1.000 20.58571 ? 39  VAL A C   1 
ATOM   273  O O   . VAL A 1 39  ? -4.38476  38.08642 18.73049 1.000 22.63691 ? 39  VAL A O   1 
ATOM   274  C CB  . VAL A 1 39  ? -7.21207  36.87284 18.37536 1.000 21.19533 ? 39  VAL A CB  1 
ATOM   275  C CG1 . VAL A 1 39  ? -7.11251  35.79513 19.46684 1.000 23.55451 ? 39  VAL A CG1 1 
ATOM   276  C CG2 . VAL A 1 39  ? -8.63238  36.96155 17.80023 1.000 23.77378 ? 39  VAL A CG2 1 
ATOM   277  N N   . VAL A 1 40  ? -5.24705  38.05398 20.82077 1.000 21.07177 ? 40  VAL A N   1 
ATOM   278  C CA  . VAL A 1 40  ? -4.03932  37.60946 21.50759 1.000 20.61779 ? 40  VAL A CA  1 
ATOM   279  C C   . VAL A 1 40  ? -4.34176  36.21576 22.03416 1.000 20.43103 ? 40  VAL A C   1 
ATOM   280  O O   . VAL A 1 40  ? -5.19318  36.05050 22.91541 1.000 22.10751 ? 40  VAL A O   1 
ATOM   281  C CB  . VAL A 1 40  ? -3.63690  38.54816 22.65260 1.000 20.99368 ? 40  VAL A CB  1 
ATOM   282  C CG1 . VAL A 1 40  ? -2.52721  37.88610 23.47794 1.000 22.32503 ? 40  VAL A CG1 1 
ATOM   283  C CG2 . VAL A 1 40  ? -3.16611  39.88856 22.10634 1.000 21.50651 ? 40  VAL A CG2 1 
ATOM   284  N N   . PHE A 1 41  ? -3.66040  35.21420 21.49010 1.000 23.21452 ? 41  PHE A N   1 
ATOM   285  C CA  . PHE A 1 41  ? -3.84800  33.81639 21.86607 1.000 21.47612 ? 41  PHE A CA  1 
ATOM   286  C C   . PHE A 1 41  ? -2.57192  33.36249 22.56082 1.000 19.25772 ? 41  PHE A C   1 
ATOM   287  O O   . PHE A 1 41  ? -1.49856  33.36730 21.94801 1.000 22.51976 ? 41  PHE A O   1 
ATOM   288  C CB  . PHE A 1 41  ? -4.14354  32.98035 20.61493 1.000 21.86698 ? 41  PHE A CB  1 
ATOM   289  C CG  . PHE A 1 41  ? -4.36891  31.51268 20.87155 1.000 24.99208 ? 41  PHE A CG  1 
ATOM   290  C CD1 . PHE A 1 41  ? -5.18894  31.08561 21.90553 1.000 23.78856 ? 41  PHE A CD1 1 
ATOM   291  C CD2 . PHE A 1 41  ? -3.78767  30.57118 20.03945 1.000 25.51352 ? 41  PHE A CD2 1 
ATOM   292  C CE1 . PHE A 1 41  ? -5.40856  29.71878 22.12721 1.000 25.02783 ? 41  PHE A CE1 1 
ATOM   293  C CE2 . PHE A 1 41  ? -4.00361  29.20919 20.24986 1.000 24.26973 ? 41  PHE A CE2 1 
ATOM   294  C CZ  . PHE A 1 41  ? -4.80963  28.79306 21.29305 1.000 22.77208 ? 41  PHE A CZ  1 
ATOM   295  N N   . PHE A 1 42  ? -2.67195  32.99757 23.83629 1.000 20.61944 ? 42  PHE A N   1 
ATOM   296  C CA  . PHE A 1 42  ? -1.47067  32.61114 24.56965 1.000 19.92074 ? 42  PHE A CA  1 
ATOM   297  C C   . PHE A 1 42  ? -1.64217  31.25209 25.23175 1.000 23.02147 ? 42  PHE A C   1 
ATOM   298  O O   . PHE A 1 42  ? -2.70586  30.93390 25.77009 1.000 22.20481 ? 42  PHE A O   1 
ATOM   299  C CB  . PHE A 1 42  ? -1.05073  33.68504 25.61923 1.000 22.10551 ? 42  PHE A CB  1 
ATOM   300  C CG  . PHE A 1 42  ? -1.95152  33.78083 26.84152 1.000 21.46943 ? 42  PHE A CG  1 
ATOM   301  C CD1 . PHE A 1 42  ? -1.63691  33.08717 28.00620 1.000 23.24087 ? 42  PHE A CD1 1 
ATOM   302  C CD2 . PHE A 1 42  ? -3.07587  34.60600 26.84066 1.000 19.56083 ? 42  PHE A CD2 1 
ATOM   303  C CE1 . PHE A 1 42  ? -2.43386  33.17834 29.14280 1.000 25.18676 ? 42  PHE A CE1 1 
ATOM   304  C CE2 . PHE A 1 42  ? -3.88614  34.70721 27.97522 1.000 21.79660 ? 42  PHE A CE2 1 
ATOM   305  C CZ  . PHE A 1 42  ? -3.56892  34.00074 29.12974 1.000 24.65270 ? 42  PHE A CZ  1 
ATOM   306  N N   . PHE A 1 43  ? -0.56576  30.47131 25.18782 1.000 22.15747 ? 43  PHE A N   1 
ATOM   307  C CA  . PHE A 1 43  ? -0.46935  29.17317 25.84300 1.000 23.55612 ? 43  PHE A CA  1 
ATOM   308  C C   . PHE A 1 43  ? 0.24474   29.33533 27.17174 1.000 22.12235 ? 43  PHE A C   1 
ATOM   309  O O   . PHE A 1 43  ? 1.17280   30.13821 27.28300 1.000 24.81795 ? 43  PHE A O   1 
ATOM   310  C CB  . PHE A 1 43  ? 0.34068   28.19191 24.99717 1.000 21.88383 ? 43  PHE A CB  1 
ATOM   311  C CG  . PHE A 1 43  ? -0.29139  27.83045 23.69887 1.000 24.70406 ? 43  PHE A CG  1 
ATOM   312  C CD1 . PHE A 1 43  ? -0.19059  28.67778 22.60527 1.000 24.45490 ? 43  PHE A CD1 1 
ATOM   313  C CD2 . PHE A 1 43  ? -0.95177  26.62020 23.55381 1.000 27.49172 ? 43  PHE A CD2 1 
ATOM   314  C CE1 . PHE A 1 43  ? -0.75975  28.34415 21.39543 1.000 27.24556 ? 43  PHE A CE1 1 
ATOM   315  C CE2 . PHE A 1 43  ? -1.52715  26.27392 22.34601 1.000 25.94183 ? 43  PHE A CE2 1 
ATOM   316  C CZ  . PHE A 1 43  ? -1.42945  27.12133 21.26662 1.000 27.88194 ? 43  PHE A CZ  1 
ATOM   317  N N   . TYR A 1 44  ? -0.15774  28.55506 28.16302 1.000 22.12608 ? 44  TYR A N   1 
ATOM   318  C CA  . TYR A 1 44  ? 0.62430   28.41349 29.38103 1.000 22.01740 ? 44  TYR A CA  1 
ATOM   319  C C   . TYR A 1 44  ? 0.74268   26.92016 29.67371 1.000 22.14079 ? 44  TYR A C   1 
ATOM   320  O O   . TYR A 1 44  ? -0.07675  26.13227 29.20168 1.000 24.40002 ? 44  TYR A O   1 
ATOM   321  C CB  . TYR A 1 44  ? -0.00056  29.15780 30.57353 1.000 22.19011 ? 44  TYR A CB  1 
ATOM   322  C CG  . TYR A 1 44  ? -1.36967  28.67446 30.98301 1.000 25.11120 ? 44  TYR A CG  1 
ATOM   323  C CD1 . TYR A 1 44  ? -2.50636  29.12559 30.32309 1.000 24.51477 ? 44  TYR A CD1 1 
ATOM   324  C CD2 . TYR A 1 44  ? -1.52553  27.75852 32.02247 1.000 23.52841 ? 44  TYR A CD2 1 
ATOM   325  C CE1 . TYR A 1 44  ? -3.75714  28.68930 30.68151 1.000 24.67898 ? 44  TYR A CE1 1 
ATOM   326  C CE2 . TYR A 1 44  ? -2.78544  27.30971 32.39670 1.000 22.53782 ? 44  TYR A CE2 1 
ATOM   327  C CZ  . TYR A 1 44  ? -3.89683  27.78175 31.71676 1.000 23.31120 ? 44  TYR A CZ  1 
ATOM   328  O OH  . TYR A 1 44  ? -5.15864  27.36139 32.05667 1.000 24.43630 ? 44  TYR A OH  1 
ATOM   329  N N   . PRO A 1 45  ? 1.76883   26.50413 30.41270 1.000 23.02706 ? 45  PRO A N   1 
ATOM   330  C CA  . PRO A 1 45  ? 2.06367   25.05670 30.46293 1.000 22.78831 ? 45  PRO A CA  1 
ATOM   331  C C   . PRO A 1 45  ? 1.03666   24.22709 31.22902 1.000 25.79743 ? 45  PRO A C   1 
ATOM   332  O O   . PRO A 1 45  ? 0.46566   23.28890 30.65140 1.000 25.48409 ? 45  PRO A O   1 
ATOM   333  C CB  . PRO A 1 45  ? 3.45390   25.00585 31.11697 1.000 22.58743 ? 45  PRO A CB  1 
ATOM   334  C CG  . PRO A 1 45  ? 4.05837   26.38588 30.83013 1.000 25.42723 ? 45  PRO A CG  1 
ATOM   335  C CD  . PRO A 1 45  ? 2.87865   27.31185 30.94538 1.000 23.14749 ? 45  PRO A CD  1 
ATOM   336  N N   . LEU A 1 46  ? 0.77574   24.53570 32.50211 1.000 24.59008 ? 46  LEU A N   1 
ATOM   337  C CA  . LEU A 1 46  ? -0.12604  23.71487 33.30336 1.000 25.83778 ? 46  LEU A CA  1 
ATOM   338  C C   . LEU A 1 46  ? -0.90750  24.57307 34.28863 1.000 26.06221 ? 46  LEU A C   1 
ATOM   339  O O   . LEU A 1 46  ? -0.44981  25.64363 34.70210 1.000 26.17648 ? 46  LEU A O   1 
ATOM   340  C CB  . LEU A 1 46  ? 0.64018   22.63781 34.08629 1.000 26.32270 ? 46  LEU A CB  1 
ATOM   341  C CG  . LEU A 1 46  ? 1.23017   21.49342 33.27453 1.000 29.97528 ? 46  LEU A CG  1 
ATOM   342  C CD1 . LEU A 1 46  ? 2.22831   20.72198 34.13215 1.000 27.75261 ? 46  LEU A CD1 1 
ATOM   343  C CD2 . LEU A 1 46  ? 0.12825   20.59038 32.74458 1.000 29.76989 ? 46  LEU A CD2 1 
ATOM   344  N N   . ASP A 1 47  ? -2.08108  24.07048 34.68055 1.000 24.79802 ? 47  ASP A N   1 
ATOM   345  C CA  . ASP A 1 47  ? -2.85915  24.64278 35.77211 1.000 25.99297 ? 47  ASP A CA  1 
ATOM   346  C C   . ASP A 1 47  ? -2.20376  24.36372 37.12766 1.000 26.78334 ? 47  ASP A C   1 
ATOM   347  O O   . ASP A 1 47  ? -1.41813  23.41929 37.29167 1.000 27.52177 ? 47  ASP A O   1 
ATOM   348  C CB  . ASP A 1 47  ? -4.28146  24.06611 35.80574 1.000 27.09053 ? 47  ASP A CB  1 
ATOM   349  C CG  . ASP A 1 47  ? -5.15057  24.53379 34.64520 1.000 27.01759 ? 47  ASP A CG  1 
ATOM   350  O OD1 . ASP A 1 47  ? -4.80071  25.53418 33.99333 1.000 27.82986 ? 47  ASP A OD1 1 
ATOM   351  O OD2 . ASP A 1 47  ? -6.19609  23.88588 34.38837 1.000 25.91363 ? 47  ASP A OD2 1 
ATOM   352  N N   . PHE A 1 48  ? -2.58684  25.18654 38.11545 1.000 25.87370 ? 48  PHE A N   1 
ATOM   353  C CA  . PHE A 1 48  ? -2.18577  25.04439 39.52119 1.000 26.84500 ? 48  PHE A CA  1 
ATOM   354  C C   . PHE A 1 48  ? -0.67064  25.15638 39.68380 1.000 30.20464 ? 48  PHE A C   1 
ATOM   355  O O   . PHE A 1 48  ? -0.05221  24.44932 40.48102 1.000 31.23706 ? 48  PHE A O   1 
ATOM   356  C CB  . PHE A 1 48  ? -2.72956  23.74167 40.12021 1.000 25.64083 ? 48  PHE A CB  1 
ATOM   357  C CG  . PHE A 1 48  ? -4.23801  23.72886 40.26423 1.000 27.38491 ? 48  PHE A CG  1 
ATOM   358  C CD1 . PHE A 1 48  ? -4.84887  24.35253 41.34153 1.000 29.72472 ? 48  PHE A CD1 1 
ATOM   359  C CD2 . PHE A 1 48  ? -5.03768  23.11578 39.31170 1.000 29.60010 ? 48  PHE A CD2 1 
ATOM   360  C CE1 . PHE A 1 48  ? -6.23307  24.35287 41.47586 1.000 30.45044 ? 48  PHE A CE1 1 
ATOM   361  C CE2 . PHE A 1 48  ? -6.42457  23.10879 39.43820 1.000 27.60157 ? 48  PHE A CE2 1 
ATOM   362  C CZ  . PHE A 1 48  ? -7.01989  23.72488 40.52308 1.000 28.16839 ? 48  PHE A CZ  1 
ATOM   363  N N   . THR A 1 49  ? -0.07417  26.07201 38.92820 1.000 27.92705 ? 49  THR A N   1 
ATOM   364  C CA  . THR A 1 49  ? 1.35436   26.32609 38.89400 1.000 28.78945 ? 49  THR A CA  1 
ATOM   365  C C   . THR A 1 49  ? 1.63675   27.69895 39.50747 1.000 25.91811 ? 49  THR A C   1 
ATOM   366  O O   . THR A 1 49  ? 0.73653   28.36145 40.04095 1.000 26.02668 ? 49  THR A O   1 
ATOM   367  C CB  . THR A 1 49  ? 1.84756   26.22943 37.45517 1.000 26.75733 ? 49  THR A CB  1 
ATOM   368  O OG1 . THR A 1 49  ? 0.97670   26.99516 36.60764 1.000 27.15950 ? 49  THR A OG1 1 
ATOM   369  C CG2 . THR A 1 49  ? 1.86396   24.76154 36.97988 1.000 25.84063 ? 49  THR A CG2 1 
ATOM   370  N N   . PHE A 1 50  ? 2.89512   28.14743 39.44170 1.000 27.51839 ? 50  PHE A N   1 
ATOM   371  C CA  . PHE A 1 50  ? 3.21554   29.37787 40.14929 1.000 26.64875 ? 50  PHE A CA  1 
ATOM   372  C C   . PHE A 1 50  ? 3.87630   30.47611 39.32514 1.000 27.63183 ? 50  PHE A C   1 
ATOM   373  O O   . PHE A 1 50  ? 4.09943   31.56165 39.86790 1.000 30.57261 ? 50  PHE A O   1 
ATOM   374  C CB  . PHE A 1 50  ? 4.04117   29.08147 41.41948 1.000 28.60974 ? 50  PHE A CB  1 
ATOM   375  C CG  . PHE A 1 50  ? 5.45219   28.62333 41.19150 0.649 32.38240 ? 50  PHE A CG  1 
ATOM   376  C CD1 . PHE A 1 50  ? 6.49477   29.53990 41.16254 1.000 40.99192 ? 50  PHE A CD1 1 
ATOM   377  C CD2 . PHE A 1 50  ? 5.75036   27.27048 41.12048 0.438 34.96500 ? 50  PHE A CD2 1 
ATOM   378  C CE1 . PHE A 1 50  ? 7.80598   29.11327 41.00689 1.000 42.13216 ? 50  PHE A CE1 1 
ATOM   379  C CE2 . PHE A 1 50  ? 7.05738   26.83768 40.96460 1.000 43.93402 ? 50  PHE A CE2 1 
ATOM   380  C CZ  . PHE A 1 50  ? 8.08548   27.76471 40.91056 1.000 41.03500 ? 50  PHE A CZ  1 
ATOM   381  N N   . VAL A 1 51  ? 4.12193   30.28137 38.03438 1.000 23.75305 ? 51  VAL A N   1 
ATOM   382  C CA  . VAL A 1 51  ? 4.38423   31.41612 37.15132 1.000 26.03197 ? 51  VAL A CA  1 
ATOM   383  C C   . VAL A 1 51  ? 3.16131   31.75569 36.30693 1.000 24.64030 ? 51  VAL A C   1 
ATOM   384  O O   . VAL A 1 51  ? 2.78191   32.92319 36.20449 1.000 24.62248 ? 51  VAL A O   1 
ATOM   385  C CB  . VAL A 1 51  ? 5.61881   31.16619 36.26193 1.000 27.70432 ? 51  VAL A CB  1 
ATOM   386  C CG1 . VAL A 1 51  ? 5.75589   32.29939 35.22430 1.000 26.76851 ? 51  VAL A CG1 1 
ATOM   387  C CG2 . VAL A 1 51  ? 6.85946   31.06165 37.11650 1.000 28.86720 ? 51  VAL A CG2 1 
ATOM   388  N N   . SER A 1 52  ? 2.51392   30.73396 35.74745 1.000 23.45229 ? 52  SER A N   1 
ATOM   389  C CA  . SER A 1 52  ? 1.31832   30.96271 34.93172 1.000 24.34309 ? 52  SER A CA  1 
ATOM   390  C C   . SER A 1 52  ? 0.24840   31.81652 35.59396 1.000 25.14931 ? 52  SER A C   1 
ATOM   391  O O   . SER A 1 52  ? -0.33865  32.66204 34.88445 1.000 24.55565 ? 52  SER A O   1 
ATOM   392  C CB  . SER A 1 52  ? 0.70735   29.62087 34.50721 1.000 24.99269 ? 52  SER A CB  1 
ATOM   393  O OG  . SER A 1 52  ? 1.62105   28.92164 33.69313 1.000 25.47713 ? 52  SER A OG  1 
ATOM   394  N N   . PRO A 1 53  ? -0.11131  31.65597 36.86968 1.000 23.84940 ? 53  PRO A N   1 
ATOM   395  C CA  . PRO A 1 53  ? -1.21798  32.46693 37.40583 1.000 23.99978 ? 53  PRO A CA  1 
ATOM   396  C C   . PRO A 1 53  ? -0.94597  33.96315 37.36843 1.000 23.78173 ? 53  PRO A C   1 
ATOM   397  O O   . PRO A 1 53  ? -1.87663  34.74729 37.13701 1.000 23.81933 ? 53  PRO A O   1 
ATOM   398  C CB  . PRO A 1 53  ? -1.38183  31.94974 38.84598 1.000 25.14490 ? 53  PRO A CB  1 
ATOM   399  C CG  . PRO A 1 53  ? -0.04271  31.37151 39.17673 1.000 25.49892 ? 53  PRO A CG  1 
ATOM   400  C CD  . PRO A 1 53  ? 0.39251   30.72480 37.89882 1.000 25.77249 ? 53  PRO A CD  1 
ATOM   401  N N   . THR A 1 54  ? 0.30094   34.38875 37.59218 1.000 23.93499 ? 54  THR A N   1 
ATOM   402  C CA  . THR A 1 54  ? 0.61813   35.81199 37.47647 1.000 25.74444 ? 54  THR A CA  1 
ATOM   403  C C   . THR A 1 54  ? 0.23923   36.34564 36.09692 1.000 25.17475 ? 54  THR A C   1 
ATOM   404  O O   . THR A 1 54  ? -0.36024  37.42530 35.98275 1.000 25.27779 ? 54  THR A O   1 
ATOM   405  C CB  . THR A 1 54  ? 2.10582   36.04353 37.75989 1.000 27.63443 ? 54  THR A CB  1 
ATOM   406  O OG1 . THR A 1 54  ? 2.40603   35.64348 39.10684 1.000 28.53400 ? 54  THR A OG1 1 
ATOM   407  C CG2 . THR A 1 54  ? 2.45931   37.52261 37.59888 1.000 29.56460 ? 54  THR A CG2 1 
ATOM   408  N N   . GLU A 1 55  ? 0.55764   35.58554 35.04179 1.000 25.17318 ? 55  GLU A N   1 
ATOM   409  C CA  . GLU A 1 55  ? 0.23748   35.99692 33.67423 1.000 25.30916 ? 55  GLU A CA  1 
ATOM   410  C C   . GLU A 1 55  ? -1.26442  35.99874 33.43269 1.000 25.00990 ? 55  GLU A C   1 
ATOM   411  O O   . GLU A 1 55  ? -1.81985  36.96331 32.88840 1.000 23.61316 ? 55  GLU A O   1 
ATOM   412  C CB  . GLU A 1 55  ? 0.87259   35.04354 32.66175 1.000 27.95245 ? 55  GLU A CB  1 
ATOM   413  C CG  . GLU A 1 55  ? 2.31373   34.73079 32.83539 1.000 32.29072 ? 55  GLU A CG  1 
ATOM   414  C CD  . GLU A 1 55  ? 2.80348   33.91473 31.66373 1.000 25.84218 ? 55  GLU A CD  1 
ATOM   415  O OE1 . GLU A 1 55  ? 2.42573   32.72102 31.55749 1.000 25.89395 ? 55  GLU A OE1 1 
ATOM   416  O OE2 . GLU A 1 55  ? 3.52407   34.47856 30.82758 1.000 27.81132 ? 55  GLU A OE2 1 
ATOM   417  N N   . ILE A 1 56  ? -1.91755  34.87891 33.74778 1.000 23.22625 ? 56  ILE A N   1 
ATOM   418  C CA  . ILE A 1 56  ? -3.34652  34.73939 33.47633 1.000 22.77934 ? 56  ILE A CA  1 
ATOM   419  C C   . ILE A 1 56  ? -4.12714  35.83824 34.18192 1.000 22.30346 ? 56  ILE A C   1 
ATOM   420  O O   . ILE A 1 56  ? -4.98445  36.50222 33.58263 1.000 23.68254 ? 56  ILE A O   1 
ATOM   421  C CB  . ILE A 1 56  ? -3.84009  33.35138 33.91091 1.000 22.04296 ? 56  ILE A CB  1 
ATOM   422  C CG1 . ILE A 1 56  ? -3.14923  32.25142 33.09493 1.000 24.94173 ? 56  ILE A CG1 1 
ATOM   423  C CG2 . ILE A 1 56  ? -5.34098  33.27248 33.74416 1.000 24.20766 ? 56  ILE A CG2 1 
ATOM   424  C CD1 . ILE A 1 56  ? -3.26413  30.86681 33.72566 1.000 25.14483 ? 56  ILE A CD1 1 
ATOM   425  N N   . ILE A 1 57  ? -3.83694  36.04047 35.46926 1.000 23.08565 ? 57  ILE A N   1 
ATOM   426  C CA  . ILE A 1 57  ? -4.53709  37.05533 36.25670 1.000 21.74984 ? 57  ILE A CA  1 
ATOM   427  C C   . ILE A 1 57  ? -4.28697  38.44437 35.68002 1.000 23.82364 ? 57  ILE A C   1 
ATOM   428  O O   . ILE A 1 57  ? -5.19010  39.29431 35.65233 1.000 24.69389 ? 57  ILE A O   1 
ATOM   429  C CB  . ILE A 1 57  ? -4.11569  36.94865 37.73752 1.000 21.44074 ? 57  ILE A CB  1 
ATOM   430  C CG1 . ILE A 1 57  ? -4.62826  35.62465 38.33134 1.000 26.40062 ? 57  ILE A CG1 1 
ATOM   431  C CG2 . ILE A 1 57  ? -4.62155  38.15530 38.54566 1.000 25.43446 ? 57  ILE A CG2 1 
ATOM   432  C CD1 . ILE A 1 57  ? -3.96783  35.21408 39.64741 1.000 27.57494 ? 57  ILE A CD1 1 
ATOM   433  N N   . ALA A 1 58  ? -3.06506  38.69824 35.19890 1.000 23.06830 ? 58  ALA A N   1 
ATOM   434  C CA  . ALA A 1 58  ? -2.76139  40.00777 34.62281 1.000 23.10726 ? 58  ALA A CA  1 
ATOM   435  C C   . ALA A 1 58  ? -3.56316  40.24822 33.34492 1.000 24.31952 ? 58  ALA A C   1 
ATOM   436  O O   . ALA A 1 58  ? -4.16757  41.31466 33.16488 1.000 23.35311 ? 58  ALA A O   1 
ATOM   437  C CB  . ALA A 1 58  ? -1.25731  40.13388 34.35487 1.000 25.69234 ? 58  ALA A CB  1 
ATOM   438  N N   . PHE A 1 59  ? -3.58874  39.26327 32.43989 1.000 22.40089 ? 59  PHE A N   1 
ATOM   439  C CA  . PHE A 1 59  ? -4.37636  39.42930 31.22117 1.000 21.36260 ? 59  PHE A CA  1 
ATOM   440  C C   . PHE A 1 59  ? -5.85632  39.56988 31.54442 1.000 24.01335 ? 59  PHE A C   1 
ATOM   441  O O   . PHE A 1 59  ? -6.56175  40.37320 30.92186 1.000 25.52413 ? 59  PHE A O   1 
ATOM   442  C CB  . PHE A 1 59  ? -4.14049  38.25273 30.26579 1.000 21.92950 ? 59  PHE A CB  1 
ATOM   443  C CG  . PHE A 1 59  ? -2.90200  38.39969 29.43014 1.000 20.62254 ? 59  PHE A CG  1 
ATOM   444  C CD1 . PHE A 1 59  ? -2.86617  39.30487 28.38576 1.000 20.39774 ? 59  PHE A CD1 1 
ATOM   445  C CD2 . PHE A 1 59  ? -1.76506  37.65229 29.70562 1.000 25.65766 ? 59  PHE A CD2 1 
ATOM   446  C CE1 . PHE A 1 59  ? -1.72471  39.47043 27.61629 1.000 24.56166 ? 59  PHE A CE1 1 
ATOM   447  C CE2 . PHE A 1 59  ? -0.62000  37.79611 28.93693 1.000 26.95449 ? 59  PHE A CE2 1 
ATOM   448  C CZ  . PHE A 1 59  ? -0.59498  38.71575 27.88886 1.000 25.63458 ? 59  PHE A CZ  1 
ATOM   449  N N   . SER A 1 60  ? -6.34306  38.80289 32.52264 1.000 22.90318 ? 60  SER A N   1 
ATOM   450  C CA  . SER A 1 60  ? -7.74281  38.90655 32.92284 1.000 23.35771 ? 60  SER A CA  1 
ATOM   451  C C   . SER A 1 60  ? -8.03068  40.26219 33.55778 1.000 25.69346 ? 60  SER A C   1 
ATOM   452  O O   . SER A 1 60  ? -8.99427  40.94360 33.18170 1.000 25.26695 ? 60  SER A O   1 
ATOM   453  C CB  . SER A 1 60  ? -8.09432  37.77968 33.89418 1.000 23.95322 ? 60  SER A CB  1 
ATOM   454  O OG  . SER A 1 60  ? -9.42748  37.92033 34.36236 1.000 23.93433 ? 60  SER A OG  1 
ATOM   455  N N   . ASP A 1 61  ? -7.19815  40.66478 34.52467 1.000 24.04155 ? 61  ASP A N   1 
ATOM   456  C CA  . ASP A 1 61  ? -7.40525  41.93631 35.21893 1.000 25.14679 ? 61  ASP A CA  1 
ATOM   457  C C   . ASP A 1 61  ? -7.45340  43.10199 34.24069 1.000 26.19871 ? 61  ASP A C   1 
ATOM   458  O O   . ASP A 1 61  ? -8.19616  44.06964 34.45093 1.000 26.03927 ? 61  ASP A O   1 
ATOM   459  C CB  . ASP A 1 61  ? -6.28686  42.18232 36.23212 1.000 25.52153 ? 61  ASP A CB  1 
ATOM   460  C CG  . ASP A 1 61  ? -6.46648  41.41501 37.53938 1.000 27.14435 ? 61  ASP A CG  1 
ATOM   461  O OD1 . ASP A 1 61  ? -7.51083  40.75500 37.75077 1.000 28.42561 ? 61  ASP A OD1 1 
ATOM   462  O OD2 . ASP A 1 61  ? -5.53137  41.48954 38.36886 1.000 28.49051 ? 61  ASP A OD2 1 
ATOM   463  N N   . ARG A 1 62  ? -6.64616  43.04531 33.18349 1.000 23.53682 ? 62  ARG A N   1 
ATOM   464  C CA  . ARG A 1 62  ? -6.50504  44.16045 32.25874 1.000 23.88232 ? 62  ARG A CA  1 
ATOM   465  C C   . ARG A 1 62  ? -7.23434  43.91464 30.94247 1.000 23.23989 ? 62  ARG A C   1 
ATOM   466  O O   . ARG A 1 62  ? -6.92881  44.56227 29.93743 1.000 25.57529 ? 62  ARG A O   1 
ATOM   467  C CB  . ARG A 1 62  ? -5.01843  44.45788 32.03719 1.000 24.89814 ? 62  ARG A CB  1 
ATOM   468  C CG  . ARG A 1 62  ? -4.31081  44.85836 33.34244 1.000 25.49329 ? 62  ARG A CG  1 
ATOM   469  C CD  . ARG A 1 62  ? -2.82725  45.11503 33.15891 1.000 25.63915 ? 62  ARG A CD  1 
ATOM   470  N NE  . ARG A 1 62  ? -2.56358  46.24049 32.26451 1.000 23.08072 ? 62  ARG A NE  1 
ATOM   471  C CZ  . ARG A 1 62  ? -1.34081  46.61778 31.89471 1.000 26.68730 ? 62  ARG A CZ  1 
ATOM   472  N NH1 . ARG A 1 62  ? -0.28238  45.93887 32.33193 1.000 25.70154 ? 62  ARG A NH1 1 
ATOM   473  N NH2 . ARG A 1 62  ? -1.17533  47.64904 31.07341 1.000 26.81940 ? 62  ARG A NH2 1 
ATOM   474  N N   . ALA A 1 63  ? -8.22015  43.00686 30.93636 1.000 24.61104 ? 63  ALA A N   1 
ATOM   475  C CA  . ALA A 1 63  ? -8.91279  42.69054 29.69121 1.000 25.96126 ? 63  ALA A CA  1 
ATOM   476  C C   . ALA A 1 63  ? -9.57445  43.92081 29.07304 1.000 26.06990 ? 63  ALA A C   1 
ATOM   477  O O   . ALA A 1 63  ? -9.68988  44.00545 27.84503 1.000 28.00031 ? 63  ALA A O   1 
ATOM   478  C CB  . ALA A 1 63  ? -9.95237  41.59286 29.92262 1.000 28.63202 ? 63  ALA A CB  1 
ATOM   479  N N   . GLU A 1 64  ? -9.98750  44.89265 29.89352 1.000 26.81562 ? 64  GLU A N   1 
ATOM   480  C CA  . GLU A 1 64  ? -10.64029 46.07461 29.33060 1.000 31.24229 ? 64  GLU A CA  1 
ATOM   481  C C   . GLU A 1 64  ? -9.68947  46.88505 28.45434 1.000 28.99964 ? 64  GLU A C   1 
ATOM   482  O O   . GLU A 1 64  ? -10.12872 47.51548 27.48661 1.000 28.27302 ? 64  GLU A O   1 
ATOM   483  C CB  . GLU A 1 64  ? -11.21314 46.94456 30.44926 1.000 35.13880 ? 64  GLU A CB  1 
ATOM   484  C CG  . GLU A 1 64  ? -12.14759 48.05760 29.96890 1.000 43.81248 ? 64  GLU A CG  1 
ATOM   485  C CD  . GLU A 1 64  ? -13.33249 47.54571 29.15982 1.000 47.56067 ? 64  GLU A CD  1 
ATOM   486  O OE1 . GLU A 1 64  ? -13.90391 46.49239 29.52318 1.000 48.59799 ? 64  GLU A OE1 1 
ATOM   487  O OE2 . GLU A 1 64  ? -13.69105 48.20621 28.15690 1.000 53.06806 ? 64  GLU A OE2 1 
ATOM   488  N N   . GLU A 1 65  ? -8.38993  46.87758 28.76121 1.000 26.59044 ? 65  GLU A N   1 
ATOM   489  C CA  . GLU A 1 65  ? -7.44442  47.56596 27.88968 1.000 25.58805 ? 65  GLU A CA  1 
ATOM   490  C C   . GLU A 1 65  ? -7.37569  46.91081 26.52179 1.000 25.51632 ? 65  GLU A C   1 
ATOM   491  O O   . GLU A 1 65  ? -7.18517  47.59556 25.51385 1.000 24.41247 ? 65  GLU A O   1 
ATOM   492  C CB  . GLU A 1 65  ? -6.06421  47.61615 28.54253 1.000 28.27416 ? 65  GLU A CB  1 
ATOM   493  C CG  . GLU A 1 65  ? -6.03269  48.52294 29.77158 1.000 29.63285 ? 65  GLU A CG  1 
ATOM   494  C CD  . GLU A 1 65  ? -4.75183  48.40460 30.58298 1.000 27.16794 ? 65  GLU A CD  1 
ATOM   495  O OE1 . GLU A 1 65  ? -3.68596  48.81566 30.08175 1.000 29.25322 ? 65  GLU A OE1 1 
ATOM   496  O OE2 . GLU A 1 65  ? -4.81613  47.90569 31.72481 1.000 28.14728 ? 65  GLU A OE2 1 
ATOM   497  N N   . PHE A 1 66  ? -7.52519  45.58485 26.46142 1.000 24.01626 ? 66  PHE A N   1 
ATOM   498  C CA  . PHE A 1 66  ? -7.58571  44.92927 25.16501 1.000 23.88941 ? 66  PHE A CA  1 
ATOM   499  C C   . PHE A 1 66  ? -8.91268  45.20141 24.47500 1.000 23.08661 ? 66  PHE A C   1 
ATOM   500  O O   . PHE A 1 66  ? -8.95203  45.38878 23.25319 1.000 25.05523 ? 66  PHE A O   1 
ATOM   501  C CB  . PHE A 1 66  ? -7.34396  43.43482 25.34219 1.000 23.31331 ? 66  PHE A CB  1 
ATOM   502  C CG  . PHE A 1 66  ? -5.92916  43.11743 25.73048 1.000 22.76255 ? 66  PHE A CG  1 
ATOM   503  C CD1 . PHE A 1 66  ? -4.95669  42.97715 24.75884 1.000 23.05241 ? 66  PHE A CD1 1 
ATOM   504  C CD2 . PHE A 1 66  ? -5.56828  43.00368 27.06181 1.000 24.50927 ? 66  PHE A CD2 1 
ATOM   505  C CE1 . PHE A 1 66  ? -3.63999  42.70640 25.11054 1.000 23.77238 ? 66  PHE A CE1 1 
ATOM   506  C CE2 . PHE A 1 66  ? -4.25125  42.74186 27.42079 1.000 23.14285 ? 66  PHE A CE2 1 
ATOM   507  C CZ  . PHE A 1 66  ? -3.29323  42.58671 26.44862 1.000 22.61851 ? 66  PHE A CZ  1 
ATOM   508  N N   . LYS A 1 67  ? -10.00014 45.25973 25.24470 1.000 24.70165 ? 67  LYS A N   1 
ATOM   509  C CA  . LYS A 1 67  ? -11.30008 45.56851 24.65383 1.000 29.24533 ? 67  LYS A CA  1 
ATOM   510  C C   . LYS A 1 67  ? -11.28754 46.94173 23.99025 1.000 28.95135 ? 67  LYS A C   1 
ATOM   511  O O   . LYS A 1 67  ? -11.88818 47.12883 22.92558 1.000 28.57517 ? 67  LYS A O   1 
ATOM   512  C CB  . LYS A 1 67  ? -12.39537 45.48995 25.71648 1.000 31.72293 ? 67  LYS A CB  1 
ATOM   513  C CG  . LYS A 1 67  ? -13.79802 45.76458 25.17582 1.000 41.88571 ? 67  LYS A CG  1 
ATOM   514  C CD  . LYS A 1 67  ? -14.87500 45.46269 26.21207 1.000 46.20914 ? 67  LYS A CD  1 
ATOM   515  C CE  . LYS A 1 67  ? -16.24827 45.90278 25.71180 1.000 52.71291 ? 67  LYS A CE  1 
ATOM   516  N NZ  . LYS A 1 67  ? -17.34810 45.40652 26.58659 1.000 58.08653 ? 67  LYS A NZ  1 
ATOM   517  N N   . LYS A 1 68  ? -10.57943 47.90475 24.58433 1.000 28.31252 ? 68  LYS A N   1 
ATOM   518  C CA  . LYS A 1 68  ? -10.47737 49.22957 23.97480 1.000 28.66288 ? 68  LYS A CA  1 
ATOM   519  C C   . LYS A 1 68  ? -9.74488  49.19123 22.64554 1.000 31.30004 ? 68  LYS A C   1 
ATOM   520  O O   . LYS A 1 68  ? -9.96625  50.06770 21.80158 1.000 29.62060 ? 68  LYS A O   1 
ATOM   521  C CB  . LYS A 1 68  ? -9.77565  50.19941 24.92723 1.000 31.43502 ? 68  LYS A CB  1 
ATOM   522  C CG  . LYS A 1 68  ? -10.48559 50.36089 26.25724 1.000 38.36901 ? 68  LYS A CG  1 
ATOM   523  C CD  . LYS A 1 68  ? -10.31932 51.76062 26.83341 1.000 46.16110 ? 68  LYS A CD  1 
ATOM   524  C CE  . LYS A 1 68  ? -11.35976 52.02899 27.92103 1.000 50.25594 ? 68  LYS A CE  1 
ATOM   525  N NZ  . LYS A 1 68  ? -11.12652 51.22358 29.15302 1.000 48.83144 ? 68  LYS A NZ  1 
ATOM   526  N N   . LEU A 1 69  ? -8.87397  48.20259 22.44540 1.000 25.87781 ? 69  LEU A N   1 
ATOM   527  C CA  . LEU A 1 69  ? -8.20677  47.98087 21.17681 1.000 26.23916 ? 69  LEU A CA  1 
ATOM   528  C C   . LEU A 1 69  ? -8.97177  47.01313 20.27888 1.000 25.55234 ? 69  LEU A C   1 
ATOM   529  O O   . LEU A 1 69  ? -8.41589  46.54518 19.28386 1.000 27.82877 ? 69  LEU A O   1 
ATOM   530  C CB  . LEU A 1 69  ? -6.78423  47.46190 21.42002 1.000 25.91472 ? 69  LEU A CB  1 
ATOM   531  C CG  . LEU A 1 69  ? -5.84838  48.41011 22.17771 1.000 26.45743 ? 69  LEU A CG  1 
ATOM   532  C CD1 . LEU A 1 69  ? -4.48339  47.74241 22.39784 1.000 26.41462 ? 69  LEU A CD1 1 
ATOM   533  C CD2 . LEU A 1 69  ? -5.68667  49.72905 21.41333 1.000 28.41273 ? 69  LEU A CD2 1 
ATOM   534  N N   . ASN A 1 70  ? -10.23259 46.71686 20.59959 1.000 26.70350 ? 70  ASN A N   1 
ATOM   535  C CA  . ASN A 1 70  ? -11.02699 45.75353 19.82980 1.000 27.67016 ? 70  ASN A CA  1 
ATOM   536  C C   . ASN A 1 70  ? -10.27434 44.43075 19.69098 1.000 24.66677 ? 70  ASN A C   1 
ATOM   537  O O   . ASN A 1 70  ? -10.18830 43.84526 18.60836 1.000 27.51719 ? 70  ASN A O   1 
ATOM   538  C CB  . ASN A 1 70  ? -11.40863 46.31126 18.45308 1.000 31.60388 ? 70  ASN A CB  1 
ATOM   539  C CG  . ASN A 1 70  ? -12.35528 45.38852 17.67531 1.000 36.18316 ? 70  ASN A CG  1 
ATOM   540  O OD1 . ASN A 1 70  ? -13.34507 44.88963 18.21373 1.000 37.09591 ? 70  ASN A OD1 1 
ATOM   541  N ND2 . ASN A 1 70  ? -12.03758 45.15327 16.40465 1.000 36.78261 ? 70  ASN A ND2 1 
ATOM   542  N N   . CYS A 1 71  ? -9.70211  43.96864 20.79671 1.000 24.25476 ? 71  CYS A N   1 
ATOM   543  C CA  . CYS A 1 71  ? -8.83943  42.79294 20.76761 1.000 24.20318 ? 71  CYS A CA  1 
ATOM   544  C C   . CYS A 1 71  ? -9.30397  41.77098 21.80353 1.000 23.92411 ? 71  CYS A C   1 
ATOM   545  O O   . CYS A 1 71  ? -9.50620  42.11277 22.97477 1.000 24.48166 ? 71  CYS A O   1 
ATOM   546  C CB  . CYS A 1 71  ? -7.38384  43.21639 21.00820 1.000 21.57741 ? 71  CYS A CB  1 
ATOM   547  S SG  . CYS A 1 71  ? -6.19125  41.83543 21.09688 1.000 25.12874 ? 71  CYS A SG  1 
ATOM   548  N N   . GLN A 1 72  ? -9.49015  40.52147 21.36571 1.000 22.48342 ? 72  GLN A N   1 
ATOM   549  C CA  . GLN A 1 72  ? -9.91152  39.43985 22.24762 1.000 24.14185 ? 72  GLN A CA  1 
ATOM   550  C C   . GLN A 1 72  ? -8.68596  38.68676 22.75245 1.000 23.09583 ? 72  GLN A C   1 
ATOM   551  O O   . GLN A 1 72  ? -7.83078  38.30702 21.95487 1.000 27.28862 ? 72  GLN A O   1 
ATOM   552  C CB  . GLN A 1 72  ? -10.83811 38.47640 21.49504 1.000 24.18283 ? 72  GLN A CB  1 
ATOM   553  C CG  . GLN A 1 72  ? -11.19527 37.21877 22.28428 1.000 25.17976 ? 72  GLN A CG  1 
ATOM   554  C CD  . GLN A 1 72  ? -12.08683 37.53462 23.45593 1.000 28.59129 ? 72  GLN A CD  1 
ATOM   555  O OE1 . GLN A 1 72  ? -13.16095 38.13025 23.29532 1.000 31.28340 ? 72  GLN A OE1 1 
ATOM   556  N NE2 . GLN A 1 72  ? -11.64344 37.17545 24.64790 1.000 27.32783 ? 72  GLN A NE2 1 
ATOM   557  N N   . VAL A 1 73  ? -8.60363  38.47338 24.06644 1.000 21.72213 ? 73  VAL A N   1 
ATOM   558  C CA  . VAL A 1 73  ? -7.53475  37.67326 24.67312 1.000 21.49412 ? 73  VAL A CA  1 
ATOM   559  C C   . VAL A 1 73  ? -8.07080  36.27840 24.96877 1.000 21.33050 ? 73  VAL A C   1 
ATOM   560  O O   . VAL A 1 73  ? -9.16723  36.13757 25.51705 1.000 24.94612 ? 73  VAL A O   1 
ATOM   561  C CB  . VAL A 1 73  ? -7.01107  38.33070 25.96024 1.000 22.19230 ? 73  VAL A CB  1 
ATOM   562  C CG1 . VAL A 1 73  ? -5.95677  37.44895 26.62038 1.000 23.95595 ? 73  VAL A CG1 1 
ATOM   563  C CG2 . VAL A 1 73  ? -6.41742  39.70530 25.64536 1.000 22.21018 ? 73  VAL A CG2 1 
ATOM   564  N N   . ILE A 1 74  ? -7.29072  35.25093 24.62249 1.000 21.50676 ? 74  ILE A N   1 
ATOM   565  C CA  . ILE A 1 74  ? -7.65666  33.85157 24.86068 1.000 22.84955 ? 74  ILE A CA  1 
ATOM   566  C C   . ILE A 1 74  ? -6.43809  33.12398 25.40622 1.000 20.87851 ? 74  ILE A C   1 
ATOM   567  O O   . ILE A 1 74  ? -5.37239  33.15764 24.78425 1.000 22.05956 ? 74  ILE A O   1 
ATOM   568  C CB  . ILE A 1 74  ? -8.13433  33.14542 23.57630 1.000 21.36986 ? 74  ILE A CB  1 
ATOM   569  C CG1 . ILE A 1 74  ? -9.33369  33.86732 22.96587 1.000 23.17724 ? 74  ILE A CG1 1 
ATOM   570  C CG2 . ILE A 1 74  ? -8.48860  31.66303 23.87564 1.000 23.44883 ? 74  ILE A CG2 1 
ATOM   571  C CD1 . ILE A 1 74  ? -9.64896  33.39355 21.55203 1.000 26.98237 ? 74  ILE A CD1 1 
ATOM   572  N N   . GLY A 1 75  ? -6.59266  32.45372 26.55471 1.000 21.91811 ? 75  GLY A N   1 
ATOM   573  C CA  . GLY A 1 75  ? -5.54703  31.60846 27.09576 1.000 19.64556 ? 75  GLY A CA  1 
ATOM   574  C C   . GLY A 1 75  ? -5.82399  30.13301 26.82040 1.000 22.17586 ? 75  GLY A C   1 
ATOM   575  O O   . GLY A 1 75  ? -6.95511  29.75934 26.53584 1.000 23.99349 ? 75  GLY A O   1 
ATOM   576  N N   . ALA A 1 76  ? -4.77791  29.30525 26.92699 1.000 20.32847 ? 76  ALA A N   1 
ATOM   577  C CA  . ALA A 1 76  ? -4.89780  27.88005 26.61886 1.000 22.31549 ? 76  ALA A CA  1 
ATOM   578  C C   . ALA A 1 76  ? -3.83298  27.07450 27.35310 1.000 22.60213 ? 76  ALA A C   1 
ATOM   579  O O   . ALA A 1 76  ? -2.69847  27.52348 27.51982 1.000 22.16731 ? 76  ALA A O   1 
ATOM   580  C CB  . ALA A 1 76  ? -4.77420  27.63491 25.10977 1.000 22.96688 ? 76  ALA A CB  1 
ATOM   581  N N   . SER A 1 77  ? -4.20093  25.85545 27.75837 1.000 23.21988 ? 77  SER A N   1 
ATOM   582  C CA  . SER A 1 77  ? -3.20670  24.87659 28.17701 1.000 23.22481 ? 77  SER A CA  1 
ATOM   583  C C   . SER A 1 77  ? -3.74953  23.49924 27.86701 1.000 23.77874 ? 77  SER A C   1 
ATOM   584  O O   . SER A 1 77  ? -4.91948  23.33984 27.52103 1.000 23.71456 ? 77  SER A O   1 
ATOM   585  C CB  . SER A 1 77  ? -2.85043  24.97492 29.66068 1.000 24.04369 ? 77  SER A CB  1 
ATOM   586  O OG  . SER A 1 77  ? -3.69278  24.18473 30.46863 1.000 26.93787 ? 77  SER A OG  1 
ATOM   587  N N   . VAL A 1 78  ? -2.88183  22.49736 28.02746 1.000 23.24395 ? 78  VAL A N   1 
ATOM   588  C CA  . VAL A 1 78  ? -3.30088  21.11786 27.77168 1.000 23.79330 ? 78  VAL A CA  1 
ATOM   589  C C   . VAL A 1 78  ? -4.18641  20.52510 28.85656 1.000 26.28019 ? 78  VAL A C   1 
ATOM   590  O O   . VAL A 1 78  ? -4.72418  19.42252 28.65525 1.000 25.26181 ? 78  VAL A O   1 
ATOM   591  C CB  . VAL A 1 78  ? -2.07948  20.19543 27.59586 1.000 22.57231 ? 78  VAL A CB  1 
ATOM   592  C CG1 . VAL A 1 78  ? -1.22255  20.65285 26.42907 1.000 23.68261 ? 78  VAL A CG1 1 
ATOM   593  C CG2 . VAL A 1 78  ? -1.26603  20.10392 28.90115 1.000 23.38391 ? 78  VAL A CG2 1 
ATOM   594  N N   . ASP A 1 79  ? -4.33202  21.18432 30.00766 1.000 22.70637 ? 79  ASP A N   1 
ATOM   595  C CA  . ASP A 1 79  ? -5.20195  20.66232 31.05867 1.000 25.72820 ? 79  ASP A CA  1 
ATOM   596  C C   . ASP A 1 79  ? -6.65239  20.64332 30.58460 1.000 26.19907 ? 79  ASP A C   1 
ATOM   597  O O   . ASP A 1 79  ? -7.05805  21.42112 29.71454 1.000 24.96178 ? 79  ASP A O   1 
ATOM   598  C CB  . ASP A 1 79  ? -5.13483  21.50416 32.33883 1.000 23.73497 ? 79  ASP A CB  1 
ATOM   599  C CG  . ASP A 1 79  ? -3.72724  21.71235 32.86458 1.000 31.86510 ? 79  ASP A CG  1 
ATOM   600  O OD1 . ASP A 1 79  ? -3.27934  20.89679 33.69218 1.000 33.51204 ? 79  ASP A OD1 1 
ATOM   601  O OD2 . ASP A 1 79  ? -3.09312  22.73424 32.50826 0.595 25.59033 ? 79  ASP A OD2 1 
ATOM   602  N N   . SER A 1 80  ? -7.44462  19.75947 31.18827 1.000 25.56723 ? 80  SER A N   1 
ATOM   603  C CA  . SER A 1 80  ? -8.86251  19.69310 30.86780 1.000 26.01138 ? 80  SER A CA  1 
ATOM   604  C C   . SER A 1 80  ? -9.56193  20.99159 31.25693 1.000 26.97773 ? 80  SER A C   1 
ATOM   605  O O   . SER A 1 80  ? -9.11822  21.73034 32.13798 1.000 25.29404 ? 80  SER A O   1 
ATOM   606  C CB  . SER A 1 80  ? -9.53452  18.53138 31.59907 1.000 29.32114 ? 80  SER A CB  1 
ATOM   607  O OG  . SER A 1 80  ? -9.65999  18.82894 32.98252 1.000 29.64630 ? 80  SER A OG  1 
ATOM   608  N N   . HIS A 1 81  ? -10.69598 21.24374 30.60482 1.000 25.89149 ? 81  HIS A N   1 
ATOM   609  C CA  . HIS A 1 81  ? -11.52418 22.37914 30.99407 1.000 23.31579 ? 81  HIS A CA  1 
ATOM   610  C C   . HIS A 1 81  ? -12.03075 22.23889 32.42932 1.000 25.26294 ? 81  HIS A C   1 
ATOM   611  O O   . HIS A 1 81  ? -12.21981 23.24677 33.12037 1.000 26.38963 ? 81  HIS A O   1 
ATOM   612  C CB  . HIS A 1 81  ? -12.68294 22.55408 30.00198 1.000 23.96792 ? 81  HIS A CB  1 
ATOM   613  C CG  . HIS A 1 81  ? -13.47995 21.30662 29.76063 1.000 30.99318 ? 81  HIS A CG  1 
ATOM   614  N ND1 . HIS A 1 81  ? -12.99579 20.24548 29.02557 1.000 32.24033 ? 81  HIS A ND1 1 
ATOM   615  C CD2 . HIS A 1 81  ? -14.73684 20.96530 30.13342 1.000 28.93139 ? 81  HIS A CD2 1 
ATOM   616  C CE1 . HIS A 1 81  ? -13.91375 19.29449 28.97061 1.000 33.09070 ? 81  HIS A CE1 1 
ATOM   617  N NE2 . HIS A 1 81  ? -14.98049 19.70562 29.63428 1.000 29.77036 ? 81  HIS A NE2 1 
ATOM   618  N N   . PHE A 1 82  ? -12.22063 21.00366 32.91829 1.000 28.24777 ? 82  PHE A N   1 
ATOM   619  C CA  . PHE A 1 82  ? -12.59241 20.83726 34.32096 1.000 26.80026 ? 82  PHE A CA  1 
ATOM   620  C C   . PHE A 1 82  ? -11.48567 21.33440 35.23956 1.000 25.31097 ? 82  PHE A C   1 
ATOM   621  O O   . PHE A 1 82  ? -11.75781 21.93639 36.28676 1.000 27.46871 ? 82  PHE A O   1 
ATOM   622  C CB  . PHE A 1 82  ? -12.89826 19.36942 34.63265 1.000 26.94699 ? 82  PHE A CB  1 
ATOM   623  C CG  . PHE A 1 82  ? -14.07620 18.81669 33.88362 1.000 29.81591 ? 82  PHE A CG  1 
ATOM   624  C CD1 . PHE A 1 82  ? -15.36690 19.06221 34.32589 1.000 30.37917 ? 82  PHE A CD1 1 
ATOM   625  C CD2 . PHE A 1 82  ? -13.88848 18.03003 32.75050 1.000 32.16885 ? 82  PHE A CD2 1 
ATOM   626  C CE1 . PHE A 1 82  ? -16.45316 18.55124 33.64670 1.000 34.59012 ? 82  PHE A CE1 1 
ATOM   627  C CE2 . PHE A 1 82  ? -14.97334 17.50219 32.06294 1.000 31.25330 ? 82  PHE A CE2 1 
ATOM   628  C CZ  . PHE A 1 82  ? -16.26092 17.76543 32.51628 1.000 32.17983 ? 82  PHE A CZ  1 
ATOM   629  N N   . SER A 1 83  ? -10.23076 21.07430 34.87302 1.000 26.24253 ? 83  SER A N   1 
ATOM   630  C CA  . SER A 1 83  ? -9.11426  21.57158 35.66866 1.000 25.88023 ? 83  SER A CA  1 
ATOM   631  C C   . SER A 1 83  ? -9.08097  23.09589 35.65469 1.000 25.49036 ? 83  SER A C   1 
ATOM   632  O O   . SER A 1 83  ? -8.89448  23.72729 36.70060 1.000 25.38609 ? 83  SER A O   1 
ATOM   633  C CB  . SER A 1 83  ? -7.80261  20.99724 35.13850 1.000 26.61054 ? 83  SER A CB  1 
ATOM   634  O OG  . SER A 1 83  ? -6.67335  21.66434 35.69620 1.000 28.78802 ? 83  SER A OG  1 
ATOM   635  N N   . HIS A 1 84  ? -9.27809  23.69881 34.47944 1.000 25.07221 ? 84  HIS A N   1 
ATOM   636  C CA  . HIS A 1 84  ? -9.35420  25.15764 34.37877 1.000 24.66861 ? 84  HIS A CA  1 
ATOM   637  C C   . HIS A 1 84  ? -10.36845 25.72330 35.35817 1.000 28.61185 ? 84  HIS A C   1 
ATOM   638  O O   . HIS A 1 84  ? -10.06810 26.65075 36.12082 1.000 26.44504 ? 84  HIS A O   1 
ATOM   639  C CB  . HIS A 1 84  ? -9.74117  25.57386 32.95636 1.000 24.91681 ? 84  HIS A CB  1 
ATOM   640  C CG  . HIS A 1 84  ? -8.68180  25.33202 31.92872 1.000 24.28523 ? 84  HIS A CG  1 
ATOM   641  N ND1 . HIS A 1 84  ? -7.44019  24.80713 32.23132 1.000 24.45586 ? 84  HIS A ND1 1 
ATOM   642  C CD2 . HIS A 1 84  ? -8.68104  25.55615 30.59246 1.000 23.08900 ? 84  HIS A CD2 1 
ATOM   643  C CE1 . HIS A 1 84  ? -6.72045  24.72963 31.12531 1.000 23.23823 ? 84  HIS A CE1 1 
ATOM   644  N NE2 . HIS A 1 84  ? -7.45288  25.17158 30.11580 1.000 23.54027 ? 84  HIS A NE2 1 
ATOM   645  N N   . LEU A 1 85  ? -11.58922 25.17842 35.34274 1.000 25.87505 ? 85  LEU A N   1 
ATOM   646  C CA  . LEU A 1 85  ? -12.64346 25.71499 36.19731 1.000 28.26842 ? 85  LEU A CA  1 
ATOM   647  C C   . LEU A 1 85  ? -12.32447 25.50849 37.67406 1.000 25.68140 ? 85  LEU A C   1 
ATOM   648  O O   . LEU A 1 85  ? -12.61970 26.37329 38.50312 1.000 27.62614 ? 85  LEU A O   1 
ATOM   649  C CB  . LEU A 1 85  ? -13.98736 25.07905 35.83653 1.000 28.64971 ? 85  LEU A CB  1 
ATOM   650  C CG  . LEU A 1 85  ? -15.17718 25.55327 36.67423 1.000 28.45183 ? 85  LEU A CG  1 
ATOM   651  C CD1 . LEU A 1 85  ? -15.33622 27.06990 36.58019 1.000 31.54717 ? 85  LEU A CD1 1 
ATOM   652  C CD2 . LEU A 1 85  ? -16.45539 24.84593 36.23546 1.000 33.81299 ? 85  LEU A CD2 1 
ATOM   653  N N   . ALA A 1 86  ? -11.72983 24.36179 38.02857 1.000 26.45450 ? 86  ALA A N   1 
ATOM   654  C CA  . ALA A 1 86  ? -11.32390 24.14726 39.41484 1.000 26.97375 ? 86  ALA A CA  1 
ATOM   655  C C   . ALA A 1 86  ? -10.33958 25.21850 39.86989 1.000 26.91105 ? 86  ALA A C   1 
ATOM   656  O O   . ALA A 1 86  ? -10.39990 25.68201 41.01385 1.000 28.36289 ? 86  ALA A O   1 
ATOM   657  C CB  . ALA A 1 86  ? -10.71357 22.75331 39.57465 1.000 26.89627 ? 86  ALA A CB  1 
ATOM   658  N N   . TRP A 1 87  ? -9.43624  25.63629 38.97895 1.000 27.97439 ? 87  TRP A N   1 
ATOM   659  C CA  . TRP A 1 87  ? -8.48119  26.68961 39.32727 1.000 27.92732 ? 87  TRP A CA  1 
ATOM   660  C C   . TRP A 1 87  ? -9.16767  28.04749 39.43730 1.000 28.38393 ? 87  TRP A C   1 
ATOM   661  O O   . TRP A 1 87  ? -8.86528  28.83475 40.34218 1.000 26.44574 ? 87  TRP A O   1 
ATOM   662  C CB  . TRP A 1 87  ? -7.36821  26.74086 38.28665 1.000 24.74424 ? 87  TRP A CB  1 
ATOM   663  C CG  . TRP A 1 87  ? -6.07857  27.31764 38.77942 1.000 24.72824 ? 87  TRP A CG  1 
ATOM   664  C CD1 . TRP A 1 87  ? -5.73541  27.58019 40.07020 1.000 26.96701 ? 87  TRP A CD1 1 
ATOM   665  C CD2 . TRP A 1 87  ? -4.95596  27.69810 37.97616 1.000 26.15857 ? 87  TRP A CD2 1 
ATOM   666  N NE1 . TRP A 1 87  ? -4.45598  28.10610 40.12351 1.000 26.86929 ? 87  TRP A NE1 1 
ATOM   667  C CE2 . TRP A 1 87  ? -3.95866  28.18027 38.84880 1.000 26.93265 ? 87  TRP A CE2 1 
ATOM   668  C CE3 . TRP A 1 87  ? -4.69697  27.67812 36.60296 1.000 24.56069 ? 87  TRP A CE3 1 
ATOM   669  C CZ2 . TRP A 1 87  ? -2.72202  28.64062 38.38923 1.000 24.30170 ? 87  TRP A CZ2 1 
ATOM   670  C CZ3 . TRP A 1 87  ? -3.46765  28.13798 36.14999 1.000 23.85071 ? 87  TRP A CZ3 1 
ATOM   671  C CH2 . TRP A 1 87  ? -2.49579  28.60510 37.04378 1.000 23.84358 ? 87  TRP A CH2 1 
ATOM   672  N N   . VAL A 1 88  ? -10.09197 28.34078 38.51854 1.000 25.70688 ? 88  VAL A N   1 
ATOM   673  C CA  . VAL A 1 88  ? -10.88775 29.56509 38.61297 1.000 27.76323 ? 88  VAL A CA  1 
ATOM   674  C C   . VAL A 1 88  ? -11.64378 29.61784 39.93731 1.000 27.29393 ? 88  VAL A C   1 
ATOM   675  O O   . VAL A 1 88  ? -11.70743 30.66437 40.59416 1.000 28.10254 ? 88  VAL A O   1 
ATOM   676  C CB  . VAL A 1 88  ? -11.84648 29.64993 37.41140 1.000 26.13455 ? 88  VAL A CB  1 
ATOM   677  C CG1 . VAL A 1 88  ? -12.90632 30.73583 37.61969 1.000 29.18142 ? 88  VAL A CG1 1 
ATOM   678  C CG2 . VAL A 1 88  ? -11.06131 29.86076 36.12588 1.000 26.80514 ? 88  VAL A CG2 1 
ATOM   679  N N   . ASN A 1 89  ? -12.22444 28.48773 40.35170 1.000 28.42992 ? 89  ASN A N   1 
ATOM   680  C CA  . ASN A 1 89  ? -13.03423 28.41413 41.56229 1.000 28.91037 ? 89  ASN A CA  1 
ATOM   681  C C   . ASN A 1 89  ? -12.20647 28.32215 42.83887 1.000 34.11729 ? 89  ASN A C   1 
ATOM   682  O O   . ASN A 1 89  ? -12.77845 28.40392 43.93400 1.000 34.61410 ? 89  ASN A O   1 
ATOM   683  C CB  . ASN A 1 89  ? -13.97666 27.21193 41.48865 1.000 29.10155 ? 89  ASN A CB  1 
ATOM   684  C CG  . ASN A 1 89  ? -15.16431 27.45750 40.58385 1.000 31.29898 ? 89  ASN A CG  1 
ATOM   685  O OD1 . ASN A 1 89  ? -15.52188 28.59512 40.31793 1.000 31.38142 ? 89  ASN A OD1 1 
ATOM   686  N ND2 . ASN A 1 89  ? -15.79034 26.37839 40.11476 1.000 33.33662 ? 89  ASN A ND2 1 
ATOM   687  N N   . THR A 1 90  ? -10.89333 28.14712 42.73234 1.000 29.90621 ? 90  THR A N   1 
ATOM   688  C CA  . THR A 1 90  ? -10.04287 28.19291 43.91211 1.000 29.91997 ? 90  THR A CA  1 
ATOM   689  C C   . THR A 1 90  ? -9.87141  29.64473 44.34439 1.000 30.71701 ? 90  THR A C   1 
ATOM   690  O O   . THR A 1 90  ? -9.54099  30.49130 43.51089 1.000 28.98894 ? 90  THR A O   1 
ATOM   691  C CB  . THR A 1 90  ? -8.68417  27.55031 43.61159 1.000 30.59008 ? 90  THR A CB  1 
ATOM   692  O OG1 . THR A 1 90  ? -8.88284  26.19960 43.17053 1.000 30.84015 ? 90  THR A OG1 1 
ATOM   693  C CG2 . THR A 1 90  ? -7.78296  27.54246 44.84640 1.000 32.07056 ? 90  THR A CG2 1 
ATOM   694  N N   . PRO A 1 91  ? -10.11772 29.97645 45.61401 1.000 34.01496 ? 91  PRO A N   1 
ATOM   695  C CA  . PRO A 1 91  ? -9.96704  31.37067 46.04508 1.000 34.80505 ? 91  PRO A CA  1 
ATOM   696  C C   . PRO A 1 91  ? -8.55512  31.86752 45.77926 1.000 34.85620 ? 91  PRO A C   1 
ATOM   697  O O   . PRO A 1 91  ? -7.58159  31.12006 45.90791 1.000 33.49636 ? 91  PRO A O   1 
ATOM   698  C CB  . PRO A 1 91  ? -10.27283 31.32275 47.54809 1.000 39.50066 ? 91  PRO A CB  1 
ATOM   699  C CG  . PRO A 1 91  ? -10.98611 30.03520 47.77867 1.000 37.28620 ? 91  PRO A CG  1 
ATOM   700  C CD  . PRO A 1 91  ? -10.49471 29.08143 46.72253 1.000 35.82765 ? 91  PRO A CD  1 
ATOM   701  N N   . LYS A 1 92  ? -8.45235  33.14106 45.38737 1.000 34.90310 ? 92  LYS A N   1 
ATOM   702  C CA  . LYS A 1 92  ? -7.14204  33.70614 45.07923 1.000 34.47764 ? 92  LYS A CA  1 
ATOM   703  C C   . LYS A 1 92  ? -6.19798  33.62605 46.27436 1.000 34.69780 ? 92  LYS A C   1 
ATOM   704  O O   . LYS A 1 92  ? -4.98595  33.46783 46.09362 1.000 35.56931 ? 92  LYS A O   1 
ATOM   705  C CB  . LYS A 1 92  ? -7.28454  35.15312 44.60612 1.000 35.69226 ? 92  LYS A CB  1 
ATOM   706  C CG  . LYS A 1 92  ? -7.98920  35.30111 43.26686 1.000 34.24829 ? 92  LYS A CG  1 
ATOM   707  C CD  . LYS A 1 92  ? -7.83266  36.71334 42.73212 1.000 36.01189 ? 92  LYS A CD  1 
ATOM   708  C CE  . LYS A 1 92  ? -6.38794  36.99965 42.34932 1.000 34.76855 ? 92  LYS A CE  1 
ATOM   709  N NZ  . LYS A 1 92  ? -6.20235  38.44517 42.02012 1.000 35.34294 ? 92  LYS A NZ  1 
ATOM   710  N N   . LYS A 1 93  ? -6.73046  33.70621 47.49670 1.000 36.34213 ? 93  LYS A N   1 
ATOM   711  C CA  . LYS A 1 93  ? -5.87764  33.63230 48.67929 1.000 39.03214 ? 93  LYS A CA  1 
ATOM   712  C C   . LYS A 1 93  ? -5.22027  32.26555 48.84429 1.000 40.06783 ? 93  LYS A C   1 
ATOM   713  O O   . LYS A 1 93  ? -4.26850  32.14180 49.62300 1.000 38.01324 ? 93  LYS A O   1 
ATOM   714  C CB  . LYS A 1 93  ? -6.68240  33.96756 49.93454 1.000 39.63691 ? 93  LYS A CB  1 
ATOM   715  C CG  . LYS A 1 93  ? -7.20624  35.38713 49.97052 1.000 45.10862 ? 93  LYS A CG  1 
ATOM   716  C CD  . LYS A 1 93  ? -6.21195  36.36366 49.35490 1.000 48.86088 ? 93  LYS A CD  1 
ATOM   717  N NZ  . LYS A 1 93  ? -5.12354  38.52586 49.94891 1.000 41.41929 ? 93  LYS A NZ  1 
ATOM   718  N N   . GLN A 1 94  ? -5.70777  31.23574 48.14614 1.000 35.55088 ? 94  GLN A N   1 
ATOM   719  C CA  . GLN A 1 94  ? -5.11159  29.90663 48.18712 1.000 35.25942 ? 94  GLN A CA  1 
ATOM   720  C C   . GLN A 1 94  ? -4.34010  29.58539 46.91279 1.000 35.29327 ? 94  GLN A C   1 
ATOM   721  O O   . GLN A 1 94  ? -4.06037  28.41426 46.63733 1.000 35.42712 ? 94  GLN A O   1 
ATOM   722  C CB  . GLN A 1 94  ? -6.18837  28.84907 48.44083 1.000 36.94055 ? 94  GLN A CB  1 
ATOM   723  C CG  . GLN A 1 94  ? -6.87946  29.00655 49.78450 1.000 42.82206 ? 94  GLN A CG  1 
ATOM   724  C CD  . GLN A 1 94  ? -8.15361  28.19249 49.88757 1.000 45.93698 ? 94  GLN A CD  1 
ATOM   725  O OE1 . GLN A 1 94  ? -8.38525  27.27562 49.10017 1.000 48.63041 ? 94  GLN A OE1 1 
ATOM   726  N NE2 . GLN A 1 94  ? -8.98767  28.52633 50.85984 1.000 48.36966 ? 94  GLN A NE2 1 
ATOM   727  N N   . GLY A 1 95  ? -3.99672  30.59947 46.12723 1.000 30.84481 ? 95  GLY A N   1 
ATOM   728  C CA  . GLY A 1 95  ? -3.29483  30.38770 44.87972 1.000 29.56219 ? 95  GLY A CA  1 
ATOM   729  C C   . GLY A 1 95  ? -4.18264  30.15597 43.67963 1.000 30.07257 ? 95  GLY A C   1 
ATOM   730  O O   . GLY A 1 95  ? -3.67870  29.74227 42.62857 1.000 30.75952 ? 95  GLY A O   1 
ATOM   731  N N   . GLY A 1 96  ? -5.48627  30.41442 43.79829 1.000 29.96389 ? 96  GLY A N   1 
ATOM   732  C CA  . GLY A 1 96  ? -6.38839  30.24908 42.68163 1.000 27.92331 ? 96  GLY A CA  1 
ATOM   733  C C   . GLY A 1 96  ? -6.39227  31.44826 41.74809 1.000 28.20309 ? 96  GLY A C   1 
ATOM   734  O O   . GLY A 1 96  ? -5.83382  32.50978 42.03523 1.000 28.62580 ? 96  GLY A O   1 
ATOM   735  N N   . LEU A 1 97  ? -7.04378  31.26038 40.59748 1.000 26.46318 ? 97  LEU A N   1 
ATOM   736  C CA  . LEU A 1 97  ? -7.16418  32.34012 39.62108 1.000 27.31832 ? 97  LEU A CA  1 
ATOM   737  C C   . LEU A 1 97  ? -8.22191  33.35919 40.02488 1.000 25.74322 ? 97  LEU A C   1 
ATOM   738  O O   . LEU A 1 97  ? -8.06363  34.55990 39.77277 1.000 27.81611 ? 97  LEU A O   1 
ATOM   739  C CB  . LEU A 1 97  ? -7.51763  31.77590 38.24656 1.000 25.25333 ? 97  LEU A CB  1 
ATOM   740  C CG  . LEU A 1 97  ? -6.49916  30.87474 37.54875 1.000 23.59700 ? 97  LEU A CG  1 
ATOM   741  C CD1 . LEU A 1 97  ? -7.04806  30.44110 36.20509 1.000 25.14667 ? 97  LEU A CD1 1 
ATOM   742  C CD2 . LEU A 1 97  ? -5.17725  31.61780 37.39089 1.000 24.77758 ? 97  LEU A CD2 1 
ATOM   743  N N   . GLY A 1 98  ? -9.30874  32.90133 40.63329 1.000 26.49749 ? 98  GLY A N   1 
ATOM   744  C CA  . GLY A 1 98  ? -10.45985 33.74019 40.85657 1.000 27.73759 ? 98  GLY A CA  1 
ATOM   745  C C   . GLY A 1 98  ? -11.24085 33.93957 39.57164 1.000 27.83567 ? 98  GLY A C   1 
ATOM   746  O O   . GLY A 1 98  ? -10.89502 33.39451 38.51845 1.000 26.79962 ? 98  GLY A O   1 
ATOM   747  N N   . PRO A 1 99  ? -12.31307 34.73105 39.63634 1.000 28.29794 ? 99  PRO A N   1 
ATOM   748  C CA  . PRO A 1 99  ? -13.12305 34.98615 38.43503 1.000 28.84295 ? 99  PRO A CA  1 
ATOM   749  C C   . PRO A 1 99  ? -12.29275 35.56643 37.29565 1.000 26.41677 ? 99  PRO A C   1 
ATOM   750  O O   . PRO A 1 99  ? -11.43382 36.42590 37.50136 1.000 29.28415 ? 99  PRO A O   1 
ATOM   751  C CB  . PRO A 1 99  ? -14.17594 35.99026 38.92430 1.000 31.87231 ? 99  PRO A CB  1 
ATOM   752  C CG  . PRO A 1 99  ? -14.28135 35.73823 40.39619 1.000 35.76193 ? 99  PRO A CG  1 
ATOM   753  C CD  . PRO A 1 99  ? -12.90728 35.31429 40.85182 1.000 32.13939 ? 99  PRO A CD  1 
ATOM   754  N N   . MET A 1 100 ? -12.57890 35.10134 36.08228 1.000 26.50321 ? 100 MET A N   1 
ATOM   755  C CA  . MET A 1 100 ? -11.81428 35.44404 34.89231 1.000 24.87972 ? 100 MET A CA  1 
ATOM   756  C C   . MET A 1 100 ? -12.62817 36.32429 33.95656 1.000 27.05461 ? 100 MET A C   1 
ATOM   757  O O   . MET A 1 100 ? -13.84115 36.13593 33.80906 1.000 27.31109 ? 100 MET A O   1 
ATOM   758  C CB  . MET A 1 100 ? -11.37654 34.18447 34.14385 1.000 25.71240 ? 100 MET A CB  1 
ATOM   759  C CG  . MET A 1 100 ? -10.36766 33.33192 34.92608 1.000 24.33117 ? 100 MET A CG  1 
ATOM   760  S SD  . MET A 1 100 ? -8.70074  34.00000 34.78257 1.000 27.18910 ? 100 MET A SD  1 
ATOM   761  C CE  . MET A 1 100 ? -8.55189  34.97286 36.28187 1.000 28.23841 ? 100 MET A CE  1 
ATOM   762  N N   . ASN A 1 101 ? -11.94248 37.25788 33.29884 1.000 26.28807 ? 101 ASN A N   1 
ATOM   763  C CA  . ASN A 1 101 ? -12.53092 38.07101 32.24177 1.000 24.99561 ? 101 ASN A CA  1 
ATOM   764  C C   . ASN A 1 101 ? -12.19378 37.56245 30.84538 1.000 26.45902 ? 101 ASN A C   1 
ATOM   765  O O   . ASN A 1 101 ? -12.62435 38.16867 29.86044 1.000 26.19299 ? 101 ASN A O   1 
ATOM   766  C CB  . ASN A 1 101 ? -12.07278 39.52696 32.37332 1.000 26.41236 ? 101 ASN A CB  1 
ATOM   767  C CG  . ASN A 1 101 ? -12.61274 40.19516 33.61516 1.000 31.30533 ? 101 ASN A CG  1 
ATOM   768  O OD1 . ASN A 1 101 ? -13.79177 40.06964 33.93589 1.000 30.23838 ? 101 ASN A OD1 1 
ATOM   769  N ND2 . ASN A 1 101 ? -11.74763 40.91051 34.32722 1.000 25.70758 ? 101 ASN A ND2 1 
ATOM   770  N N   . ILE A 1 102 ? -11.43300 36.47586 30.73556 1.000 23.51624 ? 102 ILE A N   1 
ATOM   771  C CA  . ILE A 1 102 ? -11.01732 35.93033 29.44377 1.000 20.72806 ? 102 ILE A CA  1 
ATOM   772  C C   . ILE A 1 102 ? -11.35242 34.44339 29.43298 1.000 23.54989 ? 102 ILE A C   1 
ATOM   773  O O   . ILE A 1 102 ? -11.43353 33.81946 30.50150 1.000 25.63852 ? 102 ILE A O   1 
ATOM   774  C CB  . ILE A 1 102 ? -9.51669  36.13704 29.18865 1.000 21.77801 ? 102 ILE A CB  1 
ATOM   775  C CG1 . ILE A 1 102 ? -8.69569  35.48473 30.31008 1.000 24.55647 ? 102 ILE A CG1 1 
ATOM   776  C CG2 . ILE A 1 102 ? -9.19745  37.64070 29.06999 1.000 23.06686 ? 102 ILE A CG2 1 
ATOM   777  C CD1 . ILE A 1 102 ? -7.20170  35.33542 29.98740 1.000 24.71090 ? 102 ILE A CD1 1 
ATOM   778  N N   . PRO A 1 103 ? -11.55508 33.84722 28.26426 1.000 22.98444 ? 103 PRO A N   1 
ATOM   779  C CA  . PRO A 1 103 ? -11.76757 32.39441 28.19851 1.000 23.44077 ? 103 PRO A CA  1 
ATOM   780  C C   . PRO A 1 103 ? -10.44713 31.64596 28.26922 1.000 24.02350 ? 103 PRO A C   1 
ATOM   781  O O   . PRO A 1 103 ? -9.40331  32.14156 27.84007 1.000 23.78288 ? 103 PRO A O   1 
ATOM   782  C CB  . PRO A 1 103 ? -12.43773 32.20242 26.83378 1.000 23.17523 ? 103 PRO A CB  1 
ATOM   783  C CG  . PRO A 1 103 ? -11.97355 33.37274 26.00758 1.000 26.71207 ? 103 PRO A CG  1 
ATOM   784  C CD  . PRO A 1 103 ? -11.75096 34.51271 26.96265 1.000 25.66037 ? 103 PRO A CD  1 
ATOM   785  N N   . LEU A 1 104 ? -10.51422 30.41237 28.78843 1.000 23.79533 ? 104 LEU A N   1 
ATOM   786  C CA  . LEU A 1 104 ? -9.34582  29.54299 28.91717 1.000 22.28561 ? 104 LEU A CA  1 
ATOM   787  C C   . LEU A 1 104 ? -9.63352  28.25294 28.16355 1.000 22.30957 ? 104 LEU A C   1 
ATOM   788  O O   . LEU A 1 104 ? -10.48596 27.46667 28.58586 1.000 25.94631 ? 104 LEU A O   1 
ATOM   789  C CB  . LEU A 1 104 ? -9.02217  29.26548 30.38263 1.000 22.19137 ? 104 LEU A CB  1 
ATOM   790  C CG  . LEU A 1 104 ? -8.65131  30.53081 31.17628 1.000 20.27004 ? 104 LEU A CG  1 
ATOM   791  C CD1 . LEU A 1 104 ? -8.54649  30.21987 32.66374 1.000 28.90896 ? 104 LEU A CD1 1 
ATOM   792  C CD2 . LEU A 1 104 ? -7.33723  31.10902 30.64667 1.000 22.87863 ? 104 LEU A CD2 1 
ATOM   793  N N   . VAL A 1 105 ? -8.92754  28.05376 27.05931 1.000 21.66120 ? 105 VAL A N   1 
ATOM   794  C CA  . VAL A 1 105 ? -9.12249  26.90566 26.17049 1.000 21.59902 ? 105 VAL A CA  1 
ATOM   795  C C   . VAL A 1 105 ? -8.40717  25.68483 26.73313 1.000 24.95498 ? 105 VAL A C   1 
ATOM   796  O O   . VAL A 1 105 ? -7.33134  25.79177 27.33109 1.000 22.45224 ? 105 VAL A O   1 
ATOM   797  C CB  . VAL A 1 105 ? -8.60232  27.26923 24.76188 1.000 24.28071 ? 105 VAL A CB  1 
ATOM   798  C CG1 . VAL A 1 105 ? -8.24782  26.01799 23.93906 1.000 25.25348 ? 105 VAL A CG1 1 
ATOM   799  C CG2 . VAL A 1 105 ? -9.60827  28.15143 24.02076 1.000 25.09129 ? 105 VAL A CG2 1 
ATOM   800  N N   . SER A 1 106 ? -9.00531  24.50903 26.52925 1.000 22.46889 ? 106 SER A N   1 
ATOM   801  C CA  . SER A 1 106 ? -8.39993  23.23262 26.89103 1.000 24.60070 ? 106 SER A CA  1 
ATOM   802  C C   . SER A 1 106 ? -7.91649  22.52049 25.62684 1.000 24.54892 ? 106 SER A C   1 
ATOM   803  O O   . SER A 1 106 ? -8.66637  22.39890 24.64799 1.000 23.71239 ? 106 SER A O   1 
ATOM   804  C CB  . SER A 1 106 ? -9.40712  22.36907 27.65766 1.000 25.98610 ? 106 SER A CB  1 
ATOM   805  O OG  . SER A 1 106 ? -8.91081  21.05434 27.87188 1.000 25.64770 ? 106 SER A OG  1 
ATOM   806  N N   . ASP A 1 107 ? -6.66767  22.04559 25.65802 1.000 23.87285 ? 107 ASP A N   1 
ATOM   807  C CA  . ASP A 1 107 ? -6.00631  21.40737 24.51555 1.000 22.19286 ? 107 ASP A CA  1 
ATOM   808  C C   . ASP A 1 107 ? -5.53136  20.00664 24.91052 1.000 23.34571 ? 107 ASP A C   1 
ATOM   809  O O   . ASP A 1 107 ? -4.33617  19.70450 24.82943 1.000 22.99655 ? 107 ASP A O   1 
ATOM   810  C CB  . ASP A 1 107 ? -4.83140  22.26645 24.04640 1.000 22.73155 ? 107 ASP A CB  1 
ATOM   811  C CG  . ASP A 1 107 ? -4.12152  21.72102 22.80848 1.000 23.98661 ? 107 ASP A CG  1 
ATOM   812  O OD1 . ASP A 1 107 ? -4.74696  21.00440 21.98304 1.000 26.01721 ? 107 ASP A OD1 1 
ATOM   813  O OD2 . ASP A 1 107 ? -2.90628  22.01049 22.66751 1.000 24.94087 ? 107 ASP A OD2 1 
ATOM   814  N N   . PRO A 1 108 ? -6.45024  19.12966 25.33405 1.000 26.12359 ? 108 PRO A N   1 
ATOM   815  C CA  . PRO A 1 108 ? -6.02494  17.83755 25.90829 1.000 24.38957 ? 108 PRO A CA  1 
ATOM   816  C C   . PRO A 1 108 ? -5.41248  16.88839 24.89050 1.000 26.35880 ? 108 PRO A C   1 
ATOM   817  O O   . PRO A 1 108 ? -4.69188  15.95186 25.28121 1.000 24.60851 ? 108 PRO A O   1 
ATOM   818  C CB  . PRO A 1 108 ? -7.32929  17.26763 26.48387 1.000 27.76503 ? 108 PRO A CB  1 
ATOM   819  C CG  . PRO A 1 108 ? -8.38955  17.78907 25.55234 1.000 25.57243 ? 108 PRO A CG  1 
ATOM   820  C CD  . PRO A 1 108 ? -7.91875  19.22351 25.22216 1.000 26.36472 ? 108 PRO A CD  1 
ATOM   821  N N   . LYS A 1 109 ? -5.67489  17.07783 23.60599 1.000 25.14159 ? 109 LYS A N   1 
ATOM   822  C CA  . LYS A 1 109 ? -5.03324  16.23380 22.60635 1.000 27.69220 ? 109 LYS A CA  1 
ATOM   823  C C   . LYS A 1 109 ? -3.69480  16.77788 22.14220 1.000 26.65604 ? 109 LYS A C   1 
ATOM   824  O O   . LYS A 1 109 ? -3.00930  16.10230 21.37158 1.000 27.16171 ? 109 LYS A O   1 
ATOM   825  C CB  . LYS A 1 109 ? -5.96868  16.02395 21.41444 1.000 31.53926 ? 109 LYS A CB  1 
ATOM   826  C CG  . LYS A 1 109 ? -7.33089  15.48743 21.84998 1.000 31.61085 ? 109 LYS A CG  1 
ATOM   827  C CD  . LYS A 1 109 ? -8.22028  15.15009 20.66147 1.000 41.59470 ? 109 LYS A CD  1 
ATOM   828  C CE  . LYS A 1 109 ? -8.53481  16.38500 19.85217 1.000 46.52741 ? 109 LYS A CE  1 
ATOM   829  N NZ  . LYS A 1 109 ? -8.75533  16.02967 18.43211 1.000 56.69851 ? 109 LYS A NZ  1 
ATOM   830  N N   . ARG A 1 110 ? -3.29913  17.96757 22.61156 1.000 23.90275 ? 110 ARG A N   1 
ATOM   831  C CA  . ARG A 1 110 ? -2.03643  18.63311 22.28692 1.000 26.65191 ? 110 ARG A CA  1 
ATOM   832  C C   . ARG A 1 110 ? -1.94183  19.06401 20.82473 1.000 25.56485 ? 110 ARG A C   1 
ATOM   833  O O   . ARG A 1 110 ? -0.87021  19.48930 20.37486 1.000 26.44590 ? 110 ARG A O   1 
ATOM   834  C CB  . ARG A 1 110 ? -0.82439  17.75753 22.65510 1.000 25.77408 ? 110 ARG A CB  1 
ATOM   835  C CG  . ARG A 1 110 ? -0.40558  17.80106 24.13831 1.000 23.06491 ? 110 ARG A CG  1 
ATOM   836  C CD  . ARG A 1 110 ? -1.41848  17.17749 25.09627 1.000 24.49375 ? 110 ARG A CD  1 
ATOM   837  N NE  . ARG A 1 110 ? -0.82982  16.94694 26.42065 1.000 24.45351 ? 110 ARG A NE  1 
ATOM   838  C CZ  . ARG A 1 110 ? -1.48496  16.46568 27.47030 1.000 23.41810 ? 110 ARG A CZ  1 
ATOM   839  N NH1 . ARG A 1 110 ? -2.77067  16.14431 27.37680 1.000 25.86159 ? 110 ARG A NH1 1 
ATOM   840  N NH2 . ARG A 1 110 ? -0.85389  16.30432 28.62794 1.000 25.29406 ? 110 ARG A NH2 1 
ATOM   841  N N   . THR A 1 111 ? -3.03695  18.99320 20.06596 1.000 25.31278 ? 111 THR A N   1 
ATOM   842  C CA  . THR A 1 111 ? -2.95750  19.31485 18.64633 1.000 25.56612 ? 111 THR A CA  1 
ATOM   843  C C   . THR A 1 111 ? -2.88459  20.81651 18.40135 1.000 25.09818 ? 111 THR A C   1 
ATOM   844  O O   . THR A 1 111 ? -2.29180  21.24861 17.40584 1.000 27.83047 ? 111 THR A O   1 
ATOM   845  C CB  . THR A 1 111 ? -4.16138  18.74654 17.90446 1.000 27.67779 ? 111 THR A CB  1 
ATOM   846  O OG1 . THR A 1 111 ? -5.35802  19.15682 18.57470 1.000 29.92872 ? 111 THR A OG1 1 
ATOM   847  C CG2 . THR A 1 111 ? -4.09923  17.21299 17.87223 1.000 27.12234 ? 111 THR A CG2 1 
ATOM   848  N N   . ILE A 1 112 ? -3.48854  21.62092 19.27356 1.000 24.29759 ? 112 ILE A N   1 
ATOM   849  C CA  . ILE A 1 112 ? -3.40175  23.07092 19.09466 1.000 23.69394 ? 112 ILE A CA  1 
ATOM   850  C C   . ILE A 1 112 ? -1.97718  23.54687 19.35703 1.000 22.51970 ? 112 ILE A C   1 
ATOM   851  O O   . ILE A 1 112 ? -1.39206  24.27902 18.55211 1.000 24.71036 ? 112 ILE A O   1 
ATOM   852  C CB  . ILE A 1 112 ? -4.42086  23.78969 19.99233 1.000 22.94885 ? 112 ILE A CB  1 
ATOM   853  C CG1 . ILE A 1 112 ? -5.82997  23.26455 19.73203 1.000 24.93552 ? 112 ILE A CG1 1 
ATOM   854  C CG2 . ILE A 1 112 ? -4.38427  25.30815 19.72628 1.000 24.80615 ? 112 ILE A CG2 1 
ATOM   855  C CD1 . ILE A 1 112 ? -6.86842  23.76966 20.74576 1.000 26.96153 ? 112 ILE A CD1 1 
ATOM   856  N N   . ALA A 1 113 ? -1.39013  23.11323 20.47522 1.000 25.30235 ? 113 ALA A N   1 
ATOM   857  C CA  . ALA A 1 113 ? 0.01723   23.39969 20.74130 1.000 23.01293 ? 113 ALA A CA  1 
ATOM   858  C C   . ALA A 1 113 ? 0.91186   22.94761 19.59097 1.000 25.80425 ? 113 ALA A C   1 
ATOM   859  O O   . ALA A 1 113 ? 1.80716   23.68341 19.16258 1.000 24.65517 ? 113 ALA A O   1 
ATOM   860  C CB  . ALA A 1 113 ? 0.44057   22.73021 22.04902 1.000 24.81486 ? 113 ALA A CB  1 
ATOM   861  N N   . GLN A 1 114 ? 0.68272   21.73846 19.06112 1.000 25.28378 ? 114 GLN A N   1 
ATOM   862  C CA  . GLN A 1 114 ? 1.48701   21.29345 17.92778 1.000 27.17050 ? 114 GLN A CA  1 
ATOM   863  C C   . GLN A 1 114 ? 1.27810   22.19682 16.71179 1.000 24.65709 ? 114 GLN A C   1 
ATOM   864  O O   . GLN A 1 114 ? 2.23980   22.56177 16.02485 1.000 27.20026 ? 114 GLN A O   1 
ATOM   865  C CB  . GLN A 1 114 ? 1.15380   19.83794 17.58923 1.000 26.68612 ? 114 GLN A CB  1 
ATOM   866  C CG  . GLN A 1 114 ? 1.73604   18.85689 18.58626 1.000 30.02676 ? 114 GLN A CG  1 
ATOM   867  C CD  . GLN A 1 114 ? 1.26195   17.42081 18.36448 1.000 36.78825 ? 114 GLN A CD  1 
ATOM   868  O OE1 . GLN A 1 114 ? 0.10166   17.18192 18.01622 1.000 35.12988 ? 114 GLN A OE1 1 
ATOM   869  N NE2 . GLN A 1 114 ? 2.16218   16.46028 18.56497 1.000 38.75379 ? 114 GLN A NE2 1 
ATOM   870  N N   . ASP A 1 115 ? 0.02366   22.55771 16.42895 1.000 26.30474 ? 115 ASP A N   1 
ATOM   871  C CA  . ASP A 1 115 ? -0.27209  23.42962 15.29542 1.000 25.88117 ? 115 ASP A CA  1 
ATOM   872  C C   . ASP A 1 115 ? 0.48552   24.74592 15.40321 1.000 27.52872 ? 115 ASP A C   1 
ATOM   873  O O   . ASP A 1 115 ? 0.91499   25.31579 14.39203 1.000 26.95864 ? 115 ASP A O   1 
ATOM   874  C CB  . ASP A 1 115 ? -1.77673  23.69691 15.23447 1.000 28.55229 ? 115 ASP A CB  1 
ATOM   875  C CG  . ASP A 1 115 ? -2.46631  22.91993 14.14970 1.000 42.28410 ? 115 ASP A CG  1 
ATOM   876  O OD1 . ASP A 1 115 ? -1.86965  22.77395 13.06123 1.000 49.64366 ? 115 ASP A OD1 1 
ATOM   877  O OD2 . ASP A 1 115 ? -3.60247  22.45377 14.39729 1.000 39.41190 ? 115 ASP A OD2 1 
ATOM   878  N N   . TYR A 1 116 ? 0.65671   25.24191 16.62285 1.000 27.43327 ? 116 TYR A N   1 
ATOM   879  C CA  . TYR A 1 116 ? 1.30389   26.52390 16.85203 1.000 25.26775 ? 116 TYR A CA  1 
ATOM   880  C C   . TYR A 1 116 ? 2.79793   26.38209 17.10006 1.000 27.06193 ? 116 TYR A C   1 
ATOM   881  O O   . TYR A 1 116 ? 3.48357   27.38314 17.33318 1.000 26.33680 ? 116 TYR A O   1 
ATOM   882  C CB  . TYR A 1 116 ? 0.59836   27.25136 17.99919 1.000 23.26840 ? 116 TYR A CB  1 
ATOM   883  C CG  . TYR A 1 116 ? -0.60381  27.98414 17.46097 1.000 24.30838 ? 116 TYR A CG  1 
ATOM   884  C CD1 . TYR A 1 116 ? -1.81866  27.33080 17.25807 1.000 25.62640 ? 116 TYR A CD1 1 
ATOM   885  C CD2 . TYR A 1 116 ? -0.50504  29.31432 17.08504 1.000 25.06697 ? 116 TYR A CD2 1 
ATOM   886  C CE1 . TYR A 1 116 ? -2.91422  28.00094 16.72447 1.000 24.90091 ? 116 TYR A CE1 1 
ATOM   887  C CE2 . TYR A 1 116 ? -1.58660  29.98746 16.55577 1.000 26.50586 ? 116 TYR A CE2 1 
ATOM   888  C CZ  . TYR A 1 116 ? -2.77993  29.33979 16.37579 1.000 25.61158 ? 116 TYR A CZ  1 
ATOM   889  O OH  . TYR A 1 116 ? -3.83206  30.04914 15.83709 1.000 28.02114 ? 116 TYR A OH  1 
ATOM   890  N N   . GLY A 1 117 ? 3.32329   25.16947 16.98580 1.000 25.88635 ? 117 GLY A N   1 
ATOM   891  C CA  . GLY A 1 117 ? 4.74636   24.94980 17.14279 1.000 27.68754 ? 117 GLY A CA  1 
ATOM   892  C C   . GLY A 1 117 ? 5.28072   25.18128 18.53594 1.000 26.46346 ? 117 GLY A C   1 
ATOM   893  O O   . GLY A 1 117 ? 6.46915   25.48466 18.68930 1.000 27.42514 ? 117 GLY A O   1 
ATOM   894  N N   . VAL A 1 118 ? 4.44916   25.03814 19.56412 1.000 23.93948 ? 118 VAL A N   1 
ATOM   895  C CA  . VAL A 1 118 ? 4.91947   25.33620 20.90910 1.000 24.14863 ? 118 VAL A CA  1 
ATOM   896  C C   . VAL A 1 118 ? 4.77295   24.14286 21.85005 1.000 24.66890 ? 118 VAL A C   1 
ATOM   897  O O   . VAL A 1 118 ? 4.79540   24.31457 23.05780 1.000 24.51421 ? 118 VAL A O   1 
ATOM   898  C CB  . VAL A 1 118 ? 4.21897   26.58144 21.48796 1.000 23.96032 ? 118 VAL A CB  1 
ATOM   899  C CG1 . VAL A 1 118 ? 4.64690   27.84498 20.71919 1.000 24.83987 ? 118 VAL A CG1 1 
ATOM   900  C CG2 . VAL A 1 118 ? 2.71905   26.40688 21.48549 1.000 25.57226 ? 118 VAL A CG2 1 
ATOM   901  N N   . LEU A 1 119 ? 4.64410   22.92211 21.32566 1.000 24.12550 ? 119 LEU A N   1 
ATOM   902  C CA  . LEU A 1 119 ? 4.57913   21.76961 22.21295 1.000 26.41921 ? 119 LEU A CA  1 
ATOM   903  C C   . LEU A 1 119 ? 5.98656   21.37400 22.63370 1.000 26.39367 ? 119 LEU A C   1 
ATOM   904  O O   . LEU A 1 119 ? 6.88061   21.24937 21.78869 1.000 28.16129 ? 119 LEU A O   1 
ATOM   905  C CB  . LEU A 1 119 ? 3.88675   20.58334 21.53940 1.000 27.74391 ? 119 LEU A CB  1 
ATOM   906  C CG  . LEU A 1 119 ? 3.69795   19.39114 22.48761 1.000 28.41551 ? 119 LEU A CG  1 
ATOM   907  C CD1 . LEU A 1 119 ? 2.63838   19.70490 23.53628 1.000 28.80555 ? 119 LEU A CD1 1 
ATOM   908  C CD2 . LEU A 1 119 ? 3.31437   18.16390 21.69706 1.000 31.62632 ? 119 LEU A CD2 1 
ATOM   909  N N   . LYS A 1 120 ? 6.18221   21.20140 23.93914 1.000 24.70837 ? 120 LYS A N   1 
ATOM   910  C CA  . LYS A 1 120 ? 7.42151   20.65300 24.48237 1.000 25.56075 ? 120 LYS A CA  1 
ATOM   911  C C   . LYS A 1 120 ? 7.26680   19.13952 24.41182 1.000 28.00706 ? 120 LYS A C   1 
ATOM   912  O O   . LYS A 1 120 ? 6.63580   18.52843 25.27319 1.000 27.83692 ? 120 LYS A O   1 
ATOM   913  C CB  . LYS A 1 120 ? 7.65986   21.15241 25.90466 1.000 26.38000 ? 120 LYS A CB  1 
ATOM   914  C CG  . LYS A 1 120 ? 8.96767   20.66659 26.54714 1.000 28.46601 ? 120 LYS A CG  1 
ATOM   915  C CD  . LYS A 1 120 ? 9.22955   21.35260 27.88394 1.000 26.91205 ? 120 LYS A CD  1 
ATOM   916  C CE  . LYS A 1 120 ? 10.55468  20.90822 28.50485 1.000 32.51264 ? 120 LYS A CE  1 
ATOM   917  N NZ  . LYS A 1 120 ? 10.52599  19.48344 28.95957 1.000 31.93963 ? 120 LYS A NZ  1 
ATOM   918  N N   . ALA A 1 121 ? 7.81738   18.54754 23.35161 1.000 27.85471 ? 121 ALA A N   1 
ATOM   919  C CA  . ALA A 1 121 ? 7.44883   17.18689 22.96080 1.000 31.68565 ? 121 ALA A CA  1 
ATOM   920  C C   . ALA A 1 121 ? 7.81936   16.15199 24.01670 1.000 32.38984 ? 121 ALA A C   1 
ATOM   921  O O   . ALA A 1 121 ? 7.09452   15.16121 24.18610 1.000 32.66956 ? 121 ALA A O   1 
ATOM   922  C CB  . ALA A 1 121 ? 8.10091   16.83962 21.62271 1.000 31.71628 ? 121 ALA A CB  1 
ATOM   923  N N   . ASP A 1 122 ? 8.91833   16.35379 24.74194 1.000 31.51539 ? 122 ASP A N   1 
ATOM   924  C CA  . ASP A 1 122 ? 9.32627   15.35531 25.72582 1.000 34.42333 ? 122 ASP A CA  1 
ATOM   925  C C   . ASP A 1 122 ? 8.53069   15.43452 27.01855 1.000 35.24890 ? 122 ASP A C   1 
ATOM   926  O O   . ASP A 1 122 ? 8.79066   14.65190 27.93621 1.000 36.58195 ? 122 ASP A O   1 
ATOM   927  C CB  . ASP A 1 122 ? 10.82722  15.47200 26.03114 1.000 35.36891 ? 122 ASP A CB  1 
ATOM   928  C CG  . ASP A 1 122 ? 11.21169  16.80215 26.66684 1.000 39.67245 ? 122 ASP A CG  1 
ATOM   929  O OD1 . ASP A 1 122 ? 10.31796  17.61401 27.00701 1.000 32.13017 ? 122 ASP A OD1 1 
ATOM   930  O OD2 . ASP A 1 122 ? 12.43137  17.03376 26.82769 0.899 41.87423 ? 122 ASP A OD2 1 
ATOM   931  N N   . GLU A 1 123 ? 7.58345   16.36255 27.12147 1.000 31.26661 ? 123 GLU A N   1 
ATOM   932  C CA  . GLU A 1 123 ? 6.79741   16.52484 28.33026 1.000 27.84993 ? 123 GLU A CA  1 
ATOM   933  C C   . GLU A 1 123 ? 5.30147   16.62183 28.07347 1.000 25.91554 ? 123 GLU A C   1 
ATOM   934  O O   . GLU A 1 123 ? 4.52231   16.42912 29.01353 1.000 28.76564 ? 123 GLU A O   1 
ATOM   935  C CB  . GLU A 1 123 ? 7.26517   17.77175 29.10695 1.000 27.53480 ? 123 GLU A CB  1 
ATOM   936  C CG  . GLU A 1 123 ? 6.79698   17.81000 30.54167 1.000 30.48419 ? 123 GLU A CG  1 
ATOM   937  C CD  . GLU A 1 123 ? 7.54121   18.81376 31.41667 1.000 30.88855 ? 123 GLU A CD  1 
ATOM   938  O OE1 . GLU A 1 123 ? 8.53839   19.42476 30.96406 1.000 32.99593 ? 123 GLU A OE1 1 
ATOM   939  O OE2 . GLU A 1 123 ? 7.12011   18.97522 32.57946 1.000 33.86405 ? 123 GLU A OE2 1 
ATOM   940  N N   . GLY A 1 124 ? 4.87106   16.90257 26.84714 1.000 24.78235 ? 124 GLY A N   1 
ATOM   941  C CA  . GLY A 1 124 ? 3.45175   16.93521 26.56353 1.000 25.86932 ? 124 GLY A CA  1 
ATOM   942  C C   . GLY A 1 124 ? 2.74693   18.18662 27.02503 1.000 25.31690 ? 124 GLY A C   1 
ATOM   943  O O   . GLY A 1 124 ? 1.51992   18.17907 27.16923 1.000 23.29215 ? 124 GLY A O   1 
ATOM   944  N N   . ILE A 1 125 ? 3.49063   19.26334 27.27158 1.000 23.61392 ? 125 ILE A N   1 
ATOM   945  C CA  . ILE A 1 125 ? 2.90911   20.53922 27.66955 1.000 22.52595 ? 125 ILE A CA  1 
ATOM   946  C C   . ILE A 1 125 ? 3.41311   21.60735 26.70911 1.000 24.24211 ? 125 ILE A C   1 
ATOM   947  O O   . ILE A 1 125 ? 4.39301   21.41501 25.98732 1.000 23.92458 ? 125 ILE A O   1 
ATOM   948  C CB  . ILE A 1 125 ? 3.24956   20.90593 29.12821 1.000 23.57194 ? 125 ILE A CB  1 
ATOM   949  C CG1 . ILE A 1 125 ? 4.75340   21.19153 29.26719 1.000 26.53061 ? 125 ILE A CG1 1 
ATOM   950  C CG2 . ILE A 1 125 ? 2.78145   19.78537 30.09043 1.000 22.71324 ? 125 ILE A CG2 1 
ATOM   951  C CD1 . ILE A 1 125 ? 5.19621   21.49621 30.67920 1.000 27.06014 ? 125 ILE A CD1 1 
ATOM   952  N N   . SER A 1 126 ? 2.72150   22.74932 26.69018 1.000 22.61539 ? 126 SER A N   1 
ATOM   953  C CA  . SER A 1 126 ? 3.15912   23.83779 25.83396 1.000 22.69999 ? 126 SER A CA  1 
ATOM   954  C C   . SER A 1 126 ? 4.21637   24.69169 26.53227 1.000 22.22121 ? 126 SER A C   1 
ATOM   955  O O   . SER A 1 126 ? 4.19571   24.87837 27.75270 1.000 23.62487 ? 126 SER A O   1 
ATOM   956  C CB  . SER A 1 126 ? 1.98014   24.73324 25.42525 1.000 23.18424 ? 126 SER A CB  1 
ATOM   957  O OG  . SER A 1 126 ? 1.48713   25.46914 26.53246 1.000 24.83698 ? 126 SER A OG  1 
ATOM   958  N N   . PHE A 1 127 ? 5.14087   25.21729 25.73569 1.000 22.36442 ? 127 PHE A N   1 
ATOM   959  C CA  . PHE A 1 127 ? 5.92033   26.36849 26.15575 1.000 21.17633 ? 127 PHE A CA  1 
ATOM   960  C C   . PHE A 1 127 ? 4.98608   27.58061 26.29773 1.000 23.21498 ? 127 PHE A C   1 
ATOM   961  O O   . PHE A 1 127 ? 3.78761   27.50991 26.01001 1.000 24.58798 ? 127 PHE A O   1 
ATOM   962  C CB  . PHE A 1 127 ? 7.03019   26.64486 25.14202 1.000 22.65826 ? 127 PHE A CB  1 
ATOM   963  C CG  . PHE A 1 127 ? 8.15389   25.62887 25.16305 1.000 22.63618 ? 127 PHE A CG  1 
ATOM   964  C CD1 . PHE A 1 127 ? 9.02013   25.56142 26.23680 1.000 25.38561 ? 127 PHE A CD1 1 
ATOM   965  C CD2 . PHE A 1 127 ? 8.35407   24.77668 24.08471 1.000 27.22147 ? 127 PHE A CD2 1 
ATOM   966  C CE1 . PHE A 1 127 ? 10.06468  24.63791 26.24742 1.000 27.14003 ? 127 PHE A CE1 1 
ATOM   967  C CE2 . PHE A 1 127 ? 9.39332   23.84996 24.09414 1.000 27.18667 ? 127 PHE A CE2 1 
ATOM   968  C CZ  . PHE A 1 127 ? 10.24549  23.79400 25.17014 1.000 26.00562 ? 127 PHE A CZ  1 
ATOM   969  N N   . ARG A 1 128 ? 5.54194   28.71743 26.72832 1.000 21.03869 ? 128 ARG A N   1 
ATOM   970  C CA  . ARG A 1 128 ? 4.76955   29.95655 26.87683 1.000 22.34209 ? 128 ARG A CA  1 
ATOM   971  C C   . ARG A 1 128 ? 4.71011   30.69389 25.54085 1.000 23.62694 ? 128 ARG A C   1 
ATOM   972  O O   . ARG A 1 128 ? 5.35352   31.72730 25.33127 1.000 26.74262 ? 128 ARG A O   1 
ATOM   973  C CB  . ARG A 1 128 ? 5.37993   30.85131 27.95075 1.000 23.14604 ? 128 ARG A CB  1 
ATOM   974  C CG  . ARG A 1 128 ? 5.36933   30.24155 29.33025 1.000 24.80698 ? 128 ARG A CG  1 
ATOM   975  C CD  . ARG A 1 128 ? 5.70644   31.26518 30.43273 1.000 22.31147 ? 128 ARG A CD  1 
ATOM   976  N NE  . ARG A 1 128 ? 5.92943   30.49654 31.64026 1.000 23.02673 ? 128 ARG A NE  1 
ATOM   977  C CZ  . ARG A 1 128 ? 4.97282   30.04400 32.44029 1.000 25.73080 ? 128 ARG A CZ  1 
ATOM   978  N NH1 . ARG A 1 128 ? 3.69804   30.37116 32.22824 1.000 24.32326 ? 128 ARG A NH1 1 
ATOM   979  N NH2 . ARG A 1 128 ? 5.30162   29.26729 33.46315 1.000 26.29878 ? 128 ARG A NH2 1 
ATOM   980  N N   . GLY A 1 129 ? 3.88584   30.17809 24.63366 1.000 23.40251 ? 129 GLY A N   1 
ATOM   981  C CA  . GLY A 1 129 ? 3.70268   30.81307 23.33920 1.000 22.81862 ? 129 GLY A CA  1 
ATOM   982  C C   . GLY A 1 129 ? 2.61110   31.87170 23.38261 1.000 22.52905 ? 129 GLY A C   1 
ATOM   983  O O   . GLY A 1 129 ? 1.58130   31.69715 24.03334 1.000 25.04406 ? 129 GLY A O   1 
ATOM   984  N N   . LEU A 1 130 ? 2.85528   32.97998 22.68164 1.000 21.74907 ? 130 LEU A N   1 
ATOM   985  C CA  . LEU A 1 130 ? 1.85863   34.04076 22.55661 1.000 22.61675 ? 130 LEU A CA  1 
ATOM   986  C C   . LEU A 1 130 ? 1.82845   34.48573 21.10560 1.000 21.61217 ? 130 LEU A C   1 
ATOM   987  O O   . LEU A 1 130 ? 2.87840   34.66546 20.48513 1.000 21.49501 ? 130 LEU A O   1 
ATOM   988  C CB  . LEU A 1 130 ? 2.17337   35.22525 23.48772 1.000 20.94021 ? 130 LEU A CB  1 
ATOM   989  C CG  . LEU A 1 130 ? 1.22154   36.43631 23.40208 1.000 21.32969 ? 130 LEU A CG  1 
ATOM   990  C CD1 . LEU A 1 130 ? 1.07081   37.07625 24.78636 1.000 23.72059 ? 130 LEU A CD1 1 
ATOM   991  C CD2 . LEU A 1 130 ? 1.74087   37.43983 22.41069 1.000 22.45439 ? 130 LEU A CD2 1 
ATOM   992  N N   . PHE A 1 131 ? 0.62877   34.64055 20.55920 1.000 20.55731 ? 131 PHE A N   1 
ATOM   993  C CA  . PHE A 1 131 ? 0.46225   34.90714 19.13772 1.000 21.28430 ? 131 PHE A CA  1 
ATOM   994  C C   . PHE A 1 131 ? -0.50003  36.06554 18.97359 1.000 20.68178 ? 131 PHE A C   1 
ATOM   995  O O   . PHE A 1 131 ? -1.55277  36.08342 19.61087 1.000 22.21820 ? 131 PHE A O   1 
ATOM   996  C CB  . PHE A 1 131 ? -0.04799  33.64326 18.42822 1.000 22.62059 ? 131 PHE A CB  1 
ATOM   997  C CG  . PHE A 1 131 ? 0.88236   32.48815 18.58835 1.000 20.47067 ? 131 PHE A CG  1 
ATOM   998  C CD1 . PHE A 1 131 ? 0.78155   31.64988 19.68990 1.000 23.73974 ? 131 PHE A CD1 1 
ATOM   999  C CD2 . PHE A 1 131 ? 1.91001   32.28647 17.67967 1.000 25.05889 ? 131 PHE A CD2 1 
ATOM   1000 C CE1 . PHE A 1 131 ? 1.68106   30.61325 19.87389 1.000 22.01420 ? 131 PHE A CE1 1 
ATOM   1001 C CE2 . PHE A 1 131 ? 2.80504   31.24044 17.84768 1.000 24.80841 ? 131 PHE A CE2 1 
ATOM   1002 C CZ  . PHE A 1 131 ? 2.68199   30.40224 18.94578 1.000 23.98278 ? 131 PHE A CZ  1 
ATOM   1003 N N   . ILE A 1 132 ? -0.12205  37.04675 18.16086 1.000 21.68982 ? 132 ILE A N   1 
ATOM   1004 C CA  . ILE A 1 132 ? -0.99427  38.17311 17.85408 1.000 21.11626 ? 132 ILE A CA  1 
ATOM   1005 C C   . ILE A 1 132 ? -1.51140  37.97651 16.44099 1.000 22.88804 ? 132 ILE A C   1 
ATOM   1006 O O   . ILE A 1 132 ? -0.72627  37.88260 15.48603 1.000 22.19561 ? 132 ILE A O   1 
ATOM   1007 C CB  . ILE A 1 132 ? -0.27589  39.52166 18.01082 1.000 22.15046 ? 132 ILE A CB  1 
ATOM   1008 C CG1 . ILE A 1 132 ? 0.25672   39.64588 19.43684 1.000 22.39200 ? 132 ILE A CG1 1 
ATOM   1009 C CG2 . ILE A 1 132 ? -1.24904  40.66166 17.69494 1.000 21.67473 ? 132 ILE A CG2 1 
ATOM   1010 C CD1 . ILE A 1 132 ? 1.02047   40.94416 19.69676 1.000 25.17508 ? 132 ILE A CD1 1 
ATOM   1011 N N   . ILE A 1 133 ? -2.83569  37.92464 16.31945 1.000 22.94210 ? 133 ILE A N   1 
ATOM   1012 C CA  . ILE A 1 133 ? -3.53502  37.60642 15.07957 1.000 20.16982 ? 133 ILE A CA  1 
ATOM   1013 C C   . ILE A 1 133 ? -4.42231  38.79732 14.73883 1.000 23.14058 ? 133 ILE A C   1 
ATOM   1014 O O   . ILE A 1 133 ? -5.14342  39.30021 15.60984 1.000 25.36942 ? 133 ILE A O   1 
ATOM   1015 C CB  . ILE A 1 133 ? -4.36440  36.31758 15.23835 1.000 23.90393 ? 133 ILE A CB  1 
ATOM   1016 C CG1 . ILE A 1 133 ? -3.44849  35.16240 15.66194 1.000 23.25408 ? 133 ILE A CG1 1 
ATOM   1017 C CG2 . ILE A 1 133 ? -5.13596  36.01388 13.96720 1.000 24.35796 ? 133 ILE A CG2 1 
ATOM   1018 C CD1 . ILE A 1 133 ? -4.15937  34.05080 16.43380 1.000 26.44529 ? 133 ILE A CD1 1 
ATOM   1019 N N   . ASP A 1 134 ? -4.35591  39.26452 13.49077 1.000 24.10303 ? 134 ASP A N   1 
ATOM   1020 C CA  . ASP A 1 134 ? -5.09450  40.48039 13.16813 1.000 23.95306 ? 134 ASP A CA  1 
ATOM   1021 C C   . ASP A 1 134 ? -6.56001  40.15682 12.86584 1.000 27.76398 ? 134 ASP A C   1 
ATOM   1022 O O   . ASP A 1 134 ? -7.00502  39.00690 12.92249 1.000 26.39785 ? 134 ASP A O   1 
ATOM   1023 C CB  . ASP A 1 134 ? -4.39889  41.26984 12.04924 1.000 25.84296 ? 134 ASP A CB  1 
ATOM   1024 C CG  . ASP A 1 134 ? -4.47245  40.61006 10.66802 1.000 26.64567 ? 134 ASP A CG  1 
ATOM   1025 O OD1 . ASP A 1 134 ? -5.31128  39.71975 10.41133 1.000 28.21713 ? 134 ASP A OD1 1 
ATOM   1026 O OD2 . ASP A 1 134 ? -3.65216  41.00886 9.81429  1.000 28.16338 ? 134 ASP A OD2 1 
ATOM   1027 N N   . ASP A 1 135 ? -7.33237  41.20329 12.57217 1.000 26.77608 ? 135 ASP A N   1 
ATOM   1028 C CA  . ASP A 1 135 ? -8.76636  41.04780 12.35797 1.000 27.86548 ? 135 ASP A CA  1 
ATOM   1029 C C   . ASP A 1 135 ? -9.09369  40.27414 11.08786 1.000 30.40329 ? 135 ASP A C   1 
ATOM   1030 O O   . ASP A 1 135 ? -10.24061 39.84201 10.92927 1.000 32.81598 ? 135 ASP A O   1 
ATOM   1031 C CB  . ASP A 1 135 ? -9.41836  42.42933 12.31605 1.000 29.30901 ? 135 ASP A CB  1 
ATOM   1032 C CG  . ASP A 1 135 ? -8.78517  43.32026 11.28348 1.000 34.98385 ? 135 ASP A CG  1 
ATOM   1033 O OD1 . ASP A 1 135 ? -7.59100  43.65715 11.43927 1.000 33.45347 ? 135 ASP A OD1 1 
ATOM   1034 O OD2 . ASP A 1 135 ? -9.47832  43.66861 10.30430 1.000 37.54151 ? 135 ASP A OD2 1 
ATOM   1035 N N   . LYS A 1 136 ? -8.13265  40.10268 10.18304 1.000 28.11421 ? 136 LYS A N   1 
ATOM   1036 C CA  . LYS A 1 136 ? -8.30090  39.24128 9.01731  1.000 29.66119 ? 136 LYS A CA  1 
ATOM   1037 C C   . LYS A 1 136 ? -7.88747  37.80366 9.29367  1.000 30.94413 ? 136 LYS A C   1 
ATOM   1038 O O   . LYS A 1 136 ? -7.95608  36.96854 8.38584  1.000 30.95956 ? 136 LYS A O   1 
ATOM   1039 C CB  . LYS A 1 136 ? -7.49056  39.77107 7.82648  1.000 29.12485 ? 136 LYS A CB  1 
ATOM   1040 C CG  . LYS A 1 136 ? -7.63445  41.25994 7.56839  1.000 39.93213 ? 136 LYS A CG  1 
ATOM   1041 C CD  . LYS A 1 136 ? -9.07874  41.64589 7.32657  1.000 44.00644 ? 136 LYS A CD  1 
ATOM   1042 C CE  . LYS A 1 136 ? -9.18322  43.09173 6.83365  1.000 48.50184 ? 136 LYS A CE  1 
ATOM   1043 N NZ  . LYS A 1 136 ? -7.90831  43.56984 6.21493  1.000 53.40037 ? 136 LYS A NZ  1 
ATOM   1044 N N   . GLY A 1 137 ? -7.43711  37.50351 10.50871 1.000 27.31912 ? 137 GLY A N   1 
ATOM   1045 C CA  . GLY A 1 137 ? -6.98812  36.16668 10.84312 1.000 26.46217 ? 137 GLY A CA  1 
ATOM   1046 C C   . GLY A 1 137 ? -5.54125  35.88230 10.52335 1.000 27.06140 ? 137 GLY A C   1 
ATOM   1047 O O   . GLY A 1 137 ? -5.11579  34.72423 10.64225 1.000 27.99230 ? 137 GLY A O   1 
ATOM   1048 N N   . ILE A 1 138 ? -4.76929  36.89537 10.11748 1.000 25.75503 ? 138 ILE A N   1 
ATOM   1049 C CA  . ILE A 1 138 ? -3.38283  36.70965 9.70890  1.000 27.85189 ? 138 ILE A CA  1 
ATOM   1050 C C   . ILE A 1 138 ? -2.48687  36.81606 10.93371 1.000 25.26251 ? 138 ILE A C   1 
ATOM   1051 O O   . ILE A 1 138 ? -2.63687  37.72605 11.76099 1.000 24.42380 ? 138 ILE A O   1 
ATOM   1052 C CB  . ILE A 1 138 ? -2.98196  37.74470 8.63842  1.000 26.54818 ? 138 ILE A CB  1 
ATOM   1053 C CG1 . ILE A 1 138 ? -3.87315  37.60431 7.39786  1.000 28.73786 ? 138 ILE A CG1 1 
ATOM   1054 C CG2 . ILE A 1 138 ? -1.53177  37.57636 8.24082  1.000 28.24429 ? 138 ILE A CG2 1 
ATOM   1055 C CD1 . ILE A 1 138 ? -3.66475  36.30868 6.65202  1.000 31.59152 ? 138 ILE A CD1 1 
ATOM   1056 N N   . LEU A 1 139 ? -1.53113  35.90529 11.03831 1.000 24.64488 ? 139 LEU A N   1 
ATOM   1057 C CA  . LEU A 1 139 ? -0.58759  35.95796 12.14684 1.000 23.63803 ? 139 LEU A CA  1 
ATOM   1058 C C   . LEU A 1 139 ? 0.41880   37.08494 11.94946 1.000 23.93650 ? 139 LEU A C   1 
ATOM   1059 O O   . LEU A 1 139 ? 1.10359   37.15172 10.92024 1.000 24.57534 ? 139 LEU A O   1 
ATOM   1060 C CB  . LEU A 1 139 ? 0.14067   34.62342 12.27176 1.000 23.58962 ? 139 LEU A CB  1 
ATOM   1061 C CG  . LEU A 1 139 ? 1.13618   34.53767 13.41971 1.000 24.29731 ? 139 LEU A CG  1 
ATOM   1062 C CD1 . LEU A 1 139 ? 0.39401   34.60625 14.74915 1.000 21.48582 ? 139 LEU A CD1 1 
ATOM   1063 C CD2 . LEU A 1 139 ? 1.88476   33.20851 13.27388 1.000 25.66619 ? 139 LEU A CD2 1 
ATOM   1064 N N   . ARG A 1 140 ? 0.53554   37.95610 12.96224 1.000 22.74397 ? 140 ARG A N   1 
ATOM   1065 C CA  . ARG A 1 140 ? 1.43287   39.09888 12.90115 1.000 22.23237 ? 140 ARG A CA  1 
ATOM   1066 C C   . ARG A 1 140 ? 2.64081   39.00121 13.82380 1.000 22.22611 ? 140 ARG A C   1 
ATOM   1067 O O   . ARG A 1 140 ? 3.64849   39.65699 13.55133 1.000 22.22153 ? 140 ARG A O   1 
ATOM   1068 C CB  . ARG A 1 140 ? 0.67692   40.39507 13.24365 1.000 22.88383 ? 140 ARG A CB  1 
ATOM   1069 C CG  . ARG A 1 140 ? -0.66646  40.57639 12.50632 1.000 26.56954 ? 140 ARG A CG  1 
ATOM   1070 C CD  . ARG A 1 140 ? -0.51310  40.54463 10.98455 1.000 28.70800 ? 140 ARG A CD  1 
ATOM   1071 N NE  . ARG A 1 140 ? 0.40091   41.56304 10.48151 1.000 28.39442 ? 140 ARG A NE  1 
ATOM   1072 C CZ  . ARG A 1 140 ? 0.07478   42.84709 10.31235 1.000 29.99579 ? 140 ARG A CZ  1 
ATOM   1073 N NH1 . ARG A 1 140 ? -1.15159  43.27588 10.60666 1.000 29.02325 ? 140 ARG A NH1 1 
ATOM   1074 N NH2 . ARG A 1 140 ? 0.97655   43.70175 9.84759  1.000 27.88430 ? 140 ARG A NH2 1 
ATOM   1075 N N   . GLN A 1 141 ? 2.57525   38.21004 14.89491 1.000 22.58071 ? 141 GLN A N   1 
ATOM   1076 C CA  . GLN A 1 141 ? 3.62821   38.23901 15.90445 1.000 22.46057 ? 141 GLN A CA  1 
ATOM   1077 C C   . GLN A 1 141 ? 3.68022   36.89767 16.61537 1.000 22.79423 ? 141 GLN A C   1 
ATOM   1078 O O   . GLN A 1 141 ? 2.63697   36.31886 16.93813 1.000 21.88137 ? 141 GLN A O   1 
ATOM   1079 C CB  . GLN A 1 141 ? 3.39234   39.36754 16.92340 1.000 23.00259 ? 141 GLN A CB  1 
ATOM   1080 C CG  . GLN A 1 141 ? 4.66929   39.88863 17.59159 1.000 22.36266 ? 141 GLN A CG  1 
ATOM   1081 C CD  . GLN A 1 141 ? 5.16628   39.01118 18.74498 1.000 24.66255 ? 141 GLN A CD  1 
ATOM   1082 O OE1 . GLN A 1 141 ? 4.42127   38.19974 19.32198 1.000 24.57995 ? 141 GLN A OE1 1 
ATOM   1083 N NE2 . GLN A 1 141 ? 6.43211   39.18531 19.09250 1.000 24.94901 ? 141 GLN A NE2 1 
ATOM   1084 N N   . ILE A 1 142 ? 4.90191   36.41882 16.85212 1.000 22.55004 ? 142 ILE A N   1 
ATOM   1085 C CA  . ILE A 1 142 ? 5.16964   35.16672 17.55587 1.000 21.81899 ? 142 ILE A CA  1 
ATOM   1086 C C   . ILE A 1 142 ? 6.06354   35.46379 18.75404 1.000 22.79795 ? 142 ILE A C   1 
ATOM   1087 O O   . ILE A 1 142 ? 7.12858   36.06913 18.59853 1.000 23.71238 ? 142 ILE A O   1 
ATOM   1088 C CB  . ILE A 1 142 ? 5.85810   34.14729 16.63358 1.000 21.11389 ? 142 ILE A CB  1 
ATOM   1089 C CG1 . ILE A 1 142 ? 4.94024   33.75826 15.47084 1.000 24.50164 ? 142 ILE A CG1 1 
ATOM   1090 C CG2 . ILE A 1 142 ? 6.32906   32.90810 17.42688 1.000 24.39911 ? 142 ILE A CG2 1 
ATOM   1091 C CD1 . ILE A 1 142 ? 5.66016   32.93891 14.39502 1.000 25.18723 ? 142 ILE A CD1 1 
ATOM   1092 N N   . THR A 1 143 ? 5.65224   35.00258 19.93451 1.000 23.38074 ? 143 THR A N   1 
ATOM   1093 C CA  . THR A 1 143 ? 6.45198   35.09598 21.15186 1.000 21.30971 ? 143 THR A CA  1 
ATOM   1094 C C   . THR A 1 143 ? 6.46038   33.72512 21.80819 1.000 21.74731 ? 143 THR A C   1 
ATOM   1095 O O   . THR A 1 143 ? 5.39333   33.16545 22.05756 1.000 23.86820 ? 143 THR A O   1 
ATOM   1096 C CB  . THR A 1 143 ? 5.86395   36.13988 22.11458 1.000 24.58250 ? 143 THR A CB  1 
ATOM   1097 O OG1 . THR A 1 143 ? 5.83810   37.42838 21.47588 1.000 22.47989 ? 143 THR A OG1 1 
ATOM   1098 C CG2 . THR A 1 143 ? 6.66038   36.22308 23.42377 1.000 23.34635 ? 143 THR A CG2 1 
ATOM   1099 N N   . VAL A 1 144 ? 7.64387   33.18306 22.09594 1.000 21.21630 ? 144 VAL A N   1 
ATOM   1100 C CA  . VAL A 1 144 ? 7.72727   31.90202 22.80556 1.000 21.46320 ? 144 VAL A CA  1 
ATOM   1101 C C   . VAL A 1 144 ? 8.79548   32.00513 23.88546 1.000 23.97254 ? 144 VAL A C   1 
ATOM   1102 O O   . VAL A 1 144 ? 9.96627   32.25924 23.57657 1.000 24.06059 ? 144 VAL A O   1 
ATOM   1103 C CB  . VAL A 1 144 ? 8.04256   30.72842 21.86715 1.000 22.71429 ? 144 VAL A CB  1 
ATOM   1104 C CG1 . VAL A 1 144 ? 7.78532   29.40195 22.59758 1.000 25.35011 ? 144 VAL A CG1 1 
ATOM   1105 C CG2 . VAL A 1 144 ? 7.20730   30.82207 20.60182 1.000 23.96522 ? 144 VAL A CG2 1 
ATOM   1106 N N   . ASN A 1 145 ? 8.39385   31.82103 25.14494 1.000 22.56265 ? 145 ASN A N   1 
ATOM   1107 C CA  . ASN A 1 145 ? 9.30414   31.82045 26.28311 1.000 22.29591 ? 145 ASN A CA  1 
ATOM   1108 C C   . ASN A 1 145 ? 9.48352   30.39821 26.78932 1.000 22.52098 ? 145 ASN A C   1 
ATOM   1109 O O   . ASN A 1 145 ? 8.51870   29.63431 26.86032 1.000 23.04262 ? 145 ASN A O   1 
ATOM   1110 C CB  . ASN A 1 145 ? 8.77666   32.64881 27.46353 1.000 20.70514 ? 145 ASN A CB  1 
ATOM   1111 C CG  . ASN A 1 145 ? 8.65770   34.12128 27.16490 1.000 23.22654 ? 145 ASN A CG  1 
ATOM   1112 O OD1 . ASN A 1 145 ? 8.88620   34.58045 26.04772 1.000 24.09571 ? 145 ASN A OD1 1 
ATOM   1113 N ND2 . ASN A 1 145 ? 8.28046   34.88019 28.18823 1.000 23.92598 ? 145 ASN A ND2 1 
ATOM   1114 N N   . ASP A 1 146 ? 10.70637  30.07111 27.19744 1.000 22.39472 ? 146 ASP A N   1 
ATOM   1115 C CA  . ASP A 1 146 ? 10.92701  28.87036 27.99337 1.000 22.19000 ? 146 ASP A CA  1 
ATOM   1116 C C   . ASP A 1 146 ? 10.04638  28.89622 29.24679 1.000 22.98745 ? 146 ASP A C   1 
ATOM   1117 O O   . ASP A 1 146 ? 9.56932   29.95087 29.68734 1.000 24.02578 ? 146 ASP A O   1 
ATOM   1118 C CB  . ASP A 1 146 ? 12.40519  28.76993 28.37678 1.000 23.66777 ? 146 ASP A CB  1 
ATOM   1119 C CG  . ASP A 1 146 ? 12.82176  27.36521 28.81608 1.000 24.69233 ? 146 ASP A CG  1 
ATOM   1120 O OD1 . ASP A 1 146 ? 11.98222  26.43428 28.83352 1.000 25.27725 ? 146 ASP A OD1 1 
ATOM   1121 O OD2 . ASP A 1 146 ? 14.01774  27.20473 29.14767 1.000 29.63343 ? 146 ASP A OD2 1 
ATOM   1122 N N   . LEU A 1 147 ? 9.85090   27.71432 29.83767 1.000 22.88390 ? 147 LEU A N   1 
ATOM   1123 C CA  . LEU A 1 147 ? 8.91579   27.56596 30.95489 1.000 21.85203 ? 147 LEU A CA  1 
ATOM   1124 C C   . LEU A 1 147 ? 9.10057   28.54381 32.11552 1.000 23.18188 ? 147 LEU A C   1 
ATOM   1125 O O   . LEU A 1 147 ? 8.08003   28.98821 32.67034 1.000 24.44836 ? 147 LEU A O   1 
ATOM   1126 C CB  . LEU A 1 147 ? 8.98615   26.12231 31.48839 1.000 23.49253 ? 147 LEU A CB  1 
ATOM   1127 C CG  . LEU A 1 147 ? 8.73567   25.04415 30.44078 1.000 23.88661 ? 147 LEU A CG  1 
ATOM   1128 C CD1 . LEU A 1 147 ? 8.84568   23.67147 31.09641 1.000 27.45284 ? 147 LEU A CD1 1 
ATOM   1129 C CD2 . LEU A 1 147 ? 7.37345   25.21519 29.78347 1.000 26.10135 ? 147 LEU A CD2 1 
ATOM   1130 N N   . PRO A 1 148 ? 10.31573  28.91465 32.54519 1.000 24.24241 ? 148 PRO A N   1 
ATOM   1131 C CA  . PRO A 1 148 ? 10.44267  29.66656 33.80870 1.000 24.94881 ? 148 PRO A CA  1 
ATOM   1132 C C   . PRO A 1 148 ? 10.00285  31.12355 33.76944 1.000 24.26616 ? 148 PRO A C   1 
ATOM   1133 O O   . PRO A 1 148 ? 9.86558   31.70670 34.85521 1.000 25.92801 ? 148 PRO A O   1 
ATOM   1134 C CB  . PRO A 1 148 ? 11.94646  29.59177 34.11473 1.000 28.03102 ? 148 PRO A CB  1 
ATOM   1135 C CG  . PRO A 1 148 ? 12.45112  28.43744 33.31985 1.000 27.84385 ? 148 PRO A CG  1 
ATOM   1136 C CD  . PRO A 1 148 ? 11.63643  28.46089 32.06806 1.000 23.25220 ? 148 PRO A CD  1 
ATOM   1137 N N   . VAL A 1 149 ? 9.81405   31.74504 32.59987 1.000 22.06787 ? 149 VAL A N   1 
ATOM   1138 C CA  . VAL A 1 149 ? 9.74083   33.20533 32.50325 1.000 22.35623 ? 149 VAL A CA  1 
ATOM   1139 C C   . VAL A 1 149 ? 8.43257   33.63104 31.84870 1.000 24.67754 ? 149 VAL A C   1 
ATOM   1140 O O   . VAL A 1 149 ? 8.11085   33.18648 30.74143 1.000 24.01416 ? 149 VAL A O   1 
ATOM   1141 C CB  . VAL A 1 149 ? 10.93856  33.78173 31.73025 1.000 23.53128 ? 149 VAL A CB  1 
ATOM   1142 C CG1 . VAL A 1 149 ? 10.72313  35.27639 31.42563 1.000 21.67276 ? 149 VAL A CG1 1 
ATOM   1143 C CG2 . VAL A 1 149 ? 12.21749  33.57865 32.53053 1.000 26.99277 ? 149 VAL A CG2 1 
ATOM   1144 N N   . GLY A 1 150 ? 7.71653   34.54662 32.51541 1.000 24.37451 ? 150 GLY A N   1 
ATOM   1145 C CA  . GLY A 1 150 ? 6.40940   34.97533 32.06440 1.000 27.18933 ? 150 GLY A CA  1 
ATOM   1146 C C   . GLY A 1 150 ? 6.44547   36.14886 31.09734 1.000 25.54085 ? 150 GLY A C   1 
ATOM   1147 O O   . GLY A 1 150 ? 7.48537   36.74141 30.81712 1.000 24.10800 ? 150 GLY A O   1 
ATOM   1148 N N   . ARG A 1 151 ? 5.26807   36.46649 30.57965 1.000 23.11463 ? 151 ARG A N   1 
ATOM   1149 C CA  . ARG A 1 151 ? 5.08477   37.50721 29.57922 1.000 22.87657 ? 151 ARG A CA  1 
ATOM   1150 C C   . ARG A 1 151 ? 4.57990   38.79013 30.23024 1.000 24.09596 ? 151 ARG A C   1 
ATOM   1151 O O   . ARG A 1 151 ? 4.18529   38.81245 31.39105 1.000 25.94280 ? 151 ARG A O   1 
ATOM   1152 C CB  . ARG A 1 151 ? 4.12603   37.01054 28.49601 1.000 23.87954 ? 151 ARG A CB  1 
ATOM   1153 C CG  . ARG A 1 151 ? 4.79772   35.90641 27.69544 1.000 26.79750 ? 151 ARG A CG  1 
ATOM   1154 C CD  . ARG A 1 151 ? 3.85864   34.88134 27.16020 1.000 27.82221 ? 151 ARG A CD  1 
ATOM   1155 N NE  . ARG A 1 151 ? 3.28892   34.03407 28.20112 1.000 22.17317 ? 151 ARG A NE  1 
ATOM   1156 C CZ  . ARG A 1 151 ? 2.56220   32.95645 27.91771 1.000 23.18992 ? 151 ARG A CZ  1 
ATOM   1157 N NH1 . ARG A 1 151 ? 2.35809   32.63362 26.64355 1.000 26.32458 ? 151 ARG A NH1 1 
ATOM   1158 N NH2 . ARG A 1 151 ? 2.03306   32.22673 28.88756 1.000 22.71912 ? 151 ARG A NH2 1 
ATOM   1159 N N   . SER A 1 152 ? 4.59388   39.86634 29.45089 1.000 21.94816 ? 152 SER A N   1 
ATOM   1160 C CA  . SER A 1 152 ? 4.22623   41.21128 29.89997 1.000 21.29506 ? 152 SER A CA  1 
ATOM   1161 C C   . SER A 1 152 ? 2.97836   41.68641 29.16951 1.000 22.25293 ? 152 SER A C   1 
ATOM   1162 O O   . SER A 1 152 ? 2.95644   41.71868 27.93399 1.000 22.60881 ? 152 SER A O   1 
ATOM   1163 C CB  . SER A 1 152 ? 5.37262   42.19730 29.64417 1.000 22.31626 ? 152 SER A CB  1 
ATOM   1164 O OG  . SER A 1 152 ? 4.90257   43.55045 29.60930 1.000 21.66568 ? 152 SER A OG  1 
ATOM   1165 N N   . VAL A 1 153 ? 1.95222   42.07745 29.93182 1.000 20.24688 ? 153 VAL A N   1 
ATOM   1166 C CA  . VAL A 1 153 ? 0.76929   42.67445 29.32082 1.000 20.11832 ? 153 VAL A CA  1 
ATOM   1167 C C   . VAL A 1 153 ? 1.11195   44.00037 28.64244 1.000 20.88662 ? 153 VAL A C   1 
ATOM   1168 O O   . VAL A 1 153 ? 0.60424   44.29873 27.55265 1.000 21.69417 ? 153 VAL A O   1 
ATOM   1169 C CB  . VAL A 1 153 ? -0.33889  42.84758 30.37322 1.000 22.18764 ? 153 VAL A CB  1 
ATOM   1170 C CG1 . VAL A 1 153 ? -1.50544  43.63095 29.77286 1.000 25.27548 ? 153 VAL A CG1 1 
ATOM   1171 C CG2 . VAL A 1 153 ? -0.79727  41.47769 30.88212 1.000 25.94821 ? 153 VAL A CG2 1 
ATOM   1172 N N   . ASP A 1 154 ? 1.95751   44.82399 29.27473 1.000 23.63687 ? 154 ASP A N   1 
ATOM   1173 C CA  . ASP A 1 154 ? 2.34990   46.09305 28.66141 1.000 24.73190 ? 154 ASP A CA  1 
ATOM   1174 C C   . ASP A 1 154 ? 2.93961   45.86938 27.27633 1.000 21.88531 ? 154 ASP A C   1 
ATOM   1175 O O   . ASP A 1 154 ? 2.60149   46.57638 26.31561 1.000 21.71867 ? 154 ASP A O   1 
ATOM   1176 C CB  . ASP A 1 154 ? 3.38568   46.81541 29.53116 1.000 24.41076 ? 154 ASP A CB  1 
ATOM   1177 C CG  . ASP A 1 154 ? 2.78339   47.50931 30.73669 1.000 32.76332 ? 154 ASP A CG  1 
ATOM   1178 O OD1 . ASP A 1 154 ? 1.55089   47.66996 30.81269 1.000 31.83838 ? 154 ASP A OD1 1 
ATOM   1179 O OD2 . ASP A 1 154 ? 3.57642   47.93843 31.60512 1.000 36.44463 ? 154 ASP A OD2 1 
ATOM   1180 N N   . GLU A 1 155 ? 3.87166   44.91550 27.17005 1.000 23.55628 ? 155 GLU A N   1 
ATOM   1181 C CA  . GLU A 1 155 ? 4.50145   44.63831 25.88385 1.000 23.17682 ? 155 GLU A CA  1 
ATOM   1182 C C   . GLU A 1 155 ? 3.47228   44.15796 24.87445 1.000 22.12908 ? 155 GLU A C   1 
ATOM   1183 O O   . GLU A 1 155 ? 3.50178   44.56114 23.70501 1.000 22.56758 ? 155 GLU A O   1 
ATOM   1184 C CB  . GLU A 1 155 ? 5.61689   43.59458 26.04200 1.000 22.44581 ? 155 GLU A CB  1 
ATOM   1185 C CG  . GLU A 1 155 ? 6.23114   43.14510 24.72338 1.000 23.75733 ? 155 GLU A CG  1 
ATOM   1186 C CD  . GLU A 1 155 ? 7.04358   44.21234 23.98356 1.000 23.39094 ? 155 GLU A CD  1 
ATOM   1187 O OE1 . GLU A 1 155 ? 7.06945   45.40085 24.39478 1.000 23.53382 ? 155 GLU A OE1 1 
ATOM   1188 O OE2 . GLU A 1 155 ? 7.66390   43.85138 22.96274 1.000 25.58029 ? 155 GLU A OE2 1 
ATOM   1189 N N   . THR A 1 156 ? 2.54988   43.29854 25.31277 1.000 21.76542 ? 156 THR A N   1 
ATOM   1190 C CA  . THR A 1 156 ? 1.52702   42.79349 24.40263 1.000 19.88843 ? 156 THR A CA  1 
ATOM   1191 C C   . THR A 1 156 ? 0.63170   43.91842 23.89801 1.000 21.25652 ? 156 THR A C   1 
ATOM   1192 O O   . THR A 1 156 ? 0.30624   43.98075 22.70595 1.000 21.20066 ? 156 THR A O   1 
ATOM   1193 C CB  . THR A 1 156 ? 0.70690   41.72009 25.10456 1.000 21.77688 ? 156 THR A CB  1 
ATOM   1194 O OG1 . THR A 1 156 ? 1.60706   40.74459 25.65441 1.000 21.32523 ? 156 THR A OG1 1 
ATOM   1195 C CG2 . THR A 1 156 ? -0.22328  41.03502 24.11539 1.000 21.60794 ? 156 THR A CG2 1 
ATOM   1196 N N   . LEU A 1 157 ? 0.21828   44.81377 24.79530 1.000 21.17882 ? 157 LEU A N   1 
ATOM   1197 C CA  . LEU A 1 157 ? -0.57776  45.96262 24.37072 1.000 23.02324 ? 157 LEU A CA  1 
ATOM   1198 C C   . LEU A 1 157 ? 0.19678   46.83936 23.39653 1.000 23.74146 ? 157 LEU A C   1 
ATOM   1199 O O   . LEU A 1 157 ? -0.36851  47.33172 22.41042 1.000 21.71233 ? 157 LEU A O   1 
ATOM   1200 C CB  . LEU A 1 157 ? -1.01616  46.77995 25.59053 1.000 20.82724 ? 157 LEU A CB  1 
ATOM   1201 C CG  . LEU A 1 157 ? -2.09637  46.13459 26.45200 1.000 22.63972 ? 157 LEU A CG  1 
ATOM   1202 C CD1 . LEU A 1 157 ? -2.13622  46.78947 27.82006 1.000 24.49060 ? 157 LEU A CD1 1 
ATOM   1203 C CD2 . LEU A 1 157 ? -3.46990  46.21173 25.77025 1.000 24.85718 ? 157 LEU A CD2 1 
ATOM   1204 N N   . ARG A 1 158 ? 1.49266   47.05169 23.65593 1.000 21.68812 ? 158 ARG A N   1 
ATOM   1205 C CA  . ARG A 1 158 ? 2.29749   47.85985 22.74450 1.000 21.98946 ? 158 ARG A CA  1 
ATOM   1206 C C   . ARG A 1 158 ? 2.25925   47.28025 21.33694 1.000 23.45831 ? 158 ARG A C   1 
ATOM   1207 O O   . ARG A 1 158 ? 2.06300   48.00597 20.35134 1.000 22.58127 ? 158 ARG A O   1 
ATOM   1208 C CB  . ARG A 1 158 ? 3.74030   47.95412 23.24814 1.000 23.15322 ? 158 ARG A CB  1 
ATOM   1209 C CG  . ARG A 1 158 ? 4.64627   48.74924 22.32175 1.000 22.85214 ? 158 ARG A CG  1 
ATOM   1210 C CD  . ARG A 1 158 ? 6.11780   48.63637 22.70754 1.000 24.89963 ? 158 ARG A CD  1 
ATOM   1211 N NE  . ARG A 1 158 ? 6.70092   47.34284 22.33676 1.000 22.32009 ? 158 ARG A NE  1 
ATOM   1212 C CZ  . ARG A 1 158 ? 7.16420   47.04267 21.12308 1.000 25.71053 ? 158 ARG A CZ  1 
ATOM   1213 N NH1 . ARG A 1 158 ? 7.10695   47.94279 20.14039 1.000 27.74976 ? 158 ARG A NH1 1 
ATOM   1214 N NH2 . ARG A 1 158 ? 7.68779   45.83859 20.89321 1.000 23.98995 ? 158 ARG A NH2 1 
ATOM   1215 N N   . LEU A 1 159 ? 2.42204   45.95615 21.22999 1.000 21.27694 ? 159 LEU A N   1 
ATOM   1216 C CA  . LEU A 1 159 ? 2.45098   45.31374 19.92274 1.000 22.07864 ? 159 LEU A CA  1 
ATOM   1217 C C   . LEU A 1 159 ? 1.08840   45.37439 19.24019 1.000 20.34624 ? 159 LEU A C   1 
ATOM   1218 O O   . LEU A 1 159 ? 0.99984   45.66753 18.04348 1.000 22.07587 ? 159 LEU A O   1 
ATOM   1219 C CB  . LEU A 1 159 ? 2.91369   43.86105 20.07251 1.000 20.77980 ? 159 LEU A CB  1 
ATOM   1220 C CG  . LEU A 1 159 ? 4.37523   43.67802 20.48591 1.000 22.64925 ? 159 LEU A CG  1 
ATOM   1221 C CD1 . LEU A 1 159 ? 4.57762   42.26076 21.04797 1.000 20.62440 ? 159 LEU A CD1 1 
ATOM   1222 C CD2 . LEU A 1 159 ? 5.29859   43.92356 19.29088 1.000 24.43258 ? 159 LEU A CD2 1 
ATOM   1223 N N   . VAL A 1 160 ? 0.01729   45.06548 19.97151 1.000 21.29297 ? 160 VAL A N   1 
ATOM   1224 C CA  . VAL A 1 160 ? -1.30777  45.08379 19.35552 1.000 21.04911 ? 160 VAL A CA  1 
ATOM   1225 C C   . VAL A 1 160 ? -1.60652  46.46719 18.79860 1.000 24.40740 ? 160 VAL A C   1 
ATOM   1226 O O   . VAL A 1 160 ? -1.99759  46.62355 17.63751 1.000 23.02436 ? 160 VAL A O   1 
ATOM   1227 C CB  . VAL A 1 160 ? -2.38450  44.65335 20.35955 1.000 21.36600 ? 160 VAL A CB  1 
ATOM   1228 C CG1 . VAL A 1 160 ? -3.76199  44.93714 19.77503 1.000 23.29294 ? 160 VAL A CG1 1 
ATOM   1229 C CG2 . VAL A 1 160 ? -2.23681  43.14707 20.66001 1.000 20.29866 ? 160 VAL A CG2 1 
ATOM   1230 N N   . GLN A 1 161 ? -1.39317  47.49276 19.61552 1.000 22.54179 ? 161 GLN A N   1 
ATOM   1231 C CA  . GLN A 1 161 ? -1.68298  48.84916 19.16295 1.000 22.45494 ? 161 GLN A CA  1 
ATOM   1232 C C   . GLN A 1 161 ? -0.82351  49.23479 17.95947 1.000 23.05173 ? 161 GLN A C   1 
ATOM   1233 O O   . GLN A 1 161 ? -1.32386  49.82074 16.99096 1.000 24.21511 ? 161 GLN A O   1 
ATOM   1234 C CB  . GLN A 1 161 ? -1.47728  49.82165 20.31516 1.000 23.55176 ? 161 GLN A CB  1 
ATOM   1235 C CG  . GLN A 1 161 ? -1.85840  51.23359 19.94653 1.000 27.39615 ? 161 GLN A CG  1 
ATOM   1236 C CD  . GLN A 1 161 ? -1.59961  52.19700 21.07237 1.000 30.25094 ? 161 GLN A CD  1 
ATOM   1237 O OE1 . GLN A 1 161 ? -2.53167  52.74179 21.65698 1.000 33.72457 ? 161 GLN A OE1 1 
ATOM   1238 N NE2 . GLN A 1 161 ? -0.32829  52.40545 21.39329 1.000 33.88261 ? 161 GLN A NE2 1 
ATOM   1239 N N   . ALA A 1 162 ? 0.46655   48.89352 17.99058 1.000 22.42487 ? 162 ALA A N   1 
ATOM   1240 C CA  . ALA A 1 162 ? 1.36260   49.25775 16.89797 1.000 25.02265 ? 162 ALA A CA  1 
ATOM   1241 C C   . ALA A 1 162 ? 0.97875   48.56650 15.58947 1.000 24.51000 ? 162 ALA A C   1 
ATOM   1242 O O   . ALA A 1 162 ? 1.05654   49.17723 14.51657 1.000 25.88409 ? 162 ALA A O   1 
ATOM   1243 C CB  . ALA A 1 162 ? 2.80830   48.93220 17.27651 1.000 23.56444 ? 162 ALA A CB  1 
ATOM   1244 N N   . PHE A 1 163 ? 0.57961   47.29046 15.64325 1.000 21.89190 ? 163 PHE A N   1 
ATOM   1245 C CA  . PHE A 1 163 ? 0.12497   46.64327 14.41403 1.000 22.78965 ? 163 PHE A CA  1 
ATOM   1246 C C   . PHE A 1 163 ? -1.12335  47.32825 13.87147 1.000 23.18712 ? 163 PHE A C   1 
ATOM   1247 O O   . PHE A 1 163 ? -1.26047  47.51444 12.65585 1.000 26.33502 ? 163 PHE A O   1 
ATOM   1248 C CB  . PHE A 1 163 ? -0.14169  45.14513 14.64049 1.000 21.76836 ? 163 PHE A CB  1 
ATOM   1249 C CG  . PHE A 1 163 ? 1.10703   44.31171 14.64262 1.000 24.28636 ? 163 PHE A CG  1 
ATOM   1250 C CD1 . PHE A 1 163 ? 1.87924   44.19704 13.49210 1.000 26.36305 ? 163 PHE A CD1 1 
ATOM   1251 C CD2 . PHE A 1 163 ? 1.52728   43.66975 15.80341 1.000 25.76690 ? 163 PHE A CD2 1 
ATOM   1252 C CE1 . PHE A 1 163 ? 3.05271   43.45357 13.50063 1.000 26.34434 ? 163 PHE A CE1 1 
ATOM   1253 C CE2 . PHE A 1 163 ? 2.69573   42.92862 15.81734 1.000 26.91791 ? 163 PHE A CE2 1 
ATOM   1254 C CZ  . PHE A 1 163 ? 3.45288   42.82042 14.66128 1.000 26.71274 ? 163 PHE A CZ  1 
ATOM   1255 N N   . GLN A 1 164 ? -2.04272  47.71681 14.75808 1.000 23.54243 ? 164 GLN A N   1 
ATOM   1256 C CA  . GLN A 1 164 ? -3.27226  48.35618 14.30241 1.000 22.90544 ? 164 GLN A CA  1 
ATOM   1257 C C   . GLN A 1 164 ? -2.97796  49.72306 13.69861 1.000 25.66790 ? 164 GLN A C   1 
ATOM   1258 O O   . GLN A 1 164 ? -3.59813  50.11926 12.70554 1.000 26.14791 ? 164 GLN A O   1 
ATOM   1259 C CB  . GLN A 1 164 ? -4.25449  48.48614 15.46210 1.000 24.54515 ? 164 GLN A CB  1 
ATOM   1260 C CG  . GLN A 1 164 ? -4.79927  47.14895 15.94944 1.000 23.11357 ? 164 GLN A CG  1 
ATOM   1261 C CD  . GLN A 1 164 ? -5.65439  47.29053 17.18884 1.000 26.60213 ? 164 GLN A CD  1 
ATOM   1262 O OE1 . GLN A 1 164 ? -5.51960  48.25676 17.94641 1.000 28.95155 ? 164 GLN A OE1 1 
ATOM   1263 N NE2 . GLN A 1 164 ? -6.54454  46.32535 17.41231 1.000 26.23552 ? 164 GLN A NE2 1 
ATOM   1264 N N   . PHE A 1 165 ? -2.01730  50.44470 14.27187 1.000 23.97405 ? 165 PHE A N   1 
ATOM   1265 C CA  . PHE A 1 165 ? -1.65942  51.74272 13.70646 1.000 25.71589 ? 165 PHE A CA  1 
ATOM   1266 C C   . PHE A 1 165 ? -1.02104  51.58763 12.33064 1.000 26.97944 ? 165 PHE A C   1 
ATOM   1267 O O   . PHE A 1 165 ? -1.32003  52.35601 11.40927 1.000 27.91866 ? 165 PHE A O   1 
ATOM   1268 C CB  . PHE A 1 165 ? -0.71815  52.48398 14.65498 1.000 24.95634 ? 165 PHE A CB  1 
ATOM   1269 C CG  . PHE A 1 165 ? -1.39587  53.04465 15.87997 1.000 27.92209 ? 165 PHE A CG  1 
ATOM   1270 C CD1 . PHE A 1 165 ? -2.77494  53.08707 15.97546 1.000 30.44185 ? 165 PHE A CD1 1 
ATOM   1271 C CD2 . PHE A 1 165 ? -0.64131  53.51861 16.93823 1.000 31.32732 ? 165 PHE A CD2 1 
ATOM   1272 C CE1 . PHE A 1 165 ? -3.39215  53.61148 17.10798 1.000 31.61203 ? 165 PHE A CE1 1 
ATOM   1273 C CE2 . PHE A 1 165 ? -1.24760  54.03582 18.06984 1.000 27.84790 ? 165 PHE A CE2 1 
ATOM   1274 C CZ  . PHE A 1 165 ? -2.61704  54.09192 18.15143 1.000 28.27370 ? 165 PHE A CZ  1 
ATOM   1275 N N   . THR A 1 166 ? -0.13952  50.60125 12.16433 1.000 25.46490 ? 166 THR A N   1 
ATOM   1276 C CA  . THR A 1 166 ? 0.49184   50.43330 10.86274 1.000 26.41895 ? 166 THR A CA  1 
ATOM   1277 C C   . THR A 1 166 ? -0.47855  49.83556 9.84719  1.000 28.40162 ? 166 THR A C   1 
ATOM   1278 O O   . THR A 1 166 ? -0.32207  50.07084 8.64273  1.000 32.58984 ? 166 THR A O   1 
ATOM   1279 C CB  . THR A 1 166 ? 1.76318   49.58832 10.98631 1.000 30.97484 ? 166 THR A CB  1 
ATOM   1280 O OG1 . THR A 1 166 ? 1.46395   48.35170 11.64727 1.000 28.64061 ? 166 THR A OG1 1 
ATOM   1281 C CG2 . THR A 1 166 ? 2.81646   50.34337 11.78614 1.000 31.00797 ? 166 THR A CG2 1 
ATOM   1282 N N   . ASP A 1 167 ? -1.48636  49.08107 10.31043 1.000 26.50633 ? 167 ASP A N   1 
ATOM   1283 C CA  . ASP A 1 167 ? -2.55661  48.63103 9.42586  1.000 28.23036 ? 167 ASP A CA  1 
ATOM   1284 C C   . ASP A 1 167 ? -3.22712  49.81588 8.74111  1.000 30.83435 ? 167 ASP A C   1 
ATOM   1285 O O   . ASP A 1 167 ? -3.58482  49.74407 7.55939  1.000 32.88722 ? 167 ASP A O   1 
ATOM   1286 C CB  . ASP A 1 167 ? -3.61559  47.84982 10.21110 1.000 28.05586 ? 167 ASP A CB  1 
ATOM   1287 C CG  . ASP A 1 167 ? -3.20072  46.41289 10.54070 1.000 29.16100 ? 167 ASP A CG  1 
ATOM   1288 O OD1 . ASP A 1 167 ? -2.17792  45.92403 10.01787 1.000 29.77337 ? 167 ASP A OD1 1 
ATOM   1289 O OD2 . ASP A 1 167 ? -3.92692  45.78318 11.34462 1.000 29.38311 ? 167 ASP A OD2 1 
ATOM   1290 N N   . LYS A 1 168 ? -3.42804  50.90762 9.48157  1.000 31.03959 ? 168 LYS A N   1 
ATOM   1291 C CA  . LYS A 1 168 ? -4.21048  52.02074 8.95907  1.000 33.63160 ? 168 LYS A CA  1 
ATOM   1292 C C   . LYS A 1 168 ? -3.36197  52.95261 8.10553  1.000 35.36274 ? 168 LYS A C   1 
ATOM   1293 O O   . LYS A 1 168 ? -3.84362  53.47799 7.09535  1.000 36.08755 ? 168 LYS A O   1 
ATOM   1294 C CB  . LYS A 1 168 ? -4.87245  52.78093 10.11076 1.000 33.43610 ? 168 LYS A CB  1 
ATOM   1295 C CG  . LYS A 1 168 ? -6.25346  52.22389 10.48478 1.000 39.08324 ? 168 LYS A CG  1 
ATOM   1296 C CD  . LYS A 1 168 ? -6.40812  52.05222 11.98260 1.000 40.83777 ? 168 LYS A CD  1 
ATOM   1297 C CE  . LYS A 1 168 ? -7.61001  51.17426 12.32536 1.000 47.53732 ? 168 LYS A CE  1 
ATOM   1298 N NZ  . LYS A 1 168 ? -7.54516  50.66678 13.73752 1.000 48.61198 ? 168 LYS A NZ  1 
ATOM   1299 N N   . HIS A 1 169 ? -2.10211  53.16653 8.48027  1.000 33.56225 ? 169 HIS A N   1 
ATOM   1300 C CA  . HIS A 1 169 ? -1.23472  54.04971 7.71145  1.000 35.59393 ? 169 HIS A CA  1 
ATOM   1301 C C   . HIS A 1 169 ? 0.18937   53.52291 7.76501  1.000 41.20613 ? 169 HIS A C   1 
ATOM   1302 O O   . HIS A 1 169 ? 0.71733   53.27201 8.85073  1.000 41.23232 ? 169 HIS A O   1 
ATOM   1303 C CB  . HIS A 1 169 ? -1.31492  55.48839 8.23999  1.000 37.15209 ? 169 HIS A CB  1 
ATOM   1304 C CG  . HIS A 1 169 ? -2.62131  56.14721 7.93554  1.000 36.60798 ? 169 HIS A CG  1 
ATOM   1305 N ND1 . HIS A 1 169 ? -3.58709  56.37237 8.89337  1.000 35.05208 ? 169 HIS A ND1 1 
ATOM   1306 C CD2 . HIS A 1 169 ? -3.14803  56.56927 6.76284  1.000 32.36569 ? 169 HIS A CD2 1 
ATOM   1307 C CE1 . HIS A 1 169 ? -4.64266  56.92794 8.32529  1.000 29.15524 ? 169 HIS A CE1 1 
ATOM   1308 N NE2 . HIS A 1 169 ? -4.40134  57.06112 7.03478  1.000 34.29660 ? 169 HIS A NE2 1 
ATOM   1309 N N   . GLY A 1 170 ? 0.79707   53.34819 6.59462  1.000 51.10960 ? 170 GLY A N   1 
ATOM   1310 C CA  . GLY A 1 170 ? 2.15982   52.85182 6.50325  1.000 52.46489 ? 170 GLY A CA  1 
ATOM   1311 C C   . GLY A 1 170 ? 2.43861   52.08400 5.22567  1.000 58.00827 ? 170 GLY A C   1 
ATOM   1312 O O   . GLY A 1 170 ? 3.57154   52.06591 4.73750  1.000 68.51547 ? 170 GLY A O   1 
ATOM   1313 N N   . SER B 1 3   ? 10.26351  24.56238 9.43942  1.000 55.46050 ? 3   SER B N   1 
ATOM   1314 C CA  . SER B 1 3   ? 11.15992  25.58718 8.92026  1.000 55.51865 ? 3   SER B CA  1 
ATOM   1315 C C   . SER B 1 3   ? 12.02741  26.17358 10.03247 1.000 51.09564 ? 3   SER B C   1 
ATOM   1316 O O   . SER B 1 3   ? 11.53499  26.86404 10.92860 1.000 52.47627 ? 3   SER B O   1 
ATOM   1317 N N   . GLY B 1 4   ? 13.31975  25.88632 9.97444  1.000 50.39007 ? 4   GLY B N   1 
ATOM   1318 C CA  . GLY B 1 4   ? 14.25242  26.40703 10.94699 1.000 44.14081 ? 4   GLY B CA  1 
ATOM   1319 C C   . GLY B 1 4   ? 14.60022  25.38988 12.02129 1.000 44.43973 ? 4   GLY B C   1 
ATOM   1320 O O   . GLY B 1 4   ? 13.88594  24.41228 12.26012 1.000 44.81699 ? 4   GLY B O   1 
ATOM   1321 N N   . ASN B 1 5   ? 15.72668  25.64179 12.68682 1.000 38.59614 ? 5   ASN B N   1 
ATOM   1322 C CA  . ASN B 1 5   ? 16.23470  24.76469 13.73224 1.000 39.24859 ? 5   ASN B CA  1 
ATOM   1323 C C   . ASN B 1 5   ? 16.29810  25.44612 15.09444 1.000 37.05630 ? 5   ASN B C   1 
ATOM   1324 O O   . ASN B 1 5   ? 16.92998  24.91195 16.01371 1.000 37.77454 ? 5   ASN B O   1 
ATOM   1325 C CB  . ASN B 1 5   ? 17.61519  24.23697 13.33912 1.000 39.43325 ? 5   ASN B CB  1 
ATOM   1326 C CG  . ASN B 1 5   ? 17.59080  23.50482 12.01772 1.000 45.91324 ? 5   ASN B CG  1 
ATOM   1327 O OD1 . ASN B 1 5   ? 16.75199  22.62803 11.80311 1.000 46.92428 ? 5   ASN B OD1 1 
ATOM   1328 N ND2 . ASN B 1 5   ? 18.49899  23.86686 11.11800 1.000 44.84210 ? 5   ASN B ND2 1 
ATOM   1329 N N   . ALA B 1 6   ? 15.66395  26.60700 15.25157 1.000 34.63612 ? 6   ALA B N   1 
ATOM   1330 C CA  . ALA B 1 6   ? 15.63183  27.29588 16.53827 1.000 32.86039 ? 6   ALA B CA  1 
ATOM   1331 C C   . ALA B 1 6   ? 14.53647  26.68308 17.40428 1.000 35.25213 ? 6   ALA B C   1 
ATOM   1332 O O   . ALA B 1 6   ? 13.34554  26.88447 17.14469 1.000 36.43355 ? 6   ALA B O   1 
ATOM   1333 C CB  . ALA B 1 6   ? 15.39919  28.79135 16.33360 1.000 31.25391 ? 6   ALA B CB  1 
ATOM   1334 N N   . LYS B 1 7   ? 14.93387  25.93751 18.43681 1.000 27.98495 ? 7   LYS B N   1 
ATOM   1335 C CA  . LYS B 1 7   ? 14.00437  25.24238 19.32081 1.000 31.09721 ? 7   LYS B CA  1 
ATOM   1336 C C   . LYS B 1 7   ? 14.29494  25.61757 20.76669 1.000 26.37124 ? 7   LYS B C   1 
ATOM   1337 O O   . LYS B 1 7   ? 15.44122  25.51144 21.21418 1.000 26.78497 ? 7   LYS B O   1 
ATOM   1338 C CB  . LYS B 1 7   ? 14.12280  23.71676 19.17230 1.000 31.85090 ? 7   LYS B CB  1 
ATOM   1339 C CG  . LYS B 1 7   ? 13.84996  23.15477 17.78336 1.000 38.87727 ? 7   LYS B CG  1 
ATOM   1340 C CD  . LYS B 1 7   ? 14.39207  21.71776 17.70625 1.000 44.10408 ? 7   LYS B CD  1 
ATOM   1341 C CE  . LYS B 1 7   ? 14.57814  21.25138 16.26365 1.000 53.82262 ? 7   LYS B CE  1 
ATOM   1342 N NZ  . LYS B 1 7   ? 15.84179  20.47188 16.06621 1.000 55.77875 ? 7   LYS B NZ  1 
ATOM   1343 N N   . ILE B 1 8   ? 13.25690  26.03659 21.49822 1.000 27.35688 ? 8   ILE B N   1 
ATOM   1344 C CA  . ILE B 1 8   ? 13.42273  26.36626 22.91148 1.000 26.12643 ? 8   ILE B CA  1 
ATOM   1345 C C   . ILE B 1 8   ? 13.96251  25.15469 23.65932 1.000 27.34806 ? 8   ILE B C   1 
ATOM   1346 O O   . ILE B 1 8   ? 13.50733  24.02377 23.45043 1.000 25.74087 ? 8   ILE B O   1 
ATOM   1347 C CB  . ILE B 1 8   ? 12.08462  26.82000 23.52467 1.000 24.99373 ? 8   ILE B CB  1 
ATOM   1348 C CG1 . ILE B 1 8   ? 11.49966  28.02716 22.76809 1.000 27.78286 ? 8   ILE B CG1 1 
ATOM   1349 C CG2 . ILE B 1 8   ? 12.24703  27.10246 25.02224 1.000 25.24395 ? 8   ILE B CG2 1 
ATOM   1350 C CD1 . ILE B 1 8   ? 12.23088  29.32313 23.01998 1.000 28.37935 ? 8   ILE B CD1 1 
ATOM   1351 N N   . GLY B 1 9   ? 14.94684  25.38244 24.53027 1.000 26.49994 ? 9   GLY B N   1 
ATOM   1352 C CA  . GLY B 1 9   ? 15.51741  24.31467 25.33077 1.000 29.28239 ? 9   GLY B CA  1 
ATOM   1353 C C   . GLY B 1 9   ? 16.58006  23.49538 24.63275 1.000 32.35636 ? 9   GLY B C   1 
ATOM   1354 O O   . GLY B 1 9   ? 17.14869  22.58180 25.25214 1.000 35.77287 ? 9   GLY B O   1 
ATOM   1355 N N   . HIS B 1 10  ? 16.86528  23.78754 23.37129 1.000 28.84531 ? 10  HIS B N   1 
ATOM   1356 C CA  . HIS B 1 10  ? 17.88359  23.11801 22.58311 1.000 31.17307 ? 10  HIS B CA  1 
ATOM   1357 C C   . HIS B 1 10  ? 18.97003  24.11919 22.21722 1.000 31.13209 ? 10  HIS B C   1 
ATOM   1358 O O   . HIS B 1 10  ? 18.74345  25.33581 22.26534 1.000 29.46924 ? 10  HIS B O   1 
ATOM   1359 C CB  . HIS B 1 10  ? 17.26896  22.50664 21.31414 1.000 32.90274 ? 10  HIS B CB  1 
ATOM   1360 C CG  . HIS B 1 10  ? 16.31898  21.38112 21.58902 1.000 38.78865 ? 10  HIS B CG  1 
ATOM   1361 N ND1 . HIS B 1 10  ? 16.51776  20.10342 21.10665 1.000 41.45327 ? 10  HIS B ND1 1 
ATOM   1362 C CD2 . HIS B 1 10  ? 15.16563  21.33958 22.29994 1.000 37.50150 ? 10  HIS B CD2 1 
ATOM   1363 C CE1 . HIS B 1 10  ? 15.52893  19.32399 21.50934 1.000 45.45531 ? 10  HIS B CE1 1 
ATOM   1364 N NE2 . HIS B 1 10  ? 14.69613  20.04795 22.23686 1.000 40.92799 ? 10  HIS B NE2 1 
ATOM   1365 N N   . PRO B 1 11  ? 20.16824  23.65172 21.86981 1.000 31.32199 ? 11  PRO B N   1 
ATOM   1366 C CA  . PRO B 1 11  ? 21.24393  24.58622 21.51297 1.000 29.75957 ? 11  PRO B CA  1 
ATOM   1367 C C   . PRO B 1 11  ? 20.83578  25.48417 20.35385 1.000 28.76852 ? 11  PRO B C   1 
ATOM   1368 O O   . PRO B 1 11  ? 20.29611  25.02318 19.34502 1.000 30.40682 ? 11  PRO B O   1 
ATOM   1369 C CB  . PRO B 1 11  ? 22.40421  23.65697 21.13310 1.000 32.28987 ? 11  PRO B CB  1 
ATOM   1370 C CG  . PRO B 1 11  ? 22.14175  22.42676 21.90358 1.000 29.95982 ? 11  PRO B CG  1 
ATOM   1371 C CD  . PRO B 1 11  ? 20.65115  22.25821 21.90179 1.000 32.16166 ? 11  PRO B CD  1 
ATOM   1372 N N   . ALA B 1 12  ? 21.05468  26.78136 20.52442 1.000 27.97938 ? 12  ALA B N   1 
ATOM   1373 C CA  . ALA B 1 12  ? 20.76378  27.70484 19.44306 1.000 27.30766 ? 12  ALA B CA  1 
ATOM   1374 C C   . ALA B 1 12  ? 21.65521  27.37674 18.24869 1.000 27.18328 ? 12  ALA B C   1 
ATOM   1375 O O   . ALA B 1 12  ? 22.83665  27.05648 18.42873 1.000 32.42385 ? 12  ALA B O   1 
ATOM   1376 C CB  . ALA B 1 12  ? 20.99205  29.15415 19.88581 1.000 26.04956 ? 12  ALA B CB  1 
ATOM   1377 N N   . PRO B 1 13  ? 21.12789  27.43648 17.02769 1.000 29.13383 ? 13  PRO B N   1 
ATOM   1378 C CA  . PRO B 1 13  ? 21.94940  27.11583 15.85018 1.000 31.27678 ? 13  PRO B CA  1 
ATOM   1379 C C   . PRO B 1 13  ? 23.18767  27.99355 15.77254 1.000 32.51241 ? 13  PRO B C   1 
ATOM   1380 O O   . PRO B 1 13  ? 23.10851  29.22280 15.83311 1.000 31.94785 ? 13  PRO B O   1 
ATOM   1381 C CB  . PRO B 1 13  ? 20.99845  27.37108 14.67326 1.000 32.51664 ? 13  PRO B CB  1 
ATOM   1382 C CG  . PRO B 1 13  ? 19.62538  27.18071 15.25197 1.000 34.58531 ? 13  PRO B CG  1 
ATOM   1383 C CD  . PRO B 1 13  ? 19.71837  27.68595 16.67628 1.000 28.66279 ? 13  PRO B CD  1 
ATOM   1384 N N   . ASN B 1 14  ? 24.34294  27.35176 15.64818 1.000 31.98738 ? 14  ASN B N   1 
ATOM   1385 C CA  . ASN B 1 14  ? 25.56714  28.11726 15.51082 1.000 33.24750 ? 14  ASN B CA  1 
ATOM   1386 C C   . ASN B 1 14  ? 25.60374  28.78755 14.14248 1.000 30.97708 ? 14  ASN B C   1 
ATOM   1387 O O   . ASN B 1 14  ? 24.86767  28.43350 13.21801 1.000 32.97105 ? 14  ASN B O   1 
ATOM   1388 C CB  . ASN B 1 14  ? 26.79405  27.21936 15.70487 1.000 37.32429 ? 14  ASN B CB  1 
ATOM   1389 C CG  . ASN B 1 14  ? 28.04774  27.99790 16.13365 1.000 39.34550 ? 14  ASN B CG  1 
ATOM   1390 O OD1 . ASN B 1 14  ? 28.00654  29.20235 16.40080 1.000 35.81902 ? 14  ASN B OD1 1 
ATOM   1391 N ND2 . ASN B 1 14  ? 29.17350  27.29345 16.20647 1.000 42.28873 ? 14  ASN B ND2 1 
ATOM   1392 N N   . PHE B 1 15  ? 26.44448  29.80452 14.03713 1.000 35.19715 ? 15  PHE B N   1 
ATOM   1393 C CA  . PHE B 1 15  ? 26.70176  30.43252 12.75575 1.000 34.62211 ? 15  PHE B CA  1 
ATOM   1394 C C   . PHE B 1 15  ? 28.12334  30.95650 12.79141 1.000 31.88146 ? 15  PHE B C   1 
ATOM   1395 O O   . PHE B 1 15  ? 28.67524  31.21037 13.86411 1.000 32.37194 ? 15  PHE B O   1 
ATOM   1396 C CB  . PHE B 1 15  ? 25.69723  31.55914 12.44638 1.000 36.19108 ? 15  PHE B CB  1 
ATOM   1397 C CG  . PHE B 1 15  ? 25.70706  32.69334 13.45020 1.000 33.38322 ? 15  PHE B CG  1 
ATOM   1398 C CD1 . PHE B 1 15  ? 26.70880  33.65278 13.42986 1.000 33.59691 ? 15  PHE B CD1 1 
ATOM   1399 C CD2 . PHE B 1 15  ? 24.70557  32.80318 14.40186 1.000 32.69438 ? 15  PHE B CD2 1 
ATOM   1400 C CE1 . PHE B 1 15  ? 26.72119  34.68625 14.34424 1.000 35.50715 ? 15  PHE B CE1 1 
ATOM   1401 C CE2 . PHE B 1 15  ? 24.71309  33.85413 15.31959 1.000 30.54674 ? 15  PHE B CE2 1 
ATOM   1402 C CZ  . PHE B 1 15  ? 25.72341  34.78064 15.29003 1.000 30.89019 ? 15  PHE B CZ  1 
ATOM   1403 N N   . LYS B 1 16  ? 28.71942  31.09634 11.61299 1.000 32.34224 ? 16  LYS B N   1 
ATOM   1404 C CA  . LYS B 1 16  ? 29.98278  31.80401 11.45987 1.000 35.66704 ? 16  LYS B CA  1 
ATOM   1405 C C   . LYS B 1 16  ? 29.79870  32.78367 10.31667 1.000 34.66610 ? 16  LYS B C   1 
ATOM   1406 O O   . LYS B 1 16  ? 29.39414  32.38334 9.22204  1.000 34.22701 ? 16  LYS B O   1 
ATOM   1407 C CB  . LYS B 1 16  ? 31.15022  30.84703 11.18378 1.000 37.80885 ? 16  LYS B CB  1 
ATOM   1408 C CG  . LYS B 1 16  ? 32.51195  31.52656 11.32677 1.000 42.68432 ? 16  LYS B CG  1 
ATOM   1409 C CD  . LYS B 1 16  ? 33.64727  30.65979 10.78045 1.000 50.37702 ? 16  LYS B CD  1 
ATOM   1410 C CE  . LYS B 1 16  ? 34.99393  31.35196 10.95098 1.000 50.08392 ? 16  LYS B CE  1 
ATOM   1411 N NZ  . LYS B 1 16  ? 35.78146  30.78919 12.08662 1.000 56.64996 ? 16  LYS B NZ  1 
ATOM   1412 N N   . ALA B 1 17  ? 30.04796  34.06505 10.57914 1.000 32.98552 ? 17  ALA B N   1 
ATOM   1413 C CA  . ALA B 1 17  ? 29.73102  35.09220 9.60026  1.000 31.92150 ? 17  ALA B CA  1 
ATOM   1414 C C   . ALA B 1 17  ? 30.63624  36.29231 9.80181  1.000 30.89935 ? 17  ALA B C   1 
ATOM   1415 O O   . ALA B 1 17  ? 31.19961  36.50242 10.87866 1.000 32.93249 ? 17  ALA B O   1 
ATOM   1416 C CB  . ALA B 1 17  ? 28.26137  35.53263 9.69016  1.000 32.48528 ? 17  ALA B CB  1 
ATOM   1417 N N   . THR B 1 18  ? 30.74786  37.09059 8.74495  1.000 31.14454 ? 18  THR B N   1 
ATOM   1418 C CA  . THR B 1 18  ? 31.45877  38.35585 8.80846  1.000 30.45127 ? 18  THR B CA  1 
ATOM   1419 C C   . THR B 1 18  ? 30.56989  39.40737 9.45613  1.000 28.10360 ? 18  THR B C   1 
ATOM   1420 O O   . THR B 1 18  ? 29.39645  39.54888 9.09626  1.000 31.81829 ? 18  THR B O   1 
ATOM   1421 C CB  . THR B 1 18  ? 31.86838  38.80341 7.40519  1.000 34.08649 ? 18  THR B CB  1 
ATOM   1422 O OG1 . THR B 1 18  ? 32.62080  37.75883 6.77649  1.000 33.27371 ? 18  THR B OG1 1 
ATOM   1423 C CG2 . THR B 1 18  ? 32.71395  40.06895 7.47436  1.000 35.42704 ? 18  THR B CG2 1 
ATOM   1424 N N   . ALA B 1 19  ? 31.12998  40.13448 10.41349 1.000 30.31694 ? 19  ALA B N   1 
ATOM   1425 C CA  . ALA B 1 19  ? 30.42608  41.19883 11.10682 1.000 29.79587 ? 19  ALA B CA  1 
ATOM   1426 C C   . ALA B 1 19  ? 31.24528  42.47542 11.01965 1.000 30.41198 ? 19  ALA B C   1 
ATOM   1427 O O   . ALA B 1 19  ? 32.47571  42.42828 10.93054 1.000 30.52212 ? 19  ALA B O   1 
ATOM   1428 C CB  . ALA B 1 19  ? 30.17964  40.82866 12.58086 1.000 30.14209 ? 19  ALA B CB  1 
ATOM   1429 N N   . VAL B 1 20  ? 30.55757  43.61791 11.02573 1.000 26.92622 ? 20  VAL B N   1 
ATOM   1430 C CA  . VAL B 1 20  ? 31.19841  44.89589 11.29557 1.000 28.39191 ? 20  VAL B CA  1 
ATOM   1431 C C   . VAL B 1 20  ? 31.19054  45.07827 12.80456 1.000 30.01653 ? 20  VAL B C   1 
ATOM   1432 O O   . VAL B 1 20  ? 30.12353  45.08919 13.42905 1.000 28.26722 ? 20  VAL B O   1 
ATOM   1433 C CB  . VAL B 1 20  ? 30.48052  46.05870 10.59146 1.000 26.33545 ? 20  VAL B CB  1 
ATOM   1434 C CG1 . VAL B 1 20  ? 31.23428  47.36564 10.83571 1.000 28.20488 ? 20  VAL B CG1 1 
ATOM   1435 C CG2 . VAL B 1 20  ? 30.36875  45.77322 9.09567  1.000 29.59423 ? 20  VAL B CG2 1 
ATOM   1436 N N   . MET B 1 21  ? 32.37205  45.18055 13.38937 1.000 28.69801 ? 21  MET B N   1 
ATOM   1437 C CA  . MET B 1 21  ? 32.53841  45.22651 14.83119 1.000 28.74804 ? 21  MET B CA  1 
ATOM   1438 C C   . MET B 1 21  ? 32.41670  46.65847 15.33023 1.000 26.73427 ? 21  MET B C   1 
ATOM   1439 O O   . MET B 1 21  ? 32.47790  47.60467 14.54223 1.000 29.82730 ? 21  MET B O   1 
ATOM   1440 C CB  . MET B 1 21  ? 33.89550  44.63307 15.21183 1.000 31.73431 ? 21  MET B CB  1 
ATOM   1441 C CG  . MET B 1 21  ? 34.08642  43.18336 14.72385 1.000 30.41888 ? 21  MET B CG  1 
ATOM   1442 S SD  . MET B 1 21  ? 32.83718  42.01894 15.30968 1.000 32.85608 ? 21  MET B SD  1 
ATOM   1443 C CE  . MET B 1 21  ? 33.38112  41.79726 16.99797 1.000 32.45205 ? 21  MET B CE  1 
ATOM   1444 N N   . PRO B 1 22  ? 32.21368  46.85324 16.63612 1.000 27.96816 ? 22  PRO B N   1 
ATOM   1445 C CA  . PRO B 1 22  ? 32.09561  48.22656 17.16213 1.000 30.73098 ? 22  PRO B CA  1 
ATOM   1446 C C   . PRO B 1 22  ? 33.24490  49.14809 16.78087 1.000 31.52881 ? 22  PRO B C   1 
ATOM   1447 O O   . PRO B 1 22  ? 33.03788  50.36286 16.67091 1.000 30.81180 ? 22  PRO B O   1 
ATOM   1448 C CB  . PRO B 1 22  ? 32.02793  48.00220 18.67905 1.000 30.08379 ? 22  PRO B CB  1 
ATOM   1449 C CG  . PRO B 1 22  ? 31.34250  46.68139 18.81300 1.000 28.37307 ? 22  PRO B CG  1 
ATOM   1450 C CD  . PRO B 1 22  ? 31.83368  45.84496 17.64663 1.000 30.61939 ? 22  PRO B CD  1 
ATOM   1451 N N   . ASP B 1 23  ? 34.44661  48.61793 16.54976 1.000 33.01005 ? 23  ASP B N   1 
ATOM   1452 C CA  . ASP B 1 23  ? 35.55950  49.48484 16.17298 1.000 35.33902 ? 23  ASP B CA  1 
ATOM   1453 C C   . ASP B 1 23  ? 35.53735  49.86798 14.69931 1.000 37.07616 ? 23  ASP B C   1 
ATOM   1454 O O   . ASP B 1 23  ? 36.44667  50.57455 14.24121 1.000 38.63870 ? 23  ASP B O   1 
ATOM   1455 C CB  . ASP B 1 23  ? 36.89674  48.82467 16.53758 1.000 36.82883 ? 23  ASP B CB  1 
ATOM   1456 C CG  . ASP B 1 23  ? 37.21707  47.60218 15.68690 1.000 37.80802 ? 23  ASP B CG  1 
ATOM   1457 O OD1 . ASP B 1 23  ? 36.36144  47.14182 14.89728 1.000 34.78614 ? 23  ASP B OD1 1 
ATOM   1458 O OD2 . ASP B 1 23  ? 38.34752  47.07968 15.82651 1.000 44.16569 ? 23  ASP B OD2 1 
ATOM   1459 N N   . GLY B 1 24  ? 34.51786  49.43935 13.95629 1.000 32.81373 ? 24  GLY B N   1 
ATOM   1460 C CA  . GLY B 1 24  ? 34.35735  49.81423 12.56920 1.000 35.60224 ? 24  GLY B CA  1 
ATOM   1461 C C   . GLY B 1 24  ? 35.02732  48.89693 11.57301 1.000 39.36806 ? 24  GLY B C   1 
ATOM   1462 O O   . GLY B 1 24  ? 34.99974  49.19118 10.37038 1.000 39.69667 ? 24  GLY B O   1 
ATOM   1463 N N   . GLN B 1 25  ? 35.61603  47.79277 12.02363 1.000 31.45909 ? 25  GLN B N   1 
ATOM   1464 C CA  . GLN B 1 25  ? 36.34021  46.88724 11.14779 1.000 35.98548 ? 25  GLN B CA  1 
ATOM   1465 C C   . GLN B 1 25  ? 35.62056  45.54971 11.04038 1.000 35.38648 ? 25  GLN B C   1 
ATOM   1466 O O   . GLN B 1 25  ? 34.83724  45.16360 11.91321 1.000 32.31870 ? 25  GLN B O   1 
ATOM   1467 C CB  . GLN B 1 25  ? 37.77489  46.67107 11.64510 1.000 37.76238 ? 25  GLN B CB  1 
ATOM   1468 C CG  . GLN B 1 25  ? 38.61445  47.94110 11.68906 1.000 43.35108 ? 25  GLN B CG  1 
ATOM   1469 C CD  . GLN B 1 25  ? 40.02371  47.69103 12.19793 1.000 46.08568 ? 25  GLN B CD  1 
ATOM   1470 O OE1 . GLN B 1 25  ? 40.29901  46.66632 12.81957 1.000 53.92897 ? 25  GLN B OE1 1 
ATOM   1471 N NE2 . GLN B 1 25  ? 40.92005  48.62904 11.93913 1.000 52.77573 ? 25  GLN B NE2 1 
ATOM   1472 N N   . PHE B 1 26  ? 35.89858  44.84561 9.94493  1.000 34.43722 ? 26  PHE B N   1 
ATOM   1473 C CA  . PHE B 1 26  ? 35.34290  43.51955 9.73413  1.000 34.23071 ? 26  PHE B CA  1 
ATOM   1474 C C   . PHE B 1 26  ? 36.02136  42.50341 10.64394 1.000 35.50706 ? 26  PHE B C   1 
ATOM   1475 O O   . PHE B 1 26  ? 37.20081  42.62740 10.98303 1.000 37.60821 ? 26  PHE B O   1 
ATOM   1476 C CB  . PHE B 1 26  ? 35.51656  43.08246 8.27673  1.000 35.25793 ? 26  PHE B CB  1 
ATOM   1477 C CG  . PHE B 1 26  ? 34.87251  44.00293 7.27865  1.000 36.55691 ? 26  PHE B CG  1 
ATOM   1478 C CD1 . PHE B 1 26  ? 33.61290  44.53245 7.51027  1.000 28.96434 ? 26  PHE B CD1 1 
ATOM   1479 C CD2 . PHE B 1 26  ? 35.52359  44.32632 6.09718  1.000 36.28632 ? 26  PHE B CD2 1 
ATOM   1480 C CE1 . PHE B 1 26  ? 33.01366  45.37480 6.58614  1.000 33.71553 ? 26  PHE B CE1 1 
ATOM   1481 C CE2 . PHE B 1 26  ? 34.92950  45.17654 5.16839  1.000 36.01304 ? 26  PHE B CE2 1 
ATOM   1482 C CZ  . PHE B 1 26  ? 33.67680  45.70072 5.41090  1.000 31.50493 ? 26  PHE B CZ  1 
ATOM   1483 N N   . LYS B 1 27  ? 35.25265  41.49928 11.05406 1.000 33.53305 ? 27  LYS B N   1 
ATOM   1484 C CA  . LYS B 1 27  ? 35.79749  40.34759 11.75802 1.000 34.61774 ? 27  LYS B CA  1 
ATOM   1485 C C   . LYS B 1 27  ? 34.81540  39.19672 11.61671 1.000 35.30283 ? 27  LYS B C   1 
ATOM   1486 O O   . LYS B 1 27  ? 33.60168  39.39706 11.69377 1.000 33.65150 ? 27  LYS B O   1 
ATOM   1487 C CB  . LYS B 1 27  ? 36.06194  40.64703 13.24142 1.000 37.13098 ? 27  LYS B CB  1 
ATOM   1488 C CG  . LYS B 1 27  ? 36.68050  39.47798 14.00980 1.000 37.56804 ? 27  LYS B CG  1 
ATOM   1489 C CD  . LYS B 1 27  ? 37.03562  39.87098 15.43657 1.000 39.10163 ? 27  LYS B CD  1 
ATOM   1490 C CE  . LYS B 1 27  ? 37.47931  38.66679 16.25601 1.000 45.36462 ? 27  LYS B CE  1 
ATOM   1491 N NZ  . LYS B 1 27  ? 36.43412  38.25143 17.24662 1.000 49.69546 ? 27  LYS B NZ  1 
ATOM   1492 N N   . ASP B 1 28  ? 35.34332  37.99802 11.39259 1.000 35.12453 ? 28  ASP B N   1 
ATOM   1493 C CA  . ASP B 1 28  ? 34.50622  36.80794 11.32961 1.000 33.45035 ? 28  ASP B CA  1 
ATOM   1494 C C   . ASP B 1 28  ? 34.25237  36.31379 12.74797 1.000 37.22874 ? 28  ASP B C   1 
ATOM   1495 O O   . ASP B 1 28  ? 35.19901  36.05088 13.49821 1.000 35.92108 ? 28  ASP B O   1 
ATOM   1496 C CB  . ASP B 1 28  ? 35.17693  35.72114 10.49072 1.000 33.84049 ? 28  ASP B CB  1 
ATOM   1497 C CG  . ASP B 1 28  ? 35.11365  36.00744 8.99834  1.000 41.14550 ? 28  ASP B CG  1 
ATOM   1498 O OD1 . ASP B 1 28  ? 34.55981  37.06115 8.59772  1.000 37.37805 ? 28  ASP B OD1 1 
ATOM   1499 O OD2 . ASP B 1 28  ? 35.63814  35.18144 8.22152  1.000 44.40026 ? 28  ASP B OD2 1 
ATOM   1500 N N   . ILE B 1 29  ? 32.97949  36.19212 13.12299 1.000 33.12884 ? 29  ILE B N   1 
ATOM   1501 C CA  . ILE B 1 29  ? 32.61794  35.79169 14.47545 1.000 33.32297 ? 29  ILE B CA  1 
ATOM   1502 C C   . ILE B 1 29  ? 31.65303  34.61586 14.41040 1.000 32.47845 ? 29  ILE B C   1 
ATOM   1503 O O   . ILE B 1 29  ? 31.01128  34.35850 13.38989 1.000 32.85504 ? 29  ILE B O   1 
ATOM   1504 C CB  . ILE B 1 29  ? 32.00242  36.95940 15.28231 1.000 31.01714 ? 29  ILE B CB  1 
ATOM   1505 C CG1 . ILE B 1 29  ? 30.67287  37.39447 14.66013 1.000 31.44700 ? 29  ILE B CG1 1 
ATOM   1506 C CG2 . ILE B 1 29  ? 32.97775  38.13868 15.34356 1.000 32.05275 ? 29  ILE B CG2 1 
ATOM   1507 C CD1 . ILE B 1 29  ? 29.92558  38.45341 15.48241 1.000 30.24444 ? 29  ILE B CD1 1 
ATOM   1508 N N   . SER B 1 30  ? 31.57119  33.88745 15.52538 1.000 31.62761 ? 30  SER B N   1 
ATOM   1509 C CA  . SER B 1 30  ? 30.65925  32.76362 15.67272 1.000 30.67618 ? 30  SER B CA  1 
ATOM   1510 C C   . SER B 1 30  ? 29.84005  32.92899 16.94219 1.000 30.96001 ? 30  SER B C   1 
ATOM   1511 O O   . SER B 1 30  ? 30.31128  33.49605 17.93225 1.000 31.07675 ? 30  SER B O   1 
ATOM   1512 C CB  . SER B 1 30  ? 31.40514  31.41829 15.74153 1.000 33.68431 ? 30  SER B CB  1 
ATOM   1513 O OG  . SER B 1 30  ? 32.18479  31.19919 14.58311 1.000 40.09978 ? 30  SER B OG  1 
ATOM   1514 N N   . LEU B 1 31  ? 28.61131  32.41125 16.91196 1.000 28.64741 ? 31  LEU B N   1 
ATOM   1515 C CA  . LEU B 1 31  ? 27.79001  32.43864 18.11850 1.000 33.09471 ? 31  LEU B CA  1 
ATOM   1516 C C   . LEU B 1 31  ? 28.51629  31.76392 19.27708 1.000 33.29859 ? 31  LEU B C   1 
ATOM   1517 O O   . LEU B 1 31  ? 28.46811  32.24009 20.41769 1.000 31.67523 ? 31  LEU B O   1 
ATOM   1518 C CB  . LEU B 1 31  ? 26.44258  31.77025 17.85096 1.000 32.90059 ? 31  LEU B CB  1 
ATOM   1519 C CG  . LEU B 1 31  ? 25.53304  31.58126 19.06988 1.000 33.10938 ? 31  LEU B CG  1 
ATOM   1520 C CD1 . LEU B 1 31  ? 25.20724  32.93536 19.70104 1.000 33.30257 ? 31  LEU B CD1 1 
ATOM   1521 C CD2 . LEU B 1 31  ? 24.25886  30.82318 18.69140 1.000 33.65197 ? 31  LEU B CD2 1 
ATOM   1522 N N   . SER B 1 32  ? 29.24695  30.68639 18.98387 1.000 33.01376 ? 32  SER B N   1 
ATOM   1523 C CA  . SER B 1 32  ? 29.97926  29.95337 20.00863 1.000 34.07432 ? 32  SER B CA  1 
ATOM   1524 C C   . SER B 1 32  ? 31.10338  30.77004 20.63493 1.000 34.36600 ? 32  SER B C   1 
ATOM   1525 O O   . SER B 1 32  ? 31.57657  30.40840 21.71868 1.000 35.80225 ? 32  SER B O   1 
ATOM   1526 C CB  . SER B 1 32  ? 30.54811  28.67149 19.40820 1.000 35.32034 ? 32  SER B CB  1 
ATOM   1527 O OG  . SER B 1 32  ? 31.33435  28.96723 18.26731 1.000 36.43413 ? 32  SER B OG  1 
ATOM   1528 N N   . ASP B 1 33  ? 31.54909  31.85162 19.98411 1.000 29.43853 ? 33  ASP B N   1 
ATOM   1529 C CA  . ASP B 1 33  ? 32.52559  32.74291 20.60757 1.000 31.61981 ? 33  ASP B CA  1 
ATOM   1530 C C   . ASP B 1 33  ? 32.02213  33.27793 21.93901 1.000 33.02889 ? 33  ASP B C   1 
ATOM   1531 O O   . ASP B 1 33  ? 32.82421  33.66689 22.79371 1.000 32.73822 ? 33  ASP B O   1 
ATOM   1532 C CB  . ASP B 1 33  ? 32.85209  33.94133 19.70573 1.000 34.97268 ? 33  ASP B CB  1 
ATOM   1533 C CG  . ASP B 1 33  ? 33.47869  33.54852 18.38232 1.000 38.01632 ? 33  ASP B CG  1 
ATOM   1534 O OD1 . ASP B 1 33  ? 33.90276  32.38733 18.22285 1.000 37.15902 ? 33  ASP B OD1 1 
ATOM   1535 O OD2 . ASP B 1 33  ? 33.54451  34.42921 17.49853 1.000 35.37902 ? 33  ASP B OD2 1 
ATOM   1536 N N   . TYR B 1 34  ? 30.70226  33.34802 22.11558 1.000 32.29340 ? 34  TYR B N   1 
ATOM   1537 C CA  . TYR B 1 34  ? 30.10390  34.00536 23.26589 1.000 31.43331 ? 34  TYR B CA  1 
ATOM   1538 C C   . TYR B 1 34  ? 29.58327  33.02508 24.30759 1.000 31.54581 ? 34  TYR B C   1 
ATOM   1539 O O   . TYR B 1 34  ? 28.83538  33.42968 25.20216 1.000 31.54502 ? 34  TYR B O   1 
ATOM   1540 C CB  . TYR B 1 34  ? 28.99691  34.95212 22.79327 1.000 31.30970 ? 34  TYR B CB  1 
ATOM   1541 C CG  . TYR B 1 34  ? 29.55823  35.96681 21.82761 1.000 29.46188 ? 34  TYR B CG  1 
ATOM   1542 C CD1 . TYR B 1 34  ? 30.22648  37.09114 22.29473 1.000 31.56848 ? 34  TYR B CD1 1 
ATOM   1543 C CD2 . TYR B 1 34  ? 29.48415  35.76662 20.44958 1.000 32.12421 ? 34  TYR B CD2 1 
ATOM   1544 C CE1 . TYR B 1 34  ? 30.77851  38.01404 21.42138 1.000 32.32108 ? 34  TYR B CE1 1 
ATOM   1545 C CE2 . TYR B 1 34  ? 30.03228  36.68183 19.57026 1.000 28.25987 ? 34  TYR B CE2 1 
ATOM   1546 C CZ  . TYR B 1 34  ? 30.68241  37.79848 20.05665 1.000 31.60226 ? 34  TYR B CZ  1 
ATOM   1547 O OH  . TYR B 1 34  ? 31.23420  38.70842 19.18139 1.000 33.35011 ? 34  TYR B OH  1 
ATOM   1548 N N   . LYS B 1 35  ? 29.97586  31.75548 24.23089 1.000 34.46102 ? 35  LYS B N   1 
ATOM   1549 C CA  . LYS B 1 35  ? 29.70176  30.83905 25.32716 1.000 33.50941 ? 35  LYS B CA  1 
ATOM   1550 C C   . LYS B 1 35  ? 30.22777  31.42739 26.62768 1.000 33.05210 ? 35  LYS B C   1 
ATOM   1551 O O   . LYS B 1 35  ? 31.28501  32.06264 26.65883 1.000 33.56076 ? 35  LYS B O   1 
ATOM   1552 C CB  . LYS B 1 35  ? 30.34263  29.47677 25.06283 1.000 34.54976 ? 35  LYS B CB  1 
ATOM   1553 C CG  . LYS B 1 35  ? 29.57112  28.61338 24.08806 1.000 41.69665 ? 35  LYS B CG  1 
ATOM   1554 C CD  . LYS B 1 35  ? 28.54545  27.75173 24.80954 1.000 43.31577 ? 35  LYS B CD  1 
ATOM   1555 C CE  . LYS B 1 35  ? 28.48356  26.35032 24.20479 1.000 47.37469 ? 35  LYS B CE  1 
ATOM   1556 N NZ  . LYS B 1 35  ? 28.33246  26.39272 22.71873 1.000 48.24741 ? 35  LYS B NZ  1 
ATOM   1557 N N   . GLY B 1 36  ? 29.46547  31.23770 27.70155 1.000 33.72330 ? 36  GLY B N   1 
ATOM   1558 C CA  . GLY B 1 36  ? 29.73680  31.90221 28.95416 1.000 33.33151 ? 36  GLY B CA  1 
ATOM   1559 C C   . GLY B 1 36  ? 29.01859  33.21903 29.13904 1.000 34.47729 ? 36  GLY B C   1 
ATOM   1560 O O   . GLY B 1 36  ? 29.05160  33.77622 30.24214 1.000 35.35504 ? 36  GLY B O   1 
ATOM   1561 N N   . LYS B 1 37  ? 28.38274  33.74054 28.09304 1.000 31.38616 ? 37  LYS B N   1 
ATOM   1562 C CA  . LYS B 1 37  ? 27.58572  34.95381 28.16796 1.000 31.64587 ? 37  LYS B CA  1 
ATOM   1563 C C   . LYS B 1 37  ? 26.19895  34.66412 27.61324 1.000 28.22170 ? 37  LYS B C   1 
ATOM   1564 O O   . LYS B 1 37  ? 26.03841  33.83003 26.71548 1.000 29.09240 ? 37  LYS B O   1 
ATOM   1565 C CB  . LYS B 1 37  ? 28.21246  36.09998 27.35666 1.000 31.28609 ? 37  LYS B CB  1 
ATOM   1566 C CG  . LYS B 1 37  ? 29.66110  36.38648 27.70313 1.000 39.46427 ? 37  LYS B CG  1 
ATOM   1567 C CD  . LYS B 1 37  ? 30.07159  37.75769 27.21587 1.000 41.88354 ? 37  LYS B CD  1 
ATOM   1568 C CE  . LYS B 1 37  ? 31.54019  38.03010 27.51744 1.000 49.34214 ? 37  LYS B CE  1 
ATOM   1569 N NZ  . LYS B 1 37  ? 32.20011  38.82312 26.43809 1.000 53.47118 ? 37  LYS B NZ  1 
ATOM   1570 N N   . TYR B 1 38  ? 25.19634  35.35253 28.15789 1.000 28.28146 ? 38  TYR B N   1 
ATOM   1571 C CA  . TYR B 1 38  ? 23.91610  35.43555 27.46565 1.000 28.26669 ? 38  TYR B CA  1 
ATOM   1572 C C   . TYR B 1 38  ? 24.11099  36.18701 26.15580 1.000 25.83531 ? 38  TYR B C   1 
ATOM   1573 O O   . TYR B 1 38  ? 25.00756  37.01720 26.02535 1.000 25.68149 ? 38  TYR B O   1 
ATOM   1574 C CB  . TYR B 1 38  ? 22.87004  36.15514 28.32690 1.000 28.78752 ? 38  TYR B CB  1 
ATOM   1575 C CG  . TYR B 1 38  ? 21.94977  35.20328 29.05035 1.000 26.43215 ? 38  TYR B CG  1 
ATOM   1576 C CD1 . TYR B 1 38  ? 22.41353  34.43013 30.10597 1.000 26.61729 ? 38  TYR B CD1 1 
ATOM   1577 C CD2 . TYR B 1 38  ? 20.62317  35.07129 28.67172 1.000 26.73385 ? 38  TYR B CD2 1 
ATOM   1578 C CE1 . TYR B 1 38  ? 21.57620  33.54186 30.76504 1.000 27.84498 ? 38  TYR B CE1 1 
ATOM   1579 C CE2 . TYR B 1 38  ? 19.77749  34.19512 29.32315 1.000 26.65727 ? 38  TYR B CE2 1 
ATOM   1580 C CZ  . TYR B 1 38  ? 20.26043  33.43363 30.37554 1.000 25.94098 ? 38  TYR B CZ  1 
ATOM   1581 O OH  . TYR B 1 38  ? 19.43219  32.55421 31.02605 1.000 26.63744 ? 38  TYR B OH  1 
ATOM   1582 N N   . VAL B 1 39  ? 23.26376  35.89453 25.17706 1.000 24.59068 ? 39  VAL B N   1 
ATOM   1583 C CA  . VAL B 1 39  ? 23.32370  36.56761 23.88639 1.000 24.53613 ? 39  VAL B CA  1 
ATOM   1584 C C   . VAL B 1 39  ? 21.91568  36.97244 23.48868 1.000 21.42778 ? 39  VAL B C   1 
ATOM   1585 O O   . VAL B 1 39  ? 20.98639  36.16292 23.57991 1.000 23.78224 ? 39  VAL B O   1 
ATOM   1586 C CB  . VAL B 1 39  ? 23.94507  35.67475 22.79077 1.000 26.41278 ? 39  VAL B CB  1 
ATOM   1587 C CG1 . VAL B 1 39  ? 23.88093  36.38505 21.41875 1.000 24.92875 ? 39  VAL B CG1 1 
ATOM   1588 C CG2 . VAL B 1 39  ? 25.37959  35.31631 23.14100 1.000 26.05791 ? 39  VAL B CG2 1 
ATOM   1589 N N   . VAL B 1 40  ? 21.76029  38.22480 23.07148 1.000 22.02379 ? 40  VAL B N   1 
ATOM   1590 C CA  . VAL B 1 40  ? 20.58067  38.67385 22.34080 1.000 22.04654 ? 40  VAL B CA  1 
ATOM   1591 C C   . VAL B 1 40  ? 20.99118  38.77574 20.87828 1.000 21.68400 ? 40  VAL B C   1 
ATOM   1592 O O   . VAL B 1 40  ? 21.84416  39.59536 20.52287 1.000 25.55586 ? 40  VAL B O   1 
ATOM   1593 C CB  . VAL B 1 40  ? 20.06130  40.01518 22.86923 1.000 22.97355 ? 40  VAL B CB  1 
ATOM   1594 C CG1 . VAL B 1 40  ? 18.97698  40.57607 21.93513 1.000 24.86533 ? 40  VAL B CG1 1 
ATOM   1595 C CG2 . VAL B 1 40  ? 19.53019  39.83719 24.28805 1.000 22.99917 ? 40  VAL B CG2 1 
ATOM   1596 N N   . PHE B 1 41  ? 20.40015  37.93131 20.03434 1.000 22.42878 ? 41  PHE B N   1 
ATOM   1597 C CA  . PHE B 1 41  ? 20.69616  37.87298 18.60571 1.000 20.54188 ? 41  PHE B CA  1 
ATOM   1598 C C   . PHE B 1 41  ? 19.43888  38.31823 17.86857 1.000 23.52508 ? 41  PHE B C   1 
ATOM   1599 O O   . PHE B 1 41  ? 18.39900  37.65429 17.96422 1.000 23.68265 ? 41  PHE B O   1 
ATOM   1600 C CB  . PHE B 1 41  ? 21.10418  36.44979 18.21725 1.000 21.80947 ? 41  PHE B CB  1 
ATOM   1601 C CG  . PHE B 1 41  ? 21.46554  36.28429 16.76778 1.000 23.80452 ? 41  PHE B CG  1 
ATOM   1602 C CD1 . PHE B 1 41  ? 22.27729  37.20211 16.12782 1.000 25.44840 ? 41  PHE B CD1 1 
ATOM   1603 C CD2 . PHE B 1 41  ? 21.00653  35.18198 16.05411 1.000 28.55559 ? 41  PHE B CD2 1 
ATOM   1604 C CE1 . PHE B 1 41  ? 22.61405  37.04479 14.79909 1.000 25.50251 ? 41  PHE B CE1 1 
ATOM   1605 C CE2 . PHE B 1 41  ? 21.33592  35.01615 14.71973 1.000 25.52980 ? 41  PHE B CE2 1 
ATOM   1606 C CZ  . PHE B 1 41  ? 22.14218  35.93961 14.09198 1.000 26.44273 ? 41  PHE B CZ  1 
ATOM   1607 N N   . PHE B 1 42  ? 19.51246  39.44939 17.16283 1.000 23.80620 ? 42  PHE B N   1 
ATOM   1608 C CA  . PHE B 1 42  ? 18.32826  39.95975 16.48090 1.000 23.27772 ? 42  PHE B CA  1 
ATOM   1609 C C   . PHE B 1 42  ? 18.59057  40.22179 15.00435 1.000 24.26316 ? 42  PHE B C   1 
ATOM   1610 O O   . PHE B 1 42  ? 19.66493  40.69632 14.61587 1.000 23.89090 ? 42  PHE B O   1 
ATOM   1611 C CB  . PHE B 1 42  ? 17.77280  41.23147 17.16740 1.000 21.60756 ? 42  PHE B CB  1 
ATOM   1612 C CG  . PHE B 1 42  ? 18.58062  42.49254 16.93335 1.000 24.13249 ? 42  PHE B CG  1 
ATOM   1613 C CD1 . PHE B 1 42  ? 19.63007  42.83202 17.77827 1.000 23.91880 ? 42  PHE B CD1 1 
ATOM   1614 C CD2 . PHE B 1 42  ? 18.25998  43.35729 15.90148 1.000 22.90838 ? 42  PHE B CD2 1 
ATOM   1615 C CE1 . PHE B 1 42  ? 20.35501  44.00255 17.57972 1.000 24.67813 ? 42  PHE B CE1 1 
ATOM   1616 C CE2 . PHE B 1 42  ? 18.97816  44.53388 15.69717 1.000 24.12215 ? 42  PHE B CE2 1 
ATOM   1617 C CZ  . PHE B 1 42  ? 20.02541  44.85854 16.53468 1.000 25.41432 ? 42  PHE B CZ  1 
ATOM   1618 N N   . PHE B 1 43  ? 17.58673  39.89338 14.19171 1.000 23.95893 ? 43  PHE B N   1 
ATOM   1619 C CA  . PHE B 1 43  ? 17.56734  40.14643 12.76162 1.000 24.23287 ? 43  PHE B CA  1 
ATOM   1620 C C   . PHE B 1 43  ? 16.74487  41.39043 12.46332 1.000 23.63029 ? 43  PHE B C   1 
ATOM   1621 O O   . PHE B 1 43  ? 15.74096  41.66287 13.12440 1.000 26.53022 ? 43  PHE B O   1 
ATOM   1622 C CB  . PHE B 1 43  ? 16.93477  38.98309 11.98845 1.000 23.19479 ? 43  PHE B CB  1 
ATOM   1623 C CG  . PHE B 1 43  ? 17.69527  37.70395 12.06101 1.000 28.27802 ? 43  PHE B CG  1 
ATOM   1624 C CD1 . PHE B 1 43  ? 17.50183  36.83012 13.12419 1.000 29.05217 ? 43  PHE B CD1 1 
ATOM   1625 C CD2 . PHE B 1 43  ? 18.56804  37.34557 11.04942 1.000 32.32684 ? 43  PHE B CD2 1 
ATOM   1626 C CE1 . PHE B 1 43  ? 18.18242  35.62985 13.18705 1.000 29.01774 ? 43  PHE B CE1 1 
ATOM   1627 C CE2 . PHE B 1 43  ? 19.25338  36.12795 11.10692 1.000 27.28960 ? 43  PHE B CE2 1 
ATOM   1628 C CZ  . PHE B 1 43  ? 19.05859  35.28005 12.17425 1.000 30.00004 ? 43  PHE B CZ  1 
ATOM   1629 N N   . TYR B 1 44  ? 17.15236  42.11208 11.42894 1.000 23.23357 ? 44  TYR B N   1 
ATOM   1630 C CA  . TYR B 1 44  ? 16.32783  43.15821 10.84109 1.000 23.92119 ? 44  TYR B CA  1 
ATOM   1631 C C   . TYR B 1 44  ? 16.31312  42.97673 9.32706  1.000 27.10513 ? 44  TYR B C   1 
ATOM   1632 O O   . TYR B 1 44  ? 17.22623  42.36351 8.76528  1.000 26.48103 ? 44  TYR B O   1 
ATOM   1633 C CB  . TYR B 1 44  ? 16.83104  44.56489 11.23191 1.000 24.19284 ? 44  TYR B CB  1 
ATOM   1634 C CG  . TYR B 1 44  ? 18.23814  44.87482 10.76826 1.000 25.73505 ? 44  TYR B CG  1 
ATOM   1635 C CD1 . TYR B 1 44  ? 19.34348  44.45332 11.50268 1.000 23.78457 ? 44  TYR B CD1 1 
ATOM   1636 C CD2 . TYR B 1 44  ? 18.46346  45.56983 9.58477  1.000 24.12545 ? 44  TYR B CD2 1 
ATOM   1637 C CE1 . TYR B 1 44  ? 20.62519  44.71855 11.07529 1.000 26.95980 ? 44  TYR B CE1 1 
ATOM   1638 C CE2 . TYR B 1 44  ? 19.75095  45.84025 9.14738  1.000 24.54657 ? 44  TYR B CE2 1 
ATOM   1639 C CZ  . TYR B 1 44  ? 20.82494  45.40997 9.89461  1.000 26.19612 ? 44  TYR B CZ  1 
ATOM   1640 O OH  . TYR B 1 44  ? 22.10451  45.67520 9.46661  1.000 27.91491 ? 44  TYR B OH  1 
ATOM   1641 N N   . PRO B 1 45  ? 15.26156  43.45361 8.63980  1.000 25.29642 ? 45  PRO B N   1 
ATOM   1642 C CA  . PRO B 1 45  ? 15.09556  43.10365 7.21739  1.000 28.29500 ? 45  PRO B CA  1 
ATOM   1643 C C   . PRO B 1 45  ? 16.22362  43.56371 6.29670  1.000 30.28519 ? 45  PRO B C   1 
ATOM   1644 O O   . PRO B 1 45  ? 16.82678  42.72665 5.61068  1.000 29.93014 ? 45  PRO B O   1 
ATOM   1645 C CB  . PRO B 1 45  ? 13.76737  43.77889 6.85347  1.000 28.42598 ? 45  PRO B CB  1 
ATOM   1646 C CG  . PRO B 1 45  ? 13.00986  43.80741 8.14200  1.000 30.71892 ? 45  PRO B CG  1 
ATOM   1647 C CD  . PRO B 1 45  ? 14.04435  44.06697 9.20375  1.000 28.52750 ? 45  PRO B CD  1 
ATOM   1648 N N   . LEU B 1 46  ? 16.51749  44.87096 6.26888  1.000 29.86886 ? 46  LEU B N   1 
ATOM   1649 C CA  . LEU B 1 46  ? 17.43213  45.46823 5.29701  1.000 32.23781 ? 46  LEU B CA  1 
ATOM   1650 C C   . LEU B 1 46  ? 18.12455  46.70016 5.86427  1.000 25.73174 ? 46  LEU B C   1 
ATOM   1651 O O   . LEU B 1 46  ? 17.54626  47.43277 6.67200  1.000 30.34192 ? 46  LEU B O   1 
ATOM   1652 C CB  . LEU B 1 46  ? 16.70403  45.91691 4.02526  1.000 39.21120 ? 46  LEU B CB  1 
ATOM   1653 C CG  . LEU B 1 46  ? 15.69115  44.97236 3.42672  1.000 38.65541 ? 46  LEU B CG  1 
ATOM   1654 C CD1 . LEU B 1 46  ? 14.78231  45.71398 2.51064  1.000 41.34577 ? 46  LEU B CD1 1 
ATOM   1655 C CD2 . LEU B 1 46  ? 16.50514  43.96986 2.68245  1.000 42.23420 ? 46  LEU B CD2 1 
ATOM   1656 N N   . ASP B 1 47  ? 19.34766  46.94049 5.38555  1.000 26.89732 ? 47  ASP B N   1 
ATOM   1657 C CA  . ASP B 1 47  ? 20.04193  48.19902 5.63515  1.000 27.28052 ? 47  ASP B CA  1 
ATOM   1658 C C   . ASP B 1 47  ? 19.35553  49.34317 4.89092  1.000 30.17193 ? 47  ASP B C   1 
ATOM   1659 O O   . ASP B 1 47  ? 18.60548  49.13514 3.93399  1.000 30.77430 ? 47  ASP B O   1 
ATOM   1660 C CB  . ASP B 1 47  ? 21.50273  48.13070 5.18030  1.000 26.69381 ? 47  ASP B CB  1 
ATOM   1661 C CG  . ASP B 1 47  ? 22.35613  47.20281 6.03487  1.000 27.12371 ? 47  ASP B CG  1 
ATOM   1662 O OD1 . ASP B 1 47  ? 21.86369  46.71263 7.06654  1.000 28.14123 ? 47  ASP B OD1 1 
ATOM   1663 O OD2 . ASP B 1 47  ? 23.52960  46.96680 5.66734  1.000 28.33035 ? 47  ASP B OD2 1 
ATOM   1664 N N   . PHE B 1 48  ? 19.63883  50.56607 5.34347  1.000 27.83365 ? 48  PHE B N   1 
ATOM   1665 C CA  . PHE B 1 48  ? 19.22814  51.79019 4.64228  1.000 32.55749 ? 48  PHE B CA  1 
ATOM   1666 C C   . PHE B 1 48  ? 17.70817  51.90765 4.56520  1.000 35.09350 ? 48  PHE B C   1 
ATOM   1667 O O   . PHE B 1 48  ? 17.14392  52.37246 3.57022  1.000 37.00911 ? 48  PHE B O   1 
ATOM   1668 C CB  . PHE B 1 48  ? 19.87019  51.85911 3.25538  1.000 31.62293 ? 48  PHE B CB  1 
ATOM   1669 C CG  . PHE B 1 48  ? 21.37534  51.82026 3.29709  1.000 30.34432 ? 48  PHE B CG  1 
ATOM   1670 C CD1 . PHE B 1 48  ? 22.06828  50.71301 2.84132  1.000 41.33360 ? 48  PHE B CD1 1 
ATOM   1671 C CD2 . PHE B 1 48  ? 22.08996  52.89307 3.80710  1.000 41.07854 ? 48  PHE B CD2 1 
ATOM   1672 C CE1 . PHE B 1 48  ? 23.44881  50.67571 2.89054  1.000 38.14768 ? 48  PHE B CE1 1 
ATOM   1673 C CE2 . PHE B 1 48  ? 23.47485  52.86189 3.85685  1.000 41.54508 ? 48  PHE B CE2 1 
ATOM   1674 C CZ  . PHE B 1 48  ? 24.14913  51.74618 3.40267  1.000 39.76048 ? 48  PHE B CZ  1 
ATOM   1675 N N   . THR B 1 49  ? 17.04534  51.49799 5.63717  1.000 30.87255 ? 49  THR B N   1 
ATOM   1676 C CA  . THR B 1 49  ? 15.60319  51.53701 5.78559  1.000 31.04892 ? 49  THR B CA  1 
ATOM   1677 C C   . THR B 1 49  ? 15.23477  52.53255 6.88403  1.000 33.27673 ? 49  THR B C   1 
ATOM   1678 O O   . THR B 1 49  ? 16.07733  53.29973 7.37191  1.000 32.78548 ? 49  THR B O   1 
ATOM   1679 C CB  . THR B 1 49  ? 15.07579  50.13897 6.09520  1.000 35.56455 ? 49  THR B CB  1 
ATOM   1680 O OG1 . THR B 1 49  ? 15.93078  49.52921 7.06861  1.000 36.37809 ? 49  THR B OG1 1 
ATOM   1681 C CG2 . THR B 1 49  ? 15.05677  49.28365 4.83761  1.000 36.00648 ? 49  THR B CG2 1 
ATOM   1682 N N   . PHE B 1 50  ? 13.96724  52.51532 7.28929  1.000 34.32759 ? 50  PHE B N   1 
ATOM   1683 C CA  . PHE B 1 50  ? 13.44448  53.56845 8.14900  1.000 36.18557 ? 50  PHE B CA  1 
ATOM   1684 C C   . PHE B 1 50  ? 13.10673  53.11224 9.56222  1.000 35.68740 ? 50  PHE B C   1 
ATOM   1685 O O   . PHE B 1 50  ? 13.29428  53.88909 10.49950 1.000 38.35724 ? 50  PHE B O   1 
ATOM   1686 C CB  . PHE B 1 50  ? 12.20475  54.20459 7.50243  1.000 35.32939 ? 50  PHE B CB  1 
ATOM   1687 C CG  . PHE B 1 50  ? 12.47629  54.82883 6.15148  1.000 40.39772 ? 50  PHE B CG  1 
ATOM   1688 C CD1 . PHE B 1 50  ? 13.76977  55.16808 5.77046  1.000 39.57445 ? 50  PHE B CD1 1 
ATOM   1689 C CD2 . PHE B 1 50  ? 11.44041  55.07990 5.26652  1.000 44.46243 ? 50  PHE B CD2 1 
ATOM   1690 C CE1 . PHE B 1 50  ? 14.02556  55.73459 4.53537  1.000 40.96145 ? 50  PHE B CE1 1 
ATOM   1691 C CE2 . PHE B 1 50  ? 11.68935  55.64657 4.02977  1.000 42.92095 ? 50  PHE B CE2 1 
ATOM   1692 C CZ  . PHE B 1 50  ? 12.98010  55.97550 3.66221  1.000 46.87497 ? 50  PHE B CZ  1 
ATOM   1693 N N   . VAL B 1 51  ? 12.62847  51.88146 9.74906  1.000 29.12493 ? 51  VAL B N   1 
ATOM   1694 C CA  . VAL B 1 51  ? 12.32232  51.39312 11.08976 1.000 32.11623 ? 51  VAL B CA  1 
ATOM   1695 C C   . VAL B 1 51  ? 13.52618  50.69863 11.71246 1.000 30.76047 ? 51  VAL B C   1 
ATOM   1696 O O   . VAL B 1 51  ? 13.83259  50.91027 12.89130 1.000 27.83007 ? 51  VAL B O   1 
ATOM   1697 C CB  . VAL B 1 51  ? 11.09738  50.45251 11.05046 1.000 33.28425 ? 51  VAL B CB  1 
ATOM   1698 C CG1 . VAL B 1 51  ? 10.89783  49.78847 12.40731 1.000 30.12061 ? 51  VAL B CG1 1 
ATOM   1699 C CG2 . VAL B 1 51  ? 9.84756   51.21305 10.62822 1.000 34.11458 ? 51  VAL B CG2 1 
ATOM   1700 N N   . SER B 1 52  ? 14.19770  49.84787 10.93476 1.000 27.41253 ? 52  SER B N   1 
ATOM   1701 C CA  . SER B 1 52  ? 15.39147  49.15375 11.41614 1.000 24.65284 ? 52  SER B CA  1 
ATOM   1702 C C   . SER B 1 52  ? 16.43358  50.05559 12.07560 1.000 25.66915 ? 52  SER B C   1 
ATOM   1703 O O   . SER B 1 52  ? 16.93940  49.68452 13.14408 1.000 23.80932 ? 52  SER B O   1 
ATOM   1704 C CB  . SER B 1 52  ? 16.01498  48.37216 10.25411 1.000 28.42660 ? 52  SER B CB  1 
ATOM   1705 O OG  . SER B 1 52  ? 15.13535  47.34762 9.83143  1.000 26.95025 ? 52  SER B OG  1 
ATOM   1706 N N   . PRO B 1 53  ? 16.81551  51.21341 11.51172 1.000 25.76009 ? 53  PRO B N   1 
ATOM   1707 C CA  . PRO B 1 53  ? 17.85539  52.01505 12.18679 1.000 25.03032 ? 53  PRO B CA  1 
ATOM   1708 C C   . PRO B 1 53  ? 17.45983  52.43591 13.58854 1.000 23.49776 ? 53  PRO B C   1 
ATOM   1709 O O   . PRO B 1 53  ? 18.31908  52.52568 14.46932 1.000 23.74229 ? 53  PRO B O   1 
ATOM   1710 C CB  . PRO B 1 53  ? 18.02365  53.23511 11.26573 1.000 28.29434 ? 53  PRO B CB  1 
ATOM   1711 C CG  . PRO B 1 53  ? 16.73638  53.30665 10.49549 1.000 27.55751 ? 53  PRO B CG  1 
ATOM   1712 C CD  . PRO B 1 53  ? 16.38257  51.85783 10.26248 1.000 26.71374 ? 53  PRO B CD  1 
ATOM   1713 N N   . THR B 1 54  ? 16.17676  52.72368 13.81509 1.000 25.94258 ? 54  THR B N   1 
ATOM   1714 C CA  . THR B 1 54  ? 15.73981  53.12278 15.14626 1.000 26.35305 ? 54  THR B CA  1 
ATOM   1715 C C   . THR B 1 54  ? 15.95491  51.99300 16.14234 1.000 26.48047 ? 54  THR B C   1 
ATOM   1716 O O   . THR B 1 54  ? 16.39971  52.22511 17.27331 1.000 25.88500 ? 54  THR B O   1 
ATOM   1717 C CB  . THR B 1 54  ? 14.27154  53.54658 15.08733 1.000 32.08731 ? 54  THR B CB  1 
ATOM   1718 O OG1 . THR B 1 54  ? 14.13708  54.62632 14.15412 1.000 37.84249 ? 54  THR B OG1 1 
ATOM   1719 C CG2 . THR B 1 54  ? 13.77745  54.00109 16.44707 1.000 38.59876 ? 54  THR B CG2 1 
ATOM   1720 N N   . GLU B 1 55  ? 15.67584  50.75596 15.71742 1.000 24.41075 ? 55  GLU B N   1 
ATOM   1721 C CA  . GLU B 1 55  ? 15.90399  49.58801 16.56422 1.000 26.00269 ? 55  GLU B CA  1 
ATOM   1722 C C   . GLU B 1 55  ? 17.38489  49.38018 16.82774 1.000 25.98416 ? 55  GLU B C   1 
ATOM   1723 O O   . GLU B 1 55  ? 17.80079  49.16136 17.97125 1.000 25.55817 ? 55  GLU B O   1 
ATOM   1724 C CB  . GLU B 1 55  ? 15.34956  48.33598 15.89115 1.000 26.81910 ? 55  GLU B CB  1 
ATOM   1725 C CG  . GLU B 1 55  ? 13.87856  48.30818 15.65691 1.000 28.16458 ? 55  GLU B CG  1 
ATOM   1726 C CD  . GLU B 1 55  ? 13.46404  46.92874 15.20617 1.000 23.71819 ? 55  GLU B CD  1 
ATOM   1727 O OE1 . GLU B 1 55  ? 13.87649  46.51739 14.09729 1.000 27.66201 ? 55  GLU B OE1 1 
ATOM   1728 O OE2 . GLU B 1 55  ? 12.76660  46.24856 15.97322 1.000 26.31297 ? 55  GLU B OE2 1 
ATOM   1729 N N   . ILE B 1 56  ? 18.18672  49.38273 15.76094 1.000 22.83076 ? 56  ILE B N   1 
ATOM   1730 C CA  . ILE B 1 56  ? 19.61671  49.11196 15.89140 1.000 24.28778 ? 56  ILE B CA  1 
ATOM   1731 C C   . ILE B 1 56  ? 20.26985  50.14562 16.79963 1.000 25.13133 ? 56  ILE B C   1 
ATOM   1732 O O   . ILE B 1 56  ? 21.05651  49.81015 17.69260 1.000 23.91225 ? 56  ILE B O   1 
ATOM   1733 C CB  . ILE B 1 56  ? 20.27831  49.08586 14.50193 1.000 22.96260 ? 56  ILE B CB  1 
ATOM   1734 C CG1 . ILE B 1 56  ? 19.73766  47.92719 13.65338 1.000 23.70511 ? 56  ILE B CG1 1 
ATOM   1735 C CG2 . ILE B 1 56  ? 21.78691  49.00592 14.61174 1.000 23.84805 ? 56  ILE B CG2 1 
ATOM   1736 C CD1 . ILE B 1 56  ? 19.92926  48.15698 12.15728 1.000 24.02728 ? 56  ILE B CD1 1 
ATOM   1737 N N   . ILE B 1 57  ? 19.94748  51.42301 16.58444 1.000 23.34976 ? 57  ILE B N   1 
ATOM   1738 C CA  . ILE B 1 57  ? 20.53118  52.48488 17.40185 1.000 23.25146 ? 57  ILE B CA  1 
ATOM   1739 C C   . ILE B 1 57  ? 20.08984  52.35148 18.85655 1.000 24.51220 ? 57  ILE B C   1 
ATOM   1740 O O   . ILE B 1 57  ? 20.87958  52.58032 19.77795 1.000 23.40118 ? 57  ILE B O   1 
ATOM   1741 C CB  . ILE B 1 57  ? 20.17966  53.86303 16.80212 1.000 22.62250 ? 57  ILE B CB  1 
ATOM   1742 C CG1 . ILE B 1 57  ? 20.93238  54.06214 15.48269 1.000 24.56190 ? 57  ILE B CG1 1 
ATOM   1743 C CG2 . ILE B 1 57  ? 20.49827  55.01945 17.79024 1.000 25.06374 ? 57  ILE B CG2 1 
ATOM   1744 C CD1 . ILE B 1 57  ? 20.36522  55.18473 14.59799 1.000 24.55395 ? 57  ILE B CD1 1 
ATOM   1745 N N   . ALA B 1 58  ? 18.83218  51.96935 19.09066 1.000 23.93873 ? 58  ALA B N   1 
ATOM   1746 C CA  . ALA B 1 58  ? 18.35794  51.80790 20.46633 1.000 24.11780 ? 58  ALA B CA  1 
ATOM   1747 C C   . ALA B 1 58  ? 19.15977  50.74155 21.19960 1.000 27.98149 ? 58  ALA B C   1 
ATOM   1748 O O   . ALA B 1 58  ? 19.58076  50.93985 22.34777 1.000 26.10804 ? 58  ALA B O   1 
ATOM   1749 C CB  . ALA B 1 58  ? 16.86589  51.45960 20.48406 1.000 26.03260 ? 58  ALA B CB  1 
ATOM   1750 N N   . PHE B 1 59  ? 19.38983  49.59884 20.54611 1.000 22.49574 ? 59  PHE B N   1 
ATOM   1751 C CA  . PHE B 1 59  ? 20.17313  48.54393 21.17931 1.000 24.15225 ? 59  PHE B CA  1 
ATOM   1752 C C   . PHE B 1 59  ? 21.62101  48.97029 21.36085 1.000 26.18710 ? 59  PHE B C   1 
ATOM   1753 O O   . PHE B 1 59  ? 22.22364  48.71128 22.40645 1.000 26.82800 ? 59  PHE B O   1 
ATOM   1754 C CB  . PHE B 1 59  ? 20.09476  47.25616 20.35564 1.000 24.28574 ? 59  PHE B CB  1 
ATOM   1755 C CG  . PHE B 1 59  ? 18.88378  46.42265 20.65759 1.000 23.18036 ? 59  PHE B CG  1 
ATOM   1756 C CD1 . PHE B 1 59  ? 18.84524  45.61785 21.78839 1.000 24.78095 ? 59  PHE B CD1 1 
ATOM   1757 C CD2 . PHE B 1 59  ? 17.78784  46.43915 19.80709 1.000 23.98595 ? 59  PHE B CD2 1 
ATOM   1758 C CE1 . PHE B 1 59  ? 17.72405  44.85048 22.07657 1.000 23.46336 ? 59  PHE B CE1 1 
ATOM   1759 C CE2 . PHE B 1 59  ? 16.65655  45.67616 20.08882 1.000 25.49228 ? 59  PHE B CE2 1 
ATOM   1760 C CZ  . PHE B 1 59  ? 16.63049  44.87570 21.22594 1.000 24.62805 ? 59  PHE B CZ  1 
ATOM   1761 N N   . SER B 1 60  ? 22.19688  49.62100 20.35259 1.000 24.33811 ? 60  SER B N   1 
ATOM   1762 C CA  . SER B 1 60  ? 23.58236  50.06085 20.46101 1.000 25.55887 ? 60  SER B CA  1 
ATOM   1763 C C   . SER B 1 60  ? 23.73463  51.09881 21.56301 1.000 25.12742 ? 60  SER B C   1 
ATOM   1764 O O   . SER B 1 60  ? 24.67014  51.01952 22.36860 1.000 26.58293 ? 60  SER B O   1 
ATOM   1765 C CB  . SER B 1 60  ? 24.05607  50.63065 19.12100 1.000 26.65511 ? 60  SER B CB  1 
ATOM   1766 O OG  . SER B 1 60  ? 25.30298  51.29574 19.25186 1.000 26.42489 ? 60  SER B OG  1 
ATOM   1767 N N   . ASP B 1 61  ? 22.81734  52.07720 21.61125 1.000 24.83784 ? 61  ASP B N   1 
ATOM   1768 C CA  . ASP B 1 61  ? 22.88867  53.13911 22.61682 1.000 26.76056 ? 61  ASP B CA  1 
ATOM   1769 C C   . ASP B 1 61  ? 22.87824  52.56367 24.02705 1.000 30.02982 ? 61  ASP B C   1 
ATOM   1770 O O   . ASP B 1 61  ? 23.51463  53.10846 24.93562 1.000 30.94159 ? 61  ASP B O   1 
ATOM   1771 C CB  . ASP B 1 61  ? 21.71257  54.10946 22.45528 1.000 24.82958 ? 61  ASP B CB  1 
ATOM   1772 C CG  . ASP B 1 61  ? 21.92583  55.13143 21.35865 1.000 29.11258 ? 61  ASP B CG  1 
ATOM   1773 O OD1 . ASP B 1 61  ? 23.02002  55.15338 20.76204 1.000 27.74959 ? 61  ASP B OD1 1 
ATOM   1774 O OD2 . ASP B 1 61  ? 20.98908  55.92969 21.09497 1.000 29.27765 ? 61  ASP B OD2 1 
ATOM   1775 N N   . ARG B 1 62  ? 22.14430  51.46907 24.23253 1.000 26.31941 ? 62  ARG B N   1 
ATOM   1776 C CA  . ARG B 1 62  ? 21.93699  50.89785 25.55689 1.000 28.47482 ? 62  ARG B CA  1 
ATOM   1777 C C   . ARG B 1 62  ? 22.74447  49.62448 25.77081 1.000 26.70179 ? 62  ARG B C   1 
ATOM   1778 O O   . ARG B 1 62  ? 22.44565  48.84790 26.68584 1.000 28.19623 ? 62  ARG B O   1 
ATOM   1779 C CB  . ARG B 1 62  ? 20.44517  50.64919 25.79203 1.000 26.10725 ? 62  ARG B CB  1 
ATOM   1780 C CG  . ARG B 1 62  ? 19.62905  51.94567 25.69872 1.000 27.36766 ? 62  ARG B CG  1 
ATOM   1781 C CD  . ARG B 1 62  ? 18.14544  51.74319 25.95640 1.000 27.53374 ? 62  ARG B CD  1 
ATOM   1782 N NE  . ARG B 1 62  ? 17.87048  51.21044 27.28313 1.000 28.46508 ? 62  ARG B NE  1 
ATOM   1783 C CZ  . ARG B 1 62  ? 16.65336  50.88726 27.71236 1.000 26.54779 ? 62  ARG B CZ  1 
ATOM   1784 N NH1 . ARG B 1 62  ? 15.60680  51.04018 26.91298 1.000 28.07204 ? 62  ARG B NH1 1 
ATOM   1785 N NH2 . ARG B 1 62  ? 16.48659  50.40931 28.93459 1.000 28.65908 ? 62  ARG B NH2 1 
ATOM   1786 N N   . ALA B 1 63  ? 23.78903  49.41735 24.96102 1.000 26.38375 ? 63  ALA B N   1 
ATOM   1787 C CA  . ALA B 1 63  ? 24.61131  48.21725 25.07242 1.000 29.69545 ? 63  ALA B CA  1 
ATOM   1788 C C   . ALA B 1 63  ? 25.18460  48.04027 26.47462 1.000 29.65405 ? 63  ALA B C   1 
ATOM   1789 O O   . ALA B 1 63  ? 25.35363  46.90294 26.93320 1.000 30.50287 ? 63  ALA B O   1 
ATOM   1790 C CB  . ALA B 1 63  ? 25.73697  48.26288 24.03590 1.000 29.92896 ? 63  ALA B CB  1 
ATOM   1791 N N   . GLU B 1 64  ? 25.46815  49.14261 27.17514 1.000 33.67627 ? 64  GLU B N   1 
ATOM   1792 C CA  . GLU B 1 64  ? 26.03851  49.03756 28.51620 1.000 36.29608 ? 64  GLU B CA  1 
ATOM   1793 C C   . GLU B 1 64  ? 25.07890  48.34022 29.47568 1.000 33.45511 ? 64  GLU B C   1 
ATOM   1794 O O   . GLU B 1 64  ? 25.50938  47.58180 30.35154 1.000 33.76328 ? 64  GLU B O   1 
ATOM   1795 C CB  . GLU B 1 64  ? 26.41493  50.42767 29.03674 1.000 36.94801 ? 64  GLU B CB  1 
ATOM   1796 C CG  . GLU B 1 64  ? 27.35984  50.41167 30.24116 1.000 45.82544 ? 64  GLU B CG  1 
ATOM   1797 C CD  . GLU B 1 64  ? 28.66823  49.67751 29.97578 1.000 46.24832 ? 64  GLU B CD  1 
ATOM   1798 O OE1 . GLU B 1 64  ? 29.16609  49.70355 28.82814 1.000 52.14292 ? 64  GLU B OE1 1 
ATOM   1799 O OE2 . GLU B 1 64  ? 29.20551  49.06969 30.92335 1.000 56.40236 ? 64  GLU B OE2 1 
ATOM   1800 N N   . GLU B 1 65  ? 23.77145  48.57414 29.32510 1.000 29.88816 ? 65  GLU B N   1 
ATOM   1801 C CA  . GLU B 1 65  ? 22.81932  47.87673 30.18523 1.000 29.34176 ? 65  GLU B CA  1 
ATOM   1802 C C   . GLU B 1 65  ? 22.86424  46.37435 29.95865 1.000 31.00702 ? 65  GLU B C   1 
ATOM   1803 O O   . GLU B 1 65  ? 22.61964  45.59725 30.89078 1.000 31.91757 ? 65  GLU B O   1 
ATOM   1804 C CB  . GLU B 1 65  ? 21.40742  48.40813 29.95882 1.000 27.64806 ? 65  GLU B CB  1 
ATOM   1805 C CG  . GLU B 1 65  ? 21.24329  49.85167 30.40766 1.000 30.55324 ? 65  GLU B CG  1 
ATOM   1806 C CD  . GLU B 1 65  ? 19.92219  50.44979 29.99100 1.000 28.23877 ? 65  GLU B CD  1 
ATOM   1807 O OE1 . GLU B 1 65  ? 18.87500  49.99176 30.49551 1.000 34.17071 ? 65  GLU B OE1 1 
ATOM   1808 O OE2 . GLU B 1 65  ? 19.93274  51.39628 29.17392 1.000 31.07036 ? 65  GLU B OE2 1 
ATOM   1809 N N   . PHE B 1 66  ? 23.17744  45.94244 28.73665 1.000 27.29578 ? 66  PHE B N   1 
ATOM   1810 C CA  . PHE B 1 66  ? 23.33952  44.51208 28.49942 1.000 26.80312 ? 66  PHE B CA  1 
ATOM   1811 C C   . PHE B 1 66  ? 24.68550  44.00183 28.99898 1.000 30.89401 ? 66  PHE B C   1 
ATOM   1812 O O   . PHE B 1 66  ? 24.76881  42.86925 29.48197 1.000 28.96983 ? 66  PHE B O   1 
ATOM   1813 C CB  . PHE B 1 66  ? 23.17344  44.19105 27.01295 1.000 27.64198 ? 66  PHE B CB  1 
ATOM   1814 C CG  . PHE B 1 66  ? 21.76406  44.37165 26.51256 1.000 24.43380 ? 66  PHE B CG  1 
ATOM   1815 C CD1 . PHE B 1 66  ? 20.85437  43.31400 26.55666 1.000 27.52541 ? 66  PHE B CD1 1 
ATOM   1816 C CD2 . PHE B 1 66  ? 21.34687  45.59325 26.01768 1.000 25.97336 ? 66  PHE B CD2 1 
ATOM   1817 C CE1 . PHE B 1 66  ? 19.54653  43.49093 26.09950 1.000 25.49153 ? 66  PHE B CE1 1 
ATOM   1818 C CE2 . PHE B 1 66  ? 20.04886  45.77602 25.56297 1.000 26.78099 ? 66  PHE B CE2 1 
ATOM   1819 C CZ  . PHE B 1 66  ? 19.14684  44.71996 25.60001 1.000 24.68559 ? 66  PHE B CZ  1 
ATOM   1820 N N   . LYS B 1 67  ? 25.73708  44.81932 28.90872 1.000 32.76523 ? 67  LYS B N   1 
ATOM   1821 C CA  . LYS B 1 67  ? 27.03976  44.39145 29.41660 1.000 33.43809 ? 67  LYS B CA  1 
ATOM   1822 C C   . LYS B 1 67  ? 26.99565  44.15425 30.92245 1.000 33.05741 ? 67  LYS B C   1 
ATOM   1823 O O   . LYS B 1 67  ? 27.62803  43.21850 31.42794 1.000 33.31429 ? 67  LYS B O   1 
ATOM   1824 C CB  . LYS B 1 67  ? 28.11067  45.42696 29.07261 1.000 40.03195 ? 67  LYS B CB  1 
ATOM   1825 C CG  . LYS B 1 67  ? 29.53454  44.90378 29.26521 1.000 47.53473 ? 67  LYS B CG  1 
ATOM   1826 C CD  . LYS B 1 67  ? 30.56465  45.78100 28.56220 1.000 55.00154 ? 67  LYS B CD  1 
ATOM   1827 C CE  . LYS B 1 67  ? 31.73397  46.10849 29.48591 1.000 55.09952 ? 67  LYS B CE  1 
ATOM   1828 N NZ  . LYS B 1 67  ? 32.17154  44.91498 30.26613 1.000 57.03746 ? 67  LYS B NZ  1 
ATOM   1829 N N   . LYS B 1 68  ? 26.25175  44.98731 31.65578 1.000 34.14461 ? 68  LYS B N   1 
ATOM   1830 C CA  . LYS B 1 68  ? 26.11001  44.77906 33.09281 1.000 36.89006 ? 68  LYS B CA  1 
ATOM   1831 C C   . LYS B 1 68  ? 25.37558  43.48700 33.41132 1.000 39.72477 ? 68  LYS B C   1 
ATOM   1832 O O   . LYS B 1 68  ? 25.52309  42.95384 34.51613 1.000 38.49993 ? 68  LYS B O   1 
ATOM   1833 C CB  . LYS B 1 68  ? 25.38832  45.96083 33.73327 1.000 37.31598 ? 68  LYS B CB  1 
ATOM   1834 C CG  . LYS B 1 68  ? 26.28457  47.17280 33.93639 1.000 44.42794 ? 68  LYS B CG  1 
ATOM   1835 C CD  . LYS B 1 68  ? 25.56485  48.29473 34.66962 1.000 51.21423 ? 68  LYS B CD  1 
ATOM   1836 C CE  . LYS B 1 68  ? 26.53900  49.41214 35.05436 1.000 51.51459 ? 68  LYS B CE  1 
ATOM   1837 N NZ  . LYS B 1 68  ? 26.26499  50.68261 34.31682 1.000 53.59773 ? 68  LYS B NZ  1 
ATOM   1838 N N   . LEU B 1 69  ? 24.59213  42.97103 32.47058 1.000 33.79937 ? 69  LEU B N   1 
ATOM   1839 C CA  . LEU B 1 69  ? 23.96837  41.66486 32.60242 1.000 34.04382 ? 69  LEU B CA  1 
ATOM   1840 C C   . LEU B 1 69  ? 24.81793  40.54385 32.01050 1.000 34.25086 ? 69  LEU B C   1 
ATOM   1841 O O   . LEU B 1 69  ? 24.31635  39.42549 31.85203 1.000 33.45408 ? 69  LEU B O   1 
ATOM   1842 C CB  . LEU B 1 69  ? 22.58736  41.67347 31.93828 1.000 33.40179 ? 69  LEU B CB  1 
ATOM   1843 C CG  . LEU B 1 69  ? 21.53314  42.62337 32.50635 1.000 36.73443 ? 69  LEU B CG  1 
ATOM   1844 C CD1 . LEU B 1 69  ? 20.25412  42.53543 31.68450 1.000 32.37092 ? 69  LEU B CD1 1 
ATOM   1845 C CD2 . LEU B 1 69  ? 21.25407  42.30205 33.96798 1.000 37.58425 ? 69  LEU B CD2 1 
ATOM   1846 N N   . ASN B 1 70  ? 26.08819  40.80990 31.69247 1.000 32.13855 ? 70  ASN B N   1 
ATOM   1847 C CA  . ASN B 1 70  ? 26.96005  39.82240 31.05218 1.000 33.28196 ? 70  ASN B CA  1 
ATOM   1848 C C   . ASN B 1 70  ? 26.29092  39.24711 29.80312 1.000 30.07729 ? 70  ASN B C   1 
ATOM   1849 O O   . ASN B 1 70  ? 26.24254  38.03533 29.59003 1.000 31.10167 ? 70  ASN B O   1 
ATOM   1850 C CB  . ASN B 1 70  ? 27.34531  38.70143 32.02869 1.000 35.79675 ? 70  ASN B CB  1 
ATOM   1851 C CG  . ASN B 1 70  ? 28.47097  37.81833 31.49788 1.000 43.01056 ? 70  ASN B CG  1 
ATOM   1852 O OD1 . ASN B 1 70  ? 29.39695  38.30028 30.84358 1.000 47.71515 ? 70  ASN B OD1 1 
ATOM   1853 N ND2 . ASN B 1 70  ? 28.38226  36.51769 31.76028 1.000 46.31286 ? 70  ASN B ND2 1 
ATOM   1854 N N   . CYS B 1 71  ? 25.74687  40.13407 28.97688 1.000 28.02546 ? 71  CYS B N   1 
ATOM   1855 C CA  . CYS B 1 71  ? 24.97542  39.71417 27.81636 1.000 28.99178 ? 71  CYS B CA  1 
ATOM   1856 C C   . CYS B 1 71  ? 25.46111  40.48380 26.59712 1.000 27.83640 ? 71  CYS B C   1 
ATOM   1857 O O   . CYS B 1 71  ? 25.53726  41.71531 26.62598 1.000 26.70575 ? 71  CYS B O   1 
ATOM   1858 C CB  . CYS B 1 71  ? 23.48586  39.95872 28.06496 1.000 30.16808 ? 71  CYS B CB  1 
ATOM   1859 S SG  . CYS B 1 71  ? 22.37337  39.66648 26.65741 1.000 27.68718 ? 71  CYS B SG  1 
ATOM   1860 N N   . GLN B 1 72  ? 25.80422  39.75212 25.54305 1.000 26.11077 ? 72  GLN B N   1 
ATOM   1861 C CA  . GLN B 1 72  ? 26.27018  40.32335 24.28555 1.000 26.56427 ? 72  GLN B CA  1 
ATOM   1862 C C   . GLN B 1 72  ? 25.08456  40.50900 23.34858 1.000 24.15036 ? 72  GLN B C   1 
ATOM   1863 O O   . GLN B 1 72  ? 24.28071  39.59106 23.17959 1.000 26.73411 ? 72  GLN B O   1 
ATOM   1864 C CB  . GLN B 1 72  ? 27.29775  39.38885 23.63486 1.000 27.55305 ? 72  GLN B CB  1 
ATOM   1865 C CG  . GLN B 1 72  ? 27.76122  39.83095 22.23630 1.000 28.61480 ? 72  GLN B CG  1 
ATOM   1866 C CD  . GLN B 1 72  ? 28.60362  41.07762 22.28196 1.000 32.21561 ? 72  GLN B CD  1 
ATOM   1867 O OE1 . GLN B 1 72  ? 29.60488  41.13193 22.99747 1.000 34.33422 ? 72  GLN B OE1 1 
ATOM   1868 N NE2 . GLN B 1 72  ? 28.19805  42.10124 21.53314 1.000 29.74790 ? 72  GLN B NE2 1 
ATOM   1869 N N   . VAL B 1 73  ? 24.98108  41.67962 22.73077 1.000 25.16995 ? 73  VAL B N   1 
ATOM   1870 C CA  . VAL B 1 73  ? 23.94720  41.93583 21.73136 1.000 23.21216 ? 73  VAL B CA  1 
ATOM   1871 C C   . VAL B 1 73  ? 24.57900  41.86590 20.34897 1.000 24.13974 ? 73  VAL B C   1 
ATOM   1872 O O   . VAL B 1 73  ? 25.64196  42.45135 20.11561 1.000 25.90293 ? 73  VAL B O   1 
ATOM   1873 C CB  . VAL B 1 73  ? 23.27339  43.30116 21.94914 1.000 23.63073 ? 73  VAL B CB  1 
ATOM   1874 C CG1 . VAL B 1 73  ? 22.32820  43.62182 20.76911 1.000 24.38313 ? 73  VAL B CG1 1 
ATOM   1875 C CG2 . VAL B 1 73  ? 22.50624  43.31554 23.28912 1.000 23.33703 ? 73  VAL B CG2 1 
ATOM   1876 N N   . ILE B 1 74  ? 23.92130  41.15902 19.43062 1.000 22.89984 ? 74  ILE B N   1 
ATOM   1877 C CA  . ILE B 1 74  ? 24.38426  41.01702 18.05238 1.000 22.25298 ? 74  ILE B CA  1 
ATOM   1878 C C   . ILE B 1 74  ? 23.19848  41.22361 17.12032 1.000 22.59150 ? 74  ILE B C   1 
ATOM   1879 O O   . ILE B 1 74  ? 22.18016  40.54023 17.25764 1.000 22.69999 ? 74  ILE B O   1 
ATOM   1880 C CB  . ILE B 1 74  ? 25.00662  39.62893 17.80239 1.000 23.66218 ? 74  ILE B CB  1 
ATOM   1881 C CG1 . ILE B 1 74  ? 26.09307  39.32378 18.83881 1.000 24.48697 ? 74  ILE B CG1 1 
ATOM   1882 C CG2 . ILE B 1 74  ? 25.54032  39.52953 16.36402 1.000 23.79722 ? 74  ILE B CG2 1 
ATOM   1883 C CD1 . ILE B 1 74  ? 26.63079  37.89317 18.75054 1.000 27.22980 ? 74  ILE B CD1 1 
ATOM   1884 N N   . GLY B 1 75  ? 23.32731  42.15980 16.16980 1.000 22.61778 ? 75  GLY B N   1 
ATOM   1885 C CA  . GLY B 1 75  ? 22.33359  42.33267 15.13111 1.000 23.67152 ? 75  GLY B CA  1 
ATOM   1886 C C   . GLY B 1 75  ? 22.76081  41.66604 13.82890 1.000 25.20858 ? 75  GLY B C   1 
ATOM   1887 O O   . GLY B 1 75  ? 23.93558  41.37524 13.62962 1.000 25.03329 ? 75  GLY B O   1 
ATOM   1888 N N   . ALA B 1 76  ? 21.79578  41.43978 12.93387 1.000 24.09860 ? 76  ALA B N   1 
ATOM   1889 C CA  . ALA B 1 76  ? 22.09518  40.73384 11.68838 1.000 24.02712 ? 76  ALA B CA  1 
ATOM   1890 C C   . ALA B 1 76  ? 21.06715  41.07370 10.61328 1.000 25.70648 ? 76  ALA B C   1 
ATOM   1891 O O   . ALA B 1 76  ? 19.88451  41.23685 10.90442 1.000 25.04832 ? 76  ALA B O   1 
ATOM   1892 C CB  . ALA B 1 76  ? 22.11763  39.21664 11.90720 1.000 24.09246 ? 76  ALA B CB  1 
ATOM   1893 N N   . SER B 1 77  ? 21.52426  41.13955 9.36126  1.000 24.97837 ? 77  SER B N   1 
ATOM   1894 C CA  . SER B 1 77  ? 20.61134  41.17161 8.22549  1.000 26.78883 ? 77  SER B CA  1 
ATOM   1895 C C   . SER B 1 77  ? 21.26414  40.46600 7.04446  1.000 27.19614 ? 77  SER B C   1 
ATOM   1896 O O   . SER B 1 77  ? 22.45484  40.14068 7.05953  1.000 27.79220 ? 77  SER B O   1 
ATOM   1897 C CB  . SER B 1 77  ? 20.22047  42.60060 7.82050  1.000 28.13083 ? 77  SER B CB  1 
ATOM   1898 O OG  . SER B 1 77  ? 21.22412  43.19955 7.01585  1.000 28.51146 ? 77  SER B OG  1 
ATOM   1899 N N   . VAL B 1 78  ? 20.46299  40.24913 5.99684  1.000 28.50174 ? 78  VAL B N   1 
ATOM   1900 C CA  . VAL B 1 78  ? 20.96554  39.57453 4.80150  1.000 28.71357 ? 78  VAL B CA  1 
ATOM   1901 C C   . VAL B 1 78  ? 21.81005  40.48107 3.91961  1.000 32.38537 ? 78  VAL B C   1 
ATOM   1902 O O   . VAL B 1 78  ? 22.30938  40.02209 2.88475  1.000 31.53151 ? 78  VAL B O   1 
ATOM   1903 C CB  . VAL B 1 78  ? 19.79980  38.99372 3.97256  1.000 29.50296 ? 78  VAL B CB  1 
ATOM   1904 C CG1 . VAL B 1 78  ? 19.00421  37.97241 4.79763  1.000 31.86366 ? 78  VAL B CG1 1 
ATOM   1905 C CG2 . VAL B 1 78  ? 18.89195  40.10423 3.46090  1.000 31.56531 ? 78  VAL B CG2 1 
ATOM   1906 N N   . ASP B 1 79  ? 21.98004  41.75440 4.27880  1.000 30.10055 ? 79  ASP B N   1 
ATOM   1907 C CA  . ASP B 1 79  ? 22.82988  42.63764 3.48610  1.000 31.11083 ? 79  ASP B CA  1 
ATOM   1908 C C   . ASP B 1 79  ? 24.29746  42.23075 3.57807  1.000 32.13631 ? 79  ASP B C   1 
ATOM   1909 O O   . ASP B 1 79  ? 24.72621  41.53789 4.50329  1.000 32.41441 ? 79  ASP B O   1 
ATOM   1910 C CB  . ASP B 1 79  ? 22.70225  44.09003 3.94846  1.000 29.57971 ? 79  ASP B CB  1 
ATOM   1911 C CG  . ASP B 1 79  ? 21.32288  44.62673 3.77944  1.000 30.26932 ? 79  ASP B CG  1 
ATOM   1912 O OD1 . ASP B 1 79  ? 20.50860  44.45258 4.71027  1.000 35.50645 ? 79  ASP B OD1 1 
ATOM   1913 O OD2 . ASP B 1 79  ? 21.04255  45.22291 2.71896  1.000 35.62019 ? 79  ASP B OD2 1 
ATOM   1914 N N   . SER B 1 80  ? 25.08068  42.70463 2.61016  1.000 30.94202 ? 80  SER B N   1 
ATOM   1915 C CA  . SER B 1 80  ? 26.51559  42.46620 2.62419  1.000 30.31367 ? 80  SER B CA  1 
ATOM   1916 C C   . SER B 1 80  ? 27.18562  43.19806 3.78430  1.000 33.14784 ? 80  SER B C   1 
ATOM   1917 O O   . SER B 1 80  ? 26.66632  44.18121 4.32958  1.000 31.50223 ? 80  SER B O   1 
ATOM   1918 C CB  . SER B 1 80  ? 27.15742  42.91444 1.30862  1.000 33.59079 ? 80  SER B CB  1 
ATOM   1919 O OG  . SER B 1 80  ? 27.50714  44.28610 1.35488  1.000 37.02431 ? 80  SER B OG  1 
ATOM   1920 N N   . HIS B 1 81  ? 28.38219  42.72696 4.13637  1.000 29.83966 ? 81  HIS B N   1 
ATOM   1921 C CA  . HIS B 1 81  ? 29.13163  43.39416 5.19224  1.000 32.31565 ? 81  HIS B CA  1 
ATOM   1922 C C   . HIS B 1 81  ? 29.60967  44.76953 4.74648  1.000 32.06901 ? 81  HIS B C   1 
ATOM   1923 O O   . HIS B 1 81  ? 29.75178  45.67052 5.58405  1.000 29.36973 ? 81  HIS B O   1 
ATOM   1924 C CB  . HIS B 1 81  ? 30.29773  42.51712 5.67452  1.000 32.97248 ? 81  HIS B CB  1 
ATOM   1925 C CG  . HIS B 1 81  ? 31.37649  42.28403 4.65530  1.000 36.32153 ? 81  HIS B CG  1 
ATOM   1926 N ND1 . HIS B 1 81  ? 31.13610  41.70305 3.42723  1.000 36.39819 ? 81  HIS B ND1 1 
ATOM   1927 C CD2 . HIS B 1 81  ? 32.71164  42.51392 4.70587  1.000 34.10770 ? 81  HIS B CD2 1 
ATOM   1928 C CE1 . HIS B 1 81  ? 32.27078  41.61123 2.75465  1.000 35.09712 ? 81  HIS B CE1 1 
ATOM   1929 N NE2 . HIS B 1 81  ? 33.24344  42.09419 3.50909  1.000 37.77343 ? 81  HIS B NE2 1 
ATOM   1930 N N   . PHE B 1 82  ? 29.82482  44.96392 3.43700  1.000 31.40063 ? 82  PHE B N   1 
ATOM   1931 C CA  . PHE B 1 82  ? 30.14714  46.30164 2.93484  1.000 31.83240 ? 82  PHE B CA  1 
ATOM   1932 C C   . PHE B 1 82  ? 28.98642  47.26635 3.14193  1.000 29.72597 ? 82  PHE B C   1 
ATOM   1933 O O   . PHE B 1 82  ? 29.19815  48.44139 3.46836  1.000 29.98287 ? 82  PHE B O   1 
ATOM   1934 C CB  . PHE B 1 82  ? 30.50695  46.24647 1.44619  1.000 29.88315 ? 82  PHE B CB  1 
ATOM   1935 C CG  . PHE B 1 82  ? 31.86345  45.67755 1.17204  1.000 32.84112 ? 82  PHE B CG  1 
ATOM   1936 C CD1 . PHE B 1 82  ? 33.00565  46.40342 1.46570  1.000 34.75380 ? 82  PHE B CD1 1 
ATOM   1937 C CD2 . PHE B 1 82  ? 31.99521  44.41599 0.62419  1.000 34.06946 ? 82  PHE B CD2 1 
ATOM   1938 C CE1 . PHE B 1 82  ? 34.25377  45.87886 1.22030  1.000 33.31790 ? 82  PHE B CE1 1 
ATOM   1939 C CE2 . PHE B 1 82  ? 33.24560  43.88538 0.37062  1.000 34.40092 ? 82  PHE B CE2 1 
ATOM   1940 C CZ  . PHE B 1 82  ? 34.37489  44.61343 0.67668  1.000 33.05777 ? 82  PHE B CZ  1 
ATOM   1941 N N   . SER B 1 83  ? 27.75869  46.79975 2.90102  1.000 28.89606 ? 83  SER B N   1 
ATOM   1942 C CA  . SER B 1 83  ? 26.57235  47.60644 3.16277  1.000 30.03333 ? 83  SER B CA  1 
ATOM   1943 C C   . SER B 1 83  ? 26.49344  48.02625 4.62790  1.000 29.44590 ? 83  SER B C   1 
ATOM   1944 O O   . SER B 1 83  ? 26.20798  49.19185 4.94131  1.000 26.59990 ? 83  SER B O   1 
ATOM   1945 C CB  . SER B 1 83  ? 25.32868  46.81698 2.76842  1.000 29.35672 ? 83  SER B CB  1 
ATOM   1946 O OG  . SER B 1 83  ? 24.16687  47.58324 2.97871  1.000 35.57221 ? 83  SER B OG  1 
ATOM   1947 N N   . HIS B 1 84  ? 26.69527  47.07622 5.54288  1.000 27.25754 ? 84  HIS B N   1 
ATOM   1948 C CA  . HIS B 1 84  ? 26.71671  47.40784 6.96588  1.000 27.22749 ? 84  HIS B CA  1 
ATOM   1949 C C   . HIS B 1 84  ? 27.71655  48.52188 7.24831  1.000 28.95867 ? 84  HIS B C   1 
ATOM   1950 O O   . HIS B 1 84  ? 27.40490  49.49651 7.93947  1.000 25.68102 ? 84  HIS B O   1 
ATOM   1951 C CB  . HIS B 1 84  ? 27.08178  46.17784 7.79724  1.000 24.53239 ? 84  HIS B CB  1 
ATOM   1952 C CG  . HIS B 1 84  ? 26.01454  45.13214 7.86352  1.000 24.79221 ? 84  HIS B CG  1 
ATOM   1953 N ND1 . HIS B 1 84  ? 24.79001  45.26433 7.24633  1.000 26.67322 ? 84  HIS B ND1 1 
ATOM   1954 C CD2 . HIS B 1 84  ? 25.99409  43.93065 8.48709  1.000 25.16902 ? 84  HIS B CD2 1 
ATOM   1955 C CE1 . HIS B 1 84  ? 24.06203  44.18612 7.48329  1.000 26.60960 ? 84  HIS B CE1 1 
ATOM   1956 N NE2 . HIS B 1 84  ? 24.76791  43.36499 8.23875  1.000 26.68426 ? 84  HIS B NE2 1 
ATOM   1957 N N   . LEU B 1 85  ? 28.93798  48.38485 6.72155  1.000 28.03892 ? 85  LEU B N   1 
ATOM   1958 C CA  . LEU B 1 85  ? 29.97466  49.37640 6.98676  1.000 28.88058 ? 85  LEU B CA  1 
ATOM   1959 C C   . LEU B 1 85  ? 29.59871  50.73959 6.41469  1.000 26.95270 ? 85  LEU B C   1 
ATOM   1960 O O   . LEU B 1 85  ? 29.81771  51.77159 7.05607  1.000 28.63395 ? 85  LEU B O   1 
ATOM   1961 C CB  . LEU B 1 85  ? 31.30921  48.89466 6.41086  1.000 30.50034 ? 85  LEU B CB  1 
ATOM   1962 C CG  . LEU B 1 85  ? 32.48484  49.84980 6.62795  1.000 29.19840 ? 85  LEU B CG  1 
ATOM   1963 C CD1 . LEU B 1 85  ? 32.75851  50.04851 8.10191  1.000 33.87992 ? 85  LEU B CD1 1 
ATOM   1964 C CD2 . LEU B 1 85  ? 33.72042  49.33586 5.89554  1.000 36.31553 ? 85  LEU B CD2 1 
ATOM   1965 N N   . ALA B 1 86  ? 29.01700  50.76322 5.21494  1.000 28.32291 ? 86  ALA B N   1 
ATOM   1966 C CA  . ALA B 1 86  ? 28.57939  52.03172 4.63964  1.000 25.74646 ? 86  ALA B CA  1 
ATOM   1967 C C   . ALA B 1 86  ? 27.51295  52.69238 5.50708  1.000 26.96138 ? 86  ALA B C   1 
ATOM   1968 O O   . ALA B 1 86  ? 27.49833  53.91945 5.65799  1.000 27.20254 ? 86  ALA B O   1 
ATOM   1969 C CB  . ALA B 1 86  ? 28.05773  51.80926 3.22034  1.000 29.56729 ? 86  ALA B CB  1 
ATOM   1970 N N   . TRP B 1 87  ? 26.61822  51.89117 6.09012  1.000 26.80185 ? 87  TRP B N   1 
ATOM   1971 C CA  . TRP B 1 87  ? 25.55458  52.44541 6.92586  1.000 26.81582 ? 87  TRP B CA  1 
ATOM   1972 C C   . TRP B 1 87  ? 26.10929  52.97422 8.24216  1.000 27.47036 ? 87  TRP B C   1 
ATOM   1973 O O   . TRP B 1 87  ? 25.68739  54.03407 8.71787  1.000 25.78537 ? 87  TRP B O   1 
ATOM   1974 C CB  . TRP B 1 87  ? 24.48413  51.38286 7.17859  1.000 26.45351 ? 87  TRP B CB  1 
ATOM   1975 C CG  . TRP B 1 87  ? 23.09957  51.93264 7.38204  1.000 26.39486 ? 87  TRP B CG  1 
ATOM   1976 C CD1 . TRP B 1 87  ? 22.65913  53.20317 7.09739  1.000 28.29223 ? 87  TRP B CD1 1 
ATOM   1977 C CD2 . TRP B 1 87  ? 21.97193  51.22559 7.90604  1.000 26.52232 ? 87  TRP B CD2 1 
ATOM   1978 N NE1 . TRP B 1 87  ? 21.32373  53.31885 7.41188  1.000 28.15338 ? 87  TRP B NE1 1 
ATOM   1979 C CE2 . TRP B 1 87  ? 20.87883  52.11746 7.90546  1.000 27.57587 ? 87  TRP B CE2 1 
ATOM   1980 C CE3 . TRP B 1 87  ? 21.77818  49.92079 8.36941  1.000 26.34060 ? 87  TRP B CE3 1 
ATOM   1981 C CZ2 . TRP B 1 87  ? 19.61405  51.74821 8.36733  1.000 29.18685 ? 87  TRP B CZ2 1 
ATOM   1982 C CZ3 . TRP B 1 87  ? 20.51909  49.55314 8.82651  1.000 26.89357 ? 87  TRP B CZ3 1 
ATOM   1983 C CH2 . TRP B 1 87  ? 19.45307  50.46419 8.81931  1.000 25.89968 ? 87  TRP B CH2 1 
ATOM   1984 N N   . VAL B 1 88  ? 27.05791  52.24741 8.84236  1.000 25.25210 ? 88  VAL B N   1 
ATOM   1985 C CA  . VAL B 1 88  ? 27.70633  52.71016 10.06672 1.000 23.10109 ? 88  VAL B CA  1 
ATOM   1986 C C   . VAL B 1 88  ? 28.45294  54.01163 9.80960  1.000 28.61611 ? 88  VAL B C   1 
ATOM   1987 O O   . VAL B 1 88  ? 28.43596  54.93532 10.63740 1.000 27.87079 ? 88  VAL B O   1 
ATOM   1988 C CB  . VAL B 1 88  ? 28.64899  51.61800 10.61059 1.000 27.74322 ? 88  VAL B CB  1 
ATOM   1989 C CG1 . VAL B 1 88  ? 29.60899  52.19906 11.65704 1.000 27.84517 ? 88  VAL B CG1 1 
ATOM   1990 C CG2 . VAL B 1 88  ? 27.84457  50.45134 11.18060 1.000 23.86718 ? 88  VAL B CG2 1 
ATOM   1991 N N   . ASN B 1 89  ? 29.11380  54.11030 8.65510  1.000 27.50309 ? 89  ASN B N   1 
ATOM   1992 C CA  . ASN B 1 89  ? 29.90776  55.28793 8.32091  1.000 28.18197 ? 89  ASN B CA  1 
ATOM   1993 C C   . ASN B 1 89  ? 29.05611  56.46069 7.86804  1.000 30.13308 ? 89  ASN B C   1 
ATOM   1994 O O   . ASN B 1 89  ? 29.60086  57.53998 7.61644  1.000 32.20660 ? 89  ASN B O   1 
ATOM   1995 C CB  . ASN B 1 89  ? 30.93006  54.95426 7.23106  1.000 30.04428 ? 89  ASN B CB  1 
ATOM   1996 C CG  . ASN B 1 89  ? 32.11568  54.16379 7.75829  1.000 33.93347 ? 89  ASN B CG  1 
ATOM   1997 O OD1 . ASN B 1 89  ? 32.45338  54.24118 8.93972  1.000 36.81233 ? 89  ASN B OD1 1 
ATOM   1998 N ND2 . ASN B 1 89  ? 32.77917  53.42753 6.86954  1.000 32.36108 ? 89  ASN B ND2 1 
ATOM   1999 N N   . THR B 1 90  ? 27.74808  56.27451 7.74608  1.000 26.70105 ? 90  THR B N   1 
ATOM   2000 C CA  . THR B 1 90  ? 26.83943  57.38072 7.47421  1.000 27.75110 ? 90  THR B CA  1 
ATOM   2001 C C   . THR B 1 90  ? 26.39520  57.97808 8.80005  1.000 27.61876 ? 90  THR B C   1 
ATOM   2002 O O   . THR B 1 90  ? 25.85054  57.25140 9.63974  1.000 26.31325 ? 90  THR B O   1 
ATOM   2003 C CB  . THR B 1 90  ? 25.63545  56.89010 6.68620  1.000 28.46399 ? 90  THR B CB  1 
ATOM   2004 O OG1 . THR B 1 90  ? 26.09004  56.31594 5.45475  1.000 30.31408 ? 90  THR B OG1 1 
ATOM   2005 C CG2 . THR B 1 90  ? 24.67354  58.03216 6.38238  1.000 25.91749 ? 90  THR B CG2 1 
ATOM   2006 N N   . PRO B 1 91  ? 26.62321  59.27008 9.04750  1.000 28.23540 ? 91  PRO B N   1 
ATOM   2007 C CA  . PRO B 1 91  ? 26.24786  59.83733 10.34628 1.000 27.56214 ? 91  PRO B CA  1 
ATOM   2008 C C   . PRO B 1 91  ? 24.76064  59.69834 10.62140 1.000 26.05934 ? 91  PRO B C   1 
ATOM   2009 O O   . PRO B 1 91  ? 23.92263  59.78411 9.71830  1.000 28.22016 ? 91  PRO B O   1 
ATOM   2010 C CB  . PRO B 1 91  ? 26.64883  61.31444 10.21916 1.000 29.55265 ? 91  PRO B CB  1 
ATOM   2011 C CG  . PRO B 1 91  ? 27.75046  61.30639 9.21352  1.000 33.59420 ? 91  PRO B CG  1 
ATOM   2012 C CD  . PRO B 1 91  ? 27.38215  60.22732 8.22201  1.000 30.45244 ? 91  PRO B CD  1 
ATOM   2013 N N   . LYS B 1 92  ? 24.44817  59.51519 11.90424 1.000 27.49342 ? 92  LYS B N   1 
ATOM   2014 C CA  . LYS B 1 92  ? 23.06184  59.42665 12.33987 1.000 28.58716 ? 92  LYS B CA  1 
ATOM   2015 C C   . LYS B 1 92  ? 22.27730  60.66519 11.91707 1.000 31.57694 ? 92  LYS B C   1 
ATOM   2016 O O   . LYS B 1 92  ? 21.10792  60.56236 11.52825 1.000 32.27634 ? 92  LYS B O   1 
ATOM   2017 C CB  . LYS B 1 92  ? 23.02725  59.22631 13.85878 1.000 33.01268 ? 92  LYS B CB  1 
ATOM   2018 C CG  . LYS B 1 92  ? 21.70072  58.78075 14.42453 1.000 37.69929 ? 92  LYS B CG  1 
ATOM   2019 C CD  . LYS B 1 92  ? 21.84634  58.35410 15.88002 1.000 33.47719 ? 92  LYS B CD  1 
ATOM   2020 C CE  . LYS B 1 92  ? 22.29115  59.51206 16.76716 1.000 39.08729 ? 92  LYS B CE  1 
ATOM   2021 N NZ  . LYS B 1 92  ? 22.38340  59.12296 18.21025 1.000 34.06611 ? 92  LYS B NZ  1 
ATOM   2022 N N   . LYS B 1 93  ? 22.92102  61.84124 11.95930 1.000 30.15156 ? 93  LYS B N   1 
ATOM   2023 C CA  . LYS B 1 93  ? 22.30944  63.08951 11.49710 1.000 34.86402 ? 93  LYS B CA  1 
ATOM   2024 C C   . LYS B 1 93  ? 21.80270  62.99824 10.06888 1.000 35.07450 ? 93  LYS B C   1 
ATOM   2025 O O   . LYS B 1 93  ? 20.89555  63.74863 9.68344  1.000 34.34009 ? 93  LYS B O   1 
ATOM   2026 C CB  . LYS B 1 93  ? 23.32024  64.24205 11.56026 1.000 36.31618 ? 93  LYS B CB  1 
ATOM   2027 C CG  . LYS B 1 93  ? 23.58494  64.81161 12.93503 1.000 43.22524 ? 93  LYS B CG  1 
ATOM   2028 C CD  . LYS B 1 93  ? 24.58552  65.96900 12.86403 1.000 46.34321 ? 93  LYS B CD  1 
ATOM   2029 C CE  . LYS B 1 93  ? 25.41778  65.93912 11.58078 1.000 50.76905 ? 93  LYS B CE  1 
ATOM   2030 N NZ  . LYS B 1 93  ? 26.69729  66.70298 11.70654 1.000 53.80879 ? 93  LYS B NZ  1 
ATOM   2031 N N   . GLN B 1 94  ? 22.41781  62.13930 9.25221  1.000 28.88310 ? 94  GLN B N   1 
ATOM   2032 C CA  . GLN B 1 94  ? 22.09173  62.03718 7.83944  1.000 31.42649 ? 94  GLN B CA  1 
ATOM   2033 C C   . GLN B 1 94  ? 21.30745  60.77463 7.51338  1.000 29.85863 ? 94  GLN B C   1 
ATOM   2034 O O   . GLN B 1 94  ? 21.22403  60.39010 6.34445  1.000 33.85235 ? 94  GLN B O   1 
ATOM   2035 C CB  . GLN B 1 94  ? 23.36679  62.10468 7.00055  1.000 33.64417 ? 94  GLN B CB  1 
ATOM   2036 C CG  . GLN B 1 94  ? 24.01973  63.47329 7.02691  1.000 42.43461 ? 94  GLN B CG  1 
ATOM   2037 C CD  . GLN B 1 94  ? 25.52455  63.39109 6.98982  1.000 46.25014 ? 94  GLN B CD  1 
ATOM   2038 O OE1 . GLN B 1 94  ? 26.09597  62.62975 6.20594  1.000 52.13833 ? 94  GLN B OE1 1 
ATOM   2039 N NE2 . GLN B 1 94  ? 26.18067  64.16730 7.84425  1.000 51.96349 ? 94  GLN B NE2 1 
ATOM   2040 N N   . GLY B 1 95  ? 20.72035  60.13006 8.51351  1.000 28.31966 ? 95  GLY B N   1 
ATOM   2041 C CA  . GLY B 1 95  ? 19.93037  58.94426 8.26670  1.000 31.00811 ? 95  GLY B CA  1 
ATOM   2042 C C   . GLY B 1 95  ? 20.68702  57.64045 8.35841  1.000 31.84320 ? 95  GLY B C   1 
ATOM   2043 O O   . GLY B 1 95  ? 20.12540  56.59244 8.01587  1.000 34.91016 ? 95  GLY B O   1 
ATOM   2044 N N   . GLY B 1 96  ? 21.94060  57.66946 8.80667  1.000 27.25886 ? 96  GLY B N   1 
ATOM   2045 C CA  . GLY B 1 96  ? 22.73356  56.47140 8.96653  1.000 25.83156 ? 96  GLY B CA  1 
ATOM   2046 C C   . GLY B 1 96  ? 22.68144  55.93023 10.38511 1.000 26.27607 ? 96  GLY B C   1 
ATOM   2047 O O   . GLY B 1 96  ? 21.95500  56.41718 11.25439 1.000 26.57393 ? 96  GLY B O   1 
ATOM   2048 N N   . LEU B 1 97  ? 23.47153  54.87437 10.61324 1.000 25.66445 ? 97  LEU B N   1 
ATOM   2049 C CA  . LEU B 1 97  ? 23.55992  54.31098 11.95379 1.000 24.36164 ? 97  LEU B CA  1 
ATOM   2050 C C   . LEU B 1 97  ? 24.50424  55.09699 12.85408 1.000 24.83741 ? 97  LEU B C   1 
ATOM   2051 O O   . LEU B 1 97  ? 24.27437  55.17886 14.06483 1.000 25.79503 ? 97  LEU B O   1 
ATOM   2052 C CB  . LEU B 1 97  ? 24.02683  52.85313 11.89512 1.000 24.48620 ? 97  LEU B CB  1 
ATOM   2053 C CG  . LEU B 1 97  ? 23.09435  51.86032 11.20703 1.000 26.18951 ? 97  LEU B CG  1 
ATOM   2054 C CD1 . LEU B 1 97  ? 23.71209  50.46303 11.24229 1.000 24.13713 ? 97  LEU B CD1 1 
ATOM   2055 C CD2 . LEU B 1 97  ? 21.72777  51.84256 11.86371 1.000 27.08110 ? 97  LEU B CD2 1 
ATOM   2056 N N   . GLY B 1 98  ? 25.57155  55.66430 12.30400 1.000 24.04472 ? 98  GLY B N   1 
ATOM   2057 C CA  . GLY B 1 98  ? 26.61923  56.20435 13.13900 1.000 25.55738 ? 98  GLY B CA  1 
ATOM   2058 C C   . GLY B 1 98  ? 27.39929  55.10378 13.83875 1.000 26.23548 ? 98  GLY B C   1 
ATOM   2059 O O   . GLY B 1 98  ? 27.16802  53.90907 13.61296 1.000 26.12681 ? 98  GLY B O   1 
ATOM   2060 N N   . PRO B 1 99  ? 28.34065  55.48851 14.70383 1.000 27.38153 ? 99  PRO B N   1 
ATOM   2061 C CA  . PRO B 1 99  ? 29.16899  54.48956 15.39578 1.000 27.22188 ? 99  PRO B CA  1 
ATOM   2062 C C   . PRO B 1 99  ? 28.32726  53.55402 16.25110 1.000 27.66766 ? 99  PRO B C   1 
ATOM   2063 O O   . PRO B 1 99  ? 27.36462  53.96922 16.89755 1.000 27.47209 ? 99  PRO B O   1 
ATOM   2064 C CB  . PRO B 1 99  ? 30.10766  55.33930 16.26024 1.000 30.88127 ? 99  PRO B CB  1 
ATOM   2065 C CG  . PRO B 1 99  ? 30.12295  56.67914 15.60755 1.000 33.34188 ? 99  PRO B CG  1 
ATOM   2066 C CD  . PRO B 1 99  ? 28.75739  56.86787 15.00625 1.000 27.70982 ? 99  PRO B CD  1 
ATOM   2067 N N   . MET B 1 100 ? 28.71669  52.28150 16.26655 1.000 26.61662 ? 100 MET B N   1 
ATOM   2068 C CA  . MET B 1 100 ? 27.94241  51.23138 16.90901 1.000 26.71373 ? 100 MET B CA  1 
ATOM   2069 C C   . MET B 1 100 ? 28.68932  50.65639 18.10530 1.000 29.72576 ? 100 MET B C   1 
ATOM   2070 O O   . MET B 1 100 ? 29.91757  50.54899 18.09644 1.000 30.18928 ? 100 MET B O   1 
ATOM   2071 C CB  . MET B 1 100 ? 27.64071  50.10020 15.91624 1.000 26.82791 ? 100 MET B CB  1 
ATOM   2072 C CG  . MET B 1 100 ? 26.69239  50.49031 14.79740 1.000 29.37503 ? 100 MET B CG  1 
ATOM   2073 S SD  . MET B 1 100 ? 24.97121  50.48508 15.33542 1.000 26.34029 ? 100 MET B SD  1 
ATOM   2074 C CE  . MET B 1 100 ? 24.69859  52.22334 15.71691 1.000 27.22983 ? 100 MET B CE  1 
ATOM   2075 N N   . ASN B 1 101 ? 27.93115  50.25213 19.12344 1.000 26.28243 ? 101 ASN B N   1 
ATOM   2076 C CA  . ASN B 1 101 ? 28.48042  49.52587 20.25963 1.000 25.16028 ? 101 ASN B CA  1 
ATOM   2077 C C   . ASN B 1 101 ? 28.24860  48.02802 20.17050 1.000 29.48799 ? 101 ASN B C   1 
ATOM   2078 O O   . ASN B 1 101 ? 28.64569  47.29835 21.08443 1.000 29.15457 ? 101 ASN B O   1 
ATOM   2079 C CB  . ASN B 1 101 ? 27.88585  50.06257 21.56126 1.000 27.18718 ? 101 ASN B CB  1 
ATOM   2080 C CG  . ASN B 1 101 ? 28.26234  51.49979 21.80351 1.000 31.88309 ? 101 ASN B CG  1 
ATOM   2081 O OD1 . ASN B 1 101 ? 29.41530  51.88753 21.59531 1.000 33.02096 ? 101 ASN B OD1 1 
ATOM   2082 N ND2 . ASN B 1 101 ? 27.29462  52.30886 22.21424 1.000 29.55834 ? 101 ASN B ND2 1 
ATOM   2083 N N   . ILE B 1 102 ? 27.60579  47.55760 19.10744 1.000 27.44801 ? 102 ILE B N   1 
ATOM   2084 C CA  . ILE B 1 102 ? 27.29969  46.14062 18.93246 1.000 25.43898 ? 102 ILE B CA  1 
ATOM   2085 C C   . ILE B 1 102 ? 27.79026  45.69210 17.56284 1.000 26.76692 ? 102 ILE B C   1 
ATOM   2086 O O   . ILE B 1 102 ? 27.84871  46.50686 16.63285 1.000 25.42880 ? 102 ILE B O   1 
ATOM   2087 C CB  . ILE B 1 102 ? 25.79310  45.87018 19.07146 1.000 25.85567 ? 102 ILE B CB  1 
ATOM   2088 C CG1 . ILE B 1 102 ? 25.00859  46.72288 18.06138 1.000 26.08136 ? 102 ILE B CG1 1 
ATOM   2089 C CG2 . ILE B 1 102 ? 25.34296  46.12160 20.49474 1.000 24.96406 ? 102 ILE B CG2 1 
ATOM   2090 C CD1 . ILE B 1 102 ? 23.51323  46.41954 18.00839 1.000 25.02996 ? 102 ILE B CD1 1 
ATOM   2091 N N   . PRO B 1 103 ? 28.12841  44.42038 17.38865 1.000 26.75800 ? 103 PRO B N   1 
ATOM   2092 C CA  . PRO B 1 103 ? 28.45575  43.92154 16.05035 1.000 26.99668 ? 103 PRO B CA  1 
ATOM   2093 C C   . PRO B 1 103 ? 27.20886  43.72752 15.20444 1.000 25.67934 ? 103 PRO B C   1 
ATOM   2094 O O   . PRO B 1 103 ? 26.11174  43.46675 15.70605 1.000 25.39994 ? 103 PRO B O   1 
ATOM   2095 C CB  . PRO B 1 103 ? 29.14830  42.58185 16.32921 1.000 27.00551 ? 103 PRO B CB  1 
ATOM   2096 C CG  . PRO B 1 103 ? 28.63609  42.15316 17.65762 1.000 29.14176 ? 103 PRO B CG  1 
ATOM   2097 C CD  . PRO B 1 103 ? 28.27677  43.38833 18.43456 1.000 24.83055 ? 103 PRO B CD  1 
ATOM   2098 N N   . LEU B 1 104 ? 27.39227  43.86361 13.89398 1.000 25.74941 ? 104 LEU B N   1 
ATOM   2099 C CA  . LEU B 1 104 ? 26.32180  43.66274 12.92023 1.000 23.81023 ? 104 LEU B CA  1 
ATOM   2100 C C   . LEU B 1 104 ? 26.76859  42.59335 11.93594 1.000 25.88434 ? 104 LEU B C   1 
ATOM   2101 O O   . LEU B 1 104 ? 27.70754  42.81064 11.16333 1.000 27.15314 ? 104 LEU B O   1 
ATOM   2102 C CB  . LEU B 1 104 ? 25.99339  44.96287 12.19127 1.000 23.47160 ? 104 LEU B CB  1 
ATOM   2103 C CG  . LEU B 1 104 ? 25.37978  46.04934 13.06919 1.000 22.60160 ? 104 LEU B CG  1 
ATOM   2104 C CD1 . LEU B 1 104 ? 25.17508  47.29702 12.22599 1.000 26.19580 ? 104 LEU B CD1 1 
ATOM   2105 C CD2 . LEU B 1 104 ? 24.06018  45.56896 13.65437 1.000 25.95554 ? 104 LEU B CD2 1 
ATOM   2106 N N   . VAL B 1 105 ? 26.07768  41.46626 11.95218 1.000 24.75808 ? 105 VAL B N   1 
ATOM   2107 C CA  . VAL B 1 105 ? 26.42087  40.29079 11.16034 1.000 23.08860 ? 105 VAL B CA  1 
ATOM   2108 C C   . VAL B 1 105 ? 25.79657  40.41353 9.77797  1.000 26.31155 ? 105 VAL B C   1 
ATOM   2109 O O   . VAL B 1 105 ? 24.67603  40.91348 9.62473  1.000 25.28725 ? 105 VAL B O   1 
ATOM   2110 C CB  . VAL B 1 105 ? 25.93889  39.01828 11.88561 1.000 26.11674 ? 105 VAL B CB  1 
ATOM   2111 C CG1 . VAL B 1 105 ? 25.79182  37.84546 10.91966 1.000 29.40326 ? 105 VAL B CG1 1 
ATOM   2112 C CG2 . VAL B 1 105 ? 26.87575  38.68610 13.04571 1.000 29.19983 ? 105 VAL B CG2 1 
ATOM   2113 N N   . SER B 1 106 ? 26.52559  39.94976 8.76422  1.000 26.87130 ? 106 SER B N   1 
ATOM   2114 C CA  . SER B 1 106 ? 26.03062  39.86516 7.39801  1.000 26.97970 ? 106 SER B CA  1 
ATOM   2115 C C   . SER B 1 106 ? 25.67221  38.41443 7.08550  1.000 28.26653 ? 106 SER B C   1 
ATOM   2116 O O   . SER B 1 106 ? 26.48882  37.51635 7.30185  1.000 29.70489 ? 106 SER B O   1 
ATOM   2117 C CB  . SER B 1 106 ? 27.09479  40.37291 6.42148  1.000 30.54691 ? 106 SER B CB  1 
ATOM   2118 O OG  . SER B 1 106 ? 26.71456  40.12402 5.07866  1.000 37.44006 ? 106 SER B OG  1 
ATOM   2119 N N   . ASP B 1 107 ? 24.45929  38.19419 6.57919  1.000 27.68539 ? 107 ASP B N   1 
ATOM   2120 C CA  . ASP B 1 107 ? 23.94307  36.86391 6.24561  1.000 29.65343 ? 107 ASP B CA  1 
ATOM   2121 C C   . ASP B 1 107 ? 23.54124  36.82086 4.76747  1.000 31.38531 ? 107 ASP B C   1 
ATOM   2122 O O   . ASP B 1 107 ? 22.37719  36.57917 4.42719  1.000 30.62163 ? 107 ASP B O   1 
ATOM   2123 C CB  . ASP B 1 107 ? 22.76892  36.53545 7.16758  1.000 28.70124 ? 107 ASP B CB  1 
ATOM   2124 C CG  . ASP B 1 107 ? 22.13766  35.17803 6.89727  1.000 31.14255 ? 107 ASP B CG  1 
ATOM   2125 O OD1 . ASP B 1 107 ? 22.86236  34.21587 6.55299  1.000 32.94210 ? 107 ASP B OD1 1 
ATOM   2126 O OD2 . ASP B 1 107 ? 20.90086  35.08241 7.05607  1.000 30.61698 ? 107 ASP B OD2 1 
ATOM   2127 N N   . PRO B 1 108 ? 24.49561  37.04324 3.85721  1.000 32.85115 ? 108 PRO B N   1 
ATOM   2128 C CA  . PRO B 1 108 ? 24.12900  37.28379 2.44883  1.000 34.57054 ? 108 PRO B CA  1 
ATOM   2129 C C   . PRO B 1 108 ? 23.57474  36.06513 1.73016  1.000 38.60853 ? 108 PRO B C   1 
ATOM   2130 O O   . PRO B 1 108 ? 22.83508  36.23428 0.75140  1.000 41.08142 ? 108 PRO B O   1 
ATOM   2131 C CB  . PRO B 1 108 ? 25.45038  37.74368 1.82147  1.000 36.24381 ? 108 PRO B CB  1 
ATOM   2132 C CG  . PRO B 1 108 ? 26.48981  37.04285 2.62281  1.000 38.44479 ? 108 PRO B CG  1 
ATOM   2133 C CD  . PRO B 1 108 ? 25.95519  36.98443 4.04289  1.000 33.32454 ? 108 PRO B CD  1 
ATOM   2134 N N   . LYS B 1 109 ? 23.90495  34.85406 2.17158  1.000 37.77620 ? 109 LYS B N   1 
ATOM   2135 C CA  . LYS B 1 109 ? 23.33197  33.63819 1.60838  1.000 41.88822 ? 109 LYS B CA  1 
ATOM   2136 C C   . LYS B 1 109 ? 22.03168  33.23231 2.28749  1.000 42.08540 ? 109 LYS B C   1 
ATOM   2137 O O   . LYS B 1 109 ? 21.44438  32.20992 1.91173  1.000 39.30009 ? 109 LYS B O   1 
ATOM   2138 C CB  . LYS B 1 109 ? 24.34228  32.48538 1.69187  1.000 42.17325 ? 109 LYS B CB  1 
ATOM   2139 C CG  . LYS B 1 109 ? 25.73954  32.86052 1.22568  1.000 47.35675 ? 109 LYS B CG  1 
ATOM   2140 C CE  . LYS B 1 109 ? 27.74145  31.64357 0.34513  0.900 52.05341 ? 109 LYS B CE  1 
ATOM   2141 N NZ  . LYS B 1 109 ? 28.15541  30.33378 -0.22683 1.000 61.43434 ? 109 LYS B NZ  1 
ATOM   2142 N N   . ARG B 1 110 ? 21.58277  33.99831 3.28264  1.000 36.56416 ? 110 ARG B N   1 
ATOM   2143 C CA  . ARG B 1 110 ? 20.32196  33.80169 3.99379  1.000 34.54994 ? 110 ARG B CA  1 
ATOM   2144 C C   . ARG B 1 110 ? 20.27725  32.50628 4.79669  1.000 31.90963 ? 110 ARG B C   1 
ATOM   2145 O O   . ARG B 1 110 ? 19.20749  32.11984 5.26999  1.000 33.97434 ? 110 ARG B O   1 
ATOM   2146 C CB  . ARG B 1 110 ? 19.12442  33.86385 3.03505  1.000 35.38343 ? 110 ARG B CB  1 
ATOM   2147 C CG  . ARG B 1 110 ? 19.05736  35.16687 2.23474  1.000 39.90830 ? 110 ARG B CG  1 
ATOM   2148 C CD  . ARG B 1 110 ? 18.06558  35.06375 1.08297  1.000 43.66931 ? 110 ARG B CD  1 
ATOM   2149 N NE  . ARG B 1 110 ? 18.48455  34.05120 0.11445  1.000 50.25699 ? 110 ARG B NE  1 
ATOM   2150 C CZ  . ARG B 1 110 ? 19.04686  34.32428 -1.05883 1.000 51.54901 ? 110 ARG B CZ  1 
ATOM   2151 N NH1 . ARG B 1 110 ? 19.26035  35.58373 -1.41979 1.000 46.63933 ? 110 ARG B NH1 1 
ATOM   2152 N NH2 . ARG B 1 110 ? 19.40299  33.33317 -1.86595 1.000 52.79239 ? 110 ARG B NH2 1 
ATOM   2153 N N   . THR B 1 111 ? 21.41046  31.83518 4.99218  1.000 32.96609 ? 111 THR B N   1 
ATOM   2154 C CA  . THR B 1 111 ? 21.37317  30.55750 5.69867  1.000 35.67353 ? 111 THR B CA  1 
ATOM   2155 C C   . THR B 1 111 ? 21.16918  30.72208 7.20101  1.000 32.59238 ? 111 THR B C   1 
ATOM   2156 O O   . THR B 1 111 ? 20.57698  29.84084 7.83614  1.000 33.31952 ? 111 THR B O   1 
ATOM   2157 C CB  . THR B 1 111 ? 22.65172  29.76463 5.43032  1.000 40.36279 ? 111 THR B CB  1 
ATOM   2158 O OG1 . THR B 1 111 ? 23.78342  30.48239 5.94035  1.000 38.88273 ? 111 THR B OG1 1 
ATOM   2159 C CG2 . THR B 1 111 ? 22.82519  29.52711 3.92840  1.000 39.46396 ? 111 THR B CG2 1 
ATOM   2160 N N   . ILE B 1 112 ? 21.66190  31.81324 7.79215  1.000 30.61632 ? 112 ILE B N   1 
ATOM   2161 C CA  . ILE B 1 112 ? 21.40152  32.04596 9.21139  1.000 29.82298 ? 112 ILE B CA  1 
ATOM   2162 C C   . ILE B 1 112 ? 19.92772  32.36454 9.43029  1.000 27.73844 ? 112 ILE B C   1 
ATOM   2163 O O   . ILE B 1 112 ? 19.29798  31.83797 10.35263 1.000 27.19426 ? 112 ILE B O   1 
ATOM   2164 C CB  . ILE B 1 112 ? 22.31726  33.15504 9.76838  1.000 31.01239 ? 112 ILE B CB  1 
ATOM   2165 C CG1 . ILE B 1 112 ? 23.78813  32.84020 9.46831  1.000 30.89983 ? 112 ILE B CG1 1 
ATOM   2166 C CG2 . ILE B 1 112 ? 22.11872  33.29196 11.28015 1.000 28.61177 ? 112 ILE B CG2 1 
ATOM   2167 C CD1 . ILE B 1 112 ? 24.74410  33.97469 9.75068  1.000 29.65032 ? 112 ILE B CD1 1 
ATOM   2168 N N   . ALA B 1 113 ? 19.34658  33.22208 8.58162  1.000 27.29564 ? 113 ALA B N   1 
ATOM   2169 C CA  . ALA B 1 113 ? 17.92042  33.51459 8.70154  1.000 28.18336 ? 113 ALA B CA  1 
ATOM   2170 C C   . ALA B 1 113 ? 17.08171  32.25062 8.55757  1.000 30.59453 ? 113 ALA B C   1 
ATOM   2171 O O   . ALA B 1 113 ? 16.10619  32.05239 9.29304  1.000 30.57469 ? 113 ALA B O   1 
ATOM   2172 C CB  . ALA B 1 113 ? 17.50388  34.55693 7.66074  1.000 31.42162 ? 113 ALA B CB  1 
ATOM   2173 N N   . GLN B 1 114 ? 17.44915  31.37331 7.62280  1.000 33.17914 ? 114 GLN B N   1 
ATOM   2174 C CA  . GLN B 1 114 ? 16.71005  30.12080 7.49120  1.000 31.82369 ? 114 GLN B CA  1 
ATOM   2175 C C   . GLN B 1 114 ? 16.88499  29.23802 8.72174  1.000 30.67696 ? 114 GLN B C   1 
ATOM   2176 O O   . GLN B 1 114 ? 15.91409  28.65176 9.20865  1.000 31.60653 ? 114 GLN B O   1 
ATOM   2177 C CB  . GLN B 1 114 ? 17.15094  29.37761 6.23136  1.000 38.83898 ? 114 GLN B CB  1 
ATOM   2178 C CG  . GLN B 1 114 ? 16.89581  30.14756 4.95736  1.000 42.69286 ? 114 GLN B CG  1 
ATOM   2179 C CD  . GLN B 1 114 ? 17.27232  29.36159 3.71523  1.000 53.32505 ? 114 GLN B CD  1 
ATOM   2180 O OE1 . GLN B 1 114 ? 16.44289  28.65041 3.14209  1.000 55.88339 ? 114 GLN B OE1 1 
ATOM   2181 N NE2 . GLN B 1 114 ? 18.53307  29.47893 3.29635  1.000 51.57560 ? 114 GLN B NE2 1 
ATOM   2182 N N   . ASP B 1 115 ? 18.11369  29.13607 9.23503  1.000 27.46120 ? 115 ASP B N   1 
ATOM   2183 C CA  . ASP B 1 115 ? 18.37109  28.33601 10.42968 1.000 29.86239 ? 115 ASP B CA  1 
ATOM   2184 C C   . ASP B 1 115 ? 17.52482  28.80660 11.60273 1.000 30.93832 ? 115 ASP B C   1 
ATOM   2185 O O   . ASP B 1 115 ? 17.07642  27.99461 12.41669 1.000 29.28678 ? 115 ASP B O   1 
ATOM   2186 C CB  . ASP B 1 115 ? 19.85391  28.40115 10.79225 1.000 32.35921 ? 115 ASP B CB  1 
ATOM   2187 C CG  . ASP B 1 115 ? 20.58836  27.11407 10.50131 1.000 40.44730 ? 115 ASP B CG  1 
ATOM   2188 O OD1 . ASP B 1 115 ? 19.93363  26.05362 10.44937 1.000 46.64632 ? 115 ASP B OD1 1 
ATOM   2189 O OD2 . ASP B 1 115 ? 21.82337  27.16909 10.33852 1.000 39.20557 ? 115 ASP B OD2 1 
ATOM   2190 N N   . TYR B 1 116 ? 17.29816  30.11994 11.70781 1.000 27.03940 ? 116 TYR B N   1 
ATOM   2191 C CA  . TYR B 1 116 ? 16.49571  30.68085 12.78767 1.000 27.86337 ? 116 TYR B CA  1 
ATOM   2192 C C   . TYR B 1 116 ? 15.01949  30.80119 12.42745 1.000 31.27187 ? 116 TYR B C   1 
ATOM   2193 O O   . TYR B 1 116 ? 14.23021  31.28058 13.24756 1.000 31.63364 ? 116 TYR B O   1 
ATOM   2194 C CB  . TYR B 1 116 ? 17.08424  32.04160 13.22043 1.000 26.20418 ? 116 TYR B CB  1 
ATOM   2195 C CG  . TYR B 1 116 ? 18.23604  31.81452 14.16622 1.000 27.76269 ? 116 TYR B CG  1 
ATOM   2196 C CD1 . TYR B 1 116 ? 19.49642  31.45012 13.68892 1.000 26.41059 ? 116 TYR B CD1 1 
ATOM   2197 C CD2 . TYR B 1 116 ? 18.04295  31.86219 15.54495 1.000 27.93082 ? 116 TYR B CD2 1 
ATOM   2198 C CE1 . TYR B 1 116 ? 20.54509  31.17440 14.56682 1.000 27.88571 ? 116 TYR B CE1 1 
ATOM   2199 C CE2 . TYR B 1 116 ? 19.08258  31.60390 16.42749 1.000 26.94538 ? 116 TYR B CE2 1 
ATOM   2200 C CZ  . TYR B 1 116 ? 20.33038  31.25171 15.93564 1.000 28.20405 ? 116 TYR B CZ  1 
ATOM   2201 O OH  . TYR B 1 116 ? 21.35581  30.98670 16.82086 1.000 28.12038 ? 116 TYR B OH  1 
ATOM   2202 N N   . GLY B 1 117 ? 14.61851  30.33933 11.24215 1.000 28.51545 ? 117 GLY B N   1 
ATOM   2203 C CA  . GLY B 1 117 ? 13.21064  30.29138 10.91164 1.000 25.54424 ? 117 GLY B CA  1 
ATOM   2204 C C   . GLY B 1 117 ? 12.55016  31.62988 10.67924 1.000 31.01749 ? 117 GLY B C   1 
ATOM   2205 O O   . GLY B 1 117 ? 11.33022  31.73868 10.83368 1.000 31.90312 ? 117 GLY B O   1 
ATOM   2206 N N   . VAL B 1 118 ? 13.31519  32.65544 10.31036 1.000 28.17616 ? 118 VAL B N   1 
ATOM   2207 C CA  . VAL B 1 118 ? 12.76524  33.99651 10.16284 1.000 27.50087 ? 118 VAL B CA  1 
ATOM   2208 C C   . VAL B 1 118 ? 12.93962  34.53044 8.74158  1.000 30.19481 ? 118 VAL B C   1 
ATOM   2209 O O   . VAL B 1 118 ? 12.88404  35.73349 8.52627  1.000 29.33200 ? 118 VAL B O   1 
ATOM   2210 C CB  . VAL B 1 118 ? 13.37927  34.97041 11.19096 1.000 26.83015 ? 118 VAL B CB  1 
ATOM   2211 C CG1 . VAL B 1 118 ? 12.97975  34.58622 12.61045 1.000 28.19225 ? 118 VAL B CG1 1 
ATOM   2212 C CG2 . VAL B 1 118 ? 14.89128  35.04221 11.02188 1.000 29.36950 ? 118 VAL B CG2 1 
ATOM   2213 N N   . LEU B 1 119 ? 13.14680  33.66137 7.75499  1.000 33.89984 ? 119 LEU B N   1 
ATOM   2214 C CA  . LEU B 1 119 ? 13.24188  34.13831 6.37873  1.000 33.39569 ? 119 LEU B CA  1 
ATOM   2215 C C   . LEU B 1 119 ? 11.84930  34.37291 5.79716  1.000 34.37969 ? 119 LEU B C   1 
ATOM   2216 O O   . LEU B 1 119 ? 10.97890  33.50254 5.87388  1.000 37.31494 ? 119 LEU B O   1 
ATOM   2217 C CB  . LEU B 1 119 ? 14.01597  33.14628 5.50813  1.000 34.07056 ? 119 LEU B CB  1 
ATOM   2218 C CG  . LEU B 1 119 ? 14.37536  33.69965 4.12438  1.000 36.88244 ? 119 LEU B CG  1 
ATOM   2219 C CD1 . LEU B 1 119 ? 15.26130  34.92773 4.23705  1.000 37.58273 ? 119 LEU B CD1 1 
ATOM   2220 C CD2 . LEU B 1 119 ? 15.04387  32.64223 3.25733  1.000 41.28077 ? 119 LEU B CD2 1 
ATOM   2221 N N   . LYS B 1 120 ? 11.63536  35.56524 5.23552  1.000 32.69507 ? 120 LYS B N   1 
ATOM   2222 C CA  . LYS B 1 120 ? 10.42749  35.88041 4.47048  1.000 32.59788 ? 120 LYS B CA  1 
ATOM   2223 C C   . LYS B 1 120 ? 10.71659  35.42447 3.04823  1.000 36.62623 ? 120 LYS B C   1 
ATOM   2224 O O   . LYS B 1 120 ? 11.31992  36.14481 2.25224  1.000 36.13004 ? 120 LYS B O   1 
ATOM   2225 C CB  . LYS B 1 120 ? 10.09799  37.36861 4.54821  1.000 31.41363 ? 120 LYS B CB  1 
ATOM   2226 C CG  . LYS B 1 120 ? 8.75361   37.74217 3.94249  1.000 33.29304 ? 120 LYS B CG  1 
ATOM   2227 C CD  . LYS B 1 120 ? 8.41083   39.20597 4.18273  1.000 33.93355 ? 120 LYS B CD  1 
ATOM   2228 C CE  . LYS B 1 120 ? 7.01234   39.53587 3.68723  1.000 42.90648 ? 120 LYS B CE  1 
ATOM   2229 N NZ  . LYS B 1 120 ? 6.86034   39.20556 2.24067  1.000 43.60431 ? 120 LYS B NZ  1 
ATOM   2230 N N   . ALA B 1 121 ? 10.29990  34.19281 2.74035  1.000 38.39038 ? 121 ALA B N   1 
ATOM   2231 C CA  . ALA B 1 121 ? 10.83280  33.48434 1.57786  1.000 43.63520 ? 121 ALA B CA  1 
ATOM   2232 C C   . ALA B 1 121 ? 10.58809  34.24174 0.27595  1.000 42.48885 ? 121 ALA B C   1 
ATOM   2233 O O   . ALA B 1 121 ? 11.45255  34.25939 -0.60980 1.000 43.23701 ? 121 ALA B O   1 
ATOM   2234 C CB  . ALA B 1 121 ? 10.22894  32.08225 1.50532  1.000 42.32122 ? 121 ALA B CB  1 
ATOM   2235 N N   . ASP B 1 122 ? 9.42817   34.88560 0.14257  1.000 41.95857 ? 122 ASP B N   1 
ATOM   2236 C CA  . ASP B 1 122 ? 9.08728   35.50419 -1.13227 1.000 42.43522 ? 122 ASP B CA  1 
ATOM   2237 C C   . ASP B 1 122 ? 9.83964   36.80656 -1.38720 1.000 48.01701 ? 122 ASP B C   1 
ATOM   2238 O O   . ASP B 1 122 ? 9.71728   37.36447 -2.48539 1.000 47.44880 ? 122 ASP B O   1 
ATOM   2239 C CB  . ASP B 1 122 ? 7.57131   35.72997 -1.21944 1.000 45.52343 ? 122 ASP B CB  1 
ATOM   2240 C CG  . ASP B 1 122 ? 7.04167   36.68699 -0.15563 1.000 50.09004 ? 122 ASP B CG  1 
ATOM   2241 O OD1 . ASP B 1 122 ? 5.84293   37.03210 -0.23306 1.000 51.94261 ? 122 ASP B OD1 1 
ATOM   2242 O OD2 . ASP B 1 122 ? 7.80402   37.09958 0.74915  1.000 46.76038 ? 122 ASP B OD2 1 
ATOM   2243 N N   . GLU B 1 123 ? 10.62282  37.29505 -0.41996 1.000 39.31009 ? 123 GLU B N   1 
ATOM   2244 C CA  . GLU B 1 123 ? 11.38157  38.52267 -0.59639 1.000 40.04389 ? 123 GLU B CA  1 
ATOM   2245 C C   . GLU B 1 123 ? 12.87531  38.37292 -0.34517 1.000 37.00341 ? 123 GLU B C   1 
ATOM   2246 O O   . GLU B 1 123 ? 13.62384  39.31423 -0.62722 1.000 35.83720 ? 123 GLU B O   1 
ATOM   2247 C CB  . GLU B 1 123 ? 10.83702  39.62649 0.32278  1.000 37.21011 ? 123 GLU B CB  1 
ATOM   2248 C CG  . GLU B 1 123 ? 9.40591   40.03678 0.03891  1.000 42.28950 ? 123 GLU B CG  1 
ATOM   2249 C CD  . GLU B 1 123 ? 9.10011   41.42439 0.57310  1.000 45.95135 ? 123 GLU B CD  1 
ATOM   2250 O OE1 . GLU B 1 123 ? 9.58680   42.41282 -0.02114 1.000 50.41172 ? 123 GLU B OE1 1 
ATOM   2251 O OE2 . GLU B 1 123 ? 8.38578   41.53573 1.59224  1.000 45.37768 ? 123 GLU B OE2 1 
ATOM   2252 N N   . GLY B 1 124 ? 13.33100  37.23572 0.17238  1.000 34.27437 ? 124 GLY B N   1 
ATOM   2253 C CA  . GLY B 1 124 ? 14.74755  37.06744 0.45655  1.000 35.90892 ? 124 GLY B CA  1 
ATOM   2254 C C   . GLY B 1 124 ? 15.26341  37.95184 1.57262  1.000 33.59617 ? 124 GLY B C   1 
ATOM   2255 O O   . GLY B 1 124 ? 16.43902  38.33322 1.56190  1.000 33.29035 ? 124 GLY B O   1 
ATOM   2256 N N   . ILE B 1 125 ? 14.40462  38.30616 2.53129  1.000 31.49829 ? 125 ILE B N   1 
ATOM   2257 C CA  . ILE B 1 125 ? 14.77362  39.16040 3.65471  1.000 27.98256 ? 125 ILE B CA  1 
ATOM   2258 C C   . ILE B 1 125 ? 14.21177  38.53257 4.92264  1.000 28.97930 ? 125 ILE B C   1 
ATOM   2259 O O   . ILE B 1 125 ? 13.28293  37.72625 4.88225  1.000 30.08707 ? 125 ILE B O   1 
ATOM   2260 C CB  . ILE B 1 125 ? 14.24482  40.60472 3.49231  1.000 29.84634 ? 125 ILE B CB  1 
ATOM   2261 C CG1 . ILE B 1 125 ? 12.71797  40.63287 3.61115  1.000 30.43067 ? 125 ILE B CG1 1 
ATOM   2262 C CG2 . ILE B 1 125 ? 14.64602  41.17329 2.14245  1.000 35.42366 ? 125 ILE B CG2 1 
ATOM   2263 C CD1 . ILE B 1 125 ? 12.12386  42.02796 3.52078  1.000 31.85162 ? 125 ILE B CD1 1 
ATOM   2264 N N   . SER B 1 126 ? 14.77498  38.91709 6.06564  1.000 28.06526 ? 126 SER B N   1 
ATOM   2265 C CA  . SER B 1 126 ? 14.31167  38.35116 7.32363  1.000 25.62670 ? 126 SER B CA  1 
ATOM   2266 C C   . SER B 1 126 ? 13.17732  39.18790 7.89744  1.000 25.11442 ? 126 SER B C   1 
ATOM   2267 O O   . SER B 1 126 ? 13.09957  40.40274 7.68502  1.000 27.03363 ? 126 SER B O   1 
ATOM   2268 C CB  . SER B 1 126 ? 15.44901  38.26100 8.34580  1.000 24.03270 ? 126 SER B CB  1 
ATOM   2269 O OG  . SER B 1 126 ? 15.76251  39.55760 8.84816  1.000 27.93769 ? 126 SER B OG  1 
ATOM   2270 N N   . PHE B 1 127 ? 12.28468  38.51363 8.61633  1.000 26.04305 ? 127 PHE B N   1 
ATOM   2271 C CA  . PHE B 1 127 ? 11.37951  39.18349 9.53430  1.000 22.91159 ? 127 PHE B CA  1 
ATOM   2272 C C   . PHE B 1 127 ? 12.18210  39.77949 10.69233 1.000 23.95803 ? 127 PHE B C   1 
ATOM   2273 O O   . PHE B 1 127 ? 13.39948  39.60650 10.79355 1.000 25.35945 ? 127 PHE B O   1 
ATOM   2274 C CB  . PHE B 1 127 ? 10.33623  38.19784 10.05539 1.000 24.16383 ? 127 PHE B CB  1 
ATOM   2275 C CG  . PHE B 1 127 ? 9.27520   37.84433 9.05021  1.000 26.84168 ? 127 PHE B CG  1 
ATOM   2276 C CD1 . PHE B 1 127 ? 8.33355   38.78698 8.65322  1.000 27.34638 ? 127 PHE B CD1 1 
ATOM   2277 C CD2 . PHE B 1 127 ? 9.21621   36.56456 8.51006  1.000 29.99786 ? 127 PHE B CD2 1 
ATOM   2278 C CE1 . PHE B 1 127 ? 7.34645   38.46043 7.72801  1.000 30.53456 ? 127 PHE B CE1 1 
ATOM   2279 C CE2 . PHE B 1 127 ? 8.22786   36.22768 7.58337  1.000 31.74003 ? 127 PHE B CE2 1 
ATOM   2280 C CZ  . PHE B 1 127 ? 7.29831   37.17131 7.19305  1.000 27.46278 ? 127 PHE B CZ  1 
ATOM   2281 N N   . ARG B 1 128 ? 11.48633  40.47494 11.59418 1.000 22.08104 ? 128 ARG B N   1 
ATOM   2282 C CA  . ARG B 1 128 ? 12.12953  41.07447 12.76900 1.000 20.17191 ? 128 ARG B CA  1 
ATOM   2283 C C   . ARG B 1 128 ? 12.20816  40.03654 13.88349 1.000 22.86156 ? 128 ARG B C   1 
ATOM   2284 O O   . ARG B 1 128 ? 11.42484  40.04060 14.83781 1.000 24.93419 ? 128 ARG B O   1 
ATOM   2285 C CB  . ARG B 1 128 ? 11.37031  42.31486 13.22604 1.000 23.18661 ? 128 ARG B CB  1 
ATOM   2286 C CG  . ARG B 1 128 ? 11.50572  43.48318 12.29181 1.000 26.71939 ? 128 ARG B CG  1 
ATOM   2287 C CD  . ARG B 1 128 ? 10.90856  44.79018 12.84680 1.000 26.22331 ? 128 ARG B CD  1 
ATOM   2288 N NE  . ARG B 1 128 ? 10.61460  45.63657 11.69229 1.000 27.36183 ? 128 ARG B NE  1 
ATOM   2289 C CZ  . ARG B 1 128 ? 11.52249  46.33492 11.02156 1.000 25.92404 ? 128 ARG B CZ  1 
ATOM   2290 N NH1 . ARG B 1 128 ? 12.78752  46.38340 11.43497 1.000 27.82832 ? 128 ARG B NH1 1 
ATOM   2291 N NH2 . ARG B 1 128 ? 11.16409  46.98950 9.93418  1.000 27.64086 ? 128 ARG B NH2 1 
ATOM   2292 N N   . GLY B 1 129 ? 13.19444  39.14827 13.76276 1.000 22.99117 ? 129 GLY B N   1 
ATOM   2293 C CA  . GLY B 1 129 ? 13.38179  38.07123 14.72944 1.000 23.01052 ? 129 GLY B CA  1 
ATOM   2294 C C   . GLY B 1 129 ? 14.38186  38.45954 15.81080 1.000 23.35749 ? 129 GLY B C   1 
ATOM   2295 O O   . GLY B 1 129 ? 15.38429  39.11881 15.54299 1.000 25.43666 ? 129 GLY B O   1 
ATOM   2296 N N   . LEU B 1 130 ? 14.07696  38.06420 17.04222 1.000 22.96237 ? 130 LEU B N   1 
ATOM   2297 C CA  . LEU B 1 130 ? 14.97698  38.28729 18.16570 1.000 22.10802 ? 130 LEU B CA  1 
ATOM   2298 C C   . LEU B 1 130 ? 15.01016  37.02507 19.00849 1.000 22.16069 ? 130 LEU B C   1 
ATOM   2299 O O   . LEU B 1 130 ? 13.96474  36.42732 19.28093 1.000 22.46239 ? 130 LEU B O   1 
ATOM   2300 C CB  . LEU B 1 130 ? 14.53114  39.49044 19.01087 1.000 22.26986 ? 130 LEU B CB  1 
ATOM   2301 C CG  . LEU B 1 130 ? 15.39595  39.85124 20.22353 1.000 22.26933 ? 130 LEU B CG  1 
ATOM   2302 C CD1 . LEU B 1 130 ? 15.35177  41.36150 20.44995 1.000 22.90047 ? 130 LEU B CD1 1 
ATOM   2303 C CD2 . LEU B 1 130 ? 14.92365  39.10515 21.47921 1.000 25.16439 ? 130 LEU B CD2 1 
ATOM   2304 N N   . PHE B 1 131 ? 16.21339  36.63375 19.43621 1.000 23.24040 ? 131 PHE B N   1 
ATOM   2305 C CA  . PHE B 1 131 ? 16.42680  35.37065 20.12833 1.000 21.37570 ? 131 PHE B CA  1 
ATOM   2306 C C   . PHE B 1 131 ? 17.30234  35.60978 21.34257 1.000 22.12096 ? 131 PHE B C   1 
ATOM   2307 O O   . PHE B 1 131 ? 18.29243  36.34277 21.26371 1.000 22.92652 ? 131 PHE B O   1 
ATOM   2308 C CB  . PHE B 1 131 ? 17.07277  34.35412 19.19920 1.000 23.78624 ? 131 PHE B CB  1 
ATOM   2309 C CG  . PHE B 1 131 ? 16.25254  34.09009 17.98251 1.000 25.17607 ? 131 PHE B CG  1 
ATOM   2310 C CD1 . PHE B 1 131 ? 15.32138  33.05696 17.97388 1.000 23.37271 ? 131 PHE B CD1 1 
ATOM   2311 C CD2 . PHE B 1 131 ? 16.37291  34.90581 16.86348 1.000 23.69397 ? 131 PHE B CD2 1 
ATOM   2312 C CE1 . PHE B 1 131 ? 14.53638  32.82976 16.85058 1.000 24.78322 ? 131 PHE B CE1 1 
ATOM   2313 C CE2 . PHE B 1 131 ? 15.59085  34.69194 15.74338 1.000 26.29279 ? 131 PHE B CE2 1 
ATOM   2314 C CZ  . PHE B 1 131 ? 14.67428  33.65884 15.73217 1.000 25.24959 ? 131 PHE B CZ  1 
ATOM   2315 N N   . ILE B 1 132 ? 16.92572  35.00496 22.46337 1.000 21.53461 ? 132 ILE B N   1 
ATOM   2316 C CA  . ILE B 1 132 ? 17.69790  35.10773 23.69526 1.000 22.14833 ? 132 ILE B CA  1 
ATOM   2317 C C   . ILE B 1 132 ? 18.29761  33.74212 23.98111 1.000 22.69253 ? 132 ILE B C   1 
ATOM   2318 O O   . ILE B 1 132 ? 17.57189  32.74867 24.10522 1.000 24.00922 ? 132 ILE B O   1 
ATOM   2319 C CB  . ILE B 1 132 ? 16.84207  35.60040 24.86544 1.000 24.65103 ? 132 ILE B CB  1 
ATOM   2320 C CG1 . ILE B 1 132 ? 16.28784  36.98483 24.52522 1.000 22.85641 ? 132 ILE B CG1 1 
ATOM   2321 C CG2 . ILE B 1 132 ? 17.67942  35.64400 26.15205 1.000 25.47699 ? 132 ILE B CG2 1 
ATOM   2322 C CD1 . ILE B 1 132 ? 15.35113  37.53428 25.56747 1.000 22.97442 ? 132 ILE B CD1 1 
ATOM   2323 N N   . ILE B 1 133 ? 19.62462  33.70939 24.06647 1.000 23.54335 ? 133 ILE B N   1 
ATOM   2324 C CA  . ILE B 1 133 ? 20.42071  32.49630 24.18879 1.000 23.99874 ? 133 ILE B CA  1 
ATOM   2325 C C   . ILE B 1 133 ? 21.19917  32.58879 25.49191 1.000 22.33313 ? 133 ILE B C   1 
ATOM   2326 O O   . ILE B 1 133 ? 21.82699  33.61789 25.75819 1.000 24.82449 ? 133 ILE B O   1 
ATOM   2327 C CB  . ILE B 1 133 ? 21.37580  32.34981 22.98711 1.000 23.82147 ? 133 ILE B CB  1 
ATOM   2328 C CG1 . ILE B 1 133 ? 20.56406  32.29472 21.68714 1.000 23.99607 ? 133 ILE B CG1 1 
ATOM   2329 C CG2 . ILE B 1 133 ? 22.25531  31.10634 23.14422 1.000 24.56191 ? 133 ILE B CG2 1 
ATOM   2330 C CD1 . ILE B 1 133 ? 21.29446  32.81952 20.47264 1.000 29.56302 ? 133 ILE B CD1 1 
ATOM   2331 N N   . ASP B 1 134 ? 21.15733  31.52881 26.30607 1.000 26.19665 ? 134 ASP B N   1 
ATOM   2332 C CA  . ASP B 1 134 ? 21.81072  31.62274 27.60565 1.000 27.80137 ? 134 ASP B CA  1 
ATOM   2333 C C   . ASP B 1 134 ? 23.30879  31.33774 27.47995 1.000 30.10599 ? 134 ASP B C   1 
ATOM   2334 O O   . ASP B 1 134 ? 23.83396  31.05349 26.39670 1.000 26.52919 ? 134 ASP B O   1 
ATOM   2335 C CB  . ASP B 1 134 ? 21.11135  30.72921 28.64096 1.000 26.15094 ? 134 ASP B CB  1 
ATOM   2336 C CG  . ASP B 1 134 ? 21.33448  29.23609 28.44021 1.000 29.12754 ? 134 ASP B CG  1 
ATOM   2337 O OD1 . ASP B 1 134 ? 22.25335  28.80420 27.70733 1.000 27.33421 ? 134 ASP B OD1 1 
ATOM   2338 O OD2 . ASP B 1 134 ? 20.55549  28.46911 29.05978 1.000 28.75542 ? 134 ASP B OD2 1 
ATOM   2339 N N   . ASP B 1 135 ? 24.00712  31.45850 28.61353 1.000 29.03294 ? 135 ASP B N   1 
ATOM   2340 C CA  . ASP B 1 135 ? 25.45863  31.31364 28.66775 1.000 32.67012 ? 135 ASP B CA  1 
ATOM   2341 C C   . ASP B 1 135 ? 25.92835  29.90559 28.32989 1.000 32.22169 ? 135 ASP B C   1 
ATOM   2342 O O   . ASP B 1 135 ? 27.12741  29.70883 28.09267 1.000 33.11082 ? 135 ASP B O   1 
ATOM   2343 C CB  . ASP B 1 135 ? 25.95994  31.69955 30.05914 1.000 30.95663 ? 135 ASP B CB  1 
ATOM   2344 C CG  . ASP B 1 135 ? 25.29665  30.88339 31.15194 1.000 38.68229 ? 135 ASP B CG  1 
ATOM   2345 O OD1 . ASP B 1 135 ? 24.05212  30.92915 31.25275 1.000 34.79004 ? 135 ASP B OD1 1 
ATOM   2346 O OD2 . ASP B 1 135 ? 26.01144  30.17661 31.89527 1.000 39.41498 ? 135 ASP B OD2 1 
ATOM   2347 N N   . LYS B 1 136 ? 25.03219  28.92726 28.31776 1.000 30.87692 ? 136 LYS B N   1 
ATOM   2348 C CA  . LYS B 1 136 ? 25.36596  27.58386 27.87043 1.000 31.24108 ? 136 LYS B CA  1 
ATOM   2349 C C   . LYS B 1 136 ? 25.03254  27.36303 26.40128 1.000 31.51519 ? 136 LYS B C   1 
ATOM   2350 O O   . LYS B 1 136 ? 25.19564  26.24549 25.89976 1.000 33.13701 ? 136 LYS B O   1 
ATOM   2351 C CB  . LYS B 1 136 ? 24.64444  26.54953 28.74264 1.000 32.32197 ? 136 LYS B CB  1 
ATOM   2352 C CG  . LYS B 1 136 ? 25.09396  26.56522 30.20366 1.000 39.23193 ? 136 LYS B CG  1 
ATOM   2353 C CD  . LYS B 1 136 ? 24.10672  25.81161 31.09256 1.000 46.40009 ? 136 LYS B CD  1 
ATOM   2354 C CE  . LYS B 1 136 ? 24.08930  26.36634 32.51788 1.000 51.02995 ? 136 LYS B CE  1 
ATOM   2355 N NZ  . LYS B 1 136 ? 23.04850  27.43162 32.70554 1.000 53.02314 ? 136 LYS B NZ  1 
ATOM   2356 N N   . GLY B 1 137 ? 24.58631  28.40429 25.69583 1.000 29.75841 ? 137 GLY B N   1 
ATOM   2357 C CA  . GLY B 1 137 ? 24.23366  28.27779 24.29836 1.000 29.91247 ? 137 GLY B CA  1 
ATOM   2358 C C   . GLY B 1 137 ? 22.83499  27.77416 24.02749 1.000 27.92197 ? 137 GLY B C   1 
ATOM   2359 O O   . GLY B 1 137 ? 22.50376  27.52054 22.86469 1.000 27.35328 ? 137 GLY B O   1 
ATOM   2360 N N   . ILE B 1 138 ? 21.99356  27.63968 25.05526 1.000 26.91804 ? 138 ILE B N   1 
ATOM   2361 C CA  . ILE B 1 138 ? 20.64391  27.11002 24.89784 1.000 25.64610 ? 138 ILE B CA  1 
ATOM   2362 C C   . ILE B 1 138 ? 19.68760  28.24386 24.54320 1.000 23.42764 ? 138 ILE B C   1 
ATOM   2363 O O   . ILE B 1 138 ? 19.71840  29.31697 25.15526 1.000 23.95456 ? 138 ILE B O   1 
ATOM   2364 C CB  . ILE B 1 138 ? 20.19223  26.38368 26.17659 1.000 27.42166 ? 138 ILE B CB  1 
ATOM   2365 C CG1 . ILE B 1 138 ? 21.17101  25.25080 26.51539 1.000 30.38192 ? 138 ILE B CG1 1 
ATOM   2366 C CG2 . ILE B 1 138 ? 18.77482  25.82244 25.99596 1.000 28.61918 ? 138 ILE B CG2 1 
ATOM   2367 C CD1 . ILE B 1 138 ? 21.29411  24.23537 25.41389 1.000 29.66419 ? 138 ILE B CD1 1 
ATOM   2368 N N   . LEU B 1 139 ? 18.82002  28.00119 23.56472 1.000 24.73585 ? 139 LEU B N   1 
ATOM   2369 C CA  . LEU B 1 139 ? 17.81917  28.99836 23.20564 1.000 23.01665 ? 139 LEU B CA  1 
ATOM   2370 C C   . LEU B 1 139 ? 16.73132  29.05639 24.26995 1.000 21.34881 ? 139 LEU B C   1 
ATOM   2371 O O   . LEU B 1 139 ? 16.14893  28.03097 24.63214 1.000 22.82891 ? 139 LEU B O   1 
ATOM   2372 C CB  . LEU B 1 139 ? 17.21957  28.66999 21.84052 1.000 24.87527 ? 139 LEU B CB  1 
ATOM   2373 C CG  . LEU B 1 139 ? 16.16116  29.61179 21.27504 1.000 23.78839 ? 139 LEU B CG  1 
ATOM   2374 C CD1 . LEU B 1 139 ? 16.77703  30.98101 20.97552 1.000 25.99265 ? 139 LEU B CD1 1 
ATOM   2375 C CD2 . LEU B 1 139 ? 15.54607  29.01548 20.01261 1.000 27.52320 ? 139 LEU B CD2 1 
ATOM   2376 N N   . ARG B 1 140 ? 16.44997  30.26897 24.77051 1.000 21.95971 ? 140 ARG B N   1 
ATOM   2377 C CA  . ARG B 1 140 ? 15.46773  30.46418 25.82669 1.000 21.91971 ? 140 ARG B CA  1 
ATOM   2378 C C   . ARG B 1 140 ? 14.23472  31.23966 25.38773 1.000 21.85642 ? 140 ARG B C   1 
ATOM   2379 O O   . ARG B 1 140 ? 13.19944  31.13581 26.05500 1.000 23.52065 ? 140 ARG B O   1 
ATOM   2380 C CB  . ARG B 1 140 ? 16.09639  31.20603 27.02023 1.000 24.73994 ? 140 ARG B CB  1 
ATOM   2381 C CG  . ARG B 1 140 ? 17.42472  30.61811 27.51384 1.000 25.24919 ? 140 ARG B CG  1 
ATOM   2382 C CD  . ARG B 1 140 ? 17.29320  29.17486 27.98213 1.000 27.57491 ? 140 ARG B CD  1 
ATOM   2383 N NE  . ARG B 1 140 ? 16.30852  28.96602 29.04694 1.000 27.54819 ? 140 ARG B NE  1 
ATOM   2384 C CZ  . ARG B 1 140 ? 16.51509  29.22168 30.33747 1.000 28.44104 ? 140 ARG B CZ  1 
ATOM   2385 N NH1 . ARG B 1 140 ? 17.67773  29.72206 30.74893 1.000 30.51748 ? 140 ARG B NH1 1 
ATOM   2386 N NH2 . ARG B 1 140 ? 15.56132  28.97306 31.22611 1.000 26.50496 ? 140 ARG B NH2 1 
ATOM   2387 N N   . GLN B 1 141 ? 14.31340  32.00385 24.29905 1.000 21.02588 ? 141 GLN B N   1 
ATOM   2388 C CA  . GLN B 1 141 ? 13.22028  32.89641 23.93007 1.000 22.98393 ? 141 GLN B CA  1 
ATOM   2389 C C   . GLN B 1 141 ? 13.23835  33.16399 22.43035 1.000 24.12296 ? 141 GLN B C   1 
ATOM   2390 O O   . GLN B 1 141 ? 14.29923  33.40246 21.84875 1.000 23.05245 ? 141 GLN B O   1 
ATOM   2391 C CB  . GLN B 1 141 ? 13.32784  34.22456 24.69371 1.000 22.43043 ? 141 GLN B CB  1 
ATOM   2392 C CG  . GLN B 1 141 ? 11.99241  34.93244 24.94279 1.000 22.32654 ? 141 GLN B CG  1 
ATOM   2393 C CD  . GLN B 1 141 ? 11.48928  35.72319 23.74977 1.000 22.06171 ? 141 GLN B CD  1 
ATOM   2394 O OE1 . GLN B 1 141 ? 12.26317  36.15570 22.89096 1.000 23.51183 ? 141 GLN B OE1 1 
ATOM   2395 N NE2 . GLN B 1 141 ? 10.17165  35.92809 23.70126 1.000 22.42799 ? 141 GLN B NE2 1 
ATOM   2396 N N   . ILE B 1 142 ? 12.05484  33.14995 21.82023 1.000 22.28236 ? 142 ILE B N   1 
ATOM   2397 C CA  . ILE B 1 142 ? 11.86975  33.45983 20.40561 1.000 21.57291 ? 142 ILE B CA  1 
ATOM   2398 C C   . ILE B 1 142 ? 10.87824  34.60638 20.29553 1.000 21.14020 ? 142 ILE B C   1 
ATOM   2399 O O   . ILE B 1 142 ? 9.79599   34.55148 20.89072 1.000 22.64557 ? 142 ILE B O   1 
ATOM   2400 C CB  . ILE B 1 142 ? 11.34661  32.24672 19.61861 1.000 23.66236 ? 142 ILE B CB  1 
ATOM   2401 C CG1 . ILE B 1 142 ? 12.39356  31.13240 19.57276 1.000 22.14503 ? 142 ILE B CG1 1 
ATOM   2402 C CG2 . ILE B 1 142 ? 10.91608  32.67107 18.21357 1.000 25.12777 ? 142 ILE B CG2 1 
ATOM   2403 C CD1 . ILE B 1 142 ? 11.80051  29.77818 19.20896 1.000 24.50071 ? 142 ILE B CD1 1 
ATOM   2404 N N   . THR B 1 143 ? 11.24410  35.63129 19.52708 1.000 21.10023 ? 143 THR B N   1 
ATOM   2405 C CA  . THR B 1 143 ? 10.37749  36.76923 19.22748 1.000 21.99530 ? 143 THR B CA  1 
ATOM   2406 C C   . THR B 1 143 ? 10.44734  37.01772 17.73072 1.000 24.33061 ? 143 THR B C   1 
ATOM   2407 O O   . THR B 1 143 ? 11.53966  37.19892 17.19162 1.000 24.84601 ? 143 THR B O   1 
ATOM   2408 C CB  . THR B 1 143 ? 10.83660  38.02523 19.98518 1.000 20.66125 ? 143 THR B CB  1 
ATOM   2409 O OG1 . THR B 1 143 ? 10.78274  37.79229 21.39500 1.000 23.94251 ? 143 THR B OG1 1 
ATOM   2410 C CG2 . THR B 1 143 ? 9.96023   39.22728 19.63306 1.000 25.74881 ? 143 THR B CG2 1 
ATOM   2411 N N   . VAL B 1 144 ? 9.30276   37.03121 17.05085 1.000 24.03137 ? 144 VAL B N   1 
ATOM   2412 C CA  . VAL B 1 144 ? 9.28851   37.34368 15.62156 1.000 22.45602 ? 144 VAL B CA  1 
ATOM   2413 C C   . VAL B 1 144 ? 8.15523   38.31972 15.35555 1.000 22.26013 ? 144 VAL B C   1 
ATOM   2414 O O   . VAL B 1 144 ? 6.98488   37.99864 15.59697 1.000 22.74606 ? 144 VAL B O   1 
ATOM   2415 C CB  . VAL B 1 144 ? 9.13013   36.09459 14.73253 1.000 23.54407 ? 144 VAL B CB  1 
ATOM   2416 C CG1 . VAL B 1 144 ? 9.36530   36.48866 13.27667 1.000 25.28035 ? 144 VAL B CG1 1 
ATOM   2417 C CG2 . VAL B 1 144 ? 10.10649  34.99700 15.15005 1.000 24.60088 ? 144 VAL B CG2 1 
ATOM   2418 N N   . ASN B 1 145 ? 8.50133   39.51008 14.86883 1.000 23.69670 ? 145 ASN B N   1 
ATOM   2419 C CA  . ASN B 1 145 ? 7.52594   40.51121 14.46463 1.000 22.33197 ? 145 ASN B CA  1 
ATOM   2420 C C   . ASN B 1 145 ? 7.43152   40.57551 12.94825 1.000 23.26925 ? 145 ASN B C   1 
ATOM   2421 O O   . ASN B 1 145 ? 8.44844   40.53386 12.24933 1.000 22.93948 ? 145 ASN B O   1 
ATOM   2422 C CB  . ASN B 1 145 ? 7.90431   41.91890 14.94332 1.000 21.96573 ? 145 ASN B CB  1 
ATOM   2423 C CG  . ASN B 1 145 ? 7.87912   42.08297 16.44515 1.000 23.43760 ? 145 ASN B CG  1 
ATOM   2424 O OD1 . ASN B 1 145 ? 7.70012   41.12982 17.20306 1.000 24.79925 ? 145 ASN B OD1 1 
ATOM   2425 N ND2 . ASN B 1 145 ? 8.07642   43.32543 16.88504 1.000 23.08813 ? 145 ASN B ND2 1 
ATOM   2426 N N   . ASP B 1 146 ? 6.21221   40.74762 12.45028 1.000 23.80257 ? 146 ASP B N   1 
ATOM   2427 C CA  . ASP B 1 146 ? 6.03409   41.17872 11.07406 1.000 22.58535 ? 146 ASP B CA  1 
ATOM   2428 C C   . ASP B 1 146 ? 6.77018   42.50118 10.84731 1.000 27.00795 ? 146 ASP B C   1 
ATOM   2429 O O   . ASP B 1 146 ? 7.01015   43.27719 11.77929 1.000 25.22020 ? 146 ASP B O   1 
ATOM   2430 C CB  . ASP B 1 146 ? 4.54207   41.31510 10.76634 1.000 27.50156 ? 146 ASP B CB  1 
ATOM   2431 C CG  . ASP B 1 146 ? 4.22783   41.33331 9.26928  1.000 28.94677 ? 146 ASP B CG  1 
ATOM   2432 O OD1 . ASP B 1 146 ? 5.12258   41.11185 8.42428  1.000 28.24042 ? 146 ASP B OD1 1 
ATOM   2433 O OD2 . ASP B 1 146 ? 3.04747   41.56938 8.95339  1.000 31.15356 ? 146 ASP B OD2 1 
ATOM   2434 N N   . LEU B 1 147 ? 7.11170   42.75552 9.58122  1.000 25.30824 ? 147 LEU B N   1 
ATOM   2435 C CA  . LEU B 1 147 ? 7.95778   43.89406 9.21588  1.000 26.64227 ? 147 LEU B CA  1 
ATOM   2436 C C   . LEU B 1 147 ? 7.54420   45.25024 9.78125  1.000 26.56565 ? 147 LEU B C   1 
ATOM   2437 O O   . LEU B 1 147 ? 8.44785   46.03816 10.11146 1.000 27.49853 ? 147 LEU B O   1 
ATOM   2438 C CB  . LEU B 1 147 ? 8.04130   43.99521 7.68509  1.000 26.61781 ? 147 LEU B CB  1 
ATOM   2439 C CG  . LEU B 1 147 ? 8.43137   42.69032 6.99061  1.000 30.70258 ? 147 LEU B CG  1 
ATOM   2440 C CD1 . LEU B 1 147 ? 8.47195   42.88364 5.47939  1.000 33.72376 ? 147 LEU B CD1 1 
ATOM   2441 C CD2 . LEU B 1 147 ? 9.77281   42.19165 7.51250  1.000 31.84282 ? 147 LEU B CD2 1 
ATOM   2442 N N   . PRO B 1 148 ? 6.25708   45.61188 9.88598  1.000 26.54354 ? 148 PRO B N   1 
ATOM   2443 C CA  . PRO B 1 148 ? 5.92616   47.00550 10.23973 1.000 28.11112 ? 148 PRO B CA  1 
ATOM   2444 C C   . PRO B 1 148 ? 6.25999   47.41772 11.66353 1.000 26.26270 ? 148 PRO B C   1 
ATOM   2445 O O   . PRO B 1 148 ? 6.31376   48.62628 11.92202 1.000 26.71606 ? 148 PRO B O   1 
ATOM   2446 C CB  . PRO B 1 148 ? 4.40806   47.08144 10.00777 1.000 31.14251 ? 148 PRO B CB  1 
ATOM   2447 C CG  . PRO B 1 148 ? 4.09685   45.97187 9.10394  1.000 32.59079 ? 148 PRO B CG  1 
ATOM   2448 C CD  . PRO B 1 148 ? 5.05351   44.88244 9.43430  1.000 26.13147 ? 148 PRO B CD  1 
ATOM   2449 N N   . VAL B 1 149 ? 6.47131   46.49671 12.59933 1.000 23.49046 ? 149 VAL B N   1 
ATOM   2450 C CA  . VAL B 1 149 ? 6.46053   46.83956 14.01988 1.000 23.20734 ? 149 VAL B CA  1 
ATOM   2451 C C   . VAL B 1 149 ? 7.77674   46.43200 14.66868 1.000 26.44795 ? 149 VAL B C   1 
ATOM   2452 O O   . VAL B 1 149 ? 8.20168   45.27583 14.55856 1.000 25.71424 ? 149 VAL B O   1 
ATOM   2453 C CB  . VAL B 1 149 ? 5.26280   46.19498 14.74101 1.000 24.74043 ? 149 VAL B CB  1 
ATOM   2454 C CG1 . VAL B 1 149 ? 5.38986   46.38522 16.25223 1.000 26.51056 ? 149 VAL B CG1 1 
ATOM   2455 C CG2 . VAL B 1 149 ? 3.95875   46.83448 14.23268 1.000 24.51985 ? 149 VAL B CG2 1 
ATOM   2456 N N   . GLY B 1 150 ? 8.40831   47.38533 15.36584 1.000 25.69037 ? 150 GLY B N   1 
ATOM   2457 C CA  . GLY B 1 150 ? 9.71790   47.16868 15.94440 1.000 27.22215 ? 150 GLY B CA  1 
ATOM   2458 C C   . GLY B 1 150 ? 9.67962   46.58376 17.35079 1.000 26.85883 ? 150 GLY B C   1 
ATOM   2459 O O   . GLY B 1 150 ? 8.63002   46.31842 17.93246 1.000 26.26096 ? 150 GLY B O   1 
ATOM   2460 N N   . ARG B 1 151 ? 10.87055  46.37911 17.89437 1.000 24.77440 ? 151 ARG B N   1 
ATOM   2461 C CA  . ARG B 1 151 ? 11.06004  45.71828 19.17777 1.000 24.79408 ? 151 ARG B CA  1 
ATOM   2462 C C   . ARG B 1 151 ? 11.39150  46.72803 20.27034 1.000 25.77362 ? 151 ARG B C   1 
ATOM   2463 O O   . ARG B 1 151 ? 11.70696  47.89265 20.00021 1.000 26.94924 ? 151 ARG B O   1 
ATOM   2464 C CB  . ARG B 1 151 ? 12.15568  44.65860 19.04801 1.000 25.22839 ? 151 ARG B CB  1 
ATOM   2465 C CG  . ARG B 1 151 ? 11.63857  43.49614 18.20259 1.000 24.64066 ? 151 ARG B CG  1 
ATOM   2466 C CD  . ARG B 1 151 ? 12.71182  42.80961 17.46048 1.000 27.05803 ? 151 ARG B CD  1 
ATOM   2467 N NE  . ARG B 1 151 ? 13.25027  43.58936 16.35270 1.000 25.25236 ? 151 ARG B NE  1 
ATOM   2468 C CZ  . ARG B 1 151 ? 14.07310  43.05333 15.45923 1.000 23.65463 ? 151 ARG B CZ  1 
ATOM   2469 N NH1 . ARG B 1 151 ? 14.38545  41.76843 15.57356 1.000 24.04966 ? 151 ARG B NH1 1 
ATOM   2470 N NH2 . ARG B 1 151 ? 14.57440  43.77597 14.47169 1.000 23.70968 ? 151 ARG B NH2 1 
ATOM   2471 N N   . SER B 1 152 ? 11.33009  46.25874 21.51961 1.000 24.84489 ? 152 SER B N   1 
ATOM   2472 C CA  . SER B 1 152 ? 11.54550  47.09564 22.69589 1.000 24.83701 ? 152 SER B CA  1 
ATOM   2473 C C   . SER B 1 152 ? 12.81240  46.64132 23.41409 1.000 23.04247 ? 152 SER B C   1 
ATOM   2474 O O   . SER B 1 152 ? 12.94293  45.46341 23.77291 1.000 23.47028 ? 152 SER B O   1 
ATOM   2475 C CB  . SER B 1 152 ? 10.33928  47.02192 23.63835 1.000 26.68666 ? 152 SER B CB  1 
ATOM   2476 O OG  . SER B 1 152 ? 10.69042  47.41382 24.96481 1.000 24.27945 ? 152 SER B OG  1 
ATOM   2477 N N   . VAL B 1 153 ? 13.74487  47.57280 23.62635 1.000 24.59615 ? 153 VAL B N   1 
ATOM   2478 C CA  . VAL B 1 153 ? 14.91858  47.23740 24.42753 1.000 21.46678 ? 153 VAL B CA  1 
ATOM   2479 C C   . VAL B 1 153 ? 14.50888  46.95258 25.86925 1.000 21.49849 ? 153 VAL B C   1 
ATOM   2480 O O   . VAL B 1 153 ? 15.02469  46.02097 26.49259 1.000 23.86701 ? 153 VAL B O   1 
ATOM   2481 C CB  . VAL B 1 153 ? 15.98401  48.35049 24.34434 1.000 22.74053 ? 153 VAL B CB  1 
ATOM   2482 C CG1 . VAL B 1 153 ? 17.14481  48.03334 25.28556 1.000 24.75843 ? 153 VAL B CG1 1 
ATOM   2483 C CG2 . VAL B 1 153 ? 16.50108  48.49026 22.91987 1.000 24.25161 ? 153 VAL B CG2 1 
ATOM   2484 N N   . ASP B 1 154 ? 13.57834  47.74765 26.42260 1.000 24.62231 ? 154 ASP B N   1 
ATOM   2485 C CA  . ASP B 1 154 ? 13.07980  47.49216 27.77727 1.000 24.39519 ? 154 ASP B CA  1 
ATOM   2486 C C   . ASP B 1 154 ? 12.59894  46.05545 27.92839 1.000 23.15013 ? 154 ASP B C   1 
ATOM   2487 O O   . ASP B 1 154 ? 12.92768  45.37264 28.90563 1.000 23.02117 ? 154 ASP B O   1 
ATOM   2488 C CB  . ASP B 1 154 ? 11.91686  48.43252 28.11986 1.000 24.53695 ? 154 ASP B CB  1 
ATOM   2489 C CG  . ASP B 1 154 ? 12.36374  49.81748 28.53982 1.000 31.94725 ? 154 ASP B CG  1 
ATOM   2490 O OD1 . ASP B 1 154 ? 13.56976  50.04418 28.76252 1.000 29.60688 ? 154 ASP B OD1 1 
ATOM   2491 O OD2 . ASP B 1 154 ? 11.46488  50.67770 28.68149 1.000 32.36636 ? 154 ASP B OD2 1 
ATOM   2492 N N   . GLU B 1 155 ? 11.77758  45.59456 26.98402 1.000 22.37694 ? 155 GLU B N   1 
ATOM   2493 C CA  . GLU B 1 155 ? 11.23203  44.24728 27.09573 1.000 22.96293 ? 155 GLU B CA  1 
ATOM   2494 C C   . GLU B 1 155 ? 12.33976  43.21145 27.00165 1.000 23.06432 ? 155 GLU B C   1 
ATOM   2495 O O   . GLU B 1 155 ? 12.31910  42.20151 27.71464 1.000 22.70806 ? 155 GLU B O   1 
ATOM   2496 C CB  . GLU B 1 155 ? 10.17827  44.00686 26.01202 1.000 24.21987 ? 155 GLU B CB  1 
ATOM   2497 C CG  . GLU B 1 155 ? 9.72361   42.53109 25.88158 1.000 21.80126 ? 155 GLU B CG  1 
ATOM   2498 C CD  . GLU B 1 155 ? 8.82703   42.06102 27.02059 1.000 21.67835 ? 155 GLU B CD  1 
ATOM   2499 O OE1 . GLU B 1 155 ? 8.65504   42.79284 28.02698 1.000 23.41470 ? 155 GLU B OE1 1 
ATOM   2500 O OE2 . GLU B 1 155 ? 8.29903   40.93535 26.92259 1.000 24.44264 ? 155 GLU B OE2 1 
ATOM   2501 N N   . THR B 1 156 ? 13.31020  43.44900 26.11899 1.000 21.59704 ? 156 THR B N   1 
ATOM   2502 C CA  . THR B 1 156 ? 14.41972  42.51196 25.97116 1.000 21.42395 ? 156 THR B CA  1 
ATOM   2503 C C   . THR B 1 156 ? 15.23492  42.42288 27.25545 1.000 22.76621 ? 156 THR B C   1 
ATOM   2504 O O   . THR B 1 156 ? 15.59478  41.32753 27.69482 1.000 21.72649 ? 156 THR B O   1 
ATOM   2505 C CB  . THR B 1 156 ? 15.30067  42.92417 24.78941 1.000 22.40527 ? 156 THR B CB  1 
ATOM   2506 O OG1 . THR B 1 156 ? 14.47881  43.11703 23.62768 1.000 21.88000 ? 156 THR B OG1 1 
ATOM   2507 C CG2 . THR B 1 156 ? 16.34291  41.83243 24.49294 1.000 22.74272 ? 156 THR B CG2 1 
ATOM   2508 N N   . LEU B 1 157 ? 15.51646  43.56692 27.88171 1.000 21.86787 ? 157 LEU B N   1 
ATOM   2509 C CA  . LEU B 1 157 ? 16.23143  43.55665 29.15530 1.000 22.62143 ? 157 LEU B CA  1 
ATOM   2510 C C   . LEU B 1 157 ? 15.42422  42.84085 30.23188 1.000 22.69101 ? 157 LEU B C   1 
ATOM   2511 O O   . LEU B 1 157 ? 15.98028  42.07395 31.02598 1.000 23.18924 ? 157 LEU B O   1 
ATOM   2512 C CB  . LEU B 1 157 ? 16.55965  44.99317 29.58796 1.000 22.63996 ? 157 LEU B CB  1 
ATOM   2513 C CG  . LEU B 1 157 ? 17.65132  45.70632 28.77856 1.000 25.56327 ? 157 LEU B CG  1 
ATOM   2514 C CD1 . LEU B 1 157 ? 17.57131  47.21084 28.97004 1.000 26.28169 ? 157 LEU B CD1 1 
ATOM   2515 C CD2 . LEU B 1 157 ? 19.03617  45.18624 29.17528 1.000 27.35920 ? 157 LEU B CD2 1 
ATOM   2516 N N   . ARG B 1 158 ? 14.10633  43.06791 30.27111 1.000 23.42352 ? 158 ARG B N   1 
ATOM   2517 C CA  . ARG B 1 158 ? 13.27421  42.35340 31.23639 1.000 22.51750 ? 158 ARG B CA  1 
ATOM   2518 C C   . ARG B 1 158 ? 13.43216  40.84714 31.08788 1.000 23.48488 ? 158 ARG B C   1 
ATOM   2519 O O   . ARG B 1 158 ? 13.58152  40.12295 32.08411 1.000 24.16717 ? 158 ARG B O   1 
ATOM   2520 C CB  . ARG B 1 158 ? 11.80100  42.73803 31.07409 1.000 24.28709 ? 158 ARG B CB  1 
ATOM   2521 C CG  . ARG B 1 158 ? 10.88321  41.95803 32.02303 1.000 26.80936 ? 158 ARG B CG  1 
ATOM   2522 C CD  . ARG B 1 158 ? 9.40026   42.13615 31.70101 1.000 27.04543 ? 158 ARG B CD  1 
ATOM   2523 N NE  . ARG B 1 158 ? 8.97913   41.38462 30.51578 1.000 23.18318 ? 158 ARG B NE  1 
ATOM   2524 C CZ  . ARG B 1 158 ? 8.68327   40.08672 30.52050 1.000 23.56166 ? 158 ARG B CZ  1 
ATOM   2525 N NH1 . ARG B 1 158 ? 8.75542   39.37638 31.65123 1.000 22.59767 ? 158 ARG B NH1 1 
ATOM   2526 N NH2 . ARG B 1 158 ? 8.29847   39.49559 29.39631 1.000 24.22069 ? 158 ARG B NH2 1 
ATOM   2527 N N   . LEU B 1 159 ? 13.41067  40.35807 29.84595 1.000 21.57084 ? 159 LEU B N   1 
ATOM   2528 C CA  . LEU B 1 159 ? 13.51122  38.92232 29.61281 1.000 22.23180 ? 159 LEU B CA  1 
ATOM   2529 C C   . LEU B 1 159 ? 14.87827  38.39021 30.02444 1.000 21.81565 ? 159 LEU B C   1 
ATOM   2530 O O   . LEU B 1 159 ? 14.96993  37.37455 30.71851 1.000 22.22961 ? 159 LEU B O   1 
ATOM   2531 C CB  . LEU B 1 159 ? 13.22886  38.62033 28.14195 1.000 22.19335 ? 159 LEU B CB  1 
ATOM   2532 C CG  . LEU B 1 159 ? 11.75880  38.75215 27.72850 1.000 22.91849 ? 159 LEU B CG  1 
ATOM   2533 C CD1 . LEU B 1 159 ? 11.61446  38.82513 26.21723 1.000 25.04343 ? 159 LEU B CD1 1 
ATOM   2534 C CD2 . LEU B 1 159 ? 10.92762  37.59331 28.29559 1.000 21.04780 ? 159 LEU B CD2 1 
ATOM   2535 N N   . VAL B 1 160 ? 15.95491  39.05753 29.59544 1.000 22.50076 ? 160 VAL B N   1 
ATOM   2536 C CA  . VAL B 1 160 ? 17.29459  38.59382 29.96116 1.000 24.55418 ? 160 VAL B CA  1 
ATOM   2537 C C   . VAL B 1 160 ? 17.42172  38.50881 31.47634 1.000 23.82208 ? 160 VAL B C   1 
ATOM   2538 O O   . VAL B 1 160 ? 17.84586  37.48729 32.02394 1.000 23.50118 ? 160 VAL B O   1 
ATOM   2539 C CB  . VAL B 1 160 ? 18.37613  39.50619 29.35620 1.000 25.24993 ? 160 VAL B CB  1 
ATOM   2540 C CG1 . VAL B 1 160 ? 19.75674  39.12503 29.89832 1.000 26.33559 ? 160 VAL B CG1 1 
ATOM   2541 C CG2 . VAL B 1 160 ? 18.35112  39.42684 27.83366 1.000 24.46291 ? 160 VAL B CG2 1 
ATOM   2542 N N   . GLN B 1 161 ? 17.00686  39.56961 32.17784 1.000 24.22831 ? 161 GLN B N   1 
ATOM   2543 C CA  . GLN B 1 161 ? 17.08733  39.57777 33.63632 1.000 25.96904 ? 161 GLN B CA  1 
ATOM   2544 C C   . GLN B 1 161 ? 16.28153  38.44013 34.24450 1.000 27.74895 ? 161 GLN B C   1 
ATOM   2545 O O   . GLN B 1 161 ? 16.73070  37.78864 35.19628 1.000 26.33331 ? 161 GLN B O   1 
ATOM   2546 C CB  . GLN B 1 161 ? 16.59327  40.92324 34.18330 1.000 27.22585 ? 161 GLN B CB  1 
ATOM   2547 C CG  . GLN B 1 161 ? 17.53273  42.08347 33.94575 1.000 37.14836 ? 161 GLN B CG  1 
ATOM   2548 C CD  . GLN B 1 161 ? 16.83901  43.43762 34.06203 1.000 41.20417 ? 161 GLN B CD  1 
ATOM   2549 O OE1 . GLN B 1 161 ? 17.14705  44.37161 33.31993 1.000 40.95588 ? 161 GLN B OE1 1 
ATOM   2550 N NE2 . GLN B 1 161 ? 15.88876  43.54225 34.98970 1.000 44.63882 ? 161 GLN B NE2 1 
ATOM   2551 N N   . ALA B 1 162 ? 15.08810  38.17948 33.70023 1.000 24.34470 ? 162 ALA B N   1 
ATOM   2552 C CA  . ALA B 1 162 ? 14.22466  37.14685 34.26431 1.000 25.16940 ? 162 ALA B CA  1 
ATOM   2553 C C   . ALA B 1 162 ? 14.80405  35.75324 34.04362 1.000 25.47567 ? 162 ALA B C   1 
ATOM   2554 O O   . ALA B 1 162 ? 14.73614  34.89857 34.93617 1.000 25.78624 ? 162 ALA B O   1 
ATOM   2555 C CB  . ALA B 1 162 ? 12.81515  37.25705 33.67015 1.000 24.30671 ? 162 ALA B CB  1 
ATOM   2556 N N   . PHE B 1 163 ? 15.39961  35.50421 32.87349 1.000 22.50479 ? 163 PHE B N   1 
ATOM   2557 C CA  . PHE B 1 163 ? 16.02528  34.20274 32.65840 1.000 24.69505 ? 163 PHE B CA  1 
ATOM   2558 C C   . PHE B 1 163 ? 17.22245  34.02068 33.57964 1.000 25.24077 ? 163 PHE B C   1 
ATOM   2559 O O   . PHE B 1 163 ? 17.42859  32.93520 34.13356 1.000 26.73942 ? 163 PHE B O   1 
ATOM   2560 C CB  . PHE B 1 163 ? 16.43183  34.03839 31.19382 1.000 25.50852 ? 163 PHE B CB  1 
ATOM   2561 C CG  . PHE B 1 163 ? 15.28286  33.70889 30.29291 1.000 22.25739 ? 163 PHE B CG  1 
ATOM   2562 C CD1 . PHE B 1 163 ? 14.61681  32.50314 30.42050 1.000 25.42855 ? 163 PHE B CD1 1 
ATOM   2563 C CD2 . PHE B 1 163 ? 14.86323  34.60656 29.32588 1.000 26.86189 ? 163 PHE B CD2 1 
ATOM   2564 C CE1 . PHE B 1 163 ? 13.54245  32.19938 29.60340 1.000 24.55465 ? 163 PHE B CE1 1 
ATOM   2565 C CE2 . PHE B 1 163 ? 13.79074  34.30126 28.49675 1.000 24.06490 ? 163 PHE B CE2 1 
ATOM   2566 C CZ  . PHE B 1 163 ? 13.13407  33.09879 28.64313 1.000 26.41579 ? 163 PHE B CZ  1 
ATOM   2567 N N   . GLN B 1 164 ? 18.00316  35.07877 33.78427 1.000 26.20624 ? 164 GLN B N   1 
ATOM   2568 C CA  . GLN B 1 164 ? 19.14196  34.95965 34.68724 1.000 28.90094 ? 164 GLN B CA  1 
ATOM   2569 C C   . GLN B 1 164 ? 18.67565  34.72702 36.12002 1.000 28.78890 ? 164 GLN B C   1 
ATOM   2570 O O   . GLN B 1 164 ? 19.27713  33.93342 36.85637 1.000 27.68476 ? 164 GLN B O   1 
ATOM   2571 C CB  . GLN B 1 164 ? 20.01715  36.20178 34.57327 1.000 28.44813 ? 164 GLN B CB  1 
ATOM   2572 C CG  . GLN B 1 164 ? 20.70081  36.27917 33.21435 1.000 29.47694 ? 164 GLN B CG  1 
ATOM   2573 C CD  . GLN B 1 164 ? 21.52765  37.52775 33.02362 1.000 34.02608 ? 164 GLN B CD  1 
ATOM   2574 O OE1 . GLN B 1 164 ? 21.32266  38.54419 33.70136 1.000 32.23972 ? 164 GLN B OE1 1 
ATOM   2575 N NE2 . GLN B 1 164 ? 22.46475  37.46930 32.08169 1.000 30.31772 ? 164 GLN B NE2 1 
ATOM   2576 N N   . PHE B 1 165 ? 17.57776  35.37605 36.51311 1.000 28.01837 ? 165 PHE B N   1 
ATOM   2577 C CA  . PHE B 1 165 ? 17.03559  35.17313 37.85201 1.000 28.40871 ? 165 PHE B CA  1 
ATOM   2578 C C   . PHE B 1 165 ? 16.61480  33.72486 38.06373 1.000 30.33630 ? 165 PHE B C   1 
ATOM   2579 O O   . PHE B 1 165 ? 16.99581  33.09418 39.05636 1.000 30.06932 ? 165 PHE B O   1 
ATOM   2580 C CB  . PHE B 1 165 ? 15.85864  36.11647 38.08651 1.000 27.28337 ? 165 PHE B CB  1 
ATOM   2581 C CG  . PHE B 1 165 ? 15.25040  35.97416 39.44613 1.000 32.08974 ? 165 PHE B CG  1 
ATOM   2582 C CD1 . PHE B 1 165 ? 15.85906  36.54865 40.54711 1.000 31.46017 ? 165 PHE B CD1 1 
ATOM   2583 C CD2 . PHE B 1 165 ? 14.07984  35.25359 39.62724 1.000 32.25018 ? 165 PHE B CD2 1 
ATOM   2584 C CE1 . PHE B 1 165 ? 15.30270  36.42447 41.79444 1.000 33.85241 ? 165 PHE B CE1 1 
ATOM   2585 C CE2 . PHE B 1 165 ? 13.51849  35.12101 40.88937 1.000 35.40778 ? 165 PHE B CE2 1 
ATOM   2586 C CZ  . PHE B 1 165 ? 14.13609  35.69868 41.97320 1.000 32.06654 ? 165 PHE B CZ  1 
ATOM   2587 N N   . THR B 1 166 ? 15.83330  33.16836 37.13359 1.000 27.76850 ? 166 THR B N   1 
ATOM   2588 C CA  . THR B 1 166 ? 15.37898  31.79485 37.31153 1.000 26.37482 ? 166 THR B CA  1 
ATOM   2589 C C   . THR B 1 166 ? 16.51652  30.79114 37.14852 1.000 27.98378 ? 166 THR B C   1 
ATOM   2590 O O   . THR B 1 166 ? 16.42929  29.68548 37.69300 1.000 30.21637 ? 166 THR B O   1 
ATOM   2591 C CB  . THR B 1 166 ? 14.23073  31.47783 36.34324 1.000 30.73098 ? 166 THR B CB  1 
ATOM   2592 O OG1 . THR B 1 166 ? 14.63413  31.74846 34.99688 1.000 28.10745 ? 166 THR B OG1 1 
ATOM   2593 C CG2 . THR B 1 166 ? 13.01000  32.33118 36.67868 1.000 28.72544 ? 166 THR B CG2 1 
ATOM   2594 N N   . ASP B 1 167 ? 17.59253  31.16347 36.44645 1.000 27.37914 ? 167 ASP B N   1 
ATOM   2595 C CA  . ASP B 1 167 ? 18.75896  30.28418 36.35518 1.000 27.23838 ? 167 ASP B CA  1 
ATOM   2596 C C   . ASP B 1 167 ? 19.36150  29.99511 37.73020 1.000 31.09393 ? 167 ASP B C   1 
ATOM   2597 O O   . ASP B 1 167 ? 20.00992  28.96070 37.91383 1.000 33.20705 ? 167 ASP B O   1 
ATOM   2598 C CB  . ASP B 1 167 ? 19.82977  30.90758 35.45828 1.000 27.72705 ? 167 ASP B CB  1 
ATOM   2599 C CG  . ASP B 1 167 ? 19.53800  30.74501 33.97341 1.000 27.38543 ? 167 ASP B CG  1 
ATOM   2600 O OD1 . ASP B 1 167 ? 18.60242  30.00803 33.60358 1.000 27.59824 ? 167 ASP B OD1 1 
ATOM   2601 O OD2 . ASP B 1 167 ? 20.27420  31.35682 33.17548 1.000 30.13844 ? 167 ASP B OD2 1 
ATOM   2602 N N   . LYS B 1 168 ? 19.17281  30.89878 38.69796 1.000 32.92618 ? 168 LYS B N   1 
ATOM   2603 C CA  . LYS B 1 168 ? 19.74335  30.72225 40.03065 1.000 34.68870 ? 168 LYS B CA  1 
ATOM   2604 C C   . LYS B 1 168 ? 18.94657  29.75445 40.89759 1.000 38.48797 ? 168 LYS B C   1 
ATOM   2605 O O   . LYS B 1 168 ? 19.46012  29.29512 41.92415 1.000 44.73407 ? 168 LYS B O   1 
ATOM   2606 C CB  . LYS B 1 168 ? 19.84475  32.07194 40.74005 1.000 33.51146 ? 168 LYS B CB  1 
ATOM   2607 C CG  . LYS B 1 168 ? 20.59664  33.13579 39.98922 1.000 32.77091 ? 168 LYS B CG  1 
ATOM   2608 C CD  . LYS B 1 168 ? 20.67711  34.41540 40.80743 1.000 39.04309 ? 168 LYS B CD  1 
ATOM   2609 C CE  . LYS B 1 168 ? 20.72947  35.65192 39.91838 1.000 40.47986 ? 168 LYS B CE  1 
ATOM   2610 N NZ  . LYS B 1 168 ? 22.01424  35.78181 39.16389 1.000 40.91746 ? 168 LYS B NZ  1 
ATOM   2611 N N   . HIS B 1 169 ? 17.71281  29.43219 40.52045 1.000 38.65830 ? 169 HIS B N   1 
ATOM   2612 C CA  . HIS B 1 169 ? 16.92893  28.49425 41.30832 1.000 40.17345 ? 169 HIS B CA  1 
ATOM   2613 C C   . HIS B 1 169 ? 17.49189  27.07968 41.16656 1.000 45.64613 ? 169 HIS B C   1 
ATOM   2614 O O   . HIS B 1 169 ? 18.23347  26.76298 40.23106 1.000 48.36817 ? 169 HIS B O   1 
ATOM   2615 C CB  . HIS B 1 169 ? 15.45771  28.54882 40.88722 1.000 42.09100 ? 169 HIS B CB  1 
ATOM   2616 C CG  . HIS B 1 169 ? 14.70966  29.71671 41.46109 0.669 37.60306 ? 169 HIS B CG  1 
ATOM   2617 N ND1 . HIS B 1 169 ? 13.50151  30.14932 40.95746 0.381 39.29681 ? 169 HIS B ND1 1 
ATOM   2618 C CD2 . HIS B 1 169 ? 14.99647  30.53624 42.50104 0.417 38.07243 ? 169 HIS B CD2 1 
ATOM   2619 C CE1 . HIS B 1 169 ? 13.07956  31.18752 41.65718 0.320 39.31923 ? 169 HIS B CE1 1 
ATOM   2620 N NE2 . HIS B 1 169 ? 13.96513  31.43916 42.60497 0.823 39.66388 ? 169 HIS B NE2 1 
ATOM   2621 N N   . GLY B 1 170 ? 17.14954  26.23085 42.12899 1.000 47.73029 ? 170 GLY B N   1 
ATOM   2622 C CA  . GLY B 1 170 ? 17.61949  24.85702 42.13880 1.000 48.88351 ? 170 GLY B CA  1 
ATOM   2623 C C   . GLY B 1 170 ? 16.62385  23.88958 42.74907 1.000 51.64788 ? 170 GLY B C   1 
ATOM   2624 O O   . GLY B 1 170 ? 15.77197  23.33867 42.04796 0.654 53.75454 ? 170 GLY B O   1 
HETATM 2625 C CAU . ROA C 2 .   ? 7.57677   24.18082 34.42590 0.773 29.29461 ? 201 ROA A CAU 1 
HETATM 2626 C CAV . ROA C 2 .   ? 8.20866   22.93885 34.51406 0.613 29.86683 ? 201 ROA A CAV 1 
HETATM 2627 O OAY . ROA C 2 .   ? 9.58112   22.82837 34.78411 1.000 36.88955 ? 201 ROA A OAY 1 
HETATM 2628 C CAW . ROA C 2 .   ? 7.48293   21.77704 34.32665 1.000 36.05143 ? 201 ROA A CAW 1 
HETATM 2629 O OAZ . ROA C 2 .   ? 8.11488   20.52883 34.40206 1.000 34.93166 ? 201 ROA A OAZ 1 
HETATM 2630 C CAX . ROA C 2 .   ? 6.13313   21.82687 34.05368 1.000 33.09848 ? 201 ROA A CAX 1 
HETATM 2631 C CAT . ROA C 2 .   ? 5.49806   23.05066 33.96345 1.000 28.42244 ? 201 ROA A CAT 1 
HETATM 2632 C CAS . ROA C 2 .   ? 6.20913   24.21559 34.15544 1.000 29.86998 ? 201 ROA A CAS 1 
HETATM 2633 C CAO . ROA C 2 .   ? 5.42435   25.52054 34.01324 1.000 32.76287 ? 201 ROA A CAO 1 
HETATM 2634 C CAN . ROA C 2 .   ? 4.95593   26.03141 35.35718 1.000 29.55876 ? 201 ROA A CAN 1 
HETATM 2635 C CAP . ROA C 2 .   ? 3.86703   27.06958 35.10604 1.000 32.92519 ? 201 ROA A CAP 1 
HETATM 2636 O OAR . ROA C 2 .   ? 2.88666   26.77868 34.35265 1.000 29.63906 ? 201 ROA A OAR 1 
HETATM 2637 O OAQ . ROA C 2 .   ? 3.94044   28.19333 35.68118 1.000 29.45422 ? 201 ROA A OAQ 1 
HETATM 2638 O OAM . ROA C 2 .   ? 6.08654   26.64628 35.85766 1.000 37.38274 ? 201 ROA A OAM 1 
HETATM 2639 C CAK . ROA C 2 .   ? 6.06249   27.00831 37.20016 1.000 37.67121 ? 201 ROA A CAK 1 
HETATM 2640 O OAL . ROA C 2 .   ? 5.09644   26.83971 37.86937 1.000 40.37204 ? 201 ROA A OAL 1 
HETATM 2641 C CAJ . ROA C 2 .   ? 7.34346   27.60884 37.75350 1.000 36.77210 ? 201 ROA A CAJ 1 
HETATM 2642 C CAI . ROA C 2 .   ? 8.38932   27.63290 36.95451 1.000 38.07976 ? 201 ROA A CAI 1 
HETATM 2643 C CAC . ROA C 2 .   ? 9.70969   28.20670 37.44824 1.000 38.49875 ? 201 ROA A CAC 1 
HETATM 2644 C CAD . ROA C 2 .   ? 10.89800  27.62123 37.03435 1.000 37.55404 ? 201 ROA A CAD 1 
HETATM 2645 C CAE . ROA C 2 .   ? 12.09793  28.14190 37.49067 1.000 36.53633 ? 201 ROA A CAE 1 
HETATM 2646 O OAG . ROA C 2 .   ? 13.30349  27.55748 37.07480 1.000 43.25958 ? 201 ROA A OAG 1 
HETATM 2647 C CAF . ROA C 2 .   ? 12.10185  29.22893 38.35182 0.403 36.06240 ? 201 ROA A CAF 1 
HETATM 2648 O OAH . ROA C 2 .   ? 13.30583  29.75339 38.82311 0.635 35.78737 ? 201 ROA A OAH 1 
HETATM 2649 C CAB . ROA C 2 .   ? 10.91618  29.80882 38.76330 0.828 38.85537 ? 201 ROA A CAB 1 
HETATM 2650 C CAA . ROA C 2 .   ? 9.71764   29.29129 38.30721 0.124 36.71510 ? 201 ROA A CAA 1 
HETATM 2651 O O   . HOH D 3 .   ? -0.59147  17.14420 15.84496 1.000 43.75083 ? 301 HOH A O   1 
HETATM 2652 O O   . HOH D 3 .   ? 4.62198   33.95907 40.01073 1.000 38.23756 ? 302 HOH A O   1 
HETATM 2653 O O   . HOH D 3 .   ? 13.53916  19.02481 27.77174 1.000 49.53797 ? 303 HOH A O   1 
HETATM 2654 O O   . HOH D 3 .   ? -5.99661  23.94567 12.61113 1.000 42.05615 ? 304 HOH A O   1 
HETATM 2655 O O   . HOH D 3 .   ? -7.44141  17.93061 17.39939 1.000 48.06994 ? 305 HOH A O   1 
HETATM 2656 O O   . HOH D 3 .   ? -2.670    39.070   49.592   1.000 40.02076 ? 306 HOH A O   1 
HETATM 2657 O O   . HOH D 3 .   ? -4.01709  33.75772 43.73282 1.000 32.70406 ? 307 HOH A O   1 
HETATM 2658 O O   . HOH D 3 .   ? -9.56450  39.54118 36.37005 1.000 31.10590 ? 308 HOH A O   1 
HETATM 2659 O O   . HOH D 3 .   ? -5.55113  40.91549 40.89510 1.000 33.76605 ? 309 HOH A O   1 
HETATM 2660 O O   . HOH D 3 .   ? -5.41537  17.08281 29.54692 1.000 31.85443 ? 310 HOH A O   1 
HETATM 2661 O O   . HOH D 3 .   ? -3.54013  41.16934 7.21428  1.000 40.61864 ? 311 HOH A O   1 
HETATM 2662 O O   . HOH D 3 .   ? -16.31183 30.24943 13.64678 1.000 36.06964 ? 312 HOH A O   1 
HETATM 2663 O O   . HOH D 3 .   ? 4.45924   21.15626 16.14545 1.000 38.88404 ? 313 HOH A O   1 
HETATM 2664 O O   . HOH D 3 .   ? -11.90542 43.10265 9.46259  1.000 47.84883 ? 314 HOH A O   1 
HETATM 2665 O O   . HOH D 3 .   ? -6.77043  19.32068 21.90819 1.000 26.49434 ? 315 HOH A O   1 
HETATM 2666 O O   . HOH D 3 .   ? -15.58544 35.11330 23.83070 1.000 35.29442 ? 316 HOH A O   1 
HETATM 2667 O O   . HOH D 3 .   ? -14.41422 18.78062 24.96246 1.000 35.08587 ? 317 HOH A O   1 
HETATM 2668 O O   . HOH D 3 .   ? -5.34752  50.88312 17.70928 1.000 40.24091 ? 318 HOH A O   1 
HETATM 2669 O O   . HOH D 3 .   ? 15.74929  25.26873 28.64000 1.000 36.38486 ? 319 HOH A O   1 
HETATM 2670 O O   . HOH D 3 .   ? -3.09023  50.47130 28.09494 1.000 36.36671 ? 320 HOH A O   1 
HETATM 2671 O O   . HOH D 3 .   ? -8.21975  24.08133 44.62752 1.000 39.59257 ? 321 HOH A O   1 
HETATM 2672 O O   . HOH D 3 .   ? -5.17598  23.88363 15.99017 1.000 34.86082 ? 322 HOH A O   1 
HETATM 2673 O O   . HOH D 3 .   ? -5.09714  53.40578 21.37926 1.000 41.20594 ? 323 HOH A O   1 
HETATM 2674 O O   . HOH D 3 .   ? -7.18227  47.56003 32.90694 1.000 36.65254 ? 324 HOH A O   1 
HETATM 2675 O O   . HOH D 3 .   ? -18.68334 22.17616 25.39738 1.000 41.27436 ? 325 HOH A O   1 
HETATM 2676 O O   . HOH D 3 .   ? -14.64890 39.19676 21.35241 1.000 37.59240 ? 326 HOH A O   1 
HETATM 2677 O O   . HOH D 3 .   ? 7.21079   46.87879 26.63070 1.000 31.47335 ? 327 HOH A O   1 
HETATM 2678 O O   . HOH D 3 .   ? -9.54949  36.76665 39.40148 1.000 26.77463 ? 328 HOH A O   1 
HETATM 2679 O O   . HOH D 3 .   ? -1.35664  15.29521 19.26127 1.000 31.48184 ? 329 HOH A O   1 
HETATM 2680 O O   . HOH D 3 .   ? -6.42721  46.69997 11.73131 1.000 40.57019 ? 330 HOH A O   1 
HETATM 2681 O O   . HOH D 3 .   ? -10.91406 19.30253 27.42966 1.000 35.65081 ? 331 HOH A O   1 
HETATM 2682 O O   . HOH D 3 .   ? -2.10889  20.86190 36.12700 1.000 33.36191 ? 332 HOH A O   1 
HETATM 2683 O O   . HOH D 3 .   ? 7.92445   41.33822 21.99055 1.000 23.03431 ? 333 HOH A O   1 
HETATM 2684 O O   . HOH D 3 .   ? -20.18558 26.81760 20.25463 1.000 47.73741 ? 334 HOH A O   1 
HETATM 2685 O O   . HOH D 3 .   ? -3.58383  13.51915 24.76584 1.000 31.85554 ? 335 HOH A O   1 
HETATM 2686 O O   . HOH D 3 .   ? -14.41705 39.11117 36.40749 1.000 36.79961 ? 336 HOH A O   1 
HETATM 2687 O O   . HOH D 3 .   ? -0.01560  23.37599 27.96911 1.000 23.61417 ? 337 HOH A O   1 
HETATM 2688 O O   . HOH D 3 .   ? -10.82173 34.47208 45.08561 1.000 42.55508 ? 338 HOH A O   1 
HETATM 2689 O O   . HOH D 3 .   ? 12.46866  23.76887 29.21155 1.000 37.92702 ? 339 HOH A O   1 
HETATM 2690 O O   . HOH D 3 .   ? -3.54996  49.56921 33.49271 1.000 37.06754 ? 340 HOH A O   1 
HETATM 2691 O O   . HOH D 3 .   ? -15.92857 36.78364 35.47547 1.000 36.15633 ? 341 HOH A O   1 
HETATM 2692 O O   . HOH D 3 .   ? -9.22627  44.84851 16.23521 1.000 40.07887 ? 342 HOH A O   1 
HETATM 2693 O O   . HOH D 3 .   ? -6.72465  32.50913 10.96074 1.000 36.63172 ? 343 HOH A O   1 
HETATM 2694 O O   . HOH D 3 .   ? 0.50839   46.50992 9.82125  1.000 32.15012 ? 344 HOH A O   1 
HETATM 2695 O O   . HOH D 3 .   ? -11.88660 24.37876 42.93776 1.000 38.64487 ? 345 HOH A O   1 
HETATM 2696 O O   . HOH D 3 .   ? -8.02141  39.00164 39.82010 1.000 31.32485 ? 346 HOH A O   1 
HETATM 2697 O O   . HOH D 3 .   ? -21.50990 28.14010 27.42589 1.000 39.37453 ? 347 HOH A O   1 
HETATM 2698 O O   . HOH D 3 .   ? -6.05645  39.47783 44.57986 1.000 39.85391 ? 348 HOH A O   1 
HETATM 2699 O O   . HOH D 3 .   ? -13.06575 38.05408 27.13238 1.000 35.19560 ? 349 HOH A O   1 
HETATM 2700 O O   . HOH D 3 .   ? -5.08900  44.15412 38.97623 1.000 37.65532 ? 350 HOH A O   1 
HETATM 2701 O O   . HOH D 3 .   ? -13.42042 43.77152 29.34051 1.000 47.09047 ? 351 HOH A O   1 
HETATM 2702 O O   . HOH D 3 .   ? 6.18509   39.62132 23.13375 1.000 24.10081 ? 352 HOH A O   1 
HETATM 2703 O O   . HOH D 3 .   ? -4.82752  20.17360 37.12903 1.000 39.77640 ? 353 HOH A O   1 
HETATM 2704 O O   . HOH D 3 .   ? -2.80514  41.48582 37.86558 1.000 27.01910 ? 354 HOH A O   1 
HETATM 2705 O O   . HOH D 3 .   ? 9.71964   34.02197 36.37744 1.000 34.46152 ? 355 HOH A O   1 
HETATM 2706 O O   . HOH D 3 .   ? -16.94999 27.83144 16.54534 1.000 39.44417 ? 356 HOH A O   1 
HETATM 2707 O O   . HOH D 3 .   ? -12.06068 31.54341 31.96396 1.000 26.91978 ? 357 HOH A O   1 
HETATM 2708 O O   . HOH D 3 .   ? 1.87459   37.60386 41.00121 1.000 37.74403 ? 358 HOH A O   1 
HETATM 2709 O O   . HOH D 3 .   ? 9.79453   19.76334 21.82506 1.000 38.33167 ? 359 HOH A O   1 
HETATM 2710 O O   . HOH D 3 .   ? 10.53809  20.72839 32.38707 1.000 38.11889 ? 360 HOH A O   1 
HETATM 2711 O O   . HOH D 3 .   ? 6.32591   47.92802 31.19323 1.000 42.00608 ? 361 HOH A O   1 
HETATM 2712 O O   . HOH D 3 .   ? 2.02900   49.28586 26.58348 1.000 29.79733 ? 362 HOH A O   1 
HETATM 2713 O O   . HOH D 3 .   ? 6.87303   32.86030 10.41367 1.000 33.70069 ? 363 HOH A O   1 
HETATM 2714 O O   . HOH D 3 .   ? -11.93940 39.16169 37.61757 1.000 31.43720 ? 364 HOH A O   1 
HETATM 2715 O O   . HOH D 3 .   ? -1.53836  27.92946 41.59321 1.000 36.54647 ? 365 HOH A O   1 
HETATM 2716 O O   . HOH D 3 .   ? 5.75185   39.59693 26.92654 1.000 24.07679 ? 366 HOH A O   1 
HETATM 2717 O O   . HOH D 3 .   ? -19.47787 20.78713 19.97578 1.000 47.71097 ? 367 HOH A O   1 
HETATM 2718 O O   . HOH D 3 .   ? -5.95284  50.10014 25.59595 1.000 29.27711 ? 368 HOH A O   1 
HETATM 2719 O O   . HOH D 3 .   ? -11.00455 20.99415 24.01990 1.000 29.65689 ? 369 HOH A O   1 
HETATM 2720 O O   . HOH D 3 .   ? -20.93042 30.71960 28.54260 1.000 43.81862 ? 370 HOH A O   1 
HETATM 2721 O O   . HOH D 3 .   ? 5.99724   33.25106 6.78009  1.000 40.25158 ? 371 HOH A O   1 
HETATM 2722 O O   . HOH D 3 .   ? -16.83527 37.25615 13.48321 1.000 48.46774 ? 372 HOH A O   1 
HETATM 2723 O O   . HOH D 3 .   ? -19.70568 25.21792 34.75155 1.000 37.90980 ? 373 HOH A O   1 
HETATM 2724 O O   . HOH D 3 .   ? -13.95924 25.79332 13.81443 1.000 43.98355 ? 374 HOH A O   1 
HETATM 2725 O O   . HOH D 3 .   ? -11.73493 42.28555 24.67362 1.000 42.18579 ? 375 HOH A O   1 
HETATM 2726 O O   . HOH D 3 .   ? 1.83559   15.84923 29.59148 1.000 27.19000 ? 376 HOH A O   1 
HETATM 2727 O O   . HOH D 3 .   ? -16.09322 39.62773 32.37862 1.000 41.47726 ? 377 HOH A O   1 
HETATM 2728 O O   . HOH D 3 .   ? -10.24919 44.91426 32.72050 1.000 37.34451 ? 378 HOH A O   1 
HETATM 2729 O O   . HOH D 3 .   ? 5.66420   28.99552 16.57295 1.000 38.83983 ? 379 HOH A O   1 
HETATM 2730 O O   . HOH D 3 .   ? -13.91973 31.34443 34.07342 1.000 26.05191 ? 380 HOH A O   1 
HETATM 2731 O O   . HOH D 3 .   ? 2.15105   50.82354 20.46381 1.000 27.33582 ? 381 HOH A O   1 
HETATM 2732 O O   . HOH D 3 .   ? -14.14478 21.63817 37.76586 1.000 35.78178 ? 382 HOH A O   1 
HETATM 2733 O O   . HOH D 3 .   ? 4.14812   39.74682 24.91533 1.000 30.47186 ? 383 HOH A O   1 
HETATM 2734 O O   . HOH D 3 .   ? -6.66732  34.67411 7.32300  1.000 36.08561 ? 384 HOH A O   1 
HETATM 2735 O O   . HOH D 3 .   ? 8.40278   35.71550 35.01407 1.000 33.21304 ? 385 HOH A O   1 
HETATM 2736 O O   . HOH D 3 .   ? 0.06113   31.42116 10.55486 1.000 29.43663 ? 386 HOH A O   1 
HETATM 2737 O O   . HOH D 3 .   ? 15.53230  27.34190 35.31883 1.000 44.34966 ? 387 HOH A O   1 
HETATM 2738 O O   . HOH D 3 .   ? -9.33380  37.57006 13.81581 1.000 27.67814 ? 388 HOH A O   1 
HETATM 2739 O O   . HOH D 3 .   ? -14.74642 33.19202 35.76662 1.000 28.01090 ? 389 HOH A O   1 
HETATM 2740 O O   . HOH D 3 .   ? -0.96696  39.38357 37.96609 1.000 27.43018 ? 390 HOH A O   1 
HETATM 2741 O O   . HOH D 3 .   ? -17.20433 29.96866 38.45943 1.000 37.04478 ? 391 HOH A O   1 
HETATM 2742 O O   . HOH D 3 .   ? -6.28260  17.90889 33.03189 1.000 32.85611 ? 392 HOH A O   1 
HETATM 2743 O O   . HOH D 3 .   ? 2.90875   44.67895 31.97181 1.000 29.71848 ? 393 HOH A O   1 
HETATM 2744 O O   . HOH D 3 .   ? -9.75766  34.92313 13.91926 1.000 32.46672 ? 394 HOH A O   1 
HETATM 2745 O O   . HOH D 3 .   ? 5.010     16.705   18.807   1.000 44.97554 ? 395 HOH A O   1 
HETATM 2746 O O   . HOH D 3 .   ? 4.91325   27.13053 13.86099 1.000 41.03504 ? 396 HOH A O   1 
HETATM 2747 O O   . HOH D 3 .   ? 14.52269  25.92954 31.67502 1.000 36.80002 ? 397 HOH A O   1 
HETATM 2748 O O   . HOH D 3 .   ? 1.40597   49.48579 33.04223 1.000 43.31434 ? 398 HOH A O   1 
HETATM 2749 O O   . HOH D 3 .   ? -16.69439 32.44655 20.79823 1.000 32.72608 ? 399 HOH A O   1 
HETATM 2750 O O   . HOH D 3 .   ? 6.490     13.284   22.083   1.000 35.32079 ? 400 HOH A O   1 
HETATM 2751 O O   . HOH D 3 .   ? -7.31023  29.81744 9.80742  1.000 43.34535 ? 401 HOH A O   1 
HETATM 2752 O O   . HOH D 3 .   ? 8.40354   23.41316 20.61038 1.000 39.33919 ? 402 HOH A O   1 
HETATM 2753 O O   . HOH D 3 .   ? -9.91277  44.24596 36.78193 1.000 44.30315 ? 403 HOH A O   1 
HETATM 2754 O O   . HOH D 3 .   ? -18.671   19.388   23.297   1.000 44.69017 ? 404 HOH A O   1 
HETATM 2755 O O   . HOH D 3 .   ? -4.27321  26.62057 44.35127 1.000 38.81434 ? 405 HOH A O   1 
HETATM 2756 O O   . HOH D 3 .   ? -1.72759  23.60869 24.80064 1.000 31.16608 ? 406 HOH A O   1 
HETATM 2757 O O   . HOH D 3 .   ? -12.31415 42.62494 36.62542 1.000 43.67664 ? 407 HOH A O   1 
HETATM 2758 O O   . HOH D 3 .   ? 0.12294   43.78256 34.27212 1.000 26.90075 ? 408 HOH A O   1 
HETATM 2759 O O   . HOH D 3 .   ? -17.47528 18.25513 29.11751 1.000 34.23100 ? 409 HOH A O   1 
HETATM 2760 O O   . HOH D 3 .   ? -2.09234  44.95877 7.24875  1.000 47.46235 ? 410 HOH A O   1 
HETATM 2761 O O   . HOH D 3 .   ? -10.23587 40.08784 25.90068 1.000 39.85396 ? 411 HOH A O   1 
HETATM 2762 O O   . HOH D 3 .   ? 11.00097  18.25654 23.90575 1.000 40.22488 ? 412 HOH A O   1 
HETATM 2763 O O   . HOH D 3 .   ? -21.21907 29.43200 36.38170 1.000 44.14698 ? 413 HOH A O   1 
HETATM 2764 O O   . HOH D 3 .   ? -20.87139 23.58785 26.26508 1.000 36.13889 ? 414 HOH A O   1 
HETATM 2765 O O   . HOH D 3 .   ? -20.79530 33.33888 37.06279 1.000 52.48212 ? 415 HOH A O   1 
HETATM 2766 O O   . HOH D 3 .   ? -18.59304 26.30118 39.16317 1.000 36.60080 ? 416 HOH A O   1 
HETATM 2767 O O   . HOH D 3 .   ? 13.12828  19.14348 30.33116 1.000 48.07923 ? 417 HOH A O   1 
HETATM 2768 O O   . HOH D 3 .   ? 7.58636   37.47431 26.93733 1.000 24.46592 ? 418 HOH A O   1 
HETATM 2769 O O   . HOH D 3 .   ? -18.64670 34.94038 15.22254 1.000 50.52680 ? 419 HOH A O   1 
HETATM 2770 O O   . HOH D 3 .   ? -12.36049 40.13165 8.87417  1.000 45.80794 ? 420 HOH A O   1 
HETATM 2771 O O   . HOH D 3 .   ? -9.44195  34.86157 47.89664 1.000 39.87172 ? 421 HOH A O   1 
HETATM 2772 O O   . HOH D 3 .   ? -1.80474  19.44956 15.08504 1.000 36.67680 ? 422 HOH A O   1 
HETATM 2773 O O   . HOH D 3 .   ? -6.16099  21.47695 16.88718 1.000 36.30247 ? 423 HOH A O   1 
HETATM 2774 O O   . HOH D 3 .   ? 6.28726   50.81355 20.08586 1.000 38.14658 ? 424 HOH A O   1 
HETATM 2775 O O   . HOH D 3 .   ? 2.02102   41.88611 32.91500 1.000 28.76090 ? 425 HOH A O   1 
HETATM 2776 O O   . HOH D 3 .   ? 4.15076   37.78211 34.19801 1.000 38.57087 ? 426 HOH A O   1 
HETATM 2777 O O   . HOH D 3 .   ? -5.70480  52.24498 15.48981 1.000 40.44457 ? 427 HOH A O   1 
HETATM 2778 O O   . HOH D 3 .   ? -18.88240 28.08802 37.39537 1.000 36.27723 ? 428 HOH A O   1 
HETATM 2779 O O   . HOH D 3 .   ? -20.63904 24.86837 23.17339 1.000 36.77950 ? 429 HOH A O   1 
HETATM 2780 O O   . HOH D 3 .   ? -15.36715 39.40580 29.97820 1.000 43.22993 ? 430 HOH A O   1 
HETATM 2781 O O   . HOH D 3 .   ? -0.68246  23.55059 43.28737 1.000 46.22567 ? 431 HOH A O   1 
HETATM 2782 O O   . HOH D 3 .   ? -14.85194 23.51060 40.10240 1.000 40.48983 ? 432 HOH A O   1 
HETATM 2783 O O   . HOH D 3 .   ? 5.51052   21.81059 18.63688 1.000 29.25130 ? 433 HOH A O   1 
HETATM 2784 O O   . HOH D 3 .   ? -6.43918  26.47228 9.76315  1.000 37.39157 ? 434 HOH A O   1 
HETATM 2785 O O   . HOH D 3 .   ? -12.36325 32.00047 43.25999 1.000 40.71334 ? 435 HOH A O   1 
HETATM 2786 O O   . HOH D 3 .   ? -18.87861 34.37265 29.55537 1.000 35.16119 ? 436 HOH A O   1 
HETATM 2787 O O   . HOH D 3 .   ? -14.41384 32.12759 40.50437 1.000 42.33397 ? 437 HOH A O   1 
HETATM 2788 O O   . HOH D 3 .   ? -3.133    38.093   42.143   1.000 35.93519 ? 438 HOH A O   1 
HETATM 2789 O O   . HOH D 3 .   ? -8.26432  32.53173 8.64331  1.000 47.19364 ? 439 HOH A O   1 
HETATM 2790 O O   . HOH D 3 .   ? -8.82446  22.07034 17.27027 1.000 37.79477 ? 440 HOH A O   1 
HETATM 2791 O O   . HOH D 3 .   ? -3.53083  24.08988 10.75109 1.000 53.71609 ? 441 HOH A O   1 
HETATM 2792 O O   . HOH D 3 .   ? -2.33457  13.36813 22.75180 1.000 37.83232 ? 442 HOH A O   1 
HETATM 2793 O O   . HOH D 3 .   ? -9.11824  20.58770 20.16069 1.000 45.72287 ? 443 HOH A O   1 
HETATM 2794 O O   . HOH D 3 .   ? -7.10602  46.95219 35.47733 1.000 45.78739 ? 444 HOH A O   1 
HETATM 2795 O O   . HOH D 3 .   ? 0.29736   49.87621 28.78370 1.000 35.77280 ? 445 HOH A O   1 
HETATM 2796 O O   . HOH D 3 .   ? 0.40384   20.38088 13.22380 1.000 43.53119 ? 446 HOH A O   1 
HETATM 2797 O O   . HOH D 3 .   ? -9.91127  30.50087 10.99634 1.000 47.71495 ? 447 HOH A O   1 
HETATM 2798 O O   . HOH D 3 .   ? 1.39184   47.56907 7.20182  1.000 41.92053 ? 448 HOH A O   1 
HETATM 2799 O O   . HOH D 3 .   ? -12.81453 42.94364 31.79694 1.000 40.42450 ? 449 HOH A O   1 
HETATM 2800 O O   . HOH D 3 .   ? 2.60938   52.27114 23.23975 1.000 41.84118 ? 450 HOH A O   1 
HETATM 2801 O O   . HOH D 3 .   ? 2.09686   39.33638 34.14462 1.000 44.44481 ? 451 HOH A O   1 
HETATM 2802 O O   . HOH D 3 .   ? -9.86068  21.91774 15.01700 1.000 45.04872 ? 452 HOH A O   1 
HETATM 2803 O O   . HOH D 3 .   ? -17.99796 35.47248 37.25046 1.000 52.36163 ? 453 HOH A O   1 
HETATM 2804 O O   . HOH D 3 .   ? -10.58057 23.97922 13.59649 1.000 45.31780 ? 454 HOH A O   1 
HETATM 2805 O O   . HOH D 3 .   ? -19.64567 36.78243 33.13581 1.000 46.23082 ? 455 HOH A O   1 
HETATM 2806 O O   . HOH D 3 .   ? -1.28917  48.57465 34.83522 1.000 48.61529 ? 456 HOH A O   1 
HETATM 2807 O O   . HOH D 3 .   ? -11.57520 25.40997 45.74527 1.000 44.32620 ? 457 HOH A O   1 
HETATM 2808 O O   . HOH D 3 .   ? 0.72315   50.71572 24.54349 1.000 34.61682 ? 458 HOH A O   1 
HETATM 2809 O O   . HOH D 3 .   ? -12.20734 41.45027 26.81195 1.000 40.94529 ? 459 HOH A O   1 
HETATM 2810 O O   . HOH D 3 .   ? 3.42209   49.44283 7.41796  1.000 49.01262 ? 460 HOH A O   1 
HETATM 2811 O O   . HOH D 3 .   ? -1.76088  25.96170 43.53195 1.000 41.28580 ? 461 HOH A O   1 
HETATM 2812 O O   . HOH D 3 .   ? -15.28353 40.16190 9.68537  1.000 52.38750 ? 462 HOH A O   1 
HETATM 2813 O O   . HOH D 3 .   ? -17.68176 38.01328 33.92713 1.000 44.24981 ? 463 HOH A O   1 
HETATM 2814 O O   . HOH D 3 .   ? -19.80811 36.64337 30.79749 1.000 48.97169 ? 464 HOH A O   1 
HETATM 2815 O O   . HOH D 3 .   ? -18.14783 19.61406 26.18637 1.000 42.91854 ? 465 HOH A O   1 
HETATM 2816 O O   . HOH D 3 .   ? -8.77160  49.72975 31.97196 1.000 46.27395 ? 466 HOH A O   1 
HETATM 2817 O O   . HOH D 3 .   ? -22.03410 26.82437 35.75560 1.000 46.96761 ? 467 HOH A O   1 
HETATM 2818 O O   . HOH D 3 .   ? -16.978   18.407   19.534   1.000 45.59205 ? 468 HOH A O   1 
HETATM 2819 O O   . HOH D 3 .   ? -20.07389 32.92243 27.14776 1.000 47.96183 ? 469 HOH A O   1 
HETATM 2820 O O   . HOH D 3 .   ? 5.63029   36.01160 35.72608 1.000 43.05516 ? 470 HOH A O   1 
HETATM 2821 O O   . HOH D 3 .   ? -9.40477  33.13839 11.85125 1.000 37.07024 ? 471 HOH A O   1 
HETATM 2822 O O   . HOH D 3 .   ? 8.43684   28.77482 17.07940 1.000 49.73320 ? 472 HOH A O   1 
HETATM 2823 O O   . HOH D 3 .   ? -4.33833  37.57370 45.88851 1.000 39.42701 ? 473 HOH A O   1 
HETATM 2824 O O   . HOH D 3 .   ? -5.11359  52.62317 29.14798 1.000 46.97842 ? 474 HOH A O   1 
HETATM 2825 O O   . HOH D 3 .   ? -11.74110 18.59996 25.02036 1.000 39.51771 ? 475 HOH A O   1 
HETATM 2826 O O   . HOH D 3 .   ? -17.89165 34.92469 20.30145 1.000 45.74178 ? 476 HOH A O   1 
HETATM 2827 O O   . HOH D 3 .   ? 12.31012  22.49403 31.56690 1.000 41.60656 ? 477 HOH A O   1 
HETATM 2828 O O   . HOH D 3 .   ? -15.19363 35.57342 26.37106 1.000 34.13893 ? 478 HOH A O   1 
HETATM 2829 O O   . HOH D 3 .   ? -0.71839  41.08496 6.39054  1.000 45.46223 ? 479 HOH A O   1 
HETATM 2830 O O   . HOH D 3 .   ? 1.19641   40.99043 37.75606 1.000 36.02245 ? 480 HOH A O   1 
HETATM 2831 O O   . HOH D 3 .   ? -7.89445  15.71459 29.85071 1.000 41.41168 ? 481 HOH A O   1 
HETATM 2832 O O   . HOH D 3 .   ? -1.84497  42.53394 40.30111 1.000 46.39566 ? 482 HOH A O   1 
HETATM 2833 O O   . HOH D 3 .   ? -1.88475  43.39608 36.16008 1.000 34.37168 ? 483 HOH A O   1 
HETATM 2834 O O   . HOH D 3 .   ? -7.98658  44.97909 39.03063 1.000 52.89144 ? 484 HOH A O   1 
HETATM 2835 O O   . HOH D 3 .   ? -17.07203 17.65151 24.36844 1.000 46.03360 ? 485 HOH A O   1 
HETATM 2836 O O   . HOH D 3 .   ? -10.77960 38.28934 41.64967 1.000 38.73728 ? 486 HOH A O   1 
HETATM 2837 O O   . HOH D 3 .   ? -11.15745 47.26539 33.96112 1.000 50.39765 ? 487 HOH A O   1 
HETATM 2838 O O   . HOH D 3 .   ? -0.99481  38.08915 40.41941 1.000 34.34250 ? 488 HOH A O   1 
HETATM 2839 O O   . HOH D 3 .   ? -5.149    12.989   19.125   1.000 44.49311 ? 489 HOH A O   1 
HETATM 2840 O O   . HOH D 3 .   ? -7.76084  13.55395 27.38956 1.000 44.51558 ? 490 HOH A O   1 
HETATM 2841 O O   . HOH D 3 .   ? -16.07163 32.41197 38.12214 1.000 32.63287 ? 491 HOH A O   1 
HETATM 2842 O O   . HOH D 3 .   ? -5.41104  24.39390 45.27938 1.000 43.47822 ? 492 HOH A O   1 
HETATM 2843 O O   . HOH D 3 .   ? -6.85519  51.51141 27.87301 1.000 41.57235 ? 493 HOH A O   1 
HETATM 2844 O O   . HOH D 3 .   ? -3.09823  26.07974 9.14319  1.000 47.20863 ? 494 HOH A O   1 
HETATM 2845 O O   . HOH D 3 .   ? -7.58055  48.24755 9.88769  1.000 48.49542 ? 495 HOH A O   1 
HETATM 2846 O O   . HOH D 3 .   ? -12.81285 39.68091 40.39420 1.000 47.23490 ? 496 HOH A O   1 
HETATM 2847 O O   . HOH D 3 .   ? -6.33490  52.34442 24.20719 1.000 38.09950 ? 497 HOH A O   1 
HETATM 2848 O O   . HOH D 3 .   ? -15.73945 40.42615 38.13761 1.000 52.90081 ? 498 HOH A O   1 
HETATM 2849 O O   . HOH D 3 .   ? -3.24359  50.26643 25.53495 1.000 38.35026 ? 499 HOH A O   1 
HETATM 2850 O O   . HOH D 3 .   ? -17.66733 36.03996 27.48087 1.000 43.96629 ? 500 HOH A O   1 
HETATM 2851 O O   . HOH D 3 .   ? -3.73418  45.58230 36.80330 1.000 37.47693 ? 501 HOH A O   1 
HETATM 2852 O O   . HOH D 3 .   ? -8.99940  38.93339 45.88970 1.000 49.52396 ? 502 HOH A O   1 
HETATM 2853 O O   . HOH D 3 .   ? -17.28206 38.41851 28.61166 1.000 43.67753 ? 503 HOH A O   1 
HETATM 2854 O O   . HOH D 3 .   ? -11.18103 36.96428 44.09060 1.000 44.25877 ? 504 HOH A O   1 
HETATM 2855 O O   . HOH D 3 .   ? -4.54354  40.24966 4.75654  1.000 47.60050 ? 505 HOH A O   1 
HETATM 2856 O O   . HOH D 3 .   ? -9.82194  14.47103 24.42616 1.000 42.31454 ? 506 HOH A O   1 
HETATM 2857 O O   . HOH D 3 .   ? -22.65699 26.76866 23.45424 1.000 50.65556 ? 507 HOH A O   1 
HETATM 2858 O O   . HOH D 3 .   ? -19.72971 36.26114 25.64791 1.000 52.53730 ? 508 HOH A O   1 
HETATM 2859 O O   . HOH E 3 .   ? 22.05895  29.40876 32.16622 1.000 44.60072 ? 201 HOH B O   1 
HETATM 2860 O O   . HOH E 3 .   ? 30.84273  39.76360 24.77388 1.000 39.91106 ? 202 HOH B O   1 
HETATM 2861 O O   . HOH E 3 .   ? 18.73250  46.19454 33.20667 1.000 43.61426 ? 203 HOH B O   1 
HETATM 2862 O O   . HOH E 3 .   ? 36.55638  50.79678 9.27038  1.000 44.25000 ? 204 HOH B O   1 
HETATM 2863 O O   . HOH E 3 .   ? 29.34331  39.99012 3.16552  1.000 41.96332 ? 205 HOH B O   1 
HETATM 2864 O O   . HOH E 3 .   ? 18.38896  48.61378 32.52113 1.000 45.37946 ? 206 HOH B O   1 
HETATM 2865 O O   . HOH E 3 .   ? 25.26348  53.64335 20.17902 1.000 30.22971 ? 207 HOH B O   1 
HETATM 2866 O O   . HOH E 3 .   ? 20.33670  57.93022 19.70034 1.000 40.71886 ? 208 HOH B O   1 
HETATM 2867 O O   . HOH E 3 .   ? 14.40053  47.20120 7.40020  1.000 33.80807 ? 209 HOH B O   1 
HETATM 2868 O O   . HOH E 3 .   ? 8.97205   50.31657 28.31604 1.000 44.83886 ? 210 HOH B O   1 
HETATM 2869 O O   . HOH E 3 .   ? 33.70261  29.79915 18.69240 1.000 40.73130 ? 211 HOH B O   1 
HETATM 2870 O O   . HOH E 3 .   ? 20.01251  22.63409 18.44449 1.000 43.99336 ? 212 HOH B O   1 
HETATM 2871 O O   . HOH E 3 .   ? 24.27620  27.21617 20.56631 1.000 37.14028 ? 213 HOH B O   1 
HETATM 2872 O O   . HOH E 3 .   ? 17.40138  40.40640 6.64409  1.000 27.06090 ? 214 HOH B O   1 
HETATM 2873 O O   . HOH E 3 .   ? 32.43016  40.72288 20.34844 1.000 39.74495 ? 215 HOH B O   1 
HETATM 2874 O O   . HOH E 3 .   ? 16.03420  29.61342 33.92056 1.000 31.95716 ? 216 HOH B O   1 
HETATM 2875 O O   . HOH E 3 .   ? 31.74538  52.42409 18.35685 1.000 38.55116 ? 217 HOH B O   1 
HETATM 2876 O O   . HOH E 3 .   ? 25.13573  36.24012 31.19241 1.000 40.98283 ? 218 HOH B O   1 
HETATM 2877 O O   . HOH E 3 .   ? 8.16868   45.26083 28.88559 1.000 31.44810 ? 219 HOH B O   1 
HETATM 2878 O O   . HOH E 3 .   ? 14.04432  33.79600 -0.23706 1.000 46.45814 ? 220 HOH B O   1 
HETATM 2879 O O   . HOH E 3 .   ? 28.55472  29.39201 31.70620 1.000 43.05647 ? 221 HOH B O   1 
HETATM 2880 O O   . HOH E 3 .   ? 18.32194  22.77301 16.79741 1.000 48.14548 ? 222 HOH B O   1 
HETATM 2881 O O   . HOH E 3 .   ? 38.98581  43.19604 12.88637 1.000 44.75630 ? 223 HOH B O   1 
HETATM 2882 O O   . HOH E 3 .   ? 25.00357  55.31464 24.68734 1.000 43.26365 ? 224 HOH B O   1 
HETATM 2883 O O   . HOH E 3 .   ? 8.83602   37.59416 -5.00246 1.000 46.59543 ? 225 HOH B O   1 
HETATM 2884 O O   . HOH E 3 .   ? 12.94686  40.93589 34.56240 1.000 30.07244 ? 226 HOH B O   1 
HETATM 2885 O O   . HOH E 3 .   ? 24.91488  33.90660 4.82792  1.000 37.56108 ? 227 HOH B O   1 
HETATM 2886 O O   . HOH E 3 .   ? 30.53923  49.25448 13.63128 1.000 30.81643 ? 228 HOH B O   1 
HETATM 2887 O O   . HOH E 3 .   ? 20.84751  25.92855 29.96859 1.000 41.26532 ? 229 HOH B O   1 
HETATM 2888 O O   . HOH E 3 .   ? 10.40627  43.72604 21.86145 1.000 24.29284 ? 230 HOH B O   1 
HETATM 2889 O O   . HOH E 3 .   ? 22.56543  32.47589 34.12287 1.000 40.40856 ? 231 HOH B O   1 
HETATM 2890 O O   . HOH E 3 .   ? 22.28808  52.65792 28.64733 1.000 39.96929 ? 232 HOH B O   1 
HETATM 2891 O O   . HOH E 3 .   ? 19.70323  57.95589 11.29895 1.000 34.47065 ? 233 HOH B O   1 
HETATM 2892 O O   . HOH E 3 .   ? 20.32546  27.35004 6.74772  1.000 42.63627 ? 234 HOH B O   1 
HETATM 2893 O O   . HOH E 3 .   ? 23.28812  29.37068 11.02643 1.000 38.74721 ? 235 HOH B O   1 
HETATM 2894 O O   . HOH E 3 .   ? 6.08253   50.68370 10.13649 1.000 37.59832 ? 236 HOH B O   1 
HETATM 2895 O O   . HOH E 3 .   ? 29.49269  57.42201 11.09772 1.000 40.58085 ? 237 HOH B O   1 
HETATM 2896 O O   . HOH E 3 .   ? 30.08628  53.94954 19.91236 1.000 37.15239 ? 238 HOH B O   1 
HETATM 2897 O O   . HOH E 3 .   ? 26.31455  31.67978 25.03072 1.000 29.95714 ? 239 HOH B O   1 
HETATM 2898 O O   . HOH E 3 .   ? 33.65309  38.62215 4.38146  1.000 45.46980 ? 240 HOH B O   1 
HETATM 2899 O O   . HOH E 3 .   ? 23.84785  56.76665 18.69369 1.000 31.58104 ? 241 HOH B O   1 
HETATM 2900 O O   . HOH E 3 .   ? 8.32160   39.19532 24.79050 1.000 23.39430 ? 242 HOH B O   1 
HETATM 2901 O O   . HOH E 3 .   ? 13.15406  46.61671 31.35042 1.000 32.66759 ? 243 HOH B O   1 
HETATM 2902 O O   . HOH E 3 .   ? 24.34130  24.38374 24.04927 1.000 36.93975 ? 244 HOH B O   1 
HETATM 2903 O O   . HOH E 3 .   ? 25.71451  51.94715 26.13706 1.000 37.29533 ? 245 HOH B O   1 
HETATM 2904 O O   . HOH E 3 .   ? 20.50135  39.29578 36.23213 1.000 40.95791 ? 246 HOH B O   1 
HETATM 2905 O O   . HOH E 3 .   ? 29.23100  44.71285 21.87258 1.000 35.86555 ? 247 HOH B O   1 
HETATM 2906 O O   . HOH E 3 .   ? 10.25166  39.99946 22.97882 1.000 24.16711 ? 248 HOH B O   1 
HETATM 2907 O O   . HOH E 3 .   ? 22.89657  45.86667 0.75619  1.000 46.17282 ? 249 HOH B O   1 
HETATM 2908 O O   . HOH E 3 .   ? 10.55194  49.82493 18.37612 1.000 45.61043 ? 250 HOH B O   1 
HETATM 2909 O O   . HOH E 3 .   ? 21.17480  46.34057 33.14530 1.000 38.20043 ? 251 HOH B O   1 
HETATM 2910 O O   . HOH E 3 .   ? 25.36415  55.91035 16.52084 1.000 29.86183 ? 252 HOH B O   1 
HETATM 2911 O O   . HOH E 3 .   ? 1.31143   40.09514 7.34444  1.000 39.04974 ? 253 HOH B O   1 
HETATM 2912 O O   . HOH E 3 .   ? 20.04143  57.19507 23.39645 1.000 45.57002 ? 254 HOH B O   1 
HETATM 2913 O O   . HOH E 3 .   ? 17.68067  25.99957 19.28868 1.000 29.17413 ? 255 HOH B O   1 
HETATM 2914 O O   . HOH E 3 .   ? 25.25612  62.26244 13.43586 1.000 31.55531 ? 256 HOH B O   1 
HETATM 2915 O O   . HOH E 3 .   ? 32.01657  28.45041 14.08372 1.000 48.61477 ? 257 HOH B O   1 
HETATM 2916 O O   . HOH E 3 .   ? 29.01284  36.64645 6.45760  1.000 32.60523 ? 258 HOH B O   1 
HETATM 2917 O O   . HOH E 3 .   ? 12.05987  41.90583 22.87705 1.000 30.25704 ? 259 HOH B O   1 
HETATM 2918 O O   . HOH E 3 .   ? 31.81223  50.49688 22.05383 1.000 42.14313 ? 260 HOH B O   1 
HETATM 2919 O O   . HOH E 3 .   ? 13.58685  52.71764 29.62721 1.000 40.50323 ? 261 HOH B O   1 
HETATM 2920 O O   . HOH E 3 .   ? 24.29882  24.57799 15.18569 1.000 39.99625 ? 262 HOH B O   1 
HETATM 2921 O O   . HOH E 3 .   ? 18.44371  54.67790 6.72981  1.000 36.57052 ? 263 HOH B O   1 
HETATM 2922 O O   . HOH E 3 .   ? 22.08898  33.70010 36.92949 1.000 36.86895 ? 264 HOH B O   1 
HETATM 2923 O O   . HOH E 3 .   ? 18.64551  38.24569 -0.20577 1.000 35.57368 ? 265 HOH B O   1 
HETATM 2924 O O   . HOH E 3 .   ? 33.87693  52.87723 10.97050 1.000 41.79380 ? 266 HOH B O   1 
HETATM 2925 O O   . HOH E 3 .   ? 28.54703  47.36889 14.01506 1.000 26.95778 ? 267 HOH B O   1 
HETATM 2926 O O   . HOH E 3 .   ? 27.53522  55.07112 19.50551 1.000 30.94592 ? 268 HOH B O   1 
HETATM 2927 O O   . HOH E 3 .   ? 26.47417  59.74060 13.88128 1.000 28.37306 ? 269 HOH B O   1 
HETATM 2928 O O   . HOH E 3 .   ? 31.36035  58.91174 9.38405  1.000 44.21481 ? 270 HOH B O   1 
HETATM 2929 O O   . HOH E 3 .   ? 26.89415  28.52081 21.49047 1.000 35.89709 ? 271 HOH B O   1 
HETATM 2930 O O   . HOH E 3 .   ? 18.32958  53.56933 30.07894 1.000 40.58946 ? 272 HOH B O   1 
HETATM 2931 O O   . HOH E 3 .   ? 24.64354  29.46579 8.46621  1.000 40.61393 ? 273 HOH B O   1 
HETATM 2932 O O   . HOH E 3 .   ? 31.20413  51.56149 14.83914 1.000 30.02194 ? 274 HOH B O   1 
HETATM 2933 O O   . HOH E 3 .   ? 11.94445  30.76547 14.88383 1.000 40.51068 ? 275 HOH B O   1 
HETATM 2934 O O   . HOH E 3 .   ? 40.46954  48.78862 16.69794 1.000 52.35449 ? 276 HOH B O   1 
HETATM 2935 O O   . HOH E 3 .   ? 7.40916   50.04958 15.66154 1.000 37.87135 ? 277 HOH B O   1 
HETATM 2936 O O   . HOH E 3 .   ? 16.72550  54.76688 18.55834 1.000 30.87333 ? 278 HOH B O   1 
HETATM 2937 O O   . HOH E 3 .   ? 10.72597  25.85984 20.15979 1.000 32.68154 ? 279 HOH B O   1 
HETATM 2938 O O   . HOH E 3 .   ? 13.43163  28.37172 7.79729  1.000 41.42149 ? 280 HOH B O   1 
HETATM 2939 O O   . HOH E 3 .   ? 23.60614  43.77098 0.38212  1.000 44.02629 ? 281 HOH B O   1 
HETATM 2940 O O   . HOH E 3 .   ? 13.39063  50.27936 22.70765 1.000 29.72127 ? 282 HOH B O   1 
HETATM 2941 O O   . HOH E 3 .   ? 12.74416  48.83970 8.37704  1.000 34.14432 ? 283 HOH B O   1 
HETATM 2942 O O   . HOH E 3 .   ? 11.75305  22.44932 21.76514 1.000 36.08773 ? 284 HOH B O   1 
HETATM 2943 O O   . HOH E 3 .   ? 26.47501  43.84467 23.95971 1.000 37.23632 ? 285 HOH B O   1 
HETATM 2944 O O   . HOH E 3 .   ? 27.61852  55.10799 22.93612 1.000 41.01908 ? 286 HOH B O   1 
HETATM 2945 O O   . HOH E 3 .   ? 18.17930  55.18376 20.96717 1.000 32.83284 ? 287 HOH B O   1 
HETATM 2946 O O   . HOH E 3 .   ? 33.70652  31.58398 25.10182 1.000 47.94450 ? 288 HOH B O   1 
HETATM 2947 O O   . HOH E 3 .   ? 33.66015  37.17736 18.64265 1.000 34.43728 ? 289 HOH B O   1 
HETATM 2948 O O   . HOH E 3 .   ? 16.203    56.678   14.401   1.000 38.39067 ? 290 HOH B O   1 
HETATM 2949 O O   . HOH E 3 .   ? 30.71270  55.60765 12.36117 1.000 42.46956 ? 291 HOH B O   1 
HETATM 2950 O O   . HOH E 3 .   ? 11.85472  24.61776 14.36699 1.000 52.76657 ? 292 HOH B O   1 
HETATM 2951 O O   . HOH E 3 .   ? 20.92688  38.41835 0.28952  1.000 42.48484 ? 293 HOH B O   1 
HETATM 2952 O O   . HOH E 3 .   ? 8.66350   49.38465 25.79187 1.000 43.07892 ? 294 HOH B O   1 
HETATM 2953 O O   . HOH E 3 .   ? 12.66405  30.75907 7.56223  1.000 34.28465 ? 295 HOH B O   1 
HETATM 2954 O O   . HOH E 3 .   ? 16.336    42.189   37.573   1.000 47.68075 ? 296 HOH B O   1 
HETATM 2955 O O   . HOH E 3 .   ? 17.57353  26.80321 37.35508 1.000 43.22096 ? 297 HOH B O   1 
HETATM 2956 O O   . HOH E 3 .   ? 18.31053  38.67562 37.53316 1.000 38.75249 ? 298 HOH B O   1 
HETATM 2957 O O   . HOH E 3 .   ? 26.84248  30.85240 22.46108 1.000 34.79657 ? 299 HOH B O   1 
HETATM 2958 O O   . HOH E 3 .   ? 22.38824  38.28324 37.62694 1.000 45.91230 ? 300 HOH B O   1 
HETATM 2959 O O   . HOH E 3 .   ? 29.41559  27.96440 28.78912 1.000 45.33319 ? 301 HOH B O   1 
HETATM 2960 O O   . HOH E 3 .   ? 29.20979  55.67667 3.99757  1.000 41.05143 ? 302 HOH B O   1 
HETATM 2961 O O   . HOH E 3 .   ? 38.27555  37.60959 11.14354 1.000 41.53668 ? 303 HOH B O   1 
HETATM 2962 O O   . HOH E 3 .   ? 31.09601  47.92041 22.64815 1.000 41.82159 ? 304 HOH B O   1 
HETATM 2963 O O   . HOH E 3 .   ? 37.59786  44.35025 14.91290 1.000 48.72495 ? 305 HOH B O   1 
HETATM 2964 O O   . HOH E 3 .   ? 8.72886   42.92724 19.77288 1.000 26.48873 ? 306 HOH B O   1 
HETATM 2965 O O   . HOH E 3 .   ? 12.90524  43.60790 35.17713 1.000 43.70083 ? 307 HOH B O   1 
HETATM 2966 O O   . HOH E 3 .   ? 12.62984  50.36150 25.30506 1.000 30.60373 ? 308 HOH B O   1 
HETATM 2967 O O   . HOH E 3 .   ? 15.27147  52.19257 24.16376 1.000 32.14623 ? 309 HOH B O   1 
HETATM 2968 O O   . HOH E 3 .   ? 18.29868  25.55677 7.97967  1.000 44.53109 ? 310 HOH B O   1 
HETATM 2969 O O   . HOH E 3 .   ? 23.58756  26.59391 7.97122  1.000 49.54032 ? 311 HOH B O   1 
HETATM 2970 O O   . HOH E 3 .   ? 19.41598  37.52184 8.01271  1.000 39.32975 ? 312 HOH B O   1 
HETATM 2971 O O   . HOH E 3 .   ? 28.86661  48.22499 26.21662 1.000 48.18008 ? 313 HOH B O   1 
HETATM 2972 O O   . HOH E 3 .   ? 20.816    61.601   18.939   1.000 39.26727 ? 314 HOH B O   1 
HETATM 2973 O O   . HOH E 3 .   ? 19.195    62.274   5.131    1.000 41.02291 ? 315 HOH B O   1 
HETATM 2974 O O   . HOH E 3 .   ? 9.60302   32.87938 8.49747  1.000 43.66197 ? 316 HOH B O   1 
HETATM 2975 O O   . HOH E 3 .   ? 18.07884  22.50938 28.15511 1.000 47.53432 ? 317 HOH B O   1 
HETATM 2976 O O   . HOH E 3 .   ? 31.84229  36.47178 30.83363 1.000 48.90370 ? 318 HOH B O   1 
HETATM 2977 O O   . HOH E 3 .   ? 29.50271  58.13986 4.61592  1.000 45.89555 ? 319 HOH B O   1 
HETATM 2978 O O   . HOH E 3 .   ? 13.14254  27.66901 13.86512 1.000 44.96969 ? 320 HOH B O   1 
HETATM 2979 O O   . HOH E 3 .   ? 9.81462   40.06260 34.45112 1.000 34.50270 ? 321 HOH B O   1 
HETATM 2980 O O   . HOH E 3 .   ? 36.22721  42.30959 2.74784  1.000 37.07513 ? 322 HOH B O   1 
HETATM 2981 O O   . HOH E 3 .   ? 14.15334  45.47083 33.29157 1.000 41.67315 ? 323 HOH B O   1 
HETATM 2982 O O   . HOH E 3 .   ? 35.28590  46.18319 18.27735 1.000 36.91139 ? 324 HOH B O   1 
HETATM 2983 O O   . HOH E 3 .   ? 17.36468  31.15458 0.16355  1.000 54.10985 ? 325 HOH B O   1 
HETATM 2984 O O   . HOH E 3 .   ? 32.59601  27.09508 16.11120 1.000 53.13042 ? 326 HOH B O   1 
HETATM 2985 O O   . HOH E 3 .   ? 25.76780  24.96493 21.62385 1.000 46.65975 ? 327 HOH B O   1 
HETATM 2986 O O   . HOH E 3 .   ? 12.08882  35.59096 36.47213 1.000 37.75754 ? 328 HOH B O   1 
HETATM 2987 O O   . HOH E 3 .   ? 35.81863  52.55148 7.08506  1.000 42.45593 ? 329 HOH B O   1 
HETATM 2988 O O   . HOH E 3 .   ? 14.80900  48.66040 31.35130 1.000 41.63037 ? 330 HOH B O   1 
HETATM 2989 O O   . HOH E 3 .   ? 11.37021  50.34483 7.25678  1.000 46.47709 ? 331 HOH B O   1 
HETATM 2990 O O   . HOH E 3 .   ? 6.40225   43.92299 2.33359  1.000 50.92610 ? 332 HOH B O   1 
HETATM 2991 O O   . HOH E 3 .   ? 27.63093  63.88020 12.94098 1.000 44.91971 ? 333 HOH B O   1 
HETATM 2992 O O   . HOH E 3 .   ? 7.05210   34.09860 2.29463  1.000 51.54187 ? 334 HOH B O   1 
HETATM 2993 O O   . HOH E 3 .   ? 28.32572  50.68445 24.92630 1.000 39.78957 ? 335 HOH B O   1 
HETATM 2994 O O   . HOH E 3 .   ? 9.80342   50.40799 21.06938 1.000 48.93238 ? 336 HOH B O   1 
HETATM 2995 O O   . HOH E 3 .   ? 21.90554  54.74410 27.36233 1.000 46.49101 ? 337 HOH B O   1 
HETATM 2996 O O   . HOH E 3 .   ? 17.74845  53.59704 23.22274 1.000 38.56272 ? 338 HOH B O   1 
HETATM 2997 O O   . HOH E 3 .   ? 21.76644  24.11209 12.49665 1.000 51.31450 ? 339 HOH B O   1 
HETATM 2998 O O   . HOH E 3 .   ? 33.64494  53.69349 17.23871 1.000 46.57486 ? 340 HOH B O   1 
HETATM 2999 O O   . HOH E 3 .   ? 13.11298  21.17443 25.40643 1.000 49.76876 ? 341 HOH B O   1 
HETATM 3000 O O   . HOH E 3 .   ? 27.77011  65.29092 14.73106 1.000 56.07722 ? 342 HOH B O   1 
HETATM 3001 O O   . HOH E 3 .   ? 18.65559  55.55231 4.31181  1.000 49.34924 ? 343 HOH B O   1 
HETATM 3002 O O   . HOH E 3 .   ? 31.72065  25.34984 18.57445 1.000 54.25371 ? 344 HOH B O   1 
HETATM 3003 O O   . HOH E 3 .   ? 33.54094  51.37313 20.19115 1.000 42.31082 ? 345 HOH B O   1 
HETATM 3004 O O   . HOH E 3 .   ? 11.68904  48.17943 6.42112  1.000 41.02877 ? 346 HOH B O   1 
HETATM 3005 O O   . HOH E 3 .   ? 32.67792  34.53368 29.14592 1.000 51.17137 ? 347 HOH B O   1 
HETATM 3006 O O   . HOH E 3 .   ? 17.406    38.565   -2.826   1.000 39.60925 ? 348 HOH B O   1 
HETATM 3007 O O   . HOH E 3 .   ? 9.86192   46.56444 30.79143 1.000 42.57479 ? 349 HOH B O   1 
HETATM 3008 O O   . HOH E 3 .   ? 28.96225  24.94672 19.19577 1.000 51.08841 ? 350 HOH B O   1 
HETATM 3009 O O   . HOH E 3 .   ? 13.66316  39.66552 36.95000 1.000 39.21937 ? 351 HOH B O   1 
HETATM 3010 O O   . HOH E 3 .   ? 23.62241  29.94590 35.56869 1.000 47.60226 ? 352 HOH B O   1 
HETATM 3011 O O   . HOH E 3 .   ? 10.470    53.527   14.731   1.000 44.05285 ? 353 HOH B O   1 
HETATM 3012 O O   . HOH E 3 .   ? 35.77860  39.82669 5.50759  1.000 44.77555 ? 354 HOH B O   1 
HETATM 3013 O O   . HOH E 3 .   ? 31.68261  43.47262 20.11775 1.000 40.27960 ? 355 HOH B O   1 
HETATM 3014 O O   . HOH E 3 .   ? 38.21577  51.89412 10.87722 1.000 51.27452 ? 356 HOH B O   1 
HETATM 3015 O O   . HOH E 3 .   ? 25.91749  58.59520 16.35058 1.000 33.30727 ? 357 HOH B O   1 
HETATM 3016 O O   . HOH E 3 .   ? 28.79146  45.75026 24.83500 1.000 50.33623 ? 358 HOH B O   1 
HETATM 3017 O O   . HOH E 3 .   ? 10.359    55.994   12.412   1.000 42.50089 ? 359 HOH B O   1 
HETATM 3018 O O   . HOH E 3 .   ? 9.45651   31.10970 14.42638 1.000 48.86545 ? 360 HOH B O   1 
HETATM 3019 O O   . HOH E 3 .   ? 36.57713  43.69554 17.33125 1.000 49.40296 ? 361 HOH B O   1 
HETATM 3020 O O   . HOH E 3 .   ? 23.567    62.999   15.882   1.000 39.51289 ? 362 HOH B O   1 
HETATM 3021 O O   . HOH E 3 .   ? 14.11125  22.66741 28.09903 1.000 46.81894 ? 363 HOH B O   1 
HETATM 3022 O O   . HOH E 3 .   ? 12.76995  51.94164 20.19702 1.000 44.49196 ? 364 HOH B O   1 
HETATM 3023 O O   . HOH E 3 .   ? 8.68886   50.96074 23.81981 1.000 48.93812 ? 365 HOH B O   1 
HETATM 3024 O O   . HOH E 3 .   ? 24.43735  22.17795 25.01478 1.000 41.69955 ? 366 HOH B O   1 
HETATM 3025 O O   . HOH E 3 .   ? 34.79367  37.18871 21.09921 1.000 48.19998 ? 367 HOH B O   1 
HETATM 3026 O O   . HOH E 3 .   ? 14.46366  31.21308 0.15231  1.000 47.97074 ? 368 HOH B O   1 
HETATM 3027 O O   . HOH E 3 .   ? 26.23658  53.82576 28.26046 1.000 50.86229 ? 369 HOH B O   1 
HETATM 3028 O O   . HOH E 3 .   ? 28.70956  39.69384 0.34086  1.000 44.46536 ? 370 HOH B O   1 
HETATM 3029 O O   . HOH E 3 .   ? 21.20540  23.53168 14.59977 1.000 49.31303 ? 371 HOH B O   1 
HETATM 3030 O O   . HOH E 3 .   ? 32.41628  53.46226 13.41310 1.000 37.39843 ? 372 HOH B O   1 
HETATM 3031 O O   . HOH E 3 .   ? 10.02196  46.73799 5.53358  1.000 46.66098 ? 373 HOH B O   1 
HETATM 3032 O O   . HOH E 3 .   ? 28.96772  59.78868 12.91863 1.000 36.50357 ? 374 HOH B O   1 
HETATM 3033 O O   . HOH E 3 .   ? 27.49194  57.63047 19.64266 1.000 46.97884 ? 375 HOH B O   1 
HETATM 3034 O O   . HOH E 3 .   ? 33.10718  46.65235 21.96159 1.000 46.99870 ? 376 HOH B O   1 
HETATM 3035 O O   . HOH E 3 .   ? 34.04415  44.50556 20.28124 1.000 44.75099 ? 377 HOH B O   1 
HETATM 3036 O O   . HOH E 3 .   ? 18.83807  55.44227 25.28717 1.000 43.91846 ? 378 HOH B O   1 
HETATM 3037 O O   . HOH E 3 .   ? 12.04609  37.91473 37.72859 1.000 43.46254 ? 379 HOH B O   1 
HETATM 3038 O O   . HOH E 3 .   ? 32.29839  27.13815 11.75463 1.000 52.15466 ? 380 HOH B O   1 
HETATM 3039 O O   . HOH E 3 .   ? 10.966    55.973   18.029   1.000 38.96064 ? 381 HOH B O   1 
HETATM 3040 O O   . HOH E 3 .   ? 29.77049  62.49291 12.07751 1.000 48.72636 ? 382 HOH B O   1 
HETATM 3041 O O   . HOH E 3 .   ? 10.06841  44.88047 34.28915 1.000 47.05919 ? 383 HOH B O   1 
HETATM 3042 O O   . HOH E 3 .   ? 28.13703  37.27213 -0.87400 1.000 50.02388 ? 384 HOH B O   1 
# 
