data_7HZP
# 
_entry.id   7HZP 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   7HZP         pdb_00007hzp 10.2210/pdb7hzp/pdb 
WWPDB D_1001408133 ?            ?                   
# 
_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       2025-02-12 
# 
_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.entry_id                        7HZP 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-14 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
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 'Protease 2A'                                                     15892.732 1   3.4.22.29 ? ? ? 
2 non-polymer syn 'ZINC ION'                                                        65.409    1   ?         ? ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                              78.133    2   ?         ? ? ? 
4 non-polymer syn 'SULFATE ION'                                                     96.063    1   ?         ? ? ? 
5 non-polymer syn '1-methyl-N-[2-(1,3-oxazol-4-yl)ethyl]-1H-indazole-3-carboxamide' 270.287   1   ?         ? ? ? 
6 water       nat water                                                             18.015    232 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'P2A,Picornain 2A,Protein 2A' 
# 
_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       
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                        ZN    
3 'DIMETHYL SULFOXIDE'                                              DMS   
4 'SULFATE ION'                                                     SO4   
5 '1-methyl-N-[2-(1,3-oxazol-4-yl)ethyl]-1H-indazole-3-carboxamide' A1BQ2 
6 water                                                             HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   ALA n 
1 4   ILE n 
1 5   TYR n 
1 6   VAL n 
1 7   GLY n 
1 8   ASN n 
1 9   TYR n 
1 10  ARG n 
1 11  VAL n 
1 12  VAL n 
1 13  ASN n 
1 14  ARG n 
1 15  HIS n 
1 16  LEU n 
1 17  ALA n 
1 18  THR n 
1 19  HIS n 
1 20  ASN n 
1 21  ASP n 
1 22  TRP n 
1 23  ALA n 
1 24  ASN n 
1 25  LEU n 
1 26  VAL n 
1 27  TRP n 
1 28  GLU n 
1 29  ASP n 
1 30  SER n 
1 31  SER n 
1 32  ARG n 
1 33  ASP n 
1 34  LEU n 
1 35  LEU n 
1 36  VAL n 
1 37  SER n 
1 38  SER n 
1 39  THR n 
1 40  THR n 
1 41  ALA n 
1 42  GLN n 
1 43  GLY n 
1 44  CYS n 
1 45  ASP n 
1 46  THR n 
1 47  ILE n 
1 48  ALA n 
1 49  ARG n 
1 50  CYS n 
1 51  ASP n 
1 52  CYS n 
1 53  GLN n 
1 54  THR n 
1 55  GLY n 
1 56  VAL n 
1 57  TYR n 
1 58  TYR n 
1 59  CYS n 
1 60  SER n 
1 61  SER n 
1 62  ARG n 
1 63  ARG n 
1 64  LYS n 
1 65  HIS n 
1 66  TYR n 
1 67  PRO n 
1 68  VAL n 
1 69  SER n 
1 70  PHE n 
1 71  SER n 
1 72  LYS n 
1 73  PRO n 
1 74  SER n 
1 75  LEU n 
1 76  ILE n 
1 77  PHE n 
1 78  VAL n 
1 79  GLU n 
1 80  ALA n 
1 81  SER n 
1 82  GLU n 
1 83  TYR n 
1 84  TYR n 
1 85  PRO n 
1 86  ALA n 
1 87  ARG n 
1 88  TYR n 
1 89  GLN n 
1 90  SER n 
1 91  HIS n 
1 92  LEU n 
1 93  MET n 
1 94  LEU n 
1 95  ALA n 
1 96  VAL n 
1 97  GLY n 
1 98  HIS n 
1 99  SER n 
1 100 GLU n 
1 101 PRO n 
1 102 GLY n 
1 103 ASP n 
1 104 CYS n 
1 105 GLY n 
1 106 GLY n 
1 107 ILE n 
1 108 LEU n 
1 109 ARG n 
1 110 CYS n 
1 111 GLN n 
1 112 HIS n 
1 113 GLY n 
1 114 VAL n 
1 115 VAL n 
1 116 GLY n 
1 117 ILE n 
1 118 VAL n 
1 119 SER n 
1 120 THR n 
1 121 GLY n 
1 122 GLY n 
1 123 ASN n 
1 124 GLY n 
1 125 LEU n 
1 126 VAL n 
1 127 GLY n 
1 128 PHE n 
1 129 ALA n 
1 130 ASP n 
1 131 VAL n 
1 132 ARG n 
1 133 ASP n 
1 134 LEU n 
1 135 LEU n 
1 136 TRP n 
1 137 LEU n 
1 138 ASP n 
1 139 GLU n 
1 140 GLU n 
1 141 ALA n 
1 142 MET n 
1 143 GLU n 
1 144 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   144 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Coxsackievirus A16' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     31704 
_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 
A1BQ2 non-polymer         . '1-methyl-N-[2-(1,3-oxazol-4-yl)ethyl]-1H-indazole-3-carboxamide' ? 'C14 H14 N4 O2'  270.287 
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 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                              ? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                         ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                   ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                           ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                         ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                             ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                        ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                           ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                            ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                        ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                     ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                           ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                            ? 'C3 H7 N O3'     105.093 
SO4   non-polymer         . 'SULFATE ION'                                                     ? 'O4 S -2'        96.063  
THR   'L-peptide linking' y THREONINE                                                         ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                        ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                          ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                            ? 'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION'                                                        ? 'Zn 2'           65.409  
# 
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   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 146 GLU GLU A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BQ2 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BQ2 
_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 
B 2 ZN    1   201 1   ZN    ZN  A . 
C 3 DMS   1   202 0   DMS   DMS A . 
D 3 DMS   1   203 3   DMS   DMS A . 
E 4 SO4   1   204 1   SO4   SO4 A . 
F 5 A1BQ2 1   205 301 A1BQ2 LIG A . 
G 6 HOH   1   301 43  HOH   HOH A . 
G 6 HOH   2   302 48  HOH   HOH A . 
G 6 HOH   3   303 220 HOH   HOH A . 
G 6 HOH   4   304 245 HOH   HOH A . 
G 6 HOH   5   305 191 HOH   HOH A . 
G 6 HOH   6   306 226 HOH   HOH A . 
G 6 HOH   7   307 152 HOH   HOH A . 
G 6 HOH   8   308 79  HOH   HOH A . 
G 6 HOH   9   309 40  HOH   HOH A . 
G 6 HOH   10  310 30  HOH   HOH A . 
G 6 HOH   11  311 15  HOH   HOH A . 
G 6 HOH   12  312 50  HOH   HOH A . 
G 6 HOH   13  313 154 HOH   HOH A . 
G 6 HOH   14  314 36  HOH   HOH A . 
G 6 HOH   15  315 53  HOH   HOH A . 
G 6 HOH   16  316 113 HOH   HOH A . 
G 6 HOH   17  317 77  HOH   HOH A . 
G 6 HOH   18  318 24  HOH   HOH A . 
G 6 HOH   19  319 229 HOH   HOH A . 
G 6 HOH   20  320 19  HOH   HOH A . 
G 6 HOH   21  321 182 HOH   HOH A . 
G 6 HOH   22  322 132 HOH   HOH A . 
G 6 HOH   23  323 178 HOH   HOH A . 
G 6 HOH   24  324 58  HOH   HOH A . 
G 6 HOH   25  325 35  HOH   HOH A . 
G 6 HOH   26  326 49  HOH   HOH A . 
G 6 HOH   27  327 153 HOH   HOH A . 
G 6 HOH   28  328 104 HOH   HOH A . 
G 6 HOH   29  329 107 HOH   HOH A . 
G 6 HOH   30  330 186 HOH   HOH A . 
G 6 HOH   31  331 221 HOH   HOH A . 
G 6 HOH   32  332 121 HOH   HOH A . 
G 6 HOH   33  333 146 HOH   HOH A . 
G 6 HOH   34  334 34  HOH   HOH A . 
G 6 HOH   35  335 72  HOH   HOH A . 
G 6 HOH   36  336 68  HOH   HOH A . 
G 6 HOH   37  337 63  HOH   HOH A . 
G 6 HOH   38  338 231 HOH   HOH A . 
G 6 HOH   39  339 111 HOH   HOH A . 
G 6 HOH   40  340 254 HOH   HOH A . 
G 6 HOH   41  341 59  HOH   HOH A . 
G 6 HOH   42  342 108 HOH   HOH A . 
G 6 HOH   43  343 131 HOH   HOH A . 
G 6 HOH   44  344 84  HOH   HOH A . 
G 6 HOH   45  345 41  HOH   HOH A . 
G 6 HOH   46  346 94  HOH   HOH A . 
G 6 HOH   47  347 190 HOH   HOH A . 
G 6 HOH   48  348 106 HOH   HOH A . 
G 6 HOH   49  349 119 HOH   HOH A . 
G 6 HOH   50  350 181 HOH   HOH A . 
G 6 HOH   51  351 255 HOH   HOH A . 
G 6 HOH   52  352 4   HOH   HOH A . 
G 6 HOH   53  353 150 HOH   HOH A . 
G 6 HOH   54  354 3   HOH   HOH A . 
G 6 HOH   55  355 14  HOH   HOH A . 
G 6 HOH   56  356 216 HOH   HOH A . 
G 6 HOH   57  357 37  HOH   HOH A . 
G 6 HOH   58  358 13  HOH   HOH A . 
G 6 HOH   59  359 20  HOH   HOH A . 
G 6 HOH   60  360 7   HOH   HOH A . 
G 6 HOH   61  361 251 HOH   HOH A . 
G 6 HOH   62  362 2   HOH   HOH A . 
G 6 HOH   63  363 82  HOH   HOH A . 
G 6 HOH   64  364 16  HOH   HOH A . 
G 6 HOH   65  365 25  HOH   HOH A . 
G 6 HOH   66  366 252 HOH   HOH A . 
G 6 HOH   67  367 257 HOH   HOH A . 
G 6 HOH   68  368 42  HOH   HOH A . 
G 6 HOH   69  369 170 HOH   HOH A . 
G 6 HOH   70  370 62  HOH   HOH A . 
G 6 HOH   71  371 250 HOH   HOH A . 
G 6 HOH   72  372 38  HOH   HOH A . 
G 6 HOH   73  373 9   HOH   HOH A . 
G 6 HOH   74  374 174 HOH   HOH A . 
G 6 HOH   75  375 27  HOH   HOH A . 
G 6 HOH   76  376 95  HOH   HOH A . 
G 6 HOH   77  377 28  HOH   HOH A . 
G 6 HOH   78  378 237 HOH   HOH A . 
G 6 HOH   79  379 26  HOH   HOH A . 
G 6 HOH   80  380 184 HOH   HOH A . 
G 6 HOH   81  381 256 HOH   HOH A . 
G 6 HOH   82  382 126 HOH   HOH A . 
G 6 HOH   83  383 51  HOH   HOH A . 
G 6 HOH   84  384 264 HOH   HOH A . 
G 6 HOH   85  385 33  HOH   HOH A . 
G 6 HOH   86  386 97  HOH   HOH A . 
G 6 HOH   87  387 227 HOH   HOH A . 
G 6 HOH   88  388 177 HOH   HOH A . 
G 6 HOH   89  389 200 HOH   HOH A . 
G 6 HOH   90  390 64  HOH   HOH A . 
G 6 HOH   91  391 211 HOH   HOH A . 
G 6 HOH   92  392 162 HOH   HOH A . 
G 6 HOH   93  393 116 HOH   HOH A . 
G 6 HOH   94  394 218 HOH   HOH A . 
G 6 HOH   95  395 12  HOH   HOH A . 
G 6 HOH   96  396 70  HOH   HOH A . 
G 6 HOH   97  397 144 HOH   HOH A . 
G 6 HOH   98  398 76  HOH   HOH A . 
G 6 HOH   99  399 185 HOH   HOH A . 
G 6 HOH   100 400 169 HOH   HOH A . 
G 6 HOH   101 401 124 HOH   HOH A . 
G 6 HOH   102 402 29  HOH   HOH A . 
G 6 HOH   103 403 8   HOH   HOH A . 
G 6 HOH   104 404 91  HOH   HOH A . 
G 6 HOH   105 405 151 HOH   HOH A . 
G 6 HOH   106 406 263 HOH   HOH A . 
G 6 HOH   107 407 93  HOH   HOH A . 
G 6 HOH   108 408 123 HOH   HOH A . 
G 6 HOH   109 409 147 HOH   HOH A . 
G 6 HOH   110 410 168 HOH   HOH A . 
G 6 HOH   111 411 6   HOH   HOH A . 
G 6 HOH   112 412 238 HOH   HOH A . 
G 6 HOH   113 413 141 HOH   HOH A . 
G 6 HOH   114 414 32  HOH   HOH A . 
G 6 HOH   115 415 11  HOH   HOH A . 
G 6 HOH   116 416 23  HOH   HOH A . 
G 6 HOH   117 417 105 HOH   HOH A . 
G 6 HOH   118 418 10  HOH   HOH A . 
G 6 HOH   119 419 214 HOH   HOH A . 
G 6 HOH   120 420 128 HOH   HOH A . 
G 6 HOH   121 421 67  HOH   HOH A . 
G 6 HOH   122 422 158 HOH   HOH A . 
G 6 HOH   123 423 183 HOH   HOH A . 
G 6 HOH   124 424 133 HOH   HOH A . 
G 6 HOH   125 425 89  HOH   HOH A . 
G 6 HOH   126 426 203 HOH   HOH A . 
G 6 HOH   127 427 210 HOH   HOH A . 
G 6 HOH   128 428 69  HOH   HOH A . 
G 6 HOH   129 429 176 HOH   HOH A . 
G 6 HOH   130 430 157 HOH   HOH A . 
G 6 HOH   131 431 140 HOH   HOH A . 
G 6 HOH   132 432 159 HOH   HOH A . 
G 6 HOH   133 433 100 HOH   HOH A . 
G 6 HOH   134 434 101 HOH   HOH A . 
G 6 HOH   135 435 261 HOH   HOH A . 
G 6 HOH   136 436 167 HOH   HOH A . 
G 6 HOH   137 437 71  HOH   HOH A . 
G 6 HOH   138 438 161 HOH   HOH A . 
G 6 HOH   139 439 85  HOH   HOH A . 
G 6 HOH   140 440 103 HOH   HOH A . 
G 6 HOH   141 441 219 HOH   HOH A . 
G 6 HOH   142 442 39  HOH   HOH A . 
G 6 HOH   143 443 80  HOH   HOH A . 
G 6 HOH   144 444 110 HOH   HOH A . 
G 6 HOH   145 445 122 HOH   HOH A . 
G 6 HOH   146 446 197 HOH   HOH A . 
G 6 HOH   147 447 198 HOH   HOH A . 
G 6 HOH   148 448 96  HOH   HOH A . 
G 6 HOH   149 449 135 HOH   HOH A . 
G 6 HOH   150 450 239 HOH   HOH A . 
G 6 HOH   151 451 224 HOH   HOH A . 
G 6 HOH   152 452 201 HOH   HOH A . 
G 6 HOH   153 453 90  HOH   HOH A . 
G 6 HOH   154 454 236 HOH   HOH A . 
G 6 HOH   155 455 171 HOH   HOH A . 
G 6 HOH   156 456 205 HOH   HOH A . 
G 6 HOH   157 457 61  HOH   HOH A . 
G 6 HOH   158 458 207 HOH   HOH A . 
G 6 HOH   159 459 223 HOH   HOH A . 
G 6 HOH   160 460 232 HOH   HOH A . 
G 6 HOH   161 461 88  HOH   HOH A . 
G 6 HOH   162 462 192 HOH   HOH A . 
G 6 HOH   163 463 87  HOH   HOH A . 
G 6 HOH   164 464 175 HOH   HOH A . 
G 6 HOH   165 465 189 HOH   HOH A . 
G 6 HOH   166 466 65  HOH   HOH A . 
G 6 HOH   167 467 248 HOH   HOH A . 
G 6 HOH   168 468 136 HOH   HOH A . 
G 6 HOH   169 469 212 HOH   HOH A . 
G 6 HOH   170 470 156 HOH   HOH A . 
G 6 HOH   171 471 213 HOH   HOH A . 
G 6 HOH   172 472 233 HOH   HOH A . 
G 6 HOH   173 473 99  HOH   HOH A . 
G 6 HOH   174 474 164 HOH   HOH A . 
G 6 HOH   175 475 78  HOH   HOH A . 
G 6 HOH   176 476 258 HOH   HOH A . 
G 6 HOH   177 477 234 HOH   HOH A . 
G 6 HOH   178 478 208 HOH   HOH A . 
G 6 HOH   179 479 148 HOH   HOH A . 
G 6 HOH   180 480 138 HOH   HOH A . 
G 6 HOH   181 481 52  HOH   HOH A . 
G 6 HOH   182 482 230 HOH   HOH A . 
G 6 HOH   183 483 241 HOH   HOH A . 
G 6 HOH   184 484 243 HOH   HOH A . 
G 6 HOH   185 485 114 HOH   HOH A . 
G 6 HOH   186 486 262 HOH   HOH A . 
G 6 HOH   187 487 134 HOH   HOH A . 
G 6 HOH   188 488 46  HOH   HOH A . 
G 6 HOH   189 489 47  HOH   HOH A . 
G 6 HOH   190 490 129 HOH   HOH A . 
G 6 HOH   191 491 193 HOH   HOH A . 
G 6 HOH   192 492 127 HOH   HOH A . 
G 6 HOH   193 493 56  HOH   HOH A . 
G 6 HOH   194 494 75  HOH   HOH A . 
G 6 HOH   195 495 86  HOH   HOH A . 
G 6 HOH   196 496 74  HOH   HOH A . 
G 6 HOH   197 497 259 HOH   HOH A . 
G 6 HOH   198 498 125 HOH   HOH A . 
G 6 HOH   199 499 17  HOH   HOH A . 
G 6 HOH   200 500 57  HOH   HOH A . 
G 6 HOH   201 501 246 HOH   HOH A . 
G 6 HOH   202 502 180 HOH   HOH A . 
G 6 HOH   203 503 215 HOH   HOH A . 
G 6 HOH   204 504 5   HOH   HOH A . 
G 6 HOH   205 505 202 HOH   HOH A . 
G 6 HOH   206 506 102 HOH   HOH A . 
G 6 HOH   207 507 83  HOH   HOH A . 
G 6 HOH   208 508 165 HOH   HOH A . 
G 6 HOH   209 509 92  HOH   HOH A . 
G 6 HOH   210 510 217 HOH   HOH A . 
G 6 HOH   211 511 98  HOH   HOH A . 
G 6 HOH   212 512 199 HOH   HOH A . 
G 6 HOH   213 513 118 HOH   HOH A . 
G 6 HOH   214 514 187 HOH   HOH A . 
G 6 HOH   215 515 112 HOH   HOH A . 
G 6 HOH   216 516 235 HOH   HOH A . 
G 6 HOH   217 517 253 HOH   HOH A . 
G 6 HOH   218 518 73  HOH   HOH A . 
G 6 HOH   219 519 117 HOH   HOH A . 
G 6 HOH   220 520 225 HOH   HOH A . 
G 6 HOH   221 521 204 HOH   HOH A . 
G 6 HOH   222 522 179 HOH   HOH A . 
G 6 HOH   223 523 209 HOH   HOH A . 
G 6 HOH   224 524 222 HOH   HOH A . 
G 6 HOH   225 525 242 HOH   HOH A . 
G 6 HOH   226 526 247 HOH   HOH A . 
G 6 HOH   227 527 260 HOH   HOH A . 
G 6 HOH   228 528 120 HOH   HOH A . 
G 6 HOH   229 529 142 HOH   HOH A . 
G 6 HOH   230 530 206 HOH   HOH A . 
G 6 HOH   231 531 228 HOH   HOH A . 
G 6 HOH   232 532 244 HOH   HOH A . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0267 ? 1 
refinement       REFMAC5 .        ? 2 
'data scaling'   Aimless .        ? 3 
phasing          PHASER  .        ? 4 
'data reduction' XDS     .        ? 5 
# 
_cell.entry_id           7HZP 
_cell.length_a           88.680 
_cell.length_b           58.239 
_cell.length_c           32.887 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.81 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HZP 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
# 
_exptl.entry_id          7HZP 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.67 
_exptl_crystal.density_percent_sol   53.96 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-09-25 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92206 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92206 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HZP 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             44.34 
_reflns.d_resolution_high            1.57 
_reflns.number_obs                   23372 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            0.775 
_reflns.pdbx_netI_over_sigmaI        1.8 
_reflns.pdbx_redundancy              6.7 
_reflns.pdbx_Rrim_I_all              0.843 
_reflns.pdbx_Rpim_I_all              0.327 
_reflns.pdbx_CC_half                 0.936 
_reflns.pdbx_number_measured_all     155785 
_reflns.pdbx_chi_squared             0.98 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_CC_star                 ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.57 
_reflns_shell.d_res_low                   1.66 
_reflns_shell.number_measured_all         21329 
_reflns_shell.number_unique_obs           3404 
_reflns_shell.Rmerge_I_obs                9.99 
_reflns_shell.pdbx_chi_squared            0.73 
_reflns_shell.pdbx_redundancy             6.3 
_reflns_shell.percent_possible_obs        100.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.3 
_reflns_shell.pdbx_Rrim_I_all             12.080 
_reflns_shell.pdbx_Rpim_I_all             4.783 
_reflns_shell.pdbx_CC_half                0.388 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.pdbx_CC_star                ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7HZP 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     16584 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             44.37 
_refine.ls_d_res_high                            1.60 
_refine.ls_percent_reflns_obs                    79.38 
_refine.ls_R_factor_obs                          0.26443 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.26134 
_refine.ls_R_factor_R_free                       0.32116 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.2 
_refine.ls_number_reflns_R_free                  914 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.789 
_refine.correlation_coeff_Fo_to_Fc_free          0.739 
_refine.B_iso_mean                               12.506 
_refine.aniso_B[1][1]                            0.06 
_refine.aniso_B[2][2]                            0.40 
_refine.aniso_B[3][3]                            -0.46 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.05 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.233 
_refine.pdbx_overall_ESU_R_Free                  0.201 
_refine.overall_SU_ML                            0.197 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             5.842 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.pdbx_number_atoms_protein        1083 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         34 
_refine_hist.number_atoms_solvent             232 
_refine_hist.number_atoms_total               1349 
_refine_hist.d_res_high                       1.60 
_refine_hist.d_res_low                        44.37 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.005  0.014  ? 2333 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.014  ? 1575 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.421  1.632  ? 2498 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.188  1.599  ? 3624 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       6.884  5.000  ? 238  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       32.183 21.188 ? 101  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       15.132 15.000 ? 256  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       19.779 15.000 ? 15   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.050  0.200  ? 224  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.005  0.020  ? 2384 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.001  0.020  ? 466  'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  0.685  1.146  ? 1184 'X-RAY DIFFRACTION' ? 
r_mcbond_other               0.705  1.079  ? 1118 'X-RAY DIFFRACTION' ? 
r_mcangle_it                 1.433  1.559  ? 1150 'X-RAY DIFFRACTION' ? 
r_mcangle_other              1.433  1.558  ? 1151 'X-RAY DIFFRACTION' ? 
r_scbond_it                  0.673  1.318  ? 1149 'X-RAY DIFFRACTION' ? 
r_scbond_other               0.655  1.294  ? 1146 'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              1.086  1.774  ? 1343 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       7.221  13.273 ? 2010 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         7.219  13.283 ? 2011 'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.603 
_refine_ls_shell.d_res_low                        1.645 
_refine_ls_shell.number_reflns_R_work             610 
_refine_ls_shell.R_factor_R_work                  0.350 
_refine_ls_shell.percent_reflns_obs               40.10 
_refine_ls_shell.R_factor_R_free                  0.395 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             44 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.number_reflns_obs                ? 
# 
_struct.entry_id                  7HZP 
_struct.title                     
;Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre -- Crystal structure of Coxsackievirus A16 (G-10) 2A protease in complex with ASAP-0031281-001 (A71EV2A-x2846)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HZP 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
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 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
G N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7HZP 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_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,F,G 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_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 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2 AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3 AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4 AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5 AA5 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P6 AA6 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 B ZN . ZN ? ? A CYS 56  A ZN 201 1_555 ? ? ? ? ? ? ? 2.372 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 B ZN . ZN ? ? A CYS 58  A ZN 201 1_555 ? ? ? ? ? ? ? 2.358 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 B ZN . ZN ? ? A CYS 116 A ZN 201 1_555 ? ? ? ? ? ? ? 2.277 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 B ZN . ZN ? ? A HIS 118 A ZN 201 1_555 ? ? ? ? ? ? ? 2.121 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? B ZN . ? A ZN 201 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 107.6 ? 
2 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? B ZN . ? A ZN 201 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 106.5 ? 
3 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? B ZN . ? A ZN 201 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 117.6 ? 
4 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? B ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 108.5 ? 
5 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? B ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 96.9  ? 
6 SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? B ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 119.0 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
# 
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 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? 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 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
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 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N GLY A 43  ? N GLY A 49  O GLY A 7   ? O GLY A 13  
AA2 1 2 O VAL A 68  ? O VAL A 74  N GLY A 55  ? N GLY A 61  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7HZP 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 411 ? ? O A HOH 436 ? ? 1.45 
2 1 O A HOH 383 ? ? O A HOH 453 ? ? 1.75 
3 1 O A HOH 436 ? ? O A HOH 455 ? ? 2.09 
4 1 O A HOH 323 ? ? O A HOH 424 ? ? 2.18 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 505 ? ? 1_555 O A HOH 505 ? ? 2_556 1.11 
2 1 O A HOH 358 ? ? 1_555 O A HOH 358 ? ? 2_556 1.68 
3 1 O A HOH 386 ? ? 1_555 O A HOH 475 ? ? 4_556 2.09 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 14  ? ? -100.34 45.82  
2 1 SER A 125 ? ? -132.88 -37.97 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 526 ? 6.19 . 
2 1 O ? A HOH 527 ? 6.56 . 
3 1 O ? A HOH 528 ? 6.63 . 
4 1 O ? A HOH 529 ? 6.68 . 
5 1 O ? A HOH 530 ? 6.85 . 
6 1 O ? A HOH 531 ? 6.93 . 
7 1 O ? A HOH 532 ? 8.35 . 
# 
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 ALA 147 ? A ALA 141 
2 1 Y 1 A MET 148 ? A MET 142 
3 1 Y 1 A GLU 149 ? A GLU 143 
4 1 Y 1 A GLN 150 ? A GLN 144 
# 
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 
A1BQ2 N1   N  Y N 1   
A1BQ2 N3   N  Y N 2   
A1BQ2 C4   C  N N 3   
A1BQ2 C5   C  Y N 4   
A1BQ2 C6   C  Y N 5   
A1BQ2 C7   C  Y N 6   
A1BQ2 C8   C  Y N 7   
A1BQ2 C10  C  Y N 8   
A1BQ2 C13  C  Y N 9   
A1BQ2 N    N  Y N 10  
A1BQ2 C    C  N N 11  
A1BQ2 O    O  N N 12  
A1BQ2 C1   C  Y N 13  
A1BQ2 C11  C  Y N 14  
A1BQ2 C12  C  Y N 15  
A1BQ2 C2   C  N N 16  
A1BQ2 C3   C  N N 17  
A1BQ2 C9   C  Y N 18  
A1BQ2 N2   N  N N 19  
A1BQ2 O1   O  Y N 20  
A1BQ2 H6   H  N N 21  
A1BQ2 H7   H  N N 22  
A1BQ2 H8   H  N N 23  
A1BQ2 H9   H  N N 24  
A1BQ2 H11  H  N N 25  
A1BQ2 H1   H  N N 26  
A1BQ2 H    H  N N 27  
A1BQ2 H2   H  N N 28  
A1BQ2 H12  H  N N 29  
A1BQ2 H13  H  N N 30  
A1BQ2 H5   H  N N 31  
A1BQ2 H4   H  N N 32  
A1BQ2 H10  H  N N 33  
A1BQ2 H3   H  N N 34  
ALA   N    N  N N 35  
ALA   CA   C  N S 36  
ALA   C    C  N N 37  
ALA   O    O  N N 38  
ALA   CB   C  N N 39  
ALA   OXT  O  N N 40  
ALA   H    H  N N 41  
ALA   H2   H  N N 42  
ALA   HA   H  N N 43  
ALA   HB1  H  N N 44  
ALA   HB2  H  N N 45  
ALA   HB3  H  N N 46  
ALA   HXT  H  N N 47  
ARG   N    N  N N 48  
ARG   CA   C  N S 49  
ARG   C    C  N N 50  
ARG   O    O  N N 51  
ARG   CB   C  N N 52  
ARG   CG   C  N N 53  
ARG   CD   C  N N 54  
ARG   NE   N  N N 55  
ARG   CZ   C  N N 56  
ARG   NH1  N  N N 57  
ARG   NH2  N  N N 58  
ARG   OXT  O  N N 59  
ARG   H    H  N N 60  
ARG   H2   H  N N 61  
ARG   HA   H  N N 62  
ARG   HB2  H  N N 63  
ARG   HB3  H  N N 64  
ARG   HG2  H  N N 65  
ARG   HG3  H  N N 66  
ARG   HD2  H  N N 67  
ARG   HD3  H  N N 68  
ARG   HE   H  N N 69  
ARG   HH11 H  N N 70  
ARG   HH12 H  N N 71  
ARG   HH21 H  N N 72  
ARG   HH22 H  N N 73  
ARG   HXT  H  N N 74  
ASN   N    N  N N 75  
ASN   CA   C  N S 76  
ASN   C    C  N N 77  
ASN   O    O  N N 78  
ASN   CB   C  N N 79  
ASN   CG   C  N N 80  
ASN   OD1  O  N N 81  
ASN   ND2  N  N N 82  
ASN   OXT  O  N N 83  
ASN   H    H  N N 84  
ASN   H2   H  N N 85  
ASN   HA   H  N N 86  
ASN   HB2  H  N N 87  
ASN   HB3  H  N N 88  
ASN   HD21 H  N N 89  
ASN   HD22 H  N N 90  
ASN   HXT  H  N N 91  
ASP   N    N  N N 92  
ASP   CA   C  N S 93  
ASP   C    C  N N 94  
ASP   O    O  N N 95  
ASP   CB   C  N N 96  
ASP   CG   C  N N 97  
ASP   OD1  O  N N 98  
ASP   OD2  O  N N 99  
ASP   OXT  O  N N 100 
ASP   H    H  N N 101 
ASP   H2   H  N N 102 
ASP   HA   H  N N 103 
ASP   HB2  H  N N 104 
ASP   HB3  H  N N 105 
ASP   HD2  H  N N 106 
ASP   HXT  H  N N 107 
CYS   N    N  N N 108 
CYS   CA   C  N R 109 
CYS   C    C  N N 110 
CYS   O    O  N N 111 
CYS   CB   C  N N 112 
CYS   SG   S  N N 113 
CYS   OXT  O  N N 114 
CYS   H    H  N N 115 
CYS   H2   H  N N 116 
CYS   HA   H  N N 117 
CYS   HB2  H  N N 118 
CYS   HB3  H  N N 119 
CYS   HG   H  N N 120 
CYS   HXT  H  N N 121 
DMS   S    S  N N 122 
DMS   O    O  N N 123 
DMS   C1   C  N N 124 
DMS   C2   C  N N 125 
DMS   H11  H  N N 126 
DMS   H12  H  N N 127 
DMS   H13  H  N N 128 
DMS   H21  H  N N 129 
DMS   H22  H  N N 130 
DMS   H23  H  N N 131 
GLN   N    N  N N 132 
GLN   CA   C  N S 133 
GLN   C    C  N N 134 
GLN   O    O  N N 135 
GLN   CB   C  N N 136 
GLN   CG   C  N N 137 
GLN   CD   C  N N 138 
GLN   OE1  O  N N 139 
GLN   NE2  N  N N 140 
GLN   OXT  O  N N 141 
GLN   H    H  N N 142 
GLN   H2   H  N N 143 
GLN   HA   H  N N 144 
GLN   HB2  H  N N 145 
GLN   HB3  H  N N 146 
GLN   HG2  H  N N 147 
GLN   HG3  H  N N 148 
GLN   HE21 H  N N 149 
GLN   HE22 H  N N 150 
GLN   HXT  H  N N 151 
GLU   N    N  N N 152 
GLU   CA   C  N S 153 
GLU   C    C  N N 154 
GLU   O    O  N N 155 
GLU   CB   C  N N 156 
GLU   CG   C  N N 157 
GLU   CD   C  N N 158 
GLU   OE1  O  N N 159 
GLU   OE2  O  N N 160 
GLU   OXT  O  N N 161 
GLU   H    H  N N 162 
GLU   H2   H  N N 163 
GLU   HA   H  N N 164 
GLU   HB2  H  N N 165 
GLU   HB3  H  N N 166 
GLU   HG2  H  N N 167 
GLU   HG3  H  N N 168 
GLU   HE2  H  N N 169 
GLU   HXT  H  N N 170 
GLY   N    N  N N 171 
GLY   CA   C  N N 172 
GLY   C    C  N N 173 
GLY   O    O  N N 174 
GLY   OXT  O  N N 175 
GLY   H    H  N N 176 
GLY   H2   H  N N 177 
GLY   HA2  H  N N 178 
GLY   HA3  H  N N 179 
GLY   HXT  H  N N 180 
HIS   N    N  N N 181 
HIS   CA   C  N S 182 
HIS   C    C  N N 183 
HIS   O    O  N N 184 
HIS   CB   C  N N 185 
HIS   CG   C  Y N 186 
HIS   ND1  N  Y N 187 
HIS   CD2  C  Y N 188 
HIS   CE1  C  Y N 189 
HIS   NE2  N  Y N 190 
HIS   OXT  O  N N 191 
HIS   H    H  N N 192 
HIS   H2   H  N N 193 
HIS   HA   H  N N 194 
HIS   HB2  H  N N 195 
HIS   HB3  H  N N 196 
HIS   HD1  H  N N 197 
HIS   HD2  H  N N 198 
HIS   HE1  H  N N 199 
HIS   HE2  H  N N 200 
HIS   HXT  H  N N 201 
HOH   O    O  N N 202 
HOH   H1   H  N N 203 
HOH   H2   H  N N 204 
ILE   N    N  N N 205 
ILE   CA   C  N S 206 
ILE   C    C  N N 207 
ILE   O    O  N N 208 
ILE   CB   C  N S 209 
ILE   CG1  C  N N 210 
ILE   CG2  C  N N 211 
ILE   CD1  C  N N 212 
ILE   OXT  O  N N 213 
ILE   H    H  N N 214 
ILE   H2   H  N N 215 
ILE   HA   H  N N 216 
ILE   HB   H  N N 217 
ILE   HG12 H  N N 218 
ILE   HG13 H  N N 219 
ILE   HG21 H  N N 220 
ILE   HG22 H  N N 221 
ILE   HG23 H  N N 222 
ILE   HD11 H  N N 223 
ILE   HD12 H  N N 224 
ILE   HD13 H  N N 225 
ILE   HXT  H  N N 226 
LEU   N    N  N N 227 
LEU   CA   C  N S 228 
LEU   C    C  N N 229 
LEU   O    O  N N 230 
LEU   CB   C  N N 231 
LEU   CG   C  N N 232 
LEU   CD1  C  N N 233 
LEU   CD2  C  N N 234 
LEU   OXT  O  N N 235 
LEU   H    H  N N 236 
LEU   H2   H  N N 237 
LEU   HA   H  N N 238 
LEU   HB2  H  N N 239 
LEU   HB3  H  N N 240 
LEU   HG   H  N N 241 
LEU   HD11 H  N N 242 
LEU   HD12 H  N N 243 
LEU   HD13 H  N N 244 
LEU   HD21 H  N N 245 
LEU   HD22 H  N N 246 
LEU   HD23 H  N N 247 
LEU   HXT  H  N N 248 
LYS   N    N  N N 249 
LYS   CA   C  N S 250 
LYS   C    C  N N 251 
LYS   O    O  N N 252 
LYS   CB   C  N N 253 
LYS   CG   C  N N 254 
LYS   CD   C  N N 255 
LYS   CE   C  N N 256 
LYS   NZ   N  N N 257 
LYS   OXT  O  N N 258 
LYS   H    H  N N 259 
LYS   H2   H  N N 260 
LYS   HA   H  N N 261 
LYS   HB2  H  N N 262 
LYS   HB3  H  N N 263 
LYS   HG2  H  N N 264 
LYS   HG3  H  N N 265 
LYS   HD2  H  N N 266 
LYS   HD3  H  N N 267 
LYS   HE2  H  N N 268 
LYS   HE3  H  N N 269 
LYS   HZ1  H  N N 270 
LYS   HZ2  H  N N 271 
LYS   HZ3  H  N N 272 
LYS   HXT  H  N N 273 
MET   N    N  N N 274 
MET   CA   C  N S 275 
MET   C    C  N N 276 
MET   O    O  N N 277 
MET   CB   C  N N 278 
MET   CG   C  N N 279 
MET   SD   S  N N 280 
MET   CE   C  N N 281 
MET   OXT  O  N N 282 
MET   H    H  N N 283 
MET   H2   H  N N 284 
MET   HA   H  N N 285 
MET   HB2  H  N N 286 
MET   HB3  H  N N 287 
MET   HG2  H  N N 288 
MET   HG3  H  N N 289 
MET   HE1  H  N N 290 
MET   HE2  H  N N 291 
MET   HE3  H  N N 292 
MET   HXT  H  N N 293 
PHE   N    N  N N 294 
PHE   CA   C  N S 295 
PHE   C    C  N N 296 
PHE   O    O  N N 297 
PHE   CB   C  N N 298 
PHE   CG   C  Y N 299 
PHE   CD1  C  Y N 300 
PHE   CD2  C  Y N 301 
PHE   CE1  C  Y N 302 
PHE   CE2  C  Y N 303 
PHE   CZ   C  Y N 304 
PHE   OXT  O  N N 305 
PHE   H    H  N N 306 
PHE   H2   H  N N 307 
PHE   HA   H  N N 308 
PHE   HB2  H  N N 309 
PHE   HB3  H  N N 310 
PHE   HD1  H  N N 311 
PHE   HD2  H  N N 312 
PHE   HE1  H  N N 313 
PHE   HE2  H  N N 314 
PHE   HZ   H  N N 315 
PHE   HXT  H  N N 316 
PRO   N    N  N N 317 
PRO   CA   C  N S 318 
PRO   C    C  N N 319 
PRO   O    O  N N 320 
PRO   CB   C  N N 321 
PRO   CG   C  N N 322 
PRO   CD   C  N N 323 
PRO   OXT  O  N N 324 
PRO   H    H  N N 325 
PRO   HA   H  N N 326 
PRO   HB2  H  N N 327 
PRO   HB3  H  N N 328 
PRO   HG2  H  N N 329 
PRO   HG3  H  N N 330 
PRO   HD2  H  N N 331 
PRO   HD3  H  N N 332 
PRO   HXT  H  N N 333 
SER   N    N  N N 334 
SER   CA   C  N S 335 
SER   C    C  N N 336 
SER   O    O  N N 337 
SER   CB   C  N N 338 
SER   OG   O  N N 339 
SER   OXT  O  N N 340 
SER   H    H  N N 341 
SER   H2   H  N N 342 
SER   HA   H  N N 343 
SER   HB2  H  N N 344 
SER   HB3  H  N N 345 
SER   HG   H  N N 346 
SER   HXT  H  N N 347 
SO4   S    S  N N 348 
SO4   O1   O  N N 349 
SO4   O2   O  N N 350 
SO4   O3   O  N N 351 
SO4   O4   O  N N 352 
THR   N    N  N N 353 
THR   CA   C  N S 354 
THR   C    C  N N 355 
THR   O    O  N N 356 
THR   CB   C  N R 357 
THR   OG1  O  N N 358 
THR   CG2  C  N N 359 
THR   OXT  O  N N 360 
THR   H    H  N N 361 
THR   H2   H  N N 362 
THR   HA   H  N N 363 
THR   HB   H  N N 364 
THR   HG1  H  N N 365 
THR   HG21 H  N N 366 
THR   HG22 H  N N 367 
THR   HG23 H  N N 368 
THR   HXT  H  N N 369 
TRP   N    N  N N 370 
TRP   CA   C  N S 371 
TRP   C    C  N N 372 
TRP   O    O  N N 373 
TRP   CB   C  N N 374 
TRP   CG   C  Y N 375 
TRP   CD1  C  Y N 376 
TRP   CD2  C  Y N 377 
TRP   NE1  N  Y N 378 
TRP   CE2  C  Y N 379 
TRP   CE3  C  Y N 380 
TRP   CZ2  C  Y N 381 
TRP   CZ3  C  Y N 382 
TRP   CH2  C  Y N 383 
TRP   OXT  O  N N 384 
TRP   H    H  N N 385 
TRP   H2   H  N N 386 
TRP   HA   H  N N 387 
TRP   HB2  H  N N 388 
TRP   HB3  H  N N 389 
TRP   HD1  H  N N 390 
TRP   HE1  H  N N 391 
TRP   HE3  H  N N 392 
TRP   HZ2  H  N N 393 
TRP   HZ3  H  N N 394 
TRP   HH2  H  N N 395 
TRP   HXT  H  N N 396 
TYR   N    N  N N 397 
TYR   CA   C  N S 398 
TYR   C    C  N N 399 
TYR   O    O  N N 400 
TYR   CB   C  N N 401 
TYR   CG   C  Y N 402 
TYR   CD1  C  Y N 403 
TYR   CD2  C  Y N 404 
TYR   CE1  C  Y N 405 
TYR   CE2  C  Y N 406 
TYR   CZ   C  Y N 407 
TYR   OH   O  N N 408 
TYR   OXT  O  N N 409 
TYR   H    H  N N 410 
TYR   H2   H  N N 411 
TYR   HA   H  N N 412 
TYR   HB2  H  N N 413 
TYR   HB3  H  N N 414 
TYR   HD1  H  N N 415 
TYR   HD2  H  N N 416 
TYR   HE1  H  N N 417 
TYR   HE2  H  N N 418 
TYR   HH   H  N N 419 
TYR   HXT  H  N N 420 
VAL   N    N  N N 421 
VAL   CA   C  N S 422 
VAL   C    C  N N 423 
VAL   O    O  N N 424 
VAL   CB   C  N N 425 
VAL   CG1  C  N N 426 
VAL   CG2  C  N N 427 
VAL   OXT  O  N N 428 
VAL   H    H  N N 429 
VAL   H2   H  N N 430 
VAL   HA   H  N N 431 
VAL   HB   H  N N 432 
VAL   HG11 H  N N 433 
VAL   HG12 H  N N 434 
VAL   HG13 H  N N 435 
VAL   HG21 H  N N 436 
VAL   HG22 H  N N 437 
VAL   HG23 H  N N 438 
VAL   HXT  H  N N 439 
ZN    ZN   ZN N N 440 
# 
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 
A1BQ2 C   N    sing N N 1   
A1BQ2 N   N1   sing Y N 2   
A1BQ2 N1  C1   doub Y N 3   
A1BQ2 C1  C2   sing N N 4   
A1BQ2 C2  O    doub N N 5   
A1BQ2 N2  C2   sing N N 6   
A1BQ2 C3  N2   sing N N 7   
A1BQ2 C4  C3   sing N N 8   
A1BQ2 C5  C4   sing N N 9   
A1BQ2 C5  C6   doub Y N 10  
A1BQ2 C6  O1   sing Y N 11  
A1BQ2 O1  C7   sing Y N 12  
A1BQ2 C7  N3   doub Y N 13  
A1BQ2 N3  C5   sing Y N 14  
A1BQ2 C8  C1   sing Y N 15  
A1BQ2 C8  C9   doub Y N 16  
A1BQ2 C9  C10  sing Y N 17  
A1BQ2 C10 C11  doub Y N 18  
A1BQ2 C11 C12  sing Y N 19  
A1BQ2 C12 C13  doub Y N 20  
A1BQ2 C13 C8   sing Y N 21  
A1BQ2 N   C13  sing Y N 22  
A1BQ2 C4  H6   sing N N 23  
A1BQ2 C4  H7   sing N N 24  
A1BQ2 C6  H8   sing N N 25  
A1BQ2 C7  H9   sing N N 26  
A1BQ2 C10 H11  sing N N 27  
A1BQ2 C   H1   sing N N 28  
A1BQ2 C   H    sing N N 29  
A1BQ2 C   H2   sing N N 30  
A1BQ2 C11 H12  sing N N 31  
A1BQ2 C12 H13  sing N N 32  
A1BQ2 C3  H5   sing N N 33  
A1BQ2 C3  H4   sing N N 34  
A1BQ2 C9  H10  sing N N 35  
A1BQ2 N2  H3   sing N N 36  
ALA   N   CA   sing N N 37  
ALA   N   H    sing N N 38  
ALA   N   H2   sing N N 39  
ALA   CA  C    sing N N 40  
ALA   CA  CB   sing N N 41  
ALA   CA  HA   sing N N 42  
ALA   C   O    doub N N 43  
ALA   C   OXT  sing N N 44  
ALA   CB  HB1  sing N N 45  
ALA   CB  HB2  sing N N 46  
ALA   CB  HB3  sing N N 47  
ALA   OXT HXT  sing N N 48  
ARG   N   CA   sing N N 49  
ARG   N   H    sing N N 50  
ARG   N   H2   sing N N 51  
ARG   CA  C    sing N N 52  
ARG   CA  CB   sing N N 53  
ARG   CA  HA   sing N N 54  
ARG   C   O    doub N N 55  
ARG   C   OXT  sing N N 56  
ARG   CB  CG   sing N N 57  
ARG   CB  HB2  sing N N 58  
ARG   CB  HB3  sing N N 59  
ARG   CG  CD   sing N N 60  
ARG   CG  HG2  sing N N 61  
ARG   CG  HG3  sing N N 62  
ARG   CD  NE   sing N N 63  
ARG   CD  HD2  sing N N 64  
ARG   CD  HD3  sing N N 65  
ARG   NE  CZ   sing N N 66  
ARG   NE  HE   sing N N 67  
ARG   CZ  NH1  sing N N 68  
ARG   CZ  NH2  doub N N 69  
ARG   NH1 HH11 sing N N 70  
ARG   NH1 HH12 sing N N 71  
ARG   NH2 HH21 sing N N 72  
ARG   NH2 HH22 sing N N 73  
ARG   OXT HXT  sing N N 74  
ASN   N   CA   sing N N 75  
ASN   N   H    sing N N 76  
ASN   N   H2   sing N N 77  
ASN   CA  C    sing N N 78  
ASN   CA  CB   sing N N 79  
ASN   CA  HA   sing N N 80  
ASN   C   O    doub N N 81  
ASN   C   OXT  sing N N 82  
ASN   CB  CG   sing N N 83  
ASN   CB  HB2  sing N N 84  
ASN   CB  HB3  sing N N 85  
ASN   CG  OD1  doub N N 86  
ASN   CG  ND2  sing N N 87  
ASN   ND2 HD21 sing N N 88  
ASN   ND2 HD22 sing N N 89  
ASN   OXT HXT  sing N N 90  
ASP   N   CA   sing N N 91  
ASP   N   H    sing N N 92  
ASP   N   H2   sing N N 93  
ASP   CA  C    sing N N 94  
ASP   CA  CB   sing N N 95  
ASP   CA  HA   sing N N 96  
ASP   C   O    doub N N 97  
ASP   C   OXT  sing N N 98  
ASP   CB  CG   sing N N 99  
ASP   CB  HB2  sing N N 100 
ASP   CB  HB3  sing N N 101 
ASP   CG  OD1  doub N N 102 
ASP   CG  OD2  sing N N 103 
ASP   OD2 HD2  sing N N 104 
ASP   OXT HXT  sing N N 105 
CYS   N   CA   sing N N 106 
CYS   N   H    sing N N 107 
CYS   N   H2   sing N N 108 
CYS   CA  C    sing N N 109 
CYS   CA  CB   sing N N 110 
CYS   CA  HA   sing N N 111 
CYS   C   O    doub N N 112 
CYS   C   OXT  sing N N 113 
CYS   CB  SG   sing N N 114 
CYS   CB  HB2  sing N N 115 
CYS   CB  HB3  sing N N 116 
CYS   SG  HG   sing N N 117 
CYS   OXT HXT  sing N N 118 
DMS   S   O    doub N N 119 
DMS   S   C1   sing N N 120 
DMS   S   C2   sing N N 121 
DMS   C1  H11  sing N N 122 
DMS   C1  H12  sing N N 123 
DMS   C1  H13  sing N N 124 
DMS   C2  H21  sing N N 125 
DMS   C2  H22  sing N N 126 
DMS   C2  H23  sing N N 127 
GLN   N   CA   sing N N 128 
GLN   N   H    sing N N 129 
GLN   N   H2   sing N N 130 
GLN   CA  C    sing N N 131 
GLN   CA  CB   sing N N 132 
GLN   CA  HA   sing N N 133 
GLN   C   O    doub N N 134 
GLN   C   OXT  sing N N 135 
GLN   CB  CG   sing N N 136 
GLN   CB  HB2  sing N N 137 
GLN   CB  HB3  sing N N 138 
GLN   CG  CD   sing N N 139 
GLN   CG  HG2  sing N N 140 
GLN   CG  HG3  sing N N 141 
GLN   CD  OE1  doub N N 142 
GLN   CD  NE2  sing N N 143 
GLN   NE2 HE21 sing N N 144 
GLN   NE2 HE22 sing N N 145 
GLN   OXT HXT  sing N N 146 
GLU   N   CA   sing N N 147 
GLU   N   H    sing N N 148 
GLU   N   H2   sing N N 149 
GLU   CA  C    sing N N 150 
GLU   CA  CB   sing N N 151 
GLU   CA  HA   sing N N 152 
GLU   C   O    doub N N 153 
GLU   C   OXT  sing N N 154 
GLU   CB  CG   sing N N 155 
GLU   CB  HB2  sing N N 156 
GLU   CB  HB3  sing N N 157 
GLU   CG  CD   sing N N 158 
GLU   CG  HG2  sing N N 159 
GLU   CG  HG3  sing N N 160 
GLU   CD  OE1  doub N N 161 
GLU   CD  OE2  sing N N 162 
GLU   OE2 HE2  sing N N 163 
GLU   OXT HXT  sing N N 164 
GLY   N   CA   sing N N 165 
GLY   N   H    sing N N 166 
GLY   N   H2   sing N N 167 
GLY   CA  C    sing N N 168 
GLY   CA  HA2  sing N N 169 
GLY   CA  HA3  sing N N 170 
GLY   C   O    doub N N 171 
GLY   C   OXT  sing N N 172 
GLY   OXT HXT  sing N N 173 
HIS   N   CA   sing N N 174 
HIS   N   H    sing N N 175 
HIS   N   H2   sing N N 176 
HIS   CA  C    sing N N 177 
HIS   CA  CB   sing N N 178 
HIS   CA  HA   sing N N 179 
HIS   C   O    doub N N 180 
HIS   C   OXT  sing N N 181 
HIS   CB  CG   sing N N 182 
HIS   CB  HB2  sing N N 183 
HIS   CB  HB3  sing N N 184 
HIS   CG  ND1  sing Y N 185 
HIS   CG  CD2  doub Y N 186 
HIS   ND1 CE1  doub Y N 187 
HIS   ND1 HD1  sing N N 188 
HIS   CD2 NE2  sing Y N 189 
HIS   CD2 HD2  sing N N 190 
HIS   CE1 NE2  sing Y N 191 
HIS   CE1 HE1  sing N N 192 
HIS   NE2 HE2  sing N N 193 
HIS   OXT HXT  sing N N 194 
HOH   O   H1   sing N N 195 
HOH   O   H2   sing N N 196 
ILE   N   CA   sing N N 197 
ILE   N   H    sing N N 198 
ILE   N   H2   sing N N 199 
ILE   CA  C    sing N N 200 
ILE   CA  CB   sing N N 201 
ILE   CA  HA   sing N N 202 
ILE   C   O    doub N N 203 
ILE   C   OXT  sing N N 204 
ILE   CB  CG1  sing N N 205 
ILE   CB  CG2  sing N N 206 
ILE   CB  HB   sing N N 207 
ILE   CG1 CD1  sing N N 208 
ILE   CG1 HG12 sing N N 209 
ILE   CG1 HG13 sing N N 210 
ILE   CG2 HG21 sing N N 211 
ILE   CG2 HG22 sing N N 212 
ILE   CG2 HG23 sing N N 213 
ILE   CD1 HD11 sing N N 214 
ILE   CD1 HD12 sing N N 215 
ILE   CD1 HD13 sing N N 216 
ILE   OXT HXT  sing N N 217 
LEU   N   CA   sing N N 218 
LEU   N   H    sing N N 219 
LEU   N   H2   sing N N 220 
LEU   CA  C    sing N N 221 
LEU   CA  CB   sing N N 222 
LEU   CA  HA   sing N N 223 
LEU   C   O    doub N N 224 
LEU   C   OXT  sing N N 225 
LEU   CB  CG   sing N N 226 
LEU   CB  HB2  sing N N 227 
LEU   CB  HB3  sing N N 228 
LEU   CG  CD1  sing N N 229 
LEU   CG  CD2  sing N N 230 
LEU   CG  HG   sing N N 231 
LEU   CD1 HD11 sing N N 232 
LEU   CD1 HD12 sing N N 233 
LEU   CD1 HD13 sing N N 234 
LEU   CD2 HD21 sing N N 235 
LEU   CD2 HD22 sing N N 236 
LEU   CD2 HD23 sing N N 237 
LEU   OXT HXT  sing N N 238 
LYS   N   CA   sing N N 239 
LYS   N   H    sing N N 240 
LYS   N   H2   sing N N 241 
LYS   CA  C    sing N N 242 
LYS   CA  CB   sing N N 243 
LYS   CA  HA   sing N N 244 
LYS   C   O    doub N N 245 
LYS   C   OXT  sing N N 246 
LYS   CB  CG   sing N N 247 
LYS   CB  HB2  sing N N 248 
LYS   CB  HB3  sing N N 249 
LYS   CG  CD   sing N N 250 
LYS   CG  HG2  sing N N 251 
LYS   CG  HG3  sing N N 252 
LYS   CD  CE   sing N N 253 
LYS   CD  HD2  sing N N 254 
LYS   CD  HD3  sing N N 255 
LYS   CE  NZ   sing N N 256 
LYS   CE  HE2  sing N N 257 
LYS   CE  HE3  sing N N 258 
LYS   NZ  HZ1  sing N N 259 
LYS   NZ  HZ2  sing N N 260 
LYS   NZ  HZ3  sing N N 261 
LYS   OXT HXT  sing N N 262 
MET   N   CA   sing N N 263 
MET   N   H    sing N N 264 
MET   N   H2   sing N N 265 
MET   CA  C    sing N N 266 
MET   CA  CB   sing N N 267 
MET   CA  HA   sing N N 268 
MET   C   O    doub N N 269 
MET   C   OXT  sing N N 270 
MET   CB  CG   sing N N 271 
MET   CB  HB2  sing N N 272 
MET   CB  HB3  sing N N 273 
MET   CG  SD   sing N N 274 
MET   CG  HG2  sing N N 275 
MET   CG  HG3  sing N N 276 
MET   SD  CE   sing N N 277 
MET   CE  HE1  sing N N 278 
MET   CE  HE2  sing N N 279 
MET   CE  HE3  sing N N 280 
MET   OXT HXT  sing N N 281 
PHE   N   CA   sing N N 282 
PHE   N   H    sing N N 283 
PHE   N   H2   sing N N 284 
PHE   CA  C    sing N N 285 
PHE   CA  CB   sing N N 286 
PHE   CA  HA   sing N N 287 
PHE   C   O    doub N N 288 
PHE   C   OXT  sing N N 289 
PHE   CB  CG   sing N N 290 
PHE   CB  HB2  sing N N 291 
PHE   CB  HB3  sing N N 292 
PHE   CG  CD1  doub Y N 293 
PHE   CG  CD2  sing Y N 294 
PHE   CD1 CE1  sing Y N 295 
PHE   CD1 HD1  sing N N 296 
PHE   CD2 CE2  doub Y N 297 
PHE   CD2 HD2  sing N N 298 
PHE   CE1 CZ   doub Y N 299 
PHE   CE1 HE1  sing N N 300 
PHE   CE2 CZ   sing Y N 301 
PHE   CE2 HE2  sing N N 302 
PHE   CZ  HZ   sing N N 303 
PHE   OXT HXT  sing N N 304 
PRO   N   CA   sing N N 305 
PRO   N   CD   sing N N 306 
PRO   N   H    sing N N 307 
PRO   CA  C    sing N N 308 
PRO   CA  CB   sing N N 309 
PRO   CA  HA   sing N N 310 
PRO   C   O    doub N N 311 
PRO   C   OXT  sing N N 312 
PRO   CB  CG   sing N N 313 
PRO   CB  HB2  sing N N 314 
PRO   CB  HB3  sing N N 315 
PRO   CG  CD   sing N N 316 
PRO   CG  HG2  sing N N 317 
PRO   CG  HG3  sing N N 318 
PRO   CD  HD2  sing N N 319 
PRO   CD  HD3  sing N N 320 
PRO   OXT HXT  sing N N 321 
SER   N   CA   sing N N 322 
SER   N   H    sing N N 323 
SER   N   H2   sing N N 324 
SER   CA  C    sing N N 325 
SER   CA  CB   sing N N 326 
SER   CA  HA   sing N N 327 
SER   C   O    doub N N 328 
SER   C   OXT  sing N N 329 
SER   CB  OG   sing N N 330 
SER   CB  HB2  sing N N 331 
SER   CB  HB3  sing N N 332 
SER   OG  HG   sing N N 333 
SER   OXT HXT  sing N N 334 
SO4   S   O1   doub N N 335 
SO4   S   O2   doub N N 336 
SO4   S   O3   sing N N 337 
SO4   S   O4   sing N N 338 
THR   N   CA   sing N N 339 
THR   N   H    sing N N 340 
THR   N   H2   sing N N 341 
THR   CA  C    sing N N 342 
THR   CA  CB   sing N N 343 
THR   CA  HA   sing N N 344 
THR   C   O    doub N N 345 
THR   C   OXT  sing N N 346 
THR   CB  OG1  sing N N 347 
THR   CB  CG2  sing N N 348 
THR   CB  HB   sing N N 349 
THR   OG1 HG1  sing N N 350 
THR   CG2 HG21 sing N N 351 
THR   CG2 HG22 sing N N 352 
THR   CG2 HG23 sing N N 353 
THR   OXT HXT  sing N N 354 
TRP   N   CA   sing N N 355 
TRP   N   H    sing N N 356 
TRP   N   H2   sing N N 357 
TRP   CA  C    sing N N 358 
TRP   CA  CB   sing N N 359 
TRP   CA  HA   sing N N 360 
TRP   C   O    doub N N 361 
TRP   C   OXT  sing N N 362 
TRP   CB  CG   sing N N 363 
TRP   CB  HB2  sing N N 364 
TRP   CB  HB3  sing N N 365 
TRP   CG  CD1  doub Y N 366 
TRP   CG  CD2  sing Y N 367 
TRP   CD1 NE1  sing Y N 368 
TRP   CD1 HD1  sing N N 369 
TRP   CD2 CE2  doub Y N 370 
TRP   CD2 CE3  sing Y N 371 
TRP   NE1 CE2  sing Y N 372 
TRP   NE1 HE1  sing N N 373 
TRP   CE2 CZ2  sing Y N 374 
TRP   CE3 CZ3  doub Y N 375 
TRP   CE3 HE3  sing N N 376 
TRP   CZ2 CH2  doub Y N 377 
TRP   CZ2 HZ2  sing N N 378 
TRP   CZ3 CH2  sing Y N 379 
TRP   CZ3 HZ3  sing N N 380 
TRP   CH2 HH2  sing N N 381 
TRP   OXT HXT  sing N N 382 
TYR   N   CA   sing N N 383 
TYR   N   H    sing N N 384 
TYR   N   H2   sing N N 385 
TYR   CA  C    sing N N 386 
TYR   CA  CB   sing N N 387 
TYR   CA  HA   sing N N 388 
TYR   C   O    doub N N 389 
TYR   C   OXT  sing N N 390 
TYR   CB  CG   sing N N 391 
TYR   CB  HB2  sing N N 392 
TYR   CB  HB3  sing N N 393 
TYR   CG  CD1  doub Y N 394 
TYR   CG  CD2  sing Y N 395 
TYR   CD1 CE1  sing Y N 396 
TYR   CD1 HD1  sing N N 397 
TYR   CD2 CE2  doub Y N 398 
TYR   CD2 HD2  sing N N 399 
TYR   CE1 CZ   doub Y N 400 
TYR   CE1 HE1  sing N N 401 
TYR   CE2 CZ   sing Y N 402 
TYR   CE2 HE2  sing N N 403 
TYR   CZ  OH   sing N N 404 
TYR   OH  HH   sing N N 405 
TYR   OXT HXT  sing N N 406 
VAL   N   CA   sing N N 407 
VAL   N   H    sing N N 408 
VAL   N   H2   sing N N 409 
VAL   CA  C    sing N N 410 
VAL   CA  CB   sing N N 411 
VAL   CA  HA   sing N N 412 
VAL   C   O    doub N N 413 
VAL   C   OXT  sing N N 414 
VAL   CB  CG1  sing N N 415 
VAL   CB  CG2  sing N N 416 
VAL   CB  HB   sing N N 417 
VAL   CG1 HG11 sing N N 418 
VAL   CG1 HG12 sing N N 419 
VAL   CG1 HG13 sing N N 420 
VAL   CG2 HG21 sing N N 421 
VAL   CG2 HG22 sing N N 422 
VAL   CG2 HG23 sing N N 423 
VAL   OXT HXT  sing N N 424 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002330 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.type             'experimental model' 
# 
_atom_sites.entry_id                    7HZP 
_atom_sites.fract_transf_matrix[1][1]   0.011276 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000159 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017171 
_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]   0.030410 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 20.103 6.881   23.553 1.00 12.99 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 21.280 6.942   22.648 1.00 12.32 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 21.187 5.817   21.628 1.00 12.09 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 20.464 4.821   21.932 1.00 12.32 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 22.568 6.866   23.420 1.00 12.90 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 22.709 5.624   24.086 1.00 13.41 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.887 5.968   20.491 1.00 11.23 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 22.056 4.916   19.459 1.00 9.99  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 22.333 5.499   18.081 1.00 9.53  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.992 6.672   17.836 1.00 9.41  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.992 4.729   17.224 1.00 8.69  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 23.437 5.155   15.881 1.00 8.66  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 23.276 3.986   14.910 1.00 8.29  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 23.319 2.804   15.357 1.00 7.70  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.877 5.625   15.939 1.00 8.44  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 23.103 4.314   13.637 1.00 8.39  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 23.204 3.356   12.505 1.00 8.44  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.593 3.535   11.866 1.00 8.80  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.985 4.696   11.569 1.00 8.62  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 22.043 3.574   11.508 1.00 8.48  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.679 3.600   12.206 1.00 8.49  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 22.088 2.525   10.413 1.00 8.37  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.550 4.293   11.419 1.00 9.02  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 25.316 2.433   11.629 1.00 9.26  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.634 2.419   10.930 1.00 10.02 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.521 1.611   9.624  1.00 10.49 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.469 0.367   9.666  1.00 11.15 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.735 1.908   11.872 1.00 9.90  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.888 2.698   13.150 1.00 10.08 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.719 3.802   13.204 1.00 9.75  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 27.183 2.371   14.297 1.00 10.30 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.843 4.569   14.352 1.00 10.26 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 27.320 3.105   15.472 1.00 10.68 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 28.145 4.221   15.502 1.00 11.08 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 28.259 4.981   16.645 1.00 10.82 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.544 2.309   8.482  1.00 10.89 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.432 1.734   7.109  1.00 11.16 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.495 2.405   6.229  1.00 11.38 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.579 3.664   6.239  1.00 10.61 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 25.018 1.919   6.527  1.00 11.07 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.524 3.358   6.664  1.00 10.95 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.937 1.448   5.076  1.00 11.41 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.265 1.599   5.492  1.00 11.66 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.521 2.026   4.837  1.00 12.55 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.381 2.852   5.782  1.00 12.49 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.529 2.454   6.961  1.00 12.18 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.865 4.004   5.305  1.00 13.49 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.597 4.989   6.143  1.00 13.03 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.650 6.132   6.541  1.00 11.44 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 31.075 7.294   6.462  1.00 9.80  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.875 5.478   5.456  1.00 14.50 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.980 4.432   5.443  1.00 16.33 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.720 4.260   6.412  1.00 17.94 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 34.108 3.723   4.339  1.00 18.12 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.427 5.805   6.984  1.00 10.53 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.416 6.778   7.482  1.00 10.08 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.921 6.379   8.876  1.00 9.37  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.707 5.190   9.090  1.00 10.25 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.196 6.869   6.560  1.00 9.60  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.465 7.447   5.196  1.00 9.60  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.084 8.683   5.049  1.00 9.74  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.069 6.775   4.045  1.00 9.66  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.327 9.220   3.797  1.00 9.75  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.312 7.294   2.783  1.00 9.82  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.936 8.526   2.663  1.00 9.82  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.172 9.070   1.441  1.00 10.70 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.732 7.371   9.751  1.00 8.65  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 27.092 7.260   11.094 1.00 7.79  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.806 8.113   11.064 1.00 7.24  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.919 9.325   10.813 1.00 7.13  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 28.108 7.673   12.168 1.00 7.82  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 27.560 7.962   13.561 1.00 8.10  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 28.635 8.331   14.582 1.00 7.93  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 28.160 9.297   15.585 1.00 8.19  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 27.635 9.016   16.786 1.00 7.93  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 27.496 7.759   17.175 1.00 7.73  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 27.231 10.003  17.593 1.00 7.74  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.635 7.506   11.306 1.00 6.60  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 23.305 8.193   11.384 1.00 6.31  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.885 8.299   12.854 1.00 6.14  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.703 7.247   13.506 1.00 6.05  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 22.239 7.445   10.562 1.00 6.21  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.960 8.258   10.430 1.00 6.21  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.783 7.038   9.191  1.00 6.19  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.720 9.528   13.359 1.00 5.91  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 22.305 9.797   14.768 1.00 5.86  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 21.085 10.715  14.762 1.00 5.54  ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.874 11.432  13.762 1.00 5.19  ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 23.431 10.444  15.592 1.00 6.15  ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 24.419 9.407   16.096 1.00 6.46  ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 24.153 11.539  14.821 1.00 6.11  ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 20.401 10.772  15.900 1.00 5.20  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 19.461 11.889  16.196 1.00 5.23  ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 20.254 13.190  16.089 1.00 5.21  ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 21.377 13.262  16.666 1.00 4.93  ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 18.801 11.761  17.567 1.00 5.15  ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.933 10.532  17.658 1.00 5.24  ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 18.396 9.443   18.015 1.00 5.13  ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 16.657 10.713  17.338 1.00 5.42  ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 19.693 14.193  15.419 1.00 5.33  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 20.382 15.491  15.238 1.00 5.39  ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 20.657 16.073  16.628 1.00 5.61  ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 21.748 16.648  16.834 1.00 5.73  ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 19.577 16.431  14.353 1.00 5.52  ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 20.291 17.746  14.079 1.00 5.68  ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 19.373 18.620  13.264 1.00 6.06  ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.948 19.879  12.831 1.00 6.22  ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.825 21.027  13.473 1.00 6.45  ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 19.211 21.085  14.641 1.00 6.84  ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 20.319 22.133  12.935 1.00 6.99  ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 19.706 15.904  17.553 1.00 5.80  ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 19.758 16.501  18.910 1.00 6.08  ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 20.794 15.770  19.774 1.00 6.75  ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 21.099 16.284  20.859 1.00 7.33  ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 18.345 16.624  19.519 1.00 5.89  ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 17.774 15.371  20.077 1.00 5.68  ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 17.100 14.458  19.273 1.00 5.47  ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 17.752 14.883  21.333 1.00 5.55  ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 16.722 13.440  20.005 1.00 5.43  ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 17.076 13.685  21.288 1.00 5.48  ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 21.323 14.619  19.344 1.00 7.31  ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 22.319 13.855  20.147 1.00 8.04  ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 23.679 13.808  19.442 1.00 8.80  ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 24.614 13.134  19.995 1.00 8.49  ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 21.736 12.456  20.405 1.00 8.28  ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 20.492 12.438  21.303 1.00 8.14  ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 20.056 11.018  21.628 1.00 8.33  ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 20.733 13.210  22.600 1.00 8.14  ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 23.815 14.496  18.292 1.00 9.59  ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 25.082 14.558  17.520 1.00 10.41 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 26.151 15.230  18.379 1.00 11.03 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 25.767 16.168  19.116 1.00 11.30 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 24.925 15.328  16.226 1.00 10.75 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 27.414 14.784  18.274 1.00 11.57 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 28.553 15.325  19.079 1.00 12.63 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 29.287 16.422  18.302 1.00 13.48 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 28.982 16.609  17.107 1.00 12.82 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 29.553 14.224  19.449 1.00 12.89 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 30.102 13.717  18.232 1.00 13.06 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 28.931 13.083  20.228 1.00 13.09 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 30.194 17.121  18.988 1.00 15.21 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 31.213 18.055  18.440 1.00 17.65 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 31.788 17.439  17.159 1.00 16.52 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 31.724 18.078  16.077 1.00 17.29 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 32.253 18.341  19.555 1.00 20.07 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 33.612 18.779  19.103 1.00 24.30 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 34.176 19.989  19.513 1.00 27.12 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 34.533 18.182  18.304 1.00 26.14 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 35.370 20.113  18.963 1.00 30.35 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 35.606 19.024  18.202 1.00 27.37 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 32.277 16.208  17.291 1.00 16.24 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 32.933 15.389  16.235 1.00 15.54 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.980 15.186  15.043 1.00 13.94 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 32.439 15.333  13.908 1.00 13.43 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 33.393 14.067  16.853 1.00 17.39 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 34.531 13.416  16.105 1.00 20.61 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 35.616 13.996  15.993 1.00 22.82 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 34.298 12.216  15.595 1.00 22.14 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 30.694 14.859  15.277 1.00 11.94 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 29.694 14.659  14.184 1.00 11.13 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 29.493 15.957  13.371 1.00 10.43 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 29.321 15.878  12.137 1.00 9.95  ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 28.314 14.237  14.698 1.00 11.11 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 28.229 12.808  15.198 1.00 11.56 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 28.793 11.910  14.538 1.00 12.15 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 27.610 12.615  16.255 1.00 11.45 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 29.471 17.123  14.016 1.00 9.85  ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 29.289 18.409  13.283 1.00 9.68  ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 30.524 18.733  12.420 1.00 9.62  ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 30.329 19.154  11.237 1.00 9.31  ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.914 19.540  14.248 1.00 9.11  ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 27.481 19.453  14.689 1.00 9.27  ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 27.025 19.024  15.902 1.00 8.99  ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 26.317 19.759  13.905 1.00 8.96  ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 25.661 19.055  15.928 1.00 9.41  ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 25.196 19.526  14.722 1.00 9.21  ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 26.112 20.244  12.608 1.00 9.30  ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.890 19.757  14.283 1.00 8.76  ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.830 20.495  12.183 1.00 8.81  ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.733 20.224  12.998 1.00 8.93  ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.734 18.520  12.956 1.00 9.45  ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 33.022 18.667  12.233 1.00 9.99  ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 33.058 17.764  10.990 1.00 10.02 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.673 18.165  9.973  1.00 9.63  ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 34.167 18.331  13.157 1.00 10.35 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 32.452 16.575  11.082 1.00 9.92  ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.478 15.532  10.015 1.00 10.31 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 31.130 15.433  9.305  1.00 9.71  ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.869 14.350  8.685  1.00 9.78  ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.867 14.170  10.580 1.00 11.24 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 34.333 14.129  10.939 1.00 12.33 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 35.185 14.561  10.162 1.00 12.39 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.624 13.646  12.127 1.00 13.21 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 30.345 16.515  9.351  1.00 8.94  ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.953 16.565  8.842  1.00 8.78  ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.938 16.241  7.356  1.00 8.57  ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.668 16.892  6.599  1.00 8.26  ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.345 17.957  9.021  1.00 8.93  ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.939 18.105  8.448  1.00 8.82  ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.925 17.311  9.259  1.00 8.79  ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.535 19.570  8.399  1.00 8.99  ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 28.065 15.309  6.986  1.00 8.91  ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.729 14.932  5.592  1.00 8.83  ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.417 15.628  5.237  1.00 9.11  ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.395 16.348  4.211  1.00 9.91  ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.612 13.403  5.432  1.00 8.84  ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 27.000 13.015  4.091  1.00 8.71  ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.951 12.716  5.648  1.00 8.82  ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.373 15.391  6.039  1.00 8.94  ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.983 15.843  5.778  1.00 8.92  ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 23.193 15.939  7.087  1.00 8.47  ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.338 15.047  7.937  1.00 8.59  ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.295 14.899  4.781  1.00 9.01  ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.844 15.213  4.570  1.00 9.34  ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.299 16.151  3.734  1.00 9.74  ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.742 14.557  5.210  1.00 9.39  ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.932 16.119  3.811  1.00 9.78  ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.562 15.145  4.706  1.00 9.55  ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.647 13.558  6.178  1.00 9.19  ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.300 14.768  5.158  1.00 9.62  ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.396 13.172  6.609  1.00 9.39  ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.240 13.762  6.098  1.00 9.35  ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.382 16.980  7.257  1.00 8.38  ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.449 17.067  8.412  1.00 8.16  ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 20.175 17.811  8.008  1.00 8.13  ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 20.227 18.608  7.061  1.00 7.88  ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 22.125 17.725  9.619  1.00 8.23  ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.756 19.082  9.344  1.00 8.55  ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.851 20.316  9.415  1.00 8.92  ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 22.290 21.346  8.914  1.00 9.55  ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.726 20.283  10.021 1.00 9.53  ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 19.088 17.579  8.759  1.00 8.22  ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.731 18.165  8.542  1.00 7.78  ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 17.043 18.291  9.911  1.00 7.22  ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.657 17.259  10.489 1.00 6.77  ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.969 17.291  7.535  1.00 8.37  ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.586 17.775  7.170  1.00 8.67  ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.857 18.158  8.082  1.00 10.32 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.229 17.708  5.982  1.00 8.89  ? 35  ASP   A OD2 1 
ATOM   240  N  N   A SER   A 1 30  ? 16.915 19.526  10.410 0.45 6.99  ? 36  SER   A N   1 
ATOM   241  N  N   B SER   A 1 30  ? 16.910 19.524  10.419 0.40 7.10  ? 36  SER   A N   1 
ATOM   242  C  CA  A SER   A 1 30  ? 16.312 19.865  11.728 0.45 6.90  ? 36  SER   A CA  1 
ATOM   243  C  CA  B SER   A 1 30  ? 16.310 19.833  11.747 0.40 7.07  ? 36  SER   A CA  1 
ATOM   244  C  C   A SER   A 1 30  ? 14.867 19.339  11.798 0.45 6.88  ? 36  SER   A C   1 
ATOM   245  C  C   B SER   A 1 30  ? 14.861 19.325  11.800 0.40 6.97  ? 36  SER   A C   1 
ATOM   246  O  O   A SER   A 1 30  ? 14.483 18.767  12.846 0.45 6.74  ? 36  SER   A O   1 
ATOM   247  O  O   B SER   A 1 30  ? 14.464 18.755  12.844 0.40 6.84  ? 36  SER   A O   1 
ATOM   248  C  CB  A SER   A 1 30  ? 16.368 21.350  11.967 0.45 6.90  ? 36  SER   A CB  1 
ATOM   249  C  CB  B SER   A 1 30  ? 16.379 21.304  12.068 0.40 7.16  ? 36  SER   A CB  1 
ATOM   250  O  OG  A SER   A 1 30  ? 15.847 21.693  13.237 0.45 6.91  ? 36  SER   A OG  1 
ATOM   251  O  OG  B SER   A 1 30  ? 15.781 22.087  11.045 0.40 7.50  ? 36  SER   A OG  1 
ATOM   252  N  N   . SER   A 1 31  ? 14.119 19.494  10.702 1.00 6.96  ? 37  SER   A N   1 
ATOM   253  C  CA  . SER   A 1 31  ? 12.701 19.073  10.616 1.00 6.98  ? 37  SER   A CA  1 
ATOM   254  C  C   . SER   A 1 31  ? 12.573 17.539  10.637 1.00 6.79  ? 37  SER   A C   1 
ATOM   255  O  O   . SER   A 1 31  ? 11.457 17.093  10.909 1.00 6.61  ? 37  SER   A O   1 
ATOM   256  C  CB  . SER   A 1 31  ? 12.013 19.686  9.410  1.00 7.31  ? 37  SER   A CB  1 
ATOM   257  O  OG  . SER   A 1 31  ? 12.221 18.890  8.269  1.00 7.90  ? 37  SER   A OG  1 
ATOM   258  N  N   . ARG   A 1 32  ? 13.642 16.777  10.369 1.00 6.38  ? 38  ARG   A N   1 
ATOM   259  C  CA  . ARG   A 1 32  ? 13.649 15.291  10.387 1.00 6.29  ? 38  ARG   A CA  1 
ATOM   260  C  C   . ARG   A 1 32  ? 14.315 14.767  11.671 1.00 6.12  ? 38  ARG   A C   1 
ATOM   261  O  O   . ARG   A 1 32  ? 14.201 13.565  11.929 1.00 6.28  ? 38  ARG   A O   1 
ATOM   262  C  CB  . ARG   A 1 32  ? 14.384 14.733  9.163  1.00 6.18  ? 38  ARG   A CB  1 
ATOM   263  C  CG  . ARG   A 1 32  ? 13.630 14.905  7.856  1.00 6.30  ? 38  ARG   A CG  1 
ATOM   264  C  CD  . ARG   A 1 32  ? 14.290 14.232  6.666  1.00 5.93  ? 38  ARG   A CD  1 
ATOM   265  N  NE  . ARG   A 1 32  ? 14.270 12.780  6.731  1.00 5.75  ? 38  ARG   A NE  1 
ATOM   266  C  CZ  . ARG   A 1 32  ? 14.328 11.962  5.686  1.00 6.02  ? 38  ARG   A CZ  1 
ATOM   267  N  NH1 . ARG   A 1 32  ? 14.385 12.447  4.459  1.00 6.09  ? 38  ARG   A NH1 1 
ATOM   268  N  NH2 . ARG   A 1 32  ? 14.283 10.650  5.856  1.00 5.96  ? 38  ARG   A NH2 1 
ATOM   269  N  N   . ASP   A 1 33  ? 14.961 15.635  12.438 1.00 6.17  ? 39  ASP   A N   1 
ATOM   270  C  CA  . ASP   A 1 33  ? 15.817 15.297  13.615 1.00 6.22  ? 39  ASP   A CA  1 
ATOM   271  C  C   . ASP   A 1 33  ? 16.879 14.251  13.228 1.00 6.01  ? 39  ASP   A C   1 
ATOM   272  O  O   . ASP   A 1 33  ? 17.150 13.386  14.079 1.00 5.66  ? 39  ASP   A O   1 
ATOM   273  C  CB  . ASP   A 1 33  ? 14.988 14.762  14.798 1.00 6.33  ? 39  ASP   A CB  1 
ATOM   274  C  CG  . ASP   A 1 33  ? 15.769 14.530  16.104 1.00 6.53  ? 39  ASP   A CG  1 
ATOM   275  O  OD1 . ASP   A 1 33  ? 16.709 15.308  16.395 1.00 6.18  ? 39  ASP   A OD1 1 
ATOM   276  O  OD2 . ASP   A 1 33  ? 15.414 13.579  16.860 1.00 6.53  ? 39  ASP   A OD2 1 
ATOM   277  N  N   . LEU   A 1 34  ? 17.436 14.322  12.009 1.00 5.98  ? 40  LEU   A N   1 
ATOM   278  C  CA  . LEU   A 1 34  ? 18.487 13.391  11.493 1.00 6.06  ? 40  LEU   A CA  1 
ATOM   279  C  C   . LEU   A 1 34  ? 19.804 14.122  11.216 1.00 6.20  ? 40  LEU   A C   1 
ATOM   280  O  O   . LEU   A 1 34  ? 19.780 15.257  10.638 1.00 6.16  ? 40  LEU   A O   1 
ATOM   281  C  CB  . LEU   A 1 34  ? 18.014 12.720  10.192 1.00 6.08  ? 40  LEU   A CB  1 
ATOM   282  C  CG  . LEU   A 1 34  ? 17.058 11.530  10.317 1.00 5.98  ? 40  LEU   A CG  1 
ATOM   283  C  CD1 . LEU   A 1 34  ? 16.875 10.913  8.943  1.00 5.94  ? 40  LEU   A CD1 1 
ATOM   284  C  CD2 . LEU   A 1 34  ? 17.535 10.486  11.318 1.00 5.97  ? 40  LEU   A CD2 1 
ATOM   285  N  N   . LEU   A 1 35  ? 20.929 13.490  11.579 1.00 6.34  ? 41  LEU   A N   1 
ATOM   286  C  CA  . LEU   A 1 35  ? 22.292 13.934  11.184 1.00 6.43  ? 41  LEU   A CA  1 
ATOM   287  C  C   . LEU   A 1 35  ? 23.086 12.716  10.722 1.00 6.71  ? 41  LEU   A C   1 
ATOM   288  O  O   . LEU   A 1 35  ? 23.006 11.653  11.374 1.00 7.01  ? 41  LEU   A O   1 
ATOM   289  C  CB  . LEU   A 1 35  ? 22.998 14.635  12.349 1.00 6.36  ? 41  LEU   A CB  1 
ATOM   290  C  CG  . LEU   A 1 35  ? 24.377 15.220  12.031 1.00 6.35  ? 41  LEU   A CG  1 
ATOM   291  C  CD1 . LEU   A 1 35  ? 24.651 16.492  12.803 1.00 6.44  ? 41  LEU   A CD1 1 
ATOM   292  C  CD2 . LEU   A 1 35  ? 25.484 14.225  12.280 1.00 6.33  ? 41  LEU   A CD2 1 
ATOM   293  N  N   . VAL   A 1 36  ? 23.845 12.888  9.650  1.00 6.69  ? 42  VAL   A N   1 
ATOM   294  C  CA  . VAL   A 1 36  ? 24.780 11.867  9.111  1.00 7.18  ? 42  VAL   A CA  1 
ATOM   295  C  C   . VAL   A 1 36  ? 26.179 12.488  9.095  1.00 7.67  ? 42  VAL   A C   1 
ATOM   296  O  O   . VAL   A 1 36  ? 26.299 13.618  8.609  1.00 7.84  ? 42  VAL   A O   1 
ATOM   297  C  CB  . VAL   A 1 36  ? 24.356 11.399  7.704  1.00 7.02  ? 42  VAL   A CB  1 
ATOM   298  C  CG1 . VAL   A 1 36  ? 25.342 10.384  7.151  1.00 7.07  ? 42  VAL   A CG1 1 
ATOM   299  C  CG2 . VAL   A 1 36  ? 22.937 10.847  7.689  1.00 6.88  ? 42  VAL   A CG2 1 
ATOM   300  N  N   . SER   A 1 37  ? 27.172 11.767  9.619  1.00 8.59  ? 43  SER   A N   1 
ATOM   301  C  CA  . SER   A 1 37  ? 28.606 12.154  9.673  1.00 10.05 ? 43  SER   A CA  1 
ATOM   302  C  C   . SER   A 1 37  ? 29.427 11.022  9.051  1.00 11.51 ? 43  SER   A C   1 
ATOM   303  O  O   . SER   A 1 37  ? 28.924 9.886   8.980  1.00 11.30 ? 43  SER   A O   1 
ATOM   304  C  CB  . SER   A 1 37  ? 29.035 12.438  11.103 1.00 9.67  ? 43  SER   A CB  1 
ATOM   305  O  OG  . SER   A 1 37  ? 28.741 11.341  11.966 1.00 9.28  ? 43  SER   A OG  1 
ATOM   306  N  N   . SER   A 1 38  ? 30.649 11.336  8.608  0.50 12.06 ? 44  SER   A N   1 
ATOM   307  C  CA  . SER   A 1 38  ? 31.626 10.375  8.031  0.50 12.90 ? 44  SER   A CA  1 
ATOM   308  C  C   . SER   A 1 38  ? 32.340 9.624   9.156  0.50 13.45 ? 44  SER   A C   1 
ATOM   309  O  O   . SER   A 1 38  ? 32.518 10.207  10.235 0.50 13.68 ? 44  SER   A O   1 
ATOM   310  C  CB  . SER   A 1 38  ? 32.610 11.077  7.130  0.50 12.99 ? 44  SER   A CB  1 
ATOM   311  O  OG  . SER   A 1 38  ? 33.241 12.152  7.806  0.50 13.08 ? 44  SER   A OG  1 
ATOM   312  N  N   . THR   A 1 39  ? 32.710 8.369   8.893  0.50 14.29 ? 45  THR   A N   1 
ATOM   313  C  CA  . THR   A 1 39  ? 33.448 7.480   9.829  0.50 14.79 ? 45  THR   A CA  1 
ATOM   314  C  C   . THR   A 1 39  ? 34.736 6.986   9.166  0.50 15.59 ? 45  THR   A C   1 
ATOM   315  O  O   . THR   A 1 39  ? 34.789 6.969   7.914  0.50 15.41 ? 45  THR   A O   1 
ATOM   316  C  CB  . THR   A 1 39  ? 32.610 6.265   10.245 0.50 14.70 ? 45  THR   A CB  1 
ATOM   317  O  OG1 . THR   A 1 39  ? 32.418 5.459   9.083  0.50 14.37 ? 45  THR   A OG1 1 
ATOM   318  C  CG2 . THR   A 1 39  ? 31.276 6.635   10.856 0.50 14.66 ? 45  THR   A CG2 1 
ATOM   319  N  N   . THR   A 1 40  ? 35.707 6.577   9.990  0.50 16.09 ? 46  THR   A N   1 
ATOM   320  C  CA  . THR   A 1 40  ? 36.987 5.943   9.575  0.50 16.66 ? 46  THR   A CA  1 
ATOM   321  C  C   . THR   A 1 40  ? 36.714 4.484   9.194  0.50 16.47 ? 46  THR   A C   1 
ATOM   322  O  O   . THR   A 1 40  ? 37.124 4.068   8.093  0.50 16.61 ? 46  THR   A O   1 
ATOM   323  C  CB  . THR   A 1 40  ? 38.043 6.058   10.685 0.50 16.97 ? 46  THR   A CB  1 
ATOM   324  O  OG1 . THR   A 1 40  ? 39.265 5.486   10.219 0.50 17.00 ? 46  THR   A OG1 1 
ATOM   325  C  CG2 . THR   A 1 40  ? 37.634 5.379   11.974 0.50 17.22 ? 46  THR   A CG2 1 
ATOM   326  N  N   . ALA   A 1 41  ? 36.037 3.744   10.075 0.50 16.36 ? 47  ALA   A N   1 
ATOM   327  C  CA  . ALA   A 1 41  ? 35.792 2.291   9.939  0.50 16.07 ? 47  ALA   A CA  1 
ATOM   328  C  C   . ALA   A 1 41  ? 34.495 2.064   9.160  0.50 15.84 ? 47  ALA   A C   1 
ATOM   329  O  O   . ALA   A 1 41  ? 33.672 3.004   9.076  0.50 16.17 ? 47  ALA   A O   1 
ATOM   330  C  CB  . ALA   A 1 41  ? 35.751 1.645   11.301 0.50 15.90 ? 47  ALA   A CB  1 
ATOM   331  N  N   . GLN   A 1 42  ? 34.331 0.863   8.598  0.50 14.98 ? 48  GLN   A N   1 
ATOM   332  C  CA  . GLN   A 1 42  ? 33.132 0.465   7.820  0.50 14.36 ? 48  GLN   A CA  1 
ATOM   333  C  C   . GLN   A 1 42  ? 32.079 -0.115  8.765  0.50 13.53 ? 48  GLN   A C   1 
ATOM   334  O  O   . GLN   A 1 42  ? 32.441 -0.968  9.592  0.50 13.36 ? 48  GLN   A O   1 
ATOM   335  C  CB  . GLN   A 1 42  ? 33.498 -0.572  6.762  0.50 14.76 ? 48  GLN   A CB  1 
ATOM   336  C  CG  . GLN   A 1 42  ? 34.526 -0.075  5.764  0.50 15.01 ? 48  GLN   A CG  1 
ATOM   337  C  CD  . GLN   A 1 42  ? 33.989 -0.148  4.358  0.50 15.19 ? 48  GLN   A CD  1 
ATOM   338  O  OE1 . GLN   A 1 42  ? 34.477 -0.911  3.525  0.50 15.31 ? 48  GLN   A OE1 1 
ATOM   339  N  NE2 . GLN   A 1 42  ? 32.950 0.631   4.097  0.50 15.01 ? 48  GLN   A NE2 1 
ATOM   340  N  N   . GLY   A 1 43  ? 30.830 0.332   8.618  0.50 12.69 ? 49  GLY   A N   1 
ATOM   341  C  CA  . GLY   A 1 43  ? 29.666 -0.146  9.387  0.50 12.07 ? 49  GLY   A CA  1 
ATOM   342  C  C   . GLY   A 1 43  ? 29.098 -1.426  8.802  0.50 11.45 ? 49  GLY   A C   1 
ATOM   343  O  O   . GLY   A 1 43  ? 29.384 -1.725  7.624  0.50 11.15 ? 49  GLY   A O   1 
ATOM   344  N  N   . CYS   A 1 44  ? 28.331 -2.165  9.606  0.50 11.06 ? 50  CYS   A N   1 
ATOM   345  C  CA  . CYS   A 1 44  ? 27.820 -3.522  9.281  0.50 10.60 ? 50  CYS   A CA  1 
ATOM   346  C  C   . CYS   A 1 44  ? 26.290 -3.519  9.200  0.50 10.64 ? 50  CYS   A C   1 
ATOM   347  O  O   . CYS   A 1 44  ? 25.712 -4.620  9.137  0.50 10.74 ? 50  CYS   A O   1 
ATOM   348  C  CB  . CYS   A 1 44  ? 28.267 -4.535  10.329 0.50 10.27 ? 50  CYS   A CB  1 
ATOM   349  S  SG  . CYS   A 1 44  ? 30.066 -4.721  10.437 0.50 9.75  ? 50  CYS   A SG  1 
ATOM   350  N  N   . ASP   A 1 45  ? 25.652 -2.343  9.207  0.50 10.82 ? 51  ASP   A N   1 
ATOM   351  C  CA  . ASP   A 1 45  ? 24.167 -2.226  9.185  0.50 11.00 ? 51  ASP   A CA  1 
ATOM   352  C  C   . ASP   A 1 45  ? 23.699 -2.114  7.729  0.50 11.25 ? 51  ASP   A C   1 
ATOM   353  O  O   . ASP   A 1 45  ? 24.368 -1.422  6.934  0.50 11.41 ? 51  ASP   A O   1 
ATOM   354  C  CB  . ASP   A 1 45  ? 23.664 -1.056  10.037 0.50 10.73 ? 51  ASP   A CB  1 
ATOM   355  C  CG  . ASP   A 1 45  ? 23.868 -1.231  11.536 0.50 10.70 ? 51  ASP   A CG  1 
ATOM   356  O  OD1 . ASP   A 1 45  ? 23.800 -2.388  12.014 0.50 10.43 ? 51  ASP   A OD1 1 
ATOM   357  O  OD2 . ASP   A 1 45  ? 24.101 -0.213  12.219 0.50 10.40 ? 51  ASP   A OD2 1 
ATOM   358  N  N   . THR   A 1 46  ? 22.609 -2.807  7.397  0.50 11.44 ? 52  THR   A N   1 
ATOM   359  C  CA  . THR   A 1 46  ? 21.920 -2.740  6.085  0.50 11.78 ? 52  THR   A CA  1 
ATOM   360  C  C   . THR   A 1 46  ? 20.659 -1.880  6.236  0.50 12.00 ? 52  THR   A C   1 
ATOM   361  O  O   . THR   A 1 46  ? 19.897 -2.129  7.190  0.50 11.86 ? 52  THR   A O   1 
ATOM   362  C  CB  . THR   A 1 46  ? 21.577 -4.142  5.570  0.50 11.90 ? 52  THR   A CB  1 
ATOM   363  O  OG1 . THR   A 1 46  ? 22.795 -4.844  5.318  0.50 12.24 ? 52  THR   A OG1 1 
ATOM   364  C  CG2 . THR   A 1 46  ? 20.738 -4.114  4.312  0.50 11.87 ? 52  THR   A CG2 1 
ATOM   365  N  N   . ILE   A 1 47  ? 20.472 -0.900  5.346  1.00 12.45 ? 53  ILE   A N   1 
ATOM   366  C  CA  . ILE   A 1 47  ? 19.261 -0.030  5.331  1.00 12.02 ? 53  ILE   A CA  1 
ATOM   367  C  C   . ILE   A 1 47  ? 18.179 -0.781  4.553  1.00 12.01 ? 53  ILE   A C   1 
ATOM   368  O  O   . ILE   A 1 47  ? 18.483 -1.261  3.449  1.00 12.62 ? 53  ILE   A O   1 
ATOM   369  C  CB  . ILE   A 1 47  ? 19.551 1.357   4.722  1.00 12.13 ? 53  ILE   A CB  1 
ATOM   370  C  CG1 . ILE   A 1 47  ? 20.780 2.049   5.320  1.00 11.95 ? 53  ILE   A CG1 1 
ATOM   371  C  CG2 . ILE   A 1 47  ? 18.317 2.244   4.817  1.00 12.28 ? 53  ILE   A CG2 1 
ATOM   372  C  CD1 . ILE   A 1 47  ? 20.693 2.317   6.808  1.00 11.87 ? 53  ILE   A CD1 1 
ATOM   373  N  N   . ALA   A 1 48  ? 16.958 -0.858  5.094  1.00 10.92 ? 54  ALA   A N   1 
ATOM   374  C  CA  . ALA   A 1 48  ? 15.815 -1.496  4.406  1.00 10.93 ? 54  ALA   A CA  1 
ATOM   375  C  C   . ALA   A 1 48  ? 15.424 -0.646  3.194  1.00 10.09 ? 54  ALA   A C   1 
ATOM   376  O  O   . ALA   A 1 48  ? 15.505 0.596   3.292  1.00 8.63  ? 54  ALA   A O   1 
ATOM   377  C  CB  . ALA   A 1 48  ? 14.661 -1.680  5.369  1.00 11.34 ? 54  ALA   A CB  1 
ATOM   378  N  N   . ARG   A 1 49  ? 15.101 -1.296  2.080  1.00 9.93  ? 55  ARG   A N   1 
ATOM   379  C  CA  . ARG   A 1 49  ? 14.483 -0.658  0.891  1.00 10.70 ? 55  ARG   A CA  1 
ATOM   380  C  C   . ARG   A 1 49  ? 13.145 -1.356  0.608  1.00 10.38 ? 55  ARG   A C   1 
ATOM   381  O  O   . ARG   A 1 49  ? 13.145 -2.380  -0.098 1.00 11.12 ? 55  ARG   A O   1 
ATOM   382  C  CB  . ARG   A 1 49  ? 15.458 -0.697  -0.288 1.00 11.34 ? 55  ARG   A CB  1 
ATOM   383  C  CG  . ARG   A 1 49  ? 16.812 -0.060  -0.010 1.00 12.26 ? 55  ARG   A CG  1 
ATOM   384  C  CD  . ARG   A 1 49  ? 16.811 1.410   0.408  1.00 12.86 ? 55  ARG   A CD  1 
ATOM   385  N  NE  . ARG   A 1 49  ? 18.126 1.782   0.920  1.00 13.30 ? 55  ARG   A NE  1 
ATOM   386  C  CZ  . ARG   A 1 49  ? 18.434 2.961   1.466  1.00 13.03 ? 55  ARG   A CZ  1 
ATOM   387  N  NH1 . ARG   A 1 49  ? 17.530 3.921   1.551  1.00 13.46 ? 55  ARG   A NH1 1 
ATOM   388  N  NH2 . ARG   A 1 49  ? 19.661 3.188   1.903  1.00 13.47 ? 55  ARG   A NH2 1 
ATOM   389  N  N   . CYS   A 1 50  ? 12.050 -0.797  1.128  1.00 10.15 ? 56  CYS   A N   1 
ATOM   390  C  CA  . CYS   A 1 50  ? 10.714 -1.443  1.221  1.00 9.54  ? 56  CYS   A CA  1 
ATOM   391  C  C   . CYS   A 1 50  ? 9.685  -0.408  1.689  1.00 9.61  ? 56  CYS   A C   1 
ATOM   392  O  O   . CYS   A 1 50  ? 10.074 0.732   1.988  1.00 9.79  ? 56  CYS   A O   1 
ATOM   393  C  CB  . CYS   A 1 50  ? 10.744 -2.581  2.234  1.00 9.31  ? 56  CYS   A CB  1 
ATOM   394  S  SG  . CYS   A 1 50  ? 11.115 -1.952  3.888  1.00 8.55  ? 56  CYS   A SG  1 
ATOM   395  N  N   A ASP   A 1 51  ? 8.399  -0.775  1.737  0.25 9.46  ? 57  ASP   A N   1 
ATOM   396  N  N   B ASP   A 1 51  ? 8.425  -0.854  1.772  0.25 9.75  ? 57  ASP   A N   1 
ATOM   397  C  CA  A ASP   A 1 51  ? 7.329  0.053   2.365  0.25 9.30  ? 57  ASP   A CA  1 
ATOM   398  C  CA  B ASP   A 1 51  ? 7.239  -0.083  2.231  0.25 9.78  ? 57  ASP   A CA  1 
ATOM   399  C  C   A ASP   A 1 51  ? 6.665  -0.754  3.488  0.25 9.27  ? 57  ASP   A C   1 
ATOM   400  C  C   B ASP   A 1 51  ? 6.692  -0.684  3.535  0.25 9.52  ? 57  ASP   A C   1 
ATOM   401  O  O   A ASP   A 1 51  ? 5.441  -0.617  3.668  0.25 9.46  ? 57  ASP   A O   1 
ATOM   402  O  O   B ASP   A 1 51  ? 5.568  -0.308  3.909  0.25 9.60  ? 57  ASP   A O   1 
ATOM   403  C  CB  A ASP   A 1 51  ? 6.292  0.546   1.351  0.25 9.20  ? 57  ASP   A CB  1 
ATOM   404  C  CB  B ASP   A 1 51  ? 6.145  -0.112  1.161  0.25 10.11 ? 57  ASP   A CB  1 
ATOM   405  C  CG  A ASP   A 1 51  ? 5.492  -0.563  0.692  0.25 9.12  ? 57  ASP   A CG  1 
ATOM   406  C  CG  B ASP   A 1 51  ? 5.024  0.882   1.392  0.25 10.29 ? 57  ASP   A CG  1 
ATOM   407  O  OD1 A ASP   A 1 51  ? 5.842  -1.732  0.905  0.25 8.92  ? 57  ASP   A OD1 1 
ATOM   408  O  OD1 B ASP   A 1 51  ? 5.332  2.057   1.655  0.25 10.49 ? 57  ASP   A OD1 1 
ATOM   409  O  OD2 A ASP   A 1 51  ? 4.540  -0.239  -0.057 0.25 9.24  ? 57  ASP   A OD2 1 
ATOM   410  O  OD2 B ASP   A 1 51  ? 3.851  0.473   1.307  0.25 10.85 ? 57  ASP   A OD2 1 
ATOM   411  N  N   . CYS   A 1 52  ? 7.448  -1.575  4.194  1.00 9.32  ? 58  CYS   A N   1 
ATOM   412  C  CA  . CYS   A 1 52  ? 7.001  -2.316  5.419  1.00 9.07  ? 58  CYS   A CA  1 
ATOM   413  C  C   . CYS   A 1 52  ? 6.364  -1.355  6.439  1.00 8.77  ? 58  CYS   A C   1 
ATOM   414  O  O   . CYS   A 1 52  ? 6.823  -0.188  6.571  1.00 8.27  ? 58  CYS   A O   1 
ATOM   415  C  CB  . CYS   A 1 52  ? 8.156  -3.069  6.088  1.00 9.09  ? 58  CYS   A CB  1 
ATOM   416  S  SG  . CYS   A 1 52  ? 8.689  -4.578  5.222  1.00 10.37 ? 58  CYS   A SG  1 
ATOM   417  N  N   . GLN   A 1 53  ? 5.309  -1.820  7.113  1.00 8.57  ? 59  GLN   A N   1 
ATOM   418  C  CA  . GLN   A 1 53  ? 4.635  -1.133  8.240  1.00 8.19  ? 59  GLN   A CA  1 
ATOM   419  C  C   . GLN   A 1 53  ? 4.609  -2.041  9.469  1.00 7.57  ? 59  GLN   A C   1 
ATOM   420  O  O   . GLN   A 1 53  ? 3.843  -1.733  10.378 1.00 7.30  ? 59  GLN   A O   1 
ATOM   421  C  CB  . GLN   A 1 53  ? 3.210  -0.735  7.865  1.00 8.88  ? 59  GLN   A CB  1 
ATOM   422  C  CG  . GLN   A 1 53  ? 3.130  0.390   6.839  1.00 9.49  ? 59  GLN   A CG  1 
ATOM   423  C  CD  . GLN   A 1 53  ? 1.713  0.894   6.689  1.00 9.49  ? 59  GLN   A CD  1 
ATOM   424  O  OE1 . GLN   A 1 53  ? 1.108  0.813   5.606  1.00 10.10 ? 59  GLN   A OE1 1 
ATOM   425  N  NE2 . GLN   A 1 53  ? 1.146  1.376   7.794  1.00 9.88  ? 59  GLN   A NE2 1 
ATOM   426  N  N   . THR   A 1 54  ? 5.414  -3.105  9.508  1.00 7.29  ? 60  THR   A N   1 
ATOM   427  C  CA  . THR   A 1 54  ? 5.578  -3.981  10.707 1.00 6.98  ? 60  THR   A CA  1 
ATOM   428  C  C   . THR   A 1 54  ? 7.073  -4.228  10.943 1.00 6.52  ? 60  THR   A C   1 
ATOM   429  O  O   . THR   A 1 54  ? 7.838  -4.334  9.967  1.00 6.22  ? 60  THR   A O   1 
ATOM   430  C  CB  . THR   A 1 54  ? 4.827  -5.318  10.574 1.00 7.64  ? 60  THR   A CB  1 
ATOM   431  O  OG1 . THR   A 1 54  ? 5.275  -5.952  9.382  1.00 8.32  ? 60  THR   A OG1 1 
ATOM   432  C  CG2 . THR   A 1 54  ? 3.320  -5.194  10.476 1.00 7.67  ? 60  THR   A CG2 1 
ATOM   433  N  N   . GLY   A 1 55  ? 7.470  -4.354  12.201 1.00 5.81  ? 61  GLY   A N   1 
ATOM   434  C  CA  . GLY   A 1 55  ? 8.895  -4.498  12.542 1.00 5.60  ? 61  GLY   A CA  1 
ATOM   435  C  C   . GLY   A 1 55  ? 9.097  -4.654  14.029 1.00 5.19  ? 61  GLY   A C   1 
ATOM   436  O  O   . GLY   A 1 55  ? 8.144  -5.011  14.697 1.00 5.28  ? 61  GLY   A O   1 
ATOM   437  N  N   . VAL   A 1 56  ? 10.329 -4.453  14.491 1.00 4.87  ? 62  VAL   A N   1 
ATOM   438  C  CA  . VAL   A 1 56  ? 10.733 -4.556  15.931 1.00 4.80  ? 62  VAL   A CA  1 
ATOM   439  C  C   . VAL   A 1 56  ? 11.632 -3.354  16.259 1.00 4.65  ? 62  VAL   A C   1 
ATOM   440  O  O   . VAL   A 1 56  ? 12.508 -3.037  15.413 1.00 4.65  ? 62  VAL   A O   1 
ATOM   441  C  CB  . VAL   A 1 56  ? 11.441 -5.908  16.177 1.00 4.80  ? 62  VAL   A CB  1 
ATOM   442  C  CG1 . VAL   A 1 56  ? 11.802 -6.148  17.635 1.00 4.94  ? 62  VAL   A CG1 1 
ATOM   443  C  CG2 . VAL   A 1 56  ? 10.617 -7.085  15.687 1.00 4.89  ? 62  VAL   A CG2 1 
ATOM   444  N  N   . TYR   A 1 57  ? 11.426 -2.711  17.419 1.00 4.55  ? 63  TYR   A N   1 
ATOM   445  C  CA  . TYR   A 1 57  ? 12.316 -1.630  17.927 1.00 4.43  ? 63  TYR   A CA  1 
ATOM   446  C  C   . TYR   A 1 57  ? 12.889 -1.989  19.303 1.00 4.66  ? 63  TYR   A C   1 
ATOM   447  O  O   . TYR   A 1 57  ? 12.234 -2.717  20.090 1.00 4.33  ? 63  TYR   A O   1 
ATOM   448  C  CB  . TYR   A 1 57  ? 11.579 -0.283  17.915 1.00 4.41  ? 63  TYR   A CB  1 
ATOM   449  C  CG  . TYR   A 1 57  ? 10.684 0.007   19.093 1.00 4.29  ? 63  TYR   A CG  1 
ATOM   450  C  CD1 . TYR   A 1 57  ? 9.387  -0.489  19.144 1.00 4.25  ? 63  TYR   A CD1 1 
ATOM   451  C  CD2 . TYR   A 1 57  ? 11.120 0.793   20.158 1.00 4.17  ? 63  TYR   A CD2 1 
ATOM   452  C  CE1 . TYR   A 1 57  ? 8.555  -0.217  20.213 1.00 4.20  ? 63  TYR   A CE1 1 
ATOM   453  C  CE2 . TYR   A 1 57  ? 10.295 1.068   21.240 1.00 4.21  ? 63  TYR   A CE2 1 
ATOM   454  C  CZ  . TYR   A 1 57  ? 8.997  0.565   21.270 1.00 4.32  ? 63  TYR   A CZ  1 
ATOM   455  O  OH  . TYR   A 1 57  ? 8.173  0.811   22.343 1.00 4.35  ? 63  TYR   A OH  1 
ATOM   456  N  N   . TYR   A 1 58  ? 14.095 -1.482  19.580 1.00 4.68  ? 64  TYR   A N   1 
ATOM   457  C  CA  . TYR   A 1 58  ? 14.733 -1.567  20.920 1.00 4.95  ? 64  TYR   A CA  1 
ATOM   458  C  C   . TYR   A 1 58  ? 14.284 -0.384  21.792 1.00 5.16  ? 64  TYR   A C   1 
ATOM   459  O  O   . TYR   A 1 58  ? 14.386 0.767   21.308 1.00 5.35  ? 64  TYR   A O   1 
ATOM   460  C  CB  . TYR   A 1 58  ? 16.261 -1.621  20.832 1.00 4.83  ? 64  TYR   A CB  1 
ATOM   461  C  CG  . TYR   A 1 58  ? 16.892 -1.712  22.199 1.00 4.93  ? 64  TYR   A CG  1 
ATOM   462  C  CD1 . TYR   A 1 58  ? 16.635 -2.796  23.028 1.00 5.09  ? 64  TYR   A CD1 1 
ATOM   463  C  CD2 . TYR   A 1 58  ? 17.701 -0.703  22.695 1.00 4.99  ? 64  TYR   A CD2 1 
ATOM   464  C  CE1 . TYR   A 1 58  ? 17.181 -2.886  24.297 1.00 5.06  ? 64  TYR   A CE1 1 
ATOM   465  C  CE2 . TYR   A 1 58  ? 18.232 -0.766  23.968 1.00 5.06  ? 64  TYR   A CE2 1 
ATOM   466  C  CZ  . TYR   A 1 58  ? 17.986 -1.864  24.775 1.00 5.08  ? 64  TYR   A CZ  1 
ATOM   467  O  OH  . TYR   A 1 58  ? 18.489 -1.932  26.045 1.00 5.53  ? 64  TYR   A OH  1 
ATOM   468  N  N   . CYS   A 1 59  ? 13.873 -0.663  23.041 1.00 5.62  ? 65  CYS   A N   1 
ATOM   469  C  CA  . CYS   A 1 59  ? 13.410 0.298   24.078 1.00 5.98  ? 65  CYS   A CA  1 
ATOM   470  C  C   . CYS   A 1 59  ? 14.371 0.205   25.264 1.00 6.56  ? 65  CYS   A C   1 
ATOM   471  O  O   . CYS   A 1 59  ? 14.211 -0.693  26.069 1.00 6.15  ? 65  CYS   A O   1 
ATOM   472  C  CB  . CYS   A 1 59  ? 11.968 -0.013  24.475 1.00 5.89  ? 65  CYS   A CB  1 
ATOM   473  S  SG  . CYS   A 1 59  ? 11.296 1.033   25.801 1.00 5.78  ? 65  CYS   A SG  1 
ATOM   474  N  N   . SER   A 1 60  ? 15.351 1.109   25.354 1.00 7.71  ? 66  SER   A N   1 
ATOM   475  C  CA  . SER   A 1 60  ? 16.398 1.049   26.406 1.00 8.31  ? 66  SER   A CA  1 
ATOM   476  C  C   . SER   A 1 60  ? 15.725 1.181   27.778 1.00 8.67  ? 66  SER   A C   1 
ATOM   477  O  O   . SER   A 1 60  ? 16.114 0.422   28.699 1.00 8.56  ? 66  SER   A O   1 
ATOM   478  C  CB  . SER   A 1 60  ? 17.512 2.061   26.204 1.00 9.10  ? 66  SER   A CB  1 
ATOM   479  O  OG  . SER   A 1 60  ? 17.115 3.365   26.605 1.00 10.78 ? 66  SER   A OG  1 
ATOM   480  N  N   . SER   A 1 61  ? 14.693 2.026   27.887 1.00 8.55  ? 67  SER   A N   1 
ATOM   481  C  CA  . SER   A 1 61  ? 13.934 2.250   29.151 1.00 8.42  ? 67  SER   A CA  1 
ATOM   482  C  C   . SER   A 1 61  ? 13.206 0.974   29.633 1.00 8.37  ? 67  SER   A C   1 
ATOM   483  O  O   . SER   A 1 61  ? 12.753 0.996   30.792 1.00 8.48  ? 67  SER   A O   1 
ATOM   484  C  CB  . SER   A 1 61  ? 13.003 3.421   29.016 1.00 8.35  ? 67  SER   A CB  1 
ATOM   485  O  OG  . SER   A 1 61  ? 11.893 3.101   28.207 1.00 8.39  ? 67  SER   A OG  1 
ATOM   486  N  N   . ARG   A 1 62  ? 13.096 -0.089  28.814 1.00 7.98  ? 68  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 62  ? 12.590 -1.422  29.257 1.00 8.26  ? 68  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 62  ? 13.592 -2.569  29.038 1.00 8.63  ? 68  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 62  ? 13.216 -3.713  29.376 1.00 8.66  ? 68  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 62  ? 11.286 -1.721  28.518 1.00 8.15  ? 68  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 62  ? 10.154 -0.763  28.861 1.00 8.32  ? 68  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 62  ? 9.516  -1.136  30.181 1.00 8.45  ? 68  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 62  ? 8.477  -0.188  30.572 1.00 8.63  ? 68  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 62  ? 8.662  0.917   31.303 1.00 8.44  ? 68  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 62  ? 9.857  1.232   31.795 1.00 7.97  ? 68  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 62  ? 7.621  1.698   31.553 1.00 8.45  ? 68  ARG   A NH2 1 
ATOM   497  N  N   . ARG   A 1 63  ? 14.786 -2.315  28.485 1.00 9.05  ? 69  ARG   A N   1 
ATOM   498  C  CA  . ARG   A 1 63  ? 15.755 -3.338  28.007 1.00 9.84  ? 69  ARG   A CA  1 
ATOM   499  C  C   . ARG   A 1 63  ? 15.057 -4.422  27.155 1.00 9.67  ? 69  ARG   A C   1 
ATOM   500  O  O   . ARG   A 1 63  ? 15.404 -5.618  27.297 1.00 9.65  ? 69  ARG   A O   1 
ATOM   501  C  CB  . ARG   A 1 63  ? 16.488 -3.946  29.215 1.00 10.76 ? 69  ARG   A CB  1 
ATOM   502  C  CG  . ARG   A 1 63  ? 17.401 -2.956  29.928 1.00 11.43 ? 69  ARG   A CG  1 
ATOM   503  C  CD  . ARG   A 1 63  ? 18.231 -3.561  31.049 1.00 12.59 ? 69  ARG   A CD  1 
ATOM   504  N  NE  . ARG   A 1 63  ? 18.879 -2.545  31.890 1.00 13.37 ? 69  ARG   A NE  1 
ATOM   505  C  CZ  . ARG   A 1 63  ? 18.795 -2.439  33.233 1.00 14.71 ? 69  ARG   A CZ  1 
ATOM   506  N  NH1 . ARG   A 1 63  ? 18.044 -3.262  33.948 1.00 14.71 ? 69  ARG   A NH1 1 
ATOM   507  N  NH2 . ARG   A 1 63  ? 19.458 -1.473  33.866 1.00 16.03 ? 69  ARG   A NH2 1 
ATOM   508  N  N   . LYS   A 1 64  ? 14.087 -4.067  26.303 1.00 9.46  ? 70  LYS   A N   1 
ATOM   509  C  CA  . LYS   A 1 64  ? 13.290 -5.087  25.582 1.00 9.18  ? 70  LYS   A CA  1 
ATOM   510  C  C   . LYS   A 1 64  ? 13.160 -4.711  24.108 1.00 8.53  ? 70  LYS   A C   1 
ATOM   511  O  O   . LYS   A 1 64  ? 13.279 -3.521  23.774 1.00 8.29  ? 70  LYS   A O   1 
ATOM   512  C  CB  . LYS   A 1 64  ? 11.888 -5.260  26.185 1.00 10.38 ? 70  LYS   A CB  1 
ATOM   513  C  CG  . LYS   A 1 64  ? 11.850 -6.015  27.509 1.00 11.69 ? 70  LYS   A CG  1 
ATOM   514  C  CD  . LYS   A 1 64  ? 10.651 -6.943  27.687 1.00 13.09 ? 70  LYS   A CD  1 
ATOM   515  C  CE  . LYS   A 1 64  ? 10.811 -7.920  28.837 1.00 13.61 ? 70  LYS   A CE  1 
ATOM   516  N  NZ  . LYS   A 1 64  ? 11.091 -7.215  30.111 1.00 14.40 ? 70  LYS   A NZ  1 
ATOM   517  N  N   . HIS   A 1 65  ? 12.813 -5.704  23.292 1.00 7.42  ? 71  HIS   A N   1 
ATOM   518  C  CA  . HIS   A 1 65  ? 12.621 -5.577  21.822 1.00 7.06  ? 71  HIS   A CA  1 
ATOM   519  C  C   . HIS   A 1 65  ? 11.139 -5.844  21.495 1.00 6.57  ? 71  HIS   A C   1 
ATOM   520  O  O   . HIS   A 1 65  ? 10.715 -6.994  21.588 1.00 6.24  ? 71  HIS   A O   1 
ATOM   521  C  CB  . HIS   A 1 65  ? 13.578 -6.533  21.090 1.00 7.16  ? 71  HIS   A CB  1 
ATOM   522  C  CG  . HIS   A 1 65  ? 15.030 -6.254  21.304 1.00 7.07  ? 71  HIS   A CG  1 
ATOM   523  N  ND1 . HIS   A 1 65  ? 15.790 -5.545  20.390 1.00 6.84  ? 71  HIS   A ND1 1 
ATOM   524  C  CD2 . HIS   A 1 65  ? 15.874 -6.621  22.297 1.00 6.70  ? 71  HIS   A CD2 1 
ATOM   525  C  CE1 . HIS   A 1 65  ? 17.029 -5.443  20.823 1.00 6.75  ? 71  HIS   A CE1 1 
ATOM   526  N  NE2 . HIS   A 1 65  ? 17.108 -6.108  21.991 1.00 6.95  ? 71  HIS   A NE2 1 
ATOM   527  N  N   . TYR   A 1 66  ? 10.386 -4.809  21.111 1.00 6.00  ? 72  TYR   A N   1 
ATOM   528  C  CA  . TYR   A 1 66  ? 8.914  -4.858  20.977 1.00 6.06  ? 72  TYR   A CA  1 
ATOM   529  C  C   . TYR   A 1 66  ? 8.537  -4.905  19.505 1.00 5.88  ? 72  TYR   A C   1 
ATOM   530  O  O   . TYR   A 1 66  ? 8.934  -4.032  18.734 1.00 5.24  ? 72  TYR   A O   1 
ATOM   531  C  CB  . TYR   A 1 66  ? 8.252  -3.610  21.560 1.00 5.98  ? 72  TYR   A CB  1 
ATOM   532  C  CG  . TYR   A 1 66  ? 8.301  -3.513  23.054 1.00 6.17  ? 72  TYR   A CG  1 
ATOM   533  C  CD1 . TYR   A 1 66  ? 7.635  -4.428  23.857 1.00 6.28  ? 72  TYR   A CD1 1 
ATOM   534  C  CD2 . TYR   A 1 66  ? 9.021  -2.501  23.671 1.00 6.17  ? 72  TYR   A CD2 1 
ATOM   535  C  CE1 . TYR   A 1 66  ? 7.678  -4.339  25.241 1.00 6.22  ? 72  TYR   A CE1 1 
ATOM   536  C  CE2 . TYR   A 1 66  ? 9.049  -2.383  25.048 1.00 6.04  ? 72  TYR   A CE2 1 
ATOM   537  C  CZ  . TYR   A 1 66  ? 8.383  -3.302  25.834 1.00 6.30  ? 72  TYR   A CZ  1 
ATOM   538  O  OH  . TYR   A 1 66  ? 8.462  -3.169  27.190 1.00 6.47  ? 72  TYR   A OH  1 
ATOM   539  N  N   . PRO   A 1 67  ? 7.747  -5.916  19.090 1.00 5.96  ? 73  PRO   A N   1 
ATOM   540  C  CA  . PRO   A 1 67  ? 7.223  -5.966  17.724 1.00 6.06  ? 73  PRO   A CA  1 
ATOM   541  C  C   . PRO   A 1 67  ? 6.053  -4.976  17.589 1.00 6.02  ? 73  PRO   A C   1 
ATOM   542  O  O   . PRO   A 1 67  ? 5.268  -4.913  18.494 1.00 6.02  ? 73  PRO   A O   1 
ATOM   543  C  CB  . PRO   A 1 67  ? 6.781  -7.431  17.539 1.00 6.12  ? 73  PRO   A CB  1 
ATOM   544  C  CG  . PRO   A 1 67  ? 6.592  -7.994  18.946 1.00 6.25  ? 73  PRO   A CG  1 
ATOM   545  C  CD  . PRO   A 1 67  ? 7.386  -7.103  19.895 1.00 6.23  ? 73  PRO   A CD  1 
ATOM   546  N  N   . VAL   A 1 68  ? 6.008  -4.193  16.507 1.00 5.80  ? 74  VAL   A N   1 
ATOM   547  C  CA  . VAL   A 1 68  ? 5.029  -3.077  16.312 1.00 5.65  ? 74  VAL   A CA  1 
ATOM   548  C  C   . VAL   A 1 68  ? 4.602  -3.000  14.841 1.00 5.44  ? 74  VAL   A C   1 
ATOM   549  O  O   . VAL   A 1 68  ? 5.406  -3.341  13.936 1.00 4.93  ? 74  VAL   A O   1 
ATOM   550  C  CB  . VAL   A 1 68  ? 5.578  -1.691  16.733 1.00 5.63  ? 74  VAL   A CB  1 
ATOM   551  C  CG1 . VAL   A 1 68  ? 5.734  -1.574  18.242 1.00 5.82  ? 74  VAL   A CG1 1 
ATOM   552  C  CG2 . VAL   A 1 68  ? 6.886  -1.357  16.053 1.00 5.88  ? 74  VAL   A CG2 1 
ATOM   553  N  N   . SER   A 1 69  ? 3.384  -2.492  14.644 1.00 5.47  ? 75  SER   A N   1 
ATOM   554  C  CA  . SER   A 1 69  ? 2.908  -1.870  13.379 1.00 5.70  ? 75  SER   A CA  1 
ATOM   555  C  C   . SER   A 1 69  ? 3.142  -0.358  13.452 1.00 5.46  ? 75  SER   A C   1 
ATOM   556  O  O   . SER   A 1 69  ? 2.937  0.226   14.504 1.00 5.39  ? 75  SER   A O   1 
ATOM   557  C  CB  . SER   A 1 69  ? 1.445  -2.168  13.141 1.00 5.85  ? 75  SER   A CB  1 
ATOM   558  O  OG  . SER   A 1 69  ? 1.147  -3.528  13.326 1.00 6.63  ? 75  SER   A OG  1 
ATOM   559  N  N   . PHE   A 1 70  ? 3.543  0.277   12.358 1.00 5.69  ? 76  PHE   A N   1 
ATOM   560  C  CA  . PHE   A 1 70  ? 3.823  1.736   12.342 1.00 5.92  ? 76  PHE   A CA  1 
ATOM   561  C  C   . PHE   A 1 70  ? 3.246  2.329   11.061 1.00 6.52  ? 76  PHE   A C   1 
ATOM   562  O  O   . PHE   A 1 70  ? 3.077  1.605   10.082 1.00 6.69  ? 76  PHE   A O   1 
ATOM   563  C  CB  . PHE   A 1 70  ? 5.324  2.007   12.502 1.00 5.73  ? 76  PHE   A CB  1 
ATOM   564  C  CG  . PHE   A 1 70  ? 6.248  1.242   11.583 1.00 5.62  ? 76  PHE   A CG  1 
ATOM   565  C  CD1 . PHE   A 1 70  ? 6.741  -0.005  11.936 1.00 5.42  ? 76  PHE   A CD1 1 
ATOM   566  C  CD2 . PHE   A 1 70  ? 6.621  1.760   10.357 1.00 5.56  ? 76  PHE   A CD2 1 
ATOM   567  C  CE1 . PHE   A 1 70  ? 7.591  -0.711  11.097 1.00 5.33  ? 76  PHE   A CE1 1 
ATOM   568  C  CE2 . PHE   A 1 70  ? 7.469  1.056   9.519  1.00 5.59  ? 76  PHE   A CE2 1 
ATOM   569  C  CZ  . PHE   A 1 70  ? 7.959  -0.179  9.892  1.00 5.45  ? 76  PHE   A CZ  1 
ATOM   570  N  N   . SER   A 1 71  ? 2.931  3.614   11.104 1.00 7.05  ? 77  SER   A N   1 
ATOM   571  C  CA  . SER   A 1 71  ? 2.383  4.383   9.971  1.00 7.95  ? 77  SER   A CA  1 
ATOM   572  C  C   . SER   A 1 71  ? 3.502  4.668   8.960  1.00 8.82  ? 77  SER   A C   1 
ATOM   573  O  O   . SER   A 1 71  ? 4.700  4.579   9.320  1.00 8.57  ? 77  SER   A O   1 
ATOM   574  C  CB  . SER   A 1 71  ? 1.747  5.643   10.484 1.00 8.02  ? 77  SER   A CB  1 
ATOM   575  O  OG  . SER   A 1 71  ? 2.685  6.408   11.230 1.00 7.92  ? 77  SER   A OG  1 
ATOM   576  N  N   . LYS   A 1 72  ? 3.131  4.951   7.716  1.00 9.83  ? 78  LYS   A N   1 
ATOM   577  C  CA  . LYS   A 1 72  ? 4.091  5.390   6.674  1.00 10.48 ? 78  LYS   A CA  1 
ATOM   578  C  C   . LYS   A 1 72  ? 4.561  6.796   7.008  1.00 10.07 ? 78  LYS   A C   1 
ATOM   579  O  O   . LYS   A 1 72  ? 3.794  7.589   7.534  1.00 9.60  ? 78  LYS   A O   1 
ATOM   580  C  CB  . LYS   A 1 72  ? 3.445  5.339   5.280  1.00 11.15 ? 78  LYS   A CB  1 
ATOM   581  C  CG  . LYS   A 1 72  ? 3.071  3.934   4.807  1.00 11.51 ? 78  LYS   A CG  1 
ATOM   582  C  CD  . LYS   A 1 72  ? 2.507  3.912   3.398  1.00 11.88 ? 78  LYS   A CD  1 
ATOM   583  C  CE  . LYS   A 1 72  ? 2.204  2.504   2.959  1.00 12.29 ? 78  LYS   A CE  1 
ATOM   584  N  NZ  . LYS   A 1 72  ? 1.928  2.398   1.502  1.00 12.87 ? 78  LYS   A NZ  1 
ATOM   585  N  N   . PRO   A 1 73  ? 5.812  7.157   6.655  1.00 9.66  ? 79  PRO   A N   1 
ATOM   586  C  CA  . PRO   A 1 73  ? 6.368  8.443   7.064  1.00 10.18 ? 79  PRO   A CA  1 
ATOM   587  C  C   . PRO   A 1 73  ? 5.528  9.638   6.572  1.00 10.10 ? 79  PRO   A C   1 
ATOM   588  O  O   . PRO   A 1 73  ? 5.067  9.613   5.457  1.00 10.43 ? 79  PRO   A O   1 
ATOM   589  C  CB  . PRO   A 1 73  ? 7.771  8.508   6.428  1.00 9.88  ? 79  PRO   A CB  1 
ATOM   590  C  CG  . PRO   A 1 73  ? 8.038  7.133   5.863  1.00 10.24 ? 79  PRO   A CG  1 
ATOM   591  C  CD  . PRO   A 1 73  ? 6.749  6.334   5.879  1.00 9.62  ? 79  PRO   A CD  1 
ATOM   592  N  N   . SER   A 1 74  ? 5.348  10.646  7.427  1.00 10.03 ? 80  SER   A N   1 
ATOM   593  C  CA  . SER   A 1 74  ? 4.498  11.831  7.136  1.00 10.74 ? 80  SER   A CA  1 
ATOM   594  C  C   . SER   A 1 74  ? 4.949  13.041  7.949  1.00 10.14 ? 80  SER   A C   1 
ATOM   595  O  O   . SER   A 1 74  ? 5.799  12.911  8.835  1.00 9.65  ? 80  SER   A O   1 
ATOM   596  C  CB  . SER   A 1 74  ? 3.032  11.580  7.407  1.00 11.01 ? 80  SER   A CB  1 
ATOM   597  O  OG  . SER   A 1 74  ? 2.719  10.205  7.393  1.00 12.50 ? 80  SER   A OG  1 
ATOM   598  N  N   . LEU   A 1 75  ? 4.359  14.182  7.626  1.00 10.19 ? 81  LEU   A N   1 
ATOM   599  C  CA  . LEU   A 1 75  ? 4.538  15.466  8.329  1.00 11.16 ? 81  LEU   A CA  1 
ATOM   600  C  C   . LEU   A 1 75  ? 3.560  15.435  9.502  1.00 11.53 ? 81  LEU   A C   1 
ATOM   601  O  O   . LEU   A 1 75  ? 2.340  15.282  9.266  1.00 11.96 ? 81  LEU   A O   1 
ATOM   602  C  CB  . LEU   A 1 75  ? 4.251  16.595  7.339  1.00 10.89 ? 81  LEU   A CB  1 
ATOM   603  C  CG  . LEU   A 1 75  ? 4.671  17.995  7.779  1.00 11.99 ? 81  LEU   A CG  1 
ATOM   604  C  CD1 . LEU   A 1 75  ? 6.180  18.096  7.955  1.00 12.17 ? 81  LEU   A CD1 1 
ATOM   605  C  CD2 . LEU   A 1 75  ? 4.191  19.049  6.785  1.00 12.07 ? 81  LEU   A CD2 1 
ATOM   606  N  N   . ILE   A 1 76  ? 4.086  15.565  10.725 0.85 11.33 ? 82  ILE   A N   1 
ATOM   607  C  CA  . ILE   A 1 76  ? 3.335  15.367  12.003 0.85 11.33 ? 82  ILE   A CA  1 
ATOM   608  C  C   . ILE   A 1 76  ? 3.689  16.506  12.963 0.85 10.95 ? 82  ILE   A C   1 
ATOM   609  O  O   . ILE   A 1 76  ? 4.893  16.721  13.192 0.85 10.77 ? 82  ILE   A O   1 
ATOM   610  C  CB  . ILE   A 1 76  ? 3.672  14.005  12.645 0.85 11.68 ? 82  ILE   A CB  1 
ATOM   611  C  CG1 . ILE   A 1 76  ? 3.614  12.842  11.646 0.85 12.02 ? 82  ILE   A CG1 1 
ATOM   612  C  CG2 . ILE   A 1 76  ? 2.793  13.764  13.866 0.85 11.51 ? 82  ILE   A CG2 1 
ATOM   613  C  CD1 . ILE   A 1 76  ? 2.220  12.473  11.205 0.85 12.28 ? 82  ILE   A CD1 1 
ATOM   614  N  N   . PHE   A 1 77  ? 2.689  17.176  13.540 0.85 10.71 ? 83  PHE   A N   1 
ATOM   615  C  CA  . PHE   A 1 77  ? 2.915  18.211  14.578 0.85 10.67 ? 83  PHE   A CA  1 
ATOM   616  C  C   . PHE   A 1 77  ? 3.358  17.522  15.870 0.85 10.29 ? 83  PHE   A C   1 
ATOM   617  O  O   . PHE   A 1 77  ? 2.622  16.645  16.344 0.85 10.51 ? 83  PHE   A O   1 
ATOM   618  C  CB  . PHE   A 1 77  ? 1.683  19.080  14.826 0.85 10.89 ? 83  PHE   A CB  1 
ATOM   619  C  CG  . PHE   A 1 77  ? 1.986  20.287  15.677 0.85 10.99 ? 83  PHE   A CG  1 
ATOM   620  C  CD1 . PHE   A 1 77  ? 2.798  21.305  15.198 0.85 10.96 ? 83  PHE   A CD1 1 
ATOM   621  C  CD2 . PHE   A 1 77  ? 1.467  20.407  16.955 0.85 11.20 ? 83  PHE   A CD2 1 
ATOM   622  C  CE1 . PHE   A 1 77  ? 3.068  22.422  15.974 0.85 11.10 ? 83  PHE   A CE1 1 
ATOM   623  C  CE2 . PHE   A 1 77  ? 1.741  21.522  17.731 0.85 11.21 ? 83  PHE   A CE2 1 
ATOM   624  C  CZ  . PHE   A 1 77  ? 2.553  22.521  17.246 0.85 11.24 ? 83  PHE   A CZ  1 
ATOM   625  N  N   . VAL   A 1 78  ? 4.519  17.930  16.398 0.85 9.89  ? 84  VAL   A N   1 
ATOM   626  C  CA  . VAL   A 1 78  ? 5.185  17.369  17.609 0.85 9.68  ? 84  VAL   A CA  1 
ATOM   627  C  C   . VAL   A 1 78  ? 5.360  18.492  18.641 0.85 9.48  ? 84  VAL   A C   1 
ATOM   628  O  O   . VAL   A 1 78  ? 5.836  19.579  18.251 0.85 9.41  ? 84  VAL   A O   1 
ATOM   629  C  CB  . VAL   A 1 78  ? 6.545  16.740  17.242 0.85 9.58  ? 84  VAL   A CB  1 
ATOM   630  C  CG1 . VAL   A 1 78  ? 7.285  16.262  18.476 0.85 9.61  ? 84  VAL   A CG1 1 
ATOM   631  C  CG2 . VAL   A 1 78  ? 6.397  15.608  16.234 0.85 9.51  ? 84  VAL   A CG2 1 
ATOM   632  N  N   . GLU   A 1 79  ? 5.020  18.229  19.906 0.85 9.16  ? 85  GLU   A N   1 
ATOM   633  C  CA  . GLU   A 1 79  ? 5.107  19.218  21.016 0.85 9.38  ? 85  GLU   A CA  1 
ATOM   634  C  C   . GLU   A 1 79  ? 6.574  19.502  21.369 0.85 9.24  ? 85  GLU   A C   1 
ATOM   635  O  O   . GLU   A 1 79  ? 7.457  18.696  21.003 0.85 9.14  ? 85  GLU   A O   1 
ATOM   636  C  CB  . GLU   A 1 79  ? 4.353  18.733  22.255 0.85 9.71  ? 85  GLU   A CB  1 
ATOM   637  C  CG  . GLU   A 1 79  ? 2.844  18.742  22.097 0.85 9.87  ? 85  GLU   A CG  1 
ATOM   638  C  CD  . GLU   A 1 79  ? 2.227  20.092  21.758 0.85 10.21 ? 85  GLU   A CD  1 
ATOM   639  O  OE1 . GLU   A 1 79  ? 2.799  21.138  22.149 0.85 10.49 ? 85  GLU   A OE1 1 
ATOM   640  O  OE2 . GLU   A 1 79  ? 1.183  20.097  21.095 0.85 10.98 ? 85  GLU   A OE2 1 
ATOM   641  N  N   . ALA   A 1 80  ? 6.812  20.608  22.076 0.85 8.97  ? 86  ALA   A N   1 
ATOM   642  C  CA  . ALA   A 1 80  ? 8.152  21.104  22.464 0.85 8.95  ? 86  ALA   A CA  1 
ATOM   643  C  C   . ALA   A 1 80  ? 8.900  20.062  23.306 0.85 8.96  ? 86  ALA   A C   1 
ATOM   644  O  O   . ALA   A 1 80  ? 8.257  19.264  24.010 0.85 9.08  ? 86  ALA   A O   1 
ATOM   645  C  CB  . ALA   A 1 80  ? 8.024  22.405  23.216 0.85 8.80  ? 86  ALA   A CB  1 
ATOM   646  N  N   . SER   A 1 81  ? 10.228 20.096  23.230 0.85 8.88  ? 87  SER   A N   1 
ATOM   647  C  CA  . SER   A 1 81  ? 11.166 19.359  24.116 0.85 8.95  ? 87  SER   A CA  1 
ATOM   648  C  C   . SER   A 1 81  ? 12.284 20.313  24.547 0.85 9.14  ? 87  SER   A C   1 
ATOM   649  O  O   . SER   A 1 81  ? 12.218 21.503  24.154 0.85 9.01  ? 87  SER   A O   1 
ATOM   650  C  CB  . SER   A 1 81  ? 11.725 18.150  23.413 0.85 8.75  ? 87  SER   A CB  1 
ATOM   651  O  OG  . SER   A 1 81  ? 12.625 18.533  22.384 0.85 8.60  ? 87  SER   A OG  1 
ATOM   652  N  N   . GLU   A 1 82  ? 13.257 19.792  25.307 0.85 9.46  ? 88  GLU   A N   1 
ATOM   653  C  CA  . GLU   A 1 82  ? 14.587 20.399  25.600 0.85 9.80  ? 88  GLU   A CA  1 
ATOM   654  C  C   . GLU   A 1 82  ? 15.210 20.994  24.333 0.85 9.40  ? 88  GLU   A C   1 
ATOM   655  O  O   . GLU   A 1 82  ? 15.852 22.048  24.431 0.85 9.15  ? 88  GLU   A O   1 
ATOM   656  C  CB  . GLU   A 1 82  ? 15.577 19.318  26.054 0.85 10.73 ? 88  GLU   A CB  1 
ATOM   657  C  CG  . GLU   A 1 82  ? 15.737 19.143  27.554 0.85 11.40 ? 88  GLU   A CG  1 
ATOM   658  C  CD  . GLU   A 1 82  ? 17.065 18.494  27.921 0.85 11.85 ? 88  GLU   A CD  1 
ATOM   659  O  OE1 . GLU   A 1 82  ? 17.069 17.319  28.354 0.85 12.10 ? 88  GLU   A OE1 1 
ATOM   660  O  OE2 . GLU   A 1 82  ? 18.107 19.168  27.758 0.85 13.21 ? 88  GLU   A OE2 1 
ATOM   661  N  N   . TYR   A 1 83  ? 15.048 20.290  23.207 0.85 8.72  ? 89  TYR   A N   1 
ATOM   662  C  CA  . TYR   A 1 83  ? 15.918 20.345  22.006 0.85 8.49  ? 89  TYR   A CA  1 
ATOM   663  C  C   . TYR   A 1 83  ? 15.258 21.103  20.852 0.85 8.11  ? 89  TYR   A C   1 
ATOM   664  O  O   . TYR   A 1 83  ? 16.005 21.683  20.057 0.85 8.00  ? 89  TYR   A O   1 
ATOM   665  C  CB  . TYR   A 1 83  ? 16.280 18.919  21.586 0.85 8.52  ? 89  TYR   A CB  1 
ATOM   666  C  CG  . TYR   A 1 83  ? 17.016 18.142  22.646 0.85 8.67  ? 89  TYR   A CG  1 
ATOM   667  C  CD1 . TYR   A 1 83  ? 18.372 18.335  22.845 0.85 8.67  ? 89  TYR   A CD1 1 
ATOM   668  C  CD2 . TYR   A 1 83  ? 16.358 17.242  23.468 0.85 8.68  ? 89  TYR   A CD2 1 
ATOM   669  C  CE1 . TYR   A 1 83  ? 19.065 17.640  23.823 0.85 8.84  ? 89  TYR   A CE1 1 
ATOM   670  C  CE2 . TYR   A 1 83  ? 17.037 16.526  24.440 0.85 8.78  ? 89  TYR   A CE2 1 
ATOM   671  C  CZ  . TYR   A 1 83  ? 18.394 16.739  24.627 0.85 8.92  ? 89  TYR   A CZ  1 
ATOM   672  O  OH  . TYR   A 1 83  ? 19.091 16.048  25.578 0.85 9.38  ? 89  TYR   A OH  1 
ATOM   673  N  N   . TYR   A 1 84  ? 13.925 21.066  20.738 0.85 7.90  ? 90  TYR   A N   1 
ATOM   674  C  CA  . TYR   A 1 84  ? 13.151 21.747  19.666 0.85 8.00  ? 90  TYR   A CA  1 
ATOM   675  C  C   . TYR   A 1 84  ? 11.903 22.402  20.249 0.85 8.19  ? 90  TYR   A C   1 
ATOM   676  O  O   . TYR   A 1 84  ? 11.276 21.849  21.146 0.85 8.03  ? 90  TYR   A O   1 
ATOM   677  C  CB  . TYR   A 1 84  ? 12.705 20.760  18.586 0.85 7.82  ? 90  TYR   A CB  1 
ATOM   678  C  CG  . TYR   A 1 84  ? 13.804 20.027  17.858 0.85 7.78  ? 90  TYR   A CG  1 
ATOM   679  C  CD1 . TYR   A 1 84  ? 14.387 20.553  16.716 0.85 7.71  ? 90  TYR   A CD1 1 
ATOM   680  C  CD2 . TYR   A 1 84  ? 14.226 18.774  18.276 0.85 7.75  ? 90  TYR   A CD2 1 
ATOM   681  C  CE1 . TYR   A 1 84  ? 15.380 19.874  16.031 0.85 7.61  ? 90  TYR   A CE1 1 
ATOM   682  C  CE2 . TYR   A 1 84  ? 15.228 18.086  17.605 0.85 7.78  ? 90  TYR   A CE2 1 
ATOM   683  C  CZ  . TYR   A 1 84  ? 15.801 18.630  16.468 0.85 7.65  ? 90  TYR   A CZ  1 
ATOM   684  O  OH  . TYR   A 1 84  ? 16.779 17.949  15.799 0.85 7.35  ? 90  TYR   A OH  1 
ATOM   685  N  N   . PRO   A 1 85  ? 11.455 23.563  19.712 0.85 8.42  ? 91  PRO   A N   1 
ATOM   686  C  CA  . PRO   A 1 85  ? 10.137 24.098  20.059 0.85 8.54  ? 91  PRO   A CA  1 
ATOM   687  C  C   . PRO   A 1 85  ? 9.035  23.237  19.423 0.85 8.50  ? 91  PRO   A C   1 
ATOM   688  O  O   . PRO   A 1 85  ? 9.354  22.434  18.555 0.85 8.08  ? 91  PRO   A O   1 
ATOM   689  C  CB  . PRO   A 1 85  ? 10.168 25.514  19.455 0.85 8.48  ? 91  PRO   A CB  1 
ATOM   690  C  CG  . PRO   A 1 85  ? 11.075 25.369  18.255 0.85 8.38  ? 91  PRO   A CG  1 
ATOM   691  C  CD  . PRO   A 1 85  ? 12.148 24.390  18.707 0.85 8.46  ? 91  PRO   A CD  1 
ATOM   692  N  N   . ALA   A 1 86  ? 7.775  23.422  19.834 0.85 8.82  ? 92  ALA   A N   1 
ATOM   693  C  CA  . ALA   A 1 86  ? 6.618  22.739  19.206 0.85 9.02  ? 92  ALA   A CA  1 
ATOM   694  C  C   . ALA   A 1 86  ? 6.672  23.020  17.701 0.85 9.28  ? 92  ALA   A C   1 
ATOM   695  O  O   . ALA   A 1 86  ? 6.810  24.213  17.322 0.85 9.31  ? 92  ALA   A O   1 
ATOM   696  C  CB  . ALA   A 1 86  ? 5.315  23.179  19.829 0.85 9.10  ? 92  ALA   A CB  1 
ATOM   697  N  N   . ARG   A 1 87  ? 6.614  21.969  16.874 0.85 9.40  ? 93  ARG   A N   1 
ATOM   698  C  CA  . ARG   A 1 87  ? 6.776  22.098  15.405 0.85 9.55  ? 93  ARG   A CA  1 
ATOM   699  C  C   . ARG   A 1 87  ? 6.278  20.862  14.661 0.85 9.79  ? 93  ARG   A C   1 
ATOM   700  O  O   . ARG   A 1 87  ? 6.025  19.817  15.295 0.85 9.91  ? 93  ARG   A O   1 
ATOM   701  C  CB  . ARG   A 1 87  ? 8.258  22.259  15.053 0.85 9.89  ? 93  ARG   A CB  1 
ATOM   702  C  CG  . ARG   A 1 87  ? 9.039  20.953  15.145 0.85 10.06 ? 93  ARG   A CG  1 
ATOM   703  C  CD  . ARG   A 1 87  ? 10.475 21.115  15.599 0.85 10.10 ? 93  ARG   A CD  1 
ATOM   704  N  NE  . ARG   A 1 87  ? 11.361 20.146  14.960 0.85 10.10 ? 93  ARG   A NE  1 
ATOM   705  C  CZ  . ARG   A 1 87  ? 11.309 18.822  15.124 0.85 10.13 ? 93  ARG   A CZ  1 
ATOM   706  N  NH1 . ARG   A 1 87  ? 10.408 18.266  15.918 0.85 10.07 ? 93  ARG   A NH1 1 
ATOM   707  N  NH2 . ARG   A 1 87  ? 12.173 18.050  14.488 0.85 10.14 ? 93  ARG   A NH2 1 
ATOM   708  N  N   . TYR   A 1 88  ? 6.230  20.996  13.337 1.00 10.25 ? 94  TYR   A N   1 
ATOM   709  C  CA  . TYR   A 1 88  ? 5.968  19.893  12.375 1.00 9.89  ? 94  TYR   A CA  1 
ATOM   710  C  C   . TYR   A 1 88  ? 7.285  19.151  12.049 1.00 8.91  ? 94  TYR   A C   1 
ATOM   711  O  O   . TYR   A 1 88  ? 8.200  19.747  11.470 1.00 8.53  ? 94  TYR   A O   1 
ATOM   712  C  CB  . TYR   A 1 88  ? 5.344  20.435  11.083 1.00 10.57 ? 94  TYR   A CB  1 
ATOM   713  C  CG  . TYR   A 1 88  ? 3.912  20.845  11.264 1.00 11.26 ? 94  TYR   A CG  1 
ATOM   714  C  CD1 . TYR   A 1 88  ? 2.894  19.929  11.109 1.00 11.81 ? 94  TYR   A CD1 1 
ATOM   715  C  CD2 . TYR   A 1 88  ? 3.577  22.126  11.671 1.00 11.65 ? 94  TYR   A CD2 1 
ATOM   716  C  CE1 . TYR   A 1 88  ? 1.570  20.287  11.307 1.00 12.30 ? 94  TYR   A CE1 1 
ATOM   717  C  CE2 . TYR   A 1 88  ? 2.260  22.505  11.866 1.00 12.50 ? 94  TYR   A CE2 1 
ATOM   718  C  CZ  . TYR   A 1 88  ? 1.248  21.583  11.670 1.00 12.26 ? 94  TYR   A CZ  1 
ATOM   719  O  OH  . TYR   A 1 88  ? -0.050 21.942  11.859 1.00 13.11 ? 94  TYR   A OH  1 
ATOM   720  N  N   . GLN   A 1 89  ? 7.365  17.872  12.429 0.85 8.57  ? 95  GLN   A N   1 
ATOM   721  C  CA  . GLN   A 1 89  ? 8.488  16.960  12.089 0.85 8.54  ? 95  GLN   A CA  1 
ATOM   722  C  C   . GLN   A 1 89  ? 8.104  16.140  10.854 0.85 8.51  ? 95  GLN   A C   1 
ATOM   723  O  O   . GLN   A 1 89  ? 6.983  15.568  10.848 0.85 8.74  ? 95  GLN   A O   1 
ATOM   724  C  CB  . GLN   A 1 89  ? 8.827  16.036  13.260 0.85 8.37  ? 95  GLN   A CB  1 
ATOM   725  C  CG  . GLN   A 1 89  ? 9.982  15.091  12.952 0.85 8.36  ? 95  GLN   A CG  1 
ATOM   726  C  CD  . GLN   A 1 89  ? 10.769 14.675  14.171 0.85 8.02  ? 95  GLN   A CD  1 
ATOM   727  O  OE1 . GLN   A 1 89  ? 10.833 15.390  15.169 0.85 8.03  ? 95  GLN   A OE1 1 
ATOM   728  N  NE2 . GLN   A 1 89  ? 11.392 13.510  14.091 0.85 7.95  ? 95  GLN   A NE2 1 
ATOM   729  N  N   . SER   A 1 90  ? 9.005  16.082  9.861  1.00 8.48  ? 96  SER   A N   1 
ATOM   730  C  CA  . SER   A 1 90  ? 8.760  15.414  8.552  1.00 8.36  ? 96  SER   A CA  1 
ATOM   731  C  C   . SER   A 1 90  ? 9.338  13.997  8.565  1.00 7.88  ? 96  SER   A C   1 
ATOM   732  O  O   . SER   A 1 90  ? 10.297 13.739  9.326  1.00 7.95  ? 96  SER   A O   1 
ATOM   733  C  CB  . SER   A 1 90  ? 9.328  16.243  7.409  1.00 8.49  ? 96  SER   A CB  1 
ATOM   734  O  OG  . SER   A 1 90  ? 10.751 16.287  7.473  1.00 8.81  ? 96  SER   A OG  1 
ATOM   735  N  N   . HIS   A 1 91  ? 8.770  13.109  7.754  1.00 7.22  ? 97  HIS   A N   1 
ATOM   736  C  CA  . HIS   A 1 91  ? 9.292  11.733  7.546  1.00 7.08  ? 97  HIS   A CA  1 
ATOM   737  C  C   . HIS   A 1 91  ? 9.218  10.958  8.866  1.00 7.06  ? 97  HIS   A C   1 
ATOM   738  O  O   . HIS   A 1 91  ? 10.153 10.190  9.131  1.00 6.76  ? 97  HIS   A O   1 
ATOM   739  C  CB  . HIS   A 1 91  ? 10.728 11.799  6.985  1.00 7.08  ? 97  HIS   A CB  1 
ATOM   740  C  CG  . HIS   A 1 91  ? 10.863 12.473  5.656  1.00 7.19  ? 97  HIS   A CG  1 
ATOM   741  N  ND1 . HIS   A 1 91  ? 11.016 11.761  4.467  1.00 7.35  ? 97  HIS   A ND1 1 
ATOM   742  C  CD2 . HIS   A 1 91  ? 10.958 13.775  5.324  1.00 7.22  ? 97  HIS   A CD2 1 
ATOM   743  C  CE1 . HIS   A 1 91  ? 11.120 12.614  3.463  1.00 7.00  ? 97  HIS   A CE1 1 
ATOM   744  N  NE2 . HIS   A 1 91  ? 11.086 13.849  3.961  1.00 6.89  ? 97  HIS   A NE2 1 
ATOM   745  N  N   . LEU   A 1 92  ? 8.153  11.161  9.652  1.00 7.14  ? 98  LEU   A N   1 
ATOM   746  C  CA  . LEU   A 1 92  ? 7.953  10.570  11.007 1.00 7.48  ? 98  LEU   A CA  1 
ATOM   747  C  C   . LEU   A 1 92  ? 6.927  9.433   10.938 1.00 7.87  ? 98  LEU   A C   1 
ATOM   748  O  O   . LEU   A 1 92  ? 5.824  9.651   10.399 1.00 8.68  ? 98  LEU   A O   1 
ATOM   749  C  CB  . LEU   A 1 92  ? 7.508  11.662  11.988 1.00 7.42  ? 98  LEU   A CB  1 
ATOM   750  C  CG  . LEU   A 1 92  ? 7.304  11.210  13.436 1.00 7.62  ? 98  LEU   A CG  1 
ATOM   751  C  CD1 . LEU   A 1 92  ? 8.568  10.543  13.927 1.00 7.59  ? 98  LEU   A CD1 1 
ATOM   752  C  CD2 . LEU   A 1 92  ? 6.917  12.360  14.361 1.00 7.53  ? 98  LEU   A CD2 1 
ATOM   753  N  N   . MET   A 1 93  ? 7.275  8.270   11.500 1.00 8.02  ? 99  MET   A N   1 
ATOM   754  C  CA  . MET   A 1 93  ? 6.434  7.052   11.577 1.00 7.99  ? 99  MET   A CA  1 
ATOM   755  C  C   . MET   A 1 93  ? 6.000  6.824   13.036 1.00 7.85  ? 99  MET   A C   1 
ATOM   756  O  O   . MET   A 1 93  ? 6.890  6.692   13.898 1.00 7.84  ? 99  MET   A O   1 
ATOM   757  C  CB  . MET   A 1 93  ? 7.223  5.843   11.075 1.00 8.16  ? 99  MET   A CB  1 
ATOM   758  C  CG  . MET   A 1 93  ? 7.695  5.969   9.633  1.00 8.60  ? 99  MET   A CG  1 
ATOM   759  S  SD  . MET   A 1 93  ? 8.801  4.618   9.160  1.00 9.85  ? 99  MET   A SD  1 
ATOM   760  C  CE  . MET   A 1 93  ? 10.277 5.019   10.091 1.00 9.81  ? 99  MET   A CE  1 
ATOM   761  N  N   . LEU   A 1 94  ? 4.689  6.771   13.339 1.00 7.42  ? 100 LEU   A N   1 
ATOM   762  C  CA  . LEU   A 1 94  ? 4.195  6.471   14.722 1.00 7.70  ? 100 LEU   A CA  1 
ATOM   763  C  C   . LEU   A 1 94  ? 3.783  4.989   14.906 1.00 7.79  ? 100 LEU   A C   1 
ATOM   764  O  O   . LEU   A 1 94  ? 3.285  4.342   13.925 1.00 7.90  ? 100 LEU   A O   1 
ATOM   765  C  CB  . LEU   A 1 94  ? 2.981  7.330   15.063 1.00 7.60  ? 100 LEU   A CB  1 
ATOM   766  C  CG  . LEU   A 1 94  ? 3.114  8.848   14.972 1.00 8.00  ? 100 LEU   A CG  1 
ATOM   767  C  CD1 . LEU   A 1 94  ? 1.825  9.488   15.468 1.00 8.26  ? 100 LEU   A CD1 1 
ATOM   768  C  CD2 . LEU   A 1 94  ? 4.300  9.397   15.749 1.00 8.11  ? 100 LEU   A CD2 1 
ATOM   769  N  N   . ALA   A 1 95  ? 3.957  4.495   16.138 1.00 7.29  ? 101 ALA   A N   1 
ATOM   770  C  CA  . ALA   A 1 95  ? 3.505  3.179   16.635 1.00 7.10  ? 101 ALA   A CA  1 
ATOM   771  C  C   . ALA   A 1 95  ? 2.962  3.315   18.061 1.00 6.72  ? 101 ALA   A C   1 
ATOM   772  O  O   . ALA   A 1 95  ? 3.300  4.312   18.764 1.00 6.27  ? 101 ALA   A O   1 
ATOM   773  C  CB  . ALA   A 1 95  ? 4.643  2.182   16.593 1.00 7.21  ? 101 ALA   A CB  1 
ATOM   774  N  N   . VAL   A 1 96  ? 2.129  2.352   18.468 1.00 6.39  ? 102 VAL   A N   1 
ATOM   775  C  CA  . VAL   A 1 96  ? 1.650  2.180   19.864 1.00 6.26  ? 102 VAL   A CA  1 
ATOM   776  C  C   . VAL   A 1 96  ? 2.747  1.448   20.643 1.00 6.35  ? 102 VAL   A C   1 
ATOM   777  O  O   . VAL   A 1 96  ? 2.996  0.232   20.383 1.00 6.57  ? 102 VAL   A O   1 
ATOM   778  C  CB  . VAL   A 1 96  ? 0.279  1.488   19.933 1.00 6.37  ? 102 VAL   A CB  1 
ATOM   779  C  CG1 . VAL   A 1 96  ? -0.221 1.358   21.381 1.00 6.29  ? 102 VAL   A CG1 1 
ATOM   780  C  CG2 . VAL   A 1 96  ? -0.729 2.249   19.082 1.00 6.43  ? 102 VAL   A CG2 1 
ATOM   781  N  N   . GLY   A 1 97  ? 3.436  2.183   21.517 1.00 6.09  ? 103 GLY   A N   1 
ATOM   782  C  CA  . GLY   A 1 97  ? 4.521  1.583   22.311 1.00 6.25  ? 103 GLY   A CA  1 
ATOM   783  C  C   . GLY   A 1 97  ? 4.998  2.473   23.435 1.00 6.15  ? 103 GLY   A C   1 
ATOM   784  O  O   . GLY   A 1 97  ? 4.706  3.669   23.404 1.00 6.09  ? 103 GLY   A O   1 
ATOM   785  N  N   . HIS   A 1 98  ? 5.764  1.908   24.375 1.00 6.24  ? 104 HIS   A N   1 
ATOM   786  C  CA  . HIS   A 1 98  ? 6.440  2.704   25.433 1.00 6.55  ? 104 HIS   A CA  1 
ATOM   787  C  C   . HIS   A 1 98  ? 7.731  3.341   24.900 1.00 6.42  ? 104 HIS   A C   1 
ATOM   788  O  O   . HIS   A 1 98  ? 8.506  2.678   24.177 1.00 6.36  ? 104 HIS   A O   1 
ATOM   789  C  CB  . HIS   A 1 98  ? 6.746  1.856   26.687 1.00 6.94  ? 104 HIS   A CB  1 
ATOM   790  C  CG  . HIS   A 1 98  ? 7.468  2.639   27.734 1.00 7.41  ? 104 HIS   A CG  1 
ATOM   791  N  ND1 . HIS   A 1 98  ? 6.843  3.608   28.490 1.00 7.87  ? 104 HIS   A ND1 1 
ATOM   792  C  CD2 . HIS   A 1 98  ? 8.765  2.682   28.082 1.00 7.88  ? 104 HIS   A CD2 1 
ATOM   793  C  CE1 . HIS   A 1 98  ? 7.726  4.179   29.297 1.00 8.08  ? 104 HIS   A CE1 1 
ATOM   794  N  NE2 . HIS   A 1 98  ? 8.919  3.645   29.055 1.00 7.87  ? 104 HIS   A NE2 1 
ATOM   795  N  N   A SER   A 1 99  ? 7.963  4.601   25.267 0.45 6.29  ? 105 SER   A N   1 
ATOM   796  N  N   B SER   A 1 99  ? 7.976  4.582   25.315 0.40 6.58  ? 105 SER   A N   1 
ATOM   797  C  CA  A SER   A 1 99  ? 9.225  5.332   24.993 0.45 6.19  ? 105 SER   A CA  1 
ATOM   798  C  CA  B SER   A 1 99  ? 9.207  5.339   24.994 0.40 6.65  ? 105 SER   A CA  1 
ATOM   799  C  C   A SER   A 1 99  ? 9.407  6.450   26.025 0.45 6.36  ? 105 SER   A C   1 
ATOM   800  C  C   B SER   A 1 99  ? 9.402  6.469   26.011 0.40 6.63  ? 105 SER   A C   1 
ATOM   801  O  O   A SER   A 1 99  ? 8.399  6.911   26.584 0.45 6.36  ? 105 SER   A O   1 
ATOM   802  O  O   B SER   A 1 99  ? 8.395  6.960   26.547 0.40 6.60  ? 105 SER   A O   1 
ATOM   803  C  CB  A SER   A 1 99  ? 9.245  5.864   23.583 0.45 5.99  ? 105 SER   A CB  1 
ATOM   804  C  CB  B SER   A 1 99  ? 9.137  5.851   23.585 0.40 6.76  ? 105 SER   A CB  1 
ATOM   805  O  OG  A SER   A 1 99  ? 8.305  6.917   23.420 0.45 5.57  ? 105 SER   A OG  1 
ATOM   806  O  OG  B SER   A 1 99  ? 10.387 5.702   22.946 0.40 7.01  ? 105 SER   A OG  1 
ATOM   807  N  N   . GLU   A 1 100 ? 10.660 6.846   26.247 1.00 6.56  ? 106 GLU   A N   1 
ATOM   808  C  CA  . GLU   A 1 100 ? 11.056 7.998   27.106 1.00 7.02  ? 106 GLU   A CA  1 
ATOM   809  C  C   . GLU   A 1 100 ? 12.138 8.744   26.325 1.00 6.79  ? 106 GLU   A C   1 
ATOM   810  O  O   . GLU   A 1 100 ? 12.656 8.190   25.370 1.00 6.39  ? 106 GLU   A O   1 
ATOM   811  C  CB  . GLU   A 1 100 ? 11.537 7.475   28.468 1.00 7.37  ? 106 GLU   A CB  1 
ATOM   812  C  CG  . GLU   A 1 100 ? 10.468 6.699   29.208 1.00 7.96  ? 106 GLU   A CG  1 
ATOM   813  C  CD  . GLU   A 1 100 ? 10.874 6.073   30.533 1.00 8.91  ? 106 GLU   A CD  1 
ATOM   814  O  OE1 . GLU   A 1 100 ? 11.756 6.636   31.211 1.00 10.36 ? 106 GLU   A OE1 1 
ATOM   815  O  OE2 . GLU   A 1 100 ? 10.328 5.015   30.878 1.00 9.82  ? 106 GLU   A OE2 1 
ATOM   816  N  N   . PRO   A 1 101 ? 12.483 10.017  26.654 1.00 6.82  ? 107 PRO   A N   1 
ATOM   817  C  CA  . PRO   A 1 101 ? 13.504 10.752  25.903 1.00 6.70  ? 107 PRO   A CA  1 
ATOM   818  C  C   . PRO   A 1 101 ? 14.801 9.977   25.601 1.00 6.30  ? 107 PRO   A C   1 
ATOM   819  O  O   . PRO   A 1 101 ? 15.236 10.004  24.468 1.00 6.18  ? 107 PRO   A O   1 
ATOM   820  C  CB  . PRO   A 1 101 ? 13.795 11.949  26.821 1.00 6.64  ? 107 PRO   A CB  1 
ATOM   821  C  CG  . PRO   A 1 101 ? 12.466 12.224  27.488 1.00 6.86  ? 107 PRO   A CG  1 
ATOM   822  C  CD  . PRO   A 1 101 ? 11.843 10.858  27.697 1.00 6.88  ? 107 PRO   A CD  1 
ATOM   823  N  N   . GLY   A 1 102 ? 15.382 9.320   26.609 1.00 6.21  ? 108 GLY   A N   1 
ATOM   824  C  CA  . GLY   A 1 102 ? 16.659 8.588   26.485 1.00 6.19  ? 108 GLY   A CA  1 
ATOM   825  C  C   . GLY   A 1 102 ? 16.566 7.373   25.562 1.00 6.09  ? 108 GLY   A C   1 
ATOM   826  O  O   . GLY   A 1 102 ? 17.624 6.851   25.160 1.00 6.65  ? 108 GLY   A O   1 
ATOM   827  N  N   . ASP   A 1 103 ? 15.355 6.943   25.200 1.00 5.88  ? 109 ASP   A N   1 
ATOM   828  C  CA  . ASP   A 1 103 ? 15.133 5.869   24.199 1.00 5.59  ? 109 ASP   A CA  1 
ATOM   829  C  C   . ASP   A 1 103 ? 15.477 6.362   22.783 1.00 5.38  ? 109 ASP   A C   1 
ATOM   830  O  O   . ASP   A 1 103 ? 15.639 5.507   21.924 1.00 5.52  ? 109 ASP   A O   1 
ATOM   831  C  CB  . ASP   A 1 103 ? 13.713 5.296   24.314 1.00 5.49  ? 109 ASP   A CB  1 
ATOM   832  C  CG  . ASP   A 1 103 ? 13.503 4.456   25.563 1.00 5.42  ? 109 ASP   A CG  1 
ATOM   833  O  OD1 . ASP   A 1 103 ? 14.443 3.766   25.948 1.00 5.17  ? 109 ASP   A OD1 1 
ATOM   834  O  OD2 . ASP   A 1 103 ? 12.386 4.502   26.141 1.00 5.47  ? 109 ASP   A OD2 1 
ATOM   835  N  N   . CYS   A 1 104 ? 15.702 7.660   22.535 1.00 5.43  ? 110 CYS   A N   1 
ATOM   836  C  CA  . CYS   A 1 104 ? 16.039 8.150   21.162 1.00 5.43  ? 110 CYS   A CA  1 
ATOM   837  C  C   . CYS   A 1 104 ? 17.337 7.456   20.679 1.00 5.54  ? 110 CYS   A C   1 
ATOM   838  O  O   . CYS   A 1 104 ? 18.301 7.293   21.489 1.00 5.70  ? 110 CYS   A O   1 
ATOM   839  C  CB  . CYS   A 1 104 ? 16.128 9.679   21.110 1.00 5.47  ? 110 CYS   A CB  1 
ATOM   840  S  SG  . CYS   A 1 104 ? 14.520 10.536  21.152 1.00 5.30  ? 110 CYS   A SG  1 
ATOM   841  N  N   . GLY   A 1 105 ? 17.373 6.999   19.432 1.00 5.37  ? 111 GLY   A N   1 
ATOM   842  C  CA  . GLY   A 1 105 ? 18.525 6.304   18.835 1.00 5.46  ? 111 GLY   A CA  1 
ATOM   843  C  C   . GLY   A 1 105 ? 18.290 4.798   18.799 1.00 5.37  ? 111 GLY   A C   1 
ATOM   844  O  O   . GLY   A 1 105 ? 19.066 4.100   18.121 1.00 5.21  ? 111 GLY   A O   1 
ATOM   845  N  N   . GLY   A 1 106 ? 17.258 4.323   19.516 1.00 5.25  ? 112 GLY   A N   1 
ATOM   846  C  CA  . GLY   A 1 106 ? 16.786 2.933   19.418 1.00 5.33  ? 112 GLY   A CA  1 
ATOM   847  C  C   . GLY   A 1 106 ? 16.418 2.619   17.979 1.00 5.47  ? 112 GLY   A C   1 
ATOM   848  O  O   . GLY   A 1 106 ? 15.813 3.490   17.328 1.00 5.51  ? 112 GLY   A O   1 
ATOM   849  N  N   . ILE   A 1 107 ? 16.811 1.453   17.466 1.00 5.68  ? 113 ILE   A N   1 
ATOM   850  C  CA  . ILE   A 1 107 ? 16.631 1.131   16.013 1.00 6.02  ? 113 ILE   A CA  1 
ATOM   851  C  C   . ILE   A 1 107 ? 15.309 0.383   15.820 1.00 6.25  ? 113 ILE   A C   1 
ATOM   852  O  O   . ILE   A 1 107 ? 15.023 -0.563  16.601 1.00 6.06  ? 113 ILE   A O   1 
ATOM   853  C  CB  . ILE   A 1 107 ? 17.854 0.361   15.452 1.00 6.00  ? 113 ILE   A CB  1 
ATOM   854  C  CG1 . ILE   A 1 107 ? 19.081 1.273   15.392 1.00 6.16  ? 113 ILE   A CG1 1 
ATOM   855  C  CG2 . ILE   A 1 107 ? 17.561 -0.262  14.097 1.00 6.02  ? 113 ILE   A CG2 1 
ATOM   856  C  CD1 . ILE   A 1 107 ? 20.378 0.593   15.056 1.00 6.22  ? 113 ILE   A CD1 1 
ATOM   857  N  N   . LEU   A 1 108 ? 14.569 0.792   14.786 1.00 6.86  ? 114 LEU   A N   1 
ATOM   858  C  CA  . LEU   A 1 108 ? 13.408 0.061   14.211 1.00 7.56  ? 114 LEU   A CA  1 
ATOM   859  C  C   . LEU   A 1 108 ? 13.879 -0.701  12.974 1.00 8.31  ? 114 LEU   A C   1 
ATOM   860  O  O   . LEU   A 1 108 ? 14.463 -0.087  12.088 1.00 7.90  ? 114 LEU   A O   1 
ATOM   861  C  CB  . LEU   A 1 108 ? 12.318 1.071   13.853 1.00 7.13  ? 114 LEU   A CB  1 
ATOM   862  C  CG  . LEU   A 1 108 ? 11.053 0.467   13.244 1.00 7.14  ? 114 LEU   A CG  1 
ATOM   863  C  CD1 . LEU   A 1 108 ? 10.178 -0.142  14.315 1.00 7.03  ? 114 LEU   A CD1 1 
ATOM   864  C  CD2 . LEU   A 1 108 ? 10.285 1.506   12.447 1.00 7.02  ? 114 LEU   A CD2 1 
ATOM   865  N  N   . ARG   A 1 109 ? 13.597 -2.008  12.927 0.50 8.63  ? 115 ARG   A N   1 
ATOM   866  C  CA  . ARG   A 1 109 ? 14.049 -2.934  11.855 0.50 9.09  ? 115 ARG   A CA  1 
ATOM   867  C  C   . ARG   A 1 109 ? 12.873 -3.785  11.363 0.50 9.12  ? 115 ARG   A C   1 
ATOM   868  O  O   . ARG   A 1 109 ? 12.006 -4.122  12.185 0.50 9.28  ? 115 ARG   A O   1 
ATOM   869  C  CB  . ARG   A 1 109 ? 15.196 -3.815  12.362 0.50 9.36  ? 115 ARG   A CB  1 
ATOM   870  C  CG  . ARG   A 1 109 ? 15.536 -3.610  13.831 0.50 9.55  ? 115 ARG   A CG  1 
ATOM   871  C  CD  . ARG   A 1 109 ? 16.410 -4.725  14.356 0.50 9.78  ? 115 ARG   A CD  1 
ATOM   872  N  NE  . ARG   A 1 109 ? 17.583 -4.840  13.508 0.50 9.99  ? 115 ARG   A NE  1 
ATOM   873  C  CZ  . ARG   A 1 109 ? 18.697 -4.129  13.658 0.50 10.13 ? 115 ARG   A CZ  1 
ATOM   874  N  NH1 . ARG   A 1 109 ? 18.802 -3.260  14.648 0.50 10.33 ? 115 ARG   A NH1 1 
ATOM   875  N  NH2 . ARG   A 1 109 ? 19.711 -4.305  12.828 0.50 10.18 ? 115 ARG   A NH2 1 
ATOM   876  N  N   . CYS   A 1 110 ? 12.856 -4.085  10.059 1.00 9.39  ? 116 CYS   A N   1 
ATOM   877  C  CA  . CYS   A 1 110 ? 11.929 -5.064  9.412  1.00 9.59  ? 116 CYS   A CA  1 
ATOM   878  C  C   . CYS   A 1 110 ? 12.789 -6.184  8.805  1.00 9.75  ? 116 CYS   A C   1 
ATOM   879  O  O   . CYS   A 1 110 ? 14.008 -6.159  8.998  1.00 10.40 ? 116 CYS   A O   1 
ATOM   880  C  CB  . CYS   A 1 110 ? 11.123 -4.403  8.295  1.00 9.71  ? 116 CYS   A CB  1 
ATOM   881  S  SG  . CYS   A 1 110 ? 12.173 -3.796  6.946  1.00 9.98  ? 116 CYS   A SG  1 
ATOM   882  N  N   . GLN   A 1 111 ? 12.181 -7.117  8.065  1.00 10.73 ? 117 GLN   A N   1 
ATOM   883  C  CA  . GLN   A 1 111 ? 12.858 -8.252  7.381  1.00 11.83 ? 117 GLN   A CA  1 
ATOM   884  C  C   . GLN   A 1 111 ? 13.937 -7.749  6.406  1.00 11.69 ? 117 GLN   A C   1 
ATOM   885  O  O   . GLN   A 1 111 ? 14.904 -8.479  6.199  1.00 12.81 ? 117 GLN   A O   1 
ATOM   886  C  CB  . GLN   A 1 111 ? 11.835 -9.146  6.660  1.00 12.28 ? 117 GLN   A CB  1 
ATOM   887  C  CG  . GLN   A 1 111 ? 11.027 -8.449  5.567  1.00 13.37 ? 117 GLN   A CG  1 
ATOM   888  C  CD  . GLN   A 1 111 ? 9.882  -9.256  4.995  1.00 14.00 ? 117 GLN   A CD  1 
ATOM   889  O  OE1 . GLN   A 1 111 ? 8.758  -9.219  5.484  1.00 14.83 ? 117 GLN   A OE1 1 
ATOM   890  N  NE2 . GLN   A 1 111 ? 10.126 -9.930  3.879  1.00 16.18 ? 117 GLN   A NE2 1 
ATOM   891  N  N   . HIS   A 1 112 ? 13.812 -6.537  5.859  1.00 11.60 ? 118 HIS   A N   1 
ATOM   892  C  CA  . HIS   A 1 112 ? 14.731 -5.993  4.822  1.00 11.33 ? 118 HIS   A CA  1 
ATOM   893  C  C   . HIS   A 1 112 ? 15.947 -5.275  5.434  1.00 10.80 ? 118 HIS   A C   1 
ATOM   894  O  O   . HIS   A 1 112 ? 16.894 -5.007  4.655  1.00 11.34 ? 118 HIS   A O   1 
ATOM   895  C  CB  . HIS   A 1 112 ? 13.960 -5.100  3.849  1.00 11.09 ? 118 HIS   A CB  1 
ATOM   896  C  CG  . HIS   A 1 112 ? 12.787 -5.780  3.221  1.00 11.67 ? 118 HIS   A CG  1 
ATOM   897  N  ND1 . HIS   A 1 112 ? 11.492 -5.576  3.668  1.00 11.67 ? 118 HIS   A ND1 1 
ATOM   898  C  CD2 . HIS   A 1 112 ? 12.692 -6.642  2.181  1.00 12.27 ? 118 HIS   A CD2 1 
ATOM   899  C  CE1 . HIS   A 1 112 ? 10.655 -6.278  2.929  1.00 12.51 ? 118 HIS   A CE1 1 
ATOM   900  N  NE2 . HIS   A 1 112 ? 11.368 -6.959  2.023  1.00 12.66 ? 118 HIS   A NE2 1 
ATOM   901  N  N   . GLY   A 1 113 ? 15.935 -4.951  6.735  1.00 9.97  ? 119 GLY   A N   1 
ATOM   902  C  CA  . GLY   A 1 113 ? 17.017 -4.201  7.404  1.00 8.86  ? 119 GLY   A CA  1 
ATOM   903  C  C   . GLY   A 1 113 ? 16.501 -3.039  8.243  1.00 8.41  ? 119 GLY   A C   1 
ATOM   904  O  O   . GLY   A 1 113 ? 15.335 -3.069  8.665  1.00 8.46  ? 119 GLY   A O   1 
ATOM   905  N  N   . VAL   A 1 114 ? 17.356 -2.035  8.473  1.00 7.32  ? 120 VAL   A N   1 
ATOM   906  C  CA  . VAL   A 1 114 ? 17.106 -0.864  9.380  1.00 6.85  ? 120 VAL   A CA  1 
ATOM   907  C  C   . VAL   A 1 114 ? 16.118 0.097   8.717  1.00 6.36  ? 120 VAL   A C   1 
ATOM   908  O  O   . VAL   A 1 114 ? 16.346 0.458   7.563  1.00 6.87  ? 120 VAL   A O   1 
ATOM   909  C  CB  . VAL   A 1 114 ? 18.432 -0.158  9.707  1.00 6.73  ? 120 VAL   A CB  1 
ATOM   910  C  CG1 . VAL   A 1 114 ? 18.242 1.156   10.451 1.00 6.53  ? 120 VAL   A CG1 1 
ATOM   911  C  CG2 . VAL   A 1 114 ? 19.345 -1.086  10.472 1.00 7.01  ? 120 VAL   A CG2 1 
ATOM   912  N  N   . VAL   A 1 115 ? 15.056 0.491   9.423  1.00 5.85  ? 121 VAL   A N   1 
ATOM   913  C  CA  . VAL   A 1 115 ? 13.968 1.378   8.913  1.00 5.47  ? 121 VAL   A CA  1 
ATOM   914  C  C   . VAL   A 1 115 ? 14.145 2.819   9.422  1.00 5.17  ? 121 VAL   A C   1 
ATOM   915  O  O   . VAL   A 1 115 ? 13.954 3.755   8.639  1.00 4.79  ? 121 VAL   A O   1 
ATOM   916  C  CB  . VAL   A 1 115 ? 12.605 0.827   9.327  1.00 5.40  ? 121 VAL   A CB  1 
ATOM   917  C  CG1 . VAL   A 1 115 ? 11.465 1.763   8.946  1.00 5.46  ? 121 VAL   A CG1 1 
ATOM   918  C  CG2 . VAL   A 1 115 ? 12.388 -0.576  8.793  1.00 5.61  ? 121 VAL   A CG2 1 
ATOM   919  N  N   . GLY   A 1 116 ? 14.434 2.978   10.713 1.00 4.92  ? 122 GLY   A N   1 
ATOM   920  C  CA  . GLY   A 1 116 ? 14.668 4.299   11.316 1.00 4.77  ? 122 GLY   A CA  1 
ATOM   921  C  C   . GLY   A 1 116 ? 15.113 4.227   12.768 1.00 4.64  ? 122 GLY   A C   1 
ATOM   922  O  O   . GLY   A 1 116 ? 15.530 3.123   13.256 1.00 4.35  ? 122 GLY   A O   1 
ATOM   923  N  N   . ILE   A 1 117 ? 15.048 5.371   13.452 1.00 4.58  ? 123 ILE   A N   1 
ATOM   924  C  CA  . ILE   A 1 117 ? 15.508 5.501   14.865 1.00 4.83  ? 123 ILE   A CA  1 
ATOM   925  C  C   . ILE   A 1 117 ? 14.448 6.257   15.676 1.00 4.85  ? 123 ILE   A C   1 
ATOM   926  O  O   . ILE   A 1 117 ? 13.875 7.191   15.131 1.00 4.71  ? 123 ILE   A O   1 
ATOM   927  C  CB  . ILE   A 1 117 ? 16.907 6.161   14.924 1.00 5.03  ? 123 ILE   A CB  1 
ATOM   928  C  CG1 . ILE   A 1 117 ? 16.958 7.510   14.215 1.00 5.06  ? 123 ILE   A CG1 1 
ATOM   929  C  CG2 . ILE   A 1 117 ? 17.991 5.246   14.376 1.00 5.21  ? 123 ILE   A CG2 1 
ATOM   930  C  CD1 . ILE   A 1 117 ? 18.179 8.325   14.638 1.00 5.25  ? 123 ILE   A CD1 1 
ATOM   931  N  N   . VAL   A 1 118 ? 14.208 5.845   16.934 1.00 4.90  ? 124 VAL   A N   1 
ATOM   932  C  CA  . VAL   A 1 118 ? 13.334 6.570   17.907 1.00 5.00  ? 124 VAL   A CA  1 
ATOM   933  C  C   . VAL   A 1 118 ? 13.743 8.046   17.941 1.00 5.21  ? 124 VAL   A C   1 
ATOM   934  O  O   . VAL   A 1 118 ? 14.952 8.353   18.131 1.00 5.26  ? 124 VAL   A O   1 
ATOM   935  C  CB  . VAL   A 1 118 ? 13.392 5.941   19.318 1.00 5.06  ? 124 VAL   A CB  1 
ATOM   936  C  CG1 . VAL   A 1 118 ? 12.687 6.772   20.388 1.00 5.09  ? 124 VAL   A CG1 1 
ATOM   937  C  CG2 . VAL   A 1 118 ? 12.872 4.523   19.335 1.00 4.97  ? 124 VAL   A CG2 1 
ATOM   938  N  N   . SER   A 1 119 ? 12.762 8.945   17.789 1.00 5.47  ? 125 SER   A N   1 
ATOM   939  C  CA  . SER   A 1 119 ? 12.937 10.419  17.796 1.00 5.76  ? 125 SER   A CA  1 
ATOM   940  C  C   . SER   A 1 119 ? 11.902 11.127  18.696 1.00 5.95  ? 125 SER   A C   1 
ATOM   941  O  O   . SER   A 1 119 ? 12.274 12.145  19.327 1.00 6.15  ? 125 SER   A O   1 
ATOM   942  C  CB  . SER   A 1 119 ? 12.911 10.921  16.390 1.00 5.70  ? 125 SER   A CB  1 
ATOM   943  O  OG  . SER   A 1 119 ? 13.028 12.327  16.344 1.00 5.71  ? 125 SER   A OG  1 
ATOM   944  N  N   . THR   A 1 120 ? 10.645 10.667  18.733 1.00 6.45  ? 126 THR   A N   1 
ATOM   945  C  CA  . THR   A 1 120 ? 9.505  11.314  19.460 1.00 6.93  ? 126 THR   A CA  1 
ATOM   946  C  C   . THR   A 1 120 ? 8.780  10.273  20.317 1.00 7.36  ? 126 THR   A C   1 
ATOM   947  O  O   . THR   A 1 120 ? 9.043  9.102   20.112 1.00 7.07  ? 126 THR   A O   1 
ATOM   948  C  CB  . THR   A 1 120 ? 8.510  11.991  18.507 1.00 6.85  ? 126 THR   A CB  1 
ATOM   949  O  OG1 . THR   A 1 120 ? 7.663  11.003  17.910 1.00 6.76  ? 126 THR   A OG1 1 
ATOM   950  C  CG2 . THR   A 1 120 ? 9.194  12.776  17.405 1.00 6.97  ? 126 THR   A CG2 1 
ATOM   951  N  N   . GLY   A 1 121 ? 7.890  10.703  21.214 1.00 8.77  ? 127 GLY   A N   1 
ATOM   952  C  CA  . GLY   A 1 121 ? 7.061  9.781   22.016 1.00 9.31  ? 127 GLY   A CA  1 
ATOM   953  C  C   . GLY   A 1 121 ? 6.251  10.430  23.127 1.00 10.64 ? 127 GLY   A C   1 
ATOM   954  O  O   . GLY   A 1 121 ? 6.256  11.687  23.235 1.00 11.12 ? 127 GLY   A O   1 
ATOM   955  N  N   . GLY   A 1 122 ? 5.576  9.574   23.907 1.00 11.93 ? 128 GLY   A N   1 
ATOM   956  C  CA  . GLY   A 1 122 ? 4.728  9.893   25.072 1.00 13.12 ? 128 GLY   A CA  1 
ATOM   957  C  C   . GLY   A 1 122 ? 3.277  9.538   24.794 1.00 13.95 ? 128 GLY   A C   1 
ATOM   958  O  O   . GLY   A 1 122 ? 2.947  9.257   23.607 1.00 13.64 ? 128 GLY   A O   1 
ATOM   959  N  N   . ASN   A 1 123 ? 2.432  9.531   25.827 1.00 15.34 ? 129 ASN   A N   1 
ATOM   960  C  CA  . ASN   A 1 123 ? 0.971  9.257   25.705 1.00 15.87 ? 129 ASN   A CA  1 
ATOM   961  C  C   . ASN   A 1 123 ? 0.771  7.864   25.085 1.00 14.00 ? 129 ASN   A C   1 
ATOM   962  O  O   . ASN   A 1 123 ? -0.229 7.686   24.348 1.00 14.30 ? 129 ASN   A O   1 
ATOM   963  C  CB  . ASN   A 1 123 ? 0.212  10.286  24.850 1.00 18.26 ? 129 ASN   A CB  1 
ATOM   964  C  CG  . ASN   A 1 123 ? 0.395  11.745  25.238 1.00 20.75 ? 129 ASN   A CG  1 
ATOM   965  O  OD1 . ASN   A 1 123 ? 1.190  12.066  26.137 1.00 23.36 ? 129 ASN   A OD1 1 
ATOM   966  N  ND2 . ASN   A 1 123 ? -0.300 12.633  24.524 1.00 20.48 ? 129 ASN   A ND2 1 
ATOM   967  N  N   . GLY   A 1 124 ? 1.700  6.926   25.327 1.00 12.23 ? 130 GLY   A N   1 
ATOM   968  C  CA  . GLY   A 1 124 ? 1.695  5.552   24.777 1.00 10.81 ? 130 GLY   A CA  1 
ATOM   969  C  C   . GLY   A 1 124 ? 2.079  5.457   23.296 1.00 9.73  ? 130 GLY   A C   1 
ATOM   970  O  O   . GLY   A 1 124 ? 1.786  4.431   22.700 1.00 9.54  ? 130 GLY   A O   1 
ATOM   971  N  N   . LEU   A 1 125 ? 2.682  6.483   22.700 1.00 9.10  ? 131 LEU   A N   1 
ATOM   972  C  CA  . LEU   A 1 125 ? 3.171  6.457   21.295 1.00 9.05  ? 131 LEU   A CA  1 
ATOM   973  C  C   . LEU   A 1 125 ? 4.707  6.464   21.254 1.00 8.08  ? 131 LEU   A C   1 
ATOM   974  O  O   . LEU   A 1 125 ? 5.364  6.878   22.248 1.00 8.79  ? 131 LEU   A O   1 
ATOM   975  C  CB  . LEU   A 1 125 ? 2.627  7.670   20.532 1.00 9.84  ? 131 LEU   A CB  1 
ATOM   976  C  CG  . LEU   A 1 125 ? 1.108  7.791   20.468 1.00 10.04 ? 131 LEU   A CG  1 
ATOM   977  C  CD1 . LEU   A 1 125 ? 0.713  9.041   19.702 1.00 10.70 ? 131 LEU   A CD1 1 
ATOM   978  C  CD2 . LEU   A 1 125 ? 0.495  6.568   19.828 1.00 10.11 ? 131 LEU   A CD2 1 
ATOM   979  N  N   . VAL   A 1 126 ? 5.269  6.000   20.146 1.00 6.77  ? 132 VAL   A N   1 
ATOM   980  C  CA  . VAL   A 1 126 ? 6.713  6.177   19.852 1.00 5.98  ? 132 VAL   A CA  1 
ATOM   981  C  C   . VAL   A 1 126 ? 6.834  6.631   18.393 1.00 5.67  ? 132 VAL   A C   1 
ATOM   982  O  O   . VAL   A 1 126 ? 6.141  6.049   17.513 1.00 4.94  ? 132 VAL   A O   1 
ATOM   983  C  CB  . VAL   A 1 126 ? 7.500  4.891   20.162 1.00 5.93  ? 132 VAL   A CB  1 
ATOM   984  C  CG1 . VAL   A 1 126 ? 6.989  3.682   19.408 1.00 6.00  ? 132 VAL   A CG1 1 
ATOM   985  C  CG2 . VAL   A 1 126 ? 8.991  5.080   19.965 1.00 5.87  ? 132 VAL   A CG2 1 
ATOM   986  N  N   . GLY   A 1 127 ? 7.659  7.651   18.153 1.00 5.27  ? 133 GLY   A N   1 
ATOM   987  C  CA  . GLY   A 1 127 ? 7.912  8.163   16.793 1.00 5.19  ? 133 GLY   A CA  1 
ATOM   988  C  C   . GLY   A 1 127 ? 9.295  7.803   16.316 1.00 5.05  ? 133 GLY   A C   1 
ATOM   989  O  O   . GLY   A 1 127 ? 10.204 7.917   17.102 1.00 5.16  ? 133 GLY   A O   1 
ATOM   990  N  N   . PHE   A 1 128 ? 9.412  7.345   15.074 1.00 5.09  ? 134 PHE   A N   1 
ATOM   991  C  CA  . PHE   A 1 128 ? 10.686 6.941   14.414 1.00 4.98  ? 134 PHE   A CA  1 
ATOM   992  C  C   . PHE   A 1 128 ? 10.934 7.889   13.245 1.00 4.93  ? 134 PHE   A C   1 
ATOM   993  O  O   . PHE   A 1 128 ? 10.008 8.137   12.503 1.00 4.91  ? 134 PHE   A O   1 
ATOM   994  C  CB  . PHE   A 1 128 ? 10.617 5.504   13.894 1.00 5.08  ? 134 PHE   A CB  1 
ATOM   995  C  CG  . PHE   A 1 128 ? 10.132 4.511   14.920 1.00 5.18  ? 134 PHE   A CG  1 
ATOM   996  C  CD1 . PHE   A 1 128 ? 11.022 3.923   15.806 1.00 5.04  ? 134 PHE   A CD1 1 
ATOM   997  C  CD2 . PHE   A 1 128 ? 8.785  4.212   15.025 1.00 5.16  ? 134 PHE   A CD2 1 
ATOM   998  C  CE1 . PHE   A 1 128 ? 10.573 3.033   16.769 1.00 5.10  ? 134 PHE   A CE1 1 
ATOM   999  C  CE2 . PHE   A 1 128 ? 8.347  3.306   15.973 1.00 5.24  ? 134 PHE   A CE2 1 
ATOM   1000 C  CZ  . PHE   A 1 128 ? 9.244  2.703   16.827 1.00 5.10  ? 134 PHE   A CZ  1 
ATOM   1001 N  N   . ALA   A 1 129 ? 12.162 8.393   13.112 1.00 4.84  ? 135 ALA   A N   1 
ATOM   1002 C  CA  . ALA   A 1 129 ? 12.630 9.126   11.921 1.00 5.03  ? 135 ALA   A CA  1 
ATOM   1003 C  C   . ALA   A 1 129 ? 13.006 8.084   10.873 1.00 5.13  ? 135 ALA   A C   1 
ATOM   1004 O  O   . ALA   A 1 129 ? 13.919 7.311   11.162 1.00 5.13  ? 135 ALA   A O   1 
ATOM   1005 C  CB  . ALA   A 1 129 ? 13.800 10.009  12.296 1.00 4.99  ? 135 ALA   A CB  1 
ATOM   1006 N  N   . ASP   A 1 130 ? 12.300 8.027   9.743  1.00 5.45  ? 136 ASP   A N   1 
ATOM   1007 C  CA  . ASP   A 1 130 ? 12.588 7.077   8.631  1.00 5.91  ? 136 ASP   A CA  1 
ATOM   1008 C  C   . ASP   A 1 130 ? 13.950 7.393   8.017  1.00 5.93  ? 136 ASP   A C   1 
ATOM   1009 O  O   . ASP   A 1 130 ? 14.257 8.574   7.897  1.00 6.14  ? 136 ASP   A O   1 
ATOM   1010 C  CB  . ASP   A 1 130 ? 11.511 7.170   7.550  1.00 6.44  ? 136 ASP   A CB  1 
ATOM   1011 C  CG  . ASP   A 1 130 ? 11.632 6.138   6.450  1.00 6.74  ? 136 ASP   A CG  1 
ATOM   1012 O  OD1 . ASP   A 1 130 ? 11.736 4.967   6.780  1.00 6.83  ? 136 ASP   A OD1 1 
ATOM   1013 O  OD2 . ASP   A 1 130 ? 11.603 6.537   5.260  1.00 7.84  ? 136 ASP   A OD2 1 
ATOM   1014 N  N   . VAL   A 1 131 ? 14.737 6.382   7.643  1.00 6.15  ? 137 VAL   A N   1 
ATOM   1015 C  CA  . VAL   A 1 131 ? 15.967 6.579   6.818  1.00 6.42  ? 137 VAL   A CA  1 
ATOM   1016 C  C   . VAL   A 1 131 ? 15.855 5.850   5.461  1.00 6.50  ? 137 VAL   A C   1 
ATOM   1017 O  O   . VAL   A 1 131 ? 16.830 5.890   4.687  1.00 6.69  ? 137 VAL   A O   1 
ATOM   1018 C  CB  . VAL   A 1 131 ? 17.231 6.129   7.587  1.00 6.24  ? 137 VAL   A CB  1 
ATOM   1019 C  CG1 . VAL   A 1 131 ? 17.427 6.900   8.893  1.00 6.42  ? 137 VAL   A CG1 1 
ATOM   1020 C  CG2 . VAL   A 1 131 ? 17.218 4.644   7.854  1.00 6.14  ? 137 VAL   A CG2 1 
ATOM   1021 N  N   . ARG   A 1 132 ? 14.758 5.155   5.155  1.00 6.59  ? 138 ARG   A N   1 
ATOM   1022 C  CA  . ARG   A 1 132 ? 14.723 4.254   3.973  1.00 6.98  ? 138 ARG   A CA  1 
ATOM   1023 C  C   . ARG   A 1 132 ? 14.769 5.050   2.659  1.00 7.50  ? 138 ARG   A C   1 
ATOM   1024 O  O   . ARG   A 1 132 ? 15.035 4.433   1.608  1.00 8.09  ? 138 ARG   A O   1 
ATOM   1025 C  CB  . ARG   A 1 132 ? 13.474 3.378   4.024  1.00 6.86  ? 138 ARG   A CB  1 
ATOM   1026 C  CG  . ARG   A 1 132 ? 13.462 2.375   5.170  1.00 6.72  ? 138 ARG   A CG  1 
ATOM   1027 C  CD  . ARG   A 1 132 ? 12.135 1.623   5.223  1.00 6.45  ? 138 ARG   A CD  1 
ATOM   1028 N  NE  . ARG   A 1 132 ? 11.059 2.469   5.691  1.00 6.22  ? 138 ARG   A NE  1 
ATOM   1029 C  CZ  . ARG   A 1 132 ? 9.779  2.101   5.792  1.00 6.13  ? 138 ARG   A CZ  1 
ATOM   1030 N  NH1 . ARG   A 1 132 ? 9.405  0.875   5.461  1.00 6.09  ? 138 ARG   A NH1 1 
ATOM   1031 N  NH2 . ARG   A 1 132 ? 8.889  2.949   6.270  1.00 5.96  ? 138 ARG   A NH2 1 
ATOM   1032 N  N   . ASP   A 1 133 ? 14.420 6.337   2.679  1.00 7.79  ? 139 ASP   A N   1 
ATOM   1033 C  CA  . ASP   A 1 133 ? 14.380 7.205   1.472  1.00 8.36  ? 139 ASP   A CA  1 
ATOM   1034 C  C   . ASP   A 1 133 ? 15.778 7.744   1.142  1.00 8.60  ? 139 ASP   A C   1 
ATOM   1035 O  O   . ASP   A 1 133 ? 15.935 8.247   0.031  1.00 9.08  ? 139 ASP   A O   1 
ATOM   1036 C  CB  . ASP   A 1 133 ? 13.408 8.363   1.667  1.00 8.71  ? 139 ASP   A CB  1 
ATOM   1037 C  CG  . ASP   A 1 133 ? 13.899 9.358   2.694  1.00 8.82  ? 139 ASP   A CG  1 
ATOM   1038 O  OD1 . ASP   A 1 133 ? 14.419 8.899   3.725  1.00 8.92  ? 139 ASP   A OD1 1 
ATOM   1039 O  OD2 . ASP   A 1 133 ? 13.762 10.576  2.457  1.00 9.17  ? 139 ASP   A OD2 1 
ATOM   1040 N  N   . LEU   A 1 134 ? 16.759 7.639   2.055  1.00 8.89  ? 140 LEU   A N   1 
ATOM   1041 C  CA  . LEU   A 1 134 ? 18.140 8.158   1.834  1.00 8.89  ? 140 LEU   A CA  1 
ATOM   1042 C  C   . LEU   A 1 134 ? 18.960 7.099   1.081  1.00 9.50  ? 140 LEU   A C   1 
ATOM   1043 O  O   . LEU   A 1 134 ? 19.776 6.400   1.730  1.00 9.02  ? 140 LEU   A O   1 
ATOM   1044 C  CB  . LEU   A 1 134 ? 18.797 8.516   3.174  1.00 8.55  ? 140 LEU   A CB  1 
ATOM   1045 C  CG  . LEU   A 1 134 ? 18.010 9.433   4.103  1.00 8.55  ? 140 LEU   A CG  1 
ATOM   1046 C  CD1 . LEU   A 1 134 ? 18.657 9.451   5.487  1.00 8.32  ? 140 LEU   A CD1 1 
ATOM   1047 C  CD2 . LEU   A 1 134 ? 17.858 10.845  3.549  1.00 8.43  ? 140 LEU   A CD2 1 
ATOM   1048 N  N   . LEU   A 1 135 ? 18.759 6.999   -0.244 1.00 9.76  ? 141 LEU   A N   1 
ATOM   1049 C  CA  . LEU   A 1 135 ? 19.325 5.894   -1.071 1.00 10.30 ? 141 LEU   A CA  1 
ATOM   1050 C  C   . LEU   A 1 135 ? 20.855 6.027   -1.131 1.00 10.28 ? 141 LEU   A C   1 
ATOM   1051 O  O   . LEU   A 1 135 ? 21.564 4.977   -1.150 1.00 10.12 ? 141 LEU   A O   1 
ATOM   1052 C  CB  . LEU   A 1 135 ? 18.698 5.904   -2.469 1.00 10.38 ? 141 LEU   A CB  1 
ATOM   1053 C  CG  . LEU   A 1 135 ? 17.174 6.040   -2.514 1.00 11.11 ? 141 LEU   A CG  1 
ATOM   1054 C  CD1 . LEU   A 1 135 ? 16.656 5.924   -3.946 1.00 11.58 ? 141 LEU   A CD1 1 
ATOM   1055 C  CD2 . LEU   A 1 135 ? 16.492 5.015   -1.615 1.00 11.47 ? 141 LEU   A CD2 1 
ATOM   1056 N  N   . TRP   A 1 136 ? 21.351 7.272   -1.096 1.00 10.41 ? 142 TRP   A N   1 
ATOM   1057 C  CA  . TRP   A 1 136 ? 22.804 7.595   -1.103 1.00 10.79 ? 142 TRP   A CA  1 
ATOM   1058 C  C   . TRP   A 1 136 ? 23.533 6.950   0.093  1.00 11.50 ? 142 TRP   A C   1 
ATOM   1059 O  O   . TRP   A 1 136 ? 24.775 6.859   0.007  1.00 11.54 ? 142 TRP   A O   1 
ATOM   1060 C  CB  . TRP   A 1 136 ? 23.036 9.113   -1.179 1.00 10.34 ? 142 TRP   A CB  1 
ATOM   1061 C  CG  . TRP   A 1 136 ? 22.379 9.910   -0.094 1.00 10.26 ? 142 TRP   A CG  1 
ATOM   1062 C  CD1 . TRP   A 1 136 ? 21.162 10.530  -0.142 1.00 9.81  ? 142 TRP   A CD1 1 
ATOM   1063 C  CD2 . TRP   A 1 136 ? 22.907 10.165  1.215  1.00 9.68  ? 142 TRP   A CD2 1 
ATOM   1064 N  NE1 . TRP   A 1 136 ? 20.899 11.141  1.052  1.00 9.72  ? 142 TRP   A NE1 1 
ATOM   1065 C  CE2 . TRP   A 1 136 ? 21.962 10.953  1.894  1.00 9.73  ? 142 TRP   A CE2 1 
ATOM   1066 C  CE3 . TRP   A 1 136 ? 24.098 9.829   1.862  1.00 9.64  ? 142 TRP   A CE3 1 
ATOM   1067 C  CZ2 . TRP   A 1 136 ? 22.164 11.386  3.200  1.00 9.46  ? 142 TRP   A CZ2 1 
ATOM   1068 C  CZ3 . TRP   A 1 136 ? 24.300 10.263  3.147  1.00 9.32  ? 142 TRP   A CZ3 1 
ATOM   1069 C  CH2 . TRP   A 1 136 ? 23.350 11.038  3.801  1.00 9.38  ? 142 TRP   A CH2 1 
ATOM   1070 N  N   . LEU   A 1 137 ? 22.832 6.503   1.146  1.00 12.63 ? 143 LEU   A N   1 
ATOM   1071 C  CA  . LEU   A 1 137 ? 23.453 5.805   2.316  1.00 15.17 ? 143 LEU   A CA  1 
ATOM   1072 C  C   . LEU   A 1 137 ? 24.094 4.459   1.919  1.00 18.09 ? 143 LEU   A C   1 
ATOM   1073 O  O   . LEU   A 1 137 ? 25.045 4.069   2.616  1.00 15.80 ? 143 LEU   A O   1 
ATOM   1074 C  CB  . LEU   A 1 137 ? 22.432 5.578   3.437  1.00 14.91 ? 143 LEU   A CB  1 
ATOM   1075 C  CG  . LEU   A 1 137 ? 22.155 6.764   4.359  1.00 14.35 ? 143 LEU   A CG  1 
ATOM   1076 C  CD1 . LEU   A 1 137 ? 20.982 6.446   5.265  1.00 14.51 ? 143 LEU   A CD1 1 
ATOM   1077 C  CD2 . LEU   A 1 137 ? 23.384 7.119   5.205  1.00 13.78 ? 143 LEU   A CD2 1 
ATOM   1078 N  N   . ASP   A 1 138 ? 23.615 3.779   0.865  1.00 23.88 ? 144 ASP   A N   1 
ATOM   1079 C  CA  . ASP   A 1 138 ? 24.121 2.446   0.407  1.00 30.26 ? 144 ASP   A CA  1 
ATOM   1080 C  C   . ASP   A 1 138 ? 25.364 2.557   -0.493 1.00 35.94 ? 144 ASP   A C   1 
ATOM   1081 O  O   . ASP   A 1 138 ? 25.785 1.495   -0.994 1.00 36.59 ? 144 ASP   A O   1 
ATOM   1082 C  CB  . ASP   A 1 138 ? 23.110 1.669   -0.443 1.00 31.28 ? 144 ASP   A CB  1 
ATOM   1083 C  CG  . ASP   A 1 138 ? 21.807 1.378   0.263  1.00 35.72 ? 144 ASP   A CG  1 
ATOM   1084 O  OD1 . ASP   A 1 138 ? 21.845 1.221   1.501  1.00 40.25 ? 144 ASP   A OD1 1 
ATOM   1085 O  OD2 . ASP   A 1 138 ? 20.762 1.330   -0.426 1.00 37.33 ? 144 ASP   A OD2 1 
ATOM   1086 N  N   . GLU   A 1 139 ? 25.907 3.759   -0.737 1.00 43.57 ? 145 GLU   A N   1 
ATOM   1087 C  CA  . GLU   A 1 139 ? 27.068 3.977   -1.652 1.00 49.66 ? 145 GLU   A CA  1 
ATOM   1088 C  C   . GLU   A 1 139 ? 27.869 5.221   -1.243 1.00 57.36 ? 145 GLU   A C   1 
ATOM   1089 O  O   . GLU   A 1 139 ? 27.308 6.083   -0.530 1.00 61.21 ? 145 GLU   A O   1 
ATOM   1090 C  CB  . GLU   A 1 139 ? 26.580 4.133   -3.093 1.00 50.20 ? 145 GLU   A CB  1 
ATOM   1091 C  CG  . GLU   A 1 139 ? 25.886 5.460   -3.364 1.00 49.43 ? 145 GLU   A CG  1 
ATOM   1092 C  CD  . GLU   A 1 139 ? 24.768 5.401   -4.390 1.00 51.89 ? 145 GLU   A CD  1 
ATOM   1093 O  OE1 . GLU   A 1 139 ? 24.546 6.416   -5.080 1.00 50.75 ? 145 GLU   A OE1 1 
ATOM   1094 O  OE2 . GLU   A 1 139 ? 24.106 4.345   -4.482 1.00 51.97 ? 145 GLU   A OE2 1 
ATOM   1095 N  N   . GLU   A 1 140 ? 29.125 5.316   -1.704 1.00 64.14 ? 146 GLU   A N   1 
ATOM   1096 C  CA  . GLU   A 1 140 ? 30.013 6.505   -1.552 1.00 65.22 ? 146 GLU   A CA  1 
ATOM   1097 C  C   . GLU   A 1 140 ? 30.076 6.903   -0.069 1.00 68.09 ? 146 GLU   A C   1 
ATOM   1098 O  O   . GLU   A 1 140 ? 30.967 6.490   0.683  1.00 66.89 ? 146 GLU   A O   1 
ATOM   1099 C  CB  . GLU   A 1 140 ? 29.523 7.629   -2.477 1.00 66.04 ? 146 GLU   A CB  1 
ATOM   1100 C  CG  . GLU   A 1 140 ? 29.712 9.041   -1.936 1.00 68.12 ? 146 GLU   A CG  1 
ATOM   1101 C  CD  . GLU   A 1 140 ? 31.151 9.457   -1.688 1.00 70.31 ? 146 GLU   A CD  1 
ATOM   1102 O  OE1 . GLU   A 1 140 ? 31.445 9.931   -0.565 1.00 65.70 ? 146 GLU   A OE1 1 
ATOM   1103 O  OE2 . GLU   A 1 140 ? 31.977 9.307   -2.620 1.00 75.42 ? 146 GLU   A OE2 1 
HETATM 1104 ZN ZN  . ZN    B 2 .   ? 10.974 -4.029  5.024  1.00 9.08  ? 201 ZN    A ZN  1 
HETATM 1105 S  S   . DMS   C 3 .   ? 15.475 21.372  7.323  1.00 27.05 ? 202 DMS   A S   1 
HETATM 1106 O  O   . DMS   C 3 .   ? 14.998 21.231  8.737  1.00 27.62 ? 202 DMS   A O   1 
HETATM 1107 C  C1  . DMS   C 3 .   ? 14.018 21.323  6.306  1.00 26.89 ? 202 DMS   A C1  1 
HETATM 1108 C  C2  . DMS   C 3 .   ? 15.920 23.077  7.095  1.00 26.32 ? 202 DMS   A C2  1 
HETATM 1109 S  S   . DMS   D 3 .   ? 1.138  -2.297  23.754 1.00 56.34 ? 203 DMS   A S   1 
HETATM 1110 O  O   . DMS   D 3 .   ? 1.325  -0.919  24.297 1.00 45.26 ? 203 DMS   A O   1 
HETATM 1111 C  C1  . DMS   D 3 .   ? 1.599  -3.430  25.044 1.00 53.48 ? 203 DMS   A C1  1 
HETATM 1112 C  C2  . DMS   D 3 .   ? -0.609 -2.637  23.754 1.00 52.90 ? 203 DMS   A C2  1 
HETATM 1113 S  S   . SO4   E 4 .   ? -0.263 24.715  14.265 1.00 84.57 ? 204 SO4   A S   1 
HETATM 1114 O  O1  . SO4   E 4 .   ? -0.940 24.696  12.998 1.00 87.58 ? 204 SO4   A O1  1 
HETATM 1115 O  O2  . SO4   E 4 .   ? -1.186 25.112  15.296 1.00 83.74 ? 204 SO4   A O2  1 
HETATM 1116 O  O3  . SO4   E 4 .   ? 0.249  23.400  14.545 1.00 80.50 ? 204 SO4   A O3  1 
HETATM 1117 O  O4  . SO4   E 4 .   ? 0.827  25.654  14.211 1.00 86.20 ? 204 SO4   A O4  1 
HETATM 1118 N  N1  . A1BQ2 F 5 .   ? 11.605 11.231  22.566 0.85 4.23  ? 205 A1BQ2 A N1  1 
HETATM 1119 N  N3  . A1BQ2 F 5 .   ? 11.812 16.896  20.326 0.85 3.83  ? 205 A1BQ2 A N3  1 
HETATM 1120 C  C4  . A1BQ2 F 5 .   ? 13.675 15.208  20.257 0.85 3.86  ? 205 A1BQ2 A C4  1 
HETATM 1121 C  C5  . A1BQ2 F 5 .   ? 12.463 15.864  19.676 0.85 3.81  ? 205 A1BQ2 A C5  1 
HETATM 1122 C  C6  . A1BQ2 F 5 .   ? 11.839 15.626  18.515 0.85 3.80  ? 205 A1BQ2 A C6  1 
HETATM 1123 C  C7  . A1BQ2 F 5 .   ? 10.847 17.199  19.539 0.85 3.78  ? 205 A1BQ2 A C7  1 
HETATM 1124 C  C8  . A1BQ2 F 5 .   ? 10.243 11.964  24.242 0.85 4.24  ? 205 A1BQ2 A C8  1 
HETATM 1125 C  C10 . A1BQ2 F 5 .   ? 8.660  11.932  26.040 0.85 4.26  ? 205 A1BQ2 A C10 1 
HETATM 1126 C  C13 . A1BQ2 F 5 .   ? 10.023 10.593  24.057 0.85 4.27  ? 205 A1BQ2 A C13 1 
HETATM 1127 N  N   . A1BQ2 F 5 .   ? 10.840 10.198  23.040 0.85 4.21  ? 205 A1BQ2 A N   1 
HETATM 1128 C  C   . A1BQ2 F 5 .   ? 10.957 8.879   22.446 0.85 4.24  ? 205 A1BQ2 A C   1 
HETATM 1129 O  O   . A1BQ2 F 5 .   ? 11.917 14.479  23.986 0.85 4.22  ? 205 A1BQ2 A O   1 
HETATM 1130 C  C1  . A1BQ2 F 5 .   ? 11.258 12.299  23.287 0.85 4.21  ? 205 A1BQ2 A C1  1 
HETATM 1131 C  C11 . A1BQ2 F 5 .   ? 8.461  10.571  25.853 0.85 4.24  ? 205 A1BQ2 A C11 1 
HETATM 1132 C  C12 . A1BQ2 F 5 .   ? 9.140  9.882   24.857 0.85 4.25  ? 205 A1BQ2 A C12 1 
HETATM 1133 C  C2  . A1BQ2 F 5 .   ? 11.952 13.622  23.103 0.85 4.12  ? 205 A1BQ2 A C2  1 
HETATM 1134 C  C3  . A1BQ2 F 5 .   ? 13.522 14.881  21.726 0.85 3.91  ? 205 A1BQ2 A C3  1 
HETATM 1135 C  C9  . A1BQ2 F 5 .   ? 9.542  12.637  25.238 0.85 4.24  ? 205 A1BQ2 A C9  1 
HETATM 1136 N  N2  . A1BQ2 F 5 .   ? 12.599 13.779  21.949 0.85 4.00  ? 205 A1BQ2 A N2  1 
HETATM 1137 O  O1  . A1BQ2 F 5 .   ? 10.781 16.480  18.398 0.85 3.76  ? 205 A1BQ2 A O1  1 
HETATM 1138 O  O   . HOH   G 6 .   ? 5.529  6.286   24.449 1.00 15.79 ? 301 HOH   A O   1 
HETATM 1139 O  O   . HOH   G 6 .   ? 0.631  11.029  28.113 1.00 33.63 ? 302 HOH   A O   1 
HETATM 1140 O  O   . HOH   G 6 .   ? 32.181 3.121   3.152  1.00 33.40 ? 303 HOH   A O   1 
HETATM 1141 O  O   . HOH   G 6 .   ? 33.297 6.312   0.915  1.00 27.73 ? 304 HOH   A O   1 
HETATM 1142 O  O   . HOH   G 6 .   ? 25.693 11.680  21.549 1.00 28.15 ? 305 HOH   A O   1 
HETATM 1143 O  O   . HOH   G 6 .   ? -2.924 24.244  11.709 1.00 41.20 ? 306 HOH   A O   1 
HETATM 1144 O  O   . HOH   G 6 .   ? 6.386  3.437   3.357  1.00 19.56 ? 307 HOH   A O   1 
HETATM 1145 O  O   . HOH   G 6 .   ? 11.435 -3.828  -1.045 1.00 18.58 ? 308 HOH   A O   1 
HETATM 1146 O  O   . HOH   G 6 .   ? 15.795 -4.163  34.314 1.00 21.20 ? 309 HOH   A O   1 
HETATM 1147 O  O   . HOH   G 6 .   ? 3.042  8.533   9.678  1.00 16.80 ? 310 HOH   A O   1 
HETATM 1148 O  O   . HOH   G 6 .   ? 16.278 -2.666  16.843 1.00 9.73  ? 311 HOH   A O   1 
HETATM 1149 O  O   . HOH   G 6 .   ? 18.997 19.555  16.560 1.00 14.69 ? 312 HOH   A O   1 
HETATM 1150 O  O   . HOH   G 6 .   ? 16.086 -7.991  27.007 1.00 47.05 ? 313 HOH   A O   1 
HETATM 1151 O  O   . HOH   G 6 .   ? 22.455 -0.507  3.210  1.00 13.10 ? 314 HOH   A O   1 
HETATM 1152 O  O   . HOH   G 6 .   ? 3.190  11.007  21.821 1.00 13.72 ? 315 HOH   A O   1 
HETATM 1153 O  O   . HOH   G 6 .   ? 13.999 23.612  11.948 1.00 35.18 ? 316 HOH   A O   1 
HETATM 1154 O  O   . HOH   G 6 .   ? 24.091 0.442   14.966 1.00 13.02 ? 317 HOH   A O   1 
HETATM 1155 O  O   . HOH   G 6 .   ? 10.564 5.331   3.302  1.00 16.97 ? 318 HOH   A O   1 
HETATM 1156 O  O   . HOH   G 6 .   ? 26.571 8.507   -0.709 1.00 37.74 ? 319 HOH   A O   1 
HETATM 1157 O  O   . HOH   G 6 .   ? 6.150  2.263   6.446  1.00 13.72 ? 320 HOH   A O   1 
HETATM 1158 O  O   . HOH   G 6 .   ? 30.154 4.921   2.521  1.00 18.87 ? 321 HOH   A O   1 
HETATM 1159 O  O   . HOH   G 6 .   ? 20.742 2.663   -2.607 1.00 26.23 ? 322 HOH   A O   1 
HETATM 1160 O  O   . HOH   G 6 .   ? 31.352 11.495  18.422 1.00 20.13 ? 323 HOH   A O   1 
HETATM 1161 O  O   . HOH   G 6 .   ? 3.044  7.714   27.522 0.85 37.79 ? 324 HOH   A O   1 
HETATM 1162 O  O   . HOH   G 6 .   ? 19.317 20.652  5.811  1.00 35.87 ? 325 HOH   A O   1 
HETATM 1163 O  O   . HOH   G 6 .   ? 21.497 22.993  10.711 1.00 19.71 ? 326 HOH   A O   1 
HETATM 1164 O  O   . HOH   G 6 .   ? 24.813 8.589   -6.420 1.00 32.92 ? 327 HOH   A O   1 
HETATM 1165 O  O   . HOH   G 6 .   ? 4.923  -4.447  21.001 1.00 12.71 ? 328 HOH   A O   1 
HETATM 1166 O  O   . HOH   G 6 .   ? 27.688 3.586   18.732 1.00 20.96 ? 329 HOH   A O   1 
HETATM 1167 O  O   . HOH   G 6 .   ? 16.793 23.654  14.611 1.00 32.66 ? 330 HOH   A O   1 
HETATM 1168 O  O   . HOH   G 6 .   ? 4.835  3.726   -0.265 1.00 30.03 ? 331 HOH   A O   1 
HETATM 1169 O  O   . HOH   G 6 .   ? 27.543 3.759   1.967  1.00 16.78 ? 332 HOH   A O   1 
HETATM 1170 O  O   . HOH   G 6 .   ? 31.194 19.004  6.622  1.00 27.04 ? 333 HOH   A O   1 
HETATM 1171 O  O   . HOH   G 6 .   ? 20.006 0.059   26.773 1.00 12.91 ? 334 HOH   A O   1 
HETATM 1172 O  O   . HOH   G 6 .   ? 1.747  -1.454  4.471  1.00 25.74 ? 335 HOH   A O   1 
HETATM 1173 O  O   . HOH   G 6 .   ? 7.609  -4.908  28.969 1.00 21.64 ? 336 HOH   A O   1 
HETATM 1174 O  O   . HOH   G 6 .   ? 2.071  8.951   11.610 1.00 33.94 ? 337 HOH   A O   1 
HETATM 1175 O  O   . HOH   G 6 .   ? 8.837  21.580  9.665  1.00 35.64 ? 338 HOH   A O   1 
HETATM 1176 O  O   . HOH   G 6 .   ? 15.240 11.919  0.707  1.00 21.20 ? 339 HOH   A O   1 
HETATM 1177 O  O   . HOH   G 6 .   ? 29.747 3.296   9.359  1.00 11.41 ? 340 HOH   A O   1 
HETATM 1178 O  O   . HOH   G 6 .   ? 10.600 8.908   4.555  1.00 19.37 ? 341 HOH   A O   1 
HETATM 1179 O  O   . HOH   G 6 .   ? 1.341  8.398   5.992  1.00 25.48 ? 342 HOH   A O   1 
HETATM 1180 O  O   . HOH   G 6 .   ? 31.408 -3.372  8.217  1.00 44.84 ? 343 HOH   A O   1 
HETATM 1181 O  O   . HOH   G 6 .   ? 20.366 8.939   25.285 1.00 12.06 ? 344 HOH   A O   1 
HETATM 1182 O  O   . HOH   G 6 .   ? -0.815 2.630   5.018  1.00 26.99 ? 345 HOH   A O   1 
HETATM 1183 O  O   . HOH   G 6 .   ? 29.652 11.343  1.614  0.50 18.53 ? 346 HOH   A O   1 
HETATM 1184 O  O   . HOH   G 6 .   ? 7.950  26.011  15.616 1.00 20.77 ? 347 HOH   A O   1 
HETATM 1185 O  O   . HOH   G 6 .   ? 4.794  -5.097  6.834  1.00 35.36 ? 348 HOH   A O   1 
HETATM 1186 O  O   . HOH   G 6 .   ? 22.241 -4.642  11.854 1.00 22.72 ? 349 HOH   A O   1 
HETATM 1187 O  O   . HOH   G 6 .   ? 17.994 -6.044  26.517 1.00 23.67 ? 350 HOH   A O   1 
HETATM 1188 O  O   . HOH   G 6 .   ? 21.866 21.545  6.211  1.00 11.97 ? 351 HOH   A O   1 
HETATM 1189 O  O   . HOH   G 6 .   ? 21.186 9.250   18.332 1.00 6.77  ? 352 HOH   A O   1 
HETATM 1190 O  O   . HOH   G 6 .   ? 11.190 23.852  25.142 1.00 18.56 ? 353 HOH   A O   1 
HETATM 1191 O  O   . HOH   G 6 .   ? 5.210  13.062  21.097 1.00 25.01 ? 354 HOH   A O   1 
HETATM 1192 O  O   . HOH   G 6 .   ? 3.071  14.056  17.157 1.00 21.90 ? 355 HOH   A O   1 
HETATM 1193 O  O   . HOH   G 6 .   ? 11.772 10.961  0.592  1.00 22.63 ? 356 HOH   A O   1 
HETATM 1194 O  O   . HOH   G 6 .   ? 1.484  -2.064  20.128 1.00 14.26 ? 357 HOH   A O   1 
HETATM 1195 O  O   . HOH   G 6 .   ? 0.253  15.451  17.127 1.00 21.09 ? 358 HOH   A O   1 
HETATM 1196 O  O   . HOH   G 6 .   ? 11.350 5.138   33.503 1.00 8.52  ? 359 HOH   A O   1 
HETATM 1197 O  O   . HOH   G 6 .   ? 9.027  3.196   2.696  1.00 10.41 ? 360 HOH   A O   1 
HETATM 1198 O  O   . HOH   G 6 .   ? 8.977  19.690  18.264 0.85 8.10  ? 361 HOH   A O   1 
HETATM 1199 O  O   . HOH   G 6 .   ? 15.822 2.802   22.579 1.00 7.24  ? 362 HOH   A O   1 
HETATM 1200 O  O   . HOH   G 6 .   ? 14.955 9.785   29.330 1.00 11.77 ? 363 HOH   A O   1 
HETATM 1201 O  O   . HOH   G 6 .   ? 18.327 21.548  9.065  1.00 6.81  ? 364 HOH   A O   1 
HETATM 1202 O  O   . HOH   G 6 .   ? 1.557  1.885   24.386 1.00 6.65  ? 365 HOH   A O   1 
HETATM 1203 O  O   . HOH   G 6 .   ? 16.567 12.438  23.962 0.85 11.88 ? 366 HOH   A O   1 
HETATM 1204 O  O   . HOH   G 6 .   ? 14.752 -4.933  17.837 1.00 24.79 ? 367 HOH   A O   1 
HETATM 1205 O  O   . HOH   G 6 .   ? 34.938 20.635  9.445  1.00 14.09 ? 368 HOH   A O   1 
HETATM 1206 O  O   . HOH   G 6 .   ? 8.872  16.714  25.074 0.85 9.05  ? 369 HOH   A O   1 
HETATM 1207 O  O   . HOH   G 6 .   ? 13.217 -8.394  24.089 1.00 7.33  ? 370 HOH   A O   1 
HETATM 1208 O  O   . HOH   G 6 .   ? 30.913 -1.270  4.627  1.00 28.24 ? 371 HOH   A O   1 
HETATM 1209 O  O   . HOH   G 6 .   ? 4.791  -1.731  21.391 1.00 16.12 ? 372 HOH   A O   1 
HETATM 1210 O  O   . HOH   G 6 .   ? 12.697 2.498   33.208 1.00 9.36  ? 373 HOH   A O   1 
HETATM 1211 O  O   . HOH   G 6 .   ? 8.559  3.997   32.945 1.00 11.26 ? 374 HOH   A O   1 
HETATM 1212 O  O   . HOH   G 6 .   ? 23.777 18.122  18.187 1.00 8.12  ? 375 HOH   A O   1 
HETATM 1213 O  O   . HOH   G 6 .   ? 21.225 -4.704  9.027  1.00 14.46 ? 376 HOH   A O   1 
HETATM 1214 O  O   . HOH   G 6 .   ? 11.656 12.302  11.400 1.00 2.56  ? 377 HOH   A O   1 
HETATM 1215 O  O   . HOH   G 6 .   ? 36.690 2.411   5.436  1.00 40.32 ? 378 HOH   A O   1 
HETATM 1216 O  O   . HOH   G 6 .   ? 31.855 2.912   11.307 1.00 15.81 ? 379 HOH   A O   1 
HETATM 1217 O  O   . HOH   G 6 .   ? 11.027 15.711  26.431 0.85 15.36 ? 380 HOH   A O   1 
HETATM 1218 O  O   . HOH   G 6 .   ? 19.010 -6.435  24.130 1.00 11.45 ? 381 HOH   A O   1 
HETATM 1219 O  O   . HOH   G 6 .   ? 6.049  -6.888  14.040 1.00 25.34 ? 382 HOH   A O   1 
HETATM 1220 O  O   . HOH   G 6 .   ? 18.913 -0.110  18.695 1.00 6.50  ? 383 HOH   A O   1 
HETATM 1221 O  O   . HOH   G 6 .   ? 13.683 23.789  9.053  0.85 21.47 ? 384 HOH   A O   1 
HETATM 1222 O  O   . HOH   G 6 .   ? 1.011  0.362   16.676 1.00 9.40  ? 385 HOH   A O   1 
HETATM 1223 O  O   . HOH   G 6 .   ? 31.985 21.709  20.336 1.00 35.06 ? 386 HOH   A O   1 
HETATM 1224 O  O   . HOH   G 6 .   ? -0.810 21.614  9.061  1.00 29.71 ? 387 HOH   A O   1 
HETATM 1225 O  O   . HOH   G 6 .   ? 0.487  4.734   6.499  1.00 23.00 ? 388 HOH   A O   1 
HETATM 1226 O  O   . HOH   G 6 .   ? 8.366  -10.407 8.123  1.00 38.47 ? 389 HOH   A O   1 
HETATM 1227 O  O   . HOH   G 6 .   ? 7.255  25.811  21.442 1.00 26.81 ? 390 HOH   A O   1 
HETATM 1228 O  O   . HOH   G 6 .   ? 19.254 0.977   -2.913 1.00 15.59 ? 391 HOH   A O   1 
HETATM 1229 O  O   . HOH   G 6 .   ? 23.308 -4.709  2.428  1.00 29.56 ? 392 HOH   A O   1 
HETATM 1230 O  O   . HOH   G 6 .   ? 23.365 16.705  22.683 1.00 31.77 ? 393 HOH   A O   1 
HETATM 1231 O  O   . HOH   G 6 .   ? -0.037 16.837  10.032 1.00 14.32 ? 394 HOH   A O   1 
HETATM 1232 O  O   . HOH   G 6 .   ? 13.351 11.297  9.113  1.00 3.18  ? 395 HOH   A O   1 
HETATM 1233 O  O   . HOH   G 6 .   ? 31.581 9.082   4.156  1.00 14.59 ? 396 HOH   A O   1 
HETATM 1234 O  O   . HOH   G 6 .   ? 6.715  8.236   28.629 1.00 11.53 ? 397 HOH   A O   1 
HETATM 1235 O  O   . HOH   G 6 .   ? 6.626  -2.840  -1.735 1.00 19.52 ? 398 HOH   A O   1 
HETATM 1236 O  O   . HOH   G 6 .   ? 5.640  13.338  25.628 1.00 12.65 ? 399 HOH   A O   1 
HETATM 1237 O  O   . HOH   G 6 .   ? 8.124  -3.460  0.105  1.00 12.60 ? 400 HOH   A O   1 
HETATM 1238 O  O   . HOH   G 6 .   ? 4.132  4.385   27.521 1.00 22.42 ? 401 HOH   A O   1 
HETATM 1239 O  O   . HOH   G 6 .   ? 18.626 2.623   22.768 1.00 9.36  ? 402 HOH   A O   1 
HETATM 1240 O  O   . HOH   G 6 .   ? 6.952  13.573  5.423  1.00 9.16  ? 403 HOH   A O   1 
HETATM 1241 O  O   . HOH   G 6 .   ? 22.616 -2.512  14.765 1.00 24.00 ? 404 HOH   A O   1 
HETATM 1242 O  O   . HOH   G 6 .   ? 19.229 -5.994  33.582 1.00 21.17 ? 405 HOH   A O   1 
HETATM 1243 O  O   . HOH   G 6 .   ? 31.731 -0.073  12.370 1.00 17.58 ? 406 HOH   A O   1 
HETATM 1244 O  O   . HOH   G 6 .   ? 5.452  26.626  18.531 1.00 23.19 ? 407 HOH   A O   1 
HETATM 1245 O  O   . HOH   G 6 .   ? 8.880  -6.891  8.726  1.00 17.55 ? 408 HOH   A O   1 
HETATM 1246 O  O   . HOH   G 6 .   ? 12.334 17.478  5.088  1.00 24.24 ? 409 HOH   A O   1 
HETATM 1247 O  O   . HOH   G 6 .   ? -0.159 17.283  12.467 1.00 21.92 ? 410 HOH   A O   1 
HETATM 1248 O  O   . HOH   G 6 .   ? 7.729  13.742  21.371 1.00 11.35 ? 411 HOH   A O   1 
HETATM 1249 O  O   . HOH   G 6 .   ? 38.618 7.362   7.901  0.50 16.18 ? 412 HOH   A O   1 
HETATM 1250 O  O   . HOH   G 6 .   ? 24.410 3.469   25.433 1.00 25.51 ? 413 HOH   A O   1 
HETATM 1251 O  O   . HOH   G 6 .   ? 0.605  12.239  21.619 1.00 24.33 ? 414 HOH   A O   1 
HETATM 1252 O  O   . HOH   G 6 .   ? 6.080  -1.144  24.232 1.00 2.73  ? 415 HOH   A O   1 
HETATM 1253 O  O   . HOH   G 6 .   ? 22.813 19.143  5.065  1.00 6.69  ? 416 HOH   A O   1 
HETATM 1254 O  O   . HOH   G 6 .   ? 14.385 15.400  3.453  1.00 13.59 ? 417 HOH   A O   1 
HETATM 1255 O  O   . HOH   G 6 .   ? 23.175 8.798   20.207 1.00 7.22  ? 418 HOH   A O   1 
HETATM 1256 O  O   . HOH   G 6 .   ? 20.131 4.388   25.442 1.00 19.97 ? 419 HOH   A O   1 
HETATM 1257 O  O   . HOH   G 6 .   ? 7.261  11.446  4.172  1.00 31.47 ? 420 HOH   A O   1 
HETATM 1258 O  O   . HOH   G 6 .   ? 15.407 -9.720  3.362  0.50 14.35 ? 421 HOH   A O   1 
HETATM 1259 O  O   . HOH   G 6 .   ? 18.073 11.077  -0.313 1.00 23.66 ? 422 HOH   A O   1 
HETATM 1260 O  O   . HOH   G 6 .   ? 5.965  19.635  26.128 1.00 29.46 ? 423 HOH   A O   1 
HETATM 1261 O  O   . HOH   G 6 .   ? 31.207 10.962  16.317 1.00 25.05 ? 424 HOH   A O   1 
HETATM 1262 O  O   . HOH   G 6 .   ? 24.472 2.190   18.348 1.00 10.87 ? 425 HOH   A O   1 
HETATM 1263 O  O   . HOH   G 6 .   ? 3.690  15.444  20.545 1.00 8.45  ? 426 HOH   A O   1 
HETATM 1264 O  O   . HOH   G 6 .   ? 17.094 13.626  25.996 1.00 16.68 ? 427 HOH   A O   1 
HETATM 1265 O  O   . HOH   G 6 .   ? 25.329 7.600   19.490 1.00 16.92 ? 428 HOH   A O   1 
HETATM 1266 O  O   . HOH   G 6 .   ? 6.754  23.844  11.980 1.00 18.83 ? 429 HOH   A O   1 
HETATM 1267 O  O   . HOH   G 6 .   ? 25.599 15.493  22.238 1.00 33.89 ? 430 HOH   A O   1 
HETATM 1268 O  O   . HOH   G 6 .   ? 18.921 21.008  25.259 1.00 24.87 ? 431 HOH   A O   1 
HETATM 1269 O  O   . HOH   G 6 .   ? 17.874 9.536   -2.177 1.00 9.43  ? 432 HOH   A O   1 
HETATM 1270 O  O   . HOH   G 6 .   ? 19.199 13.807  1.699  1.00 31.24 ? 433 HOH   A O   1 
HETATM 1271 O  O   . HOH   G 6 .   ? 35.951 9.644   11.058 1.00 30.20 ? 434 HOH   A O   1 
HETATM 1272 O  O   . HOH   G 6 .   ? 4.590  9.741   28.276 0.85 16.64 ? 435 HOH   A O   1 
HETATM 1273 O  O   . HOH   G 6 .   ? 7.902  14.469  22.614 1.00 2.97  ? 436 HOH   A O   1 
HETATM 1274 O  O   . HOH   G 6 .   ? 36.808 17.257  9.192  1.00 33.50 ? 437 HOH   A O   1 
HETATM 1275 O  O   . HOH   G 6 .   ? 5.224  1.013   -3.030 0.50 12.14 ? 438 HOH   A O   1 
HETATM 1276 O  O   . HOH   G 6 .   ? 18.876 20.304  19.195 1.00 17.96 ? 439 HOH   A O   1 
HETATM 1277 O  O   . HOH   G 6 .   ? 26.589 -4.211  5.978  1.00 52.21 ? 440 HOH   A O   1 
HETATM 1278 O  O   . HOH   G 6 .   ? 4.356  7.487   3.029  1.00 33.28 ? 441 HOH   A O   1 
HETATM 1279 O  O   . HOH   G 6 .   ? 37.175 -0.802  9.052  1.00 26.72 ? 442 HOH   A O   1 
HETATM 1280 O  O   . HOH   G 6 .   ? 1.764  -2.338  17.549 1.00 7.53  ? 443 HOH   A O   1 
HETATM 1281 O  O   . HOH   G 6 .   ? 8.884  -4.940  31.236 1.00 20.34 ? 444 HOH   A O   1 
HETATM 1282 O  O   . HOH   G 6 .   ? 31.092 6.822   16.427 1.00 33.26 ? 445 HOH   A O   1 
HETATM 1283 O  O   . HOH   G 6 .   ? 22.507 -8.223  5.343  1.00 27.28 ? 446 HOH   A O   1 
HETATM 1284 O  O   . HOH   G 6 .   ? 9.209  -8.329  -0.275 1.00 37.24 ? 447 HOH   A O   1 
HETATM 1285 O  O   . HOH   G 6 .   ? 4.079  14.857  4.251  1.00 21.07 ? 448 HOH   A O   1 
HETATM 1286 O  O   . HOH   G 6 .   ? 25.884 19.709  4.933  0.50 10.28 ? 449 HOH   A O   1 
HETATM 1287 O  O   . HOH   G 6 .   ? -0.038 7.116   28.364 1.00 40.28 ? 450 HOH   A O   1 
HETATM 1288 O  O   . HOH   G 6 .   ? 22.521 -2.741  32.622 1.00 27.88 ? 451 HOH   A O   1 
HETATM 1289 O  O   . HOH   G 6 .   ? 3.699  -3.882  2.771  1.00 43.14 ? 452 HOH   A O   1 
HETATM 1290 O  O   . HOH   G 6 .   ? 20.068 0.935   19.494 1.00 7.24  ? 453 HOH   A O   1 
HETATM 1291 O  O   . HOH   G 6 .   ? 4.578  21.662  25.237 1.00 27.67 ? 454 HOH   A O   1 
HETATM 1292 O  O   . HOH   G 6 .   ? 6.336  15.821  22.900 1.00 21.12 ? 455 HOH   A O   1 
HETATM 1293 O  O   . HOH   G 6 .   ? 24.407 -0.031  -4.011 1.00 31.20 ? 456 HOH   A O   1 
HETATM 1294 O  O   . HOH   G 6 .   ? 18.697 -2.583  18.234 1.00 9.27  ? 457 HOH   A O   1 
HETATM 1295 O  O   . HOH   G 6 .   ? 19.806 9.404   -3.646 1.00 20.70 ? 458 HOH   A O   1 
HETATM 1296 O  O   . HOH   G 6 .   ? 21.973 13.424  -1.621 1.00 27.98 ? 459 HOH   A O   1 
HETATM 1297 O  O   . HOH   G 6 .   ? 9.007  20.587  7.694  1.00 27.73 ? 460 HOH   A O   1 
HETATM 1298 O  O   . HOH   G 6 .   ? 29.052 20.623  19.017 1.00 41.51 ? 461 HOH   A O   1 
HETATM 1299 O  O   . HOH   G 6 .   ? 35.188 6.777   13.651 1.00 25.23 ? 462 HOH   A O   1 
HETATM 1300 O  O   . HOH   G 6 .   ? 37.626 0.546   6.933  1.00 27.03 ? 463 HOH   A O   1 
HETATM 1301 O  O   . HOH   G 6 .   ? 7.622  -4.803  2.383  1.00 22.75 ? 464 HOH   A O   1 
HETATM 1302 O  O   . HOH   G 6 .   ? 7.749  -7.526  1.417  1.00 22.30 ? 465 HOH   A O   1 
HETATM 1303 O  O   . HOH   G 6 .   ? 2.780  2.101   26.577 1.00 11.91 ? 466 HOH   A O   1 
HETATM 1304 O  O   . HOH   G 6 .   ? 27.055 -2.252  13.806 1.00 26.73 ? 467 HOH   A O   1 
HETATM 1305 O  O   . HOH   G 6 .   ? 10.625 20.141  27.919 0.85 20.85 ? 468 HOH   A O   1 
HETATM 1306 O  O   . HOH   G 6 .   ? 19.220 -8.154  13.030 1.00 19.01 ? 469 HOH   A O   1 
HETATM 1307 O  O   . HOH   G 6 .   ? 29.490 -1.700  13.118 1.00 30.91 ? 470 HOH   A O   1 
HETATM 1308 O  O   . HOH   G 6 .   ? 3.440  -6.490  14.348 1.00 46.64 ? 471 HOH   A O   1 
HETATM 1309 O  O   . HOH   G 6 .   ? 20.402 7.589   27.574 1.00 30.13 ? 472 HOH   A O   1 
HETATM 1310 O  O   . HOH   G 6 .   ? 5.028  -1.786  26.500 1.00 23.59 ? 473 HOH   A O   1 
HETATM 1311 O  O   . HOH   G 6 .   ? 20.771 12.717  26.205 1.00 24.69 ? 474 HOH   A O   1 
HETATM 1312 O  O   . HOH   G 6 .   ? 13.429 -8.630  11.840 1.00 22.66 ? 475 HOH   A O   1 
HETATM 1313 O  O   . HOH   G 6 .   ? 27.795 22.185  16.390 1.00 18.95 ? 476 HOH   A O   1 
HETATM 1314 O  O   . HOH   G 6 .   ? 24.544 10.089  -4.018 1.00 31.85 ? 477 HOH   A O   1 
HETATM 1315 O  O   . HOH   G 6 .   ? 3.480  -6.520  21.475 1.00 45.67 ? 478 HOH   A O   1 
HETATM 1316 O  O   . HOH   G 6 .   ? 17.206 -7.930  29.782 1.00 43.12 ? 479 HOH   A O   1 
HETATM 1317 O  O   . HOH   G 6 .   ? 2.732  -7.004  16.469 1.00 38.35 ? 480 HOH   A O   1 
HETATM 1318 O  O   . HOH   G 6 .   ? 29.901 15.668  2.559  1.00 34.02 ? 481 HOH   A O   1 
HETATM 1319 O  O   . HOH   G 6 .   ? 38.744 18.481  15.884 0.50 31.48 ? 482 HOH   A O   1 
HETATM 1320 O  O   . HOH   G 6 .   ? 23.745 13.538  -0.251 1.00 28.45 ? 483 HOH   A O   1 
HETATM 1321 O  O   . HOH   G 6 .   ? 1.451  21.244  8.279  1.00 41.08 ? 484 HOH   A O   1 
HETATM 1322 O  O   . HOH   G 6 .   ? 31.939 11.835  2.876  1.00 31.36 ? 485 HOH   A O   1 
HETATM 1323 O  O   . HOH   G 6 .   ? 1.679  8.682   29.654 0.85 22.33 ? 486 HOH   A O   1 
HETATM 1324 O  O   . HOH   G 6 .   ? 18.939 11.224  25.564 1.00 20.19 ? 487 HOH   A O   1 
HETATM 1325 O  O   . HOH   G 6 .   ? 32.103 8.590   14.923 1.00 34.79 ? 488 HOH   A O   1 
HETATM 1326 O  O   . HOH   G 6 .   ? 32.716 4.223   12.994 1.00 20.58 ? 489 HOH   A O   1 
HETATM 1327 O  O   . HOH   G 6 .   ? 16.098 -6.861  33.139 1.00 31.65 ? 490 HOH   A O   1 
HETATM 1328 O  O   . HOH   G 6 .   ? 12.412 18.581  29.221 0.85 23.98 ? 491 HOH   A O   1 
HETATM 1329 O  O   . HOH   G 6 .   ? 16.625 14.413  1.519  1.00 17.52 ? 492 HOH   A O   1 
HETATM 1330 O  O   . HOH   G 6 .   ? 24.161 9.516   23.556 1.00 24.95 ? 493 HOH   A O   1 
HETATM 1331 O  O   . HOH   G 6 .   ? 4.610  24.959  22.399 1.00 22.94 ? 494 HOH   A O   1 
HETATM 1332 O  O   . HOH   G 6 .   ? 8.969  7.863   2.122  1.00 11.75 ? 495 HOH   A O   1 
HETATM 1333 O  O   . HOH   G 6 .   ? 31.833 8.869   17.856 0.50 21.70 ? 496 HOH   A O   1 
HETATM 1334 O  O   . HOH   G 6 .   ? 14.201 14.651  30.238 0.85 18.24 ? 497 HOH   A O   1 
HETATM 1335 O  O   . HOH   G 6 .   ? 7.738  -7.489  27.322 1.00 39.81 ? 498 HOH   A O   1 
HETATM 1336 O  O   . HOH   G 6 .   ? 32.242 14.166  22.035 1.00 23.09 ? 499 HOH   A O   1 
HETATM 1337 O  O   . HOH   G 6 .   ? 19.587 -7.104  7.884  0.50 18.27 ? 500 HOH   A O   1 
HETATM 1338 O  O   . HOH   G 6 .   ? 17.696 12.739  28.109 1.00 21.22 ? 501 HOH   A O   1 
HETATM 1339 O  O   . HOH   G 6 .   ? 6.914  27.756  20.187 1.00 21.58 ? 502 HOH   A O   1 
HETATM 1340 O  O   . HOH   G 6 .   ? 20.527 -5.774  29.241 1.00 28.42 ? 503 HOH   A O   1 
HETATM 1341 O  O   . HOH   G 6 .   ? 36.211 2.167   14.303 1.00 32.06 ? 504 HOH   A O   1 
HETATM 1342 O  O   . HOH   G 6 .   ? 0.009  12.931  16.940 1.00 22.10 ? 505 HOH   A O   1 
HETATM 1343 O  O   . HOH   G 6 .   ? 11.909 -13.112 6.650  1.00 21.01 ? 506 HOH   A O   1 
HETATM 1344 O  O   . HOH   G 6 .   ? 30.898 1.337   15.759 1.00 29.50 ? 507 HOH   A O   1 
HETATM 1345 O  O   . HOH   G 6 .   ? 19.254 -7.069  31.241 1.00 20.35 ? 508 HOH   A O   1 
HETATM 1346 O  O   . HOH   G 6 .   ? 37.870 19.570  11.216 1.00 39.11 ? 509 HOH   A O   1 
HETATM 1347 O  O   . HOH   G 6 .   ? 9.406  24.198  12.417 1.00 36.02 ? 510 HOH   A O   1 
HETATM 1348 O  O   . HOH   G 6 .   ? 8.945  10.278  29.788 0.85 15.78 ? 511 HOH   A O   1 
HETATM 1349 O  O   . HOH   G 6 .   ? 27.152 14.078  23.828 1.00 34.18 ? 512 HOH   A O   1 
HETATM 1350 O  O   . HOH   G 6 .   ? 14.647 12.143  -2.251 1.00 20.54 ? 513 HOH   A O   1 
HETATM 1351 O  O   . HOH   G 6 .   ? 5.432  12.358  28.177 1.00 11.71 ? 514 HOH   A O   1 
HETATM 1352 O  O   . HOH   G 6 .   ? 37.564 17.604  13.606 1.00 28.69 ? 515 HOH   A O   1 
HETATM 1353 O  O   . HOH   G 6 .   ? 3.271  17.366  25.198 1.00 27.86 ? 516 HOH   A O   1 
HETATM 1354 O  O   . HOH   G 6 .   ? 8.523  13.492  -0.183 0.85 30.06 ? 517 HOH   A O   1 
HETATM 1355 O  O   . HOH   G 6 .   ? 32.322 6.390   14.305 1.00 38.92 ? 518 HOH   A O   1 
HETATM 1356 O  O   . HOH   G 6 .   ? 10.776 25.399  14.545 1.00 14.51 ? 519 HOH   A O   1 
HETATM 1357 O  O   . HOH   G 6 .   ? -2.920 29.838  15.526 1.00 32.49 ? 520 HOH   A O   1 
HETATM 1358 O  O   . HOH   G 6 .   ? 0.288  13.347  19.380 1.00 22.60 ? 521 HOH   A O   1 
HETATM 1359 O  O   . HOH   G 6 .   ? 9.885  14.701  28.621 1.00 17.37 ? 522 HOH   A O   1 
HETATM 1360 O  O   . HOH   G 6 .   ? 4.006  -5.300  24.063 1.00 40.73 ? 523 HOH   A O   1 
HETATM 1361 O  O   . HOH   G 6 .   ? 20.956 11.920  -4.089 1.00 27.47 ? 524 HOH   A O   1 
HETATM 1362 O  O   . HOH   G 6 .   ? 6.623  23.908  8.485  1.00 23.04 ? 525 HOH   A O   1 
HETATM 1363 O  O   . HOH   G 6 .   ? 25.900 -4.649  -1.719 0.50 15.68 ? 526 HOH   A O   1 
HETATM 1364 O  O   . HOH   G 6 .   ? 7.718  12.991  30.045 0.85 29.34 ? 527 HOH   A O   1 
HETATM 1365 O  O   . HOH   G 6 .   ? 33.515 6.493   20.387 1.00 37.69 ? 528 HOH   A O   1 
HETATM 1366 O  O   . HOH   G 6 .   ? 15.100 -14.147 2.453  1.00 42.10 ? 529 HOH   A O   1 
HETATM 1367 O  O   . HOH   G 6 .   ? 40.246 18.497  13.193 1.00 19.82 ? 530 HOH   A O   1 
HETATM 1368 O  O   . HOH   G 6 .   ? 34.482 10.321  22.391 1.00 36.76 ? 531 HOH   A O   1 
HETATM 1369 O  O   . HOH   G 6 .   ? 2.924  24.242  4.403  1.00 44.76 ? 532 HOH   A O   1 
# 
