data_7HZN
# 
_entry.id   7HZN 
# 
_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   7HZN         pdb_00007hzn 10.2210/pdb7hzn/pdb 
WWPDB D_1001408131 ?            ?                   
# 
_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                        7HZN 
_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           Y 
_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    5   ?         ? ? ? 
4 non-polymer syn 'SULFATE ION'                      96.063    1   ?         ? ? ? 
5 non-polymer syn N,N-dimethylpyridine-3-sulfonamide 186.231   1   ?         ? ? ? 
6 water       nat water                              18.015    239 ?         ? ? ? 
# 
_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 N,N-dimethylpyridine-3-sulfonamide ZUG 
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 
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  
ZUG non-polymer         . N,N-dimethylpyridine-3-sulfonamide ? 'C7 H10 N2 O2 S' 186.231 
# 
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        ZUG 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   ZUG 
_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 -1  DMS DMS A . 
D 3 DMS 1   203 0   DMS DMS A . 
E 3 DMS 1   204 1   DMS DMS A . 
F 3 DMS 1   205 3   DMS DMS A . 
G 3 DMS 1   206 6   DMS DMS A . 
H 4 SO4 1   207 1   SO4 SO4 A . 
I 5 ZUG 1   208 246 ZUG LIG A . 
J 6 HOH 1   301 137 HOH HOH A . 
J 6 HOH 2   302 227 HOH HOH A . 
J 6 HOH 3   303 150 HOH HOH A . 
J 6 HOH 4   304 215 HOH HOH A . 
J 6 HOH 5   305 238 HOH HOH A . 
J 6 HOH 6   306 3   HOH HOH A . 
J 6 HOH 7   307 193 HOH HOH A . 
J 6 HOH 8   308 34  HOH HOH A . 
J 6 HOH 9   309 107 HOH HOH A . 
J 6 HOH 10  310 133 HOH HOH A . 
J 6 HOH 11  311 217 HOH HOH A . 
J 6 HOH 12  312 30  HOH HOH A . 
J 6 HOH 13  313 152 HOH HOH A . 
J 6 HOH 14  314 248 HOH HOH A . 
J 6 HOH 15  315 186 HOH HOH A . 
J 6 HOH 16  316 148 HOH HOH A . 
J 6 HOH 17  317 57  HOH HOH A . 
J 6 HOH 18  318 116 HOH HOH A . 
J 6 HOH 19  319 191 HOH HOH A . 
J 6 HOH 20  320 103 HOH HOH A . 
J 6 HOH 21  321 147 HOH HOH A . 
J 6 HOH 22  322 234 HOH HOH A . 
J 6 HOH 23  323 4   HOH HOH A . 
J 6 HOH 24  324 52  HOH HOH A . 
J 6 HOH 25  325 77  HOH HOH A . 
J 6 HOH 26  326 47  HOH HOH A . 
J 6 HOH 27  327 131 HOH HOH A . 
J 6 HOH 28  328 181 HOH HOH A . 
J 6 HOH 29  329 178 HOH HOH A . 
J 6 HOH 30  330 59  HOH HOH A . 
J 6 HOH 31  331 173 HOH HOH A . 
J 6 HOH 32  332 180 HOH HOH A . 
J 6 HOH 33  333 124 HOH HOH A . 
J 6 HOH 34  334 211 HOH HOH A . 
J 6 HOH 35  335 46  HOH HOH A . 
J 6 HOH 36  336 68  HOH HOH A . 
J 6 HOH 37  337 16  HOH HOH A . 
J 6 HOH 38  338 138 HOH HOH A . 
J 6 HOH 39  339 249 HOH HOH A . 
J 6 HOH 40  340 37  HOH HOH A . 
J 6 HOH 41  341 88  HOH HOH A . 
J 6 HOH 42  342 104 HOH HOH A . 
J 6 HOH 43  343 29  HOH HOH A . 
J 6 HOH 44  344 33  HOH HOH A . 
J 6 HOH 45  345 72  HOH HOH A . 
J 6 HOH 46  346 60  HOH HOH A . 
J 6 HOH 47  347 94  HOH HOH A . 
J 6 HOH 48  348 21  HOH HOH A . 
J 6 HOH 49  349 81  HOH HOH A . 
J 6 HOH 50  350 27  HOH HOH A . 
J 6 HOH 51  351 7   HOH HOH A . 
J 6 HOH 52  352 144 HOH HOH A . 
J 6 HOH 53  353 13  HOH HOH A . 
J 6 HOH 54  354 2   HOH HOH A . 
J 6 HOH 55  355 205 HOH HOH A . 
J 6 HOH 56  356 109 HOH HOH A . 
J 6 HOH 57  357 141 HOH HOH A . 
J 6 HOH 58  358 67  HOH HOH A . 
J 6 HOH 59  359 53  HOH HOH A . 
J 6 HOH 60  360 24  HOH HOH A . 
J 6 HOH 61  361 97  HOH HOH A . 
J 6 HOH 62  362 49  HOH HOH A . 
J 6 HOH 63  363 170 HOH HOH A . 
J 6 HOH 64  364 184 HOH HOH A . 
J 6 HOH 65  365 96  HOH HOH A . 
J 6 HOH 66  366 168 HOH HOH A . 
J 6 HOH 67  367 247 HOH HOH A . 
J 6 HOH 68  368 167 HOH HOH A . 
J 6 HOH 69  369 43  HOH HOH A . 
J 6 HOH 70  370 119 HOH HOH A . 
J 6 HOH 71  371 161 HOH HOH A . 
J 6 HOH 72  372 28  HOH HOH A . 
J 6 HOH 73  373 197 HOH HOH A . 
J 6 HOH 74  374 169 HOH HOH A . 
J 6 HOH 75  375 216 HOH HOH A . 
J 6 HOH 76  376 79  HOH HOH A . 
J 6 HOH 77  377 182 HOH HOH A . 
J 6 HOH 78  378 14  HOH HOH A . 
J 6 HOH 79  379 71  HOH HOH A . 
J 6 HOH 80  380 25  HOH HOH A . 
J 6 HOH 81  381 90  HOH HOH A . 
J 6 HOH 82  382 63  HOH HOH A . 
J 6 HOH 83  383 91  HOH HOH A . 
J 6 HOH 84  384 108 HOH HOH A . 
J 6 HOH 85  385 113 HOH HOH A . 
J 6 HOH 86  386 179 HOH HOH A . 
J 6 HOH 87  387 26  HOH HOH A . 
J 6 HOH 88  388 42  HOH HOH A . 
J 6 HOH 89  389 36  HOH HOH A . 
J 6 HOH 90  390 9   HOH HOH A . 
J 6 HOH 91  391 45  HOH HOH A . 
J 6 HOH 92  392 195 HOH HOH A . 
J 6 HOH 93  393 183 HOH HOH A . 
J 6 HOH 94  394 62  HOH HOH A . 
J 6 HOH 95  395 20  HOH HOH A . 
J 6 HOH 96  396 19  HOH HOH A . 
J 6 HOH 97  397 54  HOH HOH A . 
J 6 HOH 98  398 204 HOH HOH A . 
J 6 HOH 99  399 100 HOH HOH A . 
J 6 HOH 100 400 118 HOH HOH A . 
J 6 HOH 101 401 15  HOH HOH A . 
J 6 HOH 102 402 55  HOH HOH A . 
J 6 HOH 103 403 174 HOH HOH A . 
J 6 HOH 104 404 66  HOH HOH A . 
J 6 HOH 105 405 48  HOH HOH A . 
J 6 HOH 106 406 177 HOH HOH A . 
J 6 HOH 107 407 50  HOH HOH A . 
J 6 HOH 108 408 12  HOH HOH A . 
J 6 HOH 109 409 78  HOH HOH A . 
J 6 HOH 110 410 82  HOH HOH A . 
J 6 HOH 111 411 245 HOH HOH A . 
J 6 HOH 112 412 111 HOH HOH A . 
J 6 HOH 113 413 95  HOH HOH A . 
J 6 HOH 114 414 212 HOH HOH A . 
J 6 HOH 115 415 112 HOH HOH A . 
J 6 HOH 116 416 121 HOH HOH A . 
J 6 HOH 117 417 84  HOH HOH A . 
J 6 HOH 118 418 40  HOH HOH A . 
J 6 HOH 119 419 106 HOH HOH A . 
J 6 HOH 120 420 35  HOH HOH A . 
J 6 HOH 121 421 105 HOH HOH A . 
J 6 HOH 122 422 41  HOH HOH A . 
J 6 HOH 123 423 176 HOH HOH A . 
J 6 HOH 124 424 70  HOH HOH A . 
J 6 HOH 125 425 214 HOH HOH A . 
J 6 HOH 126 426 219 HOH HOH A . 
J 6 HOH 127 427 155 HOH HOH A . 
J 6 HOH 128 428 146 HOH HOH A . 
J 6 HOH 129 429 126 HOH HOH A . 
J 6 HOH 130 430 80  HOH HOH A . 
J 6 HOH 131 431 38  HOH HOH A . 
J 6 HOH 132 432 17  HOH HOH A . 
J 6 HOH 133 433 18  HOH HOH A . 
J 6 HOH 134 434 220 HOH HOH A . 
J 6 HOH 135 435 58  HOH HOH A . 
J 6 HOH 136 436 5   HOH HOH A . 
J 6 HOH 137 437 120 HOH HOH A . 
J 6 HOH 138 438 11  HOH HOH A . 
J 6 HOH 139 439 64  HOH HOH A . 
J 6 HOH 140 440 76  HOH HOH A . 
J 6 HOH 141 441 102 HOH HOH A . 
J 6 HOH 142 442 132 HOH HOH A . 
J 6 HOH 143 443 31  HOH HOH A . 
J 6 HOH 144 444 198 HOH HOH A . 
J 6 HOH 145 445 213 HOH HOH A . 
J 6 HOH 146 446 39  HOH HOH A . 
J 6 HOH 147 447 69  HOH HOH A . 
J 6 HOH 148 448 237 HOH HOH A . 
J 6 HOH 149 449 192 HOH HOH A . 
J 6 HOH 150 450 203 HOH HOH A . 
J 6 HOH 151 451 10  HOH HOH A . 
J 6 HOH 152 452 51  HOH HOH A . 
J 6 HOH 153 453 101 HOH HOH A . 
J 6 HOH 154 454 93  HOH HOH A . 
J 6 HOH 155 455 224 HOH HOH A . 
J 6 HOH 156 456 23  HOH HOH A . 
J 6 HOH 157 457 136 HOH HOH A . 
J 6 HOH 158 458 135 HOH HOH A . 
J 6 HOH 159 459 89  HOH HOH A . 
J 6 HOH 160 460 6   HOH HOH A . 
J 6 HOH 161 461 123 HOH HOH A . 
J 6 HOH 162 462 74  HOH HOH A . 
J 6 HOH 163 463 200 HOH HOH A . 
J 6 HOH 164 464 230 HOH HOH A . 
J 6 HOH 165 465 61  HOH HOH A . 
J 6 HOH 166 466 159 HOH HOH A . 
J 6 HOH 167 467 251 HOH HOH A . 
J 6 HOH 168 468 156 HOH HOH A . 
J 6 HOH 169 469 110 HOH HOH A . 
J 6 HOH 170 470 218 HOH HOH A . 
J 6 HOH 171 471 171 HOH HOH A . 
J 6 HOH 172 472 210 HOH HOH A . 
J 6 HOH 173 473 233 HOH HOH A . 
J 6 HOH 174 474 117 HOH HOH A . 
J 6 HOH 175 475 22  HOH HOH A . 
J 6 HOH 176 476 226 HOH HOH A . 
J 6 HOH 177 477 246 HOH HOH A . 
J 6 HOH 178 478 231 HOH HOH A . 
J 6 HOH 179 479 158 HOH HOH A . 
J 6 HOH 180 480 98  HOH HOH A . 
J 6 HOH 181 481 175 HOH HOH A . 
J 6 HOH 182 482 65  HOH HOH A . 
J 6 HOH 183 483 154 HOH HOH A . 
J 6 HOH 184 484 87  HOH HOH A . 
J 6 HOH 185 485 201 HOH HOH A . 
J 6 HOH 186 486 228 HOH HOH A . 
J 6 HOH 187 487 250 HOH HOH A . 
J 6 HOH 188 488 162 HOH HOH A . 
J 6 HOH 189 489 157 HOH HOH A . 
J 6 HOH 190 490 151 HOH HOH A . 
J 6 HOH 191 491 207 HOH HOH A . 
J 6 HOH 192 492 134 HOH HOH A . 
J 6 HOH 193 493 239 HOH HOH A . 
J 6 HOH 194 494 99  HOH HOH A . 
J 6 HOH 195 495 140 HOH HOH A . 
J 6 HOH 196 496 240 HOH HOH A . 
J 6 HOH 197 497 253 HOH HOH A . 
J 6 HOH 198 498 127 HOH HOH A . 
J 6 HOH 199 499 83  HOH HOH A . 
J 6 HOH 200 500 225 HOH HOH A . 
J 6 HOH 201 501 199 HOH HOH A . 
J 6 HOH 202 502 86  HOH HOH A . 
J 6 HOH 203 503 223 HOH HOH A . 
J 6 HOH 204 504 232 HOH HOH A . 
J 6 HOH 205 505 190 HOH HOH A . 
J 6 HOH 206 506 73  HOH HOH A . 
J 6 HOH 207 507 172 HOH HOH A . 
J 6 HOH 208 508 221 HOH HOH A . 
J 6 HOH 209 509 185 HOH HOH A . 
J 6 HOH 210 510 163 HOH HOH A . 
J 6 HOH 211 511 122 HOH HOH A . 
J 6 HOH 212 512 229 HOH HOH A . 
J 6 HOH 213 513 189 HOH HOH A . 
J 6 HOH 214 514 85  HOH HOH A . 
J 6 HOH 215 515 32  HOH HOH A . 
J 6 HOH 216 516 209 HOH HOH A . 
J 6 HOH 217 517 202 HOH HOH A . 
J 6 HOH 218 518 129 HOH HOH A . 
J 6 HOH 219 519 252 HOH HOH A . 
J 6 HOH 220 520 165 HOH HOH A . 
J 6 HOH 221 521 236 HOH HOH A . 
J 6 HOH 222 522 56  HOH HOH A . 
J 6 HOH 223 523 208 HOH HOH A . 
J 6 HOH 224 524 187 HOH HOH A . 
J 6 HOH 225 525 142 HOH HOH A . 
J 6 HOH 226 526 114 HOH HOH A . 
J 6 HOH 227 527 241 HOH HOH A . 
J 6 HOH 228 528 75  HOH HOH A . 
J 6 HOH 229 529 235 HOH HOH A . 
J 6 HOH 230 530 206 HOH HOH A . 
J 6 HOH 231 531 153 HOH HOH A . 
J 6 HOH 232 532 222 HOH HOH A . 
J 6 HOH 233 533 92  HOH HOH A . 
J 6 HOH 234 534 125 HOH HOH A . 
J 6 HOH 235 535 160 HOH HOH A . 
J 6 HOH 236 536 243 HOH HOH A . 
J 6 HOH 237 537 242 HOH HOH A . 
J 6 HOH 238 538 164 HOH HOH A . 
J 6 HOH 239 539 244 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           7HZN 
_cell.length_a           86.973 
_cell.length_b           56.731 
_cell.length_c           32.645 
_cell.angle_alpha        90.00 
_cell.angle_beta         95.46 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HZN 
_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          7HZN 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.52 
_exptl_crystal.density_percent_sol   51.23 
_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   2024-09-05 
_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   0.92134 
_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        0.92134 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HZN 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             47.51 
_reflns.d_resolution_high            1.33 
_reflns.number_obs                   35567 
_reflns.percent_possible_obs         97.8 
_reflns.pdbx_Rmerge_I_obs            0.116 
_reflns.pdbx_netI_over_sigmaI        11.1 
_reflns.pdbx_redundancy              5.8 
_reflns.pdbx_Rrim_I_all              0.126 
_reflns.pdbx_Rpim_I_all              0.050 
_reflns.pdbx_CC_half                 0.996 
_reflns.pdbx_number_measured_all     207562 
_reflns.pdbx_chi_squared             0.68 
_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                  1.33 
_reflns_shell.d_res_low                   1.35 
_reflns_shell.number_measured_all         4432 
_reflns_shell.number_unique_obs           1438 
_reflns_shell.Rmerge_I_obs                1.710 
_reflns_shell.pdbx_chi_squared            0.18 
_reflns_shell.pdbx_redundancy             3.1 
_reflns_shell.percent_possible_obs        75.8 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.6 
_reflns_shell.pdbx_Rrim_I_all             2.084 
_reflns_shell.pdbx_Rpim_I_all             1.155 
_reflns_shell.pdbx_CC_half                0.279 
_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                                 7HZN 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     33578 
_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                             47.45 
_refine.ls_d_res_high                            1.33 
_refine.ls_percent_reflns_obs                    97.00 
_refine.ls_R_factor_obs                          0.18395 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.18319 
_refine.ls_R_factor_R_free                       0.19796 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  1772 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.961 
_refine.correlation_coeff_Fo_to_Fc_free          0.956 
_refine.B_iso_mean                               16.312 
_refine.aniso_B[1][1]                            -0.20 
_refine.aniso_B[2][2]                            0.74 
_refine.aniso_B[3][3]                            -0.45 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.39 
_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                       0.059 
_refine.pdbx_overall_ESU_R_Free                  0.058 
_refine.overall_SU_ML                            0.054 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             1.414 
_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         38 
_refine_hist.number_atoms_solvent             239 
_refine_hist.number_atoms_total               1360 
_refine_hist.d_res_high                       1.33 
_refine_hist.d_res_low                        47.45 
# 
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             0.011  0.013  ? 1435 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.015  ? 1201 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.717  1.617  ? 1806 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.392  1.600  ? 2764 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.062  5.000  ? 169  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       32.904 21.385 ? 65   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       11.383 15.000 ? 199  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       24.443 15.000 ? 9    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.088  0.200  ? 165  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.010  0.020  ? 1592 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.001  0.020  ? 310  '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                  1.276  1.444  ? 714  'X-RAY DIFFRACTION' ? 
r_mcbond_other               1.280  1.440  ? 710  'X-RAY DIFFRACTION' ? 
r_mcangle_it                 1.989  2.136  ? 831  'X-RAY DIFFRACTION' ? 
r_mcangle_other              1.988  2.139  ? 832  'X-RAY DIFFRACTION' ? 
r_scbond_it                  2.028  1.766  ? 719  'X-RAY DIFFRACTION' ? 
r_scbond_other               1.945  1.733  ? 718  'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              2.789  2.502  ? 970  'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       5.972  19.479 ? 1517 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         5.970  19.494 ? 1518 '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                       1.329 
_refine_ls_shell.d_res_low                        1.363 
_refine_ls_shell.number_reflns_R_work             1772 
_refine_ls_shell.R_factor_R_work                  0.355 
_refine_ls_shell.percent_reflns_obs               68.72 
_refine_ls_shell.R_factor_R_free                  0.332 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             87 
_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                  7HZN 
_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-0018764-002 (A71EV2A-x2448)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HZN 
_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 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 4 ? 
I N N 5 ? 
J 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              7HZN 
_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,H,I,J 
# 
_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 ? ? ? ? ? ? ? 2.337 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 B ZN . ZN ? ? A CYS 58  A ZN 201 1_555 ? ? ? ? ? ? ? 2.324 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 B ZN . ZN ? ? A CYS 116 A ZN 201 1_555 ? ? ? ? ? ? ? 2.302 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 B ZN . ZN ? ? A HIS 118 A ZN 201 1_555 ? ? ? ? ? ? ? 2.014 ? ? 
# 
_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_555 108.9 ? 
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_555 106.2 ? 
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_555 106.9 ? 
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_555 100.5 ? 
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_555 116.2 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
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 
AA1 3 4 ? 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 ILE A 4   ? VAL A 6   ? ILE A 10  VAL A 12  
AA1 2 TYR A 9   ? ASN A 13  ? TYR A 15  ASN A 19  
AA1 3 LEU A 34  ? SER A 38  ? LEU A 40  SER A 44  
AA1 4 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
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 ? THR A 120 ? GLY A 119 THR A 126 
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 ILE A 4   ? N ILE A 10  O VAL A 11  ? O VAL A 17  
AA1 2 3 N VAL A 12  ? N VAL A 18  O LEU A 35  ? O LEU A 41  
AA1 3 4 O VAL A 36  ? O VAL A 42  N VAL A 26  ? N VAL A 32  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N CYS A 110 ? N CYS A 116 O GLY A 113 ? O GLY A 119 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O VAL A 126 ? O VAL A 132 N ALA A 95  ? N ALA A 101 
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7HZN 
_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 314 ? ? O A HOH 468 ? ? 1.90 
2 1 OE1 A GLU 106 ? ? O A HOH 301 ? ? 2.06 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O2 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    SO4 
_pdbx_validate_symm_contact.auth_seq_id_1     207 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O2 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    SO4 
_pdbx_validate_symm_contact.auth_seq_id_2     207 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_556 
_pdbx_validate_symm_contact.dist              1.59 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       539 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   7.73 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
DMS S    S  N N 88  
DMS O    O  N N 89  
DMS C1   C  N N 90  
DMS C2   C  N N 91  
DMS H11  H  N N 92  
DMS H12  H  N N 93  
DMS H13  H  N N 94  
DMS H21  H  N N 95  
DMS H22  H  N N 96  
DMS H23  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
LEU N    N  N N 193 
LEU CA   C  N S 194 
LEU C    C  N N 195 
LEU O    O  N N 196 
LEU CB   C  N N 197 
LEU CG   C  N N 198 
LEU CD1  C  N N 199 
LEU CD2  C  N N 200 
LEU OXT  O  N N 201 
LEU H    H  N N 202 
LEU H2   H  N N 203 
LEU HA   H  N N 204 
LEU HB2  H  N N 205 
LEU HB3  H  N N 206 
LEU HG   H  N N 207 
LEU HD11 H  N N 208 
LEU HD12 H  N N 209 
LEU HD13 H  N N 210 
LEU HD21 H  N N 211 
LEU HD22 H  N N 212 
LEU HD23 H  N N 213 
LEU HXT  H  N N 214 
LYS N    N  N N 215 
LYS CA   C  N S 216 
LYS C    C  N N 217 
LYS O    O  N N 218 
LYS CB   C  N N 219 
LYS CG   C  N N 220 
LYS CD   C  N N 221 
LYS CE   C  N N 222 
LYS NZ   N  N N 223 
LYS OXT  O  N N 224 
LYS H    H  N N 225 
LYS H2   H  N N 226 
LYS HA   H  N N 227 
LYS HB2  H  N N 228 
LYS HB3  H  N N 229 
LYS HG2  H  N N 230 
LYS HG3  H  N N 231 
LYS HD2  H  N N 232 
LYS HD3  H  N N 233 
LYS HE2  H  N N 234 
LYS HE3  H  N N 235 
LYS HZ1  H  N N 236 
LYS HZ2  H  N N 237 
LYS HZ3  H  N N 238 
LYS HXT  H  N N 239 
MET N    N  N N 240 
MET CA   C  N S 241 
MET C    C  N N 242 
MET O    O  N N 243 
MET CB   C  N N 244 
MET CG   C  N N 245 
MET SD   S  N N 246 
MET CE   C  N N 247 
MET OXT  O  N N 248 
MET H    H  N N 249 
MET H2   H  N N 250 
MET HA   H  N N 251 
MET HB2  H  N N 252 
MET HB3  H  N N 253 
MET HG2  H  N N 254 
MET HG3  H  N N 255 
MET HE1  H  N N 256 
MET HE2  H  N N 257 
MET HE3  H  N N 258 
MET HXT  H  N N 259 
PHE N    N  N N 260 
PHE CA   C  N S 261 
PHE C    C  N N 262 
PHE O    O  N N 263 
PHE CB   C  N N 264 
PHE CG   C  Y N 265 
PHE CD1  C  Y N 266 
PHE CD2  C  Y N 267 
PHE CE1  C  Y N 268 
PHE CE2  C  Y N 269 
PHE CZ   C  Y N 270 
PHE OXT  O  N N 271 
PHE H    H  N N 272 
PHE H2   H  N N 273 
PHE HA   H  N N 274 
PHE HB2  H  N N 275 
PHE HB3  H  N N 276 
PHE HD1  H  N N 277 
PHE HD2  H  N N 278 
PHE HE1  H  N N 279 
PHE HE2  H  N N 280 
PHE HZ   H  N N 281 
PHE HXT  H  N N 282 
PRO N    N  N N 283 
PRO CA   C  N S 284 
PRO C    C  N N 285 
PRO O    O  N N 286 
PRO CB   C  N N 287 
PRO CG   C  N N 288 
PRO CD   C  N N 289 
PRO OXT  O  N N 290 
PRO H    H  N N 291 
PRO HA   H  N N 292 
PRO HB2  H  N N 293 
PRO HB3  H  N N 294 
PRO HG2  H  N N 295 
PRO HG3  H  N N 296 
PRO HD2  H  N N 297 
PRO HD3  H  N N 298 
PRO HXT  H  N N 299 
SER N    N  N N 300 
SER CA   C  N S 301 
SER C    C  N N 302 
SER O    O  N N 303 
SER CB   C  N N 304 
SER OG   O  N N 305 
SER OXT  O  N N 306 
SER H    H  N N 307 
SER H2   H  N N 308 
SER HA   H  N N 309 
SER HB2  H  N N 310 
SER HB3  H  N N 311 
SER HG   H  N N 312 
SER HXT  H  N N 313 
SO4 S    S  N N 314 
SO4 O1   O  N N 315 
SO4 O2   O  N N 316 
SO4 O3   O  N N 317 
SO4 O4   O  N N 318 
THR N    N  N N 319 
THR CA   C  N S 320 
THR C    C  N N 321 
THR O    O  N N 322 
THR CB   C  N R 323 
THR OG1  O  N N 324 
THR CG2  C  N N 325 
THR OXT  O  N N 326 
THR H    H  N N 327 
THR H2   H  N N 328 
THR HA   H  N N 329 
THR HB   H  N N 330 
THR HG1  H  N N 331 
THR HG21 H  N N 332 
THR HG22 H  N N 333 
THR HG23 H  N N 334 
THR HXT  H  N N 335 
TRP N    N  N N 336 
TRP CA   C  N S 337 
TRP C    C  N N 338 
TRP O    O  N N 339 
TRP CB   C  N N 340 
TRP CG   C  Y N 341 
TRP CD1  C  Y N 342 
TRP CD2  C  Y N 343 
TRP NE1  N  Y N 344 
TRP CE2  C  Y N 345 
TRP CE3  C  Y N 346 
TRP CZ2  C  Y N 347 
TRP CZ3  C  Y N 348 
TRP CH2  C  Y N 349 
TRP OXT  O  N N 350 
TRP H    H  N N 351 
TRP H2   H  N N 352 
TRP HA   H  N N 353 
TRP HB2  H  N N 354 
TRP HB3  H  N N 355 
TRP HD1  H  N N 356 
TRP HE1  H  N N 357 
TRP HE3  H  N N 358 
TRP HZ2  H  N N 359 
TRP HZ3  H  N N 360 
TRP HH2  H  N N 361 
TRP HXT  H  N N 362 
TYR N    N  N N 363 
TYR CA   C  N S 364 
TYR C    C  N N 365 
TYR O    O  N N 366 
TYR CB   C  N N 367 
TYR CG   C  Y N 368 
TYR CD1  C  Y N 369 
TYR CD2  C  Y N 370 
TYR CE1  C  Y N 371 
TYR CE2  C  Y N 372 
TYR CZ   C  Y N 373 
TYR OH   O  N N 374 
TYR OXT  O  N N 375 
TYR H    H  N N 376 
TYR H2   H  N N 377 
TYR HA   H  N N 378 
TYR HB2  H  N N 379 
TYR HB3  H  N N 380 
TYR HD1  H  N N 381 
TYR HD2  H  N N 382 
TYR HE1  H  N N 383 
TYR HE2  H  N N 384 
TYR HH   H  N N 385 
TYR HXT  H  N N 386 
VAL N    N  N N 387 
VAL CA   C  N S 388 
VAL C    C  N N 389 
VAL O    O  N N 390 
VAL CB   C  N N 391 
VAL CG1  C  N N 392 
VAL CG2  C  N N 393 
VAL OXT  O  N N 394 
VAL H    H  N N 395 
VAL H2   H  N N 396 
VAL HA   H  N N 397 
VAL HB   H  N N 398 
VAL HG11 H  N N 399 
VAL HG12 H  N N 400 
VAL HG13 H  N N 401 
VAL HG21 H  N N 402 
VAL HG22 H  N N 403 
VAL HG23 H  N N 404 
VAL HXT  H  N N 405 
ZN  ZN   ZN N N 406 
ZUG N1   N  N N 407 
ZUG C4   C  Y N 408 
ZUG C5   C  Y N 409 
ZUG C6   C  Y N 410 
ZUG C7   C  Y N 411 
ZUG C1   C  N N 412 
ZUG C2   C  N N 413 
ZUG S1   S  N N 414 
ZUG O1   O  N N 415 
ZUG O2   O  N N 416 
ZUG C3   C  Y N 417 
ZUG N2   N  Y N 418 
ZUG H1   H  N N 419 
ZUG H2   H  N N 420 
ZUG H3   H  N N 421 
ZUG H4   H  N N 422 
ZUG H5   H  N N 423 
ZUG H6   H  N N 424 
ZUG H7   H  N N 425 
ZUG H8   H  N N 426 
ZUG H9   H  N N 427 
ZUG H10  H  N N 428 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
SO4 S   O1   doub N N 299 
SO4 S   O2   doub N N 300 
SO4 S   O3   sing N N 301 
SO4 S   O4   sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TRP N   CA   sing N N 319 
TRP N   H    sing N N 320 
TRP N   H2   sing N N 321 
TRP CA  C    sing N N 322 
TRP CA  CB   sing N N 323 
TRP CA  HA   sing N N 324 
TRP C   O    doub N N 325 
TRP C   OXT  sing N N 326 
TRP CB  CG   sing N N 327 
TRP CB  HB2  sing N N 328 
TRP CB  HB3  sing N N 329 
TRP CG  CD1  doub Y N 330 
TRP CG  CD2  sing Y N 331 
TRP CD1 NE1  sing Y N 332 
TRP CD1 HD1  sing N N 333 
TRP CD2 CE2  doub Y N 334 
TRP CD2 CE3  sing Y N 335 
TRP NE1 CE2  sing Y N 336 
TRP NE1 HE1  sing N N 337 
TRP CE2 CZ2  sing Y N 338 
TRP CE3 CZ3  doub Y N 339 
TRP CE3 HE3  sing N N 340 
TRP CZ2 CH2  doub Y N 341 
TRP CZ2 HZ2  sing N N 342 
TRP CZ3 CH2  sing Y N 343 
TRP CZ3 HZ3  sing N N 344 
TRP CH2 HH2  sing N N 345 
TRP OXT HXT  sing N N 346 
TYR N   CA   sing N N 347 
TYR N   H    sing N N 348 
TYR N   H2   sing N N 349 
TYR CA  C    sing N N 350 
TYR CA  CB   sing N N 351 
TYR CA  HA   sing N N 352 
TYR C   O    doub N N 353 
TYR C   OXT  sing N N 354 
TYR CB  CG   sing N N 355 
TYR CB  HB2  sing N N 356 
TYR CB  HB3  sing N N 357 
TYR CG  CD1  doub Y N 358 
TYR CG  CD2  sing Y N 359 
TYR CD1 CE1  sing Y N 360 
TYR CD1 HD1  sing N N 361 
TYR CD2 CE2  doub Y N 362 
TYR CD2 HD2  sing N N 363 
TYR CE1 CZ   doub Y N 364 
TYR CE1 HE1  sing N N 365 
TYR CE2 CZ   sing Y N 366 
TYR CE2 HE2  sing N N 367 
TYR CZ  OH   sing N N 368 
TYR OH  HH   sing N N 369 
TYR OXT HXT  sing N N 370 
VAL N   CA   sing N N 371 
VAL N   H    sing N N 372 
VAL N   H2   sing N N 373 
VAL CA  C    sing N N 374 
VAL CA  CB   sing N N 375 
VAL CA  HA   sing N N 376 
VAL C   O    doub N N 377 
VAL C   OXT  sing N N 378 
VAL CB  CG1  sing N N 379 
VAL CB  CG2  sing N N 380 
VAL CB  HB   sing N N 381 
VAL CG1 HG11 sing N N 382 
VAL CG1 HG12 sing N N 383 
VAL CG1 HG13 sing N N 384 
VAL CG2 HG21 sing N N 385 
VAL CG2 HG22 sing N N 386 
VAL CG2 HG23 sing N N 387 
VAL OXT HXT  sing N N 388 
ZUG C5  C6   doub Y N 389 
ZUG C5  C4   sing Y N 390 
ZUG C2  N1   sing N N 391 
ZUG C6  N2   sing Y N 392 
ZUG C4  C3   doub Y N 393 
ZUG N2  C7   doub Y N 394 
ZUG N1  C1   sing N N 395 
ZUG N1  S1   sing N N 396 
ZUG C3  C7   sing Y N 397 
ZUG C3  S1   sing N N 398 
ZUG O1  S1   doub N N 399 
ZUG S1  O2   doub N N 400 
ZUG C4  H1   sing N N 401 
ZUG C5  H2   sing N N 402 
ZUG C6  H3   sing N N 403 
ZUG C7  H4   sing N N 404 
ZUG C1  H5   sing N N 405 
ZUG C1  H6   sing N N 406 
ZUG C1  H7   sing N N 407 
ZUG C2  H8   sing N N 408 
ZUG C2  H9   sing N N 409 
ZUG C2  H10  sing N N 410 
# 
_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                    7HZN 
_atom_sites.fract_transf_matrix[1][1]   0.011498 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001100 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017627 
_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]   0.030772 
_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   ? 18.088 6.518   24.895 1.00 17.00  ? 7   SER A N   1 
ATOM   2    C  CA  . SER A 1 1   ? 19.297 6.633   24.094 1.00 16.07  ? 7   SER A CA  1 
ATOM   3    C  C   . SER A 1 1   ? 19.370 5.490   23.084 1.00 16.04  ? 7   SER A C   1 
ATOM   4    O  O   . SER A 1 1   ? 18.656 4.468   23.238 1.00 17.76  ? 7   SER A O   1 
ATOM   5    C  CB  . SER A 1 1   ? 20.540 6.661   24.956 1.00 20.10  ? 7   SER A CB  1 
ATOM   6    O  OG  . SER A 1 1   ? 20.597 5.443   25.655 1.00 22.39  ? 7   SER A OG  1 
ATOM   7    N  N   . GLY A 1 2   ? 20.206 5.671   22.101 1.00 15.82  ? 8   GLY A N   1 
ATOM   8    C  CA  . GLY A 1 2   ? 20.482 4.655   21.087 1.00 14.84  ? 8   GLY A CA  1 
ATOM   9    C  C   . GLY A 1 2   ? 20.786 5.243   19.741 1.00 14.02  ? 8   GLY A C   1 
ATOM   10   O  O   . GLY A 1 2   ? 20.485 6.398   19.472 1.00 17.51  ? 8   GLY A O   1 
ATOM   11   N  N   . ALA A 1 3   ? 21.440 4.442   18.906 1.00 13.61  ? 9   ALA A N   1 
ATOM   12   C  CA  . ALA A 1 3   ? 21.881 4.850   17.564 1.00 13.22  ? 9   ALA A CA  1 
ATOM   13   C  C   . ALA A 1 3   ? 21.741 3.687   16.595 1.00 12.08  ? 9   ALA A C   1 
ATOM   14   O  O   . ALA A 1 3   ? 21.672 2.514   17.030 1.00 12.37  ? 9   ALA A O   1 
ATOM   15   C  CB  . ALA A 1 3   ? 23.301 5.329   17.578 1.00 14.75  ? 9   ALA A CB  1 
ATOM   16   N  N   . ILE A 1 4   ? 21.794 4.024   15.322 1.00 13.11  ? 10  ILE A N   1 
ATOM   17   C  CA  . ILE A 1 4   ? 21.985 3.069   14.214 1.00 13.40  ? 10  ILE A CA  1 
ATOM   18   C  C   . ILE A 1 4   ? 23.436 3.185   13.761 1.00 14.37  ? 10  ILE A C   1 
ATOM   19   O  O   . ILE A 1 4   ? 23.883 4.340   13.481 1.00 14.23  ? 10  ILE A O   1 
ATOM   20   C  CB  . ILE A 1 4   ? 21.002 3.313   13.036 1.00 12.29  ? 10  ILE A CB  1 
ATOM   21   C  CG1 . ILE A 1 4   ? 19.552 3.526   13.481 1.00 13.68  ? 10  ILE A CG1 1 
ATOM   22   C  CG2 . ILE A 1 4   ? 21.091 2.135   12.049 1.00 13.21  ? 10  ILE A CG2 1 
ATOM   23   C  CD1 . ILE A 1 4   ? 18.635 4.061   12.393 1.00 13.58  ? 10  ILE A CD1 1 
ATOM   24   N  N   . TYR A 1 5   ? 24.069 2.030   13.525 1.00 15.99  ? 11  TYR A N   1 
ATOM   25   C  CA  . TYR A 1 5   ? 25.470 1.913   13.047 1.00 17.05  ? 11  TYR A CA  1 
ATOM   26   C  C   . TYR A 1 5   ? 25.443 1.169   11.719 1.00 17.08  ? 11  TYR A C   1 
ATOM   27   O  O   . TYR A 1 5   ? 25.417 -0.052  11.748 1.00 17.02  ? 11  TYR A O   1 
ATOM   28   C  CB  . TYR A 1 5   ? 26.351 1.255   14.123 1.00 18.18  ? 11  TYR A CB  1 
ATOM   29   C  CG  . TYR A 1 5   ? 26.504 2.114   15.361 1.00 17.14  ? 11  TYR A CG  1 
ATOM   30   C  CD1 . TYR A 1 5   ? 27.374 3.193   15.367 1.00 18.44  ? 11  TYR A CD1 1 
ATOM   31   C  CD2 . TYR A 1 5   ? 25.751 1.866   16.489 1.00 19.48  ? 11  TYR A CD2 1 
ATOM   32   C  CE1 . TYR A 1 5   ? 27.471 4.014   16.477 1.00 16.70  ? 11  TYR A CE1 1 
ATOM   33   C  CE2 . TYR A 1 5   ? 25.838 2.676   17.608 1.00 20.87  ? 11  TYR A CE2 1 
ATOM   34   C  CZ  . TYR A 1 5   ? 26.706 3.742   17.604 1.00 18.29  ? 11  TYR A CZ  1 
ATOM   35   O  OH  . TYR A 1 5   ? 26.760 4.475   18.767 1.00 18.73  ? 11  TYR A OH  1 
ATOM   36   N  N   . VAL A 1 6   ? 25.488 1.924   10.642 1.00 16.11  ? 12  VAL A N   1 
ATOM   37   C  CA  . VAL A 1 6   ? 25.485 1.387   9.245  1.00 16.28  ? 12  VAL A CA  1 
ATOM   38   C  C   . VAL A 1 6   ? 26.720 1.897   8.495  1.00 17.27  ? 12  VAL A C   1 
ATOM   39   O  O   . VAL A 1 6   ? 26.955 3.119   8.435  1.00 17.79  ? 12  VAL A O   1 
ATOM   40   C  CB  . VAL A 1 6   ? 24.171 1.731   8.511  1.00 16.72  ? 12  VAL A CB  1 
ATOM   41   C  CG1 . VAL A 1 6   ? 23.816 3.193   8.466  1.00 16.16  ? 12  VAL A CG1 1 
ATOM   42   C  CG2 . VAL A 1 6   ? 24.184 1.140   7.123  1.00 16.71  ? 12  VAL A CG2 1 
ATOM   43   N  N   . GLY A 1 7   ? 27.514 0.990   7.899  1.00 19.01  ? 13  GLY A N   1 
ATOM   44   C  CA  . GLY A 1 7   ? 28.771 1.426   7.276  1.00 18.57  ? 13  GLY A CA  1 
ATOM   45   C  C   . GLY A 1 7   ? 29.618 2.223   8.264  1.00 17.03  ? 13  GLY A C   1 
ATOM   46   O  O   . GLY A 1 7   ? 29.761 1.766   9.413  1.00 18.73  ? 13  GLY A O   1 
ATOM   47   N  N   . ASN A 1 8   ? 30.058 3.386   7.817  1.00 20.57  ? 14  ASN A N   1 
ATOM   48   C  CA  . ASN A 1 8   ? 30.873 4.321   8.619  1.00 20.90  ? 14  ASN A CA  1 
ATOM   49   C  C   . ASN A 1 8   ? 29.998 5.494   9.074  1.00 22.86  ? 14  ASN A C   1 
ATOM   50   O  O   . ASN A 1 8   ? 30.520 6.626   9.151  1.00 20.54  ? 14  ASN A O   1 
ATOM   51   C  CB  . ASN A 1 8   ? 32.143 4.705   7.856  1.00 23.24  ? 14  ASN A CB  1 
ATOM   52   C  CG  . ASN A 1 8   ? 33.174 3.587   7.890  1.00 23.65  ? 14  ASN A CG  1 
ATOM   53   O  OD1 . ASN A 1 8   ? 33.988 3.513   8.814  1.00 29.18  ? 14  ASN A OD1 1 
ATOM   54   N  ND2 . ASN A 1 8   ? 33.119 2.674   6.925  1.00 23.05  ? 14  ASN A ND2 1 
ATOM   55   N  N   . TYR A 1 9   ? 28.704 5.222   9.354  1.00 19.49  ? 15  TYR A N   1 
ATOM   56   C  CA  . TYR A 1 9   ? 27.730 6.272   9.765  1.00 17.94  ? 15  TYR A CA  1 
ATOM   57   C  C   . TYR A 1 9   ? 27.129 5.878   11.118 1.00 14.97  ? 15  TYR A C   1 
ATOM   58   O  O   . TYR A 1 9   ? 26.892 4.694   11.408 1.00 16.15  ? 15  TYR A O   1 
ATOM   59   C  CB  . TYR A 1 9   ? 26.602 6.445   8.744  1.00 18.46  ? 15  TYR A CB  1 
ATOM   60   C  CG  . TYR A 1 9   ? 27.005 6.870   7.365  1.00 18.62  ? 15  TYR A CG  1 
ATOM   61   C  CD1 . TYR A 1 9   ? 27.639 8.079   7.122  1.00 20.17  ? 15  TYR A CD1 1 
ATOM   62   C  CD2 . TYR A 1 9   ? 26.708 6.071   6.258  1.00 20.41  ? 15  TYR A CD2 1 
ATOM   63   C  CE1 . TYR A 1 9   ? 28.007 8.484   5.845  1.00 22.37  ? 15  TYR A CE1 1 
ATOM   64   C  CE2 . TYR A 1 9   ? 27.058 6.469   4.982  1.00 21.06  ? 15  TYR A CE2 1 
ATOM   65   C  CZ  . TYR A 1 9   ? 27.715 7.669   4.766  1.00 23.41  ? 15  TYR A CZ  1 
ATOM   66   O  OH  . TYR A 1 9   ? 28.076 8.030   3.501  1.00 27.04  ? 15  TYR A OH  1 
ATOM   67   N  N   . ARG A 1 10  ? 26.860 6.889   11.956 1.00 14.53  ? 16  ARG A N   1 
ATOM   68   C  CA  . ARG A 1 10  ? 26.146 6.808   13.249 1.00 15.29  ? 16  ARG A CA  1 
ATOM   69   C  C   . ARG A 1 10  ? 24.918 7.697   13.098 1.00 14.62  ? 16  ARG A C   1 
ATOM   70   O  O   . ARG A 1 10  ? 25.078 8.912   12.832 1.00 15.79  ? 16  ARG A O   1 
ATOM   71   C  CB  . ARG A 1 10  ? 27.043 7.224   14.434 1.00 16.09  ? 16  ARG A CB  1 
ATOM   72   C  CG  . ARG A 1 10  ? 26.331 7.534   15.747 1.00 15.40  ? 16  ARG A CG  1 
ATOM   73   C  CD  . ARG A 1 10  ? 27.363 7.771   16.870 1.00 15.81  ? 16  ARG A CD  1 
ATOM   74   N  NE  . ARG A 1 10  ? 26.932 8.785   17.823 1.00 15.26  ? 16  ARG A NE  1 
ATOM   75   C  CZ  . ARG A 1 10  ? 26.251 8.596   18.938 1.00 15.18  ? 16  ARG A CZ  1 
ATOM   76   N  NH1 . ARG A 1 10  ? 25.831 7.392   19.305 1.00 16.63  ? 16  ARG A NH1 1 
ATOM   77   N  NH2 . ARG A 1 10  ? 25.933 9.651   19.695 1.00 15.15  ? 16  ARG A NH2 1 
ATOM   78   N  N   . VAL A 1 11  ? 23.725 7.114   13.218 1.00 12.97  ? 17  VAL A N   1 
ATOM   79   C  CA  . VAL A 1 11  ? 22.443 7.863   13.118 1.00 12.76  ? 17  VAL A CA  1 
ATOM   80   C  C   . VAL A 1 11  ? 21.874 7.986   14.523 1.00 11.84  ? 17  VAL A C   1 
ATOM   81   O  O   . VAL A 1 11  ? 21.580 6.952   15.157 1.00 11.32  ? 17  VAL A O   1 
ATOM   82   C  CB  . VAL A 1 11  ? 21.460 7.129   12.186 1.00 12.49  ? 17  VAL A CB  1 
ATOM   83   C  CG1 . VAL A 1 11  ? 20.213 8.014   12.005 1.00 13.07  ? 17  VAL A CG1 1 
ATOM   84   C  CG2 . VAL A 1 11  ? 22.125 6.741   10.865 1.00 12.89  ? 17  VAL A CG2 1 
ATOM   85   N  N   . VAL A 1 12  ? 21.676 9.215   14.975 1.00 12.66  ? 18  VAL A N   1 
ATOM   86   C  CA  . VAL A 1 12  ? 21.185 9.516   16.321 1.00 12.73  ? 18  VAL A CA  1 
ATOM   87   C  C   . VAL A 1 12  ? 20.037 10.505  16.225 1.00 11.80  ? 18  VAL A C   1 
ATOM   88   O  O   . VAL A 1 12  ? 19.893 11.215  15.211 1.00 11.57  ? 18  VAL A O   1 
ATOM   89   C  CB  . VAL A 1 12  ? 22.290 10.054  17.256 1.00 13.41  ? 18  VAL A CB  1 
ATOM   90   C  CG1 . VAL A 1 12  ? 23.260 8.947   17.569 1.00 16.61  ? 18  VAL A CG1 1 
ATOM   91   C  CG2 . VAL A 1 12  ? 23.003 11.313  16.752 1.00 13.08  ? 18  VAL A CG2 1 
ATOM   92   N  N   . ASN A 1 13  ? 19.276 10.548  17.306 1.00 11.01  ? 19  ASN A N   1 
ATOM   93   C  CA  . ASN A 1 13  ? 18.319 11.675  17.488 1.00 11.14  ? 19  ASN A CA  1 
ATOM   94   C  C   . ASN A 1 13  ? 19.113 12.985  17.511 1.00 11.58  ? 19  ASN A C   1 
ATOM   95   O  O   . ASN A 1 13  ? 20.041 13.102  18.299 1.00 11.06  ? 19  ASN A O   1 
ATOM   96   C  CB  . ASN A 1 13  ? 17.484 11.559  18.764 1.00 12.15  ? 19  ASN A CB  1 
ATOM   97   C  CG  . ASN A 1 13  ? 16.601 10.333  18.823 1.00 11.67  ? 19  ASN A CG  1 
ATOM   98   O  OD1 . ASN A 1 13  ? 16.995 9.302   19.363 1.00 13.11  ? 19  ASN A OD1 1 
ATOM   99   N  ND2 . ASN A 1 13  ? 15.402 10.411  18.269 1.00 12.25  ? 19  ASN A ND2 1 
ATOM   100  N  N   . ARG A 1 14  ? 18.705 13.990  16.721 1.00 11.28  ? 20  ARG A N   1 
ATOM   101  C  CA  . ARG A 1 14  ? 19.415 15.304  16.699 1.00 11.79  ? 20  ARG A CA  1 
ATOM   102  C  C   . ARG A 1 14  ? 19.534 15.875  18.111 1.00 12.93  ? 20  ARG A C   1 
ATOM   103  O  O   . ARG A 1 14  ? 20.613 16.391  18.474 1.00 12.03  ? 20  ARG A O   1 
ATOM   104  C  CB  . ARG A 1 14  ? 18.739 16.311  15.785 1.00 12.46  ? 20  ARG A CB  1 
ATOM   105  C  CG  . ARG A 1 14  ? 19.567 17.555  15.469 1.00 13.37  ? 20  ARG A CG  1 
ATOM   106  C  CD  . ARG A 1 14  ? 18.822 18.458  14.505 1.00 14.83  ? 20  ARG A CD  1 
ATOM   107  N  NE  . ARG A 1 14  ? 19.531 19.713  14.168 1.00 15.07  ? 20  ARG A NE  1 
ATOM   108  C  CZ  . ARG A 1 14  ? 19.547 20.808  14.935 1.00 15.35  ? 20  ARG A CZ  1 
ATOM   109  N  NH1 . ARG A 1 14  ? 19.125 20.796  16.187 1.00 17.37  ? 20  ARG A NH1 1 
ATOM   110  N  NH2 . ARG A 1 14  ? 20.154 21.919  14.504 1.00 17.82  ? 20  ARG A NH2 1 
ATOM   111  N  N   . HIS A 1 15  ? 18.464 15.739  18.923 1.00 12.87  ? 21  HIS A N   1 
ATOM   112  C  CA  . HIS A 1 15  ? 18.428 16.339  20.273 1.00 13.10  ? 21  HIS A CA  1 
ATOM   113  C  C   . HIS A 1 15  ? 19.399 15.639  21.200 1.00 12.49  ? 21  HIS A C   1 
ATOM   114  O  O   . HIS A 1 15  ? 19.654 16.174  22.279 1.00 14.87  ? 21  HIS A O   1 
ATOM   115  C  CB  . HIS A 1 15  ? 16.986 16.484  20.781 1.00 12.50  ? 21  HIS A CB  1 
ATOM   116  C  CG  . HIS A 1 15  ? 16.357 15.203  21.245 1.00 13.39  ? 21  HIS A CG  1 
ATOM   117  N  ND1 . HIS A 1 15  ? 15.628 14.390  20.368 1.00 13.13  ? 21  HIS A ND1 1 
ATOM   118  C  CD2 . HIS A 1 15  ? 16.282 14.628  22.482 1.00 14.49  ? 21  HIS A CD2 1 
ATOM   119  C  CE1 . HIS A 1 15  ? 15.207 13.334  21.054 1.00 12.75  ? 21  HIS A CE1 1 
ATOM   120  N  NE2 . HIS A 1 15  ? 15.562 13.451  22.349 1.00 14.76  ? 21  HIS A NE2 1 
ATOM   121  N  N   . LEU A 1 16  ? 19.881 14.446  20.881 1.00 12.32  ? 22  LEU A N   1 
ATOM   122  C  CA  . LEU A 1 16  ? 20.818 13.662  21.744 1.00 12.43  ? 22  LEU A CA  1 
ATOM   123  C  C   . LEU A 1 16  ? 22.216 13.639  21.132 1.00 12.79  ? 22  LEU A C   1 
ATOM   124  O  O   . LEU A 1 16  ? 23.114 12.978  21.751 1.00 14.18  ? 22  LEU A O   1 
ATOM   125  C  CB  . LEU A 1 16  ? 20.264 12.249  21.917 1.00 13.11  ? 22  LEU A CB  1 
ATOM   126  C  CG  . LEU A 1 16  ? 18.935 12.150  22.679 1.00 14.13  ? 22  LEU A CG  1 
ATOM   127  C  CD1 . LEU A 1 16  ? 18.523 10.709  22.909 1.00 15.39  ? 22  LEU A CD1 1 
ATOM   128  C  CD2 . LEU A 1 16  ? 19.005 12.862  24.052 1.00 13.95  ? 22  LEU A CD2 1 
ATOM   129  N  N   . ALA A 1 17  ? 22.447 14.360  20.030 1.00 12.15  ? 23  ALA A N   1 
ATOM   130  C  CA  . ALA A 1 17  ? 23.775 14.364  19.382 1.00 12.90  ? 23  ALA A CA  1 
ATOM   131  C  C   . ALA A 1 17  ? 24.818 14.992  20.322 1.00 13.39  ? 23  ALA A C   1 
ATOM   132  O  O   . ALA A 1 17  ? 24.484 15.983  21.021 1.00 14.09  ? 23  ALA A O   1 
ATOM   133  C  CB  . ALA A 1 17  ? 23.720 15.093  18.063 1.00 13.13  ? 23  ALA A CB  1 
ATOM   134  N  N   . THR A 1 18  ? 26.029 14.481  20.295 1.00 13.55  ? 24  THR A N   1 
ATOM   135  C  CA  . THR A 1 18  ? 27.111 14.922  21.213 1.00 14.36  ? 24  THR A CA  1 
ATOM   136  C  C   . THR A 1 18  ? 27.950 15.981  20.515 1.00 14.23  ? 24  THR A C   1 
ATOM   137  O  O   . THR A 1 18  ? 27.802 16.213  19.308 1.00 13.41  ? 24  THR A O   1 
ATOM   138  C  CB  . THR A 1 18  ? 27.997 13.731  21.630 1.00 13.99  ? 24  THR A CB  1 
ATOM   139  O  OG1 . THR A 1 18  ? 28.656 13.217  20.470 1.00 15.22  ? 24  THR A OG1 1 
ATOM   140  C  CG2 . THR A 1 18  ? 27.212 12.606  22.276 1.00 15.51  ? 24  THR A CG2 1 
ATOM   141  N  N   . HIS A 1 19  ? 28.899 16.600  21.249 1.00 13.48  ? 25  HIS A N   1 
ATOM   142  C  CA  . HIS A 1 19  ? 29.877 17.510  20.594 1.00 14.69  ? 25  HIS A CA  1 
ATOM   143  C  C   . HIS A 1 19  ? 30.665 16.752  19.501 1.00 14.86  ? 25  HIS A C   1 
ATOM   144  O  O   . HIS A 1 19  ? 30.883 17.302  18.390 1.00 15.11  ? 25  HIS A O   1 
ATOM   145  C  CB  . HIS A 1 19  ? 30.832 18.171  21.623 1.00 15.90  ? 25  HIS A CB  1 
ATOM   146  C  CG  . HIS A 1 19  ? 32.047 18.777  20.967 1.00 17.90  ? 25  HIS A CG  1 
ATOM   147  N  ND1 . HIS A 1 19  ? 32.043 19.995  20.292 1.00 19.52  ? 25  HIS A ND1 1 
ATOM   148  C  CD2 . HIS A 1 19  ? 33.297 18.244  20.729 1.00 19.47  ? 25  HIS A CD2 1 
ATOM   149  C  CE1 . HIS A 1 19  ? 33.235 20.240  19.784 1.00 20.23  ? 25  HIS A CE1 1 
ATOM   150  N  NE2 . HIS A 1 19  ? 34.029 19.155  20.008 1.00 21.51  ? 25  HIS A NE2 1 
ATOM   151  N  N   . ASN A 1 20  ? 31.076 15.502  19.749 1.00 14.39  ? 26  ASN A N   1 
ATOM   152  C  CA  . ASN A 1 20  ? 31.847 14.705  18.777 1.00 15.40  ? 26  ASN A CA  1 
ATOM   153  C  C   . ASN A 1 20  ? 30.995 14.418  17.528 1.00 14.03  ? 26  ASN A C   1 
ATOM   154  O  O   . ASN A 1 20  ? 31.513 14.492  16.386 1.00 16.20  ? 26  ASN A O   1 
ATOM   155  C  CB  . ASN A 1 20  ? 32.301 13.378  19.366 1.00 17.88  ? 26  ASN A CB  1 
ATOM   156  C  CG  . ASN A 1 20  ? 33.207 12.631  18.412 1.00 23.06  ? 26  ASN A CG  1 
ATOM   157  O  OD1 . ASN A 1 20  ? 34.375 12.999  18.229 1.00 27.97  ? 26  ASN A OD1 1 
ATOM   158  N  ND2 . ASN A 1 20  ? 32.663 11.630  17.744 1.00 25.28  ? 26  ASN A ND2 1 
ATOM   159  N  N   . ASP A 1 21  ? 29.686 14.200  17.709 1.00 14.58  ? 27  ASP A N   1 
ATOM   160  C  CA  . ASP A 1 21  ? 28.798 14.047  16.533 1.00 13.01  ? 27  ASP A CA  1 
ATOM   161  C  C   . ASP A 1 21  ? 28.870 15.294  15.656 1.00 12.67  ? 27  ASP A C   1 
ATOM   162  O  O   . ASP A 1 21  ? 28.969 15.197  14.434 1.00 13.25  ? 27  ASP A O   1 
ATOM   163  C  CB  . ASP A 1 21  ? 27.341 13.732  16.889 1.00 12.85  ? 27  ASP A CB  1 
ATOM   164  C  CG  . ASP A 1 21  ? 27.125 12.354  17.473 1.00 13.39  ? 27  ASP A CG  1 
ATOM   165  O  OD1 . ASP A 1 21  ? 27.767 11.383  16.955 1.00 14.41  ? 27  ASP A OD1 1 
ATOM   166  O  OD2 . ASP A 1 21  ? 26.317 12.230  18.410 1.00 13.86  ? 27  ASP A OD2 1 
ATOM   167  N  N   . TRP A 1 22  ? 28.673 16.471  16.256 1.00 12.84  ? 28  TRP A N   1 
ATOM   168  C  CA  . TRP A 1 22  ? 28.671 17.762  15.535 1.00 12.66  ? 28  TRP A CA  1 
ATOM   169  C  C   . TRP A 1 22  ? 30.036 18.038  14.889 1.00 12.07  ? 28  TRP A C   1 
ATOM   170  O  O   . TRP A 1 22  ? 30.058 18.596  13.822 1.00 12.92  ? 28  TRP A O   1 
ATOM   171  C  CB  . TRP A 1 22  ? 28.234 18.914  16.460 1.00 13.07  ? 28  TRP A CB  1 
ATOM   172  C  CG  . TRP A 1 22  ? 26.741 19.023  16.680 1.00 13.21  ? 28  TRP A CG  1 
ATOM   173  C  CD1 . TRP A 1 22  ? 26.023 18.595  17.761 1.00 12.76  ? 28  TRP A CD1 1 
ATOM   174  C  CD2 . TRP A 1 22  ? 25.796 19.540  15.726 1.00 11.63  ? 28  TRP A CD2 1 
ATOM   175  N  NE1 . TRP A 1 22  ? 24.678 18.853  17.565 1.00 11.70  ? 28  TRP A NE1 1 
ATOM   176  C  CE2 . TRP A 1 22  ? 24.514 19.412  16.308 1.00 12.14  ? 28  TRP A CE2 1 
ATOM   177  C  CE3 . TRP A 1 22  ? 25.922 20.150  14.458 1.00 12.26  ? 28  TRP A CE3 1 
ATOM   178  C  CZ2 . TRP A 1 22  ? 23.386 19.926  15.670 1.00 12.24  ? 28  TRP A CZ2 1 
ATOM   179  C  CZ3 . TRP A 1 22  ? 24.778 20.564  13.807 1.00 11.55  ? 28  TRP A CZ3 1 
ATOM   180  C  CH2 . TRP A 1 22  ? 23.526 20.443  14.410 1.00 13.18  ? 28  TRP A CH2 1 
ATOM   181  N  N   . ALA A 1 23  ? 31.125 17.620  15.528 1.00 13.57  ? 29  ALA A N   1 
ATOM   182  C  CA  . ALA A 1 23  ? 32.495 17.831  15.008 1.00 14.21  ? 29  ALA A CA  1 
ATOM   183  C  C   . ALA A 1 23  ? 32.798 16.881  13.846 1.00 16.90  ? 29  ALA A C   1 
ATOM   184  O  O   . ALA A 1 23  ? 33.832 17.094  13.144 1.00 17.71  ? 29  ALA A O   1 
ATOM   185  C  CB  . ALA A 1 23  ? 33.478 17.691  16.161 1.00 14.28  ? 29  ALA A CB  1 
ATOM   186  N  N   . ASN A 1 24  ? 31.982 15.833  13.674 1.00 18.10  ? 30  ASN A N   1 
ATOM   187  C  CA  . ASN A 1 24  ? 32.175 14.793  12.619 1.00 17.06  ? 30  ASN A CA  1 
ATOM   188  C  C   . ASN A 1 24  ? 30.865 14.695  11.821 1.00 17.04  ? 30  ASN A C   1 
ATOM   189  O  O   . ASN A 1 24  ? 30.465 13.571  11.399 1.00 16.79  ? 30  ASN A O   1 
ATOM   190  C  CB  . ASN A 1 24  ? 32.635 13.463  13.225 1.00 18.04  ? 30  ASN A CB  1 
ATOM   191  C  CG  . ASN A 1 24  ? 34.020 13.564  13.839 1.00 18.39  ? 30  ASN A CG  1 
ATOM   192  O  OD1 . ASN A 1 24  ? 35.031 13.516  13.137 1.00 23.54  ? 30  ASN A OD1 1 
ATOM   193  N  ND2 . ASN A 1 24  ? 34.060 13.749  15.135 1.00 19.37  ? 30  ASN A ND2 1 
ATOM   194  N  N   . LEU A 1 25  ? 30.184 15.817  11.634 1.00 16.50  ? 31  LEU A N   1 
ATOM   195  C  CA  . LEU A 1 25  ? 28.830 15.869  11.017 1.00 16.13  ? 31  LEU A CA  1 
ATOM   196  C  C   . LEU A 1 25  ? 28.859 15.420  9.561  1.00 17.14  ? 31  LEU A C   1 
ATOM   197  O  O   . LEU A 1 25  ? 29.718 15.911  8.768  1.00 18.60  ? 31  LEU A O   1 
ATOM   198  C  CB  . LEU A 1 25  ? 28.334 17.311  11.045 1.00 16.24  ? 31  LEU A CB  1 
ATOM   199  C  CG  . LEU A 1 25  ? 26.905 17.523  10.544 1.00 16.32  ? 31  LEU A CG  1 
ATOM   200  C  CD1 . LEU A 1 25  ? 25.920 16.694  11.311 1.00 19.38  ? 31  LEU A CD1 1 
ATOM   201  C  CD2 . LEU A 1 25  ? 26.525 18.981  10.635 1.00 17.18  ? 31  LEU A CD2 1 
ATOM   202  N  N   . VAL A 1 26  ? 27.907 14.561  9.193  1.00 15.57  ? 32  VAL A N   1 
ATOM   203  C  CA  . VAL A 1 26  ? 27.618 14.221  7.774  1.00 17.65  ? 32  VAL A CA  1 
ATOM   204  C  C   . VAL A 1 26  ? 26.355 14.966  7.323  1.00 16.39  ? 32  VAL A C   1 
ATOM   205  O  O   . VAL A 1 26  ? 26.352 15.594  6.235  1.00 18.38  ? 32  VAL A O   1 
ATOM   206  C  CB  . VAL A 1 26  ? 27.508 12.694  7.633  1.00 16.37  ? 32  VAL A CB  1 
ATOM   207  C  CG1 . VAL A 1 26  ? 27.035 12.299  6.225  1.00 17.69  ? 32  VAL A CG1 1 
ATOM   208  C  CG2 . VAL A 1 26  ? 28.807 12.017  7.957  1.00 17.01  ? 32  VAL A CG2 1 
ATOM   209  N  N   . TRP A 1 27  ? 25.293 14.961  8.133  1.00 15.51  ? 33  TRP A N   1 
ATOM   210  C  CA  . TRP A 1 27  ? 23.968 15.476  7.714  1.00 16.37  ? 33  TRP A CA  1 
ATOM   211  C  C   . TRP A 1 27  ? 23.089 15.647  8.954  1.00 14.71  ? 33  TRP A C   1 
ATOM   212  O  O   . TRP A 1 27  ? 23.189 14.798  9.856  1.00 13.54  ? 33  TRP A O   1 
ATOM   213  C  CB  . TRP A 1 27  ? 23.338 14.536  6.664  1.00 17.41  ? 33  TRP A CB  1 
ATOM   214  C  CG  . TRP A 1 27  ? 21.901 14.794  6.326  1.00 16.82  ? 33  TRP A CG  1 
ATOM   215  C  CD1 . TRP A 1 27  ? 21.413 15.659  5.393  1.00 18.37  ? 33  TRP A CD1 1 
ATOM   216  C  CD2 . TRP A 1 27  ? 20.732 14.187  6.928  1.00 15.23  ? 33  TRP A CD2 1 
ATOM   217  N  NE1 . TRP A 1 27  ? 20.031 15.643  5.371  1.00 19.57  ? 33  TRP A NE1 1 
ATOM   218  C  CE2 . TRP A 1 27  ? 19.593 14.751  6.303  1.00 17.10  ? 33  TRP A CE2 1 
ATOM   219  C  CE3 . TRP A 1 27  ? 20.533 13.251  7.925  1.00 15.63  ? 33  TRP A CE3 1 
ATOM   220  C  CZ2 . TRP A 1 27  ? 18.294 14.352  6.607  1.00 17.04  ? 33  TRP A CZ2 1 
ATOM   221  C  CZ3 . TRP A 1 27  ? 19.245 12.864  8.233  1.00 15.79  ? 33  TRP A CZ3 1 
ATOM   222  C  CH2 . TRP A 1 27  ? 18.150 13.417  7.592  1.00 16.67  ? 33  TRP A CH2 1 
ATOM   223  N  N   . GLU A 1 28  ? 22.275 16.696  9.005  1.00 14.59  ? 34  GLU A N   1 
ATOM   224  C  CA  . GLU A 1 28  ? 21.307 16.854  10.109 1.00 14.94  ? 34  GLU A CA  1 
ATOM   225  C  C   . GLU A 1 28  ? 20.054 17.582  9.616  1.00 13.91  ? 34  GLU A C   1 
ATOM   226  O  O   . GLU A 1 28  ? 20.115 18.370  8.647  1.00 16.60  ? 34  GLU A O   1 
ATOM   227  C  CB  . GLU A 1 28  ? 21.955 17.535  11.309 1.00 15.67  ? 34  GLU A CB  1 
ATOM   228  C  CG  . GLU A 1 28  ? 22.507 18.913  10.953 1.00 14.82  ? 34  GLU A CG  1 
ATOM   229  C  CD  . GLU A 1 28  ? 21.554 20.104  10.953 1.00 15.96  ? 34  GLU A CD  1 
ATOM   230  O  OE1 . GLU A 1 28  ? 21.904 21.138  10.307 1.00 15.99  ? 34  GLU A OE1 1 
ATOM   231  O  OE2 . GLU A 1 28  ? 20.495 20.025  11.569 1.00 15.55  ? 34  GLU A OE2 1 
ATOM   232  N  N   . ASP A 1 29  ? 18.915 17.275  10.241 1.00 14.86  ? 35  ASP A N   1 
ATOM   233  C  CA  . ASP A 1 29  ? 17.602 17.892  9.903  1.00 14.81  ? 35  ASP A CA  1 
ATOM   234  C  C   . ASP A 1 29  ? 16.775 17.979  11.189 1.00 15.23  ? 35  ASP A C   1 
ATOM   235  O  O   . ASP A 1 29  ? 16.312 16.949  11.702 1.00 14.39  ? 35  ASP A O   1 
ATOM   236  C  CB  . ASP A 1 29  ? 16.944 17.065  8.795  1.00 15.95  ? 35  ASP A CB  1 
ATOM   237  C  CG  . ASP A 1 29  ? 15.603 17.564  8.311  1.00 16.67  ? 35  ASP A CG  1 
ATOM   238  O  OD1 . ASP A 1 29  ? 14.808 18.055  9.138  1.00 20.35  ? 35  ASP A OD1 1 
ATOM   239  O  OD2 . ASP A 1 29  ? 15.358 17.411  7.096  1.00 22.33  ? 35  ASP A OD2 1 
ATOM   240  N  N   A SER A 1 30  ? 16.606 19.187  11.730 0.25 14.89  ? 36  SER A N   1 
ATOM   241  N  N   B SER A 1 30  ? 16.617 19.198  11.710 0.25 16.22  ? 36  SER A N   1 
ATOM   242  C  CA  A SER A 1 30  ? 15.820 19.453  12.959 0.25 15.00  ? 36  SER A CA  1 
ATOM   243  C  CA  B SER A 1 30  ? 15.828 19.529  12.922 0.25 17.21  ? 36  SER A CA  1 
ATOM   244  C  C   A SER A 1 30  ? 14.363 19.024  12.753 0.25 15.14  ? 36  SER A C   1 
ATOM   245  C  C   B SER A 1 30  ? 14.376 19.069  12.756 0.25 16.38  ? 36  SER A C   1 
ATOM   246  O  O   A SER A 1 30  ? 13.794 18.407  13.674 0.25 15.89  ? 36  SER A O   1 
ATOM   247  O  O   B SER A 1 30  ? 13.823 18.496  13.712 0.25 17.30  ? 36  SER A O   1 
ATOM   248  C  CB  A SER A 1 30  ? 15.891 20.906  13.328 0.25 14.60  ? 36  SER A CB  1 
ATOM   249  C  CB  B SER A 1 30  ? 15.886 21.010  13.182 0.25 18.04  ? 36  SER A CB  1 
ATOM   250  O  OG  A SER A 1 30  ? 14.976 21.208  14.367 0.25 13.72  ? 36  SER A OG  1 
ATOM   251  O  OG  B SER A 1 30  ? 15.830 21.742  11.963 0.25 20.29  ? 36  SER A OG  1 
ATOM   252  N  N   . SER A 1 31  ? 13.786 19.308  11.582 1.00 15.77  ? 37  SER A N   1 
ATOM   253  C  CA  . SER A 1 31  ? 12.368 18.941  11.308 1.00 15.29  ? 37  SER A CA  1 
ATOM   254  C  C   . SER A 1 31  ? 12.152 17.434  11.474 1.00 14.57  ? 37  SER A C   1 
ATOM   255  O  O   . SER A 1 31  ? 11.071 17.048  11.874 1.00 15.85  ? 37  SER A O   1 
ATOM   256  C  CB  . SER A 1 31  ? 11.881 19.375  9.969  1.00 16.64  ? 37  SER A CB  1 
ATOM   257  O  OG  . SER A 1 31  ? 12.414 18.595  8.948  1.00 24.35  ? 37  SER A OG  1 
ATOM   258  N  N   . ARG A 1 32  ? 13.180 16.618  11.229 1.00 12.47  ? 38  ARG A N   1 
ATOM   259  C  CA  . ARG A 1 32  ? 13.089 15.140  11.326 1.00 13.15  ? 38  ARG A CA  1 
ATOM   260  C  C   . ARG A 1 32  ? 13.624 14.610  12.663 1.00 13.19  ? 38  ARG A C   1 
ATOM   261  O  O   . ARG A 1 32  ? 13.527 13.394  12.894 1.00 12.40  ? 38  ARG A O   1 
ATOM   262  C  CB  . ARG A 1 32  ? 13.916 14.539  10.187 1.00 14.35  ? 38  ARG A CB  1 
ATOM   263  C  CG  . ARG A 1 32  ? 13.372 14.813  8.803  1.00 14.75  ? 38  ARG A CG  1 
ATOM   264  C  CD  . ARG A 1 32  ? 14.231 14.104  7.744  1.00 14.61  ? 38  ARG A CD  1 
ATOM   265  N  NE  . ARG A 1 32  ? 14.123 12.658  7.747  1.00 12.66  ? 38  ARG A NE  1 
ATOM   266  C  CZ  . ARG A 1 32  ? 14.144 11.885  6.654  1.00 13.22  ? 38  ARG A CZ  1 
ATOM   267  N  NH1 . ARG A 1 32  ? 14.371 12.429  5.460  1.00 14.39  ? 38  ARG A NH1 1 
ATOM   268  N  NH2 . ARG A 1 32  ? 13.978 10.575  6.760  1.00 13.82  ? 38  ARG A NH2 1 
ATOM   269  N  N   . ASP A 1 33  ? 14.230 15.452  13.497 1.00 12.68  ? 39  ASP A N   1 
ATOM   270  C  CA  . ASP A 1 33  ? 14.953 15.025  14.722 1.00 11.18  ? 39  ASP A CA  1 
ATOM   271  C  C   . ASP A 1 33  ? 16.068 14.004  14.396 1.00 10.59  ? 39  ASP A C   1 
ATOM   272  O  O   . ASP A 1 33  ? 16.264 13.076  15.225 1.00 11.78  ? 39  ASP A O   1 
ATOM   273  C  CB  . ASP A 1 33  ? 14.016 14.439  15.792 1.00 11.24  ? 39  ASP A CB  1 
ATOM   274  C  CG  . ASP A 1 33  ? 14.700 14.135  17.125 1.00 11.84  ? 39  ASP A CG  1 
ATOM   275  O  OD1 . ASP A 1 33  ? 15.610 14.899  17.509 1.00 13.06  ? 39  ASP A OD1 1 
ATOM   276  O  OD2 . ASP A 1 33  ? 14.320 13.131  17.779 1.00 12.15  ? 39  ASP A OD2 1 
ATOM   277  N  N   . LEU A 1 34  ? 16.823 14.181  13.290 1.00 11.88  ? 40  LEU A N   1 
ATOM   278  C  CA  . LEU A 1 34  ? 17.916 13.260  12.905 1.00 11.96  ? 40  LEU A CA  1 
ATOM   279  C  C   . LEU A 1 34  ? 19.248 13.986  12.720 1.00 11.55  ? 40  LEU A C   1 
ATOM   280  O  O   . LEU A 1 34  ? 19.263 15.122  12.230 1.00 11.67  ? 40  LEU A O   1 
ATOM   281  C  CB  . LEU A 1 34  ? 17.576 12.501  11.617 1.00 12.02  ? 40  LEU A CB  1 
ATOM   282  C  CG  . LEU A 1 34  ? 16.516 11.394  11.709 1.00 11.87  ? 40  LEU A CG  1 
ATOM   283  C  CD1 . LEU A 1 34  ? 16.341 10.713  10.325 1.00 12.61  ? 40  LEU A CD1 1 
ATOM   284  C  CD2 . LEU A 1 34  ? 16.858 10.355  12.752 1.00 12.25  ? 40  LEU A CD2 1 
ATOM   285  N  N   . LEU A 1 35  ? 20.307 13.293  13.115 1.00 11.45  ? 41  LEU A N   1 
ATOM   286  C  CA  . LEU A 1 35  ? 21.687 13.691  12.828 1.00 11.48  ? 41  LEU A CA  1 
ATOM   287  C  C   . LEU A 1 35  ? 22.497 12.434  12.511 1.00 11.78  ? 41  LEU A C   1 
ATOM   288  O  O   . LEU A 1 35  ? 22.335 11.409  13.204 1.00 11.58  ? 41  LEU A O   1 
ATOM   289  C  CB  . LEU A 1 35  ? 22.234 14.490  14.026 1.00 12.30  ? 41  LEU A CB  1 
ATOM   290  C  CG  . LEU A 1 35  ? 23.630 15.077  13.830 1.00 12.58  ? 41  LEU A CG  1 
ATOM   291  C  CD1 . LEU A 1 35  ? 23.774 16.440  14.494 1.00 12.20  ? 41  LEU A CD1 1 
ATOM   292  C  CD2 . LEU A 1 35  ? 24.721 14.116  14.275 1.00 12.78  ? 41  LEU A CD2 1 
ATOM   293  N  N   . VAL A 1 36  ? 23.401 12.597  11.555 1.00 11.48  ? 42  VAL A N   1 
ATOM   294  C  CA  . VAL A 1 36  ? 24.321 11.514  11.126 1.00 13.30  ? 42  VAL A CA  1 
ATOM   295  C  C   . VAL A 1 36  ? 25.750 12.053  11.220 1.00 14.20  ? 42  VAL A C   1 
ATOM   296  O  O   . VAL A 1 36  ? 26.008 13.174  10.674 1.00 13.58  ? 42  VAL A O   1 
ATOM   297  C  CB  . VAL A 1 36  ? 23.993 11.017  9.718  1.00 14.04  ? 42  VAL A CB  1 
ATOM   298  C  CG1 . VAL A 1 36  ? 24.971 9.945   9.274  1.00 15.14  ? 42  VAL A CG1 1 
ATOM   299  C  CG2 . VAL A 1 36  ? 22.557 10.518  9.602  1.00 14.38  ? 42  VAL A CG2 1 
ATOM   300  N  N   . SER A 1 37  ? 26.605 11.283  11.899 1.00 14.07  ? 43  SER A N   1 
ATOM   301  C  CA  . SER A 1 37  ? 28.050 11.566  12.030 1.00 14.32  ? 43  SER A CA  1 
ATOM   302  C  C   . SER A 1 37  ? 28.835 10.401  11.443 1.00 16.56  ? 43  SER A C   1 
ATOM   303  O  O   . SER A 1 37  ? 28.296 9.241   11.301 1.00 15.94  ? 43  SER A O   1 
ATOM   304  C  CB  . SER A 1 37  ? 28.421 11.869  13.471 1.00 13.86  ? 43  SER A CB  1 
ATOM   305  O  OG  . SER A 1 37  ? 28.174 10.762  14.297 1.00 14.30  ? 43  SER A OG  1 
ATOM   306  N  N   . SER A 1 38  ? 30.106 10.658  11.152 1.00 17.25  ? 44  SER A N   1 
ATOM   307  C  CA  . SER A 1 38  ? 31.052 9.648   10.615 1.00 19.16  ? 44  SER A CA  1 
ATOM   308  C  C   . SER A 1 38  ? 31.691 8.817   11.733 1.00 18.70  ? 44  SER A C   1 
ATOM   309  O  O   . SER A 1 38  ? 31.972 9.397   12.798 1.00 20.97  ? 44  SER A O   1 
ATOM   310  C  CB  . SER A 1 38  ? 32.084 10.359  9.816  1.00 19.85  ? 44  SER A CB  1 
ATOM   311  O  OG  . SER A 1 38  ? 32.912 11.138  10.671 1.00 24.21  ? 44  SER A OG  1 
ATOM   312  N  N   . THR A 1 39  ? 32.007 7.529   11.503 1.00 20.00  ? 45  THR A N   1 
ATOM   313  C  CA  . THR A 1 39  ? 32.589 6.590   12.513 1.00 22.58  ? 45  THR A CA  1 
ATOM   314  C  C   . THR A 1 39  ? 33.930 6.010   12.001 1.00 25.36  ? 45  THR A C   1 
ATOM   315  O  O   . THR A 1 39  ? 34.101 5.931   10.770 1.00 26.89  ? 45  THR A O   1 
ATOM   316  C  CB  . THR A 1 39  ? 31.687 5.387   12.826 1.00 23.41  ? 45  THR A CB  1 
ATOM   317  O  OG1 . THR A 1 39  ? 31.543 4.557   11.668 1.00 24.33  ? 45  THR A OG1 1 
ATOM   318  C  CG2 . THR A 1 39  ? 30.294 5.808   13.239 1.00 23.25  ? 45  THR A CG2 1 
ATOM   319  N  N   . THR A 1 40  ? 34.824 5.576   12.892 1.00 27.82  ? 46  THR A N   1 
ATOM   320  C  CA  . THR A 1 40  ? 36.086 4.957   12.421 1.00 28.89  ? 46  THR A CA  1 
ATOM   321  C  C   . THR A 1 40  ? 35.800 3.477   12.127 1.00 30.54  ? 46  THR A C   1 
ATOM   322  O  O   . THR A 1 40  ? 36.239 3.024   11.077 1.00 33.39  ? 46  THR A O   1 
ATOM   323  C  CB  . THR A 1 40  ? 37.236 5.306   13.370 1.00 30.02  ? 46  THR A CB  1 
ATOM   324  O  OG1 . THR A 1 40  ? 36.886 4.969   14.708 1.00 34.72  ? 46  THR A OG1 1 
ATOM   325  C  CG2 . THR A 1 40  ? 37.549 6.787   13.353 1.00 32.74  ? 46  THR A CG2 1 
ATOM   326  N  N   . ALA A 1 41  ? 35.068 2.771   12.992 1.00 27.89  ? 47  ALA A N   1 
ATOM   327  C  CA  . ALA A 1 41  ? 34.754 1.329   12.805 1.00 24.97  ? 47  ALA A CA  1 
ATOM   328  C  C   . ALA A 1 41  ? 33.429 1.188   12.052 1.00 26.47  ? 47  ALA A C   1 
ATOM   329  O  O   . ALA A 1 41  ? 32.486 1.972   12.371 1.00 26.56  ? 47  ALA A O   1 
ATOM   330  C  CB  . ALA A 1 41  ? 34.723 0.632   14.135 1.00 26.90  ? 47  ALA A CB  1 
ATOM   331  N  N   . GLN A 1 42  ? 33.349 0.234   11.106 1.00 23.46  ? 48  GLN A N   1 
ATOM   332  C  CA  . GLN A 1 42  ? 32.080 -0.172  10.423 1.00 23.17  ? 48  GLN A CA  1 
ATOM   333  C  C   . GLN A 1 42  ? 31.066 -0.786  11.402 1.00 18.45  ? 48  GLN A C   1 
ATOM   334  O  O   . GLN A 1 42  ? 31.449 -1.436  12.396 1.00 23.34  ? 48  GLN A O   1 
ATOM   335  C  CB  . GLN A 1 42  ? 32.406 -1.119  9.268  1.00 24.51  ? 48  GLN A CB  1 
ATOM   336  C  CG  . GLN A 1 42  ? 33.080 -0.378  8.125  1.00 32.54  ? 48  GLN A CG  1 
ATOM   337  C  CD  . GLN A 1 42  ? 33.378 -1.258  6.946  1.00 39.94  ? 48  GLN A CD  1 
ATOM   338  O  OE1 . GLN A 1 42  ? 33.866 -2.376  7.093  1.00 43.67  ? 48  GLN A OE1 1 
ATOM   339  N  NE2 . GLN A 1 42  ? 33.059 -0.763  5.764  1.00 50.11  ? 48  GLN A NE2 1 
ATOM   340  N  N   . GLY A 1 43  ? 29.769 -0.544  11.165 1.00 20.07  ? 49  GLY A N   1 
ATOM   341  C  CA  . GLY A 1 43  ? 28.663 -1.001  12.033 1.00 19.72  ? 49  GLY A CA  1 
ATOM   342  C  C   . GLY A 1 43  ? 27.907 -2.228  11.553 1.00 17.60  ? 49  GLY A C   1 
ATOM   343  O  O   . GLY A 1 43  ? 28.115 -2.658  10.406 1.00 18.39  ? 49  GLY A O   1 
ATOM   344  N  N   . CYS A 1 44  ? 27.088 -2.806  12.430 1.00 18.72  ? 50  CYS A N   1 
ATOM   345  C  CA  . CYS A 1 44  ? 26.508 -4.155  12.281 1.00 18.52  ? 50  CYS A CA  1 
ATOM   346  C  C   . CYS A 1 44  ? 25.101 -4.014  11.668 1.00 17.68  ? 50  CYS A C   1 
ATOM   347  O  O   . CYS A 1 44  ? 24.561 -5.035  11.369 1.00 18.54  ? 50  CYS A O   1 
ATOM   348  C  CB  . CYS A 1 44  ? 26.380 -4.944  13.593 1.00 19.70  ? 50  CYS A CB  1 
ATOM   349  S  SG  . CYS A 1 44  ? 27.915 -5.381  14.487 1.00 24.13  ? 50  CYS A SG  1 
ATOM   350  N  N   . ASP A 1 45  ? 24.536 -2.809  11.540 1.00 16.22  ? 51  ASP A N   1 
ATOM   351  C  CA  . ASP A 1 45  ? 23.102 -2.673  11.150 1.00 15.01  ? 51  ASP A CA  1 
ATOM   352  C  C   . ASP A 1 45  ? 22.949 -2.543  9.633  1.00 14.70  ? 51  ASP A C   1 
ATOM   353  O  O   . ASP A 1 45  ? 23.790 -1.926  8.946  1.00 16.28  ? 51  ASP A O   1 
ATOM   354  C  CB  . ASP A 1 45  ? 22.436 -1.484  11.852 1.00 14.50  ? 51  ASP A CB  1 
ATOM   355  C  CG  . ASP A 1 45  ? 22.448 -1.566  13.357 1.00 15.25  ? 51  ASP A CG  1 
ATOM   356  O  OD1 . ASP A 1 45  ? 22.189 -2.650  13.922 1.00 21.15  ? 51  ASP A OD1 1 
ATOM   357  O  OD2 . ASP A 1 45  ? 22.640 -0.496  13.992 1.00 16.94  ? 51  ASP A OD2 1 
ATOM   358  N  N   . THR A 1 46  ? 21.798 -3.039  9.159  1.00 14.24  ? 52  THR A N   1 
ATOM   359  C  CA  . THR A 1 46  ? 21.287 -2.960  7.769  1.00 14.32  ? 52  THR A CA  1 
ATOM   360  C  C   . THR A 1 46  ? 20.013 -2.097  7.762  1.00 13.19  ? 52  THR A C   1 
ATOM   361  O  O   . THR A 1 46  ? 19.151 -2.325  8.581  1.00 15.14  ? 52  THR A O   1 
ATOM   362  C  CB  . THR A 1 46  ? 20.976 -4.360  7.220  1.00 15.57  ? 52  THR A CB  1 
ATOM   363  O  OG1 . THR A 1 46  ? 22.170 -5.157  7.175  1.00 18.52  ? 52  THR A OG1 1 
ATOM   364  C  CG2 . THR A 1 46  ? 20.431 -4.300  5.806  1.00 17.86  ? 52  THR A CG2 1 
ATOM   365  N  N   . ILE A 1 47  ? 19.935 -1.144  6.843  1.00 13.53  ? 53  ILE A N   1 
ATOM   366  C  CA  . ILE A 1 47  ? 18.729 -0.273  6.720  1.00 12.19  ? 53  ILE A CA  1 
ATOM   367  C  C   . ILE A 1 47  ? 17.719 -0.974  5.805  1.00 12.52  ? 53  ILE A C   1 
ATOM   368  O  O   . ILE A 1 47  ? 18.090 -1.538  4.757  1.00 12.94  ? 53  ILE A O   1 
ATOM   369  C  CB  . ILE A 1 47  ? 19.082 1.128   6.186  1.00 12.77  ? 53  ILE A CB  1 
ATOM   370  C  CG1 . ILE A 1 47  ? 20.233 1.806   6.962  1.00 14.47  ? 53  ILE A CG1 1 
ATOM   371  C  CG2 . ILE A 1 47  ? 17.841 2.007   6.138  1.00 12.89  ? 53  ILE A CG2 1 
ATOM   372  C  CD1 . ILE A 1 47  ? 19.993 1.952   8.436  1.00 15.44  ? 53  ILE A CD1 1 
ATOM   373  N  N   . ALA A 1 48  ? 16.463 -1.006  6.252  1.00 12.07  ? 54  ALA A N   1 
ATOM   374  C  CA  . ALA A 1 48  ? 15.312 -1.510  5.470  1.00 11.82  ? 54  ALA A CA  1 
ATOM   375  C  C   . ALA A 1 48  ? 15.103 -0.606  4.255  1.00 10.69  ? 54  ALA A C   1 
ATOM   376  O  O   . ALA A 1 48  ? 15.187 0.649   4.412  1.00 12.02  ? 54  ALA A O   1 
ATOM   377  C  CB  . ALA A 1 48  ? 14.084 -1.543  6.337  1.00 12.28  ? 54  ALA A CB  1 
ATOM   378  N  N   . ARG A 1 49  ? 14.730 -1.202  3.115  1.00 11.77  ? 55  ARG A N   1 
ATOM   379  C  CA  . ARG A 1 49  ? 14.361 -0.472  1.881  1.00 12.00  ? 55  ARG A CA  1 
ATOM   380  C  C   . ARG A 1 49  ? 13.057 -1.073  1.395  1.00 11.16  ? 55  ARG A C   1 
ATOM   381  O  O   . ARG A 1 49  ? 13.090 -2.118  0.801  1.00 12.43  ? 55  ARG A O   1 
ATOM   382  C  CB  . ARG A 1 49  ? 15.461 -0.546  0.812  1.00 11.43  ? 55  ARG A CB  1 
ATOM   383  C  CG  . ARG A 1 49  ? 16.808 0.033   1.242  1.00 12.49  ? 55  ARG A CG  1 
ATOM   384  C  CD  . ARG A 1 49  ? 16.881 1.523   1.590  1.00 12.07  ? 55  ARG A CD  1 
ATOM   385  N  NE  . ARG A 1 49  ? 18.225 1.898   2.129  1.00 13.93  ? 55  ARG A NE  1 
ATOM   386  C  CZ  . ARG A 1 49  ? 18.480 3.011   2.822  1.00 14.60  ? 55  ARG A CZ  1 
ATOM   387  N  NH1 . ARG A 1 49  ? 17.527 3.862   3.081  1.00 14.22  ? 55  ARG A NH1 1 
ATOM   388  N  NH2 . ARG A 1 49  ? 19.684 3.250   3.332  1.00 16.62  ? 55  ARG A NH2 1 
ATOM   389  N  N   . CYS A 1 50  ? 11.955 -0.490  1.821  1.00 11.66  ? 56  CYS A N   1 
ATOM   390  C  CA  . CYS A 1 50  ? 10.614 -1.108  1.813  1.00 11.47  ? 56  CYS A CA  1 
ATOM   391  C  C   . CYS A 1 50  ? 9.532  -0.120  2.242  1.00 11.68  ? 56  CYS A C   1 
ATOM   392  O  O   . CYS A 1 50  ? 9.859  1.025   2.677  1.00 11.68  ? 56  CYS A O   1 
ATOM   393  C  CB  . CYS A 1 50  ? 10.593 -2.297  2.762  1.00 12.19  ? 56  CYS A CB  1 
ATOM   394  S  SG  . CYS A 1 50  ? 10.604 -1.784  4.536  1.00 11.83  ? 56  CYS A SG  1 
ATOM   395  N  N   A ASP A 1 51  ? 8.260  -0.508  2.133  0.33 11.48  ? 57  ASP A N   1 
ATOM   396  N  N   B ASP A 1 51  ? 8.293  -0.610  2.150  0.29 12.19  ? 57  ASP A N   1 
ATOM   397  C  CA  A ASP A 1 51  ? 7.125  0.268   2.717  0.33 11.95  ? 57  ASP A CA  1 
ATOM   398  C  CA  B ASP A 1 51  ? 7.018  0.082   2.471  0.29 13.27  ? 57  ASP A CA  1 
ATOM   399  C  C   A ASP A 1 51  ? 6.348  -0.624  3.688  0.33 11.72  ? 57  ASP A C   1 
ATOM   400  C  C   B ASP A 1 51  ? 6.349  -0.593  3.686  0.29 12.45  ? 57  ASP A C   1 
ATOM   401  O  O   A ASP A 1 51  ? 5.107  -0.543  3.760  0.33 12.95  ? 57  ASP A O   1 
ATOM   402  O  O   B ASP A 1 51  ? 5.165  -0.306  3.934  0.29 13.53  ? 57  ASP A O   1 
ATOM   403  C  CB  A ASP A 1 51  ? 6.186  0.836   1.651  0.33 12.44  ? 57  ASP A CB  1 
ATOM   404  C  CB  B ASP A 1 51  ? 6.108  0.036   1.230  0.29 14.74  ? 57  ASP A CB  1 
ATOM   405  C  CG  A ASP A 1 51  ? 5.485  -0.217  0.812  0.33 13.80  ? 57  ASP A CG  1 
ATOM   406  C  CG  B ASP A 1 51  ? 4.984  1.061   1.147  0.29 16.53  ? 57  ASP A CG  1 
ATOM   407  O  OD1 A ASP A 1 51  ? 5.697  -1.422  1.061  0.33 14.27  ? 57  ASP A OD1 1 
ATOM   408  O  OD1 B ASP A 1 51  ? 5.151  2.184   1.677  0.29 19.13  ? 57  ASP A OD1 1 
ATOM   409  O  OD2 A ASP A 1 51  ? 4.710  0.189   -0.081 0.33 16.36  ? 57  ASP A OD2 1 
ATOM   410  O  OD2 B ASP A 1 51  ? 3.938  0.727   0.554  0.29 18.21  ? 57  ASP A OD2 1 
ATOM   411  N  N   . CYS A 1 52  ? 7.058  -1.427  4.468  1.00 12.14  ? 58  CYS A N   1 
ATOM   412  C  CA  . CYS A 1 52  ? 6.399  -2.176  5.577  1.00 11.16  ? 58  CYS A CA  1 
ATOM   413  C  C   . CYS A 1 52  ? 5.729  -1.187  6.555  1.00 11.32  ? 58  CYS A C   1 
ATOM   414  O  O   . CYS A 1 52  ? 6.210  -0.044  6.757  1.00 12.80  ? 58  CYS A O   1 
ATOM   415  C  CB  . CYS A 1 52  ? 7.355  -3.010  6.415  1.00 13.06  ? 58  CYS A CB  1 
ATOM   416  S  SG  . CYS A 1 52  ? 8.090  -4.422  5.585  1.00 13.42  ? 58  CYS A SG  1 
ATOM   417  N  N   . GLN A 1 53  ? 4.602  -1.661  7.126  1.00 11.78  ? 59  GLN A N   1 
ATOM   418  C  CA  . GLN A 1 53  ? 3.847  -1.003  8.210  1.00 11.54  ? 59  GLN A CA  1 
ATOM   419  C  C   . GLN A 1 53  ? 3.687  -1.910  9.425  1.00 10.57  ? 59  GLN A C   1 
ATOM   420  O  O   . GLN A 1 53  ? 2.886  -1.606  10.338 1.00 12.61  ? 59  GLN A O   1 
ATOM   421  C  CB  . GLN A 1 53  ? 2.473  -0.520  7.730  1.00 11.93  ? 59  GLN A CB  1 
ATOM   422  C  CG  . GLN A 1 53  ? 2.541  0.688   6.818  1.00 13.59  ? 59  GLN A CG  1 
ATOM   423  C  CD  . GLN A 1 53  ? 1.174  1.278   6.566  1.00 13.97  ? 59  GLN A CD  1 
ATOM   424  O  OE1 . GLN A 1 53  ? 0.572  1.034   5.515  1.00 17.46  ? 59  GLN A OE1 1 
ATOM   425  N  NE2 . GLN A 1 53  ? 0.607  1.994   7.533  1.00 14.27  ? 59  GLN A NE2 1 
ATOM   426  N  N   . THR A 1 54  ? 4.468  -2.963  9.501  1.00 11.79  ? 60  THR A N   1 
ATOM   427  C  CA  . THR A 1 54  ? 4.578  -3.817  10.708 1.00 12.57  ? 60  THR A CA  1 
ATOM   428  C  C   . THR A 1 54  ? 6.041  -4.094  11.046 1.00 11.02  ? 60  THR A C   1 
ATOM   429  O  O   . THR A 1 54  ? 6.896  -4.222  10.158 1.00 13.63  ? 60  THR A O   1 
ATOM   430  C  CB  . THR A 1 54  ? 3.780  -5.123  10.657 1.00 13.80  ? 60  THR A CB  1 
ATOM   431  O  OG1 . THR A 1 54  ? 4.421  -5.945  9.711  1.00 18.51  ? 60  THR A OG1 1 
ATOM   432  C  CG2 . THR A 1 54  ? 2.327  -4.926  10.337 1.00 15.04  ? 60  THR A CG2 1 
ATOM   433  N  N   . GLY A 1 55  ? 6.353  -4.101  12.343 1.00 10.13  ? 61  GLY A N   1 
ATOM   434  C  CA  . GLY A 1 55  ? 7.700  -4.290  12.827 1.00 10.79  ? 61  GLY A CA  1 
ATOM   435  C  C   . GLY A 1 55  ? 7.732  -4.515  14.315 1.00 10.34  ? 61  GLY A C   1 
ATOM   436  O  O   . GLY A 1 55  ? 6.719  -4.837  14.934 1.00 11.51  ? 61  GLY A O   1 
ATOM   437  N  N   . VAL A 1 56  ? 8.928  -4.416  14.850 1.00 10.43  ? 62  VAL A N   1 
ATOM   438  C  CA  . VAL A 1 56  ? 9.181  -4.595  16.308 1.00 10.95  ? 62  VAL A CA  1 
ATOM   439  C  C   . VAL A 1 56  ? 10.026 -3.432  16.779 1.00 10.73  ? 62  VAL A C   1 
ATOM   440  O  O   . VAL A 1 56  ? 11.057 -3.172  16.144 1.00 11.05  ? 62  VAL A O   1 
ATOM   441  C  CB  . VAL A 1 56  ? 9.835  -5.961  16.610 1.00 11.51  ? 62  VAL A CB  1 
ATOM   442  C  CG1 . VAL A 1 56  ? 10.248 -6.082  18.072 1.00 11.97  ? 62  VAL A CG1 1 
ATOM   443  C  CG2 . VAL A 1 56  ? 8.902  -7.091  16.226 1.00 11.89  ? 62  VAL A CG2 1 
ATOM   444  N  N   . TYR A 1 57  ? 9.697  -2.785  17.910 1.00 11.15  ? 63  TYR A N   1 
ATOM   445  C  CA  . TYR A 1 57  ? 10.596 -1.731  18.455 1.00 10.48  ? 63  TYR A CA  1 
ATOM   446  C  C   . TYR A 1 57  ? 11.046 -1.986  19.902 1.00 10.78  ? 63  TYR A C   1 
ATOM   447  O  O   . TYR A 1 57  ? 10.358 -2.728  20.634 1.00 10.86  ? 63  TYR A O   1 
ATOM   448  C  CB  . TYR A 1 57  ? 9.946  -0.338  18.402 1.00 11.56  ? 63  TYR A CB  1 
ATOM   449  C  CG  . TYR A 1 57  ? 9.041  0.041   19.563 1.00 11.28  ? 63  TYR A CG  1 
ATOM   450  C  CD1 . TYR A 1 57  ? 7.779  -0.505  19.669 1.00 11.87  ? 63  TYR A CD1 1 
ATOM   451  C  CD2 . TYR A 1 57  ? 9.464  0.902   20.574 1.00 11.84  ? 63  TYR A CD2 1 
ATOM   452  C  CE1 . TYR A 1 57  ? 6.906  -0.160  20.702 1.00 12.34  ? 63  TYR A CE1 1 
ATOM   453  C  CE2 . TYR A 1 57  ? 8.609  1.271   21.612 1.00 11.48  ? 63  TYR A CE2 1 
ATOM   454  C  CZ  . TYR A 1 57  ? 7.336  0.713   21.702 1.00 11.28  ? 63  TYR A CZ  1 
ATOM   455  O  OH  . TYR A 1 57  ? 6.486  1.037   22.731 1.00 12.60  ? 63  TYR A OH  1 
ATOM   456  N  N   . TYR A 1 58  ? 12.177 -1.445  20.268 1.00 10.85  ? 64  TYR A N   1 
ATOM   457  C  CA  . TYR A 1 58  ? 12.728 -1.560  21.626 1.00 11.34  ? 64  TYR A CA  1 
ATOM   458  C  C   . TYR A 1 58  ? 12.300 -0.361  22.464 1.00 11.05  ? 64  TYR A C   1 
ATOM   459  O  O   . TYR A 1 58  ? 12.568 0.824   22.080 1.00 10.71  ? 64  TYR A O   1 
ATOM   460  C  CB  . TYR A 1 58  ? 14.248 -1.668  21.628 1.00 11.37  ? 64  TYR A CB  1 
ATOM   461  C  CG  . TYR A 1 58  ? 14.768 -1.828  23.030 1.00 13.03  ? 64  TYR A CG  1 
ATOM   462  C  CD1 . TYR A 1 58  ? 14.396 -2.929  23.774 1.00 14.44  ? 64  TYR A CD1 1 
ATOM   463  C  CD2 . TYR A 1 58  ? 15.573 -0.866  23.606 1.00 12.56  ? 64  TYR A CD2 1 
ATOM   464  C  CE1 . TYR A 1 58  ? 14.831 -3.072  25.090 1.00 14.45  ? 64  TYR A CE1 1 
ATOM   465  C  CE2 . TYR A 1 58  ? 16.015 -0.985  24.917 1.00 14.68  ? 64  TYR A CE2 1 
ATOM   466  C  CZ  . TYR A 1 58  ? 15.616 -2.076  25.653 1.00 14.70  ? 64  TYR A CZ  1 
ATOM   467  O  OH  . TYR A 1 58  ? 16.114 -2.184  26.927 1.00 16.36  ? 64  TYR A OH  1 
ATOM   468  N  N   . CYS A 1 59  ? 11.724 -0.656  23.607 1.00 11.86  ? 65  CYS A N   1 
ATOM   469  C  CA  . CYS A 1 59  ? 11.262 0.294   24.642 1.00 10.97  ? 65  CYS A CA  1 
ATOM   470  C  C   . CYS A 1 59  ? 12.124 0.187   25.914 1.00 12.36  ? 65  CYS A C   1 
ATOM   471  O  O   . CYS A 1 59  ? 11.851 -0.712  26.766 1.00 12.77  ? 65  CYS A O   1 
ATOM   472  C  CB  . CYS A 1 59  ? 9.802  0.047   24.973 1.00 11.29  ? 65  CYS A CB  1 
ATOM   473  S  SG  . CYS A 1 59  ? 9.125  1.137   26.242 1.00 12.89  ? 65  CYS A SG  1 
ATOM   474  N  N   . SER A 1 60  ? 13.076 1.088   26.078 1.00 12.10  ? 66  SER A N   1 
ATOM   475  C  CA  . SER A 1 60  ? 14.039 0.999   27.202 1.00 13.57  ? 66  SER A CA  1 
ATOM   476  C  C   . SER A 1 60  ? 13.305 1.158   28.545 1.00 12.62  ? 66  SER A C   1 
ATOM   477  O  O   . SER A 1 60  ? 13.716 0.520   29.536 1.00 12.72  ? 66  SER A O   1 
ATOM   478  C  CB  . SER A 1 60  ? 15.197 1.995   27.018 1.00 14.37  ? 66  SER A CB  1 
ATOM   479  O  OG  . SER A 1 60  ? 14.820 3.335   27.222 1.00 19.17  ? 66  SER A OG  1 
ATOM   480  N  N   . SER A 1 61  ? 12.189 1.887   28.621 1.00 11.44  ? 67  SER A N   1 
ATOM   481  C  CA  . SER A 1 61  ? 11.480 2.191   29.891 1.00 11.98  ? 67  SER A CA  1 
ATOM   482  C  C   . SER A 1 61  ? 10.651 0.958   30.290 1.00 11.63  ? 67  SER A C   1 
ATOM   483  O  O   . SER A 1 61  ? 10.012 0.986   31.361 1.00 12.01  ? 67  SER A O   1 
ATOM   484  C  CB  . SER A 1 61  ? 10.646 3.437   29.851 1.00 11.76  ? 67  SER A CB  1 
ATOM   485  O  OG  . SER A 1 61  ? 9.604  3.355   28.847 1.00 11.94  ? 67  SER A OG  1 
ATOM   486  N  N   . ARG A 1 62  ? 10.686 -0.118  29.484 1.00 11.14  ? 68  ARG A N   1 
ATOM   487  C  CA  . ARG A 1 62  ? 10.002 -1.389  29.784 1.00 11.95  ? 68  ARG A CA  1 
ATOM   488  C  C   . ARG A 1 62  ? 11.008 -2.533  29.718 1.00 11.72  ? 68  ARG A C   1 
ATOM   489  O  O   . ARG A 1 62  ? 10.613 -3.666  30.029 1.00 12.93  ? 68  ARG A O   1 
ATOM   490  C  CB  . ARG A 1 62  ? 8.812  -1.592  28.853 1.00 12.24  ? 68  ARG A CB  1 
ATOM   491  C  CG  . ARG A 1 62  ? 7.667  -0.622  29.108 1.00 13.09  ? 68  ARG A CG  1 
ATOM   492  C  CD  . ARG A 1 62  ? 6.842  -0.897  30.357 1.00 13.66  ? 68  ARG A CD  1 
ATOM   493  N  NE  . ARG A 1 62  ? 5.811  0.081   30.569 1.00 14.00  ? 68  ARG A NE  1 
ATOM   494  C  CZ  . ARG A 1 62  ? 5.949  1.273   31.138 1.00 12.66  ? 68  ARG A CZ  1 
ATOM   495  N  NH1 . ARG A 1 62  ? 7.093  1.642   31.676 1.00 13.31  ? 68  ARG A NH1 1 
ATOM   496  N  NH2 . ARG A 1 62  ? 4.905  2.070   31.246 1.00 14.82  ? 68  ARG A NH2 1 
ATOM   497  N  N   . ARG A 1 63  ? 12.250 -2.307  29.286 1.00 12.65  ? 69  ARG A N   1 
ATOM   498  C  CA  . ARG A 1 63  ? 13.230 -3.375  28.970 1.00 13.50  ? 69  ARG A CA  1 
ATOM   499  C  C   . ARG A 1 63  ? 12.558 -4.412  28.086 1.00 14.58  ? 69  ARG A C   1 
ATOM   500  O  O   . ARG A 1 63  ? 12.696 -5.630  28.368 1.00 15.41  ? 69  ARG A O   1 
ATOM   501  C  CB  . ARG A 1 63  ? 13.785 -4.004  30.253 1.00 13.38  ? 69  ARG A CB  1 
ATOM   502  C  CG  . ARG A 1 63  ? 14.702 -3.073  31.025 1.00 13.94  ? 69  ARG A CG  1 
ATOM   503  C  CD  . ARG A 1 63  ? 15.317 -3.786  32.223 1.00 14.40  ? 69  ARG A CD  1 
ATOM   504  N  NE  . ARG A 1 63  ? 16.143 -2.933  33.095 1.00 16.91  ? 69  ARG A NE  1 
ATOM   505  C  CZ  . ARG A 1 63  ? 15.903 -2.657  34.382 1.00 16.63  ? 69  ARG A CZ  1 
ATOM   506  N  NH1 . ARG A 1 63  ? 14.821 -3.136  34.990 1.00 15.64  ? 69  ARG A NH1 1 
ATOM   507  N  NH2 . ARG A 1 63  ? 16.760 -1.903  35.056 1.00 17.79  ? 69  ARG A NH2 1 
ATOM   508  N  N   . LYS A 1 64  ? 11.820 -3.989  27.047 1.00 14.58  ? 70  LYS A N   1 
ATOM   509  C  CA  . LYS A 1 64  ? 11.017 -4.952  26.256 1.00 16.02  ? 70  LYS A CA  1 
ATOM   510  C  C   . LYS A 1 64  ? 10.960 -4.495  24.804 1.00 13.82  ? 70  LYS A C   1 
ATOM   511  O  O   . LYS A 1 64  ? 10.946 -3.278  24.573 1.00 13.06  ? 70  LYS A O   1 
ATOM   512  C  CB  . LYS A 1 64  ? 9.587  -5.122  26.768 1.00 18.16  ? 70  LYS A CB  1 
ATOM   513  C  CG  . LYS A 1 64  ? 9.439  -5.978  28.018 1.00 25.58  ? 70  LYS A CG  1 
ATOM   514  C  CD  . LYS A 1 64  ? 8.037  -6.525  28.219 1.00 31.43  ? 70  LYS A CD  1 
ATOM   515  C  CE  . LYS A 1 64  ? 7.926  -7.353  29.487 1.00 36.31  ? 70  LYS A CE  1 
ATOM   516  N  NZ  . LYS A 1 64  ? 8.442  -6.618  30.671 1.00 44.04  ? 70  LYS A NZ  1 
ATOM   517  N  N   . HIS A 1 65  ? 10.954 -5.447  23.910 1.00 13.06  ? 71  HIS A N   1 
ATOM   518  C  CA  . HIS A 1 65  ? 10.598 -5.257  22.495 1.00 12.81  ? 71  HIS A CA  1 
ATOM   519  C  C   . HIS A 1 65  ? 9.119  -5.557  22.319 1.00 13.38  ? 71  HIS A C   1 
ATOM   520  O  O   . HIS A 1 65  ? 8.610  -6.555  22.891 1.00 15.92  ? 71  HIS A O   1 
ATOM   521  C  CB  . HIS A 1 65  ? 11.473 -6.149  21.621 1.00 12.53  ? 71  HIS A CB  1 
ATOM   522  C  CG  . HIS A 1 65  ? 12.929 -5.872  21.649 1.00 12.57  ? 71  HIS A CG  1 
ATOM   523  N  ND1 . HIS A 1 65  ? 13.644 -5.192  20.670 1.00 15.73  ? 71  HIS A ND1 1 
ATOM   524  C  CD2 . HIS A 1 65  ? 13.833 -6.211  22.583 1.00 13.74  ? 71  HIS A CD2 1 
ATOM   525  C  CE1 . HIS A 1 65  ? 14.921 -5.118  21.016 1.00 12.76  ? 71  HIS A CE1 1 
ATOM   526  N  NE2 . HIS A 1 65  ? 15.071 -5.788  22.148 1.00 17.68  ? 71  HIS A NE2 1 
ATOM   527  N  N   . TYR A 1 66  ? 8.422  -4.772  21.508 1.00 11.36  ? 72  TYR A N   1 
ATOM   528  C  CA  . TYR A 1 66  ? 6.981  -4.892  21.209 1.00 12.18  ? 72  TYR A CA  1 
ATOM   529  C  C   . TYR A 1 66  ? 6.757  -4.968  19.696 1.00 12.05  ? 72  TYR A C   1 
ATOM   530  O  O   . TYR A 1 66  ? 7.251  -4.117  18.944 1.00 12.02  ? 72  TYR A O   1 
ATOM   531  C  CB  . TYR A 1 66  ? 6.237  -3.662  21.740 1.00 12.70  ? 72  TYR A CB  1 
ATOM   532  C  CG  . TYR A 1 66  ? 6.219  -3.540  23.238 1.00 14.14  ? 72  TYR A CG  1 
ATOM   533  C  CD1 . TYR A 1 66  ? 5.338  -4.296  24.018 1.00 15.65  ? 72  TYR A CD1 1 
ATOM   534  C  CD2 . TYR A 1 66  ? 7.036  -2.638  23.882 1.00 14.59  ? 72  TYR A CD2 1 
ATOM   535  C  CE1 . TYR A 1 66  ? 5.353  -4.184  25.403 1.00 14.99  ? 72  TYR A CE1 1 
ATOM   536  C  CE2 . TYR A 1 66  ? 7.054  -2.505  25.266 1.00 14.46  ? 72  TYR A CE2 1 
ATOM   537  C  CZ  . TYR A 1 66  ? 6.185  -3.289  26.024 1.00 14.91  ? 72  TYR A CZ  1 
ATOM   538  O  OH  . TYR A 1 66  ? 6.124  -3.146  27.398 1.00 16.64  ? 72  TYR A OH  1 
ATOM   539  N  N   . PRO A 1 67  ? 5.921  -5.913  19.236 1.00 12.33  ? 73  PRO A N   1 
ATOM   540  C  CA  . PRO A 1 67  ? 5.417  -5.876  17.864 1.00 12.62  ? 73  PRO A CA  1 
ATOM   541  C  C   . PRO A 1 67  ? 4.384  -4.752  17.709 1.00 13.65  ? 73  PRO A C   1 
ATOM   542  O  O   . PRO A 1 67  ? 3.432  -4.673  18.489 1.00 14.83  ? 73  PRO A O   1 
ATOM   543  C  CB  . PRO A 1 67  ? 4.808  -7.264  17.649 1.00 13.84  ? 73  PRO A CB  1 
ATOM   544  C  CG  . PRO A 1 67  ? 4.493  -7.790  19.001 1.00 15.21  ? 73  PRO A CG  1 
ATOM   545  C  CD  . PRO A 1 67  ? 5.427  -7.093  19.977 1.00 13.41  ? 73  PRO A CD  1 
ATOM   546  N  N   . VAL A 1 68  ? 4.523  -3.982  16.634 1.00 12.41  ? 74  VAL A N   1 
ATOM   547  C  CA  . VAL A 1 68  ? 3.593  -2.846  16.364 1.00 11.86  ? 74  VAL A CA  1 
ATOM   548  C  C   . VAL A 1 68  ? 3.246  -2.763  14.893 1.00 11.78  ? 74  VAL A C   1 
ATOM   549  O  O   . VAL A 1 68  ? 4.042  -3.178  14.012 1.00 13.64  ? 74  VAL A O   1 
ATOM   550  C  CB  . VAL A 1 68  ? 4.181  -1.502  16.833 1.00 12.44  ? 74  VAL A CB  1 
ATOM   551  C  CG1 . VAL A 1 68  ? 4.234  -1.414  18.336 1.00 13.69  ? 74  VAL A CG1 1 
ATOM   552  C  CG2 . VAL A 1 68  ? 5.564  -1.246  16.259 1.00 13.42  ? 74  VAL A CG2 1 
ATOM   553  N  N   . SER A 1 69  ? 2.074  -2.221  14.637 1.00 11.98  ? 75  SER A N   1 
ATOM   554  C  CA  . SER A 1 69  ? 1.678  -1.637  13.328 1.00 11.81  ? 75  SER A CA  1 
ATOM   555  C  C   . SER A 1 69  ? 1.941  -0.138  13.418 1.00 11.84  ? 75  SER A C   1 
ATOM   556  O  O   . SER A 1 69  ? 1.710  0.467   14.480 1.00 12.68  ? 75  SER A O   1 
ATOM   557  C  CB  . SER A 1 69  ? 0.210  -1.890  13.077 1.00 13.50  ? 75  SER A CB  1 
ATOM   558  O  OG  . SER A 1 69  ? -0.074 -3.287  13.023 1.00 19.90  ? 75  SER A OG  1 
ATOM   559  N  N   . PHE A 1 70  ? 2.403  0.469   12.351 1.00 10.32  ? 76  PHE A N   1 
ATOM   560  C  CA  . PHE A 1 70  ? 2.727  1.908   12.314 1.00 10.08  ? 76  PHE A CA  1 
ATOM   561  C  C   . PHE A 1 70  ? 2.275  2.538   11.013 1.00 10.86  ? 76  PHE A C   1 
ATOM   562  O  O   . PHE A 1 70  ? 2.209  1.871   9.946  1.00 12.61  ? 76  PHE A O   1 
ATOM   563  C  CB  . PHE A 1 70  ? 4.217  2.178   12.592 1.00 10.34  ? 76  PHE A CB  1 
ATOM   564  C  CG  . PHE A 1 70  ? 5.220  1.428   11.740 1.00 10.82  ? 76  PHE A CG  1 
ATOM   565  C  CD1 . PHE A 1 70  ? 5.619  0.139   12.072 1.00 11.52  ? 76  PHE A CD1 1 
ATOM   566  C  CD2 . PHE A 1 70  ? 5.709  1.974   10.533 1.00 11.61  ? 76  PHE A CD2 1 
ATOM   567  C  CE1 . PHE A 1 70  ? 6.486  -0.586  11.269 1.00 12.78  ? 76  PHE A CE1 1 
ATOM   568  C  CE2 . PHE A 1 70  ? 6.615  1.229   9.770  1.00 10.47  ? 76  PHE A CE2 1 
ATOM   569  C  CZ  . PHE A 1 70  ? 6.987  -0.040  10.134 1.00 12.20  ? 76  PHE A CZ  1 
ATOM   570  N  N   . SER A 1 71  ? 2.008  3.831   11.112 1.00 11.40  ? 77  SER A N   1 
ATOM   571  C  CA  . SER A 1 71  ? 1.609  4.657   9.937  1.00 12.73  ? 77  SER A CA  1 
ATOM   572  C  C   . SER A 1 71  ? 2.814  4.932   9.040  1.00 12.48  ? 77  SER A C   1 
ATOM   573  O  O   . SER A 1 71  ? 3.944  4.888   9.492  1.00 12.78  ? 77  SER A O   1 
ATOM   574  C  CB  . SER A 1 71  ? 0.963  5.940   10.415 1.00 12.33  ? 77  SER A CB  1 
ATOM   575  O  OG  . SER A 1 71  ? 1.848  6.727   11.230 1.00 14.55  ? 77  SER A OG  1 
ATOM   576  N  N   . LYS A 1 72  ? 2.569  5.175   7.750  0.62 14.17  ? 78  LYS A N   1 
ATOM   577  C  CA  . LYS A 1 72  ? 3.637  5.583   6.796  0.62 14.18  ? 78  LYS A CA  1 
ATOM   578  C  C   . LYS A 1 72  ? 4.177  6.954   7.205  0.62 14.20  ? 78  LYS A C   1 
ATOM   579  O  O   . LYS A 1 72  ? 3.467  7.761   7.813  0.62 14.74  ? 78  LYS A O   1 
ATOM   580  C  CB  . LYS A 1 72  ? 3.097  5.561   5.365  0.62 15.07  ? 78  LYS A CB  1 
ATOM   581  C  CG  . LYS A 1 72  ? 2.637  4.189   4.897  0.62 16.21  ? 78  LYS A CG  1 
ATOM   582  C  CD  . LYS A 1 72  ? 2.171  4.141   3.450  0.62 17.86  ? 78  LYS A CD  1 
ATOM   583  C  CE  . LYS A 1 72  ? 2.300  2.741   2.881  0.62 19.96  ? 78  LYS A CE  1 
ATOM   584  N  NZ  . LYS A 1 72  ? 1.856  2.653   1.469  0.62 22.52  ? 78  LYS A NZ  1 
ATOM   585  N  N   . PRO A 1 73  ? 5.456  7.279   6.899  0.62 14.02  ? 79  PRO A N   1 
ATOM   586  C  CA  . PRO A 1 73  ? 6.018  8.557   7.321  0.62 14.73  ? 79  PRO A CA  1 
ATOM   587  C  C   . PRO A 1 73  ? 5.182  9.725   6.784  0.62 15.20  ? 79  PRO A C   1 
ATOM   588  O  O   . PRO A 1 73  ? 4.757  9.696   5.613  0.62 15.59  ? 79  PRO A O   1 
ATOM   589  C  CB  . PRO A 1 73  ? 7.439  8.587   6.739  0.62 14.27  ? 79  PRO A CB  1 
ATOM   590  C  CG  . PRO A 1 73  ? 7.753  7.150   6.382  0.62 14.76  ? 79  PRO A CG  1 
ATOM   591  C  CD  . PRO A 1 73  ? 6.428  6.437   6.193  0.62 14.05  ? 79  PRO A CD  1 
ATOM   592  N  N   . SER A 1 74  ? 4.940  10.715  7.642  0.62 15.73  ? 80  SER A N   1 
ATOM   593  C  CA  . SER A 1 74  ? 4.200  11.941  7.259  0.62 17.08  ? 80  SER A CA  1 
ATOM   594  C  C   . SER A 1 74  ? 4.628  13.125  8.129  0.62 16.59  ? 80  SER A C   1 
ATOM   595  O  O   . SER A 1 74  ? 5.587  13.017  8.960  0.62 15.23  ? 80  SER A O   1 
ATOM   596  C  CB  . SER A 1 74  ? 2.688  11.723  7.273  0.62 18.67  ? 80  SER A CB  1 
ATOM   597  O  OG  . SER A 1 74  ? 2.319  10.634  8.108  0.62 23.75  ? 80  SER A OG  1 
ATOM   598  N  N   . LEU A 1 75  ? 3.973  14.256  7.890  0.62 16.18  ? 81  LEU A N   1 
ATOM   599  C  CA  . LEU A 1 75  ? 4.221  15.558  8.547  0.62 16.18  ? 81  LEU A CA  1 
ATOM   600  C  C   . LEU A 1 75  ? 3.158  15.726  9.629  0.62 15.48  ? 81  LEU A C   1 
ATOM   601  O  O   . LEU A 1 75  ? 1.986  15.996  9.270  0.62 16.51  ? 81  LEU A O   1 
ATOM   602  C  CB  . LEU A 1 75  ? 4.155  16.649  7.475  0.62 16.81  ? 81  LEU A CB  1 
ATOM   603  C  CG  . LEU A 1 75  ? 4.500  18.064  7.934  0.62 17.98  ? 81  LEU A CG  1 
ATOM   604  C  CD1 . LEU A 1 75  ? 5.913  18.133  8.497  0.62 18.31  ? 81  LEU A CD1 1 
ATOM   605  C  CD2 . LEU A 1 75  ? 4.338  19.044  6.782  0.62 17.91  ? 81  LEU A CD2 1 
ATOM   606  N  N   . ILE A 1 76  ? 3.538  15.526  10.894 0.62 14.78  ? 82  ILE A N   1 
ATOM   607  C  CA  . ILE A 1 76  ? 2.576  15.362  12.018 0.62 15.75  ? 82  ILE A CA  1 
ATOM   608  C  C   . ILE A 1 76  ? 2.858  16.379  13.121 0.62 14.34  ? 82  ILE A C   1 
ATOM   609  O  O   . ILE A 1 76  ? 4.029  16.579  13.466 0.62 14.65  ? 82  ILE A O   1 
ATOM   610  C  CB  . ILE A 1 76  ? 2.621  13.926  12.579 0.62 16.69  ? 82  ILE A CB  1 
ATOM   611  C  CG1 . ILE A 1 76  ? 2.656  12.880  11.459 0.62 17.23  ? 82  ILE A CG1 1 
ATOM   612  C  CG2 . ILE A 1 76  ? 1.470  13.715  13.555 0.62 17.37  ? 82  ILE A CG2 1 
ATOM   613  C  CD1 . ILE A 1 76  ? 1.445  12.875  10.556 0.62 18.76  ? 82  ILE A CD1 1 
ATOM   614  N  N   . PHE A 1 77  ? 1.793  16.914  13.707 1.00 13.32  ? 83  PHE A N   1 
ATOM   615  C  CA  . PHE A 1 77  ? 1.872  17.781  14.895 1.00 13.31  ? 83  PHE A CA  1 
ATOM   616  C  C   . PHE A 1 77  ? 2.252  16.952  16.119 1.00 13.01  ? 83  PHE A C   1 
ATOM   617  O  O   . PHE A 1 77  ? 1.614  15.864  16.347 1.00 13.91  ? 83  PHE A O   1 
ATOM   618  C  CB  . PHE A 1 77  ? 0.585  18.573  15.148 1.00 13.71  ? 83  PHE A CB  1 
ATOM   619  C  CG  . PHE A 1 77  ? 0.795  19.623  16.202 1.00 14.57  ? 83  PHE A CG  1 
ATOM   620  C  CD1 . PHE A 1 77  ? 1.611  20.700  15.892 1.00 15.35  ? 83  PHE A CD1 1 
ATOM   621  C  CD2 . PHE A 1 77  ? 0.259  19.540  17.476 1.00 17.06  ? 83  PHE A CD2 1 
ATOM   622  C  CE1 . PHE A 1 77  ? 1.818  21.724  16.811 1.00 16.80  ? 83  PHE A CE1 1 
ATOM   623  C  CE2 . PHE A 1 77  ? 0.502  20.538  18.410 1.00 18.84  ? 83  PHE A CE2 1 
ATOM   624  C  CZ  . PHE A 1 77  ? 1.306  21.600  18.075 1.00 17.22  ? 83  PHE A CZ  1 
ATOM   625  N  N   . VAL A 1 78  ? 3.271  17.371  16.885 1.00 13.18  ? 84  VAL A N   1 
ATOM   626  C  CA  . VAL A 1 78  ? 3.733  16.664  18.105 1.00 13.01  ? 84  VAL A CA  1 
ATOM   627  C  C   . VAL A 1 78  ? 3.568  17.622  19.291 1.00 12.75  ? 84  VAL A C   1 
ATOM   628  O  O   . VAL A 1 78  ? 4.100  18.774  19.241 1.00 14.53  ? 84  VAL A O   1 
ATOM   629  C  CB  . VAL A 1 78  ? 5.176  16.159  17.920 1.00 13.34  ? 84  VAL A CB  1 
ATOM   630  C  CG1 . VAL A 1 78  ? 5.676  15.414  19.140 1.00 13.26  ? 84  VAL A CG1 1 
ATOM   631  C  CG2 . VAL A 1 78  ? 5.263  15.300  16.667 1.00 12.80  ? 84  VAL A CG2 1 
ATOM   632  N  N   . GLU A 1 79  ? 2.909  17.218  20.350 1.00 13.24  ? 85  GLU A N   1 
ATOM   633  C  CA  . GLU A 1 79  ? 2.774  18.062  21.559 1.00 13.31  ? 85  GLU A CA  1 
ATOM   634  C  C   . GLU A 1 79  ? 4.138  18.236  22.233 1.00 14.03  ? 85  GLU A C   1 
ATOM   635  O  O   . GLU A 1 79  ? 5.107  17.459  21.973 1.00 14.25  ? 85  GLU A O   1 
ATOM   636  C  CB  . GLU A 1 79  ? 1.778  17.417  22.524 1.00 14.21  ? 85  GLU A CB  1 
ATOM   637  C  CG  . GLU A 1 79  ? 0.364  17.370  21.980 1.00 15.82  ? 85  GLU A CG  1 
ATOM   638  C  CD  . GLU A 1 79  ? -0.322 18.699  21.697 1.00 17.23  ? 85  GLU A CD  1 
ATOM   639  O  OE1 . GLU A 1 79  ? 0.083  19.749  22.238 1.00 18.43  ? 85  GLU A OE1 1 
ATOM   640  O  OE2 . GLU A 1 79  ? -1.292 18.682  20.904 1.00 18.67  ? 85  GLU A OE2 1 
ATOM   641  N  N   . ALA A 1 80  ? 4.264  19.246  23.070 1.00 17.07  ? 86  ALA A N   1 
ATOM   642  C  CA  . ALA A 1 80  ? 5.529  19.542  23.775 1.00 16.49  ? 86  ALA A CA  1 
ATOM   643  C  C   . ALA A 1 80  ? 6.015  18.330  24.560 1.00 16.48  ? 86  ALA A C   1 
ATOM   644  O  O   . ALA A 1 80  ? 5.193  17.619  25.168 1.00 16.21  ? 86  ALA A O   1 
ATOM   645  C  CB  . ALA A 1 80  ? 5.359  20.733  24.674 1.00 17.62  ? 86  ALA A CB  1 
ATOM   646  N  N   . SER A 1 81  ? 7.338  18.133  24.565 1.00 16.24  ? 87  SER A N   1 
ATOM   647  C  CA  . SER A 1 81  ? 8.036  17.087  25.354 1.00 17.63  ? 87  SER A CA  1 
ATOM   648  C  C   . SER A 1 81  ? 9.116  17.764  26.190 1.00 17.94  ? 87  SER A C   1 
ATOM   649  O  O   . SER A 1 81  ? 9.313  18.996  26.066 1.00 18.49  ? 87  SER A O   1 
ATOM   650  C  CB  . SER A 1 81  ? 8.656  16.053  24.471 1.00 16.34  ? 87  SER A CB  1 
ATOM   651  O  OG  . SER A 1 81  ? 9.723  16.605  23.702 1.00 16.39  ? 87  SER A OG  1 
ATOM   652  N  N   . GLU A 1 82  ? 9.857  16.994  26.980 1.00 19.45  ? 88  GLU A N   1 
ATOM   653  C  CA  . GLU A 1 82  ? 10.946 17.588  27.794 1.00 19.74  ? 88  GLU A CA  1 
ATOM   654  C  C   . GLU A 1 82  ? 12.070 18.134  26.893 1.00 21.08  ? 88  GLU A C   1 
ATOM   655  O  O   . GLU A 1 82  ? 12.820 18.988  27.380 1.00 20.99  ? 88  GLU A O   1 
ATOM   656  C  CB  . GLU A 1 82  ? 11.381 16.617  28.901 1.00 21.68  ? 88  GLU A CB  1 
ATOM   657  C  CG  . GLU A 1 82  ? 12.214 15.471  28.423 1.00 26.94  ? 88  GLU A CG  1 
ATOM   658  C  CD  . GLU A 1 82  ? 12.886 14.691  29.549 1.00 30.64  ? 88  GLU A CD  1 
ATOM   659  O  OE1 . GLU A 1 82  ? 12.207 14.419  30.567 1.00 34.81  ? 88  GLU A OE1 1 
ATOM   660  O  OE2 . GLU A 1 82  ? 14.087 14.350  29.383 1.00 37.32  ? 88  GLU A OE2 1 
ATOM   661  N  N   . TYR A 1 83  ? 12.151 17.771  25.599 1.00 16.96  ? 89  TYR A N   1 
ATOM   662  C  CA  . TYR A 1 83  ? 13.318 18.091  24.724 1.00 15.95  ? 89  TYR A CA  1 
ATOM   663  C  C   . TYR A 1 83  ? 12.927 18.884  23.472 1.00 16.23  ? 89  TYR A C   1 
ATOM   664  O  O   . TYR A 1 83  ? 13.839 19.414  22.769 1.00 18.45  ? 89  TYR A O   1 
ATOM   665  C  CB  . TYR A 1 83  ? 14.057 16.793  24.343 1.00 15.41  ? 89  TYR A CB  1 
ATOM   666  C  CG  . TYR A 1 83  ? 13.214 15.659  23.793 1.00 15.45  ? 89  TYR A CG  1 
ATOM   667  C  CD1 . TYR A 1 83  ? 12.597 14.759  24.642 1.00 15.79  ? 89  TYR A CD1 1 
ATOM   668  C  CD2 . TYR A 1 83  ? 12.910 15.553  22.439 1.00 15.10  ? 89  TYR A CD2 1 
ATOM   669  C  CE1 . TYR A 1 83  ? 11.809 13.721  24.163 1.00 16.68  ? 89  TYR A CE1 1 
ATOM   670  C  CE2 . TYR A 1 83  ? 12.083 14.546  21.949 1.00 15.79  ? 89  TYR A CE2 1 
ATOM   671  C  CZ  . TYR A 1 83  ? 11.562 13.602  22.807 1.00 15.04  ? 89  TYR A CZ  1 
ATOM   672  O  OH  . TYR A 1 83  ? 10.768 12.585  22.345 1.00 15.18  ? 89  TYR A OH  1 
ATOM   673  N  N   . TYR A 1 84  ? 11.635 19.027  23.160 1.00 15.57  ? 90  TYR A N   1 
ATOM   674  C  CA  . TYR A 1 84  ? 11.169 19.952  22.085 1.00 15.34  ? 90  TYR A CA  1 
ATOM   675  C  C   . TYR A 1 84  ? 9.858  20.639  22.434 1.00 15.81  ? 90  TYR A C   1 
ATOM   676  O  O   . TYR A 1 84  ? 9.056  20.113  23.180 1.00 14.81  ? 90  TYR A O   1 
ATOM   677  C  CB  . TYR A 1 84  ? 10.864 19.215  20.787 1.00 15.66  ? 90  TYR A CB  1 
ATOM   678  C  CG  . TYR A 1 84  ? 12.079 18.776  19.997 1.00 15.03  ? 90  TYR A CG  1 
ATOM   679  C  CD1 . TYR A 1 84  ? 13.059 19.664  19.565 1.00 16.55  ? 90  TYR A CD1 1 
ATOM   680  C  CD2 . TYR A 1 84  ? 12.193 17.475  19.562 1.00 15.34  ? 90  TYR A CD2 1 
ATOM   681  C  CE1 . TYR A 1 84  ? 14.132 19.253  18.776 1.00 17.09  ? 90  TYR A CE1 1 
ATOM   682  C  CE2 . TYR A 1 84  ? 13.272 17.043  18.798 1.00 16.70  ? 90  TYR A CE2 1 
ATOM   683  C  CZ  . TYR A 1 84  ? 14.243 17.925  18.375 1.00 15.20  ? 90  TYR A CZ  1 
ATOM   684  O  OH  . TYR A 1 84  ? 15.300 17.476  17.595 1.00 16.38  ? 90  TYR A OH  1 
ATOM   685  N  N   . PRO A 1 85  ? 9.625  21.859  21.912 1.00 15.89  ? 91  PRO A N   1 
ATOM   686  C  CA  . PRO A 1 85  ? 8.314  22.496  22.055 1.00 15.88  ? 91  PRO A CA  1 
ATOM   687  C  C   . PRO A 1 85  ? 7.277  21.723  21.226 1.00 16.50  ? 91  PRO A C   1 
ATOM   688  O  O   . PRO A 1 85  ? 7.638  20.851  20.466 1.00 15.19  ? 91  PRO A O   1 
ATOM   689  C  CB  . PRO A 1 85  ? 8.549  23.879  21.452 1.00 16.07  ? 91  PRO A CB  1 
ATOM   690  C  CG  . PRO A 1 85  ? 9.621  23.640  20.423 1.00 18.07  ? 91  PRO A CG  1 
ATOM   691  C  CD  . PRO A 1 85  ? 10.544 22.620  21.061 1.00 17.15  ? 91  PRO A CD  1 
ATOM   692  N  N   . ALA A 1 86  ? 6.019  22.103  21.330 1.00 15.60  ? 92  ALA A N   1 
ATOM   693  C  CA  . ALA A 1 86  ? 4.967  21.618  20.428 1.00 17.74  ? 92  ALA A CA  1 
ATOM   694  C  C   . ALA A 1 86  ? 5.334  22.107  19.026 1.00 16.23  ? 92  ALA A C   1 
ATOM   695  O  O   . ALA A 1 86  ? 5.714  23.315  18.894 1.00 19.79  ? 92  ALA A O   1 
ATOM   696  C  CB  . ALA A 1 86  ? 3.633  22.148  20.891 1.00 18.45  ? 92  ALA A CB  1 
ATOM   697  N  N   . ARG A 1 87  ? 5.394  21.237  18.022 1.00 15.78  ? 93  ARG A N   1 
ATOM   698  C  CA  . ARG A 1 87  ? 5.834  21.594  16.660 1.00 17.53  ? 93  ARG A CA  1 
ATOM   699  C  C   . ARG A 1 87  ? 5.439  20.496  15.647 1.00 16.08  ? 93  ARG A C   1 
ATOM   700  O  O   . ARG A 1 87  ? 4.972  19.358  16.027 1.00 14.68  ? 93  ARG A O   1 
ATOM   701  C  CB  . ARG A 1 87  ? 7.343  21.862  16.733 1.00 17.24  ? 93  ARG A CB  1 
ATOM   702  C  CG  . ARG A 1 87  ? 8.121  20.564  16.809 1.00 16.75  ? 93  ARG A CG  1 
ATOM   703  C  CD  . ARG A 1 87  ? 9.625  20.679  16.986 1.00 17.33  ? 93  ARG A CD  1 
ATOM   704  N  NE  . ARG A 1 87  ? 10.195 19.366  16.704 1.00 17.53  ? 93  ARG A NE  1 
ATOM   705  C  CZ  . ARG A 1 87  ? 11.277 19.115  15.970 1.00 17.68  ? 93  ARG A CZ  1 
ATOM   706  N  NH1 . ARG A 1 87  ? 12.016 20.074  15.422 1.00 18.77  ? 93  ARG A NH1 1 
ATOM   707  N  NH2 . ARG A 1 87  ? 11.567 17.864  15.707 1.00 20.93  ? 93  ARG A NH2 1 
ATOM   708  N  N   . TYR A 1 88  ? 5.550  20.805  14.378 1.00 16.07  ? 94  TYR A N   1 
ATOM   709  C  CA  . TYR A 1 88  ? 5.432  19.831  13.280 1.00 16.14  ? 94  TYR A CA  1 
ATOM   710  C  C   . TYR A 1 88  ? 6.753  19.107  13.086 1.00 17.09  ? 94  TYR A C   1 
ATOM   711  O  O   . TYR A 1 88  ? 7.833  19.719  13.101 1.00 20.08  ? 94  TYR A O   1 
ATOM   712  C  CB  . TYR A 1 88  ? 4.967  20.533  12.014 1.00 16.44  ? 94  TYR A CB  1 
ATOM   713  C  CG  . TYR A 1 88  ? 3.481  20.752  12.016 1.00 17.15  ? 94  TYR A CG  1 
ATOM   714  C  CD1 . TYR A 1 88  ? 2.667  19.706  11.686 1.00 18.52  ? 94  TYR A CD1 1 
ATOM   715  C  CD2 . TYR A 1 88  ? 2.893  21.945  12.412 1.00 21.88  ? 94  TYR A CD2 1 
ATOM   716  C  CE1 . TYR A 1 88  ? 1.297  19.817  11.673 1.00 22.10  ? 94  TYR A CE1 1 
ATOM   717  C  CE2 . TYR A 1 88  ? 1.500  22.076  12.415 1.00 21.78  ? 94  TYR A CE2 1 
ATOM   718  C  CZ  . TYR A 1 88  ? 0.704  20.996  12.049 1.00 21.87  ? 94  TYR A CZ  1 
ATOM   719  O  OH  . TYR A 1 88  ? -0.670 20.986  12.032 1.00 26.16  ? 94  TYR A OH  1 
ATOM   720  N  N   . GLN A 1 89  ? 6.691  17.778  13.058 1.00 13.40  ? 95  GLN A N   1 
ATOM   721  C  CA  . GLN A 1 89  ? 7.857  16.917  12.772 1.00 13.96  ? 95  GLN A CA  1 
ATOM   722  C  C   . GLN A 1 89  ? 7.604  16.133  11.477 1.00 14.19  ? 95  GLN A C   1 
ATOM   723  O  O   . GLN A 1 89  ? 6.477  15.622  11.254 1.00 14.40  ? 95  GLN A O   1 
ATOM   724  C  CB  . GLN A 1 89  ? 8.094  16.004  13.955 1.00 14.37  ? 95  GLN A CB  1 
ATOM   725  C  CG  . GLN A 1 89  ? 9.315  15.131  13.788 1.00 14.84  ? 95  GLN A CG  1 
ATOM   726  C  CD  . GLN A 1 89  ? 9.911  14.589  15.086 1.00 14.27  ? 95  GLN A CD  1 
ATOM   727  O  OE1 . GLN A 1 89  ? 9.954  15.251  16.119 1.00 15.83  ? 95  GLN A OE1 1 
ATOM   728  N  NE2 . GLN A 1 89  ? 10.465 13.400  14.968 1.00 14.38  ? 95  GLN A NE2 1 
ATOM   729  N  N   . SER A 1 90  ? 8.555  16.124  10.548 1.00 13.44  ? 96  SER A N   1 
ATOM   730  C  CA  . SER A 1 90  ? 8.436  15.454  9.244  1.00 13.07  ? 96  SER A CA  1 
ATOM   731  C  C   . SER A 1 90  ? 8.970  14.005  9.314  1.00 12.45  ? 96  SER A C   1 
ATOM   732  O  O   . SER A 1 90  ? 9.774  13.681  10.222 1.00 12.34  ? 96  SER A O   1 
ATOM   733  C  CB  . SER A 1 90  ? 9.116  16.230  8.143  1.00 14.83  ? 96  SER A CB  1 
ATOM   734  O  OG  . SER A 1 90  ? 10.518 16.322  8.378  1.00 15.71  ? 96  SER A OG  1 
ATOM   735  N  N   . HIS A 1 91  ? 8.606  13.217  8.319  1.00 11.97  ? 97  HIS A N   1 
ATOM   736  C  CA  . HIS A 1 91  ? 9.083  11.813  8.168  1.00 11.85  ? 97  HIS A CA  1 
ATOM   737  C  C   . HIS A 1 91  ? 8.826  10.989  9.461  1.00 12.21  ? 97  HIS A C   1 
ATOM   738  O  O   . HIS A 1 91  ? 9.681  10.175  9.833  1.00 12.13  ? 97  HIS A O   1 
ATOM   739  C  CB  . HIS A 1 91  ? 10.560 11.826  7.737  1.00 13.64  ? 97  HIS A CB  1 
ATOM   740  C  CG  . HIS A 1 91  ? 10.788 12.520  6.438  1.00 13.11  ? 97  HIS A CG  1 
ATOM   741  N  ND1 . HIS A 1 91  ? 10.950 11.827  5.229  1.00 15.02  ? 97  HIS A ND1 1 
ATOM   742  C  CD2 . HIS A 1 91  ? 10.991 13.834  6.165  1.00 14.42  ? 97  HIS A CD2 1 
ATOM   743  C  CE1 . HIS A 1 91  ? 11.190 12.718  4.272  1.00 15.20  ? 97  HIS A CE1 1 
ATOM   744  N  NE2 . HIS A 1 91  ? 11.178 13.923  4.806  1.00 17.47  ? 97  HIS A NE2 1 
ATOM   745  N  N   . LEU A 1 92  ? 7.704  11.254  10.128 1.00 11.60  ? 98  LEU A N   1 
ATOM   746  C  CA  . LEU A 1 92  ? 7.362  10.607  11.417 1.00 11.15  ? 98  LEU A CA  1 
ATOM   747  C  C   . LEU A 1 92  ? 6.301  9.516   11.209 1.00 11.65  ? 98  LEU A C   1 
ATOM   748  O  O   . LEU A 1 92  ? 5.297  9.763   10.500 1.00 11.00  ? 98  LEU A O   1 
ATOM   749  C  CB  . LEU A 1 92  ? 6.882  11.668  12.409 1.00 11.38  ? 98  LEU A CB  1 
ATOM   750  C  CG  . LEU A 1 92  ? 6.579  11.159  13.811 1.00 12.27  ? 98  LEU A CG  1 
ATOM   751  C  CD1 . LEU A 1 92  ? 7.839  10.793  14.517 1.00 12.87  ? 98  LEU A CD1 1 
ATOM   752  C  CD2 . LEU A 1 92  ? 5.817  12.188  14.647 1.00 12.76  ? 98  LEU A CD2 1 
ATOM   753  N  N   . MET A 1 93  ? 6.513  8.364   11.827 1.00 11.19  ? 99  MET A N   1 
ATOM   754  C  CA  . MET A 1 93  ? 5.581  7.209   11.837 1.00 11.33  ? 99  MET A CA  1 
ATOM   755  C  C   . MET A 1 93  ? 4.990  7.075   13.227 1.00 11.01  ? 99  MET A C   1 
ATOM   756  O  O   . MET A 1 93  ? 5.753  7.225   14.172 1.00 11.90  ? 99  MET A O   1 
ATOM   757  C  CB  . MET A 1 93  ? 6.351  5.956   11.405 1.00 11.22  ? 99  MET A CB  1 
ATOM   758  C  CG  . MET A 1 93  ? 6.917  6.048   9.999  1.00 12.27  ? 99  MET A CG  1 
ATOM   759  S  SD  . MET A 1 93  ? 8.057  4.711   9.586  1.00 13.34  ? 99  MET A SD  1 
ATOM   760  C  CE  . MET A 1 93  ? 9.412  5.009   10.717 1.00 11.61  ? 99  MET A CE  1 
ATOM   761  N  N   . LEU A 1 94  ? 3.709  6.726   13.367 1.00 10.98  ? 100 LEU A N   1 
ATOM   762  C  CA  . LEU A 1 94  ? 3.134  6.545   14.721 1.00 10.48  ? 100 LEU A CA  1 
ATOM   763  C  C   . LEU A 1 94  ? 2.650  5.115   14.896 1.00 10.84  ? 100 LEU A C   1 
ATOM   764  O  O   . LEU A 1 94  ? 2.090  4.539   13.929 1.00 11.30  ? 100 LEU A O   1 
ATOM   765  C  CB  . LEU A 1 94  ? 1.950  7.500   14.924 1.00 11.14  ? 100 LEU A CB  1 
ATOM   766  C  CG  . LEU A 1 94  ? 2.275  8.983   14.995 1.00 11.99  ? 100 LEU A CG  1 
ATOM   767  C  CD1 . LEU A 1 94  ? 1.033  9.857   14.996 1.00 13.44  ? 100 LEU A CD1 1 
ATOM   768  C  CD2 . LEU A 1 94  ? 3.155  9.250   16.228 1.00 13.42  ? 100 LEU A CD2 1 
ATOM   769  N  N   . ALA A 1 95  ? 2.781  4.610   16.117 1.00 9.85   ? 101 ALA A N   1 
ATOM   770  C  CA  . ALA A 1 95  ? 2.172  3.357   16.567 1.00 9.96   ? 101 ALA A CA  1 
ATOM   771  C  C   . ALA A 1 95  ? 1.556  3.534   17.953 1.00 10.94  ? 101 ALA A C   1 
ATOM   772  O  O   . ALA A 1 95  ? 1.903  4.488   18.668 1.00 11.16  ? 101 ALA A O   1 
ATOM   773  C  CB  . ALA A 1 95  ? 3.186  2.242   16.605 1.00 11.16  ? 101 ALA A CB  1 
ATOM   774  N  N   . VAL A 1 96  ? 0.665  2.622   18.321 1.00 11.23  ? 102 VAL A N   1 
ATOM   775  C  CA  . VAL A 1 96  ? 0.095  2.549   19.691 1.00 11.39  ? 102 VAL A CA  1 
ATOM   776  C  C   . VAL A 1 96  ? 1.080  1.784   20.564 1.00 11.33  ? 102 VAL A C   1 
ATOM   777  O  O   . VAL A 1 96  ? 1.388  0.587   20.281 1.00 11.74  ? 102 VAL A O   1 
ATOM   778  C  CB  . VAL A 1 96  ? -1.314 1.931   19.709 1.00 11.31  ? 102 VAL A CB  1 
ATOM   779  C  CG1 . VAL A 1 96  ? -1.843 1.811   21.156 1.00 11.43  ? 102 VAL A CG1 1 
ATOM   780  C  CG2 . VAL A 1 96  ? -2.251 2.741   18.855 1.00 10.96  ? 102 VAL A CG2 1 
ATOM   781  N  N   . GLY A 1 97  ? 1.602  2.445   21.580 1.00 11.82  ? 103 GLY A N   1 
ATOM   782  C  CA  . GLY A 1 97  ? 2.644  1.857   22.423 1.00 11.49  ? 103 GLY A CA  1 
ATOM   783  C  C   . GLY A 1 97  ? 3.182  2.853   23.432 1.00 11.94  ? 103 GLY A C   1 
ATOM   784  O  O   . GLY A 1 97  ? 2.854  4.012   23.367 1.00 13.10  ? 103 GLY A O   1 
ATOM   785  N  N   . HIS A 1 98  ? 4.062  2.386   24.299 1.00 11.55  ? 104 HIS A N   1 
ATOM   786  C  CA  . HIS A 1 98  ? 4.684  3.186   25.368 1.00 12.03  ? 104 HIS A CA  1 
ATOM   787  C  C   . HIS A 1 98  ? 5.963  3.849   24.871 1.00 10.26  ? 104 HIS A C   1 
ATOM   788  O  O   . HIS A 1 98  ? 6.880  3.158   24.374 1.00 11.35  ? 104 HIS A O   1 
ATOM   789  C  CB  . HIS A 1 98  ? 4.922  2.310   26.607 1.00 11.38  ? 104 HIS A CB  1 
ATOM   790  C  CG  . HIS A 1 98  ? 5.387  3.122   27.753 1.00 12.44  ? 104 HIS A CG  1 
ATOM   791  N  ND1 . HIS A 1 98  ? 4.572  4.079   28.341 1.00 15.03  ? 104 HIS A ND1 1 
ATOM   792  C  CD2 . HIS A 1 98  ? 6.598  3.254   28.305 1.00 13.61  ? 104 HIS A CD2 1 
ATOM   793  C  CE1 . HIS A 1 98  ? 5.284  4.680   29.288 1.00 13.99  ? 104 HIS A CE1 1 
ATOM   794  N  NE2 . HIS A 1 98  ? 6.500  4.215   29.255 1.00 14.38  ? 104 HIS A NE2 1 
ATOM   795  N  N   . SER A 1 99  ? 6.092  5.153   25.166 1.00 11.14  ? 105 SER A N   1 
ATOM   796  C  CA  . SER A 1 99  ? 7.294  5.935   24.837 1.00 12.28  ? 105 SER A CA  1 
ATOM   797  C  C   . SER A 1 99  ? 7.412  7.135   25.778 1.00 12.73  ? 105 SER A C   1 
ATOM   798  O  O   . SER A 1 99  ? 6.479  7.991   25.830 1.00 15.07  ? 105 SER A O   1 
ATOM   799  C  CB  . SER A 1 99  ? 7.282  6.374   23.365 1.00 11.86  ? 105 SER A CB  1 
ATOM   800  O  OG  . SER A 1 99  ? 8.443  7.182   23.070 1.00 12.98  ? 105 SER A OG  1 
ATOM   801  N  N   . GLU A 1 100 ? 8.505  7.175   26.493 1.00 12.71  ? 106 GLU A N   1 
ATOM   802  C  CA  . GLU A 1 100 ? 8.966  8.315   27.355 1.00 14.02  ? 106 GLU A CA  1 
ATOM   803  C  C   . GLU A 1 100 ? 10.210 8.931   26.726 1.00 15.64  ? 106 GLU A C   1 
ATOM   804  O  O   . GLU A 1 100 ? 10.884 8.341   25.855 1.00 14.76  ? 106 GLU A O   1 
ATOM   805  C  CB  . GLU A 1 100 ? 9.320  7.810   28.769 1.00 17.46  ? 106 GLU A CB  1 
ATOM   806  C  CG  . GLU A 1 100 ? 8.153  7.225   29.532 1.00 19.34  ? 106 GLU A CG  1 
ATOM   807  C  CD  . GLU A 1 100 ? 8.554  6.517   30.836 1.00 19.75  ? 106 GLU A CD  1 
ATOM   808  O  OE1 . GLU A 1 100 ? 9.539  6.948   31.501 1.00 25.79  ? 106 GLU A OE1 1 
ATOM   809  O  OE2 . GLU A 1 100 ? 7.921  5.567   31.202 1.00 20.65  ? 106 GLU A OE2 1 
ATOM   810  N  N   . PRO A 1 101 ? 10.644 10.138  27.166 1.00 15.88  ? 107 PRO A N   1 
ATOM   811  C  CA  . PRO A 1 101 ? 11.792 10.772  26.515 1.00 15.85  ? 107 PRO A CA  1 
ATOM   812  C  C   . PRO A 1 101 ? 13.055 9.905   26.401 1.00 17.37  ? 107 PRO A C   1 
ATOM   813  O  O   . PRO A 1 101 ? 13.749 9.907   25.347 1.00 17.64  ? 107 PRO A O   1 
ATOM   814  C  CB  . PRO A 1 101 ? 11.994 11.975  27.437 1.00 16.54  ? 107 PRO A CB  1 
ATOM   815  C  CG  . PRO A 1 101 ? 10.587 12.355  27.795 1.00 16.21  ? 107 PRO A CG  1 
ATOM   816  C  CD  . PRO A 1 101 ? 9.981  11.009  28.169 1.00 16.62  ? 107 PRO A CD  1 
ATOM   817  N  N   . GLY A 1 102 ? 13.387 9.168   27.468 1.00 16.54  ? 108 GLY A N   1 
ATOM   818  C  CA  . GLY A 1 102 ? 14.582 8.322   27.489 1.00 16.40  ? 108 GLY A CA  1 
ATOM   819  C  C   . GLY A 1 102 ? 14.516 7.135   26.539 1.00 13.78  ? 108 GLY A C   1 
ATOM   820  O  O   . GLY A 1 102 ? 15.569 6.494   26.303 1.00 14.15  ? 108 GLY A O   1 
ATOM   821  N  N   . ASP A 1 103 ? 13.322 6.869   25.973 1.00 12.92  ? 109 ASP A N   1 
ATOM   822  C  CA  . ASP A 1 103 ? 13.170 5.769   24.994 1.00 12.65  ? 109 ASP A CA  1 
ATOM   823  C  C   . ASP A 1 103 ? 13.701 6.189   23.608 1.00 11.13  ? 109 ASP A C   1 
ATOM   824  O  O   . ASP A 1 103 ? 13.893 5.343   22.765 1.00 11.52  ? 109 ASP A O   1 
ATOM   825  C  CB  . ASP A 1 103 ? 11.706 5.308   24.885 1.00 12.50  ? 109 ASP A CB  1 
ATOM   826  C  CG  . ASP A 1 103 ? 11.274 4.580   26.159 1.00 12.05  ? 109 ASP A CG  1 
ATOM   827  O  OD1 . ASP A 1 103 ? 12.106 3.805   26.666 1.00 14.74  ? 109 ASP A OD1 1 
ATOM   828  O  OD2 . ASP A 1 103 ? 10.139 4.773   26.607 1.00 11.30  ? 109 ASP A OD2 1 
ATOM   829  N  N   . CYS A 1 104 ? 13.951 7.464   23.378 1.00 11.98  ? 110 CYS A N   1 
ATOM   830  C  CA  . CYS A 1 104 ? 14.470 7.950   22.092 1.00 11.60  ? 110 CYS A CA  1 
ATOM   831  C  C   . CYS A 1 104 ? 15.740 7.182   21.736 1.00 12.02  ? 110 CYS A C   1 
ATOM   832  O  O   . CYS A 1 104 ? 16.651 6.994   22.584 1.00 12.81  ? 110 CYS A O   1 
ATOM   833  C  CB  . CYS A 1 104 ? 14.707 9.463   22.089 1.00 12.32  ? 110 CYS A CB  1 
ATOM   834  S  SG  . CYS A 1 104 ? 13.180 10.436  22.002 1.00 13.51  ? 110 CYS A SG  1 
ATOM   835  N  N   . GLY A 1 105 ? 15.808 6.732   20.480 1.00 11.48  ? 111 GLY A N   1 
ATOM   836  C  CA  . GLY A 1 105 ? 16.968 6.024   19.935 1.00 10.19  ? 111 GLY A CA  1 
ATOM   837  C  C   . GLY A 1 105 ? 16.769 4.518   19.886 1.00 10.24  ? 111 GLY A C   1 
ATOM   838  O  O   . GLY A 1 105 ? 17.588 3.824   19.244 1.00 11.69  ? 111 GLY A O   1 
ATOM   839  N  N   . GLY A 1 106 ? 15.710 3.984   20.496 1.00 10.98  ? 112 GLY A N   1 
ATOM   840  C  CA  . GLY A 1 106 ? 15.424 2.547   20.339 1.00 10.66  ? 112 GLY A CA  1 
ATOM   841  C  C   . GLY A 1 106 ? 15.084 2.261   18.896 1.00 10.58  ? 112 GLY A C   1 
ATOM   842  O  O   . GLY A 1 106 ? 14.393 3.072   18.244 1.00 10.82  ? 112 GLY A O   1 
ATOM   843  N  N   . ILE A 1 107 ? 15.510 1.103   18.419 1.00 10.32  ? 113 ILE A N   1 
ATOM   844  C  CA  . ILE A 1 107 ? 15.287 0.748   16.997 1.00 10.53  ? 113 ILE A CA  1 
ATOM   845  C  C   . ILE A 1 107 ? 13.898 0.187   16.786 1.00 9.37   ? 113 ILE A C   1 
ATOM   846  O  O   . ILE A 1 107 ? 13.456 -0.709  17.574 1.00 10.75  ? 113 ILE A O   1 
ATOM   847  C  CB  . ILE A 1 107 ? 16.387 -0.229  16.581 1.00 12.44  ? 113 ILE A CB  1 
ATOM   848  C  CG1 . ILE A 1 107 ? 17.694 0.560   16.357 1.00 14.82  ? 113 ILE A CG1 1 
ATOM   849  C  CG2 . ILE A 1 107 ? 15.961 -1.062  15.356 1.00 13.17  ? 113 ILE A CG2 1 
ATOM   850  C  CD1 . ILE A 1 107 ? 18.888 -0.321  16.179 1.00 17.32  ? 113 ILE A CD1 1 
ATOM   851  N  N   . LEU A 1 108 ? 13.291 0.540   15.653 1.00 9.88   ? 114 LEU A N   1 
ATOM   852  C  CA  . LEU A 1 108 ? 12.132 -0.145  15.021 1.00 10.82  ? 114 LEU A CA  1 
ATOM   853  C  C   . LEU A 1 108 ? 12.689 -0.938  13.829 1.00 10.22  ? 114 LEU A C   1 
ATOM   854  O  O   . LEU A 1 108 ? 13.428 -0.364  13.028 1.00 10.70  ? 114 LEU A O   1 
ATOM   855  C  CB  . LEU A 1 108 ? 11.083 0.900   14.612 1.00 11.28  ? 114 LEU A CB  1 
ATOM   856  C  CG  . LEU A 1 108 ? 9.991  0.393   13.674 1.00 11.48  ? 114 LEU A CG  1 
ATOM   857  C  CD1 . LEU A 1 108 ? 9.046  -0.541  14.419 1.00 11.86  ? 114 LEU A CD1 1 
ATOM   858  C  CD2 . LEU A 1 108 ? 9.224  1.594   13.102 1.00 11.41  ? 114 LEU A CD2 1 
ATOM   859  N  N   . ARG A 1 109 ? 12.381 -2.227  13.774 1.00 11.03  ? 115 ARG A N   1 
ATOM   860  C  CA  . ARG A 1 109 ? 12.888 -3.107  12.691 1.00 11.38  ? 115 ARG A CA  1 
ATOM   861  C  C   . ARG A 1 109 ? 11.750 -3.874  12.048 1.00 11.38  ? 115 ARG A C   1 
ATOM   862  O  O   . ARG A 1 109 ? 10.787 -4.242  12.733 1.00 11.46  ? 115 ARG A O   1 
ATOM   863  C  CB  . ARG A 1 109 ? 14.021 -4.012  13.156 1.00 12.44  ? 115 ARG A CB  1 
ATOM   864  C  CG  . ARG A 1 109 ? 13.566 -5.039  14.173 1.00 12.43  ? 115 ARG A CG  1 
ATOM   865  C  CD  . ARG A 1 109 ? 14.679 -5.867  14.773 1.00 14.04  ? 115 ARG A CD  1 
ATOM   866  N  NE  . ARG A 1 109 ? 15.497 -5.092  15.685 1.00 17.58  ? 115 ARG A NE  1 
ATOM   867  C  CZ  . ARG A 1 109 ? 16.824 -4.848  15.545 1.00 19.85  ? 115 ARG A CZ  1 
ATOM   868  N  NH1 . ARG A 1 109 ? 17.479 -5.257  14.479 1.00 23.26  ? 115 ARG A NH1 1 
ATOM   869  N  NH2 . ARG A 1 109 ? 17.484 -4.212  16.495 1.00 22.79  ? 115 ARG A NH2 1 
ATOM   870  N  N   . CYS A 1 110 ? 11.918 -4.160  10.762 1.00 11.52  ? 116 CYS A N   1 
ATOM   871  C  CA  . CYS A 1 110 ? 11.028 -5.078  9.999  1.00 12.15  ? 116 CYS A CA  1 
ATOM   872  C  C   . CYS A 1 110 ? 11.855 -6.237  9.427  1.00 12.18  ? 116 CYS A C   1 
ATOM   873  O  O   . CYS A 1 110 ? 13.070 -6.346  9.682  1.00 13.49  ? 116 CYS A O   1 
ATOM   874  C  CB  . CYS A 1 110 ? 10.294 -4.335  8.881  1.00 12.79  ? 116 CYS A CB  1 
ATOM   875  S  SG  . CYS A 1 110 ? 11.436 -3.734  7.581  1.00 11.70  ? 116 CYS A SG  1 
ATOM   876  N  N   . GLN A 1 111 ? 11.224 -7.035  8.591  1.00 14.15  ? 117 GLN A N   1 
ATOM   877  C  CA  . GLN A 1 111 ? 11.915 -8.171  7.959  1.00 14.33  ? 117 GLN A CA  1 
ATOM   878  C  C   . GLN A 1 111 ? 13.082 -7.702  7.072  1.00 14.82  ? 117 GLN A C   1 
ATOM   879  O  O   . GLN A 1 111 ? 13.970 -8.492  6.825  1.00 17.06  ? 117 GLN A O   1 
ATOM   880  C  CB  . GLN A 1 111 ? 10.919 -8.999  7.149  1.00 16.26  ? 117 GLN A CB  1 
ATOM   881  C  CG  . GLN A 1 111 ? 10.453 -8.341  5.860  1.00 18.39  ? 117 GLN A CG  1 
ATOM   882  C  CD  . GLN A 1 111 ? 9.461  -9.151  5.063  1.00 23.00  ? 117 GLN A CD  1 
ATOM   883  O  OE1 . GLN A 1 111 ? 8.248  -9.110  5.276  1.00 28.19  ? 117 GLN A OE1 1 
ATOM   884  N  NE2 . GLN A 1 111 ? 10.000 -9.883  4.114  1.00 23.95  ? 117 GLN A NE2 1 
ATOM   885  N  N   . HIS A 1 112 ? 13.113 -6.453  6.596  1.00 14.34  ? 118 HIS A N   1 
ATOM   886  C  CA  . HIS A 1 112 ? 14.184 -5.935  5.720  1.00 13.21  ? 118 HIS A CA  1 
ATOM   887  C  C   . HIS A 1 112 ? 15.347 -5.251  6.473  1.00 14.51  ? 118 HIS A C   1 
ATOM   888  O  O   . HIS A 1 112 ? 16.353 -4.879  5.795  1.00 15.33  ? 118 HIS A O   1 
ATOM   889  C  CB  . HIS A 1 112 ? 13.520 -4.938  4.772  1.00 12.88  ? 118 HIS A CB  1 
ATOM   890  C  CG  . HIS A 1 112 ? 12.383 -5.493  3.973  1.00 13.13  ? 118 HIS A CG  1 
ATOM   891  N  ND1 . HIS A 1 112 ? 11.045 -5.246  4.264  1.00 11.99  ? 118 HIS A ND1 1 
ATOM   892  C  CD2 . HIS A 1 112 ? 12.399 -6.354  2.917  1.00 12.79  ? 118 HIS A CD2 1 
ATOM   893  C  CE1 . HIS A 1 112 ? 10.293 -5.923  3.397  1.00 14.39  ? 118 HIS A CE1 1 
ATOM   894  N  NE2 . HIS A 1 112 ? 11.113 -6.596  2.549  1.00 14.14  ? 118 HIS A NE2 1 
ATOM   895  N  N   . GLY A 1 113 ? 15.198 -5.009  7.779  1.00 12.53  ? 119 GLY A N   1 
ATOM   896  C  CA  . GLY A 1 113 ? 16.217 -4.338  8.597  1.00 12.08  ? 119 GLY A CA  1 
ATOM   897  C  C   . GLY A 1 113 ? 15.690 -3.162  9.407  1.00 10.66  ? 119 GLY A C   1 
ATOM   898  O  O   . GLY A 1 113 ? 14.492 -3.153  9.780  1.00 11.66  ? 119 GLY A O   1 
ATOM   899  N  N   . VAL A 1 114 ? 16.537 -2.187  9.660  1.00 10.50  ? 120 VAL A N   1 
ATOM   900  C  CA  . VAL A 1 114 ? 16.186 -1.069  10.561 1.00 10.95  ? 120 VAL A CA  1 
ATOM   901  C  C   . VAL A 1 114 ? 15.311 -0.086  9.775  1.00 10.88  ? 120 VAL A C   1 
ATOM   902  O  O   . VAL A 1 114 ? 15.718 0.421   8.708  1.00 12.03  ? 120 VAL A O   1 
ATOM   903  C  CB  . VAL A 1 114 ? 17.457 -0.404  11.104 1.00 11.76  ? 120 VAL A CB  1 
ATOM   904  C  CG1 . VAL A 1 114 ? 17.110 0.881   11.835 1.00 11.19  ? 120 VAL A CG1 1 
ATOM   905  C  CG2 . VAL A 1 114 ? 18.280 -1.375  11.959 1.00 13.22  ? 120 VAL A CG2 1 
ATOM   906  N  N   . VAL A 1 115 ? 14.131 0.194   10.308 1.00 9.79   ? 121 VAL A N   1 
ATOM   907  C  CA  . VAL A 1 115 ? 13.156 1.191   9.735  1.00 10.69  ? 121 VAL A CA  1 
ATOM   908  C  C   . VAL A 1 115 ? 13.391 2.609   10.257 1.00 10.74  ? 121 VAL A C   1 
ATOM   909  O  O   . VAL A 1 115 ? 13.245 3.605   9.491  1.00 11.64  ? 121 VAL A O   1 
ATOM   910  C  CB  . VAL A 1 115 ? 11.748 0.709   10.085 1.00 11.55  ? 121 VAL A CB  1 
ATOM   911  C  CG1 . VAL A 1 115 ? 10.652 1.673   9.607  1.00 12.39  ? 121 VAL A CG1 1 
ATOM   912  C  CG2 . VAL A 1 115 ? 11.483 -0.686  9.547  1.00 13.57  ? 121 VAL A CG2 1 
ATOM   913  N  N   . GLY A 1 116 ? 13.722 2.741   11.519 1.00 10.15  ? 122 GLY A N   1 
ATOM   914  C  CA  . GLY A 1 116 ? 13.841 4.069   12.143 1.00 11.24  ? 122 GLY A CA  1 
ATOM   915  C  C   . GLY A 1 116 ? 14.199 3.994   13.611 1.00 10.53  ? 122 GLY A C   1 
ATOM   916  O  O   . GLY A 1 116 ? 14.442 2.875   14.110 1.00 11.63  ? 122 GLY A O   1 
ATOM   917  N  N   . ILE A 1 117 ? 14.135 5.127   14.320 1.00 10.66  ? 123 ILE A N   1 
ATOM   918  C  CA  . ILE A 1 117 ? 14.440 5.167   15.785 1.00 11.17  ? 123 ILE A CA  1 
ATOM   919  C  C   . ILE A 1 117 ? 13.311 5.923   16.501 1.00 10.91  ? 123 ILE A C   1 
ATOM   920  O  O   . ILE A 1 117 ? 12.702 6.850   15.930 1.00 10.21  ? 123 ILE A O   1 
ATOM   921  C  CB  . ILE A 1 117 ? 15.818 5.763   16.135 1.00 10.56  ? 123 ILE A CB  1 
ATOM   922  C  CG1 . ILE A 1 117 ? 16.034 7.131   15.474 1.00 12.04  ? 123 ILE A CG1 1 
ATOM   923  C  CG2 . ILE A 1 117 ? 16.936 4.770   15.800 1.00 10.99  ? 123 ILE A CG2 1 
ATOM   924  C  CD1 . ILE A 1 117 ? 17.310 7.798   15.881 1.00 12.47  ? 123 ILE A CD1 1 
ATOM   925  N  N   . VAL A 1 118 ? 13.069 5.543   17.748 1.00 10.21  ? 124 VAL A N   1 
ATOM   926  C  CA  . VAL A 1 118 ? 12.071 6.257   18.573 1.00 9.52   ? 124 VAL A CA  1 
ATOM   927  C  C   . VAL A 1 118 ? 12.436 7.737   18.649 1.00 10.42  ? 124 VAL A C   1 
ATOM   928  O  O   . VAL A 1 118 ? 13.628 8.082   18.903 1.00 8.81   ? 124 VAL A O   1 
ATOM   929  C  CB  . VAL A 1 118 ? 11.953 5.647   19.979 1.00 9.31   ? 124 VAL A CB  1 
ATOM   930  C  CG1 . VAL A 1 118 ? 11.075 6.521   20.888 1.00 9.14   ? 124 VAL A CG1 1 
ATOM   931  C  CG2 . VAL A 1 118 ? 11.460 4.214   19.986 1.00 9.44   ? 124 VAL A CG2 1 
ATOM   932  N  N   . SER A 1 119 ? 11.466 8.610   18.424 1.00 10.09  ? 125 SER A N   1 
ATOM   933  C  CA  . SER A 1 119 ? 11.679 10.072  18.472 1.00 10.25  ? 125 SER A CA  1 
ATOM   934  C  C   . SER A 1 119 ? 10.576 10.805  19.250 1.00 10.84  ? 125 SER A C   1 
ATOM   935  O  O   . SER A 1 119 ? 10.850 11.922  19.729 1.00 12.00  ? 125 SER A O   1 
ATOM   936  C  CB  . SER A 1 119 ? 11.725 10.587  17.037 1.00 10.10  ? 125 SER A CB  1 
ATOM   937  O  OG  . SER A 1 119 ? 11.945 12.001  17.014 1.00 12.05  ? 125 SER A OG  1 
ATOM   938  N  N   . THR A 1 120 ? 9.367  10.257  19.366 1.00 10.62  ? 126 THR A N   1 
ATOM   939  C  CA  . THR A 1 120 ? 8.267  10.942  20.111 1.00 11.31  ? 126 THR A CA  1 
ATOM   940  C  C   . THR A 1 120 ? 7.523  9.974   21.025 1.00 10.97  ? 126 THR A C   1 
ATOM   941  O  O   . THR A 1 120 ? 7.638  8.741   20.831 1.00 10.80  ? 126 THR A O   1 
ATOM   942  C  CB  . THR A 1 120 ? 7.264  11.674  19.187 1.00 12.41  ? 126 THR A CB  1 
ATOM   943  O  OG1 . THR A 1 120 ? 6.363  10.716  18.600 1.00 12.24  ? 126 THR A OG1 1 
ATOM   944  C  CG2 . THR A 1 120 ? 7.963  12.495  18.124 1.00 11.88  ? 126 THR A CG2 1 
ATOM   945  N  N   . GLY A 1 121 ? 6.756  10.513  21.955 1.00 12.29  ? 127 GLY A N   1 
ATOM   946  C  CA  . GLY A 1 121 ? 5.883  9.710   22.813 1.00 12.78  ? 127 GLY A CA  1 
ATOM   947  C  C   . GLY A 1 121 ? 4.788  10.545  23.429 1.00 14.40  ? 127 GLY A C   1 
ATOM   948  O  O   . GLY A 1 121 ? 4.554  11.660  22.959 1.00 15.22  ? 127 GLY A O   1 
ATOM   949  N  N   . GLY A 1 122 ? 4.134  9.990   24.436 1.00 14.80  ? 128 GLY A N   1 
ATOM   950  C  CA  . GLY A 1 122 ? 2.980  10.587  25.133 1.00 15.14  ? 128 GLY A CA  1 
ATOM   951  C  C   . GLY A 1 122 ? 1.645  10.159  24.574 1.00 15.63  ? 128 GLY A C   1 
ATOM   952  O  O   . GLY A 1 122 ? 1.520  9.726   23.372 1.00 14.72  ? 128 GLY A O   1 
ATOM   953  N  N   . ASN A 1 123 ? 0.620  10.249  25.417 1.00 15.96  ? 129 ASN A N   1 
ATOM   954  C  CA  . ASN A 1 123 ? -0.789 9.960   25.027 1.00 16.78  ? 129 ASN A CA  1 
ATOM   955  C  C   . ASN A 1 123 ? -0.905 8.580   24.361 1.00 15.04  ? 129 ASN A C   1 
ATOM   956  O  O   . ASN A 1 123 ? -1.727 8.415   23.412 1.00 16.14  ? 129 ASN A O   1 
ATOM   957  C  CB  . ASN A 1 123 ? -1.413 10.988  24.084 1.00 18.09  ? 129 ASN A CB  1 
ATOM   958  C  CG  . ASN A 1 123 ? -1.784 12.286  24.766 1.00 23.50  ? 129 ASN A CG  1 
ATOM   959  O  OD1 . ASN A 1 123 ? -2.264 12.295  25.899 1.00 26.98  ? 129 ASN A OD1 1 
ATOM   960  N  ND2 . ASN A 1 123 ? -1.604 13.391  24.056 1.00 25.93  ? 129 ASN A ND2 1 
ATOM   961  N  N   . GLY A 1 124 ? -0.158 7.594   24.840 1.00 14.14  ? 130 GLY A N   1 
ATOM   962  C  CA  . GLY A 1 124 ? -0.309 6.209   24.402 1.00 12.44  ? 130 GLY A CA  1 
ATOM   963  C  C   . GLY A 1 124 ? 0.232  5.898   23.010 1.00 11.51  ? 130 GLY A C   1 
ATOM   964  O  O   . GLY A 1 124 ? -0.045 4.816   22.550 1.00 12.04  ? 130 GLY A O   1 
ATOM   965  N  N   . LEU A 1 125 ? 0.959  6.817   22.361 1.00 11.59  ? 131 LEU A N   1 
ATOM   966  C  CA  . LEU A 1 125 ? 1.624  6.581   21.077 1.00 11.67  ? 131 LEU A CA  1 
ATOM   967  C  C   . LEU A 1 125 ? 3.140  6.571   21.250 1.00 11.19  ? 131 LEU A C   1 
ATOM   968  O  O   . LEU A 1 125 ? 3.694  7.230   22.170 1.00 12.75  ? 131 LEU A O   1 
ATOM   969  C  CB  . LEU A 1 125 ? 1.227  7.623   20.027 1.00 12.98  ? 131 LEU A CB  1 
ATOM   970  C  CG  . LEU A 1 125 ? -0.271 7.824   19.787 1.00 13.29  ? 131 LEU A CG  1 
ATOM   971  C  CD1 . LEU A 1 125 ? -0.486 8.704   18.551 1.00 14.93  ? 131 LEU A CD1 1 
ATOM   972  C  CD2 . LEU A 1 125 ? -0.959 6.474   19.598 1.00 13.80  ? 131 LEU A CD2 1 
ATOM   973  N  N   . VAL A 1 126 ? 3.787  5.878   20.313 1.00 10.58  ? 132 VAL A N   1 
ATOM   974  C  CA  . VAL A 1 126 ? 5.253  5.997   20.096 1.00 11.50  ? 132 VAL A CA  1 
ATOM   975  C  C   . VAL A 1 126 ? 5.468  6.429   18.649 1.00 11.22  ? 132 VAL A C   1 
ATOM   976  O  O   . VAL A 1 126 ? 4.796  5.903   17.760 1.00 11.98  ? 132 VAL A O   1 
ATOM   977  C  CB  . VAL A 1 126 ? 5.952  4.671   20.438 1.00 11.68  ? 132 VAL A CB  1 
ATOM   978  C  CG1 . VAL A 1 126 ? 5.368  3.449   19.770 1.00 13.85  ? 132 VAL A CG1 1 
ATOM   979  C  CG2 . VAL A 1 126 ? 7.447  4.793   20.169 1.00 11.52  ? 132 VAL A CG2 1 
ATOM   980  N  N   . GLY A 1 127 ? 6.301  7.448   18.449 1.00 10.95  ? 133 GLY A N   1 
ATOM   981  C  CA  . GLY A 1 127 ? 6.654  8.015   17.153 1.00 10.57  ? 133 GLY A CA  1 
ATOM   982  C  C   . GLY A 1 127 ? 8.081  7.663   16.776 1.00 10.29  ? 133 GLY A C   1 
ATOM   983  O  O   . GLY A 1 127 ? 8.932  7.734   17.648 1.00 11.35  ? 133 GLY A O   1 
ATOM   984  N  N   . PHE A 1 128 ? 8.308  7.272   15.528 1.00 10.36  ? 134 PHE A N   1 
ATOM   985  C  CA  . PHE A 1 128 ? 9.609  6.842   14.970 1.00 9.94   ? 134 PHE A CA  1 
ATOM   986  C  C   . PHE A 1 128 ? 10.012 7.764   13.829 1.00 10.69  ? 134 PHE A C   1 
ATOM   987  O  O   . PHE A 1 128 ? 9.204  8.037   12.927 1.00 11.54  ? 134 PHE A O   1 
ATOM   988  C  CB  . PHE A 1 128 ? 9.537  5.394   14.495 1.00 9.95   ? 134 PHE A CB  1 
ATOM   989  C  CG  . PHE A 1 128 ? 8.909  4.420   15.459 1.00 10.23  ? 134 PHE A CG  1 
ATOM   990  C  CD1 . PHE A 1 128 ? 9.718  3.819   16.419 1.00 10.49  ? 134 PHE A CD1 1 
ATOM   991  C  CD2 . PHE A 1 128 ? 7.550  4.087   15.396 1.00 10.68  ? 134 PHE A CD2 1 
ATOM   992  C  CE1 . PHE A 1 128 ? 9.176  2.889   17.301 1.00 10.00  ? 134 PHE A CE1 1 
ATOM   993  C  CE2 . PHE A 1 128 ? 7.025  3.130   16.272 1.00 10.44  ? 134 PHE A CE2 1 
ATOM   994  C  CZ  . PHE A 1 128 ? 7.843  2.564   17.235 1.00 10.09  ? 134 PHE A CZ  1 
ATOM   995  N  N   . ALA A 1 129 ? 11.265 8.183   13.878 1.00 10.68  ? 135 ALA A N   1 
ATOM   996  C  CA  . ALA A 1 129 ? 11.890 8.959   12.788 1.00 10.23  ? 135 ALA A CA  1 
ATOM   997  C  C   . ALA A 1 129 ? 12.328 7.957   11.707 1.00 10.08  ? 135 ALA A C   1 
ATOM   998  O  O   . ALA A 1 129 ? 13.181 7.110   11.993 1.00 11.32  ? 135 ALA A O   1 
ATOM   999  C  CB  . ALA A 1 129 ? 13.021 9.762   13.362 1.00 10.40  ? 135 ALA A CB  1 
ATOM   1000 N  N   . ASP A 1 130 ? 11.695 7.983   10.525 1.00 9.20   ? 136 ASP A N   1 
ATOM   1001 C  CA  . ASP A 1 130 ? 12.061 7.059   9.439  1.00 9.49   ? 136 ASP A CA  1 
ATOM   1002 C  C   . ASP A 1 130 ? 13.482 7.327   8.960  1.00 10.11  ? 136 ASP A C   1 
ATOM   1003 O  O   . ASP A 1 130 ? 13.877 8.498   8.838  1.00 11.52  ? 136 ASP A O   1 
ATOM   1004 C  CB  . ASP A 1 130 ? 11.090 7.207   8.267  1.00 10.18  ? 136 ASP A CB  1 
ATOM   1005 C  CG  . ASP A 1 130 ? 11.300 6.245   7.101  1.00 10.93  ? 136 ASP A CG  1 
ATOM   1006 O  OD1 . ASP A 1 130 ? 11.291 5.012   7.320  1.00 11.85  ? 136 ASP A OD1 1 
ATOM   1007 O  OD2 . ASP A 1 130 ? 11.475 6.768   5.947  1.00 14.24  ? 136 ASP A OD2 1 
ATOM   1008 N  N   . VAL A 1 131 ? 14.160 6.292   8.486  1.00 10.32  ? 137 VAL A N   1 
ATOM   1009 C  CA  . VAL A 1 131 ? 15.475 6.430   7.776  1.00 11.28  ? 137 VAL A CA  1 
ATOM   1010 C  C   . VAL A 1 131 ? 15.445 5.696   6.407  1.00 11.02  ? 137 VAL A C   1 
ATOM   1011 O  O   . VAL A 1 131 ? 16.493 5.672   5.759  1.00 12.08  ? 137 VAL A O   1 
ATOM   1012 C  CB  . VAL A 1 131 ? 16.648 5.938   8.654  1.00 11.66  ? 137 VAL A CB  1 
ATOM   1013 C  CG1 . VAL A 1 131 ? 16.740 6.790   9.915  1.00 11.40  ? 137 VAL A CG1 1 
ATOM   1014 C  CG2 . VAL A 1 131 ? 16.553 4.481   8.976  1.00 10.87  ? 137 VAL A CG2 1 
ATOM   1015 N  N   . ARG A 1 132 ? 14.340 5.053   6.010  1.00 11.40  ? 138 ARG A N   1 
ATOM   1016 C  CA  . ARG A 1 132 ? 14.374 4.166   4.812  1.00 10.40  ? 138 ARG A CA  1 
ATOM   1017 C  C   . ARG A 1 132 ? 14.515 4.983   3.524  1.00 10.52  ? 138 ARG A C   1 
ATOM   1018 O  O   . ARG A 1 132 ? 14.852 4.363   2.507  1.00 12.22  ? 138 ARG A O   1 
ATOM   1019 C  CB  . ARG A 1 132 ? 13.105 3.318   4.763  1.00 9.77   ? 138 ARG A CB  1 
ATOM   1020 C  CG  . ARG A 1 132 ? 12.956 2.366   5.939  1.00 10.16  ? 138 ARG A CG  1 
ATOM   1021 C  CD  . ARG A 1 132 ? 11.606 1.677   5.895  1.00 10.15  ? 138 ARG A CD  1 
ATOM   1022 N  NE  . ARG A 1 132 ? 10.530 2.597   6.162  1.00 10.16  ? 138 ARG A NE  1 
ATOM   1023 C  CZ  . ARG A 1 132 ? 9.262  2.243   6.263  1.00 10.28  ? 138 ARG A CZ  1 
ATOM   1024 N  NH1 . ARG A 1 132 ? 8.899  1.006   5.901  1.00 10.64  ? 138 ARG A NH1 1 
ATOM   1025 N  NH2 . ARG A 1 132 ? 8.400  3.134   6.727  1.00 10.80  ? 138 ARG A NH2 1 
ATOM   1026 N  N   . ASP A 1 133 ? 14.205 6.264   3.562  1.00 10.86  ? 139 ASP A N   1 
ATOM   1027 C  CA  . ASP A 1 133 ? 14.390 7.151   2.390  1.00 12.50  ? 139 ASP A CA  1 
ATOM   1028 C  C   . ASP A 1 133 ? 15.863 7.575   2.230  1.00 13.25  ? 139 ASP A C   1 
ATOM   1029 O  O   . ASP A 1 133 ? 16.177 8.170   1.148  1.00 15.03  ? 139 ASP A O   1 
ATOM   1030 C  CB  . ASP A 1 133 ? 13.485 8.369   2.468  1.00 13.20  ? 139 ASP A CB  1 
ATOM   1031 C  CG  . ASP A 1 133 ? 13.767 9.331   3.599  1.00 15.21  ? 139 ASP A CG  1 
ATOM   1032 O  OD1 . ASP A 1 133 ? 14.050 8.838   4.717  1.00 14.00  ? 139 ASP A OD1 1 
ATOM   1033 O  OD2 . ASP A 1 133 ? 13.627 10.564  3.375  1.00 17.75  ? 139 ASP A OD2 1 
ATOM   1034 N  N   . LEU A 1 134 ? 16.706 7.363   3.230  1.00 12.97  ? 140 LEU A N   1 
ATOM   1035 C  CA  . LEU A 1 134 ? 18.071 7.917   3.199  1.00 12.98  ? 140 LEU A CA  1 
ATOM   1036 C  C   . LEU A 1 134 ? 18.988 6.897   2.497  1.00 13.17  ? 140 LEU A C   1 
ATOM   1037 O  O   . LEU A 1 134 ? 19.771 6.184   3.154  1.00 14.86  ? 140 LEU A O   1 
ATOM   1038 C  CB  . LEU A 1 134 ? 18.519 8.269   4.623  1.00 12.49  ? 140 LEU A CB  1 
ATOM   1039 C  CG  . LEU A 1 134 ? 17.658 9.270   5.404  1.00 14.00  ? 140 LEU A CG  1 
ATOM   1040 C  CD1 . LEU A 1 134 ? 18.209 9.466   6.832  1.00 13.38  ? 140 LEU A CD1 1 
ATOM   1041 C  CD2 . LEU A 1 134 ? 17.567 10.613  4.718  1.00 14.93  ? 140 LEU A CD2 1 
ATOM   1042 N  N   . LEU A 1 135 ? 18.865 6.779   1.163  1.00 13.33  ? 141 LEU A N   1 
ATOM   1043 C  CA  . LEU A 1 135 ? 19.568 5.684   0.442  1.00 14.85  ? 141 LEU A CA  1 
ATOM   1044 C  C   . LEU A 1 135 ? 21.085 5.824   0.516  1.00 15.09  ? 141 LEU A C   1 
ATOM   1045 O  O   . LEU A 1 135 ? 21.747 4.821   0.377  1.00 17.46  ? 141 LEU A O   1 
ATOM   1046 C  CB  . LEU A 1 135 ? 19.113 5.633   -1.026 1.00 16.42  ? 141 LEU A CB  1 
ATOM   1047 C  CG  . LEU A 1 135 ? 17.614 5.626   -1.299 1.00 17.54  ? 141 LEU A CG  1 
ATOM   1048 C  CD1 . LEU A 1 135 ? 17.395 5.389   -2.794 1.00 19.54  ? 141 LEU A CD1 1 
ATOM   1049 C  CD2 . LEU A 1 135 ? 16.817 4.584   -0.517 1.00 16.85  ? 141 LEU A CD2 1 
ATOM   1050 N  N   . TRP A 1 136 ? 21.589 7.053   0.701  1.00 15.73  ? 142 TRP A N   1 
ATOM   1051 C  CA  . TRP A 1 136 ? 23.042 7.343   0.766  1.00 15.80  ? 142 TRP A CA  1 
ATOM   1052 C  C   . TRP A 1 136 ? 23.694 6.686   1.980  1.00 16.04  ? 142 TRP A C   1 
ATOM   1053 O  O   . TRP A 1 136 ? 24.941 6.509   1.974  1.00 17.03  ? 142 TRP A O   1 
ATOM   1054 C  CB  . TRP A 1 136 ? 23.286 8.847   0.696  1.00 13.78  ? 142 TRP A CB  1 
ATOM   1055 C  CG  . TRP A 1 136 ? 22.571 9.668   1.720  1.00 14.42  ? 142 TRP A CG  1 
ATOM   1056 C  CD1 . TRP A 1 136 ? 21.390 10.331  1.567  1.00 16.50  ? 142 TRP A CD1 1 
ATOM   1057 C  CD2 . TRP A 1 136 ? 22.981 9.815   3.090  1.00 13.99  ? 142 TRP A CD2 1 
ATOM   1058 N  NE1 . TRP A 1 136 ? 21.066 10.968  2.738  1.00 15.99  ? 142 TRP A NE1 1 
ATOM   1059 C  CE2 . TRP A 1 136 ? 22.011 10.674  3.675  1.00 14.70  ? 142 TRP A CE2 1 
ATOM   1060 C  CE3 . TRP A 1 136 ? 24.132 9.444   3.807  1.00 15.38  ? 142 TRP A CE3 1 
ATOM   1061 C  CZ2 . TRP A 1 136 ? 22.152 11.102  4.995  1.00 15.08  ? 142 TRP A CZ2 1 
ATOM   1062 C  CZ3 . TRP A 1 136 ? 24.245 9.853   5.122  1.00 15.88  ? 142 TRP A CZ3 1 
ATOM   1063 C  CH2 . TRP A 1 136 ? 23.265 10.673  5.685  1.00 14.67  ? 142 TRP A CH2 1 
ATOM   1064 N  N   . LEU A 1 137 ? 22.928 6.233   2.966  1.00 16.60  ? 143 LEU A N   1 
ATOM   1065 C  CA  . LEU A 1 137 ? 23.486 5.540   4.157  1.00 16.82  ? 143 LEU A CA  1 
ATOM   1066 C  C   . LEU A 1 137 ? 24.130 4.198   3.742  1.00 20.47  ? 143 LEU A C   1 
ATOM   1067 O  O   . LEU A 1 137 ? 24.956 3.678   4.511  1.00 20.38  ? 143 LEU A O   1 
ATOM   1068 C  CB  . LEU A 1 137 ? 22.383 5.271   5.178  1.00 15.35  ? 143 LEU A CB  1 
ATOM   1069 C  CG  . LEU A 1 137 ? 21.904 6.450   6.026  1.00 13.41  ? 143 LEU A CG  1 
ATOM   1070 C  CD1 . LEU A 1 137 ? 20.695 6.002   6.853  1.00 15.15  ? 143 LEU A CD1 1 
ATOM   1071 C  CD2 . LEU A 1 137 ? 23.010 6.938   6.950  1.00 14.76  ? 143 LEU A CD2 1 
ATOM   1072 N  N   . ASP A 1 138 ? 23.725 3.635   2.598  1.00 20.26  ? 144 ASP A N   1 
ATOM   1073 C  CA  . ASP A 1 138 ? 24.148 2.272   2.169  1.00 23.27  ? 144 ASP A CA  1 
ATOM   1074 C  C   . ASP A 1 138 ? 25.483 2.276   1.426  1.00 27.02  ? 144 ASP A C   1 
ATOM   1075 O  O   . ASP A 1 138 ? 25.978 1.151   1.162  1.00 26.18  ? 144 ASP A O   1 
ATOM   1076 C  CB  . ASP A 1 138 ? 23.109 1.617   1.255  1.00 24.38  ? 144 ASP A CB  1 
ATOM   1077 C  CG  . ASP A 1 138 ? 21.769 1.302   1.901  1.00 21.29  ? 144 ASP A CG  1 
ATOM   1078 O  OD1 . ASP A 1 138 ? 21.673 1.399   3.126  1.00 25.32  ? 144 ASP A OD1 1 
ATOM   1079 O  OD2 . ASP A 1 138 ? 20.785 1.064   1.146  1.00 25.06  ? 144 ASP A OD2 1 
ATOM   1080 N  N   . GLU A 1 139 ? 26.042 3.451   1.129  1.00 32.67  ? 145 GLU A N   1 
ATOM   1081 C  CA  . GLU A 1 139 ? 27.272 3.611   0.297  1.00 40.54  ? 145 GLU A CA  1 
ATOM   1082 C  C   . GLU A 1 139 ? 28.231 4.653   0.903  1.00 41.64  ? 145 GLU A C   1 
ATOM   1083 O  O   . GLU A 1 139 ? 27.854 5.320   1.898  1.00 34.67  ? 145 GLU A O   1 
ATOM   1084 C  CB  . GLU A 1 139 ? 26.857 4.028   -1.113 1.00 46.34  ? 145 GLU A CB  1 
ATOM   1085 C  CG  . GLU A 1 139 ? 26.206 5.409   -1.171 1.00 51.44  ? 145 GLU A CG  1 
ATOM   1086 C  CD  . GLU A 1 139 ? 25.194 5.628   -2.286 1.00 58.85  ? 145 GLU A CD  1 
ATOM   1087 O  OE1 . GLU A 1 139 ? 24.654 6.759   -2.384 1.00 62.29  ? 145 GLU A OE1 1 
ATOM   1088 O  OE2 . GLU A 1 139 ? 24.950 4.682   -3.060 1.00 66.67  ? 145 GLU A OE2 1 
ATOM   1089 N  N   . GLU A 1 140 ? 29.435 4.757   0.327  1.00 51.13  ? 146 GLU A N   1 
ATOM   1090 C  CA  . GLU A 1 140 ? 30.305 5.970   0.333  1.00 56.93  ? 146 GLU A CA  1 
ATOM   1091 C  C   . GLU A 1 140 ? 30.354 6.570   1.740  1.00 65.40  ? 146 GLU A C   1 
ATOM   1092 O  O   . GLU A 1 140 ? 31.205 7.406   2.045  1.00 74.00  ? 146 GLU A O   1 
ATOM   1093 C  CB  . GLU A 1 140 ? 29.795 6.949   -0.730 1.00 56.37  ? 146 GLU A CB  1 
ATOM   1094 C  CG  . GLU A 1 140 ? 29.704 8.408   -0.292 1.00 61.78  ? 146 GLU A CG  1 
ATOM   1095 C  CD  . GLU A 1 140 ? 31.011 9.187   -0.230 1.00 64.54  ? 146 GLU A CD  1 
ATOM   1096 O  OE1 . GLU A 1 140 ? 31.075 10.164  0.548  1.00 61.53  ? 146 GLU A OE1 1 
ATOM   1097 O  OE2 . GLU A 1 140 ? 31.964 8.824   -0.956 1.00 62.80  ? 146 GLU A OE2 1 
HETATM 1098 ZN ZN  . ZN  B 2 .   ? 10.347 -3.870  5.558  1.00 12.16  ? 201 ZN  A ZN  1 
HETATM 1099 S  S   . DMS C 3 .   ? 18.633 -7.360  8.472  1.00 29.97  ? 202 DMS A S   1 
HETATM 1100 O  O   . DMS C 3 .   ? 19.815 -8.338  8.561  1.00 42.44  ? 202 DMS A O   1 
HETATM 1101 C  C1  . DMS C 3 .   ? 17.161 -8.397  8.388  1.00 27.68  ? 202 DMS A C1  1 
HETATM 1102 C  C2  . DMS C 3 .   ? 18.481 -6.776  10.117 1.00 28.83  ? 202 DMS A C2  1 
HETATM 1103 S  S   . DMS D 3 .   ? 15.532 21.225  8.614  1.00 33.95  ? 203 DMS A S   1 
HETATM 1104 O  O   . DMS D 3 .   ? 14.718 21.359  9.882  1.00 28.84  ? 203 DMS A O   1 
HETATM 1105 C  C1  . DMS D 3 .   ? 14.317 21.109  7.310  1.00 35.53  ? 203 DMS A C1  1 
HETATM 1106 C  C2  . DMS D 3 .   ? 16.153 22.858  8.250  1.00 32.53  ? 203 DMS A C2  1 
HETATM 1107 S  S   . DMS E 3 .   ? 19.315 -3.069  24.012 1.00 62.60  ? 204 DMS A S   1 
HETATM 1108 O  O   . DMS E 3 .   ? 19.175 -4.082  25.106 1.00 58.92  ? 204 DMS A O   1 
HETATM 1109 C  C1  . DMS E 3 .   ? 20.575 -3.711  22.928 1.00 64.11  ? 204 DMS A C1  1 
HETATM 1110 C  C2  . DMS E 3 .   ? 17.942 -3.333  22.931 1.00 55.65  ? 204 DMS A C2  1 
HETATM 1111 S  S   . DMS F 3 .   ? -0.590 -1.116  23.270 1.00 41.19  ? 205 DMS A S   1 
HETATM 1112 O  O   . DMS F 3 .   ? -0.242 0.034   24.155 1.00 36.59  ? 205 DMS A O   1 
HETATM 1113 C  C1  . DMS F 3 .   ? 0.455  -2.458  23.786 1.00 38.77  ? 205 DMS A C1  1 
HETATM 1114 C  C2  . DMS F 3 .   ? -2.145 -1.770  23.852 1.00 40.75  ? 205 DMS A C2  1 
HETATM 1115 S  S   . DMS G 3 .   ? 13.147 21.982  24.987 1.00 29.45  ? 206 DMS A S   1 
HETATM 1116 O  O   . DMS G 3 .   ? 14.104 22.836  24.178 1.00 36.97  ? 206 DMS A O   1 
HETATM 1117 C  C1  . DMS G 3 .   ? 13.017 22.859  26.523 1.00 33.69  ? 206 DMS A C1  1 
HETATM 1118 C  C2  . DMS G 3 .   ? 11.542 22.376  24.388 1.00 29.64  ? 206 DMS A C2  1 
HETATM 1119 S  S   . SO4 H 4 .   ? -0.950 23.547  14.632 1.00 146.53 ? 207 SO4 A S   1 
HETATM 1120 O  O1  . SO4 H 4 .   ? -1.361 23.715  13.261 1.00 131.37 ? 207 SO4 A O1  1 
HETATM 1121 O  O2  . SO4 H 4 .   ? -1.731 24.408  15.476 1.00 69.81  ? 207 SO4 A O2  1 
HETATM 1122 O  O3  . SO4 H 4 .   ? -1.150 22.180  15.032 1.00 162.53 ? 207 SO4 A O3  1 
HETATM 1123 O  O4  . SO4 H 4 .   ? 0.442  23.885  14.770 1.00 150.18 ? 207 SO4 A O4  1 
HETATM 1124 N  N1  . ZUG I 5 .   ? 7.834  13.859  3.463  0.62 34.25  ? 208 ZUG A N1  1 
HETATM 1125 C  C4  . ZUG I 5 .   ? 4.846  14.741  3.916  0.62 35.27  ? 208 ZUG A C4  1 
HETATM 1126 C  C5  . ZUG I 5 .   ? 3.580  14.827  3.362  0.62 37.09  ? 208 ZUG A C5  1 
HETATM 1127 C  C6  . ZUG I 5 .   ? 2.901  13.657  3.076  0.62 38.16  ? 208 ZUG A C6  1 
HETATM 1128 C  C7  . ZUG I 5 .   ? 4.640  12.367  3.817  0.62 36.45  ? 208 ZUG A C7  1 
HETATM 1129 C  C1  . ZUG I 5 .   ? 8.500  12.861  2.618  0.62 35.57  ? 208 ZUG A C1  1 
HETATM 1130 C  C2  . ZUG I 5 .   ? 8.471  15.181  3.532  0.62 33.89  ? 208 ZUG A C2  1 
HETATM 1131 S  S1  . ZUG I 5 .   ? 7.024  13.331  4.776  0.62 32.31  ? 208 ZUG A S1  1 
HETATM 1132 O  O1  . ZUG I 5 .   ? 7.197  14.268  5.841  0.62 30.35  ? 208 ZUG A O1  1 
HETATM 1133 O  O2  . ZUG I 5 .   ? 7.316  11.947  4.977  0.62 32.64  ? 208 ZUG A O2  1 
HETATM 1134 C  C3  . ZUG I 5 .   ? 5.385  13.487  4.143  0.62 34.07  ? 208 ZUG A C3  1 
HETATM 1135 N  N2  . ZUG I 5 .   ? 3.407  12.438  3.298  0.62 38.59  ? 208 ZUG A N2  1 
HETATM 1136 O  O   . HOH J 6 .   ? 11.546 7.397   31.345 1.00 37.55  ? 301 HOH A O   1 
HETATM 1137 O  O   . HOH J 6 .   ? -2.168 22.273  10.911 1.00 31.89  ? 302 HOH A O   1 
HETATM 1138 O  O   . HOH J 6 .   ? 32.963 -4.527  7.285  1.00 46.49  ? 303 HOH A O   1 
HETATM 1139 O  O   . HOH J 6 .   ? 16.716 -4.175  28.027 1.00 39.29  ? 304 HOH A O   1 
HETATM 1140 O  O   . HOH J 6 .   ? 37.602 4.208   9.505  1.00 44.94  ? 305 HOH A O   1 
HETATM 1141 O  O   . HOH J 6 .   ? 3.105  13.127  21.686 1.00 9.92   ? 306 HOH A O   1 
HETATM 1142 O  O   . HOH J 6 .   ? 12.437 20.393  29.411 1.00 41.87  ? 307 HOH A O   1 
HETATM 1143 O  O   . HOH J 6 .   ? 17.794 -0.619  27.925 1.00 21.18  ? 308 HOH A O   1 
HETATM 1144 O  O   . HOH J 6 .   ? 25.583 3.543   20.810 1.00 31.41  ? 309 HOH A O   1 
HETATM 1145 O  O   . HOH J 6 .   ? 30.385 10.512  17.915 1.00 26.91  ? 310 HOH A O   1 
HETATM 1146 O  O   . HOH J 6 .   ? 9.390  21.685  12.654 1.00 48.77  ? 311 HOH A O   1 
HETATM 1147 O  O   . HOH J 6 .   ? 2.534  9.089   10.165 1.00 16.07  ? 312 HOH A O   1 
HETATM 1148 O  O   . HOH J 6 .   ? 6.087  3.665   3.581  1.00 19.73  ? 313 HOH A O   1 
HETATM 1149 O  O   . HOH J 6 .   ? 25.732 -2.768  14.649 1.00 20.99  ? 314 HOH A O   1 
HETATM 1150 O  O   . HOH J 6 .   ? 15.985 21.858  16.679 1.00 29.37  ? 315 HOH A O   1 
HETATM 1151 O  O   . HOH J 6 .   ? 12.637 -7.215  30.451 1.00 34.86  ? 316 HOH A O   1 
HETATM 1152 O  O   . HOH J 6 .   ? 17.586 -6.354  4.007  1.00 24.70  ? 317 HOH A O   1 
HETATM 1153 O  O   . HOH J 6 .   ? 22.403 17.073  22.194 1.00 32.63  ? 318 HOH A O   1 
HETATM 1154 O  O   . HOH J 6 .   ? 23.856 11.528  23.818 1.00 28.72  ? 319 HOH A O   1 
HETATM 1155 O  O   . HOH J 6 .   ? 26.353 -1.930  8.317  1.00 20.76  ? 320 HOH A O   1 
HETATM 1156 O  O   . HOH J 6 .   ? 12.533 17.884  6.405  1.00 42.04  ? 321 HOH A O   1 
HETATM 1157 O  O   . HOH J 6 .   ? 24.274 9.302   -3.056 1.00 44.11  ? 322 HOH A O   1 
HETATM 1158 O  O   . HOH J 6 .   ? 19.634 8.891   19.831 1.00 14.45  ? 323 HOH A O   1 
HETATM 1159 O  O   . HOH J 6 .   ? 28.169 15.503  4.295  1.00 31.88  ? 324 HOH A O   1 
HETATM 1160 O  O   . HOH J 6 .   ? 22.652 -0.049  16.619 1.00 21.47  ? 325 HOH A O   1 
HETATM 1161 O  O   . HOH J 6 .   ? 30.295 1.828   13.902 1.00 19.42  ? 326 HOH A O   1 
HETATM 1162 O  O   . HOH J 6 .   ? 29.592 -3.291  8.265  1.00 29.22  ? 327 HOH A O   1 
HETATM 1163 O  O   . HOH J 6 .   ? 23.246 21.050  7.991  1.00 23.50  ? 328 HOH A O   1 
HETATM 1164 O  O   . HOH J 6 .   ? 29.711 10.756  20.579 1.00 27.33  ? 329 HOH A O   1 
HETATM 1165 O  O   . HOH J 6 .   ? 10.588 9.175   5.080  1.00 19.00  ? 330 HOH A O   1 
HETATM 1166 O  O   . HOH J 6 .   ? 1.955  20.796  23.862 1.00 18.63  ? 331 HOH A O   1 
HETATM 1167 O  O   . HOH J 6 .   ? 7.353  25.252  17.993 1.00 24.73  ? 332 HOH A O   1 
HETATM 1168 O  O   . HOH J 6 .   ? 2.067  4.678   27.540 1.00 35.50  ? 333 HOH A O   1 
HETATM 1169 O  O   . HOH J 6 .   ? 16.337 0.413   30.185 1.00 23.81  ? 334 HOH A O   1 
HETATM 1170 O  O   . HOH J 6 .   ? 30.515 9.344   15.082 1.00 31.27  ? 335 HOH A O   1 
HETATM 1171 O  O   . HOH J 6 .   ? 4.624  -4.654  29.078 1.00 26.76  ? 336 HOH A O   1 
HETATM 1172 O  O   . HOH J 6 .   ? 18.221 21.441  10.722 1.00 20.02  ? 337 HOH A O   1 
HETATM 1173 O  O   . HOH J 6 .   ? 0.997  -5.688  17.854 1.00 41.89  ? 338 HOH A O   1 
HETATM 1174 O  O   . HOH J 6 .   ? 24.016 10.412  21.816 1.00 38.64  ? 339 HOH A O   1 
HETATM 1175 O  O   . HOH J 6 .   ? 0.155  -1.784  19.769 1.00 21.89  ? 340 HOH A O   1 
HETATM 1176 O  O   . HOH J 6 .   ? 25.732 18.336  21.580 1.00 22.24  ? 341 HOH A O   1 
HETATM 1177 O  O   . HOH J 6 .   ? 2.461  -3.850  20.896 1.00 22.41  ? 342 HOH A O   1 
HETATM 1178 O  O   . HOH J 6 .   ? 16.788 2.555   23.778 1.00 17.14  ? 343 HOH A O   1 
HETATM 1179 O  O   . HOH J 6 .   ? -0.166 0.518   16.460 1.00 12.50  ? 344 HOH A O   1 
HETATM 1180 O  O   . HOH J 6 .   ? 2.838  -1.987  3.263  1.00 38.75  ? 345 HOH A O   1 
HETATM 1181 O  O   . HOH J 6 .   ? 22.826 -6.246  9.598  1.00 19.93  ? 346 HOH A O   1 
HETATM 1182 O  O   . HOH J 6 .   ? 27.634 10.643  2.813  1.00 39.59  ? 347 HOH A O   1 
HETATM 1183 O  O   . HOH J 6 .   ? 15.357 12.048  24.735 1.00 19.23  ? 348 HOH A O   1 
HETATM 1184 O  O   . HOH J 6 .   ? 31.729 19.171  11.717 1.00 23.84  ? 349 HOH A O   1 
HETATM 1185 O  O   . HOH J 6 .   ? 22.139 18.522  19.305 1.00 22.06  ? 350 HOH A O   1 
HETATM 1186 O  O   . HOH J 6 .   ? 8.753  3.520   3.014  1.00 16.14  ? 351 HOH A O   1 
HETATM 1187 O  O   . HOH J 6 .   ? 4.590  8.638   27.723 1.00 29.12  ? 352 HOH A O   1 
HETATM 1188 O  O   . HOH J 6 .   ? -0.870 15.432  17.449 1.00 18.50  ? 353 HOH A O   1 
HETATM 1189 O  O   . HOH J 6 .   ? 13.885 2.675   23.648 1.00 11.56  ? 354 HOH A O   1 
HETATM 1190 O  O   . HOH J 6 .   ? 20.940 -1.030  -0.646 1.00 27.14  ? 355 HOH A O   1 
HETATM 1191 O  O   . HOH J 6 .   ? 16.586 19.571  22.991 1.00 20.82  ? 356 HOH A O   1 
HETATM 1192 O  O   . HOH J 6 .   ? 22.158 3.584   24.331 1.00 40.05  ? 357 HOH A O   1 
HETATM 1193 O  O   . HOH J 6 .   ? 14.402 -10.845 8.212  1.00 23.57  ? 358 HOH A O   1 
HETATM 1194 O  O   . HOH J 6 .   ? 1.668  11.143  21.001 1.00 14.98  ? 359 HOH A O   1 
HETATM 1195 O  O   . HOH J 6 .   ? 10.348 5.639   3.685  1.00 13.67  ? 360 HOH A O   1 
HETATM 1196 O  O   . HOH J 6 .   ? 29.646 21.204  19.615 1.00 21.69  ? 361 HOH A O   1 
HETATM 1197 O  O   . HOH J 6 .   ? 21.110 23.175  12.222 1.00 21.47  ? 362 HOH A O   1 
HETATM 1198 O  O   . HOH J 6 .   ? 4.767  14.876  25.186 1.00 24.59  ? 363 HOH A O   1 
HETATM 1199 O  O   . HOH J 6 .   ? 9.118  21.767  25.906 1.00 30.28  ? 364 HOH A O   1 
HETATM 1200 O  O   . HOH J 6 .   ? 2.299  14.504  5.679  1.00 32.40  ? 365 HOH A O   1 
HETATM 1201 O  O   . HOH J 6 .   ? -2.157 16.299  19.741 1.00 17.28  ? 366 HOH A O   1 
HETATM 1202 O  O   . HOH J 6 .   ? 25.097 -1.451  1.664  1.00 40.74  ? 367 HOH A O   1 
HETATM 1203 O  O   . HOH J 6 .   ? 4.792  14.732  22.490 1.00 16.31  ? 368 HOH A O   1 
HETATM 1204 O  O   . HOH J 6 .   ? 3.538  6.630   24.895 1.00 16.70  ? 369 HOH A O   1 
HETATM 1205 O  O   . HOH J 6 .   ? 20.669 -4.983  13.680 1.00 32.10  ? 370 HOH A O   1 
HETATM 1206 O  O   . HOH J 6 .   ? 5.359  1.622   -2.393 1.00 24.66  ? 371 HOH A O   1 
HETATM 1207 O  O   . HOH J 6 .   ? 11.114 12.182  12.167 1.00 15.44  ? 372 HOH A O   1 
HETATM 1208 O  O   . HOH J 6 .   ? 21.860 -7.561  5.777  1.00 30.43  ? 373 HOH A O   1 
HETATM 1209 O  O   . HOH J 6 .   ? 7.913  -3.054  0.552  1.00 16.87  ? 374 HOH A O   1 
HETATM 1210 O  O   . HOH J 6 .   ? 11.501 11.010  1.608  1.00 27.80  ? 375 HOH A O   1 
HETATM 1211 O  O   . HOH J 6 .   ? 8.405  -4.136  31.975 1.00 24.42  ? 376 HOH A O   1 
HETATM 1212 O  O   . HOH J 6 .   ? 29.728 4.017   5.104  1.00 33.17  ? 377 HOH A O   1 
HETATM 1213 O  O   . HOH J 6 .   ? 1.851  13.347  17.570 1.00 14.80  ? 378 HOH A O   1 
HETATM 1214 O  O   . HOH J 6 .   ? 33.992 18.167  10.553 1.00 29.25  ? 379 HOH A O   1 
HETATM 1215 O  O   . HOH J 6 .   ? -0.885 2.835   24.356 1.00 16.82  ? 380 HOH A O   1 
HETATM 1216 O  O   . HOH J 6 .   ? 19.570 1.835   19.127 1.00 19.03  ? 381 HOH A O   1 
HETATM 1217 O  O   . HOH J 6 .   ? -2.967 9.581   21.168 1.00 17.53  ? 382 HOH A O   1 
HETATM 1218 O  O   . HOH J 6 .   ? 20.242 -3.638  16.595 1.00 26.25  ? 383 HOH A O   1 
HETATM 1219 O  O   . HOH J 6 .   ? 0.632  8.898   6.663  1.00 37.10  ? 384 HOH A O   1 
HETATM 1220 O  O   . HOH J 6 .   ? 13.232 23.311  13.668 1.00 34.49  ? 385 HOH A O   1 
HETATM 1221 O  O   . HOH J 6 .   ? 8.173  14.856  27.720 1.00 26.97  ? 386 HOH A O   1 
HETATM 1222 O  O   . HOH J 6 .   ? 28.589 2.488   11.880 1.00 19.30  ? 387 HOH A O   1 
HETATM 1223 O  O   . HOH J 6 .   ? 6.255  -7.978  23.526 1.00 23.97  ? 388 HOH A O   1 
HETATM 1224 O  O   . HOH J 6 .   ? 22.011 -0.802  4.865  1.00 18.81  ? 389 HOH A O   1 
HETATM 1225 O  O   . HOH J 6 .   ? 13.036 2.640   1.193  1.00 11.85  ? 390 HOH A O   1 
HETATM 1226 O  O   . HOH J 6 .   ? 10.624 14.587  18.811 1.00 14.22  ? 391 HOH A O   1 
HETATM 1227 O  O   . HOH J 6 .   ? 18.100 16.837  24.548 1.00 38.84  ? 392 HOH A O   1 
HETATM 1228 O  O   . HOH J 6 .   ? 2.687  18.221  26.337 1.00 31.43  ? 393 HOH A O   1 
HETATM 1229 O  O   . HOH J 6 .   ? 11.361 -8.156  24.629 1.00 25.00  ? 394 HOH A O   1 
HETATM 1230 O  O   . HOH J 6 .   ? 8.669  5.230   33.921 1.00 18.55  ? 395 HOH A O   1 
HETATM 1231 O  O   . HOH J 6 .   ? 5.622  2.707   6.283  1.00 16.14  ? 396 HOH A O   1 
HETATM 1232 O  O   . HOH J 6 .   ? 9.084  15.618  21.109 1.00 15.76  ? 397 HOH A O   1 
HETATM 1233 O  O   . HOH J 6 .   ? -0.985 14.131  21.377 1.00 15.91  ? 398 HOH A O   1 
HETATM 1234 O  O   . HOH J 6 .   ? 19.215 13.135  2.663  1.00 28.56  ? 399 HOH A O   1 
HETATM 1235 O  O   . HOH J 6 .   ? 11.410 11.781  31.298 1.00 27.16  ? 400 HOH A O   1 
HETATM 1236 O  O   . HOH J 6 .   ? 13.953 -3.517  17.700 1.00 18.97  ? 401 HOH A O   1 
HETATM 1237 O  O   . HOH J 6 .   ? 7.492  18.001  20.371 1.00 16.64  ? 402 HOH A O   1 
HETATM 1238 O  O   . HOH J 6 .   ? 5.805  4.256   32.849 1.00 19.00  ? 403 HOH A O   1 
HETATM 1239 O  O   . HOH J 6 .   ? 8.665  17.297  17.944 1.00 21.77  ? 404 HOH A O   1 
HETATM 1240 O  O   . HOH J 6 .   ? 1.098  11.363  28.004 1.00 30.95  ? 405 HOH A O   1 
HETATM 1241 O  O   . HOH J 6 .   ? -0.017 5.434   6.557  1.00 20.99  ? 406 HOH A O   1 
HETATM 1242 O  O   . HOH J 6 .   ? 17.745 18.949  17.888 1.00 17.57  ? 407 HOH A O   1 
HETATM 1243 O  O   . HOH J 6 .   ? 13.018 10.987  9.969  1.00 12.18  ? 408 HOH A O   1 
HETATM 1244 O  O   . HOH J 6 .   ? 13.137 -8.193  11.873 1.00 26.30  ? 409 HOH A O   1 
HETATM 1245 O  O   . HOH J 6 .   ? 12.682 9.487   30.228 1.00 21.53  ? 410 HOH A O   1 
HETATM 1246 O  O   . HOH J 6 .   ? 31.096 6.486   4.759  1.00 33.63  ? 411 HOH A O   1 
HETATM 1247 O  O   . HOH J 6 .   ? 15.431 11.768  1.493  1.00 27.10  ? 412 HOH A O   1 
HETATM 1248 O  O   . HOH J 6 .   ? 20.149 -4.772  10.751 1.00 26.43  ? 413 HOH A O   1 
HETATM 1249 O  O   . HOH J 6 .   ? 16.546 -6.528  12.075 1.00 38.54  ? 414 HOH A O   1 
HETATM 1250 O  O   . HOH J 6 .   ? 36.589 16.920  13.955 1.00 28.25  ? 415 HOH A O   1 
HETATM 1251 O  O   . HOH J 6 .   ? 27.688 3.055   3.849  1.00 42.21  ? 416 HOH A O   1 
HETATM 1252 O  O   . HOH J 6 .   ? 18.219 8.933   26.485 1.00 26.60  ? 417 HOH A O   1 
HETATM 1253 O  O   . HOH J 6 .   ? 15.189 -3.929  1.642  1.00 15.74  ? 418 HOH A O   1 
HETATM 1254 O  O   . HOH J 6 .   ? 3.509  -4.215  6.275  1.00 24.02  ? 419 HOH A O   1 
HETATM 1255 O  O   . HOH J 6 .   ? 18.671 20.547  7.372  1.00 38.12  ? 420 HOH A O   1 
HETATM 1256 O  O   . HOH J 6 .   ? 14.984 15.126  4.542  1.00 23.79  ? 421 HOH A O   1 
HETATM 1257 O  O   . HOH J 6 .   ? -1.277 3.147   4.729  1.00 34.40  ? 422 HOH A O   1 
HETATM 1258 O  O   . HOH J 6 .   ? 6.390  23.526  13.732 1.00 26.37  ? 423 HOH A O   1 
HETATM 1259 O  O   . HOH J 6 .   ? 31.520 8.224   6.919  1.00 29.31  ? 424 HOH A O   1 
HETATM 1260 O  O   . HOH J 6 .   ? 17.655 4.216   26.649 1.00 28.57  ? 425 HOH A O   1 
HETATM 1261 O  O   . HOH J 6 .   ? 5.936  8.433   3.251  1.00 32.45  ? 426 HOH A O   1 
HETATM 1262 O  O   . HOH J 6 .   ? 3.469  -0.682  28.982 1.00 27.62  ? 427 HOH A O   1 
HETATM 1263 O  O   . HOH J 6 .   ? 30.973 18.544  9.051  1.00 33.75  ? 428 HOH A O   1 
HETATM 1264 O  O   . HOH J 6 .   ? 4.400  -6.437  14.126 1.00 30.44  ? 429 HOH A O   1 
HETATM 1265 O  O   . HOH J 6 .   ? 0.323  -2.118  16.988 1.00 20.57  ? 430 HOH A O   1 
HETATM 1266 O  O   . HOH J 6 .   ? 3.073  -1.314  21.751 1.00 16.30  ? 431 HOH A O   1 
HETATM 1267 O  O   . HOH J 6 .   ? 31.412 14.503  22.492 1.00 20.99  ? 432 HOH A O   1 
HETATM 1268 O  O   . HOH J 6 .   ? 3.732  11.867  19.237 1.00 16.69  ? 433 HOH A O   1 
HETATM 1269 O  O   . HOH J 6 .   ? 31.448 2.124   4.535  1.00 41.84  ? 434 HOH A O   1 
HETATM 1270 O  O   . HOH J 6 .   ? 2.012  7.502   26.864 1.00 20.27  ? 435 HOH A O   1 
HETATM 1271 O  O   . HOH J 6 .   ? 33.881 3.658   15.566 1.00 28.43  ? 436 HOH A O   1 
HETATM 1272 O  O   . HOH J 6 .   ? 29.375 5.718   19.429 1.00 31.35  ? 437 HOH A O   1 
HETATM 1273 O  O   . HOH J 6 .   ? 4.306  -0.579  24.143 1.00 14.25  ? 438 HOH A O   1 
HETATM 1274 O  O   . HOH J 6 .   ? 5.273  24.381  23.111 1.00 18.85  ? 439 HOH A O   1 
HETATM 1275 O  O   . HOH J 6 .   ? 6.171  -2.768  -1.563 1.00 29.78  ? 440 HOH A O   1 
HETATM 1276 O  O   . HOH J 6 .   ? 28.406 16.251  24.177 1.00 24.63  ? 441 HOH A O   1 
HETATM 1277 O  O   . HOH J 6 .   ? 20.894 2.733   -1.591 1.00 24.56  ? 442 HOH A O   1 
HETATM 1278 O  O   . HOH J 6 .   ? 9.700  9.861   23.521 1.00 17.39  ? 443 HOH A O   1 
HETATM 1279 O  O   . HOH J 6 .   ? 9.345  -7.640  0.367  1.00 33.41  ? 444 HOH A O   1 
HETATM 1280 O  O   . HOH J 6 .   ? 1.376  -5.680  14.106 1.00 33.35  ? 445 HOH A O   1 
HETATM 1281 O  O   . HOH J 6 .   ? 35.467 -1.864  10.761 1.00 24.08  ? 446 HOH A O   1 
HETATM 1282 O  O   . HOH J 6 .   ? 23.753 7.016   21.440 1.00 21.64  ? 447 HOH A O   1 
HETATM 1283 O  O   . HOH J 6 .   ? 36.065 1.433   8.173  1.00 38.54  ? 448 HOH A O   1 
HETATM 1284 O  O   . HOH J 6 .   ? 34.091 6.406   15.701 1.00 33.17  ? 449 HOH A O   1 
HETATM 1285 O  O   . HOH J 6 .   ? 1.709  14.431  20.263 1.00 14.21  ? 450 HOH A O   1 
HETATM 1286 O  O   . HOH J 6 .   ? 21.438 8.445   21.966 1.00 16.48  ? 451 HOH A O   1 
HETATM 1287 O  O   . HOH J 6 .   ? 17.288 -0.730  20.077 1.00 17.13  ? 452 HOH A O   1 
HETATM 1288 O  O   . HOH J 6 .   ? 35.188 9.605   12.023 1.00 40.46  ? 453 HOH A O   1 
HETATM 1289 O  O   . HOH J 6 .   ? 3.570  25.497  18.749 1.00 33.01  ? 454 HOH A O   1 
HETATM 1290 O  O   . HOH J 6 .   ? 19.633 -2.203  34.012 1.00 30.85  ? 455 HOH A O   1 
HETATM 1291 O  O   . HOH J 6 .   ? 22.881 18.652  6.711  1.00 19.71  ? 456 HOH A O   1 
HETATM 1292 O  O   . HOH J 6 .   ? 15.732 18.070  27.753 1.00 34.31  ? 457 HOH A O   1 
HETATM 1293 O  O   . HOH J 6 .   ? 24.475 17.575  4.801  1.00 40.71  ? 458 HOH A O   1 
HETATM 1294 O  O   . HOH J 6 .   ? 22.923 2.111   20.344 1.00 25.00  ? 459 HOH A O   1 
HETATM 1295 O  O   . HOH J 6 .   ? 7.345  13.566  22.146 1.00 13.07  ? 460 HOH A O   1 
HETATM 1296 O  O   . HOH J 6 .   ? 8.146  -7.040  9.126  1.00 28.94  ? 461 HOH A O   1 
HETATM 1297 O  O   . HOH J 6 .   ? 25.601 9.216   22.790 1.00 28.16  ? 462 HOH A O   1 
HETATM 1298 O  O   . HOH J 6 .   ? 6.897  -9.337  8.113  1.00 41.58  ? 463 HOH A O   1 
HETATM 1299 O  O   . HOH J 6 .   ? 36.565 19.304  18.140 1.00 32.57  ? 464 HOH A O   1 
HETATM 1300 O  O   . HOH J 6 .   ? 16.888 -3.612  19.534 1.00 17.41  ? 465 HOH A O   1 
HETATM 1301 O  O   . HOH J 6 .   ? 18.296 9.331   -0.904 1.00 24.07  ? 466 HOH A O   1 
HETATM 1302 O  O   . HOH J 6 .   ? 10.025 14.837  1.382  0.62 28.87  ? 467 HOH A O   1 
HETATM 1303 O  O   . HOH J 6 .   ? 27.220 -1.933  15.484 1.00 23.92  ? 468 HOH A O   1 
HETATM 1304 O  O   . HOH J 6 .   ? 6.048  -4.763  31.700 1.00 30.88  ? 469 HOH A O   1 
HETATM 1305 O  O   . HOH J 6 .   ? -1.105 16.420  25.088 1.00 38.01  ? 470 HOH A O   1 
HETATM 1306 O  O   . HOH J 6 .   ? 1.562  13.656  23.386 1.00 20.37  ? 471 HOH A O   1 
HETATM 1307 O  O   . HOH J 6 .   ? 16.008 13.497  26.861 1.00 35.43  ? 472 HOH A O   1 
HETATM 1308 O  O   . HOH J 6 .   ? 21.595 7.469   -3.376 1.00 34.81  ? 473 HOH A O   1 
HETATM 1309 O  O   . HOH J 6 .   ? 10.823 23.136  14.836 1.00 24.73  ? 474 HOH A O   1 
HETATM 1310 O  O   . HOH J 6 .   ? 8.261  12.214  24.518 1.00 19.97  ? 475 HOH A O   1 
HETATM 1311 O  O   . HOH J 6 .   ? -3.992 24.503  11.352 1.00 37.21  ? 476 HOH A O   1 
HETATM 1312 O  O   . HOH J 6 .   ? 15.604 11.385  28.916 1.00 29.03  ? 477 HOH A O   1 
HETATM 1313 O  O   . HOH J 6 .   ? 8.324  20.658  9.837  1.00 42.42  ? 478 HOH A O   1 
HETATM 1314 O  O   . HOH J 6 .   ? 17.853 11.250  1.036  1.00 29.28  ? 479 HOH A O   1 
HETATM 1315 O  O   . HOH J 6 .   ? 8.739  10.386  31.701 1.00 27.66  ? 480 HOH A O   1 
HETATM 1316 O  O   . HOH J 6 .   ? 6.683  -4.453  2.591  1.00 21.46  ? 481 HOH A O   1 
HETATM 1317 O  O   . HOH J 6 .   ? 0.704  2.560   26.443 1.00 30.15  ? 482 HOH A O   1 
HETATM 1318 O  O   . HOH J 6 .   ? 13.582 -8.110  25.994 1.00 32.40  ? 483 HOH A O   1 
HETATM 1319 O  O   . HOH J 6 .   ? 37.051 -0.145  9.640  1.00 32.49  ? 484 HOH A O   1 
HETATM 1320 O  O   . HOH J 6 .   ? 4.051  -4.124  2.792  1.00 47.53  ? 485 HOH A O   1 
HETATM 1321 O  O   . HOH J 6 .   ? 28.340 8.885   22.295 1.00 42.21  ? 486 HOH A O   1 
HETATM 1322 O  O   . HOH J 6 .   ? 29.615 -1.902  6.082  1.00 35.32  ? 487 HOH A O   1 
HETATM 1323 O  O   . HOH J 6 .   ? 19.089 -4.699  34.355 1.00 44.88  ? 488 HOH A O   1 
HETATM 1324 O  O   . HOH J 6 .   ? 23.363 15.868  24.546 1.00 44.14  ? 489 HOH A O   1 
HETATM 1325 O  O   . HOH J 6 .   ? 16.842 -6.306  34.797 1.00 30.70  ? 490 HOH A O   1 
HETATM 1326 O  O   . HOH J 6 .   ? 20.375 9.522   -1.904 1.00 24.65  ? 491 HOH A O   1 
HETATM 1327 O  O   . HOH J 6 .   ? 17.049 11.010  26.883 1.00 36.68  ? 492 HOH A O   1 
HETATM 1328 O  O   . HOH J 6 .   ? -2.705 7.798   27.665 1.00 50.96  ? 493 HOH A O   1 
HETATM 1329 O  O   . HOH J 6 .   ? 2.884  -1.298  26.565 1.00 27.78  ? 494 HOH A O   1 
HETATM 1330 O  O   . HOH J 6 .   ? 23.067 -9.546  6.844  1.00 30.54  ? 495 HOH A O   1 
HETATM 1331 O  O   . HOH J 6 .   ? 20.931 14.877  1.672  1.00 38.06  ? 496 HOH A O   1 
HETATM 1332 O  O   . HOH J 6 .   ? 7.293  18.127  5.388  0.62 30.47  ? 497 HOH A O   1 
HETATM 1333 O  O   . HOH J 6 .   ? 16.899 14.273  3.051  1.00 38.63  ? 498 HOH A O   1 
HETATM 1334 O  O   . HOH J 6 .   ? 29.577 -0.356  15.727 1.00 28.55  ? 499 HOH A O   1 
HETATM 1335 O  O   . HOH J 6 .   ? 38.212 0.402   13.550 1.00 46.58  ? 500 HOH A O   1 
HETATM 1336 O  O   . HOH J 6 .   ? 24.669 13.455  25.384 1.00 38.66  ? 501 HOH A O   1 
HETATM 1337 O  O   . HOH J 6 .   ? 8.854  7.794   3.064  1.00 26.36  ? 502 HOH A O   1 
HETATM 1338 O  O   . HOH J 6 .   ? 20.543 13.396  -0.456 1.00 57.23  ? 503 HOH A O   1 
HETATM 1339 O  O   . HOH J 6 .   ? 8.925  20.029  7.388  1.00 32.93  ? 504 HOH A O   1 
HETATM 1340 O  O   . HOH J 6 .   ? 6.228  25.558  15.514 1.00 34.34  ? 505 HOH A O   1 
HETATM 1341 O  O   . HOH J 6 .   ? 31.274 3.327   16.053 1.00 30.42  ? 506 HOH A O   1 
HETATM 1342 O  O   . HOH J 6 .   ? 6.661  13.099  26.255 1.00 24.94  ? 507 HOH A O   1 
HETATM 1343 O  O   . HOH J 6 .   ? 5.459  6.278   2.501  1.00 27.37  ? 508 HOH A O   1 
HETATM 1344 O  O   . HOH J 6 .   ? 2.442  14.575  26.080 1.00 35.37  ? 509 HOH A O   1 
HETATM 1345 O  O   . HOH J 6 .   ? 5.397  11.414  28.198 1.00 30.14  ? 510 HOH A O   1 
HETATM 1346 O  O   . HOH J 6 .   ? 30.401 5.769   17.025 1.00 36.20  ? 511 HOH A O   1 
HETATM 1347 O  O   . HOH J 6 .   ? 26.701 10.139  0.085  1.00 34.44  ? 512 HOH A O   1 
HETATM 1348 O  O   . HOH J 6 .   ? 6.883  -7.117  1.765  1.00 32.31  ? 513 HOH A O   1 
HETATM 1349 O  O   . HOH J 6 .   ? 18.160 19.736  20.395 1.00 23.48  ? 514 HOH A O   1 
HETATM 1350 O  O   . HOH J 6 .   ? -1.145 11.559  20.178 1.00 17.02  ? 515 HOH A O   1 
HETATM 1351 O  O   . HOH J 6 .   ? 1.896  -4.009  26.928 1.00 32.66  ? 516 HOH A O   1 
HETATM 1352 O  O   . HOH J 6 .   ? -0.917 12.524  17.498 1.00 14.11  ? 517 HOH A O   1 
HETATM 1353 O  O   . HOH J 6 .   ? 12.343 -6.416  33.419 1.00 30.40  ? 518 HOH A O   1 
HETATM 1354 O  O   . HOH J 6 .   ? 1.394  16.462  4.926  0.62 29.78  ? 519 HOH A O   1 
HETATM 1355 O  O   . HOH J 6 .   ? 15.466 -7.458  31.300 1.00 44.65  ? 520 HOH A O   1 
HETATM 1356 O  O   . HOH J 6 .   ? 1.688  20.518  26.445 1.00 40.62  ? 521 HOH A O   1 
HETATM 1357 O  O   . HOH J 6 .   ? 21.968 9.578   24.411 1.00 23.16  ? 522 HOH A O   1 
HETATM 1358 O  O   . HOH J 6 .   ? 2.003  -5.862  22.613 1.00 31.86  ? 523 HOH A O   1 
HETATM 1359 O  O   . HOH J 6 .   ? 2.893  12.732  28.450 1.00 32.65  ? 524 HOH A O   1 
HETATM 1360 O  O   . HOH J 6 .   ? 13.553 -12.733 3.866  1.00 40.51  ? 525 HOH A O   1 
HETATM 1361 O  O   . HOH J 6 .   ? 31.655 10.953  6.243  1.00 34.87  ? 526 HOH A O   1 
HETATM 1362 O  O   . HOH J 6 .   ? 24.930 11.317  -1.770 1.00 40.37  ? 527 HOH A O   1 
HETATM 1363 O  O   . HOH J 6 .   ? 2.629  23.695  24.025 1.00 32.99  ? 528 HOH A O   1 
HETATM 1364 O  O   . HOH J 6 .   ? 0.795  16.775  26.288 1.00 37.48  ? 529 HOH A O   1 
HETATM 1365 O  O   . HOH J 6 .   ? 37.604 18.169  15.769 1.00 31.13  ? 530 HOH A O   1 
HETATM 1366 O  O   . HOH J 6 .   ? 20.292 10.345  26.749 1.00 33.94  ? 531 HOH A O   1 
HETATM 1367 O  O   . HOH J 6 .   ? 21.990 11.796  -2.025 1.00 33.25  ? 532 HOH A O   1 
HETATM 1368 O  O   . HOH J 6 .   ? 3.568  -7.727  23.365 1.00 34.95  ? 533 HOH A O   1 
HETATM 1369 O  O   . HOH J 6 .   ? 3.986  -7.508  25.734 1.00 42.51  ? 534 HOH A O   1 
HETATM 1370 O  O   . HOH J 6 .   ? 38.722 -4.081  6.254  1.00 48.11  ? 535 HOH A O   1 
HETATM 1371 O  O   . HOH J 6 .   ? 3.016  22.540  8.644  1.00 45.08  ? 536 HOH A O   1 
HETATM 1372 O  O   . HOH J 6 .   ? 5.368  22.588  8.957  1.00 42.16  ? 537 HOH A O   1 
HETATM 1373 O  O   . HOH J 6 .   ? 19.208 12.558  27.703 1.00 33.98  ? 538 HOH A O   1 
HETATM 1374 O  O   . HOH J 6 .   ? 3.570  22.616  5.604  1.00 44.49  ? 539 HOH A O   1 
# 
