data_7HX2
# 
_entry.id   7HX2 
# 
_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   7HX2         pdb_00007hx2 10.2210/pdb7hx2/pdb 
WWPDB D_1001408038 ?            ?                   
# 
_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       2025-02-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_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                        7HX2 
_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   2025-01-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                                    15892.732 1  3.4.22.29 ? ? ? 
2 non-polymer syn '(3S)-1-[(2-methoxyphenyl)methyl]-6-oxopiperidine-3-carboxamide' 262.304   1  ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                       65.409    1  ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                             78.133    1  ?         ? ? ? 
5 water       nat water                                                            18.015    83 ?         ? ? ? 
# 
_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 '(3S)-1-[(2-methoxyphenyl)methyl]-6-oxopiperidine-3-carboxamide' A1BOE 
3 'ZINC ION'                                                       ZN    
4 'DIMETHYL SULFOXIDE'                                             DMS   
5 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 
A1BOE non-polymer         . '(3S)-1-[(2-methoxyphenyl)methyl]-6-oxopiperidine-3-carboxamide' ? 'C14 H18 N2 O3'  262.304 
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 
THR   'L-peptide linking' y THREONINE                                                        ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                       ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                         ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                           ? 'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION'                                                       ? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 ?   ?   ?   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        A1BOE 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BOE 
_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 A1BOE 1  201 201 A1BOE LIG A . 
C 3 ZN    1  202 1   ZN    ZN  A . 
D 4 DMS   1  203 6   DMS   DMS A . 
E 5 HOH   1  301 72  HOH   HOH A . 
E 5 HOH   2  302 9   HOH   HOH A . 
E 5 HOH   3  303 15  HOH   HOH A . 
E 5 HOH   4  304 65  HOH   HOH A . 
E 5 HOH   5  305 85  HOH   HOH A . 
E 5 HOH   6  306 79  HOH   HOH A . 
E 5 HOH   7  307 11  HOH   HOH A . 
E 5 HOH   8  308 4   HOH   HOH A . 
E 5 HOH   9  309 77  HOH   HOH A . 
E 5 HOH   10 310 24  HOH   HOH A . 
E 5 HOH   11 311 67  HOH   HOH A . 
E 5 HOH   12 312 1   HOH   HOH A . 
E 5 HOH   13 313 41  HOH   HOH A . 
E 5 HOH   14 314 38  HOH   HOH A . 
E 5 HOH   15 315 78  HOH   HOH A . 
E 5 HOH   16 316 80  HOH   HOH A . 
E 5 HOH   17 317 76  HOH   HOH A . 
E 5 HOH   18 318 40  HOH   HOH A . 
E 5 HOH   19 319 56  HOH   HOH A . 
E 5 HOH   20 320 10  HOH   HOH A . 
E 5 HOH   21 321 31  HOH   HOH A . 
E 5 HOH   22 322 54  HOH   HOH A . 
E 5 HOH   23 323 12  HOH   HOH A . 
E 5 HOH   24 324 27  HOH   HOH A . 
E 5 HOH   25 325 58  HOH   HOH A . 
E 5 HOH   26 326 62  HOH   HOH A . 
E 5 HOH   27 327 37  HOH   HOH A . 
E 5 HOH   28 328 43  HOH   HOH A . 
E 5 HOH   29 329 16  HOH   HOH A . 
E 5 HOH   30 330 14  HOH   HOH A . 
E 5 HOH   31 331 3   HOH   HOH A . 
E 5 HOH   32 332 75  HOH   HOH A . 
E 5 HOH   33 333 66  HOH   HOH A . 
E 5 HOH   34 334 45  HOH   HOH A . 
E 5 HOH   35 335 26  HOH   HOH A . 
E 5 HOH   36 336 52  HOH   HOH A . 
E 5 HOH   37 337 28  HOH   HOH A . 
E 5 HOH   38 338 5   HOH   HOH A . 
E 5 HOH   39 339 13  HOH   HOH A . 
E 5 HOH   40 340 25  HOH   HOH A . 
E 5 HOH   41 341 42  HOH   HOH A . 
E 5 HOH   42 342 17  HOH   HOH A . 
E 5 HOH   43 343 74  HOH   HOH A . 
E 5 HOH   44 344 82  HOH   HOH A . 
E 5 HOH   45 345 29  HOH   HOH A . 
E 5 HOH   46 346 18  HOH   HOH A . 
E 5 HOH   47 347 64  HOH   HOH A . 
E 5 HOH   48 348 68  HOH   HOH A . 
E 5 HOH   49 349 57  HOH   HOH A . 
E 5 HOH   50 350 73  HOH   HOH A . 
E 5 HOH   51 351 55  HOH   HOH A . 
E 5 HOH   52 352 33  HOH   HOH A . 
E 5 HOH   53 353 81  HOH   HOH A . 
E 5 HOH   54 354 61  HOH   HOH A . 
E 5 HOH   55 355 19  HOH   HOH A . 
E 5 HOH   56 356 53  HOH   HOH A . 
E 5 HOH   57 357 34  HOH   HOH A . 
E 5 HOH   58 358 8   HOH   HOH A . 
E 5 HOH   59 359 60  HOH   HOH A . 
E 5 HOH   60 360 86  HOH   HOH A . 
E 5 HOH   61 361 6   HOH   HOH A . 
E 5 HOH   62 362 59  HOH   HOH A . 
E 5 HOH   63 363 39  HOH   HOH A . 
E 5 HOH   64 364 48  HOH   HOH A . 
E 5 HOH   65 365 50  HOH   HOH A . 
E 5 HOH   66 366 22  HOH   HOH A . 
E 5 HOH   67 367 30  HOH   HOH A . 
E 5 HOH   68 368 32  HOH   HOH A . 
E 5 HOH   69 369 69  HOH   HOH A . 
E 5 HOH   70 370 70  HOH   HOH A . 
E 5 HOH   71 371 44  HOH   HOH A . 
E 5 HOH   72 372 51  HOH   HOH A . 
E 5 HOH   73 373 23  HOH   HOH A . 
E 5 HOH   74 374 7   HOH   HOH A . 
E 5 HOH   75 375 83  HOH   HOH A . 
E 5 HOH   76 376 20  HOH   HOH A . 
E 5 HOH   77 377 35  HOH   HOH A . 
E 5 HOH   78 378 71  HOH   HOH A . 
E 5 HOH   79 379 63  HOH   HOH A . 
E 5 HOH   80 380 21  HOH   HOH A . 
E 5 HOH   81 381 2   HOH   HOH A . 
E 5 HOH   82 382 47  HOH   HOH A . 
E 5 HOH   83 383 84  HOH   HOH A . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       BUSTER  '2.10.4 (23-JAN-2024)' ? 1 
'data scaling'   Aimless .                      ? 2 
phasing          PHASER  .                      ? 3 
'data reduction' XDS     .                      ? 4 
# 
_cell.entry_id           7HX2 
_cell.length_a           73.099 
_cell.length_b           61.033 
_cell.length_c           32.597 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.86 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HX2 
_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          7HX2 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.28 
_exptl_crystal.density_percent_sol   46.17 
_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   2024-11-21 
_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   0.92203 
_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        0.92203 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HX2 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             46.81 
_reflns.d_resolution_high            1.48 
_reflns.number_obs                   23903 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            0.158 
_reflns.pdbx_netI_over_sigmaI        4.7 
_reflns.pdbx_redundancy              6.5 
_reflns.pdbx_Rrim_I_all              0.171 
_reflns.pdbx_Rpim_I_all              0.066 
_reflns.pdbx_CC_half                 0.991 
_reflns.pdbx_number_measured_all     156437 
_reflns.pdbx_chi_squared             0.26 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.48 
_reflns_shell.d_res_low                   1.50 
_reflns_shell.number_measured_all         5768 
_reflns_shell.number_unique_obs           1160 
_reflns_shell.Rmerge_I_obs                3.317 
_reflns_shell.pdbx_chi_squared            0.03 
_reflns_shell.pdbx_redundancy             5.0 
_reflns_shell.percent_possible_obs        99.0 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.2 
_reflns_shell.pdbx_Rrim_I_all             3.692 
_reflns_shell.pdbx_Rpim_I_all             1.595 
_reflns_shell.pdbx_CC_half                0.121 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7HX2 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     20963 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             19.60 
_refine.ls_d_res_high                            1.480 
_refine.ls_percent_reflns_obs                    87.8 
_refine.ls_R_factor_obs                          0.2260 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2239 
_refine.ls_R_factor_R_free                       0.2710 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.460 
_refine.ls_number_reflns_R_free                  935 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.958 
_refine.correlation_coeff_Fo_to_Fc_free          0.927 
_refine.B_iso_mean                               32.88 
_refine.aniso_B[1][1]                            -1.80790 
_refine.aniso_B[2][2]                            4.24870 
_refine.aniso_B[3][3]                            -2.44080 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -4.73350 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             0.093 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.099 
_refine.pdbx_overall_SU_R_Blow_DPI               0.094 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.099 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HX2 
_refine_analyze.Luzzati_coordinate_error_obs    0.27 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1074 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         24 
_refine_hist.number_atoms_solvent             83 
_refine_hist.number_atoms_total               1181 
_refine_hist.d_res_high                       1.480 
_refine_hist.d_res_low                        19.60 
# 
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 
t_bond_d                  0.010 ? 2.00  1127 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.95  ? 2.00  1533 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  376  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  203  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1127 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.89  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           15.00 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  138  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  934  'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   47 
_refine_ls_shell.d_res_high                       1.48 
_refine_ls_shell.d_res_low                        1.51 
_refine_ls_shell.number_reflns_R_work             437 
_refine_ls_shell.R_factor_R_work                  0.4907 
_refine_ls_shell.percent_reflns_obs               35.72 
_refine_ls_shell.R_factor_R_free                  0.3784 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.17 
_refine_ls_shell.number_reflns_R_free             19 
_refine_ls_shell.number_reflns_all                456 
_refine_ls_shell.R_factor_all                     0.4864 
# 
_struct.entry_id                  7HX2 
_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-0032526-001 (A71EV2A-x4029)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HX2 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN, HYDROLASE
;
# 
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 4 ? 
E N N 5 ? 
# 
_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              7HX2 
_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 
# 
_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 C ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.344 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.175 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.370 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.167 ? ? 
# 
_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 ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 109.0 ? 
2 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 107.6 ? 
3 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 112.9 ? 
4 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 118.0 ? 
5 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 97.7  ? 
6 SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 111.5 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N GLY A 43  ? N GLY A 49  O GLY A 7   ? O GLY A 13  
AA2 1 2 O 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 LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O ASP A 130 ? O ASP A 136 N HIS A 91  ? N HIS A 97  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7HX2 
_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 
# 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         15.2329 
_pdbx_refine_tls.origin_y         7.0508 
_pdbx_refine_tls.origin_z         14.1468 
_pdbx_refine_tls.T[1][1]          0.0256 
_pdbx_refine_tls.T[2][2]          0.0418 
_pdbx_refine_tls.T[3][3]          -0.1473 
_pdbx_refine_tls.T[1][2]          -0.0083 
_pdbx_refine_tls.T[1][3]          -0.1114 
_pdbx_refine_tls.T[2][3]          -0.0071 
_pdbx_refine_tls.L[1][1]          0.8787 
_pdbx_refine_tls.L[2][2]          3.1727 
_pdbx_refine_tls.L[3][3]          1.0046 
_pdbx_refine_tls.L[1][2]          0.8790 
_pdbx_refine_tls.L[1][3]          -0.1484 
_pdbx_refine_tls.L[2][3]          -1.1572 
_pdbx_refine_tls.S[1][1]          -0.0850 
_pdbx_refine_tls.S[1][2]          0.0479 
_pdbx_refine_tls.S[1][3]          0.0499 
_pdbx_refine_tls.S[2][1]          0.1581 
_pdbx_refine_tls.S[2][2]          0.0861 
_pdbx_refine_tls.S[2][3]          -0.1349 
_pdbx_refine_tls.S[3][1]          0.0099 
_pdbx_refine_tls.S[3][2]          -0.0813 
_pdbx_refine_tls.S[3][3]          -0.0011 
# 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '{ A|* }' 
# 
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 GLU 146 ? A GLU 140 
2 1 Y 1 A ALA 147 ? A ALA 141 
3 1 Y 1 A MET 148 ? A MET 142 
4 1 Y 1 A GLU 149 ? A GLU 143 
5 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 
A1BOE N1   N  N N 1   
A1BOE C4   C  Y N 2   
A1BOE C5   C  Y N 3   
A1BOE C6   C  Y N 4   
A1BOE C7   C  N N 5   
A1BOE C8   C  N N 6   
A1BOE C10  C  N N 7   
A1BOE C13  C  N N 8   
A1BOE O2   O  N N 9   
A1BOE C12  C  N N 10  
A1BOE C11  C  N N 11  
A1BOE C9   C  N R 12  
A1BOE O1   O  N N 13  
A1BOE N    N  N N 14  
A1BOE C1   C  Y N 15  
A1BOE O    O  N N 16  
A1BOE C    C  N N 17  
A1BOE C3   C  Y N 18  
A1BOE C2   C  Y N 19  
A1BOE H13  H  N N 20  
A1BOE H12  H  N N 21  
A1BOE H6   H  N N 22  
A1BOE H7   H  N N 23  
A1BOE H9   H  N N 24  
A1BOE H8   H  N N 25  
A1BOE H11  H  N N 26  
A1BOE H10  H  N N 27  
A1BOE H17  H  N N 28  
A1BOE H16  H  N N 29  
A1BOE H15  H  N N 30  
A1BOE H14  H  N N 31  
A1BOE H    H  N N 32  
A1BOE H3   H  N N 33  
A1BOE H2   H  N N 34  
A1BOE H1   H  N N 35  
A1BOE H5   H  N N 36  
A1BOE H4   H  N N 37  
ALA   N    N  N N 38  
ALA   CA   C  N S 39  
ALA   C    C  N N 40  
ALA   O    O  N N 41  
ALA   CB   C  N N 42  
ALA   OXT  O  N N 43  
ALA   H    H  N N 44  
ALA   H2   H  N N 45  
ALA   HA   H  N N 46  
ALA   HB1  H  N N 47  
ALA   HB2  H  N N 48  
ALA   HB3  H  N N 49  
ALA   HXT  H  N N 50  
ARG   N    N  N N 51  
ARG   CA   C  N S 52  
ARG   C    C  N N 53  
ARG   O    O  N N 54  
ARG   CB   C  N N 55  
ARG   CG   C  N N 56  
ARG   CD   C  N N 57  
ARG   NE   N  N N 58  
ARG   CZ   C  N N 59  
ARG   NH1  N  N N 60  
ARG   NH2  N  N N 61  
ARG   OXT  O  N N 62  
ARG   H    H  N N 63  
ARG   H2   H  N N 64  
ARG   HA   H  N N 65  
ARG   HB2  H  N N 66  
ARG   HB3  H  N N 67  
ARG   HG2  H  N N 68  
ARG   HG3  H  N N 69  
ARG   HD2  H  N N 70  
ARG   HD3  H  N N 71  
ARG   HE   H  N N 72  
ARG   HH11 H  N N 73  
ARG   HH12 H  N N 74  
ARG   HH21 H  N N 75  
ARG   HH22 H  N N 76  
ARG   HXT  H  N N 77  
ASN   N    N  N N 78  
ASN   CA   C  N S 79  
ASN   C    C  N N 80  
ASN   O    O  N N 81  
ASN   CB   C  N N 82  
ASN   CG   C  N N 83  
ASN   OD1  O  N N 84  
ASN   ND2  N  N N 85  
ASN   OXT  O  N N 86  
ASN   H    H  N N 87  
ASN   H2   H  N N 88  
ASN   HA   H  N N 89  
ASN   HB2  H  N N 90  
ASN   HB3  H  N N 91  
ASN   HD21 H  N N 92  
ASN   HD22 H  N N 93  
ASN   HXT  H  N N 94  
ASP   N    N  N N 95  
ASP   CA   C  N S 96  
ASP   C    C  N N 97  
ASP   O    O  N N 98  
ASP   CB   C  N N 99  
ASP   CG   C  N N 100 
ASP   OD1  O  N N 101 
ASP   OD2  O  N N 102 
ASP   OXT  O  N N 103 
ASP   H    H  N N 104 
ASP   H2   H  N N 105 
ASP   HA   H  N N 106 
ASP   HB2  H  N N 107 
ASP   HB3  H  N N 108 
ASP   HD2  H  N N 109 
ASP   HXT  H  N N 110 
CYS   N    N  N N 111 
CYS   CA   C  N R 112 
CYS   C    C  N N 113 
CYS   O    O  N N 114 
CYS   CB   C  N N 115 
CYS   SG   S  N N 116 
CYS   OXT  O  N N 117 
CYS   H    H  N N 118 
CYS   H2   H  N N 119 
CYS   HA   H  N N 120 
CYS   HB2  H  N N 121 
CYS   HB3  H  N N 122 
CYS   HG   H  N N 123 
CYS   HXT  H  N N 124 
DMS   S    S  N N 125 
DMS   O    O  N N 126 
DMS   C1   C  N N 127 
DMS   C2   C  N N 128 
DMS   H11  H  N N 129 
DMS   H12  H  N N 130 
DMS   H13  H  N N 131 
DMS   H21  H  N N 132 
DMS   H22  H  N N 133 
DMS   H23  H  N N 134 
GLN   N    N  N N 135 
GLN   CA   C  N S 136 
GLN   C    C  N N 137 
GLN   O    O  N N 138 
GLN   CB   C  N N 139 
GLN   CG   C  N N 140 
GLN   CD   C  N N 141 
GLN   OE1  O  N N 142 
GLN   NE2  N  N N 143 
GLN   OXT  O  N N 144 
GLN   H    H  N N 145 
GLN   H2   H  N N 146 
GLN   HA   H  N N 147 
GLN   HB2  H  N N 148 
GLN   HB3  H  N N 149 
GLN   HG2  H  N N 150 
GLN   HG3  H  N N 151 
GLN   HE21 H  N N 152 
GLN   HE22 H  N N 153 
GLN   HXT  H  N N 154 
GLU   N    N  N N 155 
GLU   CA   C  N S 156 
GLU   C    C  N N 157 
GLU   O    O  N N 158 
GLU   CB   C  N N 159 
GLU   CG   C  N N 160 
GLU   CD   C  N N 161 
GLU   OE1  O  N N 162 
GLU   OE2  O  N N 163 
GLU   OXT  O  N N 164 
GLU   H    H  N N 165 
GLU   H2   H  N N 166 
GLU   HA   H  N N 167 
GLU   HB2  H  N N 168 
GLU   HB3  H  N N 169 
GLU   HG2  H  N N 170 
GLU   HG3  H  N N 171 
GLU   HE2  H  N N 172 
GLU   HXT  H  N N 173 
GLY   N    N  N N 174 
GLY   CA   C  N N 175 
GLY   C    C  N N 176 
GLY   O    O  N N 177 
GLY   OXT  O  N N 178 
GLY   H    H  N N 179 
GLY   H2   H  N N 180 
GLY   HA2  H  N N 181 
GLY   HA3  H  N N 182 
GLY   HXT  H  N N 183 
HIS   N    N  N N 184 
HIS   CA   C  N S 185 
HIS   C    C  N N 186 
HIS   O    O  N N 187 
HIS   CB   C  N N 188 
HIS   CG   C  Y N 189 
HIS   ND1  N  Y N 190 
HIS   CD2  C  Y N 191 
HIS   CE1  C  Y N 192 
HIS   NE2  N  Y N 193 
HIS   OXT  O  N N 194 
HIS   H    H  N N 195 
HIS   H2   H  N N 196 
HIS   HA   H  N N 197 
HIS   HB2  H  N N 198 
HIS   HB3  H  N N 199 
HIS   HD1  H  N N 200 
HIS   HD2  H  N N 201 
HIS   HE1  H  N N 202 
HIS   HE2  H  N N 203 
HIS   HXT  H  N N 204 
HOH   O    O  N N 205 
HOH   H1   H  N N 206 
HOH   H2   H  N N 207 
ILE   N    N  N N 208 
ILE   CA   C  N S 209 
ILE   C    C  N N 210 
ILE   O    O  N N 211 
ILE   CB   C  N S 212 
ILE   CG1  C  N N 213 
ILE   CG2  C  N N 214 
ILE   CD1  C  N N 215 
ILE   OXT  O  N N 216 
ILE   H    H  N N 217 
ILE   H2   H  N N 218 
ILE   HA   H  N N 219 
ILE   HB   H  N N 220 
ILE   HG12 H  N N 221 
ILE   HG13 H  N N 222 
ILE   HG21 H  N N 223 
ILE   HG22 H  N N 224 
ILE   HG23 H  N N 225 
ILE   HD11 H  N N 226 
ILE   HD12 H  N N 227 
ILE   HD13 H  N N 228 
ILE   HXT  H  N N 229 
LEU   N    N  N N 230 
LEU   CA   C  N S 231 
LEU   C    C  N N 232 
LEU   O    O  N N 233 
LEU   CB   C  N N 234 
LEU   CG   C  N N 235 
LEU   CD1  C  N N 236 
LEU   CD2  C  N N 237 
LEU   OXT  O  N N 238 
LEU   H    H  N N 239 
LEU   H2   H  N N 240 
LEU   HA   H  N N 241 
LEU   HB2  H  N N 242 
LEU   HB3  H  N N 243 
LEU   HG   H  N N 244 
LEU   HD11 H  N N 245 
LEU   HD12 H  N N 246 
LEU   HD13 H  N N 247 
LEU   HD21 H  N N 248 
LEU   HD22 H  N N 249 
LEU   HD23 H  N N 250 
LEU   HXT  H  N N 251 
LYS   N    N  N N 252 
LYS   CA   C  N S 253 
LYS   C    C  N N 254 
LYS   O    O  N N 255 
LYS   CB   C  N N 256 
LYS   CG   C  N N 257 
LYS   CD   C  N N 258 
LYS   CE   C  N N 259 
LYS   NZ   N  N N 260 
LYS   OXT  O  N N 261 
LYS   H    H  N N 262 
LYS   H2   H  N N 263 
LYS   HA   H  N N 264 
LYS   HB2  H  N N 265 
LYS   HB3  H  N N 266 
LYS   HG2  H  N N 267 
LYS   HG3  H  N N 268 
LYS   HD2  H  N N 269 
LYS   HD3  H  N N 270 
LYS   HE2  H  N N 271 
LYS   HE3  H  N N 272 
LYS   HZ1  H  N N 273 
LYS   HZ2  H  N N 274 
LYS   HZ3  H  N N 275 
LYS   HXT  H  N N 276 
MET   N    N  N N 277 
MET   CA   C  N S 278 
MET   C    C  N N 279 
MET   O    O  N N 280 
MET   CB   C  N N 281 
MET   CG   C  N N 282 
MET   SD   S  N N 283 
MET   CE   C  N N 284 
MET   OXT  O  N N 285 
MET   H    H  N N 286 
MET   H2   H  N N 287 
MET   HA   H  N N 288 
MET   HB2  H  N N 289 
MET   HB3  H  N N 290 
MET   HG2  H  N N 291 
MET   HG3  H  N N 292 
MET   HE1  H  N N 293 
MET   HE2  H  N N 294 
MET   HE3  H  N N 295 
MET   HXT  H  N N 296 
PHE   N    N  N N 297 
PHE   CA   C  N S 298 
PHE   C    C  N N 299 
PHE   O    O  N N 300 
PHE   CB   C  N N 301 
PHE   CG   C  Y N 302 
PHE   CD1  C  Y N 303 
PHE   CD2  C  Y N 304 
PHE   CE1  C  Y N 305 
PHE   CE2  C  Y N 306 
PHE   CZ   C  Y N 307 
PHE   OXT  O  N N 308 
PHE   H    H  N N 309 
PHE   H2   H  N N 310 
PHE   HA   H  N N 311 
PHE   HB2  H  N N 312 
PHE   HB3  H  N N 313 
PHE   HD1  H  N N 314 
PHE   HD2  H  N N 315 
PHE   HE1  H  N N 316 
PHE   HE2  H  N N 317 
PHE   HZ   H  N N 318 
PHE   HXT  H  N N 319 
PRO   N    N  N N 320 
PRO   CA   C  N S 321 
PRO   C    C  N N 322 
PRO   O    O  N N 323 
PRO   CB   C  N N 324 
PRO   CG   C  N N 325 
PRO   CD   C  N N 326 
PRO   OXT  O  N N 327 
PRO   H    H  N N 328 
PRO   HA   H  N N 329 
PRO   HB2  H  N N 330 
PRO   HB3  H  N N 331 
PRO   HG2  H  N N 332 
PRO   HG3  H  N N 333 
PRO   HD2  H  N N 334 
PRO   HD3  H  N N 335 
PRO   HXT  H  N N 336 
SER   N    N  N N 337 
SER   CA   C  N S 338 
SER   C    C  N N 339 
SER   O    O  N N 340 
SER   CB   C  N N 341 
SER   OG   O  N N 342 
SER   OXT  O  N N 343 
SER   H    H  N N 344 
SER   H2   H  N N 345 
SER   HA   H  N N 346 
SER   HB2  H  N N 347 
SER   HB3  H  N N 348 
SER   HG   H  N N 349 
SER   HXT  H  N N 350 
THR   N    N  N N 351 
THR   CA   C  N S 352 
THR   C    C  N N 353 
THR   O    O  N N 354 
THR   CB   C  N R 355 
THR   OG1  O  N N 356 
THR   CG2  C  N N 357 
THR   OXT  O  N N 358 
THR   H    H  N N 359 
THR   H2   H  N N 360 
THR   HA   H  N N 361 
THR   HB   H  N N 362 
THR   HG1  H  N N 363 
THR   HG21 H  N N 364 
THR   HG22 H  N N 365 
THR   HG23 H  N N 366 
THR   HXT  H  N N 367 
TRP   N    N  N N 368 
TRP   CA   C  N S 369 
TRP   C    C  N N 370 
TRP   O    O  N N 371 
TRP   CB   C  N N 372 
TRP   CG   C  Y N 373 
TRP   CD1  C  Y N 374 
TRP   CD2  C  Y N 375 
TRP   NE1  N  Y N 376 
TRP   CE2  C  Y N 377 
TRP   CE3  C  Y N 378 
TRP   CZ2  C  Y N 379 
TRP   CZ3  C  Y N 380 
TRP   CH2  C  Y N 381 
TRP   OXT  O  N N 382 
TRP   H    H  N N 383 
TRP   H2   H  N N 384 
TRP   HA   H  N N 385 
TRP   HB2  H  N N 386 
TRP   HB3  H  N N 387 
TRP   HD1  H  N N 388 
TRP   HE1  H  N N 389 
TRP   HE3  H  N N 390 
TRP   HZ2  H  N N 391 
TRP   HZ3  H  N N 392 
TRP   HH2  H  N N 393 
TRP   HXT  H  N N 394 
TYR   N    N  N N 395 
TYR   CA   C  N S 396 
TYR   C    C  N N 397 
TYR   O    O  N N 398 
TYR   CB   C  N N 399 
TYR   CG   C  Y N 400 
TYR   CD1  C  Y N 401 
TYR   CD2  C  Y N 402 
TYR   CE1  C  Y N 403 
TYR   CE2  C  Y N 404 
TYR   CZ   C  Y N 405 
TYR   OH   O  N N 406 
TYR   OXT  O  N N 407 
TYR   H    H  N N 408 
TYR   H2   H  N N 409 
TYR   HA   H  N N 410 
TYR   HB2  H  N N 411 
TYR   HB3  H  N N 412 
TYR   HD1  H  N N 413 
TYR   HD2  H  N N 414 
TYR   HE1  H  N N 415 
TYR   HE2  H  N N 416 
TYR   HH   H  N N 417 
TYR   HXT  H  N N 418 
VAL   N    N  N N 419 
VAL   CA   C  N S 420 
VAL   C    C  N N 421 
VAL   O    O  N N 422 
VAL   CB   C  N N 423 
VAL   CG1  C  N N 424 
VAL   CG2  C  N N 425 
VAL   OXT  O  N N 426 
VAL   H    H  N N 427 
VAL   H2   H  N N 428 
VAL   HA   H  N N 429 
VAL   HB   H  N N 430 
VAL   HG11 H  N N 431 
VAL   HG12 H  N N 432 
VAL   HG13 H  N N 433 
VAL   HG21 H  N N 434 
VAL   HG22 H  N N 435 
VAL   HG23 H  N N 436 
VAL   HXT  H  N N 437 
ZN    ZN   ZN N N 438 
# 
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 
A1BOE C   O    sing N N 1   
A1BOE O   C1   sing N N 2   
A1BOE C1  C2   doub Y N 3   
A1BOE C2  C3   sing Y N 4   
A1BOE C3  C4   doub Y N 5   
A1BOE C4  C5   sing Y N 6   
A1BOE C5  C6   doub Y N 7   
A1BOE C1  C6   sing Y N 8   
A1BOE C6  C7   sing N N 9   
A1BOE C7  N    sing N N 10  
A1BOE N   C8   sing N N 11  
A1BOE C8  C9   sing N N 12  
A1BOE C10 C9   sing N N 13  
A1BOE N1  C10  sing N N 14  
A1BOE O1  C10  doub N N 15  
A1BOE C9  C11  sing N N 16  
A1BOE C11 C12  sing N N 17  
A1BOE C12 C13  sing N N 18  
A1BOE N   C13  sing N N 19  
A1BOE C13 O2   doub N N 20  
A1BOE N1  H13  sing N N 21  
A1BOE N1  H12  sing N N 22  
A1BOE C4  H6   sing N N 23  
A1BOE C5  H7   sing N N 24  
A1BOE C7  H9   sing N N 25  
A1BOE C7  H8   sing N N 26  
A1BOE C8  H11  sing N N 27  
A1BOE C8  H10  sing N N 28  
A1BOE C12 H17  sing N N 29  
A1BOE C12 H16  sing N N 30  
A1BOE C11 H15  sing N N 31  
A1BOE C11 H14  sing N N 32  
A1BOE C9  H    sing N N 33  
A1BOE C   H3   sing N N 34  
A1BOE C   H2   sing N N 35  
A1BOE C   H1   sing N N 36  
A1BOE C3  H5   sing N N 37  
A1BOE C2  H4   sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
DMS   S   O    doub N N 121 
DMS   S   C1   sing N N 122 
DMS   S   C2   sing N N 123 
DMS   C1  H11  sing N N 124 
DMS   C1  H12  sing N N 125 
DMS   C1  H13  sing N N 126 
DMS   C2  H21  sing N N 127 
DMS   C2  H22  sing N N 128 
DMS   C2  H23  sing N N 129 
GLN   N   CA   sing N N 130 
GLN   N   H    sing N N 131 
GLN   N   H2   sing N N 132 
GLN   CA  C    sing N N 133 
GLN   CA  CB   sing N N 134 
GLN   CA  HA   sing N N 135 
GLN   C   O    doub N N 136 
GLN   C   OXT  sing N N 137 
GLN   CB  CG   sing N N 138 
GLN   CB  HB2  sing N N 139 
GLN   CB  HB3  sing N N 140 
GLN   CG  CD   sing N N 141 
GLN   CG  HG2  sing N N 142 
GLN   CG  HG3  sing N N 143 
GLN   CD  OE1  doub N N 144 
GLN   CD  NE2  sing N N 145 
GLN   NE2 HE21 sing N N 146 
GLN   NE2 HE22 sing N N 147 
GLN   OXT HXT  sing N N 148 
GLU   N   CA   sing N N 149 
GLU   N   H    sing N N 150 
GLU   N   H2   sing N N 151 
GLU   CA  C    sing N N 152 
GLU   CA  CB   sing N N 153 
GLU   CA  HA   sing N N 154 
GLU   C   O    doub N N 155 
GLU   C   OXT  sing N N 156 
GLU   CB  CG   sing N N 157 
GLU   CB  HB2  sing N N 158 
GLU   CB  HB3  sing N N 159 
GLU   CG  CD   sing N N 160 
GLU   CG  HG2  sing N N 161 
GLU   CG  HG3  sing N N 162 
GLU   CD  OE1  doub N N 163 
GLU   CD  OE2  sing N N 164 
GLU   OE2 HE2  sing N N 165 
GLU   OXT HXT  sing N N 166 
GLY   N   CA   sing N N 167 
GLY   N   H    sing N N 168 
GLY   N   H2   sing N N 169 
GLY   CA  C    sing N N 170 
GLY   CA  HA2  sing N N 171 
GLY   CA  HA3  sing N N 172 
GLY   C   O    doub N N 173 
GLY   C   OXT  sing N N 174 
GLY   OXT HXT  sing N N 175 
HIS   N   CA   sing N N 176 
HIS   N   H    sing N N 177 
HIS   N   H2   sing N N 178 
HIS   CA  C    sing N N 179 
HIS   CA  CB   sing N N 180 
HIS   CA  HA   sing N N 181 
HIS   C   O    doub N N 182 
HIS   C   OXT  sing N N 183 
HIS   CB  CG   sing N N 184 
HIS   CB  HB2  sing N N 185 
HIS   CB  HB3  sing N N 186 
HIS   CG  ND1  sing Y N 187 
HIS   CG  CD2  doub Y N 188 
HIS   ND1 CE1  doub Y N 189 
HIS   ND1 HD1  sing N N 190 
HIS   CD2 NE2  sing Y N 191 
HIS   CD2 HD2  sing N N 192 
HIS   CE1 NE2  sing Y N 193 
HIS   CE1 HE1  sing N N 194 
HIS   NE2 HE2  sing N N 195 
HIS   OXT HXT  sing N N 196 
HOH   O   H1   sing N N 197 
HOH   O   H2   sing N N 198 
ILE   N   CA   sing N N 199 
ILE   N   H    sing N N 200 
ILE   N   H2   sing N N 201 
ILE   CA  C    sing N N 202 
ILE   CA  CB   sing N N 203 
ILE   CA  HA   sing N N 204 
ILE   C   O    doub N N 205 
ILE   C   OXT  sing N N 206 
ILE   CB  CG1  sing N N 207 
ILE   CB  CG2  sing N N 208 
ILE   CB  HB   sing N N 209 
ILE   CG1 CD1  sing N N 210 
ILE   CG1 HG12 sing N N 211 
ILE   CG1 HG13 sing N N 212 
ILE   CG2 HG21 sing N N 213 
ILE   CG2 HG22 sing N N 214 
ILE   CG2 HG23 sing N N 215 
ILE   CD1 HD11 sing N N 216 
ILE   CD1 HD12 sing N N 217 
ILE   CD1 HD13 sing N N 218 
ILE   OXT HXT  sing N N 219 
LEU   N   CA   sing N N 220 
LEU   N   H    sing N N 221 
LEU   N   H2   sing N N 222 
LEU   CA  C    sing N N 223 
LEU   CA  CB   sing N N 224 
LEU   CA  HA   sing N N 225 
LEU   C   O    doub N N 226 
LEU   C   OXT  sing N N 227 
LEU   CB  CG   sing N N 228 
LEU   CB  HB2  sing N N 229 
LEU   CB  HB3  sing N N 230 
LEU   CG  CD1  sing N N 231 
LEU   CG  CD2  sing N N 232 
LEU   CG  HG   sing N N 233 
LEU   CD1 HD11 sing N N 234 
LEU   CD1 HD12 sing N N 235 
LEU   CD1 HD13 sing N N 236 
LEU   CD2 HD21 sing N N 237 
LEU   CD2 HD22 sing N N 238 
LEU   CD2 HD23 sing N N 239 
LEU   OXT HXT  sing N N 240 
LYS   N   CA   sing N N 241 
LYS   N   H    sing N N 242 
LYS   N   H2   sing N N 243 
LYS   CA  C    sing N N 244 
LYS   CA  CB   sing N N 245 
LYS   CA  HA   sing N N 246 
LYS   C   O    doub N N 247 
LYS   C   OXT  sing N N 248 
LYS   CB  CG   sing N N 249 
LYS   CB  HB2  sing N N 250 
LYS   CB  HB3  sing N N 251 
LYS   CG  CD   sing N N 252 
LYS   CG  HG2  sing N N 253 
LYS   CG  HG3  sing N N 254 
LYS   CD  CE   sing N N 255 
LYS   CD  HD2  sing N N 256 
LYS   CD  HD3  sing N N 257 
LYS   CE  NZ   sing N N 258 
LYS   CE  HE2  sing N N 259 
LYS   CE  HE3  sing N N 260 
LYS   NZ  HZ1  sing N N 261 
LYS   NZ  HZ2  sing N N 262 
LYS   NZ  HZ3  sing N N 263 
LYS   OXT HXT  sing N N 264 
MET   N   CA   sing N N 265 
MET   N   H    sing N N 266 
MET   N   H2   sing N N 267 
MET   CA  C    sing N N 268 
MET   CA  CB   sing N N 269 
MET   CA  HA   sing N N 270 
MET   C   O    doub N N 271 
MET   C   OXT  sing N N 272 
MET   CB  CG   sing N N 273 
MET   CB  HB2  sing N N 274 
MET   CB  HB3  sing N N 275 
MET   CG  SD   sing N N 276 
MET   CG  HG2  sing N N 277 
MET   CG  HG3  sing N N 278 
MET   SD  CE   sing N N 279 
MET   CE  HE1  sing N N 280 
MET   CE  HE2  sing N N 281 
MET   CE  HE3  sing N N 282 
MET   OXT HXT  sing N N 283 
PHE   N   CA   sing N N 284 
PHE   N   H    sing N N 285 
PHE   N   H2   sing N N 286 
PHE   CA  C    sing N N 287 
PHE   CA  CB   sing N N 288 
PHE   CA  HA   sing N N 289 
PHE   C   O    doub N N 290 
PHE   C   OXT  sing N N 291 
PHE   CB  CG   sing N N 292 
PHE   CB  HB2  sing N N 293 
PHE   CB  HB3  sing N N 294 
PHE   CG  CD1  doub Y N 295 
PHE   CG  CD2  sing Y N 296 
PHE   CD1 CE1  sing Y N 297 
PHE   CD1 HD1  sing N N 298 
PHE   CD2 CE2  doub Y N 299 
PHE   CD2 HD2  sing N N 300 
PHE   CE1 CZ   doub Y N 301 
PHE   CE1 HE1  sing N N 302 
PHE   CE2 CZ   sing Y N 303 
PHE   CE2 HE2  sing N N 304 
PHE   CZ  HZ   sing N N 305 
PHE   OXT HXT  sing N N 306 
PRO   N   CA   sing N N 307 
PRO   N   CD   sing N N 308 
PRO   N   H    sing N N 309 
PRO   CA  C    sing N N 310 
PRO   CA  CB   sing N N 311 
PRO   CA  HA   sing N N 312 
PRO   C   O    doub N N 313 
PRO   C   OXT  sing N N 314 
PRO   CB  CG   sing N N 315 
PRO   CB  HB2  sing N N 316 
PRO   CB  HB3  sing N N 317 
PRO   CG  CD   sing N N 318 
PRO   CG  HG2  sing N N 319 
PRO   CG  HG3  sing N N 320 
PRO   CD  HD2  sing N N 321 
PRO   CD  HD3  sing N N 322 
PRO   OXT HXT  sing N N 323 
SER   N   CA   sing N N 324 
SER   N   H    sing N N 325 
SER   N   H2   sing N N 326 
SER   CA  C    sing N N 327 
SER   CA  CB   sing N N 328 
SER   CA  HA   sing N N 329 
SER   C   O    doub N N 330 
SER   C   OXT  sing N N 331 
SER   CB  OG   sing N N 332 
SER   CB  HB2  sing N N 333 
SER   CB  HB3  sing N N 334 
SER   OG  HG   sing N N 335 
SER   OXT HXT  sing N N 336 
THR   N   CA   sing N N 337 
THR   N   H    sing N N 338 
THR   N   H2   sing N N 339 
THR   CA  C    sing N N 340 
THR   CA  CB   sing N N 341 
THR   CA  HA   sing N N 342 
THR   C   O    doub N N 343 
THR   C   OXT  sing N N 344 
THR   CB  OG1  sing N N 345 
THR   CB  CG2  sing N N 346 
THR   CB  HB   sing N N 347 
THR   OG1 HG1  sing N N 348 
THR   CG2 HG21 sing N N 349 
THR   CG2 HG22 sing N N 350 
THR   CG2 HG23 sing N N 351 
THR   OXT HXT  sing N N 352 
TRP   N   CA   sing N N 353 
TRP   N   H    sing N N 354 
TRP   N   H2   sing N N 355 
TRP   CA  C    sing N N 356 
TRP   CA  CB   sing N N 357 
TRP   CA  HA   sing N N 358 
TRP   C   O    doub N N 359 
TRP   C   OXT  sing N N 360 
TRP   CB  CG   sing N N 361 
TRP   CB  HB2  sing N N 362 
TRP   CB  HB3  sing N N 363 
TRP   CG  CD1  doub Y N 364 
TRP   CG  CD2  sing Y N 365 
TRP   CD1 NE1  sing Y N 366 
TRP   CD1 HD1  sing N N 367 
TRP   CD2 CE2  doub Y N 368 
TRP   CD2 CE3  sing Y N 369 
TRP   NE1 CE2  sing Y N 370 
TRP   NE1 HE1  sing N N 371 
TRP   CE2 CZ2  sing Y N 372 
TRP   CE3 CZ3  doub Y N 373 
TRP   CE3 HE3  sing N N 374 
TRP   CZ2 CH2  doub Y N 375 
TRP   CZ2 HZ2  sing N N 376 
TRP   CZ3 CH2  sing Y N 377 
TRP   CZ3 HZ3  sing N N 378 
TRP   CH2 HH2  sing N N 379 
TRP   OXT HXT  sing N N 380 
TYR   N   CA   sing N N 381 
TYR   N   H    sing N N 382 
TYR   N   H2   sing N N 383 
TYR   CA  C    sing N N 384 
TYR   CA  CB   sing N N 385 
TYR   CA  HA   sing N N 386 
TYR   C   O    doub N N 387 
TYR   C   OXT  sing N N 388 
TYR   CB  CG   sing N N 389 
TYR   CB  HB2  sing N N 390 
TYR   CB  HB3  sing N N 391 
TYR   CG  CD1  doub Y N 392 
TYR   CG  CD2  sing Y N 393 
TYR   CD1 CE1  sing Y N 394 
TYR   CD1 HD1  sing N N 395 
TYR   CD2 CE2  doub Y N 396 
TYR   CD2 HD2  sing N N 397 
TYR   CE1 CZ   doub Y N 398 
TYR   CE1 HE1  sing N N 399 
TYR   CE2 CZ   sing Y N 400 
TYR   CE2 HE2  sing N N 401 
TYR   CZ  OH   sing N N 402 
TYR   OH  HH   sing N N 403 
TYR   OXT HXT  sing N N 404 
VAL   N   CA   sing N N 405 
VAL   N   H    sing N N 406 
VAL   N   H2   sing N N 407 
VAL   CA  C    sing N N 408 
VAL   CA  CB   sing N N 409 
VAL   CA  HA   sing N N 410 
VAL   C   O    doub N N 411 
VAL   C   OXT  sing N N 412 
VAL   CB  CG1  sing N N 413 
VAL   CB  CG2  sing N N 414 
VAL   CB  HB   sing N N 415 
VAL   CG1 HG11 sing N N 416 
VAL   CG1 HG12 sing N N 417 
VAL   CG1 HG13 sing N N 418 
VAL   CG2 HG21 sing N N 419 
VAL   CG2 HG22 sing N N 420 
VAL   CG2 HG23 sing N N 421 
VAL   OXT HXT  sing N N 422 
# 
_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_1002329 
_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.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7HX2 
_atom_sites.fract_transf_matrix[1][1]   0.013680 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000683 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016385 
_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]   0.030716 
_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   ? 19.145 6.422   24.069 1.00 33.27 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.327 6.452   23.203 1.00 34.07 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.338 5.305   22.185 1.00 33.10 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.561 4.348   22.310 1.00 33.47 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.605 6.481   24.048 1.00 36.82 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.931 5.190   24.539 1.00 40.14 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.194 5.420   21.174 1.00 31.64 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.321 4.414   20.136 1.00 30.83 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.646 5.005   18.772 1.00 30.24 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.267 6.149   18.467 1.00 29.59 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.404 4.249   17.982 1.00 29.72 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.789 4.664   16.641 1.00 30.39 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.738 3.482   15.651 1.00 29.71 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.733 2.326   16.070 1.00 29.36 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.199 5.255   16.676 1.00 31.20 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.732 3.785   14.346 1.00 28.31 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.809 2.822   13.258 1.00 29.18 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.184 3.013   12.628 1.00 30.44 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.589 4.142   12.356 1.00 30.47 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.700 3.060   12.190 1.00 28.73 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.293 3.110   12.807 1.00 28.46 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.781 2.011   11.070 1.00 30.21 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.237 3.759   11.830 1.00 29.39 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.903 1.915   12.395 1.00 31.29 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.223 1.981   11.792 1.00 32.52 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.187 1.232   10.490 1.00 34.34 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.107 0.000   10.501 1.00 35.40 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.266 1.350   12.733 1.00 32.27 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.462 2.162   13.987 1.00 32.18 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.293 3.272   13.996 1.00 32.78 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.745 1.880   15.136 1.00 32.78 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.459 4.039   15.145 1.00 33.47 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.867 2.663   16.272 1.00 33.74 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.721 3.744   16.270 1.00 33.86 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.840 4.481   17.400 1.00 35.05 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.228 1.959   9.372  1.00 34.43 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.215 1.372   8.033  1.00 35.39 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.357 1.999   7.238  1.00 36.66 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.457 3.229   7.193  1.00 37.24 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.840 1.558   7.343  1.00 35.82 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.357 3.006   7.423  1.00 35.73 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.868 1.062   5.900  1.00 37.18 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.258 1.173   6.697  1.00 36.62 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.420 1.650   5.949  1.00 37.51 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.251 2.657   6.725  1.00 38.42 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.521 2.439   7.907  1.00 39.16 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.559 3.810   6.123  1.00 38.46 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.303 4.851   6.844  1.00 38.38 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.359 5.873   7.500  1.00 37.04 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.768 7.016   7.727  1.00 37.79 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.293 5.540   5.916  1.00 40.79 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.503 4.692   5.620  1.00 47.21 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 33.930 3.858   6.435  1.00 49.24 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 34.112 4.912   4.458  1.00 49.00 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.119 5.459   7.848  1.00 34.79 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.133 6.375   8.431  1.00 33.09 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.600 5.960   9.783  1.00 31.03 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.436 4.779   10.067 1.00 30.89 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.931 6.568   7.475  1.00 32.94 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.295 7.153   6.131  1.00 33.95 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.798 8.441   6.026  1.00 35.26 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.062 6.448   4.957  1.00 34.75 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.104 8.996   4.789  1.00 36.01 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.343 7.002   3.713  1.00 35.74 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.885 8.268   3.636  1.00 36.81 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.178 8.825   2.414  1.00 38.94 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.254 6.956   10.589 1.00 28.89 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.635 6.763   11.887 1.00 27.79 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.343 7.600   11.846 1.00 26.38 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.404 8.793   11.597 1.00 25.55 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.578 7.267   13.007 1.00 29.21 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.925 7.400   14.383 1.00 32.53 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.963 7.698   15.462 1.00 34.44 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.533 8.719   16.421 1.00 34.98 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 27.126 8.462   17.663 1.00 36.99 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 27.092 7.216   18.114 1.00 36.70 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.779 9.455   18.472 1.00 36.59 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.188 6.984   12.074 1.00 26.15 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.899 7.694   12.062 1.00 26.32 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.396 7.799   13.492 1.00 27.10 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.247 6.767   14.158 1.00 27.51 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.856 6.941   11.214 1.00 26.66 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.550 7.769   11.103 1.00 26.88 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.421 6.605   9.830  1.00 26.68 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.124 9.020   13.966 1.00 25.48 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.624 9.192   15.344 1.00 25.46 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.407 10.147  15.328 1.00 24.76 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.181 10.844  14.329 1.00 24.46 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.736 9.798   16.253 1.00 26.90 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.824 8.779   16.574 1.00 28.14 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.320 11.065  15.632 1.00 26.94 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.678 10.264  16.464 1.00 23.19 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.634 11.299  16.593 1.00 23.30 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.398 12.634  16.604 1.00 24.42 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.368 12.777  17.369 1.00 26.40 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.915 11.184  17.959 1.00 22.43 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.068 9.943   18.071 1.00 26.46 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.567 8.870   18.438 1.00 28.67 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.791 10.054  17.725 1.00 24.52 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.976 13.600  15.794 1.00 23.81 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.666 14.888  15.730 1.00 24.43 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.798 15.557  17.110 1.00 25.36 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.855 16.144  17.392 1.00 26.26 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.959 15.835  14.750 1.00 24.72 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.703 17.150  14.467 1.00 25.03 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.714 18.052  13.719 1.00 25.47 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.283 19.268  13.134 1.00 26.97 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.399 20.426  13.767 1.00 30.25 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 19.099 20.519  15.064 1.00 30.46 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.866 21.492  13.127 1.00 30.98 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.761 15.421  17.985 1.00 25.56 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.798 16.064  19.310 1.00 27.52 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.796 15.416  20.316 1.00 28.49 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 20.157 16.033  21.349 1.00 28.56 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 17.383 16.183  19.927 1.00 28.96 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.786 14.893  20.393 1.00 29.55 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 16.157 14.020  19.501 1.00 29.93 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.732 14.366  21.647 1.00 29.61 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.728 13.006  20.239 1.00 31.20 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 16.049 13.165  21.544 1.00 30.65 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 20.250 14.191  20.001 1.00 28.43 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 21.225 13.474  20.806 1.00 30.19 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.629 13.497  20.174 1.00 30.86 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.545 12.925  20.764 1.00 30.89 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.767 12.014  21.022 1.00 30.35 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.430 11.831  21.766 1.00 31.42 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 19.185 10.367  22.071 1.00 31.09 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.388 12.654  23.094 1.00 31.32 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.812 14.126  18.977 1.00 30.76 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 24.129 14.143  18.348 1.00 31.35 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 25.190 14.791  19.246 1.00 31.97 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.890 15.749  19.940 1.00 31.81 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 24.068 14.877  17.019 1.00 30.98 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.404 14.248  19.261 1.00 32.81 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.493 14.787  20.092 1.00 34.47 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.320 15.861  19.327 1.00 35.10 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 28.100 16.071  18.134 1.00 35.31 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.384 13.611  20.587 1.00 36.05 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 29.111 13.119  19.465 1.00 37.85 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.580 12.479  21.213 1.00 36.73 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.303 16.514  19.986 1.00 35.48 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 30.195 17.461  19.319 1.00 36.88 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.945 16.769  18.166 1.00 36.24 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 31.144 17.369  17.120 1.00 36.29 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.231 18.030  20.320 1.00 39.59 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.638 18.820  21.441 1.00 46.53 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 30.032 20.038  21.220 1.00 49.95 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 30.678 18.589  22.777 1.00 50.00 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 29.695 20.501  22.415 1.00 51.30 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 30.061 19.660  23.386 1.00 51.86 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.363 15.510  18.368 1.00 35.93 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 32.059 14.758  17.326 1.00 36.83 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.176 14.485  16.103 1.00 34.64 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.661 14.564  14.971 1.00 33.55 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.625 13.456  17.901 1.00 41.47 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.465 12.670  16.913 1.00 49.58 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.670 12.898  16.781 1.00 52.29 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 32.855 11.713  16.213 1.00 51.49 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.871 14.194  16.312 1.00 33.93 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.926 14.014  15.202 1.00 33.03 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.832 15.313  14.390 1.00 32.22 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.933 15.280  13.162 1.00 31.27 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.527 13.645  15.722 1.00 33.68 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.415 12.226  16.236 1.00 35.04 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.962 11.332  15.596 1.00 35.64 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.767 12.021  17.283 1.00 35.72 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.703 16.461  15.071 1.00 32.38 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.602 17.746  14.362 1.00 33.76 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.914 18.143  13.653 1.00 35.18 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.877 18.805  12.623 1.00 35.68 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.137 18.848  15.326 1.00 33.27 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.648 18.882  15.484 1.00 32.12 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.920 18.400  16.530 1.00 32.44 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.706 19.442  14.561 1.00 31.07 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.578 18.628  16.314 1.00 32.43 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.422 19.284  15.121 1.00 31.67 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.826 20.076  13.321 1.00 30.85 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.268 19.741  14.484 1.00 31.14 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.685 20.531  12.694 1.00 30.91 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.421 20.329  13.256 1.00 31.04 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.062 17.726  14.203 1.00 35.59 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.369 18.008  13.610 1.00 36.02 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.658 17.128  12.378 1.00 35.46 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.584 17.434  11.627 1.00 36.04 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.467 17.815  14.650 1.00 36.31 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.927 16.001  12.215 1.00 33.53 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.071 15.085  11.079 1.00 32.34 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.712 14.942  10.365 1.00 31.53 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.320 13.843  9.960  1.00 30.23 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.534 13.727  11.600 1.00 33.45 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.941 13.792  12.123 1.00 36.39 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.893 13.929  11.349 1.00 38.81 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.096 13.712  13.444 1.00 35.61 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.967 16.057  10.261 1.00 30.96 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.622 16.080  9.716  1.00 30.32 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.592 15.707  8.256  1.00 30.74 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.367 16.265  7.484  1.00 31.69 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.047 17.505  9.901  1.00 29.93 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.645 17.773  9.372  1.00 30.15 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.610 16.859  10.031 1.00 29.91 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.264 19.255  9.537  1.00 30.38 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.668 14.793  7.865  1.00 29.50 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.411 14.411  6.468  1.00 29.72 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.080 15.084  6.004  1.00 29.63 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 25.990 15.689  4.922  1.00 29.22 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.292 12.871  6.317  1.00 30.18 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.812 12.494  4.907  1.00 30.21 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.604 12.174  6.678  1.00 30.97 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.051 14.963  6.853  1.00 29.30 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.699 15.424  6.573  1.00 29.00 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.899 15.524  7.881  1.00 27.90 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.106 14.743  8.811  1.00 27.92 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.026 14.393  5.626  1.00 29.27 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.564 14.632  5.376  1.00 30.33 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.016 15.611  4.602  1.00 31.82 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.466 13.932  5.977  1.00 30.28 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.642 15.527  4.642  1.00 32.29 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.280 14.521  5.498  1.00 31.28 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.369 12.884  6.897  1.00 30.61 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.020 14.040  5.842  1.00 31.21 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.117 12.408  7.232  1.00 30.99 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 17.962 13.006  6.734  1.00 30.84 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.001 16.500  7.961  1.00 26.64 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.115 16.614  9.118  1.00 26.06 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.780 17.207  8.672  1.00 25.46 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.744 18.024  7.749  1.00 23.86 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.749 17.380  10.306 1.00 27.55 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.323 18.755  9.973  1.00 28.27 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.321 19.886  9.877  1.00 30.91 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.602 20.874  9.159  1.00 33.95 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.238 19.773  10.492 1.00 30.04 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.693 16.796  9.320  1.00 25.83 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.377 17.343  9.011  1.00 26.63 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.587 17.527  10.291 1.00 27.03 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.120 16.553  10.846 1.00 27.66 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.625 16.467  7.993  1.00 28.34 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.420 17.161  7.405  1.00 32.89 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.787 17.957  8.122  1.00 34.67 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.094 16.891  6.230  1.00 33.94 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.460 18.769  10.774 1.00 26.84 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.741 19.078  12.010 0.50 27.36 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.748 19.023  12.030 0.50 26.99 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.276 18.612  11.924 1.00 27.21 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.713 18.118  12.897 1.00 25.82 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.793 20.580  12.265 0.50 29.47 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.866 20.485  12.434 0.50 28.06 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 15.004 20.960  13.379 0.50 32.84 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 15.289 21.307  11.436 0.50 29.70 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.670 18.757  10.731 1.00 26.37 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.280 18.356  10.563 1.00 26.78 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 12.101 16.840  10.691 1.00 25.95 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.993 16.417  10.983 1.00 26.84 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.689 18.918  9.268  1.00 28.66 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 11.841 18.012  8.188  1.00 33.58 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.180 16.028  10.522 1.00 24.08 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 13.117 14.563  10.682 1.00 22.57 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.720 14.061  11.996 1.00 23.10 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.642 12.860  12.281 1.00 23.61 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.859 13.844  9.530  1.00 22.25 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.244 14.103  8.197  1.00 23.21 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 13.993 13.446  7.042  1.00 25.11 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 13.965 11.977  7.108  1.00 24.53 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.027 11.176  6.040  1.00 25.67 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.093 11.691  4.813  1.00 25.13 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.003 9.858   6.190  1.00 26.43 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.407 14.936  12.758 1.00 23.45 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 15.130 14.541  13.977 1.00 22.66 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.248 13.568  13.630 1.00 22.30 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.569 12.713  14.442 1.00 23.53 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.221 13.986  15.092 1.00 23.67 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.966 13.722  16.395 1.00 26.03 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.836 14.558  16.772 1.00 24.11 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.726 12.667  17.012 1.00 25.61 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.887 13.724  12.445 1.00 22.32 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.996 12.838  12.071 1.00 22.97 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.291 13.615  11.848 1.00 24.50 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.271 14.751  11.383 1.00 25.34 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.710 12.058  10.788 1.00 22.30 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.729 10.864  10.890 1.00 22.71 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.667 10.130  9.538  1.00 21.14 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.152 9.852   11.989 1.00 23.43 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.415 12.963  12.134 1.00 24.17 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.731 13.501  11.837 1.00 24.82 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.606 12.302  11.452 1.00 25.67 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.543 11.257  12.086 1.00 26.85 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.352 14.299  13.027 1.00 24.57 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.755 14.904  12.760 1.00 26.22 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.928 16.274  13.403 1.00 25.64 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.886 13.922  13.142 1.00 28.33 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.387 12.443  10.404 1.00 26.35 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.318 11.429  9.957  1.00 26.12 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.722 12.030  10.025 1.00 26.85 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.951 13.156  9.547  1.00 26.88 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 23.992 10.945  8.514  1.00 26.42 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.062 9.971   8.019  1.00 26.45 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.601 10.317  8.448  1.00 27.04 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.647 11.293  10.630 1.00 27.07 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.052 11.685  10.720 1.00 28.05 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.942 10.579  10.130 1.00 30.11 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.482 9.446   9.928  1.00 29.18 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.454 12.010  12.159 1.00 28.14 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.278 10.910  13.042 1.00 28.53 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.191 10.931  9.777  1.00 32.19 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.101 9.951   9.203  1.00 35.52 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.925 9.234   10.287 1.00 38.38 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.171 9.781   11.366 1.00 38.51 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.000 10.597  8.158  1.00 37.21 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.684 11.697  8.731  1.00 40.66 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.308 7.989   10.012 1.00 40.59 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.115 7.166   10.921 1.00 42.99 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.349 6.638   10.161 1.00 45.98 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.344 6.560   8.927  1.00 46.26 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.304 5.949   11.453 1.00 44.21 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.056 5.034   10.384 1.00 46.04 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 31.007 6.338   12.114 1.00 44.10 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.375 6.226   10.900 1.00 47.82 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.590 5.647   10.330 1.00 50.15 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.401 4.118   10.205 1.00 52.30 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 36.814 3.517   9.210  1.00 53.03 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.815 6.030   11.194 1.00 51.72 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.520 5.787   12.576 1.00 53.17 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 38.215 7.483   11.024 1.00 51.91 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.777 3.492   11.215 1.00 52.74 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.504 2.056   11.192 1.00 53.45 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.322 1.755   10.271 1.00 54.05 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.427 2.589   10.132 1.00 54.17 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.205 1.566   12.599 1.00 53.76 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.308 0.571   9.639  1.00 54.24 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.220 0.211   8.724  1.00 54.64 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.067 -0.495  9.450  1.00 53.48 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.265 -1.541  10.062 1.00 53.71 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.745 -0.667  7.578  1.00 57.56 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 32.967 -0.512  6.268  1.00 63.19 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 33.480 0.642   5.435  1.00 69.50 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 34.644 1.064   5.549  1.00 71.85 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 32.626 1.184   4.567  1.00 69.97 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.876 0.089   9.366  1.00 51.47 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.660 -0.442  9.972  1.00 49.72 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 29.069 -1.571  9.156  1.00 47.40 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.321 -1.664  7.947  1.00 46.92 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.289 -2.442  9.805  1.00 45.80 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.727 -3.582  9.088  1.00 45.42 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.228 -3.828  9.369  1.00 43.08 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.742 -4.941  9.135  1.00 43.29 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.569 -4.840  9.294  1.00 47.76 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 29.258 -5.022  10.964 1.00 56.19 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.476 -2.766  9.764  1.00 40.30 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.022 -2.864  9.893  1.00 38.50 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.448 -2.883  8.454  1.00 37.08 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.002 -2.260  7.540  1.00 36.88 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.422 -1.657  10.650 1.00 39.67 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.394 -1.774  12.166 1.00 43.58 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 22.989 -2.840  12.669 1.00 45.76 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.763 -0.783  12.852 1.00 43.53 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.334 -3.574  8.265  1.00 35.85 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.678 -3.645  6.967  1.00 35.42 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.461 -2.716  6.964  1.00 33.04 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.610 -2.871  7.834  1.00 32.80 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.258 -5.092  6.718  1.00 37.97 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.447 -5.867  6.511  1.00 39.38 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.338 -5.227  5.512  1.00 38.97 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.366 -1.753  6.022  1.00 30.65 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.174 -0.890  5.965  1.00 28.80 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.080 -1.580  5.151  1.00 28.66 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.356 -2.058  4.041  1.00 29.47 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.462 0.526   5.411  1.00 28.72 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.688 1.193   6.080  1.00 29.39 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.210 1.418   5.516  1.00 28.32 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.501 1.465   7.640  1.00 30.01 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.847 -1.624  5.656  1.00 27.52 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.735 -2.224  4.906  1.00 27.49 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.349 -1.284  3.733  1.00 27.14 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.381 -0.061  3.891  1.00 25.97 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.538 -2.399  5.822  1.00 27.39 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.034 -1.852  2.568  1.00 27.89 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.554 -1.115  1.396  1.00 28.73 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.232 -1.833  1.075  1.00 29.94 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.243 -2.895  0.437  1.00 30.11 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.572 -1.220  0.250  1.00 29.91 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 16.957 -0.660  0.635  1.00 33.27 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 16.971 0.827   1.073  1.00 33.45 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.328 1.267   1.399  1.00 33.10 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.620 2.399   2.036  1.00 32.77 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.651 3.225   2.417  1.00 30.91 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 19.878 2.702   2.317  1.00 31.96 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.124 -1.331  1.648  1.00 29.85 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.836 -2.025  1.607  1.00 30.59 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.699  -1.065  2.043  1.00 30.99 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 9.935  0.061   2.496  1.00 30.76 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 10.915 -3.196  2.584  1.00 32.32 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 10.938 -2.661  4.333  1.00 32.76 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.469  -1.597  2.071  1.00 31.57 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.336  -0.858  2.590  1.00 32.46 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.671  -1.635  3.729  1.00 32.65 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.481  -1.457  3.935  1.00 33.70 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.327  -0.466  1.490  1.00 35.16 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.649  -1.632  0.799  1.00 43.59 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 5.904  -2.797  1.196  1.00 44.41 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.871  -1.387  -0.157 1.00 48.69 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.435  -2.459  4.489  1.00 31.62 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 6.944  -3.214  5.660  1.00 30.85 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.181  -2.267  6.625  1.00 30.20 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.599  -1.127  6.823  1.00 30.77 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.117  -3.872  6.407  1.00 31.37 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.809  -5.367  5.629  1.00 30.95 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.118  -2.745  7.249  1.00 28.24 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.439  -2.013  8.311  1.00 27.67 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.351  -2.819  9.586  1.00 27.12 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.555  -2.489  10.454 1.00 26.98 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.058  -1.491  7.906  1.00 29.50 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 3.097  -0.319  6.957  1.00 32.20 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.685  0.161   6.698  1.00 37.37 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.163  0.064   5.575  1.00 40.48 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 1.014  0.655   7.743  1.00 34.62 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.191  -3.862  9.726  1.00 26.65 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.329  -4.667  10.925 1.00 26.91 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 6.838  -4.832  11.152 1.00 24.69 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.619  -4.943  10.205 1.00 24.79 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.656  -6.057  10.818 1.00 30.02 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.294  -6.812  9.788  1.00 33.03 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.159  -5.979  10.577 1.00 30.14 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.218  -4.896  12.413 1.00 23.00 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.609  -5.096  12.768 1.00 21.87 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.777  -5.225  14.268 1.00 22.11 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.813  -5.482  14.968 1.00 22.56 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 9.988  -5.050  14.748 1.00 21.66 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.311 -5.195  16.184 1.00 21.45 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.200 -4.033  16.609 1.00 21.44 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.167 -3.747  15.920 1.00 21.80 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 11.012 -6.557  16.441 1.00 22.16 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.525 -6.660  17.889 1.00 23.28 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.058 -7.711  16.146 1.00 23.26 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 10.935 -3.427  17.773 1.00 21.32 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.802 -2.333  18.229 1.00 21.57 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.345 -2.580  19.619 1.00 23.20 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.704 -3.258  20.405 1.00 23.38 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.096 -0.972  18.147 1.00 21.08 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.158 -0.658  19.292 1.00 21.95 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.871  -1.186  19.333 1.00 23.04 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.545 0.199   20.318 1.00 21.93 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 7.993  -0.865  20.369 1.00 24.09 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.682  0.514   21.366 1.00 23.17 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.413  -0.037  21.401 1.00 23.96 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.557  0.315   22.417 1.00 25.23 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.498 -1.976  19.922 1.00 22.92 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 14.090 -2.136  21.242 1.00 24.09 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.665 -0.964  22.118 1.00 24.39 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.791 0.201   21.708 1.00 23.00 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.615 -2.265  21.165 1.00 24.21 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.209 -2.399  22.542 1.00 25.40 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 15.944 -3.515  23.322 1.00 26.01 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 16.966 -1.375  23.099 1.00 26.70 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.458 -3.636  24.608 1.00 27.15 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.462 -1.472  24.400 1.00 27.33 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.190 -2.599  25.150 1.00 28.41 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.677 -2.729  26.415 1.00 29.76 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 13.131 -1.275  23.320 1.00 25.90 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.639 -0.280  24.268 1.00 27.77 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.521 -0.353  25.507 1.00 29.42 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.352 -1.262  26.343 1.00 29.51 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 11.174 -0.544  24.609 1.00 29.16 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.500 0.533   25.909 1.00 29.96 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.490 0.592   25.621 1.00 30.08 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.412 0.543   26.734 1.00 31.10 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 14.736 0.722   28.078 1.00 30.09 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 15.154 0.082   29.027 1.00 30.36 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.566 1.525   26.562 1.00 35.08 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 16.123 2.851   26.740 1.00 39.09 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.645 1.505   28.150 1.00 29.33 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 12.930 1.705   29.423 1.00 29.72 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 12.209 0.448   29.941 1.00 30.29 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 11.693 0.443   31.071 1.00 31.36 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 11.973 2.888   29.348 1.00 30.71 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 10.918 2.644   28.433 1.00 33.71 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 12.210 -0.631  29.139 1.00 29.65 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 11.658 -1.893  29.566 1.00 30.07 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 12.664 -3.032  29.415 1.00 31.48 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.315 -4.174  29.729 1.00 33.14 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.373 -2.220  28.789 1.00 31.07 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 9.196  -1.275  29.035 1.00 33.15 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.542  -1.559  30.391 1.00 34.80 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.390  -0.685  30.604 1.00 37.21 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.451  0.509   31.195 1.00 38.12 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.610  0.976   31.652 1.00 36.70 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.353  1.245   31.333 1.00 36.17 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 13.893 -2.763  28.894 1.00 31.01 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 14.911 -3.776  28.562 1.00 31.14 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.276 -4.918  27.748 1.00 30.17 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.514 -6.105  28.022 1.00 30.62 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 15.632 -4.308  29.804 1.00 32.88 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.745 -3.380  30.315 1.00 37.46 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.522 -4.072  31.430 1.00 42.09 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 18.105 -3.118  32.366 1.00 46.27 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 17.837 -3.090  33.673 1.00 48.40 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 16.974 -3.959  34.204 1.00 46.82 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.407 -2.179  34.454 1.00 47.58 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.404 -4.546  26.785 1.00 28.58 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.683 -5.564  26.009 1.00 27.58 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.531 -5.120  24.548 1.00 26.42 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.552 -3.930  24.249 1.00 25.24 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.234 -5.710  26.536 1.00 29.70 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 11.070 -6.533  27.820 1.00 37.48 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.606  -6.529  28.282 1.00 44.06 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.333  -7.523  29.398 1.00 49.96 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 10.136 -7.241  30.629 1.00 53.55 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.317 -6.096  23.677 1.00 26.30 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 11.979 -5.831  22.265 1.00 26.59 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.462 -6.105  22.150 1.00 26.43 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 9.943  -7.043  22.791 1.00 26.93 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 12.729 -6.781  21.301 1.00 28.13 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.217 -6.582  21.270 1.00 32.60 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 14.834 -5.819  20.276 1.00 35.46 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.166 -7.056  22.102 1.00 34.09 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.126 -5.851  20.550 1.00 34.93 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.376 -6.584  21.633 1.00 35.55 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 9.745  -5.272  21.392 1.00 24.78 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.324  -5.454  21.202 1.00 24.45 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 7.999  -5.549  19.723 1.00 24.71 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.440  -4.711  18.950 1.00 23.75 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.541  -4.261  21.736 1.00 24.26 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.550  -4.136  23.253 1.00 24.54 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 6.788  -4.987  24.051 1.00 26.18 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.283  -3.143  23.881 1.00 25.60 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 6.776  -4.863  25.452 1.00 27.64 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.268  -2.998  25.276 1.00 26.60 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.530  -3.875  26.057 1.00 28.24 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.505  -3.712  27.430 1.00 31.48 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.145  -6.513  19.339 1.00 24.98 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.681  -6.552  17.933 1.00 25.42 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.591  -5.457  17.773 1.00 25.61 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.759  -5.266  18.690 1.00 26.19 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 6.073  -7.956  17.806 1.00 26.01 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.594  -8.271  19.231 1.00 26.25 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.527  -7.568  20.182 1.00 25.12 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.603  -4.721  16.668 1.00 24.43 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.631  -3.642  16.452 1.00 24.75 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.167  -3.569  15.000 1.00 25.36 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 4.910  -3.918  14.069 1.00 25.39 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.251  -2.247  16.805 1.00 25.91 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.325  -1.999  18.317 1.00 26.56 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.607  -2.061  16.145 1.00 26.01 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 2.962  -3.005  14.802 1.00 25.80 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.448  -2.596  13.505 1.00 27.06 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.654  -1.072  13.517 1.00 25.98 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.396  -0.439  14.552 1.00 25.98 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 0.955  -2.870  13.384 1.00 30.45 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.754  -4.261  13.222 1.00 35.48 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.153  -0.494  12.422 1.00 25.48 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.396  0.934   12.384 1.00 25.13 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.868  1.559   11.098 1.00 27.20 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.686  0.871   10.092 1.00 27.18 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.898  1.256   12.618 1.00 24.65 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.863  0.516   11.718 1.00 24.86 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.405  -0.701  12.107 1.00 25.79 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.248  1.053   10.489 1.00 24.84 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.287  -1.384  11.276 1.00 26.69 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.149  0.385   9.672  1.00 26.00 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.665  -0.837  10.069 1.00 26.27 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.617  2.869   11.132 1.00 27.66 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.084  3.571   9.989  1.00 28.61 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.183  3.895   8.939  1.00 28.66 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.374  3.709   9.221  1.00 29.15 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.344  4.816   10.473 1.00 30.59 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.218  5.725   11.115 1.00 30.62 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.802  4.317   7.718  1.00 28.04 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.791  4.656   6.693  1.00 29.17 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.434  6.000   7.062  1.00 28.84 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.795  6.789   7.733  1.00 29.30 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 3.142  4.694   5.269  1.00 31.25 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.764  3.291   4.768  1.00 36.42 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.444  3.244   3.246  1.00 41.74 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 1.906  1.881   2.856  1.00 47.10 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 1.840  1.678   1.380  1.00 50.15 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.662  6.302   6.626  1.00 29.14 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.282  7.593   7.004  1.00 29.52 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.431  8.789   6.600  1.00 29.65 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 4.935  8.857   5.456  1.00 28.31 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.609  7.589   6.247  1.00 31.15 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.903  6.145   5.980  1.00 32.37 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.557  5.501   5.774  1.00 29.60 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 5.212  9.708   7.557  1.00 29.71 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.344  10.847  7.276  1.00 31.64 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.653  12.080  8.155  1.00 31.82 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.488  11.999  9.050  1.00 31.72 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 2.878  10.411  7.399  1.00 34.28 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.514  10.319  8.764  1.00 39.94 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 3.992  13.227  7.860  1.00 31.27 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 4.090  14.484  8.605  1.00 32.14 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 3.149  14.352  9.782  1.00 33.58 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 1.929  14.307  9.587  1.00 34.24 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.557  15.659  7.734  1.00 32.29 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.532  16.620  7.093  1.00 34.14 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 3.769  17.817  6.493  1.00 34.85 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 5.596  17.085  8.044  1.00 33.89 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.686  14.328  11.000 1.00 33.45 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 2.869  14.193  12.191 1.00 34.50 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 3.201  15.319  13.166 1.00 36.65 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.366  15.684  13.299 1.00 36.25 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 3.146  12.785  12.779 1.00 34.64 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.408  11.707  11.964 1.00 36.10 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 2.822  12.684  14.260 1.00 34.46 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 2.975  10.453  12.101 1.00 38.59 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 2.180  15.883  13.833 1.00 38.38 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.392  16.955  14.796 1.00 39.83 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 3.050  16.421  16.082 1.00 40.13 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 2.576  15.455  16.672 1.00 40.96 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 1.074  17.681  15.101 1.00 40.52 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 1.285  18.911  15.946 1.00 41.54 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 1.812  20.062  15.398 1.00 42.58 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 0.990  18.901  17.297 1.00 42.46 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 2.029  21.185  16.183 1.00 43.52 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 1.187  20.034  18.074 1.00 43.26 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 1.730  21.158  17.521 1.00 43.01 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 4.170  17.018  16.488 1.00 39.05 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 4.915  16.577  17.649 1.00 38.41 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 4.991  17.697  18.666 1.00 38.76 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 5.584  18.745  18.393 1.00 39.28 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 6.334  16.069  17.262 1.00 38.28 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 7.163  15.772  18.509 1.00 39.31 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 6.263  14.840  16.364 1.00 37.56 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 4.435  17.461  19.864 1.00 38.39 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 4.440  18.442  20.954 1.00 38.16 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 5.828  18.963  21.290 1.00 37.80 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 6.824  18.241  21.159 1.00 37.09 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 3.852  17.813  22.215 1.00 40.97 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 2.414  17.388  22.061 1.00 48.02 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 1.488  18.549  21.781 1.00 59.19 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 1.619  19.598  22.454 1.00 62.44 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 0.637  18.413  20.873 1.00 62.07 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 5.895  20.188  21.816 1.00 37.97 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 7.170  20.770  22.249 1.00 38.76 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 7.897  19.900  23.277 1.00 39.15 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 7.262  19.177  24.052 1.00 39.82 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 6.941  22.149  22.860 1.00 38.61 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 9.231  19.962  23.245 1.00 38.95 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 10.148 19.336  24.199 1.00 40.18 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 11.253 20.400  24.474 1.00 42.23 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 11.164 21.531  23.961 1.00 42.93 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 10.758 18.063  23.599 1.00 39.83 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 11.700 18.390  22.589 1.00 39.95 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 12.315 20.042  25.212 1.00 43.26 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 13.426 20.980  25.437 1.00 44.97 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 14.325 21.154  24.192 1.00 44.63 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 15.115 22.098  24.135 1.00 45.22 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 14.266 20.535  26.633 1.00 49.51 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 13.451 20.390  27.908 1.00 57.52 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 13.079 18.955  28.239 1.00 66.81 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 12.755 18.186  27.299 1.00 67.64 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 13.129 18.601  29.442 1.00 68.84 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 14.197 20.251  23.200 1.00 43.21 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 15.015 20.243  21.991 1.00 42.35 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 14.369 20.927  20.795 1.00 39.66 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 15.078 21.438  19.928 1.00 39.71 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 15.392 18.805  21.645 1.00 43.20 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 16.238 18.196  22.737 1.00 45.22 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 17.577 18.536  22.874 1.00 46.99 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 15.688 17.326  23.666 1.00 46.69 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 18.351 18.013  23.900 1.00 48.69 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 16.455 16.786  24.686 1.00 48.33 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 17.787 17.133  24.801 1.00 50.31 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 18.556 16.623  25.821 1.00 53.93 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 13.037 20.938  20.743 1.00 36.94 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 12.327 21.566  19.632 1.00 35.07 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 11.052 22.241  20.142 1.00 35.38 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 10.393 21.694  21.030 1.00 35.80 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 11.872 20.481  18.607 1.00 33.59 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 12.952 19.599  18.014 1.00 31.67 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 13.729 20.038  16.948 1.00 31.24 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 13.106 18.284  18.428 1.00 30.81 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 14.676 19.207  16.353 1.00 31.00 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 14.046 17.445  17.842 1.00 30.38 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 14.831 17.908  16.803 1.00 30.22 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 15.801 17.091  16.260 1.00 27.70 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 10.587 23.332  19.493 1.00 35.05 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 9.230  23.839  19.811 1.00 34.90 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 8.182  22.865  19.207 1.00 34.98 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 8.551  21.951  18.454 1.00 34.78 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 9.180  25.179  19.066 1.00 35.01 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 10.099 24.970  17.887 1.00 35.80 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 11.194 24.046  18.350 1.00 34.54 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 6.872  23.068  19.472 1.00 34.69 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 5.841  22.201  18.876 1.00 34.89 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 5.899  22.394  17.325 1.00 34.39 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 6.062  23.521  16.856 1.00 35.15 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 4.473  22.565  19.422 1.00 35.55 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 5.924  21.302  16.556 1.00 32.55 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 6.121  21.393  15.108 1.00 31.47 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.632  20.120  14.416 1.00 31.84 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 5.328  19.143  15.097 1.00 32.61 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.643  21.589  14.830 1.00 30.32 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 8.454  20.270  14.938 1.00 30.04 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 9.887  20.410  15.377 1.00 30.57 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.770 19.354  14.843 1.00 31.11 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 10.835 18.112  15.317 1.00 31.01 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 11.704 17.245  14.807 1.00 27.68 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 10.075 17.742  16.345 1.00 32.06 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 5.674  20.082  13.064 1.00 31.40 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 5.374  18.855  12.341 1.00 31.58 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.699  18.157  12.087 1.00 30.08 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.598  18.778  11.526 1.00 29.79 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.739  19.176  10.977 1.00 33.09 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 3.282  19.533  11.110 1.00 35.30 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 2.307  18.547  11.129 1.00 37.17 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 2.888  20.841  11.343 1.00 37.18 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 0.967  18.860  11.306 1.00 39.21 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 1.549  21.174  11.493 1.00 39.20 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.590  20.177  11.493 1.00 41.16 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -0.734 20.511  11.630 1.00 44.73 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 6.839  16.886  12.496 1.00 28.10 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 8.035  16.114  12.166 1.00 26.81 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.702  15.280  10.923 1.00 26.84 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.612  14.686  10.846 1.00 27.80 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 8.483  15.220  13.343 1.00 27.07 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.696  14.299  13.013 1.00 26.56 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 10.363 13.774  14.279 1.00 27.75 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 10.533 14.510  15.280 1.00 28.74 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 10.796 12.496  14.247 1.00 26.28 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.576  15.283  9.913  1.00 25.12 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.310  14.516  8.676  1.00 24.34 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 8.947  13.103  8.730  1.00 24.39 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 9.810  12.835  9.601  1.00 23.55 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 8.860  15.277  7.477  1.00 24.31 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 10.264 15.432  7.601  1.00 25.94 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.540  12.211  7.779  1.00 23.88 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 9.091  10.853  7.698  1.00 24.04 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 8.966  10.093  9.050  1.00 24.24 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 9.861  9.300   9.404  1.00 24.54 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.561 10.919  7.267  1.00 24.99 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 10.736 11.553  5.919  1.00 27.45 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.705 10.793  4.753  1.00 29.89 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 10.841 12.861  5.578  1.00 28.98 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 10.839 11.651  3.751  1.00 30.12 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 10.925 12.904  4.189  1.00 29.96 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 7.885  10.372  9.806  1.00 23.41 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.649  9.748   11.110 1.00 25.00 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.607  8.643   10.990 1.00 25.73 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.633  8.826   10.263 1.00 26.74 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 7.142  10.814  12.098 1.00 25.62 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 6.990  10.401  13.556 1.00 27.57 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.306  9.903   14.104 1.00 27.20 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.430  11.563  14.365 1.00 28.74 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 6.798  7.522   11.709 1.00 24.64 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 5.887  6.369   11.692 1.00 24.94 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.426  6.090   13.122 1.00 25.90 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.294  5.951   13.988 1.00 26.39 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.646  5.143   11.157 1.00 24.96 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.118  5.315   9.672  1.00 26.51 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.255  3.976   9.230  1.00 30.39 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.588  4.234   10.358 1.00 29.80 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 4.093  6.018   13.404 1.00 25.67 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.662  5.721   14.793 1.00 26.28 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 3.210  4.266   14.919 1.00 25.72 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.729  3.664   13.932 1.00 25.37 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.490  6.640   15.242 1.00 27.37 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.726  8.159   15.147 1.00 29.63 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.522  8.934   15.677 1.00 30.54 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 3.959  8.566   15.899 1.00 30.18 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.277  3.753   16.159 1.00 25.43 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 2.836  2.424   16.570 1.00 26.15 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.294  2.563   18.009 1.00 26.21 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.631  3.512   18.724 1.00 25.88 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 4.016  1.448   16.570 1.00 26.26 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.463  1.607   18.422 1.00 26.42 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 0.952  1.547   19.782 1.00 27.66 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 2.045  0.808   20.573 1.00 29.02 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.394  -0.344  20.255 1.00 29.70 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.415 0.809   19.844 1.00 28.38 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -0.926 0.696   21.267 1.00 28.43 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.459 1.500   18.957 1.00 28.93 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.641  1.503   21.528 1.00 28.44 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.706  0.918   22.318 1.00 28.45 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 4.322  1.894   23.289 1.00 28.71 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 4.033  3.099   23.256 1.00 28.99 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 5.151  1.367   24.188 1.00 27.42 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 5.775  2.191   25.213 1.00 27.86 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 7.023  2.933   24.699 1.00 27.66 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 7.901  2.333   24.084 1.00 27.31 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 6.106  1.338   26.454 1.00 29.28 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 6.621  2.188   27.568 1.00 34.65 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 5.833  3.181   28.135 1.00 37.14 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 7.860  2.250   28.105 1.00 36.59 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 6.602  3.776   29.037 1.00 38.26 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 7.833  3.252   29.049 1.00 38.29 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 7.130  4.208   25.030 1.00 28.46 ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 8.272  5.011   24.654 1.00 30.06 ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 8.455  6.164   25.665 1.00 31.80 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 7.490  6.875   25.941 1.00 33.58 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 8.028  5.593   23.260 1.00 32.28 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 9.124  6.362   22.803 1.00 36.79 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 9.677  6.335   26.225 1.00 30.75 ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 10.078 7.443   27.091 1.00 31.13 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 11.236 8.216   26.419 1.00 31.86 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 11.890 7.647   25.554 1.00 31.86 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 10.469 6.930   28.496 1.00 32.53 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 9.281  6.378   29.255 1.00 36.94 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 9.623  5.723   30.587 1.00 38.57 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 10.513 6.240   31.297 1.00 36.32 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 9.008  4.687   30.917 1.00 40.71 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 11.513 9.515   26.740 1.00 33.08 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 12.560 10.244  25.985 1.00 32.51 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 13.904 9.516   25.849 1.00 31.22 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 14.533 9.585   24.798 1.00 31.25 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 12.684 11.573  26.728 1.00 34.09 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 11.316 11.771  27.349 1.00 34.76 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 10.809 10.392  27.693 1.00 32.64 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 14.335 8.825   26.897 1.00 30.02 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 15.591 8.074   26.882 1.00 29.67 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 15.590 6.872   25.945 1.00 29.07 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 16.633 6.234   25.738 1.00 29.19 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 14.401 6.485   25.443 1.00 27.76 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 14.264 5.388   24.483 1.00 27.12 ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 14.654 5.834   23.065 1.00 26.23 ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 14.787 4.973   22.196 1.00 25.64 ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 12.835 4.796   24.446 1.00 27.95 ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 12.544 4.032   25.716 1.00 30.05 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 13.444 3.342   26.195 1.00 29.61 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 11.418 4.150   26.239 1.00 29.43 ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 14.844 7.166   22.810 1.00 25.92 ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 15.235 7.605   21.442 1.00 26.21 ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 16.546 6.920   21.034 1.00 26.49 ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.412 6.752   21.890 1.00 26.30 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 15.349 9.122   21.362 1.00 26.32 ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 13.762 9.975   21.510 1.00 29.06 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 16.621 6.414   19.811 1.00 25.31 ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.813 5.706   19.378 1.00 26.00 ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.617 4.197   19.283 1.00 26.13 ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 18.370 3.535   18.582 1.00 26.55 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 16.611 3.641   19.968 1.00 24.82 ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 16.287 2.223   19.848 1.00 23.71 ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 15.901 1.913   18.397 1.00 23.08 ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 15.179 2.689   17.753 1.00 21.13 ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 16.448 0.832   17.863 1.00 23.05 ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 16.215 0.457   16.486 1.00 24.45 ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 14.895 -0.266  16.261 1.00 24.02 ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 14.507 -1.122  17.074 1.00 24.71 ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.450 -0.369  16.026 1.00 27.05 ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 18.609 0.592   15.672 1.00 29.38 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.157 -1.273  14.843 1.00 28.51 ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 19.975 -0.116  15.447 1.00 31.56 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 14.257 0.023   15.115 1.00 23.01 ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 13.067 -0.690  14.663 1.00 22.69 ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.561 -1.516  13.461 1.00 22.87 ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 14.249 -0.974  12.596 1.00 22.74 ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 11.945 0.276   14.218 1.00 22.96 ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 10.739 -0.393  13.475 1.00 24.20 ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 9.902  -1.239  14.441 1.00 23.81 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 9.825  0.680   12.861 1.00 25.87 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 13.270 -2.826  13.436 1.00 23.18 ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 13.740 -3.688  12.367 1.00 25.04 ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.632 -4.534  11.828 1.00 25.70 ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 11.850 -5.059  12.614 1.00 25.33 ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 14.758 -4.700  12.901 1.00 27.97 ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 16.026 -4.157  13.437 1.00 34.89 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 16.889 -5.329  13.907 1.00 40.84 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 18.119 -5.390  13.117 1.00 46.87 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 19.237 -4.741  13.429 1.00 50.21 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 19.309 -4.026  14.549 1.00 52.27 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 20.301 -4.828  12.645 1.00 50.52 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 12.683 -4.827  10.533 1.00 26.69 ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 11.758 -5.790  9.928  1.00 28.33 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 12.635 -6.954  9.362  1.00 30.84 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 13.863 -6.933  9.514  1.00 31.05 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 10.976 -5.099  8.822  1.00 28.26 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.023 -4.537  7.458  1.00 25.49 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 12.022 -7.966  8.727  1.00 32.91 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 12.796 -9.058  8.127  1.00 34.96 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 13.860 -8.540  7.092  1.00 35.19 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 14.792 -9.276  6.789  1.00 37.27 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 11.857 -10.042 7.413  1.00 38.36 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 11.094 -9.382  6.265  1.00 44.47 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 10.226 -10.350 5.510  1.00 51.48 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 9.004  -10.140 5.370  1.00 53.98 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 10.846 -11.423 4.998  1.00 51.39 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 13.748 -7.302  6.577  1.00 33.14 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 14.723 -6.789  5.594  1.00 32.17 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 15.881 -5.965  6.197  1.00 30.29 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 16.797 -5.558  5.474  1.00 30.43 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 14.006 -5.949  4.526  1.00 33.31 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 12.872 -6.650  3.850  1.00 37.91 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 11.572 -6.475  4.276  1.00 40.84 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 12.869 -7.455  2.757  1.00 38.89 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 10.822 -7.193  3.459  1.00 40.31 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 11.561 -7.831  2.550  1.00 39.66 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 15.807 -5.666  7.487  1.00 28.51 ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 16.850 -4.888  8.147  1.00 26.71 ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.324 -3.722  8.951  1.00 24.73 ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.156 -3.696  9.337  1.00 25.53 ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.193 -2.748  9.181  1.00 23.06 ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 16.884 -1.554  9.938  1.00 23.21 ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 15.900 -0.660  9.207  1.00 22.87 ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.143 -0.254  8.057  1.00 24.65 ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.178 -0.788  10.312 1.00 25.42 ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 17.837 0.512   11.031 1.00 26.52 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 19.103 -1.668  11.181 1.00 25.26 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 14.789 -0.342  9.875  1.00 21.71 ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 13.749 0.528   9.312  1.00 21.88 ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 13.938 1.984   9.778  1.00 21.35 ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 13.755 2.926   9.017  1.00 22.67 ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.347 -0.003  9.733  1.00 22.98 ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.242 0.969   9.355  1.00 24.05 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.077 -1.400  9.186  1.00 23.55 ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.213 2.158   11.072 1.00 19.97 ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.394 3.496   11.635 1.00 19.86 ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 14.747 3.474   13.110 1.00 21.35 ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 15.016 2.410   13.655 1.00 21.11 ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 14.715 4.629   13.759 1.00 22.10 ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 15.022 4.695   15.205 1.00 22.42 ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 13.928 5.425   15.970 1.00 22.97 ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 13.313 6.356   15.444 1.00 21.89 ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 16.377 5.387   15.441 1.00 23.32 ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.458 6.738   14.732 1.00 24.67 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.544 4.467   15.084 1.00 24.61 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.720 7.552   15.110 1.00 25.76 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 13.717 5.075   17.249 1.00 22.13 ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 12.746 5.780   18.088 1.00 22.57 ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 13.106 7.279   18.134 1.00 23.46 ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 14.284 7.625   18.302 1.00 24.35 ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 12.724 5.174   19.526 1.00 23.16 ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 11.849 6.011   20.426 1.00 23.81 ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 12.212 3.734   19.499 1.00 23.28 ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 12.083 8.140   18.016 1.00 23.00 ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 12.234 9.568   17.987 1.00 24.60 ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 11.163 10.287  18.817 1.00 25.50 ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 11.436 11.373  19.350 1.00 25.56 ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 12.188 10.047  16.541 1.00 25.78 ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 12.371 11.443  16.482 1.00 27.45 ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 9.952  9.704   18.942 1.00 25.64 ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 8.868  10.333  19.725 1.00 26.82 ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 8.112  9.318   20.632 1.00 28.89 ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 8.353  8.120   20.548 1.00 29.06 ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 7.886  11.076  18.780 1.00 28.15 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 7.085  10.108  18.081 1.00 28.74 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 8.586  11.964  17.768 1.00 28.02 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 7.197  9.798   21.470 1.00 30.61 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 6.404  8.932   22.335 1.00 32.11 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 5.410  9.696   23.181 1.00 33.53 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 5.297  10.911  23.069 1.00 34.21 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 4.732  8.995   24.071 1.00 34.80 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 3.729  9.613   24.941 1.00 35.81 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 2.328  9.168   24.560 1.00 36.18 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 2.085  8.841   23.394 1.00 35.32 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 1.408  9.111   25.537 1.00 36.38 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 0.019  8.687   25.300 1.00 36.99 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? -0.069 7.216   24.809 1.00 36.52 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -1.001 6.881   24.066 1.00 37.67 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -0.668 9.607   24.259 1.00 38.75 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -0.913 11.021  24.715 1.00 42.83 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -1.235 11.284  25.887 1.00 44.36 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -0.806 11.961  23.783 1.00 44.00 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 0.902  6.377   25.168 1.00 33.93 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 0.889  4.985   24.729 1.00 32.99 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 1.234  4.804   23.251 1.00 31.41 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 0.947  3.758   22.664 1.00 31.09 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 1.871  5.798   22.645 1.00 30.09 ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 2.309  5.709   21.256 1.00 30.13 ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.842  5.778   21.226 1.00 30.29 ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 4.447  6.334   22.139 1.00 32.06 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.750  6.894   20.422 1.00 30.10 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 0.226  6.983   20.359 1.00 31.82 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.211 8.287   19.731 1.00 32.42 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.342 5.815   19.579 1.00 33.04 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 4.455  5.255   20.165 1.00 27.50 ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 5.886  5.349   19.954 1.00 25.63 ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 6.072  5.755   18.483 1.00 24.88 ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 5.409  5.209   17.606 1.00 24.74 ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 6.646  4.044   20.279 1.00 25.24 ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 5.996  2.834   19.625 1.00 25.37 ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 8.111  4.147   19.883 1.00 25.62 ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 6.918  6.751   18.244 1.00 23.81 ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 7.212  7.206   16.888 1.00 24.10 ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.637  6.888   16.486 1.00 24.23 ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 9.561  7.023   17.294 1.00 24.86 ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 8.823  6.510   15.219 1.00 23.82 ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 10.104 6.108   14.639 1.00 23.99 ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.433 6.966   13.445 1.00 24.69 ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.611  7.145   12.555 1.00 26.02 ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 10.074 4.629   14.173 1.00 23.12 ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.554  3.665   15.215 1.00 22.76 ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 10.401 3.135   16.180 1.00 22.19 ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 8.245  3.203   15.167 1.00 22.77 ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 9.923  2.265   17.146 1.00 22.49 ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.780  2.292   16.111 1.00 22.99 ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 8.618  1.847   17.111 1.00 22.33 ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.659 7.474   13.423 1.00 23.92 ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 12.167 8.257   12.313 1.00 23.77 ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.598 7.244   11.248 1.00 24.24 ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.505 6.444   11.496 1.00 24.39 ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.368 9.067   12.773 1.00 23.60 ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 11.936 7.243   10.086 1.00 23.78 ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.259 6.308   9.006  1.00 24.35 ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.640 6.613   8.414  1.00 25.08 ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 14.006 7.786   8.300  1.00 25.76 ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.230 6.454   7.852  1.00 24.82 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.391 5.400   6.778  1.00 28.25 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.417 4.213   7.118  1.00 26.53 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.505 5.768   5.594  1.00 32.05 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.404 5.567   8.030  1.00 23.67 ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.662 5.800   7.329  1.00 23.25 ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 15.699 5.070   5.956  1.00 24.05 ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 16.691 5.178   5.265  1.00 24.64 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 16.892 5.430   8.162  1.00 23.43 ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 16.960 6.262   9.454  1.00 22.56 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 16.904 3.933   8.471  1.00 23.13 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 14.627 4.348   5.574  1.00 23.43 ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 14.558 3.522   4.386  1.00 23.85 ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 14.658 4.271   3.069  1.00 25.83 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.005 3.651   2.056  1.00 28.19 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.288 2.662   4.400  1.00 25.15 ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.259 1.645   5.535  1.00 25.69 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 11.966 0.886   5.465  1.00 26.17 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 10.872 1.756   5.880  1.00 26.30 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 9.624  1.358   6.055  1.00 28.55 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.275  0.099   5.784  1.00 25.68 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 8.705  2.213   6.499  1.00 29.37 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.318 5.572   3.062  1.00 25.59 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 14.427 6.398   1.858  1.00 26.12 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 15.853 6.951   1.627  1.00 26.96 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 16.131 7.466   0.527  1.00 27.93 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 13.458 7.592   1.910  1.00 28.10 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 13.744 8.579   3.028  1.00 31.52 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 14.032 8.126   4.171  1.00 28.93 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 13.661 9.798   2.779  1.00 34.04 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 16.748 6.869   2.655  1.00 26.04 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.130 7.380   2.561  1.00 25.71 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 18.974 6.332   1.825  1.00 25.61 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 19.781 5.638   2.441  1.00 25.82 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 18.701 7.713   3.976  1.00 25.36 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 17.810 8.642   4.823  1.00 25.24 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.362 8.833   6.263  1.00 24.72 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.551 9.985   4.134  1.00 24.88 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 18.762 6.196   0.497  1.00 24.85 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 19.453 5.192   -0.299 1.00 26.97 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 20.961 5.390   -0.326 1.00 30.67 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 21.683 4.397   -0.426 1.00 32.27 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 18.928 5.180   -1.756 1.00 27.60 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 17.423 5.232   -1.964 1.00 28.40 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.105 5.085   -3.478 1.00 28.84 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 16.688 4.152   -1.155 1.00 27.97 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 21.446 6.651   -0.202 1.00 31.36 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 22.883 6.943   -0.208 1.00 32.93 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 23.648 6.356   0.982  1.00 35.29 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 24.871 6.274   0.931  1.00 36.48 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 23.154 8.454   -0.313 1.00 32.40 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 22.447 9.269   0.717  1.00 32.29 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 21.220 9.854   0.600  1.00 32.71 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 22.903 9.550   2.051  1.00 31.88 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 20.876 10.466  1.784  1.00 32.47 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 21.912 10.337  2.673  1.00 32.11 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 24.088 9.283   2.751  1.00 31.98 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 22.045 10.801  3.987  1.00 32.27 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.217 9.749   4.047  1.00 32.10 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.212 10.512  4.642  1.00 31.83 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 22.950 5.952   2.050  1.00 35.96 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 23.608 5.323   3.202  1.00 37.26 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.374 4.037   2.801  1.00 41.22 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.269 3.612   3.532  1.00 41.28 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 22.558 4.959   4.255  1.00 35.62 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 21.987 6.102   5.076  1.00 34.62 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 20.912 5.596   6.017  1.00 33.42 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 23.092 6.824   5.866  1.00 34.82 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 24.002 3.420   1.652  1.00 43.69 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 24.557 2.178   1.112  1.00 47.12 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 25.603 2.343   0.019  1.00 50.00 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 26.062 1.331   -0.524 1.00 50.76 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 23.419 1.354   0.511  1.00 49.57 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 22.615 0.621   1.544  1.00 55.45 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 23.227 0.047   2.471  1.00 58.08 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 21.376 0.607   1.426  1.00 57.00 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 25.928 3.582   -0.362 1.00 51.17 ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 26.890 3.846   -1.424 1.00 53.12 ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 27.942 4.853   -0.965 1.00 54.25 ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 28.591 5.511   -1.789 1.00 55.07 ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 26.161 4.345   -2.687 1.00 56.68 ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 25.265 5.554   -2.457 1.00 63.02 ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 24.373 5.929   -3.629 1.00 70.63 ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 24.149 7.143   -3.849 1.00 71.18 ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 23.899 5.005   -4.329 1.00 73.68 ? 145 GLU   A OE2 1 
HETATM 1078 N  N1  . A1BOE B 2 .   ? 11.581 14.075  18.190 1.00 29.20 ? 201 A1BOE A N1  1 
HETATM 1079 C  C4  . A1BOE B 2 .   ? 10.351 9.891   23.108 1.00 31.80 ? 201 A1BOE A C4  1 
HETATM 1080 C  C5  . A1BOE B 2 .   ? 10.442 11.257  22.922 1.00 32.17 ? 201 A1BOE A C5  1 
HETATM 1081 C  C6  . A1BOE B 2 .   ? 9.606  12.137  23.613 1.00 32.58 ? 201 A1BOE A C6  1 
HETATM 1082 C  C7  . A1BOE B 2 .   ? 9.713  13.630  23.408 1.00 32.47 ? 201 A1BOE A C7  1 
HETATM 1083 C  C8  . A1BOE B 2 .   ? 10.681 13.881  21.145 1.00 31.64 ? 201 A1BOE A C8  1 
HETATM 1084 C  C10 . A1BOE B 2 .   ? 11.209 15.108  18.944 1.00 30.90 ? 201 A1BOE A C10 1 
HETATM 1085 C  C13 . A1BOE B 2 .   ? 12.027 14.363  23.209 1.00 32.62 ? 201 A1BOE A C13 1 
HETATM 1086 O  O2  . A1BOE B 2 .   ? 12.182 14.248  24.416 1.00 33.70 ? 201 A1BOE A O2  1 
HETATM 1087 C  C12 . A1BOE B 2 .   ? 13.137 14.924  22.351 1.00 32.29 ? 201 A1BOE A C12 1 
HETATM 1088 C  C11 . A1BOE B 2 .   ? 12.925 14.940  20.828 1.00 32.64 ? 201 A1BOE A C11 1 
HETATM 1089 C  C9  . A1BOE B 2 .   ? 11.441 14.999  20.442 1.00 31.87 ? 201 A1BOE A C9  1 
HETATM 1090 O  O1  . A1BOE B 2 .   ? 10.656 16.099  18.474 1.00 31.34 ? 201 A1BOE A O1  1 
HETATM 1091 N  N   . A1BOE B 2 .   ? 10.876 13.997  22.594 1.00 32.42 ? 201 A1BOE A N   1 
HETATM 1092 C  C1  . A1BOE B 2 .   ? 8.684  11.597  24.515 1.00 32.85 ? 201 A1BOE A C1  1 
HETATM 1093 O  O   . A1BOE B 2 .   ? 7.944  12.518  25.216 1.00 33.54 ? 201 A1BOE A O   1 
HETATM 1094 C  C   . A1BOE B 2 .   ? 6.933  12.029  26.106 1.00 32.89 ? 201 A1BOE A C   1 
HETATM 1095 C  C3  . A1BOE B 2 .   ? 9.430  9.377   23.981 1.00 32.01 ? 201 A1BOE A C3  1 
HETATM 1096 C  C2  . A1BOE B 2 .   ? 8.593  10.221  24.691 1.00 32.40 ? 201 A1BOE A C2  1 
HETATM 1097 ZN ZN  . ZN    C 3 .   ? 10.881 -4.751  5.392  1.00 28.23 2 202 ZN    A ZN  1 
HETATM 1098 S  S   . DMS   D 4 .   ? 19.720 -0.460  19.753 1.00 57.58 ? 203 DMS   A S   1 
HETATM 1099 O  O   . DMS   D 4 .   ? 18.259 -0.680  19.439 1.00 56.40 ? 203 DMS   A O   1 
HETATM 1100 C  C1  . DMS   D 4 .   ? 19.867 0.213   21.451 1.00 57.47 ? 203 DMS   A C1  1 
HETATM 1101 C  C2  . DMS   D 4 .   ? 20.458 0.983   18.922 1.00 57.32 ? 203 DMS   A C2  1 
HETATM 1102 O  O   . HOH   E 5 .   ? 12.756 6.847   30.882 1.00 32.87 ? 301 HOH   A O   1 
HETATM 1103 O  O   . HOH   E 5 .   ? 23.534 -0.066  15.884 1.00 48.49 ? 302 HOH   A O   1 
HETATM 1104 O  O   . HOH   E 5 .   ? 2.850  7.919   9.967  1.00 54.77 ? 303 HOH   A O   1 
HETATM 1105 O  O   . HOH   E 5 .   ? 8.080  -3.990  0.477  1.00 30.80 ? 304 HOH   A O   1 
HETATM 1106 O  O   . HOH   E 5 .   ? 6.258  8.431   27.640 1.00 48.90 ? 305 HOH   A O   1 
HETATM 1107 O  O   . HOH   E 5 .   ? 23.855 21.550  8.010  1.00 36.28 ? 306 HOH   A O   1 
HETATM 1108 O  O   . HOH   E 5 .   ? 10.675 8.067   4.647  1.00 33.28 ? 307 HOH   A O   1 
HETATM 1109 O  O   . HOH   E 5 .   ? 0.548  -0.396  16.413 1.00 25.23 ? 308 HOH   A O   1 
HETATM 1110 O  O   . HOH   E 5 .   ? 9.792  -4.907  31.827 1.00 45.63 ? 309 HOH   A O   1 
HETATM 1111 O  O   . HOH   E 5 .   ? 8.902  2.482   2.854  1.00 31.56 ? 310 HOH   A O   1 
HETATM 1112 O  O   . HOH   E 5 .   ? -0.230 15.381  8.466  1.00 60.55 ? 311 HOH   A O   1 
HETATM 1113 O  O   . HOH   E 5 .   ? 20.310 8.613   18.845 1.00 25.39 ? 312 HOH   A O   1 
HETATM 1114 O  O   . HOH   E 5 .   ? 15.729 11.864  24.072 1.00 26.91 ? 313 HOH   A O   1 
HETATM 1115 O  O   . HOH   E 5 .   ? 3.784  -4.926  21.160 1.00 31.35 ? 314 HOH   A O   1 
HETATM 1116 O  O   . HOH   E 5 .   ? 12.111 10.652  0.767  1.00 52.45 ? 315 HOH   A O   1 
HETATM 1117 O  O   . HOH   E 5 .   ? 29.571 3.038   10.351 1.00 35.07 ? 316 HOH   A O   1 
HETATM 1118 O  O   . HOH   E 5 .   ? 8.245  19.272  18.438 1.00 34.31 ? 317 HOH   A O   1 
HETATM 1119 O  O   . HOH   E 5 .   ? 4.457  5.611   24.740 1.00 33.68 ? 318 HOH   A O   1 
HETATM 1120 O  O   . HOH   E 5 .   ? 12.322 21.151  13.088 1.00 42.92 ? 319 HOH   A O   1 
HETATM 1121 O  O   . HOH   E 5 .   ? 17.730 2.498   23.075 1.00 32.46 ? 320 HOH   A O   1 
HETATM 1122 O  O   . HOH   E 5 .   ? 30.320 10.685  19.372 1.00 43.11 ? 321 HOH   A O   1 
HETATM 1123 O  O   . HOH   E 5 .   ? 11.411 17.033  5.685  1.00 66.34 ? 322 HOH   A O   1 
HETATM 1124 O  O   . HOH   E 5 .   ? 11.234 11.451  11.488 1.00 20.81 ? 323 HOH   A O   1 
HETATM 1125 O  O   . HOH   E 5 .   ? 11.566 2.035   33.297 1.00 24.73 ? 324 HOH   A O   1 
HETATM 1126 O  O   . HOH   E 5 .   ? 9.807  17.835  20.428 1.00 31.79 ? 325 HOH   A O   1 
HETATM 1127 O  O   . HOH   E 5 .   ? 7.224  16.532  24.803 1.00 45.91 ? 326 HOH   A O   1 
HETATM 1128 O  O   . HOH   E 5 .   ? 1.095  -2.741  19.833 1.00 39.95 ? 327 HOH   A O   1 
HETATM 1129 O  O   . HOH   E 5 .   ? 23.338 17.958  19.362 1.00 43.62 ? 328 HOH   A O   1 
HETATM 1130 O  O   . HOH   E 5 .   ? 18.001 20.955  9.348  1.00 33.44 ? 329 HOH   A O   1 
HETATM 1131 O  O   . HOH   E 5 .   ? 3.168  3.773   27.615 1.00 40.86 ? 330 HOH   A O   1 
HETATM 1132 O  O   . HOH   E 5 .   ? 15.000 2.282   23.103 1.00 22.62 ? 331 HOH   A O   1 
HETATM 1133 O  O   . HOH   E 5 .   ? 11.059 15.586  3.428  1.00 55.02 ? 332 HOH   A O   1 
HETATM 1134 O  O   . HOH   E 5 .   ? -0.028 12.551  21.167 1.00 68.20 ? 333 HOH   A O   1 
HETATM 1135 O  O   . HOH   E 5 .   ? 0.274  1.610   24.343 1.00 30.36 ? 334 HOH   A O   1 
HETATM 1136 O  O   . HOH   E 5 .   ? 10.297 4.587   3.344  1.00 33.22 ? 335 HOH   A O   1 
HETATM 1137 O  O   . HOH   E 5 .   ? 6.909  15.592  22.176 1.00 34.24 ? 336 HOH   A O   1 
HETATM 1138 O  O   . HOH   E 5 .   ? 10.011 4.223   33.534 1.00 33.74 ? 337 HOH   A O   1 
HETATM 1139 O  O   . HOH   E 5 .   ? 13.149 10.356  9.310  1.00 23.54 ? 338 HOH   A O   1 
HETATM 1140 O  O   . HOH   E 5 .   ? 5.250  -1.485  24.132 1.00 28.01 ? 339 HOH   A O   1 
HETATM 1141 O  O   . HOH   E 5 .   ? 6.927  3.595   32.848 1.00 33.76 ? 340 HOH   A O   1 
HETATM 1142 O  O   . HOH   E 5 .   ? 19.398 8.840   25.571 1.00 34.62 ? 341 HOH   A O   1 
HETATM 1143 O  O   . HOH   E 5 .   ? 4.083  -5.334  6.610  1.00 39.17 ? 342 HOH   A O   1 
HETATM 1144 O  O   . HOH   E 5 .   ? 13.729 8.982   29.694 1.00 35.46 ? 343 HOH   A O   1 
HETATM 1145 O  O   . HOH   E 5 .   ? 3.428  21.827  22.770 1.00 50.67 ? 344 HOH   A O   1 
HETATM 1146 O  O   . HOH   E 5 .   ? 5.836  1.662   6.562  1.00 41.19 ? 345 HOH   A O   1 
HETATM 1147 O  O   . HOH   E 5 .   ? 18.202 18.593  17.045 1.00 25.59 ? 346 HOH   A O   1 
HETATM 1148 O  O   . HOH   E 5 .   ? 1.878  13.166  5.860  1.00 44.05 ? 347 HOH   A O   1 
HETATM 1149 O  O   . HOH   E 5 .   ? 14.729 -4.398  17.140 1.00 35.19 ? 348 HOH   A O   1 
HETATM 1150 O  O   . HOH   E 5 .   ? 14.152 -4.724  34.083 1.00 32.22 ? 349 HOH   A O   1 
HETATM 1151 O  O   . HOH   E 5 .   ? 21.086 18.816  21.420 1.00 41.18 ? 350 HOH   A O   1 
HETATM 1152 O  O   . HOH   E 5 .   ? 6.404  13.117  21.458 1.00 32.19 ? 351 HOH   A O   1 
HETATM 1153 O  O   . HOH   E 5 .   ? 23.898 2.085   19.314 1.00 37.09 ? 352 HOH   A O   1 
HETATM 1154 O  O   . HOH   E 5 .   ? 14.495 14.405  3.735  1.00 37.89 ? 353 HOH   A O   1 
HETATM 1155 O  O   . HOH   E 5 .   ? 12.022 -7.985  12.964 1.00 39.00 ? 354 HOH   A O   1 
HETATM 1156 O  O   . HOH   E 5 .   ? 1.470  -2.660  17.330 1.00 38.86 ? 355 HOH   A O   1 
HETATM 1157 O  O   . HOH   E 5 .   ? 6.058  22.648  11.585 1.00 33.12 ? 356 HOH   A O   1 
HETATM 1158 O  O   . HOH   E 5 .   ? 6.764  12.594  5.375  1.00 32.83 ? 357 HOH   A O   1 
HETATM 1159 O  O   . HOH   E 5 .   ? 8.463  -7.629  9.129  1.00 50.50 ? 358 HOH   A O   1 
HETATM 1160 O  O   . HOH   E 5 .   ? 14.587 20.973  8.403  1.00 40.37 ? 359 HOH   A O   1 
HETATM 1161 O  O   . HOH   E 5 .   ? 16.149 -11.196 4.806  1.00 56.69 ? 360 HOH   A O   1 
HETATM 1162 O  O   . HOH   E 5 .   ? 19.690 23.529  15.495 1.00 35.88 ? 361 HOH   A O   1 
HETATM 1163 O  O   . HOH   E 5 .   ? 4.024  14.566  20.897 1.00 45.98 ? 362 HOH   A O   1 
HETATM 1164 O  O   . HOH   E 5 .   ? 4.100  -2.493  21.758 1.00 40.95 ? 363 HOH   A O   1 
HETATM 1165 O  O   . HOH   E 5 .   ? 4.133  10.112  19.125 1.00 34.97 ? 364 HOH   A O   1 
HETATM 1166 O  O   . HOH   E 5 .   ? 18.707 12.783  1.798  1.00 55.51 ? 365 HOH   A O   1 
HETATM 1167 O  O   . HOH   E 5 .   ? 22.391 18.734  5.638  1.00 47.39 ? 366 HOH   A O   1 
HETATM 1168 O  O   . HOH   E 5 .   ? 28.652 16.228  23.203 1.00 51.21 ? 367 HOH   A O   1 
HETATM 1169 O  O   . HOH   E 5 .   ? 22.190 8.609   20.953 1.00 32.17 ? 368 HOH   A O   1 
HETATM 1170 O  O   . HOH   E 5 .   ? 4.588  -1.467  28.862 1.00 41.66 ? 369 HOH   A O   1 
HETATM 1171 O  O   . HOH   E 5 .   ? 1.682  8.740   4.089  1.00 51.95 ? 370 HOH   A O   1 
HETATM 1172 O  O   . HOH   E 5 .   ? -1.905 -4.493  15.537 0.50 33.32 ? 371 HOH   A O   1 
HETATM 1173 O  O   . HOH   E 5 .   ? 8.909  19.217  6.454  1.00 56.04 ? 372 HOH   A O   1 
HETATM 1174 O  O   . HOH   E 5 .   ? 8.823  22.306  26.627 1.00 47.76 ? 373 HOH   A O   1 
HETATM 1175 O  O   . HOH   E 5 .   ? 21.060 21.559  17.944 1.00 37.67 ? 374 HOH   A O   1 
HETATM 1176 O  O   . HOH   E 5 .   ? 2.344  13.834  22.823 1.00 47.85 ? 375 HOH   A O   1 
HETATM 1177 O  O   . HOH   E 5 .   ? 2.179  1.772   26.639 1.00 38.62 ? 376 HOH   A O   1 
HETATM 1178 O  O   . HOH   E 5 .   ? -0.124 -3.255  9.326  1.00 60.00 ? 377 HOH   A O   1 
HETATM 1179 O  O   . HOH   E 5 .   ? 3.970  -2.195  26.481 1.00 46.05 ? 378 HOH   A O   1 
HETATM 1180 O  O   . HOH   E 5 .   ? 9.076  15.906  26.962 1.00 47.15 ? 379 HOH   A O   1 
HETATM 1181 O  O   . HOH   E 5 .   ? 0.784  -1.886  23.904 1.00 44.08 ? 380 HOH   A O   1 
HETATM 1182 O  O   . HOH   E 5 .   ? 20.410 -3.603  23.166 1.00 58.98 ? 381 HOH   A O   1 
HETATM 1183 O  O   . HOH   E 5 .   ? -0.043 11.972  17.378 1.00 65.18 ? 382 HOH   A O   1 
HETATM 1184 O  O   . HOH   E 5 .   ? 7.486  10.517  29.566 1.00 59.41 ? 383 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER   A 1   ? 0.5571 0.4344 0.2724 -0.0180 -0.1832 -0.0046 7   SER   A N   
2    C CA  . SER   A 1   ? 0.5492 0.4443 0.3008 -0.0183 -0.1910 -0.0001 7   SER   A CA  
3    C C   . SER   A 1   ? 0.5193 0.4381 0.3001 -0.0144 -0.1821 0.0011  7   SER   A C   
4    O O   . SER   A 1   ? 0.5265 0.4464 0.2989 -0.0128 -0.1744 -0.0005 7   SER   A O   
5    C CB  . SER   A 1   ? 0.5887 0.4692 0.3411 -0.0256 -0.2128 0.0071  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.6299 0.5087 0.3865 -0.0276 -0.2196 0.0123  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.4845 0.4202 0.2977 -0.0131 -0.1820 0.0036  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.4600 0.4136 0.2980 -0.0100 -0.1719 0.0040  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.4396 0.4094 0.3001 -0.0081 -0.1634 0.0030  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.4335 0.4042 0.2864 -0.0080 -0.1611 0.0003  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.4204 0.4009 0.3080 -0.0066 -0.1580 0.0056  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.4181 0.4114 0.3251 -0.0055 -0.1478 0.0048  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.4042 0.4036 0.3211 -0.0038 -0.1327 0.0027  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.4009 0.3959 0.3187 -0.0028 -0.1325 0.0036  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.4180 0.4143 0.3529 -0.0064 -0.1568 0.0119  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.3822 0.3891 0.3042 -0.0041 -0.1202 0.0001  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.3912 0.3991 0.3185 -0.0039 -0.1044 -0.0026 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.3951 0.4077 0.3538 -0.0021 -0.0983 0.0018  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.3908 0.4090 0.3578 -0.0031 -0.1010 0.0039  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.3927 0.4019 0.2971 -0.0078 -0.0947 -0.0082 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.3981 0.4057 0.2775 -0.0093 -0.1008 -0.0102 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.4139 0.4179 0.3161 -0.0096 -0.0785 -0.0116 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.4137 0.4257 0.2773 -0.0137 -0.0961 -0.0122 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.4003 0.4103 0.3784 0.0008  -0.0890 0.0037  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.4027 0.4172 0.4157 0.0035  -0.0798 0.0089  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.4297 0.4374 0.4376 0.0035  -0.0560 0.0033  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.4462 0.4453 0.4535 0.0055  -0.0477 0.0014  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.3875 0.4035 0.4350 0.0075  -0.0889 0.0185  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.3846 0.4032 0.4347 0.0052  -0.1136 0.0250  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.3826 0.4086 0.4541 0.0038  -0.1216 0.0316  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.4027 0.4135 0.4292 0.0034  -0.1284 0.0241  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.3933 0.4170 0.4616 0.0000  -0.1451 0.0371  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.4179 0.4254 0.4385 -0.0001 -0.1499 0.0289  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.4113 0.4240 0.4514 -0.0022 -0.1587 0.0351  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.4325 0.4373 0.4619 -0.0072 -0.1805 0.0395  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.4327 0.4415 0.4338 0.0005  -0.0450 0.0006  12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.4528 0.4502 0.4417 -0.0016 -0.0215 -0.0052 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.4589 0.4603 0.4738 -0.0001 -0.0083 -0.0010 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.4619 0.4730 0.4799 -0.0024 -0.0168 0.0020  12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.4757 0.4659 0.4193 -0.0097 -0.0206 -0.0130 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.4738 0.4750 0.4088 -0.0130 -0.0346 -0.0113 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.5047 0.4787 0.4292 -0.0145 0.0023  -0.0187 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.4536 0.4474 0.4902 0.0041  0.0126  0.0002  13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.4540 0.4511 0.5202 0.0064  0.0290  0.0054  13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.4455 0.4626 0.5515 0.0091  0.0114  0.0168  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.4445 0.4696 0.5737 0.0126  -0.0066 0.0236  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.4428 0.4663 0.5522 0.0059  0.0137  0.0190  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.4245 0.4652 0.5684 0.0066  -0.0049 0.0298  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.4159 0.4606 0.5308 0.0014  -0.0302 0.0271  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.4175 0.4717 0.5466 -0.0006 -0.0424 0.0331  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.4448 0.4906 0.6144 0.0064  0.0115  0.0355  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.5111 0.5569 0.7259 0.0135  0.0338  0.0427  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.5262 0.5748 0.7700 0.0193  0.0290  0.0486  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.5318 0.5742 0.7558 0.0133  0.0594  0.0435  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.4028 0.4399 0.4793 -0.0005 -0.0374 0.0187  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.3898 0.4288 0.4388 -0.0044 -0.0571 0.0159  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.3673 0.4042 0.4075 -0.0030 -0.0754 0.0157  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.3680 0.3994 0.4063 -0.0005 -0.0715 0.0139  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.4039 0.4361 0.4118 -0.0098 -0.0490 0.0072  15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.4173 0.4484 0.4240 -0.0136 -0.0332 0.0071  15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.4262 0.4659 0.4475 -0.0150 -0.0394 0.0125  15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.4387 0.4572 0.4244 -0.0170 -0.0124 0.0014  15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.4374 0.4752 0.4555 -0.0192 -0.0247 0.0130  15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.4553 0.4691 0.4335 -0.0219 0.0024  0.0013  15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.4593 0.4839 0.4553 -0.0227 -0.0035 0.0073  15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.4907 0.5102 0.4785 -0.0280 0.0114  0.0078  15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.3427 0.3816 0.3735 -0.0050 -0.0942 0.0170  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.3360 0.3693 0.3506 -0.0049 -0.1109 0.0161  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.3306 0.3610 0.3106 -0.0076 -0.1145 0.0098  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.3194 0.3525 0.2991 -0.0096 -0.1183 0.0110  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.3464 0.3804 0.3831 -0.0055 -0.1305 0.0252  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.4004 0.4237 0.4119 -0.0074 -0.1488 0.0239  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.4190 0.4391 0.4503 -0.0102 -0.1694 0.0340  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.4395 0.4467 0.4430 -0.0148 -0.1863 0.0325  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.4782 0.4701 0.4572 -0.0172 -0.1995 0.0319  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.4745 0.4644 0.4553 -0.0157 -0.1997 0.0335  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.4877 0.4640 0.4387 -0.0216 -0.2119 0.0299  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.3379 0.3633 0.2921 -0.0075 -0.1129 0.0043  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.3497 0.3737 0.2767 -0.0093 -0.1151 0.0001  17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.3670 0.3829 0.2796 -0.0081 -0.1281 -0.0001 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.3754 0.3865 0.2835 -0.0069 -0.1297 -0.0006 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.3602 0.3841 0.2688 -0.0114 -0.1033 -0.0045 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.3692 0.3945 0.2576 -0.0134 -0.1061 -0.0059 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.3574 0.3827 0.2737 -0.0138 -0.0887 -0.0051 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.3509 0.3630 0.2543 -0.0086 -0.1363 0.0001  18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.3614 0.3606 0.2454 -0.0080 -0.1462 -0.0009 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.3600 0.3564 0.2245 -0.0071 -0.1431 -0.0040 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.3515 0.3564 0.2214 -0.0077 -0.1376 -0.0038 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.3802 0.3701 0.2716 -0.0102 -0.1617 0.0035  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.3883 0.3799 0.3010 -0.0108 -0.1674 0.0090  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.3751 0.3694 0.2793 -0.0118 -0.1638 0.0059  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.3518 0.3346 0.1945 -0.0059 -0.1464 -0.0061 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.3598 0.3374 0.1880 -0.0039 -0.1423 -0.0080 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.3748 0.3461 0.2072 -0.0053 -0.1499 -0.0068 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.4041 0.3638 0.2351 -0.0082 -0.1615 -0.0055 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.3634 0.3227 0.1661 -0.0022 -0.1426 -0.0105 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.4146 0.3788 0.2121 -0.0010 -0.1353 -0.0110 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.4430 0.4056 0.2409 -0.0027 -0.1395 -0.0105 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.3884 0.3593 0.1838 0.0016  -0.1250 -0.0109 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.3630 0.3411 0.2008 -0.0044 -0.1450 -0.0062 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.3712 0.3434 0.2136 -0.0061 -0.1517 -0.0048 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.3990 0.3454 0.2194 -0.0068 -0.1601 -0.0071 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.4121 0.3499 0.2358 -0.0110 -0.1718 -0.0051 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.3700 0.3511 0.2184 -0.0046 -0.1447 -0.0034 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.3725 0.3499 0.2288 -0.0067 -0.1509 -0.0012 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.3755 0.3584 0.2340 -0.0044 -0.1438 0.0006  20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.3910 0.3741 0.2596 -0.0067 -0.1480 0.0036  20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.4411 0.4067 0.3014 -0.0061 -0.1530 0.0026  20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.4586 0.4019 0.2970 -0.0038 -0.1541 -0.0020 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.4462 0.4135 0.3172 -0.0086 -0.1565 0.0060  20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.4142 0.3462 0.2109 -0.0036 -0.1542 -0.0107 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.4589 0.3602 0.2266 -0.0051 -0.1596 -0.0140 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.4801 0.3664 0.2360 -0.0114 -0.1744 -0.0131 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.4990 0.3568 0.2293 -0.0161 -0.1839 -0.0146 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.4888 0.3770 0.2346 0.0005  -0.1454 -0.0178 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.4982 0.3888 0.2359 0.0018  -0.1397 -0.0185 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.4874 0.4043 0.2453 0.0046  -0.1317 -0.0160 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.5159 0.3839 0.2254 -0.0002 -0.1417 -0.0212 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.5102 0.4211 0.2543 0.0048  -0.1286 -0.0171 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.5226 0.4046 0.2374 0.0021  -0.1341 -0.0201 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.4675 0.3712 0.2415 -0.0122 -0.1769 -0.0099 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.4937 0.3880 0.2652 -0.0180 -0.1918 -0.0065 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.4860 0.3953 0.2914 -0.0217 -0.2030 0.0004  22  LEU   A C   
124  O O   . LEU   A 16  ? 0.4859 0.3905 0.2974 -0.0266 -0.2168 0.0058  22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.4943 0.3950 0.2638 -0.0158 -0.1863 -0.0068 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.5231 0.4092 0.2614 -0.0127 -0.1750 -0.0121 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.5177 0.4087 0.2550 -0.0123 -0.1729 -0.0110 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.5470 0.3968 0.2463 -0.0168 -0.1812 -0.0150 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.4707 0.3982 0.2998 -0.0197 -0.1969 0.0016  23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.4620 0.4040 0.3253 -0.0228 -0.2043 0.0087  23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.4763 0.4008 0.3376 -0.0307 -0.2251 0.0142  23  ALA   A C   
132  O O   . ALA   A 17  ? 0.4914 0.3929 0.3243 -0.0337 -0.2311 0.0109  23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.4455 0.4045 0.3269 -0.0205 -0.1940 0.0086  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.4740 0.4075 0.3649 -0.0344 -0.2361 0.0232  24  THR   A N   
135  C CA  . THR   A 18  ? 0.4990 0.4175 0.3930 -0.0438 -0.2594 0.0315  24  THR   A CA  
136  C C   . THR   A 18  ? 0.4943 0.4232 0.4160 -0.0465 -0.2630 0.0370  24  THR   A C   
137  O O   . THR   A 18  ? 0.4849 0.4331 0.4236 -0.0409 -0.2465 0.0346  24  THR   A O   
138  C CB  . THR   A 18  ? 0.5097 0.4334 0.4266 -0.0468 -0.2713 0.0412  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.5067 0.4594 0.4721 -0.0421 -0.2614 0.0473  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.5294 0.4448 0.4215 -0.0439 -0.2666 0.0363  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.5020 0.4177 0.4283 -0.0564 -0.2853 0.0454  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.5063 0.4323 0.4626 -0.0601 -0.2905 0.0526  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.4691 0.4289 0.4788 -0.0549 -0.2785 0.0603  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.4580 0.4327 0.4881 -0.0528 -0.2679 0.0611  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.5472 0.4537 0.5034 -0.0734 -0.3199 0.0631  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.6670 0.5341 0.5669 -0.0805 -0.3318 0.0558  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.7235 0.5767 0.5978 -0.0794 -0.3245 0.0471  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.7324 0.5693 0.5981 -0.0898 -0.3508 0.0571  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.7702 0.5841 0.5948 -0.0871 -0.3367 0.0423  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.7846 0.5863 0.5997 -0.0942 -0.3530 0.0478  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.4549 0.4244 0.4860 -0.0531 -0.2792 0.0660  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.4406 0.4379 0.5207 -0.0473 -0.2646 0.0727  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.4108 0.4211 0.4841 -0.0381 -0.2363 0.0619  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.3811 0.4092 0.4846 -0.0354 -0.2220 0.0650  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.4909 0.4921 0.5928 -0.0469 -0.2713 0.0809  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.5671 0.5938 0.7229 -0.0407 -0.2555 0.0891  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.5825 0.6207 0.7837 -0.0440 -0.2632 0.1032  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.5899 0.6245 0.7420 -0.0320 -0.2323 0.0809  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.4187 0.4189 0.4516 -0.0344 -0.2284 0.0499  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.4075 0.4175 0.4300 -0.0279 -0.2053 0.0407  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.3964 0.4097 0.4180 -0.0292 -0.2007 0.0393  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.3744 0.4021 0.4116 -0.0268 -0.1846 0.0393  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.4334 0.4313 0.4149 -0.0250 -0.2013 0.0304  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.4512 0.4484 0.4319 -0.0226 -0.2002 0.0303  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.4448 0.4558 0.4534 -0.0198 -0.1907 0.0338  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.4750 0.4562 0.4260 -0.0236 -0.2077 0.0266  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.4102 0.4077 0.4126 -0.0337 -0.2148 0.0387  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.4275 0.4262 0.4290 -0.0351 -0.2118 0.0380  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.4271 0.4403 0.4693 -0.0387 -0.2133 0.0484  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.4281 0.4501 0.4774 -0.0383 -0.2030 0.0484  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.4403 0.4145 0.4093 -0.0388 -0.2253 0.0342  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.4408 0.4051 0.3744 -0.0335 -0.2151 0.0239  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.4604 0.4078 0.3643 -0.0321 -0.2174 0.0184  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.4275 0.3986 0.3545 -0.0292 -0.2010 0.0195  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.4684 0.4130 0.3509 -0.0265 -0.2041 0.0110  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.4490 0.4082 0.3460 -0.0248 -0.1952 0.0122  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.4143 0.3997 0.3582 -0.0293 -0.1930 0.0222  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.4439 0.4070 0.3322 -0.0203 -0.1830 0.0087  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.4187 0.4062 0.3496 -0.0257 -0.1823 0.0184  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.4319 0.4097 0.3378 -0.0211 -0.1777 0.0123  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.4219 0.4379 0.4926 -0.0424 -0.2260 0.0585  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.4069 0.4383 0.5233 -0.0455 -0.2270 0.0706  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.3831 0.4355 0.5285 -0.0393 -0.2024 0.0720  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.3743 0.4400 0.5551 -0.0405 -0.1959 0.0806  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.4038 0.4314 0.5444 -0.0521 -0.2501 0.0831  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.3636 0.4168 0.4937 -0.0331 -0.1885 0.0642  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.3382 0.4046 0.4858 -0.0278 -0.1638 0.0633  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.3425 0.4047 0.4508 -0.0250 -0.1485 0.0505  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.3277 0.3911 0.4297 -0.0211 -0.1337 0.0456  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.3444 0.4137 0.5128 -0.0243 -0.1633 0.0675  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.3635 0.4401 0.5790 -0.0273 -0.1775 0.0831  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.3764 0.4663 0.6318 -0.0268 -0.1667 0.0919  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.3580 0.4252 0.5697 -0.0314 -0.2021 0.0878  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.3460 0.4019 0.4285 -0.0275 -0.1533 0.0460  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.3505 0.4028 0.3987 -0.0260 -0.1434 0.0365  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.3525 0.4124 0.4032 -0.0260 -0.1220 0.0352  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.3559 0.4220 0.4260 -0.0285 -0.1155 0.0406  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.3543 0.3989 0.3839 -0.0287 -0.1536 0.0350  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.3681 0.4099 0.3678 -0.0275 -0.1463 0.0282  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.3743 0.4103 0.3517 -0.0238 -0.1459 0.0217  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.3770 0.4112 0.3660 -0.0293 -0.1554 0.0286  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.3451 0.4024 0.3734 -0.0243 -0.1111 0.0282  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.3507 0.4091 0.3693 -0.0264 -0.0917 0.0256  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.3615 0.4163 0.3482 -0.0297 -0.0939 0.0216  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.3583 0.4136 0.3384 -0.0344 -0.0868 0.0231  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.3590 0.4143 0.3736 -0.0239 -0.0790 0.0214  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.3685 0.4183 0.3609 -0.0282 -0.0606 0.0172  32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.3552 0.4149 0.4066 -0.0200 -0.0749 0.0270  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.3645 0.4154 0.3332 -0.0273 -0.1037 0.0176  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.3696 0.4184 0.3138 -0.0292 -0.1060 0.0154  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.3605 0.4046 0.2948 -0.0248 -0.1176 0.0129  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.3612 0.4022 0.2975 -0.0215 -0.1209 0.0108  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.3795 0.4269 0.3056 -0.0327 -0.0939 0.0124  33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.4004 0.4471 0.3050 -0.0354 -0.0978 0.0121  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.4212 0.4693 0.3185 -0.0401 -0.1000 0.0162  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.4044 0.4499 0.2961 -0.0334 -0.1009 0.0094  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.4316 0.4803 0.3150 -0.0412 -0.1045 0.0170  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.4203 0.4678 0.3004 -0.0370 -0.1046 0.0128  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.4098 0.4529 0.3004 -0.0291 -0.1013 0.0055  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.4224 0.4709 0.2925 -0.0364 -0.1075 0.0129  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.4193 0.4621 0.2963 -0.0288 -0.1036 0.0046  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.4191 0.4652 0.2875 -0.0322 -0.1065 0.0084  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.3488 0.3909 0.2724 -0.0247 -0.1230 0.0136  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.3477 0.3828 0.2595 -0.0202 -0.1297 0.0109  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.3430 0.3799 0.2445 -0.0204 -0.1283 0.0127  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.3203 0.3611 0.2253 -0.0239 -0.1277 0.0168  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.3689 0.3936 0.2842 -0.0180 -0.1407 0.0108  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.3754 0.3987 0.3000 -0.0204 -0.1457 0.0147  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.4137 0.4322 0.3286 -0.0190 -0.1465 0.0154  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.4487 0.4698 0.3716 -0.0218 -0.1476 0.0194  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.4091 0.4217 0.3104 -0.0149 -0.1451 0.0126  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.3520 0.3864 0.2429 -0.0169 -0.1279 0.0108  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.3623 0.3997 0.2498 -0.0162 -0.1268 0.0145  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.3726 0.4009 0.2534 -0.0094 -0.1272 0.0124  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.3833 0.4108 0.2570 -0.0076 -0.1244 0.0098  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.3823 0.4291 0.2653 -0.0216 -0.1224 0.0173  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.4372 0.4898 0.3228 -0.0233 -0.1239 0.0248  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.4592 0.5086 0.3497 -0.0171 -0.1250 0.0266  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.4497 0.5082 0.3318 -0.0313 -0.1238 0.0295  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.3732 0.3921 0.2545 -0.0058 -0.1294 0.0131  36  SER   A N   
241  C CA  A SER   A 30  ? 0.3877 0.3926 0.2593 0.0009  -0.1268 0.0105  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.3831 0.3881 0.2544 0.0008  -0.1268 0.0103  36  SER   A CA  
243  C C   . SER   A 30  ? 0.3822 0.3953 0.2563 0.0037  -0.1194 0.0142  36  SER   A C   
244  O O   . SER   A 30  ? 0.3703 0.3756 0.2351 0.0080  -0.1145 0.0113  36  SER   A O   
245  C CB  A SER   A 30  ? 0.4184 0.4106 0.2905 0.0036  -0.1285 0.0113  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.4018 0.3923 0.2719 0.0037  -0.1287 0.0104  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.4707 0.4458 0.3313 0.0103  -0.1224 0.0086  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.4145 0.4150 0.2988 0.0033  -0.1274 0.0174  36  SER   A OG  
249  N N   . SER   A 31  ? 0.3622 0.3907 0.2491 0.0002  -0.1193 0.0219  37  SER   A N   
250  C CA  . SER   A 31  ? 0.3617 0.4000 0.2558 0.0014  -0.1148 0.0282  37  SER   A CA  
251  C C   . SER   A 31  ? 0.3521 0.3955 0.2385 -0.0014 -0.1133 0.0257  37  SER   A C   
252  O O   . SER   A 31  ? 0.3604 0.4085 0.2511 0.0008  -0.1089 0.0297  37  SER   A O   
253  C CB  . SER   A 31  ? 0.3759 0.4278 0.2851 -0.0036 -0.1184 0.0389  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.4364 0.4983 0.3412 -0.0135 -0.1226 0.0408  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.3318 0.3740 0.2091 -0.0058 -0.1160 0.0197  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.3145 0.3590 0.1840 -0.0081 -0.1142 0.0167  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.3290 0.3608 0.1877 -0.0035 -0.1136 0.0091  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.3375 0.3695 0.1899 -0.0046 -0.1120 0.0068  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.3094 0.3594 0.1764 -0.0164 -0.1158 0.0160  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.3175 0.3765 0.1878 -0.0239 -0.1177 0.0236  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.3446 0.4032 0.2062 -0.0328 -0.1167 0.0219  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.3417 0.3976 0.1928 -0.0355 -0.1132 0.0177  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.3612 0.4144 0.1998 -0.0448 -0.1110 0.0177  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.3564 0.4092 0.1893 -0.0533 -0.1122 0.0219  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.3755 0.4240 0.2046 -0.0465 -0.1073 0.0135  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.3391 0.3580 0.1941 0.0001  -0.1163 0.0057  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.3382 0.3422 0.1806 0.0020  -0.1192 -0.0001 39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.3307 0.3395 0.1771 -0.0022 -0.1233 -0.0019 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.3511 0.3529 0.1899 -0.0018 -0.1252 -0.0047 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.3584 0.3533 0.1875 0.0061  -0.1136 -0.0019 39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.4008 0.3761 0.2120 0.0065  -0.1185 -0.0071 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.3824 0.3449 0.1888 0.0056  -0.1255 -0.0090 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.3996 0.3718 0.2015 0.0066  -0.1167 -0.0086 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.3236 0.3426 0.1821 -0.0063 -0.1239 0.0002  40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.3284 0.3507 0.1939 -0.0093 -0.1244 -0.0010 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.3438 0.3652 0.2219 -0.0108 -0.1292 0.0003  40  LEU   A C   
277  O O   . LEU   A 34  ? 0.3527 0.3755 0.2346 -0.0116 -0.1304 0.0026  40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.3160 0.3485 0.1829 -0.0140 -0.1173 0.0001  40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.3240 0.3578 0.1812 -0.0147 -0.1134 -0.0008 40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.3034 0.3420 0.1579 -0.0216 -0.1075 -0.0001 40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.3365 0.3631 0.1907 -0.0117 -0.1148 -0.0042 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.3369 0.3570 0.2246 -0.0113 -0.1319 0.0002  41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.3382 0.3604 0.2443 -0.0133 -0.1356 0.0034  41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.3421 0.3698 0.2635 -0.0138 -0.1300 0.0043  41  LEU   A C   
285  O O   . LEU   A 35  ? 0.3591 0.3836 0.2774 -0.0121 -0.1306 0.0028  41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.3392 0.3494 0.2451 -0.0131 -0.1492 0.0047  41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.3513 0.3646 0.2804 -0.0162 -0.1553 0.0100  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.3503 0.3513 0.2727 -0.0180 -0.1670 0.0111  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.3706 0.3861 0.3195 -0.0168 -0.1596 0.0139  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.3428 0.3777 0.2806 -0.0160 -0.1231 0.0069  42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.3326 0.3713 0.2885 -0.0157 -0.1142 0.0084  42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.3308 0.3733 0.3160 -0.0161 -0.1188 0.0150  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.3288 0.3741 0.3185 -0.0186 -0.1202 0.0175  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.3385 0.3793 0.2862 -0.0187 -0.0975 0.0059  42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.3321 0.3734 0.2994 -0.0176 -0.0846 0.0071  42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.3563 0.3936 0.2774 -0.0198 -0.0955 0.0011  42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.3261 0.3693 0.3332 -0.0142 -0.1223 0.0191  43  SER   A N   
298  C CA  . SER   A 37  ? 0.3249 0.3737 0.3670 -0.0149 -0.1272 0.0280  43  SER   A CA  
299  C C   . SER   A 37  ? 0.3394 0.3942 0.4104 -0.0121 -0.1120 0.0316  43  SER   A C   
300  O O   . SER   A 37  ? 0.3324 0.3837 0.3927 -0.0096 -0.1013 0.0267  43  SER   A O   
301  C CB  . SER   A 37  ? 0.3267 0.3691 0.3734 -0.0164 -0.1497 0.0329  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.3352 0.3721 0.3768 -0.0143 -0.1545 0.0322  43  SER   A OG  
303  N N   . SER   A 38  ? 0.3508 0.4138 0.4587 -0.0124 -0.1092 0.0405  44  SER   A N   
304  C CA  . SER   A 38  ? 0.3804 0.4486 0.5206 -0.0086 -0.0917 0.0450  44  SER   A CA  
305  C C   . SER   A 38  ? 0.4049 0.4758 0.5778 -0.0060 -0.1041 0.0543  44  SER   A C   
306  O O   . SER   A 38  ? 0.4049 0.4752 0.5833 -0.0092 -0.1279 0.0603  44  SER   A O   
307  C CB  . SER   A 38  ? 0.3905 0.4664 0.5569 -0.0098 -0.0780 0.0508  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.4247 0.5072 0.6129 -0.0132 -0.0968 0.0600  44  SER   A OG  
309  N N   . THR   A 39  ? 0.4264 0.4976 0.6182 -0.0008 -0.0885 0.0555  45  THR   A N   
310  C CA  . THR   A 39  ? 0.4438 0.5182 0.6715 0.0022  -0.0983 0.0659  45  THR   A CA  
311  C C   . THR   A 39  ? 0.4614 0.5446 0.7409 0.0074  -0.0773 0.0753  45  THR   A C   
312  O O   . THR   A 39  ? 0.4670 0.5483 0.7423 0.0093  -0.0507 0.0698  45  THR   A O   
313  C CB  . THR   A 39  ? 0.4708 0.5352 0.6737 0.0048  -0.0989 0.0589  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.4984 0.5576 0.6931 0.0089  -0.0711 0.0511  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.4892 0.5443 0.6423 0.0007  -0.1145 0.0496  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.4661 0.5572 0.7936 0.0094  -0.0885 0.0900  46  THR   A N   
317  C CA  . THR   A 40  ? 0.4733 0.5736 0.8584 0.0157  -0.0685 0.1015  46  THR   A CA  
318  C C   . THR   A 40  ? 0.5032 0.5949 0.8892 0.0231  -0.0502 0.0972  46  THR   A C   
319  O O   . THR   A 40  ? 0.5068 0.5962 0.9117 0.0292  -0.0192 0.0963  46  THR   A O   
320  C CB  . THR   A 40  ? 0.4694 0.5840 0.9119 0.0133  -0.0918 0.1224  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.4935 0.6027 0.9239 0.0093  -0.1226 0.1259  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.4667 0.5895 0.9162 0.0064  -0.1031 0.1278  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.5188 0.6030 0.8822 0.0222  -0.0684 0.0943  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.5321 0.6066 0.8921 0.0283  -0.0542 0.0898  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.5637 0.6230 0.8669 0.0279  -0.0332 0.0704  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.5806 0.6372 0.8404 0.0219  -0.0407 0.0609  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.5393 0.6106 0.8926 0.0261  -0.0826 0.0943  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.5697 0.6178 0.8734 0.0336  -0.0077 0.0652  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.5987 0.6296 0.8476 0.0312  0.0111  0.0479  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.6005 0.6217 0.8099 0.0290  -0.0024 0.0399  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.5992 0.6164 0.8253 0.0335  -0.0036 0.0438  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.6360 0.6540 0.8971 0.0368  0.0483  0.0448  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.7309 0.7316 0.9384 0.0310  0.0692  0.0296  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.8064 0.8131 1.0212 0.0283  0.0800  0.0318  48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.8138 0.8353 1.0810 0.0326  0.0818  0.0446  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.8331 0.8285 0.9968 0.0202  0.0866  0.0205  48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.5927 0.6104 0.7525 0.0222  -0.0118 0.0297  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.5865 0.5959 0.7069 0.0193  -0.0233 0.0220  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.5719 0.5636 0.6655 0.0192  -0.0015 0.0118  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.5703 0.5528 0.6595 0.0189  0.0226  0.0073  49  GLY   A O   
341  N N   . CYS   A 44  ? 0.5610 0.5451 0.6341 0.0185  -0.0095 0.0083  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.5713 0.5362 0.6181 0.0173  0.0094  -0.0010 50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.5594 0.5181 0.5594 0.0105  -0.0019 -0.0089 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.5737 0.5166 0.5545 0.0091  0.0076  -0.0145 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.5925 0.5497 0.6724 0.0250  0.0208  0.0040  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.6800 0.6524 0.8025 0.0303  -0.0060 0.0188  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.5265 0.4963 0.5085 0.0060  -0.0200 -0.0091 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.5184 0.4844 0.4602 -0.0005 -0.0283 -0.0152 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.5147 0.4687 0.4253 -0.0078 -0.0125 -0.0231 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.5110 0.4645 0.4257 -0.0088 -0.0013 -0.0237 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.5313 0.5109 0.4653 -0.0024 -0.0485 -0.0127 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.5765 0.5606 0.5189 0.0006  -0.0670 -0.0074 51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.6090 0.5859 0.5438 0.0009  -0.0682 -0.0081 51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.5693 0.5620 0.5227 0.0016  -0.0805 -0.0025 51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.5135 0.4569 0.3917 -0.0140 -0.0127 -0.0284 52  THR   A N   
356  C CA  . THR   A 46  ? 0.5244 0.4535 0.3679 -0.0237 -0.0018 -0.0348 52  THR   A CA  
357  C C   . THR   A 46  ? 0.4979 0.4377 0.3196 -0.0309 -0.0171 -0.0339 52  THR   A C   
358  O O   . THR   A 46  ? 0.4941 0.4409 0.3112 -0.0310 -0.0308 -0.0320 52  THR   A O   
359  C CB  . THR   A 46  ? 0.5708 0.4785 0.3934 -0.0275 0.0076  -0.0401 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.5854 0.4811 0.4299 -0.0203 0.0259  -0.0408 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.6038 0.4937 0.3831 -0.0408 0.0137  -0.0460 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.4712 0.4121 0.2814 -0.0366 -0.0146 -0.0342 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.4500 0.4010 0.2433 -0.0432 -0.0288 -0.0318 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.4652 0.4010 0.2226 -0.0556 -0.0278 -0.0345 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.4893 0.4046 0.2259 -0.0625 -0.0138 -0.0391 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.4441 0.4044 0.2426 -0.0444 -0.0301 -0.0290 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.4367 0.4092 0.2707 -0.0339 -0.0307 -0.0258 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.4389 0.4110 0.2263 -0.0494 -0.0456 -0.0249 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.4342 0.4207 0.2853 -0.0267 -0.0476 -0.0220 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.4508 0.3948 0.1999 -0.0592 -0.0418 -0.0313 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.4651 0.3964 0.1829 -0.0727 -0.0444 -0.0315 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.4673 0.3970 0.1671 -0.0835 -0.0471 -0.0287 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.4416 0.3883 0.1568 -0.0797 -0.0536 -0.0242 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.4585 0.4025 0.1796 -0.0729 -0.0587 -0.0264 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.4959 0.4026 0.1614 -0.0975 -0.0423 -0.0312 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.5164 0.4170 0.1582 -0.1111 -0.0470 -0.0274 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.5437 0.4345 0.1593 -0.1260 -0.0589 -0.0236 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.5657 0.4285 0.1499 -0.1359 -0.0513 -0.0292 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.5472 0.4223 0.1669 -0.1159 -0.0281 -0.0343 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.5758 0.4611 0.2273 -0.1007 -0.0152 -0.0369 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.5596 0.4728 0.2386 -0.0941 -0.0268 -0.0299 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.5428 0.4634 0.2513 -0.0815 -0.0156 -0.0317 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.5216 0.4646 0.2590 -0.0731 -0.0241 -0.0269 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.4915 0.4507 0.2321 -0.0745 -0.0414 -0.0209 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.5005 0.4488 0.2651 -0.0633 -0.0151 -0.0275 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.5295 0.4433 0.1613 -0.1263 -0.0765 -0.0140 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.5441 0.4554 0.1628 -0.1383 -0.0896 -0.0078 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.5315 0.4713 0.1746 -0.1379 -0.1070 0.0055  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.5136 0.4730 0.1822 -0.1271 -0.1076 0.0081  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.5641 0.4732 0.1908 -0.1305 -0.0847 -0.0127 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.5436 0.4852 0.2159 -0.1099 -0.0878 -0.0098 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.5393 0.4816 0.1786 -0.1485 -0.1199 0.0140  57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.5319 0.5013 0.2000 -0.1468 -0.1338 0.0276  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.5249 0.5052 0.2106 -0.1406 -0.1353 0.0300  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.5272 0.5235 0.2297 -0.1450 -0.1470 0.0428  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.5708 0.5387 0.2266 -0.1661 -0.1507 0.0410  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.6950 0.6415 0.3196 -0.1859 -0.1594 0.0437  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.7140 0.6467 0.3268 -0.1840 -0.1512 0.0347  57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.7658 0.7076 0.3766 -0.2043 -0.1755 0.0555  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.5148 0.4871 0.1994 -0.1304 -0.1234 0.0189  58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.4975 0.4780 0.1967 -0.1237 -0.1233 0.0201  58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.4688 0.4770 0.2017 -0.1137 -0.1278 0.0299  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.4677 0.4864 0.2150 -0.1042 -0.1252 0.0295  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.5075 0.4782 0.2062 -0.1112 -0.1100 0.0077  58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.5249 0.4616 0.1896 -0.1204 -0.1011 -0.0030 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.4365 0.4546 0.1817 -0.1154 -0.1328 0.0381  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.4115 0.4520 0.1876 -0.1043 -0.1321 0.0461  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.4026 0.4435 0.1842 -0.0958 -0.1255 0.0432  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.3887 0.4446 0.1918 -0.0894 -0.1238 0.0509  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.4227 0.4800 0.2180 -0.1130 -0.1432 0.0633  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.4537 0.5165 0.2533 -0.1167 -0.1494 0.0686  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.5040 0.5858 0.3302 -0.1239 -0.1609 0.0881  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.5473 0.6259 0.3649 -0.1411 -0.1750 0.0976  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.4519 0.5525 0.3109 -0.1117 -0.1549 0.0954  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.4088 0.4322 0.1715 -0.0954 -0.1205 0.0324  60  THR   A N   
416  C CA  . THR   A 54  ? 0.4125 0.4330 0.1771 -0.0876 -0.1148 0.0288  60  THR   A CA  
417  C C   . THR   A 54  ? 0.3922 0.3989 0.1470 -0.0791 -0.1073 0.0160  60  THR   A C   
418  O O   . THR   A 54  ? 0.4022 0.3964 0.1434 -0.0833 -0.1056 0.0096  60  THR   A O   
419  C CB  . THR   A 54  ? 0.4583 0.4701 0.2123 -0.0986 -0.1187 0.0318  60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.5120 0.5024 0.2406 -0.1082 -0.1191 0.0243  60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.4504 0.4768 0.2181 -0.1085 -0.1276 0.0469  60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.3680 0.3760 0.1300 -0.0678 -0.1029 0.0132  61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.3585 0.3554 0.1169 -0.0599 -0.0981 0.0039  61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.3597 0.3568 0.1234 -0.0504 -0.0966 0.0037  61  GLY   A C   
425  O O   . GLY   A 55  ? 0.3631 0.3652 0.1287 -0.0510 -0.0970 0.0094  61  GLY   A O   
426  N N   . VAL   A 56  ? 0.3555 0.3463 0.1212 -0.0427 -0.0953 -0.0018 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.3541 0.3407 0.1202 -0.0354 -0.0961 -0.0018 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.3517 0.3393 0.1236 -0.0280 -0.0977 -0.0040 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.3548 0.3411 0.1325 -0.0271 -0.0975 -0.0075 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.3687 0.3419 0.1312 -0.0357 -0.0961 -0.0046 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.3852 0.3521 0.1471 -0.0294 -0.0996 -0.0036 62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.3864 0.3563 0.1409 -0.0437 -0.0952 -0.0022 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.3515 0.3384 0.1202 -0.0232 -0.0987 -0.0020 63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.3549 0.3390 0.1255 -0.0177 -0.1019 -0.0041 63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.3832 0.3539 0.1443 -0.0147 -0.1066 -0.0040 63  TYR   A C   
436  O O   . TYR   A 57  ? 0.3908 0.3559 0.1414 -0.0158 -0.1052 -0.0017 63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.3456 0.3375 0.1179 -0.0157 -0.0990 -0.0023 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.3612 0.3489 0.1240 -0.0128 -0.0947 0.0006  63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.3724 0.3665 0.1364 -0.0153 -0.0889 0.0057  63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.3685 0.3442 0.1205 -0.0084 -0.0955 -0.0012 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.3896 0.3792 0.1466 -0.0120 -0.0815 0.0089  63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.3913 0.3587 0.1305 -0.0058 -0.0883 0.0007  63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.3976 0.3723 0.1403 -0.0070 -0.0800 0.0057  63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.4203 0.3863 0.1522 -0.0038 -0.0696 0.0081  63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.3805 0.3455 0.1447 -0.0120 -0.1131 -0.0054 64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.4041 0.3540 0.1573 -0.0113 -0.1210 -0.0040 64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.4166 0.3578 0.1525 -0.0097 -0.1206 -0.0043 64  TYR   A C   
448  O O   . TYR   A 58  ? 0.3960 0.3414 0.1365 -0.0079 -0.1198 -0.0060 64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.4018 0.3486 0.1697 -0.0106 -0.1303 -0.0031 64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.4264 0.3565 0.1823 -0.0119 -0.1419 0.0004  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.4409 0.3614 0.1858 -0.0140 -0.1441 0.0032  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.4469 0.3685 0.1989 -0.0123 -0.1518 0.0015  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.4664 0.3691 0.1963 -0.0168 -0.1563 0.0075  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.4667 0.3694 0.2023 -0.0159 -0.1648 0.0056  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.4875 0.3806 0.2113 -0.0183 -0.1670 0.0087  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.5178 0.3902 0.2226 -0.0233 -0.1812 0.0137  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.4478 0.3746 0.1618 -0.0108 -0.1198 -0.0028 65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.4838 0.3960 0.1752 -0.0096 -0.1161 -0.0038 65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.5200 0.4083 0.1895 -0.0130 -0.1283 -0.0028 65  CYS   A C   
460  O O   . CYS   A 59  ? 0.5304 0.4067 0.1841 -0.0160 -0.1300 -0.0003 65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.5043 0.4173 0.1863 -0.0088 -0.1022 -0.0021 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.5331 0.4221 0.1833 -0.0067 -0.0922 -0.0035 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.5314 0.4119 0.1997 -0.0138 -0.1384 -0.0038 66  SER   A N   
464  C CA  . SER   A 60  ? 0.5586 0.4158 0.2072 -0.0191 -0.1538 -0.0012 66  SER   A CA  
465  C C   . SER   A 60  ? 0.5693 0.3982 0.1756 -0.0223 -0.1498 -0.0021 66  SER   A C   
466  O O   . SER   A 60  ? 0.5853 0.3957 0.1724 -0.0282 -0.1607 0.0017  66  SER   A O   
467  C CB  . SER   A 60  ? 0.6071 0.4616 0.2642 -0.0206 -0.1665 -0.0008 66  SER   A CB  
468  O OG  . SER   A 60  ? 0.6675 0.5114 0.3064 -0.0194 -0.1601 -0.0054 66  SER   A OG  
469  N N   . SER   A 61  ? 0.5656 0.3907 0.1582 -0.0186 -0.1330 -0.0062 67  SER   A N   
470  C CA  . SER   A 61  ? 0.5946 0.3898 0.1449 -0.0209 -0.1242 -0.0076 67  SER   A CA  
471  C C   . SER   A 61  ? 0.6056 0.3988 0.1464 -0.0224 -0.1174 -0.0043 67  SER   A C   
472  O O   . SER   A 61  ? 0.6407 0.4067 0.1440 -0.0254 -0.1101 -0.0047 67  SER   A O   
473  C CB  . SER   A 61  ? 0.6108 0.4022 0.1538 -0.0151 -0.1053 -0.0120 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.6291 0.4493 0.2022 -0.0086 -0.0899 -0.0106 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.5786 0.3975 0.1506 -0.0211 -0.1197 -0.0011 68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.5862 0.4040 0.1522 -0.0234 -0.1160 0.0027  68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.5971 0.4203 0.1787 -0.0271 -0.1333 0.0070  68  ARG   A C   
478  O O   . ARG   A 62  ? 0.6197 0.4416 0.1980 -0.0294 -0.1324 0.0106  68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.5835 0.4254 0.1716 -0.0186 -0.0984 0.0034  68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.6147 0.4523 0.1926 -0.0142 -0.0785 0.0019  68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.6568 0.4676 0.1980 -0.0169 -0.0680 0.0032  68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.6904 0.4971 0.2263 -0.0114 -0.0452 0.0025  68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.7186 0.5010 0.2287 -0.0096 -0.0381 -0.0022 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.7167 0.4761 0.2015 -0.0145 -0.0543 -0.0063 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.6946 0.4744 0.2052 -0.0033 -0.0147 -0.0021 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.5820 0.4121 0.1841 -0.0272 -0.1479 0.0074  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.5727 0.4111 0.1993 -0.0287 -0.1618 0.0122  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.5469 0.4047 0.1949 -0.0260 -0.1519 0.0124  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.5526 0.4069 0.2039 -0.0284 -0.1577 0.0169  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.6101 0.4239 0.2152 -0.0360 -0.1789 0.0187  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.6768 0.4744 0.2722 -0.0408 -0.1964 0.0209  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.7479 0.5236 0.3279 -0.0495 -0.2171 0.0301  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.8207 0.5685 0.3691 -0.0579 -0.2325 0.0320  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.8757 0.5890 0.3742 -0.0670 -0.2380 0.0337  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.8657 0.5704 0.3429 -0.0680 -0.2281 0.0340  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 0.8853 0.5702 0.3522 -0.0760 -0.2530 0.0351  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.5165 0.3925 0.1769 -0.0219 -0.1375 0.0083  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.4934 0.3850 0.1694 -0.0214 -0.1288 0.0087  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.4636 0.3764 0.1637 -0.0184 -0.1223 0.0052  70  LYS   A C   
500  O O   . LYS   A 64  ? 0.4466 0.3637 0.1486 -0.0160 -0.1202 0.0027  70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.5272 0.4159 0.1855 -0.0223 -0.1160 0.0100  70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.6405 0.5094 0.2741 -0.0265 -0.1188 0.0141  70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.7293 0.5965 0.3482 -0.0267 -0.1028 0.0157  70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.8178 0.6670 0.4134 -0.0315 -0.1037 0.0203  70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.8833 0.7041 0.4474 -0.0352 -0.1145 0.0208  70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.4536 0.3771 0.1687 -0.0197 -0.1189 0.0054  71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.4461 0.3864 0.1777 -0.0194 -0.1124 0.0028  71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.4431 0.3908 0.1703 -0.0221 -0.1034 0.0053  71  HIS   A C   
509  O O   . HIS   A 65  ? 0.4544 0.3960 0.1728 -0.0247 -0.1022 0.0085  71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.4596 0.4023 0.2071 -0.0206 -0.1139 0.0013  71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.5132 0.4520 0.2736 -0.0175 -0.1209 0.0007  71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.5417 0.4890 0.3165 -0.0156 -0.1189 -0.0023 71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.5346 0.4628 0.2980 -0.0166 -0.1302 0.0042  71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.5321 0.4747 0.3202 -0.0131 -0.1261 -0.0004 71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.5454 0.4769 0.3285 -0.0138 -0.1339 0.0040  71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.4153 0.3761 0.1502 -0.0219 -0.0977 0.0054  72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.4070 0.3775 0.1446 -0.0248 -0.0905 0.0103  72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.4012 0.3851 0.1524 -0.0297 -0.0908 0.0109  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.3849 0.3745 0.1431 -0.0285 -0.0922 0.0083  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.4042 0.3775 0.1400 -0.0206 -0.0829 0.0128  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.4204 0.3763 0.1356 -0.0176 -0.0796 0.0127  72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.4464 0.3964 0.1520 -0.0198 -0.0743 0.0171  72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.4424 0.3853 0.1449 -0.0136 -0.0817 0.0087  72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.4797 0.4097 0.1607 -0.0182 -0.0702 0.0170  72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.4708 0.3924 0.1473 -0.0128 -0.0789 0.0085  72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.4980 0.4125 0.1626 -0.0152 -0.0728 0.0124  72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.5574 0.4472 0.1913 -0.0154 -0.0691 0.0121  72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.4027 0.3906 0.1558 -0.0363 -0.0900 0.0151  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.4022 0.4000 0.1636 -0.0435 -0.0919 0.0170  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.3951 0.4085 0.1693 -0.0430 -0.0888 0.0241  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.4001 0.4170 0.1778 -0.0398 -0.0827 0.0297  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.4125 0.4063 0.1696 -0.0516 -0.0933 0.0202  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.4177 0.4084 0.1711 -0.0479 -0.0893 0.0242  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.4086 0.3909 0.1549 -0.0388 -0.0882 0.0192  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.3750 0.3966 0.1567 -0.0457 -0.0917 0.0245  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.3685 0.4053 0.1664 -0.0448 -0.0897 0.0326  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.3709 0.4167 0.1758 -0.0552 -0.0969 0.0378  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.3780 0.4155 0.1712 -0.0609 -0.1017 0.0320  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.3828 0.4191 0.1827 -0.0351 -0.0863 0.0284  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.3967 0.4235 0.1888 -0.0263 -0.0787 0.0264  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.3891 0.4180 0.1811 -0.0350 -0.0911 0.0195  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.3648 0.4263 0.1893 -0.0575 -0.0972 0.0497  75  SER   A N   
543  C CA  . SER   A 69  ? 0.3743 0.4456 0.2082 -0.0672 -0.1060 0.0574  75  SER   A CA  
544  C C   . SER   A 69  ? 0.3541 0.4328 0.2002 -0.0584 -0.1026 0.0577  75  SER   A C   
545  O O   . SER   A 69  ? 0.3494 0.4315 0.2060 -0.0475 -0.0931 0.0591  75  SER   A O   
546  C CB  . SER   A 69  ? 0.4054 0.4915 0.2601 -0.0749 -0.1096 0.0733  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.4760 0.5541 0.3181 -0.0853 -0.1148 0.0736  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.3494 0.4275 0.1913 -0.0629 -0.1091 0.0559  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.3393 0.4232 0.1922 -0.0552 -0.1068 0.0561  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.3586 0.4526 0.2223 -0.0647 -0.1166 0.0662  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.3630 0.4537 0.2161 -0.0786 -0.1262 0.0692  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.3433 0.4138 0.1795 -0.0479 -0.1033 0.0420  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.3566 0.4151 0.1729 -0.0555 -0.1076 0.0339  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.3773 0.4236 0.1792 -0.0561 -0.1055 0.0266  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.3580 0.4158 0.1700 -0.0619 -0.1124 0.0337  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.3985 0.4318 0.1839 -0.0621 -0.1063 0.0193  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.3840 0.4277 0.1762 -0.0685 -0.1127 0.0258  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.3957 0.4270 0.1756 -0.0680 -0.1088 0.0185  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.3547 0.4585 0.2376 -0.0580 -0.1145 0.0718  77  SER   A N   
560  C CA  . SER   A 71  ? 0.3590 0.4730 0.2551 -0.0666 -0.1248 0.0833  77  SER   A CA  
561  C C   . SER   A 71  ? 0.3704 0.4737 0.2448 -0.0722 -0.1304 0.0750  77  SER   A C   
562  O O   . SER   A 71  ? 0.3873 0.4776 0.2427 -0.0668 -0.1245 0.0608  77  SER   A O   
563  C CB  . SER   A 71  ? 0.3686 0.4968 0.2968 -0.0565 -0.1191 0.0935  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.3736 0.4937 0.2962 -0.0434 -0.1094 0.0828  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.3603 0.4680 0.2373 -0.0840 -0.1421 0.0848  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.3858 0.4819 0.2408 -0.0901 -0.1458 0.0779  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.3766 0.4761 0.2429 -0.0770 -0.1393 0.0738  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.3699 0.4814 0.2622 -0.0676 -0.1358 0.0809  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.4136 0.5103 0.2633 -0.1087 -0.1616 0.0906  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.4901 0.5758 0.3180 -0.1245 -0.1690 0.0918  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.5674 0.6436 0.3750 -0.1460 -0.1851 0.1007  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.6471 0.7101 0.4324 -0.1624 -0.1931 0.1027  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.7030 0.7471 0.4552 -0.1852 -0.2076 0.1077  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.3903 0.4784 0.2384 -0.0764 -0.1367 0.0631  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.3907 0.4812 0.2497 -0.0650 -0.1318 0.0598  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.3802 0.4837 0.2626 -0.0656 -0.1380 0.0739  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.3628 0.4692 0.2436 -0.0789 -0.1491 0.0840  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.4230 0.5004 0.2600 -0.0691 -0.1305 0.0498  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.4501 0.5153 0.2645 -0.0767 -0.1288 0.0432  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.4119 0.4831 0.2298 -0.0860 -0.1368 0.0540  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.3719 0.4815 0.2754 -0.0520 -0.1310 0.0752  80  SER   A N   
582  C CA  . SER   A 74  ? 0.3831 0.5051 0.3140 -0.0506 -0.1348 0.0895  80  SER   A CA  
583  C C   . SER   A 74  ? 0.3820 0.5016 0.3255 -0.0353 -0.1249 0.0855  80  SER   A C   
584  O O   . SER   A 74  ? 0.3893 0.4973 0.3187 -0.0268 -0.1164 0.0722  80  SER   A O   
585  C CB  . SER   A 74  ? 0.4039 0.5399 0.3587 -0.0537 -0.1378 0.1046  80  SER   A CB  
586  O OG  . SER   A 74  ? 0.4713 0.6082 0.4381 -0.0403 -0.1242 0.1018  80  SER   A OG  
587  N N   . LEU   A 75  ? 0.3634 0.4921 0.3325 -0.0328 -0.1271 0.0979  81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.3712 0.4959 0.3541 -0.0191 -0.1175 0.0962  81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.3829 0.5097 0.3833 -0.0083 -0.1044 0.0995  81  LEU   A C   
590  O O   . LEU   A 75  ? 0.3767 0.5183 0.4059 -0.0097 -0.1055 0.1152  81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.3615 0.4961 0.3693 -0.0215 -0.1251 0.1111  81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.3912 0.5185 0.3877 -0.0237 -0.1304 0.1066  81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.3868 0.5242 0.4130 -0.0243 -0.1367 0.1235  81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.3983 0.5095 0.3799 -0.0125 -0.1199 0.0909  81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.3919 0.5032 0.3758 0.0019  -0.0920 0.0861  82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.4030 0.5113 0.3967 0.0119  -0.0768 0.0874  82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.4382 0.5279 0.4266 0.0248  -0.0634 0.0798  82  ILE   A C   
598  O O   . ILE   A 76  ? 0.4461 0.5209 0.4105 0.0251  -0.0664 0.0676  82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.4144 0.5169 0.3847 0.0089  -0.0753 0.0783  82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.4237 0.5434 0.4043 -0.0029 -0.0855 0.0888  82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.4184 0.5079 0.3831 0.0198  -0.0579 0.0734  82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.4660 0.5792 0.4213 -0.0085 -0.0883 0.0793  82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.4526 0.5417 0.4637 0.0349  -0.0482 0.0876  83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.4815 0.5478 0.4839 0.0468  -0.0330 0.0800  83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.5066 0.5479 0.4701 0.0500  -0.0243 0.0639  83  PHE   A C   
606  O O   . PHE   A 77  ? 0.5182 0.5604 0.4775 0.0500  -0.0176 0.0642  83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.4766 0.5474 0.5157 0.0572  -0.0162 0.0936  83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.5017 0.5455 0.5310 0.0691  0.0000  0.0861  83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.5151 0.5545 0.5481 0.0697  -0.0067 0.0859  83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.5271 0.5468 0.5393 0.0785  0.0222  0.0788  83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.5406 0.5516 0.5613 0.0797  0.0079  0.0784  83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.5523 0.5416 0.5497 0.0881  0.0377  0.0710  83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.5493 0.5341 0.5506 0.0886  0.0300  0.0705  83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.5102 0.5289 0.4447 0.0511  -0.0264 0.0510  84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.5235 0.5166 0.4192 0.0518  -0.0225 0.0369  84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.5445 0.5060 0.4223 0.0605  -0.0081 0.0301  84  VAL   A C   
617  O O   . VAL   A 78  ? 0.5546 0.5073 0.4306 0.0613  -0.0127 0.0276  84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.5295 0.5218 0.4034 0.0427  -0.0410 0.0278  84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.5646 0.5287 0.4002 0.0428  -0.0396 0.0152  84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.5083 0.5254 0.3932 0.0341  -0.0521 0.0327  84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.5521 0.4933 0.4132 0.0663  0.0098  0.0266  85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.5701 0.4740 0.4060 0.0738  0.0266  0.0190  85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.5866 0.4642 0.3854 0.0686  0.0138  0.0064  85  GLU   A C   
624  O O   . GLU   A 79  ? 0.5812 0.4634 0.3647 0.0598  -0.0045 0.0014  85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.6202 0.5034 0.4331 0.0774  0.0455  0.0154  85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.6893 0.5949 0.5405 0.0835  0.0618  0.0288  85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.8176 0.7266 0.7048 0.0941  0.0783  0.0387  85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 0.8767 0.7523 0.7436 0.1008  0.0929  0.0315  85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 0.8260 0.7701 0.7622 0.0950  0.0758  0.0543  85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.6039 0.4513 0.3873 0.0740  0.0242  0.0015  86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.6362 0.4541 0.3825 0.0682  0.0120  -0.0097 86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.6637 0.4584 0.3656 0.0607  0.0053  -0.0193 86  ALA   A C   
633  O O   . ALA   A 80  ? 0.6798 0.4654 0.3677 0.0627  0.0184  -0.0201 86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.6514 0.4333 0.3822 0.0752  0.0283  -0.0139 86  ALA   A CB  
635  N N   . SER   A 81  ? 0.6704 0.4567 0.3530 0.0517  -0.0160 -0.0250 87  SER   A N   
636  C CA  . SER   A 81  ? 0.7081 0.4695 0.3492 0.0428  -0.0276 -0.0327 87  SER   A CA  
637  C C   . SER   A 81  ? 0.7520 0.4846 0.3681 0.0367  -0.0410 -0.0388 87  SER   A C   
638  O O   . SER   A 81  ? 0.7565 0.4881 0.3867 0.0407  -0.0377 -0.0376 87  SER   A O   
639  C CB  . SER   A 81  ? 0.6874 0.4808 0.3452 0.0362  -0.0455 -0.0293 87  SER   A CB  
640  O OG  . SER   A 81  ? 0.6744 0.4887 0.3547 0.0319  -0.0634 -0.0269 87  SER   A OG  
641  N N   . GLU   A 82  ? 0.7838 0.4941 0.3658 0.0263  -0.0578 -0.0439 88  GLU   A N   
642  C CA  . GLU   A 82  ? 0.8212 0.5058 0.3818 0.0184  -0.0740 -0.0478 88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.7923 0.5118 0.3918 0.0150  -0.0933 -0.0422 88  GLU   A C   
644  O O   . GLU   A 82  ? 0.8069 0.5116 0.3995 0.0099  -0.1051 -0.0435 88  GLU   A O   
645  C CB  . GLU   A 82  ? 0.9066 0.5554 0.4194 0.0069  -0.0880 -0.0527 88  GLU   A CB  
646  C CG  . GLU   A 82  ? 1.0358 0.6458 0.5037 0.0086  -0.0684 -0.0587 88  GLU   A CG  
647  C CD  . GLU   A 82  ? 1.1481 0.7734 0.6171 0.0086  -0.0657 -0.0561 88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 1.1279 0.7997 0.6423 0.0133  -0.0666 -0.0497 88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 1.2019 0.7902 0.6235 0.0028  -0.0631 -0.0606 88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.7469 0.5099 0.3849 0.0173  -0.0957 -0.0359 89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.7136 0.5090 0.3864 0.0140  -0.1106 -0.0306 89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.6596 0.4801 0.3670 0.0206  -0.1020 -0.0254 89  TYR   A C   
653  O O   . TYR   A 83  ? 0.6489 0.4838 0.3760 0.0175  -0.1125 -0.0222 89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.7105 0.5324 0.3985 0.0106  -0.1190 -0.0274 89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.7535 0.5524 0.4122 0.0026  -0.1319 -0.0303 89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.7806 0.5697 0.4352 -0.0061 -0.1519 -0.0294 89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.7845 0.5700 0.4195 0.0030  -0.1251 -0.0327 89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.8180 0.5851 0.4469 -0.0148 -0.1665 -0.0299 89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.8226 0.5850 0.4288 -0.0055 -0.1387 -0.0341 89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.8516 0.6047 0.4551 -0.0146 -0.1603 -0.0323 89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 0.9143 0.6440 0.4908 -0.0244 -0.1765 -0.0316 89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.6204 0.4463 0.3367 0.0292  -0.0834 -0.0232 90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.5773 0.4269 0.3282 0.0349  -0.0765 -0.0160 90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.5872 0.4207 0.3364 0.0448  -0.0549 -0.0153 90  TYR   A C   
665  O O   . TYR   A 84  ? 0.6026 0.4226 0.3351 0.0483  -0.0419 -0.0179 90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.5353 0.4243 0.3167 0.0345  -0.0777 -0.0087 90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.5031 0.4103 0.2901 0.0263  -0.0938 -0.0087 90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.4866 0.4091 0.2914 0.0219  -0.1044 -0.0055 90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.4942 0.4047 0.2718 0.0234  -0.0963 -0.0108 90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.4757 0.4143 0.2881 0.0154  -0.1153 -0.0051 90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.4802 0.4072 0.2667 0.0171  -0.1083 -0.0102 90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.4678 0.4085 0.2720 0.0135  -0.1168 -0.0074 90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.4282 0.3825 0.2416 0.0080  -0.1255 -0.0069 90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.5737 0.4125 0.3457 0.0501  -0.0493 -0.0100 91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.5709 0.4017 0.3535 0.0611  -0.0265 -0.0062 91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.5489 0.4154 0.3649 0.0641  -0.0206 0.0040  91  PRO   A C   
677  O O   . PRO   A 85  ? 0.5331 0.4274 0.3608 0.0572  -0.0348 0.0071  91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.5643 0.3969 0.3688 0.0644  -0.0270 -0.0010 91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.5592 0.4206 0.3806 0.0553  -0.0491 0.0028  91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.5540 0.4099 0.3484 0.0465  -0.0625 -0.0052 91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.5395 0.4054 0.3731 0.0740  0.0003  0.0103  92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.5188 0.4192 0.3877 0.0757  0.0039  0.0222  92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.4886 0.4240 0.3939 0.0707  -0.0126 0.0333  92  ALA   A C   
684  O O   . ALA   A 86  ? 0.4953 0.4277 0.4124 0.0727  -0.0147 0.0364  92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.5234 0.4166 0.4106 0.0876  0.0298  0.0289  92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.4522 0.4160 0.3684 0.0628  -0.0254 0.0380  93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.4215 0.4126 0.3615 0.0555  -0.0420 0.0469  93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.4122 0.4311 0.3666 0.0484  -0.0493 0.0546  93  ARG   A C   
689  O O   . ARG   A 87  ? 0.4258 0.4430 0.3702 0.0491  -0.0431 0.0515  93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.4174 0.4002 0.3342 0.0480  -0.0572 0.0371  93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.4195 0.4062 0.3157 0.0402  -0.0666 0.0296  93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.4416 0.4095 0.3105 0.0364  -0.0751 0.0182  93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.4455 0.4267 0.3097 0.0278  -0.0872 0.0157  93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.4480 0.4299 0.3005 0.0258  -0.0870 0.0120  93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.4032 0.3950 0.2536 0.0189  -0.0966 0.0099  93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.4683 0.4391 0.3108 0.0310  -0.0761 0.0103  93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.3931 0.4346 0.3655 0.0401  -0.0636 0.0636  94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.3864 0.4490 0.3644 0.0308  -0.0728 0.0693  94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.3781 0.4365 0.3281 0.0225  -0.0834 0.0578  94  TYR   A C   
700  O O   . TYR   A 88  ? 0.3775 0.4327 0.3216 0.0190  -0.0911 0.0548  94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.3886 0.4732 0.3957 0.0240  -0.0835 0.0856  94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.4007 0.4964 0.4443 0.0305  -0.0748 0.1012  94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.4142 0.5251 0.4731 0.0277  -0.0739 0.1103  94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.4196 0.5090 0.4840 0.0404  -0.0658 0.1068  94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.4231 0.5456 0.5212 0.0342  -0.0650 0.1263  94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.4286 0.5286 0.5323 0.0478  -0.0557 0.1225  94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.4414 0.5589 0.5634 0.0447  -0.0551 0.1327  94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.4676 0.5976 0.6342 0.0520  -0.0448 0.1502  94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.3583 0.4164 0.2931 0.0196  -0.0830 0.0520  95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.3496 0.4056 0.2635 0.0120  -0.0920 0.0430  95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.3417 0.4156 0.2625 0.0012  -0.1007 0.0505  95  GLN   A C   
712  O O   . GLN   A 89  ? 0.3463 0.4310 0.2790 -0.0005 -0.0994 0.0588  95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.3648 0.4070 0.2568 0.0148  -0.0873 0.0325  95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.3639 0.4052 0.2401 0.0078  -0.0957 0.0249  95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.3915 0.4156 0.2472 0.0110  -0.0936 0.0153  95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.4135 0.4199 0.2587 0.0167  -0.0897 0.0110  95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.3749 0.4013 0.2224 0.0065  -0.0969 0.0119  95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.3218 0.3977 0.2351 -0.0068 -0.1093 0.0486  96  SER   A N   
719  C CA  . SER   A 90  ? 0.3087 0.3954 0.2208 -0.0190 -0.1171 0.0547  96  SER   A CA  
720  C C   . SER   A 90  ? 0.3177 0.3994 0.2097 -0.0237 -0.1167 0.0458  96  SER   A C   
721  O O   . SER   A 90  ? 0.3140 0.3854 0.1954 -0.0181 -0.1125 0.0354  96  SER   A O   
722  C CB  . SER   A 90  ? 0.3080 0.3962 0.2196 -0.0260 -0.1243 0.0581  96  SER   A CB  
723  O OG  . SER   A 90  ? 0.3365 0.4145 0.2346 -0.0246 -0.1228 0.0472  96  SER   A OG  
724  N N   . HIS   A 91  ? 0.3114 0.3983 0.1977 -0.0350 -0.1220 0.0505  97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.3220 0.4022 0.1893 -0.0400 -0.1207 0.0426  97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.3262 0.4028 0.1921 -0.0320 -0.1144 0.0369  97  HIS   A C   
727  O O   . HIS   A 91  ? 0.3373 0.4050 0.1900 -0.0310 -0.1116 0.0275  97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.3414 0.4124 0.1957 -0.0416 -0.1191 0.0335  97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.3734 0.4452 0.2244 -0.0507 -0.1238 0.0386  97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.4118 0.4786 0.2451 -0.0638 -0.1262 0.0399  97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.3884 0.4634 0.2493 -0.0493 -0.1268 0.0432  97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.4154 0.4821 0.2467 -0.0703 -0.1304 0.0453  97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.4054 0.4783 0.2548 -0.0618 -0.1312 0.0478  97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.3089 0.3913 0.1891 -0.0260 -0.1113 0.0432  98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.3319 0.4092 0.2089 -0.0188 -0.1041 0.0389  98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.3374 0.4224 0.2179 -0.0248 -0.1052 0.0457  98  LEU   A C   
737  O O   . LEU   A 92  ? 0.3411 0.4381 0.2367 -0.0307 -0.1100 0.0575  98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.3367 0.4115 0.2253 -0.0078 -0.0964 0.0411  98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.3680 0.4319 0.2477 0.0000  -0.0871 0.0358  98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.3755 0.4249 0.2329 0.0004  -0.0892 0.0238  98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.3820 0.4396 0.2704 0.0100  -0.0771 0.0381  98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.3301 0.4081 0.1979 -0.0240 -0.1018 0.0394  99  MET   A N   
743  C CA  . MET   A 93  ? 0.3317 0.4151 0.2009 -0.0300 -0.1028 0.0449  99  MET   A CA  
744  C C   . MET   A 93  ? 0.3446 0.4243 0.2153 -0.0212 -0.0932 0.0438  99  MET   A C   
745  O O   . MET   A 93  ? 0.3603 0.4267 0.2156 -0.0155 -0.0895 0.0338  99  MET   A O   
746  C CB  . MET   A 93  ? 0.3415 0.4165 0.1905 -0.0382 -0.1068 0.0376  99  MET   A CB  
747  C CG  . MET   A 93  ? 0.3641 0.4379 0.2052 -0.0483 -0.1137 0.0378  99  MET   A CG  
748  S SD  . MET   A 93  ? 0.4268 0.4847 0.2430 -0.0544 -0.1123 0.0266  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.4220 0.4722 0.2382 -0.0413 -0.1058 0.0158  99  MET   A CE  
750  N N   . LEU   A 94  ? 0.3319 0.4222 0.2212 -0.0206 -0.0892 0.0549  100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.3422 0.4263 0.2299 -0.0125 -0.0774 0.0536  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.3361 0.4221 0.2192 -0.0191 -0.0789 0.0558  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.3260 0.4221 0.2159 -0.0298 -0.0881 0.0630  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.3446 0.4369 0.2582 -0.0049 -0.0668 0.0644  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.3717 0.4611 0.2931 0.0025  -0.0634 0.0639  100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.3719 0.4675 0.3209 0.0110  -0.0497 0.0750  100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.3950 0.4629 0.2889 0.0085  -0.0603 0.0491  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.3405 0.4151 0.2108 -0.0134 -0.0702 0.0505  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.3516 0.4255 0.2166 -0.0178 -0.0693 0.0523  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.3555 0.4215 0.2188 -0.0088 -0.0541 0.0531  101 ALA   A C   
761  O O   . ALA   A 95  ? 0.3579 0.4120 0.2133 -0.0001 -0.0459 0.0480  101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.3657 0.4263 0.2057 -0.0215 -0.0760 0.0410  101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.3552 0.4253 0.2234 -0.0118 -0.0500 0.0596  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.3762 0.4361 0.2387 -0.0046 -0.0341 0.0603  102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.4121 0.4506 0.2398 -0.0048 -0.0370 0.0479  102 VAL   A C   
766  O O   . VAL   A 96  ? 0.4233 0.4620 0.2433 -0.0121 -0.0466 0.0460  102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.3724 0.4474 0.2583 -0.0084 -0.0286 0.0742  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.3802 0.4426 0.2574 -0.0014 -0.0097 0.0747  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.3585 0.4567 0.2841 -0.0095 -0.0291 0.0891  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.4185 0.4371 0.2251 0.0023  -0.0302 0.0399  103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.4361 0.4336 0.2112 0.0014  -0.0354 0.0301  103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.4554 0.4291 0.2063 0.0075  -0.0300 0.0226  103 GLY   A C   
773  O O   . GLY   A 97  ? 0.4569 0.4297 0.2148 0.0132  -0.0220 0.0233  103 GLY   A O   
774  N N   . HIS   A 98  ? 0.4560 0.4085 0.1775 0.0056  -0.0351 0.0162  104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.4806 0.4054 0.1725 0.0086  -0.0326 0.0094  104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.4792 0.4017 0.1702 0.0082  -0.0466 0.0034  104 HIS   A C   
777  O O   . HIS   A 98  ? 0.4696 0.4005 0.1676 0.0042  -0.0609 0.0019  104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.5176 0.4183 0.1765 0.0050  -0.0340 0.0070  104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.6089 0.4764 0.2315 0.0060  -0.0317 0.0010  104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.6490 0.5016 0.2605 0.0115  -0.0124 0.0005  104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.6488 0.4954 0.2459 0.0015  -0.0469 -0.0041 104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.6869 0.5064 0.2604 0.0093  -0.0164 -0.0061 104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.6915 0.5072 0.2560 0.0027  -0.0386 -0.0083 104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.4972 0.4058 0.1784 0.0125  -0.0412 0.0002  105 SER   A N   
785  C CA  . SER   A 99  ? 0.5193 0.4239 0.1990 0.0118  -0.0536 -0.0047 105 SER   A CA  
786  C C   . SER   A 99  ? 0.5615 0.4351 0.2116 0.0143  -0.0477 -0.0098 105 SER   A C   
787  O O   . SER   A 99  ? 0.5861 0.4539 0.2358 0.0200  -0.0301 -0.0085 105 SER   A O   
788  C CB  . SER   A 99  ? 0.5272 0.4584 0.2407 0.0139  -0.0544 -0.0015 105 SER   A CB  
789  O OG  . SER   A 99  ? 0.5845 0.5140 0.2993 0.0130  -0.0660 -0.0055 105 SER   A OG  
790  N N   . GLU   A 100 ? 0.5633 0.4157 0.1892 0.0096  -0.0621 -0.0147 106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.5900 0.4093 0.1835 0.0091  -0.0614 -0.0199 106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.5936 0.4180 0.1988 0.0070  -0.0778 -0.0218 106 GLU   A C   
793  O O   . GLU   A 100 ? 0.5772 0.4251 0.2081 0.0049  -0.0903 -0.0194 106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.6340 0.4188 0.1833 0.0024  -0.0663 -0.0223 106 GLU   A CB  
795  C CG  . GLU   A 100 ? 0.6985 0.4732 0.2317 0.0046  -0.0467 -0.0208 106 GLU   A CG  
796  C CD  . GLU   A 100 ? 0.7456 0.4865 0.2335 -0.0032 -0.0518 -0.0220 106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 0.7389 0.4486 0.1926 -0.0098 -0.0642 -0.0258 106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 0.7722 0.5167 0.2580 -0.0038 -0.0445 -0.0185 106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.6220 0.4245 0.2102 0.0077  -0.0769 -0.0259 107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.6065 0.4176 0.2110 0.0057  -0.0921 -0.0264 107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.5857 0.4033 0.1973 -0.0016 -0.1145 -0.0244 107 PRO   A C   
802  O O   . PRO   A 101 ? 0.5677 0.4092 0.2103 -0.0014 -0.1226 -0.0222 107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.6488 0.4248 0.2217 0.0051  -0.0890 -0.0315 107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.6677 0.4287 0.2243 0.0115  -0.0641 -0.0330 107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.6383 0.4079 0.1940 0.0106  -0.0598 -0.0299 107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.5865 0.3828 0.1711 -0.0079 -0.1235 -0.0241 108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.5771 0.3786 0.1716 -0.0145 -0.1447 -0.0201 108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.5464 0.3813 0.1768 -0.0119 -0.1444 -0.0163 108 GLY   A C   
809  O O   . GLY   A 102 ? 0.5396 0.3828 0.1869 -0.0155 -0.1590 -0.0124 108 GLY   A O   
810  N N   . ASP   A 103 ? 0.5204 0.3723 0.1620 -0.0062 -0.1276 -0.0167 109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.4930 0.3732 0.1641 -0.0048 -0.1259 -0.0138 109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.4628 0.3675 0.1663 -0.0027 -0.1270 -0.0134 109 ASP   A C   
813  O O   . ASP   A 103 ? 0.4417 0.3656 0.1668 -0.0029 -0.1271 -0.0116 109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.5010 0.3894 0.1716 -0.0015 -0.1097 -0.0129 109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.5442 0.4115 0.1862 -0.0043 -0.1085 -0.0124 109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.5440 0.4023 0.1788 -0.0092 -0.1223 -0.0110 109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.5436 0.4030 0.1714 -0.0017 -0.0934 -0.0126 109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.4592 0.3612 0.1643 -0.0013 -0.1273 -0.0150 110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.4459 0.3699 0.1799 -0.0002 -0.1283 -0.0141 110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.4410 0.3728 0.1927 -0.0035 -0.1400 -0.0119 110 CYS   A C   
821  O O   . CYS   A 104 ? 0.4465 0.3634 0.1893 -0.0070 -0.1519 -0.0106 110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.4507 0.3673 0.1819 0.0012  -0.1284 -0.0156 110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.4898 0.4022 0.2120 0.0072  -0.1109 -0.0165 110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.4113 0.3639 0.1864 -0.0030 -0.1359 -0.0109 111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.4114 0.3707 0.2059 -0.0049 -0.1426 -0.0087 111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.4104 0.3742 0.2083 -0.0053 -0.1389 -0.0081 111 GLY   A C   
827  O O   . GLY   A 105 ? 0.4065 0.3785 0.2238 -0.0056 -0.1384 -0.0068 111 GLY   A O   
828  N N   . GLY   A 106 ? 0.4019 0.3594 0.1817 -0.0051 -0.1348 -0.0088 112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.3861 0.3471 0.1676 -0.0060 -0.1309 -0.0081 112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.3682 0.3452 0.1634 -0.0066 -0.1219 -0.0092 112 GLY   A C   
831  O O   . GLY   A 106 ? 0.3408 0.3259 0.1363 -0.0066 -0.1165 -0.0097 112 GLY   A O   
832  N N   . ILE   A 107 ? 0.3633 0.3429 0.1697 -0.0078 -0.1205 -0.0091 113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.3757 0.3642 0.1892 -0.0101 -0.1120 -0.0108 113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.3733 0.3640 0.1753 -0.0135 -0.1066 -0.0107 113 ILE   A C   
835  O O   . ILE   A 107 ? 0.3867 0.3714 0.1807 -0.0136 -0.1078 -0.0096 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.4039 0.3903 0.2338 -0.0096 -0.1105 -0.0110 113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.4264 0.4163 0.2734 -0.0077 -0.1131 -0.0099 113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.4227 0.4095 0.2512 -0.0132 -0.1001 -0.0137 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.4468 0.4350 0.3172 -0.0056 -0.1112 -0.0078 113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.3579 0.3566 0.1596 -0.0173 -0.1018 -0.0107 114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.3556 0.3571 0.1494 -0.0228 -0.0985 -0.0091 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.3598 0.3567 0.1526 -0.0280 -0.0939 -0.0121 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.3563 0.3540 0.1537 -0.0287 -0.0913 -0.0139 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.3553 0.3674 0.1495 -0.0250 -0.0982 -0.0050 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.3709 0.3877 0.1607 -0.0333 -0.0974 -0.0009 114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.3677 0.3832 0.1536 -0.0330 -0.0968 0.0020  114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.3860 0.4147 0.1823 -0.0359 -0.0989 0.0052  114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.3686 0.3581 0.1540 -0.0317 -0.0917 -0.0128 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.3972 0.3766 0.1774 -0.0367 -0.0852 -0.0166 115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.4123 0.3873 0.1769 -0.0461 -0.0849 -0.0154 115 ARG   A C   
851  O O   . ARG   A 109 ? 0.4076 0.3846 0.1701 -0.0465 -0.0886 -0.0121 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.4354 0.4042 0.2230 -0.0318 -0.0822 -0.0191 115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.5161 0.4873 0.3222 -0.0236 -0.0843 -0.0186 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.5914 0.5525 0.4079 -0.0198 -0.0825 -0.0186 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.6642 0.6206 0.4960 -0.0173 -0.0731 -0.0205 115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.6972 0.6589 0.5517 -0.0115 -0.0756 -0.0176 115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.7191 0.6878 0.5792 -0.0087 -0.0887 -0.0133 115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.6967 0.6548 0.5679 -0.0092 -0.0645 -0.0186 115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.4322 0.3977 0.1843 -0.0544 -0.0801 -0.0181 116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.4625 0.4182 0.1958 -0.0658 -0.0809 -0.0173 116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.5055 0.4385 0.2277 -0.0676 -0.0704 -0.0246 116 CYS   A C   
862  O O   . CYS   A 110 ? 0.5053 0.4344 0.2401 -0.0590 -0.0629 -0.0285 116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.4640 0.4233 0.1863 -0.0766 -0.0854 -0.0134 116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.4364 0.3839 0.1481 -0.0798 -0.0769 -0.0191 116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.5445 0.4612 0.2446 -0.0789 -0.0695 -0.0258 117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.5838 0.4744 0.2702 -0.0810 -0.0571 -0.0334 117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.5915 0.4714 0.2739 -0.0800 -0.0444 -0.0391 117 GLN   A C   
868  O O   . GLN   A 111 ? 0.6247 0.4856 0.3057 -0.0767 -0.0302 -0.0453 117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.6432 0.5145 0.2997 -0.0964 -0.0593 -0.0338 117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.7281 0.5981 0.3635 -0.1108 -0.0662 -0.0305 117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.8353 0.6827 0.4381 -0.1285 -0.0705 -0.0302 117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.8651 0.7224 0.4635 -0.1396 -0.0853 -0.0212 117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.8522 0.6678 0.4326 -0.1318 -0.0575 -0.0392 117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.5617 0.4533 0.2443 -0.0824 -0.0483 -0.0366 118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.5542 0.4358 0.2322 -0.0823 -0.0359 -0.0412 118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.5139 0.4117 0.2252 -0.0677 -0.0321 -0.0406 118 HIS   A C   
877  O O   . HIS   A 112 ? 0.5174 0.4084 0.2305 -0.0662 -0.0204 -0.0436 118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.5760 0.4575 0.2322 -0.0952 -0.0423 -0.0382 118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.6508 0.5157 0.2738 -0.1122 -0.0491 -0.0368 118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.6813 0.5627 0.3078 -0.1180 -0.0665 -0.0279 118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.6866 0.5187 0.2725 -0.1253 -0.0407 -0.0425 118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.6923 0.5528 0.2865 -0.1348 -0.0706 -0.0274 118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.7042 0.5327 0.2701 -0.1402 -0.0557 -0.0367 118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.4767 0.3942 0.2122 -0.0583 -0.0424 -0.0361 119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.4396 0.3708 0.2046 -0.0465 -0.0425 -0.0343 119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.4037 0.3564 0.1795 -0.0432 -0.0565 -0.0288 119 GLY   A C   
887  O O   . GLY   A 113 ? 0.4144 0.3738 0.1817 -0.0469 -0.0657 -0.0255 119 GLY   A O   
888  N N   . VAL   A 114 ? 0.3728 0.3352 0.1683 -0.0363 -0.0572 -0.0274 120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.3662 0.3447 0.1711 -0.0324 -0.0687 -0.0231 120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.3640 0.3490 0.1560 -0.0395 -0.0725 -0.0209 120 VAL   A C   
891  O O   . VAL   A 114 ? 0.3902 0.3713 0.1750 -0.0447 -0.0669 -0.0221 120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.3843 0.3684 0.2130 -0.0247 -0.0692 -0.0217 120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.3928 0.3889 0.2259 -0.0219 -0.0805 -0.0183 120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.3780 0.3575 0.2242 -0.0181 -0.0691 -0.0209 120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.3471 0.3413 0.1367 -0.0397 -0.0814 -0.0169 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.3483 0.3511 0.1320 -0.0455 -0.0864 -0.0122 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.3333 0.3471 0.1309 -0.0389 -0.0908 -0.0096 121 VAL   A C   
898  O O   . VAL   A 115 ? 0.3483 0.3670 0.1460 -0.0423 -0.0922 -0.0070 121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.3629 0.3696 0.1406 -0.0494 -0.0916 -0.0076 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.3716 0.3903 0.1520 -0.0537 -0.0978 0.0000  121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.3798 0.3737 0.1412 -0.0578 -0.0887 -0.0097 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.3121 0.3277 0.1188 -0.0305 -0.0938 -0.0100 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.3059 0.3271 0.1217 -0.0248 -0.0981 -0.0083 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.3254 0.3420 0.1436 -0.0178 -0.1019 -0.0093 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.3253 0.3356 0.1413 -0.0169 -0.1017 -0.0109 122 GLY   A O   
906  N N   . ILE   A 117 ? 0.3341 0.3512 0.1544 -0.0136 -0.1056 -0.0082 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.3429 0.3505 0.1585 -0.0088 -0.1102 -0.0091 123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.3535 0.3589 0.1603 -0.0060 -0.1088 -0.0074 123 ILE   A C   
909  O O   . ILE   A 117 ? 0.3360 0.3483 0.1474 -0.0057 -0.1064 -0.0051 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.3530 0.3560 0.1770 -0.0069 -0.1164 -0.0098 123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.3660 0.3747 0.1966 -0.0071 -0.1163 -0.0090 123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.3653 0.3681 0.2017 -0.0079 -0.1165 -0.0102 123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.3789 0.3822 0.2175 -0.0058 -0.1239 -0.0087 123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.3509 0.3450 0.1451 -0.0037 -0.1096 -0.0081 124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.3621 0.3497 0.1458 -0.0002 -0.1049 -0.0071 124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.3750 0.3574 0.1591 0.0024  -0.1066 -0.0080 124 VAL   A C   
917  O O   . VAL   A 118 ? 0.3887 0.3641 0.1725 0.0016  -0.1146 -0.0101 124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.3817 0.3522 0.1460 0.0006  -0.1055 -0.0084 124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.3988 0.3572 0.1486 0.0045  -0.0977 -0.0084 124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.3815 0.3571 0.1459 -0.0018 -0.1030 -0.0068 124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.3669 0.3529 0.1542 0.0053  -0.0992 -0.0055 125 SER   A N   
922  C CA  . SER   A 119 ? 0.3885 0.3692 0.1771 0.0082  -0.0991 -0.0059 125 SER   A CA  
923  C C   . SER   A 119 ? 0.4065 0.3760 0.1864 0.0137  -0.0883 -0.0050 125 SER   A C   
924  O O   . SER   A 119 ? 0.4161 0.3694 0.1858 0.0164  -0.0877 -0.0077 125 SER   A O   
925  C CB  . SER   A 119 ? 0.3905 0.3895 0.1993 0.0061  -0.1004 -0.0022 125 SER   A CB  
926  O OG  . SER   A 119 ? 0.4126 0.4065 0.2239 0.0087  -0.1009 -0.0022 125 SER   A OG  
927  N N   . THR   A 120 ? 0.4044 0.3811 0.1888 0.0153  -0.0788 -0.0007 126 THR   A N   
928  C CA  . THR   A 120 ? 0.4240 0.3907 0.2044 0.0216  -0.0646 0.0013  126 THR   A CA  
929  C C   . THR   A 120 ? 0.4560 0.4166 0.2251 0.0223  -0.0558 0.0023  126 THR   A C   
930  O O   . THR   A 120 ? 0.4567 0.4236 0.2237 0.0176  -0.0620 0.0021  126 THR   A O   
931  C CB  . THR   A 120 ? 0.4250 0.4106 0.2340 0.0244  -0.0588 0.0097  126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.4191 0.4265 0.2464 0.0206  -0.0591 0.0172  126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.4171 0.4102 0.2375 0.0225  -0.0681 0.0099  126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.4842 0.4321 0.2469 0.0283  -0.0401 0.0037  127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.5085 0.4501 0.2613 0.0292  -0.0291 0.0055  127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.5336 0.4591 0.2813 0.0370  -0.0078 0.0072  127 GLY   A C   
937  O O   . GLY   A 121 ? 0.5424 0.4617 0.2957 0.0422  -0.0015 0.0071  127 GLY   A O   
938  N N   . GLY   A 122 ? 0.5566 0.4731 0.2926 0.0379  0.0046  0.0087  128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.5770 0.4760 0.3075 0.0458  0.0292  0.0106  128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.5602 0.4855 0.3292 0.0492  0.0421  0.0235  128 GLY   A C   
941  O O   . GLY   A 122 ? 0.5269 0.4845 0.3306 0.0459  0.0308  0.0315  128 GLY   A O   
942  N N   . ASN   A 123 ? 0.5698 0.4804 0.3319 0.0546  0.0656  0.0262  129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.5561 0.4912 0.3581 0.0580  0.0798  0.0403  129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.5378 0.4976 0.3521 0.0490  0.0648  0.0459  129 ASN   A C   
945  O O   . ASN   A 123 ? 0.5284 0.5185 0.3846 0.0480  0.0646  0.0593  129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.5536 0.5142 0.4046 0.0635  0.0823  0.0516  129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.6134 0.5520 0.4619 0.0741  0.1021  0.0492  129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.6514 0.5594 0.4747 0.0802  0.1259  0.0447  129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.6155 0.5673 0.4889 0.0762  0.0937  0.0525  129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.5209 0.4677 0.3006 0.0418  0.0509  0.0366  130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.4998 0.4656 0.2879 0.0334  0.0373  0.0406  130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.4622 0.4555 0.2756 0.0273  0.0161  0.0436  130 GLY   A C   
953  O O   . GLY   A 124 ? 0.4474 0.4591 0.2749 0.0203  0.0069  0.0493  130 GLY   A O   
954  N N   . LEU   A 125 ? 0.4445 0.4380 0.2606 0.0290  0.0085  0.0395  131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.4321 0.4468 0.2661 0.0228  -0.0102 0.0413  131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.4478 0.4481 0.2549 0.0200  -0.0242 0.0289  131 LEU   A C   
957  O O   . LEU   A 125 ? 0.4870 0.4630 0.2682 0.0238  -0.0203 0.0208  131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.4158 0.4463 0.2817 0.0265  -0.0079 0.0495  131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.4195 0.4676 0.3217 0.0296  0.0050  0.0648  131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.4136 0.4724 0.3456 0.0348  0.0079  0.0727  131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.4210 0.4921 0.3421 0.0196  -0.0063 0.0745  131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.4058 0.4196 0.2196 0.0130  -0.0400 0.0282  132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.3903 0.3952 0.1882 0.0106  -0.0525 0.0189  132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.3681 0.3911 0.1860 0.0067  -0.0617 0.0219  132 VAL   A C   
965  O O   . VAL   A 126 ? 0.3552 0.3954 0.1896 0.0012  -0.0649 0.0291  132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.3937 0.3910 0.1742 0.0056  -0.0604 0.0138  132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.3859 0.3991 0.1789 -0.0007 -0.0629 0.0197  132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.4026 0.3947 0.1760 0.0034  -0.0728 0.0068  132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.3574 0.3749 0.1723 0.0088  -0.0660 0.0172  133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.3515 0.3829 0.1813 0.0048  -0.0741 0.0196  133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.3583 0.3847 0.1776 0.0009  -0.0840 0.0120  133 GLY   A C   
972  O O   . GLY   A 127 ? 0.3763 0.3874 0.1808 0.0036  -0.0860 0.0054  133 GLY   A O   
973  N N   . PHE   A 128 ? 0.3467 0.3847 0.1738 -0.0060 -0.0901 0.0139  134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.3520 0.3866 0.1732 -0.0097 -0.0963 0.0080  134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.3555 0.3973 0.1852 -0.0128 -0.0997 0.0097  134 PHE   A C   
976  O O   . PHE   A 128 ? 0.3660 0.4184 0.2041 -0.0176 -0.1007 0.0165  134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.3419 0.3780 0.1584 -0.0163 -0.0977 0.0075  134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.3415 0.3725 0.1508 -0.0148 -0.0946 0.0076  134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.3422 0.3604 0.1406 -0.0117 -0.0957 0.0021  134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.3372 0.3763 0.1517 -0.0178 -0.0918 0.0146  134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.3508 0.3629 0.1406 -0.0111 -0.0931 0.0028  134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.3437 0.3780 0.1517 -0.0168 -0.0883 0.0151  134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.3448 0.3648 0.1388 -0.0133 -0.0886 0.0088  134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.3484 0.3841 0.1765 -0.0111 -0.1025 0.0047  135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.3426 0.3832 0.1772 -0.0143 -0.1050 0.0058  135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.3495 0.3914 0.1799 -0.0220 -0.1049 0.0043  135 ALA   A C   
987  O O   . ALA   A 129 ? 0.3549 0.3901 0.1817 -0.0213 -0.1038 -0.0009 135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.3428 0.3756 0.1784 -0.0101 -0.1076 0.0015  135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.3418 0.3902 0.1717 -0.0297 -0.1059 0.0093  136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.3539 0.3980 0.1730 -0.0386 -0.1045 0.0074  136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.3651 0.4037 0.1840 -0.0387 -0.1012 0.0026  136 ASP   A C   
992  O O   . ASP   A 130 ? 0.3698 0.4119 0.1970 -0.0362 -0.1030 0.0041  136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.3595 0.4089 0.1746 -0.0490 -0.1088 0.0152  136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.4127 0.4520 0.2087 -0.0603 -0.1072 0.0130  136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.3958 0.4282 0.1840 -0.0609 -0.1041 0.0089  136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.4652 0.5009 0.2518 -0.0691 -0.1086 0.0152  136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.3529 0.3824 0.1642 -0.0415 -0.0953 -0.0026 137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.3484 0.3728 0.1621 -0.0421 -0.0893 -0.0059 137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.3686 0.3818 0.1633 -0.0526 -0.0819 -0.0076 137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.3783 0.3851 0.1729 -0.0538 -0.0736 -0.0102 137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.3473 0.3685 0.1745 -0.0339 -0.0862 -0.0099 137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.3304 0.3571 0.1696 -0.0260 -0.0946 -0.0084 137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.3481 0.3613 0.1695 -0.0339 -0.0818 -0.0134 137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.3678 0.3770 0.1456 -0.0609 -0.0845 -0.0058 138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.3868 0.3798 0.1395 -0.0727 -0.0787 -0.0080 138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.4185 0.4059 0.1571 -0.0824 -0.0777 -0.0054 138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.4627 0.4309 0.1774 -0.0915 -0.0687 -0.0093 138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.4087 0.3993 0.1476 -0.0807 -0.0855 -0.0048 138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.4129 0.4038 0.1593 -0.0733 -0.0841 -0.0082 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.4235 0.4131 0.1579 -0.0823 -0.0914 -0.0036 138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.4140 0.4221 0.1633 -0.0813 -0.1021 0.0059  138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.4403 0.4543 0.1902 -0.0869 -0.1099 0.0132  138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.4138 0.4155 0.1464 -0.0958 -0.1101 0.0119  138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.4384 0.4699 0.2077 -0.0838 -0.1167 0.0226  138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.4068 0.4079 0.1575 -0.0813 -0.0863 0.0012  139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.4191 0.4156 0.1578 -0.0905 -0.0868 0.0050  139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.4280 0.4214 0.1750 -0.0850 -0.0756 0.0005  139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.4478 0.4330 0.1805 -0.0935 -0.0722 0.0022  139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.4348 0.4471 0.1858 -0.0915 -0.1009 0.0154  139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.4631 0.4910 0.2435 -0.0771 -0.1029 0.0160  139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.4254 0.4563 0.2176 -0.0668 -0.1000 0.0109  139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.4895 0.5245 0.2792 -0.0768 -0.1080 0.0216  139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.4063 0.4061 0.1768 -0.0719 -0.0708 -0.0039 140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.3971 0.3969 0.1829 -0.0663 -0.0615 -0.0062 140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.4061 0.3876 0.1792 -0.0695 -0.0438 -0.0123 140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.4038 0.3843 0.1931 -0.0613 -0.0362 -0.0161 140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.3784 0.3909 0.1943 -0.0530 -0.0665 -0.0064 140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.3698 0.3951 0.1943 -0.0489 -0.0810 -0.0018 140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.3544 0.3853 0.1996 -0.0379 -0.0857 -0.0031 140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.3636 0.3938 0.1881 -0.0531 -0.0859 0.0038  140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.4122 0.3771 0.1549 -0.0822 -0.0369 -0.0128 141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.4532 0.3948 0.1768 -0.0866 -0.0172 -0.0194 141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.4918 0.4337 0.2398 -0.0780 -0.0006 -0.0212 141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.5162 0.4444 0.2653 -0.0747 0.0167  -0.0265 141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.4832 0.4026 0.1629 -0.1041 -0.0140 -0.0190 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.5002 0.4207 0.1580 -0.1158 -0.0333 -0.0134 141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.5310 0.4237 0.1410 -0.1354 -0.0299 -0.0128 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.4940 0.4160 0.1527 -0.1134 -0.0396 -0.0154 141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.4879 0.4454 0.2583 -0.0739 -0.0056 -0.0161 142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.4971 0.4578 0.2962 -0.0663 0.0082  -0.0154 142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.5115 0.4822 0.3471 -0.0532 0.0091  -0.0159 142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.5177 0.4888 0.3794 -0.0473 0.0228  -0.0146 142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.4808 0.4555 0.2949 -0.0663 0.0001  -0.0090 142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.4684 0.4621 0.2964 -0.0618 -0.0228 -0.0048 142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.4783 0.4756 0.2888 -0.0678 -0.0376 -0.0017 142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.4469 0.4560 0.3083 -0.0506 -0.0328 -0.0030 142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.4633 0.4764 0.2942 -0.0598 -0.0531 0.0009  142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.4474 0.4663 0.3063 -0.0501 -0.0510 -0.0002 142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.4357 0.4501 0.3294 -0.0418 -0.0285 -0.0022 142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.4386 0.4683 0.3193 -0.0416 -0.0636 0.0014  142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.4257 0.4522 0.3417 -0.0347 -0.0443 0.0007  142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.4236 0.4558 0.3299 -0.0349 -0.0609 0.0016  142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.5164 0.4948 0.3553 -0.0490 -0.0055 -0.0165 143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.5203 0.5057 0.3897 -0.0383 -0.0069 -0.0161 143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.5746 0.5443 0.4473 -0.0361 0.0144  -0.0200 143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.5622 0.5377 0.4683 -0.0270 0.0168  -0.0174 143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.4999 0.4911 0.3625 -0.0365 -0.0238 -0.0168 143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.4800 0.4864 0.3491 -0.0345 -0.0432 -0.0126 143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.4673 0.4759 0.3266 -0.0331 -0.0548 -0.0137 143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.4678 0.4848 0.3705 -0.0270 -0.0488 -0.0082 143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.6249 0.5729 0.4622 -0.0449 0.0294  -0.0257 144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.6776 0.6039 0.5089 -0.0442 0.0527  -0.0309 144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.7178 0.6308 0.5512 -0.0454 0.0781  -0.0315 144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.7374 0.6282 0.5630 -0.0448 0.1014  -0.0364 144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.7318 0.6362 0.5153 -0.0552 0.0536  -0.0375 144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.8034 0.7150 0.5883 -0.0524 0.0374  -0.0379 144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.8231 0.7432 0.6403 -0.0415 0.0371  -0.0364 144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.8342 0.7426 0.5890 -0.0617 0.0249  -0.0387 144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.7265 0.6500 0.5676 -0.0475 0.0756  -0.0267 145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.7549 0.6662 0.5972 -0.0493 0.1003  -0.0263 145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.7446 0.6799 0.6369 -0.0409 0.0974  -0.0173 145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.7553 0.6867 0.6505 -0.0436 0.1123  -0.0147 145 GLU   A O   
1073 C CB  . GLU   A 139 ? 0.8233 0.7163 0.6139 -0.0648 0.1026  -0.0292 145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 0.8991 0.8113 0.6842 -0.0698 0.0751  -0.0240 145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 1.0186 0.9129 0.7522 -0.0864 0.0721  -0.0252 145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 1.0217 0.9273 0.7556 -0.0907 0.0603  -0.0192 145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 1.0799 0.9475 0.7721 -0.0960 0.0806  -0.0313 145 GLU   A OE2 
1078 N N1  . A1BOE B .   ? 0.4542 0.4101 0.2452 0.0204  -0.0880 -0.0050 201 A1BOE A N1  
1079 C C4  . A1BOE B .   ? 0.5397 0.4333 0.2351 0.0186  -0.0689 -0.0146 201 A1BOE A C4  
1080 C C5  . A1BOE B .   ? 0.5464 0.4326 0.2433 0.0217  -0.0666 -0.0161 201 A1BOE A C5  
1081 C C6  . A1BOE B .   ? 0.5629 0.4291 0.2461 0.0275  -0.0501 -0.0172 201 A1BOE A C6  
1082 C C7  . A1BOE B .   ? 0.5641 0.4203 0.2493 0.0311  -0.0471 -0.0189 201 A1BOE A C7  
1083 C C8  . A1BOE B .   ? 0.5214 0.4237 0.2568 0.0271  -0.0682 -0.0131 201 A1BOE A C8  
1084 C C10 . A1BOE B .   ? 0.4861 0.4221 0.2658 0.0255  -0.0800 -0.0067 201 A1BOE A C10 
1085 C C13 . A1BOE B .   ? 0.5749 0.4177 0.2467 0.0210  -0.0780 -0.0248 201 A1BOE A C13 
1086 O O2  . A1BOE B .   ? 0.6108 0.4228 0.2469 0.0182  -0.0775 -0.0293 201 A1BOE A O2  
1087 C C12 . A1BOE B .   ? 0.5613 0.4157 0.2501 0.0172  -0.0939 -0.0240 201 A1BOE A C12 
1088 C C11 . A1BOE B .   ? 0.5404 0.4310 0.2687 0.0191  -0.0940 -0.0183 201 A1BOE A C11 
1089 C C9  . A1BOE B .   ? 0.5205 0.4248 0.2657 0.0259  -0.0773 -0.0135 201 A1BOE A C9  
1090 O O1  . A1BOE B .   ? 0.4852 0.4257 0.2798 0.0295  -0.0743 -0.0028 201 A1BOE A O1  
1091 N N   . A1BOE B .   ? 0.5561 0.4228 0.2530 0.0265  -0.0651 -0.0195 201 A1BOE A N   
1092 C C1  . A1BOE B .   ? 0.5754 0.4294 0.2432 0.0300  -0.0349 -0.0167 201 A1BOE A C1  
1093 O O   . A1BOE B .   ? 0.5968 0.4275 0.2502 0.0362  -0.0160 -0.0184 201 A1BOE A O   
1094 C C   . A1BOE B .   ? 0.5972 0.4153 0.2371 0.0395  0.0034  -0.0171 201 A1BOE A C   
1095 C C3  . A1BOE B .   ? 0.5510 0.4337 0.2315 0.0206  -0.0558 -0.0138 201 A1BOE A C3  
1096 C C2  . A1BOE B .   ? 0.5671 0.4302 0.2338 0.0263  -0.0382 -0.0148 201 A1BOE A C2  
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