data_7HUR
# 
_entry.id   7HUR 
# 
_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   7HUR         pdb_00007hur 10.2210/pdb7hur/pdb 
WWPDB D_1001407956 ?            ?                   
# 
_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                        7HUR 
_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-methoxypyridin-3-yl)acetyl]piperidine-3-carboxamide' 277.319   1  ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                       65.409    1  ?         ? ? ? 
4 water       nat water                                                            18.015    62 ?         ? ? ? 
# 
_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-methoxypyridin-3-yl)acetyl]piperidine-3-carboxamide' A1BOY 
3 'ZINC ION'                                                       ZN    
4 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 
A1BOY non-polymer         . '(3S)-1-[(2-methoxypyridin-3-yl)acetyl]piperidine-3-carboxamide' ? 'C14 H19 N3 O3'  277.319 
ALA   'L-peptide linking' y ALANINE                                                          ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                         ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                       ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                  ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                         ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                        ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                  ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                          ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                        ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                            ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                       ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                          ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                           ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                       ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                    ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                          ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                           ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                        ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                       ? 'C11 H12 N2 O2'  204.225 
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        A1BOY 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BOY 
_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 A1BOY 1  201 201 A1BOY LIG A . 
C 3 ZN    1  202 1   ZN    ZN  A . 
D 4 HOH   1  301 40  HOH   HOH A . 
D 4 HOH   2  302 4   HOH   HOH A . 
D 4 HOH   3  303 15  HOH   HOH A . 
D 4 HOH   4  304 9   HOH   HOH A . 
D 4 HOH   5  305 5   HOH   HOH A . 
D 4 HOH   6  306 29  HOH   HOH A . 
D 4 HOH   7  307 11  HOH   HOH A . 
D 4 HOH   8  308 12  HOH   HOH A . 
D 4 HOH   9  309 1   HOH   HOH A . 
D 4 HOH   10 310 58  HOH   HOH A . 
D 4 HOH   11 311 53  HOH   HOH A . 
D 4 HOH   12 312 3   HOH   HOH A . 
D 4 HOH   13 313 45  HOH   HOH A . 
D 4 HOH   14 314 25  HOH   HOH A . 
D 4 HOH   15 315 57  HOH   HOH A . 
D 4 HOH   16 316 41  HOH   HOH A . 
D 4 HOH   17 317 54  HOH   HOH A . 
D 4 HOH   18 318 17  HOH   HOH A . 
D 4 HOH   19 319 26  HOH   HOH A . 
D 4 HOH   20 320 6   HOH   HOH A . 
D 4 HOH   21 321 16  HOH   HOH A . 
D 4 HOH   22 322 28  HOH   HOH A . 
D 4 HOH   23 323 55  HOH   HOH A . 
D 4 HOH   24 324 22  HOH   HOH A . 
D 4 HOH   25 325 69  HOH   HOH A . 
D 4 HOH   26 326 14  HOH   HOH A . 
D 4 HOH   27 327 10  HOH   HOH A . 
D 4 HOH   28 328 24  HOH   HOH A . 
D 4 HOH   29 329 61  HOH   HOH A . 
D 4 HOH   30 330 52  HOH   HOH A . 
D 4 HOH   31 331 51  HOH   HOH A . 
D 4 HOH   32 332 13  HOH   HOH A . 
D 4 HOH   33 333 38  HOH   HOH A . 
D 4 HOH   34 334 34  HOH   HOH A . 
D 4 HOH   35 335 63  HOH   HOH A . 
D 4 HOH   36 336 33  HOH   HOH A . 
D 4 HOH   37 337 71  HOH   HOH A . 
D 4 HOH   38 338 32  HOH   HOH A . 
D 4 HOH   39 339 31  HOH   HOH A . 
D 4 HOH   40 340 60  HOH   HOH A . 
D 4 HOH   41 341 19  HOH   HOH A . 
D 4 HOH   42 342 62  HOH   HOH A . 
D 4 HOH   43 343 48  HOH   HOH A . 
D 4 HOH   44 344 59  HOH   HOH A . 
D 4 HOH   45 345 20  HOH   HOH A . 
D 4 HOH   46 346 42  HOH   HOH A . 
D 4 HOH   47 347 56  HOH   HOH A . 
D 4 HOH   48 348 18  HOH   HOH A . 
D 4 HOH   49 349 44  HOH   HOH A . 
D 4 HOH   50 350 50  HOH   HOH A . 
D 4 HOH   51 351 66  HOH   HOH A . 
D 4 HOH   52 352 43  HOH   HOH A . 
D 4 HOH   53 353 30  HOH   HOH A . 
D 4 HOH   54 354 65  HOH   HOH A . 
D 4 HOH   55 355 67  HOH   HOH A . 
D 4 HOH   56 356 8   HOH   HOH A . 
D 4 HOH   57 357 21  HOH   HOH A . 
D 4 HOH   58 358 2   HOH   HOH A . 
D 4 HOH   59 359 64  HOH   HOH A . 
D 4 HOH   60 360 70  HOH   HOH A . 
D 4 HOH   61 361 68  HOH   HOH A . 
D 4 HOH   62 362 23  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           7HUR 
_cell.length_a           73.872 
_cell.length_b           61.490 
_cell.length_c           32.732 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.70 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HUR 
_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          7HUR 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.34 
_exptl_crystal.density_percent_sol   47.35 
_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   2024-10-10 
_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   0.92209 
_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        0.92209 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HUR 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             36.89 
_reflns.d_resolution_high            2.54 
_reflns.number_obs                   4770 
_reflns.percent_possible_obs         97.8 
_reflns.pdbx_Rmerge_I_obs            0.179 
_reflns.pdbx_netI_over_sigmaI        6.0 
_reflns.pdbx_redundancy              4.1 
_reflns.pdbx_Rrim_I_all              0.204 
_reflns.pdbx_Rpim_I_all              0.095 
_reflns.pdbx_CC_half                 0.980 
_reflns.pdbx_number_measured_all     19546 
_reflns.pdbx_chi_squared             0.94 
_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                  2.54 
_reflns_shell.d_res_low                   2.68 
_reflns_shell.number_measured_all         2130 
_reflns_shell.number_unique_obs           669 
_reflns_shell.Rmerge_I_obs                0.844 
_reflns_shell.pdbx_chi_squared            0.61 
_reflns_shell.pdbx_redundancy             3.2 
_reflns_shell.percent_possible_obs        93.8 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.4 
_reflns_shell.pdbx_Rrim_I_all             0.986 
_reflns_shell.pdbx_Rpim_I_all             0.495 
_reflns_shell.pdbx_CC_half                0.652 
_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                                 7HUR 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     4670 
_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                             36.90 
_refine.ls_d_res_high                            2.543 
_refine.ls_percent_reflns_obs                    95.7 
_refine.ls_R_factor_obs                          0.2228 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2193 
_refine.ls_R_factor_R_free                       0.3059 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.260 
_refine.ls_number_reflns_R_free                  199 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.907 
_refine.correlation_coeff_Fo_to_Fc_free          0.863 
_refine.B_iso_mean                               45.77 
_refine.aniso_B[1][1]                            -6.96040 
_refine.aniso_B[2][2]                            1.63530 
_refine.aniso_B[3][3]                            5.32510 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -3.40340 
_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             3.507 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.392 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.391 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HUR 
_refine_analyze.Luzzati_coordinate_error_obs    0.37 
_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         21 
_refine_hist.number_atoms_solvent             62 
_refine_hist.number_atoms_total               1157 
_refine_hist.d_res_high                       2.543 
_refine_hist.d_res_low                        36.90 
# 
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                  0.007 ? 2.00  1125 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.88  ? 2.00  1531 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  377  '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 1125 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           2.85  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           17.19 ? ?     ?    '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  837  'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   10 
_refine_ls_shell.d_res_high                       2.54 
_refine_ls_shell.d_res_low                        2.65 
_refine_ls_shell.number_reflns_R_work             496 
_refine_ls_shell.R_factor_R_work                  0.2896 
_refine_ls_shell.percent_reflns_obs               91.31 
_refine_ls_shell.R_factor_R_free                  0.4777 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.43 
_refine_ls_shell.number_reflns_R_free             23 
_refine_ls_shell.number_reflns_all                519 
_refine_ls_shell.R_factor_all                     0.2971 
# 
_struct.entry_id                  7HUR 
_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-0031772-001 (A71EV2A-x3201)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HUR 
_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 ? 
# 
_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              7HUR 
_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 
# 
_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 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P5 AA5 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 ? ? ? ? ? ? ? 2.168 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.642 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.434 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.051 ? ? 
# 
_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 95.6  ? 
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_555 106.8 ? 
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_555 115.6 ? 
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_555 132.0 ? 
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_555 100.8 ? 
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_555 105.9 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N GLY A 43  ? N GLY A 49  O GLY A 7   ? O GLY A 13  
AA2 1 2 O VAL A 68  ? O VAL A 74  N GLY A 55  ? N GLY A 61  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O GLY A 116 ? O GLY A 122 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O VAL A 126 ? O VAL A 132 N ALA A 95  ? N ALA A 101 
AA2 6 7 O LEU A 92  ? O LEU A 98  N SER A 74  ? N SER A 80  
# 
_pdbx_entry_details.entry_id                   7HUR 
_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_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    SER 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     125 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -127.62 
_pdbx_validate_torsion.psi             -50.36 
# 
_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         15.4927 
_pdbx_refine_tls.origin_y         7.0841 
_pdbx_refine_tls.origin_z         14.2086 
_pdbx_refine_tls.T[1][1]          -0.3003 
_pdbx_refine_tls.T[2][2]          0.1205 
_pdbx_refine_tls.T[3][3]          -0.1503 
_pdbx_refine_tls.T[1][2]          -0.0254 
_pdbx_refine_tls.T[1][3]          -0.1301 
_pdbx_refine_tls.T[2][3]          0.0014 
_pdbx_refine_tls.L[1][1]          7.2739 
_pdbx_refine_tls.L[2][2]          2.1425 
_pdbx_refine_tls.L[3][3]          0.9287 
_pdbx_refine_tls.L[1][2]          1.6991 
_pdbx_refine_tls.L[1][3]          0.0584 
_pdbx_refine_tls.L[2][3]          -0.8767 
_pdbx_refine_tls.S[1][1]          -0.4674 
_pdbx_refine_tls.S[1][2]          0.2979 
_pdbx_refine_tls.S[1][3]          0.6580 
_pdbx_refine_tls.S[2][1]          0.0553 
_pdbx_refine_tls.S[2][2]          0.2432 
_pdbx_refine_tls.S[2][3]          0.0694 
_pdbx_refine_tls.S[3][1]          0.1758 
_pdbx_refine_tls.S[3][2]          0.0231 
_pdbx_refine_tls.S[3][3]          0.2242 
# 
_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 
A1BOY N1   N  N N 1   
A1BOY C4   C  Y N 2   
A1BOY C5   C  Y N 3   
A1BOY C6   C  N N 4   
A1BOY C7   C  N N 5   
A1BOY C8   C  N N 6   
A1BOY C10  C  N N 7   
A1BOY C13  C  N N 8   
A1BOY O2   O  N N 9   
A1BOY C12  C  N N 10  
A1BOY N2   N  N N 11  
A1BOY C11  C  N S 12  
A1BOY C9   C  N N 13  
A1BOY O1   O  N N 14  
A1BOY C1   C  Y N 15  
A1BOY O    O  N N 16  
A1BOY C    C  N N 17  
A1BOY C3   C  Y N 18  
A1BOY C2   C  Y N 19  
A1BOY N    N  Y N 20  
A1BOY H6   H  N N 21  
A1BOY H8   H  N N 22  
A1BOY H7   H  N N 23  
A1BOY H9   H  N N 24  
A1BOY H10  H  N N 25  
A1BOY H13  H  N N 26  
A1BOY H14  H  N N 27  
A1BOY H17  H  N N 28  
A1BOY H18  H  N N 29  
A1BOY H16  H  N N 30  
A1BOY H15  H  N N 31  
A1BOY H    H  N N 32  
A1BOY H11  H  N N 33  
A1BOY H12  H  N N 34  
A1BOY H3   H  N N 35  
A1BOY H2   H  N N 36  
A1BOY H1   H  N N 37  
A1BOY H5   H  N N 38  
A1BOY H4   H  N N 39  
ALA   N    N  N N 40  
ALA   CA   C  N S 41  
ALA   C    C  N N 42  
ALA   O    O  N N 43  
ALA   CB   C  N N 44  
ALA   OXT  O  N N 45  
ALA   H    H  N N 46  
ALA   H2   H  N N 47  
ALA   HA   H  N N 48  
ALA   HB1  H  N N 49  
ALA   HB2  H  N N 50  
ALA   HB3  H  N N 51  
ALA   HXT  H  N N 52  
ARG   N    N  N N 53  
ARG   CA   C  N S 54  
ARG   C    C  N N 55  
ARG   O    O  N N 56  
ARG   CB   C  N N 57  
ARG   CG   C  N N 58  
ARG   CD   C  N N 59  
ARG   NE   N  N N 60  
ARG   CZ   C  N N 61  
ARG   NH1  N  N N 62  
ARG   NH2  N  N N 63  
ARG   OXT  O  N N 64  
ARG   H    H  N N 65  
ARG   H2   H  N N 66  
ARG   HA   H  N N 67  
ARG   HB2  H  N N 68  
ARG   HB3  H  N N 69  
ARG   HG2  H  N N 70  
ARG   HG3  H  N N 71  
ARG   HD2  H  N N 72  
ARG   HD3  H  N N 73  
ARG   HE   H  N N 74  
ARG   HH11 H  N N 75  
ARG   HH12 H  N N 76  
ARG   HH21 H  N N 77  
ARG   HH22 H  N N 78  
ARG   HXT  H  N N 79  
ASN   N    N  N N 80  
ASN   CA   C  N S 81  
ASN   C    C  N N 82  
ASN   O    O  N N 83  
ASN   CB   C  N N 84  
ASN   CG   C  N N 85  
ASN   OD1  O  N N 86  
ASN   ND2  N  N N 87  
ASN   OXT  O  N N 88  
ASN   H    H  N N 89  
ASN   H2   H  N N 90  
ASN   HA   H  N N 91  
ASN   HB2  H  N N 92  
ASN   HB3  H  N N 93  
ASN   HD21 H  N N 94  
ASN   HD22 H  N N 95  
ASN   HXT  H  N N 96  
ASP   N    N  N N 97  
ASP   CA   C  N S 98  
ASP   C    C  N N 99  
ASP   O    O  N N 100 
ASP   CB   C  N N 101 
ASP   CG   C  N N 102 
ASP   OD1  O  N N 103 
ASP   OD2  O  N N 104 
ASP   OXT  O  N N 105 
ASP   H    H  N N 106 
ASP   H2   H  N N 107 
ASP   HA   H  N N 108 
ASP   HB2  H  N N 109 
ASP   HB3  H  N N 110 
ASP   HD2  H  N N 111 
ASP   HXT  H  N N 112 
CYS   N    N  N N 113 
CYS   CA   C  N R 114 
CYS   C    C  N N 115 
CYS   O    O  N N 116 
CYS   CB   C  N N 117 
CYS   SG   S  N N 118 
CYS   OXT  O  N N 119 
CYS   H    H  N N 120 
CYS   H2   H  N N 121 
CYS   HA   H  N N 122 
CYS   HB2  H  N N 123 
CYS   HB3  H  N N 124 
CYS   HG   H  N N 125 
CYS   HXT  H  N N 126 
GLN   N    N  N N 127 
GLN   CA   C  N S 128 
GLN   C    C  N N 129 
GLN   O    O  N N 130 
GLN   CB   C  N N 131 
GLN   CG   C  N N 132 
GLN   CD   C  N N 133 
GLN   OE1  O  N N 134 
GLN   NE2  N  N N 135 
GLN   OXT  O  N N 136 
GLN   H    H  N N 137 
GLN   H2   H  N N 138 
GLN   HA   H  N N 139 
GLN   HB2  H  N N 140 
GLN   HB3  H  N N 141 
GLN   HG2  H  N N 142 
GLN   HG3  H  N N 143 
GLN   HE21 H  N N 144 
GLN   HE22 H  N N 145 
GLN   HXT  H  N N 146 
GLU   N    N  N N 147 
GLU   CA   C  N S 148 
GLU   C    C  N N 149 
GLU   O    O  N N 150 
GLU   CB   C  N N 151 
GLU   CG   C  N N 152 
GLU   CD   C  N N 153 
GLU   OE1  O  N N 154 
GLU   OE2  O  N N 155 
GLU   OXT  O  N N 156 
GLU   H    H  N N 157 
GLU   H2   H  N N 158 
GLU   HA   H  N N 159 
GLU   HB2  H  N N 160 
GLU   HB3  H  N N 161 
GLU   HG2  H  N N 162 
GLU   HG3  H  N N 163 
GLU   HE2  H  N N 164 
GLU   HXT  H  N N 165 
GLY   N    N  N N 166 
GLY   CA   C  N N 167 
GLY   C    C  N N 168 
GLY   O    O  N N 169 
GLY   OXT  O  N N 170 
GLY   H    H  N N 171 
GLY   H2   H  N N 172 
GLY   HA2  H  N N 173 
GLY   HA3  H  N N 174 
GLY   HXT  H  N N 175 
HIS   N    N  N N 176 
HIS   CA   C  N S 177 
HIS   C    C  N N 178 
HIS   O    O  N N 179 
HIS   CB   C  N N 180 
HIS   CG   C  Y N 181 
HIS   ND1  N  Y N 182 
HIS   CD2  C  Y N 183 
HIS   CE1  C  Y N 184 
HIS   NE2  N  Y N 185 
HIS   OXT  O  N N 186 
HIS   H    H  N N 187 
HIS   H2   H  N N 188 
HIS   HA   H  N N 189 
HIS   HB2  H  N N 190 
HIS   HB3  H  N N 191 
HIS   HD1  H  N N 192 
HIS   HD2  H  N N 193 
HIS   HE1  H  N N 194 
HIS   HE2  H  N N 195 
HIS   HXT  H  N N 196 
HOH   O    O  N N 197 
HOH   H1   H  N N 198 
HOH   H2   H  N N 199 
ILE   N    N  N N 200 
ILE   CA   C  N S 201 
ILE   C    C  N N 202 
ILE   O    O  N N 203 
ILE   CB   C  N S 204 
ILE   CG1  C  N N 205 
ILE   CG2  C  N N 206 
ILE   CD1  C  N N 207 
ILE   OXT  O  N N 208 
ILE   H    H  N N 209 
ILE   H2   H  N N 210 
ILE   HA   H  N N 211 
ILE   HB   H  N N 212 
ILE   HG12 H  N N 213 
ILE   HG13 H  N N 214 
ILE   HG21 H  N N 215 
ILE   HG22 H  N N 216 
ILE   HG23 H  N N 217 
ILE   HD11 H  N N 218 
ILE   HD12 H  N N 219 
ILE   HD13 H  N N 220 
ILE   HXT  H  N N 221 
LEU   N    N  N N 222 
LEU   CA   C  N S 223 
LEU   C    C  N N 224 
LEU   O    O  N N 225 
LEU   CB   C  N N 226 
LEU   CG   C  N N 227 
LEU   CD1  C  N N 228 
LEU   CD2  C  N N 229 
LEU   OXT  O  N N 230 
LEU   H    H  N N 231 
LEU   H2   H  N N 232 
LEU   HA   H  N N 233 
LEU   HB2  H  N N 234 
LEU   HB3  H  N N 235 
LEU   HG   H  N N 236 
LEU   HD11 H  N N 237 
LEU   HD12 H  N N 238 
LEU   HD13 H  N N 239 
LEU   HD21 H  N N 240 
LEU   HD22 H  N N 241 
LEU   HD23 H  N N 242 
LEU   HXT  H  N N 243 
LYS   N    N  N N 244 
LYS   CA   C  N S 245 
LYS   C    C  N N 246 
LYS   O    O  N N 247 
LYS   CB   C  N N 248 
LYS   CG   C  N N 249 
LYS   CD   C  N N 250 
LYS   CE   C  N N 251 
LYS   NZ   N  N N 252 
LYS   OXT  O  N N 253 
LYS   H    H  N N 254 
LYS   H2   H  N N 255 
LYS   HA   H  N N 256 
LYS   HB2  H  N N 257 
LYS   HB3  H  N N 258 
LYS   HG2  H  N N 259 
LYS   HG3  H  N N 260 
LYS   HD2  H  N N 261 
LYS   HD3  H  N N 262 
LYS   HE2  H  N N 263 
LYS   HE3  H  N N 264 
LYS   HZ1  H  N N 265 
LYS   HZ2  H  N N 266 
LYS   HZ3  H  N N 267 
LYS   HXT  H  N N 268 
MET   N    N  N N 269 
MET   CA   C  N S 270 
MET   C    C  N N 271 
MET   O    O  N N 272 
MET   CB   C  N N 273 
MET   CG   C  N N 274 
MET   SD   S  N N 275 
MET   CE   C  N N 276 
MET   OXT  O  N N 277 
MET   H    H  N N 278 
MET   H2   H  N N 279 
MET   HA   H  N N 280 
MET   HB2  H  N N 281 
MET   HB3  H  N N 282 
MET   HG2  H  N N 283 
MET   HG3  H  N N 284 
MET   HE1  H  N N 285 
MET   HE2  H  N N 286 
MET   HE3  H  N N 287 
MET   HXT  H  N N 288 
PHE   N    N  N N 289 
PHE   CA   C  N S 290 
PHE   C    C  N N 291 
PHE   O    O  N N 292 
PHE   CB   C  N N 293 
PHE   CG   C  Y N 294 
PHE   CD1  C  Y N 295 
PHE   CD2  C  Y N 296 
PHE   CE1  C  Y N 297 
PHE   CE2  C  Y N 298 
PHE   CZ   C  Y N 299 
PHE   OXT  O  N N 300 
PHE   H    H  N N 301 
PHE   H2   H  N N 302 
PHE   HA   H  N N 303 
PHE   HB2  H  N N 304 
PHE   HB3  H  N N 305 
PHE   HD1  H  N N 306 
PHE   HD2  H  N N 307 
PHE   HE1  H  N N 308 
PHE   HE2  H  N N 309 
PHE   HZ   H  N N 310 
PHE   HXT  H  N N 311 
PRO   N    N  N N 312 
PRO   CA   C  N S 313 
PRO   C    C  N N 314 
PRO   O    O  N N 315 
PRO   CB   C  N N 316 
PRO   CG   C  N N 317 
PRO   CD   C  N N 318 
PRO   OXT  O  N N 319 
PRO   H    H  N N 320 
PRO   HA   H  N N 321 
PRO   HB2  H  N N 322 
PRO   HB3  H  N N 323 
PRO   HG2  H  N N 324 
PRO   HG3  H  N N 325 
PRO   HD2  H  N N 326 
PRO   HD3  H  N N 327 
PRO   HXT  H  N N 328 
SER   N    N  N N 329 
SER   CA   C  N S 330 
SER   C    C  N N 331 
SER   O    O  N N 332 
SER   CB   C  N N 333 
SER   OG   O  N N 334 
SER   OXT  O  N N 335 
SER   H    H  N N 336 
SER   H2   H  N N 337 
SER   HA   H  N N 338 
SER   HB2  H  N N 339 
SER   HB3  H  N N 340 
SER   HG   H  N N 341 
SER   HXT  H  N N 342 
THR   N    N  N N 343 
THR   CA   C  N S 344 
THR   C    C  N N 345 
THR   O    O  N N 346 
THR   CB   C  N R 347 
THR   OG1  O  N N 348 
THR   CG2  C  N N 349 
THR   OXT  O  N N 350 
THR   H    H  N N 351 
THR   H2   H  N N 352 
THR   HA   H  N N 353 
THR   HB   H  N N 354 
THR   HG1  H  N N 355 
THR   HG21 H  N N 356 
THR   HG22 H  N N 357 
THR   HG23 H  N N 358 
THR   HXT  H  N N 359 
TRP   N    N  N N 360 
TRP   CA   C  N S 361 
TRP   C    C  N N 362 
TRP   O    O  N N 363 
TRP   CB   C  N N 364 
TRP   CG   C  Y N 365 
TRP   CD1  C  Y N 366 
TRP   CD2  C  Y N 367 
TRP   NE1  N  Y N 368 
TRP   CE2  C  Y N 369 
TRP   CE3  C  Y N 370 
TRP   CZ2  C  Y N 371 
TRP   CZ3  C  Y N 372 
TRP   CH2  C  Y N 373 
TRP   OXT  O  N N 374 
TRP   H    H  N N 375 
TRP   H2   H  N N 376 
TRP   HA   H  N N 377 
TRP   HB2  H  N N 378 
TRP   HB3  H  N N 379 
TRP   HD1  H  N N 380 
TRP   HE1  H  N N 381 
TRP   HE3  H  N N 382 
TRP   HZ2  H  N N 383 
TRP   HZ3  H  N N 384 
TRP   HH2  H  N N 385 
TRP   HXT  H  N N 386 
TYR   N    N  N N 387 
TYR   CA   C  N S 388 
TYR   C    C  N N 389 
TYR   O    O  N N 390 
TYR   CB   C  N N 391 
TYR   CG   C  Y N 392 
TYR   CD1  C  Y N 393 
TYR   CD2  C  Y N 394 
TYR   CE1  C  Y N 395 
TYR   CE2  C  Y N 396 
TYR   CZ   C  Y N 397 
TYR   OH   O  N N 398 
TYR   OXT  O  N N 399 
TYR   H    H  N N 400 
TYR   H2   H  N N 401 
TYR   HA   H  N N 402 
TYR   HB2  H  N N 403 
TYR   HB3  H  N N 404 
TYR   HD1  H  N N 405 
TYR   HD2  H  N N 406 
TYR   HE1  H  N N 407 
TYR   HE2  H  N N 408 
TYR   HH   H  N N 409 
TYR   HXT  H  N N 410 
VAL   N    N  N N 411 
VAL   CA   C  N S 412 
VAL   C    C  N N 413 
VAL   O    O  N N 414 
VAL   CB   C  N N 415 
VAL   CG1  C  N N 416 
VAL   CG2  C  N N 417 
VAL   OXT  O  N N 418 
VAL   H    H  N N 419 
VAL   H2   H  N N 420 
VAL   HA   H  N N 421 
VAL   HB   H  N N 422 
VAL   HG11 H  N N 423 
VAL   HG12 H  N N 424 
VAL   HG13 H  N N 425 
VAL   HG21 H  N N 426 
VAL   HG22 H  N N 427 
VAL   HG23 H  N N 428 
VAL   HXT  H  N N 429 
ZN    ZN   ZN N N 430 
# 
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 
A1BOY C   O    sing N N 1   
A1BOY O   C1   sing N N 2   
A1BOY C1  N    doub Y N 3   
A1BOY N   C2   sing Y N 4   
A1BOY C2  C3   doub Y N 5   
A1BOY C3  C4   sing Y N 6   
A1BOY C4  C5   doub Y N 7   
A1BOY C1  C5   sing Y N 8   
A1BOY C5  C6   sing N N 9   
A1BOY C6  C7   sing N N 10  
A1BOY O1  C7   doub N N 11  
A1BOY C7  N1   sing N N 12  
A1BOY N1  C8   sing N N 13  
A1BOY C8  C9   sing N N 14  
A1BOY C9  C10  sing N N 15  
A1BOY C10 C11  sing N N 16  
A1BOY C11 C12  sing N N 17  
A1BOY N2  C12  sing N N 18  
A1BOY C12 O2   doub N N 19  
A1BOY C13 C11  sing N N 20  
A1BOY N1  C13  sing N N 21  
A1BOY C4  H6   sing N N 22  
A1BOY C6  H8   sing N N 23  
A1BOY C6  H7   sing N N 24  
A1BOY C8  H9   sing N N 25  
A1BOY C8  H10  sing N N 26  
A1BOY C10 H13  sing N N 27  
A1BOY C10 H14  sing N N 28  
A1BOY C13 H17  sing N N 29  
A1BOY C13 H18  sing N N 30  
A1BOY N2  H16  sing N N 31  
A1BOY N2  H15  sing N N 32  
A1BOY C11 H    sing N N 33  
A1BOY C9  H11  sing N N 34  
A1BOY C9  H12  sing N N 35  
A1BOY C   H3   sing N N 36  
A1BOY C   H2   sing N N 37  
A1BOY C   H1   sing N N 38  
A1BOY C3  H5   sing N N 39  
A1BOY C2  H4   sing N N 40  
ALA   N   CA   sing N N 41  
ALA   N   H    sing N N 42  
ALA   N   H2   sing N N 43  
ALA   CA  C    sing N N 44  
ALA   CA  CB   sing N N 45  
ALA   CA  HA   sing N N 46  
ALA   C   O    doub N N 47  
ALA   C   OXT  sing N N 48  
ALA   CB  HB1  sing N N 49  
ALA   CB  HB2  sing N N 50  
ALA   CB  HB3  sing N N 51  
ALA   OXT HXT  sing N N 52  
ARG   N   CA   sing N N 53  
ARG   N   H    sing N N 54  
ARG   N   H2   sing N N 55  
ARG   CA  C    sing N N 56  
ARG   CA  CB   sing N N 57  
ARG   CA  HA   sing N N 58  
ARG   C   O    doub N N 59  
ARG   C   OXT  sing N N 60  
ARG   CB  CG   sing N N 61  
ARG   CB  HB2  sing N N 62  
ARG   CB  HB3  sing N N 63  
ARG   CG  CD   sing N N 64  
ARG   CG  HG2  sing N N 65  
ARG   CG  HG3  sing N N 66  
ARG   CD  NE   sing N N 67  
ARG   CD  HD2  sing N N 68  
ARG   CD  HD3  sing N N 69  
ARG   NE  CZ   sing N N 70  
ARG   NE  HE   sing N N 71  
ARG   CZ  NH1  sing N N 72  
ARG   CZ  NH2  doub N N 73  
ARG   NH1 HH11 sing N N 74  
ARG   NH1 HH12 sing N N 75  
ARG   NH2 HH21 sing N N 76  
ARG   NH2 HH22 sing N N 77  
ARG   OXT HXT  sing N N 78  
ASN   N   CA   sing N N 79  
ASN   N   H    sing N N 80  
ASN   N   H2   sing N N 81  
ASN   CA  C    sing N N 82  
ASN   CA  CB   sing N N 83  
ASN   CA  HA   sing N N 84  
ASN   C   O    doub N N 85  
ASN   C   OXT  sing N N 86  
ASN   CB  CG   sing N N 87  
ASN   CB  HB2  sing N N 88  
ASN   CB  HB3  sing N N 89  
ASN   CG  OD1  doub N N 90  
ASN   CG  ND2  sing N N 91  
ASN   ND2 HD21 sing N N 92  
ASN   ND2 HD22 sing N N 93  
ASN   OXT HXT  sing N N 94  
ASP   N   CA   sing N N 95  
ASP   N   H    sing N N 96  
ASP   N   H2   sing N N 97  
ASP   CA  C    sing N N 98  
ASP   CA  CB   sing N N 99  
ASP   CA  HA   sing N N 100 
ASP   C   O    doub N N 101 
ASP   C   OXT  sing N N 102 
ASP   CB  CG   sing N N 103 
ASP   CB  HB2  sing N N 104 
ASP   CB  HB3  sing N N 105 
ASP   CG  OD1  doub N N 106 
ASP   CG  OD2  sing N N 107 
ASP   OD2 HD2  sing N N 108 
ASP   OXT HXT  sing N N 109 
CYS   N   CA   sing N N 110 
CYS   N   H    sing N N 111 
CYS   N   H2   sing N N 112 
CYS   CA  C    sing N N 113 
CYS   CA  CB   sing N N 114 
CYS   CA  HA   sing N N 115 
CYS   C   O    doub N N 116 
CYS   C   OXT  sing N N 117 
CYS   CB  SG   sing N N 118 
CYS   CB  HB2  sing N N 119 
CYS   CB  HB3  sing N N 120 
CYS   SG  HG   sing N N 121 
CYS   OXT HXT  sing N N 122 
GLN   N   CA   sing N N 123 
GLN   N   H    sing N N 124 
GLN   N   H2   sing N N 125 
GLN   CA  C    sing N N 126 
GLN   CA  CB   sing N N 127 
GLN   CA  HA   sing N N 128 
GLN   C   O    doub N N 129 
GLN   C   OXT  sing N N 130 
GLN   CB  CG   sing N N 131 
GLN   CB  HB2  sing N N 132 
GLN   CB  HB3  sing N N 133 
GLN   CG  CD   sing N N 134 
GLN   CG  HG2  sing N N 135 
GLN   CG  HG3  sing N N 136 
GLN   CD  OE1  doub N N 137 
GLN   CD  NE2  sing N N 138 
GLN   NE2 HE21 sing N N 139 
GLN   NE2 HE22 sing N N 140 
GLN   OXT HXT  sing N N 141 
GLU   N   CA   sing N N 142 
GLU   N   H    sing N N 143 
GLU   N   H2   sing N N 144 
GLU   CA  C    sing N N 145 
GLU   CA  CB   sing N N 146 
GLU   CA  HA   sing N N 147 
GLU   C   O    doub N N 148 
GLU   C   OXT  sing N N 149 
GLU   CB  CG   sing N N 150 
GLU   CB  HB2  sing N N 151 
GLU   CB  HB3  sing N N 152 
GLU   CG  CD   sing N N 153 
GLU   CG  HG2  sing N N 154 
GLU   CG  HG3  sing N N 155 
GLU   CD  OE1  doub N N 156 
GLU   CD  OE2  sing N N 157 
GLU   OE2 HE2  sing N N 158 
GLU   OXT HXT  sing N N 159 
GLY   N   CA   sing N N 160 
GLY   N   H    sing N N 161 
GLY   N   H2   sing N N 162 
GLY   CA  C    sing N N 163 
GLY   CA  HA2  sing N N 164 
GLY   CA  HA3  sing N N 165 
GLY   C   O    doub N N 166 
GLY   C   OXT  sing N N 167 
GLY   OXT HXT  sing N N 168 
HIS   N   CA   sing N N 169 
HIS   N   H    sing N N 170 
HIS   N   H2   sing N N 171 
HIS   CA  C    sing N N 172 
HIS   CA  CB   sing N N 173 
HIS   CA  HA   sing N N 174 
HIS   C   O    doub N N 175 
HIS   C   OXT  sing N N 176 
HIS   CB  CG   sing N N 177 
HIS   CB  HB2  sing N N 178 
HIS   CB  HB3  sing N N 179 
HIS   CG  ND1  sing Y N 180 
HIS   CG  CD2  doub Y N 181 
HIS   ND1 CE1  doub Y N 182 
HIS   ND1 HD1  sing N N 183 
HIS   CD2 NE2  sing Y N 184 
HIS   CD2 HD2  sing N N 185 
HIS   CE1 NE2  sing Y N 186 
HIS   CE1 HE1  sing N N 187 
HIS   NE2 HE2  sing N N 188 
HIS   OXT HXT  sing N N 189 
HOH   O   H1   sing N N 190 
HOH   O   H2   sing N N 191 
ILE   N   CA   sing N N 192 
ILE   N   H    sing N N 193 
ILE   N   H2   sing N N 194 
ILE   CA  C    sing N N 195 
ILE   CA  CB   sing N N 196 
ILE   CA  HA   sing N N 197 
ILE   C   O    doub N N 198 
ILE   C   OXT  sing N N 199 
ILE   CB  CG1  sing N N 200 
ILE   CB  CG2  sing N N 201 
ILE   CB  HB   sing N N 202 
ILE   CG1 CD1  sing N N 203 
ILE   CG1 HG12 sing N N 204 
ILE   CG1 HG13 sing N N 205 
ILE   CG2 HG21 sing N N 206 
ILE   CG2 HG22 sing N N 207 
ILE   CG2 HG23 sing N N 208 
ILE   CD1 HD11 sing N N 209 
ILE   CD1 HD12 sing N N 210 
ILE   CD1 HD13 sing N N 211 
ILE   OXT HXT  sing N N 212 
LEU   N   CA   sing N N 213 
LEU   N   H    sing N N 214 
LEU   N   H2   sing N N 215 
LEU   CA  C    sing N N 216 
LEU   CA  CB   sing N N 217 
LEU   CA  HA   sing N N 218 
LEU   C   O    doub N N 219 
LEU   C   OXT  sing N N 220 
LEU   CB  CG   sing N N 221 
LEU   CB  HB2  sing N N 222 
LEU   CB  HB3  sing N N 223 
LEU   CG  CD1  sing N N 224 
LEU   CG  CD2  sing N N 225 
LEU   CG  HG   sing N N 226 
LEU   CD1 HD11 sing N N 227 
LEU   CD1 HD12 sing N N 228 
LEU   CD1 HD13 sing N N 229 
LEU   CD2 HD21 sing N N 230 
LEU   CD2 HD22 sing N N 231 
LEU   CD2 HD23 sing N N 232 
LEU   OXT HXT  sing N N 233 
LYS   N   CA   sing N N 234 
LYS   N   H    sing N N 235 
LYS   N   H2   sing N N 236 
LYS   CA  C    sing N N 237 
LYS   CA  CB   sing N N 238 
LYS   CA  HA   sing N N 239 
LYS   C   O    doub N N 240 
LYS   C   OXT  sing N N 241 
LYS   CB  CG   sing N N 242 
LYS   CB  HB2  sing N N 243 
LYS   CB  HB3  sing N N 244 
LYS   CG  CD   sing N N 245 
LYS   CG  HG2  sing N N 246 
LYS   CG  HG3  sing N N 247 
LYS   CD  CE   sing N N 248 
LYS   CD  HD2  sing N N 249 
LYS   CD  HD3  sing N N 250 
LYS   CE  NZ   sing N N 251 
LYS   CE  HE2  sing N N 252 
LYS   CE  HE3  sing N N 253 
LYS   NZ  HZ1  sing N N 254 
LYS   NZ  HZ2  sing N N 255 
LYS   NZ  HZ3  sing N N 256 
LYS   OXT HXT  sing N N 257 
MET   N   CA   sing N N 258 
MET   N   H    sing N N 259 
MET   N   H2   sing N N 260 
MET   CA  C    sing N N 261 
MET   CA  CB   sing N N 262 
MET   CA  HA   sing N N 263 
MET   C   O    doub N N 264 
MET   C   OXT  sing N N 265 
MET   CB  CG   sing N N 266 
MET   CB  HB2  sing N N 267 
MET   CB  HB3  sing N N 268 
MET   CG  SD   sing N N 269 
MET   CG  HG2  sing N N 270 
MET   CG  HG3  sing N N 271 
MET   SD  CE   sing N N 272 
MET   CE  HE1  sing N N 273 
MET   CE  HE2  sing N N 274 
MET   CE  HE3  sing N N 275 
MET   OXT HXT  sing N N 276 
PHE   N   CA   sing N N 277 
PHE   N   H    sing N N 278 
PHE   N   H2   sing N N 279 
PHE   CA  C    sing N N 280 
PHE   CA  CB   sing N N 281 
PHE   CA  HA   sing N N 282 
PHE   C   O    doub N N 283 
PHE   C   OXT  sing N N 284 
PHE   CB  CG   sing N N 285 
PHE   CB  HB2  sing N N 286 
PHE   CB  HB3  sing N N 287 
PHE   CG  CD1  doub Y N 288 
PHE   CG  CD2  sing Y N 289 
PHE   CD1 CE1  sing Y N 290 
PHE   CD1 HD1  sing N N 291 
PHE   CD2 CE2  doub Y N 292 
PHE   CD2 HD2  sing N N 293 
PHE   CE1 CZ   doub Y N 294 
PHE   CE1 HE1  sing N N 295 
PHE   CE2 CZ   sing Y N 296 
PHE   CE2 HE2  sing N N 297 
PHE   CZ  HZ   sing N N 298 
PHE   OXT HXT  sing N N 299 
PRO   N   CA   sing N N 300 
PRO   N   CD   sing N N 301 
PRO   N   H    sing N N 302 
PRO   CA  C    sing N N 303 
PRO   CA  CB   sing N N 304 
PRO   CA  HA   sing N N 305 
PRO   C   O    doub N N 306 
PRO   C   OXT  sing N N 307 
PRO   CB  CG   sing N N 308 
PRO   CB  HB2  sing N N 309 
PRO   CB  HB3  sing N N 310 
PRO   CG  CD   sing N N 311 
PRO   CG  HG2  sing N N 312 
PRO   CG  HG3  sing N N 313 
PRO   CD  HD2  sing N N 314 
PRO   CD  HD3  sing N N 315 
PRO   OXT HXT  sing N N 316 
SER   N   CA   sing N N 317 
SER   N   H    sing N N 318 
SER   N   H2   sing N N 319 
SER   CA  C    sing N N 320 
SER   CA  CB   sing N N 321 
SER   CA  HA   sing N N 322 
SER   C   O    doub N N 323 
SER   C   OXT  sing N N 324 
SER   CB  OG   sing N N 325 
SER   CB  HB2  sing N N 326 
SER   CB  HB3  sing N N 327 
SER   OG  HG   sing N N 328 
SER   OXT HXT  sing N N 329 
THR   N   CA   sing N N 330 
THR   N   H    sing N N 331 
THR   N   H2   sing N N 332 
THR   CA  C    sing N N 333 
THR   CA  CB   sing N N 334 
THR   CA  HA   sing N N 335 
THR   C   O    doub N N 336 
THR   C   OXT  sing N N 337 
THR   CB  OG1  sing N N 338 
THR   CB  CG2  sing N N 339 
THR   CB  HB   sing N N 340 
THR   OG1 HG1  sing N N 341 
THR   CG2 HG21 sing N N 342 
THR   CG2 HG22 sing N N 343 
THR   CG2 HG23 sing N N 344 
THR   OXT HXT  sing N N 345 
TRP   N   CA   sing N N 346 
TRP   N   H    sing N N 347 
TRP   N   H2   sing N N 348 
TRP   CA  C    sing N N 349 
TRP   CA  CB   sing N N 350 
TRP   CA  HA   sing N N 351 
TRP   C   O    doub N N 352 
TRP   C   OXT  sing N N 353 
TRP   CB  CG   sing N N 354 
TRP   CB  HB2  sing N N 355 
TRP   CB  HB3  sing N N 356 
TRP   CG  CD1  doub Y N 357 
TRP   CG  CD2  sing Y N 358 
TRP   CD1 NE1  sing Y N 359 
TRP   CD1 HD1  sing N N 360 
TRP   CD2 CE2  doub Y N 361 
TRP   CD2 CE3  sing Y N 362 
TRP   NE1 CE2  sing Y N 363 
TRP   NE1 HE1  sing N N 364 
TRP   CE2 CZ2  sing Y N 365 
TRP   CE3 CZ3  doub Y N 366 
TRP   CE3 HE3  sing N N 367 
TRP   CZ2 CH2  doub Y N 368 
TRP   CZ2 HZ2  sing N N 369 
TRP   CZ3 CH2  sing Y N 370 
TRP   CZ3 HZ3  sing N N 371 
TRP   CH2 HH2  sing N N 372 
TRP   OXT HXT  sing N N 373 
TYR   N   CA   sing N N 374 
TYR   N   H    sing N N 375 
TYR   N   H2   sing N N 376 
TYR   CA  C    sing N N 377 
TYR   CA  CB   sing N N 378 
TYR   CA  HA   sing N N 379 
TYR   C   O    doub N N 380 
TYR   C   OXT  sing N N 381 
TYR   CB  CG   sing N N 382 
TYR   CB  HB2  sing N N 383 
TYR   CB  HB3  sing N N 384 
TYR   CG  CD1  doub Y N 385 
TYR   CG  CD2  sing Y N 386 
TYR   CD1 CE1  sing Y N 387 
TYR   CD1 HD1  sing N N 388 
TYR   CD2 CE2  doub Y N 389 
TYR   CD2 HD2  sing N N 390 
TYR   CE1 CZ   doub Y N 391 
TYR   CE1 HE1  sing N N 392 
TYR   CE2 CZ   sing Y N 393 
TYR   CE2 HE2  sing N N 394 
TYR   CZ  OH   sing N N 395 
TYR   OH  HH   sing N N 396 
TYR   OXT HXT  sing N N 397 
VAL   N   CA   sing N N 398 
VAL   N   H    sing N N 399 
VAL   N   H2   sing N N 400 
VAL   CA  C    sing N N 401 
VAL   CA  CB   sing N N 402 
VAL   CA  HA   sing N N 403 
VAL   C   O    doub N N 404 
VAL   C   OXT  sing N N 405 
VAL   CB  CG1  sing N N 406 
VAL   CB  CG2  sing N N 407 
VAL   CB  HB   sing N N 408 
VAL   CG1 HG11 sing N N 409 
VAL   CG1 HG12 sing N N 410 
VAL   CG1 HG13 sing N N 411 
VAL   CG2 HG21 sing N N 412 
VAL   CG2 HG22 sing N N 413 
VAL   CG2 HG23 sing N N 414 
VAL   OXT HXT  sing N N 415 
# 
_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                    7HUR 
_atom_sites.fract_transf_matrix[1][1]   0.013537 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000638 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016263 
_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]   0.030585 
_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   ? 19.519 5.947   24.520 1.00 42.47 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.425 6.349   23.439 1.00 42.93 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.528 5.263   22.316 1.00 42.90 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.686 4.365   22.257 1.00 42.94 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.789 6.779   23.996 1.00 44.48 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 22.244 5.970   25.068 1.00 46.72 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.480 5.405   21.393 1.00 42.60 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.651 4.447   20.312 1.00 42.66 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.918 5.057   18.954 1.00 42.30 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.539 6.205   18.697 1.00 42.36 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.523 4.259   18.051 1.00 41.50 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.876 4.685   16.695 1.00 41.04 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.893 3.505   15.699 1.00 41.02 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.888 2.352   16.120 1.00 41.30 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.251 5.353   16.726 1.00 40.67 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.902 3.794   14.377 1.00 40.49 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 23.060 2.807   13.312 1.00 40.52 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.438 3.095   12.720 1.00 40.73 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.773 4.251   12.503 1.00 40.59 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.974 2.923   12.200 1.00 40.89 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.552 3.092   12.768 1.00 41.54 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 22.056 1.748   11.220 1.00 41.24 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.575 3.834   11.770 1.00 42.43 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 25.240 2.068   12.463 1.00 41.05 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.568 2.249   11.881 1.00 41.37 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.601 1.525   10.550 1.00 42.24 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.698 0.307   10.550 1.00 42.84 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.663 1.710   12.829 1.00 40.97 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.654 2.372   14.190 1.00 41.06 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.345 3.556   14.416 1.00 41.47 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.943 1.826   15.245 1.00 41.98 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.309 4.190   15.653 1.00 41.98 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.910 2.442   16.490 1.00 42.82 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.591 3.629   16.689 1.00 43.25 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.520 4.246   17.916 1.00 44.88 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.485 2.252   9.420  1.00 42.29 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.493 1.660   8.073  1.00 42.97 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.615 2.275   7.210  1.00 43.66 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.634 3.486   6.996  1.00 44.05 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 25.094 1.678   7.372  1.00 44.16 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.281 2.930   7.713  1.00 44.70 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 25.208 1.491   5.853  1.00 44.68 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.549 1.436   6.758  1.00 43.55 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.701 1.864   5.977  1.00 43.94 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.598 2.816   6.741  1.00 44.34 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 31.029 2.507   7.853  1.00 44.66 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.882 3.990   6.168  1.00 44.13 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.688 4.996   6.868  1.00 44.27 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.771 6.103   7.450  1.00 44.94 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 31.156 7.274   7.502  1.00 45.24 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.788 5.572   5.967  1.00 44.13 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 34.007 4.692   5.803  1.00 44.87 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.674 4.313   6.774  1.00 45.56 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 34.358 4.388   4.564  1.00 44.62 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.558 5.717   7.898  1.00 44.78 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.598 6.640   8.497  1.00 44.79 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 28.103 6.142   9.885  1.00 43.54 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 28.179 4.947   10.187 1.00 43.69 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.386 6.863   7.563  1.00 45.48 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.707 7.330   6.157  1.00 46.73 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.321 8.553   5.931  1.00 47.67 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.295 6.599   5.051  1.00 47.96 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.582 9.003   4.641  1.00 48.74 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.557 7.033   3.757  1.00 48.87 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.195 8.240   3.553  1.00 49.94 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.467 8.657   2.265  1.00 51.84 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.604 7.089   10.713 1.00 42.05 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 27.001 6.916   12.041 1.00 40.95 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.658 7.680   12.002 1.00 39.88 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.626 8.841   11.617 1.00 39.78 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.944 7.485   13.134 1.00 41.89 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 27.299 7.713   14.515 1.00 44.07 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 28.323 7.936   15.631 1.00 45.69 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.899 8.958   16.596 1.00 46.51 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 27.335 8.699   17.773 1.00 46.70 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 27.106 7.447   18.147 1.00 46.08 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.968 9.693   18.573 1.00 44.98 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.548 7.029   12.329 1.00 39.37 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 23.220 7.658   12.266 1.00 39.07 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.578 7.823   13.655 1.00 39.13 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.162 6.847   14.278 1.00 39.31 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 22.299 6.910   11.270 1.00 39.14 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.931 7.594   11.143 1.00 39.51 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.979 6.784   9.909  1.00 39.17 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.499 9.068   14.137 1.00 38.76 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.928 9.368   15.451 1.00 38.76 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.701 10.301  15.365 1.00 38.58 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.428 10.903  14.324 1.00 38.20 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 23.022 9.980   16.391 1.00 39.21 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 24.181 9.018   16.592 1.00 39.65 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.507 11.336  15.880 1.00 39.29 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.984 10.440  16.484 1.00 38.66 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.905 11.394  16.643 1.00 39.16 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.612 12.744  16.740 1.00 39.44 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.524 12.874  17.560 1.00 39.98 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 18.192 11.145  17.969 1.00 40.25 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.316 9.924   17.989 1.00 43.48 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.742 8.820   18.373 1.00 44.02 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 16.054 10.108  17.605 1.00 44.42 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 19.232 13.722  15.900 1.00 39.02 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.843 15.050  15.857 1.00 39.66 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 20.007 15.702  17.236 1.00 40.53 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 21.101 16.184  17.573 1.00 40.40 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 19.092 15.976  14.897 1.00 40.68 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.715 17.363  14.768 1.00 42.91 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.998 18.188  13.727 1.00 45.92 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.723 19.418  13.414 1.00 48.73 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.497 20.591  13.995 1.00 51.30 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.572 20.706  14.938 1.00 51.98 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 20.196 21.659  13.638 1.00 50.73 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.948 15.650  18.056 1.00 40.75 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.974 16.240  19.392 1.00 41.35 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 20.028 15.606  20.333 1.00 41.52 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 20.491 16.284  21.251 1.00 41.76 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 17.565 16.251  20.022 1.00 42.27 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 17.026 14.913  20.442 1.00 44.37 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 16.394 14.077  19.544 1.00 46.02 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.967 14.351  21.674 1.00 45.41 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 16.025 13.013  20.241 1.00 46.54 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 16.339 13.136  21.529 1.00 46.29 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 20.455 14.356  20.067 1.00 41.35 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 21.472 13.673  20.879 1.00 41.90 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.879 13.656  20.230 1.00 43.20 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.786 13.000  20.764 1.00 43.40 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 21.055 12.218  21.163 1.00 41.48 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.741 11.980  21.890 1.00 41.82 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 19.448 10.481  21.996 1.00 41.70 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.753 12.624  23.269 1.00 42.06 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 23.063 14.331  19.081 1.00 43.83 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 24.363 14.319  18.404 1.00 45.08 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 25.481 14.993  19.208 1.00 45.79 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 25.349 16.142  19.595 1.00 46.40 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 24.251 14.929  17.013 1.00 45.43 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.583 14.284  19.439 1.00 45.73 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.727 14.794  20.210 1.00 46.41 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.545 15.896  19.458 1.00 47.04 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 28.199 16.251  18.331 1.00 47.59 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.618 13.613  20.677 1.00 46.93 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 29.423 13.173  19.578 1.00 47.63 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.822 12.466  21.301 1.00 47.19 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.596 16.451  20.101 1.00 46.71 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 30.485 17.446  19.520 1.00 47.39 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 31.259 16.859  18.344 1.00 47.05 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 31.485 17.551  17.347 1.00 47.06 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.465 17.969  20.588 1.00 49.22 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.928 19.136  21.358 1.00 53.21 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 31.763 20.121  21.851 1.00 55.55 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 29.645 19.463  21.651 1.00 54.84 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 30.971 20.997  22.452 1.00 56.15 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 29.687 20.646  22.354 1.00 56.09 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.662 15.591  18.453 1.00 46.74 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 32.369 14.939  17.369 1.00 47.18 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.469 14.642  16.189 1.00 46.35 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.954 14.601  15.069 1.00 46.67 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 33.078 13.702  17.833 1.00 50.12 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 34.385 13.550  17.110 1.00 55.95 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 35.441 14.012  17.579 1.00 57.10 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 34.329 12.947  15.921 1.00 57.48 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 30.159 14.456  16.423 1.00 45.20 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 29.184 14.267  15.362 1.00 44.50 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 29.109 15.568  14.547 1.00 44.46 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 29.185 15.532  13.321 1.00 43.99 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.813 13.941  15.964 1.00 44.83 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.660 12.508  16.395 1.00 46.71 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 28.331 11.641  15.804 1.00 47.78 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.873 12.253  17.331 1.00 46.85 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 29.048 16.720  15.238 1.00 44.80 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 29.014 18.026  14.589 1.00 45.74 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 30.336 18.381  13.910 1.00 46.49 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 30.321 18.990  12.847 1.00 47.14 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.548 19.114  15.561 1.00 45.72 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 27.057 19.116  15.717 1.00 46.42 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 26.338 18.553  16.731 1.00 47.37 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 26.099 19.585  14.760 1.00 46.46 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.991 18.694  16.490 1.00 47.47 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.818 19.335  15.290 1.00 47.19 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 26.200 20.222  13.521 1.00 47.30 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.650 19.686  14.616 1.00 47.79 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 25.041 20.585  12.865 1.00 48.18 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.786 20.311  13.409 1.00 48.03 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.465 17.959  14.480 1.00 46.30 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.767 18.188  13.855 1.00 47.11 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.954 17.375  12.567 1.00 48.05 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.840 17.688  11.774 1.00 48.80 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.884 17.841  14.827 1.00 47.00 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 32.188 16.290  12.402 1.00 47.83 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.269 15.401  11.249 1.00 47.94 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.919 15.264  10.560 1.00 48.44 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.596 14.197  10.031 1.00 48.96 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.776 14.039  11.682 1.00 48.29 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 34.221 14.073  12.044 1.00 49.87 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 35.091 14.019  11.173 1.00 51.37 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.502 14.179  13.332 1.00 49.41 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 30.132 16.358  10.545 1.00 48.00 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.827 16.416  9.920  1.00 48.20 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.913 16.003  8.455  1.00 48.50 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.888 16.339  7.784  1.00 48.40 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.235 17.830  10.053 1.00 48.45 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.811 18.014  9.500  1.00 50.19 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.816 17.081  10.186 1.00 51.05 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.346 19.445  9.629  1.00 50.59 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.948 15.176  8.007  1.00 48.52 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.835 14.688  6.640  1.00 48.65 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.527 15.205  6.090  1.00 49.32 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.510 15.838  5.035  1.00 49.78 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.920 13.142  6.563  1.00 49.00 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 27.617 12.649  5.154  1.00 49.33 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 29.278 12.643  7.040  1.00 49.35 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.433 14.982  6.844  1.00 49.29 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 24.075 15.382  6.506  1.00 49.62 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 23.250 15.499  7.793  1.00 49.73 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.511 14.803  8.768  1.00 49.31 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.439 14.348  5.557  1.00 49.54 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.990 14.590  5.238  1.00 49.99 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.490 15.437  4.296  1.00 50.97 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.853 13.941  5.840  1.00 49.85 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 20.110 15.373  4.286  1.00 51.12 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.697 14.464  5.226  1.00 50.61 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.702 12.988  6.856  1.00 50.04 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.413 14.046  5.575  1.00 50.97 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.434 12.586  7.205  1.00 50.84 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.305 13.105  6.560  1.00 51.05 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.265 16.398  7.795  1.00 50.05 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.389 16.593  8.943  1.00 50.77 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 20.042 17.181  8.511  1.00 50.79 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.973 17.905  7.514  1.00 50.96 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 22.067 17.446  10.051 1.00 53.46 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.617 18.790  9.600  1.00 58.50 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.669 19.966  9.741  1.00 65.70 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.807 20.934  8.959  1.00 67.88 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.783 19.918  10.625 1.00 67.43 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.967 16.850  9.240  1.00 50.47 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.639 17.398  8.938  1.00 50.70 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.913 17.666  10.246 1.00 49.71 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.438 16.728  10.869 1.00 49.73 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.821 16.451  8.038  1.00 53.13 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.629 17.097  7.345  1.00 60.10 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 15.032 18.037  7.924  1.00 61.31 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.277 16.649  6.235  1.00 63.22 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.810 18.941  10.653 1.00 48.88 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 16.139 19.323  11.895 0.50 49.07 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 16.129 19.347  11.883 0.50 49.08 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.704 18.784  11.962 1.00 48.70 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 14.309 18.238  12.986 1.00 48.54 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 16.148 20.841  12.062 0.50 50.70 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 16.090 20.870  11.982 0.50 50.71 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 16.083 21.230  13.425 0.50 53.00 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 15.477 21.432  10.831 0.50 53.03 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.948 18.881  10.858 1.00 47.78 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.580 18.378  10.813 1.00 47.54 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 12.465 16.849  10.747 1.00 46.53 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 11.354 16.330  10.724 1.00 46.34 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.801 19.021  9.668  1.00 49.29 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 12.238 18.552  8.404  1.00 51.89 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.585 16.132  10.683 1.00 45.56 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 13.573 14.672  10.683 1.00 45.43 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 14.203 14.080  11.956 1.00 45.55 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 14.120 12.862  12.159 1.00 45.99 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 14.296 14.108  9.453  1.00 46.42 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.430 14.084  8.201  1.00 50.06 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 14.155 13.520  6.988  1.00 52.64 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 14.315 12.072  7.092  1.00 55.39 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.560 11.263  6.067  1.00 57.57 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.665 11.751  4.836  1.00 57.05 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.692 9.958   6.263  1.00 57.63 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.840 14.925  12.802 1.00 44.60 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 15.572 14.514  13.994 1.00 44.18 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.679 13.530  13.598 1.00 43.76 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.962 12.602  14.344 1.00 44.03 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.639 13.942  15.086 1.00 45.19 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 15.298 13.761  16.447 1.00 47.87 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 16.180 14.572  16.790 1.00 48.57 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.926 12.806  17.167 1.00 48.74 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 17.334 13.746  12.445 1.00 42.95 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 18.399 12.864  11.988 1.00 42.69 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.741 13.570  11.821 1.00 42.88 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.792 14.736  11.443 1.00 43.22 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 18.031 12.208  10.650 1.00 42.45 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.999 11.097  10.663 1.00 43.62 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.836 10.505  9.263  1.00 43.90 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.362 10.000  11.661 1.00 44.19 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.826 12.836  12.042 1.00 42.46 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 22.165 13.351  11.807 1.00 43.00 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 23.097 12.208  11.376 1.00 43.47 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 23.140 11.146  12.007 1.00 43.75 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.749 14.122  13.020 1.00 42.83 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 24.114 14.817  12.787 1.00 43.26 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 24.168 16.159  13.456 1.00 43.47 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 25.265 13.974  13.277 1.00 43.77 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.841 12.433  10.302 1.00 43.13 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.813 11.466  9.826  1.00 43.07 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 26.202 12.067  9.969  1.00 43.32 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 26.465 13.164  9.485  1.00 43.37 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 24.521 10.975  8.379  1.00 42.88 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.660 10.105  7.858  1.00 42.92 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 23.199 10.223  8.316  1.00 42.77 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 27.064 11.382  10.687 1.00 43.59 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.445 11.797  10.863 1.00 44.34 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 29.360 10.711  10.260 1.00 45.05 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.918 9.575   10.033 1.00 44.88 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.756 12.022  12.342 1.00 45.66 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.899 10.814  13.074 1.00 47.76 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.626 11.056  9.992  1.00 45.44 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.559 10.095  9.419  1.00 46.53 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 32.293 9.311   10.506 1.00 47.93 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.488 9.814   11.612 1.00 48.34 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.554 10.805  8.515  1.00 47.71 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 33.228 11.809  9.254  1.00 49.88 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.696 8.071   10.192 1.00 48.46 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.412 7.191   11.117 1.00 49.01 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.751 6.746   10.530 1.00 50.10 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.919 6.709   9.315  1.00 50.35 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.551 5.967   11.493 1.00 49.98 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.283 5.184   10.331 1.00 51.54 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 31.251 6.343   12.146 1.00 49.83 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.694 6.383   11.392 1.00 50.97 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 37.010 5.933   10.956 1.00 52.30 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.978 4.465   10.519 1.00 53.45 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 37.428 4.147   9.418  1.00 53.94 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 38.061 6.223   12.037 1.00 53.63 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 38.172 7.634   12.214 1.00 54.36 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 39.427 5.660   11.686 1.00 54.36 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 36.445 3.571   11.375 1.00 53.63 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 36.337 2.135   11.065 1.00 54.05 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 35.044 1.823   10.261 1.00 53.75 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 34.184 2.691   10.157 1.00 53.93 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 36.398 1.316   12.353 1.00 54.46 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.916 0.609   9.680  1.00 53.33 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.777 0.202   8.842  1.00 53.55 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.542 -0.375  9.592  1.00 53.28 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.639 -1.430  10.209 1.00 53.71 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 34.269 -0.814  7.794  1.00 55.29 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 33.187 -1.357  6.863  1.00 59.42 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 33.106 -0.596  5.566  1.00 63.75 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 34.047 0.094   5.148  1.00 65.41 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 31.979 -0.717  4.895  1.00 63.96 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 31.388 0.272   9.440  1.00 52.43 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 30.116 -0.146  10.026 1.00 52.07 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 29.460 -1.218  9.183  1.00 51.44 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.589 -1.186  7.961  1.00 51.77 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.752 -2.172  9.804  1.00 50.66 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 28.176 -3.290  9.059  1.00 50.76 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.670 -3.514  9.256  1.00 50.36 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 26.194 -4.607  8.933  1.00 50.40 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.949 -4.567  9.365  1.00 51.97 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 30.724 -4.462  9.033  1.00 58.20 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.924 -2.522  9.787  1.00 49.62 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.481 -2.683  9.989  1.00 49.42 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.788 -2.641  8.626  1.00 48.50 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.120 -1.784  7.808  1.00 48.52 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.905 -1.580  10.905 1.00 51.51 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 24.464 -1.523  12.315 1.00 57.08 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 25.529 -2.126  12.558 1.00 58.29 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.860 -0.833  13.167 1.00 59.33 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.847 -3.563  8.370  1.00 47.54 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 22.152 -3.591  7.083  1.00 47.40 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.897 -2.729  7.133  1.00 47.42 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 20.096 -2.873  8.045  1.00 47.78 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.917 -5.047  6.617  1.00 48.11 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 23.078 -5.498  5.895  1.00 48.50 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.671 -5.212  5.743  1.00 48.20 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.726 -1.830  6.158  1.00 46.97 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.541 -0.975  6.100  1.00 46.58 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.444 -1.659  5.287  1.00 46.52 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.732 -2.272  4.260  1.00 46.53 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.891 0.416   5.528  1.00 46.47 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 21.077 1.043   6.285  1.00 47.02 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.663 1.338   5.498  1.00 46.60 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.851 1.235   7.742  1.00 47.75 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.193 -1.582  5.752  1.00 46.27 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 16.078 -2.212  5.047  1.00 46.36 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.578 -1.388  3.855  1.00 46.02 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.294 -0.206  3.989  1.00 45.90 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.935 -2.485  6.011  1.00 46.35 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.461 -2.020  2.695  1.00 45.63 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.931 -1.369  1.500  1.00 45.60 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.631 -2.099  1.225  1.00 45.26 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.616 -3.031  0.431  1.00 45.11 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.907 -1.526  0.316  1.00 46.19 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.307 -0.969  0.562  1.00 47.03 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.337 0.519   0.841  1.00 47.39 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.687 0.973   1.188  1.00 46.95 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.946 2.088   1.863  1.00 47.26 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.955 2.872   2.269  1.00 46.57 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 20.196 2.421   2.152  1.00 45.99 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.559 -1.734  1.944  1.00 45.22 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 11.262 -2.431  1.871  1.00 45.62 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 10.079 -1.484  2.106  1.00 46.37 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.274 -0.305  2.403  1.00 46.82 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.243 -3.586  2.874  1.00 45.94 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.132 -3.058  4.615  1.00 46.82 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.853  -2.022  2.031  1.00 46.67 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.604  -1.292  2.252  1.00 47.48 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.888  -1.741  3.552  1.00 47.52 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.700  -1.470  3.708  1.00 47.77 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.680  -1.565  1.056  1.00 49.82 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.502  -0.621  0.925  1.00 56.00 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 4.374  -1.109  0.752  1.00 57.15 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 5.715  0.610   0.995  1.00 58.93 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.600  -2.427  4.471  1.00 47.12 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 7.054  -3.011  5.702  1.00 47.03 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.306  -2.039  6.612  1.00 45.67 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.540  -0.832  6.608  1.00 46.48 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.131  -3.761  6.479  1.00 48.33 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.614  -5.339  5.733  1.00 53.62 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.350  -2.587  7.338  1.00 43.29 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.576  -1.867  8.333  1.00 41.68 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.429  -2.707  9.618  1.00 39.10 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.492  -2.480  10.385 1.00 38.76 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.193  -1.492  7.799  1.00 43.91 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 3.158  -0.375  6.776  1.00 48.90 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.721  -0.028  6.461  1.00 55.98 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.041  -0.706  5.674  1.00 58.08 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 1.210  1.027   7.090  1.00 57.23 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.322  -3.696  9.825  1.00 37.33 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.406  -4.561  10.997 1.00 36.70 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 6.884  -4.738  11.295 1.00 35.67 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.667  -5.027  10.399 1.00 35.14 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.720  -5.929  10.778 1.00 37.47 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.200  -6.533  9.577  1.00 38.40 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.211  -5.839  10.771 1.00 37.31 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.260  -4.546  12.547 1.00 35.25 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.655  -4.657  12.967 1.00 34.82 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.811  -4.930  14.450 1.00 34.50 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.827  -5.081  15.173 1.00 34.21 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 10.048 -5.028  14.915 1.00 34.34 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.340 -5.284  16.316 1.00 34.36 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.305 -4.208  16.752 1.00 34.19 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.336 -4.051  16.111 1.00 34.90 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 10.966 -6.684  16.485 1.00 35.30 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.510 -6.880  17.895 1.00 36.13 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 9.974  -7.779  16.132 1.00 35.61 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 10.991 -3.457  17.809 1.00 33.40 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.869 -2.387  18.271 1.00 33.21 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.435 -2.629  19.662 1.00 33.44 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.780 -3.249  20.491 1.00 33.35 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.178 -1.009  18.179 1.00 33.19 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.253 -0.687  19.335 1.00 34.20 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.961  -1.191  19.381 1.00 34.88 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.667 0.137   20.377 1.00 35.28 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 8.108  -0.897  20.440 1.00 35.67 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.829  0.419   21.453 1.00 35.96 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.546  -0.097  21.477 1.00 36.60 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.707  0.171   22.534 1.00 37.98 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.646 -2.110  19.935 1.00 33.46 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 14.235 -2.250  21.257 1.00 33.22 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.776 -1.091  22.152 1.00 33.78 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.710 0.052   21.696 1.00 33.89 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.766 -2.345  21.187 1.00 32.45 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.379 -2.416  22.564 1.00 32.08 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 16.219 -3.542  23.361 1.00 32.30 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 17.045 -1.328  23.106 1.00 32.69 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.733 -3.592  24.652 1.00 32.82 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.578 -1.373  24.387 1.00 33.20 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.399 -2.498  25.167 1.00 33.58 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.939 -2.535  26.427 1.00 35.14 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 13.481 -1.385  23.426 1.00 33.83 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 13.010 -0.398  24.381 1.00 34.62 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.860 -0.531  25.638 1.00 36.09 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.677 -1.504  26.361 1.00 36.51 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 11.532 -0.660  24.666 1.00 34.91 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.823 0.341   25.992 1.00 36.79 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.817 0.404   25.893 1.00 36.62 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.698 0.286   27.066 1.00 37.76 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 14.997 0.514   28.417 1.00 38.29 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 15.445 -0.039  29.427 1.00 37.96 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.953 1.156   26.956 1.00 40.02 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 16.764 2.367   26.245 1.00 43.70 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.859 1.234   28.434 1.00 38.73 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 13.107 1.418   29.684 1.00 39.15 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 12.504 0.098   30.228 1.00 39.77 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 12.079 0.037   31.383 1.00 40.36 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 12.032 2.493   29.532 1.00 39.98 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 11.104 2.232   28.492 1.00 41.56 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 12.471 -0.942  29.393 1.00 39.57 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 11.977 -2.268  29.723 1.00 39.93 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 13.052 -3.342  29.551 1.00 40.92 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.864 -4.458  30.058 1.00 41.69 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.788 -2.619  28.811 1.00 40.44 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 9.575  -1.748  29.035 1.00 42.60 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 9.013  -1.973  30.421 1.00 45.32 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.876  -1.108  30.708 1.00 47.78 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.958  0.072   31.309 1.00 49.36 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 9.139  0.564   31.665 1.00 47.62 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.863  0.786   31.530 1.00 49.98 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 14.151 -3.032  28.804 1.00 40.59 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 15.208 -3.957  28.396 1.00 41.15 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.527 -5.093  27.611 1.00 40.75 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.764 -6.268  27.887 1.00 40.90 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 15.972 -4.504  29.605 1.00 43.98 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.765 -3.470  30.385 1.00 49.23 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.265 -4.083  31.675 1.00 54.05 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 17.988 -3.120  32.509 1.00 59.21 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 18.135 -3.231  33.827 1.00 62.02 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 17.572 -4.240  34.483 1.00 62.57 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.806 -2.309  34.506 1.00 61.67 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.594 -4.720  26.697 1.00 39.85 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.754 -5.643  25.951 1.00 39.00 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.562 -5.213  24.526 1.00 37.67 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.467 -4.021  24.253 1.00 37.34 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.363 -5.700  26.595 1.00 40.54 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 11.248 -6.695  27.723 1.00 44.31 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.835  -6.770  28.253 1.00 47.97 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.782  -7.660  29.468 1.00 51.98 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 10.702 -7.183  30.537 1.00 55.26 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.437 -6.198  23.629 1.00 36.89 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 12.165 -5.993  22.214 1.00 36.99 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.640 -6.207  22.018 1.00 36.81 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 10.094 -7.193  22.525 1.00 37.13 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 12.977 -6.986  21.374 1.00 37.98 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.462 -6.765  21.431 1.00 40.74 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 15.180 -6.359  20.313 1.00 42.72 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.322 -6.909  22.466 1.00 41.80 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.442 -6.264  20.707 1.00 42.94 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.577 -6.581  21.992 1.00 42.85 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 9.941  -5.256  21.372 1.00 35.92 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.495  -5.364  21.206 1.00 35.85 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 8.059  -5.539  19.766 1.00 35.33 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.423  -4.737  18.908 1.00 35.04 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.777  -4.140  21.795 1.00 36.22 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.705  -4.092  23.306 1.00 37.73 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 6.840  -4.921  24.007 1.00 38.79 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.442  -3.163  24.029 1.00 39.03 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 6.758  -4.870  25.395 1.00 39.87 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.355  -3.090  25.416 1.00 40.05 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.508  -3.945  26.098 1.00 41.10 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.396  -3.863  27.473 1.00 43.04 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.210  -6.541  19.490 1.00 35.06 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.677  -6.682  18.121 1.00 35.04 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.544  -5.674  17.930 1.00 35.47 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.620  -5.637  18.748 1.00 35.91 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 6.149  -8.119  18.083 1.00 35.52 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.850  -8.464  19.512 1.00 36.01 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.671  -7.561  20.413 1.00 34.52 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.644  -4.803  16.922 1.00 35.08 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.627  -3.778  16.700 1.00 35.07 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.260  -3.598  15.222 1.00 34.92 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 5.047  -3.912  14.322 1.00 35.28 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.046  -2.403  17.324 1.00 35.62 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.562  -2.548  18.750 1.00 36.12 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.065  -1.677  16.458 1.00 35.99 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 3.070  -3.048  14.972 1.00 34.29 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.683  -2.648  13.624 1.00 34.40 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.715  -1.106  13.642 1.00 34.26 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.306  -0.496  14.635 1.00 34.59 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 1.317  -3.208  13.228 1.00 35.51 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.230  -2.412  13.663 1.00 37.03 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.255  -0.481  12.598 1.00 33.79 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.405  0.979   12.584 1.00 34.24 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.867  1.616   11.286 1.00 35.93 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.538  0.892   10.340 1.00 36.80 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.881  1.369   12.873 1.00 33.32 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.876  0.666   11.985 1.00 32.98 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.346  -0.589  12.304 1.00 33.33 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.291  1.235   10.800 1.00 33.81 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.203  -1.261  11.450 1.00 34.06 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.159  0.559   9.951  1.00 34.42 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.612  -0.680  10.286 1.00 33.94 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.730  2.963   11.253 1.00 36.03 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.237  3.663   10.066 1.00 36.70 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.360  3.933   9.031  1.00 38.00 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.527  3.680   9.310  1.00 37.88 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.522  4.951   10.464 1.00 37.48 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.399  5.849   11.121 1.00 40.04 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 3.006  4.374   7.813  1.00 39.06 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 4.003  4.680   6.779  1.00 40.27 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.600  6.078   7.025  1.00 41.64 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.946  6.909   7.649  1.00 41.89 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 3.395  4.526   5.367  1.00 41.54 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 3.270  3.068   4.936  1.00 44.11 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.740  2.913   3.522  1.00 46.99 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.526  1.457   3.175  1.00 50.28 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 1.809  1.279   1.877  1.00 52.43 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.862  6.338   6.634  1.00 42.67 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.483  7.646   6.944  1.00 43.71 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.634  8.871   6.608  1.00 45.34 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 5.176  8.974   5.474  1.00 45.66 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.774  7.616   6.125  1.00 44.04 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 8.113  6.184   6.020  1.00 44.16 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.806  5.445   5.932  1.00 42.43 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 5.387  9.778   7.586  1.00 46.26 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.539  10.950  7.321  1.00 47.80 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.824  12.161  8.263  1.00 49.57 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.823  12.150  8.975  1.00 49.54 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 3.058  10.550  7.329  1.00 48.45 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.553  10.402  8.644  1.00 50.28 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 3.981  13.227  8.212  1.00 50.97 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 4.110  14.453  9.017  1.00 52.59 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 3.279  14.374  10.280 1.00 53.91 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 2.052  14.397  10.197 1.00 54.06 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.600  15.659  8.224  1.00 52.80 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.617  16.415  7.421  1.00 54.69 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 3.926  17.418  6.505  1.00 55.67 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 5.587  17.112  8.322  1.00 55.10 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.926  14.338  11.445 1.00 54.64 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 3.198  14.294  12.704 1.00 55.82 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 3.576  15.487  13.571 1.00 57.22 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.754  15.815  13.699 1.00 56.81 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 3.355  12.917  13.400 1.00 56.26 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.470  11.877  12.707 1.00 57.02 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 3.032  12.974  14.891 1.00 56.76 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 3.182  10.903  11.949 1.00 58.12 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 2.563  16.177  14.107 1.00 58.48 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.782  17.332  14.968 1.00 59.64 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 3.413  16.914  16.311 1.00 60.14 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 2.744  16.342  17.174 1.00 60.21 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 1.464  18.104  15.190 1.00 59.81 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 1.628  19.229  16.182 1.00 60.83 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 2.519  20.260  15.942 1.00 61.57 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 0.957  19.212  17.390 1.00 61.86 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 2.714  21.264  16.877 1.00 62.37 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 1.157  20.219  18.326 1.00 62.61 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 2.033  21.239  18.062 1.00 62.29 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 4.696  17.209  16.482 1.00 60.59 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 5.384  16.896  17.726 1.00 61.20 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 5.398  18.127  18.620 1.00 61.99 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 5.919  19.180  18.235 1.00 61.53 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 6.783  16.281  17.531 1.00 61.53 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 7.319  15.753  18.857 1.00 62.32 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 6.753  15.172  16.490 1.00 61.51 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 4.773  17.989  19.804 1.00 62.71 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 4.657  19.012  20.839 1.00 63.72 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 6.029  19.569  21.214 1.00 64.83 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 7.055  18.912  21.000 1.00 64.91 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 3.992  18.391  22.078 1.00 66.00 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 3.286  19.377  22.990 1.00 71.39 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 1.809  19.571  22.706 1.00 78.12 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 1.109  20.143  23.575 1.00 80.09 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 1.347  19.154  21.618 1.00 79.50 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 6.056  20.781  21.773 1.00 65.54 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 7.322  21.405  22.169 1.00 66.37 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 8.054  20.640  23.268 1.00 66.83 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 7.425  20.049  24.147 1.00 67.01 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 7.091  22.839  22.612 1.00 66.38 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 9.392  20.659  23.201 1.00 66.69 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 10.310 20.062  24.169 1.00 67.08 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 11.506 21.027  24.349 1.00 67.66 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 11.494 22.121  23.772 1.00 68.06 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 10.769 18.681  23.688 1.00 68.17 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 11.670 18.752  22.595 1.00 69.72 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 12.533 20.652  25.142 1.00 67.55 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 13.709 21.512  25.309 1.00 67.83 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 14.659 21.481  24.088 1.00 66.95 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 15.513 22.362  23.943 1.00 67.12 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 14.453 21.204  26.625 1.00 71.53 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 15.493 20.094  26.545 1.00 78.65 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 15.068 18.753  27.113 1.00 86.49 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 15.887 18.131  27.832 1.00 88.00 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 13.923 18.323  26.837 1.00 88.53 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 14.521 20.460  23.230 1.00 65.72 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 15.347 20.310  22.041 1.00 65.02 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 14.716 21.028  20.838 1.00 64.67 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 15.432 21.530  19.974 1.00 64.68 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 15.545 18.817  21.712 1.00 64.54 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 16.021 17.955  22.866 1.00 64.72 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 15.140 17.137  23.559 1.00 65.28 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 17.364 17.914  23.225 1.00 65.37 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 15.575 16.324  24.602 1.00 65.99 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 17.813 17.091  24.255 1.00 65.91 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 16.913 16.302  24.948 1.00 66.60 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 17.346 15.486  25.967 1.00 67.48 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 13.382 21.057  20.767 1.00 64.34 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 12.685 21.677  19.643 1.00 64.69 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 11.392 22.366  20.086 1.00 65.06 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 10.652 21.804  20.895 1.00 65.33 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 12.243 20.592  18.628 1.00 64.43 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 13.313 19.716  18.012 1.00 64.60 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 13.990 20.115  16.869 1.00 65.21 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 13.541 18.429  18.482 1.00 65.10 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 14.940 19.295  16.269 1.00 65.85 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 14.488 17.601  17.893 1.00 65.71 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 15.185 18.036  16.781 1.00 66.36 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 16.128 17.230  16.190 1.00 67.21 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 10.991 23.469  19.422 1.00 64.82 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 9.665  24.053  19.706 1.00 64.59 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 8.521  23.240  19.043 1.00 64.31 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 8.763  22.172  18.473 1.00 64.31 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 9.776  25.475  19.125 1.00 65.31 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 11.239 25.640  18.685 1.00 65.78 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 11.709 24.250  18.401 1.00 64.28 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 7.272  23.722  19.134 1.00 63.90 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 6.127  23.043  18.525 1.00 63.85 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 6.297  23.058  16.995 1.00 63.14 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 6.475  24.120  16.398 1.00 63.45 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 4.836  23.735  18.931 1.00 64.06 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 6.291  21.873  16.373 1.00 61.69 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 6.577  21.745  14.944 1.00 60.43 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 6.027  20.421  14.362 1.00 58.95 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 5.618  19.544  15.112 1.00 58.92 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 8.117  21.760  14.780 1.00 61.16 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 8.771  20.596  15.526 1.00 63.17 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 10.275 20.591  15.450 1.00 65.82 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.815 19.364  14.857 1.00 68.07 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 11.013 18.228  15.519 1.00 69.80 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 11.538 17.179  14.904 1.00 69.25 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 10.671 18.127  16.797 1.00 69.76 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 6.079  20.261  13.029 1.00 57.63 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 5.659  19.034  12.357 1.00 56.72 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.898  18.276  11.887 1.00 55.17 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.550  18.721  10.943 1.00 55.34 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.844  19.362  11.109 1.00 57.01 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 3.382  19.647  11.338 1.00 58.29 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 2.475  18.616  11.527 1.00 59.29 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 2.885  20.937  11.238 1.00 59.51 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 1.118  18.867  11.678 1.00 60.44 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 1.528  21.200  11.361 1.00 60.62 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.646  20.163  11.587 1.00 61.62 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -0.697 20.430  11.712 1.00 63.30 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 7.207  17.129  12.499 1.00 53.44 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 8.347  16.323  12.074 1.00 52.39 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.958  15.413  10.901 1.00 51.64 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.960  14.696  10.976 1.00 52.62 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 8.908  15.505  13.250 1.00 53.35 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.972  14.490  12.844 1.00 55.17 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 10.715 13.896  14.002 1.00 57.44 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 10.698 14.413  15.126 1.00 57.99 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 11.399 12.795  13.742 1.00 57.82 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.736  15.438  9.825  1.00 50.03 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.467  14.605  8.654  1.00 49.34 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 9.203  13.247  8.712  1.00 47.95 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 10.173 13.100  9.468  1.00 48.47 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 8.811  15.362  7.373  1.00 51.22 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 10.202 15.625  7.246  1.00 54.32 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.730  12.263  7.917  1.00 46.03 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 9.271  10.900  7.825  1.00 44.85 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 9.167  10.147  9.148  1.00 43.40 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 10.069 9.399   9.508  1.00 43.37 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.716 10.877  7.278  1.00 45.60 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 10.842 11.277  5.841  1.00 47.76 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.659 10.362  4.819  1.00 49.50 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 11.144 12.481  5.300  1.00 48.92 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 10.849 11.036  3.692  1.00 50.03 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 11.136 12.317  3.930  1.00 49.86 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 8.069  10.348  9.869  1.00 42.34 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.858  9.716   11.171 1.00 41.95 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.753  8.635   11.142 1.00 39.81 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.639  8.889   10.702 1.00 39.37 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 7.543  10.788  12.232 1.00 42.90 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 7.476  10.292  13.673 1.00 44.78 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.854  10.056  14.221 1.00 45.48 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.693  11.259  14.553 1.00 45.35 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 7.085  7.432   11.621 1.00 38.41 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 6.184  6.280   11.658 1.00 37.37 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.732  6.022   13.100 1.00 36.86 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.564  5.881   14.000 1.00 37.06 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.879  5.051   11.057 1.00 36.78 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.575  5.374   9.769  1.00 37.53 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.590  4.052   9.120  1.00 39.06 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.924  4.043   10.293 1.00 33.77 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 4.421  6.016   13.324 1.00 35.92 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.882  5.844   14.663 1.00 35.67 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 3.363  4.447   14.896 1.00 35.32 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.715  3.863   14.016 1.00 35.08 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.761  6.865   14.945 1.00 35.74 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 3.186  8.330   15.036 1.00 37.10 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.995  9.229   15.066 1.00 37.21 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 4.023  8.581   16.266 1.00 38.38 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.627  3.926   16.119 1.00 34.51 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 3.160  2.628   16.602 1.00 33.76 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.576  2.766   18.023 1.00 33.83 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.916  3.698   18.758 1.00 33.71 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 4.298  1.622   16.596 1.00 33.20 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.675  1.856   18.398 1.00 33.92 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 1.111  1.850   19.739 1.00 34.65 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 2.172  1.123   20.571 1.00 35.71 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.503  -0.031  20.276 1.00 35.93 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.279 1.155   19.801 1.00 34.91 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -0.763 1.005   21.237 1.00 35.38 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.308 1.912   18.978 1.00 35.11 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.776  1.836   21.514 1.00 36.04 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.820  1.251   22.342 1.00 36.99 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 4.382  2.141   23.435 1.00 37.58 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 4.169  3.357   23.438 1.00 37.88 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 5.122  1.532   24.377 1.00 37.35 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 5.751  2.270   25.467 1.00 37.54 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 7.080  2.896   25.043 1.00 37.20 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 7.811  2.347   24.217 1.00 36.11 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 5.934  1.383   26.718 1.00 38.42 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 6.677  2.053   27.834 1.00 41.06 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 6.198  3.208   28.432 1.00 42.90 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 7.866  1.732   28.397 1.00 42.29 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 7.096  3.539   29.345 1.00 43.29 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 8.120  2.686   29.355 1.00 43.29 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 7.391  4.040   25.660 1.00 37.82 ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 8.619  4.782   25.425 1.00 38.62 ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 8.810  5.866   26.486 1.00 38.57 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 7.857  6.362   27.072 1.00 38.45 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 8.593  5.421   24.042 1.00 40.86 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 7.592  6.427   23.950 1.00 44.38 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 10.059 6.214   26.735 1.00 38.60 ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 10.484 7.275   27.653 1.00 38.86 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 11.541 8.098   26.890 1.00 39.02 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 12.165 7.566   25.973 1.00 39.23 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 11.109 6.677   28.923 1.00 40.71 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 10.298 5.552   29.532 1.00 44.93 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 10.282 5.537   31.042 1.00 48.82 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 11.235 6.075   31.645 1.00 50.60 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 9.313  5.001   31.624 1.00 49.58 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 11.789 9.377   27.231 1.00 38.65 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 12.793 10.153  26.471 1.00 38.20 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 14.138 9.444   26.240 1.00 38.06 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 14.660 9.511   25.130 1.00 38.23 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 12.925 11.440  27.278 1.00 38.97 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 11.576 11.603  27.926 1.00 39.38 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 11.119 10.205  28.257 1.00 37.92 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 14.645 8.709   27.242 1.00 37.83 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 15.912 7.965   27.150 1.00 37.55 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 15.923 6.797   26.161 1.00 37.23 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 16.972 6.207   25.879 1.00 36.99 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 14.746 6.470   25.606 1.00 36.49 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 14.555 5.403   24.644 1.00 35.96 ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 14.867 5.818   23.205 1.00 35.74 ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 15.014 4.937   22.354 1.00 35.32 ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 13.131 4.853   24.747 1.00 36.74 ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 12.938 3.960   25.941 1.00 38.71 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 13.872 3.193   26.260 1.00 38.95 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 11.851 4.018   26.552 1.00 39.72 ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 15.000 7.147   22.926 1.00 35.64 ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 15.370 7.682   21.607 1.00 35.94 ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 16.712 7.072   21.210 1.00 36.21 ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.661 7.176   21.981 1.00 36.94 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 15.457 9.206   21.643 1.00 36.59 ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 13.851 10.060  21.649 1.00 39.45 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 16.743 6.326   20.111 1.00 35.53 ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.961 5.656   19.662 1.00 35.02 ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.844 4.156   19.435 1.00 33.60 ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 18.697 3.562   18.768 1.00 33.33 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 16.824 3.536   20.024 1.00 32.28 ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 16.593 2.108   19.860 1.00 31.59 ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 16.119 1.829   18.451 1.00 31.18 ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 15.342 2.609   17.901 1.00 31.01 ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 16.599 0.744   17.839 1.00 30.57 ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 16.248 0.434   16.461 1.00 30.45 ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 14.967 -0.402  16.291 1.00 31.56 ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 14.694 -1.320  17.069 1.00 31.60 ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.452 -0.247  15.750 1.00 29.89 ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 18.730 0.588   15.879 1.00 29.44 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.140 -0.548  14.279 1.00 30.17 ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 19.931 -0.149  15.483 1.00 29.68 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 14.215 -0.093  15.222 1.00 31.97 ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 13.054 -0.824  14.760 1.00 33.05 ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.600 -1.678  13.611 1.00 34.81 ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 14.171 -1.146  12.659 1.00 34.54 ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 11.980 0.160   14.246 1.00 32.79 ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 10.796 -0.415  13.441 1.00 33.55 ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 9.844  -1.195  14.329 1.00 34.20 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 9.999  0.707   12.768 1.00 33.92 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 13.481 -2.993  13.725 1.00 36.60 ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 13.992 -3.907  12.713 1.00 39.08 ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.901 -4.795  12.122 1.00 40.94 ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 11.963 -5.189  12.814 1.00 40.70 ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 15.071 -4.810  13.319 1.00 41.67 ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 16.470 -4.531  12.818 1.00 46.78 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.419 -5.689  13.093 1.00 51.20 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 18.722 -5.446  12.471 1.00 55.38 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 19.807 -5.051  13.131 1.00 59.06 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 19.778 -4.911  14.454 1.00 58.84 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 20.937 -4.819  12.478 1.00 60.32 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 13.064 -5.141  10.841 1.00 42.12 ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 12.201 -6.074  10.122 1.00 43.36 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 13.101 -7.163  9.499  1.00 44.83 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 14.331 -7.041  9.552  1.00 44.82 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 11.382 -5.345  9.060  1.00 43.89 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.371 -4.670  7.704  1.00 47.14 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 12.516 -8.213  8.867  1.00 46.00 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 13.330 -9.263  8.230  1.00 47.24 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 14.369 -8.695  7.238  1.00 47.29 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 15.465 -9.235  7.130  1.00 47.55 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 12.470 -10.379 7.580  1.00 49.75 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 11.322 -9.927  6.663  1.00 54.28 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 10.838 -11.050 5.752  1.00 60.09 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 10.236 -12.041 6.190  1.00 61.91 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 11.095 -10.930 4.452  1.00 61.06 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 14.060 -7.547  6.619  1.00 46.89 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 14.943 -6.890  5.657  1.00 47.06 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 16.127 -6.157  6.276  1.00 46.12 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.131 -5.953  5.588  1.00 46.27 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 14.152 -5.939  4.746  1.00 48.62 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 12.947 -6.582  4.143  1.00 51.83 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 11.820 -6.840  4.901  1.00 53.84 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 12.749 -7.042  2.885  1.00 53.36 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 10.965 -7.427  4.077  1.00 54.76 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 11.480 -7.572  2.853  1.00 54.61 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 15.999 -5.747  7.538  1.00 44.71 ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.056 -5.020  8.232  1.00 43.67 ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.575 -3.841  9.059  1.00 42.55 ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.461 -3.856  9.595  1.00 42.52 ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.421 -2.803  9.164  1.00 41.44 ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 17.169 -1.591  9.956  1.00 40.52 ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 16.188 -0.615  9.282  1.00 39.76 ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.495 -0.043  8.241  1.00 39.70 ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.495 -0.890  10.354 1.00 40.62 ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 18.237 0.453   11.030 1.00 40.70 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 19.330 -1.789  11.255 1.00 41.08 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 15.033 -0.390  9.927  1.00 38.93 ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 13.963 0.490   9.455  1.00 38.45 ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 14.167 1.951   9.911  1.00 37.70 ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 14.068 2.883   9.107  1.00 37.33 ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.587 -0.051  9.925  1.00 39.16 ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.448 0.778   9.339  1.00 39.57 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.424 -1.532  9.581  1.00 39.70 ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.432 2.131   11.203 1.00 37.12 ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.659 3.448   11.781 1.00 36.86 ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 14.940 3.430   13.269 1.00 36.05 ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 14.912 2.370   13.890 1.00 36.06 ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 15.211 4.604   13.850 1.00 35.41 ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 15.494 4.729   15.277 1.00 35.66 ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 14.363 5.438   16.018 1.00 36.30 ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 13.674 6.270   15.433 1.00 36.25 ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 16.844 5.445   15.503 1.00 36.11 ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.870 6.804   14.801 1.00 36.85 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 18.021 4.576   15.061 1.00 36.50 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 18.016 7.659   15.213 1.00 38.20 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 14.170 5.125   17.318 1.00 36.95 ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 13.125 5.749   18.145 1.00 37.51 ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 13.390 7.247   18.223 1.00 38.14 ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 14.540 7.657   18.394 1.00 37.66 ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 12.987 5.085   19.531 1.00 38.02 ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 12.175 5.949   20.494 1.00 38.36 ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 12.361 3.706   19.396 1.00 38.60 ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 12.352 8.053   17.966 1.00 38.64 ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 12.522 9.482   17.903 1.00 39.72 ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 11.559 10.234  18.784 1.00 41.05 ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 11.987 11.090  19.537 1.00 41.46 ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 12.438 9.952   16.453 1.00 41.09 ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 13.039 11.220  16.247 1.00 43.11 ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 10.264 9.942   18.695 1.00 42.10 ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 9.233  10.657  19.465 1.00 42.87 ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 8.477  9.668   20.390 1.00 43.12 ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 8.800  8.485   20.413 1.00 43.17 ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 8.297  11.451  18.488 1.00 44.94 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 7.317  10.570  17.952 1.00 47.04 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 9.030  12.137  17.347 1.00 45.47 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 7.468  10.140  21.116 1.00 43.42 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 6.666  9.288   21.980 1.00 44.03 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 5.729  10.105  22.837 1.00 44.52 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 6.050  11.238  23.206 1.00 44.71 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 4.574  9.535   23.147 1.00 44.51 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 3.578  10.194  23.982 1.00 45.05 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 2.167  9.681   23.782 1.00 45.05 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 1.821  9.246   22.684 1.00 45.37 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 1.350  9.720   24.842 1.00 44.70 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? -0.057 9.286   24.805 1.00 45.40 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? -0.254 7.773   24.552 1.00 44.40 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -1.301 7.382   24.035 1.00 44.35 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -0.862 10.095  23.763 1.00 47.67 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -0.880 11.591  23.984 1.00 52.34 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -0.251 12.127  24.914 1.00 54.49 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -1.613 12.296  23.125 1.00 52.69 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 0.742  6.954   24.907 1.00 42.97 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 0.705  5.517   24.646 1.00 41.71 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 1.158  5.164   23.237 1.00 40.40 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 0.886  4.069   22.741 1.00 40.17 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 1.849  6.094   22.571 1.00 39.47 ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 2.355  5.924   21.215 1.00 39.33 ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.890  6.092   21.201 1.00 39.39 ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 4.474  6.658   22.133 1.00 39.89 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.720  6.970   20.282 1.00 39.25 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 0.203  7.074   20.320 1.00 41.08 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.263 8.336   19.653 1.00 41.85 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.464 5.842   19.695 1.00 41.61 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 4.541  5.580   20.164 1.00 38.38 ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 5.985  5.694   20.008 1.00 37.90 ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 6.249  5.962   18.516 1.00 37.82 ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 5.626  5.337   17.653 1.00 37.92 ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 6.728  4.439   20.569 1.00 37.74 ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 6.131  3.149   20.016 1.00 38.40 ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 8.233  4.499   20.325 1.00 37.07 ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 7.093  6.944   18.230 1.00 37.30 ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 7.427  7.316   16.862 1.00 37.41 ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.855  6.980   16.479 1.00 37.04 ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 9.763  7.094   17.300 1.00 36.54 ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 9.057  6.558   15.219 1.00 36.90 ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 10.373 6.165   14.682 1.00 36.45 ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.727 6.985   13.448 1.00 36.94 ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.889  7.208   12.568 1.00 36.27 ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 10.404 4.674   14.295 1.00 35.32 ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.721  3.738   15.262 1.00 34.95 ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 10.421 3.164   16.306 1.00 35.05 ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 8.381  3.426   15.120 1.00 35.17 ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 9.796  2.294   17.188 1.00 35.36 ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.755  2.575   16.018 1.00 35.46 ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 8.468  2.013   17.045 1.00 34.98 ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.976 7.433   13.391 1.00 37.74 ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 12.481 8.198   12.262 1.00 38.79 ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.905 7.201   11.227 1.00 39.91 ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.792 6.410   11.506 1.00 39.88 ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.684 9.015   12.689 1.00 38.86 ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 12.285 7.222   10.042 1.00 40.70 ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.611 6.280   8.977  1.00 41.94 ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.944 6.608   8.328  1.00 43.04 ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 14.270 7.787   8.154  1.00 44.15 ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.518 6.300   7.899  1.00 43.73 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.699 5.245   6.823  1.00 49.20 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.457 4.051   7.110  1.00 49.94 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 12.085 5.610   5.697  1.00 52.20 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.715 5.579   7.948  1.00 42.13 ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.986 5.792   7.254  1.00 41.36 ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 16.051 5.047   5.907  1.00 41.20 ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 16.979 5.281   5.149  1.00 41.37 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 17.214 5.483   8.146  1.00 41.49 ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 17.232 6.365   9.393  1.00 41.72 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 17.273 4.003   8.521  1.00 41.78 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 15.063 4.179   5.601  1.00 41.02 ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 14.939 3.381   4.367  1.00 41.32 ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 15.017 4.169   3.062  1.00 42.75 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.406 3.593   2.046  1.00 43.15 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.647 2.545   4.378  1.00 40.60 ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.594 1.529   5.506  1.00 40.11 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 12.337 0.692   5.468  1.00 39.51 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 11.157 1.471   5.835  1.00 38.46 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 9.949  0.952   6.030  1.00 37.60 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.749  -0.355  5.896  1.00 36.30 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 8.929  1.737   6.355  1.00 35.92 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.630 5.453   3.062  1.00 43.46 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 14.716 6.263   1.840  1.00 44.88 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 16.165 6.735   1.541  1.00 46.28 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 16.481 7.091   0.398  1.00 46.94 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 13.767 7.469   1.900  1.00 46.36 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 14.135 8.470   2.969  1.00 51.10 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 14.400 8.047   4.108  1.00 51.18 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 14.151 9.676   2.666  1.00 54.39 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 17.038 6.734   2.556  1.00 46.29 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.419 7.187   2.389  1.00 46.82 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 19.276 6.108   1.724  1.00 47.47 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 19.979 5.363   2.407  1.00 47.46 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 19.010 7.651   3.738  1.00 46.24 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 18.098 8.591   4.539  1.00 46.92 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.531 8.691   5.972  1.00 47.64 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.981 9.949   3.882  1.00 47.12 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 19.173 6.013   0.386  1.00 47.69 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 19.886 5.044   -0.446 1.00 48.74 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 21.401 5.260   -0.464 1.00 49.87 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 22.164 4.290   -0.535 1.00 49.90 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 19.343 5.077   -1.886 1.00 48.86 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 17.860 4.767   -2.061 1.00 49.99 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.480 4.755   -3.512 1.00 50.24 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 17.516 3.423   -1.481 1.00 51.02 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 21.833 6.526   -0.353 1.00 50.38 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 23.242 6.896   -0.349 1.00 51.48 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 24.074 6.315   0.799  1.00 52.64 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 25.306 6.401   0.759  1.00 52.68 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 23.397 8.420   -0.378 1.00 51.47 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 22.676 9.176   0.705  1.00 51.81 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 21.424 9.716   0.631  1.00 52.38 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 23.222 9.595   1.968  1.00 51.69 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 21.151 10.433  1.774  1.00 52.56 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 22.235 10.365  2.616  1.00 52.27 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 24.446 9.394   2.612  1.00 52.27 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 22.433 10.919  3.878  1.00 52.75 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.636 9.940   3.866  1.00 53.00 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.637 10.689  4.486  1.00 52.91 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 23.418 5.735   1.812  1.00 53.45 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 24.111 5.171   2.964  1.00 54.77 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.964 3.954   2.626  1.00 56.34 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.993 3.742   3.263  1.00 56.01 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 23.105 4.813   4.050  1.00 54.76 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 22.387 5.985   4.683  1.00 56.15 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 21.320 5.500   5.648  1.00 56.79 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 23.358 6.902   5.400  1.00 56.76 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 24.548 3.169   1.610  1.00 57.81 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 25.255 1.956   1.178  1.00 59.51 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 26.236 2.158   0.009  1.00 60.74 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 26.518 1.184   -0.691 1.00 61.09 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 24.254 0.851   0.793  1.00 61.75 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 23.219 0.511   1.837  1.00 66.58 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 23.587 0.399   3.023  1.00 66.73 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 22.046 0.323   1.461  1.00 69.46 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 26.770 3.384   -0.212 1.00 61.38 ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 27.715 3.597   -1.322 1.00 62.68 ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 28.772 4.674   -1.035 1.00 63.24 ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 29.923 4.558   -1.479 1.00 63.18 ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 26.992 3.871   -2.658 1.00 65.76 ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 25.755 4.751   -2.547 1.00 73.17 ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 24.725 4.559   -3.648 1.00 82.63 ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 24.012 5.537   -3.975 1.00 84.35 ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 24.631 3.431   -4.187 1.00 85.97 ? 145 GLU   A OE2 1 
HETATM 1078 N  N1  . A1BOY B 2 .   ? 10.612 13.995  22.549 1.00 49.79 ? 201 A1BOY A N1  1 
HETATM 1079 C  C4  . A1BOY B 2 .   ? 11.060 10.434  23.233 1.00 47.15 ? 201 A1BOY A C4  1 
HETATM 1080 C  C5  . A1BOY B 2 .   ? 10.096 10.952  24.087 1.00 47.64 ? 201 A1BOY A C5  1 
HETATM 1081 C  C6  . A1BOY B 2 .   ? 10.076 12.437  24.362 1.00 48.53 ? 201 A1BOY A C6  1 
HETATM 1082 C  C7  . A1BOY B 2 .   ? 9.679  13.194  23.110 1.00 49.24 ? 201 A1BOY A C7  1 
HETATM 1083 C  C8  . A1BOY B 2 .   ? 11.806 14.501  23.250 1.00 49.78 ? 201 A1BOY A C8  1 
HETATM 1084 C  C10 . A1BOY B 2 .   ? 12.874 14.884  20.987 1.00 49.94 ? 201 A1BOY A C10 1 
HETATM 1085 C  C13 . A1BOY B 2 .   ? 10.416 14.504  21.187 1.00 50.02 ? 201 A1BOY A C13 1 
HETATM 1086 O  O2  . A1BOY B 2 .   ? 10.883 15.820  18.670 1.00 50.44 ? 201 A1BOY A O2  1 
HETATM 1087 C  C12 . A1BOY B 2 .   ? 11.465 14.755  18.893 1.00 50.09 ? 201 A1BOY A C12 1 
HETATM 1088 N  N2  . A1BOY B 2 .   ? 11.936 13.978  17.929 1.00 49.76 ? 201 A1BOY A N2  1 
HETATM 1089 C  C11 . A1BOY B 2 .   ? 11.648 14.246  20.313 1.00 50.05 ? 201 A1BOY A C11 1 
HETATM 1090 C  C9  . A1BOY B 2 .   ? 13.074 14.349  22.407 1.00 49.89 ? 201 A1BOY A C9  1 
HETATM 1091 O  O1  . A1BOY B 2 .   ? 8.566  13.050  22.624 1.00 49.25 ? 201 A1BOY A O1  1 
HETATM 1092 C  C1  . A1BOY B 2 .   ? 9.142  10.033  24.564 1.00 47.32 ? 201 A1BOY A C1  1 
HETATM 1093 O  O   . A1BOY B 2 .   ? 8.236  10.550  25.427 1.00 47.29 ? 201 A1BOY A O   1 
HETATM 1094 C  C   . A1BOY B 2 .   ? 7.350  9.644   26.091 1.00 47.13 ? 201 A1BOY A C   1 
HETATM 1095 C  C3  . A1BOY B 2 .   ? 11.044 9.101   22.887 1.00 46.88 ? 201 A1BOY A C3  1 
HETATM 1096 C  C2  . A1BOY B 2 .   ? 10.059 8.309   23.401 1.00 46.83 ? 201 A1BOY A C2  1 
HETATM 1097 N  N   . A1BOY B 2 .   ? 9.107  8.752   24.231 1.00 46.99 ? 201 A1BOY A N   1 
HETATM 1098 ZN ZN  . ZN    C 3 .   ? 11.229 -4.997  5.580  1.00 64.98 2 202 ZN    A ZN  1 
HETATM 1099 O  O   . HOH   D 4 .   ? 4.687  6.086   24.339 1.00 15.50 ? 301 HOH   A O   1 
HETATM 1100 O  O   . HOH   D 4 .   ? 0.717  -0.066  16.443 1.00 29.06 ? 302 HOH   A O   1 
HETATM 1101 O  O   . HOH   D 4 .   ? 3.459  7.961   10.061 1.00 34.11 ? 303 HOH   A O   1 
HETATM 1102 O  O   . HOH   D 4 .   ? 24.010 0.150   16.102 1.00 27.42 ? 304 HOH   A O   1 
HETATM 1103 O  O   . HOH   D 4 .   ? 13.339 9.851   9.231  1.00 35.91 ? 305 HOH   A O   1 
HETATM 1104 O  O   . HOH   D 4 .   ? 5.908  1.610   6.866  1.00 36.44 ? 306 HOH   A O   1 
HETATM 1105 O  O   . HOH   D 4 .   ? 11.017 7.654   4.592  1.00 36.79 ? 307 HOH   A O   1 
HETATM 1106 O  O   . HOH   D 4 .   ? 12.348 11.396  10.840 1.00 28.23 ? 308 HOH   A O   1 
HETATM 1107 O  O   . HOH   D 4 .   ? 20.341 8.565   18.965 1.00 17.21 ? 309 HOH   A O   1 
HETATM 1108 O  O   . HOH   D 4 .   ? 30.596 10.919  18.769 1.00 22.17 ? 310 HOH   A O   1 
HETATM 1109 O  O   . HOH   D 4 .   ? 16.034 -8.570  10.967 1.00 20.43 ? 311 HOH   A O   1 
HETATM 1110 O  O   . HOH   D 4 .   ? 15.164 2.312   23.035 1.00 18.79 ? 312 HOH   A O   1 
HETATM 1111 O  O   . HOH   D 4 .   ? 0.320  1.917   24.402 1.00 35.96 ? 313 HOH   A O   1 
HETATM 1112 O  O   . HOH   D 4 .   ? 7.177  3.106   33.037 1.00 38.38 ? 314 HOH   A O   1 
HETATM 1113 O  O   . HOH   D 4 .   ? 20.157 -1.148  27.388 1.00 29.86 ? 315 HOH   A O   1 
HETATM 1114 O  O   . HOH   D 4 .   ? 16.016 11.651  23.942 1.00 31.10 ? 316 HOH   A O   1 
HETATM 1115 O  O   . HOH   D 4 .   ? 18.139 -0.212  30.251 1.00 24.13 ? 317 HOH   A O   1 
HETATM 1116 O  O   . HOH   D 4 .   ? 4.864  -5.614  6.904  1.00 24.80 ? 318 HOH   A O   1 
HETATM 1117 O  O   . HOH   D 4 .   ? 10.527 5.204   3.325  1.00 27.31 ? 319 HOH   A O   1 
HETATM 1118 O  O   . HOH   D 4 .   ? 20.557 23.262  16.007 1.00 44.33 ? 320 HOH   A O   1 
HETATM 1119 O  O   . HOH   D 4 .   ? 18.345 21.085  9.382  1.00 47.00 ? 321 HOH   A O   1 
HETATM 1120 O  O   . HOH   D 4 .   ? 10.575 3.472   33.803 1.00 34.57 ? 322 HOH   A O   1 
HETATM 1121 O  O   . HOH   D 4 .   ? -0.932 1.281   4.721  1.00 28.40 ? 323 HOH   A O   1 
HETATM 1122 O  O   . HOH   D 4 .   ? 22.695 18.749  6.003  1.00 46.13 ? 324 HOH   A O   1 
HETATM 1123 O  O   . HOH   D 4 .   ? 26.514 18.823  4.909  1.00 37.32 ? 325 HOH   A O   1 
HETATM 1124 O  O   . HOH   D 4 .   ? 3.203  3.372   28.446 1.00 34.59 ? 326 HOH   A O   1 
HETATM 1125 O  O   . HOH   D 4 .   ? 17.888 2.133   23.174 1.00 21.77 ? 327 HOH   A O   1 
HETATM 1126 O  O   . HOH   D 4 .   ? 9.614  2.655   2.998  1.00 33.67 ? 328 HOH   A O   1 
HETATM 1127 O  O   . HOH   D 4 .   ? 2.968  -2.956  3.555  1.00 24.13 ? 329 HOH   A O   1 
HETATM 1128 O  O   . HOH   D 4 .   ? 7.799  16.526  22.873 1.00 21.74 ? 330 HOH   A O   1 
HETATM 1129 O  O   . HOH   D 4 .   ? 8.980  20.592  8.858  1.00 44.96 ? 331 HOH   A O   1 
HETATM 1130 O  O   . HOH   D 4 .   ? 5.269  -1.555  23.720 1.00 22.45 ? 332 HOH   A O   1 
HETATM 1131 O  O   . HOH   D 4 .   ? 4.116  -4.269  21.561 1.00 16.27 ? 333 HOH   A O   1 
HETATM 1132 O  O   . HOH   D 4 .   ? 7.443  10.600  3.969  1.00 28.58 ? 334 HOH   A O   1 
HETATM 1133 O  O   . HOH   D 4 .   ? -0.583 16.178  10.091 1.00 31.20 ? 335 HOH   A O   1 
HETATM 1134 O  O   . HOH   D 4 .   ? 23.765 1.809   19.712 1.00 37.78 ? 336 HOH   A O   1 
HETATM 1135 O  O   . HOH   D 4 .   ? 32.831 1.812   2.655  1.00 33.61 ? 337 HOH   A O   1 
HETATM 1136 O  O   . HOH   D 4 .   ? 24.348 6.938   21.015 1.00 29.02 ? 338 HOH   A O   1 
HETATM 1137 O  O   . HOH   D 4 .   ? 30.997 11.116  21.608 1.00 37.71 ? 339 HOH   A O   1 
HETATM 1138 O  O   . HOH   D 4 .   ? 7.102  -5.096  2.591  1.00 23.20 ? 340 HOH   A O   1 
HETATM 1139 O  O   . HOH   D 4 .   ? 1.663  -2.330  18.051 1.00 32.37 ? 341 HOH   A O   1 
HETATM 1140 O  O   . HOH   D 4 .   ? 19.261 -0.505  19.517 1.00 24.24 ? 342 HOH   A O   1 
HETATM 1141 O  O   . HOH   D 4 .   ? 4.098  11.048  18.937 1.00 31.25 ? 343 HOH   A O   1 
HETATM 1142 O  O   . HOH   D 4 .   ? 7.871  -5.941  31.965 1.00 25.15 ? 344 HOH   A O   1 
HETATM 1143 O  O   . HOH   D 4 .   ? 2.254  2.150   26.157 1.00 48.94 ? 345 HOH   A O   1 
HETATM 1144 O  O   . HOH   D 4 .   ? 17.634 10.871  26.181 1.00 44.18 ? 346 HOH   A O   1 
HETATM 1145 O  O   . HOH   D 4 .   ? 34.427 11.932  20.193 1.00 42.95 ? 347 HOH   A O   1 
HETATM 1146 O  O   . HOH   D 4 .   ? 17.978 19.524  18.175 1.00 27.43 ? 348 HOH   A O   1 
HETATM 1147 O  O   . HOH   D 4 .   ? -1.955 -4.330  15.633 0.50 10.81 ? 349 HOH   A O   1 
HETATM 1148 O  O   . HOH   D 4 .   ? 17.879 10.590  0.220  1.00 33.94 ? 350 HOH   A O   1 
HETATM 1149 O  O   . HOH   D 4 .   ? 31.798 6.496   2.687  1.00 34.50 ? 351 HOH   A O   1 
HETATM 1150 O  O   . HOH   D 4 .   ? 21.291 20.347  17.695 1.00 27.48 ? 352 HOH   A O   1 
HETATM 1151 O  O   . HOH   D 4 .   ? 30.619 15.152  23.670 1.00 50.85 ? 353 HOH   A O   1 
HETATM 1152 O  O   . HOH   D 4 .   ? 24.309 15.702  23.593 1.00 29.67 ? 354 HOH   A O   1 
HETATM 1153 O  O   . HOH   D 4 .   ? -0.109 -6.083  12.047 1.00 27.20 ? 355 HOH   A O   1 
HETATM 1154 O  O   . HOH   D 4 .   ? 7.332  -9.188  5.658  1.00 35.02 ? 356 HOH   A O   1 
HETATM 1155 O  O   . HOH   D 4 .   ? 0.971  -2.123  23.530 1.00 16.20 ? 357 HOH   A O   1 
HETATM 1156 O  O   . HOH   D 4 .   ? 20.588 -3.715  22.893 1.00 29.68 ? 358 HOH   A O   1 
HETATM 1157 O  O   . HOH   D 4 .   ? 11.952 20.117  4.089  1.00 39.77 ? 359 HOH   A O   1 
HETATM 1158 O  O   . HOH   D 4 .   ? 25.183 12.584  1.086  1.00 40.13 ? 360 HOH   A O   1 
HETATM 1159 O  O   . HOH   D 4 .   ? 2.827  -5.340  26.282 1.00 25.84 ? 361 HOH   A O   1 
HETATM 1160 O  O   . HOH   D 4 .   ? 8.010  22.491  28.802 1.00 33.56 ? 362 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   ? 0.3689 0.8344 0.4102 0.0503  -0.1396 -0.0720 7   SER   A N   
2    C CA  . SER   A 1   ? 0.3718 0.8205 0.4389 0.0492  -0.1471 -0.0648 7   SER   A CA  
3    C C   . SER   A 1   ? 0.3780 0.8072 0.4446 0.0488  -0.1351 -0.0423 7   SER   A C   
4    O O   . SER   A 1   ? 0.3856 0.8083 0.4379 0.0486  -0.1220 -0.0361 7   SER   A O   
5    C CB  . SER   A 1   ? 0.3841 0.8481 0.4577 0.0500  -0.1619 -0.0652 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.4130 0.8998 0.4622 0.0518  -0.1622 -0.0543 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.3707 0.7925 0.4555 0.0472  -0.1387 -0.0334 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.3754 0.7840 0.4614 0.0452  -0.1256 -0.0195 8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.3656 0.7705 0.4709 0.0377  -0.1278 -0.0179 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.3601 0.7680 0.4815 0.0330  -0.1386 -0.0242 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.3558 0.7573 0.4636 0.0355  -0.1164 -0.0089 9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.3434 0.7509 0.4652 0.0258  -0.1159 -0.0051 9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.3465 0.7509 0.4610 0.0205  -0.0956 -0.0050 9   ALA   A C   
14   O O   . ALA   A 3   ? 0.3558 0.7493 0.4642 0.0270  -0.0830 -0.0061 9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.3278 0.7464 0.4712 0.0284  -0.1275 0.0019  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.3343 0.7517 0.4526 0.0073  -0.0923 -0.0039 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.3348 0.7571 0.4475 -0.0009 -0.0723 -0.0102 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.3254 0.7663 0.4558 -0.0023 -0.0714 -0.0044 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.3141 0.7712 0.4569 -0.0070 -0.0870 0.0069  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.3400 0.7746 0.4389 -0.0195 -0.0691 -0.0136 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.3563 0.7775 0.4447 -0.0193 -0.0757 -0.0145 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.3454 0.7863 0.4351 -0.0294 -0.0461 -0.0285 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.3614 0.8024 0.4484 -0.0381 -0.0835 -0.0075 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.3272 0.7670 0.4655 0.0019  -0.0529 -0.0115 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.3179 0.7781 0.4759 0.0011  -0.0486 -0.0072 11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.3246 0.8029 0.4775 -0.0126 -0.0250 -0.0235 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.3340 0.7991 0.4944 -0.0076 -0.0043 -0.0395 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.3090 0.7570 0.4907 0.0191  -0.0469 -0.0014 11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.3135 0.7509 0.4956 0.0299  -0.0699 0.0113  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.3100 0.7605 0.5050 0.0302  -0.0898 0.0228  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.3353 0.7537 0.5060 0.0379  -0.0714 0.0105  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.3186 0.7631 0.5133 0.0376  -0.1102 0.0277  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.3477 0.7647 0.5144 0.0450  -0.0910 0.0182  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.3451 0.7750 0.5230 0.0445  -0.1100 0.0239  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.3668 0.7984 0.5400 0.0492  -0.1284 0.0247  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.3172 0.8289 0.4606 -0.0314 -0.0279 -0.0198 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.3198 0.8607 0.4524 -0.0493 -0.0057 -0.0378 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.3100 0.8935 0.4553 -0.0584 -0.0039 -0.0279 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.3065 0.9120 0.4550 -0.0665 -0.0248 -0.0031 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.3408 0.8936 0.4435 -0.0697 -0.0064 -0.0442 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.3489 0.9011 0.4483 -0.0730 -0.0349 -0.0188 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.3360 0.9380 0.4237 -0.0951 0.0096  -0.0568 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.3002 0.8949 0.4594 -0.0562 0.0212  -0.0464 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.2861 0.9235 0.4600 -0.0634 0.0275  -0.0395 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.2839 0.9158 0.4851 -0.0496 0.0052  -0.0096 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.2928 0.8896 0.5143 -0.0283 0.0008  -0.0070 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.2674 0.9371 0.4723 -0.0630 -0.0105 0.0151  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.2606 0.9258 0.4958 -0.0522 -0.0342 0.0429  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.2753 0.9234 0.5087 -0.0537 -0.0656 0.0623  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2661 0.9284 0.5243 -0.0571 -0.0877 0.0879  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.2350 0.9516 0.4901 -0.0638 -0.0312 0.0598  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.2343 0.9612 0.5092 -0.0546 -0.0045 0.0444  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.2459 0.9403 0.5450 -0.0333 -0.0044 0.0422  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.2162 0.9942 0.4851 -0.0717 0.0184  0.0349  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.2912 0.9087 0.5013 -0.0510 -0.0666 0.0490  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.2968 0.8966 0.5087 -0.0508 -0.0920 0.0613  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.2996 0.8517 0.5032 -0.0315 -0.0949 0.0468  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.3114 0.8454 0.5030 -0.0222 -0.0762 0.0292  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.3044 0.9264 0.4971 -0.0721 -0.0933 0.0657  15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.2998 0.9794 0.4962 -0.0958 -0.0921 0.0844  15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.2915 0.9963 0.5234 -0.1014 -0.1124 0.1160  15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.3146 1.0274 0.4801 -0.1155 -0.0725 0.0719  15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.2834 1.0483 0.5201 -0.1254 -0.1127 0.1394  15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.3056 1.0814 0.4700 -0.1407 -0.0718 0.0907  15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2981 1.1014 0.4981 -0.1457 -0.0922 0.1273  15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.2988 1.1718 0.4990 -0.1726 -0.0919 0.1513  15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.2823 0.8183 0.4974 -0.0266 -0.1181 0.0548  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.2825 0.7840 0.4892 -0.0121 -0.1246 0.0433  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.2700 0.7686 0.4766 -0.0202 -0.1374 0.0458  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.2542 0.7687 0.4886 -0.0289 -0.1541 0.0616  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.2897 0.7828 0.5191 0.0009  -0.1409 0.0473  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.3267 0.7970 0.5509 0.0108  -0.1537 0.0366  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.3441 0.8112 0.5807 0.0221  -0.1654 0.0362  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.3531 0.8140 0.6002 0.0241  -0.1853 0.0266  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.3657 0.8161 0.5925 0.0312  -0.1865 0.0118  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.3699 0.8135 0.5675 0.0373  -0.1710 0.0106  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.3401 0.7895 0.5795 0.0314  -0.2024 -0.0026 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.2778 0.7582 0.4601 -0.0179 -0.1294 0.0328  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.2733 0.7520 0.4590 -0.0252 -0.1392 0.0352  17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.2830 0.7361 0.4678 -0.0114 -0.1461 0.0220  17  VAL   A C   
81   O O   . VAL   A 11  ? 0.2995 0.7362 0.4581 -0.0035 -0.1341 0.0096  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.2794 0.7681 0.4398 -0.0395 -0.1248 0.0332  17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.2803 0.7710 0.4502 -0.0480 -0.1362 0.0405  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.2689 0.7923 0.4272 -0.0558 -0.1168 0.0424  17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.2675 0.7204 0.4850 -0.0096 -0.1650 0.0242  18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.2725 0.7085 0.4915 0.0016  -0.1706 0.0065  18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.2610 0.6964 0.5085 -0.0035 -0.1796 0.0058  18  VAL   A C   
88   O O   . VAL   A 12  ? 0.2424 0.6920 0.5172 -0.0160 -0.1868 0.0248  18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.2728 0.7078 0.5094 0.0106  -0.1834 -0.0008 18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2853 0.7218 0.4994 0.0167  -0.1747 0.0025  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.2530 0.6989 0.5410 0.0037  -0.2020 0.0106  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.2669 0.6901 0.5117 0.0057  -0.1793 -0.0146 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.2618 0.6830 0.5431 0.0044  -0.1867 -0.0211 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.2454 0.6706 0.5826 0.0041  -0.2056 -0.0214 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.2541 0.6773 0.5877 0.0112  -0.2102 -0.0362 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.2851 0.6975 0.5466 0.0152  -0.1789 -0.0483 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.3422 0.7502 0.5595 0.0157  -0.1618 -0.0474 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.3637 0.7691 0.5398 0.0202  -0.1515 -0.0481 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.3493 0.7571 0.5812 0.0108  -0.1592 -0.0441 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.2192 0.6524 0.6112 -0.0054 -0.2176 -0.0026 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.2036 0.6407 0.6625 -0.0075 -0.2368 0.0023  20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.2114 0.6360 0.6926 0.0037  -0.2420 -0.0351 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.2036 0.6293 0.7022 0.0053  -0.2528 -0.0412 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.1912 0.6394 0.7149 -0.0191 -0.2485 0.0300  20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.1905 0.6431 0.7968 -0.0224 -0.2697 0.0405  20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.2003 0.6698 0.8745 -0.0358 -0.2823 0.0785  20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.2055 0.6836 0.9623 -0.0416 -0.3036 0.0990  20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.2141 0.6783 1.0566 -0.0363 -0.3159 0.0840  20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.2261 0.6696 1.0794 -0.0249 -0.3074 0.0453  20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.1776 0.6499 1.0998 -0.0429 -0.3359 0.1064  20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.2185 0.6348 0.6952 0.0105  -0.2332 -0.0621 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.2220 0.6335 0.7158 0.0190  -0.2351 -0.1040 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.2409 0.6570 0.6796 0.0242  -0.2329 -0.1215 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.2360 0.6551 0.6956 0.0266  -0.2409 -0.1515 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.2338 0.6422 0.7302 0.0243  -0.2226 -0.1289 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.2855 0.6963 0.7040 0.0282  -0.2039 -0.1321 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.3159 0.7254 0.7071 0.0235  -0.1955 -0.1032 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.3124 0.7303 0.6829 0.0349  -0.1932 -0.1605 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.3420 0.7530 0.6735 0.0286  -0.1801 -0.1141 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.3413 0.7593 0.6583 0.0354  -0.1784 -0.1455 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.2587 0.6777 0.6348 0.0245  -0.2234 -0.1020 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.2787 0.7048 0.6083 0.0289  -0.2220 -0.1092 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.2914 0.7213 0.6287 0.0255  -0.2317 -0.0851 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.3030 0.7397 0.6063 0.0289  -0.2307 -0.0841 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.2946 0.7217 0.5596 0.0328  -0.2039 -0.1031 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.3048 0.7332 0.5510 0.0363  -0.1918 -0.1232 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.3218 0.7508 0.5116 0.0389  -0.1758 -0.1091 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.3017 0.7443 0.5519 0.0392  -0.1963 -0.1602 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.2843 0.7139 0.6672 0.0182  -0.2407 -0.0621 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.2946 0.7326 0.6858 0.0141  -0.2479 -0.0378 23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.2941 0.7365 0.7091 0.0160  -0.2638 -0.0520 23  ALA   A C   
132  O O   . ALA   A 17  ? 0.2859 0.7254 0.7518 0.0143  -0.2775 -0.0698 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.2820 0.7275 0.7166 0.0032  -0.2544 -0.0069 23  ALA   A CB  
134  N N   . THR   A 18  ? 0.3014 0.7513 0.6850 0.0190  -0.2623 -0.0444 24  THR   A N   
135  C CA  . THR   A 18  ? 0.3014 0.7598 0.7020 0.0193  -0.2781 -0.0547 24  THR   A CA  
136  C C   . THR   A 18  ? 0.2865 0.7491 0.7517 0.0119  -0.2959 -0.0374 24  THR   A C   
137  O O   . THR   A 18  ? 0.2832 0.7457 0.7792 0.0059  -0.2958 -0.0149 24  THR   A O   
138  C CB  . THR   A 18  ? 0.3210 0.7890 0.6733 0.0246  -0.2709 -0.0455 24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.3266 0.7990 0.6843 0.0231  -0.2657 -0.0137 24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.3435 0.8094 0.6402 0.0307  -0.2538 -0.0537 24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.2722 0.7425 0.7600 0.0106  -0.3122 -0.0463 25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.2580 0.7341 0.8087 0.0035  -0.3302 -0.0288 25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.2521 0.7407 0.7950 0.0012  -0.3228 0.0127  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.2335 0.7301 0.8243 -0.0068 -0.3303 0.0389  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.2732 0.7566 0.8402 0.0022  -0.3482 -0.0504 25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.3108 0.7863 0.9246 -0.0013 -0.3617 -0.0897 25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.3210 0.8012 0.9882 -0.0077 -0.3835 -0.1044 25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.3330 0.7967 0.9540 0.0006  -0.3550 -0.1180 25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.3192 0.7898 1.0246 -0.0096 -0.3884 -0.1449 25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.3299 0.7909 1.0102 -0.0041 -0.3711 -0.1539 25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.2650 0.7586 0.7522 0.0076  -0.3075 0.0191  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.2686 0.7758 0.7481 0.0061  -0.2960 0.0511  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.2612 0.7698 0.7301 0.0009  -0.2807 0.0659  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.2549 0.7822 0.7362 -0.0061 -0.2758 0.0925  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.3187 0.8300 0.7558 0.0147  -0.2836 0.0525  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.3794 0.9094 0.8369 0.0130  -0.2820 0.0794  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.3821 0.9216 0.8659 0.0128  -0.2977 0.0835  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.3989 0.9382 0.8469 0.0101  -0.2630 0.0970  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.2591 0.7528 0.7055 0.0027  -0.2733 0.0493  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.2517 0.7488 0.6905 -0.0044 -0.2620 0.0624  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.2256 0.7357 0.7279 -0.0166 -0.2790 0.0846  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.2099 0.7430 0.7185 -0.0277 -0.2746 0.1134  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.2713 0.7496 0.6822 0.0005  -0.2542 0.0391  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.3180 0.7885 0.6683 0.0089  -0.2344 0.0283  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.3353 0.8145 0.6655 0.0090  -0.2215 0.0416  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.3316 0.7891 0.6594 0.0153  -0.2310 0.0066  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.2162 0.7158 0.7701 -0.0159 -0.2988 0.0716  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.1993 0.7091 0.8293 -0.0268 -0.3176 0.0942  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.1903 0.7244 0.8517 -0.0344 -0.3268 0.1256  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.1766 0.7335 0.8809 -0.0473 -0.3343 0.1613  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.1878 0.6771 0.8722 -0.0232 -0.3339 0.0655  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.2024 0.6778 0.8835 -0.0209 -0.3264 0.0499  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.2355 0.6940 0.8702 -0.0107 -0.3142 0.0124  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.1868 0.6702 0.9083 -0.0301 -0.3290 0.0768  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.2345 0.6867 0.8824 -0.0118 -0.3089 0.0111  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.2079 0.6746 0.9106 -0.0237 -0.3186 0.0508  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.1710 0.6787 0.9476 -0.0445 -0.3407 0.1232  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.2023 0.6732 0.9405 -0.0303 -0.3196 0.0694  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.1683 0.6830 0.9795 -0.0524 -0.3430 0.1438  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.1790 0.6741 0.9717 -0.0449 -0.3326 0.1168  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.1950 0.7293 0.8348 -0.0276 -0.3259 0.1166  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.1877 0.7470 0.8551 -0.0339 -0.3323 0.1461  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2008 0.7897 0.8351 -0.0411 -0.3128 0.1752  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.1908 0.8094 0.8541 -0.0498 -0.3166 0.2054  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.1933 0.7467 0.8458 -0.0246 -0.3356 0.1290  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.2200 0.8034 0.7938 -0.0377 -0.2907 0.1632  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.2244 0.8355 0.7615 -0.0451 -0.2688 0.1799  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.2353 0.8519 0.7534 -0.0548 -0.2611 0.1840  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.2557 0.8810 0.7235 -0.0570 -0.2387 0.1781  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.2499 0.8506 0.7345 -0.0323 -0.2471 0.1593  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2607 0.8687 0.7656 -0.0263 -0.2521 0.1650  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2647 0.9042 0.7827 -0.0331 -0.2453 0.1866  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2619 0.8456 0.7700 -0.0148 -0.2642 0.1462  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.2154 0.8282 0.7801 -0.0613 -0.2802 0.1942  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.2170 0.8371 0.7773 -0.0715 -0.2782 0.2034  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.2119 0.8801 0.7509 -0.0904 -0.2663 0.2330  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.1910 0.8942 0.7537 -0.1001 -0.2702 0.2600  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.1962 0.8110 0.8338 -0.0764 -0.3036 0.2181  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.2125 0.8342 0.8604 -0.0864 -0.3053 0.2312  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.2536 0.8444 0.8419 -0.0749 -0.2880 0.1941  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.1887 0.8042 0.9291 -0.0896 -0.3304 0.2466  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.2273 0.8994 0.7170 -0.0958 -0.2498 0.2242  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2224 0.9434 0.6826 -0.1165 -0.2366 0.2441  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2194 0.9563 0.6981 -0.1320 -0.2482 0.2659  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.1989 0.9866 0.7060 -0.1541 -0.2587 0.3070  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2528 0.9675 0.6413 -0.1113 -0.2060 0.2113  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2501 1.0177 0.6066 -0.1356 -0.1917 0.2240  32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2631 0.9675 0.6443 -0.0966 -0.1948 0.1959  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.2361 0.9328 0.7038 -0.1210 -0.2477 0.2418  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.2313 0.9356 0.7183 -0.1322 -0.2576 0.2581  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.2471 0.8972 0.7453 -0.1120 -0.2608 0.2273  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.2664 0.8798 0.7273 -0.0933 -0.2482 0.1900  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2405 0.9754 0.6665 -0.1491 -0.2396 0.2573  33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2392 0.9821 0.6779 -0.1608 -0.2484 0.2723  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2209 1.0099 0.7057 -0.1836 -0.2675 0.3198  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2594 0.9665 0.6684 -0.1511 -0.2391 0.2435  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2241 1.0072 0.7112 -0.1881 -0.2710 0.3217  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2503 0.9828 0.6900 -0.1682 -0.2531 0.2741  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2928 0.9522 0.6561 -0.1304 -0.2212 0.1989  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2674 0.9776 0.6918 -0.1647 -0.2484 0.2585  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.3151 0.9537 0.6629 -0.1274 -0.2167 0.1847  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2998 0.9630 0.6767 -0.1441 -0.2296 0.2128  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.2328 0.8821 0.7867 -0.1167 -0.2777 0.2448  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.2512 0.8561 0.8216 -0.0995 -0.2792 0.2150  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.2325 0.8490 0.8484 -0.1102 -0.2901 0.2385  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.2049 0.8608 0.8704 -0.1293 -0.3061 0.2844  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.2791 0.8533 0.8990 -0.0827 -0.2910 0.1951  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.3068 0.9006 1.0154 -0.0921 -0.3150 0.2303  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.3705 0.9570 1.1690 -0.0934 -0.3327 0.2421  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.3631 0.9783 1.2377 -0.1079 -0.3523 0.2872  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.4031 0.9579 1.2010 -0.0804 -0.3264 0.2082  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.2432 0.8299 0.8444 -0.0990 -0.2817 0.2106  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.2271 0.8220 0.8773 -0.1069 -0.2913 0.2307  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.2212 0.7727 0.8947 -0.0859 -0.2874 0.1915  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.2487 0.7794 0.8613 -0.0759 -0.2695 0.1593  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.2673 0.8896 0.8618 -0.1239 -0.2813 0.2453  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.3271 0.9767 0.9799 -0.1401 -0.2967 0.2846  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.3213 0.9531 1.0550 -0.1310 -0.3091 0.2873  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.3636 1.0544 0.9842 -0.1626 -0.2960 0.3114  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.1835 0.7244 0.9493 -0.0802 -0.3034 0.1936  36  SER   A N   
241  C CA  A SER   A 30  ? 0.1872 0.6926 0.9848 -0.0616 -0.2988 0.1518  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.1866 0.6923 0.9857 -0.0618 -0.2991 0.1524  36  SER   A CA  
243  C C   . SER   A 30  ? 0.1896 0.6919 0.9690 -0.0609 -0.2875 0.1462  36  SER   A C   
244  O O   . SER   A 30  ? 0.2090 0.6866 0.9487 -0.0460 -0.2713 0.1039  36  SER   A O   
245  C CB  A SER   A 30  ? 0.1698 0.6704 1.0863 -0.0598 -0.3185 0.1595  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.1683 0.6705 1.0878 -0.0608 -0.3192 0.1625  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.2020 0.6692 1.1428 -0.0411 -0.3120 0.1060  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.1648 0.6988 1.1514 -0.0787 -0.3355 0.2188  36  SER   A OG  
249  N N   . SER   A 31  ? 0.1592 0.6915 0.9648 -0.0788 -0.2962 0.1913  37  SER   A N   
250  C CA  . SER   A 31  ? 0.1602 0.6937 0.9525 -0.0806 -0.2876 0.1913  37  SER   A CA  
251  C C   . SER   A 31  ? 0.1849 0.7178 0.8654 -0.0827 -0.2675 0.1752  37  SER   A C   
252  O O   . SER   A 31  ? 0.1877 0.7219 0.8510 -0.0853 -0.2599 0.1748  37  SER   A O   
253  C CB  . SER   A 31  ? 0.1463 0.7166 1.0097 -0.1009 -0.3062 0.2478  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.1808 0.7933 0.9973 -0.1246 -0.3113 0.2873  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1955 0.7274 0.8080 -0.0822 -0.2594 0.1639  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.2271 0.7543 0.7447 -0.0825 -0.2395 0.1453  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.2554 0.7485 0.7268 -0.0611 -0.2246 0.1006  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.2868 0.7711 0.6897 -0.0582 -0.2075 0.0835  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.2426 0.8034 0.7177 -0.1022 -0.2392 0.1702  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.2733 0.8744 0.7544 -0.1274 -0.2464 0.2073  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.3073 0.9497 0.7431 -0.1493 -0.2440 0.2263  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.3742 1.0030 0.7273 -0.1463 -0.2205 0.1924  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.4073 1.0696 0.7106 -0.1666 -0.2114 0.1964  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.3768 1.0951 0.6959 -0.1934 -0.2243 0.2348  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.4350 1.0787 0.6760 -0.1613 -0.1892 0.1618  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.2351 0.7125 0.7470 -0.0479 -0.2319 0.0834  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.2502 0.7047 0.7237 -0.0310 -0.2222 0.0462  39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.2638 0.7240 0.6747 -0.0342 -0.2141 0.0505  39  ASP   A C   
269  O O   . ASP   A 33  ? 0.2897 0.7355 0.6479 -0.0238 -0.2004 0.0273  39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.2789 0.7153 0.7229 -0.0184 -0.2068 0.0140  39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.3268 0.7483 0.7439 -0.0029 -0.2003 -0.0225 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.3254 0.7454 0.7747 0.0005  -0.2116 -0.0305 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.3573 0.7719 0.7225 0.0043  -0.1850 -0.0409 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.2419 0.7267 0.6634 -0.0489 -0.2222 0.0814  40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.2526 0.7465 0.6231 -0.0523 -0.2125 0.0837  40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.2415 0.7459 0.6418 -0.0531 -0.2243 0.0955  40  LEU   A C   
277  O O   . LEU   A 34  ? 0.2204 0.7386 0.6834 -0.0604 -0.2424 0.1181  40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.2494 0.7721 0.5913 -0.0722 -0.2059 0.1058  40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.2831 0.7972 0.5772 -0.0736 -0.1895 0.0918  40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.2845 0.8332 0.5503 -0.0967 -0.1838 0.1096  40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.3159 0.8003 0.5628 -0.0562 -0.1721 0.0600  40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.2507 0.7509 0.6117 -0.0465 -0.2143 0.0840  41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.2453 0.7586 0.6298 -0.0480 -0.2235 0.0968  41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.2644 0.7878 0.5996 -0.0489 -0.2064 0.0950  41  LEU   A C   
285  O O   . LEU   A 35  ? 0.2886 0.7922 0.5814 -0.0374 -0.1912 0.0722  41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.2389 0.7313 0.6571 -0.0337 -0.2360 0.0782  41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.2278 0.7341 0.6816 -0.0364 -0.2492 0.0938  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.2112 0.7071 0.7334 -0.0328 -0.2700 0.0879  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.2497 0.7502 0.6630 -0.0265 -0.2392 0.0800  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.2451 0.8019 0.5918 -0.0630 -0.2086 0.1201  42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.2515 0.8223 0.5628 -0.0643 -0.1912 0.1168  42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.2412 0.8202 0.5845 -0.0600 -0.2013 0.1273  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.2189 0.8201 0.6089 -0.0701 -0.2189 0.1537  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.2437 0.8544 0.5312 -0.0859 -0.1793 0.1311  42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.2467 0.8754 0.5085 -0.0871 -0.1597 0.1238  42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.2574 0.8574 0.5102 -0.0898 -0.1685 0.1168  42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.2567 0.8181 0.5812 -0.0452 -0.1919 0.1092  43  SER   A N   
298  C CA  . SER   A 37  ? 0.2544 0.8240 0.6062 -0.0408 -0.1999 0.1181  43  SER   A CA  
299  C C   . SER   A 37  ? 0.2664 0.8534 0.5920 -0.0410 -0.1774 0.1164  43  SER   A C   
300  O O   . SER   A 37  ? 0.2787 0.8609 0.5656 -0.0406 -0.1560 0.1005  43  SER   A O   
301  C CB  . SER   A 37  ? 0.2784 0.8168 0.6397 -0.0237 -0.2112 0.0995  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.3247 0.8441 0.6458 -0.0107 -0.1952 0.0792  43  SER   A OG  
303  N N   . SER   A 38  ? 0.2557 0.8632 0.6076 -0.0418 -0.1813 0.1312  44  SER   A N   
304  C CA  . SER   A 38  ? 0.2683 0.8948 0.6049 -0.0412 -0.1584 0.1281  44  SER   A CA  
305  C C   . SER   A 38  ? 0.2967 0.8955 0.6288 -0.0212 -0.1520 0.1118  44  SER   A C   
306  O O   . SER   A 38  ? 0.3037 0.8814 0.6517 -0.0110 -0.1707 0.1104  44  SER   A O   
307  C CB  . SER   A 38  ? 0.2580 0.9281 0.6267 -0.0538 -0.1631 0.1554  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2736 0.9354 0.6860 -0.0477 -0.1879 0.1689  44  SER   A OG  
309  N N   . THR   A 39  ? 0.3083 0.9103 0.6225 -0.0168 -0.1256 0.0992  45  THR   A N   
310  C CA  . THR   A 39  ? 0.3213 0.9021 0.6389 0.0012  -0.1175 0.0894  45  THR   A CA  
311  C C   . THR   A 39  ? 0.3189 0.9254 0.6594 0.0026  -0.1010 0.0951  45  THR   A C   
312  O O   . THR   A 39  ? 0.3114 0.9512 0.6505 -0.0106 -0.0857 0.0965  45  THR   A O   
313  C CB  . THR   A 39  ? 0.3525 0.9064 0.6400 0.0083  -0.0998 0.0679  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.3718 0.9424 0.6442 -0.0019 -0.0737 0.0555  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.3655 0.8961 0.6316 0.0082  -0.1138 0.0618  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.3262 0.9219 0.6887 0.0176  -0.1032 0.0987  46  THR   A N   
317  C CA  . THR   A 40  ? 0.3253 0.9439 0.7181 0.0214  -0.0872 0.1048  46  THR   A CA  
318  C C   . THR   A 40  ? 0.3428 0.9576 0.7306 0.0263  -0.0525 0.0832  46  THR   A C   
319  O O   . THR   A 40  ? 0.3364 0.9813 0.7317 0.0184  -0.0291 0.0759  46  THR   A O   
320  C CB  . THR   A 40  ? 0.3333 0.9458 0.7585 0.0337  -0.1064 0.1210  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.3351 0.9573 0.7731 0.0258  -0.1353 0.1371  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.3231 0.9563 0.7861 0.0406  -0.0885 0.1281  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.3594 0.9403 0.7381 0.0381  -0.0487 0.0724  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.3661 0.9370 0.7504 0.0436  -0.0172 0.0513  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.3758 0.9455 0.7211 0.0297  -0.0028 0.0278  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.3869 0.9600 0.7021 0.0182  -0.0201 0.0328  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.3768 0.9162 0.7764 0.0609  -0.0217 0.0569  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.3695 0.9361 0.7207 0.0297  0.0284  0.0020  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.3827 0.9526 0.6993 0.0143  0.0438  -0.0235 48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.3990 0.9295 0.6960 0.0191  0.0400  -0.0316 48  GLN   A C   
331  O O   . GLN   A 42  ? 0.4043 0.9090 0.7273 0.0326  0.0522  -0.0384 48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.3909 0.9835 0.7265 0.0087  0.0813  -0.0538 48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.4515 1.0525 0.7537 -0.0096 0.1000  -0.0861 48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.4986 1.1537 0.7697 -0.0350 0.1021  -0.0881 48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.5035 1.1949 0.7868 -0.0389 0.0992  -0.0717 48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.5107 1.1767 0.7430 -0.0544 0.1064  -0.1056 48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.4018 0.9315 0.6588 0.0069  0.0249  -0.0297 49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.4149 0.9137 0.6499 0.0084  0.0209  -0.0363 49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.4097 0.9084 0.6362 -0.0022 0.0478  -0.0673 49  GLY   A C   
340  O O   . GLY   A 43  ? 0.4059 0.9380 0.6232 -0.0189 0.0629  -0.0835 49  GLY   A O   
341  N N   . CYS   A 44  ? 0.4098 0.8752 0.6398 0.0054  0.0540  -0.0762 50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.4122 0.8735 0.6430 -0.0042 0.0801  -0.1090 50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.4234 0.8656 0.6245 -0.0118 0.0738  -0.1140 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.4248 0.8543 0.6357 -0.0162 0.0938  -0.1396 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.4162 0.8574 0.7012 0.0113  0.1027  -0.1209 50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.4719 0.9378 0.8014 0.0202  0.1152  -0.1184 50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.4249 0.8641 0.5964 -0.0129 0.0475  -0.0916 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.4359 0.8592 0.5827 -0.0195 0.0418  -0.0946 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.4242 0.8749 0.5438 -0.0451 0.0506  -0.1149 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.4166 0.9036 0.5232 -0.0584 0.0458  -0.1102 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.4707 0.8870 0.5994 -0.0137 0.0134  -0.0684 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.5413 0.9392 0.6883 0.0074  0.0018  -0.0491 51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.5479 0.9415 0.7253 0.0184  0.0118  -0.0479 51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.5766 0.9684 0.7093 0.0118  -0.0175 -0.0353 51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.4184 0.8565 0.5315 -0.0537 0.0627  -0.1355 52  THR   A N   
356  C CA  . THR   A 46  ? 0.4155 0.8846 0.5010 -0.0810 0.0704  -0.1562 52  THR   A CA  
357  C C   . THR   A 46  ? 0.4237 0.8995 0.4786 -0.0920 0.0472  -0.1361 52  THR   A C   
358  O O   . THR   A 46  ? 0.4382 0.8832 0.4941 -0.0813 0.0379  -0.1255 52  THR   A O   
359  C CB  . THR   A 46  ? 0.4233 0.8807 0.5241 -0.0879 0.0980  -0.1954 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.4144 0.8923 0.5363 -0.0905 0.1218  -0.2214 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.4290 0.9046 0.4978 -0.1147 0.0990  -0.2131 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.4110 0.9307 0.4430 -0.1137 0.0380  -0.1281 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.4088 0.9393 0.4217 -0.1256 0.0157  -0.1061 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.4105 0.9549 0.4022 -0.1492 0.0244  -0.1266 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.4042 0.9782 0.3856 -0.1681 0.0427  -0.1539 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.3942 0.9670 0.4044 -0.1371 -0.0028 -0.0780 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.3970 0.9580 0.4315 -0.1157 -0.0101 -0.0620 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.3943 0.9769 0.3992 -0.1475 -0.0267 -0.0516 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.4162 0.9329 0.4651 -0.0908 -0.0231 -0.0503 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.4154 0.9407 0.4019 -0.1491 0.0124  -0.1163 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.4184 0.9561 0.3869 -0.1721 0.0179  -0.1334 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.4021 0.9982 0.3482 -0.2032 0.0046  -0.1189 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.3942 1.0043 0.3457 -0.2031 -0.0181 -0.0833 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.4290 0.9285 0.4036 -0.1609 0.0102  -0.1247 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.3919 1.0251 0.3169 -0.2311 0.0185  -0.1461 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.3777 1.0763 0.2784 -0.2658 0.0057  -0.1310 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.3784 1.0767 0.2647 -0.2846 0.0069  -0.1474 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.3749 1.0955 0.2437 -0.3061 0.0255  -0.1865 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.3722 1.1274 0.2552 -0.2874 0.0220  -0.1521 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.3770 1.1322 0.2776 -0.2686 0.0246  -0.1400 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.3725 1.1409 0.2874 -0.2635 -0.0048 -0.0864 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.3619 1.1245 0.2974 -0.2442 -0.0023 -0.0773 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.3621 1.1100 0.3237 -0.2272 -0.0241 -0.0398 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.3530 1.0896 0.3267 -0.2257 -0.0483 -0.0098 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.3410 1.0849 0.3215 -0.2114 -0.0213 -0.0343 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.3833 1.0541 0.2808 -0.2754 -0.0110 -0.1217 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.3933 1.0565 0.2834 -0.2895 -0.0113 -0.1336 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.3971 1.0691 0.2957 -0.2937 -0.0384 -0.0906 56  CYS   A C   
389  O O   . CYS   A 50  ? 0.3948 1.0743 0.3100 -0.2839 -0.0562 -0.0540 56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.4130 1.0111 0.3214 -0.2646 0.0063  -0.1604 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.4340 0.9735 0.3715 -0.2232 -0.0056 -0.1279 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.4034 1.0718 0.2979 -0.3070 -0.0410 -0.0961 57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.4068 1.0819 0.3156 -0.3111 -0.0641 -0.0584 57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.4204 1.0346 0.3504 -0.2840 -0.0607 -0.0597 57  ASP   A C   
395  O O   . ASP   A 51  ? 0.4187 1.0360 0.3604 -0.2895 -0.0740 -0.0389 57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.4253 1.1552 0.3125 -0.3527 -0.0714 -0.0600 57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.4887 1.2446 0.3946 -0.3642 -0.0984 -0.0136 57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.5028 1.2621 0.4066 -0.3795 -0.1021 -0.0165 57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.5124 1.2853 0.4415 -0.3578 -0.1161 0.0262  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.4295 0.9939 0.3669 -0.2560 -0.0433 -0.0812 58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.4394 0.9528 0.3945 -0.2322 -0.0375 -0.0831 58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.4189 0.9215 0.3947 -0.2155 -0.0540 -0.0491 58  CYS   A C   
403  O O   . CYS   A 52  ? 0.4201 0.9397 0.4063 -0.2111 -0.0684 -0.0249 58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.4668 0.9393 0.4301 -0.2069 -0.0188 -0.1040 58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.5369 1.0051 0.4955 -0.2219 0.0069  -0.1524 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.3938 0.8709 0.3801 -0.2080 -0.0510 -0.0484 59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.3702 0.8353 0.3782 -0.1905 -0.0611 -0.0235 59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.3486 0.7724 0.3646 -0.1669 -0.0477 -0.0313 59  GLN   A C   
409  O O   . GLN   A 53  ? 0.3415 0.7585 0.3727 -0.1574 -0.0516 -0.0165 59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.3860 0.8785 0.4040 -0.2110 -0.0754 -0.0037 59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.4320 0.9704 0.4555 -0.2306 -0.0944 0.0198  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.5064 1.0678 0.5526 -0.2451 -0.1097 0.0461  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.5295 1.1136 0.5636 -0.2720 -0.1123 0.0436  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.5114 1.0682 0.5950 -0.2280 -0.1196 0.0703  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.3359 0.7365 0.3461 -0.1587 -0.0318 -0.0525 60  THR   A N   
416  C CA  . THR   A 54  ? 0.3352 0.7019 0.3572 -0.1377 -0.0198 -0.0549 60  THR   A CA  
417  C C   . THR   A 54  ? 0.3269 0.6797 0.3486 -0.1222 -0.0111 -0.0649 60  THR   A C   
418  O O   . THR   A 54  ? 0.3200 0.6802 0.3349 -0.1331 -0.0049 -0.0832 60  THR   A O   
419  C CB  . THR   A 54  ? 0.3468 0.6997 0.3773 -0.1498 -0.0088 -0.0683 60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.3584 0.7192 0.3813 -0.1701 -0.0008 -0.0958 60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.3396 0.7028 0.3753 -0.1615 -0.0170 -0.0545 60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.3243 0.6616 0.3536 -0.0982 -0.0106 -0.0529 61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.3213 0.6477 0.3540 -0.0825 -0.0048 -0.0572 61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.3187 0.6307 0.3615 -0.0603 -0.0027 -0.0425 61  GLY   A C   
425  O O   . GLY   A 55  ? 0.3143 0.6255 0.3601 -0.0567 -0.0038 -0.0304 61  GLY   A O   
426  N N   . VAL   A 56  ? 0.3169 0.6221 0.3656 -0.0465 0.0004  -0.0418 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.3163 0.6163 0.3730 -0.0279 0.0007  -0.0248 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.3137 0.6251 0.3604 -0.0166 -0.0094 -0.0214 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.3221 0.6333 0.3708 -0.0176 -0.0089 -0.0301 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.3249 0.6068 0.4096 -0.0232 0.0137  -0.0236 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.3311 0.6165 0.4252 -0.0057 0.0112  0.0002  62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.3272 0.5959 0.4298 -0.0348 0.0234  -0.0282 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.3026 0.6262 0.3404 -0.0069 -0.0179 -0.0114 63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.2985 0.6333 0.3299 0.0025  -0.0285 -0.0117 63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.2991 0.6417 0.3299 0.0164  -0.0294 0.0009  63  TYR   A C   
436  O O   . TYR   A 57  ? 0.2963 0.6437 0.3272 0.0189  -0.0246 0.0127  63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.2954 0.6433 0.3222 -0.0003 -0.0394 -0.0169 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.3055 0.6652 0.3288 0.0066  -0.0401 -0.0137 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.3137 0.6733 0.3384 0.0011  -0.0334 -0.0091 63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.3155 0.6900 0.3349 0.0171  -0.0466 -0.0175 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.3192 0.6945 0.3417 0.0071  -0.0316 -0.0071 63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.3199 0.7116 0.3348 0.0220  -0.0444 -0.0194 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.3271 0.7199 0.3437 0.0175  -0.0361 -0.0136 63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.3385 0.7529 0.3515 0.0220  -0.0317 -0.0161 63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.2972 0.6462 0.3278 0.0237  -0.0368 0.0007  64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.2900 0.6544 0.3177 0.0340  -0.0406 0.0141  64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.2952 0.6822 0.3061 0.0370  -0.0498 0.0062  64  TYR   A C   
448  O O   . TYR   A 58  ? 0.2965 0.6836 0.3078 0.0349  -0.0571 -0.0097 64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.2769 0.6400 0.3162 0.0396  -0.0443 0.0189  64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.2657 0.6518 0.3013 0.0476  -0.0514 0.0356  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.2627 0.6568 0.3078 0.0499  -0.0460 0.0598  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.2710 0.6756 0.2954 0.0508  -0.0648 0.0284  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.2608 0.6861 0.3002 0.0541  -0.0544 0.0795  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.2704 0.7036 0.2873 0.0548  -0.0726 0.0425  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.2692 0.7156 0.2910 0.0558  -0.0677 0.0693  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.2795 0.7632 0.2925 0.0568  -0.0772 0.0874  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.2918 0.7014 0.2922 0.0410  -0.0489 0.0172  65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.2980 0.7349 0.2825 0.0428  -0.0538 0.0045  65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.3104 0.7782 0.2828 0.0468  -0.0599 0.0158  65  CYS   A C   
460  O O   . CYS   A 59  ? 0.3113 0.7958 0.2803 0.0464  -0.0550 0.0394  65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.3005 0.7453 0.2806 0.0397  -0.0441 0.0058  65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.3164 0.8016 0.2800 0.0416  -0.0442 -0.0131 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.3146 0.7930 0.2836 0.0489  -0.0719 0.0022  66  SER   A N   
464  C CA  . SER   A 60  ? 0.3218 0.8348 0.2781 0.0500  -0.0801 0.0139  66  SER   A CA  
465  C C   . SER   A 60  ? 0.3218 0.8805 0.2526 0.0468  -0.0785 0.0078  66  SER   A C   
466  O O   . SER   A 60  ? 0.3097 0.9051 0.2274 0.0443  -0.0823 0.0296  66  SER   A O   
467  C CB  . SER   A 60  ? 0.3486 0.8615 0.3106 0.0516  -0.0940 0.0020  66  SER   A CB  
468  O OG  . SER   A 60  ? 0.3975 0.8939 0.3690 0.0513  -0.0981 -0.0277 66  SER   A OG  
469  N N   . SER   A 61  ? 0.3281 0.8888 0.2548 0.0457  -0.0718 -0.0184 67  SER   A N   
470  C CA  . SER   A 61  ? 0.3253 0.9331 0.2289 0.0421  -0.0662 -0.0281 67  SER   A CA  
471  C C   . SER   A 61  ? 0.3295 0.9582 0.2236 0.0391  -0.0566 0.0080  67  SER   A C   
472  O O   . SER   A 61  ? 0.3277 1.0069 0.1989 0.0341  -0.0526 0.0099  67  SER   A O   
473  C CB  . SER   A 61  ? 0.3344 0.9378 0.2466 0.0429  -0.0592 -0.0651 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.3599 0.9273 0.2919 0.0441  -0.0510 -0.0587 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.3319 0.9249 0.2465 0.0408  -0.0528 0.0356  68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.3312 0.9349 0.2510 0.0381  -0.0450 0.0730  68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.3404 0.9315 0.2830 0.0398  -0.0504 0.1091  68  ARG   A C   
478  O O   . ARG   A 62  ? 0.3407 0.9479 0.2955 0.0371  -0.0468 0.1464  68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.3438 0.9128 0.2800 0.0377  -0.0331 0.0699  68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.3701 0.9544 0.2943 0.0364  -0.0257 0.0420  68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.3923 1.0350 0.2947 0.0322  -0.0195 0.0534  68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.4195 1.0812 0.3147 0.0317  -0.0096 0.0229  68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.4348 1.1247 0.3159 0.0323  -0.0103 -0.0139 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.4128 1.1150 0.2817 0.0323  -0.0224 -0.0247 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.4362 1.1417 0.3211 0.0327  0.0013  -0.0422 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.3415 0.9037 0.2969 0.0441  -0.0583 0.0998  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.3447 0.8870 0.3316 0.0474  -0.0609 0.1268  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.3414 0.8484 0.3587 0.0471  -0.0479 0.1404  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.3323 0.8418 0.3800 0.0473  -0.0456 0.1754  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.3649 0.9530 0.3532 0.0455  -0.0702 0.1640  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.4282 1.0528 0.3894 0.0435  -0.0849 0.1507  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.4713 1.1552 0.4272 0.0372  -0.0940 0.1912  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.5323 1.2607 0.4568 0.0317  -0.1087 0.1760  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.5527 1.3502 0.4535 0.0212  -0.1176 0.1982  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.5467 1.3783 0.4523 0.0156  -0.1132 0.2403  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 0.5447 1.3818 0.4168 0.0145  -0.1311 0.1780  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.3412 0.8194 0.3536 0.0451  -0.0401 0.1133  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.3326 0.7813 0.3677 0.0417  -0.0283 0.1183  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.3275 0.7384 0.3654 0.0392  -0.0248 0.0882  70  LYS   A C   
500  O O   . LYS   A 64  ? 0.3294 0.7421 0.3472 0.0389  -0.0303 0.0637  70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.3495 0.8208 0.3701 0.0373  -0.0225 0.1238  70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.3826 0.8865 0.4146 0.0357  -0.0212 0.1647  70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.4253 0.9517 0.4456 0.0305  -0.0135 0.1700  70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.4584 1.0284 0.4882 0.0273  -0.0139 0.2154  70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.4919 1.1094 0.4984 0.0278  -0.0248 0.2259  70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.3184 0.6987 0.3845 0.0355  -0.0155 0.0906  71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.3286 0.6798 0.3970 0.0288  -0.0109 0.0644  71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.3285 0.6765 0.3937 0.0204  -0.0050 0.0619  71  HIS   A C   
509  O O   . HIS   A 65  ? 0.3260 0.6763 0.4086 0.0193  0.0010  0.0824  71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.3386 0.6635 0.4412 0.0280  -0.0028 0.0630  71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.3699 0.6975 0.4804 0.0359  -0.0077 0.0648  71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.3993 0.7138 0.5099 0.0334  -0.0063 0.0420  71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.3740 0.7200 0.4940 0.0446  -0.0142 0.0888  71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.3959 0.7180 0.5177 0.0420  -0.0113 0.0518  71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.3864 0.7272 0.5144 0.0487  -0.0170 0.0800  71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.3235 0.6703 0.3710 0.0145  -0.0080 0.0414  72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.3227 0.6700 0.3696 0.0065  -0.0038 0.0408  72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.3206 0.6473 0.3745 -0.0069 -0.0012 0.0247  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.3204 0.6453 0.3655 -0.0112 -0.0069 0.0089  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.3257 0.6966 0.3537 0.0094  -0.0092 0.0343  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.3382 0.7399 0.3554 0.0177  -0.0085 0.0478  72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.3452 0.7608 0.3679 0.0159  -0.0008 0.0680  72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.3531 0.7756 0.3544 0.0253  -0.0158 0.0394  72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.3504 0.8045 0.3598 0.0208  0.0003  0.0818  72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.3584 0.8181 0.3450 0.0296  -0.0148 0.0484  72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.3649 0.8430 0.3536 0.0270  -0.0064 0.0704  72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.3799 0.9045 0.3508 0.0286  -0.0050 0.0804  72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.3154 0.6312 0.3856 -0.0157 0.0066  0.0296  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.3183 0.6216 0.3914 -0.0324 0.0081  0.0121  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.3231 0.6419 0.3828 -0.0387 0.0008  0.0103  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.3242 0.6543 0.3859 -0.0352 0.0020  0.0231  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.3204 0.6079 0.4213 -0.0392 0.0182  0.0183  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.3199 0.6195 0.4290 -0.0277 0.0197  0.0463  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.3014 0.6203 0.3897 -0.0130 0.0131  0.0528  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.3196 0.6434 0.3697 -0.0474 -0.0070 -0.0026 74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.3146 0.6546 0.3633 -0.0531 -0.0155 -0.0004 74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.3111 0.6562 0.3593 -0.0744 -0.0214 -0.0079 74  VAL   A C   
538  O O   . VAL   A 68  ? 0.3192 0.6604 0.3610 -0.0836 -0.0200 -0.0200 74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.3183 0.6716 0.3634 -0.0398 -0.0240 -0.0008 74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.3254 0.6820 0.3649 -0.0220 -0.0193 0.0040  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.3240 0.6780 0.3653 -0.0434 -0.0322 -0.0091 74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.2956 0.6549 0.3521 -0.0832 -0.0281 0.0000  75  SER   A N   
543  C CA  . SER   A 69  ? 0.2918 0.6666 0.3488 -0.1051 -0.0379 -0.0006 75  SER   A CA  
544  C C   . SER   A 69  ? 0.2802 0.6724 0.3493 -0.0998 -0.0510 0.0086  75  SER   A C   
545  O O   . SER   A 69  ? 0.2791 0.6727 0.3625 -0.0842 -0.0511 0.0140  75  SER   A O   
546  C CB  . SER   A 69  ? 0.3008 0.6816 0.3668 -0.1218 -0.0380 0.0054  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.3087 0.7039 0.3942 -0.1182 -0.0447 0.0214  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.2699 0.6772 0.3369 -0.1124 -0.0612 0.0096  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.2632 0.6858 0.3519 -0.1076 -0.0748 0.0209  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.2696 0.7229 0.3727 -0.1319 -0.0902 0.0382  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.2821 0.7475 0.3685 -0.1542 -0.0898 0.0369  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.2569 0.6714 0.3376 -0.0940 -0.0746 0.0123  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.2607 0.6757 0.3168 -0.1054 -0.0698 0.0021  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.2780 0.6721 0.3162 -0.1001 -0.0546 -0.0132 76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.2628 0.7030 0.3189 -0.1228 -0.0799 0.0089  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.2919 0.6872 0.3151 -0.1107 -0.0475 -0.0270 76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.2761 0.7223 0.3093 -0.1348 -0.0725 -0.0045 76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.2830 0.7052 0.3012 -0.1279 -0.0554 -0.0250 76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.2538 0.7227 0.3926 -0.1291 -0.1043 0.0552  77  SER   A N   
560  C CA  . SER   A 71  ? 0.2429 0.7470 0.4045 -0.1526 -0.1218 0.0804  77  SER   A CA  
561  C C   . SER   A 71  ? 0.2571 0.7827 0.4041 -0.1670 -0.1296 0.0850  77  SER   A C   
562  O O   . SER   A 71  ? 0.2683 0.7776 0.3933 -0.1556 -0.1212 0.0676  77  SER   A O   
563  C CB  . SER   A 71  ? 0.2303 0.7429 0.4507 -0.1438 -0.1334 0.1001  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.2596 0.7608 0.5011 -0.1245 -0.1354 0.0941  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.2527 0.8199 0.4113 -0.1941 -0.1455 0.1103  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.2621 0.8603 0.4078 -0.2109 -0.1531 0.1188  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.2628 0.8644 0.4547 -0.1980 -0.1665 0.1388  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.2527 0.8446 0.4944 -0.1845 -0.1738 0.1514  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.2640 0.9148 0.3995 -0.2487 -0.1651 0.1391  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.3146 0.9641 0.3973 -0.2645 -0.1494 0.1085  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.3369 1.0449 0.4037 -0.3052 -0.1610 0.1232  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.3954 1.0982 0.4167 -0.3204 -0.1442 0.0857  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.4080 1.1708 0.4134 -0.3626 -0.1564 0.0972  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.2761 0.8885 0.4567 -0.1999 -0.1678 0.1384  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.2733 0.8849 0.5027 -0.1866 -0.1805 0.1554  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.2618 0.9006 0.5604 -0.1956 -0.2027 0.1959  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.2487 0.9343 0.5518 -0.2243 -0.2158 0.2264  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.2777 0.9138 0.4817 -0.1986 -0.1809 0.1574  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.3038 0.9295 0.4444 -0.2027 -0.1600 0.1239  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.2863 0.9116 0.4143 -0.2133 -0.1564 0.1196  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.2627 0.8761 0.6190 -0.1727 -0.2068 0.1960  80  SER   A N   
582  C CA  . SER   A 74  ? 0.2474 0.8835 0.6851 -0.1790 -0.2267 0.2338  80  SER   A CA  
583  C C   . SER   A 74  ? 0.2545 0.8652 0.7638 -0.1542 -0.2315 0.2290  80  SER   A C   
584  O O   . SER   A 74  ? 0.2702 0.8527 0.7595 -0.1359 -0.2223 0.1998  80  SER   A O   
585  C CB  . SER   A 74  ? 0.2513 0.8921 0.6975 -0.1855 -0.2253 0.2404  80  SER   A CB  
586  O OG  . SER   A 74  ? 0.2849 0.8842 0.7414 -0.1584 -0.2102 0.2097  80  SER   A OG  
587  N N   . LEU   A 75  ? 0.2382 0.8620 0.8366 -0.1554 -0.2467 0.2582  81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.2370 0.8406 0.9207 -0.1347 -0.2520 0.2530  81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.2596 0.8293 0.9592 -0.1109 -0.2351 0.2162  81  LEU   A C   
590  O O   . LEU   A 75  ? 0.2459 0.8258 0.9822 -0.1148 -0.2363 0.2308  81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.1937 0.8329 0.9796 -0.1499 -0.2772 0.3070  81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.1979 0.8656 1.0144 -0.1642 -0.2968 0.3427  81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.1622 0.8749 1.0782 -0.1844 -0.3234 0.4068  81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.2042 0.8373 1.0520 -0.1411 -0.2938 0.3134  81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.2881 0.8232 0.9650 -0.0875 -0.2200 0.1708  82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.3073 0.8181 0.9956 -0.0662 -0.2024 0.1333  82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.3065 0.8007 1.0668 -0.0474 -0.2033 0.1088  82  ILE   A C   
598  O O   . ILE   A 76  ? 0.3065 0.7923 1.0598 -0.0435 -0.2082 0.0985  82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.3523 0.8447 0.9404 -0.0584 -0.1808 0.0995  82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.3713 0.8782 0.9170 -0.0753 -0.1779 0.1190  82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.3645 0.8362 0.9561 -0.0351 -0.1621 0.0559  82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.4100 0.9206 0.8776 -0.0886 -0.1760 0.1218  82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.2976 0.7894 1.1349 -0.0372 -0.1991 0.0996  83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.2909 0.7680 1.2072 -0.0198 -0.1973 0.0686  83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.3255 0.7817 1.1779 -0.0018 -0.1772 0.0101  83  PHE   A C   
606  O O   . PHE   A 77  ? 0.3378 0.7906 1.1593 0.0084  -0.1570 -0.0202 83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.2568 0.7393 1.2764 -0.0136 -0.1947 0.0708  83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.2471 0.7139 1.3503 0.0050  -0.1883 0.0277  83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.2359 0.6975 1.4061 0.0042  -0.2055 0.0340  83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.2599 0.7194 1.3710 0.0222  -0.1641 -0.0230 83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.2255 0.6716 1.4728 0.0202  -0.1991 -0.0123 83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.2490 0.6973 1.4326 0.0376  -0.1562 -0.0712 83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.2247 0.6646 1.4773 0.0364  -0.1740 -0.0672 83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.3403 0.7872 1.1747 0.0005  -0.1837 -0.0024 84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.3710 0.8044 1.1498 0.0147  -0.1686 -0.0532 84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.3551 0.7816 1.2185 0.0278  -0.1664 -0.0933 84  VAL   A C   
617  O O   . VAL   A 78  ? 0.3243 0.7475 1.2661 0.0255  -0.1833 -0.0828 84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.4022 0.8310 1.1046 0.0103  -0.1742 -0.0489 84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.4359 0.8572 1.0749 0.0231  -0.1585 -0.0957 84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.4217 0.8590 1.0564 -0.0044 -0.1759 -0.0118 84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.3679 0.7954 1.2197 0.0404  -0.1448 -0.1393 85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.3579 0.7836 1.2795 0.0530  -0.1357 -0.1915 85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.3743 0.7915 1.2973 0.0546  -0.1456 -0.2167 85  GLU   A C   
624  O O   . GLU   A 79  ? 0.4022 0.8172 1.2469 0.0494  -0.1526 -0.2034 85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.4005 0.8383 1.2688 0.0626  -0.1083 -0.2360 85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.4384 0.8828 1.3913 0.0740  -0.0928 -0.2878 85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.4980 0.9490 1.5214 0.0767  -0.0836 -0.2740 85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 0.5008 0.9616 1.5806 0.0870  -0.0642 -0.3213 85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 0.5158 0.9652 1.5396 0.0675  -0.0954 -0.2173 85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.3535 0.7664 1.3705 0.0616  -0.1458 -0.2545 86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.3624 0.7678 1.3915 0.0621  -0.1564 -0.2820 86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.4010 0.8160 1.3222 0.0648  -0.1444 -0.3224 86  ALA   A C   
633  O O   . ALA   A 80  ? 0.4150 0.8455 1.2855 0.0700  -0.1229 -0.3534 86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.3217 0.7209 1.4795 0.0687  -0.1563 -0.3224 86  ALA   A CB  
635  N N   . SER   A 81  ? 0.4113 0.8210 1.3015 0.0602  -0.1595 -0.3181 87  SER   A N   
636  C CA  . SER   A 81  ? 0.4427 0.8638 1.2422 0.0607  -0.1542 -0.3496 87  SER   A CA  
637  C C   . SER   A 81  ? 0.4366 0.8510 1.2833 0.0584  -0.1710 -0.3720 87  SER   A C   
638  O O   . SER   A 81  ? 0.4111 0.8114 1.3634 0.0575  -0.1843 -0.3649 87  SER   A O   
639  C CB  . SER   A 81  ? 0.4909 0.9134 1.1857 0.0557  -0.1561 -0.3058 87  SER   A CB  
640  O OG  . SER   A 81  ? 0.5113 0.9213 1.2163 0.0486  -0.1765 -0.2623 87  SER   A OG  
641  N N   . GLU   A 82  ? 0.4547 0.8810 1.2308 0.0565  -0.1720 -0.3964 88  GLU   A N   
642  C CA  . GLU   A 82  ? 0.4464 0.8676 1.2633 0.0528  -0.1894 -0.4160 88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.4379 0.8434 1.2624 0.0465  -0.2121 -0.3574 88  GLU   A C   
644  O O   . GLU   A 82  ? 0.4233 0.8212 1.3059 0.0429  -0.2295 -0.3622 88  GLU   A O   
645  C CB  . GLU   A 82  ? 0.5088 0.9548 1.2542 0.0509  -0.1839 -0.4638 88  GLU   A CB  
646  C CG  . GLU   A 82  ? 0.6292 1.0826 1.2764 0.0465  -0.1916 -0.4301 88  GLU   A CG  
647  C CD  . GLU   A 82  ? 0.7556 1.2306 1.3000 0.0480  -0.1743 -0.4231 88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 0.7912 1.2874 1.2649 0.0442  -0.1763 -0.4284 88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 0.7840 1.2564 1.3235 0.0521  -0.1599 -0.4094 88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.4422 0.8459 1.2092 0.0443  -0.2109 -0.3047 89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.4363 0.8328 1.2014 0.0370  -0.2281 -0.2504 89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.4049 0.7936 1.2589 0.0322  -0.2389 -0.2096 89  TYR   A C   
653  O O   . TYR   A 83  ? 0.3916 0.7785 1.2874 0.0247  -0.2574 -0.1743 89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.4637 0.8661 1.1225 0.0354  -0.2197 -0.2192 89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.4907 0.9053 1.0631 0.0393  -0.2092 -0.2481 89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.5127 0.9379 1.0296 0.0438  -0.1898 -0.2643 89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.5054 0.9249 1.0533 0.0372  -0.2199 -0.2531 89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.5411 0.9841 0.9821 0.0454  -0.1820 -0.2829 89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.5320 0.9684 1.0038 0.0390  -0.2126 -0.2718 89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.5539 1.0034 0.9731 0.0426  -0.1940 -0.2856 89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 0.5811 1.0535 0.9294 0.0426  -0.1884 -0.2975 89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.3908 0.7796 1.2742 0.0352  -0.2280 -0.2099 90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.3673 0.7547 1.3361 0.0292  -0.2390 -0.1659 90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.3454 0.7297 1.3969 0.0365  -0.2292 -0.1927 90  TYR   A C   
665  O O   . TYR   A 84  ? 0.3626 0.7509 1.3689 0.0441  -0.2083 -0.2274 90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.3827 0.7798 1.2856 0.0212  -0.2359 -0.1157 90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.4103 0.8134 1.2309 0.0134  -0.2411 -0.0858 90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.4037 0.8158 1.2583 0.0013  -0.2599 -0.0394 90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.4522 0.8560 1.1653 0.0170  -0.2258 -0.0992 90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.4331 0.8542 1.2149 -0.0060 -0.2615 -0.0148 90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.4802 0.8890 1.1275 0.0106  -0.2283 -0.0734 90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.4745 0.8920 1.1550 -0.0006 -0.2450 -0.0338 90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.5030 0.9286 1.1220 -0.0068 -0.2447 -0.0122 90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.3027 0.6837 1.4763 0.0331  -0.2435 -0.1674 91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.2713 0.6505 1.5322 0.0401  -0.2333 -0.1852 91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.2763 0.6670 1.5001 0.0364  -0.2255 -0.1456 91  PRO   A C   
677  O O   . PRO   A 85  ? 0.3060 0.7050 1.4325 0.0283  -0.2266 -0.1118 91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.2328 0.6057 1.6430 0.0361  -0.2550 -0.1607 91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.2448 0.6171 1.6376 0.0271  -0.2756 -0.1371 91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.2717 0.6540 1.5168 0.0222  -0.2696 -0.1181 91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.2441 0.6360 1.5479 0.0419  -0.2169 -0.1522 92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.2471 0.6516 1.5273 0.0375  -0.2110 -0.1149 92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.2267 0.6448 1.5275 0.0196  -0.2361 -0.0364 92  ALA   A C   
684  O O   . ALA   A 86  ? 0.1929 0.6133 1.6045 0.0141  -0.2562 -0.0059 92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.2160 0.6206 1.5975 0.0473  -0.1985 -0.1369 92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.2397 0.6701 1.4342 0.0092  -0.2349 -0.0047 93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.2178 0.6694 1.4088 -0.0109 -0.2564 0.0637  93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.2274 0.6944 1.3179 -0.0217 -0.2488 0.0880  93  ARG   A C   
689  O O   . ARG   A 87  ? 0.2548 0.7120 1.2718 -0.0124 -0.2278 0.0528  93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.2412 0.6900 1.3924 -0.0153 -0.2672 0.0660  93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.3140 0.7509 1.3353 -0.0079 -0.2492 0.0258  93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.3602 0.7942 1.3466 -0.0104 -0.2582 0.0249  93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.4214 0.8658 1.2991 -0.0197 -0.2544 0.0450  93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.4796 0.9146 1.2577 -0.0123 -0.2362 0.0148  93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.4972 0.9407 1.1933 -0.0209 -0.2331 0.0334  93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.4885 0.9091 1.2529 0.0029  -0.2206 -0.0338 93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.2032 0.6976 1.2890 -0.0429 -0.2663 0.1476  94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.2162 0.7286 1.2104 -0.0570 -0.2613 0.1698  94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.2259 0.7438 1.1263 -0.0662 -0.2625 0.1745  94  TYR   A C   
700  O O   . TYR   A 88  ? 0.2118 0.7528 1.1380 -0.0815 -0.2810 0.2139  94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.1879 0.7370 1.2414 -0.0788 -0.2806 0.2334  94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.1804 0.7315 1.3029 -0.0743 -0.2769 0.2379  94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.2147 0.7660 1.2719 -0.0745 -0.2611 0.2261  94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.1477 0.7048 1.4088 -0.0722 -0.2911 0.2611  94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.2054 0.7623 1.3285 -0.0715 -0.2581 0.2342  94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.1360 0.6985 1.4689 -0.0688 -0.2879 0.2698  94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.1723 0.7355 1.4334 -0.0684 -0.2712 0.2561  94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.1665 0.7369 1.5016 -0.0650 -0.2677 0.2660  94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.2438 0.7447 1.0419 -0.0581 -0.2430 0.1380  95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.2570 0.7624 0.9713 -0.0655 -0.2413 0.1402  95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.2557 0.7897 0.9166 -0.0879 -0.2424 0.1732  95  GLN   A C   
712  O O   . GLN   A 89  ? 0.2781 0.8113 0.9098 -0.0896 -0.2322 0.1682  95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.3039 0.7805 0.9426 -0.0474 -0.2212 0.0899  95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.3545 0.8341 0.9078 -0.0537 -0.2159 0.0908  95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.4095 0.8646 0.9084 -0.0362 -0.2013 0.0494  95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.4131 0.8527 0.9377 -0.0207 -0.1981 0.0186  95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.4388 0.8938 0.8644 -0.0397 -0.1922 0.0479  95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.2298 0.7923 0.8789 -0.1064 -0.2544 0.2053  96  SER   A N   
719  C CA  . SER   A 90  ? 0.2271 0.8242 0.8232 -0.1310 -0.2551 0.2320  96  SER   A CA  
720  C C   . SER   A 90  ? 0.2476 0.8331 0.7412 -0.1296 -0.2355 0.2013  96  SER   A C   
721  O O   . SER   A 90  ? 0.2712 0.8295 0.7408 -0.1123 -0.2264 0.1715  96  SER   A O   
722  C CB  . SER   A 90  ? 0.2207 0.8660 0.8594 -0.1556 -0.2775 0.2850  96  SER   A CB  
723  O OG  . SER   A 90  ? 0.2615 0.9088 0.8935 -0.1539 -0.2806 0.2843  96  SER   A OG  
724  N N   . HIS   A 91  ? 0.2340 0.8415 0.6733 -0.1485 -0.2295 0.2085  97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.2505 0.8499 0.6038 -0.1502 -0.2103 0.1808  97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.2587 0.8110 0.5791 -0.1251 -0.1909 0.1386  97  HIS   A C   
727  O O   . HIS   A 91  ? 0.2801 0.8145 0.5535 -0.1159 -0.1773 0.1138  97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.2625 0.8777 0.5926 -0.1560 -0.2102 0.1831  97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.2665 0.9391 0.6091 -0.1860 -0.2252 0.2240  97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.2945 1.0029 0.5834 -0.2112 -0.2184 0.2262  97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.2502 0.9538 0.6549 -0.1958 -0.2466 0.2642  97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.2741 1.0391 0.5877 -0.2366 -0.2356 0.2681  97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.2482 1.0123 0.6340 -0.2282 -0.2537 0.2956  97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.2412 0.7775 0.5900 -0.1147 -0.1896 0.1328  98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.2572 0.7575 0.5791 -0.0927 -0.1722 0.0973  98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.2424 0.7407 0.5296 -0.0992 -0.1605 0.0922  98  LEU   A C   
737  O O   . LEU   A 92  ? 0.2213 0.7375 0.5370 -0.1115 -0.1681 0.1127  98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.2546 0.7396 0.6360 -0.0738 -0.1760 0.0869  98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.2966 0.7537 0.6511 -0.0518 -0.1589 0.0496  98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.3216 0.7652 0.6411 -0.0413 -0.1545 0.0304  98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.2852 0.7367 0.7010 -0.0383 -0.1597 0.0372  98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.2500 0.7277 0.4817 -0.0913 -0.1431 0.0675  99  MET   A N   
743  C CA  . MET   A 93  ? 0.2495 0.7215 0.4491 -0.0966 -0.1309 0.0605  99  MET   A CA  
744  C C   . MET   A 93  ? 0.2519 0.6992 0.4494 -0.0747 -0.1183 0.0403  99  MET   A C   
745  O O   . MET   A 93  ? 0.2654 0.6960 0.4466 -0.0581 -0.1112 0.0222  99  MET   A O   
746  C CB  . MET   A 93  ? 0.2599 0.7309 0.4069 -0.1070 -0.1203 0.0500  99  MET   A CB  
747  C CG  . MET   A 93  ? 0.2601 0.7611 0.4046 -0.1273 -0.1300 0.0648  99  MET   A CG  
748  S SD  . MET   A 93  ? 0.2972 0.7985 0.3884 -0.1369 -0.1140 0.0439  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.2419 0.7115 0.3297 -0.1085 -0.1061 0.0267  99  MET   A CE  
750  N N   . LEU   A 94  ? 0.2327 0.6832 0.4488 -0.0758 -0.1163 0.0452  100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.2342 0.6705 0.4506 -0.0573 -0.1036 0.0279  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.2457 0.6733 0.4229 -0.0599 -0.0895 0.0231  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.2423 0.6779 0.4125 -0.0779 -0.0913 0.0350  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.2124 0.6591 0.4865 -0.0534 -0.1082 0.0342  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.2101 0.6608 0.5388 -0.0458 -0.1198 0.0335  100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.1844 0.6473 0.5819 -0.0458 -0.1250 0.0445  100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2344 0.6715 0.5524 -0.0256 -0.1112 0.0033  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.2472 0.6619 0.4023 -0.0434 -0.0764 0.0068  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.2497 0.6564 0.3768 -0.0427 -0.0625 0.0048  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.2467 0.6584 0.3804 -0.0266 -0.0523 -0.0038 101 ALA   A C   
761  O O   . ALA   A 95  ? 0.2383 0.6559 0.3866 -0.0142 -0.0537 -0.0164 101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.2590 0.6513 0.3512 -0.0412 -0.0564 -0.0012 101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.2502 0.6633 0.3755 -0.0283 -0.0417 0.0017  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.2548 0.6803 0.3815 -0.0153 -0.0299 -0.0049 102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.2810 0.7026 0.3732 -0.0065 -0.0236 -0.0090 102 VAL   A C   
766  O O   . VAL   A 96  ? 0.2943 0.7029 0.3680 -0.0121 -0.0206 0.0009  102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.2528 0.6857 0.3880 -0.0216 -0.0215 0.0075  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.2537 0.7060 0.3846 -0.0092 -0.0070 0.0021  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.2397 0.6801 0.4142 -0.0311 -0.0296 0.0155  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.2824 0.7158 0.3711 0.0059  -0.0229 -0.0240 103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.3035 0.7399 0.3621 0.0130  -0.0197 -0.0244 103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.3055 0.7623 0.3600 0.0238  -0.0202 -0.0441 103 GLY   A C   
773  O O   . GLY   A 97  ? 0.2989 0.7613 0.3790 0.0270  -0.0240 -0.0625 103 GLY   A O   
774  N N   . HIS   A 98  ? 0.3076 0.7777 0.3340 0.0284  -0.0170 -0.0400 104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.3049 0.8006 0.3209 0.0357  -0.0183 -0.0597 104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.3048 0.7854 0.3235 0.0376  -0.0320 -0.0688 104 HIS   A C   
777  O O   . HIS   A 98  ? 0.2998 0.7568 0.3154 0.0346  -0.0378 -0.0537 104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.3159 0.8430 0.3008 0.0369  -0.0109 -0.0468 104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.3438 0.9044 0.3118 0.0408  -0.0136 -0.0670 104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.3558 0.9399 0.3344 0.0435  -0.0090 -0.1013 104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.3621 0.9370 0.3077 0.0412  -0.0208 -0.0589 104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.3580 0.9711 0.3157 0.0440  -0.0134 -0.1161 104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.3662 0.9759 0.3025 0.0424  -0.0217 -0.0890 104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.3043 0.8014 0.3313 0.0423  -0.0359 -0.0957 105 SER   A N   
785  C CA  . SER   A 99  ? 0.3151 0.8030 0.3491 0.0441  -0.0494 -0.1066 105 SER   A CA  
786  C C   . SER   A 99  ? 0.3033 0.8186 0.3437 0.0482  -0.0504 -0.1409 105 SER   A C   
787  O O   . SER   A 99  ? 0.2909 0.8256 0.3443 0.0499  -0.0406 -0.1620 105 SER   A O   
788  C CB  . SER   A 99  ? 0.3418 0.8003 0.4103 0.0406  -0.0588 -0.1032 105 SER   A CB  
789  O OG  . SER   A 99  ? 0.3722 0.8340 0.4802 0.0412  -0.0574 -0.1193 105 SER   A OG  
790  N N   . GLU   A 100 ? 0.3050 0.8234 0.3381 0.0491  -0.0616 -0.1484 106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.2978 0.8407 0.3380 0.0507  -0.0657 -0.1844 106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.2983 0.8163 0.3678 0.0509  -0.0826 -0.1883 106 GLU   A C   
793  O O   . GLU   A 100 ? 0.3104 0.8044 0.3759 0.0495  -0.0895 -0.1603 106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.3236 0.9061 0.3172 0.0484  -0.0647 -0.1833 106 GLU   A CB  
795  C CG  . GLU   A 100 ? 0.3793 0.9871 0.3409 0.0464  -0.0505 -0.1629 106 GLU   A CG  
796  C CD  . GLU   A 100 ? 0.4197 1.0863 0.3489 0.0421  -0.0444 -0.1805 106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 0.4388 1.1271 0.3567 0.0391  -0.0546 -0.1978 106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 0.4246 1.1198 0.3394 0.0402  -0.0295 -0.1770 106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.2805 0.8053 0.3827 0.0519  -0.0891 -0.2230 107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.2711 0.7733 0.4070 0.0512  -0.1063 -0.2220 107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.2815 0.7782 0.3863 0.0496  -0.1165 -0.1955 107 PRO   A C   
802  O O   . PRO   A 101 ? 0.2855 0.7572 0.4098 0.0483  -0.1252 -0.1752 107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.2644 0.7838 0.4326 0.0518  -0.1100 -0.2680 107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.2606 0.7989 0.4369 0.0540  -0.0924 -0.2934 107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.2565 0.8099 0.3744 0.0531  -0.0799 -0.2667 107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.2849 0.8084 0.3441 0.0488  -0.1144 -0.1923 108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.2896 0.8119 0.3254 0.0480  -0.1231 -0.1655 108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.2969 0.7937 0.3239 0.0489  -0.1177 -0.1275 108 GLY   A C   
809  O O   . GLY   A 102 ? 0.2984 0.7889 0.3183 0.0493  -0.1232 -0.1059 108 GLY   A O   
810  N N   . ASP   A 103 ? 0.2905 0.7734 0.3224 0.0487  -0.1063 -0.1214 109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.2933 0.7535 0.3195 0.0473  -0.0995 -0.0929 109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.2902 0.7241 0.3437 0.0439  -0.1059 -0.0859 109 ASP   A C   
813  O O   . ASP   A 103 ? 0.2919 0.7105 0.3394 0.0411  -0.1008 -0.0664 109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.3051 0.7674 0.3234 0.0462  -0.0855 -0.0895 109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.3312 0.8212 0.3185 0.0474  -0.0774 -0.0815 109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.3371 0.8339 0.3091 0.0481  -0.0804 -0.0624 109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.3396 0.8477 0.3218 0.0471  -0.0681 -0.0915 109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.2785 0.7104 0.3654 0.0430  -0.1170 -0.1016 110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.2777 0.6938 0.3941 0.0377  -0.1255 -0.0905 110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.2870 0.6991 0.3895 0.0375  -0.1284 -0.0743 110 CYS   A C   
821  O O   . CYS   A 104 ? 0.2952 0.7171 0.3911 0.0418  -0.1348 -0.0795 110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.2697 0.6883 0.4321 0.0375  -0.1386 -0.1076 110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.2923 0.7117 0.4950 0.0370  -0.1351 -0.1228 110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.2841 0.6853 0.3808 0.0321  -0.1221 -0.0565 111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.2813 0.6794 0.3699 0.0322  -0.1207 -0.0436 111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.2733 0.6633 0.3401 0.0321  -0.1051 -0.0330 111 GLY   A C   
827  O O   . GLY   A 105 ? 0.2708 0.6564 0.3391 0.0308  -0.1003 -0.0246 111 GLY   A O   
828  N N   . GLY   A 106 ? 0.2619 0.6509 0.3137 0.0336  -0.0964 -0.0343 112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.2602 0.6399 0.3003 0.0329  -0.0820 -0.0241 112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.2571 0.6261 0.3016 0.0218  -0.0751 -0.0240 112 GLY   A C   
831  O O   . GLY   A 106 ? 0.2517 0.6239 0.3026 0.0143  -0.0801 -0.0278 112 GLY   A O   
832  N N   . ILE   A 107 ? 0.2521 0.6120 0.2974 0.0193  -0.0638 -0.0203 113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.2515 0.6079 0.2975 0.0057  -0.0562 -0.0251 113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.2706 0.6187 0.3099 -0.0014 -0.0462 -0.0271 113 ILE   A C   
835  O O   . ILE   A 107 ? 0.2741 0.6134 0.3133 0.0052  -0.0386 -0.0224 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.2423 0.5962 0.2970 0.0048  -0.0467 -0.0275 113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.2302 0.5943 0.2942 0.0108  -0.0574 -0.0233 113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.2453 0.6039 0.2970 -0.0125 -0.0372 -0.0379 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.2293 0.5920 0.3066 0.0136  -0.0468 -0.0240 113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.2745 0.6291 0.3111 -0.0167 -0.0473 -0.0310 114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.2913 0.6416 0.3229 -0.0280 -0.0392 -0.0343 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.3139 0.6637 0.3452 -0.0400 -0.0270 -0.0464 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.3056 0.6719 0.3348 -0.0498 -0.0301 -0.0497 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.2829 0.6477 0.3154 -0.0395 -0.0504 -0.0296 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.2931 0.6610 0.3208 -0.0570 -0.0455 -0.0316 114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.3058 0.6598 0.3338 -0.0504 -0.0384 -0.0296 114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.2877 0.6774 0.3236 -0.0704 -0.0597 -0.0212 114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.3398 0.6732 0.3774 -0.0396 -0.0125 -0.0535 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.3697 0.7013 0.4139 -0.0502 0.0027  -0.0723 115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.3949 0.7214 0.4390 -0.0663 0.0120  -0.0853 115 ARG   A C   
851  O O   . ARG   A 109 ? 0.3946 0.7082 0.4435 -0.0625 0.0117  -0.0767 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.4002 0.7144 0.4687 -0.0346 0.0140  -0.0730 115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.4593 0.7837 0.5345 -0.0335 0.0182  -0.0814 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.5094 0.8166 0.6195 -0.0210 0.0331  -0.0848 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.5551 0.8752 0.6740 -0.0202 0.0386  -0.0937 115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.5969 0.9189 0.7281 -0.0050 0.0318  -0.0779 115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.5957 0.9096 0.7304 0.0098  0.0197  -0.0540 115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.6052 0.9413 0.7456 -0.0057 0.0374  -0.0859 115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.4070 0.7472 0.4460 -0.0854 0.0210  -0.1074 116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.4229 0.7618 0.4629 -0.1045 0.0313  -0.1275 116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.4368 0.7692 0.4972 -0.1084 0.0531  -0.1585 116 CYS   A C   
862  O O   . CYS   A 110 ? 0.4330 0.7662 0.5039 -0.0970 0.0583  -0.1602 116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.4273 0.7999 0.4405 -0.1297 0.0206  -0.1282 116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.4605 0.8752 0.4555 -0.1466 0.0205  -0.1387 116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.4498 0.7775 0.5203 -0.1253 0.0665  -0.1856 117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.4584 0.7805 0.5562 -0.1299 0.0899  -0.2222 117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.4535 0.8103 0.5329 -0.1396 0.0956  -0.2394 117 GLN   A C   
868  O O   . GLN   A 111 ? 0.4494 0.8000 0.5572 -0.1323 0.1138  -0.2601 117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.4875 0.8031 0.5998 -0.1506 0.1031  -0.2551 117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.5474 0.8959 0.6190 -0.1805 0.0925  -0.2621 117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.6157 0.9662 0.7012 -0.2053 0.1093  -0.3075 117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.6384 0.9591 0.7547 -0.2044 0.1133  -0.3116 117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.6220 1.0111 0.6868 -0.2295 0.1201  -0.3440 117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.4497 0.8441 0.4880 -0.1543 0.0793  -0.2257 118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.4444 0.8801 0.4637 -0.1663 0.0820  -0.2346 118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.4306 0.8628 0.4589 -0.1436 0.0759  -0.2113 118 HIS   A C   
877  O O   . HIS   A 112 ? 0.4243 0.8845 0.4494 -0.1494 0.0843  -0.2227 118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.4615 0.9451 0.4407 -0.1942 0.0653  -0.2237 118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.5031 0.9953 0.4711 -0.2191 0.0681  -0.2440 118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.5358 0.9976 0.5123 -0.2127 0.0587  -0.2290 118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.5157 1.0452 0.4666 -0.2505 0.0803  -0.2801 118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.5452 1.0245 0.5110 -0.2403 0.0634  -0.2537 118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.5351 1.0558 0.4841 -0.2644 0.0762  -0.2864 118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.4192 0.8223 0.4574 -0.1201 0.0613  -0.1799 119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.4042 0.8039 0.4511 -0.0994 0.0526  -0.1575 119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.3948 0.7922 0.4297 -0.0898 0.0277  -0.1235 119 GLY   A C   
887  O O   . GLY   A 113 ? 0.4004 0.7850 0.4300 -0.0895 0.0198  -0.1142 119 GLY   A O   
888  N N   . VAL   A 114 ? 0.3762 0.7873 0.4110 -0.0822 0.0160  -0.1066 120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.3659 0.7756 0.3982 -0.0721 -0.0066 -0.0796 120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.3521 0.7882 0.3702 -0.0906 -0.0222 -0.0673 120 VAL   A C   
891  O O   . VAL   A 114 ? 0.3419 0.8124 0.3541 -0.1073 -0.0261 -0.0637 120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.3615 0.7748 0.4068 -0.0578 -0.0136 -0.0680 120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.3610 0.7769 0.4083 -0.0509 -0.0367 -0.0463 120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.3695 0.7570 0.4345 -0.0378 -0.0026 -0.0717 120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.3462 0.7695 0.3636 -0.0873 -0.0318 -0.0574 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.3339 0.7785 0.3487 -0.1024 -0.0473 -0.0421 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.3159 0.7671 0.3495 -0.0932 -0.0670 -0.0204 121 VAL   A C   
898  O O   . VAL   A 115 ? 0.2982 0.7795 0.3407 -0.1079 -0.0802 -0.0039 121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.3494 0.7771 0.3614 -0.1028 -0.0457 -0.0435 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.3452 0.7979 0.3605 -0.1199 -0.0610 -0.0264 121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.3632 0.7794 0.3658 -0.1104 -0.0264 -0.0665 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.3137 0.7398 0.3570 -0.0706 -0.0694 -0.0202 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.3022 0.7308 0.3676 -0.0608 -0.0863 -0.0075 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.2986 0.7039 0.3670 -0.0383 -0.0860 -0.0138 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.3091 0.6975 0.3634 -0.0300 -0.0736 -0.0223 122 GLY   A O   
906  N N   . ILE   A 117 ? 0.2826 0.6903 0.3724 -0.0299 -0.1002 -0.0091 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.2898 0.6845 0.3805 -0.0118 -0.1018 -0.0175 123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.2935 0.6874 0.3984 -0.0075 -0.1077 -0.0216 123 ILE   A C   
909  O O   . ILE   A 117 ? 0.2816 0.6846 0.4111 -0.0162 -0.1164 -0.0142 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.2891 0.6884 0.3945 -0.0052 -0.1119 -0.0163 123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.2823 0.6963 0.4217 -0.0139 -0.1280 -0.0061 123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.2981 0.6975 0.3913 -0.0053 -0.1025 -0.0146 123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.2911 0.7077 0.4527 -0.0069 -0.1402 -0.0065 123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.3079 0.6952 0.4010 0.0051  -0.1027 -0.0321 124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.3096 0.7002 0.4155 0.0101  -0.1045 -0.0414 124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.3025 0.6995 0.4473 0.0118  -0.1194 -0.0476 124 VAL   A C   
917  O O   . VAL   A 118 ? 0.2941 0.6925 0.4444 0.0155  -0.1272 -0.0504 124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.3237 0.7156 0.4053 0.0210  -0.0954 -0.0507 124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.3194 0.7219 0.4161 0.0267  -0.0967 -0.0673 124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.3410 0.7260 0.3996 0.0177  -0.0816 -0.0413 124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.2959 0.6969 0.4752 0.0078  -0.1241 -0.0469 125 SER   A N   
922  C CA  . SER   A 119 ? 0.2909 0.6964 0.5220 0.0082  -0.1384 -0.0502 125 SER   A CA  
923  C C   . SER   A 119 ? 0.2961 0.7039 0.5598 0.0156  -0.1367 -0.0703 125 SER   A C   
924  O O   . SER   A 119 ? 0.2921 0.7015 0.5815 0.0228  -0.1422 -0.0913 125 SER   A O   
925  C CB  . SER   A 119 ? 0.2954 0.7088 0.5571 -0.0065 -0.1494 -0.0235 125 SER   A CB  
926  O OG  . SER   A 119 ? 0.3016 0.7198 0.6167 -0.0071 -0.1655 -0.0194 125 SER   A OG  
927  N N   . THR   A 120 ? 0.3078 0.7175 0.5745 0.0132  -0.1286 -0.0666 126 THR   A N   
928  C CA  . THR   A 120 ? 0.3034 0.7180 0.6076 0.0202  -0.1240 -0.0866 126 THR   A CA  
929  C C   . THR   A 120 ? 0.3197 0.7391 0.5796 0.0258  -0.1059 -0.0983 126 THR   A C   
930  O O   . THR   A 120 ? 0.3388 0.7552 0.5461 0.0243  -0.0992 -0.0888 126 THR   A O   
931  C CB  . THR   A 120 ? 0.3071 0.7251 0.6752 0.0119  -0.1329 -0.0669 126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.3400 0.7611 0.6861 0.0039  -0.1257 -0.0484 126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.3015 0.7216 0.7046 0.0016  -0.1514 -0.0414 126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.3115 0.7401 0.5981 0.0317  -0.0974 -0.1176 127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.3276 0.7671 0.5782 0.0358  -0.0801 -0.1259 127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.3153 0.7700 0.6062 0.0430  -0.0705 -0.1543 127 GLY   A C   
937  O O   . GLY   A 121 ? 0.3023 0.7596 0.6370 0.0479  -0.0754 -0.1797 127 GLY   A O   
938  N N   . GLY   A 122 ? 0.3151 0.7805 0.5957 0.0435  -0.0562 -0.1518 128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.3032 0.7875 0.6212 0.0505  -0.0428 -0.1802 128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.2974 0.7878 0.6266 0.0480  -0.0320 -0.1639 128 GLY   A C   
941  O O   . GLY   A 122 ? 0.3040 0.7801 0.6397 0.0392  -0.0404 -0.1308 128 GLY   A O   
942  N N   . ASN   A 123 ? 0.2840 0.7998 0.6147 0.0544  -0.0131 -0.1879 129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.2842 0.8108 0.6301 0.0531  -0.0004 -0.1753 129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.2921 0.8156 0.5791 0.0453  0.0020  -0.1413 129 ASN   A C   
945  O O   . ASN   A 123 ? 0.2863 0.8089 0.5900 0.0401  0.0049  -0.1199 129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.2909 0.8046 0.7157 0.0503  -0.0096 -0.1601 129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.3226 0.8388 0.8272 0.0585  -0.0103 -0.1912 129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.3475 0.8733 0.8495 0.0659  -0.0045 -0.2309 129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.3032 0.8127 0.8862 0.0562  -0.0182 -0.1732 129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.2948 0.8170 0.5208 0.0440  0.0002  -0.1361 130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.2964 0.8116 0.4768 0.0368  0.0015  -0.1049 130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.2903 0.7739 0.4706 0.0271  -0.0144 -0.0793 130 GLY   A C   
953  O O   . GLY   A 124 ? 0.2976 0.7717 0.4569 0.0189  -0.0135 -0.0559 130 GLY   A O   
954  N N   . LEU   A 125 ? 0.2745 0.7446 0.4808 0.0267  -0.0286 -0.0848 131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.2794 0.7285 0.4865 0.0159  -0.0436 -0.0630 131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.2905 0.7301 0.4761 0.0187  -0.0524 -0.0698 131 LEU   A C   
957  O O   . LEU   A 125 ? 0.2941 0.7426 0.4787 0.0284  -0.0508 -0.0925 131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.2582 0.7068 0.5262 0.0103  -0.0547 -0.0550 131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.2650 0.7258 0.5700 0.0089  -0.0475 -0.0493 131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.2498 0.7133 0.6269 0.0053  -0.0602 -0.0404 131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.2825 0.7410 0.5573 -0.0031 -0.0443 -0.0255 131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.2882 0.7131 0.4570 0.0093  -0.0609 -0.0520 132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.2901 0.7069 0.4430 0.0110  -0.0690 -0.0550 132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.2859 0.6960 0.4552 -0.0022 -0.0819 -0.0372 132 VAL   A C   
965  O O   . VAL   A 126 ? 0.2895 0.6987 0.4526 -0.0147 -0.0811 -0.0214 132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.3055 0.7184 0.4099 0.0147  -0.0607 -0.0530 132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.3229 0.7275 0.4087 0.0057  -0.0530 -0.0360 132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.3035 0.7088 0.3963 0.0162  -0.0689 -0.0536 132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.2710 0.6814 0.4646 -0.0011 -0.0941 -0.0398 133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.2656 0.6786 0.4774 -0.0148 -0.1074 -0.0201 133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.2716 0.6798 0.4561 -0.0164 -0.1104 -0.0184 133 GLY   A C   
972  O O   . GLY   A 127 ? 0.2702 0.6734 0.4448 -0.0048 -0.1097 -0.0326 133 GLY   A O   
973  N N   . PHE   A 128 ? 0.2719 0.6857 0.4444 -0.0322 -0.1134 -0.0018 134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.2742 0.6873 0.4233 -0.0356 -0.1136 -0.0002 134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.2654 0.6983 0.4399 -0.0507 -0.1278 0.0191  134 PHE   A C   
976  O O   . PHE   A 128 ? 0.2458 0.6960 0.4363 -0.0666 -0.1343 0.0365  134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.2758 0.6826 0.3837 -0.0423 -0.0993 -0.0029 134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.2820 0.6747 0.3712 -0.0330 -0.0861 -0.0123 134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.2930 0.6743 0.3642 -0.0186 -0.0782 -0.0214 134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.2829 0.6780 0.3753 -0.0401 -0.0827 -0.0079 134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.3038 0.6784 0.3611 -0.0120 -0.0671 -0.0238 134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.2945 0.6801 0.3728 -0.0323 -0.0707 -0.0131 134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.2973 0.6737 0.3582 -0.0186 -0.0630 -0.0200 134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.2732 0.7079 0.4531 -0.0471 -0.1337 0.0192  135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.2705 0.7287 0.4746 -0.0617 -0.1472 0.0407  135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.2933 0.7651 0.4579 -0.0767 -0.1378 0.0436  135 ALA   A C   
987  O O   . ALA   A 129 ? 0.3065 0.7662 0.4424 -0.0690 -0.1262 0.0288  135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.2651 0.7198 0.4918 -0.0513 -0.1560 0.0381  135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.2937 0.7935 0.4594 -0.0991 -0.1425 0.0616  136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.3154 0.8351 0.4431 -0.1172 -0.1321 0.0587  136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.3219 0.8632 0.4502 -0.1229 -0.1345 0.0658  136 ASP   A C   
992  O O   . ASP   A 130 ? 0.3180 0.8755 0.4841 -0.1248 -0.1514 0.0882  136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.3265 0.8797 0.4555 -0.1433 -0.1392 0.0774  136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.4019 0.9792 0.4881 -0.1650 -0.1265 0.0665  136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.4289 0.9830 0.4857 -0.1607 -0.1091 0.0400  136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.4253 1.0475 0.5105 -0.1872 -0.1335 0.0836  136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.3216 0.8646 0.4146 -0.1262 -0.1172 0.0472  137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.3035 0.8722 0.3957 -0.1329 -0.1162 0.0524  137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.2988 0.9069 0.3595 -0.1592 -0.1039 0.0458  137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.2902 0.9319 0.3498 -0.1699 -0.1027 0.0526  137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.3152 0.8544 0.4068 -0.1095 -0.1072 0.0358  137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.3174 0.8292 0.4387 -0.0885 -0.1213 0.0409  137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.3373 0.8500 0.4000 -0.1010 -0.0845 0.0067  137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.3046 0.9128 0.3412 -0.1712 -0.0949 0.0317  138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.3064 0.9527 0.3110 -0.1988 -0.0822 0.0174  138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.3020 1.0158 0.3067 -0.2291 -0.0950 0.0451  138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.3031 1.0570 0.2793 -0.2509 -0.0815 0.0293  138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.3069 0.9409 0.2948 -0.2072 -0.0766 0.0027  138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.3207 0.8968 0.3066 -0.1822 -0.0611 -0.0240 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.3204 0.8867 0.2940 -0.1922 -0.0558 -0.0367 138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.3019 0.8670 0.2924 -0.1920 -0.0747 -0.0101 138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.2959 0.8492 0.2837 -0.1966 -0.0739 -0.0138 138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.2900 0.8299 0.2595 -0.2026 -0.0562 -0.0429 138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.2667 0.8217 0.2763 -0.1954 -0.0902 0.0113  138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.2937 1.0244 0.3332 -0.2323 -0.1203 0.0860  139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.2857 1.0863 0.3333 -0.2623 -0.1355 0.1219  139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.2926 1.1167 0.3493 -0.2607 -0.1341 0.1310  139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.2805 1.1712 0.3321 -0.2885 -0.1394 0.1538  139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.2846 1.0974 0.3796 -0.2676 -0.1639 0.1672  139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.3404 1.1131 0.4882 -0.2391 -0.1768 0.1813  139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.3622 1.0776 0.5049 -0.2103 -0.1651 0.1509  139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.3559 1.1574 0.5534 -0.2471 -0.1991 0.2232  139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.3046 1.0796 0.3747 -0.2302 -0.1274 0.1151  140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.3008 1.0934 0.3845 -0.2263 -0.1267 0.1241  140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.3151 1.1301 0.3584 -0.2353 -0.0991 0.0911  140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.3309 1.1045 0.3677 -0.2130 -0.0809 0.0595  140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.3017 1.0373 0.4179 -0.1923 -0.1324 0.1207  140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.3059 1.0136 0.4633 -0.1810 -0.1546 0.1405  140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.3288 0.9792 0.5020 -0.1489 -0.1539 0.1218  140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.2779 1.0286 0.4836 -0.1978 -0.1800 0.1879  140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.3027 1.1872 0.3220 -0.2693 -0.0958 0.0983  141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.3167 1.2365 0.2987 -0.2841 -0.0678 0.0636  141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.3227 1.2532 0.3190 -0.2736 -0.0583 0.0636  141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.3308 1.2540 0.3111 -0.2672 -0.0303 0.0234  141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.3000 1.3040 0.2526 -0.3275 -0.0702 0.0754  141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.3206 1.3243 0.2545 -0.3434 -0.0771 0.0716  141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.3032 1.3994 0.2063 -0.3893 -0.0806 0.0846  141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.3597 1.3083 0.2707 -0.3291 -0.0520 0.0154  141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.3118 1.2567 0.3459 -0.2707 -0.0817 0.1088  142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.3147 1.2718 0.3695 -0.2615 -0.0775 0.1169  142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.3483 1.2381 0.4137 -0.2257 -0.0628 0.0855  142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.3404 1.2415 0.4197 -0.2185 -0.0544 0.0855  142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.2911 1.2704 0.3942 -0.2651 -0.1094 0.1738  142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.3014 1.2235 0.4436 -0.2446 -0.1340 0.1912  142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.3023 1.2285 0.4595 -0.2552 -0.1541 0.2157  142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.3081 1.1699 0.4860 -0.2125 -0.1422 0.1878  142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.3083 1.1787 0.5100 -0.2305 -0.1717 0.2238  142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.3142 1.1458 0.5260 -0.2051 -0.1651 0.2055  142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.3219 1.1560 0.5080 -0.1906 -0.1326 0.1712  142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.3263 1.1030 0.5749 -0.1778 -0.1767 0.2015  142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.3374 1.1180 0.5582 -0.1646 -0.1469 0.1716  142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.3359 1.0892 0.5852 -0.1589 -0.1679 0.1840  142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.3815 1.2064 0.4429 -0.2046 -0.0606 0.0627  143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.4140 1.1794 0.4874 -0.1726 -0.0498 0.0392  143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.4371 1.2072 0.4963 -0.1703 -0.0169 0.0010  143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.4342 1.1793 0.5145 -0.1488 -0.0096 -0.0056 143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.4346 1.1403 0.5056 -0.1548 -0.0552 0.0278  143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.4492 1.1391 0.5452 -0.1495 -0.0846 0.0584  143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.4765 1.1166 0.5646 -0.1349 -0.0850 0.0429  143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.4488 1.1258 0.5820 -0.1325 -0.0998 0.0769  143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.4545 1.2595 0.4825 -0.1933 0.0029  -0.0249 144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.4761 1.2878 0.4971 -0.1932 0.0376  -0.0685 144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.4693 1.3533 0.4854 -0.2140 0.0517  -0.0691 144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.4701 1.3787 0.4722 -0.2254 0.0823  -0.1107 144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.5159 1.3203 0.5101 -0.2058 0.0554  -0.1077 144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.5969 1.3398 0.5930 -0.1899 0.0437  -0.1071 144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.6090 1.2964 0.6300 -0.1601 0.0414  -0.1048 144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.6375 1.3917 0.6101 -0.2086 0.0374  -0.1087 144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.4603 1.3805 0.4916 -0.2197 0.0314  -0.0256 145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.4528 1.4487 0.4800 -0.2407 0.0451  -0.0221 145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.4441 1.4501 0.5088 -0.2299 0.0282  0.0192  145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.4283 1.4682 0.5039 -0.2306 0.0468  0.0119  145 GLU   A O   
1073 C CB  . GLU   A 139 ? 0.4772 1.5537 0.4677 -0.2825 0.0418  -0.0115 145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 0.5728 1.6461 0.5614 -0.2928 0.0072  0.0292  145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 0.6848 1.8218 0.6328 -0.3318 0.0069  0.0276  145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 0.6938 1.8627 0.6484 -0.3494 -0.0229 0.0763  145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 0.7318 1.8888 0.6458 -0.3456 0.0361  -0.0225 145 GLU   A OE2 
1078 N N1  . A1BOY B .   ? 0.3497 0.7787 0.7632 0.0457  -0.1342 -0.1996 201 A1BOY A N1  
1079 C C4  . A1BOY B .   ? 0.3764 0.8179 0.5973 0.0449  -0.1098 -0.1659 201 A1BOY A C4  
1080 C C5  . A1BOY B .   ? 0.3707 0.8271 0.6124 0.0493  -0.0998 -0.1949 201 A1BOY A C5  
1081 C C6  . A1BOY B .   ? 0.3594 0.8177 0.6668 0.0522  -0.1060 -0.2269 201 A1BOY A C6  
1082 C C7  . A1BOY B .   ? 0.3524 0.7918 0.7268 0.0485  -0.1168 -0.2055 201 A1BOY A C7  
1083 C C8  . A1BOY B .   ? 0.3487 0.7819 0.7607 0.0480  -0.1424 -0.2253 201 A1BOY A C8  
1084 C C10 . A1BOY B .   ? 0.3434 0.7553 0.7989 0.0352  -0.1703 -0.1598 201 A1BOY A C10 
1085 C C13 . A1BOY B .   ? 0.3384 0.7560 0.8061 0.0384  -0.1474 -0.1652 201 A1BOY A C13 
1086 O O2  . A1BOY B .   ? 0.3100 0.7212 0.8853 0.0193  -0.1828 -0.0941 201 A1BOY A O2  
1087 C C12 . A1BOY B .   ? 0.3322 0.7428 0.8282 0.0202  -0.1750 -0.0964 201 A1BOY A C12 
1088 N N2  . A1BOY B .   ? 0.3414 0.7543 0.7949 0.0108  -0.1776 -0.0650 201 A1BOY A N2  
1089 C C11 . A1BOY B .   ? 0.3481 0.7599 0.7937 0.0312  -0.1611 -0.1356 201 A1BOY A C11 
1090 C C9  . A1BOY B .   ? 0.3575 0.7805 0.7578 0.0425  -0.1581 -0.1952 201 A1BOY A C9  
1091 O O1  . A1BOY B .   ? 0.3472 0.7845 0.7396 0.0466  -0.1110 -0.1901 201 A1BOY A O1  
1092 C C1  . A1BOY B .   ? 0.3740 0.8427 0.5813 0.0503  -0.0835 -0.1914 201 A1BOY A C1  
1093 O O   . A1BOY B .   ? 0.3604 0.8488 0.5876 0.0545  -0.0716 -0.2218 201 A1BOY A O   
1094 C C   . A1BOY B .   ? 0.3640 0.8723 0.5543 0.0552  -0.0544 -0.2194 201 A1BOY A C   
1095 C C3  . A1BOY B .   ? 0.3901 0.8269 0.5642 0.0420  -0.1030 -0.1398 201 A1BOY A C3  
1096 C C2  . A1BOY B .   ? 0.3946 0.8410 0.5436 0.0431  -0.0883 -0.1389 201 A1BOY A C2  
1097 N N   . A1BOY B .   ? 0.3862 0.8496 0.5495 0.0471  -0.0787 -0.1623 201 A1BOY A N   
# 
