data_7HVQ
# 
_entry.id   7HVQ 
# 
_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   7HVQ         pdb_00007hvq 10.2210/pdb7hvq/pdb 
WWPDB D_1001407990 ?            ?                   
# 
_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                        7HVQ 
_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-[(3-cyano-2-methoxyphenyl)acetyl]piperidine-3-carboxamide' 301.340   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                         65.409    1   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                               78.133    1   ?         ? ? ? 
5 water       nat water                                                              18.015    104 ?         ? ? ? 
# 
_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-[(3-cyano-2-methoxyphenyl)acetyl]piperidine-3-carboxamide' A1BOQ 
3 'ZINC ION'                                                         ZN    
4 'DIMETHYL SULFOXIDE'                                               DMS   
5 water                                                              HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   ALA n 
1 4   ILE n 
1 5   TYR n 
1 6   VAL n 
1 7   GLY n 
1 8   ASN n 
1 9   TYR n 
1 10  ARG n 
1 11  VAL n 
1 12  VAL n 
1 13  ASN n 
1 14  ARG n 
1 15  HIS n 
1 16  LEU n 
1 17  ALA n 
1 18  THR n 
1 19  HIS n 
1 20  ASN n 
1 21  ASP n 
1 22  TRP n 
1 23  ALA n 
1 24  ASN n 
1 25  LEU n 
1 26  VAL n 
1 27  TRP n 
1 28  GLU n 
1 29  ASP n 
1 30  SER n 
1 31  SER n 
1 32  ARG n 
1 33  ASP n 
1 34  LEU n 
1 35  LEU n 
1 36  VAL n 
1 37  SER n 
1 38  SER n 
1 39  THR n 
1 40  THR n 
1 41  ALA n 
1 42  GLN n 
1 43  GLY n 
1 44  CYS n 
1 45  ASP n 
1 46  THR n 
1 47  ILE n 
1 48  ALA n 
1 49  ARG n 
1 50  CYS n 
1 51  ASP n 
1 52  CYS n 
1 53  GLN n 
1 54  THR n 
1 55  GLY n 
1 56  VAL n 
1 57  TYR n 
1 58  TYR n 
1 59  CYS n 
1 60  SER n 
1 61  SER n 
1 62  ARG n 
1 63  ARG n 
1 64  LYS n 
1 65  HIS n 
1 66  TYR n 
1 67  PRO n 
1 68  VAL n 
1 69  SER n 
1 70  PHE n 
1 71  SER n 
1 72  LYS n 
1 73  PRO n 
1 74  SER n 
1 75  LEU n 
1 76  ILE n 
1 77  PHE n 
1 78  VAL n 
1 79  GLU n 
1 80  ALA n 
1 81  SER n 
1 82  GLU n 
1 83  TYR n 
1 84  TYR n 
1 85  PRO n 
1 86  ALA n 
1 87  ARG n 
1 88  TYR n 
1 89  GLN n 
1 90  SER n 
1 91  HIS n 
1 92  LEU n 
1 93  MET n 
1 94  LEU n 
1 95  ALA n 
1 96  VAL n 
1 97  GLY n 
1 98  HIS n 
1 99  SER n 
1 100 GLU n 
1 101 PRO n 
1 102 GLY n 
1 103 ASP n 
1 104 CYS n 
1 105 GLY n 
1 106 GLY n 
1 107 ILE n 
1 108 LEU n 
1 109 ARG n 
1 110 CYS n 
1 111 GLN n 
1 112 HIS n 
1 113 GLY n 
1 114 VAL n 
1 115 VAL n 
1 116 GLY n 
1 117 ILE n 
1 118 VAL n 
1 119 SER n 
1 120 THR n 
1 121 GLY n 
1 122 GLY n 
1 123 ASN n 
1 124 GLY n 
1 125 LEU n 
1 126 VAL n 
1 127 GLY n 
1 128 PHE n 
1 129 ALA n 
1 130 ASP n 
1 131 VAL n 
1 132 ARG n 
1 133 ASP n 
1 134 LEU n 
1 135 LEU n 
1 136 TRP n 
1 137 LEU n 
1 138 ASP n 
1 139 GLU n 
1 140 GLU n 
1 141 ALA n 
1 142 MET n 
1 143 GLU n 
1 144 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   144 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Coxsackievirus A16' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     31704 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BOQ non-polymer         . '(3S)-1-[(3-cyano-2-methoxyphenyl)acetyl]piperidine-3-carboxamide' ? 'C16 H19 N3 O3'  301.340 
ALA   'L-peptide linking' y ALANINE                                                            ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                           ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                         ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                    ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                           ? 'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                               ? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                          ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                    ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                            ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                          ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                              ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                         ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                            ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                             ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                         ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                      ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                            ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                             ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                          ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                         ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                           ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                             ? 'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION'                                                         ? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 ?   ?   ?   A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BOQ 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BOQ 
_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 A1BOQ 1   201 201 A1BOQ LIG A . 
C 3 ZN    1   202 1   ZN    ZN  A . 
D 4 DMS   1   203 6   DMS   DMS A . 
E 5 HOH   1   301 9   HOH   HOH A . 
E 5 HOH   2   302 15  HOH   HOH A . 
E 5 HOH   3   303 82  HOH   HOH A . 
E 5 HOH   4   304 99  HOH   HOH A . 
E 5 HOH   5   305 87  HOH   HOH A . 
E 5 HOH   6   306 65  HOH   HOH A . 
E 5 HOH   7   307 100 HOH   HOH A . 
E 5 HOH   8   308 24  HOH   HOH A . 
E 5 HOH   9   309 1   HOH   HOH A . 
E 5 HOH   10  310 37  HOH   HOH A . 
E 5 HOH   11  311 38  HOH   HOH A . 
E 5 HOH   12  312 11  HOH   HOH A . 
E 5 HOH   13  313 80  HOH   HOH A . 
E 5 HOH   14  314 52  HOH   HOH A . 
E 5 HOH   15  315 56  HOH   HOH A . 
E 5 HOH   16  316 102 HOH   HOH A . 
E 5 HOH   17  317 73  HOH   HOH A . 
E 5 HOH   18  318 94  HOH   HOH A . 
E 5 HOH   19  319 16  HOH   HOH A . 
E 5 HOH   20  320 63  HOH   HOH A . 
E 5 HOH   21  321 72  HOH   HOH A . 
E 5 HOH   22  322 43  HOH   HOH A . 
E 5 HOH   23  323 10  HOH   HOH A . 
E 5 HOH   24  324 29  HOH   HOH A . 
E 5 HOH   25  325 67  HOH   HOH A . 
E 5 HOH   26  326 4   HOH   HOH A . 
E 5 HOH   27  327 28  HOH   HOH A . 
E 5 HOH   28  328 62  HOH   HOH A . 
E 5 HOH   29  329 26  HOH   HOH A . 
E 5 HOH   30  330 3   HOH   HOH A . 
E 5 HOH   31  331 12  HOH   HOH A . 
E 5 HOH   32  332 25  HOH   HOH A . 
E 5 HOH   33  333 95  HOH   HOH A . 
E 5 HOH   34  334 40  HOH   HOH A . 
E 5 HOH   35  335 68  HOH   HOH A . 
E 5 HOH   36  336 76  HOH   HOH A . 
E 5 HOH   37  337 106 HOH   HOH A . 
E 5 HOH   38  338 31  HOH   HOH A . 
E 5 HOH   39  339 27  HOH   HOH A . 
E 5 HOH   40  340 101 HOH   HOH A . 
E 5 HOH   41  341 17  HOH   HOH A . 
E 5 HOH   42  342 5   HOH   HOH A . 
E 5 HOH   43  343 45  HOH   HOH A . 
E 5 HOH   44  344 58  HOH   HOH A . 
E 5 HOH   45  345 13  HOH   HOH A . 
E 5 HOH   46  346 42  HOH   HOH A . 
E 5 HOH   47  347 18  HOH   HOH A . 
E 5 HOH   48  348 74  HOH   HOH A . 
E 5 HOH   49  349 69  HOH   HOH A . 
E 5 HOH   50  350 90  HOH   HOH A . 
E 5 HOH   51  351 57  HOH   HOH A . 
E 5 HOH   52  352 34  HOH   HOH A . 
E 5 HOH   53  353 77  HOH   HOH A . 
E 5 HOH   54  354 41  HOH   HOH A . 
E 5 HOH   55  355 96  HOH   HOH A . 
E 5 HOH   56  356 50  HOH   HOH A . 
E 5 HOH   57  357 83  HOH   HOH A . 
E 5 HOH   58  358 98  HOH   HOH A . 
E 5 HOH   59  359 14  HOH   HOH A . 
E 5 HOH   60  360 8   HOH   HOH A . 
E 5 HOH   61  361 84  HOH   HOH A . 
E 5 HOH   62  362 54  HOH   HOH A . 
E 5 HOH   63  363 6   HOH   HOH A . 
E 5 HOH   64  364 53  HOH   HOH A . 
E 5 HOH   65  365 22  HOH   HOH A . 
E 5 HOH   66  366 78  HOH   HOH A . 
E 5 HOH   67  367 86  HOH   HOH A . 
E 5 HOH   68  368 70  HOH   HOH A . 
E 5 HOH   69  369 60  HOH   HOH A . 
E 5 HOH   70  370 44  HOH   HOH A . 
E 5 HOH   71  371 71  HOH   HOH A . 
E 5 HOH   72  372 75  HOH   HOH A . 
E 5 HOH   73  373 19  HOH   HOH A . 
E 5 HOH   74  374 55  HOH   HOH A . 
E 5 HOH   75  375 32  HOH   HOH A . 
E 5 HOH   76  376 91  HOH   HOH A . 
E 5 HOH   77  377 64  HOH   HOH A . 
E 5 HOH   78  378 85  HOH   HOH A . 
E 5 HOH   79  379 88  HOH   HOH A . 
E 5 HOH   80  380 33  HOH   HOH A . 
E 5 HOH   81  381 79  HOH   HOH A . 
E 5 HOH   82  382 93  HOH   HOH A . 
E 5 HOH   83  383 92  HOH   HOH A . 
E 5 HOH   84  384 59  HOH   HOH A . 
E 5 HOH   85  385 107 HOH   HOH A . 
E 5 HOH   86  386 35  HOH   HOH A . 
E 5 HOH   87  387 7   HOH   HOH A . 
E 5 HOH   88  388 89  HOH   HOH A . 
E 5 HOH   89  389 66  HOH   HOH A . 
E 5 HOH   90  390 30  HOH   HOH A . 
E 5 HOH   91  391 104 HOH   HOH A . 
E 5 HOH   92  392 20  HOH   HOH A . 
E 5 HOH   93  393 103 HOH   HOH A . 
E 5 HOH   94  394 48  HOH   HOH A . 
E 5 HOH   95  395 105 HOH   HOH A . 
E 5 HOH   96  396 51  HOH   HOH A . 
E 5 HOH   97  397 61  HOH   HOH A . 
E 5 HOH   98  398 23  HOH   HOH A . 
E 5 HOH   99  399 21  HOH   HOH A . 
E 5 HOH   100 400 97  HOH   HOH A . 
E 5 HOH   101 401 39  HOH   HOH A . 
E 5 HOH   102 402 2   HOH   HOH A . 
E 5 HOH   103 403 47  HOH   HOH A . 
E 5 HOH   104 404 81  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           7HVQ 
_cell.length_a           72.860 
_cell.length_b           61.855 
_cell.length_c           32.760 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.98 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HVQ 
_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          7HVQ 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.32 
_exptl_crystal.density_percent_sol   46.97 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-11-14 
_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   0.92201 
_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        0.92201 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HVQ 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             47.13 
_reflns.d_resolution_high            1.46 
_reflns.number_obs                   24758 
_reflns.percent_possible_obs         97.1 
_reflns.pdbx_Rmerge_I_obs            0.073 
_reflns.pdbx_netI_over_sigmaI        11.0 
_reflns.pdbx_redundancy              5.5 
_reflns.pdbx_Rrim_I_all              0.080 
_reflns.pdbx_Rpim_I_all              0.033 
_reflns.pdbx_CC_half                 0.997 
_reflns.pdbx_number_measured_all     137126 
_reflns.pdbx_chi_squared             0.75 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.46 
_reflns_shell.d_res_low                   1.53 
_reflns_shell.number_measured_all         11066 
_reflns_shell.number_unique_obs           3252 
_reflns_shell.Rmerge_I_obs                1.270 
_reflns_shell.pdbx_chi_squared            0.55 
_reflns_shell.pdbx_redundancy             3.4 
_reflns_shell.percent_possible_obs        87.8 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.8 
_reflns_shell.pdbx_Rrim_I_all             1.490 
_reflns_shell.pdbx_Rpim_I_all             0.756 
_reflns_shell.pdbx_CC_half                0.396 
_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                                 7HVQ 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     24588 
_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                             36.38 
_refine.ls_d_res_high                            1.455 
_refine.ls_percent_reflns_obs                    96.4 
_refine.ls_R_factor_obs                          0.2192 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2180 
_refine.ls_R_factor_R_free                       0.2456 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.570 
_refine.ls_number_reflns_R_free                  1124 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.958 
_refine.correlation_coeff_Fo_to_Fc_free          0.943 
_refine.B_iso_mean                               28.89 
_refine.aniso_B[1][1]                            0.55760 
_refine.aniso_B[2][2]                            -0.11680 
_refine.aniso_B[3][3]                            -0.44080 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.22030 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             0.079 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.080 
_refine.pdbx_overall_SU_R_Blow_DPI               0.081 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.081 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HVQ 
_refine_analyze.Luzzati_coordinate_error_obs    0.23 
_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         27 
_refine_hist.number_atoms_solvent             104 
_refine_hist.number_atoms_total               1205 
_refine_hist.d_res_high                       1.455 
_refine_hist.d_res_low                        36.38 
# 
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                  0.011 ? 2.00  1130 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.03  ? 2.00  1537 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  378  '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  205  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1130 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.13  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.98 ? ?     ?    '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  946  'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   51 
_refine_ls_shell.d_res_high                       1.46 
_refine_ls_shell.d_res_low                        1.47 
_refine_ls_shell.number_reflns_R_work             472 
_refine_ls_shell.R_factor_R_work                  0.3588 
_refine_ls_shell.percent_reflns_obs               79.20 
_refine_ls_shell.R_factor_R_free                  0.3177 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.07 
_refine_ls_shell.number_reflns_R_free             20 
_refine_ls_shell.number_reflns_all                492 
_refine_ls_shell.R_factor_all                     0.3572 
# 
_struct.entry_id                  7HVQ 
_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-0032627-001 (A71EV2A-x3575)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HVQ 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN, HYDROLASE
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7HVQ 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2 AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3 AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4 AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5 AA5 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P6 AA6 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.280 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.315 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.430 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.149 ? ? 
# 
_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_555 115.6 ? 
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_555 106.6 ? 
3 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 116.1 ? 
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_555 110.0 ? 
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_555 100.3 ? 
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_555 107.8 ? 
# 
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 LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O GLN A 89  ? O GLN A 95  N ILE A 76  ? N ILE A 82  
# 
_pdbx_entry_details.entry_id                   7HVQ 
_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_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OD2 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   ASP 
_pdbx_validate_close_contact.auth_seq_id_1    51 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    301 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.18 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     305 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     305 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_656 
_pdbx_validate_symm_contact.dist              1.00 
# 
_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         15.0938 
_pdbx_refine_tls.origin_y         7.1525 
_pdbx_refine_tls.origin_z         14.3071 
_pdbx_refine_tls.T[1][1]          0.0026 
_pdbx_refine_tls.T[2][2]          -0.0560 
_pdbx_refine_tls.T[3][3]          -0.0409 
_pdbx_refine_tls.T[1][2]          0.0072 
_pdbx_refine_tls.T[1][3]          -0.0053 
_pdbx_refine_tls.T[2][3]          -0.0124 
_pdbx_refine_tls.L[1][1]          1.1415 
_pdbx_refine_tls.L[2][2]          7.8177 
_pdbx_refine_tls.L[3][3]          0.6754 
_pdbx_refine_tls.L[1][2]          2.5993 
_pdbx_refine_tls.L[1][3]          -0.7358 
_pdbx_refine_tls.L[2][3]          -2.4548 
_pdbx_refine_tls.S[1][1]          -0.0930 
_pdbx_refine_tls.S[1][2]          0.1028 
_pdbx_refine_tls.S[1][3]          0.0026 
_pdbx_refine_tls.S[2][1]          0.3562 
_pdbx_refine_tls.S[2][2]          0.1564 
_pdbx_refine_tls.S[2][3]          -0.2652 
_pdbx_refine_tls.S[3][1]          -0.0638 
_pdbx_refine_tls.S[3][2]          -0.1653 
_pdbx_refine_tls.S[3][3]          -0.0634 
# 
_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 
A1BOQ N1   N  N N 1   
A1BOQ C4   C  Y N 2   
A1BOQ C5   C  Y N 3   
A1BOQ C6   C  Y N 4   
A1BOQ C7   C  Y N 5   
A1BOQ C8   C  N N 6   
A1BOQ C10  C  N N 7   
A1BOQ C13  C  N S 8   
A1BOQ C15  C  N N 9   
A1BOQ O2   O  N N 10  
A1BOQ C14  C  N N 11  
A1BOQ N2   N  N N 12  
A1BOQ C12  C  N N 13  
A1BOQ C11  C  N N 14  
A1BOQ C9   C  N N 15  
A1BOQ O1   O  N N 16  
A1BOQ C1   C  Y N 17  
A1BOQ O    O  N N 18  
A1BOQ C    C  N N 19  
A1BOQ C2   C  Y N 20  
A1BOQ C3   C  N N 21  
A1BOQ N    N  N N 22  
A1BOQ H4   H  N N 23  
A1BOQ H5   H  N N 24  
A1BOQ H6   H  N N 25  
A1BOQ H7   H  N N 26  
A1BOQ H8   H  N N 27  
A1BOQ H10  H  N N 28  
A1BOQ H9   H  N N 29  
A1BOQ H    H  N N 30  
A1BOQ H17  H  N N 31  
A1BOQ H18  H  N N 32  
A1BOQ H16  H  N N 33  
A1BOQ H15  H  N N 34  
A1BOQ H13  H  N N 35  
A1BOQ H14  H  N N 36  
A1BOQ H11  H  N N 37  
A1BOQ H12  H  N N 38  
A1BOQ H3   H  N N 39  
A1BOQ H2   H  N N 40  
A1BOQ H1   H  N N 41  
ALA   N    N  N N 42  
ALA   CA   C  N S 43  
ALA   C    C  N N 44  
ALA   O    O  N N 45  
ALA   CB   C  N N 46  
ALA   OXT  O  N N 47  
ALA   H    H  N N 48  
ALA   H2   H  N N 49  
ALA   HA   H  N N 50  
ALA   HB1  H  N N 51  
ALA   HB2  H  N N 52  
ALA   HB3  H  N N 53  
ALA   HXT  H  N N 54  
ARG   N    N  N N 55  
ARG   CA   C  N S 56  
ARG   C    C  N N 57  
ARG   O    O  N N 58  
ARG   CB   C  N N 59  
ARG   CG   C  N N 60  
ARG   CD   C  N N 61  
ARG   NE   N  N N 62  
ARG   CZ   C  N N 63  
ARG   NH1  N  N N 64  
ARG   NH2  N  N N 65  
ARG   OXT  O  N N 66  
ARG   H    H  N N 67  
ARG   H2   H  N N 68  
ARG   HA   H  N N 69  
ARG   HB2  H  N N 70  
ARG   HB3  H  N N 71  
ARG   HG2  H  N N 72  
ARG   HG3  H  N N 73  
ARG   HD2  H  N N 74  
ARG   HD3  H  N N 75  
ARG   HE   H  N N 76  
ARG   HH11 H  N N 77  
ARG   HH12 H  N N 78  
ARG   HH21 H  N N 79  
ARG   HH22 H  N N 80  
ARG   HXT  H  N N 81  
ASN   N    N  N N 82  
ASN   CA   C  N S 83  
ASN   C    C  N N 84  
ASN   O    O  N N 85  
ASN   CB   C  N N 86  
ASN   CG   C  N N 87  
ASN   OD1  O  N N 88  
ASN   ND2  N  N N 89  
ASN   OXT  O  N N 90  
ASN   H    H  N N 91  
ASN   H2   H  N N 92  
ASN   HA   H  N N 93  
ASN   HB2  H  N N 94  
ASN   HB3  H  N N 95  
ASN   HD21 H  N N 96  
ASN   HD22 H  N N 97  
ASN   HXT  H  N N 98  
ASP   N    N  N N 99  
ASP   CA   C  N S 100 
ASP   C    C  N N 101 
ASP   O    O  N N 102 
ASP   CB   C  N N 103 
ASP   CG   C  N N 104 
ASP   OD1  O  N N 105 
ASP   OD2  O  N N 106 
ASP   OXT  O  N N 107 
ASP   H    H  N N 108 
ASP   H2   H  N N 109 
ASP   HA   H  N N 110 
ASP   HB2  H  N N 111 
ASP   HB3  H  N N 112 
ASP   HD2  H  N N 113 
ASP   HXT  H  N N 114 
CYS   N    N  N N 115 
CYS   CA   C  N R 116 
CYS   C    C  N N 117 
CYS   O    O  N N 118 
CYS   CB   C  N N 119 
CYS   SG   S  N N 120 
CYS   OXT  O  N N 121 
CYS   H    H  N N 122 
CYS   H2   H  N N 123 
CYS   HA   H  N N 124 
CYS   HB2  H  N N 125 
CYS   HB3  H  N N 126 
CYS   HG   H  N N 127 
CYS   HXT  H  N N 128 
DMS   S    S  N N 129 
DMS   O    O  N N 130 
DMS   C1   C  N N 131 
DMS   C2   C  N N 132 
DMS   H11  H  N N 133 
DMS   H12  H  N N 134 
DMS   H13  H  N N 135 
DMS   H21  H  N N 136 
DMS   H22  H  N N 137 
DMS   H23  H  N N 138 
GLN   N    N  N N 139 
GLN   CA   C  N S 140 
GLN   C    C  N N 141 
GLN   O    O  N N 142 
GLN   CB   C  N N 143 
GLN   CG   C  N N 144 
GLN   CD   C  N N 145 
GLN   OE1  O  N N 146 
GLN   NE2  N  N N 147 
GLN   OXT  O  N N 148 
GLN   H    H  N N 149 
GLN   H2   H  N N 150 
GLN   HA   H  N N 151 
GLN   HB2  H  N N 152 
GLN   HB3  H  N N 153 
GLN   HG2  H  N N 154 
GLN   HG3  H  N N 155 
GLN   HE21 H  N N 156 
GLN   HE22 H  N N 157 
GLN   HXT  H  N N 158 
GLU   N    N  N N 159 
GLU   CA   C  N S 160 
GLU   C    C  N N 161 
GLU   O    O  N N 162 
GLU   CB   C  N N 163 
GLU   CG   C  N N 164 
GLU   CD   C  N N 165 
GLU   OE1  O  N N 166 
GLU   OE2  O  N N 167 
GLU   OXT  O  N N 168 
GLU   H    H  N N 169 
GLU   H2   H  N N 170 
GLU   HA   H  N N 171 
GLU   HB2  H  N N 172 
GLU   HB3  H  N N 173 
GLU   HG2  H  N N 174 
GLU   HG3  H  N N 175 
GLU   HE2  H  N N 176 
GLU   HXT  H  N N 177 
GLY   N    N  N N 178 
GLY   CA   C  N N 179 
GLY   C    C  N N 180 
GLY   O    O  N N 181 
GLY   OXT  O  N N 182 
GLY   H    H  N N 183 
GLY   H2   H  N N 184 
GLY   HA2  H  N N 185 
GLY   HA3  H  N N 186 
GLY   HXT  H  N N 187 
HIS   N    N  N N 188 
HIS   CA   C  N S 189 
HIS   C    C  N N 190 
HIS   O    O  N N 191 
HIS   CB   C  N N 192 
HIS   CG   C  Y N 193 
HIS   ND1  N  Y N 194 
HIS   CD2  C  Y N 195 
HIS   CE1  C  Y N 196 
HIS   NE2  N  Y N 197 
HIS   OXT  O  N N 198 
HIS   H    H  N N 199 
HIS   H2   H  N N 200 
HIS   HA   H  N N 201 
HIS   HB2  H  N N 202 
HIS   HB3  H  N N 203 
HIS   HD1  H  N N 204 
HIS   HD2  H  N N 205 
HIS   HE1  H  N N 206 
HIS   HE2  H  N N 207 
HIS   HXT  H  N N 208 
HOH   O    O  N N 209 
HOH   H1   H  N N 210 
HOH   H2   H  N N 211 
ILE   N    N  N N 212 
ILE   CA   C  N S 213 
ILE   C    C  N N 214 
ILE   O    O  N N 215 
ILE   CB   C  N S 216 
ILE   CG1  C  N N 217 
ILE   CG2  C  N N 218 
ILE   CD1  C  N N 219 
ILE   OXT  O  N N 220 
ILE   H    H  N N 221 
ILE   H2   H  N N 222 
ILE   HA   H  N N 223 
ILE   HB   H  N N 224 
ILE   HG12 H  N N 225 
ILE   HG13 H  N N 226 
ILE   HG21 H  N N 227 
ILE   HG22 H  N N 228 
ILE   HG23 H  N N 229 
ILE   HD11 H  N N 230 
ILE   HD12 H  N N 231 
ILE   HD13 H  N N 232 
ILE   HXT  H  N N 233 
LEU   N    N  N N 234 
LEU   CA   C  N S 235 
LEU   C    C  N N 236 
LEU   O    O  N N 237 
LEU   CB   C  N N 238 
LEU   CG   C  N N 239 
LEU   CD1  C  N N 240 
LEU   CD2  C  N N 241 
LEU   OXT  O  N N 242 
LEU   H    H  N N 243 
LEU   H2   H  N N 244 
LEU   HA   H  N N 245 
LEU   HB2  H  N N 246 
LEU   HB3  H  N N 247 
LEU   HG   H  N N 248 
LEU   HD11 H  N N 249 
LEU   HD12 H  N N 250 
LEU   HD13 H  N N 251 
LEU   HD21 H  N N 252 
LEU   HD22 H  N N 253 
LEU   HD23 H  N N 254 
LEU   HXT  H  N N 255 
LYS   N    N  N N 256 
LYS   CA   C  N S 257 
LYS   C    C  N N 258 
LYS   O    O  N N 259 
LYS   CB   C  N N 260 
LYS   CG   C  N N 261 
LYS   CD   C  N N 262 
LYS   CE   C  N N 263 
LYS   NZ   N  N N 264 
LYS   OXT  O  N N 265 
LYS   H    H  N N 266 
LYS   H2   H  N N 267 
LYS   HA   H  N N 268 
LYS   HB2  H  N N 269 
LYS   HB3  H  N N 270 
LYS   HG2  H  N N 271 
LYS   HG3  H  N N 272 
LYS   HD2  H  N N 273 
LYS   HD3  H  N N 274 
LYS   HE2  H  N N 275 
LYS   HE3  H  N N 276 
LYS   HZ1  H  N N 277 
LYS   HZ2  H  N N 278 
LYS   HZ3  H  N N 279 
LYS   HXT  H  N N 280 
MET   N    N  N N 281 
MET   CA   C  N S 282 
MET   C    C  N N 283 
MET   O    O  N N 284 
MET   CB   C  N N 285 
MET   CG   C  N N 286 
MET   SD   S  N N 287 
MET   CE   C  N N 288 
MET   OXT  O  N N 289 
MET   H    H  N N 290 
MET   H2   H  N N 291 
MET   HA   H  N N 292 
MET   HB2  H  N N 293 
MET   HB3  H  N N 294 
MET   HG2  H  N N 295 
MET   HG3  H  N N 296 
MET   HE1  H  N N 297 
MET   HE2  H  N N 298 
MET   HE3  H  N N 299 
MET   HXT  H  N N 300 
PHE   N    N  N N 301 
PHE   CA   C  N S 302 
PHE   C    C  N N 303 
PHE   O    O  N N 304 
PHE   CB   C  N N 305 
PHE   CG   C  Y N 306 
PHE   CD1  C  Y N 307 
PHE   CD2  C  Y N 308 
PHE   CE1  C  Y N 309 
PHE   CE2  C  Y N 310 
PHE   CZ   C  Y N 311 
PHE   OXT  O  N N 312 
PHE   H    H  N N 313 
PHE   H2   H  N N 314 
PHE   HA   H  N N 315 
PHE   HB2  H  N N 316 
PHE   HB3  H  N N 317 
PHE   HD1  H  N N 318 
PHE   HD2  H  N N 319 
PHE   HE1  H  N N 320 
PHE   HE2  H  N N 321 
PHE   HZ   H  N N 322 
PHE   HXT  H  N N 323 
PRO   N    N  N N 324 
PRO   CA   C  N S 325 
PRO   C    C  N N 326 
PRO   O    O  N N 327 
PRO   CB   C  N N 328 
PRO   CG   C  N N 329 
PRO   CD   C  N N 330 
PRO   OXT  O  N N 331 
PRO   H    H  N N 332 
PRO   HA   H  N N 333 
PRO   HB2  H  N N 334 
PRO   HB3  H  N N 335 
PRO   HG2  H  N N 336 
PRO   HG3  H  N N 337 
PRO   HD2  H  N N 338 
PRO   HD3  H  N N 339 
PRO   HXT  H  N N 340 
SER   N    N  N N 341 
SER   CA   C  N S 342 
SER   C    C  N N 343 
SER   O    O  N N 344 
SER   CB   C  N N 345 
SER   OG   O  N N 346 
SER   OXT  O  N N 347 
SER   H    H  N N 348 
SER   H2   H  N N 349 
SER   HA   H  N N 350 
SER   HB2  H  N N 351 
SER   HB3  H  N N 352 
SER   HG   H  N N 353 
SER   HXT  H  N N 354 
THR   N    N  N N 355 
THR   CA   C  N S 356 
THR   C    C  N N 357 
THR   O    O  N N 358 
THR   CB   C  N R 359 
THR   OG1  O  N N 360 
THR   CG2  C  N N 361 
THR   OXT  O  N N 362 
THR   H    H  N N 363 
THR   H2   H  N N 364 
THR   HA   H  N N 365 
THR   HB   H  N N 366 
THR   HG1  H  N N 367 
THR   HG21 H  N N 368 
THR   HG22 H  N N 369 
THR   HG23 H  N N 370 
THR   HXT  H  N N 371 
TRP   N    N  N N 372 
TRP   CA   C  N S 373 
TRP   C    C  N N 374 
TRP   O    O  N N 375 
TRP   CB   C  N N 376 
TRP   CG   C  Y N 377 
TRP   CD1  C  Y N 378 
TRP   CD2  C  Y N 379 
TRP   NE1  N  Y N 380 
TRP   CE2  C  Y N 381 
TRP   CE3  C  Y N 382 
TRP   CZ2  C  Y N 383 
TRP   CZ3  C  Y N 384 
TRP   CH2  C  Y N 385 
TRP   OXT  O  N N 386 
TRP   H    H  N N 387 
TRP   H2   H  N N 388 
TRP   HA   H  N N 389 
TRP   HB2  H  N N 390 
TRP   HB3  H  N N 391 
TRP   HD1  H  N N 392 
TRP   HE1  H  N N 393 
TRP   HE3  H  N N 394 
TRP   HZ2  H  N N 395 
TRP   HZ3  H  N N 396 
TRP   HH2  H  N N 397 
TRP   HXT  H  N N 398 
TYR   N    N  N N 399 
TYR   CA   C  N S 400 
TYR   C    C  N N 401 
TYR   O    O  N N 402 
TYR   CB   C  N N 403 
TYR   CG   C  Y N 404 
TYR   CD1  C  Y N 405 
TYR   CD2  C  Y N 406 
TYR   CE1  C  Y N 407 
TYR   CE2  C  Y N 408 
TYR   CZ   C  Y N 409 
TYR   OH   O  N N 410 
TYR   OXT  O  N N 411 
TYR   H    H  N N 412 
TYR   H2   H  N N 413 
TYR   HA   H  N N 414 
TYR   HB2  H  N N 415 
TYR   HB3  H  N N 416 
TYR   HD1  H  N N 417 
TYR   HD2  H  N N 418 
TYR   HE1  H  N N 419 
TYR   HE2  H  N N 420 
TYR   HH   H  N N 421 
TYR   HXT  H  N N 422 
VAL   N    N  N N 423 
VAL   CA   C  N S 424 
VAL   C    C  N N 425 
VAL   O    O  N N 426 
VAL   CB   C  N N 427 
VAL   CG1  C  N N 428 
VAL   CG2  C  N N 429 
VAL   OXT  O  N N 430 
VAL   H    H  N N 431 
VAL   H2   H  N N 432 
VAL   HA   H  N N 433 
VAL   HB   H  N N 434 
VAL   HG11 H  N N 435 
VAL   HG12 H  N N 436 
VAL   HG13 H  N N 437 
VAL   HG21 H  N N 438 
VAL   HG22 H  N N 439 
VAL   HG23 H  N N 440 
VAL   HXT  H  N N 441 
ZN    ZN   ZN N N 442 
# 
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 
A1BOQ C   O    sing N N 1   
A1BOQ O   C1   sing N N 2   
A1BOQ C1  C2   doub Y N 3   
A1BOQ C3  C2   sing N N 4   
A1BOQ N   C3   trip N N 5   
A1BOQ C2  C4   sing Y N 6   
A1BOQ C4  C5   doub Y N 7   
A1BOQ C5  C6   sing Y N 8   
A1BOQ C6  C7   doub Y N 9   
A1BOQ C1  C7   sing Y N 10  
A1BOQ C7  C8   sing N N 11  
A1BOQ C8  C9   sing N N 12  
A1BOQ O1  C9   doub N N 13  
A1BOQ C9  N1   sing N N 14  
A1BOQ N1  C10  sing N N 15  
A1BOQ C10 C11  sing N N 16  
A1BOQ C11 C12  sing N N 17  
A1BOQ C12 C13  sing N N 18  
A1BOQ C13 C14  sing N N 19  
A1BOQ N2  C14  sing N N 20  
A1BOQ C14 O2   doub N N 21  
A1BOQ C15 C13  sing N N 22  
A1BOQ N1  C15  sing N N 23  
A1BOQ C4  H4   sing N N 24  
A1BOQ C5  H5   sing N N 25  
A1BOQ C6  H6   sing N N 26  
A1BOQ C8  H7   sing N N 27  
A1BOQ C8  H8   sing N N 28  
A1BOQ C10 H10  sing N N 29  
A1BOQ C10 H9   sing N N 30  
A1BOQ C13 H    sing N N 31  
A1BOQ C15 H17  sing N N 32  
A1BOQ C15 H18  sing N N 33  
A1BOQ N2  H16  sing N N 34  
A1BOQ N2  H15  sing N N 35  
A1BOQ C12 H13  sing N N 36  
A1BOQ C12 H14  sing N N 37  
A1BOQ C11 H11  sing N N 38  
A1BOQ C11 H12  sing N N 39  
A1BOQ C   H3   sing N N 40  
A1BOQ C   H2   sing N N 41  
A1BOQ C   H1   sing N N 42  
ALA   N   CA   sing N N 43  
ALA   N   H    sing N N 44  
ALA   N   H2   sing N N 45  
ALA   CA  C    sing N N 46  
ALA   CA  CB   sing N N 47  
ALA   CA  HA   sing N N 48  
ALA   C   O    doub N N 49  
ALA   C   OXT  sing N N 50  
ALA   CB  HB1  sing N N 51  
ALA   CB  HB2  sing N N 52  
ALA   CB  HB3  sing N N 53  
ALA   OXT HXT  sing N N 54  
ARG   N   CA   sing N N 55  
ARG   N   H    sing N N 56  
ARG   N   H2   sing N N 57  
ARG   CA  C    sing N N 58  
ARG   CA  CB   sing N N 59  
ARG   CA  HA   sing N N 60  
ARG   C   O    doub N N 61  
ARG   C   OXT  sing N N 62  
ARG   CB  CG   sing N N 63  
ARG   CB  HB2  sing N N 64  
ARG   CB  HB3  sing N N 65  
ARG   CG  CD   sing N N 66  
ARG   CG  HG2  sing N N 67  
ARG   CG  HG3  sing N N 68  
ARG   CD  NE   sing N N 69  
ARG   CD  HD2  sing N N 70  
ARG   CD  HD3  sing N N 71  
ARG   NE  CZ   sing N N 72  
ARG   NE  HE   sing N N 73  
ARG   CZ  NH1  sing N N 74  
ARG   CZ  NH2  doub N N 75  
ARG   NH1 HH11 sing N N 76  
ARG   NH1 HH12 sing N N 77  
ARG   NH2 HH21 sing N N 78  
ARG   NH2 HH22 sing N N 79  
ARG   OXT HXT  sing N N 80  
ASN   N   CA   sing N N 81  
ASN   N   H    sing N N 82  
ASN   N   H2   sing N N 83  
ASN   CA  C    sing N N 84  
ASN   CA  CB   sing N N 85  
ASN   CA  HA   sing N N 86  
ASN   C   O    doub N N 87  
ASN   C   OXT  sing N N 88  
ASN   CB  CG   sing N N 89  
ASN   CB  HB2  sing N N 90  
ASN   CB  HB3  sing N N 91  
ASN   CG  OD1  doub N N 92  
ASN   CG  ND2  sing N N 93  
ASN   ND2 HD21 sing N N 94  
ASN   ND2 HD22 sing N N 95  
ASN   OXT HXT  sing N N 96  
ASP   N   CA   sing N N 97  
ASP   N   H    sing N N 98  
ASP   N   H2   sing N N 99  
ASP   CA  C    sing N N 100 
ASP   CA  CB   sing N N 101 
ASP   CA  HA   sing N N 102 
ASP   C   O    doub N N 103 
ASP   C   OXT  sing N N 104 
ASP   CB  CG   sing N N 105 
ASP   CB  HB2  sing N N 106 
ASP   CB  HB3  sing N N 107 
ASP   CG  OD1  doub N N 108 
ASP   CG  OD2  sing N N 109 
ASP   OD2 HD2  sing N N 110 
ASP   OXT HXT  sing N N 111 
CYS   N   CA   sing N N 112 
CYS   N   H    sing N N 113 
CYS   N   H2   sing N N 114 
CYS   CA  C    sing N N 115 
CYS   CA  CB   sing N N 116 
CYS   CA  HA   sing N N 117 
CYS   C   O    doub N N 118 
CYS   C   OXT  sing N N 119 
CYS   CB  SG   sing N N 120 
CYS   CB  HB2  sing N N 121 
CYS   CB  HB3  sing N N 122 
CYS   SG  HG   sing N N 123 
CYS   OXT HXT  sing N N 124 
DMS   S   O    doub N N 125 
DMS   S   C1   sing N N 126 
DMS   S   C2   sing N N 127 
DMS   C1  H11  sing N N 128 
DMS   C1  H12  sing N N 129 
DMS   C1  H13  sing N N 130 
DMS   C2  H21  sing N N 131 
DMS   C2  H22  sing N N 132 
DMS   C2  H23  sing N N 133 
GLN   N   CA   sing N N 134 
GLN   N   H    sing N N 135 
GLN   N   H2   sing N N 136 
GLN   CA  C    sing N N 137 
GLN   CA  CB   sing N N 138 
GLN   CA  HA   sing N N 139 
GLN   C   O    doub N N 140 
GLN   C   OXT  sing N N 141 
GLN   CB  CG   sing N N 142 
GLN   CB  HB2  sing N N 143 
GLN   CB  HB3  sing N N 144 
GLN   CG  CD   sing N N 145 
GLN   CG  HG2  sing N N 146 
GLN   CG  HG3  sing N N 147 
GLN   CD  OE1  doub N N 148 
GLN   CD  NE2  sing N N 149 
GLN   NE2 HE21 sing N N 150 
GLN   NE2 HE22 sing N N 151 
GLN   OXT HXT  sing N N 152 
GLU   N   CA   sing N N 153 
GLU   N   H    sing N N 154 
GLU   N   H2   sing N N 155 
GLU   CA  C    sing N N 156 
GLU   CA  CB   sing N N 157 
GLU   CA  HA   sing N N 158 
GLU   C   O    doub N N 159 
GLU   C   OXT  sing N N 160 
GLU   CB  CG   sing N N 161 
GLU   CB  HB2  sing N N 162 
GLU   CB  HB3  sing N N 163 
GLU   CG  CD   sing N N 164 
GLU   CG  HG2  sing N N 165 
GLU   CG  HG3  sing N N 166 
GLU   CD  OE1  doub N N 167 
GLU   CD  OE2  sing N N 168 
GLU   OE2 HE2  sing N N 169 
GLU   OXT HXT  sing N N 170 
GLY   N   CA   sing N N 171 
GLY   N   H    sing N N 172 
GLY   N   H2   sing N N 173 
GLY   CA  C    sing N N 174 
GLY   CA  HA2  sing N N 175 
GLY   CA  HA3  sing N N 176 
GLY   C   O    doub N N 177 
GLY   C   OXT  sing N N 178 
GLY   OXT HXT  sing N N 179 
HIS   N   CA   sing N N 180 
HIS   N   H    sing N N 181 
HIS   N   H2   sing N N 182 
HIS   CA  C    sing N N 183 
HIS   CA  CB   sing N N 184 
HIS   CA  HA   sing N N 185 
HIS   C   O    doub N N 186 
HIS   C   OXT  sing N N 187 
HIS   CB  CG   sing N N 188 
HIS   CB  HB2  sing N N 189 
HIS   CB  HB3  sing N N 190 
HIS   CG  ND1  sing Y N 191 
HIS   CG  CD2  doub Y N 192 
HIS   ND1 CE1  doub Y N 193 
HIS   ND1 HD1  sing N N 194 
HIS   CD2 NE2  sing Y N 195 
HIS   CD2 HD2  sing N N 196 
HIS   CE1 NE2  sing Y N 197 
HIS   CE1 HE1  sing N N 198 
HIS   NE2 HE2  sing N N 199 
HIS   OXT HXT  sing N N 200 
HOH   O   H1   sing N N 201 
HOH   O   H2   sing N N 202 
ILE   N   CA   sing N N 203 
ILE   N   H    sing N N 204 
ILE   N   H2   sing N N 205 
ILE   CA  C    sing N N 206 
ILE   CA  CB   sing N N 207 
ILE   CA  HA   sing N N 208 
ILE   C   O    doub N N 209 
ILE   C   OXT  sing N N 210 
ILE   CB  CG1  sing N N 211 
ILE   CB  CG2  sing N N 212 
ILE   CB  HB   sing N N 213 
ILE   CG1 CD1  sing N N 214 
ILE   CG1 HG12 sing N N 215 
ILE   CG1 HG13 sing N N 216 
ILE   CG2 HG21 sing N N 217 
ILE   CG2 HG22 sing N N 218 
ILE   CG2 HG23 sing N N 219 
ILE   CD1 HD11 sing N N 220 
ILE   CD1 HD12 sing N N 221 
ILE   CD1 HD13 sing N N 222 
ILE   OXT HXT  sing N N 223 
LEU   N   CA   sing N N 224 
LEU   N   H    sing N N 225 
LEU   N   H2   sing N N 226 
LEU   CA  C    sing N N 227 
LEU   CA  CB   sing N N 228 
LEU   CA  HA   sing N N 229 
LEU   C   O    doub N N 230 
LEU   C   OXT  sing N N 231 
LEU   CB  CG   sing N N 232 
LEU   CB  HB2  sing N N 233 
LEU   CB  HB3  sing N N 234 
LEU   CG  CD1  sing N N 235 
LEU   CG  CD2  sing N N 236 
LEU   CG  HG   sing N N 237 
LEU   CD1 HD11 sing N N 238 
LEU   CD1 HD12 sing N N 239 
LEU   CD1 HD13 sing N N 240 
LEU   CD2 HD21 sing N N 241 
LEU   CD2 HD22 sing N N 242 
LEU   CD2 HD23 sing N N 243 
LEU   OXT HXT  sing N N 244 
LYS   N   CA   sing N N 245 
LYS   N   H    sing N N 246 
LYS   N   H2   sing N N 247 
LYS   CA  C    sing N N 248 
LYS   CA  CB   sing N N 249 
LYS   CA  HA   sing N N 250 
LYS   C   O    doub N N 251 
LYS   C   OXT  sing N N 252 
LYS   CB  CG   sing N N 253 
LYS   CB  HB2  sing N N 254 
LYS   CB  HB3  sing N N 255 
LYS   CG  CD   sing N N 256 
LYS   CG  HG2  sing N N 257 
LYS   CG  HG3  sing N N 258 
LYS   CD  CE   sing N N 259 
LYS   CD  HD2  sing N N 260 
LYS   CD  HD3  sing N N 261 
LYS   CE  NZ   sing N N 262 
LYS   CE  HE2  sing N N 263 
LYS   CE  HE3  sing N N 264 
LYS   NZ  HZ1  sing N N 265 
LYS   NZ  HZ2  sing N N 266 
LYS   NZ  HZ3  sing N N 267 
LYS   OXT HXT  sing N N 268 
MET   N   CA   sing N N 269 
MET   N   H    sing N N 270 
MET   N   H2   sing N N 271 
MET   CA  C    sing N N 272 
MET   CA  CB   sing N N 273 
MET   CA  HA   sing N N 274 
MET   C   O    doub N N 275 
MET   C   OXT  sing N N 276 
MET   CB  CG   sing N N 277 
MET   CB  HB2  sing N N 278 
MET   CB  HB3  sing N N 279 
MET   CG  SD   sing N N 280 
MET   CG  HG2  sing N N 281 
MET   CG  HG3  sing N N 282 
MET   SD  CE   sing N N 283 
MET   CE  HE1  sing N N 284 
MET   CE  HE2  sing N N 285 
MET   CE  HE3  sing N N 286 
MET   OXT HXT  sing N N 287 
PHE   N   CA   sing N N 288 
PHE   N   H    sing N N 289 
PHE   N   H2   sing N N 290 
PHE   CA  C    sing N N 291 
PHE   CA  CB   sing N N 292 
PHE   CA  HA   sing N N 293 
PHE   C   O    doub N N 294 
PHE   C   OXT  sing N N 295 
PHE   CB  CG   sing N N 296 
PHE   CB  HB2  sing N N 297 
PHE   CB  HB3  sing N N 298 
PHE   CG  CD1  doub Y N 299 
PHE   CG  CD2  sing Y N 300 
PHE   CD1 CE1  sing Y N 301 
PHE   CD1 HD1  sing N N 302 
PHE   CD2 CE2  doub Y N 303 
PHE   CD2 HD2  sing N N 304 
PHE   CE1 CZ   doub Y N 305 
PHE   CE1 HE1  sing N N 306 
PHE   CE2 CZ   sing Y N 307 
PHE   CE2 HE2  sing N N 308 
PHE   CZ  HZ   sing N N 309 
PHE   OXT HXT  sing N N 310 
PRO   N   CA   sing N N 311 
PRO   N   CD   sing N N 312 
PRO   N   H    sing N N 313 
PRO   CA  C    sing N N 314 
PRO   CA  CB   sing N N 315 
PRO   CA  HA   sing N N 316 
PRO   C   O    doub N N 317 
PRO   C   OXT  sing N N 318 
PRO   CB  CG   sing N N 319 
PRO   CB  HB2  sing N N 320 
PRO   CB  HB3  sing N N 321 
PRO   CG  CD   sing N N 322 
PRO   CG  HG2  sing N N 323 
PRO   CG  HG3  sing N N 324 
PRO   CD  HD2  sing N N 325 
PRO   CD  HD3  sing N N 326 
PRO   OXT HXT  sing N N 327 
SER   N   CA   sing N N 328 
SER   N   H    sing N N 329 
SER   N   H2   sing N N 330 
SER   CA  C    sing N N 331 
SER   CA  CB   sing N N 332 
SER   CA  HA   sing N N 333 
SER   C   O    doub N N 334 
SER   C   OXT  sing N N 335 
SER   CB  OG   sing N N 336 
SER   CB  HB2  sing N N 337 
SER   CB  HB3  sing N N 338 
SER   OG  HG   sing N N 339 
SER   OXT HXT  sing N N 340 
THR   N   CA   sing N N 341 
THR   N   H    sing N N 342 
THR   N   H2   sing N N 343 
THR   CA  C    sing N N 344 
THR   CA  CB   sing N N 345 
THR   CA  HA   sing N N 346 
THR   C   O    doub N N 347 
THR   C   OXT  sing N N 348 
THR   CB  OG1  sing N N 349 
THR   CB  CG2  sing N N 350 
THR   CB  HB   sing N N 351 
THR   OG1 HG1  sing N N 352 
THR   CG2 HG21 sing N N 353 
THR   CG2 HG22 sing N N 354 
THR   CG2 HG23 sing N N 355 
THR   OXT HXT  sing N N 356 
TRP   N   CA   sing N N 357 
TRP   N   H    sing N N 358 
TRP   N   H2   sing N N 359 
TRP   CA  C    sing N N 360 
TRP   CA  CB   sing N N 361 
TRP   CA  HA   sing N N 362 
TRP   C   O    doub N N 363 
TRP   C   OXT  sing N N 364 
TRP   CB  CG   sing N N 365 
TRP   CB  HB2  sing N N 366 
TRP   CB  HB3  sing N N 367 
TRP   CG  CD1  doub Y N 368 
TRP   CG  CD2  sing Y N 369 
TRP   CD1 NE1  sing Y N 370 
TRP   CD1 HD1  sing N N 371 
TRP   CD2 CE2  doub Y N 372 
TRP   CD2 CE3  sing Y N 373 
TRP   NE1 CE2  sing Y N 374 
TRP   NE1 HE1  sing N N 375 
TRP   CE2 CZ2  sing Y N 376 
TRP   CE3 CZ3  doub Y N 377 
TRP   CE3 HE3  sing N N 378 
TRP   CZ2 CH2  doub Y N 379 
TRP   CZ2 HZ2  sing N N 380 
TRP   CZ3 CH2  sing Y N 381 
TRP   CZ3 HZ3  sing N N 382 
TRP   CH2 HH2  sing N N 383 
TRP   OXT HXT  sing N N 384 
TYR   N   CA   sing N N 385 
TYR   N   H    sing N N 386 
TYR   N   H2   sing N N 387 
TYR   CA  C    sing N N 388 
TYR   CA  CB   sing N N 389 
TYR   CA  HA   sing N N 390 
TYR   C   O    doub N N 391 
TYR   C   OXT  sing N N 392 
TYR   CB  CG   sing N N 393 
TYR   CB  HB2  sing N N 394 
TYR   CB  HB3  sing N N 395 
TYR   CG  CD1  doub Y N 396 
TYR   CG  CD2  sing Y N 397 
TYR   CD1 CE1  sing Y N 398 
TYR   CD1 HD1  sing N N 399 
TYR   CD2 CE2  doub Y N 400 
TYR   CD2 HD2  sing N N 401 
TYR   CE1 CZ   doub Y N 402 
TYR   CE1 HE1  sing N N 403 
TYR   CE2 CZ   sing Y N 404 
TYR   CE2 HE2  sing N N 405 
TYR   CZ  OH   sing N N 406 
TYR   OH  HH   sing N N 407 
TYR   OXT HXT  sing N N 408 
VAL   N   CA   sing N N 409 
VAL   N   H    sing N N 410 
VAL   N   H2   sing N N 411 
VAL   CA  C    sing N N 412 
VAL   CA  CB   sing N N 413 
VAL   CA  HA   sing N N 414 
VAL   C   O    doub N N 415 
VAL   C   OXT  sing N N 416 
VAL   CB  CG1  sing N N 417 
VAL   CB  CG2  sing N N 418 
VAL   CB  HB   sing N N 419 
VAL   CG1 HG11 sing N N 420 
VAL   CG1 HG12 sing N N 421 
VAL   CG1 HG13 sing N N 422 
VAL   CG2 HG21 sing N N 423 
VAL   CG2 HG22 sing N N 424 
VAL   CG2 HG23 sing N N 425 
VAL   OXT HXT  sing N N 426 
# 
_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                    7HVQ 
_atom_sites.fract_transf_matrix[1][1]   0.013725 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000714 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016167 
_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]   0.030566 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 18.804 6.701   24.306 1.00 31.63 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.014 6.782   23.491 1.00 32.51 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.114 5.608   22.492 1.00 30.70 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.469 4.563   22.685 1.00 30.73 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.250 6.824   24.393 1.00 35.93 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.374 5.562   25.030 1.00 40.56 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.936 5.794   21.456 1.00 28.63 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.175 4.787   20.432 1.00 27.34 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.444 5.332   19.038 1.00 25.62 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.060 6.458   18.699 1.00 25.89 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.119 4.543   18.222 1.00 23.38 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.493 4.943   16.876 1.00 23.00 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.519 3.768   15.908 1.00 22.26 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.586 2.619   16.341 1.00 22.50 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.889 5.577   16.933 1.00 24.76 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.515 4.062   14.593 1.00 21.63 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.694 3.089   13.514 1.00 21.72 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.105 3.336   12.920 1.00 23.84 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.454 4.475   12.648 1.00 23.73 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.640 3.323   12.404 1.00 22.15 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.221 3.336   12.992 1.00 21.72 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.781 2.264   11.293 1.00 23.64 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.211 3.816   12.028 1.00 20.70 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.870 2.271   12.693 1.00 26.80 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.216 2.301   12.112 1.00 28.90 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.211 1.519   10.823 1.00 30.29 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.057 0.308   10.853 1.00 31.82 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.199 1.647   13.078 1.00 30.62 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.351 2.450   14.340 1.00 31.43 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.150 3.584   14.371 1.00 33.29 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.590 2.163   15.463 1.00 32.67 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.248 4.367   15.513 1.00 34.52 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.656 2.959   16.598 1.00 33.85 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.532 4.024   16.637 1.00 35.04 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.613 4.794   17.758 1.00 36.54 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.314 2.193   9.700  1.00 30.95 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.252 1.602   8.369  1.00 32.76 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.376 2.217   7.533  1.00 34.77 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.437 3.435   7.368  1.00 34.89 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.845 1.837   7.736  1.00 34.93 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.412 3.300   7.833  1.00 34.69 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.810 1.357   6.299  1.00 36.80 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.320 1.390   7.074  1.00 36.13 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.474 1.877   6.332  1.00 38.72 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.276 2.882   7.141  1.00 40.28 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.490 2.665   8.338  1.00 41.58 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.561 4.048   6.558  1.00 39.84 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.283 5.106   7.266  1.00 39.60 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.337 6.167   7.856  1.00 36.38 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.729 7.327   8.033  1.00 35.96 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.301 5.751   6.356  1.00 43.52 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.470 4.847   6.031  1.00 51.24 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 33.905 4.016   6.839  1.00 53.48 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 34.008 4.990   4.834  1.00 54.70 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.105 5.760   8.197  1.00 33.34 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.094 6.677   8.734  1.00 31.14 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.552 6.255   10.082 1.00 28.77 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.422 5.071   10.376 1.00 28.59 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.896 6.776   7.774  1.00 29.60 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.231 7.372   6.432  1.00 30.88 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.808 8.630   6.335  1.00 32.07 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.010 6.665   5.261  1.00 31.81 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.155 9.173   5.105  1.00 33.98 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.318 7.211   4.019  1.00 33.67 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.904 8.464   3.946  1.00 35.81 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.216 9.041   2.735  1.00 38.40 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.200 7.258   10.888 1.00 26.93 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.538 7.075   12.164 1.00 24.71 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.266 7.913   12.085 1.00 21.78 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.304 9.124   11.834 1.00 20.78 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.428 7.500   13.332 1.00 25.66 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.733 7.785   14.658 1.00 28.92 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.770 8.186   15.701 1.00 32.57 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.270 9.181   16.649 1.00 33.40 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.759 8.892   17.840 1.00 34.06 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.637 7.623   18.231 1.00 31.76 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.328 9.864   18.636 1.00 33.38 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.121 7.255   12.265 1.00 20.60 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.803 7.906   12.243 1.00 19.82 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.298 8.030   13.671 1.00 19.35 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.124 7.008   14.320 1.00 18.69 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.780 7.077   11.457 1.00 19.27 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.497 7.916   11.233 1.00 18.32 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.345 6.527   10.131 1.00 18.51 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.951 9.249   14.122 1.00 19.03 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.462 9.440   15.493 1.00 19.34 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.260 10.399  15.460 1.00 17.46 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.086 11.123  14.466 1.00 17.27 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.565 10.063  16.399 1.00 22.50 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.659 9.066   16.710 1.00 25.62 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.131 11.339  15.769 1.00 23.42 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.495 10.494  16.581 1.00 16.42 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.456 11.536  16.713 1.00 14.63 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.204 12.885  16.702 1.00 16.37 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.236 13.031  17.395 1.00 18.22 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.704 11.436  18.078 1.00 15.22 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.886 10.167  18.162 1.00 18.06 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.378 9.109   18.602 1.00 19.13 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.651 10.218  17.703 1.00 16.91 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.714 13.820  15.921 1.00 15.01 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.388 15.126  15.822 1.00 15.39 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.436 15.820  17.189 1.00 18.74 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.462 16.445  17.515 1.00 20.84 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.701 16.006  14.782 1.00 15.61 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.475 17.309  14.416 1.00 16.57 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.531 18.199  13.635 1.00 17.56 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.143 19.433  13.090 1.00 17.30 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.244 20.571  13.770 1.00 20.27 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.889 20.623  15.052 1.00 19.40 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.707 21.670  13.175 1.00 19.72 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.372 15.652  18.020 1.00 18.68 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.343 16.315  19.352 1.00 21.24 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.320 15.701  20.374 1.00 24.20 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.640 16.324  21.403 1.00 27.20 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 16.914 16.410  19.911 1.00 21.87 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.349 15.118  20.419 1.00 22.42 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.704 14.249  19.573 1.00 23.00 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.282 14.629  21.691 1.00 23.02 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.337 13.204  20.323 1.00 23.54 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.642 13.400  21.614 1.00 24.49 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 19.869 14.534  20.043 1.00 23.00 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 20.842 13.876  20.901 1.00 24.50 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.279 13.909  20.313 1.00 25.73 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.166 13.231  20.861 1.00 27.76 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.357 12.430  21.163 1.00 24.63 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.020 12.342  21.946 1.00 26.15 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.573 10.901  22.152 1.00 25.67 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.101 13.065  23.294 1.00 27.50 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.491 14.566  19.142 1.00 25.19 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.819 14.574  18.528 1.00 26.04 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.863 15.232  19.428 1.00 28.23 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.541 16.195  20.097 1.00 29.34 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.791 15.257  17.168 1.00 24.50 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.094 14.722  19.413 1.00 30.08 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.223 15.206  20.227 1.00 32.55 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.063 16.284  19.474 1.00 33.80 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.810 16.548  18.301 1.00 32.90 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.116 14.016  20.572 1.00 34.63 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.723 13.582  19.359 1.00 36.83 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.367 12.910  21.242 1.00 34.73 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.114 16.849  20.119 1.00 36.28 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 29.996 17.807  19.457 1.00 38.18 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.712 17.137  18.290 1.00 37.17 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.781 17.719  17.219 1.00 36.82 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.039 18.350  20.445 1.00 42.19 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.463 19.232  21.505 1.00 49.17 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 29.829 20.414  21.193 1.00 52.56 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 30.501 19.096  22.856 1.00 52.28 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 29.476 20.951  22.352 1.00 53.76 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 29.868 20.195  23.383 1.00 53.67 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.192 15.883  18.484 1.00 36.63 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.875 15.129  17.433 1.00 37.63 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 30.975 14.890  16.255 1.00 35.34 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.423 15.048  15.125 1.00 36.80 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.393 13.793  17.927 1.00 41.40 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.292 13.116  16.923 1.00 49.44 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.386 13.616  16.613 1.00 51.97 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 32.863 11.964  16.399 1.00 50.32 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.697 14.519  16.489 1.00 31.99 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.729 14.369  15.397 1.00 29.62 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.633 15.674  14.570 1.00 28.41 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.736 15.643  13.348 1.00 29.42 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.343 14.054  15.976 1.00 28.59 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.202 12.635  16.478 1.00 29.77 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.854 11.739  15.905 1.00 28.91 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.469 12.431  17.466 1.00 30.57 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.486 16.825  15.240 1.00 26.97 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.356 18.100  14.527 1.00 26.54 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.687 18.507  13.824 1.00 28.93 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.643 19.128  12.771 1.00 28.96 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 27.870 19.200  15.493 1.00 24.82 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.380 19.277  15.613 1.00 23.34 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.613 18.798  16.636 1.00 24.86 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.469 19.805  14.635 1.00 22.22 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.279 19.057  16.386 1.00 24.28 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.160 19.626  15.140 1.00 23.28 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.630 20.404  13.381 1.00 22.39 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.030 20.107  14.473 1.00 23.04 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.505 20.853  12.705 1.00 21.71 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.219 20.675  13.238 1.00 22.00 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.837 18.095  14.375 1.00 31.28 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.162 18.407  13.805 1.00 33.94 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.492 17.526  12.582 1.00 35.19 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.369 17.885  11.790 1.00 36.46 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.258 18.230  14.863 1.00 34.68 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.818 16.371  12.455 1.00 33.57 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 31.931 15.425  11.348 1.00 32.97 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.566 15.274  10.645 1.00 29.14 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.227 14.200  10.208 1.00 27.58 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.425 14.095  11.860 1.00 35.84 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.880 14.178  12.267 1.00 41.69 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.757 14.409  11.433 1.00 44.62 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.158 13.975  13.544 1.00 42.02 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.798 16.349  10.569 1.00 27.86 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.484 16.341  9.950  1.00 25.39 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.488 15.954  8.463  1.00 26.27 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.315 16.452  7.710  1.00 28.33 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 27.891 17.749  10.097 1.00 23.96 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.492 17.969  9.471  1.00 25.04 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.412 17.122  10.192 1.00 25.93 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.106 19.405  9.552  1.00 23.13 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.566 15.049  8.037  1.00 24.71 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.366 14.678  6.631  1.00 24.94 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.010 15.336  6.163  1.00 24.37 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 25.936 16.008  5.126  1.00 25.70 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.293 13.142  6.473  1.00 26.54 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.785 12.767  5.082  1.00 27.40 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.641 12.478  6.773  1.00 28.03 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 24.965 15.195  6.986  1.00 21.88 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.627 15.711  6.691  1.00 20.12 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.796 15.756  7.980  1.00 18.51 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 22.927 14.882  8.832  1.00 17.58 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 22.971 14.722  5.697  1.00 19.90 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.494 14.897  5.442  1.00 20.51 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 20.895 15.808  4.620  1.00 22.00 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.436 14.128  6.031  1.00 19.88 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.524 15.625  4.630  1.00 21.52 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.214 14.645  5.540  1.00 20.42 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.399 13.150  7.025  1.00 19.51 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 17.976 14.071  5.870  1.00 20.13 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.183 12.580  7.347  1.00 20.14 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 17.985 13.055  6.791  1.00 19.44 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 21.886 16.716  8.076  1.00 17.09 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 20.981 16.792  9.213  1.00 16.90 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.659 17.384  8.724  1.00 16.46 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.650 18.168  7.777  1.00 16.44 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.597 17.588  10.381 1.00 19.52 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.124 18.961  10.014 1.00 20.13 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.115 20.084  9.866  1.00 22.46 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.406 21.041  9.106  1.00 25.66 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.057 20.044  10.534 1.00 21.36 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.563 16.999  9.359  1.00 15.63 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.255 17.529  9.011  1.00 15.31 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.425 17.680  10.300 1.00 15.68 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 15.992 16.664  10.852 1.00 16.04 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.581 16.639  7.954  1.00 16.74 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.282 17.169  7.406  1.00 22.67 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.591 17.907  8.126  1.00 24.45 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 14.930 16.808  6.261  1.00 24.50 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.197 18.962  10.786 1.00 15.26 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.410 19.192  11.998 0.50 15.96 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.428 19.156  12.008 0.50 16.05 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 13.987 18.657  11.831 1.00 16.43 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.395 18.186  12.786 1.00 17.70 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.323 20.682  12.332 0.50 18.20 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.409 20.627  12.413 0.50 18.55 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 16.608 21.261  12.471 0.50 20.86 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 14.801 21.364  11.370 0.50 21.53 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.430 18.758  10.604 1.00 15.80 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.036 18.314  10.390 1.00 16.84 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 11.877 16.808  10.529 1.00 17.38 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.748 16.369  10.715 1.00 19.38 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.515 18.761  9.033  1.00 20.39 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 11.966 17.960  7.956  1.00 22.88 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 12.999 16.052  10.458 1.00 14.66 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 12.990 14.571  10.625 1.00 14.53 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.592 14.115  11.958 1.00 14.93 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.568 12.914  12.246 1.00 14.78 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.730 13.844  9.467  1.00 14.15 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.086 14.100  8.116  1.00 14.43 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 13.870 13.443  6.981  1.00 14.59 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 13.870 11.981  7.122  1.00 14.22 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.003 11.138  6.091  1.00 16.21 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.134 11.607  4.845  1.00 17.44 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 13.963 9.811   6.294  1.00 16.81 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.199 15.031  12.722 1.00 15.78 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 14.939 14.749  13.960 1.00 14.28 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.091 13.778  13.656 1.00 14.55 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.362 12.913  14.468 1.00 14.72 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.007 14.185  15.068 1.00 14.66 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.736 13.940  16.391 1.00 17.02 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.558 14.779  16.774 1.00 16.10 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.495 12.880  17.032 1.00 17.53 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.723 13.864  12.459 1.00 14.10 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.884 13.005  12.129 1.00 13.06 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.146 13.795  11.892 1.00 13.79 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.130 14.892  11.346 1.00 14.99 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.653 12.175  10.834 1.00 13.31 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.561 11.071  10.901 1.00 13.99 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.502 10.350  9.519  1.00 13.31 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 16.855 10.084  12.013 1.00 14.26 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.271 13.167  12.195 1.00 12.58 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.597 13.725  11.935 1.00 15.43 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.463 12.537  11.601 1.00 16.08 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.319 11.473  12.228 1.00 18.33 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.169 14.517  13.141 1.00 16.51 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.544 15.159  12.893 1.00 17.98 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.677 16.486  13.618 1.00 19.50 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.713 14.254  13.373 1.00 19.07 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.283 12.655  10.535 1.00 16.49 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.232 11.609  10.113 1.00 18.26 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.616 12.237  10.151 1.00 20.02 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.833 13.344  9.639  1.00 20.83 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 23.942 11.023  8.711  1.00 19.42 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 24.989 9.942   8.310  1.00 21.11 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.524 10.438  8.676  1.00 19.69 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.521 11.520  10.780 1.00 21.61 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 27.906 11.944  10.883 1.00 23.90 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.825 10.862  10.337 1.00 26.46 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.465 9.689   10.288 1.00 26.07 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.255 12.302  12.321 1.00 25.06 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.216 11.221  13.232 1.00 26.65 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.071 11.260  9.980  1.00 29.26 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.050 10.292  9.481  1.00 33.28 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.829 9.595   10.614 1.00 36.97 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.000 10.152  11.698 1.00 37.47 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.026 10.968  8.525  1.00 34.32 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.609 12.096  9.158  1.00 37.71 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.297 8.386   10.357 1.00 39.29 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.047 7.578   11.326 1.00 43.76 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.346 7.100   10.687 1.00 50.58 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.415 6.982   9.462  1.00 52.03 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.241 6.320   11.712 1.00 43.35 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.152 5.474   10.573 1.00 43.64 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.836 6.637   12.214 1.00 42.09 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.336 6.743   11.520 1.00 54.55 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.632 6.167   11.118 1.00 58.31 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.555 4.614   11.078 1.00 60.35 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 37.365 3.939   10.413 1.00 62.24 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.694 6.607   12.138 1.00 60.51 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.246 6.154   13.426 1.00 63.15 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 37.902 8.103   12.162 1.00 60.27 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.654 4.032   11.868 1.00 59.77 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.472 2.593   11.902 1.00 59.56 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.313 2.218   10.969 1.00 58.91 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.430 3.039   10.689 1.00 58.79 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.187 2.142   13.321 1.00 60.17 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.327 0.986   10.475 1.00 58.53 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.326 0.474   9.543  1.00 58.64 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.080 -0.076  10.260 1.00 57.05 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.203 -0.866  11.195 1.00 58.11 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.984 -0.594  8.640  1.00 61.95 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 33.021 -1.461  7.822  1.00 67.35 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 32.631 -0.835  6.503  1.00 73.72 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 33.260 0.126   6.018  1.00 75.66 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 31.587 -1.389  5.884  1.00 74.18 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.901 0.332   9.779  1.00 53.90 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.585 -0.062  10.275 1.00 51.85 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 29.004 -1.237  9.505  1.00 49.20 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.197 -1.349  8.291  1.00 49.76 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.253 -2.088  10.184 1.00 46.05 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.735 -3.305  9.572  1.00 44.23 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.224 -3.472  9.599  1.00 40.81 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.758 -4.590  9.328  1.00 41.25 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.414 -4.508  10.200 1.00 46.71 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 30.132 -4.707  9.705  1.00 55.44 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.451 -2.417  9.933  1.00 36.92 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 23.994 -2.578  9.954  1.00 35.74 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.467 -2.572  8.551  1.00 35.27 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 23.977 -1.878  7.667  1.00 37.35 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.284 -1.458  10.738 1.00 36.39 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.539 -1.455  12.220 1.00 39.87 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.571 -2.541  12.817 1.00 40.88 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.678 -0.361  12.791 1.00 40.68 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.483 -3.367  8.343  1.00 34.53 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.811 -3.463  7.073  1.00 34.38 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.609 -2.558  7.173  1.00 31.63 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.880 -2.650  8.152  1.00 31.51 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.388 -4.908  6.848  1.00 37.40 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.594 -5.624  6.578  1.00 40.40 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.426 -5.044  5.685  1.00 36.56 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.440 -1.652  6.217  1.00 29.14 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.248 -0.820  6.195  1.00 26.49 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.233 -1.554  5.334  1.00 26.24 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.589 -2.055  4.239  1.00 27.15 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.530 0.581   5.632  1.00 25.93 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.737 1.233   6.320  1.00 26.43 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.270 1.460   5.721  1.00 25.99 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.553 1.522   7.865  1.00 26.52 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.983 -1.635  5.824  1.00 23.97 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.869 -2.241  5.099  1.00 22.89 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.475 -1.323  3.931  1.00 23.54 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.531 -0.103  4.070  1.00 23.47 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.668 -2.387  6.040  1.00 21.15 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.093 -1.921  2.752  1.00 25.20 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.627 -1.171  1.573  1.00 27.47 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.263 -1.837  1.250  1.00 29.56 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.223 -2.854  0.539  1.00 31.73 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.654 -1.302  0.427  1.00 29.54 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.058 -0.778  0.792  1.00 29.52 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.102 0.706   1.246  1.00 31.73 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.471 1.165   1.526  1.00 30.04 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.765 2.287   2.185  1.00 29.60 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.801 3.103   2.579  1.00 26.58 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 20.031 2.615   2.424  1.00 26.86 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.172 -1.332  1.887  1.00 28.65 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.881 -2.013  1.848  1.00 29.40 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.721  -1.100  2.295  1.00 29.69 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 9.939  0.036   2.691  1.00 29.16 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 10.983 -3.221  2.769  1.00 29.68 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.161 -2.783  4.536  1.00 25.00 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.474  -1.645  2.279  1.00 30.23 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.319  -0.918  2.778  1.00 31.28 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.670  -1.695  3.926  1.00 30.23 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.462  -1.617  4.111  1.00 31.28 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.302  -0.564  1.663  1.00 35.05 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.496  -1.714  1.107  1.00 42.41 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 5.814  -2.885  1.435  1.00 44.16 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.532  -1.449  0.341  1.00 47.12 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.464  -2.479  4.699  1.00 28.27 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 6.983  -3.234  5.869  1.00 24.72 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.248  -2.296  6.828  1.00 22.92 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.673  -1.153  7.040  1.00 22.07 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.151  -3.904  6.599  1.00 24.21 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.707  -5.480  5.885  1.00 26.24 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.194  -2.779  7.424  1.00 21.15 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.477  -2.094  8.477  1.00 21.37 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.450  -2.918  9.757  1.00 18.39 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.588  -2.693  10.612 1.00 18.82 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.051  -1.689  8.042  1.00 24.59 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 2.989  -0.334  7.322  1.00 27.74 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.543  0.035   7.038  1.00 30.88 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.064  -0.069  5.907  1.00 33.16 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 0.808  0.420   8.082  1.00 30.62 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.326  -3.969  9.886  1.00 17.51 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.458  -4.764  11.108 1.00 16.41 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 6.977  -4.926  11.343 1.00 14.96 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.799  -5.024  10.412 1.00 15.80 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.786  -6.168  11.059 1.00 20.64 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.468  -6.983  10.102 1.00 23.01 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.290  -6.125  10.770 1.00 21.49 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.328  -4.983  12.613 1.00 13.62 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.718  -5.092  12.992 1.00 13.19 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.854  -5.241  14.499 1.00 12.06 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.879  -5.480  15.182 1.00 13.76 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 10.079 -5.104  14.981 1.00 10.91 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.393 -5.246  16.405 1.00 11.45 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.277 -4.036  16.810 1.00 12.46 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.249 -3.746  16.139 1.00 12.56 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 11.153 -6.602  16.651 1.00 13.89 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.627 -6.711  18.115 1.00 15.63 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.242 -7.779  16.323 1.00 15.26 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 10.994 -3.401  17.958 1.00 13.02 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.846 -2.311  18.436 1.00 11.59 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.398 -2.585  19.819 1.00 13.85 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.810 -3.327  20.600 1.00 13.36 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.128 -0.912  18.368 1.00 11.72 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.137 -0.669  19.512 1.00 13.01 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.867  -1.253  19.505 1.00 14.15 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.433 0.215   20.545 1.00 14.63 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 7.928  -0.970  20.508 1.00 16.60 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.540  0.419   21.607 1.00 16.16 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.282  -0.170  21.576 1.00 16.89 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.364  0.048   22.579 1.00 19.44 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.554 -1.996  20.106 1.00 13.94 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 14.149 -2.112  21.421 1.00 15.72 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.664 -0.956  22.315 1.00 15.80 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.800 0.231   21.968 1.00 15.52 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.677 -2.114  21.342 1.00 16.69 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.273 -2.249  22.722 1.00 19.19 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 16.145 -3.431  23.439 1.00 20.93 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 16.883 -1.169  23.342 1.00 21.21 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.664 -3.553  24.728 1.00 24.19 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.414 -1.276  24.624 1.00 24.09 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.299 -2.474  25.310 1.00 26.45 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.783 -2.571  26.592 1.00 31.64 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 13.139 -1.307  23.501 1.00 16.69 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.642 -0.300  24.445 1.00 19.21 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.522 -0.308  25.721 1.00 22.13 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.386 -1.207  26.570 1.00 22.80 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 11.172 -0.571  24.746 1.00 21.33 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.495 0.357   26.155 1.00 23.51 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.452 0.677   25.823 1.00 23.05 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.395 0.744   26.921 1.00 25.81 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 14.727 0.876   28.259 1.00 27.13 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 15.210 0.273   29.209 1.00 30.52 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.408 1.874   26.735 1.00 30.42 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 15.780 3.137   26.649 1.00 37.92 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.606 1.608   28.350 1.00 26.67 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 12.878 1.790   29.636 1.00 28.02 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 12.240 0.501   30.166 1.00 28.50 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 11.756 0.486   31.310 1.00 31.00 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 11.827 2.883   29.506 1.00 29.04 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 10.759 2.544   28.639 1.00 28.93 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 12.274 -0.599  29.371 1.00 27.08 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 11.767 -1.879  29.828 1.00 26.65 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 12.832 -2.983  29.664 1.00 28.28 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.553 -4.138  30.015 1.00 28.98 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.517 -2.255  29.010 1.00 26.70 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 9.294  -1.401  29.315 1.00 27.39 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.705  -1.729  30.682 1.00 30.72 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.486  -0.962  30.936 1.00 34.30 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.455  0.253   31.471 1.00 36.13 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.580  0.842   31.872 1.00 36.36 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.297  0.884   31.635 1.00 37.89 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 14.047 -2.650  29.096 1.00 28.45 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 15.106 -3.614  28.760 1.00 30.00 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.500 -4.789  27.953 1.00 28.80 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.763 -5.968  28.234 1.00 29.50 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 15.880 -4.080  30.003 1.00 33.88 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.963 -3.104  30.435 1.00 40.65 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.741 -3.670  31.606 1.00 47.32 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 18.194 -2.616  32.509 1.00 54.64 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 18.219 -2.721  33.835 1.00 60.77 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 17.815 -3.841  34.429 1.00 62.16 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.625 -1.701  34.579 1.00 62.96 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.613 -4.457  26.971 1.00 25.61 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.921 -5.522  26.222 1.00 24.11 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.684 -5.110  24.777 1.00 21.26 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.592 -3.909  24.494 1.00 20.55 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.511 -5.756  26.813 1.00 26.48 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 11.364 -6.792  27.909 1.00 35.35 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.907  -6.762  28.378 1.00 42.49 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.440  -8.035  29.046 1.00 48.36 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 9.828  -8.087  30.484 1.00 51.02 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.528 -6.090  23.895 1.00 18.75 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 12.146 -5.834  22.517 1.00 17.33 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.637 -6.086  22.431 1.00 18.19 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 10.100 -7.007  23.093 1.00 19.78 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 12.887 -6.797  21.573 1.00 16.79 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.363 -6.585  21.552 1.00 17.02 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 14.975 -5.796  20.577 1.00 20.08 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.311 -7.075  22.362 1.00 17.93 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.277 -5.857  20.834 1.00 19.89 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.521 -6.573  21.918 1.00 20.86 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 9.935  -5.289  21.619 1.00 15.93 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.487  -5.495  21.448 1.00 15.09 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 8.152  -5.590  19.984 1.00 14.26 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.591  -4.768  19.196 1.00 12.66 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.677  -4.315  22.040 1.00 16.15 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.712  -4.263  23.550 1.00 18.49 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 6.929  -5.123  24.319 1.00 20.48 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.501  -3.338  24.213 1.00 21.19 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 6.926  -5.043  25.721 1.00 22.99 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.534  -3.278  25.607 1.00 22.62 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.757  -4.141  26.354 1.00 23.87 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.755  -4.027  27.748 1.00 27.65 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.272  -6.518  19.605 1.00 14.31 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.783  -6.555  18.207 1.00 14.43 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.696  -5.454  18.018 1.00 16.48 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.907  -5.229  18.957 1.00 18.76 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 6.158  -7.946  18.083 1.00 15.39 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.782  -8.305  19.497 1.00 15.83 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.622  -7.542  20.475 1.00 15.05 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.646  -4.781  16.858 1.00 15.62 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.701  -3.674  16.599 1.00 16.76 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.206  -3.656  15.182 1.00 16.56 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 4.936  -4.008  14.247 1.00 16.93 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.319  -2.248  16.854 1.00 18.95 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.283  -1.860  18.316 1.00 20.97 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.713  -2.118  16.261 1.00 19.67 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 2.981  -3.145  15.006 1.00 16.14 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.471  -2.716  13.693 1.00 17.01 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.666  -1.182  13.677 1.00 18.52 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.531  -0.541  14.730 1.00 20.83 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 0.980  -2.988  13.515 1.00 19.71 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.761  -4.385  13.473 1.00 27.77 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.116  -0.634  12.556 1.00 16.03 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.400  0.805   12.497 1.00 16.63 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.902  1.429   11.258 1.00 19.18 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.756  0.756   10.230 1.00 21.71 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.894  1.111   12.724 1.00 15.75 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.922  0.391   11.860 1.00 14.60 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.409  -0.852  12.234 1.00 13.56 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.358  0.939   10.655 1.00 15.50 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.367  -1.500  11.458 1.00 14.34 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.318  0.289   9.878  1.00 15.77 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.764  -0.965  10.251 1.00 15.20 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.599  2.753   11.333 1.00 18.24 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.030  3.448   10.198 1.00 20.61 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.058  3.781   9.110  1.00 21.14 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.261  3.700   9.348  1.00 19.28 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.297  4.709   10.679 1.00 23.86 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.238  5.671   11.149 1.00 24.06 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.609  4.165   7.896  1.00 23.33 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.567  4.562   6.836  1.00 24.92 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.201  5.930   7.168  1.00 24.97 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.556  6.740   7.816  1.00 26.33 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 2.840  4.577   5.475  1.00 29.48 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.385  3.165   5.087  1.00 35.64 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.075  3.044   3.574  1.00 44.15 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.128  1.587   3.170  1.00 50.26 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 2.090  1.403   1.695  1.00 54.28 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.459  6.217   6.749  1.00 23.74 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.073  7.512   7.108  1.00 24.78 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.256  8.709   6.655  1.00 25.80 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 4.839  8.792   5.476  1.00 27.14 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.451  7.500   6.427  1.00 26.09 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.564  6.218   5.700  1.00 26.98 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.388  5.331   6.022  1.00 23.98 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 4.973  9.616   7.595  1.00 25.41 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.132  10.772  7.258  1.00 27.69 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.422  11.991  8.146  1.00 27.76 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.293  11.921  9.022  1.00 25.90 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 2.655  10.366  7.315  1.00 31.51 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.268  10.150  8.660  1.00 37.08 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 3.745  13.142  7.868  1.00 28.57 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 3.902  14.369  8.646  1.00 30.14 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 2.994  14.263  9.834  1.00 31.96 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 1.771  14.172  9.650  1.00 34.41 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.413  15.579  7.823  1.00 30.75 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.415  16.249  6.969  1.00 32.97 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 3.732  17.277  6.053  1.00 35.14 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 5.439  16.940  7.803  1.00 33.72 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.540  14.326  11.042 1.00 31.31 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 2.749  14.180  12.255 1.00 33.21 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 3.075  15.333  13.205 1.00 35.02 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.249  15.672  13.386 1.00 33.94 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 3.028  12.777  12.877 1.00 34.32 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.458  11.674  11.956 1.00 35.85 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 2.451  12.664  14.293 1.00 35.19 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 2.875  10.309  12.240 1.00 37.55 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 2.037  15.994  13.756 1.00 36.33 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.266  17.116  14.671 1.00 38.95 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 2.933  16.619  15.951 1.00 38.40 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 2.594  15.557  16.464 1.00 38.63 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 0.951  17.852  15.005 1.00 41.78 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 1.155  19.168  15.722 1.00 44.73 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 1.622  20.274  15.047 1.00 46.79 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 0.897  19.285  17.079 1.00 46.67 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 1.825  21.483  15.709 1.00 48.55 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 1.066  20.506  17.733 1.00 47.57 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 1.538  21.587  17.047 1.00 48.32 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 3.968  17.326  16.391 1.00 37.41 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 4.757  16.978  17.562 1.00 37.30 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 4.792  18.202  18.472 1.00 38.83 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 5.184  19.310  18.054 1.00 37.80 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 6.195  16.477  17.197 1.00 36.82 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 7.025  16.216  18.449 1.00 36.95 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 6.144  15.226  16.337 1.00 36.71 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 4.357  17.996  19.717 1.00 40.29 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 4.292  19.048  20.728 1.00 41.88 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 5.645  19.677  21.006 1.00 42.24 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 6.682  19.007  20.890 1.00 42.37 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 3.769  18.457  22.023 1.00 46.12 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 2.303  18.116  21.969 1.00 54.89 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 1.613  18.653  23.198 1.00 64.18 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 0.916  17.866  23.877 1.00 68.35 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 1.808  19.851  23.508 1.00 68.06 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 5.639  20.952  21.435 1.00 42.02 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 6.879  21.654  21.756 1.00 42.58 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 7.694  20.922  22.825 1.00 42.98 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 7.133  20.294  23.724 1.00 44.42 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 6.574  23.085  22.219 1.00 42.86 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 9.002  20.991  22.719 1.00 41.55 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 9.911  20.388  23.670 1.00 40.96 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 11.099 21.346  23.888 1.00 42.14 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 11.187 22.428  23.273 1.00 41.99 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 10.391 19.024  23.145 1.00 41.16 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 11.256 19.191  22.032 1.00 42.18 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 12.002 20.966  24.786 1.00 42.62 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 13.234 21.688  25.050 1.00 42.96 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 14.148 21.771  23.818 1.00 41.09 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 14.965 22.684  23.706 1.00 41.72 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 13.980 21.083  26.262 1.00 48.73 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 13.666 19.620  26.594 1.00 56.67 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 13.405 19.342  28.065 1.00 69.45 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 13.258 20.315  28.842 1.00 72.61 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 13.344 18.147  28.441 1.00 74.25 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 13.994 20.830  22.869 1.00 38.12 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 14.828 20.791  21.683 1.00 35.91 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 14.166 21.427  20.443 1.00 33.22 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 14.875 21.868  19.553 1.00 33.18 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 15.243 19.330  21.379 1.00 35.22 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 15.677 18.526  22.588 1.00 35.32 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 17.002 18.511  23.002 1.00 36.21 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 14.771 17.744  23.287 1.00 36.08 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 17.407 17.750  24.095 1.00 37.10 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 15.156 17.012  24.401 1.00 37.79 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 16.476 17.011  24.802 1.00 39.16 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 16.845 16.222  25.879 1.00 42.58 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 12.823 21.460  20.370 1.00 31.57 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 12.140 22.032  19.193 1.00 29.27 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 10.854 22.758  19.556 1.00 31.63 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 10.200 22.384  20.525 1.00 32.04 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 11.712 20.902  18.199 1.00 26.01 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 12.789 19.975  17.696 1.00 22.29 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 13.622 20.350  16.647 1.00 21.22 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 12.871 18.662  18.153 1.00 22.05 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 14.563 19.475  16.128 1.00 20.40 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 13.843 17.796  17.678 1.00 20.45 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 14.646 18.179  16.621 1.00 20.01 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 15.628 17.324  16.171 1.00 17.53 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 10.418 23.757  18.754 1.00 32.00 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 9.068  24.315  18.993 1.00 33.62 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 7.997  23.338  18.431 1.00 35.05 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 8.347  22.349  17.751 1.00 34.75 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 9.091  25.643  18.234 1.00 34.22 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 10.119 25.466  17.162 1.00 33.59 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 11.053 24.323  17.541 1.00 31.65 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 6.701  23.590  18.679 1.00 36.13 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 5.631  22.731  18.142 1.00 36.93 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 5.694  22.777  16.588 1.00 35.83 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 5.929  23.845  16.015 1.00 36.83 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 4.272  23.204  18.656 1.00 37.87 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 5.704  21.590  15.935 1.00 33.14 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 5.895  21.542  14.478 1.00 30.87 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.381  20.195  13.908 1.00 29.42 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 5.066  19.297  14.679 1.00 29.08 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.411  21.673  14.179 1.00 30.03 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 8.197  20.358  14.486 1.00 29.76 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 9.601  20.600  14.957 1.00 28.56 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.525 19.517  14.592 1.00 26.89 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 10.559 18.323  15.181 1.00 24.95 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 11.460 17.415  14.804 1.00 19.88 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 9.707  18.035  16.160 1.00 24.19 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 5.362  20.056  12.566 1.00 28.78 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 5.095  18.758  11.969 1.00 29.41 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.440  18.107  11.747 1.00 25.65 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.333  18.715  11.143 1.00 25.44 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.402  18.868  10.626 1.00 32.55 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 2.973  19.337  10.754 1.00 37.63 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 1.944  18.439  11.001 1.00 40.67 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 2.659  20.685  10.680 1.00 40.52 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 0.625  18.866  11.105 1.00 43.57 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 1.352  21.127  10.817 1.00 43.30 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.337  20.216  11.025 1.00 45.83 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -0.961 20.668  11.132 1.00 50.94 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 6.595  16.869  12.240 1.00 22.75 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 7.825  16.125  11.990 1.00 20.77 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.512  15.184  10.807 1.00 20.51 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.463  14.532  10.776 1.00 21.15 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 8.261  15.333  13.226 1.00 18.84 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.501  14.423  12.945 1.00 18.51 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 10.140 13.933  14.208 1.00 18.97 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 10.296 14.653  15.194 1.00 18.26 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 10.609 12.684  14.192 1.00 15.91 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.346  15.193  9.803  1.00 17.92 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.140  14.399  8.597  1.00 18.24 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 8.857  13.042  8.707  1.00 19.16 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 9.712  12.841  9.607  1.00 18.01 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 8.634  15.193  7.390  1.00 19.37 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 10.044 15.380  7.457  1.00 20.14 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.421  12.089  7.847  1.00 19.12 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 8.995  10.760  7.754  1.00 17.70 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 8.849  10.025  9.094  1.00 16.38 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 9.746  9.255   9.440  1.00 15.76 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.471 10.888  7.320  1.00 18.53 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 10.596 11.483  5.938  1.00 21.26 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.568 10.682  4.802  1.00 24.17 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 10.594 12.780  5.552  1.00 23.47 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 10.627 11.519  3.764  1.00 25.02 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 10.628 12.787  4.164  1.00 25.59 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 7.727  10.261  9.819  1.00 16.60 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.526  9.659   11.149 1.00 16.51 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.475  8.543   11.046 1.00 16.10 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.435  8.712   10.395 1.00 17.18 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 7.025  10.755  12.113 1.00 17.93 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 6.920  10.410  13.604 1.00 19.28 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.258  10.017  14.176 1.00 18.34 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.405  11.650  14.390 1.00 22.63 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 6.722  7.424   11.750 1.00 15.18 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 5.777  6.275   11.746 1.00 15.48 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.316  6.001   13.179 1.00 17.05 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.185  5.907   14.049 1.00 18.63 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.561  5.058   11.263 1.00 15.36 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.052  5.240   9.816  1.00 18.97 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.140  3.938   9.288  1.00 21.75 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.509  4.180   10.368 1.00 18.76 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 3.999  5.864   13.455 1.00 16.14 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.556  5.604   14.828 1.00 17.25 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 3.148  4.147   15.037 1.00 17.89 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.684  3.475   14.124 1.00 19.02 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.327  6.496   15.225 1.00 19.64 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.596  7.991   15.246 1.00 23.55 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.385  8.756   15.765 1.00 26.79 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 3.823  8.343   16.040 1.00 23.82 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.243  3.715   16.266 1.00 18.29 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 2.828  2.377   16.685 1.00 18.57 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.300  2.461   18.110 1.00 20.16 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.602  3.423   18.822 1.00 20.66 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 4.014  1.427   16.662 1.00 19.64 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.458  1.499   18.484 1.00 20.74 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 0.946  1.413   19.846 1.00 23.10 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 1.995  0.613   20.603 1.00 25.06 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.288  -0.535  20.261 1.00 24.91 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.448 0.742   19.893 1.00 25.25 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -0.920 0.569   21.333 1.00 25.39 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.457 1.561   19.087 1.00 26.70 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.590  1.253   21.580 1.00 26.00 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.672  0.648   22.331 1.00 27.21 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 4.202  1.608   23.362 1.00 27.83 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 3.975  2.828   23.288 1.00 28.69 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 4.874  1.057   24.353 1.00 26.37 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 5.451  1.845   25.408 1.00 26.26 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 6.722  2.563   24.971 1.00 25.18 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 7.584  1.968   24.333 1.00 24.00 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 5.770  0.954   26.610 1.00 27.15 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 6.316  1.754   27.751 1.00 29.87 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 5.524  2.647   28.431 1.00 33.30 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 7.594  1.894   28.172 1.00 30.65 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 6.332  3.269   29.281 1.00 33.55 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 7.581  2.810   29.180 1.00 32.88 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 6.861  3.826   25.394 1.00 25.48 ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 8.070  4.604   25.211 1.00 26.66 ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 8.112  5.749   26.235 1.00 29.28 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 7.059  6.213   26.660 1.00 30.55 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 8.192  5.137   23.784 1.00 27.73 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 7.176  6.093   23.539 1.00 30.65 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 9.337  6.140   26.655 1.00 29.69 ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 9.721  7.229   27.564 1.00 31.15 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 10.855 8.027   26.918 1.00 32.19 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 11.488 7.543   25.979 1.00 32.35 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 10.143 6.669   28.926 1.00 34.99 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 8.957  6.052   29.619 1.00 41.26 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 9.258  5.384   30.945 1.00 43.55 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 10.010 5.966   31.754 1.00 45.68 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 8.737  4.274   31.174 1.00 42.00 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 11.095 9.300   27.322 1.00 33.58 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 12.065 10.133  26.564 1.00 33.89 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 13.441 9.501   26.296 1.00 32.35 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 13.934 9.569   25.151 1.00 32.86 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 12.147 11.419  27.370 1.00 35.05 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 10.823 11.484  28.112 1.00 36.48 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 10.372 10.069  28.349 1.00 34.88 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 14.008 8.840   27.298 1.00 30.20 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 15.282 8.128   27.190 1.00 29.69 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 15.297 6.955   26.215 1.00 28.28 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 16.346 6.351   25.963 1.00 29.04 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 14.124 6.584   25.689 1.00 26.51 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 13.988 5.502   24.709 1.00 23.64 ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 14.369 5.927   23.292 1.00 20.98 ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 14.580 5.066   22.417 1.00 18.62 ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 12.570 4.942   24.667 1.00 24.88 ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 12.284 4.066   25.866 1.00 25.47 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 13.204 3.397   26.329 1.00 25.22 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 11.135 4.068   26.343 1.00 25.81 ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 14.497 7.232   23.046 1.00 21.49 ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 14.891 7.732   21.712 1.00 20.83 ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 16.218 7.108   21.299 1.00 19.15 ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.108 6.980   22.150 1.00 19.99 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 14.966 9.257   21.702 1.00 21.07 ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 13.342 10.066  21.676 1.00 23.89 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 16.318 6.675   20.059 1.00 17.57 ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.537 6.009   19.613 1.00 18.50 ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.399 4.503   19.536 1.00 18.81 ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 18.221 3.841   18.889 1.00 19.06 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 16.378 3.929   20.191 1.00 17.36 ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 16.127 2.478   20.056 1.00 15.65 ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 15.837 2.092   18.599 1.00 14.46 ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 15.067 2.770   17.937 1.00 14.11 ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 16.394 0.977   18.123 1.00 13.49 ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 16.211 0.592   16.720 1.00 13.61 ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 14.918 -0.154  16.515 1.00 13.19 ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 14.571 -1.050  17.334 1.00 15.19 ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.459 -0.235  16.260 1.00 17.57 ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 18.610 0.725   15.946 1.00 19.78 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.171 -1.091  15.033 1.00 19.01 ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 19.998 -0.046  15.718 1.00 22.94 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 14.276 0.113   15.344 1.00 12.12 ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 13.102 -0.638  14.858 1.00 11.77 ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.652 -1.438  13.670 1.00 13.26 ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 14.324 -0.866  12.794 1.00 13.63 ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 12.020 0.333   14.361 1.00 12.06 ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 10.808 -0.345  13.624 1.00 13.11 ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 10.024 -1.303  14.542 1.00 14.05 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 9.844  0.760   13.109 1.00 13.88 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 13.397 -2.770  13.664 1.00 13.00 ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 13.895 -3.649  12.605 1.00 14.49 ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.779 -4.518  12.103 1.00 16.05 ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 11.982 -5.010  12.882 1.00 15.83 ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 14.900 -4.652  13.204 1.00 16.89 ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 16.211 -4.101  13.646 1.00 24.33 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.051 -5.275  14.164 1.00 29.83 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 17.657 -5.928  13.008 1.00 35.32 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 18.849 -5.612  12.517 1.00 37.07 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 19.642 -4.767  13.168 1.00 37.87 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 19.272 -6.164  11.398 1.00 38.48 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 12.816 -4.809  10.817 1.00 16.30 ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 11.910 -5.779  10.205 1.00 18.71 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 12.807 -6.928  9.679  1.00 20.62 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 14.020 -6.926  9.903  1.00 19.90 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 11.128 -5.110  9.076  1.00 20.12 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.186 -4.573  7.702  1.00 20.25 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 12.212 -7.942  9.013  1.00 23.24 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 13.013 -9.047  8.456  1.00 26.80 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 14.126 -8.609  7.445  1.00 28.05 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 15.096 -9.358  7.227  1.00 30.03 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 12.084 -10.069 7.766  1.00 30.52 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 11.405 -9.516  6.505  1.00 35.26 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 10.430 -10.519 5.907  1.00 43.63 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 9.202  -10.317 5.933  1.00 46.96 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 10.960 -11.624 5.368  1.00 43.12 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 14.006 -7.388  6.861  1.00 27.48 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 14.934 -6.862  5.850  1.00 27.18 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 16.097 -6.054  6.449  1.00 26.30 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.034 -5.699  5.721  1.00 28.10 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 14.180 -5.982  4.813  1.00 28.72 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 13.013 -6.668  4.156  1.00 31.65 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 11.713 -6.370  4.499  1.00 33.48 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 12.993 -7.550  3.127  1.00 34.03 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 10.939 -7.160  3.766  1.00 35.54 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 11.662 -7.902  2.926  1.00 35.29 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 16.011 -5.717  7.748  1.00 22.77 ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.054 -4.909  8.364  1.00 20.50 ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.509 -3.743  9.181  1.00 18.22 ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.357 -3.761  9.608  1.00 17.53 ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.343 -2.749  9.370  1.00 17.63 ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 17.002 -1.544  10.139 1.00 17.79 ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 15.996 -0.660  9.428  1.00 16.96 ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.231 -0.271  8.271  1.00 18.21 ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.271 -0.743  10.560 1.00 18.60 ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 17.879 0.563   11.250 1.00 18.29 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 19.145 -1.596  11.494 1.00 19.74 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 14.871 -0.343  10.100 1.00 15.07 ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 13.831 0.504   9.525  1.00 14.90 ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 13.969 1.985   9.971  1.00 14.06 ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 13.753 2.908   9.193  1.00 14.52 ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.424 -0.053  9.927  1.00 16.35 ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.311 0.893   9.496  1.00 18.57 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.179 -1.447  9.378  1.00 16.88 ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.264 2.177   11.259 1.00 12.10 ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.349 3.533   11.812 1.00 13.17 ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 14.716 3.546   13.288 1.00 12.92 ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 15.099 2.510   13.846 1.00 13.21 ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 14.587 4.707   13.931 1.00 12.59 ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 14.923 4.792   15.353 1.00 12.73 ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 13.852 5.529   16.114 1.00 12.31 ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 13.182 6.395   15.563 1.00 11.37 ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 16.276 5.527   15.562 1.00 14.41 ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.328 6.856   14.814 1.00 15.65 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.485 4.640   15.256 1.00 15.22 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.622 7.692   15.239 1.00 18.15 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 13.641 5.174   17.407 1.00 12.76 ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 12.643 5.880   18.204 1.00 12.25 ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 12.957 7.378   18.247 1.00 12.80 ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 14.109 7.765   18.452 1.00 14.56 ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 12.607 5.316   19.649 1.00 13.53 ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 11.606 6.112   20.470 1.00 15.08 ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 12.220 3.830   19.655 1.00 14.87 ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 11.935 8.199   18.041 1.00 12.40 ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 12.114 9.644   18.000 1.00 14.16 ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 11.084 10.417  18.839 1.00 17.70 ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 11.405 11.518  19.321 1.00 18.42 ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 12.092 10.118  16.547 1.00 15.15 ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 12.089 11.544  16.484 1.00 15.75 ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 9.863  9.851   19.015 1.00 19.27 ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 8.779  10.510  19.799 1.00 22.17 ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 7.977  9.435   20.579 1.00 24.17 ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 8.186  8.244   20.396 1.00 21.63 ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 7.800  11.326  18.860 1.00 23.63 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 6.974  10.443  18.101 1.00 25.68 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 8.472  12.378  17.948 1.00 23.64 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 7.028  9.861   21.408 1.00 27.21 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 6.146  8.942   22.094 1.00 29.74 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 5.263  9.623   23.106 1.00 33.19 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 5.268  10.847  23.232 1.00 33.63 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 4.567  8.797   23.847 1.00 36.11 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 3.655  9.221   24.900 1.00 39.69 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 2.240  8.777   24.603 1.00 42.39 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 1.887  8.591   23.440 1.00 42.12 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 1.409  8.658   25.643 1.00 44.25 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 0.007  8.258   25.507 1.00 45.73 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? -0.175 6.809   25.017 1.00 43.88 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -1.253 6.448   24.536 1.00 45.60 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -0.754 9.265   24.615 1.00 49.31 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -0.804 10.690  25.148 1.00 56.51 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -0.888 10.927  26.364 1.00 59.09 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -0.825 11.674  24.249 1.00 58.15 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 0.825  5.952   25.238 1.00 40.37 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 0.747  4.568   24.793 1.00 37.51 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 1.103  4.426   23.317 1.00 33.93 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 0.833  3.387   22.712 1.00 34.10 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 1.773  5.426   22.759 1.00 31.19 ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 2.225  5.430   21.375 1.00 28.89 ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.745  5.566   21.344 1.00 27.45 ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 4.308  6.271   22.169 1.00 30.90 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.606  6.634   20.617 1.00 29.15 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 0.068  6.631   20.506 1.00 31.87 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.471 8.014   20.194 1.00 33.60 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.399 5.605   19.476 1.00 33.04 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 4.381  5.094   20.262 1.00 22.69 ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 5.802  5.293   20.052 1.00 19.45 ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 5.971  5.718   18.574 1.00 18.62 ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 5.312  5.140   17.711 1.00 18.92 ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 6.620  4.019   20.398 1.00 19.51 ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 6.084  2.756   19.717 1.00 20.62 ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 8.103  4.208   20.113 1.00 19.55 ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 6.786  6.739   18.332 1.00 16.46 ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 7.052  7.227   16.990 1.00 16.27 ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.478  6.961   16.566 1.00 16.34 ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 9.426  7.142   17.352 1.00 17.53 ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 8.645  6.495   15.305 1.00 14.16 ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 9.966  6.159   14.765 1.00 13.49 ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.298 7.027   13.563 1.00 13.12 ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.489  7.131   12.637 1.00 13.99 ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 9.979  4.684   14.272 1.00 12.61 ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.514  3.665   15.304 1.00 12.64 ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 10.391 3.174   16.264 1.00 12.77 ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 8.187  3.234   15.340 1.00 14.67 ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 9.957  2.257   17.232 1.00 13.19 ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.769  2.287   16.288 1.00 15.29 ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 8.655  1.821   17.234 1.00 14.11 ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.513 7.589   13.558 1.00 12.17 ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 11.972 8.326   12.401 1.00 10.94 ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.413 7.260   11.362 1.00 12.14 ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.330 6.468   11.623 1.00 11.14 ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.166 9.210   12.804 1.00 11.53 ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 11.806 7.282   10.161 1.00 12.84 ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.184 6.341   9.105  1.00 15.01 ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.555 6.653   8.503  1.00 14.56 ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 13.950 7.837   8.367  1.00 14.42 ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.126 6.384   7.982  1.00 18.27 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.346 5.356   6.882  1.00 22.59 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.523 4.178   7.208  1.00 21.16 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.418 5.758   5.688  1.00 26.45 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.312 5.575   8.100  1.00 13.97 ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.600 5.812   7.421  1.00 14.91 ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 15.658 5.073   6.076  1.00 16.41 ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 16.681 5.143   5.403  1.00 18.99 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 16.850 5.471   8.271  1.00 15.96 ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 16.891 6.337   9.544  1.00 17.18 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 16.934 3.956   8.589  1.00 15.41 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 14.607 4.321   5.726  1.00 15.71 ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 14.601 3.463   4.545  1.00 16.94 ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 14.693 4.191   3.228  1.00 21.11 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.155 3.600   2.256  1.00 23.58 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.373 2.563   4.538  1.00 17.72 ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.304 1.652   5.720  1.00 18.16 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 11.984 0.899   5.665  1.00 16.49 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 10.844 1.737   6.030  1.00 18.54 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 9.611  1.296   6.227  1.00 20.23 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.308  0.027   5.985  1.00 21.03 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 8.669  2.120   6.655  1.00 20.51 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.315 5.473   3.202  1.00 21.98 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 14.427 6.255   1.972  1.00 22.72 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 15.840 6.824   1.748  1.00 22.81 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 16.131 7.323   0.640  1.00 23.88 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 13.402 7.397   1.957  1.00 24.56 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 13.592 8.405   3.064  1.00 26.71 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 13.811 7.976   4.215  1.00 25.86 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 13.491 9.636   2.784  1.00 24.62 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 16.725 6.796   2.755  1.00 21.57 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.084 7.386   2.633  1.00 22.60 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 18.989 6.414   1.917  1.00 24.98 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 19.781 5.700   2.544  1.00 25.40 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 18.623 7.738   4.017  1.00 21.79 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 17.693 8.660   4.840  1.00 21.44 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.239 8.858   6.240  1.00 20.86 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.485 10.023  4.138  1.00 22.58 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 18.817 6.335   0.585  1.00 26.46 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 19.502 5.319   -0.218 1.00 29.16 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 21.011 5.474   -0.196 1.00 31.87 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 21.729 4.467   -0.270 1.00 33.04 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 18.946 5.276   -1.650 1.00 29.63 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 17.433 5.091   -1.813 1.00 31.86 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.070 4.969   -3.295 1.00 34.76 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 16.909 3.840   -1.043 1.00 32.38 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 21.496 6.739   -0.030 1.00 32.05 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 22.914 7.070   0.013  1.00 32.01 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 23.636 6.467   1.221  1.00 33.10 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 24.860 6.395   1.203  1.00 34.59 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 23.125 8.595   -0.085 1.00 30.38 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 22.381 9.378   0.973  1.00 28.20 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 21.124 9.907   0.885  1.00 27.32 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 22.864 9.707   2.282  1.00 27.20 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 20.827 10.606  2.035  1.00 26.99 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 21.870 10.477  2.916  1.00 26.79 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 24.071 9.471   2.959  1.00 27.77 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 22.024 10.963  4.207  1.00 26.96 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.251 10.024  4.210  1.00 28.00 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.230 10.746  4.828  1.00 27.27 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 22.900 6.012   2.272  1.00 33.02 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 23.564 5.393   3.420  1.00 33.79 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.403 4.172   3.022  1.00 39.21 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.362 3.855   3.719  1.00 39.27 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 22.527 4.984   4.479  1.00 31.30 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 21.839 6.141   5.197  1.00 28.86 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 20.755 5.592   6.180  1.00 28.01 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 22.842 6.959   5.990  1.00 28.22 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 24.047 3.522   1.885  1.00 43.49 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 24.649 2.304   1.344  1.00 48.66 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 25.574 2.445   0.171  1.00 53.60 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 26.037 1.410   -0.303 1.00 55.42 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 23.541 1.385   0.852  1.00 51.62 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 22.867 0.666   1.947  1.00 57.95 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 23.564 0.255   2.895  1.00 59.77 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 21.639 0.513   1.875  1.00 61.40 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 25.749 3.648   -0.394 1.00 56.10 ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 26.622 3.800   -1.562 1.00 59.11 ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 27.720 4.831   -1.370 1.00 60.81 ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 28.740 4.755   -2.064 1.00 62.07 ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 25.823 4.084   -2.846 1.00 62.73 ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 24.903 5.288   -2.753 1.00 68.30 ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 23.596 5.120   -3.506 1.00 75.61 ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 23.007 6.150   -3.911 1.00 76.64 ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 23.157 3.959   -3.688 1.00 78.74 ? 145 GLU   A OE2 1 
HETATM 1078 N  N1  . A1BOQ B 2 .   ? 10.184 14.376  22.425 1.00 29.52 ? 201 A1BOQ A N1  1 
HETATM 1079 C  C4  . A1BOQ B 2 .   ? 7.924  9.063   25.134 1.00 42.40 ? 201 A1BOQ A C4  1 
HETATM 1080 C  C5  . A1BOQ B 2 .   ? 8.979  9.039   24.238 1.00 41.37 ? 201 A1BOQ A C5  1 
HETATM 1081 C  C6  . A1BOQ B 2 .   ? 9.647  10.205  23.916 1.00 40.48 ? 201 A1BOQ A C6  1 
HETATM 1082 C  C7  . A1BOQ B 2 .   ? 9.286  11.420  24.498 1.00 39.53 ? 201 A1BOQ A C7  1 
HETATM 1083 C  C8  . A1BOQ B 2 .   ? 10.041 12.682  24.160 1.00 35.71 ? 201 A1BOQ A C8  1 
HETATM 1084 C  C10 . A1BOQ B 2 .   ? 11.229 15.124  23.141 1.00 29.00 ? 201 A1BOQ A C10 1 
HETATM 1085 C  C13 . A1BOQ B 2 .   ? 11.185 14.667  20.247 1.00 25.70 ? 201 A1BOQ A C13 1 
HETATM 1086 C  C15 . A1BOQ B 2 .   ? 9.927  14.887  21.078 1.00 27.38 ? 201 A1BOQ A C15 1 
HETATM 1087 O  O2  . A1BOQ B 2 .   ? 10.564 16.259  18.557 1.00 24.60 ? 201 A1BOQ A O2  1 
HETATM 1088 C  C14 . A1BOQ B 2 .   ? 10.956 15.113  18.814 1.00 24.25 ? 201 A1BOQ A C14 1 
HETATM 1089 N  N2  . A1BOQ B 2 .   ? 11.219 14.211  17.886 1.00 22.63 ? 201 A1BOQ A N2  1 
HETATM 1090 C  C12 . A1BOQ B 2 .   ? 12.357 15.426  20.897 1.00 26.94 ? 201 A1BOQ A C12 1 
HETATM 1091 C  C11 . A1BOQ B 2 .   ? 12.543 15.073  22.379 1.00 27.91 ? 201 A1BOQ A C11 1 
HETATM 1092 C  C9  . A1BOQ B 2 .   ? 9.543  13.272  22.856 1.00 31.85 ? 201 A1BOQ A C9  1 
HETATM 1093 O  O1  . A1BOQ B 2 .   ? 8.610  12.777  22.241 1.00 30.09 ? 201 A1BOQ A O1  1 
HETATM 1094 C  C1  . A1BOQ B 2 .   ? 8.207  11.435  25.381 1.00 42.57 ? 201 A1BOQ A C1  1 
HETATM 1095 O  O   . A1BOQ B 2 .   ? 7.820  12.637  25.949 1.00 44.25 ? 201 A1BOQ A O   1 
HETATM 1096 C  C   . A1BOQ B 2 .   ? 6.772  13.364  25.298 1.00 44.52 ? 201 A1BOQ A C   1 
HETATM 1097 C  C2  . A1BOQ B 2 .   ? 7.508  10.268  25.702 1.00 43.62 ? 201 A1BOQ A C2  1 
HETATM 1098 C  C3  . A1BOQ B 2 .   ? 6.310  10.297  26.494 1.00 45.91 ? 201 A1BOQ A C3  1 
HETATM 1099 N  N   . A1BOQ B 2 .   ? 5.358  10.369  27.120 1.00 47.71 ? 201 A1BOQ A N   1 
HETATM 1100 ZN ZN  . ZN    C 3 .   ? 10.893 -4.753  5.652  1.00 24.47 2 202 ZN    A ZN  1 
HETATM 1101 S  S   . DMS   D 4 .   ? 19.804 -0.121  20.055 1.00 58.49 ? 203 DMS   A S   1 
HETATM 1102 O  O   . DMS   D 4 .   ? 18.334 -0.301  19.789 1.00 57.66 ? 203 DMS   A O   1 
HETATM 1103 C  C1  . DMS   D 4 .   ? 20.076 0.491   21.743 1.00 58.37 ? 203 DMS   A C1  1 
HETATM 1104 C  C2  . DMS   D 4 .   ? 20.457 1.336   19.161 1.00 58.19 ? 203 DMS   A C2  1 
HETATM 1105 O  O   . HOH   E 5 .   ? 23.727 -0.110  14.955 1.00 27.57 ? 301 HOH   A O   1 
HETATM 1106 O  O   . HOH   E 5 .   ? 2.756  7.816   9.784  1.00 37.24 ? 302 HOH   A O   1 
HETATM 1107 O  O   . HOH   E 5 .   ? 3.591  7.617   3.781  1.00 35.01 ? 303 HOH   A O   1 
HETATM 1108 O  O   . HOH   E 5 .   ? 19.997 22.564  7.842  1.00 30.01 ? 304 HOH   A O   1 
HETATM 1109 O  O   . HOH   E 5 .   ? 35.422 15.846  16.832 1.00 50.27 ? 305 HOH   A O   1 
HETATM 1110 O  O   . HOH   E 5 .   ? 22.289 -4.619  12.283 1.00 46.99 ? 306 HOH   A O   1 
HETATM 1111 O  O   . HOH   E 5 .   ? 22.881 -1.598  4.436  1.00 36.22 ? 307 HOH   A O   1 
HETATM 1112 O  O   . HOH   E 5 .   ? 8.885  2.320   2.934  1.00 27.04 ? 308 HOH   A O   1 
HETATM 1113 O  O   . HOH   E 5 .   ? 20.067 8.800   18.985 1.00 22.76 ? 309 HOH   A O   1 
HETATM 1114 O  O   . HOH   E 5 .   ? 1.000  -2.747  20.334 1.00 37.21 ? 310 HOH   A O   1 
HETATM 1115 O  O   . HOH   E 5 .   ? 3.324  -5.098  21.014 1.00 42.57 ? 311 HOH   A O   1 
HETATM 1116 O  O   . HOH   E 5 .   ? 10.434 7.942   4.624  1.00 32.50 ? 312 HOH   A O   1 
HETATM 1117 O  O   . HOH   E 5 .   ? 6.702  16.610  21.972 1.00 35.98 ? 313 HOH   A O   1 
HETATM 1118 O  O   . HOH   E 5 .   ? 10.809 -5.056  31.759 1.00 31.42 ? 314 HOH   A O   1 
HETATM 1119 O  O   . HOH   E 5 .   ? 23.609 21.935  7.970  1.00 25.59 ? 315 HOH   A O   1 
HETATM 1120 O  O   . HOH   E 5 .   ? 8.066  -3.973  0.602  1.00 28.36 ? 316 HOH   A O   1 
HETATM 1121 O  O   . HOH   E 5 .   ? 8.168  19.720  18.025 1.00 30.06 ? 317 HOH   A O   1 
HETATM 1122 O  O   . HOH   E 5 .   ? 5.525  -6.899  7.454  1.00 48.49 ? 318 HOH   A O   1 
HETATM 1123 O  O   . HOH   E 5 .   ? 17.792 21.158  9.717  1.00 22.38 ? 319 HOH   A O   1 
HETATM 1124 O  O   . HOH   E 5 .   ? 9.439  18.294  19.843 1.00 27.63 ? 320 HOH   A O   1 
HETATM 1125 O  O   . HOH   E 5 .   ? 6.552  -5.899  29.224 1.00 36.86 ? 321 HOH   A O   1 
HETATM 1126 O  O   . HOH   E 5 .   ? 23.207 18.407  19.407 1.00 42.72 ? 322 HOH   A O   1 
HETATM 1127 O  O   . HOH   E 5 .   ? 17.923 2.444   23.218 1.00 26.60 ? 323 HOH   A O   1 
HETATM 1128 O  O   . HOH   E 5 .   ? 6.154  1.266   5.981  1.00 29.07 ? 324 HOH   A O   1 
HETATM 1129 O  O   . HOH   E 5 .   ? 10.994 17.018  5.542  1.00 49.47 ? 325 HOH   A O   1 
HETATM 1130 O  O   . HOH   E 5 .   ? 0.532  -0.504  16.556 1.00 20.49 ? 326 HOH   A O   1 
HETATM 1131 O  O   . HOH   E 5 .   ? 9.933  4.303   33.906 1.00 30.02 ? 327 HOH   A O   1 
HETATM 1132 O  O   . HOH   E 5 .   ? 21.427 18.993  17.679 1.00 32.56 ? 328 HOH   A O   1 
HETATM 1133 O  O   . HOH   E 5 .   ? 10.082 4.724   3.529  1.00 24.85 ? 329 HOH   A O   1 
HETATM 1134 O  O   . HOH   E 5 .   ? 14.830 2.398   23.304 1.00 18.85 ? 330 HOH   A O   1 
HETATM 1135 O  O   . HOH   E 5 .   ? 11.231 11.415  11.404 1.00 14.05 ? 331 HOH   A O   1 
HETATM 1136 O  O   . HOH   E 5 .   ? 6.937  3.299   33.040 1.00 29.94 ? 332 HOH   A O   1 
HETATM 1137 O  O   . HOH   E 5 .   ? 10.709 14.304  1.822  1.00 48.98 ? 333 HOH   A O   1 
HETATM 1138 O  O   . HOH   E 5 .   ? 4.175  5.605   24.882 1.00 38.63 ? 334 HOH   A O   1 
HETATM 1139 O  O   . HOH   E 5 .   ? 18.130 19.072  5.578  1.00 32.39 ? 335 HOH   A O   1 
HETATM 1140 O  O   . HOH   E 5 .   ? 30.875 20.522  16.881 1.00 34.88 ? 336 HOH   A O   1 
HETATM 1141 O  O   . HOH   E 5 .   ? 6.251  17.663  24.296 1.00 40.88 ? 337 HOH   A O   1 
HETATM 1142 O  O   . HOH   E 5 .   ? 30.063 11.082  19.509 1.00 30.75 ? 338 HOH   A O   1 
HETATM 1143 O  O   . HOH   E 5 .   ? 11.200 2.108   33.576 1.00 25.00 ? 339 HOH   A O   1 
HETATM 1144 O  O   . HOH   E 5 .   ? 21.902 -5.922  10.342 1.00 36.96 ? 340 HOH   A O   1 
HETATM 1145 O  O   . HOH   E 5 .   ? 4.077  -5.284  6.620  1.00 33.12 ? 341 HOH   A O   1 
HETATM 1146 O  O   . HOH   E 5 .   ? 13.026 10.342  9.388  1.00 12.51 ? 342 HOH   A O   1 
HETATM 1147 O  O   . HOH   E 5 .   ? 0.507  1.120   24.425 1.00 41.47 ? 343 HOH   A O   1 
HETATM 1148 O  O   . HOH   E 5 .   ? 14.721 -4.706  17.216 1.00 25.98 ? 344 HOH   A O   1 
HETATM 1149 O  O   . HOH   E 5 .   ? 5.325  -1.778  24.385 1.00 24.67 ? 345 HOH   A O   1 
HETATM 1150 O  O   . HOH   E 5 .   ? 18.619 9.126   25.832 1.00 35.78 ? 346 HOH   A O   1 
HETATM 1151 O  O   . HOH   E 5 .   ? 17.929 18.798  17.056 1.00 18.11 ? 347 HOH   A O   1 
HETATM 1152 O  O   . HOH   E 5 .   ? 27.542 15.834  2.745  1.00 42.82 ? 348 HOH   A O   1 
HETATM 1153 O  O   . HOH   E 5 .   ? 16.827 -7.576  10.794 1.00 37.58 ? 349 HOH   A O   1 
HETATM 1154 O  O   . HOH   E 5 .   ? 2.043  9.486   28.365 1.00 55.65 ? 350 HOH   A O   1 
HETATM 1155 O  O   . HOH   E 5 .   ? 14.406 14.222  3.570  1.00 30.24 ? 351 HOH   A O   1 
HETATM 1156 O  O   . HOH   E 5 .   ? 6.727  12.545  5.507  1.00 28.08 ? 352 HOH   A O   1 
HETATM 1157 O  O   . HOH   E 5 .   ? -0.350 15.707  8.326  1.00 57.56 ? 353 HOH   A O   1 
HETATM 1158 O  O   . HOH   E 5 .   ? 14.959 12.196  24.202 1.00 27.48 ? 354 HOH   A O   1 
HETATM 1159 O  O   . HOH   E 5 .   ? 13.628 -11.460 4.149  1.00 43.86 ? 355 HOH   A O   1 
HETATM 1160 O  O   . HOH   E 5 .   ? 18.706 12.642  2.014  1.00 34.04 ? 356 HOH   A O   1 
HETATM 1161 O  O   . HOH   E 5 .   ? 14.005 8.932   30.241 1.00 46.97 ? 357 HOH   A O   1 
HETATM 1162 O  O   . HOH   E 5 .   ? 16.112 -11.367 5.309  1.00 47.87 ? 358 HOH   A O   1 
HETATM 1163 O  O   . HOH   E 5 .   ? 2.719  3.067   27.556 1.00 34.13 ? 359 HOH   A O   1 
HETATM 1164 O  O   . HOH   E 5 .   ? 8.681  -7.616  9.243  1.00 39.40 ? 360 HOH   A O   1 
HETATM 1165 O  O   . HOH   E 5 .   ? 4.276  10.216  19.344 1.00 56.93 ? 361 HOH   A O   1 
HETATM 1166 O  O   . HOH   E 5 .   ? 14.271 20.864  8.401  1.00 37.61 ? 362 HOH   A O   1 
HETATM 1167 O  O   . HOH   E 5 .   ? 19.569 23.616  15.443 1.00 26.09 ? 363 HOH   A O   1 
HETATM 1168 O  O   . HOH   E 5 .   ? 15.703 -4.718  1.868  1.00 29.92 ? 364 HOH   A O   1 
HETATM 1169 O  O   . HOH   E 5 .   ? 22.336 18.869  6.039  1.00 23.70 ? 365 HOH   A O   1 
HETATM 1170 O  O   . HOH   E 5 .   ? 18.049 0.773   30.038 1.00 38.35 ? 366 HOH   A O   1 
HETATM 1171 O  O   . HOH   E 5 .   ? 9.383  20.894  10.813 1.00 37.55 ? 367 HOH   A O   1 
HETATM 1172 O  O   . HOH   E 5 .   ? 5.713  22.604  10.995 1.00 43.48 ? 368 HOH   A O   1 
HETATM 1173 O  O   . HOH   E 5 .   ? 12.289 -7.991  13.253 1.00 30.97 ? 369 HOH   A O   1 
HETATM 1174 O  O   . HOH   E 5 .   ? -1.235 -4.623  15.737 0.50 35.27 ? 370 HOH   A O   1 
HETATM 1175 O  O   . HOH   E 5 .   ? 28.537 -2.042  13.201 1.00 48.25 ? 371 HOH   A O   1 
HETATM 1176 O  O   . HOH   E 5 .   ? 6.899  -5.301  2.930  1.00 33.61 ? 372 HOH   A O   1 
HETATM 1177 O  O   . HOH   E 5 .   ? 1.448  -2.734  17.651 1.00 25.75 ? 373 HOH   A O   1 
HETATM 1178 O  O   . HOH   E 5 .   ? 11.720 21.214  12.285 1.00 30.03 ? 374 HOH   A O   1 
HETATM 1179 O  O   . HOH   E 5 .   ? 21.922 8.738   21.087 1.00 29.74 ? 375 HOH   A O   1 
HETATM 1180 O  O   . HOH   E 5 .   ? 2.019  5.639   28.120 1.00 44.29 ? 376 HOH   A O   1 
HETATM 1181 O  O   . HOH   E 5 .   ? 4.785  7.434   28.518 1.00 46.83 ? 377 HOH   A O   1 
HETATM 1182 O  O   . HOH   E 5 .   ? 32.554 14.249  20.857 1.00 46.42 ? 378 HOH   A O   1 
HETATM 1183 O  O   . HOH   E 5 .   ? 30.859 15.415  22.370 1.00 38.06 ? 379 HOH   A O   1 
HETATM 1184 O  O   . HOH   E 5 .   ? 23.931 2.141   19.338 1.00 51.17 ? 380 HOH   A O   1 
HETATM 1185 O  O   . HOH   E 5 .   ? 17.203 22.614  16.980 1.00 33.46 ? 381 HOH   A O   1 
HETATM 1186 O  O   . HOH   E 5 .   ? 17.475 -7.956  24.727 1.00 46.17 ? 382 HOH   A O   1 
HETATM 1187 O  O   . HOH   E 5 .   ? 2.679  15.189  19.891 1.00 38.38 ? 383 HOH   A O   1 
HETATM 1188 O  O   . HOH   E 5 .   ? 6.163  -8.158  14.395 1.00 33.99 ? 384 HOH   A O   1 
HETATM 1189 O  O   . HOH   E 5 .   ? 10.876 17.212  26.394 1.00 46.90 ? 385 HOH   A O   1 
HETATM 1190 O  O   . HOH   E 5 .   ? 0.319  -3.211  9.686  1.00 47.71 ? 386 HOH   A O   1 
HETATM 1191 O  O   . HOH   E 5 .   ? 20.667 21.956  17.747 1.00 30.42 ? 387 HOH   A O   1 
HETATM 1192 O  O   . HOH   E 5 .   ? 7.983  -5.387  31.756 1.00 45.70 ? 388 HOH   A O   1 
HETATM 1193 O  O   . HOH   E 5 .   ? 16.836 -3.674  17.915 1.00 37.29 ? 389 HOH   A O   1 
HETATM 1194 O  O   . HOH   E 5 .   ? 27.949 16.890  23.483 1.00 49.46 ? 390 HOH   A O   1 
HETATM 1195 O  O   . HOH   E 5 .   ? 13.877 14.129  26.170 1.00 42.99 ? 391 HOH   A O   1 
HETATM 1196 O  O   . HOH   E 5 .   ? 2.084  0.758   26.698 1.00 34.68 ? 392 HOH   A O   1 
HETATM 1197 O  O   . HOH   E 5 .   ? 8.535  17.602  25.786 1.00 41.84 ? 393 HOH   A O   1 
HETATM 1198 O  O   . HOH   E 5 .   ? 3.863  12.486  18.640 1.00 51.49 ? 394 HOH   A O   1 
HETATM 1199 O  O   . HOH   E 5 .   ? 5.286  14.290  21.299 1.00 47.49 ? 395 HOH   A O   1 
HETATM 1200 O  O   . HOH   E 5 .   ? 8.943  19.709  6.355  1.00 59.14 ? 396 HOH   A O   1 
HETATM 1201 O  O   . HOH   E 5 .   ? 11.740 23.281  14.065 1.00 38.86 ? 397 HOH   A O   1 
HETATM 1202 O  O   . HOH   E 5 .   ? 8.836  22.590  26.642 1.00 43.45 ? 398 HOH   A O   1 
HETATM 1203 O  O   . HOH   E 5 .   ? 0.827  -2.390  23.713 1.00 35.80 ? 399 HOH   A O   1 
HETATM 1204 O  O   . HOH   E 5 .   ? 32.690 21.853  14.850 1.00 36.64 ? 400 HOH   A O   1 
HETATM 1205 O  O   . HOH   E 5 .   ? 3.639  -3.543  23.168 1.00 36.94 ? 401 HOH   A O   1 
HETATM 1206 O  O   . HOH   E 5 .   ? 20.260 -3.631  22.782 1.00 63.86 ? 402 HOH   A O   1 
HETATM 1207 O  O   . HOH   E 5 .   ? 0.824  11.368  18.006 1.00 54.89 ? 403 HOH   A O   1 
HETATM 1208 O  O   . HOH   E 5 .   ? 9.909  24.999  12.939 1.00 44.04 ? 404 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   ? 0.6492 0.2325 0.3200 -0.0603 -0.1647 0.0136  7   SER   A N   
2    C CA  . SER   A 1   ? 0.6191 0.2443 0.3717 -0.0588 -0.1868 0.0230  7   SER   A CA  
3    C C   . SER   A 1   ? 0.5467 0.2370 0.3826 -0.0466 -0.1750 0.0227  7   SER   A C   
4    O O   . SER   A 1   ? 0.5480 0.2442 0.3756 -0.0445 -0.1643 0.0192  7   SER   A O   
5    C CB  . SER   A 1   ? 0.6809 0.2593 0.4250 -0.0825 -0.2387 0.0419  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.7434 0.3091 0.4884 -0.0932 -0.2586 0.0509  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.4816 0.2135 0.3927 -0.0401 -0.1749 0.0262  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.4238 0.2056 0.4095 -0.0312 -0.1586 0.0253  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.3725 0.1938 0.4071 -0.0205 -0.1348 0.0194  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.3842 0.2067 0.3927 -0.0157 -0.1240 0.0126  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.3115 0.1605 0.4162 -0.0178 -0.1242 0.0222  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.2835 0.1597 0.4309 -0.0111 -0.0985 0.0168  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.2537 0.1513 0.4408 -0.0084 -0.0684 0.0112  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.2517 0.1469 0.4563 -0.0110 -0.0726 0.0155  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.2887 0.1587 0.4935 -0.0147 -0.1187 0.0316  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.2371 0.1495 0.4351 -0.0055 -0.0377 0.0019  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.2262 0.1452 0.4540 -0.0068 -0.0031 -0.0046 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.2289 0.1453 0.5316 -0.0062 0.0099  0.0030  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.2263 0.1436 0.5319 -0.0046 0.0061  0.0044  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.2480 0.1726 0.4212 -0.0095 0.0222  -0.0190 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.2610 0.1907 0.3734 -0.0087 0.0088  -0.0219 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.2658 0.1825 0.4501 -0.0162 0.0590  -0.0270 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2600 0.1966 0.3299 -0.0129 0.0225  -0.0284 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.2468 0.1591 0.6125 -0.0070 0.0289  0.0083  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.2460 0.1531 0.6989 -0.0056 0.0505  0.0179  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.2678 0.1609 0.7222 -0.0088 0.1065  0.0040  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.2861 0.1733 0.7495 -0.0108 0.1216  0.0019  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2386 0.1461 0.7787 -0.0054 0.0254  0.0416  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2518 0.1592 0.7833 -0.0083 -0.0322 0.0577  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2643 0.1705 0.8301 -0.0084 -0.0493 0.0697  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2889 0.1905 0.7621 -0.0129 -0.0673 0.0586  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2914 0.1870 0.8333 -0.0150 -0.1024 0.0834  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.3188 0.2055 0.7617 -0.0196 -0.1160 0.0707  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.3236 0.2055 0.8022 -0.0219 -0.1352 0.0841  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.3639 0.2215 0.8030 -0.0323 -0.1838 0.0960  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.2865 0.1682 0.7213 -0.0115 0.1374  -0.0064 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.3269 0.1798 0.7380 -0.0202 0.1931  -0.0219 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.3404 0.1757 0.8049 -0.0194 0.2279  -0.0192 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.3444 0.1875 0.7939 -0.0179 0.2139  -0.0186 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.3943 0.2413 0.6915 -0.0311 0.1929  -0.0392 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.3977 0.2625 0.6577 -0.0289 0.1628  -0.0383 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.4464 0.2505 0.7014 -0.0467 0.2464  -0.0543 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.3418 0.1530 0.8781 -0.0192 0.2745  -0.0155 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.3592 0.1502 0.9618 -0.0172 0.3145  -0.0104 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.3420 0.1647 1.0236 -0.0061 0.2717  0.0122  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.3319 0.1810 1.0668 -0.0002 0.2252  0.0315  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.3413 0.1600 1.0123 -0.0061 0.2785  0.0095  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.3079 0.1529 1.0439 0.0022  0.2361  0.0304  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.2883 0.1567 0.9371 0.0015  0.1808  0.0248  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2740 0.1534 0.9390 0.0049  0.1568  0.0333  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.3441 0.1708 1.1384 0.0041  0.2782  0.0342  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.4090 0.2144 1.3235 0.0079  0.3302  0.0483  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.4046 0.2233 1.4041 0.0124  0.3135  0.0685  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.4615 0.2293 1.3877 0.0053  0.3968  0.0391  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.2767 0.1512 0.8390 -0.0025 0.1623  0.0121  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.2699 0.1618 0.7515 -0.0027 0.1193  0.0066  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.2408 0.1462 0.7062 -0.0010 0.0742  0.0140  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.2353 0.1382 0.7130 -0.0022 0.0795  0.0149  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.2870 0.1694 0.6682 -0.0113 0.1407  -0.0148 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.3149 0.1759 0.6827 -0.0178 0.1798  -0.0237 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.3194 0.1876 0.7114 -0.0132 0.1702  -0.0176 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.3519 0.1784 0.6782 -0.0308 0.2273  -0.0379 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.3557 0.2007 0.7349 -0.0200 0.2077  -0.0254 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.3941 0.1897 0.6954 -0.0408 0.2648  -0.0464 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.4078 0.2143 0.7385 -0.0345 0.2555  -0.0400 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.4605 0.2344 0.7639 -0.0449 0.2922  -0.0481 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.2260 0.1405 0.6568 0.0006  0.0325  0.0182  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.2104 0.1266 0.6019 -0.0003 -0.0073 0.0224  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.2019 0.1220 0.5036 0.0001  -0.0118 0.0084  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1935 0.1154 0.4806 0.0017  -0.0162 0.0072  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.2099 0.1194 0.6458 -0.0024 -0.0525 0.0444  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.2779 0.1741 0.6467 -0.0071 -0.0946 0.0469  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.3166 0.1948 0.7262 -0.0157 -0.1416 0.0715  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.3619 0.2152 0.6920 -0.0222 -0.1746 0.0707  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.3997 0.2246 0.6698 -0.0317 -0.2028 0.0735  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.3665 0.1909 0.6492 -0.0348 -0.2059 0.0776  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.4282 0.2200 0.6200 -0.0387 -0.2241 0.0711  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.2042 0.1263 0.4524 -0.0011 -0.0089 -0.0005 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.2166 0.1436 0.3931 -0.0005 -0.0116 -0.0094 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.2254 0.1419 0.3681 0.0008  -0.0417 -0.0045 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.2194 0.1306 0.3604 -0.0009 -0.0484 -0.0023 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.2194 0.1518 0.3609 -0.0050 0.0123  -0.0196 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.2228 0.1633 0.3099 -0.0054 0.0097  -0.0230 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.2046 0.1302 0.3685 -0.0117 0.0469  -0.0257 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.2354 0.1443 0.3434 0.0028  -0.0552 -0.0039 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.2626 0.1469 0.3253 0.0015  -0.0771 -0.0007 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.2557 0.1393 0.2685 0.0060  -0.0658 -0.0068 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.2442 0.1466 0.2656 0.0089  -0.0518 -0.0098 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.3080 0.1652 0.3817 -0.0046 -0.1096 0.0112  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.3293 0.1837 0.4603 -0.0107 -0.1273 0.0240  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.3113 0.1751 0.4036 -0.0021 -0.1084 0.0121  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.2684 0.1248 0.2309 0.0055  -0.0712 -0.0069 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.2609 0.1090 0.1860 0.0105  -0.0572 -0.0096 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.2868 0.1223 0.2127 0.0097  -0.0677 -0.0076 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.3203 0.1284 0.2436 0.0021  -0.0929 -0.0024 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.3018 0.1071 0.1695 0.0085  -0.0561 -0.0101 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.3344 0.1512 0.2007 0.0100  -0.0451 -0.0114 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.3492 0.1589 0.2187 0.0042  -0.0596 -0.0101 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.3121 0.1490 0.1813 0.0169  -0.0215 -0.0114 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.2610 0.1156 0.1937 0.0156  -0.0522 -0.0091 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.2680 0.1134 0.2035 0.0155  -0.0604 -0.0075 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.3468 0.1374 0.2279 0.0106  -0.0715 -0.0067 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.3813 0.1500 0.2606 0.0040  -0.0937 -0.0028 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.2566 0.1304 0.2063 0.0218  -0.0416 -0.0079 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.2648 0.1377 0.2270 0.0223  -0.0488 -0.0066 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.2682 0.1623 0.2366 0.0275  -0.0307 -0.0046 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.2581 0.1577 0.2415 0.0284  -0.0347 -0.0034 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.3123 0.1842 0.2737 0.0305  -0.0372 -0.0031 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.3309 0.1592 0.2472 0.0297  -0.0356 -0.0047 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.2965 0.1778 0.2748 0.0318  -0.0396 -0.0015 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.3713 0.1330 0.2055 0.0114  -0.0559 -0.0094 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.4499 0.1427 0.2143 0.0030  -0.0595 -0.0105 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.5129 0.1614 0.2453 -0.0138 -0.0947 -0.0060 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.5941 0.1768 0.2626 -0.0277 -0.1087 -0.0047 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.4799 0.1465 0.2047 0.0087  -0.0240 -0.0143 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.4938 0.1541 0.2039 0.0071  -0.0185 -0.0151 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.4655 0.1821 0.2263 0.0162  -0.0073 -0.0134 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.5439 0.1426 0.1882 -0.0043 -0.0218 -0.0171 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.4886 0.1838 0.2220 0.0123  -0.0055 -0.0145 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.5480 0.1720 0.2105 0.0002  -0.0128 -0.0169 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.4714 0.1526 0.2497 -0.0151 -0.1112 -0.0016 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.5053 0.1528 0.2729 -0.0318 -0.1490 0.0080  22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.4875 0.1626 0.3274 -0.0351 -0.1781 0.0197  22  LEU   A C   
124  O O   . LEU   A 16  ? 0.5126 0.1716 0.3704 -0.0483 -0.2119 0.0331  22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.5035 0.1597 0.2726 -0.0316 -0.1444 0.0071  22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.5593 0.1775 0.2566 -0.0307 -0.1173 -0.0015 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.5473 0.1775 0.2506 -0.0302 -0.1139 -0.0017 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.6372 0.1670 0.2406 -0.0488 -0.1287 -0.0007 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.4488 0.1685 0.3399 -0.0232 -0.1630 0.0168  23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.4261 0.1709 0.3925 -0.0247 -0.1819 0.0280  23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.4736 0.1721 0.4270 -0.0418 -0.2247 0.0433  23  ALA   A C   
132  O O   . ALA   A 17  ? 0.5258 0.1795 0.4094 -0.0488 -0.2299 0.0401  23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.3780 0.1672 0.3858 -0.0115 -0.1557 0.0211  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.4708 0.1777 0.4943 -0.0494 -0.2538 0.0617  24  THR   A N   
135  C CA  . THR   A 18  ? 0.5144 0.1796 0.5428 -0.0696 -0.3041 0.0837  24  THR   A CA  
136  C C   . THR   A 18  ? 0.5049 0.1910 0.5885 -0.0647 -0.3068 0.0900  24  THR   A C   
137  O O   . THR   A 18  ? 0.4664 0.1987 0.5851 -0.0461 -0.2686 0.0768  24  THR   A O   
138  C CB  . THR   A 18  ? 0.5170 0.1855 0.6134 -0.0803 -0.3353 0.1062  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.4883 0.2162 0.6951 -0.0644 -0.3111 0.1091  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.5392 0.1912 0.5892 -0.0848 -0.3330 0.1009  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.5442 0.1948 0.6395 -0.0835 -0.3545 0.1125  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.5413 0.2115 0.6978 -0.0796 -0.3598 0.1215  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.4665 0.1978 0.7480 -0.0641 -0.3368 0.1283  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.4389 0.2047 0.7554 -0.0489 -0.3050 0.1186  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.6109 0.2285 0.7636 -0.1066 -0.4225 0.1500  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.7680 0.3119 0.7882 -0.1250 -0.4409 0.1424  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.8316 0.3700 0.7956 -0.1149 -0.4118 0.1220  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.8615 0.3284 0.7964 -0.1550 -0.4845 0.1542  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.9126 0.3701 0.7598 -0.1372 -0.4324 0.1202  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.9373 0.3455 0.7563 -0.1634 -0.4768 0.1387  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.4357 0.1758 0.7804 -0.0685 -0.3484 0.1442  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.3928 0.1809 0.8561 -0.0549 -0.3191 0.1508  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.3574 0.1821 0.8033 -0.0345 -0.2571 0.1208  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.3452 0.1988 0.8544 -0.0231 -0.2236 0.1179  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.4193 0.2063 0.9472 -0.0633 -0.3390 0.1723  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.4633 0.2899 1.1251 -0.0511 -0.3070 0.1836  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.4624 0.2966 1.2155 -0.0518 -0.3162 0.2052  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.4624 0.3103 1.1394 -0.0403 -0.2659 0.1699  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.3459 0.1649 0.7045 -0.0317 -0.2414 0.0997  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.3142 0.1635 0.6478 -0.0165 -0.1899 0.0742  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.2992 0.1601 0.6203 -0.0091 -0.1718 0.0642  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.2913 0.1784 0.6481 -0.0006 -0.1358 0.0563  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.3364 0.1725 0.5772 -0.0167 -0.1847 0.0583  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.3497 0.1827 0.5989 -0.0207 -0.1895 0.0623  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.3061 0.1603 0.6320 -0.0178 -0.1761 0.0690  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.3923 0.1974 0.5719 -0.0274 -0.2045 0.0593  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.3071 0.1427 0.5750 -0.0145 -0.1964 0.0654  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.3023 0.1484 0.5576 -0.0077 -0.1811 0.0568  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.2980 0.1595 0.6420 -0.0062 -0.1822 0.0705  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.2878 0.1699 0.6426 0.0020  -0.1543 0.0613  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.3199 0.1280 0.4950 -0.0144 -0.2038 0.0547  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.3282 0.1319 0.4268 -0.0088 -0.1797 0.0368  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.3792 0.1509 0.4145 -0.0147 -0.1856 0.0333  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.3086 0.1410 0.3947 0.0030  -0.1449 0.0228  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.3841 0.1636 0.3749 -0.0054 -0.1541 0.0187  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.3467 0.1660 0.3717 0.0049  -0.1314 0.0137  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.2880 0.1529 0.4098 0.0103  -0.1249 0.0193  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.3426 0.1824 0.3505 0.0138  -0.1028 0.0048  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.2826 0.1653 0.3770 0.0169  -0.0993 0.0092  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.3063 0.1792 0.3505 0.0187  -0.0898 0.0037  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.3087 0.1596 0.7202 -0.0149 -0.2130 0.0941  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.3044 0.1684 0.8166 -0.0136 -0.2141 0.1123  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2857 0.1787 0.8728 -0.0028 -0.1643 0.1079  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2733 0.1777 0.9342 0.0019  -0.1454 0.1157  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.3028 0.1433 0.8716 -0.0292 -0.2685 0.1452  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.2701 0.1690 0.8363 -0.0003 -0.1413 0.0961  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.2424 0.1564 0.8538 0.0066  -0.0900 0.0878  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.2221 0.1423 0.7428 0.0100  -0.0565 0.0593  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.2022 0.1244 0.7212 0.0104  -0.0278 0.0506  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.2584 0.1696 0.9337 0.0033  -0.0968 0.1036  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2949 0.2032 1.0857 -0.0009 -0.1239 0.1372  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.3024 0.2181 1.1750 0.0048  -0.0946 0.1449  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.3008 0.1945 1.1013 -0.0128 -0.1800 0.1596  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.2290 0.1504 0.6792 0.0110  -0.0627 0.0477  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.2210 0.1491 0.5947 0.0121  -0.0390 0.0272  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.2283 0.1598 0.6099 0.0110  0.0088  0.0160  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2414 0.1707 0.6642 0.0117  0.0273  0.0187  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.2204 0.1490 0.5408 0.0135  -0.0541 0.0226  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.2538 0.1915 0.5061 0.0137  -0.0354 0.0075  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.2809 0.2158 0.4884 0.0129  -0.0415 0.0033  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.2398 0.1783 0.4608 0.0161  -0.0466 0.0068  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.2238 0.1543 0.5606 0.0070  0.0294  0.0038  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2370 0.1575 0.5530 -0.0005 0.0723  -0.0082 32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2549 0.1813 0.4897 -0.0063 0.0674  -0.0173 32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2815 0.2014 0.4934 -0.0131 0.0836  -0.0218 32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2592 0.1682 0.5810 -0.0049 0.0958  -0.0125 32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2952 0.1821 0.5637 -0.0184 0.1357  -0.0266 32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2488 0.1518 0.6646 0.0002  0.1060  -0.0002 32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.2322 0.1695 0.4298 -0.0040 0.0436  -0.0172 33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.2265 0.1719 0.3659 -0.0085 0.0374  -0.0201 33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.2094 0.1637 0.3303 -0.0008 0.0116  -0.0163 33  TRP   A C   
212  O O   . TRP   A 27  ? 0.1955 0.1457 0.3267 0.0023  0.0041  -0.0152 33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2397 0.1741 0.3425 -0.0228 0.0598  -0.0266 33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2613 0.2040 0.3138 -0.0308 0.0490  -0.0242 33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2885 0.2333 0.3140 -0.0402 0.0456  -0.0201 33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2572 0.2079 0.2903 -0.0305 0.0388  -0.0219 33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2888 0.2431 0.2857 -0.0468 0.0327  -0.0129 33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2714 0.2305 0.2738 -0.0394 0.0293  -0.0143 33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2481 0.2008 0.2924 -0.0229 0.0340  -0.0231 33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2702 0.2382 0.2563 -0.0420 0.0198  -0.0079 33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2620 0.2218 0.2814 -0.0252 0.0266  -0.0199 33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2588 0.2271 0.2526 -0.0337 0.0201  -0.0119 33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.1979 0.1605 0.2909 0.0010  0.0019  -0.0138 34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.2027 0.1655 0.2739 0.0075  -0.0124 -0.0109 34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.2008 0.1759 0.2488 0.0049  -0.0091 -0.0065 34  GLU   A C   
226  O O   . GLU   A 28  ? 0.1977 0.1797 0.2472 -0.0003 -0.0055 -0.0041 34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.2390 0.1873 0.3154 0.0151  -0.0309 -0.0080 34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.2425 0.1921 0.3301 0.0170  -0.0343 -0.0059 34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2774 0.2333 0.3429 0.0197  -0.0314 -0.0036 34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.3113 0.2756 0.3883 0.0188  -0.0289 -0.0022 34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2731 0.2238 0.3146 0.0229  -0.0299 -0.0019 34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.1951 0.1717 0.2271 0.0075  -0.0106 -0.0031 35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.1886 0.1781 0.2151 0.0057  -0.0085 0.0067  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.1989 0.1790 0.2177 0.0165  -0.0068 0.0102  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.2083 0.1836 0.2176 0.0171  -0.0045 0.0091  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.2060 0.2052 0.2247 -0.0091 -0.0056 0.0112  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.2745 0.2883 0.2984 -0.0158 -0.0103 0.0278  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.2902 0.3089 0.3299 -0.0047 -0.0092 0.0361  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.3010 0.3167 0.3132 -0.0343 -0.0146 0.0344  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.1960 0.1679 0.2159 0.0244  -0.0041 0.0141  36  SER   A N   
241  C CA  A SER   A 30  ? 0.2167 0.1670 0.2227 0.0333  0.0066  0.0164  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.2181 0.1682 0.2236 0.0332  0.0064  0.0162  36  SER   A CA  
243  C C   . SER   A 30  ? 0.2120 0.1781 0.2343 0.0329  0.0172  0.0285  36  SER   A C   
244  O O   . SER   A 30  ? 0.2384 0.1864 0.2479 0.0381  0.0285  0.0283  36  SER   A O   
245  C CB  A SER   A 30  ? 0.2501 0.1855 0.2559 0.0400  0.0140  0.0193  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.2561 0.1893 0.2593 0.0399  0.0134  0.0183  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.2926 0.2135 0.2864 0.0390  0.0011  0.0109  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.2727 0.2350 0.3102 0.0385  0.0162  0.0307  36  SER   A OG  
249  N N   . SER   A 31  ? 0.1846 0.1810 0.2348 0.0245  0.0121  0.0412  37  SER   A N   
250  C CA  . SER   A 31  ? 0.1838 0.1965 0.2597 0.0215  0.0164  0.0589  37  SER   A CA  
251  C C   . SER   A 31  ? 0.1955 0.2085 0.2562 0.0163  0.0135  0.0545  37  SER   A C   
252  O O   . SER   A 31  ? 0.2119 0.2321 0.2924 0.0167  0.0191  0.0680  37  SER   A O   
253  C CB  . SER   A 31  ? 0.2103 0.2493 0.3151 0.0078  0.0032  0.0775  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.2471 0.2917 0.3305 -0.0103 -0.0122 0.0738  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1731 0.1777 0.2062 0.0122  0.0063  0.0376  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1771 0.1794 0.1957 0.0077  0.0049  0.0316  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1976 0.1751 0.1946 0.0175  0.0087  0.0185  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1998 0.1743 0.1873 0.0153  0.0079  0.0142  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1745 0.1813 0.1820 -0.0074 -0.0024 0.0250  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.1724 0.1919 0.1840 -0.0246 -0.0102 0.0390  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.1871 0.1949 0.1724 -0.0425 -0.0102 0.0299  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.1906 0.1897 0.1599 -0.0473 -0.0057 0.0228  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.2309 0.2140 0.1711 -0.0678 -0.0030 0.0196  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2586 0.2282 0.1759 -0.0875 -0.0051 0.0232  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.2455 0.2200 0.1732 -0.0710 0.0028  0.0133  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.2193 0.1753 0.2049 0.0252  0.0095  0.0129  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.2209 0.1437 0.1778 0.0284  0.0049  0.0031  39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.2206 0.1483 0.1838 0.0221  -0.0089 -0.0040 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.2330 0.1438 0.1824 0.0212  -0.0147 -0.0075 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.2407 0.1411 0.1752 0.0325  0.0173  0.0045  39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.2999 0.1551 0.1919 0.0307  0.0089  -0.0038 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.3023 0.1326 0.1767 0.0288  -0.0010 -0.0069 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.3162 0.1587 0.1909 0.0288  0.0090  -0.0056 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.2005 0.1487 0.1865 0.0168  -0.0111 -0.0050 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1819 0.1303 0.1841 0.0118  -0.0158 -0.0107 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1857 0.1297 0.2084 0.0121  -0.0224 -0.0118 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1980 0.1484 0.2233 0.0128  -0.0203 -0.0102 40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1773 0.1422 0.1861 0.0021  -0.0043 -0.0120 40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1889 0.1591 0.1835 -0.0016 -0.0002 -0.0098 40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.1806 0.1551 0.1702 -0.0166 0.0093  -0.0114 40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.1970 0.1549 0.1900 0.0030  -0.0048 -0.0135 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1658 0.1008 0.2116 0.0106  -0.0300 -0.0125 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1911 0.1231 0.2723 0.0103  -0.0361 -0.0102 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1853 0.1187 0.3071 0.0069  -0.0286 -0.0099 41  LEU   A C   
285  O O   . LEU   A 35  ? 0.2159 0.1441 0.3365 0.0059  -0.0333 -0.0090 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.2147 0.1231 0.2894 0.0118  -0.0617 -0.0040 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.2190 0.1256 0.3384 0.0107  -0.0721 0.0023  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.2538 0.1391 0.3479 0.0105  -0.0917 0.0062  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.2191 0.1170 0.3883 0.0063  -0.0881 0.0126  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1770 0.1151 0.3343 0.0047  -0.0114 -0.0109 42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1843 0.1183 0.3914 0.0022  0.0054  -0.0097 42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1875 0.1178 0.4554 0.0048  -0.0010 0.0001  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.1972 0.1299 0.4642 0.0058  0.0016  -0.0005 42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.2050 0.1359 0.3970 -0.0058 0.0421  -0.0199 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.2124 0.1304 0.4593 -0.0079 0.0686  -0.0191 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.2261 0.1610 0.3610 -0.0108 0.0420  -0.0256 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1905 0.1153 0.5153 0.0052  -0.0116 0.0117  43  SER   A N   
298  C CA  . SER   A 37  ? 0.1951 0.1168 0.5961 0.0064  -0.0210 0.0272  43  SER   A CA  
299  C C   . SER   A 37  ? 0.2023 0.1213 0.6820 0.0064  0.0089  0.0333  43  SER   A C   
300  O O   . SER   A 37  ? 0.1998 0.1165 0.6742 0.0048  0.0246  0.0282  43  SER   A O   
301  C CB  . SER   A 37  ? 0.2113 0.1228 0.6181 0.0035  -0.0713 0.0437  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.2315 0.1352 0.6460 -0.0008 -0.0901 0.0518  43  SER   A OG  
303  N N   . SER   A 38  ? 0.2111 0.1284 0.7723 0.0085  0.0173  0.0466  44  SER   A N   
304  C CA  . SER   A 38  ? 0.2336 0.1444 0.8866 0.0097  0.0521  0.0558  44  SER   A CA  
305  C C   . SER   A 38  ? 0.2519 0.1649 0.9880 0.0085  0.0170  0.0825  44  SER   A C   
306  O O   . SER   A 38  ? 0.2579 0.1718 0.9938 0.0045  -0.0373 0.0985  44  SER   A O   
307  C CB  . SER   A 38  ? 0.2288 0.1337 0.9416 0.0125  0.0847  0.0599  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2584 0.1720 1.0025 0.0139  0.0424  0.0770  44  SER   A OG  
309  N N   . THR   A 39  ? 0.2603 0.1687 1.0637 0.0095  0.0475  0.0885  45  THR   A N   
310  C CA  . THR   A 39  ? 0.2857 0.1964 1.1804 0.0071  0.0170  0.1171  45  THR   A CA  
311  C C   . THR   A 39  ? 0.3277 0.2343 1.3599 0.0117  0.0584  0.1360  45  THR   A C   
312  O O   . THR   A 39  ? 0.3502 0.2441 1.3827 0.0160  0.1229  0.1189  45  THR   A O   
313  C CB  . THR   A 39  ? 0.2950 0.2044 1.1479 0.0047  0.0186  0.1077  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.2992 0.1988 1.1602 0.0082  0.0851  0.0910  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.3227 0.2336 1.0429 0.0016  -0.0078 0.0871  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.3377 0.2493 1.4855 0.0088  0.0233  0.1725  46  THR   A N   
317  C CA  . THR   A 40  ? 0.3332 0.2426 1.6399 0.0134  0.0582  0.1995  46  THR   A CA  
318  C C   . THR   A 40  ? 0.3474 0.2513 1.6943 0.0148  0.0911  0.1997  46  THR   A C   
319  O O   . THR   A 40  ? 0.3376 0.2315 1.7957 0.0209  0.1480  0.2104  46  THR   A O   
320  C CB  . THR   A 40  ? 0.3213 0.2399 1.7378 0.0062  -0.0084 0.2454  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.3685 0.2875 1.7435 -0.0058 -0.0743 0.2569  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.3268 0.2474 1.7157 0.0041  -0.0388 0.2480  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.3653 0.2731 1.6325 0.0089  0.0550  0.1914  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.3555 0.2592 1.6481 0.0095  0.0802  0.1901  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.3935 0.2836 1.5612 0.0119  0.1346  0.1462  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.4318 0.3218 1.4800 0.0105  0.1286  0.1207  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.3653 0.2774 1.6436 -0.0004 0.0079  0.2086  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.3832 0.2590 1.5817 0.0138  0.1868  0.1396  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.4288 0.2830 1.5164 0.0118  0.2393  0.1020  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.4391 0.3043 1.4244 0.0069  0.2015  0.0884  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.4327 0.3095 1.4658 0.0062  0.1696  0.1066  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.4547 0.2777 1.6213 0.0140  0.3192  0.1014  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.5700 0.3610 1.6280 0.0070  0.3704  0.0672  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.6956 0.4504 1.6551 -0.0003 0.4202  0.0381  48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.7125 0.4624 1.6997 0.0022  0.4327  0.0421  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.7506 0.4760 1.5918 -0.0118 0.4481  0.0097  48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.4458 0.3056 1.2965 0.0027  0.2068  0.0585  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.4518 0.3199 1.1982 -0.0015 0.1791  0.0432  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.4407 0.2856 1.1433 -0.0068 0.2289  0.0232  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.4626 0.2758 1.1523 -0.0113 0.2876  0.0090  49  GLY   A O   
341  N N   . CYS   A 44  ? 0.4089 0.2631 1.0776 -0.0085 0.2063  0.0212  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.4055 0.2369 1.0380 -0.0146 0.2487  0.0051  50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.4014 0.2364 0.9126 -0.0216 0.2311  -0.0137 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.4215 0.2404 0.9055 -0.0276 0.2552  -0.0235 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.4030 0.2374 1.1344 -0.0104 0.2517  0.0233  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.4678 0.2843 1.3545 -0.0044 0.3016  0.0441  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.3680 0.2225 0.8125 -0.0212 0.1910  -0.0170 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.3848 0.2439 0.7294 -0.0274 0.1762  -0.0305 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.4125 0.2418 0.6857 -0.0412 0.2154  -0.0486 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.4453 0.2557 0.7182 -0.0453 0.2410  -0.0528 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.3992 0.2833 0.7000 -0.0229 0.1279  -0.0269 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.4253 0.3264 0.7630 -0.0155 0.0834  -0.0106 51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.4295 0.3311 0.7925 -0.0153 0.0779  -0.0049 51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.4342 0.3431 0.7683 -0.0120 0.0530  -0.0033 51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.4266 0.2469 0.6386 -0.0506 0.2193  -0.0577 52  THR   A N   
356  C CA  . THR   A 46  ? 0.4642 0.2495 0.5926 -0.0700 0.2470  -0.0723 52  THR   A CA  
357  C C   . THR   A 46  ? 0.4436 0.2513 0.5068 -0.0733 0.2081  -0.0711 52  THR   A C   
358  O O   . THR   A 46  ? 0.4326 0.2714 0.4933 -0.0649 0.1730  -0.0646 52  THR   A O   
359  C CB  . THR   A 46  ? 0.5195 0.2804 0.6212 -0.0806 0.2688  -0.0796 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.5444 0.2776 0.7129 -0.0780 0.3150  -0.0804 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.5568 0.2789 0.5535 -0.1061 0.2825  -0.0914 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.4332 0.2240 0.4500 -0.0851 0.2153  -0.0754 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.4113 0.2215 0.3735 -0.0903 0.1809  -0.0710 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.4440 0.2239 0.3290 -0.1149 0.1875  -0.0756 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.4860 0.2136 0.3322 -0.1351 0.2247  -0.0856 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.4073 0.2164 0.3615 -0.0920 0.1788  -0.0698 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.3814 0.2100 0.4130 -0.0715 0.1772  -0.0651 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.4134 0.2471 0.3270 -0.0953 0.1419  -0.0613 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.3556 0.2264 0.4255 -0.0516 0.1360  -0.0544 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.4146 0.2205 0.2759 -0.1154 0.1537  -0.0672 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.4315 0.2139 0.2242 -0.1405 0.1481  -0.0654 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.4673 0.2247 0.2024 -0.1641 0.1423  -0.0615 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.4513 0.2335 0.2071 -0.1543 0.1267  -0.0551 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.3927 0.2162 0.1947 -0.1311 0.1119  -0.0529 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.5331 0.2346 0.1897 -0.1985 0.1544  -0.0646 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.5963 0.2631 0.1842 -0.2291 0.1433  -0.0578 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.6455 0.2992 0.1785 -0.2561 0.1130  -0.0440 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.7144 0.3096 0.1817 -0.2835 0.1314  -0.0516 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.6639 0.2579 0.2005 -0.2502 0.1909  -0.0747 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.6352 0.2438 0.2427 -0.2222 0.2230  -0.0854 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.6298 0.2908 0.2848 -0.2022 0.1941  -0.0752 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.5841 0.2531 0.3044 -0.1795 0.2225  -0.0832 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.5437 0.2599 0.3209 -0.1563 0.2018  -0.0763 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.4931 0.2490 0.2677 -0.1521 0.1593  -0.0632 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.4872 0.2072 0.3263 -0.1386 0.2251  -0.0809 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.6041 0.3121 0.1724 -0.2461 0.0694  -0.0229 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.6212 0.3302 0.1656 -0.2645 0.0387  -0.0056 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.5919 0.3542 0.1820 -0.2567 -0.0050 0.0222  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.5585 0.3553 0.1942 -0.2359 -0.0090 0.0255  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.6086 0.3344 0.1846 -0.2449 0.0532  -0.0157 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.4891 0.2926 0.1683 -0.1938 0.0477  -0.0151 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.5989 0.3670 0.1827 -0.2729 -0.0358 0.0436  57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.5756 0.3942 0.2188 -0.2636 -0.0713 0.0731  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.5324 0.3895 0.2268 -0.2408 -0.0739 0.0781  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.5257 0.4076 0.2552 -0.2449 -0.1025 0.1063  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.6434 0.4377 0.2507 -0.3057 -0.1127 0.1046  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.7658 0.5237 0.3220 -0.3416 -0.1347 0.1184  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.7997 0.5431 0.3352 -0.3362 -0.1118 0.0987  57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.8362 0.5791 0.3752 -0.3769 -0.1779 0.1513  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.5037 0.3640 0.2066 -0.2177 -0.0438 0.0529  58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.4334 0.3261 0.1798 -0.1950 -0.0428 0.0545  58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.3714 0.3126 0.1869 -0.1696 -0.0548 0.0725  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.3484 0.3034 0.1868 -0.1545 -0.0498 0.0702  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.4255 0.3155 0.1788 -0.1724 -0.0107 0.0263  58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.4888 0.3263 0.1818 -0.1956 0.0116  0.0078  58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.3309 0.2936 0.1792 -0.1644 -0.0663 0.0895  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.2993 0.2995 0.2132 -0.1385 -0.0665 0.1045  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.2515 0.2631 0.1841 -0.1148 -0.0493 0.0937  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.2341 0.2672 0.2138 -0.0986 -0.0470 0.1089  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.3217 0.3375 0.2750 -0.1540 -0.0947 0.1433  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.3564 0.3751 0.3224 -0.1637 -0.1090 0.1589  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.3701 0.4085 0.3949 -0.1770 -0.1382 0.2029  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.4120 0.4331 0.4150 -0.2133 -0.1723 0.2255  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.3310 0.4005 0.4320 -0.1500 -0.1247 0.2176  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.2581 0.2517 0.1555 -0.1144 -0.0358 0.0695  60  THR   A N   
416  C CA  . THR   A 54  ? 0.2374 0.2381 0.1481 -0.0937 -0.0217 0.0583  60  THR   A CA  
417  C C   . THR   A 54  ? 0.2303 0.2158 0.1222 -0.0847 -0.0044 0.0312  60  THR   A C   
418  O O   . THR   A 54  ? 0.2576 0.2219 0.1210 -0.0989 0.0011  0.0198  60  THR   A O   
419  C CB  . THR   A 54  ? 0.2956 0.2923 0.1964 -0.1052 -0.0277 0.0636  60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.3517 0.3187 0.2041 -0.1268 -0.0250 0.0496  60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.2924 0.3035 0.2205 -0.1173 -0.0486 0.0950  60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.2055 0.1973 0.1148 -0.0627 0.0046  0.0230  61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.2050 0.1851 0.1112 -0.0541 0.0148  0.0041  61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.1862 0.1675 0.1045 -0.0353 0.0166  0.0010  61  GLY   A C   
425  O O   . GLY   A 55  ? 0.2044 0.1915 0.1271 -0.0296 0.0159  0.0100  61  GLY   A O   
426  N N   . VAL   A 56  ? 0.1735 0.1445 0.0964 -0.0283 0.0183  -0.0099 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.1834 0.1443 0.1073 -0.0165 0.0144  -0.0120 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.1991 0.1494 0.1248 -0.0103 0.0093  -0.0144 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.1957 0.1463 0.1352 -0.0138 0.0096  -0.0192 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.2133 0.1677 0.1467 -0.0193 0.0138  -0.0187 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.2418 0.1795 0.1726 -0.0120 0.0026  -0.0180 62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.2305 0.1922 0.1572 -0.0258 0.0185  -0.0165 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.2171 0.1515 0.1259 -0.0024 0.0065  -0.0113 63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.2072 0.1237 0.1094 0.0004  -0.0012 -0.0131 63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.2537 0.1379 0.1346 -0.0002 -0.0145 -0.0133 63  TYR   A C   
436  O O   . TYR   A 57  ? 0.2583 0.1296 0.1196 -0.0002 -0.0127 -0.0119 63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.2126 0.1278 0.1048 0.0057  0.0078  -0.0086 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.2463 0.1370 0.1110 0.0118  0.0194  -0.0042 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.2543 0.1564 0.1270 0.0143  0.0329  0.0030  63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.2917 0.1426 0.1217 0.0135  0.0200  -0.0062 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.3005 0.1762 0.1541 0.0208  0.0520  0.0080  63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.3342 0.1496 0.1301 0.0172  0.0388  -0.0038 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.3337 0.1627 0.1452 0.0221  0.0577  0.0031  63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.3876 0.1789 0.1723 0.0268  0.0842  0.0064  63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.2592 0.1272 0.1433 -0.0032 -0.0303 -0.0131 64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.3037 0.1324 0.1612 -0.0096 -0.0510 -0.0094 64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.3371 0.1250 0.1383 -0.0098 -0.0473 -0.0094 64  TYR   A C   
448  O O   . TYR   A 58  ? 0.3340 0.1215 0.1341 -0.0070 -0.0434 -0.0103 64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.3039 0.1310 0.1992 -0.0161 -0.0747 -0.0042 64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.3606 0.1421 0.2264 -0.0281 -0.1048 0.0047  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.3897 0.1587 0.2470 -0.0340 -0.1145 0.0087  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.4079 0.1528 0.2451 -0.0363 -0.1251 0.0100  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.4594 0.1790 0.2808 -0.0498 -0.1468 0.0193  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.4750 0.1673 0.2729 -0.0534 -0.1583 0.0207  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.5123 0.1912 0.3015 -0.0610 -0.1699 0.0258  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.6142 0.2334 0.3546 -0.0824 -0.2062 0.0382  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.3792 0.1257 0.1293 -0.0145 -0.0464 -0.0085 65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.4509 0.1432 0.1360 -0.0171 -0.0349 -0.0098 65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.5284 0.1560 0.1565 -0.0360 -0.0654 -0.0056 65  CYS   A C   
460  O O   . CYS   A 59  ? 0.5577 0.1553 0.1531 -0.0450 -0.0734 -0.0033 65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.4866 0.1720 0.1516 -0.0091 -0.0008 -0.0113 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.5734 0.1719 0.1479 -0.0145 0.0250  -0.0138 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.5513 0.1562 0.1684 -0.0443 -0.0863 -0.0026 66  SER   A N   
464  C CA  . SER   A 60  ? 0.6236 0.1661 0.1909 -0.0670 -0.1246 0.0060  66  SER   A CA  
465  C C   . SER   A 60  ? 0.7031 0.1619 0.1660 -0.0809 -0.1144 0.0031  66  SER   A C   
466  O O   . SER   A 60  ? 0.7766 0.1869 0.1964 -0.1019 -0.1456 0.0114  66  SER   A O   
467  C CB  . SER   A 60  ? 0.6829 0.2152 0.2575 -0.0738 -0.1476 0.0111  66  SER   A CB  
468  O OG  . SER   A 60  ? 0.7971 0.3101 0.3335 -0.0668 -0.1183 0.0021  66  SER   A OG  
469  N N   . SER   A 61  ? 0.7175 0.1551 0.1409 -0.0708 -0.0694 -0.0069 67  SER   A N   
470  C CA  . SER   A 61  ? 0.8007 0.1461 0.1178 -0.0838 -0.0464 -0.0115 67  SER   A CA  
471  C C   . SER   A 61  ? 0.8147 0.1519 0.1162 -0.0854 -0.0376 -0.0114 67  SER   A C   
472  O O   . SER   A 61  ? 0.9061 0.1586 0.1132 -0.1000 -0.0211 -0.0145 67  SER   A O   
473  C CB  . SER   A 61  ? 0.8250 0.1545 0.1240 -0.0695 0.0073  -0.0201 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.7755 0.1749 0.1489 -0.0444 0.0432  -0.0213 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.7417 0.1588 0.1285 -0.0727 -0.0476 -0.0081 68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.7401 0.1542 0.1184 -0.0745 -0.0439 -0.0071 68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.7328 0.1813 0.1606 -0.0833 -0.0917 0.0027  68  ARG   A C   
478  O O   . ARG   A 62  ? 0.7411 0.1913 0.1686 -0.0858 -0.0945 0.0049  68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.7001 0.1765 0.1378 -0.0495 -0.0016 -0.0115 68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.7328 0.1731 0.1348 -0.0404 0.0507  -0.0164 68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.8345 0.1878 0.1449 -0.0532 0.0725  -0.0190 68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.8987 0.2166 0.1879 -0.0422 0.1323  -0.0223 68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.9669 0.2141 0.1917 -0.0490 0.1560  -0.0270 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 1.0062 0.2054 0.1701 -0.0697 0.1200  -0.0290 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.9992 0.2187 0.2217 -0.0365 0.2170  -0.0281 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.7079 0.1856 0.1875 -0.0868 -0.1262 0.0101  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.6901 0.2079 0.2419 -0.0916 -0.1643 0.0219  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.6309 0.2158 0.2478 -0.0735 -0.1416 0.0168  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.6308 0.2217 0.2683 -0.0797 -0.1592 0.0237  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.7772 0.2300 0.2801 -0.1207 -0.2111 0.0373  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.8873 0.2933 0.3639 -0.1418 -0.2511 0.0496  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 1.0069 0.3492 0.4419 -0.1750 -0.3058 0.0703  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 1.1605 0.4140 0.5016 -0.2037 -0.3349 0.0779  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 1.3082 0.4628 0.5381 -0.2378 -0.3631 0.0866  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 1.3406 0.4770 0.5443 -0.2458 -0.3657 0.0891  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 1.3963 0.4635 0.5324 -0.2663 -0.3881 0.0927  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.5657 0.1966 0.2108 -0.0531 -0.1030 0.0060  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.5127 0.1973 0.2061 -0.0400 -0.0828 0.0020  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.4386 0.1814 0.1879 -0.0251 -0.0623 -0.0032 70  LYS   A C   
500  O O   . LYS   A 64  ? 0.4339 0.1732 0.1738 -0.0211 -0.0529 -0.0056 70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.5663 0.2282 0.2114 -0.0353 -0.0525 -0.0025 70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.7052 0.3288 0.3092 -0.0464 -0.0624 0.0008  70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.8190 0.4169 0.3786 -0.0394 -0.0228 -0.0039 70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.9037 0.4885 0.4454 -0.0434 -0.0210 -0.0022 70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.9955 0.4952 0.4480 -0.0649 -0.0369 0.0003  70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.3745 0.1638 0.1740 -0.0193 -0.0549 -0.0047 71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.3288 0.1632 0.1666 -0.0105 -0.0358 -0.0089 71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.3405 0.1853 0.1654 -0.0039 -0.0121 -0.0090 71  HIS   A C   
509  O O   . HIS   A 65  ? 0.3693 0.2035 0.1786 -0.0048 -0.0095 -0.0077 71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.2931 0.1599 0.1849 -0.0124 -0.0394 -0.0100 71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.2869 0.1481 0.2118 -0.0175 -0.0586 -0.0060 71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.3106 0.1877 0.2649 -0.0154 -0.0530 -0.0081 71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.3002 0.1415 0.2394 -0.0254 -0.0838 0.0029  71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.2987 0.1669 0.2900 -0.0206 -0.0724 -0.0004 71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.3203 0.1670 0.3054 -0.0274 -0.0940 0.0080  71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.3009 0.1666 0.1377 0.0019  0.0039  -0.0079 72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.2840 0.1636 0.1255 0.0071  0.0235  -0.0021 72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.2478 0.1682 0.1258 0.0048  0.0250  0.0013  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.2203 0.1512 0.1096 0.0033  0.0221  0.0003  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.3124 0.1677 0.1337 0.0139  0.0432  0.0027  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.3789 0.1780 0.1456 0.0124  0.0489  -0.0004 72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.4159 0.1973 0.1650 0.0131  0.0616  0.0019  72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.4407 0.1977 0.1667 0.0076  0.0415  -0.0049 72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.4904 0.2077 0.1755 0.0080  0.0696  -0.0013 72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.5030 0.1942 0.1622 0.0002  0.0450  -0.0073 72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.5340 0.2033 0.1698 -0.0002 0.0598  -0.0060 72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.6345 0.2260 0.1901 -0.0109 0.0665  -0.0089 72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.2377 0.1766 0.1295 0.0025  0.0291  0.0070  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.2220 0.1895 0.1368 -0.0054 0.0272  0.0138  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.2391 0.2151 0.1718 -0.0013 0.0355  0.0291  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.2715 0.2354 0.2060 0.0083  0.0502  0.0361  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.2295 0.2063 0.1488 -0.0111 0.0260  0.0172  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.2453 0.2039 0.1523 -0.0013 0.0340  0.0175  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.2535 0.1828 0.1356 0.0047  0.0344  0.0094  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.2181 0.2102 0.1652 -0.0091 0.0287  0.0354  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.2197 0.2223 0.1949 -0.0064 0.0335  0.0533  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.2045 0.2274 0.1972 -0.0236 0.0173  0.0680  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.2175 0.2382 0.1874 -0.0379 0.0061  0.0586  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.2532 0.2441 0.2226 0.0020  0.0400  0.0477  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.2948 0.2555 0.2465 0.0162  0.0590  0.0426  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.2703 0.2581 0.2192 -0.0044 0.0284  0.0316  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.1806 0.2180 0.2148 -0.0241 0.0170  0.0932  75  SER   A N   
543  C CA  . SER   A 69  ? 0.1798 0.2322 0.2341 -0.0430 -0.0039 0.1136  75  SER   A CA  
544  C C   . SER   A 69  ? 0.1925 0.2466 0.2645 -0.0345 0.0028  0.1171  75  SER   A C   
545  O O   . SER   A 69  ? 0.2193 0.2659 0.3063 -0.0145 0.0259  0.1153  75  SER   A O   
546  C CB  . SER   A 69  ? 0.1911 0.2607 0.2971 -0.0500 -0.0130 0.1466  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.2996 0.3671 0.3885 -0.0594 -0.0210 0.1446  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.1649 0.2206 0.2238 -0.0499 -0.0140 0.1179  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.1671 0.2246 0.2402 -0.0423 -0.0087 0.1196  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.1887 0.2575 0.2823 -0.0624 -0.0319 0.1431  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.2297 0.2944 0.3009 -0.0882 -0.0554 0.1505  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.1759 0.2167 0.2057 -0.0347 -0.0002 0.0895  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.1798 0.2094 0.1658 -0.0508 -0.0099 0.0718  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.1778 0.1972 0.1403 -0.0502 -0.0049 0.0560  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.1980 0.2231 0.1678 -0.0676 -0.0208 0.0724  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.2036 0.2079 0.1332 -0.0637 -0.0057 0.0404  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.2219 0.2272 0.1500 -0.0823 -0.0202 0.0553  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.2239 0.2187 0.1349 -0.0806 -0.0112 0.0403  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.1603 0.2384 0.2943 -0.0536 -0.0265 0.1571  77  SER   A N   
560  C CA  . SER   A 71  ? 0.1766 0.2667 0.3399 -0.0737 -0.0520 0.1853  77  SER   A CA  
561  C C   . SER   A 71  ? 0.2061 0.2821 0.3148 -0.0922 -0.0675 0.1707  77  SER   A C   
562  O O   . SER   A 71  ? 0.2028 0.2639 0.2658 -0.0835 -0.0529 0.1392  77  SER   A O   
563  C CB  . SER   A 71  ? 0.1888 0.2937 0.4241 -0.0570 -0.0375 0.2077  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.2025 0.2963 0.4152 -0.0397 -0.0167 0.1842  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.2320 0.3087 0.3460 -0.1198 -0.0978 0.1954  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.2782 0.3337 0.3348 -0.1390 -0.1083 0.1817  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.2702 0.3338 0.3446 -0.1185 -0.0918 0.1719  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.2600 0.3441 0.3965 -0.1004 -0.0831 0.1883  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.3424 0.3874 0.3903 -0.1792 -0.1487 0.2136  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.4380 0.4648 0.4514 -0.2035 -0.1659 0.2198  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.5745 0.5670 0.5361 -0.2530 -0.2067 0.2414  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.6879 0.6437 0.5780 -0.2768 -0.2112 0.2296  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.7857 0.6862 0.5906 -0.3282 -0.2417 0.2391  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.2778 0.3228 0.3014 -0.1209 -0.0843 0.1459  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.2828 0.3350 0.3238 -0.1015 -0.0704 0.1372  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.2735 0.3426 0.3641 -0.1076 -0.0863 0.1681  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.2956 0.3587 0.3769 -0.1380 -0.1156 0.1896  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.3271 0.3548 0.3095 -0.1109 -0.0652 0.1110  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.3637 0.3664 0.2951 -0.1347 -0.0709 0.1043  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.3150 0.3284 0.2675 -0.1395 -0.0829 0.1232  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.2458 0.3310 0.3885 -0.0814 -0.0675 0.1729  80  SER   A N   
582  C CA  . SER   A 74  ? 0.2477 0.3510 0.4534 -0.0842 -0.0781 0.2054  80  SER   A CA  
583  C C   . SER   A 74  ? 0.2379 0.3443 0.4724 -0.0558 -0.0493 0.1967  80  SER   A C   
584  O O   . SER   A 74  ? 0.2314 0.3226 0.4300 -0.0368 -0.0256 0.1662  80  SER   A O   
585  C CB  . SER   A 74  ? 0.2683 0.3891 0.5399 -0.0907 -0.0901 0.2428  80  SER   A CB  
586  O OG  . SER   A 74  ? 0.3266 0.4507 0.6316 -0.0622 -0.0561 0.2374  80  SER   A OG  
587  N N   . LEU   A 75  ? 0.2222 0.3442 0.5193 -0.0558 -0.0538 0.2250  81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.2330 0.3530 0.5591 -0.0312 -0.0245 0.2199  81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.2398 0.3578 0.6168 -0.0099 0.0085  0.2297  81  LEU   A C   
590  O O   . LEU   A 75  ? 0.2399 0.3762 0.6912 -0.0151 0.0027  0.2658  81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.2157 0.3532 0.5992 -0.0412 -0.0412 0.2510  81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.2606 0.3929 0.5993 -0.0528 -0.0577 0.2376  81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.2614 0.4121 0.6617 -0.0682 -0.0818 0.2756  81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.2858 0.4021 0.5932 -0.0286 -0.0277 0.2054  81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.2524 0.3440 0.5934 0.0121  0.0430  0.2014  82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.2716 0.3470 0.6431 0.0310  0.0814  0.2062  82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.3088 0.3519 0.6700 0.0507  0.1201  0.1922  82  ILE   A C   
598  O O   . ILE   A 76  ? 0.3235 0.3470 0.6192 0.0524  0.1173  0.1638  82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.3093 0.3697 0.6252 0.0318  0.0837  0.1845  82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.3131 0.4015 0.6476 0.0114  0.0496  0.2034  82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.3283 0.3576 0.6513 0.0512  0.1286  0.1813  82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.3561 0.4351 0.6356 0.0080  0.0443  0.1826  82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.3050 0.3399 0.7353 0.0640  0.1566  0.2145  83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.3573 0.3506 0.7721 0.0806  0.1993  0.2015  83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.3998 0.3384 0.7209 0.0881  0.2238  0.1665  83  PHE   A C   
606  O O   . PHE   A 77  ? 0.4106 0.3401 0.7172 0.0887  0.2308  0.1634  83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.3614 0.3505 0.8754 0.0932  0.2420  0.2342  83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.4176 0.3618 0.9200 0.1073  0.2867  0.2239  83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.4344 0.3940 0.9494 0.1045  0.2706  0.2267  83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.4745 0.3541 0.9448 0.1213  0.3461  0.2104  83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.4765 0.3913 0.9767 0.1164  0.3120  0.2166  83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.5098 0.3374 0.9602 0.1312  0.3902  0.2007  83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.5075 0.3546 0.9738 0.1291  0.3720  0.2036  83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.4219 0.3248 0.6747 0.0904  0.2288  0.1408  84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.4723 0.3171 0.6278 0.0917  0.2419  0.1097  84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.5221 0.3051 0.6481 0.1001  0.2848  0.1017  84  VAL   A C   
617  O O   . VAL   A 78  ? 0.5042 0.2919 0.6401 0.1008  0.2804  0.1024  84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.4842 0.3397 0.5749 0.0802  0.1960  0.0865  84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.5384 0.3304 0.5350 0.0784  0.2034  0.0603  84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.4594 0.3642 0.5711 0.0708  0.1617  0.0925  84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.5755 0.2945 0.6607 0.1050  0.3289  0.0940  85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.6369 0.2771 0.6774 0.1100  0.3794  0.0848  85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.6845 0.2864 0.6338 0.1004  0.3568  0.0601  85  GLU   A C   
624  O O   . GLU   A 79  ? 0.6993 0.3132 0.5972 0.0895  0.3102  0.0451  85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.7331 0.3008 0.7184 0.1109  0.4246  0.0760  85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.8056 0.3927 0.8872 0.1232  0.4651  0.1027  85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.9667 0.4579 1.0140 0.1296  0.5431  0.0985  85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 1.0338 0.4918 1.0713 0.1318  0.5762  0.0997  85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 1.0408 0.4828 1.0622 0.1310  0.5731  0.0922  85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.7055 0.2556 0.6354 0.1035  0.3919  0.0570  86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.7562 0.2625 0.5991 0.0928  0.3713  0.0361  86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.8237 0.2619 0.5474 0.0767  0.3560  0.0135  86  ALA   A C   
633  O O   . ALA   A 80  ? 0.8730 0.2588 0.5561 0.0747  0.3876  0.0099  86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.7836 0.2290 0.6159 0.0977  0.4216  0.0362  86  ALA   A CB  
635  N N   . SER   A 81  ? 0.8224 0.2610 0.4954 0.0641  0.3068  0.0011  87  SER   A N   
636  C CA  . SER   A 81  ? 0.8707 0.2471 0.4385 0.0452  0.2810  -0.0151 87  SER   A CA  
637  C C   . SER   A 81  ? 0.9206 0.2549 0.4256 0.0315  0.2544  -0.0249 87  SER   A C   
638  O O   . SER   A 81  ? 0.8978 0.2556 0.4422 0.0388  0.2584  -0.0209 87  SER   A O   
639  C CB  . SER   A 81  ? 0.8415 0.2840 0.4383 0.0425  0.2322  -0.0137 87  SER   A CB  
640  O OG  . SER   A 81  ? 0.8140 0.3271 0.4616 0.0435  0.1879  -0.0108 87  SER   A OG  
641  N N   . GLU   A 82  ? 0.9806 0.2499 0.3887 0.0098  0.2250  -0.0354 88  GLU   A N   
642  C CA  . GLU   A 82  ? 1.0189 0.2468 0.3665 -0.0078 0.1880  -0.0411 88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.9365 0.2587 0.3658 -0.0014 0.1389  -0.0347 88  GLU   A C   
644  O O   . GLU   A 82  ? 0.9542 0.2629 0.3682 -0.0083 0.1181  -0.0357 88  GLU   A O   
645  C CB  . GLU   A 82  ? 1.1590 0.2994 0.3930 -0.0366 0.1579  -0.0477 88  GLU   A CB  
646  C CG  . GLU   A 82  ? 1.2577 0.4072 0.4884 -0.0386 0.1523  -0.0468 88  GLU   A CG  
647  C CD  . GLU   A 82  ? 1.5031 0.5302 0.6055 -0.0617 0.1724  -0.0547 88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 1.6063 0.5335 0.6190 -0.0745 0.2048  -0.0621 88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 1.5698 0.5952 0.6562 -0.0686 0.1574  -0.0536 88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.8402 0.2538 0.3546 0.0110  0.1233  -0.0279 89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.7616 0.2557 0.3471 0.0155  0.0840  -0.0229 89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.6749 0.2397 0.3474 0.0337  0.1033  -0.0148 89  TYR   A C   
653  O O   . TYR   A 83  ? 0.6460 0.2556 0.3590 0.0352  0.0791  -0.0123 89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.7282 0.2677 0.3424 0.0128  0.0522  -0.0209 89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.7760 0.2512 0.3150 -0.0050 0.0340  -0.0248 89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.8077 0.2537 0.3144 -0.0232 -0.0119 -0.0231 89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.8063 0.2516 0.3129 -0.0051 0.0596  -0.0271 89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.8612 0.2471 0.3014 -0.0433 -0.0354 -0.0223 89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.8741 0.2558 0.3060 -0.0240 0.0413  -0.0296 89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.9130 0.2645 0.3104 -0.0442 -0.0084 -0.0266 89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 1.0002 0.2896 0.3278 -0.0661 -0.0328 -0.0251 89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.6402 0.2140 0.3454 0.0458  0.1451  -0.0082 90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.5599 0.1995 0.3530 0.0593  0.1573  0.0051  90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.5921 0.2045 0.4052 0.0699  0.2107  0.0139  90  TYR   A C   
665  O O   . TYR   A 84  ? 0.6273 0.1868 0.4032 0.0699  0.2437  0.0111  90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.4715 0.1862 0.3306 0.0630  0.1415  0.0151  90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.4146 0.1618 0.2706 0.0546  0.0987  0.0086  90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.3768 0.1655 0.2638 0.0524  0.0724  0.0094  90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.4214 0.1620 0.2545 0.0496  0.0890  0.0039  90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.3552 0.1711 0.2489 0.0457  0.0422  0.0048  90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.3890 0.1583 0.2295 0.0428  0.0552  -0.0003 90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.3592 0.1672 0.2340 0.0414  0.0347  0.0006  90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.3165 0.1462 0.2032 0.0352  0.0093  -0.0031 90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.5625 0.2110 0.4423 0.0790  0.2225  0.0269  91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.5729 0.2056 0.4989 0.0908  0.2759  0.0415  91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.5460 0.2355 0.5502 0.0968  0.2786  0.0609  91  PRO   A C   
677  O O   . PRO   A 85  ? 0.5210 0.2618 0.5375 0.0909  0.2381  0.0612  91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.5542 0.2134 0.5327 0.0963  0.2776  0.0518  91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.5221 0.2416 0.5124 0.0892  0.2215  0.0492  91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.5230 0.2309 0.4487 0.0787  0.1891  0.0321  91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.5440 0.2235 0.6053 0.1076  0.3262  0.0788  92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.5084 0.2414 0.6536 0.1118  0.3262  0.1023  92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.4408 0.2596 0.6610 0.1068  0.2785  0.1214  92  ALA   A C   
684  O O   . ALA   A 86  ? 0.4393 0.2735 0.6867 0.1075  0.2720  0.1276  92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.5080 0.2134 0.7174 0.1248  0.3888  0.1228  92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.3874 0.2527 0.6189 0.0983  0.2412  0.1256  93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.3225 0.2526 0.5978 0.0875  0.1948  0.1396  93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.2830 0.2514 0.5835 0.0781  0.1697  0.1521  93  ARG   A C   
689  O O   . ARG   A 87  ? 0.2926 0.2405 0.5719 0.0817  0.1856  0.1458  93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.3360 0.2632 0.5417 0.0797  0.1625  0.1137  93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.3575 0.2754 0.4978 0.0730  0.1424  0.0918  93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.3767 0.2627 0.4457 0.0705  0.1301  0.0660  93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.3598 0.2623 0.3995 0.0609  0.0978  0.0533  93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.3495 0.2389 0.3598 0.0588  0.0961  0.0452  93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.2865 0.1903 0.2787 0.0507  0.0695  0.0350  93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.3533 0.2119 0.3541 0.0649  0.1241  0.0477  93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.2471 0.2641 0.5821 0.0635  0.1297  0.1684  94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.2457 0.2892 0.5824 0.0498  0.1015  0.1756  94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.2269 0.2640 0.4835 0.0413  0.0776  0.1451  94  TYR   A C   
700  O O   . TYR   A 88  ? 0.2302 0.2716 0.4650 0.0358  0.0613  0.1356  94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.2502 0.3360 0.6507 0.0322  0.0688  0.2095  94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.2763 0.3754 0.7781 0.0382  0.0871  0.2482  94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.2971 0.4046 0.8435 0.0377  0.0924  0.2684  94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.2923 0.3945 0.8527 0.0457  0.1023  0.2659  94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.2929 0.4140 0.9485 0.0435  0.1106  0.3087  94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.2876 0.4016 0.9560 0.0524  0.1232  0.3049  94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.2993 0.4232 1.0188 0.0514  0.1276  0.3273  94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.3186 0.4559 1.1609 0.0580  0.1492  0.3706  94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.2064 0.2328 0.4251 0.0407  0.0774  0.1311  95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.2031 0.2255 0.3607 0.0323  0.0563  0.1064  95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.1868 0.2377 0.3548 0.0129  0.0285  0.1186  95  GLN   A C   
712  O O   . GLN   A 89  ? 0.1802 0.2430 0.3803 0.0090  0.0276  0.1373  95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.2058 0.1955 0.3145 0.0408  0.0702  0.0849  95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.2171 0.2063 0.2799 0.0319  0.0483  0.0641  95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.2503 0.2035 0.2668 0.0385  0.0562  0.0453  95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.2611 0.1788 0.2540 0.0465  0.0715  0.0390  95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.2173 0.1731 0.2143 0.0325  0.0440  0.0360  95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.1605 0.2176 0.3027 -0.0012 0.0074  0.1110  96  SER   A N   
719  C CA  . SER   A 90  ? 0.1632 0.2325 0.2975 -0.0249 -0.0172 0.1209  96  SER   A CA  
720  C C   . SER   A 90  ? 0.1952 0.2513 0.2814 -0.0293 -0.0177 0.0989  96  SER   A C   
721  O O   . SER   A 90  ? 0.1937 0.2345 0.2561 -0.0150 -0.0043 0.0765  96  SER   A O   
722  C CB  . SER   A 90  ? 0.1791 0.2519 0.3049 -0.0407 -0.0344 0.1248  96  SER   A CB  
723  O OG  . SER   A 90  ? 0.2072 0.2649 0.2933 -0.0352 -0.0273 0.0975  96  SER   A OG  
724  N N   . HIS   A 91  ? 0.1977 0.2564 0.2722 -0.0506 -0.0343 0.1083  97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.1987 0.2431 0.2308 -0.0582 -0.0334 0.0904  97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.1808 0.2233 0.2182 -0.0391 -0.0179 0.0811  97  HIS   A C   
727  O O   . HIS   A 91  ? 0.1871 0.2164 0.1955 -0.0356 -0.0113 0.0602  97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.2270 0.2544 0.2226 -0.0607 -0.0277 0.0669  97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.2694 0.2901 0.2481 -0.0832 -0.0404 0.0749  97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.3277 0.3270 0.2638 -0.1118 -0.0492 0.0763  97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.2892 0.3175 0.2849 -0.0836 -0.0466 0.0846  97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.3460 0.3364 0.2681 -0.1301 -0.0607 0.0857  97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.3331 0.3444 0.2948 -0.1132 -0.0608 0.0918  97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.1669 0.2196 0.2441 -0.0280 -0.0108 0.0984  98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.1696 0.2124 0.2453 -0.0110 0.0075  0.0900  98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.1556 0.2085 0.2474 -0.0194 0.0015  0.1054  98  LEU   A C   
737  O O   . LEU   A 92  ? 0.1505 0.2205 0.2819 -0.0305 -0.0110 0.1328  98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.1803 0.2161 0.2850 0.0077  0.0294  0.0972  98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.2120 0.2210 0.2995 0.0239  0.0539  0.0861  98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.2263 0.2116 0.2589 0.0259  0.0504  0.0591  98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.2535 0.2440 0.3626 0.0387  0.0818  0.0934  98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.1563 0.1980 0.2224 -0.0144 0.0087  0.0905  99  MET   A N   
743  C CA  . MET   A 93  ? 0.1531 0.2030 0.2320 -0.0214 0.0039  0.1031  99  MET   A CA  
744  C C   . MET   A 93  ? 0.1740 0.2123 0.2616 -0.0020 0.0279  0.1004  99  MET   A C   
745  O O   . MET   A 93  ? 0.2137 0.2298 0.2646 0.0082  0.0387  0.0782  99  MET   A O   
746  C CB  . MET   A 93  ? 0.1694 0.2108 0.2033 -0.0345 -0.0062 0.0855  99  MET   A CB  
747  C CG  . MET   A 93  ? 0.2236 0.2624 0.2348 -0.0570 -0.0234 0.0858  99  MET   A CG  
748  S SD  . MET   A 93  ? 0.2836 0.3008 0.2421 -0.0705 -0.0219 0.0620  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.2497 0.2584 0.2045 -0.0471 -0.0044 0.0369  99  MET   A CE  
750  N N   . LEU   A 94  ? 0.1435 0.1916 0.2781 0.0012  0.0363  0.1239  100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.1637 0.1917 0.2999 0.0186  0.0656  0.1202  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.1731 0.2042 0.3026 0.0141  0.0613  0.1206  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.1742 0.2272 0.3213 -0.0018 0.0385  0.1352  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.1716 0.2009 0.3738 0.0299  0.0913  0.1464  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.2203 0.2411 0.4335 0.0375  0.1039  0.1469  100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.2399 0.2552 0.5227 0.0505  0.1385  0.1722  100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2593 0.2438 0.4018 0.0451  0.1143  0.1150  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.1959 0.2004 0.2985 0.0264  0.0832  0.1068  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.2020 0.2055 0.2980 0.0252  0.0842  0.1063  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.2352 0.2046 0.3262 0.0410  0.1209  0.1048  101 ALA   A C   
761  O O   . ALA   A 95  ? 0.2595 0.1967 0.3287 0.0502  0.1427  0.0961  101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.2366 0.2326 0.2770 0.0183  0.0670  0.0814  101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.2355 0.2073 0.3451 0.0424  0.1295  0.1145  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.2833 0.2148 0.3795 0.0552  0.1681  0.1119  102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.3446 0.2459 0.3618 0.0522  0.1596  0.0840  102 VAL   A C   
766  O O   . VAL   A 96  ? 0.3394 0.2603 0.3469 0.0441  0.1356  0.0788  102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.2839 0.2322 0.4433 0.0580  0.1818  0.1375  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.3100 0.2082 0.4466 0.0703  0.2272  0.1321  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.2606 0.2415 0.5123 0.0582  0.1833  0.1717  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.3917 0.2428 0.3533 0.0563  0.1770  0.0680  103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.4425 0.2601 0.3313 0.0500  0.1627  0.0459  103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.4925 0.2463 0.3186 0.0504  0.1802  0.0336  103 GLY   A C   
773  O O   . GLY   A 97  ? 0.5032 0.2455 0.3414 0.0558  0.1998  0.0383  103 GLY   A O   
774  N N   . HIS   A 98  ? 0.5126 0.2198 0.2693 0.0425  0.1727  0.0196  104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.5614 0.1953 0.2411 0.0361  0.1824  0.0084  104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.5493 0.1904 0.2170 0.0295  0.1497  0.0012  104 HIS   A C   
777  O O   . HIS   A 98  ? 0.5142 0.1954 0.2023 0.0246  0.1128  -0.0014 104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.6166 0.1933 0.2217 0.0244  0.1772  -0.0005 104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.7125 0.1993 0.2230 0.0116  0.1844  -0.0102 104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.7888 0.2129 0.2636 0.0148  0.2349  -0.0104 104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.7534 0.2052 0.2061 -0.0055 0.1464  -0.0174 104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.8490 0.1950 0.2309 -0.0025 0.2260  -0.0203 104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.8406 0.2014 0.2073 -0.0161 0.1694  -0.0231 104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.5806 0.1753 0.2123 0.0286  0.1666  -0.0021 105 SER   A N   
785  C CA  . SER   A 99  ? 0.6054 0.1924 0.2151 0.0208  0.1379  -0.0086 105 SER   A CA  
786  C C   . SER   A 99  ? 0.6924 0.1940 0.2261 0.0142  0.1620  -0.0145 105 SER   A C   
787  O O   . SER   A 99  ? 0.7221 0.1898 0.2489 0.0217  0.2099  -0.0117 105 SER   A O   
788  C CB  . SER   A 99  ? 0.5694 0.2289 0.2551 0.0295  0.1259  -0.0026 105 SER   A CB  
789  O OG  . SER   A 99  ? 0.5944 0.2573 0.3130 0.0407  0.1619  0.0062  105 SER   A OG  
790  N N   . GLU   A 100 ? 0.7297 0.1918 0.2068 -0.0015 0.1293  -0.0211 106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.8059 0.1807 0.1969 -0.0150 0.1375  -0.0273 106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.8032 0.2047 0.2152 -0.0184 0.1012  -0.0270 106 GLU   A C   
793  O O   . GLU   A 100 ? 0.7584 0.2328 0.2377 -0.0140 0.0679  -0.0232 106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.9196 0.2045 0.2054 -0.0391 0.1233  -0.0320 106 GLU   A CB  
795  C CG  . GLU   A 100 ? 1.0204 0.2687 0.2785 -0.0355 0.1679  -0.0334 106 GLU   A CG  
796  C CD  . GLU   A 100 ? 1.1164 0.2727 0.2657 -0.0611 0.1560  -0.0374 106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 1.2041 0.2747 0.2571 -0.0858 0.1375  -0.0409 106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 1.0907 0.2572 0.2480 -0.0586 0.1629  -0.0358 106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.8574 0.2012 0.2174 -0.0253 0.1115  -0.0308 107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.8378 0.2172 0.2328 -0.0250 0.0811  -0.0292 107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.8009 0.2109 0.2173 -0.0365 0.0217  -0.0249 107 PRO   A C   
802  O O   . PRO   A 101 ? 0.7563 0.2406 0.2516 -0.0264 0.0043  -0.0215 107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.9097 0.2006 0.2217 -0.0365 0.0995  -0.0345 107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.9616 0.1939 0.2304 -0.0318 0.1607  -0.0385 107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.9336 0.1814 0.2104 -0.0311 0.1597  -0.0367 107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.8138 0.1670 0.1667 -0.0578 -0.0067 -0.0233 108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.7901 0.1663 0.1719 -0.0703 -0.0625 -0.0144 108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.7106 0.1766 0.1872 -0.0554 -0.0693 -0.0113 108 GLY   A C   
809  O O   . GLY   A 102 ? 0.6963 0.1900 0.2171 -0.0620 -0.1079 -0.0029 108 GLY   A O   
810  N N   . ASP   A 103 ? 0.6635 0.1707 0.1732 -0.0369 -0.0309 -0.0161 109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.5749 0.1597 0.1636 -0.0247 -0.0327 -0.0142 109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.4930 0.1464 0.1578 -0.0132 -0.0353 -0.0133 109 ASP   A C   
813  O O   . ASP   A 103 ? 0.4254 0.1333 0.1489 -0.0084 -0.0419 -0.0120 109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.5838 0.1832 0.1785 -0.0127 0.0047  -0.0164 109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.6289 0.1749 0.1638 -0.0236 0.0051  -0.0170 109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.6364 0.1656 0.1564 -0.0380 -0.0310 -0.0136 109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.6517 0.1707 0.1583 -0.0182 0.0424  -0.0191 109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.5035 0.1495 0.1635 -0.0106 -0.0290 -0.0144 110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.4543 0.1583 0.1789 -0.0019 -0.0314 -0.0135 110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.4109 0.1388 0.1781 -0.0083 -0.0635 -0.0098 110 CYS   A C   
821  O O   . CYS   A 104 ? 0.4422 0.1315 0.1859 -0.0216 -0.0924 -0.0047 110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.4703 0.1534 0.1767 -0.0004 -0.0240 -0.0145 110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.5109 0.1884 0.2085 0.0125  0.0235  -0.0150 110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.3524 0.1359 0.1795 -0.0012 -0.0576 -0.0104 111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.3411 0.1445 0.2174 -0.0058 -0.0777 -0.0066 111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.3325 0.1527 0.2297 -0.0066 -0.0760 -0.0065 111 GLY   A C   
827  O O   . GLY   A 105 ? 0.3106 0.1539 0.2598 -0.0077 -0.0802 -0.0042 111 GLY   A O   
828  N N   . GLY   A 106 ? 0.3311 0.1375 0.1909 -0.0059 -0.0664 -0.0086 112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.2968 0.1219 0.1761 -0.0060 -0.0628 -0.0090 112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.2527 0.1236 0.1730 -0.0009 -0.0434 -0.0132 112 GLY   A C   
831  O O   . GLY   A 106 ? 0.2449 0.1310 0.1603 0.0035  -0.0278 -0.0149 112 GLY   A O   
832  N N   . ILE   A 107 ? 0.2229 0.1097 0.1798 -0.0038 -0.0438 -0.0134 113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.2069 0.1222 0.1882 -0.0041 -0.0238 -0.0183 113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.2045 0.1309 0.1656 -0.0043 -0.0115 -0.0199 113 ILE   A C   
835  O O   . ILE   A 107 ? 0.2363 0.1545 0.1865 -0.0041 -0.0158 -0.0186 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.2393 0.1580 0.2703 -0.0079 -0.0224 -0.0180 113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.2576 0.1736 0.3202 -0.0076 -0.0273 -0.0149 113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.2506 0.1822 0.2896 -0.0124 0.0024  -0.0248 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.2754 0.1904 0.4059 -0.0101 -0.0252 -0.0092 113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.1861 0.1295 0.1450 -0.0075 0.0017  -0.0208 114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.1817 0.1367 0.1287 -0.0123 0.0098  -0.0186 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.1973 0.1530 0.1533 -0.0236 0.0205  -0.0246 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.2010 0.1535 0.1635 -0.0284 0.0273  -0.0280 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.1845 0.1508 0.1229 -0.0129 0.0119  -0.0104 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.1953 0.1740 0.1287 -0.0230 0.0140  -0.0023 114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.2080 0.1867 0.1390 -0.0181 0.0147  0.0013  114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.1990 0.1898 0.1388 -0.0251 0.0113  0.0118  114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.1955 0.1495 0.1490 -0.0284 0.0253  -0.0266 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.2174 0.1609 0.1721 -0.0407 0.0418  -0.0337 115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.2468 0.1898 0.1734 -0.0525 0.0439  -0.0313 115 ARG   A C   
851  O O   . ARG   A 109 ? 0.2413 0.1941 0.1661 -0.0472 0.0350  -0.0259 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.2395 0.1754 0.2269 -0.0360 0.0464  -0.0376 115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.3215 0.2539 0.3492 -0.0283 0.0421  -0.0362 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.3791 0.3054 0.4489 -0.0267 0.0445  -0.0347 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.4473 0.3596 0.5352 -0.0348 0.0763  -0.0417 115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.4582 0.3607 0.5898 -0.0344 0.0927  -0.0416 115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.4530 0.3627 0.6231 -0.0263 0.0733  -0.0323 115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.4819 0.3619 0.6183 -0.0434 0.1300  -0.0497 115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.2640 0.1891 0.1664 -0.0705 0.0570  -0.0354 116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.3092 0.2235 0.1781 -0.0879 0.0577  -0.0329 116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.3451 0.2292 0.2091 -0.0972 0.0843  -0.0462 116 CYS   A C   
862  O O   . CYS   A 110 ? 0.3259 0.2048 0.2252 -0.0874 0.1000  -0.0536 116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.3425 0.2479 0.1741 -0.1081 0.0486  -0.0239 116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.3664 0.2341 0.1690 -0.1255 0.0702  -0.0349 116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.3989 0.2605 0.2236 -0.1167 0.0903  -0.0473 117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.4596 0.2838 0.2750 -0.1271 0.1227  -0.0608 117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.4911 0.2776 0.2970 -0.1367 0.1547  -0.0717 117 GLN   A C   
868  O O   . GLN   A 111 ? 0.5194 0.2781 0.3437 -0.1372 0.1897  -0.0823 117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.5352 0.3312 0.2930 -0.1522 0.1226  -0.0598 117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.6285 0.3930 0.3181 -0.1824 0.1135  -0.0540 117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.7644 0.4982 0.3950 -0.2108 0.1048  -0.0488 117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.8043 0.5565 0.4235 -0.2201 0.0693  -0.0298 117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.7859 0.4701 0.3823 -0.2256 0.1378  -0.0637 117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.4916 0.2767 0.2756 -0.1434 0.1454  -0.0678 118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.5064 0.2529 0.2732 -0.1546 0.1750  -0.0771 118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.4636 0.2344 0.3011 -0.1298 0.1816  -0.0781 118 HIS   A C   
877  O O   . HIS   A 112 ? 0.4956 0.2363 0.3356 -0.1350 0.2117  -0.0856 118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.5546 0.2815 0.2550 -0.1793 0.1587  -0.0705 118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.6249 0.3234 0.2545 -0.2093 0.1438  -0.0640 118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.6365 0.3701 0.2656 -0.2110 0.1009  -0.0447 118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.7015 0.3337 0.2577 -0.2413 0.1668  -0.0724 118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.6967 0.3919 0.2617 -0.2423 0.0935  -0.0399 118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.7329 0.3632 0.2447 -0.2629 0.1316  -0.0572 118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.3853 0.2048 0.2750 -0.1055 0.1531  -0.0695 119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.3300 0.1687 0.2803 -0.0861 0.1511  -0.0672 119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.2868 0.1621 0.2433 -0.0729 0.1149  -0.0573 119 GLY   A C   
887  O O   . GLY   A 113 ? 0.2802 0.1729 0.2131 -0.0725 0.0929  -0.0509 119 GLY   A O   
888  N N   . VAL   A 114 ? 0.2657 0.1485 0.2556 -0.0628 0.1124  -0.0555 120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.2576 0.1662 0.2522 -0.0507 0.0836  -0.0475 120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.2607 0.1728 0.2110 -0.0602 0.0753  -0.0441 120 VAL   A C   
891  O O   . VAL   A 114 ? 0.2902 0.1831 0.2186 -0.0738 0.0898  -0.0479 120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.2502 0.1621 0.2945 -0.0391 0.0808  -0.0451 120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.2436 0.1723 0.2792 -0.0300 0.0546  -0.0385 120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.2466 0.1588 0.3446 -0.0308 0.0773  -0.0408 120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.2338 0.1663 0.1726 -0.0546 0.0535  -0.0353 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.2377 0.1776 0.1508 -0.0629 0.0426  -0.0262 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.2166 0.1707 0.1469 -0.0501 0.0322  -0.0214 121 VAL   A C   
898  O O   . VAL   A 115 ? 0.2258 0.1804 0.1456 -0.0577 0.0295  -0.0166 121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.2553 0.2081 0.1578 -0.0647 0.0297  -0.0155 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.2813 0.2465 0.1779 -0.0712 0.0153  0.0005  121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.2753 0.2118 0.1542 -0.0805 0.0372  -0.0190 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.1826 0.1433 0.1337 -0.0330 0.0250  -0.0216 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.1919 0.1578 0.1508 -0.0222 0.0164  -0.0177 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.1893 0.1471 0.1547 -0.0095 0.0075  -0.0185 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.1931 0.1441 0.1647 -0.0089 0.0057  -0.0214 122 GLY   A O   
906  N N   . ILE   A 117 ? 0.1886 0.1417 0.1481 -0.0017 0.0015  -0.0150 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.2015 0.1326 0.1497 0.0048  -0.0084 -0.0153 123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.2082 0.1279 0.1316 0.0111  -0.0030 -0.0107 123 ILE   A C   
909  O O   . ILE   A 117 ? 0.1904 0.1222 0.1193 0.0130  0.0052  -0.0056 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.2226 0.1410 0.1840 0.0051  -0.0208 -0.0165 123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.2339 0.1610 0.1999 0.0066  -0.0165 -0.0159 123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.2200 0.1406 0.2176 0.0008  -0.0247 -0.0178 123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.2672 0.1776 0.2447 0.0071  -0.0318 -0.0150 123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.2324 0.1241 0.1283 0.0131  -0.0050 -0.0110 124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.2424 0.1115 0.1113 0.0188  0.0094  -0.0075 124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.2572 0.1115 0.1178 0.0213  0.0108  -0.0074 124 VAL   A C   
917  O O   . VAL   A 118 ? 0.2871 0.1259 0.1402 0.0171  -0.0064 -0.0109 124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.2876 0.1131 0.1132 0.0165  0.0076  -0.0099 124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.3302 0.1203 0.1225 0.0216  0.0321  -0.0076 124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.2965 0.1370 0.1314 0.0149  0.0074  -0.0095 124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.2476 0.1073 0.1162 0.0275  0.0304  -0.0010 125 SER   A N   
922  C CA  . SER   A 119 ? 0.2750 0.1229 0.1401 0.0306  0.0353  -0.0002 125 SER   A CA  
923  C C   . SER   A 119 ? 0.3378 0.1515 0.1833 0.0375  0.0641  0.0041  125 SER   A C   
924  O O   . SER   A 119 ? 0.3672 0.1466 0.1860 0.0380  0.0698  0.0009  125 SER   A O   
925  C CB  . SER   A 119 ? 0.2578 0.1509 0.1672 0.0302  0.0314  0.0055  125 SER   A CB  
926  O OG  . SER   A 119 ? 0.2671 0.1522 0.1789 0.0344  0.0384  0.0081  125 SER   A OG  
927  N N   . THR   A 120 ? 0.3510 0.1699 0.2112 0.0422  0.0849  0.0120  126 THR   A N   
928  C CA  . THR   A 120 ? 0.4020 0.1855 0.2550 0.0501  0.1224  0.0183  126 THR   A CA  
929  C C   . THR   A 120 ? 0.4381 0.2027 0.2777 0.0513  0.1397  0.0199  126 THR   A C   
930  O O   . THR   A 120 ? 0.3978 0.1842 0.2396 0.0467  0.1203  0.0175  126 THR   A O   
931  C CB  . THR   A 120 ? 0.3841 0.2069 0.3068 0.0576  0.1377  0.0365  126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.3772 0.2466 0.3519 0.0566  0.1316  0.0510  126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.3701 0.2164 0.3115 0.0559  0.1210  0.0370  126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.4938 0.2167 0.3232 0.0580  0.1803  0.0246  127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.5336 0.2383 0.3580 0.0605  0.2031  0.0283  127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.6054 0.2469 0.4088 0.0671  0.2566  0.0311  127 GLY   A C   
937  O O   . GLY   A 121 ? 0.6226 0.2358 0.4195 0.0702  0.2777  0.0310  127 GLY   A O   
938  N N   . GLY   A 122 ? 0.6566 0.2707 0.4448 0.0682  0.2803  0.0323  128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.7335 0.2771 0.4974 0.0737  0.3403  0.0343  128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.7252 0.3053 0.5801 0.0865  0.3708  0.0569  128 GLY   A C   
941  O O   . GLY   A 122 ? 0.6653 0.3250 0.6099 0.0909  0.3463  0.0750  128 GLY   A O   
942  N N   . ASN   A 123 ? 0.7774 0.2940 0.6097 0.0907  0.4253  0.0581  129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.7561 0.2996 0.6820 0.1035  0.4609  0.0826  129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.7003 0.3055 0.6616 0.1009  0.4227  0.0899  129 ASN   A C   
945  O O   . ASN   A 123 ? 0.6742 0.3254 0.7330 0.1092  0.4332  0.1158  129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.7465 0.3380 0.7890 0.1157  0.4766  0.1099  129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.8661 0.3927 0.8884 0.1211  0.5279  0.1063  129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.9578 0.3886 0.8988 0.1194  0.5797  0.0911  129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.8475 0.4192 0.9429 0.1264  0.5182  0.1216  129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.6837 0.2831 0.5672 0.0885  0.3818  0.0690  130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.6211 0.2733 0.5307 0.0852  0.3472  0.0734  130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.5268 0.2646 0.4980 0.0818  0.2953  0.0826  130 GLY   A C   
953  O O   . GLY   A 124 ? 0.5003 0.2865 0.5088 0.0785  0.2698  0.0914  130 GLY   A O   
954  N N   . LEU   A 125 ? 0.4886 0.2374 0.4590 0.0800  0.2794  0.0788  131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.4231 0.2389 0.4356 0.0739  0.2340  0.0848  131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.4313 0.2354 0.3762 0.0652  0.2019  0.0610  131 LEU   A C   
957  O O   . LEU   A 125 ? 0.5124 0.2628 0.3988 0.0649  0.2153  0.0473  131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.3927 0.2353 0.4797 0.0796  0.2446  0.1065  131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.3895 0.2512 0.5703 0.0877  0.2731  0.1388  131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.3878 0.2542 0.6346 0.0952  0.2958  0.1589  131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.3662 0.2884 0.6007 0.0780  0.2347  0.1576  131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.3495 0.2024 0.3102 0.0569  0.1614  0.0594  132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.3236 0.1727 0.2428 0.0498  0.1333  0.0418  132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.2805 0.1808 0.2462 0.0451  0.1109  0.0505  132 VAL   A C   
965  O O   . VAL   A 126 ? 0.2575 0.1959 0.2654 0.0403  0.1009  0.0646  132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.3397 0.1821 0.2193 0.0421  0.1109  0.0278  132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.3286 0.2120 0.2429 0.0385  0.0998  0.0355  132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.3482 0.1905 0.2043 0.0350  0.0825  0.0147  132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.2592 0.1537 0.2126 0.0446  0.1037  0.0436  133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.2329 0.1663 0.2190 0.0385  0.0842  0.0499  133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.2421 0.1784 0.2004 0.0308  0.0598  0.0333  133 GLY   A C   
972  O O   . GLY   A 127 ? 0.2800 0.1854 0.2006 0.0323  0.0569  0.0196  133 GLY   A O   
973  N N   . PHE   A 128 ? 0.1976 0.1662 0.1744 0.0201  0.0422  0.0364  134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.1940 0.1642 0.1543 0.0127  0.0266  0.0223  134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.1795 0.1658 0.1534 0.0057  0.0192  0.0257  134 PHE   A C   
976  O O   . PHE   A 128 ? 0.1775 0.1830 0.1708 -0.0032 0.0149  0.0400  134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.1800 0.1611 0.1379 0.0028  0.0195  0.0197  134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.1875 0.1574 0.1352 0.0078  0.0253  0.0185  134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.2044 0.1514 0.1293 0.0112  0.0222  0.0062  134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.2040 0.1848 0.1685 0.0079  0.0319  0.0324  134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.2194 0.1522 0.1298 0.0140  0.0266  0.0056  134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.2193 0.1881 0.1735 0.0125  0.0392  0.0309  134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.2231 0.1667 0.1463 0.0155  0.0372  0.0164  134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.1741 0.1503 0.1380 0.0071  0.0148  0.0144  135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.1518 0.1395 0.1245 -0.0003 0.0094  0.0154  135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.1681 0.1598 0.1336 -0.0150 0.0061  0.0101  135 ALA   A C   
987  O O   . ALA   A 129 ? 0.1604 0.1417 0.1210 -0.0144 0.0078  -0.0015 135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.1657 0.1389 0.1336 0.0063  0.0071  0.0058  135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.1745 0.1752 0.1382 -0.0304 0.0017  0.0199  136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.2128 0.2032 0.1545 -0.0488 0.0030  0.0139  136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.2140 0.1899 0.1494 -0.0519 0.0119  0.0006  136 ASP   A C   
992  O O   . ASP   A 130 ? 0.2080 0.1871 0.1527 -0.0474 0.0102  0.0015  136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.2570 0.2500 0.1872 -0.0704 -0.0090 0.0310  136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.3333 0.3018 0.2232 -0.0950 -0.0067 0.0255  136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.3208 0.2812 0.2020 -0.0941 0.0017  0.0162  136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.3972 0.3484 0.2592 -0.1165 -0.0110 0.0293  136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.2167 0.1743 0.1399 -0.0601 0.0249  -0.0113 137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.2340 0.1736 0.1588 -0.0641 0.0406  -0.0220 137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.2768 0.1851 0.1616 -0.0890 0.0568  -0.0270 137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.3181 0.2029 0.2004 -0.0947 0.0782  -0.0365 137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.2356 0.1733 0.1975 -0.0485 0.0487  -0.0308 137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.2382 0.1921 0.2226 -0.0301 0.0307  -0.0259 137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.2304 0.1599 0.1953 -0.0499 0.0576  -0.0357 137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.2807 0.1829 0.1333 -0.1049 0.0489  -0.0204 138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.3276 0.1883 0.1277 -0.1329 0.0636  -0.0256 138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.4058 0.2352 0.1611 -0.1572 0.0665  -0.0237 138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.4696 0.2495 0.1767 -0.1794 0.0906  -0.0339 138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.3458 0.2066 0.1210 -0.1464 0.0472  -0.0154 138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.3330 0.2153 0.1417 -0.1265 0.0486  -0.0191 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.3179 0.2030 0.1057 -0.1403 0.0303  -0.0059 138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.3248 0.2425 0.1370 -0.1351 0.0033  0.0152  138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.3399 0.2709 0.1580 -0.1408 -0.0151 0.0324  138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.3657 0.2781 0.1553 -0.1558 -0.0143 0.0307  138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.3206 0.2815 0.1771 -0.1319 -0.0324 0.0528  138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.4046 0.2569 0.1737 -0.1537 0.0455  -0.0113 139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.4379 0.2604 0.1648 -0.1776 0.0452  -0.0079 139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.4396 0.2475 0.1797 -0.1681 0.0741  -0.0236 139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.4798 0.2513 0.1764 -0.1898 0.0831  -0.0250 139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.4460 0.2987 0.1886 -0.1796 0.0104  0.0150  139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.4357 0.3348 0.2441 -0.1456 0.0059  0.0165  139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.4063 0.3262 0.2502 -0.1212 0.0126  0.0090  139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.4020 0.3120 0.2215 -0.1458 -0.0056 0.0262  139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.3959 0.2283 0.1952 -0.1383 0.0868  -0.0330 140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.4022 0.2260 0.2307 -0.1276 0.1105  -0.0430 140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.4550 0.2295 0.2646 -0.1401 0.1526  -0.0575 140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.4430 0.2214 0.3006 -0.1242 0.1712  -0.0641 140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.3548 0.2193 0.2538 -0.0956 0.1003  -0.0422 140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.3327 0.2364 0.2457 -0.0828 0.0664  -0.0295 140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.3008 0.2278 0.2639 -0.0572 0.0577  -0.0301 140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.3505 0.2566 0.2508 -0.0900 0.0570  -0.0223 140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.5158 0.2376 0.2519 -0.1718 0.1684  -0.0608 141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.5835 0.2420 0.2825 -0.1897 0.2157  -0.0755 141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.6021 0.2495 0.3594 -0.1732 0.2575  -0.0854 141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.6216 0.2378 0.3960 -0.1724 0.2985  -0.0952 141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.6480 0.2393 0.2386 -0.2329 0.2216  -0.0761 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.6928 0.2890 0.2286 -0.2556 0.1762  -0.0604 141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.7958 0.3095 0.2155 -0.3051 0.1822  -0.0599 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.6873 0.3027 0.2404 -0.2471 0.1693  -0.0603 141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.5814 0.2568 0.3796 -0.1585 0.2467  -0.0805 142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.5603 0.2309 0.4252 -0.1424 0.2799  -0.0849 142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.5300 0.2364 0.4914 -0.1141 0.2802  -0.0815 142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.5310 0.2258 0.5574 -0.1039 0.3132  -0.0824 142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.5271 0.2203 0.4071 -0.1356 0.2613  -0.0786 142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.4690 0.2261 0.3764 -0.1174 0.2069  -0.0663 142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.4677 0.2417 0.3286 -0.1273 0.1707  -0.0577 142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.4139 0.2185 0.4012 -0.0883 0.1855  -0.0596 142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.4301 0.2571 0.3381 -0.1039 0.1360  -0.0484 142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.3995 0.2423 0.3762 -0.0815 0.1430  -0.0505 142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.3912 0.2047 0.4593 -0.0697 0.1976  -0.0580 142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.3722 0.2525 0.3995 -0.0588 0.1161  -0.0437 142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.3631 0.2171 0.4836 -0.0492 0.1625  -0.0482 142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.3537 0.2366 0.4459 -0.0446 0.1239  -0.0430 142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.5111 0.2579 0.4857 -0.1029 0.2439  -0.0754 143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.4840 0.2580 0.5419 -0.0809 0.2399  -0.0702 143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.5560 0.2906 0.6431 -0.0851 0.2901  -0.0768 143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.5218 0.2715 0.6987 -0.0682 0.2957  -0.0690 143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.4437 0.2538 0.4918 -0.0734 0.1990  -0.0646 143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.4016 0.2513 0.4438 -0.0633 0.1544  -0.0560 143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.3874 0.2619 0.4148 -0.0580 0.1247  -0.0514 143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.3637 0.2345 0.4740 -0.0448 0.1409  -0.0484 143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.6540 0.3333 0.6649 -0.1098 0.3265  -0.0892 144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.7350 0.3622 0.7516 -0.1189 0.3828  -0.0984 144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.8219 0.3854 0.8294 -0.1317 0.4451  -0.1076 144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.8618 0.3735 0.8703 -0.1403 0.4992  -0.1160 144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.8166 0.4096 0.7351 -0.1433 0.3840  -0.1073 144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.8743 0.5125 0.8151 -0.1311 0.3469  -0.1009 144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.8562 0.5259 0.8888 -0.1085 0.3450  -0.0939 144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.9409 0.5819 0.8101 -0.1453 0.3178  -0.1005 144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.8630 0.4199 0.8487 -0.1365 0.4434  -0.1075 145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.9298 0.4173 0.8987 -0.1508 0.5083  -0.1172 145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.9116 0.4246 0.9741 -0.1303 0.5147  -0.1078 145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.9347 0.3971 1.0265 -0.1334 0.5773  -0.1123 145 GLU   A O   
1073 C CB  . GLU   A 139 ? 1.0451 0.4682 0.8703 -0.1884 0.5164  -0.1288 145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 1.1153 0.5826 0.8974 -0.1918 0.4517  -0.1200 145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 1.2647 0.6925 0.9158 -0.2284 0.4295  -0.1226 145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 1.2909 0.7268 0.8942 -0.2410 0.3944  -0.1156 145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 1.3347 0.7230 0.9342 -0.2458 0.4448  -0.1292 145 GLU   A OE2 
1078 N N1  . A1BOQ B .   ? 0.6241 0.2023 0.2951 0.0406  0.1635  -0.0069 201 A1BOQ A N1  
1079 C C4  . A1BOQ B .   ? 0.8381 0.3488 0.4241 0.0312  0.2005  -0.0091 201 A1BOQ A C4  
1080 C C5  . A1BOQ B .   ? 0.7966 0.3612 0.4140 0.0282  0.1546  -0.0100 201 A1BOQ A C5  
1081 C C6  . A1BOQ B .   ? 0.7873 0.3485 0.4020 0.0268  0.1449  -0.0122 201 A1BOQ A C6  
1082 C C7  . A1BOQ B .   ? 0.8076 0.3102 0.3843 0.0277  0.1794  -0.0141 201 A1BOQ A C7  
1083 C C8  . A1BOQ B .   ? 0.7622 0.2603 0.3343 0.0255  0.1671  -0.0165 201 A1BOQ A C8  
1084 C C10 . A1BOQ B .   ? 0.6636 0.1787 0.2596 0.0272  0.1481  -0.0171 201 A1BOQ A C10 
1085 C C13 . A1BOQ B .   ? 0.5037 0.1984 0.2743 0.0445  0.1129  -0.0001 201 A1BOQ A C13 
1086 C C15 . A1BOQ B .   ? 0.5444 0.1957 0.3001 0.0510  0.1596  0.0040  201 A1BOQ A C15 
1087 O O2  . A1BOQ B .   ? 0.4348 0.1979 0.3021 0.0569  0.1244  0.0170  201 A1BOQ A O2  
1088 C C14 . A1BOQ B .   ? 0.4380 0.2005 0.2830 0.0510  0.1071  0.0105  201 A1BOQ A C14 
1089 N N2  . A1BOQ B .   ? 0.3892 0.2027 0.2681 0.0476  0.0832  0.0126  201 A1BOQ A N2  
1090 C C12 . A1BOQ B .   ? 0.5570 0.1997 0.2670 0.0343  0.0953  -0.0099 201 A1BOQ A C12 
1091 C C11 . A1BOQ B .   ? 0.6264 0.1866 0.2476 0.0216  0.0980  -0.0179 201 A1BOQ A C11 
1092 C C9  . A1BOQ B .   ? 0.6569 0.2303 0.3229 0.0411  0.1747  -0.0056 201 A1BOQ A C9  
1093 O O1  . A1BOQ B .   ? 0.5961 0.2196 0.3276 0.0513  0.1875  0.0056  201 A1BOQ A O1  
1094 C C1  . A1BOQ B .   ? 0.8755 0.3212 0.4208 0.0308  0.2294  -0.0136 201 A1BOQ A C1  
1095 O O   . A1BOQ B .   ? 0.9314 0.3112 0.4386 0.0315  0.2718  -0.0160 201 A1BOQ A O   
1096 C C   . A1BOQ B .   ? 0.8950 0.3110 0.4856 0.0501  0.3113  -0.0028 201 A1BOQ A C   
1097 C C2  . A1BOQ B .   ? 0.8854 0.3350 0.4369 0.0329  0.2413  -0.0107 201 A1BOQ A C2  
1098 C C3  . A1BOQ B .   ? 0.9378 0.3340 0.4725 0.0386  0.2995  -0.0078 201 A1BOQ A C3  
1099 N N   . A1BOQ B .   ? 0.9792 0.3300 0.5034 0.0435  0.3498  -0.0051 201 A1BOQ A N   
# 
