data_7HVM
# 
_entry.id   7HVM 
# 
_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   7HVM         pdb_00007hvm 10.2210/pdb7hvm/pdb 
WWPDB D_1001407987 ?            ?                   
# 
_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                        7HVM 
_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 'N~3~-(2-methylphenyl)pyridine-3,5-dicarboxamide' 255.272   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    149 ?         ? ? ? 
# 
_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 'N~3~-(2-methylphenyl)pyridine-3,5-dicarboxamide' A1BN5 
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 
A1BN5 non-polymer         . 'N~3~-(2-methylphenyl)pyridine-3,5-dicarboxamide' ? 'C14 H13 N3 O2'  255.272 
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        A1BN5 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BN5 
_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 A1BN5 1   201 201 A1BN5 LIG A . 
C 3 ZN    1   202 1   ZN    ZN  A . 
D 4 DMS   1   203 6   DMS   DMS A . 
E 5 HOH   1   301 135 HOH   HOH A . 
E 5 HOH   2   302 77  HOH   HOH A . 
E 5 HOH   3   303 143 HOH   HOH A . 
E 5 HOH   4   304 62  HOH   HOH A . 
E 5 HOH   5   305 136 HOH   HOH A . 
E 5 HOH   6   306 120 HOH   HOH A . 
E 5 HOH   7   307 58  HOH   HOH A . 
E 5 HOH   8   308 11  HOH   HOH A . 
E 5 HOH   9   309 125 HOH   HOH A . 
E 5 HOH   10  310 100 HOH   HOH A . 
E 5 HOH   11  311 1   HOH   HOH A . 
E 5 HOH   12  312 79  HOH   HOH A . 
E 5 HOH   13  313 122 HOH   HOH A . 
E 5 HOH   14  314 84  HOH   HOH A . 
E 5 HOH   15  315 93  HOH   HOH A . 
E 5 HOH   16  316 37  HOH   HOH A . 
E 5 HOH   17  317 103 HOH   HOH A . 
E 5 HOH   18  318 107 HOH   HOH A . 
E 5 HOH   19  319 123 HOH   HOH A . 
E 5 HOH   20  320 36  HOH   HOH A . 
E 5 HOH   21  321 112 HOH   HOH A . 
E 5 HOH   22  322 148 HOH   HOH A . 
E 5 HOH   23  323 80  HOH   HOH A . 
E 5 HOH   24  324 94  HOH   HOH A . 
E 5 HOH   25  325 15  HOH   HOH A . 
E 5 HOH   26  326 38  HOH   HOH A . 
E 5 HOH   27  327 4   HOH   HOH A . 
E 5 HOH   28  328 121 HOH   HOH A . 
E 5 HOH   29  329 95  HOH   HOH A . 
E 5 HOH   30  330 74  HOH   HOH A . 
E 5 HOH   31  331 64  HOH   HOH A . 
E 5 HOH   32  332 57  HOH   HOH A . 
E 5 HOH   33  333 45  HOH   HOH A . 
E 5 HOH   34  334 14  HOH   HOH A . 
E 5 HOH   35  335 70  HOH   HOH A . 
E 5 HOH   36  336 66  HOH   HOH A . 
E 5 HOH   37  337 12  HOH   HOH A . 
E 5 HOH   38  338 3   HOH   HOH A . 
E 5 HOH   39  339 26  HOH   HOH A . 
E 5 HOH   40  340 130 HOH   HOH A . 
E 5 HOH   41  341 24  HOH   HOH A . 
E 5 HOH   42  342 75  HOH   HOH A . 
E 5 HOH   43  343 137 HOH   HOH A . 
E 5 HOH   44  344 43  HOH   HOH A . 
E 5 HOH   45  345 60  HOH   HOH A . 
E 5 HOH   46  346 88  HOH   HOH A . 
E 5 HOH   47  347 109 HOH   HOH A . 
E 5 HOH   48  348 78  HOH   HOH A . 
E 5 HOH   49  349 48  HOH   HOH A . 
E 5 HOH   50  350 31  HOH   HOH A . 
E 5 HOH   51  351 41  HOH   HOH A . 
E 5 HOH   52  352 29  HOH   HOH A . 
E 5 HOH   53  353 27  HOH   HOH A . 
E 5 HOH   54  354 53  HOH   HOH A . 
E 5 HOH   55  355 132 HOH   HOH A . 
E 5 HOH   56  356 10  HOH   HOH A . 
E 5 HOH   57  357 119 HOH   HOH A . 
E 5 HOH   58  358 83  HOH   HOH A . 
E 5 HOH   59  359 92  HOH   HOH A . 
E 5 HOH   60  360 56  HOH   HOH A . 
E 5 HOH   61  361 73  HOH   HOH A . 
E 5 HOH   62  362 18  HOH   HOH A . 
E 5 HOH   63  363 72  HOH   HOH A . 
E 5 HOH   64  364 44  HOH   HOH A . 
E 5 HOH   65  365 68  HOH   HOH A . 
E 5 HOH   66  366 25  HOH   HOH A . 
E 5 HOH   67  367 90  HOH   HOH A . 
E 5 HOH   68  368 16  HOH   HOH A . 
E 5 HOH   69  369 42  HOH   HOH A . 
E 5 HOH   70  370 59  HOH   HOH A . 
E 5 HOH   71  371 40  HOH   HOH A . 
E 5 HOH   72  372 126 HOH   HOH A . 
E 5 HOH   73  373 50  HOH   HOH A . 
E 5 HOH   74  374 85  HOH   HOH A . 
E 5 HOH   75  375 5   HOH   HOH A . 
E 5 HOH   76  376 76  HOH   HOH A . 
E 5 HOH   77  377 9   HOH   HOH A . 
E 5 HOH   78  378 91  HOH   HOH A . 
E 5 HOH   79  379 105 HOH   HOH A . 
E 5 HOH   80  380 17  HOH   HOH A . 
E 5 HOH   81  381 52  HOH   HOH A . 
E 5 HOH   82  382 134 HOH   HOH A . 
E 5 HOH   83  383 124 HOH   HOH A . 
E 5 HOH   84  384 61  HOH   HOH A . 
E 5 HOH   85  385 34  HOH   HOH A . 
E 5 HOH   86  386 86  HOH   HOH A . 
E 5 HOH   87  387 54  HOH   HOH A . 
E 5 HOH   88  388 99  HOH   HOH A . 
E 5 HOH   89  389 96  HOH   HOH A . 
E 5 HOH   90  390 13  HOH   HOH A . 
E 5 HOH   91  391 89  HOH   HOH A . 
E 5 HOH   92  392 28  HOH   HOH A . 
E 5 HOH   93  393 8   HOH   HOH A . 
E 5 HOH   94  394 67  HOH   HOH A . 
E 5 HOH   95  395 138 HOH   HOH A . 
E 5 HOH   96  396 71  HOH   HOH A . 
E 5 HOH   97  397 87  HOH   HOH A . 
E 5 HOH   98  398 19  HOH   HOH A . 
E 5 HOH   99  399 39  HOH   HOH A . 
E 5 HOH   100 400 133 HOH   HOH A . 
E 5 HOH   101 401 128 HOH   HOH A . 
E 5 HOH   102 402 102 HOH   HOH A . 
E 5 HOH   103 403 63  HOH   HOH A . 
E 5 HOH   104 404 55  HOH   HOH A . 
E 5 HOH   105 405 129 HOH   HOH A . 
E 5 HOH   106 406 131 HOH   HOH A . 
E 5 HOH   107 407 69  HOH   HOH A . 
E 5 HOH   108 408 33  HOH   HOH A . 
E 5 HOH   109 409 110 HOH   HOH A . 
E 5 HOH   110 410 22  HOH   HOH A . 
E 5 HOH   111 411 6   HOH   HOH A . 
E 5 HOH   112 412 127 HOH   HOH A . 
E 5 HOH   113 413 46  HOH   HOH A . 
E 5 HOH   114 414 32  HOH   HOH A . 
E 5 HOH   115 415 35  HOH   HOH A . 
E 5 HOH   116 416 30  HOH   HOH A . 
E 5 HOH   117 417 108 HOH   HOH A . 
E 5 HOH   118 418 106 HOH   HOH A . 
E 5 HOH   119 419 146 HOH   HOH A . 
E 5 HOH   120 420 101 HOH   HOH A . 
E 5 HOH   121 421 118 HOH   HOH A . 
E 5 HOH   122 422 104 HOH   HOH A . 
E 5 HOH   123 423 65  HOH   HOH A . 
E 5 HOH   124 424 113 HOH   HOH A . 
E 5 HOH   125 425 144 HOH   HOH A . 
E 5 HOH   126 426 117 HOH   HOH A . 
E 5 HOH   127 427 23  HOH   HOH A . 
E 5 HOH   128 428 140 HOH   HOH A . 
E 5 HOH   129 429 98  HOH   HOH A . 
E 5 HOH   130 430 115 HOH   HOH A . 
E 5 HOH   131 431 7   HOH   HOH A . 
E 5 HOH   132 432 147 HOH   HOH A . 
E 5 HOH   133 433 139 HOH   HOH A . 
E 5 HOH   134 434 21  HOH   HOH A . 
E 5 HOH   135 435 149 HOH   HOH A . 
E 5 HOH   136 436 51  HOH   HOH A . 
E 5 HOH   137 437 142 HOH   HOH A . 
E 5 HOH   138 438 20  HOH   HOH A . 
E 5 HOH   139 439 151 HOH   HOH A . 
E 5 HOH   140 440 116 HOH   HOH A . 
E 5 HOH   141 441 150 HOH   HOH A . 
E 5 HOH   142 442 2   HOH   HOH A . 
E 5 HOH   143 443 81  HOH   HOH A . 
E 5 HOH   144 444 145 HOH   HOH A . 
E 5 HOH   145 445 82  HOH   HOH A . 
E 5 HOH   146 446 97  HOH   HOH A . 
E 5 HOH   147 447 111 HOH   HOH A . 
E 5 HOH   148 448 141 HOH   HOH A . 
E 5 HOH   149 449 114 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           7HVM 
_cell.length_a           73.685 
_cell.length_b           60.605 
_cell.length_c           32.684 
_cell.angle_alpha        90.00 
_cell.angle_beta         93.45 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HVM 
_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          7HVM 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.29 
_exptl_crystal.density_percent_sol   46.33 
_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                     7HVM 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             46.77 
_reflns.d_resolution_high            1.38 
_reflns.number_obs                   29622 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            0.067 
_reflns.pdbx_netI_over_sigmaI        12.5 
_reflns.pdbx_redundancy              6.2 
_reflns.pdbx_Rrim_I_all              0.073 
_reflns.pdbx_Rpim_I_all              0.028 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     183674 
_reflns.pdbx_chi_squared             0.91 
_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                  1.38 
_reflns_shell.d_res_low                   1.45 
_reflns_shell.number_measured_all         18120 
_reflns_shell.number_unique_obs           4270 
_reflns_shell.Rmerge_I_obs                1.157 
_reflns_shell.pdbx_chi_squared            0.76 
_reflns_shell.pdbx_redundancy             4.2 
_reflns_shell.percent_possible_obs        99.4 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.1 
_reflns_shell.pdbx_Rrim_I_all             1.325 
_reflns_shell.pdbx_Rpim_I_all             0.631 
_reflns_shell.pdbx_CC_half                0.495 
_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                                 7HVM 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     29568 
_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                             16.84 
_refine.ls_d_res_high                            1.378 
_refine.ls_percent_reflns_obs                    99.7 
_refine.ls_R_factor_obs                          0.1896 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1876 
_refine.ls_R_factor_R_free                       0.2313 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.660 
_refine.ls_number_reflns_R_free                  1377 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.960 
_refine.correlation_coeff_Fo_to_Fc_free          0.935 
_refine.B_iso_mean                               23.57 
_refine.aniso_B[1][1]                            -1.36930 
_refine.aniso_B[2][2]                            -0.25210 
_refine.aniso_B[3][3]                            1.62130 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.73980 
_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             0.058 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.065 
_refine.pdbx_overall_SU_R_Blow_DPI               0.061 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.068 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HVM 
_refine_analyze.Luzzati_coordinate_error_obs    0.17 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1074 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         24 
_refine_hist.number_atoms_solvent             149 
_refine_hist.number_atoms_total               1247 
_refine_hist.d_res_high                       1.378 
_refine_hist.d_res_low                        16.84 
# 
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                  0.012 ? 2.00  1131 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.05  ? 2.00  1540 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  373  '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  213  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1131 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.51  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.70 ? ?     ?    '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  1007 '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                       1.38 
_refine_ls_shell.d_res_low                        1.39 
_refine_ls_shell.number_reflns_R_work             555 
_refine_ls_shell.R_factor_R_work                  0.3075 
_refine_ls_shell.percent_reflns_obs               91.75 
_refine_ls_shell.R_factor_R_free                  0.3678 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            6.25 
_refine_ls_shell.number_reflns_R_free             37 
_refine_ls_shell.number_reflns_all                592 
_refine_ls_shell.R_factor_all                     0.3113 
# 
_struct.entry_id                  7HVM 
_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-0032584-001 (A71EV2A-x3564)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HVM 
_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              7HVM 
_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 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P4 AA4 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P5 AA5 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.336 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.279 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.313 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.130 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 109.6 ? 
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_555 107.7 ? 
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_555 117.5 ? 
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_555 109.0 ? 
5 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 100.8 ? 
6 SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 111.8 ? 
# 
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 GLY A 43  ? N GLY A 49  O GLY A 7   ? O GLY A 13  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7HVM 
_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   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    301 
_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    329 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.84 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 449 ? ? 1_555 O A HOH 449 ? ? 2_656 0.80 
2 1 O A HOH 302 ? ? 1_555 O A HOH 302 ? ? 2_656 0.88 
# 
_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         14.9566 
_pdbx_refine_tls.origin_y         6.8150 
_pdbx_refine_tls.origin_z         14.6053 
_pdbx_refine_tls.T[1][1]          -0.0325 
_pdbx_refine_tls.T[2][2]          -0.0242 
_pdbx_refine_tls.T[3][3]          0.0042 
_pdbx_refine_tls.T[1][2]          0.0016 
_pdbx_refine_tls.T[1][3]          -0.0071 
_pdbx_refine_tls.T[2][3]          -0.0027 
_pdbx_refine_tls.L[1][1]          1.0791 
_pdbx_refine_tls.L[2][2]          1.2884 
_pdbx_refine_tls.L[3][3]          0.7088 
_pdbx_refine_tls.L[1][2]          0.7840 
_pdbx_refine_tls.L[1][3]          -0.1228 
_pdbx_refine_tls.L[2][3]          -0.1271 
_pdbx_refine_tls.S[1][1]          -0.0453 
_pdbx_refine_tls.S[1][2]          0.0485 
_pdbx_refine_tls.S[1][3]          0.0885 
_pdbx_refine_tls.S[2][1]          0.0186 
_pdbx_refine_tls.S[2][2]          0.0828 
_pdbx_refine_tls.S[2][3]          -0.0256 
_pdbx_refine_tls.S[3][1]          0.0168 
_pdbx_refine_tls.S[3][2]          -0.0324 
_pdbx_refine_tls.S[3][3]          -0.0374 
# 
_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 
A1BN5 N1   N  Y N 1   
A1BN5 C4   C  Y N 2   
A1BN5 C5   C  Y N 3   
A1BN5 C6   C  Y N 4   
A1BN5 C7   C  N N 5   
A1BN5 C8   C  Y N 6   
A1BN5 C10  C  Y N 7   
A1BN5 C13  C  Y N 8   
A1BN5 O1   O  N N 9   
A1BN5 C12  C  N N 10  
A1BN5 N2   N  N N 11  
A1BN5 C11  C  Y N 12  
A1BN5 C9   C  Y N 13  
A1BN5 O    O  N N 14  
A1BN5 N    N  N N 15  
A1BN5 C1   C  Y N 16  
A1BN5 C    C  N N 17  
A1BN5 C3   C  Y N 18  
A1BN5 C2   C  Y N 19  
A1BN5 H5   H  N N 20  
A1BN5 H6   H  N N 21  
A1BN5 H9   H  N N 22  
A1BN5 H12  H  N N 23  
A1BN5 H11  H  N N 24  
A1BN5 H10  H  N N 25  
A1BN5 H8   H  N N 26  
A1BN5 H7   H  N N 27  
A1BN5 H1   H  N N 28  
A1BN5 H2   H  N N 29  
A1BN5 H    H  N N 30  
A1BN5 H4   H  N N 31  
A1BN5 H3   H  N N 32  
ALA   N    N  N N 33  
ALA   CA   C  N S 34  
ALA   C    C  N N 35  
ALA   O    O  N N 36  
ALA   CB   C  N N 37  
ALA   OXT  O  N N 38  
ALA   H    H  N N 39  
ALA   H2   H  N N 40  
ALA   HA   H  N N 41  
ALA   HB1  H  N N 42  
ALA   HB2  H  N N 43  
ALA   HB3  H  N N 44  
ALA   HXT  H  N N 45  
ARG   N    N  N N 46  
ARG   CA   C  N S 47  
ARG   C    C  N N 48  
ARG   O    O  N N 49  
ARG   CB   C  N N 50  
ARG   CG   C  N N 51  
ARG   CD   C  N N 52  
ARG   NE   N  N N 53  
ARG   CZ   C  N N 54  
ARG   NH1  N  N N 55  
ARG   NH2  N  N N 56  
ARG   OXT  O  N N 57  
ARG   H    H  N N 58  
ARG   H2   H  N N 59  
ARG   HA   H  N N 60  
ARG   HB2  H  N N 61  
ARG   HB3  H  N N 62  
ARG   HG2  H  N N 63  
ARG   HG3  H  N N 64  
ARG   HD2  H  N N 65  
ARG   HD3  H  N N 66  
ARG   HE   H  N N 67  
ARG   HH11 H  N N 68  
ARG   HH12 H  N N 69  
ARG   HH21 H  N N 70  
ARG   HH22 H  N N 71  
ARG   HXT  H  N N 72  
ASN   N    N  N N 73  
ASN   CA   C  N S 74  
ASN   C    C  N N 75  
ASN   O    O  N N 76  
ASN   CB   C  N N 77  
ASN   CG   C  N N 78  
ASN   OD1  O  N N 79  
ASN   ND2  N  N N 80  
ASN   OXT  O  N N 81  
ASN   H    H  N N 82  
ASN   H2   H  N N 83  
ASN   HA   H  N N 84  
ASN   HB2  H  N N 85  
ASN   HB3  H  N N 86  
ASN   HD21 H  N N 87  
ASN   HD22 H  N N 88  
ASN   HXT  H  N N 89  
ASP   N    N  N N 90  
ASP   CA   C  N S 91  
ASP   C    C  N N 92  
ASP   O    O  N N 93  
ASP   CB   C  N N 94  
ASP   CG   C  N N 95  
ASP   OD1  O  N N 96  
ASP   OD2  O  N N 97  
ASP   OXT  O  N N 98  
ASP   H    H  N N 99  
ASP   H2   H  N N 100 
ASP   HA   H  N N 101 
ASP   HB2  H  N N 102 
ASP   HB3  H  N N 103 
ASP   HD2  H  N N 104 
ASP   HXT  H  N N 105 
CYS   N    N  N N 106 
CYS   CA   C  N R 107 
CYS   C    C  N N 108 
CYS   O    O  N N 109 
CYS   CB   C  N N 110 
CYS   SG   S  N N 111 
CYS   OXT  O  N N 112 
CYS   H    H  N N 113 
CYS   H2   H  N N 114 
CYS   HA   H  N N 115 
CYS   HB2  H  N N 116 
CYS   HB3  H  N N 117 
CYS   HG   H  N N 118 
CYS   HXT  H  N N 119 
DMS   S    S  N N 120 
DMS   O    O  N N 121 
DMS   C1   C  N N 122 
DMS   C2   C  N N 123 
DMS   H11  H  N N 124 
DMS   H12  H  N N 125 
DMS   H13  H  N N 126 
DMS   H21  H  N N 127 
DMS   H22  H  N N 128 
DMS   H23  H  N N 129 
GLN   N    N  N N 130 
GLN   CA   C  N S 131 
GLN   C    C  N N 132 
GLN   O    O  N N 133 
GLN   CB   C  N N 134 
GLN   CG   C  N N 135 
GLN   CD   C  N N 136 
GLN   OE1  O  N N 137 
GLN   NE2  N  N N 138 
GLN   OXT  O  N N 139 
GLN   H    H  N N 140 
GLN   H2   H  N N 141 
GLN   HA   H  N N 142 
GLN   HB2  H  N N 143 
GLN   HB3  H  N N 144 
GLN   HG2  H  N N 145 
GLN   HG3  H  N N 146 
GLN   HE21 H  N N 147 
GLN   HE22 H  N N 148 
GLN   HXT  H  N N 149 
GLU   N    N  N N 150 
GLU   CA   C  N S 151 
GLU   C    C  N N 152 
GLU   O    O  N N 153 
GLU   CB   C  N N 154 
GLU   CG   C  N N 155 
GLU   CD   C  N N 156 
GLU   OE1  O  N N 157 
GLU   OE2  O  N N 158 
GLU   OXT  O  N N 159 
GLU   H    H  N N 160 
GLU   H2   H  N N 161 
GLU   HA   H  N N 162 
GLU   HB2  H  N N 163 
GLU   HB3  H  N N 164 
GLU   HG2  H  N N 165 
GLU   HG3  H  N N 166 
GLU   HE2  H  N N 167 
GLU   HXT  H  N N 168 
GLY   N    N  N N 169 
GLY   CA   C  N N 170 
GLY   C    C  N N 171 
GLY   O    O  N N 172 
GLY   OXT  O  N N 173 
GLY   H    H  N N 174 
GLY   H2   H  N N 175 
GLY   HA2  H  N N 176 
GLY   HA3  H  N N 177 
GLY   HXT  H  N N 178 
HIS   N    N  N N 179 
HIS   CA   C  N S 180 
HIS   C    C  N N 181 
HIS   O    O  N N 182 
HIS   CB   C  N N 183 
HIS   CG   C  Y N 184 
HIS   ND1  N  Y N 185 
HIS   CD2  C  Y N 186 
HIS   CE1  C  Y N 187 
HIS   NE2  N  Y N 188 
HIS   OXT  O  N N 189 
HIS   H    H  N N 190 
HIS   H2   H  N N 191 
HIS   HA   H  N N 192 
HIS   HB2  H  N N 193 
HIS   HB3  H  N N 194 
HIS   HD1  H  N N 195 
HIS   HD2  H  N N 196 
HIS   HE1  H  N N 197 
HIS   HE2  H  N N 198 
HIS   HXT  H  N N 199 
HOH   O    O  N N 200 
HOH   H1   H  N N 201 
HOH   H2   H  N N 202 
ILE   N    N  N N 203 
ILE   CA   C  N S 204 
ILE   C    C  N N 205 
ILE   O    O  N N 206 
ILE   CB   C  N S 207 
ILE   CG1  C  N N 208 
ILE   CG2  C  N N 209 
ILE   CD1  C  N N 210 
ILE   OXT  O  N N 211 
ILE   H    H  N N 212 
ILE   H2   H  N N 213 
ILE   HA   H  N N 214 
ILE   HB   H  N N 215 
ILE   HG12 H  N N 216 
ILE   HG13 H  N N 217 
ILE   HG21 H  N N 218 
ILE   HG22 H  N N 219 
ILE   HG23 H  N N 220 
ILE   HD11 H  N N 221 
ILE   HD12 H  N N 222 
ILE   HD13 H  N N 223 
ILE   HXT  H  N N 224 
LEU   N    N  N N 225 
LEU   CA   C  N S 226 
LEU   C    C  N N 227 
LEU   O    O  N N 228 
LEU   CB   C  N N 229 
LEU   CG   C  N N 230 
LEU   CD1  C  N N 231 
LEU   CD2  C  N N 232 
LEU   OXT  O  N N 233 
LEU   H    H  N N 234 
LEU   H2   H  N N 235 
LEU   HA   H  N N 236 
LEU   HB2  H  N N 237 
LEU   HB3  H  N N 238 
LEU   HG   H  N N 239 
LEU   HD11 H  N N 240 
LEU   HD12 H  N N 241 
LEU   HD13 H  N N 242 
LEU   HD21 H  N N 243 
LEU   HD22 H  N N 244 
LEU   HD23 H  N N 245 
LEU   HXT  H  N N 246 
LYS   N    N  N N 247 
LYS   CA   C  N S 248 
LYS   C    C  N N 249 
LYS   O    O  N N 250 
LYS   CB   C  N N 251 
LYS   CG   C  N N 252 
LYS   CD   C  N N 253 
LYS   CE   C  N N 254 
LYS   NZ   N  N N 255 
LYS   OXT  O  N N 256 
LYS   H    H  N N 257 
LYS   H2   H  N N 258 
LYS   HA   H  N N 259 
LYS   HB2  H  N N 260 
LYS   HB3  H  N N 261 
LYS   HG2  H  N N 262 
LYS   HG3  H  N N 263 
LYS   HD2  H  N N 264 
LYS   HD3  H  N N 265 
LYS   HE2  H  N N 266 
LYS   HE3  H  N N 267 
LYS   HZ1  H  N N 268 
LYS   HZ2  H  N N 269 
LYS   HZ3  H  N N 270 
LYS   HXT  H  N N 271 
MET   N    N  N N 272 
MET   CA   C  N S 273 
MET   C    C  N N 274 
MET   O    O  N N 275 
MET   CB   C  N N 276 
MET   CG   C  N N 277 
MET   SD   S  N N 278 
MET   CE   C  N N 279 
MET   OXT  O  N N 280 
MET   H    H  N N 281 
MET   H2   H  N N 282 
MET   HA   H  N N 283 
MET   HB2  H  N N 284 
MET   HB3  H  N N 285 
MET   HG2  H  N N 286 
MET   HG3  H  N N 287 
MET   HE1  H  N N 288 
MET   HE2  H  N N 289 
MET   HE3  H  N N 290 
MET   HXT  H  N N 291 
PHE   N    N  N N 292 
PHE   CA   C  N S 293 
PHE   C    C  N N 294 
PHE   O    O  N N 295 
PHE   CB   C  N N 296 
PHE   CG   C  Y N 297 
PHE   CD1  C  Y N 298 
PHE   CD2  C  Y N 299 
PHE   CE1  C  Y N 300 
PHE   CE2  C  Y N 301 
PHE   CZ   C  Y N 302 
PHE   OXT  O  N N 303 
PHE   H    H  N N 304 
PHE   H2   H  N N 305 
PHE   HA   H  N N 306 
PHE   HB2  H  N N 307 
PHE   HB3  H  N N 308 
PHE   HD1  H  N N 309 
PHE   HD2  H  N N 310 
PHE   HE1  H  N N 311 
PHE   HE2  H  N N 312 
PHE   HZ   H  N N 313 
PHE   HXT  H  N N 314 
PRO   N    N  N N 315 
PRO   CA   C  N S 316 
PRO   C    C  N N 317 
PRO   O    O  N N 318 
PRO   CB   C  N N 319 
PRO   CG   C  N N 320 
PRO   CD   C  N N 321 
PRO   OXT  O  N N 322 
PRO   H    H  N N 323 
PRO   HA   H  N N 324 
PRO   HB2  H  N N 325 
PRO   HB3  H  N N 326 
PRO   HG2  H  N N 327 
PRO   HG3  H  N N 328 
PRO   HD2  H  N N 329 
PRO   HD3  H  N N 330 
PRO   HXT  H  N N 331 
SER   N    N  N N 332 
SER   CA   C  N S 333 
SER   C    C  N N 334 
SER   O    O  N N 335 
SER   CB   C  N N 336 
SER   OG   O  N N 337 
SER   OXT  O  N N 338 
SER   H    H  N N 339 
SER   H2   H  N N 340 
SER   HA   H  N N 341 
SER   HB2  H  N N 342 
SER   HB3  H  N N 343 
SER   HG   H  N N 344 
SER   HXT  H  N N 345 
THR   N    N  N N 346 
THR   CA   C  N S 347 
THR   C    C  N N 348 
THR   O    O  N N 349 
THR   CB   C  N R 350 
THR   OG1  O  N N 351 
THR   CG2  C  N N 352 
THR   OXT  O  N N 353 
THR   H    H  N N 354 
THR   H2   H  N N 355 
THR   HA   H  N N 356 
THR   HB   H  N N 357 
THR   HG1  H  N N 358 
THR   HG21 H  N N 359 
THR   HG22 H  N N 360 
THR   HG23 H  N N 361 
THR   HXT  H  N N 362 
TRP   N    N  N N 363 
TRP   CA   C  N S 364 
TRP   C    C  N N 365 
TRP   O    O  N N 366 
TRP   CB   C  N N 367 
TRP   CG   C  Y N 368 
TRP   CD1  C  Y N 369 
TRP   CD2  C  Y N 370 
TRP   NE1  N  Y N 371 
TRP   CE2  C  Y N 372 
TRP   CE3  C  Y N 373 
TRP   CZ2  C  Y N 374 
TRP   CZ3  C  Y N 375 
TRP   CH2  C  Y N 376 
TRP   OXT  O  N N 377 
TRP   H    H  N N 378 
TRP   H2   H  N N 379 
TRP   HA   H  N N 380 
TRP   HB2  H  N N 381 
TRP   HB3  H  N N 382 
TRP   HD1  H  N N 383 
TRP   HE1  H  N N 384 
TRP   HE3  H  N N 385 
TRP   HZ2  H  N N 386 
TRP   HZ3  H  N N 387 
TRP   HH2  H  N N 388 
TRP   HXT  H  N N 389 
TYR   N    N  N N 390 
TYR   CA   C  N S 391 
TYR   C    C  N N 392 
TYR   O    O  N N 393 
TYR   CB   C  N N 394 
TYR   CG   C  Y N 395 
TYR   CD1  C  Y N 396 
TYR   CD2  C  Y N 397 
TYR   CE1  C  Y N 398 
TYR   CE2  C  Y N 399 
TYR   CZ   C  Y N 400 
TYR   OH   O  N N 401 
TYR   OXT  O  N N 402 
TYR   H    H  N N 403 
TYR   H2   H  N N 404 
TYR   HA   H  N N 405 
TYR   HB2  H  N N 406 
TYR   HB3  H  N N 407 
TYR   HD1  H  N N 408 
TYR   HD2  H  N N 409 
TYR   HE1  H  N N 410 
TYR   HE2  H  N N 411 
TYR   HH   H  N N 412 
TYR   HXT  H  N N 413 
VAL   N    N  N N 414 
VAL   CA   C  N S 415 
VAL   C    C  N N 416 
VAL   O    O  N N 417 
VAL   CB   C  N N 418 
VAL   CG1  C  N N 419 
VAL   CG2  C  N N 420 
VAL   OXT  O  N N 421 
VAL   H    H  N N 422 
VAL   H2   H  N N 423 
VAL   HA   H  N N 424 
VAL   HB   H  N N 425 
VAL   HG11 H  N N 426 
VAL   HG12 H  N N 427 
VAL   HG13 H  N N 428 
VAL   HG21 H  N N 429 
VAL   HG22 H  N N 430 
VAL   HG23 H  N N 431 
VAL   HXT  H  N N 432 
ZN    ZN   ZN N N 433 
# 
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 
A1BN5 C   C1   sing N N 1   
A1BN5 C1  C2   doub Y N 2   
A1BN5 C2  C3   sing Y N 3   
A1BN5 C3  C4   doub Y N 4   
A1BN5 C4  C5   sing Y N 5   
A1BN5 C5  C6   doub Y N 6   
A1BN5 C1  C6   sing Y N 7   
A1BN5 C6  N    sing N N 8   
A1BN5 N   C7   sing N N 9   
A1BN5 O   C7   doub N N 10  
A1BN5 C7  C8   sing N N 11  
A1BN5 C8  C9   doub Y N 12  
A1BN5 C9  N1   sing Y N 13  
A1BN5 N1  C10  doub Y N 14  
A1BN5 C10 C11  sing Y N 15  
A1BN5 C11 C12  sing N N 16  
A1BN5 N2  C12  sing N N 17  
A1BN5 C12 O1   doub N N 18  
A1BN5 C13 C11  doub Y N 19  
A1BN5 C8  C13  sing Y N 20  
A1BN5 C4  H5   sing N N 21  
A1BN5 C5  H6   sing N N 22  
A1BN5 C10 H9   sing N N 23  
A1BN5 C13 H12  sing N N 24  
A1BN5 N2  H11  sing N N 25  
A1BN5 N2  H10  sing N N 26  
A1BN5 C9  H8   sing N N 27  
A1BN5 N   H7   sing N N 28  
A1BN5 C   H1   sing N N 29  
A1BN5 C   H2   sing N N 30  
A1BN5 C   H    sing N N 31  
A1BN5 C3  H4   sing N N 32  
A1BN5 C2  H3   sing N N 33  
ALA   N   CA   sing N N 34  
ALA   N   H    sing N N 35  
ALA   N   H2   sing N N 36  
ALA   CA  C    sing N N 37  
ALA   CA  CB   sing N N 38  
ALA   CA  HA   sing N N 39  
ALA   C   O    doub N N 40  
ALA   C   OXT  sing N N 41  
ALA   CB  HB1  sing N N 42  
ALA   CB  HB2  sing N N 43  
ALA   CB  HB3  sing N N 44  
ALA   OXT HXT  sing N N 45  
ARG   N   CA   sing N N 46  
ARG   N   H    sing N N 47  
ARG   N   H2   sing N N 48  
ARG   CA  C    sing N N 49  
ARG   CA  CB   sing N N 50  
ARG   CA  HA   sing N N 51  
ARG   C   O    doub N N 52  
ARG   C   OXT  sing N N 53  
ARG   CB  CG   sing N N 54  
ARG   CB  HB2  sing N N 55  
ARG   CB  HB3  sing N N 56  
ARG   CG  CD   sing N N 57  
ARG   CG  HG2  sing N N 58  
ARG   CG  HG3  sing N N 59  
ARG   CD  NE   sing N N 60  
ARG   CD  HD2  sing N N 61  
ARG   CD  HD3  sing N N 62  
ARG   NE  CZ   sing N N 63  
ARG   NE  HE   sing N N 64  
ARG   CZ  NH1  sing N N 65  
ARG   CZ  NH2  doub N N 66  
ARG   NH1 HH11 sing N N 67  
ARG   NH1 HH12 sing N N 68  
ARG   NH2 HH21 sing N N 69  
ARG   NH2 HH22 sing N N 70  
ARG   OXT HXT  sing N N 71  
ASN   N   CA   sing N N 72  
ASN   N   H    sing N N 73  
ASN   N   H2   sing N N 74  
ASN   CA  C    sing N N 75  
ASN   CA  CB   sing N N 76  
ASN   CA  HA   sing N N 77  
ASN   C   O    doub N N 78  
ASN   C   OXT  sing N N 79  
ASN   CB  CG   sing N N 80  
ASN   CB  HB2  sing N N 81  
ASN   CB  HB3  sing N N 82  
ASN   CG  OD1  doub N N 83  
ASN   CG  ND2  sing N N 84  
ASN   ND2 HD21 sing N N 85  
ASN   ND2 HD22 sing N N 86  
ASN   OXT HXT  sing N N 87  
ASP   N   CA   sing N N 88  
ASP   N   H    sing N N 89  
ASP   N   H2   sing N N 90  
ASP   CA  C    sing N N 91  
ASP   CA  CB   sing N N 92  
ASP   CA  HA   sing N N 93  
ASP   C   O    doub N N 94  
ASP   C   OXT  sing N N 95  
ASP   CB  CG   sing N N 96  
ASP   CB  HB2  sing N N 97  
ASP   CB  HB3  sing N N 98  
ASP   CG  OD1  doub N N 99  
ASP   CG  OD2  sing N N 100 
ASP   OD2 HD2  sing N N 101 
ASP   OXT HXT  sing N N 102 
CYS   N   CA   sing N N 103 
CYS   N   H    sing N N 104 
CYS   N   H2   sing N N 105 
CYS   CA  C    sing N N 106 
CYS   CA  CB   sing N N 107 
CYS   CA  HA   sing N N 108 
CYS   C   O    doub N N 109 
CYS   C   OXT  sing N N 110 
CYS   CB  SG   sing N N 111 
CYS   CB  HB2  sing N N 112 
CYS   CB  HB3  sing N N 113 
CYS   SG  HG   sing N N 114 
CYS   OXT HXT  sing N N 115 
DMS   S   O    doub N N 116 
DMS   S   C1   sing N N 117 
DMS   S   C2   sing N N 118 
DMS   C1  H11  sing N N 119 
DMS   C1  H12  sing N N 120 
DMS   C1  H13  sing N N 121 
DMS   C2  H21  sing N N 122 
DMS   C2  H22  sing N N 123 
DMS   C2  H23  sing N N 124 
GLN   N   CA   sing N N 125 
GLN   N   H    sing N N 126 
GLN   N   H2   sing N N 127 
GLN   CA  C    sing N N 128 
GLN   CA  CB   sing N N 129 
GLN   CA  HA   sing N N 130 
GLN   C   O    doub N N 131 
GLN   C   OXT  sing N N 132 
GLN   CB  CG   sing N N 133 
GLN   CB  HB2  sing N N 134 
GLN   CB  HB3  sing N N 135 
GLN   CG  CD   sing N N 136 
GLN   CG  HG2  sing N N 137 
GLN   CG  HG3  sing N N 138 
GLN   CD  OE1  doub N N 139 
GLN   CD  NE2  sing N N 140 
GLN   NE2 HE21 sing N N 141 
GLN   NE2 HE22 sing N N 142 
GLN   OXT HXT  sing N N 143 
GLU   N   CA   sing N N 144 
GLU   N   H    sing N N 145 
GLU   N   H2   sing N N 146 
GLU   CA  C    sing N N 147 
GLU   CA  CB   sing N N 148 
GLU   CA  HA   sing N N 149 
GLU   C   O    doub N N 150 
GLU   C   OXT  sing N N 151 
GLU   CB  CG   sing N N 152 
GLU   CB  HB2  sing N N 153 
GLU   CB  HB3  sing N N 154 
GLU   CG  CD   sing N N 155 
GLU   CG  HG2  sing N N 156 
GLU   CG  HG3  sing N N 157 
GLU   CD  OE1  doub N N 158 
GLU   CD  OE2  sing N N 159 
GLU   OE2 HE2  sing N N 160 
GLU   OXT HXT  sing N N 161 
GLY   N   CA   sing N N 162 
GLY   N   H    sing N N 163 
GLY   N   H2   sing N N 164 
GLY   CA  C    sing N N 165 
GLY   CA  HA2  sing N N 166 
GLY   CA  HA3  sing N N 167 
GLY   C   O    doub N N 168 
GLY   C   OXT  sing N N 169 
GLY   OXT HXT  sing N N 170 
HIS   N   CA   sing N N 171 
HIS   N   H    sing N N 172 
HIS   N   H2   sing N N 173 
HIS   CA  C    sing N N 174 
HIS   CA  CB   sing N N 175 
HIS   CA  HA   sing N N 176 
HIS   C   O    doub N N 177 
HIS   C   OXT  sing N N 178 
HIS   CB  CG   sing N N 179 
HIS   CB  HB2  sing N N 180 
HIS   CB  HB3  sing N N 181 
HIS   CG  ND1  sing Y N 182 
HIS   CG  CD2  doub Y N 183 
HIS   ND1 CE1  doub Y N 184 
HIS   ND1 HD1  sing N N 185 
HIS   CD2 NE2  sing Y N 186 
HIS   CD2 HD2  sing N N 187 
HIS   CE1 NE2  sing Y N 188 
HIS   CE1 HE1  sing N N 189 
HIS   NE2 HE2  sing N N 190 
HIS   OXT HXT  sing N N 191 
HOH   O   H1   sing N N 192 
HOH   O   H2   sing N N 193 
ILE   N   CA   sing N N 194 
ILE   N   H    sing N N 195 
ILE   N   H2   sing N N 196 
ILE   CA  C    sing N N 197 
ILE   CA  CB   sing N N 198 
ILE   CA  HA   sing N N 199 
ILE   C   O    doub N N 200 
ILE   C   OXT  sing N N 201 
ILE   CB  CG1  sing N N 202 
ILE   CB  CG2  sing N N 203 
ILE   CB  HB   sing N N 204 
ILE   CG1 CD1  sing N N 205 
ILE   CG1 HG12 sing N N 206 
ILE   CG1 HG13 sing N N 207 
ILE   CG2 HG21 sing N N 208 
ILE   CG2 HG22 sing N N 209 
ILE   CG2 HG23 sing N N 210 
ILE   CD1 HD11 sing N N 211 
ILE   CD1 HD12 sing N N 212 
ILE   CD1 HD13 sing N N 213 
ILE   OXT HXT  sing N N 214 
LEU   N   CA   sing N N 215 
LEU   N   H    sing N N 216 
LEU   N   H2   sing N N 217 
LEU   CA  C    sing N N 218 
LEU   CA  CB   sing N N 219 
LEU   CA  HA   sing N N 220 
LEU   C   O    doub N N 221 
LEU   C   OXT  sing N N 222 
LEU   CB  CG   sing N N 223 
LEU   CB  HB2  sing N N 224 
LEU   CB  HB3  sing N N 225 
LEU   CG  CD1  sing N N 226 
LEU   CG  CD2  sing N N 227 
LEU   CG  HG   sing N N 228 
LEU   CD1 HD11 sing N N 229 
LEU   CD1 HD12 sing N N 230 
LEU   CD1 HD13 sing N N 231 
LEU   CD2 HD21 sing N N 232 
LEU   CD2 HD22 sing N N 233 
LEU   CD2 HD23 sing N N 234 
LEU   OXT HXT  sing N N 235 
LYS   N   CA   sing N N 236 
LYS   N   H    sing N N 237 
LYS   N   H2   sing N N 238 
LYS   CA  C    sing N N 239 
LYS   CA  CB   sing N N 240 
LYS   CA  HA   sing N N 241 
LYS   C   O    doub N N 242 
LYS   C   OXT  sing N N 243 
LYS   CB  CG   sing N N 244 
LYS   CB  HB2  sing N N 245 
LYS   CB  HB3  sing N N 246 
LYS   CG  CD   sing N N 247 
LYS   CG  HG2  sing N N 248 
LYS   CG  HG3  sing N N 249 
LYS   CD  CE   sing N N 250 
LYS   CD  HD2  sing N N 251 
LYS   CD  HD3  sing N N 252 
LYS   CE  NZ   sing N N 253 
LYS   CE  HE2  sing N N 254 
LYS   CE  HE3  sing N N 255 
LYS   NZ  HZ1  sing N N 256 
LYS   NZ  HZ2  sing N N 257 
LYS   NZ  HZ3  sing N N 258 
LYS   OXT HXT  sing N N 259 
MET   N   CA   sing N N 260 
MET   N   H    sing N N 261 
MET   N   H2   sing N N 262 
MET   CA  C    sing N N 263 
MET   CA  CB   sing N N 264 
MET   CA  HA   sing N N 265 
MET   C   O    doub N N 266 
MET   C   OXT  sing N N 267 
MET   CB  CG   sing N N 268 
MET   CB  HB2  sing N N 269 
MET   CB  HB3  sing N N 270 
MET   CG  SD   sing N N 271 
MET   CG  HG2  sing N N 272 
MET   CG  HG3  sing N N 273 
MET   SD  CE   sing N N 274 
MET   CE  HE1  sing N N 275 
MET   CE  HE2  sing N N 276 
MET   CE  HE3  sing N N 277 
MET   OXT HXT  sing N N 278 
PHE   N   CA   sing N N 279 
PHE   N   H    sing N N 280 
PHE   N   H2   sing N N 281 
PHE   CA  C    sing N N 282 
PHE   CA  CB   sing N N 283 
PHE   CA  HA   sing N N 284 
PHE   C   O    doub N N 285 
PHE   C   OXT  sing N N 286 
PHE   CB  CG   sing N N 287 
PHE   CB  HB2  sing N N 288 
PHE   CB  HB3  sing N N 289 
PHE   CG  CD1  doub Y N 290 
PHE   CG  CD2  sing Y N 291 
PHE   CD1 CE1  sing Y N 292 
PHE   CD1 HD1  sing N N 293 
PHE   CD2 CE2  doub Y N 294 
PHE   CD2 HD2  sing N N 295 
PHE   CE1 CZ   doub Y N 296 
PHE   CE1 HE1  sing N N 297 
PHE   CE2 CZ   sing Y N 298 
PHE   CE2 HE2  sing N N 299 
PHE   CZ  HZ   sing N N 300 
PHE   OXT HXT  sing N N 301 
PRO   N   CA   sing N N 302 
PRO   N   CD   sing N N 303 
PRO   N   H    sing N N 304 
PRO   CA  C    sing N N 305 
PRO   CA  CB   sing N N 306 
PRO   CA  HA   sing N N 307 
PRO   C   O    doub N N 308 
PRO   C   OXT  sing N N 309 
PRO   CB  CG   sing N N 310 
PRO   CB  HB2  sing N N 311 
PRO   CB  HB3  sing N N 312 
PRO   CG  CD   sing N N 313 
PRO   CG  HG2  sing N N 314 
PRO   CG  HG3  sing N N 315 
PRO   CD  HD2  sing N N 316 
PRO   CD  HD3  sing N N 317 
PRO   OXT HXT  sing N N 318 
SER   N   CA   sing N N 319 
SER   N   H    sing N N 320 
SER   N   H2   sing N N 321 
SER   CA  C    sing N N 322 
SER   CA  CB   sing N N 323 
SER   CA  HA   sing N N 324 
SER   C   O    doub N N 325 
SER   C   OXT  sing N N 326 
SER   CB  OG   sing N N 327 
SER   CB  HB2  sing N N 328 
SER   CB  HB3  sing N N 329 
SER   OG  HG   sing N N 330 
SER   OXT HXT  sing N N 331 
THR   N   CA   sing N N 332 
THR   N   H    sing N N 333 
THR   N   H2   sing N N 334 
THR   CA  C    sing N N 335 
THR   CA  CB   sing N N 336 
THR   CA  HA   sing N N 337 
THR   C   O    doub N N 338 
THR   C   OXT  sing N N 339 
THR   CB  OG1  sing N N 340 
THR   CB  CG2  sing N N 341 
THR   CB  HB   sing N N 342 
THR   OG1 HG1  sing N N 343 
THR   CG2 HG21 sing N N 344 
THR   CG2 HG22 sing N N 345 
THR   CG2 HG23 sing N N 346 
THR   OXT HXT  sing N N 347 
TRP   N   CA   sing N N 348 
TRP   N   H    sing N N 349 
TRP   N   H2   sing N N 350 
TRP   CA  C    sing N N 351 
TRP   CA  CB   sing N N 352 
TRP   CA  HA   sing N N 353 
TRP   C   O    doub N N 354 
TRP   C   OXT  sing N N 355 
TRP   CB  CG   sing N N 356 
TRP   CB  HB2  sing N N 357 
TRP   CB  HB3  sing N N 358 
TRP   CG  CD1  doub Y N 359 
TRP   CG  CD2  sing Y N 360 
TRP   CD1 NE1  sing Y N 361 
TRP   CD1 HD1  sing N N 362 
TRP   CD2 CE2  doub Y N 363 
TRP   CD2 CE3  sing Y N 364 
TRP   NE1 CE2  sing Y N 365 
TRP   NE1 HE1  sing N N 366 
TRP   CE2 CZ2  sing Y N 367 
TRP   CE3 CZ3  doub Y N 368 
TRP   CE3 HE3  sing N N 369 
TRP   CZ2 CH2  doub Y N 370 
TRP   CZ2 HZ2  sing N N 371 
TRP   CZ3 CH2  sing Y N 372 
TRP   CZ3 HZ3  sing N N 373 
TRP   CH2 HH2  sing N N 374 
TRP   OXT HXT  sing N N 375 
TYR   N   CA   sing N N 376 
TYR   N   H    sing N N 377 
TYR   N   H2   sing N N 378 
TYR   CA  C    sing N N 379 
TYR   CA  CB   sing N N 380 
TYR   CA  HA   sing N N 381 
TYR   C   O    doub N N 382 
TYR   C   OXT  sing N N 383 
TYR   CB  CG   sing N N 384 
TYR   CB  HB2  sing N N 385 
TYR   CB  HB3  sing N N 386 
TYR   CG  CD1  doub Y N 387 
TYR   CG  CD2  sing Y N 388 
TYR   CD1 CE1  sing Y N 389 
TYR   CD1 HD1  sing N N 390 
TYR   CD2 CE2  doub Y N 391 
TYR   CD2 HD2  sing N N 392 
TYR   CE1 CZ   doub Y N 393 
TYR   CE1 HE1  sing N N 394 
TYR   CE2 CZ   sing Y N 395 
TYR   CE2 HE2  sing N N 396 
TYR   CZ  OH   sing N N 397 
TYR   OH  HH   sing N N 398 
TYR   OXT HXT  sing N N 399 
VAL   N   CA   sing N N 400 
VAL   N   H    sing N N 401 
VAL   N   H2   sing N N 402 
VAL   CA  C    sing N N 403 
VAL   CA  CB   sing N N 404 
VAL   CA  HA   sing N N 405 
VAL   C   O    doub N N 406 
VAL   C   OXT  sing N N 407 
VAL   CB  CG1  sing N N 408 
VAL   CB  CG2  sing N N 409 
VAL   CB  HB   sing N N 410 
VAL   CG1 HG11 sing N N 411 
VAL   CG1 HG12 sing N N 412 
VAL   CG1 HG13 sing N N 413 
VAL   CG2 HG21 sing N N 414 
VAL   CG2 HG22 sing N N 415 
VAL   CG2 HG23 sing N N 416 
VAL   OXT HXT  sing N N 417 
# 
_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                    7HVM 
_atom_sites.fract_transf_matrix[1][1]   0.013571 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000818 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016500 
_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]   0.030652 
_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   ? 18.991 6.145   24.387 1.00 22.81 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.166 6.235   23.511 1.00 23.24 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.227 5.112   22.481 1.00 23.46 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.515 4.100   22.627 1.00 24.94 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.459 6.286   24.333 1.00 26.97 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.575 5.159   25.179 1.00 32.32 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.021 5.308   21.420 1.00 21.58 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.213 4.280   20.412 1.00 20.86 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.533 4.830   19.032 1.00 19.66 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.190 5.971   18.704 1.00 20.82 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.188 4.032   18.207 1.00 17.58 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.561 4.468   16.862 1.00 18.16 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.515 3.324   15.863 1.00 17.71 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.539 2.134   16.272 1.00 19.13 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.979 5.088   16.880 1.00 18.88 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.504 3.668   14.563 1.00 16.39 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.620 2.695   13.475 1.00 17.54 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.012 2.819   12.884 1.00 18.54 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.474 3.927   12.555 1.00 19.41 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.565 2.910   12.370 1.00 17.22 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.135 3.007   12.913 1.00 17.58 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.686 1.818   11.282 1.00 18.30 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.200 3.628   11.885 1.00 17.62 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.688 1.680   12.661 1.00 20.21 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.007 1.695   12.084 1.00 20.80 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.978 0.975   10.736 1.00 22.20 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.900 -0.249  10.702 1.00 23.70 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.043 1.062   13.047 1.00 21.05 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.207 1.862   14.322 1.00 21.53 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.056 2.960   14.371 1.00 21.96 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.447 1.580   15.444 1.00 22.91 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.149 3.752   15.515 1.00 22.36 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.505 2.386   16.584 1.00 23.71 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.368 3.464   16.619 1.00 23.39 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.466 4.214   17.772 1.00 23.60 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.008 1.728   9.644  1.00 21.69 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.963 1.121   8.301  1.00 23.79 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.091 1.680   7.474  1.00 25.16 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.277 2.901   7.405  1.00 25.30 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.557 1.340   7.652  1.00 24.76 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.135 2.807   7.677  1.00 25.17 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.500 0.773   6.240  1.00 25.93 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 27.949 0.807   6.906  1.00 26.06 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.095 1.289   6.139  1.00 26.15 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 29.998 2.187   6.978  1.00 26.16 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.268 1.866   8.132  1.00 27.32 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.356 3.339   6.470  1.00 25.93 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.130 4.307   7.230  1.00 26.54 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.235 5.458   7.757  1.00 25.45 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.678 6.595   7.856  1.00 25.45 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.282 4.830   6.418  1.00 27.63 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.405 3.806   6.331  1.00 35.29 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.310 3.764   7.176  1.00 38.59 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.330 2.934   5.345  1.00 35.50 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.001 5.127   8.129  1.00 24.20 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.066 6.106   8.638  1.00 21.93 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.556 5.688   9.996  1.00 21.19 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.360 4.491   10.276 1.00 21.80 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.837 6.235   7.694  1.00 22.51 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.186 6.781   6.328  1.00 24.91 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.822 8.007   6.190  1.00 27.60 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.892 6.065   5.175  1.00 26.91 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.177 8.502   4.939  1.00 29.99 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.178 6.583   3.915  1.00 28.52 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.854 7.781   3.804  1.00 30.91 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.202 8.291   2.580  1.00 34.44 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.243 6.714   10.821 1.00 18.83 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.587 6.543   12.109 1.00 18.27 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.296 7.390   12.037 1.00 16.93 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.373 8.602   11.843 1.00 17.41 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.486 7.027   13.279 1.00 19.38 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.776 7.233   14.633 1.00 19.87 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.772 7.472   15.778 1.00 19.63 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.317 8.499   16.718 1.00 19.70 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.818 8.290   17.932 1.00 21.48 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.583 7.053   18.360 1.00 20.78 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.485 9.314   18.702 1.00 21.66 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.124 6.760   12.271 1.00 16.21 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.847 7.505   12.263 1.00 15.21 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.389 7.598   13.689 1.00 16.50 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.185 6.546   14.338 1.00 17.60 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.798 6.747   11.420 1.00 16.54 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.518 7.587   11.251 1.00 16.92 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.355 6.360   10.057 1.00 17.50 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.078 8.801   14.140 1.00 15.08 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.646 9.040   15.528 1.00 15.43 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.468 10.032  15.515 1.00 15.74 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.241 10.754  14.529 1.00 16.04 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.804 9.632   16.383 1.00 17.87 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.886 8.603   16.607 1.00 20.73 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.369 10.943  15.772 1.00 18.45 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.740 10.099  16.633 1.00 13.75 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.737 11.162  16.789 1.00 13.27 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.493 12.490  16.773 1.00 13.82 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.499 12.651  17.490 1.00 14.67 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 18.033 11.047  18.149 1.00 14.20 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.127 9.845   18.235 1.00 14.16 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.541 8.779   18.670 1.00 14.65 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.879 9.990   17.817 1.00 14.58 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 19.020 13.428  15.970 1.00 13.84 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.715 14.728  15.839 1.00 14.08 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.880 15.411  17.210 1.00 15.05 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.951 15.973  17.492 1.00 15.81 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.943 15.640  14.862 1.00 13.12 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.721 16.905  14.439 1.00 13.60 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.740 17.750  13.615 1.00 15.54 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.347 18.972  13.054 1.00 16.58 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.500 20.099  13.729 1.00 17.41 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 19.163 20.167  15.009 1.00 19.78 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 20.057 21.164  13.144 1.00 19.10 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.859 15.303  18.091 1.00 14.88 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.933 15.956  19.412 1.00 16.57 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.880 15.284  20.407 1.00 18.00 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 20.185 15.895  21.461 1.00 19.35 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 17.548 16.153  20.049 1.00 17.58 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.880 14.901  20.530 1.00 17.95 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 16.173 14.068  19.674 1.00 18.41 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.819 14.399  21.782 1.00 18.88 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.668 13.103  20.443 1.00 17.93 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 16.026 13.268  21.723 1.00 19.53 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 20.351 14.101  20.064 1.00 16.32 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 21.308 13.353  20.856 1.00 16.74 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.722 13.342  20.226 1.00 16.75 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.641 12.715  20.773 1.00 19.66 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.795 11.929  21.146 1.00 17.62 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.443 11.875  21.860 1.00 19.66 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 19.010 10.429  22.069 1.00 20.02 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.491 12.614  23.228 1.00 20.07 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.917 14.065  19.085 1.00 15.74 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 24.241 14.074  18.455 1.00 17.13 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 25.308 14.700  19.364 1.00 16.86 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 25.065 15.662  20.051 1.00 17.92 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 24.156 14.844  17.148 1.00 18.63 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.477 14.095  19.372 1.00 17.27 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.615 14.565  20.171 1.00 18.39 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.452 15.638  19.420 1.00 19.04 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 28.234 15.876  18.242 1.00 19.39 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.517 13.373  20.523 1.00 19.70 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 29.150 12.956  19.306 1.00 20.99 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.741 12.223  21.166 1.00 20.53 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.479 16.236  20.101 1.00 19.42 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 30.384 17.162  19.423 1.00 19.73 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 31.110 16.438  18.288 1.00 19.58 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 31.253 17.012  17.213 1.00 20.26 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.448 17.697  20.399 1.00 23.09 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.910 18.381  21.607 1.00 31.29 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 29.922 19.336  21.511 1.00 35.08 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 31.300 18.285  22.905 1.00 34.21 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 29.698 19.759  22.747 1.00 36.04 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 30.513 19.168  23.620 1.00 35.79 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.480 15.146  18.485 1.00 18.96 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 32.158 14.412  17.413 1.00 20.57 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.258 14.195  16.224 1.00 19.30 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.695 14.283  15.071 1.00 19.61 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.712 13.080  17.901 1.00 22.76 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.481 12.296  16.829 1.00 31.94 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.621 12.640  16.478 1.00 34.50 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 32.893 11.218  16.291 1.00 33.90 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.951 13.919  16.487 1.00 18.17 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 29.004 13.760  15.381 1.00 17.96 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.952 15.046  14.530 1.00 17.86 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 29.011 14.967  13.296 1.00 19.00 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.586 13.463  15.890 1.00 16.75 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.428 12.065  16.425 1.00 19.52 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 28.001 11.129  15.821 1.00 19.98 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.751 11.904  17.450 1.00 18.59 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.816 16.217  15.198 1.00 17.92 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.755 17.501  14.484 1.00 17.47 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 30.102 17.847  13.775 1.00 18.65 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 30.085 18.418  12.679 1.00 19.53 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.317 18.630  15.437 1.00 18.05 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.832 18.706  15.624 1.00 17.62 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 26.104 18.265  16.698 1.00 18.88 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.892 19.217  14.677 1.00 16.55 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.752 18.501  16.481 1.00 17.87 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.598 19.048  15.228 1.00 17.12 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 26.015 19.811  13.416 1.00 17.73 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.438 19.500  14.570 1.00 16.82 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.857 20.234  12.750 1.00 18.23 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.598 20.076  13.327 1.00 17.00 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.233 17.429  14.364 1.00 19.20 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.546 17.670  13.751 1.00 21.46 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.804 16.774  12.534 1.00 22.83 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.689 17.077  11.723 1.00 24.40 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.650 17.455  14.783 1.00 21.48 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 32.051 15.652  12.402 1.00 21.10 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.198 14.740  11.252 1.00 19.62 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.824 14.621  10.531 1.00 19.52 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.437 13.554  10.104 1.00 20.15 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.688 13.368  11.729 1.00 20.43 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 34.094 13.487  12.270 1.00 24.31 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 35.040 13.555  11.501 1.00 25.64 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.212 13.600  13.592 1.00 24.46 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 30.109 15.745  10.438 1.00 19.45 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.772 15.772  9.856  1.00 18.90 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.733 15.382  8.388  1.00 21.47 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.487 15.931  7.582  1.00 23.90 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.222 17.202  10.004 1.00 18.89 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.810 17.454  9.484  1.00 19.39 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.772 16.667  10.332 1.00 20.35 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.520 18.964  9.480  1.00 20.03 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.824 14.474  8.017  1.00 20.29 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.569 14.088  6.640  1.00 21.73 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.238 14.733  6.167  1.00 21.58 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.160 15.316  5.076  1.00 24.16 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.504 12.549  6.493  1.00 23.36 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 27.018 12.150  5.098  1.00 25.45 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.875 11.924  6.810  1.00 24.49 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.190 14.620  6.992  1.00 19.88 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.862 15.075  6.633  1.00 18.30 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 23.032 15.221  7.908  1.00 17.77 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.221 14.463  8.850  1.00 18.26 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.211 14.079  5.663  1.00 18.91 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.755 14.321  5.362  1.00 19.30 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.239 15.058  4.335  1.00 21.50 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.639 13.724  6.029  1.00 18.95 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.860 14.993  4.358  1.00 21.38 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.468 14.182  5.395  1.00 19.75 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.510 12.836  7.099  1.00 18.65 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.194 13.764  5.786  1.00 19.55 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.243 12.482  7.518  1.00 18.99 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.108 12.901  6.826  1.00 18.93 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.145 16.213  7.963  1.00 17.02 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.211 16.353  9.073  1.00 17.28 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.924 17.008  8.579  1.00 16.87 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.952 17.850  7.657  1.00 17.31 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.812 17.081  10.285 1.00 16.60 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.364 18.490  10.008 1.00 18.51 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.363 19.622  9.917  1.00 19.68 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.668 20.657  9.276  1.00 23.72 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.295 19.507  10.527 1.00 19.39 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.806 16.643  9.201  1.00 16.97 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.520 17.247  8.860  1.00 17.72 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.767 17.554  10.131 1.00 17.92 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.292 16.619  10.808 1.00 16.87 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.694 16.375  7.900  1.00 17.62 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.488 17.065  7.302  1.00 20.94 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.977 18.022  7.921  1.00 24.81 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.051 16.660  6.197  1.00 22.08 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.672 18.874  10.449 1.00 18.24 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 16.008 19.298  11.674 0.50 20.68 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 16.004 19.375  11.649 0.50 19.35 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.500 19.073  11.648 1.00 21.56 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.869 19.145  12.710 1.00 24.72 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 16.315 20.754  12.005 0.50 24.20 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 16.249 20.880  11.822 0.50 18.62 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 15.762 21.035  13.280 0.50 29.48 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 15.755 21.664  10.747 0.50 16.97 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.916 18.763  10.479 1.00 18.30 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.504 18.430  10.446 1.00 18.25 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 12.265 16.946  10.716 1.00 17.68 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 11.126 16.569  10.948 1.00 19.72 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.887 18.799  9.105  1.00 20.91 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 12.343 17.986  8.042  1.00 27.32 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.331 16.111  10.762 1.00 16.30 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 13.187 14.657  10.925 1.00 15.62 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.823 14.132  12.190 1.00 15.54 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.746 12.930  12.414 1.00 15.03 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.904 13.941  9.759  1.00 17.29 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.235 14.219  8.413  1.00 18.97 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 14.012 13.547  7.278  1.00 17.69 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 13.952 12.077  7.336  1.00 17.56 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.091 11.283  6.285  1.00 17.49 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.197 11.798  5.058  1.00 18.34 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 13.973 9.967   6.421  1.00 18.02 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.535 14.953  12.959 1.00 15.50 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 15.257 14.486  14.143 1.00 14.90 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.326 13.453  13.795 1.00 13.89 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.613 12.562  14.621 1.00 13.85 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.325 13.941  15.277 1.00 14.57 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 15.056 13.645  16.594 1.00 14.99 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.959 14.435  16.977 1.00 17.26 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.744 12.608  17.247 1.00 16.11 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.963 13.585  12.605 1.00 14.40 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 18.056 12.695  12.214 1.00 14.17 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.334 13.445  11.925 1.00 14.41 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.316 14.536  11.369 1.00 14.91 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.715 11.925  10.919 1.00 14.85 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.673 10.842  11.052 1.00 15.63 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.470 10.166  9.672  1.00 17.54 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.119 9.776   12.063 1.00 15.76 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.463 12.801  12.256 1.00 13.71 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.803 13.305  11.895 1.00 14.14 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.657 12.081  11.557 1.00 15.25 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.527 11.018  12.201 1.00 15.77 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.423 14.075  13.067 1.00 14.16 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.838 14.681  12.834 1.00 15.08 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.987 16.018  13.576 1.00 16.73 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.965 13.737  13.275 1.00 17.19 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.499 12.220  10.526 1.00 15.34 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.427 11.175  10.125 1.00 15.73 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.848 11.746  10.137 1.00 16.31 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 26.111 12.832  9.593  1.00 17.28 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 24.074 10.647  8.717  1.00 15.92 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.073 9.588   8.259  1.00 17.26 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.641 10.112  8.667  1.00 17.48 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.729 11.053  10.823 1.00 16.26 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.154 11.383  10.892 1.00 16.42 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.991 10.270  10.263 1.00 18.14 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.527 9.139   10.053 1.00 19.36 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.569 11.645  12.340 1.00 17.67 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.425 10.501  13.167 1.00 18.47 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.264 10.600  9.943  1.00 19.64 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.150 9.608   9.350  1.00 22.54 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.936 8.857   10.432 1.00 24.57 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.194 9.381   11.526 1.00 25.47 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.067 10.278  8.334  1.00 23.87 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.855 11.271  8.973  1.00 27.33 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.333 7.631   10.120 1.00 26.08 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.064 6.796   11.068 1.00 27.59 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.322 6.236   10.392 1.00 30.10 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.315 6.019   9.170  1.00 29.69 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.183 5.606   11.518 1.00 28.51 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 31.969 4.734   10.415 1.00 30.29 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.814 6.042   12.034 1.00 27.20 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.329 5.900   11.198 1.00 32.28 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.510 5.251   10.641 1.00 35.14 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.274 3.745   10.581 1.00 36.69 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 36.680 3.117   9.599  1.00 38.18 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.814 5.686   11.325 1.00 37.76 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.616 5.868   12.734 1.00 39.18 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 38.373 6.958   10.719 1.00 39.26 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.609 3.151   11.599 1.00 36.67 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.345 1.711   11.582 1.00 37.68 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.151 1.391   10.687 1.00 38.35 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.178 2.151   10.645 1.00 37.59 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.096 1.185   12.995 1.00 38.33 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.223 0.276   9.966  1.00 38.74 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.145 -0.125  9.078  1.00 39.67 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.038 -0.798  9.877  1.00 39.07 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.291 -1.731  10.633 1.00 39.61 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.665 -1.078  7.987  1.00 43.54 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 32.617 -1.353  6.900  1.00 50.63 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 32.857 -0.546  5.641  1.00 58.36 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 33.912 0.084   5.451  1.00 61.06 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 31.885 -0.548  4.744  1.00 59.95 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.819 -0.306  9.728  1.00 37.28 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.669 -0.881  10.397 1.00 37.02 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 29.068 -2.002  9.577  1.00 37.36 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.310 -2.077  8.362  1.00 38.92 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.309 -2.891  10.234 1.00 36.13 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.743 -4.032  9.509  1.00 36.38 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.211 -4.095  9.546  1.00 33.41 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.676 -5.130  9.146  1.00 34.60 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.370 -5.378  9.906  1.00 39.57 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 29.433 -5.362  11.388 1.00 47.54 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.486 -3.008  9.950  1.00 29.70 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.009 -3.059  9.955  1.00 26.76 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.527 -2.929  8.483  1.00 24.08 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.273 -2.475  7.586  1.00 24.92 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.370 -1.949  10.861 1.00 28.91 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.592 -2.044  12.389 1.00 38.41 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.938 -3.144  12.872 1.00 41.75 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.447 -0.982  13.109 1.00 36.22 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.313 -3.389  8.212  1.00 21.24 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.751 -3.299  6.867  1.00 21.43 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.468 -2.485  6.988  1.00 19.53 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.681 -2.707  7.921  1.00 19.18 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.404 -4.698  6.352  1.00 24.64 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.648 -5.382  6.069  1.00 26.13 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.562 -4.658  5.052  1.00 26.05 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.305 -1.494  6.109  1.00 18.73 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.081 -0.683  6.120  1.00 17.46 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.015 -1.415  5.274  1.00 17.75 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.322 -1.870  4.145  1.00 18.65 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.323 0.733   5.544  1.00 17.35 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.480 1.460   6.255  1.00 18.51 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.034 1.587   5.622  1.00 17.69 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.219 1.643   7.758  1.00 19.51 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.783 -1.522  5.780  1.00 16.28 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.678 -2.146  5.018  1.00 16.42 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.324 -1.266  3.826  1.00 17.69 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.363 -0.030  3.927  1.00 17.04 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.449 -2.222  5.932  1.00 16.75 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 14.976 -1.907  2.689  1.00 17.50 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.550 -1.168  1.481  1.00 18.10 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.223 -1.852  1.140  1.00 18.06 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.182 -2.851  0.427  1.00 20.72 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.591 -1.267  0.359  1.00 18.72 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 16.983 -0.629  0.736  1.00 19.63 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 16.978 0.872   1.103  1.00 21.64 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.340 1.281   1.507  1.00 22.05 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.630 2.418   2.151  1.00 22.73 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.675 3.275   2.452  1.00 21.18 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 19.884 2.703   2.486  1.00 23.54 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.147 -1.278  1.635  1.00 18.03 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.842 -1.933  1.639  1.00 18.39 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.737  -0.993  2.076  1.00 19.23 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.008 0.118   2.524  1.00 19.00 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 10.899 -3.128  2.593  1.00 19.02 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 10.935 -2.657  4.360  1.00 17.72 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.466  -1.504  2.042  1.00 20.56 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.323  -0.770  2.561  1.00 21.08 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.643  -1.566  3.681  1.00 21.29 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.445  -1.384  3.899  1.00 22.22 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.306  -0.402  1.459  1.00 25.50 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.667  -1.563  0.768  1.00 33.08 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 6.004  -2.734  1.111  1.00 34.69 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.821  -1.324  -0.135 1.00 38.87 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.409  -2.346  4.493  1.00 18.64 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 6.811  -3.049  5.642  1.00 18.26 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.119  -2.059  6.580  1.00 18.79 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.563  -0.916  6.731  1.00 17.81 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 7.873  -3.810  6.441  1.00 18.41 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.544  -5.279  5.633  1.00 19.83 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.036  -2.536  7.201  1.00 17.10 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.327  -1.801  8.238  1.00 16.47 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.235  -2.668  9.499  1.00 15.61 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.442  -2.365  10.371 1.00 16.07 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 2.900  -1.371  7.839  1.00 18.15 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 2.925  -0.116  6.971  1.00 20.31 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.514  0.364   6.689  1.00 23.55 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 0.945  0.121   5.600  1.00 24.65 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 0.872  0.973   7.692  1.00 22.26 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.091  -3.734  9.641  1.00 15.13 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.212  -4.487  10.887 1.00 15.33 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 6.689  -4.707  11.115 1.00 14.96 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.494  -4.775  10.162 1.00 16.68 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.482  -5.843  10.873 1.00 18.00 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.072  -6.658  9.858  1.00 22.26 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 2.965  -5.704  10.583 1.00 18.54 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.052  -4.779  12.383 1.00 14.15 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.450  -4.951  12.777 1.00 14.04 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.564  -5.126  14.281 1.00 13.70 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.565  -5.374  14.958 1.00 14.70 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 9.791  -5.059  14.794 1.00 12.20 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.061 -5.219  16.221 1.00 12.45 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 10.967 -4.068  16.645 1.00 12.66 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 11.959 -3.797  15.965 1.00 13.81 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 10.783 -6.578  16.459 1.00 14.06 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.205 -6.738  17.930 1.00 15.43 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 9.838  -7.730  16.068 1.00 14.03 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 10.696 -3.460  17.811 1.00 12.20 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.592 -2.395  18.302 1.00 12.42 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.099 -2.658  19.680 1.00 13.47 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.451 -3.380  20.448 1.00 12.98 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 10.972 -0.978  18.259 1.00 12.35 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 9.997  -0.643  19.405 1.00 12.92 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.721  -1.185  19.436 1.00 13.97 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.367 0.212   20.451 1.00 12.87 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 7.837  -0.911  20.482 1.00 15.35 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.460  0.558   21.470 1.00 13.70 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.189  -0.016  21.478 1.00 15.26 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.267  0.288   22.478 1.00 16.64 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.265 -2.092  19.996 1.00 13.22 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 13.809 -2.228  21.324 1.00 13.15 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.374 -1.058  22.199 1.00 13.14 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.592 0.114   21.847 1.00 14.24 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.351 -2.367  21.320 1.00 13.42 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 15.894 -2.507  22.721 1.00 15.49 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 15.699 -3.678  23.450 1.00 16.45 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 16.672 -1.512  23.291 1.00 16.38 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.111 -3.783  24.777 1.00 17.74 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.140 -1.625  24.608 1.00 18.06 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 16.830 -2.756  25.352 1.00 18.53 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.278 -2.924  26.653 1.00 22.13 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 12.852 -1.380  23.394 1.00 13.25 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.368 -0.384  24.374 1.00 13.45 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.283 -0.456  25.633 1.00 14.49 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.092 -1.358  26.473 1.00 15.60 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 10.909 -0.679  24.722 1.00 14.62 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.228 0.384   26.025 1.00 16.48 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.217 0.516   25.787 1.00 14.63 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.144 0.430   26.906 1.00 16.26 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 14.435 0.579   28.258 1.00 16.49 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 14.896 -0.006  29.242 1.00 17.73 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.270 1.441   26.716 1.00 19.78 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 15.820 2.761   26.914 1.00 25.96 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.357 1.390   28.338 1.00 15.46 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 12.638 1.571   29.602 1.00 16.70 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 11.863 0.325   30.048 1.00 17.26 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 11.284 0.353   31.138 1.00 18.14 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 11.699 2.756   29.521 1.00 16.59 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 10.666 2.557   28.559 1.00 17.07 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 11.863 -0.733  29.264 1.00 16.57 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 11.281 -2.013  29.681 1.00 16.68 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 12.297 -3.156  29.528 1.00 17.99 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 11.965 -4.320  29.870 1.00 18.40 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.035 -2.350  28.849 1.00 17.12 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 8.902  -1.334  29.059 1.00 17.95 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.199  -1.651  30.360 1.00 20.49 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.055  -0.770  30.572 1.00 20.77 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.111  0.392   31.212 1.00 21.50 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.273  0.852   31.674 1.00 21.79 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.015  1.139   31.348 1.00 21.92 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 13.532 -2.887  29.017 1.00 17.76 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 14.530 -3.932  28.666 1.00 17.92 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 13.868 -5.037  27.846 1.00 18.73 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.059 -6.244  28.108 1.00 21.11 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 15.195 -4.532  29.934 1.00 19.70 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.139 -3.573  30.594 1.00 23.14 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 16.830 -4.207  31.804 1.00 26.77 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 17.585 -3.212  32.585 1.00 28.79 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 17.405 -3.005  33.892 1.00 29.92 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 16.455 -3.661  34.549 1.00 29.42 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.120 -2.079  34.534 1.00 29.78 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.038 -4.627  26.878 1.00 16.67 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.285 -5.609  26.078 1.00 17.36 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.154 -5.191  24.634 1.00 16.02 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.144 -4.015  24.327 1.00 15.44 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 10.842 -5.777  26.627 1.00 23.10 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 10.719 -6.710  27.841 1.00 29.80 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.263  -6.785  28.295 1.00 35.85 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.081  -7.669  29.513 1.00 41.57 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 9.968  -7.268  30.636 1.00 45.85 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 11.973 -6.165  23.750 1.00 15.39 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 11.612 -5.904  22.374 1.00 14.53 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.108 -6.177  22.204 1.00 15.62 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 9.576  -7.169  22.735 1.00 17.62 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 12.367 -6.830  21.386 1.00 15.53 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 13.858 -6.690  21.403 1.00 16.12 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 14.573 -5.904  20.471 1.00 18.34 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 14.731 -7.233  22.266 1.00 15.59 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 15.862 -6.005  20.844 1.00 15.60 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 15.990 -6.794  21.901 1.00 19.72 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 9.440  -5.311  21.433 1.00 13.95 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.021  -5.471  21.171 1.00 14.38 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 7.708  -5.526  19.682 1.00 14.51 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.190  -4.704  18.926 1.00 14.73 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.225  -4.272  21.722 1.00 14.54 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.265  -4.141  23.230 1.00 16.24 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 6.479  -4.952  24.037 1.00 17.67 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.045  -3.169  23.844 1.00 17.03 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 6.479  -4.808  25.431 1.00 18.95 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.056  -3.013  25.238 1.00 18.11 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.273  -3.838  26.022 1.00 20.33 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.265  -3.654  27.393 1.00 21.71 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 6.828  -6.456  19.292 1.00 14.33 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.371  -6.500  17.888 1.00 14.27 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.291  -5.406  17.698 1.00 15.98 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.368  -5.331  18.554 1.00 18.28 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 5.776  -7.928  17.770 1.00 15.59 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.255  -8.232  19.186 1.00 16.01 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.198  -7.517  20.132 1.00 14.66 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.353  -4.625  16.598 1.00 14.42 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.334  -3.571  16.430 1.00 14.73 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 3.920  -3.467  14.980 1.00 15.47 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 4.690  -3.759  14.062 1.00 15.21 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 4.931  -2.179  16.835 1.00 16.90 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 4.979  -2.005  18.364 1.00 18.34 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.292  -1.915  16.183 1.00 17.95 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 2.701  -2.912  14.751 1.00 15.14 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.286  -2.442  13.444 1.00 15.43 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.491  -0.919  13.486 1.00 14.54 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.267  -0.279  14.542 1.00 15.94 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 0.796  -2.692  13.221 1.00 18.61 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.519  -4.083  13.205 1.00 25.78 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 2.966  -0.334  12.371 1.00 14.11 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.230  1.116   12.341 1.00 14.05 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.723  1.774   11.063 1.00 15.44 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.602  1.121   10.014 1.00 16.25 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.728  1.427   12.589 1.00 14.15 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.692  0.660   11.699 1.00 13.51 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.184  -0.565  12.078 1.00 15.37 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.098  1.188   10.479 1.00 14.45 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.053  -1.274  11.241 1.00 15.77 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.011  0.512   9.674  1.00 15.22 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.470  -0.735  10.054 1.00 15.53 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.425  3.054   11.171 1.00 15.30 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 1.941  3.807   10.032 1.00 15.82 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.090  4.128   9.048  1.00 16.46 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.251  4.163   9.438  1.00 17.11 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.250  5.096   10.498 1.00 16.39 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.136  5.936   11.230 1.00 17.67 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.774  4.355   7.747  1.00 17.68 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.780  4.781   6.783  1.00 17.45 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.333  6.184   7.140  1.00 18.17 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.649  7.001   7.765  1.00 19.45 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 3.217  4.766   5.341  1.00 19.60 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.887  3.364   4.862  1.00 21.52 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.369  3.376   3.404  1.00 26.97 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.152  1.955   2.919  1.00 31.72 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 1.756  1.915   1.468  1.00 35.60 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.580  6.470   6.768  1.00 18.22 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.188  7.765   7.145  1.00 18.81 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.360  8.967   6.701  1.00 19.19 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 4.906  9.001   5.557  1.00 20.23 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.533  7.761   6.430  1.00 20.68 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.850  6.299   6.178  1.00 21.39 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.507  5.603   6.012  1.00 18.80 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 5.115  9.909   7.632  1.00 18.48 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.291  11.070  7.290  1.00 20.58 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.625  12.298  8.176  1.00 21.33 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.513  12.203  9.049  1.00 20.13 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 2.813  10.699  7.345  1.00 25.20 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.367  10.614  8.684  1.00 31.11 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 3.953  13.443  7.934  1.00 21.67 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 4.150  14.701  8.667  1.00 22.56 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 3.160  14.718  9.811  1.00 24.22 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 1.936  14.700  9.573  1.00 26.03 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.787  15.855  7.692  1.00 23.96 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.543  17.180  7.658  1.00 29.15 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 3.628  18.325  7.223  1.00 30.66 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 5.399  17.489  8.935  1.00 30.51 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.658  14.629  11.063 1.00 22.93 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 2.826  14.481  12.247 1.00 25.17 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 3.068  15.573  13.282 1.00 26.25 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.227  15.997  13.451 1.00 24.81 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 3.215  13.100  12.831 1.00 26.70 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.785  11.979  11.864 1.00 29.08 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 2.732  12.881  14.292 1.00 27.40 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 3.189  10.668  12.222 1.00 30.95 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 1.981  15.981  14.023 1.00 27.97 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.116  16.883  15.157 1.00 29.81 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 2.343  16.015  16.401 1.00 31.02 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 1.501  15.173  16.731 1.00 33.44 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 0.870  17.768  15.357 1.00 30.14 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 1.111  18.870  16.362 1.00 31.97 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 1.889  19.959  16.041 1.00 33.44 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 0.611  18.777  17.646 1.00 33.66 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 2.157  20.952  16.984 1.00 34.68 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 0.857  19.777  18.577 1.00 34.79 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 1.640  20.849  18.245 1.00 34.53 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 3.465  16.235  17.089 1.00 29.41 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 3.891  15.505  18.290 1.00 30.07 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 3.462  16.308  19.538 1.00 30.54 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 3.941  17.404  19.698 1.00 29.39 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 5.445  15.379  18.260 1.00 30.63 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 5.942  14.597  19.459 1.00 31.48 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 5.939  14.745  16.954 1.00 30.86 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 2.588  15.763  20.411 1.00 31.67 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 2.121  16.507  21.597 1.00 32.82 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 3.225  16.829  22.611 1.00 33.67 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 4.199  16.082  22.755 1.00 33.48 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 1.011  15.731  22.327 1.00 35.93 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? -0.136 15.269  21.449 1.00 41.20 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? -0.978 16.406  20.910 1.00 49.54 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? -1.149 17.421  21.624 1.00 50.14 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? -1.450 16.286  19.758 1.00 52.12 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 3.034  17.919  23.359 1.00 33.76 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 3.924  18.368  24.428 1.00 34.92 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 3.917  17.320  25.556 1.00 35.88 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 2.912  16.623  25.771 1.00 36.21 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 3.453  19.718  24.972 1.00 35.62 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 5.066  17.167  26.222 1.00 35.58 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 5.229  16.197  27.307 1.00 35.39 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 5.859  16.884  28.550 1.00 35.84 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 6.087  18.099  28.531 1.00 36.09 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 6.066  15.015  26.821 1.00 35.68 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 7.390  15.454  26.563 1.00 35.94 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 6.106  16.129  29.644 1.00 35.85 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 6.645  16.715  30.879 1.00 36.02 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 7.962  17.474  30.681 1.00 35.96 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 8.157  18.533  31.284 1.00 35.43 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 6.850  15.615  31.947 1.00 37.91 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 7.351  16.128  33.288 1.00 42.63 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 7.626  15.062  34.340 1.00 47.00 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 8.062  15.429  35.455 1.00 44.69 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 7.421  13.862  34.043 1.00 49.04 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 8.868  16.923  29.859 1.00 35.92 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 10.200 17.491  29.693 1.00 36.88 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 10.501 18.099  28.321 1.00 37.00 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 11.521 18.773  28.186 1.00 36.95 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 11.262 16.419  29.991 1.00 37.62 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 11.176 15.820  31.378 1.00 39.41 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 11.644 16.514  32.486 1.00 40.78 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 10.690 14.534  31.573 1.00 40.82 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 11.610 15.952  33.756 1.00 41.80 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 10.637 13.966  32.841 1.00 41.98 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 11.097 14.681  33.931 1.00 42.93 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 11.037 14.136  35.192 1.00 44.64 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 9.662  17.821  27.303 1.00 36.48 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 9.926  18.295  25.945 1.00 36.42 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 8.705  18.954  25.320 1.00 38.21 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 7.567  18.584  25.605 1.00 38.88 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 10.428 17.126  25.080 1.00 35.12 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 11.752 16.597  25.589 1.00 34.76 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 12.913 17.344  25.462 1.00 35.66 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 11.822 15.406  26.297 1.00 34.51 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 14.121 16.891  25.973 1.00 36.73 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 13.024 14.958  26.838 1.00 35.46 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 14.169 15.709  26.682 1.00 37.23 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 15.381 15.290  27.188 1.00 39.33 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 8.932  19.916  24.417 1.00 39.30 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 7.802  20.634  23.817 1.00 39.07 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 7.096  19.885  22.685 1.00 37.74 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 7.546  18.831  22.224 1.00 37.93 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 8.477  21.891  23.275 1.00 39.81 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 9.815  21.402  22.827 1.00 40.68 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 10.222 20.487  23.977 1.00 39.41 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 5.961  20.447  22.246 1.00 35.95 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 5.203  19.975  21.107 1.00 34.22 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 5.930  20.409  19.830 1.00 32.17 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 6.641  21.435  19.837 1.00 32.62 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 3.835  20.623  21.115 1.00 34.95 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 5.759  19.632  18.720 1.00 29.34 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 6.420  20.021  17.467 1.00 27.71 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.765  19.315  16.269 1.00 27.64 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 5.118  18.294  16.440 1.00 28.15 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.951  19.623  17.498 1.00 27.84 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 8.218  18.100  17.417 1.00 27.83 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 9.680  17.719  17.089 1.00 26.24 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.029 18.199  15.756 1.00 23.93 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 11.218 18.116  15.180 1.00 26.38 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 11.424 18.670  13.984 1.00 27.08 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 12.219 17.495  15.794 1.00 25.71 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 6.003  19.816  15.040 1.00 27.29 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 5.651  19.054  13.843 1.00 27.90 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.946  18.272  13.462 1.00 25.27 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 8.050  18.776  13.696 1.00 25.43 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 5.282  20.014  12.710 1.00 29.61 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 3.795  20.270  12.621 1.00 32.76 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 2.924  19.289  12.158 1.00 34.86 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 3.259  21.487  13.002 1.00 34.61 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 1.557  19.520  12.074 1.00 36.80 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 1.896  21.737  12.903 1.00 36.03 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 1.046  20.742  12.459 1.00 38.19 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -0.307 21.000  12.362 1.00 41.88 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 6.825  17.043  12.927 1.00 23.06 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 8.020  16.267  12.525 1.00 21.54 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.666  15.460  11.256 1.00 20.09 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.574  14.888  11.187 1.00 20.31 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 8.472  15.323  13.653 1.00 19.02 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.779  14.550  13.313 1.00 17.92 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 10.402 13.955  14.542 1.00 17.13 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 10.466 14.577  15.609 1.00 19.04 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 10.897 12.697  14.419 1.00 14.79 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.557  15.433  10.255 1.00 18.31 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.360  14.703  9.020  1.00 18.58 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 8.999  13.307  9.024  1.00 18.39 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 9.895  13.001  9.845  1.00 17.88 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 8.837  15.522  7.821  1.00 20.38 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 10.248 15.642  7.816  1.00 23.64 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.529  12.452  8.079  1.00 17.74 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 9.035  11.079  7.891  1.00 17.08 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 8.929  10.266  9.199  1.00 15.83 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 9.799  9.441   9.484  1.00 15.81 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.493 11.111  7.396  1.00 17.26 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 10.630 11.790  6.070  1.00 20.18 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.732 11.065  4.901  1.00 20.82 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 10.668 13.113  5.775  1.00 21.67 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 10.854 11.964  3.924  1.00 21.80 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 10.784 13.210  4.400  1.00 22.75 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 7.856  10.519  9.945  1.00 15.27 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.647  9.861   11.234 1.00 15.67 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.587  8.769   11.075 1.00 14.84 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.552  8.957   10.399 1.00 15.88 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 7.187  10.905  12.273 1.00 16.15 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 7.067  10.429  13.734 1.00 16.93 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.431  10.097  14.312 1.00 17.63 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.463  11.548  14.582 1.00 19.52 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 6.832  7.611   11.750 1.00 13.75 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 5.905  6.466   11.749 1.00 13.00 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.408  6.243   13.170 1.00 14.31 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.224  6.247   14.096 1.00 14.83 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.707  5.223   11.286 1.00 13.89 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.233  5.395   9.844  1.00 15.25 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.300  4.041   9.333  1.00 18.16 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.695  4.299   10.426 1.00 19.45 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 4.099  5.990   13.364 1.00 14.41 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.577  5.803   14.726 1.00 14.09 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 3.118  4.367   14.934 1.00 14.20 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.564  3.754   13.999 1.00 15.36 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.336  6.723   15.021 1.00 16.73 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.609  8.204   15.066 1.00 20.44 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.367  9.018   15.377 1.00 22.35 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 3.684  8.559   16.079 1.00 21.66 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.257  3.904   16.169 1.00 12.84 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 2.728  2.602   16.595 1.00 13.18 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.156  2.762   18.002 1.00 14.02 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.520  3.705   18.721 1.00 15.55 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 3.849  1.528   16.645 1.00 13.48 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.269  1.844   18.388 1.00 14.13 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 0.769  1.799   19.749 1.00 13.68 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 1.826  1.001   20.565 1.00 14.80 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.092  -0.197  20.321 1.00 15.16 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.617 1.129   19.810 1.00 15.07 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -1.085 0.952   21.257 1.00 16.23 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.630 1.908   18.957 1.00 16.24 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.404  1.684   21.536 1.00 16.61 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.432  1.041   22.356 1.00 16.77 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 4.026  2.007   23.350 1.00 17.66 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 3.746  3.196   23.335 1.00 19.27 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 4.922  1.462   24.194 1.00 16.83 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 5.541  2.283   25.228 1.00 16.16 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 6.834  2.961   24.808 1.00 15.77 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 7.693  2.321   24.192 1.00 15.99 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 5.782  1.422   26.495 1.00 16.54 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 6.292  2.229   27.639 1.00 17.99 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 5.494  3.161   28.281 1.00 20.43 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 7.548  2.303   28.149 1.00 18.30 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 6.277  3.750   29.178 1.00 19.74 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 7.512  3.230   29.146 1.00 18.03 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 7.012  4.239   25.158 1.00 16.01 ? 105 SER   A N   1 
ATOM   785  C  CA  A SER   A 1 99  ? 8.197  5.032   24.835 0.50 16.90 ? 105 SER   A CA  1 
ATOM   786  C  CA  B SER   A 1 99  ? 8.270  4.923   24.956 0.50 16.79 ? 105 SER   A CA  1 
ATOM   787  C  C   . SER   A 1 99  ? 8.338  6.106   25.904 1.00 18.80 ? 105 SER   A C   1 
ATOM   788  O  O   . SER   A 1 99  ? 7.333  6.769   26.205 1.00 21.10 ? 105 SER   A O   1 
ATOM   789  C  CB  A SER   A 1 99  ? 7.974  5.739   23.497 0.50 18.08 ? 105 SER   A CB  1 
ATOM   790  C  CB  B SER   A 1 99  ? 8.430  5.382   23.521 0.50 17.91 ? 105 SER   A CB  1 
ATOM   791  O  OG  A SER   A 1 99  ? 9.060  6.559   23.094 0.50 19.92 ? 105 SER   A OG  1 
ATOM   792  O  OG  B SER   A 1 99  ? 7.441  6.365   23.302 0.50 18.93 ? 105 SER   A OG  1 
ATOM   793  N  N   . GLU   A 1 100 ? 9.531  6.302   26.413 1.00 17.83 ? 106 GLU   A N   1 
ATOM   794  C  CA  . GLU   A 1 100 ? 9.937  7.379   27.334 1.00 18.82 ? 106 GLU   A CA  1 
ATOM   795  C  C   . GLU   A 1 100 ? 11.132 8.084   26.676 1.00 19.24 ? 106 GLU   A C   1 
ATOM   796  O  O   . GLU   A 1 100 ? 11.753 7.508   25.779 1.00 18.56 ? 106 GLU   A O   1 
ATOM   797  C  CB  . GLU   A 1 100 ? 10.382 6.772   28.671 1.00 20.21 ? 106 GLU   A CB  1 
ATOM   798  C  CG  . GLU   A 1 100 ? 9.211  6.193   29.403 1.00 23.35 ? 106 GLU   A CG  1 
ATOM   799  C  CD  . GLU   A 1 100 ? 9.552  5.539   30.736 1.00 24.96 ? 106 GLU   A CD  1 
ATOM   800  O  OE1 . GLU   A 1 100 ? 10.373 6.082   31.509 1.00 28.61 ? 106 GLU   A OE1 1 
ATOM   801  O  OE2 . GLU   A 1 100 ? 8.982  4.468   31.006 1.00 23.69 ? 106 GLU   A OE2 1 
ATOM   802  N  N   . PRO   A 1 101 ? 11.481 9.321   27.073 1.00 19.72 ? 107 PRO   A N   1 
ATOM   803  C  CA  . PRO   A 1 101 ? 12.568 10.044  26.367 1.00 18.98 ? 107 PRO   A CA  1 
ATOM   804  C  C   . PRO   A 1 101 ? 13.859 9.237   26.119 1.00 18.21 ? 107 PRO   A C   1 
ATOM   805  O  O   . PRO   A 1 101 ? 14.429 9.260   25.015 1.00 18.65 ? 107 PRO   A O   1 
ATOM   806  C  CB  . PRO   A 1 101 ? 12.801 11.263  27.278 1.00 20.95 ? 107 PRO   A CB  1 
ATOM   807  C  CG  . PRO   A 1 101 ? 11.437 11.526  27.836 1.00 22.64 ? 107 PRO   A CG  1 
ATOM   808  C  CD  . PRO   A 1 101 ? 10.796 10.175  28.067 1.00 20.64 ? 107 PRO   A CD  1 
ATOM   809  N  N   . GLY   A 1 102 ? 14.359 8.562   27.154 1.00 17.70 ? 108 GLY   A N   1 
ATOM   810  C  CA  . GLY   A 1 102 ? 15.580 7.771   27.062 1.00 18.39 ? 108 GLY   A CA  1 
ATOM   811  C  C   . GLY   A 1 102 ? 15.497 6.593   26.117 1.00 17.36 ? 108 GLY   A C   1 
ATOM   812  O  O   . GLY   A 1 102 ? 16.523 5.922   25.865 1.00 18.30 ? 108 GLY   A O   1 
ATOM   813  N  N   . ASP   A 1 103 ? 14.274 6.273   25.640 1.00 16.02 ? 109 ASP   A N   1 
ATOM   814  C  CA  . ASP   A 1 103 ? 14.132 5.218   24.644 1.00 15.04 ? 109 ASP   A CA  1 
ATOM   815  C  C   . ASP   A 1 103 ? 14.540 5.664   23.240 1.00 15.05 ? 109 ASP   A C   1 
ATOM   816  O  O   . ASP   A 1 103 ? 14.724 4.818   22.349 1.00 14.96 ? 109 ASP   A O   1 
ATOM   817  C  CB  . ASP   A 1 103 ? 12.686 4.738   24.595 1.00 14.21 ? 109 ASP   A CB  1 
ATOM   818  C  CG  . ASP   A 1 103 ? 12.320 3.923   25.830 1.00 16.80 ? 109 ASP   A CG  1 
ATOM   819  O  OD1 . ASP   A 1 103 ? 13.197 3.219   26.343 1.00 17.74 ? 109 ASP   A OD1 1 
ATOM   820  O  OD2 . ASP   A 1 103 ? 11.136 4.011   26.291 1.00 17.03 ? 109 ASP   A OD2 1 
ATOM   821  N  N   . CYS   A 1 104 ? 14.799 6.980   23.039 1.00 14.91 ? 110 CYS   A N   1 
ATOM   822  C  CA  . CYS   A 1 104 ? 15.258 7.440   21.702 1.00 15.13 ? 110 CYS   A CA  1 
ATOM   823  C  C   . CYS   A 1 104 ? 16.509 6.718   21.301 1.00 15.10 ? 110 CYS   A C   1 
ATOM   824  O  O   . CYS   A 1 104 ? 17.405 6.535   22.134 1.00 16.81 ? 110 CYS   A O   1 
ATOM   825  C  CB  . CYS   A 1 104 ? 15.504 8.943   21.683 1.00 14.60 ? 110 CYS   A CB  1 
ATOM   826  S  SG  . CYS   A 1 104 ? 13.991 9.953   21.663 1.00 17.23 ? 110 CYS   A SG  1 
ATOM   827  N  N   . GLY   A 1 105 ? 16.571 6.328   20.040 1.00 13.79 ? 111 GLY   A N   1 
ATOM   828  C  CA  . GLY   A 1 105 ? 17.721 5.612   19.530 1.00 14.42 ? 111 GLY   A CA  1 
ATOM   829  C  C   . GLY   A 1 105 ? 17.474 4.112   19.444 1.00 15.17 ? 111 GLY   A C   1 
ATOM   830  O  O   . GLY   A 1 105 ? 18.223 3.423   18.748 1.00 16.20 ? 111 GLY   A O   1 
ATOM   831  N  N   . GLY   A 1 106 ? 16.430 3.588   20.109 1.00 15.19 ? 112 GLY   A N   1 
ATOM   832  C  CA  . GLY   A 1 106 ? 16.083 2.173   19.966 1.00 14.30 ? 112 GLY   A CA  1 
ATOM   833  C  C   . GLY   A 1 106 ? 15.727 1.857   18.517 1.00 13.23 ? 112 GLY   A C   1 
ATOM   834  O  O   . GLY   A 1 106 ? 15.028 2.631   17.868 1.00 13.81 ? 112 GLY   A O   1 
ATOM   835  N  N   . ILE   A 1 107 ? 16.236 0.720   18.012 1.00 12.75 ? 113 ILE   A N   1 
ATOM   836  C  CA  . ILE   A 1 107 ? 16.015 0.391   16.609 1.00 13.51 ? 113 ILE   A CA  1 
ATOM   837  C  C   . ILE   A 1 107 ? 14.707 -0.365  16.372 1.00 13.52 ? 113 ILE   A C   1 
ATOM   838  O  O   . ILE   A 1 107 ? 14.354 -1.275  17.168 1.00 13.91 ? 113 ILE   A O   1 
ATOM   839  C  CB  . ILE   A 1 107 ? 17.245 -0.364  16.057 1.00 14.91 ? 113 ILE   A CB  1 
ATOM   840  C  CG1 . ILE   A 1 107 ? 18.400 0.626   15.879 1.00 16.97 ? 113 ILE   A CG1 1 
ATOM   841  C  CG2 . ILE   A 1 107 ? 16.899 -1.046  14.710 1.00 17.73 ? 113 ILE   A CG2 1 
ATOM   842  C  CD1 . ILE   A 1 107 ? 19.753 -0.115  15.439 1.00 19.13 ? 113 ILE   A CD1 1 
ATOM   843  N  N   . LEU   A 1 108 ? 14.004 0.004   15.296 1.00 12.86 ? 114 LEU   A N   1 
ATOM   844  C  CA  . LEU   A 1 108 ? 12.851 -0.721  14.740 1.00 12.58 ? 114 LEU   A CA  1 
ATOM   845  C  C   . LEU   A 1 108 ? 13.381 -1.505  13.542 1.00 12.68 ? 114 LEU   A C   1 
ATOM   846  O  O   . LEU   A 1 108 ? 14.028 -0.885  12.665 1.00 13.18 ? 114 LEU   A O   1 
ATOM   847  C  CB  . LEU   A 1 108 ? 11.771 0.322   14.309 1.00 12.19 ? 114 LEU   A CB  1 
ATOM   848  C  CG  . LEU   A 1 108 ? 10.596 -0.289  13.548 1.00 13.11 ? 114 LEU   A CG  1 
ATOM   849  C  CD1 . LEU   A 1 108 ? 9.752  -1.247  14.457 1.00 15.03 ? 114 LEU   A CD1 1 
ATOM   850  C  CD2 . LEU   A 1 108 ? 9.698  0.831   12.960 1.00 14.00 ? 114 LEU   A CD2 1 
ATOM   851  N  N   . ARG   A 1 109 ? 13.130 -2.831  13.510 1.00 13.07 ? 115 ARG   A N   1 
ATOM   852  C  CA  . ARG   A 1 109 ? 13.648 -3.713  12.450 1.00 14.24 ? 115 ARG   A CA  1 
ATOM   853  C  C   . ARG   A 1 109 ? 12.565 -4.588  11.893 1.00 14.46 ? 115 ARG   A C   1 
ATOM   854  O  O   . ARG   A 1 109 ? 11.662 -5.026  12.603 1.00 15.04 ? 115 ARG   A O   1 
ATOM   855  C  CB  . ARG   A 1 109 ? 14.729 -4.660  13.066 1.00 17.97 ? 115 ARG   A CB  1 
ATOM   856  C  CG  . ARG   A 1 109 ? 16.046 -4.034  13.503 1.00 25.39 ? 115 ARG   A CG  1 
ATOM   857  C  CD  . ARG   A 1 109 ? 16.986 -5.175  13.967 1.00 29.85 ? 115 ARG   A CD  1 
ATOM   858  N  NE  . ARG   A 1 109 ? 18.294 -5.101  13.297 1.00 36.74 ? 115 ARG   A NE  1 
ATOM   859  C  CZ  . ARG   A 1 109 ? 19.348 -4.448  13.781 1.00 39.97 ? 115 ARG   A CZ  1 
ATOM   860  N  NH1 . ARG   A 1 109 ? 19.282 -3.851  14.964 1.00 42.49 ? 115 ARG   A NH1 1 
ATOM   861  N  NH2 . ARG   A 1 109 ? 20.496 -4.450  13.119 1.00 43.17 ? 115 ARG   A NH2 1 
ATOM   862  N  N   . CYS   A 1 110 ? 12.643 -4.854  10.601 1.00 14.44 ? 116 CYS   A N   1 
ATOM   863  C  CA  . CYS   A 1 110 ? 11.751 -5.839  9.937  1.00 15.99 ? 116 CYS   A CA  1 
ATOM   864  C  C   . CYS   A 1 110 ? 12.651 -6.961  9.371  1.00 17.85 ? 116 CYS   A C   1 
ATOM   865  O  O   . CYS   A 1 110 ? 13.875 -6.948  9.561  1.00 18.73 ? 116 CYS   A O   1 
ATOM   866  C  CB  . CYS   A 1 110 ? 10.927 -5.180  8.834  1.00 16.53 ? 116 CYS   A CB  1 
ATOM   867  S  SG  . CYS   A 1 110 ? 11.943 -4.535  7.451  1.00 16.42 ? 116 CYS   A SG  1 
ATOM   868  N  N   . GLN   A 1 111 ? 12.052 -7.911  8.600  1.00 20.25 ? 117 GLN   A N   1 
ATOM   869  C  CA  . GLN   A 1 111 ? 12.854 -8.977  7.997  1.00 22.51 ? 117 GLN   A CA  1 
ATOM   870  C  C   . GLN   A 1 111 ? 13.958 -8.470  7.023  1.00 22.88 ? 117 GLN   A C   1 
ATOM   871  O  O   . GLN   A 1 111 ? 14.956 -9.174  6.771  1.00 25.51 ? 117 GLN   A O   1 
ATOM   872  C  CB  . GLN   A 1 111 ? 11.935 -9.977  7.271  1.00 26.01 ? 117 GLN   A CB  1 
ATOM   873  C  CG  . GLN   A 1 111 ? 11.175 -9.314  6.126  1.00 31.27 ? 117 GLN   A CG  1 
ATOM   874  C  CD  . GLN   A 1 111 ? 10.268 -10.272 5.386  1.00 39.12 ? 117 GLN   A CD  1 
ATOM   875  O  OE1 . GLN   A 1 111 ? 9.038  -10.107 5.365  1.00 41.77 ? 117 GLN   A OE1 1 
ATOM   876  N  NE2 . GLN   A 1 111 ? 10.864 -11.281 4.759  1.00 39.01 ? 117 GLN   A NE2 1 
ATOM   877  N  N   . HIS   A 1 112 ? 13.790 -7.260  6.480  1.00 19.25 ? 118 HIS   A N   1 
ATOM   878  C  CA  . HIS   A 1 112 ? 14.721 -6.664  5.511  1.00 18.93 ? 118 HIS   A CA  1 
ATOM   879  C  C   . HIS   A 1 112 ? 15.878 -5.869  6.137  1.00 19.46 ? 118 HIS   A C   1 
ATOM   880  O  O   . HIS   A 1 112 ? 16.830 -5.496  5.423  1.00 21.27 ? 118 HIS   A O   1 
ATOM   881  C  CB  . HIS   A 1 112 ? 13.925 -5.781  4.532  1.00 19.75 ? 118 HIS   A CB  1 
ATOM   882  C  CG  . HIS   A 1 112 ? 12.781 -6.494  3.866  1.00 21.33 ? 118 HIS   A CG  1 
ATOM   883  N  ND1 . HIS   A 1 112 ? 11.482 -6.252  4.227  1.00 21.79 ? 118 HIS   A ND1 1 
ATOM   884  C  CD2 . HIS   A 1 112 ? 12.785 -7.325  2.791  1.00 23.99 ? 118 HIS   A CD2 1 
ATOM   885  C  CE1 . HIS   A 1 112 ? 10.731 -7.043  3.466  1.00 24.01 ? 118 HIS   A CE1 1 
ATOM   886  N  NE2 . HIS   A 1 112 ? 11.475 -7.680  2.556  1.00 25.51 ? 118 HIS   A NE2 1 
ATOM   887  N  N   . GLY   A 1 113 ? 15.795 -5.579  7.448  1.00 17.57 ? 119 GLY   A N   1 
ATOM   888  C  CA  . GLY   A 1 113 ? 16.840 -4.745  8.061  1.00 16.10 ? 119 GLY   A CA  1 
ATOM   889  C  C   . GLY   A 1 113 ? 16.285 -3.653  8.969  1.00 15.55 ? 119 GLY   A C   1 
ATOM   890  O  O   . GLY   A 1 113 ? 15.131 -3.734  9.422  1.00 16.71 ? 119 GLY   A O   1 
ATOM   891  N  N   . VAL   A 1 114 ? 17.092 -2.631  9.184  1.00 15.16 ? 120 VAL   A N   1 
ATOM   892  C  CA  . VAL   A 1 114 ? 16.704 -1.497  10.005 1.00 14.94 ? 120 VAL   A CA  1 
ATOM   893  C  C   . VAL   A 1 114 ? 15.706 -0.608  9.294  1.00 15.13 ? 120 VAL   A C   1 
ATOM   894  O  O   . VAL   A 1 114 ? 15.945 -0.148  8.141  1.00 16.08 ? 120 VAL   A O   1 
ATOM   895  C  CB  . VAL   A 1 114 ? 17.960 -0.715  10.410 1.00 15.50 ? 120 VAL   A CB  1 
ATOM   896  C  CG1 . VAL   A 1 114 ? 17.555 0.557   11.165 1.00 16.10 ? 120 VAL   A CG1 1 
ATOM   897  C  CG2 . VAL   A 1 114 ? 18.874 -1.591  11.265 1.00 17.90 ? 120 VAL   A CG2 1 
ATOM   898  N  N   . VAL   A 1 115 ? 14.583 -0.325  9.968  1.00 13.17 ? 121 VAL   A N   1 
ATOM   899  C  CA  . VAL   A 1 115 ? 13.525 0.535   9.407  1.00 13.46 ? 121 VAL   A CA  1 
ATOM   900  C  C   . VAL   A 1 115 ? 13.701 1.990   9.925  1.00 14.98 ? 121 VAL   A C   1 
ATOM   901  O  O   . VAL   A 1 115 ? 13.534 2.960   9.186  1.00 15.25 ? 121 VAL   A O   1 
ATOM   902  C  CB  . VAL   A 1 115 ? 12.159 -0.029  9.837  1.00 14.07 ? 121 VAL   A CB  1 
ATOM   903  C  CG1 . VAL   A 1 115 ? 11.020 0.890   9.409  1.00 15.38 ? 121 VAL   A CG1 1 
ATOM   904  C  CG2 . VAL   A 1 115 ? 11.989 -1.439  9.270  1.00 16.17 ? 121 VAL   A CG2 1 
ATOM   905  N  N   . GLY   A 1 116 ? 13.984 2.128   11.233 1.00 14.08 ? 122 GLY   A N   1 
ATOM   906  C  CA  . GLY   A 1 116 ? 14.085 3.467   11.810 1.00 14.53 ? 122 GLY   A CA  1 
ATOM   907  C  C   . GLY   A 1 116 ? 14.499 3.433   13.272 1.00 13.15 ? 122 GLY   A C   1 
ATOM   908  O  O   . GLY   A 1 116 ? 14.850 2.362   13.784 1.00 13.83 ? 122 GLY   A O   1 
ATOM   909  N  N   . ILE   A 1 117 ? 14.464 4.620   13.922 1.00 12.98 ? 123 ILE   A N   1 
ATOM   910  C  CA  . ILE   A 1 117 ? 14.861 4.708   15.333 1.00 13.59 ? 123 ILE   A CA  1 
ATOM   911  C  C   . ILE   A 1 117 ? 13.827 5.451   16.130 1.00 13.06 ? 123 ILE   A C   1 
ATOM   912  O  O   . ILE   A 1 117 ? 13.179 6.379   15.622 1.00 13.34 ? 123 ILE   A O   1 
ATOM   913  C  CB  . ILE   A 1 117 ? 16.251 5.362   15.511 1.00 14.66 ? 123 ILE   A CB  1 
ATOM   914  C  CG1 . ILE   A 1 117 ? 16.317 6.706   14.801 1.00 15.75 ? 123 ILE   A CG1 1 
ATOM   915  C  CG2 . ILE   A 1 117 ? 17.360 4.401   15.107 1.00 17.42 ? 123 ILE   A CG2 1 
ATOM   916  C  CD1 . ILE   A 1 117 ? 17.657 7.467   15.234 1.00 17.28 ? 123 ILE   A CD1 1 
ATOM   917  N  N   . VAL   A 1 118 ? 13.625 5.038   17.410 1.00 11.74 ? 124 VAL   A N   1 
ATOM   918  C  CA  . VAL   A 1 118 ? 12.667 5.753   18.269 1.00 12.51 ? 124 VAL   A CA  1 
ATOM   919  C  C   . VAL   A 1 118 ? 13.012 7.262   18.345 1.00 13.38 ? 124 VAL   A C   1 
ATOM   920  O  O   . VAL   A 1 118 ? 14.186 7.591   18.581 1.00 12.97 ? 124 VAL   A O   1 
ATOM   921  C  CB  . VAL   A 1 118 ? 12.673 5.154   19.694 1.00 12.67 ? 124 VAL   A CB  1 
ATOM   922  C  CG1 . VAL   A 1 118 ? 11.776 6.017   20.615 1.00 13.83 ? 124 VAL   A CG1 1 
ATOM   923  C  CG2 . VAL   A 1 118 ? 12.186 3.699   19.692 1.00 13.84 ? 124 VAL   A CG2 1 
ATOM   924  N  N   . SER   A 1 119 ? 12.017 8.119   18.162 1.00 13.60 ? 125 SER   A N   1 
ATOM   925  C  CA  . SER   A 1 119 ? 12.224 9.559   18.176 1.00 14.03 ? 125 SER   A CA  1 
ATOM   926  C  C   . SER   A 1 119 ? 11.165 10.312  18.977 1.00 15.63 ? 125 SER   A C   1 
ATOM   927  O  O   . SER   A 1 119 ? 11.468 11.401  19.486 1.00 16.68 ? 125 SER   A O   1 
ATOM   928  C  CB  . SER   A 1 119 ? 12.239 10.045  16.728 1.00 14.93 ? 125 SER   A CB  1 
ATOM   929  O  OG  . SER   A 1 119 ? 12.354 11.475  16.632 1.00 15.32 ? 125 SER   A OG  1 
ATOM   930  N  N   . THR   A 1 120 ? 9.930  9.773   19.091 1.00 15.20 ? 126 THR   A N   1 
ATOM   931  C  CA  . THR   A 1 120 ? 8.862  10.460  19.843 1.00 15.92 ? 126 THR   A CA  1 
ATOM   932  C  C   . THR   A 1 120 ? 8.069  9.476   20.701 1.00 17.71 ? 126 THR   A C   1 
ATOM   933  O  O   . THR   A 1 120 ? 8.221  8.249   20.543 1.00 16.73 ? 126 THR   A O   1 
ATOM   934  C  CB  . THR   A 1 120 ? 7.906  11.228  18.877 1.00 18.55 ? 126 THR   A CB  1 
ATOM   935  O  OG1 . THR   A 1 120 ? 7.048  10.303  18.195 1.00 20.19 ? 126 THR   A OG1 1 
ATOM   936  C  CG2 . THR   A 1 120 ? 8.606  12.143  17.931 1.00 18.00 ? 126 THR   A CG2 1 
ATOM   937  N  N   . GLY   A 1 121 ? 7.244  9.992   21.616 1.00 20.19 ? 127 GLY   A N   1 
ATOM   938  C  CA  . GLY   A 1 121 ? 6.453  9.115   22.453 1.00 23.11 ? 127 GLY   A CA  1 
ATOM   939  C  C   . GLY   A 1 121 ? 5.485  9.867   23.326 1.00 27.60 ? 127 GLY   A C   1 
ATOM   940  O  O   . GLY   A 1 121 ? 5.403  11.099  23.260 1.00 30.05 ? 127 GLY   A O   1 
ATOM   941  N  N   . GLY   A 1 122 ? 4.917  9.117   24.248 1.00 29.74 ? 128 GLY   A N   1 
ATOM   942  C  CA  . GLY   A 1 122 ? 3.920  9.608   25.188 1.00 30.99 ? 128 GLY   A CA  1 
ATOM   943  C  C   . GLY   A 1 122 ? 2.525  9.193   24.760 1.00 30.73 ? 128 GLY   A C   1 
ATOM   944  O  O   . GLY   A 1 122 ? 2.328  8.725   23.631 1.00 29.92 ? 128 GLY   A O   1 
ATOM   945  N  N   . ASN   A 1 123 ? 1.526  9.396   25.636 1.00 31.09 ? 129 ASN   A N   1 
ATOM   946  C  CA  . ASN   A 1 123 ? 0.134  9.049   25.342 1.00 31.03 ? 129 ASN   A CA  1 
ATOM   947  C  C   . ASN   A 1 123 ? -0.065 7.611   24.763 1.00 28.20 ? 129 ASN   A C   1 
ATOM   948  O  O   . ASN   A 1 123 ? -0.984 7.404   23.965 1.00 28.24 ? 129 ASN   A O   1 
ATOM   949  C  CB  . ASN   A 1 123 ? -0.536 10.078  24.398 1.00 35.02 ? 129 ASN   A CB  1 
ATOM   950  C  CG  . ASN   A 1 123 ? -1.030 11.370  25.028 1.00 41.87 ? 129 ASN   A CG  1 
ATOM   951  O  OD1 . ASN   A 1 123 ? -0.782 11.654  26.211 1.00 45.05 ? 129 ASN   A OD1 1 
ATOM   952  N  ND2 . ASN   A 1 123 ? -1.739 12.197  24.234 1.00 42.79 ? 129 ASN   A ND2 1 
ATOM   953  N  N   . GLY   A 1 124 ? 0.788  6.646   25.138 1.00 25.09 ? 130 GLY   A N   1 
ATOM   954  C  CA  . GLY   A 1 124 ? 0.625  5.282   24.649 1.00 23.05 ? 130 GLY   A CA  1 
ATOM   955  C  C   . GLY   A 1 124 ? 1.057  5.044   23.198 1.00 19.85 ? 130 GLY   A C   1 
ATOM   956  O  O   . GLY   A 1 124 ? 0.731  4.002   22.636 1.00 18.45 ? 130 GLY   A O   1 
ATOM   957  N  N   . LEU   A 1 125 ? 1.759  5.985   22.589 1.00 18.75 ? 131 LEU   A N   1 
ATOM   958  C  CA  . LEU   A 1 125 ? 2.242  5.820   21.218 1.00 18.51 ? 131 LEU   A CA  1 
ATOM   959  C  C   . LEU   A 1 125 ? 3.779  5.857   21.242 1.00 18.41 ? 131 LEU   A C   1 
ATOM   960  O  O   . LEU   A 1 125 ? 4.395  6.362   22.191 1.00 20.97 ? 131 LEU   A O   1 
ATOM   961  C  CB  . LEU   A 1 125 ? 1.736  6.939   20.293 1.00 20.57 ? 131 LEU   A CB  1 
ATOM   962  C  CG  . LEU   A 1 125 ? 0.179  7.022   20.243 1.00 23.14 ? 131 LEU   A CG  1 
ATOM   963  C  CD1 . LEU   A 1 125 ? -0.299 8.349   19.698 1.00 26.32 ? 131 LEU   A CD1 1 
ATOM   964  C  CD2 . LEU   A 1 125 ? -0.394 5.867   19.453 1.00 22.19 ? 131 LEU   A CD2 1 
ATOM   965  N  N   . VAL   A 1 126 ? 4.367  5.287   20.215 1.00 14.65 ? 132 VAL   A N   1 
ATOM   966  C  CA  . VAL   A 1 126 ? 5.809  5.388   19.979 1.00 14.15 ? 132 VAL   A CA  1 
ATOM   967  C  C   . VAL   A 1 126 ? 5.999  5.841   18.544 1.00 14.49 ? 132 VAL   A C   1 
ATOM   968  O  O   . VAL   A 1 126 ? 5.340  5.327   17.641 1.00 15.55 ? 132 VAL   A O   1 
ATOM   969  C  CB  . VAL   A 1 126 ? 6.557  4.080   20.287 1.00 15.59 ? 132 VAL   A CB  1 
ATOM   970  C  CG1 . VAL   A 1 126 ? 5.963  2.873   19.584 1.00 17.29 ? 132 VAL   A CG1 1 
ATOM   971  C  CG2 . VAL   A 1 126 ? 8.070  4.198   20.008 1.00 16.13 ? 132 VAL   A CG2 1 
ATOM   972  N  N   . GLY   A 1 127 ? 6.860  6.841   18.335 1.00 14.23 ? 133 GLY   A N   1 
ATOM   973  C  CA  . GLY   A 1 127 ? 7.122  7.352   16.997 1.00 14.42 ? 133 GLY   A CA  1 
ATOM   974  C  C   . GLY   A 1 127 ? 8.548  7.046   16.575 1.00 13.93 ? 133 GLY   A C   1 
ATOM   975  O  O   . GLY   A 1 127 ? 9.479  7.157   17.384 1.00 14.26 ? 133 GLY   A O   1 
ATOM   976  N  N   . PHE   A 1 128 ? 8.728  6.610   15.316 1.00 12.30 ? 134 PHE   A N   1 
ATOM   977  C  CA  . PHE   A 1 128 ? 10.055 6.220   14.801 1.00 13.00 ? 134 PHE   A CA  1 
ATOM   978  C  C   . PHE   A 1 128 ? 10.398 7.082   13.589 1.00 13.52 ? 134 PHE   A C   1 
ATOM   979  O  O   . PHE   A 1 128 ? 9.561  7.257   12.668 1.00 13.92 ? 134 PHE   A O   1 
ATOM   980  C  CB  . PHE   A 1 128 ? 9.997  4.734   14.292 1.00 12.89 ? 134 PHE   A CB  1 
ATOM   981  C  CG  . PHE   A 1 128 ? 9.466  3.770   15.313 1.00 12.67 ? 134 PHE   A CG  1 
ATOM   982  C  CD1 . PHE   A 1 128 ? 10.308 3.206   16.255 1.00 12.55 ? 134 PHE   A CD1 1 
ATOM   983  C  CD2 . PHE   A 1 128 ? 8.127  3.392   15.305 1.00 13.71 ? 134 PHE   A CD2 1 
ATOM   984  C  CE1 . PHE   A 1 128 ? 9.817  2.302   17.186 1.00 13.00 ? 134 PHE   A CE1 1 
ATOM   985  C  CE2 . PHE   A 1 128 ? 7.655  2.433   16.201 1.00 14.62 ? 134 PHE   A CE2 1 
ATOM   986  C  CZ  . PHE   A 1 128 ? 8.505  1.890   17.143 1.00 13.65 ? 134 PHE   A CZ  1 
ATOM   987  N  N   . ALA   A 1 129 ? 11.632 7.608   13.605 1.00 12.54 ? 135 ALA   A N   1 
ATOM   988  C  CA  . ALA   A 1 129 ? 12.111 8.361   12.451 1.00 12.29 ? 135 ALA   A CA  1 
ATOM   989  C  C   . ALA   A 1 129 ? 12.539 7.311   11.396 1.00 13.14 ? 135 ALA   A C   1 
ATOM   990  O  O   . ALA   A 1 129 ? 13.444 6.503   11.636 1.00 13.84 ? 135 ALA   A O   1 
ATOM   991  C  CB  . ALA   A 1 129 ? 13.307 9.210   12.873 1.00 13.39 ? 135 ALA   A CB  1 
ATOM   992  N  N   . ASP   A 1 130 ? 11.942 7.354   10.182 1.00 13.13 ? 136 ASP   A N   1 
ATOM   993  C  CA  . ASP   A 1 130 ? 12.266 6.405   9.127  1.00 13.69 ? 136 ASP   A CA  1 
ATOM   994  C  C   . ASP   A 1 130 ? 13.626 6.702   8.550  1.00 14.01 ? 136 ASP   A C   1 
ATOM   995  O  O   . ASP   A 1 130 ? 14.001 7.877   8.418  1.00 15.23 ? 136 ASP   A O   1 
ATOM   996  C  CB  . ASP   A 1 130 ? 11.212 6.543   8.002  1.00 15.65 ? 136 ASP   A CB  1 
ATOM   997  C  CG  . ASP   A 1 130 ? 11.411 5.574   6.847  1.00 18.41 ? 136 ASP   A CG  1 
ATOM   998  O  OD1 . ASP   A 1 130 ? 11.490 4.363   7.105  1.00 18.01 ? 136 ASP   A OD1 1 
ATOM   999  O  OD2 . ASP   A 1 130 ? 11.480 6.042   5.679  1.00 21.06 ? 136 ASP   A OD2 1 
ATOM   1000 N  N   . VAL   A 1 131 ? 14.353 5.655   8.105  1.00 14.18 ? 137 VAL   A N   1 
ATOM   1001 C  CA  . VAL   A 1 131 ? 15.647 5.816   7.419  1.00 14.18 ? 137 VAL   A CA  1 
ATOM   1002 C  C   . VAL   A 1 131 ? 15.648 5.079   6.051  1.00 15.75 ? 137 VAL   A C   1 
ATOM   1003 O  O   . VAL   A 1 131 ? 16.640 5.142   5.349  1.00 16.47 ? 137 VAL   A O   1 
ATOM   1004 C  CB  . VAL   A 1 131 ? 16.857 5.353   8.265  1.00 15.16 ? 137 VAL   A CB  1 
ATOM   1005 C  CG1 . VAL   A 1 131 ? 16.954 6.176   9.579  1.00 16.64 ? 137 VAL   A CG1 1 
ATOM   1006 C  CG2 . VAL   A 1 131 ? 16.790 3.861   8.569  1.00 15.14 ? 137 VAL   A CG2 1 
ATOM   1007 N  N   . ARG   A 1 132 ? 14.561 4.362   5.700  1.00 15.57 ? 138 ARG   A N   1 
ATOM   1008 C  CA  . ARG   A 1 132 ? 14.530 3.564   4.488  1.00 15.68 ? 138 ARG   A CA  1 
ATOM   1009 C  C   . ARG   A 1 132 ? 14.614 4.358   3.218  1.00 18.12 ? 138 ARG   A C   1 
ATOM   1010 O  O   . ARG   A 1 132 ? 14.960 3.762   2.182  1.00 20.08 ? 138 ARG   A O   1 
ATOM   1011 C  CB  . ARG   A 1 132 ? 13.287 2.687   4.461  1.00 15.08 ? 138 ARG   A CB  1 
ATOM   1012 C  CG  . ARG   A 1 132 ? 13.242 1.689   5.637  1.00 14.73 ? 138 ARG   A CG  1 
ATOM   1013 C  CD  . ARG   A 1 132 ? 11.927 0.929   5.621  1.00 15.26 ? 138 ARG   A CD  1 
ATOM   1014 N  NE  . ARG   A 1 132 ? 10.821 1.824   5.963  1.00 16.77 ? 138 ARG   A NE  1 
ATOM   1015 C  CZ  . ARG   A 1 132 ? 9.563  1.433   6.090  1.00 17.27 ? 138 ARG   A CZ  1 
ATOM   1016 N  NH1 . ARG   A 1 132 ? 9.202  0.188   5.749  1.00 17.11 ? 138 ARG   A NH1 1 
ATOM   1017 N  NH2 . ARG   A 1 132 ? 8.637  2.281   6.528  1.00 16.72 ? 138 ARG   A NH2 1 
ATOM   1018 N  N   . ASP   A 1 133 ? 14.274 5.650   3.251  1.00 17.17 ? 139 ASP   A N   1 
ATOM   1019 C  CA  . ASP   A 1 133 ? 14.344 6.480   2.051  1.00 17.71 ? 139 ASP   A CA  1 
ATOM   1020 C  C   . ASP   A 1 133 ? 15.758 7.023   1.828  1.00 19.47 ? 139 ASP   A C   1 
ATOM   1021 O  O   . ASP   A 1 133 ? 15.985 7.634   0.770  1.00 21.35 ? 139 ASP   A O   1 
ATOM   1022 C  CB  . ASP   A 1 133 ? 13.317 7.618   2.136  1.00 19.39 ? 139 ASP   A CB  1 
ATOM   1023 C  CG  . ASP   A 1 133 ? 13.636 8.626   3.205  1.00 23.74 ? 139 ASP   A CG  1 
ATOM   1024 O  OD1 . ASP   A 1 133 ? 14.053 8.205   4.311  1.00 20.84 ? 139 ASP   A OD1 1 
ATOM   1025 O  OD2 . ASP   A 1 133 ? 13.470 9.866   2.937  1.00 25.20 ? 139 ASP   A OD2 1 
ATOM   1026 N  N   . LEU   A 1 134 ? 16.708 6.844   2.778  1.00 18.60 ? 140 LEU   A N   1 
ATOM   1027 C  CA  . LEU   A 1 134 ? 18.046 7.442   2.629  1.00 18.78 ? 140 LEU   A CA  1 
ATOM   1028 C  C   . LEU   A 1 134 ? 18.927 6.435   1.903  1.00 19.18 ? 140 LEU   A C   1 
ATOM   1029 O  O   . LEU   A 1 134 ? 19.733 5.707   2.499  1.00 19.15 ? 140 LEU   A O   1 
ATOM   1030 C  CB  . LEU   A 1 134 ? 18.594 7.749   4.033  1.00 17.50 ? 140 LEU   A CB  1 
ATOM   1031 C  CG  . LEU   A 1 134 ? 17.714 8.712   4.867  1.00 19.76 ? 140 LEU   A CG  1 
ATOM   1032 C  CD1 . LEU   A 1 134 ? 18.282 8.877   6.337  1.00 20.07 ? 140 LEU   A CD1 1 
ATOM   1033 C  CD2 . LEU   A 1 134 ? 17.610 10.100  4.200  1.00 21.87 ? 140 LEU   A CD2 1 
ATOM   1034 N  N   . LEU   A 1 135 ? 18.723 6.357   0.571  1.00 18.82 ? 141 LEU   A N   1 
ATOM   1035 C  CA  . LEU   A 1 135 ? 19.398 5.323   -0.215 1.00 19.43 ? 141 LEU   A CA  1 
ATOM   1036 C  C   . LEU   A 1 135 ? 20.884 5.432   -0.242 1.00 22.14 ? 141 LEU   A C   1 
ATOM   1037 O  O   . LEU   A 1 135 ? 21.580 4.413   -0.346 1.00 23.06 ? 141 LEU   A O   1 
ATOM   1038 C  CB  . LEU   A 1 135 ? 18.861 5.249   -1.662 1.00 20.55 ? 141 LEU   A CB  1 
ATOM   1039 C  CG  . LEU   A 1 135 ? 17.347 5.125   -1.852 1.00 22.73 ? 141 LEU   A CG  1 
ATOM   1040 C  CD1 . LEU   A 1 135 ? 17.049 4.833   -3.328 1.00 23.97 ? 141 LEU   A CD1 1 
ATOM   1041 C  CD2 . LEU   A 1 135 ? 16.682 4.050   -0.962 1.00 22.64 ? 141 LEU   A CD2 1 
ATOM   1042 N  N   . TRP   A 1 136 ? 21.392 6.683   -0.120 1.00 21.58 ? 142 TRP   A N   1 
ATOM   1043 C  CA  . TRP   A 1 136 ? 22.811 6.979   -0.136 1.00 22.26 ? 142 TRP   A CA  1 
ATOM   1044 C  C   . TRP   A 1 136 ? 23.559 6.333   1.040  1.00 22.54 ? 142 TRP   A C   1 
ATOM   1045 O  O   . TRP   A 1 136 ? 24.779 6.234   0.977  1.00 23.50 ? 142 TRP   A O   1 
ATOM   1046 C  CB  . TRP   A 1 136 ? 23.038 8.500   -0.214 1.00 21.90 ? 142 TRP   A CB  1 
ATOM   1047 C  CG  . TRP   A 1 136 ? 22.356 9.281   0.871  1.00 21.36 ? 142 TRP   A CG  1 
ATOM   1048 C  CD1 . TRP   A 1 136 ? 21.132 9.886   0.817  1.00 21.32 ? 142 TRP   A CD1 1 
ATOM   1049 C  CD2 . TRP   A 1 136 ? 22.849 9.484   2.208  1.00 20.91 ? 142 TRP   A CD2 1 
ATOM   1050 N  NE1 . TRP   A 1 136 ? 20.845 10.476  2.029  1.00 21.98 ? 142 TRP   A NE1 1 
ATOM   1051 C  CE2 . TRP   A 1 136 ? 21.922 10.314  2.870  1.00 21.52 ? 142 TRP   A CE2 1 
ATOM   1052 C  CE3 . TRP   A 1 136 ? 24.055 9.169   2.852  1.00 21.94 ? 142 TRP   A CE3 1 
ATOM   1053 C  CZ2 . TRP   A 1 136 ? 22.108 10.721  4.192  1.00 22.42 ? 142 TRP   A CZ2 1 
ATOM   1054 C  CZ3 . TRP   A 1 136 ? 24.238 9.565   4.165  1.00 23.35 ? 142 TRP   A CZ3 1 
ATOM   1055 C  CH2 . TRP   A 1 136 ? 23.271 10.329  4.818  1.00 22.41 ? 142 TRP   A CH2 1 
ATOM   1056 N  N   . LEU   A 1 137 ? 22.849 5.873   2.115  1.00 23.05 ? 143 LEU   A N   1 
ATOM   1057 C  CA  . LEU   A 1 137 ? 23.526 5.187   3.223  1.00 24.82 ? 143 LEU   A CA  1 
ATOM   1058 C  C   . LEU   A 1 137 ? 24.127 3.838   2.762  1.00 29.72 ? 143 LEU   A C   1 
ATOM   1059 O  O   . LEU   A 1 137 ? 25.036 3.347   3.439  1.00 31.62 ? 143 LEU   A O   1 
ATOM   1060 C  CB  . LEU   A 1 137 ? 22.572 4.892   4.388  1.00 22.93 ? 143 LEU   A CB  1 
ATOM   1061 C  CG  . LEU   A 1 137 ? 22.035 6.055   5.195  1.00 21.38 ? 143 LEU   A CG  1 
ATOM   1062 C  CD1 . LEU   A 1 137 ? 20.918 5.555   6.133  1.00 22.42 ? 143 LEU   A CD1 1 
ATOM   1063 C  CD2 . LEU   A 1 137 ? 23.137 6.666   6.087  1.00 21.85 ? 143 LEU   A CD2 1 
ATOM   1064 N  N   . ASP   A 1 138 ? 23.636 3.266   1.621  1.00 31.45 ? 144 ASP   A N   1 
ATOM   1065 C  CA  . ASP   A 1 138 ? 24.052 1.983   1.031  1.00 34.43 ? 144 ASP   A CA  1 
ATOM   1066 C  C   . ASP   A 1 138 ? 25.312 2.091   0.167  1.00 37.48 ? 144 ASP   A C   1 
ATOM   1067 O  O   . ASP   A 1 138 ? 25.801 1.062   -0.304 1.00 38.13 ? 144 ASP   A O   1 
ATOM   1068 C  CB  . ASP   A 1 138 ? 22.933 1.412   0.139  1.00 35.65 ? 144 ASP   A CB  1 
ATOM   1069 C  CG  . ASP   A 1 138 ? 21.688 0.919   0.835  1.00 38.93 ? 144 ASP   A CG  1 
ATOM   1070 O  OD1 . ASP   A 1 138 ? 21.713 0.789   2.070  1.00 39.32 ? 144 ASP   A OD1 1 
ATOM   1071 O  OD2 . ASP   A 1 138 ? 20.678 0.649   0.128  1.00 40.57 ? 144 ASP   A OD2 1 
ATOM   1072 N  N   . GLU   A 1 139 ? 25.804 3.317   -0.106 1.00 39.19 ? 145 GLU   A N   1 
ATOM   1073 C  CA  . GLU   A 1 139 ? 26.997 3.525   -0.916 1.00 42.27 ? 145 GLU   A CA  1 
ATOM   1074 C  C   . GLU   A 1 139 ? 27.904 4.584   -0.289 1.00 43.87 ? 145 GLU   A C   1 
ATOM   1075 O  O   . GLU   A 1 139 ? 28.863 5.022   -0.935 1.00 45.49 ? 145 GLU   A O   1 
ATOM   1076 C  CB  . GLU   A 1 139 ? 26.613 3.934   -2.342 1.00 46.31 ? 145 GLU   A CB  1 
ATOM   1077 C  CG  . GLU   A 1 139 ? 25.867 5.256   -2.411 1.00 53.03 ? 145 GLU   A CG  1 
ATOM   1078 C  CD  . GLU   A 1 139 ? 24.711 5.211   -3.388 1.00 62.26 ? 145 GLU   A CD  1 
ATOM   1079 O  OE1 . GLU   A 1 139 ? 24.468 6.223   -4.086 1.00 64.39 ? 145 GLU   A OE1 1 
ATOM   1080 O  OE2 . GLU   A 1 139 ? 24.055 4.147   -3.460 1.00 65.48 ? 145 GLU   A OE2 1 
HETATM 1081 N  N1  . A1BN5 B 2 .   ? 13.890 15.804  22.177 1.00 22.08 ? 201 A1BN5 A N1  1 
HETATM 1082 C  C4  . A1BN5 B 2 .   ? 7.984  11.626  25.799 1.00 25.95 ? 201 A1BN5 A C4  1 
HETATM 1083 C  C5  . A1BN5 B 2 .   ? 8.824  12.421  25.034 1.00 24.61 ? 201 A1BN5 A C5  1 
HETATM 1084 C  C6  . A1BN5 B 2 .   ? 9.699  11.823  24.123 1.00 23.82 ? 201 A1BN5 A C6  1 
HETATM 1085 C  C7  . A1BN5 B 2 .   ? 11.842 12.905  23.397 1.00 22.62 ? 201 A1BN5 A C7  1 
HETATM 1086 C  C8  . A1BN5 B 2 .   ? 12.402 13.936  22.469 1.00 21.71 ? 201 A1BN5 A C8  1 
HETATM 1087 C  C10 . A1BN5 B 2 .   ? 13.502 15.874  20.899 1.00 21.93 ? 201 A1BN5 A C10 1 
HETATM 1088 C  C13 . A1BN5 B 2 .   ? 12.012 14.030  21.136 1.00 21.51 ? 201 A1BN5 A C13 1 
HETATM 1089 O  O1  . A1BN5 B 2 .   ? 12.380 16.305  18.352 1.00 23.85 ? 201 A1BN5 A O1  1 
HETATM 1090 C  C12 . A1BN5 B 2 .   ? 12.191 15.197  18.884 1.00 22.28 ? 201 A1BN5 A C12 1 
HETATM 1091 N  N2  . A1BN5 B 2 .   ? 11.657 14.149  18.224 1.00 20.01 ? 201 A1BN5 A N2  1 
HETATM 1092 C  C11 . A1BN5 B 2 .   ? 12.570 15.014  20.325 1.00 21.32 ? 201 A1BN5 A C11 1 
HETATM 1093 C  C9  . A1BN5 B 2 .   ? 13.347 14.845  22.933 1.00 22.76 ? 201 A1BN5 A C9  1 
HETATM 1094 O  O   . A1BN5 B 2 .   ? 12.561 12.344  24.213 1.00 22.23 ? 201 A1BN5 A O   1 
HETATM 1095 N  N   . A1BN5 B 2 .   ? 10.510 12.655  23.295 1.00 23.76 ? 201 A1BN5 A N   1 
HETATM 1096 C  C1  . A1BN5 B 2 .   ? 9.748  10.420  23.983 1.00 24.31 ? 201 A1BN5 A C1  1 
HETATM 1097 C  C   . A1BN5 B 2 .   ? 10.691 9.730   23.032 1.00 23.83 ? 201 A1BN5 A C   1 
HETATM 1098 C  C3  . A1BN5 B 2 .   ? 8.006  10.254  25.654 1.00 25.38 ? 201 A1BN5 A C3  1 
HETATM 1099 C  C2  . A1BN5 B 2 .   ? 8.879  9.660   24.764 1.00 24.81 ? 201 A1BN5 A C2  1 
HETATM 1100 ZN ZN  . ZN    C 3 .   ? 10.742 -4.697  5.481  1.00 18.84 2 202 ZN    A ZN  1 
HETATM 1101 S  S   . DMS   D 4 .   ? 19.472 -0.562  19.994 1.00 38.20 ? 203 DMS   A S   1 
HETATM 1102 O  O   . DMS   D 4 .   ? 18.075 -0.856  19.544 1.00 31.06 ? 203 DMS   A O   1 
HETATM 1103 C  C1  . DMS   D 4 .   ? 19.545 -0.025  21.712 1.00 38.38 ? 203 DMS   A C1  1 
HETATM 1104 C  C2  . DMS   D 4 .   ? 20.135 0.940   19.188 1.00 38.07 ? 203 DMS   A C2  1 
HETATM 1105 O  O   . HOH   E 5 .   ? 12.644 6.778   31.001 1.00 37.09 ? 301 HOH   A O   1 
HETATM 1106 O  O   . HOH   E 5 .   ? 35.878 14.796  16.753 1.00 37.01 ? 302 HOH   A O   1 
HETATM 1107 O  O   . HOH   E 5 .   ? 23.713 -6.445  8.132  1.00 32.86 ? 303 HOH   A O   1 
HETATM 1108 O  O   . HOH   E 5 .   ? 8.163  -3.916  0.414  1.00 27.79 ? 304 HOH   A O   1 
HETATM 1109 O  O   . HOH   E 5 .   ? 4.539  13.547  22.915 1.00 38.31 ? 305 HOH   A O   1 
HETATM 1110 O  O   . HOH   E 5 .   ? 9.897  -4.917  31.664 1.00 32.40 ? 306 HOH   A O   1 
HETATM 1111 O  O   . HOH   E 5 .   ? 12.923 14.642  36.891 1.00 24.58 ? 307 HOH   A O   1 
HETATM 1112 O  O   . HOH   E 5 .   ? 10.622 8.307   4.740  1.00 23.65 ? 308 HOH   A O   1 
HETATM 1113 O  O   . HOH   E 5 .   ? 6.937  12.154  32.141 1.00 45.21 ? 309 HOH   A O   1 
HETATM 1114 O  O   . HOH   E 5 .   ? 18.993 -1.521  31.181 1.00 43.81 ? 310 HOH   A O   1 
HETATM 1115 O  O   . HOH   E 5 .   ? 20.238 8.388   19.055 1.00 16.36 ? 311 HOH   A O   1 
HETATM 1116 O  O   . HOH   E 5 .   ? 18.782 -0.961  27.533 1.00 29.44 ? 312 HOH   A O   1 
HETATM 1117 O  O   . HOH   E 5 .   ? 14.950 17.666  14.608 1.00 27.07 ? 313 HOH   A O   1 
HETATM 1118 O  O   . HOH   E 5 .   ? 0.306  19.168  22.963 1.00 41.41 ? 314 HOH   A O   1 
HETATM 1119 O  O   . HOH   E 5 .   ? 27.720 15.380  2.938  1.00 35.09 ? 315 HOH   A O   1 
HETATM 1120 O  O   . HOH   E 5 .   ? 0.727  -2.406  19.805 1.00 29.42 ? 316 HOH   A O   1 
HETATM 1121 O  O   . HOH   E 5 .   ? 30.782 9.350   13.766 1.00 35.39 ? 317 HOH   A O   1 
HETATM 1122 O  O   . HOH   E 5 .   ? 25.950 -2.533  14.494 1.00 36.57 ? 318 HOH   A O   1 
HETATM 1123 O  O   . HOH   E 5 .   ? 26.161 3.422   19.951 1.00 38.75 ? 319 HOH   A O   1 
HETATM 1124 O  O   . HOH   E 5 .   ? 15.785 17.090  16.838 1.00 26.99 ? 320 HOH   A O   1 
HETATM 1125 O  O   . HOH   E 5 .   ? 31.302 19.948  10.861 1.00 40.81 ? 321 HOH   A O   1 
HETATM 1126 O  O   . HOH   E 5 .   ? 23.956 21.282  8.033  1.00 28.52 ? 322 HOH   A O   1 
HETATM 1127 O  O   . HOH   E 5 .   ? 37.571 12.699  11.737 1.00 62.61 ? 323 HOH   A O   1 
HETATM 1128 O  O   . HOH   E 5 .   ? 9.435  17.332  21.024 1.00 35.34 ? 324 HOH   A O   1 
HETATM 1129 O  O   . HOH   E 5 .   ? 2.926  8.261   10.110 1.00 23.59 ? 325 HOH   A O   1 
HETATM 1130 O  O   . HOH   E 5 .   ? 3.552  -4.823  21.079 1.00 24.76 ? 326 HOH   A O   1 
HETATM 1131 O  O   . HOH   E 5 .   ? 0.400  -0.236  16.497 1.00 14.10 ? 327 HOH   A O   1 
HETATM 1132 O  O   . HOH   E 5 .   ? 17.638 -6.929  3.275  1.00 34.68 ? 328 HOH   A O   1 
HETATM 1133 O  O   . HOH   E 5 .   ? 11.839 8.365   31.462 1.00 28.87 ? 329 HOH   A O   1 
HETATM 1134 O  O   . HOH   E 5 .   ? 5.899  7.707   28.311 1.00 39.31 ? 330 HOH   A O   1 
HETATM 1135 O  O   . HOH   E 5 .   ? 22.158 18.392  17.764 1.00 30.63 ? 331 HOH   A O   1 
HETATM 1136 O  O   . HOH   E 5 .   ? 10.626 17.603  5.969  1.00 41.42 ? 332 HOH   A O   1 
HETATM 1137 O  O   . HOH   E 5 .   ? -0.105 2.093   24.384 1.00 24.47 ? 333 HOH   A O   1 
HETATM 1138 O  O   . HOH   E 5 .   ? 2.913  3.588   27.522 1.00 30.31 ? 334 HOH   A O   1 
HETATM 1139 O  O   . HOH   E 5 .   ? 4.455  7.563   3.278  1.00 32.44 ? 335 HOH   A O   1 
HETATM 1140 O  O   . HOH   E 5 .   ? 9.010  14.301  28.440 1.00 30.57 ? 336 HOH   A O   1 
HETATM 1141 O  O   . HOH   E 5 .   ? 11.419 11.555  11.597 1.00 16.19 ? 337 HOH   A O   1 
HETATM 1142 O  O   . HOH   E 5 .   ? 14.784 2.119   23.285 1.00 16.47 ? 338 HOH   A O   1 
HETATM 1143 O  O   . HOH   E 5 .   ? 10.350 4.836   3.493  1.00 20.47 ? 339 HOH   A O   1 
HETATM 1144 O  O   . HOH   E 5 .   ? 27.628 2.656   2.878  1.00 48.09 ? 340 HOH   A O   1 
HETATM 1145 O  O   . HOH   E 5 .   ? 8.909  2.610   2.858  1.00 23.14 ? 341 HOH   A O   1 
HETATM 1146 O  O   . HOH   E 5 .   ? 29.303 2.590   10.654 1.00 26.77 ? 342 HOH   A O   1 
HETATM 1147 O  O   . HOH   E 5 .   ? 18.192 4.528   27.543 1.00 38.19 ? 343 HOH   A O   1 
HETATM 1148 O  O   . HOH   E 5 .   ? 23.202 17.649  19.625 1.00 41.91 ? 344 HOH   A O   1 
HETATM 1149 O  O   . HOH   E 5 .   ? 5.755  -5.412  28.887 1.00 30.82 ? 345 HOH   A O   1 
HETATM 1150 O  O   . HOH   E 5 .   ? 24.564 10.122  20.941 1.00 36.23 ? 346 HOH   A O   1 
HETATM 1151 O  O   . HOH   E 5 .   ? 26.827 -1.995  6.659  1.00 42.29 ? 347 HOH   A O   1 
HETATM 1152 O  O   . HOH   E 5 .   ? 26.477 17.774  21.142 1.00 38.50 ? 348 HOH   A O   1 
HETATM 1153 O  O   . HOH   E 5 .   ? 4.644  10.154  19.558 1.00 32.50 ? 349 HOH   A O   1 
HETATM 1154 O  O   . HOH   E 5 .   ? 30.260 10.436  19.599 1.00 35.74 ? 350 HOH   A O   1 
HETATM 1155 O  O   . HOH   E 5 .   ? 15.366 12.323  24.244 1.00 23.39 ? 351 HOH   A O   1 
HETATM 1156 O  O   . HOH   E 5 .   ? 5.952  1.699   6.023  1.00 23.41 ? 352 HOH   A O   1 
HETATM 1157 O  O   . HOH   E 5 .   ? 13.248 1.989   0.883  1.00 20.69 ? 353 HOH   A O   1 
HETATM 1158 O  O   . HOH   E 5 .   ? 22.246 -1.164  3.989  1.00 29.16 ? 354 HOH   A O   1 
HETATM 1159 O  O   . HOH   E 5 .   ? 17.365 15.044  25.233 1.00 49.29 ? 355 HOH   A O   1 
HETATM 1160 O  O   . HOH   E 5 .   ? 17.821 1.955   23.235 1.00 20.83 ? 356 HOH   A O   1 
HETATM 1161 O  O   . HOH   E 5 .   ? 15.469 17.988  22.958 1.00 29.36 ? 357 HOH   A O   1 
HETATM 1162 O  O   . HOH   E 5 .   ? 13.853 8.808   29.904 1.00 25.82 ? 358 HOH   A O   1 
HETATM 1163 O  O   . HOH   E 5 .   ? 16.391 -7.328  10.747 1.00 34.05 ? 359 HOH   A O   1 
HETATM 1164 O  O   . HOH   E 5 .   ? 17.517 0.060   30.267 1.00 30.22 ? 360 HOH   A O   1 
HETATM 1165 O  O   . HOH   E 5 .   ? 14.031 20.442  6.821  1.00 42.01 ? 361 HOH   A O   1 
HETATM 1166 O  O   . HOH   E 5 .   ? 18.151 18.438  16.997 1.00 20.21 ? 362 HOH   A O   1 
HETATM 1167 O  O   . HOH   E 5 .   ? 7.388  22.286  15.068 1.00 36.01 ? 363 HOH   A O   1 
HETATM 1168 O  O   . HOH   E 5 .   ? -0.641 -4.688  15.718 0.50 26.84 ? 364 HOH   A O   1 
HETATM 1169 O  O   . HOH   E 5 .   ? 9.362  -8.634  9.133  1.00 37.51 ? 365 HOH   A O   1 
HETATM 1170 O  O   . HOH   E 5 .   ? 6.987  3.547   32.812 1.00 26.77 ? 366 HOH   A O   1 
HETATM 1171 O  O   . HOH   E 5 .   ? 15.032 11.472  1.180  1.00 36.69 ? 367 HOH   A O   1 
HETATM 1172 O  O   . HOH   E 5 .   ? 18.202 20.783  8.984  1.00 21.64 ? 368 HOH   A O   1 
HETATM 1173 O  O   . HOH   E 5 .   ? 19.047 8.629   25.795 1.00 30.62 ? 369 HOH   A O   1 
HETATM 1174 O  O   . HOH   E 5 .   ? 0.122  4.438   6.677  1.00 26.30 ? 370 HOH   A O   1 
HETATM 1175 O  O   . HOH   E 5 .   ? 4.205  5.599   24.950 1.00 25.56 ? 371 HOH   A O   1 
HETATM 1176 O  O   . HOH   E 5 .   ? 16.502 23.437  14.666 1.00 44.05 ? 372 HOH   A O   1 
HETATM 1177 O  O   . HOH   E 5 .   ? 18.922 12.579  1.677  1.00 32.03 ? 373 HOH   A O   1 
HETATM 1178 O  O   . HOH   E 5 .   ? -2.992 7.508   26.019 1.00 33.39 ? 374 HOH   A O   1 
HETATM 1179 O  O   . HOH   E 5 .   ? 13.132 10.392  9.516  1.00 15.62 ? 375 HOH   A O   1 
HETATM 1180 O  O   . HOH   E 5 .   ? 29.847 3.946   3.706  1.00 35.39 ? 376 HOH   A O   1 
HETATM 1181 O  O   . HOH   E 5 .   ? 23.154 -0.676  16.194 1.00 28.33 ? 377 HOH   A O   1 
HETATM 1182 O  O   . HOH   E 5 .   ? 35.245 10.089  10.056 1.00 39.88 ? 378 HOH   A O   1 
HETATM 1183 O  O   . HOH   E 5 .   ? 34.808 10.026  12.556 1.00 62.13 ? 379 HOH   A O   1 
HETATM 1184 O  O   . HOH   E 5 .   ? 3.668  -4.884  6.233  1.00 29.10 ? 380 HOH   A O   1 
HETATM 1185 O  O   . HOH   E 5 .   ? 14.156 18.572  18.551 1.00 53.69 ? 381 HOH   A O   1 
HETATM 1186 O  O   . HOH   E 5 .   ? 36.482 -1.516  10.301 1.00 48.38 ? 382 HOH   A O   1 
HETATM 1187 O  O   . HOH   E 5 .   ? 31.569 8.164   5.574  1.00 37.58 ? 383 HOH   A O   1 
HETATM 1188 O  O   . HOH   E 5 .   ? 31.358 19.906  16.880 1.00 28.79 ? 384 HOH   A O   1 
HETATM 1189 O  O   . HOH   E 5 .   ? 6.751  13.062  5.850  1.00 24.34 ? 385 HOH   A O   1 
HETATM 1190 O  O   . HOH   E 5 .   ? 24.532 6.809   20.422 1.00 35.04 ? 386 HOH   A O   1 
HETATM 1191 O  O   . HOH   E 5 .   ? 11.711 -7.935  12.913 1.00 29.77 ? 387 HOH   A O   1 
HETATM 1192 O  O   . HOH   E 5 .   ? 37.191 15.524  11.744 1.00 36.04 ? 388 HOH   A O   1 
HETATM 1193 O  O   . HOH   E 5 .   ? 3.389  0.558   30.181 1.00 42.12 ? 389 HOH   A O   1 
HETATM 1194 O  O   . HOH   E 5 .   ? 5.040  -1.464  24.048 1.00 18.11 ? 390 HOH   A O   1 
HETATM 1195 O  O   . HOH   E 5 .   ? 30.331 10.280  17.402 1.00 34.19 ? 391 HOH   A O   1 
HETATM 1196 O  O   . HOH   E 5 .   ? 9.760  4.386   33.848 1.00 23.87 ? 392 HOH   A O   1 
HETATM 1197 O  O   . HOH   E 5 .   ? 7.597  -7.110  8.360  1.00 31.72 ? 393 HOH   A O   1 
HETATM 1198 O  O   . HOH   E 5 .   ? 14.493 -4.554  17.275 1.00 23.39 ? 394 HOH   A O   1 
HETATM 1199 O  O   . HOH   E 5 .   ? 32.335 15.263  7.167  1.00 47.98 ? 395 HOH   A O   1 
HETATM 1200 O  O   . HOH   E 5 .   ? 28.209 -2.519  13.173 1.00 47.64 ? 396 HOH   A O   1 
HETATM 1201 O  O   . HOH   E 5 .   ? 2.328  13.554  5.435  1.00 38.17 ? 397 HOH   A O   1 
HETATM 1202 O  O   . HOH   E 5 .   ? 0.927  -2.921  17.150 1.00 24.96 ? 398 HOH   A O   1 
HETATM 1203 O  O   . HOH   E 5 .   ? 3.784  -2.177  21.780 1.00 24.26 ? 399 HOH   A O   1 
HETATM 1204 O  O   . HOH   E 5 .   ? 4.990  13.369  29.958 1.00 38.51 ? 400 HOH   A O   1 
HETATM 1205 O  O   . HOH   E 5 .   ? 7.135  16.231  23.657 1.00 41.20 ? 401 HOH   A O   1 
HETATM 1206 O  O   . HOH   E 5 .   ? 11.121 10.356  1.138  1.00 37.68 ? 402 HOH   A O   1 
HETATM 1207 O  O   . HOH   E 5 .   ? 31.024 1.924   12.733 1.00 26.97 ? 403 HOH   A O   1 
HETATM 1208 O  O   . HOH   E 5 .   ? 15.465 -4.628  1.479  1.00 26.81 ? 404 HOH   A O   1 
HETATM 1209 O  O   . HOH   E 5 .   ? 34.486 4.576   14.011 1.00 43.49 ? 405 HOH   A O   1 
HETATM 1210 O  O   . HOH   E 5 .   ? 6.368  -3.722  -1.738 1.00 55.56 ? 406 HOH   A O   1 
HETATM 1211 O  O   . HOH   E 5 .   ? 31.948 14.084  21.294 1.00 26.98 ? 407 HOH   A O   1 
HETATM 1212 O  O   . HOH   E 5 .   ? 23.599 1.729   19.636 1.00 29.91 ? 408 HOH   A O   1 
HETATM 1213 O  O   . HOH   E 5 .   ? 11.309 18.675  19.957 1.00 40.49 ? 409 HOH   A O   1 
HETATM 1214 O  O   . HOH   E 5 .   ? 22.715 18.269  5.753  1.00 29.60 ? 410 HOH   A O   1 
HETATM 1215 O  O   . HOH   E 5 .   ? 20.031 23.127  15.525 1.00 25.75 ? 411 HOH   A O   1 
HETATM 1216 O  O   . HOH   E 5 .   ? 18.269 18.909  5.294  1.00 46.90 ? 412 HOH   A O   1 
HETATM 1217 O  O   . HOH   E 5 .   ? 7.514  13.060  21.927 1.00 38.83 ? 413 HOH   A O   1 
HETATM 1218 O  O   . HOH   E 5 .   ? 22.058 8.248   21.221 1.00 24.11 ? 414 HOH   A O   1 
HETATM 1219 O  O   . HOH   E 5 .   ? 0.462  -3.050  9.706  1.00 41.96 ? 415 HOH   A O   1 
HETATM 1220 O  O   . HOH   E 5 .   ? 29.073 15.793  23.193 1.00 36.23 ? 416 HOH   A O   1 
HETATM 1221 O  O   . HOH   E 5 .   ? 16.785 -3.325  18.061 1.00 40.80 ? 417 HOH   A O   1 
HETATM 1222 O  O   . HOH   E 5 .   ? 4.486  -1.649  28.963 1.00 47.07 ? 418 HOH   A O   1 
HETATM 1223 O  O   . HOH   E 5 .   ? 26.233 8.901   21.828 1.00 39.88 ? 419 HOH   A O   1 
HETATM 1224 O  O   . HOH   E 5 .   ? 8.906  15.057  21.952 1.00 40.45 ? 420 HOH   A O   1 
HETATM 1225 O  O   . HOH   E 5 .   ? 18.115 8.845   -1.383 1.00 26.36 ? 421 HOH   A O   1 
HETATM 1226 O  O   . HOH   E 5 .   ? 7.161  10.895  4.216  1.00 55.89 ? 422 HOH   A O   1 
HETATM 1227 O  O   . HOH   E 5 .   ? 7.334  -5.489  31.398 1.00 32.33 ? 423 HOH   A O   1 
HETATM 1228 O  O   . HOH   E 5 .   ? 7.064  -5.456  2.711  1.00 28.21 ? 424 HOH   A O   1 
HETATM 1229 O  O   . HOH   E 5 .   ? 17.366 10.761  25.819 1.00 40.43 ? 425 HOH   A O   1 
HETATM 1230 O  O   . HOH   E 5 .   ? 31.877 18.231  8.896  1.00 41.20 ? 426 HOH   A O   1 
HETATM 1231 O  O   . HOH   E 5 .   ? 8.552  22.135  27.023 1.00 54.05 ? 427 HOH   A O   1 
HETATM 1232 O  O   . HOH   E 5 .   ? 4.501  -5.422  -0.616 1.00 73.60 ? 428 HOH   A O   1 
HETATM 1233 O  O   . HOH   E 5 .   ? 34.097 10.201  19.478 1.00 47.99 ? 429 HOH   A O   1 
HETATM 1234 O  O   . HOH   E 5 .   ? 17.666 10.791  0.368  1.00 34.48 ? 430 HOH   A O   1 
HETATM 1235 O  O   . HOH   E 5 .   ? 21.388 21.411  17.729 1.00 31.73 ? 431 HOH   A O   1 
HETATM 1236 O  O   . HOH   E 5 .   ? 29.285 8.540   21.096 1.00 44.39 ? 432 HOH   A O   1 
HETATM 1237 O  O   . HOH   E 5 .   ? 36.790 3.294   15.363 1.00 75.32 ? 433 HOH   A O   1 
HETATM 1238 O  O   . HOH   E 5 .   ? 0.651  -1.548  23.629 1.00 35.35 ? 434 HOH   A O   1 
HETATM 1239 O  O   . HOH   E 5 .   ? 6.289  2.769   3.448  1.00 28.09 ? 435 HOH   A O   1 
HETATM 1240 O  O   . HOH   E 5 .   ? 8.796  19.645  7.245  1.00 51.30 ? 436 HOH   A O   1 
HETATM 1241 O  O   . HOH   E 5 .   ? 12.637 19.632  21.850 1.00 42.69 ? 437 HOH   A O   1 
HETATM 1242 O  O   . HOH   E 5 .   ? 1.568  1.570   26.491 1.00 32.17 ? 438 HOH   A O   1 
HETATM 1243 O  O   . HOH   E 5 .   ? 17.643 17.383  24.350 1.00 43.92 ? 439 HOH   A O   1 
HETATM 1244 O  O   . HOH   E 5 .   ? 34.608 19.318  18.314 1.00 34.06 ? 440 HOH   A O   1 
HETATM 1245 O  O   . HOH   E 5 .   ? 8.621  6.924   2.701  1.00 31.47 ? 441 HOH   A O   1 
HETATM 1246 O  O   . HOH   E 5 .   ? 15.447 25.723  9.613  1.00 49.19 ? 442 HOH   A O   1 
HETATM 1247 O  O   . HOH   E 5 .   ? 33.005 21.245  14.999 1.00 35.31 ? 443 HOH   A O   1 
HETATM 1248 O  O   . HOH   E 5 .   ? 22.499 9.506   23.730 1.00 35.34 ? 444 HOH   A O   1 
HETATM 1249 O  O   . HOH   E 5 .   ? 31.949 3.381   14.828 1.00 34.31 ? 445 HOH   A O   1 
HETATM 1250 O  O   . HOH   E 5 .   ? 8.310  11.997  29.946 1.00 36.96 ? 446 HOH   A O   1 
HETATM 1251 O  O   . HOH   E 5 .   ? 18.326 19.719  19.536 1.00 39.85 ? 447 HOH   A O   1 
HETATM 1252 O  O   . HOH   E 5 .   ? 1.335  -5.515  0.355  1.00 69.89 ? 448 HOH   A O   1 
HETATM 1253 O  O   . HOH   E 5 .   ? 35.609 20.417  16.002 1.00 42.95 ? 449 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   ? 0.2944 0.2756 0.2966 0.0007  -0.0296 -0.0146 7   SER   A N   
2    C CA  . SER   A 1   ? 0.2942 0.2800 0.3090 0.0028  -0.0320 -0.0140 7   SER   A CA  
3    C C   . SER   A 1   ? 0.2936 0.2820 0.3158 0.0058  -0.0312 -0.0117 7   SER   A C   
4    O O   . SER   A 1   ? 0.3149 0.3009 0.3318 0.0060  -0.0306 -0.0098 7   SER   A O   
5    C CB  . SER   A 1   ? 0.3410 0.3270 0.3567 0.0008  -0.0394 -0.0133 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.4116 0.3950 0.4215 -0.0001 -0.0449 -0.0098 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.2643 0.2573 0.2981 0.0074  -0.0302 -0.0123 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.2523 0.2472 0.2930 0.0095  -0.0283 -0.0114 8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.2329 0.2323 0.2819 0.0096  -0.0239 -0.0131 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.2475 0.2480 0.2955 0.0084  -0.0215 -0.0139 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.2031 0.2047 0.2604 0.0108  -0.0223 -0.0136 9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.2069 0.2126 0.2706 0.0097  -0.0174 -0.0154 9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.2005 0.2059 0.2664 0.0098  -0.0130 -0.0166 9   ALA   A C   
14   O O   . ALA   A 3   ? 0.2193 0.2215 0.2860 0.0117  -0.0143 -0.0161 9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.2108 0.2210 0.2857 0.0098  -0.0191 -0.0167 9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1826 0.1908 0.2493 0.0071  -0.0077 -0.0182 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1968 0.2046 0.2651 0.0057  -0.0022 -0.0207 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.2039 0.2160 0.2847 0.0056  0.0010  -0.0239 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.2126 0.2288 0.2960 0.0036  0.0015  -0.0241 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1960 0.2038 0.2543 0.0009  0.0017  -0.0202 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.2047 0.2102 0.2531 0.0008  -0.0013 -0.0167 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.2106 0.2168 0.2681 -0.0018 0.0078  -0.0238 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2067 0.2144 0.2484 -0.0038 0.0006  -0.0146 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.2224 0.2336 0.3119 0.0074  0.0040  -0.0268 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.2235 0.2394 0.3273 0.0076  0.0083  -0.0304 11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.2423 0.2568 0.3445 0.0040  0.0177  -0.0353 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.2621 0.2719 0.3666 0.0058  0.0202  -0.0374 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2209 0.2379 0.3409 0.0132  0.0039  -0.0298 11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2264 0.2453 0.3465 0.0149  -0.0054 -0.0254 11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2272 0.2525 0.3547 0.0137  -0.0068 -0.0256 11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2486 0.2625 0.3595 0.0165  -0.0120 -0.0215 11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2327 0.2588 0.3579 0.0139  -0.0149 -0.0224 11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2595 0.2742 0.3670 0.0164  -0.0195 -0.0184 11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2512 0.2717 0.3659 0.0151  -0.0210 -0.0190 11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2552 0.2757 0.3658 0.0143  -0.0283 -0.0166 11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.2364 0.2540 0.3336 -0.0017 0.0229  -0.0371 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.2652 0.2811 0.3576 -0.0071 0.0323  -0.0423 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.2777 0.2995 0.3787 -0.0104 0.0389  -0.0462 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.2784 0.3047 0.3782 -0.0127 0.0366  -0.0436 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.2852 0.2981 0.3576 -0.0133 0.0320  -0.0397 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.2913 0.3078 0.3574 -0.0156 0.0271  -0.0344 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.3032 0.3142 0.3677 -0.0208 0.0413  -0.0450 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.2854 0.3074 0.3975 -0.0103 0.0476  -0.0528 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.2810 0.3094 0.4030 -0.0137 0.0551  -0.0573 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.2738 0.3094 0.4108 -0.0094 0.0489  -0.0541 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.2846 0.3206 0.4330 -0.0022 0.0418  -0.0513 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.2699 0.3106 0.4048 -0.0145 0.0504  -0.0535 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.2715 0.3186 0.4182 -0.0119 0.0443  -0.0503 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.2633 0.3080 0.3957 -0.0130 0.0353  -0.0436 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2612 0.3098 0.3961 -0.0151 0.0329  -0.0416 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.2794 0.3339 0.4366 -0.0165 0.0522  -0.0544 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.3673 0.4262 0.5471 -0.0126 0.0593  -0.0606 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.4002 0.4652 0.6007 -0.0069 0.0549  -0.0596 14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.3721 0.4277 0.5489 -0.0157 0.0702  -0.0670 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.2541 0.2923 0.3731 -0.0115 0.0307  -0.0404 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.2301 0.2656 0.3374 -0.0119 0.0235  -0.0347 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.2219 0.2540 0.3292 -0.0056 0.0156  -0.0319 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.2302 0.2593 0.3388 -0.0023 0.0159  -0.0331 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.2448 0.2764 0.3341 -0.0176 0.0256  -0.0327 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.2759 0.3100 0.3607 -0.0257 0.0324  -0.0341 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.3074 0.3451 0.3961 -0.0284 0.0318  -0.0325 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.3049 0.3373 0.3804 -0.0316 0.0395  -0.0372 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.3386 0.3784 0.4224 -0.0368 0.0382  -0.0334 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.3269 0.3613 0.3955 -0.0406 0.0457  -0.0382 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.3543 0.3926 0.4276 -0.0430 0.0451  -0.0362 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.4008 0.4408 0.4670 -0.0525 0.0513  -0.0369 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1934 0.2248 0.2973 -0.0047 0.0090  -0.0281 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1889 0.2164 0.2888 -0.0004 0.0019  -0.0253 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1777 0.2014 0.2641 -0.0026 0.0004  -0.0219 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1838 0.2083 0.2696 -0.0051 0.0000  -0.0206 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1990 0.2290 0.3083 0.0021  -0.0043 -0.0247 16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.2094 0.2347 0.3107 0.0043  -0.0114 -0.0219 16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.2028 0.2306 0.3125 0.0056  -0.0179 -0.0215 16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.2078 0.2319 0.3087 0.0042  -0.0224 -0.0203 16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2345 0.2542 0.3274 0.0052  -0.0276 -0.0189 16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2266 0.2446 0.3183 0.0078  -0.0297 -0.0175 16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2405 0.2567 0.3258 0.0031  -0.0300 -0.0192 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1731 0.1926 0.2503 -0.0013 -0.0006 -0.0203 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1644 0.1814 0.2321 -0.0026 -0.0021 -0.0168 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1825 0.1963 0.2480 0.0010  -0.0070 -0.0157 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1977 0.2094 0.2615 0.0034  -0.0085 -0.0161 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1845 0.2003 0.2437 -0.0050 0.0007  -0.0157 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1918 0.2067 0.2444 -0.0066 -0.0010 -0.0111 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1958 0.2139 0.2553 -0.0096 0.0064  -0.0181 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1654 0.1778 0.2297 0.0008  -0.0088 -0.0143 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.1723 0.1810 0.2331 0.0032  -0.0124 -0.0144 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.1783 0.1845 0.2352 0.0027  -0.0113 -0.0122 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.1811 0.1886 0.2398 0.0007  -0.0095 -0.0101 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.2014 0.2104 0.2672 0.0032  -0.0157 -0.0163 18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2345 0.2464 0.3066 0.0045  -0.0178 -0.0175 18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.2066 0.2170 0.2774 0.0006  -0.0144 -0.0165 18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.1558 0.1584 0.2081 0.0044  -0.0125 -0.0127 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.1508 0.1508 0.2027 0.0047  -0.0108 -0.0116 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.1567 0.1551 0.2135 0.0035  -0.0111 -0.0127 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.1677 0.1650 0.2248 0.0028  -0.0133 -0.0156 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.1658 0.1618 0.2119 0.0060  -0.0108 -0.0135 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.1666 0.1636 0.2077 0.0068  -0.0103 -0.0121 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.1743 0.1710 0.2114 0.0068  -0.0123 -0.0128 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.1711 0.1695 0.2135 0.0073  -0.0078 -0.0097 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.1556 0.1537 0.2165 0.0028  -0.0094 -0.0098 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.1579 0.1535 0.2237 0.0011  -0.0094 -0.0103 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.1726 0.1623 0.2368 0.0016  -0.0096 -0.0148 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.1821 0.1706 0.2480 -0.0005 -0.0111 -0.0173 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.1443 0.1392 0.2148 0.0006  -0.0081 -0.0052 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.1496 0.1418 0.2253 -0.0020 -0.0081 -0.0045 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.1731 0.1636 0.2538 -0.0019 -0.0077 0.0018  20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.1857 0.1729 0.2713 -0.0048 -0.0079 0.0041  20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.1972 0.1771 0.2872 -0.0041 -0.0070 0.0017  20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.2291 0.2045 0.3181 -0.0011 -0.0054 -0.0037 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.2184 0.1949 0.3126 -0.0073 -0.0073 0.0043  20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.1729 0.1592 0.2332 0.0037  -0.0080 -0.0163 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.1977 0.1776 0.2543 0.0029  -0.0071 -0.0214 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.2183 0.1983 0.2674 0.0008  -0.0109 -0.0248 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.2388 0.2134 0.2831 -0.0016 -0.0111 -0.0292 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.2123 0.1882 0.2674 0.0051  -0.0028 -0.0227 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.2185 0.1970 0.2667 0.0060  -0.0027 -0.0226 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.2215 0.2058 0.2721 0.0077  -0.0028 -0.0179 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.2345 0.2102 0.2728 0.0046  -0.0026 -0.0264 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.2180 0.2024 0.2609 0.0078  -0.0024 -0.0192 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.2426 0.2218 0.2777 0.0059  -0.0023 -0.0240 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.1953 0.1810 0.2439 0.0013  -0.0139 -0.0227 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.2014 0.1885 0.2461 -0.0002 -0.0187 -0.0241 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.1970 0.1894 0.2500 -0.0014 -0.0218 -0.0234 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.2329 0.2279 0.2863 -0.0023 -0.0265 -0.0237 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.2139 0.2026 0.2531 0.0014  -0.0198 -0.0224 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.2438 0.2281 0.2749 0.0019  -0.0165 -0.0234 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.2497 0.2354 0.2754 0.0029  -0.0178 -0.0213 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.2540 0.2319 0.2767 -0.0013 -0.0164 -0.0280 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.1812 0.1754 0.2415 -0.0018 -0.0192 -0.0221 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.1941 0.1939 0.2629 -0.0035 -0.0209 -0.0219 23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.1904 0.1895 0.2605 -0.0066 -0.0249 -0.0246 23  ALA   A C   
132  O O   . ALA   A 17  ? 0.2075 0.2004 0.2730 -0.0086 -0.0247 -0.0270 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.2111 0.2119 0.2850 -0.0046 -0.0171 -0.0198 23  ALA   A CB  
134  N N   . THR   A 18  ? 0.1913 0.1968 0.2683 -0.0072 -0.0285 -0.0244 24  THR   A N   
135  C CA  . THR   A 18  ? 0.2038 0.2109 0.2840 -0.0108 -0.0337 -0.0262 24  THR   A CA  
136  C C   . THR   A 18  ? 0.2083 0.2178 0.2973 -0.0140 -0.0319 -0.0269 24  THR   A C   
137  O O   . THR   A 18  ? 0.2111 0.2217 0.3039 -0.0135 -0.0270 -0.0255 24  THR   A O   
138  C CB  . THR   A 18  ? 0.2158 0.2299 0.3027 -0.0096 -0.0391 -0.0246 24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.2255 0.2470 0.3251 -0.0080 -0.0359 -0.0236 24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.2301 0.2414 0.3086 -0.0067 -0.0410 -0.0230 24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.2115 0.2224 0.3038 -0.0183 -0.0365 -0.0286 25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.2113 0.2254 0.3129 -0.0220 -0.0352 -0.0292 25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.2018 0.2260 0.3164 -0.0204 -0.0328 -0.0273 25  HIS   A C   
144  O O   . HIS   A 19  ? 0.2085 0.2338 0.3274 -0.0222 -0.0279 -0.0269 25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.2525 0.2682 0.3565 -0.0273 -0.0415 -0.0312 25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.3643 0.3700 0.4545 -0.0304 -0.0437 -0.0342 25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.4187 0.4137 0.5008 -0.0305 -0.0381 -0.0363 25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.4036 0.4085 0.4875 -0.0344 -0.0506 -0.0357 25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.4370 0.4245 0.5079 -0.0341 -0.0405 -0.0400 25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.4323 0.4252 0.5024 -0.0372 -0.0482 -0.0398 25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.1898 0.2205 0.3102 -0.0172 -0.0356 -0.0263 26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.2028 0.2424 0.3364 -0.0156 -0.0318 -0.0257 26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.1894 0.2263 0.3177 -0.0139 -0.0243 -0.0250 26  ASN   A C   
154  O O   . ASN   A 20  ? 0.1896 0.2310 0.3246 -0.0157 -0.0188 -0.0254 26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.2255 0.2713 0.3681 -0.0119 -0.0361 -0.0246 26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.3334 0.3881 0.4920 -0.0101 -0.0310 -0.0251 26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.3583 0.4212 0.5314 -0.0126 -0.0302 -0.0261 26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.3593 0.4127 0.5161 -0.0061 -0.0267 -0.0250 26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.1817 0.2113 0.2973 -0.0112 -0.0239 -0.0240 27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.1817 0.2089 0.2916 -0.0105 -0.0180 -0.0227 27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.1815 0.2066 0.2906 -0.0146 -0.0144 -0.0218 27  ASP   A C   
162  O O   . ASP   A 21  ? 0.1945 0.2224 0.3050 -0.0166 -0.0095 -0.0208 27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.1728 0.1930 0.2705 -0.0075 -0.0187 -0.0215 27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.2079 0.2292 0.3046 -0.0039 -0.0209 -0.0214 27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.2094 0.2360 0.3138 -0.0027 -0.0190 -0.0218 27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.2004 0.2170 0.2890 -0.0024 -0.0240 -0.0212 27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.1853 0.2046 0.2911 -0.0164 -0.0168 -0.0221 28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.1808 0.1965 0.2865 -0.0203 -0.0141 -0.0206 28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.1901 0.2126 0.3058 -0.0250 -0.0124 -0.0213 28  TRP   A C   
170  O O   . TRP   A 22  ? 0.2015 0.2236 0.3170 -0.0285 -0.0084 -0.0190 28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.1928 0.1994 0.2937 -0.0210 -0.0164 -0.0216 28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.1925 0.1918 0.2853 -0.0176 -0.0151 -0.0201 28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.2117 0.2074 0.2981 -0.0144 -0.0167 -0.0219 28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.1806 0.1762 0.2720 -0.0174 -0.0120 -0.0159 28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.2021 0.1924 0.2845 -0.0118 -0.0141 -0.0197 28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.1912 0.1819 0.2774 -0.0133 -0.0117 -0.0155 28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.1944 0.1906 0.2885 -0.0207 -0.0098 -0.0118 28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.1887 0.1757 0.2746 -0.0120 -0.0098 -0.0109 28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.2029 0.1948 0.2949 -0.0199 -0.0085 -0.0067 28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.1896 0.1775 0.2787 -0.0153 -0.0088 -0.0061 28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.1918 0.2212 0.3165 -0.0252 -0.0153 -0.0238 29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.2137 0.2513 0.3505 -0.0295 -0.0133 -0.0249 29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2269 0.2716 0.3687 -0.0294 -0.0070 -0.0249 29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2422 0.2928 0.3920 -0.0338 -0.0027 -0.0257 29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.2084 0.2524 0.3555 -0.0297 -0.0191 -0.0270 29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.2070 0.2509 0.3438 -0.0249 -0.0057 -0.0247 30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.1856 0.2346 0.3252 -0.0253 0.0011  -0.0257 30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.1915 0.2338 0.3162 -0.0255 0.0037  -0.0230 30  ASN   A C   
189  O O   . ASN   A 24  ? 0.2002 0.2432 0.3221 -0.0236 0.0067  -0.0239 30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.1907 0.2452 0.3401 -0.0203 0.0001  -0.0281 30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2314 0.2944 0.3980 -0.0208 -0.0027 -0.0298 30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2419 0.3123 0.4199 -0.0240 0.0027  -0.0319 30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2331 0.2951 0.4010 -0.0186 -0.0112 -0.0288 30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.1957 0.2312 0.3120 -0.0277 0.0022  -0.0196 31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.1946 0.2245 0.2990 -0.0279 0.0031  -0.0157 31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.2277 0.2604 0.3276 -0.0328 0.0091  -0.0148 31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2568 0.2923 0.3591 -0.0387 0.0128  -0.0148 31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.1982 0.2209 0.2988 -0.0296 0.0004  -0.0119 31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.2094 0.2265 0.3008 -0.0295 0.0000  -0.0066 31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.2237 0.2384 0.3111 -0.0232 -0.0025 -0.0072 31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.2198 0.2299 0.3114 -0.0316 -0.0018 -0.0026 31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.2158 0.2474 0.3079 -0.0315 0.0102  -0.0140 32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2362 0.2690 0.3203 -0.0373 0.0153  -0.0130 32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2399 0.2673 0.3128 -0.0396 0.0122  -0.0059 32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2748 0.3017 0.3414 -0.0467 0.0139  -0.0019 32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2564 0.2916 0.3396 -0.0352 0.0189  -0.0173 32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2869 0.3219 0.3582 -0.0423 0.0239  -0.0163 32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2641 0.3052 0.3613 -0.0330 0.0224  -0.0236 32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.2202 0.2439 0.2913 -0.0339 0.0074  -0.0039 33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.2038 0.2237 0.2678 -0.0348 0.0042  0.0029  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.1973 0.2134 0.2644 -0.0274 -0.0001 0.0033  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.2025 0.2193 0.2720 -0.0226 -0.0004 -0.0013 33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2141 0.2360 0.2683 -0.0386 0.0063  0.0040  33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2218 0.2415 0.2701 -0.0392 0.0020  0.0113  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2517 0.2706 0.2946 -0.0456 -0.0001 0.0189  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2178 0.2367 0.2655 -0.0339 -0.0009 0.0120  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2510 0.2693 0.2919 -0.0439 -0.0046 0.0247  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2293 0.2478 0.2733 -0.0368 -0.0047 0.0202  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2132 0.2320 0.2635 -0.0275 -0.0008 0.0071  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2267 0.2456 0.2706 -0.0333 -0.0077 0.0229  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2183 0.2363 0.2669 -0.0243 -0.0036 0.0098  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2182 0.2369 0.2640 -0.0273 -0.0066 0.0172  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.1892 0.2009 0.2566 -0.0268 -0.0033 0.0090  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.1927 0.2009 0.2629 -0.0204 -0.0059 0.0091  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.1883 0.1942 0.2585 -0.0208 -0.0085 0.0169  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.1942 0.1990 0.2646 -0.0254 -0.0094 0.0227  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.1835 0.1876 0.2597 -0.0171 -0.0066 0.0049  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.2075 0.2077 0.2881 -0.0203 -0.0068 0.0071  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2233 0.2173 0.3073 -0.0193 -0.0085 0.0130  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2746 0.2655 0.3611 -0.0232 -0.0089 0.0171  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2199 0.2119 0.3051 -0.0146 -0.0092 0.0135  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.1895 0.1949 0.2605 -0.0161 -0.0097 0.0175  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.1980 0.2023 0.2728 -0.0154 -0.0123 0.0250  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.1996 0.2003 0.2811 -0.0087 -0.0119 0.0227  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.1865 0.1891 0.2654 -0.0056 -0.0110 0.0192  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.1970 0.2068 0.2656 -0.0189 -0.0140 0.0298  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.2371 0.2474 0.3110 -0.0197 -0.0181 0.0396  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.2839 0.2902 0.3685 -0.0149 -0.0189 0.0416  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.2522 0.2668 0.3198 -0.0255 -0.0206 0.0454  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.2028 0.1974 0.2928 -0.0068 -0.0120 0.0244  36  SER   A N   
241  C CA  A SER   A 30  ? 0.2331 0.2230 0.3297 -0.0010 -0.0101 0.0210  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.2161 0.2058 0.3132 -0.0010 -0.0101 0.0213  36  SER   A CA  
243  C C   . SER   A 30  ? 0.2413 0.2342 0.3436 0.0022  -0.0107 0.0256  36  SER   A C   
244  O O   . SER   A 30  ? 0.2807 0.2711 0.3874 0.0069  -0.0078 0.0216  36  SER   A O   
245  C CB  A SER   A 30  ? 0.2778 0.2594 0.3824 -0.0001 -0.0091 0.0207  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.2068 0.1884 0.3125 -0.0005 -0.0095 0.0221  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.3449 0.3214 0.4539 0.0048  -0.0057 0.0153  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.1838 0.1647 0.2963 -0.0022 -0.0124 0.0318  36  SER   A OG  
249  N N   . SER   A 31  ? 0.1982 0.1968 0.3002 -0.0009 -0.0142 0.0337  37  SER   A N   
250  C CA  . SER   A 31  ? 0.1940 0.1972 0.3020 0.0016  -0.0155 0.0383  37  SER   A CA  
251  C C   . SER   A 31  ? 0.1881 0.1968 0.2867 0.0012  -0.0145 0.0342  37  SER   A C   
252  O O   . SER   A 31  ? 0.2112 0.2237 0.3145 0.0035  -0.0146 0.0362  37  SER   A O   
253  C CB  . SER   A 31  ? 0.2250 0.2322 0.3373 -0.0023 -0.0209 0.0498  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.3089 0.3208 0.4081 -0.0094 -0.0233 0.0519  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1745 0.1833 0.2614 -0.0014 -0.0133 0.0284  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1675 0.1803 0.2455 -0.0021 -0.0126 0.0250  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1691 0.1786 0.2428 0.0010  -0.0097 0.0164  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1642 0.1757 0.2312 0.0007  -0.0092 0.0137  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1910 0.2068 0.2593 -0.0084 -0.0137 0.0259  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.2109 0.2307 0.2792 -0.0137 -0.0174 0.0349  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.1979 0.2197 0.2545 -0.0211 -0.0170 0.0344  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.1983 0.2223 0.2465 -0.0223 -0.0151 0.0296  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.2002 0.2264 0.2380 -0.0293 -0.0146 0.0298  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2120 0.2396 0.2452 -0.0366 -0.0164 0.0353  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.2088 0.2357 0.2402 -0.0299 -0.0124 0.0252  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.1695 0.1736 0.2459 0.0030  -0.0083 0.0123  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.1646 0.1657 0.2358 0.0046  -0.0068 0.0049  39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.1532 0.1569 0.2176 0.0021  -0.0077 0.0025  39  ASP   A C   
269  O O   . ASP   A 33  ? 0.1544 0.1577 0.2140 0.0033  -0.0076 -0.0017 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.1613 0.1616 0.2307 0.0077  -0.0048 0.0021  39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.1701 0.1663 0.2331 0.0083  -0.0041 -0.0047 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.1999 0.1921 0.2637 0.0078  -0.0043 -0.0077 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.1862 0.1831 0.2428 0.0088  -0.0039 -0.0066 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1588 0.1650 0.2232 -0.0017 -0.0083 0.0050  40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1564 0.1651 0.2169 -0.0040 -0.0077 0.0020  40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1585 0.1667 0.2223 -0.0062 -0.0074 0.0005  40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1641 0.1711 0.2311 -0.0083 -0.0077 0.0040  40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1653 0.1779 0.2209 -0.0081 -0.0072 0.0050  40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1763 0.1903 0.2275 -0.0073 -0.0074 0.0057  40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.2013 0.2187 0.2464 -0.0131 -0.0067 0.0081  40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.1791 0.1915 0.2281 -0.0042 -0.0067 0.0003  40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1490 0.1587 0.2133 -0.0061 -0.0069 -0.0041 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1524 0.1637 0.2213 -0.0088 -0.0061 -0.0059 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1648 0.1803 0.2343 -0.0094 -0.0042 -0.0093 41  LEU   A C   
285  O O   . LEU   A 35  ? 0.1718 0.1872 0.2400 -0.0063 -0.0049 -0.0114 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.1523 0.1605 0.2252 -0.0070 -0.0082 -0.0088 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.1612 0.1716 0.2403 -0.0100 -0.0079 -0.0107 41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.1831 0.1882 0.2645 -0.0103 -0.0095 -0.0114 41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.1848 0.1999 0.2684 -0.0090 -0.0086 -0.0147 41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1641 0.1829 0.2360 -0.0137 -0.0011 -0.0098 42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1664 0.1894 0.2418 -0.0145 0.0023  -0.0138 42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1694 0.1959 0.2543 -0.0161 0.0033  -0.0163 42  VAL   A C   
293  O O   . VAL   A 36  ? 0.1816 0.2081 0.2669 -0.0201 0.0041  -0.0144 42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.1707 0.1951 0.2392 -0.0196 0.0069  -0.0130 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.1849 0.2127 0.2581 -0.0206 0.0122  -0.0185 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.1944 0.2161 0.2539 -0.0189 0.0052  -0.0100 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1650 0.1944 0.2585 -0.0129 0.0025  -0.0199 43  SER   A N   
298  C CA  . SER   A 37  ? 0.1613 0.1959 0.2668 -0.0140 0.0032  -0.0225 43  SER   A CA  
299  C C   . SER   A 37  ? 0.1785 0.2184 0.2925 -0.0141 0.0087  -0.0264 43  SER   A C   
300  O O   . SER   A 37  ? 0.1954 0.2339 0.3062 -0.0123 0.0109  -0.0275 43  SER   A O   
301  C CB  . SER   A 37  ? 0.1754 0.2096 0.2862 -0.0106 -0.0034 -0.0228 43  SER   A CB  
302  O OG  . SER   A 37  ? 0.1854 0.2191 0.2973 -0.0058 -0.0065 -0.0234 43  SER   A OG  
303  N N   . SER   A 38  ? 0.1914 0.2376 0.3174 -0.0165 0.0115  -0.0288 44  SER   A N   
304  C CA  . SER   A 38  ? 0.2224 0.2742 0.3597 -0.0163 0.0180  -0.0333 44  SER   A CA  
305  C C   . SER   A 38  ? 0.2416 0.2973 0.3946 -0.0102 0.0135  -0.0345 44  SER   A C   
306  O O   . SER   A 38  ? 0.2515 0.3078 0.4082 -0.0082 0.0058  -0.0322 44  SER   A O   
307  C CB  . SER   A 38  ? 0.2355 0.2929 0.3785 -0.0227 0.0247  -0.0354 44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2751 0.3362 0.4272 -0.0232 0.0202  -0.0342 44  SER   A OG  
309  N N   . THR   A 39  ? 0.2569 0.3148 0.4193 -0.0076 0.0183  -0.0378 45  THR   A N   
310  C CA  . THR   A 39  ? 0.2693 0.3306 0.4483 -0.0014 0.0137  -0.0379 45  THR   A CA  
311  C C   . THR   A 39  ? 0.2915 0.3609 0.4915 -0.0012 0.0216  -0.0427 45  THR   A C   
312  O O   . THR   A 39  ? 0.2872 0.3566 0.4844 -0.0051 0.0320  -0.0471 45  THR   A O   
313  C CB  . THR   A 39  ? 0.2857 0.3399 0.4578 0.0032  0.0114  -0.0368 45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.3094 0.3615 0.4798 0.0019  0.0211  -0.0411 45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.2785 0.3249 0.4300 0.0026  0.0059  -0.0329 45  THR   A CG2 
316  N N   . THR   A 40  ? 0.3099 0.3858 0.5307 0.0033  0.0166  -0.0418 46  THR   A N   
317  C CA  . THR   A 40  ? 0.3354 0.4196 0.5802 0.0048  0.0242  -0.0464 46  THR   A CA  
318  C C   . THR   A 40  ? 0.3548 0.4342 0.6051 0.0102  0.0276  -0.0483 46  THR   A C   
319  O O   . THR   A 40  ? 0.3700 0.4511 0.6296 0.0095  0.0392  -0.0545 46  THR   A O   
320  C CB  . THR   A 40  ? 0.3570 0.4524 0.6251 0.0061  0.0184  -0.0445 46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.3767 0.4703 0.6416 0.0088  0.0044  -0.0382 46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.3739 0.4756 0.6424 -0.0009 0.0225  -0.0462 46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.3587 0.4317 0.6030 0.0150  0.0184  -0.0436 47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.3719 0.4389 0.6209 0.0200  0.0212  -0.0450 47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.3910 0.4486 0.6174 0.0163  0.0289  -0.0484 47  ALA   A C   
326  O O   . ALA   A 41  ? 0.3902 0.4437 0.5944 0.0121  0.0263  -0.0461 47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.3810 0.4444 0.6311 0.0255  0.0083  -0.0381 47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.3950 0.4490 0.6278 0.0176  0.0383  -0.0537 48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.4168 0.4620 0.6285 0.0131  0.0456  -0.0573 48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.4167 0.4525 0.6153 0.0163  0.0379  -0.0527 48  GLN   A C   
331  O O   . GLN   A 42  ? 0.4202 0.4534 0.6315 0.0226  0.0337  -0.0506 48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.4625 0.5066 0.6852 0.0122  0.0598  -0.0661 48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.5631 0.5990 0.7616 0.0048  0.0683  -0.0706 48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.6622 0.7025 0.8526 -0.0043 0.0779  -0.0754 48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.6883 0.7378 0.8938 -0.0049 0.0810  -0.0770 48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.6924 0.7267 0.8586 -0.0122 0.0825  -0.0772 48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.4037 0.4347 0.5779 0.0117  0.0358  -0.0504 49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.4078 0.4305 0.5683 0.0135  0.0296  -0.0464 49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.4172 0.4320 0.5703 0.0114  0.0379  -0.0512 49  GLY   A C   
340  O O   . GLY   A 43  ? 0.4371 0.4525 0.5891 0.0065  0.0485  -0.0576 49  GLY   A O   
341  N N   . CYS   A 44  ? 0.4061 0.4131 0.5536 0.0143  0.0334  -0.0484 50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.4144 0.4129 0.5552 0.0120  0.0410  -0.0531 50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.3865 0.3790 0.5039 0.0079  0.0377  -0.0500 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.4062 0.3908 0.5177 0.0061  0.0423  -0.0531 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.4503 0.4434 0.6096 0.0185  0.0425  -0.0547 50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.5416 0.5400 0.7247 0.0277  0.0312  -0.0477 50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.3426 0.3386 0.4473 0.0061  0.0306  -0.0445 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.3132 0.3050 0.3985 0.0023  0.0279  -0.0415 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.2836 0.2753 0.3562 -0.0062 0.0358  -0.0457 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.2916 0.2874 0.3677 -0.0096 0.0421  -0.0498 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.3417 0.3371 0.4198 0.0033  0.0189  -0.0348 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.4602 0.4546 0.5447 0.0095  0.0103  -0.0302 51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.5013 0.4910 0.5938 0.0133  0.0095  -0.0303 51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.4321 0.4302 0.5137 0.0102  0.0044  -0.0264 51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.2541 0.2411 0.3117 -0.0105 0.0356  -0.0447 52  THR   A N   
356  C CA  . THR   A 46  ? 0.2612 0.2481 0.3048 -0.0198 0.0413  -0.0475 52  THR   A CA  
357  C C   . THR   A 46  ? 0.2406 0.2307 0.2709 -0.0229 0.0344  -0.0406 52  THR   A C   
358  O O   . THR   A 46  ? 0.2375 0.2256 0.2658 -0.0195 0.0283  -0.0363 52  THR   A O   
359  C CB  . THR   A 46  ? 0.3066 0.2849 0.3448 -0.0232 0.0474  -0.0528 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.3216 0.2971 0.3741 -0.0206 0.0557  -0.0601 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.3309 0.3086 0.3503 -0.0346 0.0515  -0.0547 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.2313 0.2264 0.2542 -0.0291 0.0351  -0.0392 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.2173 0.2159 0.2303 -0.0319 0.0286  -0.0321 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.2268 0.2225 0.2253 -0.0402 0.0302  -0.0325 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.2412 0.2347 0.2327 -0.0476 0.0371  -0.0377 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.2142 0.2189 0.2261 -0.0352 0.0274  -0.0289 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.2233 0.2308 0.2492 -0.0287 0.0265  -0.0294 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.2196 0.2277 0.2248 -0.0370 0.0203  -0.0208 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.2338 0.2409 0.2664 -0.0203 0.0196  -0.0258 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.2097 0.2056 0.2033 -0.0398 0.0244  -0.0273 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.2164 0.2109 0.1967 -0.0482 0.0246  -0.0267 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.2338 0.2337 0.2047 -0.0572 0.0236  -0.0232 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.2223 0.2278 0.1974 -0.0552 0.0195  -0.0179 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.2202 0.2160 0.2004 -0.0451 0.0180  -0.0208 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.2368 0.2343 0.1940 -0.0677 0.0271  -0.0260 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.2466 0.2490 0.1921 -0.0784 0.0251  -0.0217 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.2499 0.2522 0.1842 -0.0857 0.0216  -0.0189 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.2891 0.2860 0.2120 -0.0939 0.0268  -0.0249 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.2577 0.2574 0.1959 -0.0860 0.0338  -0.0287 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.2645 0.2652 0.2162 -0.0785 0.0378  -0.0318 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.2852 0.2928 0.2442 -0.0743 0.0307  -0.0235 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.2860 0.2940 0.2579 -0.0678 0.0349  -0.0276 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.2899 0.3018 0.2719 -0.0615 0.0302  -0.0227 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.2693 0.2846 0.2509 -0.0603 0.0220  -0.0141 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.2961 0.3087 0.2895 -0.0566 0.0340  -0.0268 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.2460 0.2546 0.1844 -0.0832 0.0130  -0.0100 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.2521 0.2619 0.1847 -0.0878 0.0088  -0.0067 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.2571 0.2761 0.1975 -0.0848 -0.0004 0.0039  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.2495 0.2723 0.2003 -0.0780 -0.0030 0.0080  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.2611 0.2638 0.1979 -0.0816 0.0124  -0.0126 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.2382 0.2425 0.1927 -0.0664 0.0089  -0.0094 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.2740 0.2963 0.2110 -0.0895 -0.0048 0.0080  57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.2740 0.3055 0.2215 -0.0860 -0.0126 0.0175  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.2751 0.3053 0.2285 -0.0805 -0.0123 0.0161  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.2824 0.3203 0.2415 -0.0812 -0.0176 0.0229  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.3294 0.3691 0.2705 -0.0972 -0.0199 0.0261  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.4306 0.4688 0.3576 -0.1087 -0.0199 0.0240  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.4556 0.4850 0.3774 -0.1080 -0.0134 0.0151  57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.5036 0.5489 0.4245 -0.1190 -0.0267 0.0314  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.2441 0.2655 0.1984 -0.0742 -0.0063 0.0083  58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.2383 0.2578 0.1975 -0.0691 -0.0061 0.0078  58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.2379 0.2654 0.2106 -0.0617 -0.0104 0.0143  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.2220 0.2524 0.2023 -0.0565 -0.0115 0.0166  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.2434 0.2525 0.2037 -0.0624 -0.0004 0.0002  58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.2694 0.2669 0.2173 -0.0694 0.0064  -0.0089 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.2146 0.2450 0.1902 -0.0617 -0.0119 0.0167  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.2002 0.2370 0.1887 -0.0548 -0.0139 0.0212  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.1913 0.2223 0.1796 -0.0504 -0.0106 0.0174  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.1927 0.2285 0.1891 -0.0469 -0.0110 0.0202  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.2151 0.2639 0.2105 -0.0592 -0.0192 0.0293  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.2384 0.2941 0.2392 -0.0604 -0.0237 0.0354  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.2716 0.3399 0.2833 -0.0634 -0.0297 0.0446  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.2856 0.3593 0.2918 -0.0732 -0.0347 0.0493  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.2482 0.3218 0.2758 -0.0558 -0.0292 0.0471  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.1917 0.2117 0.1714 -0.0506 -0.0068 0.0110  60  THR   A N   
416  C CA  . THR   A 54  ? 0.1967 0.2096 0.1760 -0.0460 -0.0044 0.0083  60  THR   A CA  
417  C C   . THR   A 54  ? 0.1958 0.1993 0.1734 -0.0413 -0.0018 0.0030  60  THR   A C   
418  O O   . THR   A 54  ? 0.2197 0.2203 0.1939 -0.0437 -0.0002 -0.0001 60  THR   A O   
419  C CB  . THR   A 54  ? 0.2343 0.2433 0.2062 -0.0522 -0.0035 0.0074  60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.2937 0.2955 0.2566 -0.0579 -0.0015 0.0029  60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.2367 0.2565 0.2114 -0.0580 -0.0066 0.0129  60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.1860 0.1852 0.1665 -0.0349 -0.0012 0.0022  61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.1868 0.1782 0.1684 -0.0296 0.0001  -0.0017 61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.1835 0.1707 0.1662 -0.0245 -0.0008 -0.0010 61  GLY   A C   
425  O O   . GLY   A 55  ? 0.1965 0.1851 0.1770 -0.0259 -0.0012 0.0014  61  GLY   A O   
426  N N   . VAL   A 56  ? 0.1653 0.1475 0.1508 -0.0193 -0.0012 -0.0030 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.1701 0.1478 0.1552 -0.0153 -0.0030 -0.0019 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.1700 0.1504 0.1607 -0.0104 -0.0046 -0.0024 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.1828 0.1634 0.1783 -0.0089 -0.0042 -0.0046 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.1945 0.1616 0.1780 -0.0147 -0.0031 -0.0033 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.2139 0.1760 0.1964 -0.0112 -0.0065 -0.0010 62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.1976 0.1607 0.1748 -0.0204 -0.0012 -0.0032 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.1641 0.1458 0.1538 -0.0084 -0.0060 -0.0008 63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.1650 0.1480 0.1589 -0.0045 -0.0077 -0.0017 63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.1814 0.1589 0.1714 -0.0029 -0.0107 -0.0010 63  TYR   A C   
436  O O   . TYR   A 57  ? 0.1788 0.1525 0.1618 -0.0050 -0.0109 0.0008  63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.1605 0.1508 0.1578 -0.0041 -0.0064 -0.0013 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.1687 0.1598 0.1624 -0.0046 -0.0052 -0.0004 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.1821 0.1753 0.1732 -0.0077 -0.0031 0.0012  63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.1688 0.1586 0.1616 -0.0026 -0.0056 -0.0018 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.2002 0.1945 0.1886 -0.0085 -0.0007 0.0014  63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.1804 0.1708 0.1695 -0.0038 -0.0029 -0.0021 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.1999 0.1927 0.1872 -0.0066 -0.0001 -0.0006 63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.2180 0.2118 0.2024 -0.0081 0.0039  -0.0015 63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.1770 0.1540 0.1711 0.0001  -0.0133 -0.0019 64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.1792 0.1516 0.1690 0.0007  -0.0173 -0.0006 64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.1796 0.1546 0.1651 -0.0001 -0.0167 -0.0014 64  TYR   A C   
448  O O   . TYR   A 58  ? 0.1904 0.1697 0.1811 0.0013  -0.0154 -0.0034 64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.1806 0.1513 0.1779 0.0037  -0.0215 -0.0007 64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.2099 0.1763 0.2022 0.0034  -0.0272 0.0019  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.2264 0.1861 0.2123 0.0019  -0.0302 0.0055  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.2199 0.1886 0.2137 0.0040  -0.0304 0.0012  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.2465 0.2021 0.2254 0.0002  -0.0363 0.0089  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.2447 0.2096 0.2318 0.0022  -0.0365 0.0039  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.2554 0.2139 0.2345 0.0001  -0.0396 0.0080  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.3052 0.2596 0.2761 -0.0028 -0.0465 0.0118  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.1857 0.1567 0.1610 -0.0028 -0.0173 -0.0001 65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.1901 0.1619 0.1592 -0.0046 -0.0153 -0.0019 65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.2077 0.1741 0.1688 -0.0063 -0.0209 -0.0008 65  CYS   A C   
460  O O   . CYS   A 59  ? 0.2268 0.1879 0.1780 -0.0095 -0.0233 0.0021  65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.2066 0.1791 0.1696 -0.0078 -0.0104 -0.0016 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.2330 0.2054 0.1879 -0.0108 -0.0058 -0.0049 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.2079 0.1756 0.1724 -0.0051 -0.0233 -0.0028 66  SER   A N   
464  C CA  . SER   A 60  ? 0.2324 0.1957 0.1897 -0.0075 -0.0299 -0.0011 66  SER   A CA  
465  C C   . SER   A 60  ? 0.2422 0.2013 0.1830 -0.0133 -0.0284 -0.0019 66  SER   A C   
466  O O   . SER   A 60  ? 0.2629 0.2170 0.1937 -0.0170 -0.0345 0.0016  66  SER   A O   
467  C CB  . SER   A 60  ? 0.2734 0.2397 0.2385 -0.0057 -0.0327 -0.0032 66  SER   A CB  
468  O OG  . SER   A 60  ? 0.3519 0.3196 0.3147 -0.0069 -0.0277 -0.0079 66  SER   A OG  
469  N N   . SER   A 61  ? 0.2293 0.1904 0.1677 -0.0145 -0.0204 -0.0062 67  SER   A N   
470  C CA  . SER   A 61  ? 0.2515 0.2087 0.1744 -0.0206 -0.0169 -0.0082 67  SER   A CA  
471  C C   . SER   A 61  ? 0.2630 0.2168 0.1761 -0.0241 -0.0165 -0.0045 67  SER   A C   
472  O O   . SER   A 61  ? 0.2801 0.2303 0.1787 -0.0302 -0.0135 -0.0058 67  SER   A O   
473  C CB  . SER   A 61  ? 0.2479 0.2082 0.1741 -0.0201 -0.0075 -0.0142 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.2487 0.2144 0.1856 -0.0168 -0.0021 -0.0137 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.2518 0.2061 0.1717 -0.0213 -0.0190 -0.0003 68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.2578 0.2075 0.1686 -0.0249 -0.0198 0.0040  68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.2751 0.2201 0.1886 -0.0233 -0.0288 0.0100  68  ARG   A C   
478  O O   . ARG   A 62  ? 0.2844 0.2238 0.1908 -0.0262 -0.0308 0.0146  68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.2597 0.2139 0.1770 -0.0238 -0.0129 0.0032  68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.2685 0.2278 0.1859 -0.0252 -0.0037 -0.0019 68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.3075 0.2626 0.2085 -0.0325 -0.0004 -0.0020 68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.3087 0.2688 0.2118 -0.0337 0.0098  -0.0074 68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.3190 0.2788 0.2190 -0.0349 0.0141  -0.0129 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.3264 0.2815 0.2201 -0.0355 0.0085  -0.0137 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.3211 0.2856 0.2262 -0.0353 0.0244  -0.0180 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.2679 0.2145 0.1924 -0.0186 -0.0341 0.0104  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.2683 0.2117 0.2011 -0.0155 -0.0414 0.0154  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.2777 0.2191 0.2147 -0.0141 -0.0381 0.0167  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.3108 0.2453 0.2459 -0.0149 -0.0425 0.0219  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.2966 0.2331 0.2190 -0.0196 -0.0505 0.0216  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.3402 0.2786 0.2605 -0.0211 -0.0558 0.0209  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.3916 0.3238 0.3018 -0.0260 -0.0665 0.0283  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.4185 0.3525 0.3227 -0.0297 -0.0714 0.0273  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.4412 0.3707 0.3248 -0.0385 -0.0744 0.0287  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.4422 0.3658 0.3096 -0.0442 -0.0720 0.0309  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 0.4408 0.3718 0.3188 -0.0425 -0.0788 0.0271  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.2480 0.1951 0.1904 -0.0125 -0.0307 0.0125  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.2563 0.2021 0.2013 -0.0126 -0.0272 0.0132  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.2332 0.1855 0.1898 -0.0093 -0.0227 0.0094  70  LYS   A C   
500  O O   . LYS   A 64  ? 0.2223 0.1812 0.1833 -0.0078 -0.0203 0.0062  70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.3328 0.2784 0.2665 -0.0180 -0.0222 0.0133  70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.4250 0.3621 0.3451 -0.0231 -0.0259 0.0182  70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.5045 0.4429 0.4148 -0.0286 -0.0195 0.0175  70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.5850 0.5147 0.4799 -0.0349 -0.0225 0.0226  70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.6437 0.5696 0.5287 -0.0372 -0.0282 0.0244  70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.2247 0.1747 0.1855 -0.0090 -0.0213 0.0098  71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.2094 0.1652 0.1776 -0.0081 -0.0168 0.0066  71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.2241 0.1823 0.1870 -0.0125 -0.0124 0.0069  71  HIS   A C   
509  O O   . HIS   A 65  ? 0.2538 0.2063 0.2093 -0.0158 -0.0127 0.0094  71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.2210 0.1725 0.1967 -0.0062 -0.0171 0.0058  71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.2258 0.1760 0.2104 -0.0017 -0.0207 0.0055  71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.2489 0.2050 0.2430 0.0010  -0.0190 0.0020  71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.2208 0.1650 0.2067 0.0001  -0.0263 0.0088  71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.2124 0.1664 0.2140 0.0045  -0.0232 0.0030  71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.2681 0.2153 0.2658 0.0043  -0.0281 0.0073  71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.1985 0.1654 0.1660 -0.0126 -0.0088 0.0049  72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.2031 0.1745 0.1687 -0.0166 -0.0052 0.0056  72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.2012 0.1775 0.1725 -0.0179 -0.0036 0.0047  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.2004 0.1812 0.1782 -0.0155 -0.0038 0.0033  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.2021 0.1812 0.1692 -0.0165 -0.0023 0.0050  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.2278 0.2027 0.1864 -0.0174 -0.0023 0.0051  72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.2501 0.2215 0.1997 -0.0220 -0.0008 0.0069  72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.2380 0.2124 0.1965 -0.0148 -0.0036 0.0034  72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.2710 0.2385 0.2105 -0.0243 -0.0004 0.0070  72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.2565 0.2267 0.2049 -0.0171 -0.0035 0.0031  72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.2891 0.2559 0.2275 -0.0220 -0.0018 0.0050  72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.3120 0.2747 0.2384 -0.0256 -0.0013 0.0046  72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.2003 0.1759 0.1684 -0.0225 -0.0023 0.0057  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.1966 0.1774 0.1681 -0.0256 -0.0012 0.0051  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.2123 0.2052 0.1898 -0.0265 0.0000  0.0069  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.2406 0.2365 0.2174 -0.0276 0.0017  0.0084  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.2176 0.1923 0.1825 -0.0311 -0.0004 0.0057  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.2257 0.1975 0.1853 -0.0317 -0.0002 0.0080  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.2091 0.1788 0.1692 -0.0263 -0.0019 0.0077  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.1882 0.1878 0.1717 -0.0263 -0.0006 0.0070  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.1857 0.1965 0.1774 -0.0265 -0.0002 0.0098  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.1919 0.2093 0.1865 -0.0308 -0.0020 0.0119  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.1913 0.2048 0.1818 -0.0326 -0.0029 0.0101  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.2103 0.2233 0.2086 -0.0205 -0.0001 0.0090  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.2306 0.2398 0.2264 -0.0176 0.0019  0.0074  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.2251 0.2340 0.2230 -0.0182 -0.0018 0.0069  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.1814 0.2096 0.1841 -0.0328 -0.0026 0.0159  75  SER   A N   
543  C CA  . SER   A 69  ? 0.1808 0.2171 0.1882 -0.0366 -0.0058 0.0196  75  SER   A CA  
544  C C   . SER   A 69  ? 0.1642 0.2056 0.1826 -0.0309 -0.0064 0.0215  75  SER   A C   
545  O O   . SER   A 69  ? 0.1793 0.2219 0.2045 -0.0258 -0.0038 0.0209  75  SER   A O   
546  C CB  . SER   A 69  ? 0.2161 0.2622 0.2289 -0.0418 -0.0070 0.0241  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.3118 0.3530 0.3146 -0.0477 -0.0063 0.0225  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.1578 0.2012 0.1770 -0.0323 -0.0094 0.0233  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.1524 0.1994 0.1819 -0.0273 -0.0103 0.0255  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.1653 0.2207 0.2007 -0.0314 -0.0151 0.0321  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.1778 0.2344 0.2052 -0.0389 -0.0178 0.0337  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.1583 0.1965 0.1829 -0.0230 -0.0087 0.0206  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.1557 0.1882 0.1694 -0.0271 -0.0091 0.0177  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.1849 0.2094 0.1897 -0.0279 -0.0069 0.0130  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.1671 0.2018 0.1800 -0.0305 -0.0112 0.0197  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.1945 0.2134 0.1914 -0.0314 -0.0059 0.0096  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.1821 0.2113 0.1851 -0.0346 -0.0099 0.0159  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.1909 0.2123 0.1868 -0.0348 -0.0069 0.0105  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.1573 0.2179 0.2063 -0.0270 -0.0161 0.0360  77  SER   A N   
560  C CA  . SER   A 71  ? 0.1587 0.2274 0.2152 -0.0304 -0.0217 0.0439  77  SER   A CA  
561  C C   . SER   A 71  ? 0.1713 0.2352 0.2187 -0.0332 -0.0237 0.0436  77  SER   A C   
562  O O   . SER   A 71  ? 0.1844 0.2400 0.2258 -0.0298 -0.0203 0.0375  77  SER   A O   
563  C CB  . SER   A 71  ? 0.1571 0.2321 0.2336 -0.0241 -0.0218 0.0484  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.1749 0.2427 0.2536 -0.0171 -0.0180 0.0439  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.1854 0.2548 0.2314 -0.0403 -0.0295 0.0504  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.1866 0.2522 0.2243 -0.0438 -0.0310 0.0507  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.1927 0.2564 0.2413 -0.0366 -0.0305 0.0521  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.2022 0.2699 0.2668 -0.0306 -0.0310 0.0556  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.2133 0.2855 0.2459 -0.0543 -0.0378 0.0586  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.2425 0.3143 0.2608 -0.0631 -0.0377 0.0558  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.3120 0.3900 0.3228 -0.0753 -0.0450 0.0636  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.3784 0.4542 0.3728 -0.0850 -0.0438 0.0592  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.4297 0.5104 0.4127 -0.0987 -0.0507 0.0658  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.1980 0.2554 0.2388 -0.0372 -0.0289 0.0487  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.2033 0.2579 0.2535 -0.0309 -0.0281 0.0492  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.2013 0.2621 0.2658 -0.0304 -0.0337 0.0595  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.2136 0.2797 0.2753 -0.0379 -0.0395 0.0671  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.2328 0.2818 0.2711 -0.0348 -0.0266 0.0457  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.2475 0.2938 0.2713 -0.0399 -0.0236 0.0395  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.2127 0.2650 0.2365 -0.0438 -0.0268 0.0435  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.1873 0.2475 0.2674 -0.0220 -0.0318 0.0597  80  SER   A N   
582  C CA  . SER   A 74  ? 0.2064 0.2719 0.3037 -0.0203 -0.0366 0.0695  80  SER   A CA  
583  C C   . SER   A 74  ? 0.2133 0.2732 0.3239 -0.0116 -0.0328 0.0672  80  SER   A C   
584  O O   . SER   A 74  ? 0.2026 0.2551 0.3071 -0.0078 -0.0270 0.0579  80  SER   A O   
585  C CB  . SER   A 74  ? 0.2579 0.3333 0.3663 -0.0208 -0.0395 0.0751  80  SER   A CB  
586  O OG  . SER   A 74  ? 0.3297 0.4046 0.4476 -0.0133 -0.0332 0.0692  80  SER   A OG  
587  N N   . LEU   A 75  ? 0.2105 0.2735 0.3393 -0.0089 -0.0364 0.0757  81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.2190 0.2761 0.3622 -0.0011 -0.0328 0.0742  81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.2340 0.2938 0.3924 0.0058  -0.0276 0.0710  81  LEU   A C   
590  O O   . LEU   A 75  ? 0.2489 0.3179 0.4220 0.0061  -0.0307 0.0781  81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.2314 0.2907 0.3882 -0.0023 -0.0399 0.0866  81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.2980 0.3486 0.4610 0.0006  -0.0395 0.0878  81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.3082 0.3619 0.4949 0.0035  -0.0448 0.0999  81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.3195 0.3600 0.4799 0.0066  -0.0305 0.0753  81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.2215 0.2742 0.3755 0.0104  -0.0196 0.0600  82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.2461 0.3004 0.4097 0.0154  -0.0130 0.0548  82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.2594 0.3053 0.4326 0.0220  -0.0059 0.0486  82  ILE   A C   
598  O O   . ILE   A 76  ? 0.2474 0.2843 0.4110 0.0219  -0.0048 0.0439  82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.2726 0.3255 0.4165 0.0125  -0.0099 0.0467  82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.3027 0.3636 0.4386 0.0058  -0.0157 0.0521  82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.2810 0.3322 0.4277 0.0167  -0.0016 0.0386  82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.3331 0.3918 0.4512 0.0027  -0.0137 0.0457  82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.2739 0.3228 0.4658 0.0272  -0.0004 0.0477  83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.2978 0.3380 0.4970 0.0327  0.0083  0.0396  83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.3197 0.3564 0.5026 0.0317  0.0154  0.0284  83  PHE   A C   
606  O O   . PHE   A 77  ? 0.3478 0.3915 0.5313 0.0308  0.0176  0.0278  83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.2909 0.3353 0.5190 0.0386  0.0122  0.0432  83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.3151 0.3484 0.5511 0.0438  0.0214  0.0347  83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.3359 0.3599 0.5746 0.0450  0.0196  0.0359  83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.3364 0.3677 0.5747 0.0461  0.0323  0.0248  83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.3536 0.3661 0.5978 0.0488  0.0285  0.0272  83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.3528 0.3729 0.5960 0.0496  0.0415  0.0159  83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.3519 0.3624 0.5978 0.0509  0.0395  0.0169  83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.3075 0.3336 0.4763 0.0313  0.0185  0.0202  84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.3235 0.3445 0.4745 0.0294  0.0238  0.0102  84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.3288 0.3438 0.4879 0.0328  0.0341  0.0020  84  VAL   A C   
617  O O   . VAL   A 78  ? 0.3152 0.3222 0.4792 0.0349  0.0363  -0.0006 84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.3394 0.3528 0.4717 0.0264  0.0201  0.0068  84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.3578 0.3663 0.4720 0.0240  0.0237  -0.0018 84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.3429 0.3611 0.4687 0.0229  0.0115  0.0139  84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.3419 0.3601 0.5014 0.0327  0.0409  -0.0023 85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.3561 0.3684 0.5226 0.0351  0.0523  -0.0111 85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.3773 0.3768 0.5252 0.0324  0.0560  -0.0211 85  GLU   A C   
624  O O   . GLU   A 79  ? 0.3829 0.3795 0.5095 0.0281  0.0510  -0.0225 85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.3927 0.4116 0.5607 0.0341  0.0592  -0.0140 85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.4490 0.4819 0.6344 0.0355  0.0554  -0.0045 85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.5428 0.5803 0.7592 0.0416  0.0569  0.0009  85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 0.5487 0.5796 0.7767 0.0453  0.0663  -0.0056 85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 0.5680 0.6153 0.7970 0.0423  0.0485  0.0119  85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.3782 0.3699 0.5347 0.0347  0.0652  -0.0283 86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.4026 0.3816 0.5426 0.0313  0.0700  -0.0387 86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.4224 0.4006 0.5405 0.0256  0.0736  -0.0452 86  ALA   A C   
633  O O   . ALA   A 80  ? 0.4228 0.4084 0.5444 0.0254  0.0775  -0.0445 86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.4087 0.3798 0.5649 0.0347  0.0809  -0.0455 86  ALA   A CB  
635  N N   . SER   A 81  ? 0.4289 0.3987 0.5244 0.0204  0.0712  -0.0505 87  SER   A N   
636  C CA  . SER   A 81  ? 0.4349 0.4026 0.5073 0.0140  0.0728  -0.0556 87  SER   A CA  
637  C C   . SER   A 81  ? 0.4499 0.4050 0.5070 0.0088  0.0789  -0.0665 87  SER   A C   
638  O O   . SER   A 81  ? 0.4524 0.4005 0.5184 0.0107  0.0826  -0.0705 87  SER   A O   
639  C CB  . SER   A 81  ? 0.4419 0.4137 0.5000 0.0115  0.0611  -0.0491 87  SER   A CB  
640  O OG  . SER   A 81  ? 0.4491 0.4154 0.5011 0.0106  0.0543  -0.0489 87  SER   A OG  
641  N N   . GLU   A 82  ? 0.4590 0.4105 0.4926 0.0016  0.0798  -0.0712 88  GLU   A N   
642  C CA  . GLU   A 82  ? 0.4709 0.4106 0.4871 -0.0051 0.0853  -0.0816 88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.4738 0.4065 0.4860 -0.0061 0.0787  -0.0824 88  GLU   A C   
644  O O   . GLU   A 82  ? 0.4710 0.3938 0.4812 -0.0086 0.0854  -0.0909 88  GLU   A O   
645  C CB  . GLU   A 82  ? 0.5044 0.4423 0.4937 -0.0137 0.0838  -0.0836 88  GLU   A CB  
646  C CG  . GLU   A 82  ? 0.5753 0.5014 0.5432 -0.0226 0.0890  -0.0940 88  GLU   A CG  
647  C CD  . GLU   A 82  ? 0.6407 0.5646 0.5806 -0.0322 0.0859  -0.0946 88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 0.6214 0.5356 0.5410 -0.0411 0.0890  -0.1025 88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 0.6648 0.5962 0.6025 -0.0314 0.0798  -0.0868 88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.4722 0.4098 0.4830 -0.0048 0.0661  -0.0741 89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.4875 0.4200 0.4936 -0.0067 0.0591  -0.0744 89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.4813 0.4174 0.5069 -0.0002 0.0543  -0.0679 89  TYR   A C   
653  O O   . TYR   A 83  ? 0.4829 0.4141 0.5070 -0.0017 0.0503  -0.0689 89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.5026 0.4369 0.4897 -0.0118 0.0483  -0.0709 89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.5345 0.4642 0.4989 -0.0199 0.0507  -0.0761 89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.5602 0.4799 0.5093 -0.0275 0.0540  -0.0847 89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.5531 0.4882 0.5098 -0.0211 0.0488  -0.0719 89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.5824 0.4977 0.5082 -0.0364 0.0554  -0.0888 89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.5767 0.5072 0.5112 -0.0294 0.0503  -0.0756 89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.5973 0.5180 0.5159 -0.0373 0.0535  -0.0839 89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 0.6286 0.5444 0.5231 -0.0469 0.0547  -0.0873 89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.4662 0.4109 0.5088 0.0061  0.0539  -0.0607 90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.4587 0.4074 0.5176 0.0111  0.0485  -0.0533 90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.4728 0.4244 0.5547 0.0173  0.0542  -0.0503 90  TYR   A C   
665  O O   . TYR   A 84  ? 0.4780 0.4339 0.5653 0.0189  0.0601  -0.0508 90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.4408 0.3983 0.4955 0.0112  0.0384  -0.0450 90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.4431 0.3979 0.4799 0.0061  0.0319  -0.0469 90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.4563 0.4066 0.4921 0.0043  0.0282  -0.0482 90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.4444 0.4008 0.4659 0.0025  0.0296  -0.0473 90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.4750 0.4239 0.4967 -0.0005 0.0219  -0.0496 90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.4621 0.4162 0.4691 -0.0022 0.0231  -0.0483 90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.4853 0.4362 0.4932 -0.0036 0.0191  -0.0495 90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.5161 0.4659 0.5122 -0.0081 0.0119  -0.0498 90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.4822 0.4323 0.5788 0.0207  0.0520  -0.0462 91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.4703 0.4229 0.5911 0.0268  0.0563  -0.0421 91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.4458 0.4111 0.5770 0.0299  0.0505  -0.0313 91  PRO   A C   
677  O O   . PRO   A 85  ? 0.4500 0.4216 0.5697 0.0274  0.0431  -0.0269 91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.4792 0.4243 0.6090 0.0280  0.0545  -0.0408 91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.4949 0.4413 0.6095 0.0239  0.0449  -0.0380 91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.4864 0.4317 0.5794 0.0188  0.0458  -0.0451 91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.4143 0.3833 0.5684 0.0351  0.0540  -0.0271 92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.3840 0.3649 0.5512 0.0376  0.0481  -0.0160 92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.3569 0.3381 0.5273 0.0375  0.0387  -0.0072 92  ALA   A C   
684  O O   . ALA   A 86  ? 0.3651 0.3369 0.5374 0.0377  0.0392  -0.0093 92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.3836 0.3677 0.5767 0.0432  0.0547  -0.0141 92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.3177 0.3091 0.4880 0.0363  0.0304  0.0024  93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.2964 0.2883 0.4682 0.0349  0.0220  0.0107  93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.2900 0.2937 0.4664 0.0337  0.0146  0.0217  93  ARG   A C   
689  O O   . ARG   A 87  ? 0.2952 0.3064 0.4680 0.0328  0.0151  0.0215  93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.3068 0.2941 0.4570 0.0300  0.0185  0.0066  93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.3101 0.3040 0.4434 0.0264  0.0150  0.0063  93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.2959 0.2876 0.4136 0.0222  0.0103  0.0049  93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.2643 0.2579 0.3870 0.0207  0.0048  0.0128  93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.2985 0.2911 0.4125 0.0171  0.0011  0.0132  93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.3055 0.2992 0.4242 0.0150  -0.0031 0.0206  93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.2951 0.2857 0.3961 0.0151  0.0015  0.0066  93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.2832 0.2884 0.4651 0.0323  0.0075  0.0311  94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.2884 0.3038 0.4680 0.0286  -0.0005 0.0407  94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.2631 0.2770 0.4199 0.0228  -0.0039 0.0379  94  TYR   A C   
700  O O   . TYR   A 88  ? 0.2701 0.2761 0.4201 0.0221  -0.0027 0.0333  94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.3040 0.3212 0.4997 0.0289  -0.0067 0.0527  94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.3336 0.3584 0.5526 0.0331  -0.0070 0.0597  94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.3561 0.3930 0.5756 0.0306  -0.0111 0.0651  94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.3509 0.3710 0.5929 0.0395  -0.0030 0.0607  94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.3700 0.4154 0.6130 0.0343  -0.0118 0.0720  94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.3580 0.3860 0.6249 0.0439  -0.0032 0.0675  94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.3807 0.4221 0.6484 0.0413  -0.0077 0.0733  94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.4152 0.4660 0.7099 0.0456  -0.0083 0.0806  94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.2364 0.2577 0.3822 0.0187  -0.0075 0.0401  95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.2239 0.2439 0.3506 0.0136  -0.0097 0.0372  95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.2047 0.2328 0.3260 0.0079  -0.0157 0.0448  95  GLN   A C   
712  O O   . GLN   A 89  ? 0.2035 0.2386 0.3294 0.0078  -0.0168 0.0481  95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.1971 0.2144 0.3112 0.0142  -0.0053 0.0274  95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.1891 0.2048 0.2869 0.0099  -0.0072 0.0241  95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.1837 0.1950 0.2721 0.0112  -0.0037 0.0152  95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.2089 0.2148 0.2998 0.0141  0.0000  0.0101  95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.1574 0.1704 0.2340 0.0085  -0.0049 0.0131  95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.1855 0.2129 0.2973 0.0026  -0.0193 0.0473  96  SER   A N   
719  C CA  . SER   A 90  ? 0.1896 0.2233 0.2932 -0.0043 -0.0242 0.0533  96  SER   A CA  
720  C C   . SER   A 90  ? 0.1927 0.2265 0.2793 -0.0080 -0.0222 0.0465  96  SER   A C   
721  O O   . SER   A 90  ? 0.1900 0.2187 0.2707 -0.0055 -0.0181 0.0380  96  SER   A O   
722  C CB  . SER   A 90  ? 0.2130 0.2457 0.3158 -0.0093 -0.0288 0.0607  96  SER   A CB  
723  O OG  . SER   A 90  ? 0.2593 0.2861 0.3526 -0.0110 -0.0261 0.0548  96  SER   A OG  
724  N N   . HIS   A 91  ? 0.1851 0.2246 0.2642 -0.0143 -0.0256 0.0507  97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.1820 0.2212 0.2458 -0.0185 -0.0236 0.0449  97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.1671 0.2042 0.2301 -0.0134 -0.0192 0.0373  97  HIS   A C   
727  O O   . HIS   A 91  ? 0.1713 0.2046 0.2248 -0.0137 -0.0163 0.0305  97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.1890 0.2236 0.2433 -0.0217 -0.0217 0.0407  97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.2263 0.2625 0.2781 -0.0285 -0.0255 0.0480  97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.2380 0.2765 0.2767 -0.0376 -0.0266 0.0494  97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.2427 0.2778 0.3028 -0.0280 -0.0283 0.0543  97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.2503 0.2895 0.2884 -0.0429 -0.0303 0.0567  97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.2586 0.2958 0.3101 -0.0371 -0.0319 0.0605  97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.1556 0.1954 0.2293 -0.0089 -0.0188 0.0390  98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.1617 0.1995 0.2343 -0.0048 -0.0146 0.0325  98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.1501 0.1936 0.2202 -0.0080 -0.0156 0.0346  98  LEU   A C   
737  O O   . LEU   A 92  ? 0.1583 0.2091 0.2359 -0.0104 -0.0192 0.0419  98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.1639 0.2001 0.2496 0.0016  -0.0117 0.0316  98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.1759 0.2086 0.2589 0.0052  -0.0066 0.0244  98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.1911 0.2165 0.2624 0.0055  -0.0051 0.0174  98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.2046 0.2361 0.3011 0.0104  -0.0027 0.0235  98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.1406 0.1808 0.2009 -0.0081 -0.0127 0.0285  99  MET   A N   
743  C CA  . MET   A 93  ? 0.1311 0.1752 0.1877 -0.0113 -0.0129 0.0293  99  MET   A CA  
744  C C   . MET   A 93  ? 0.1473 0.1899 0.2066 -0.0070 -0.0087 0.0254  99  MET   A C   
745  O O   . MET   A 93  ? 0.1577 0.1934 0.2123 -0.0037 -0.0059 0.0196  99  MET   A O   
746  C CB  . MET   A 93  ? 0.1489 0.1885 0.1905 -0.0159 -0.0127 0.0253  99  MET   A CB  
747  C CG  . MET   A 93  ? 0.1673 0.2080 0.2040 -0.0216 -0.0155 0.0281  99  MET   A CG  
748  S SD  . MET   A 93  ? 0.2115 0.2457 0.2329 -0.0262 -0.0130 0.0216  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.2296 0.2565 0.2527 -0.0190 -0.0096 0.0150  99  MET   A CE  
750  N N   . LEU   A 94  ? 0.1441 0.1932 0.2102 -0.0077 -0.0083 0.0284  100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.1397 0.1877 0.2079 -0.0045 -0.0033 0.0244  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.1442 0.1924 0.2030 -0.0086 -0.0027 0.0232  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.1574 0.2109 0.2151 -0.0138 -0.0061 0.0273  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.1644 0.2200 0.2512 -0.0013 -0.0012 0.0279  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.2080 0.2620 0.3066 0.0036  -0.0004 0.0286  100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.2230 0.2840 0.3421 0.0073  0.0025  0.0317  100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2295 0.2733 0.3201 0.0069  0.0036  0.0210  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.1309 0.1737 0.1833 -0.0070 0.0014  0.0181  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.1382 0.1803 0.1824 -0.0107 0.0027  0.0171  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.1484 0.1898 0.1945 -0.0086 0.0084  0.0140  101 ALA   A C   
761  O O   . ALA   A 95  ? 0.1678 0.2061 0.2169 -0.0045 0.0114  0.0109  101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.1503 0.1828 0.1791 -0.0125 0.0014  0.0136  101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.1499 0.1937 0.1933 -0.0122 0.0104  0.0144  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.1453 0.1876 0.1870 -0.0118 0.0165  0.0110  102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.1696 0.1999 0.1931 -0.0128 0.0160  0.0072  102 VAL   A C   
766  O O   . VAL   A 96  ? 0.1788 0.2048 0.1922 -0.0163 0.0131  0.0081  102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.1585 0.2088 0.2052 -0.0159 0.0189  0.0135  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.1756 0.2235 0.2177 -0.0168 0.0261  0.0095  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.1623 0.2256 0.2293 -0.0148 0.0180  0.0186  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.1954 0.2202 0.2155 -0.0102 0.0187  0.0031  103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.2062 0.2205 0.2104 -0.0113 0.0170  0.0006  103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.2201 0.2295 0.2213 -0.0091 0.0195  -0.0037 103 GLY   A C   
773  O O   . GLY   A 97  ? 0.2359 0.2489 0.2476 -0.0062 0.0229  -0.0054 103 GLY   A O   
774  N N   . HIS   A 98  ? 0.2174 0.2179 0.2042 -0.0108 0.0171  -0.0053 104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.2126 0.2078 0.1935 -0.0105 0.0187  -0.0095 104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.2077 0.2003 0.1912 -0.0071 0.0140  -0.0102 104 HIS   A C   
777  O O   . HIS   A 98  ? 0.2116 0.2023 0.1937 -0.0063 0.0081  -0.0078 104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.2259 0.2133 0.1891 -0.0154 0.0179  -0.0100 104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.2491 0.2310 0.2036 -0.0169 0.0198  -0.0145 104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.2788 0.2623 0.2353 -0.0179 0.0283  -0.0194 104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.2582 0.2335 0.2035 -0.0177 0.0141  -0.0149 104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.2757 0.2526 0.2219 -0.0200 0.0279  -0.0232 104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.2580 0.2302 0.1970 -0.0202 0.0188  -0.0202 104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.2096 0.2016 0.1970 -0.0053 0.0169  -0.0140 105 SER   A N   
785  C CA  A SER   A 99  ? 0.2206 0.2104 0.2110 -0.0027 0.0132  -0.0151 105 SER   A CA  
786  C CA  B SER   A 99  ? 0.2202 0.2091 0.2086 -0.0032 0.0128  -0.0151 105 SER   A CA  
787  C C   . SER   A 99  ? 0.2476 0.2328 0.2340 -0.0038 0.0173  -0.0206 105 SER   A C   
788  O O   . SER   A 99  ? 0.2742 0.2613 0.2663 -0.0035 0.0247  -0.0234 105 SER   A O   
789  C CB  A SER   A 99  ? 0.2283 0.2244 0.2344 0.0011  0.0131  -0.0128 105 SER   A CB  
790  C CB  B SER   A 99  ? 0.2280 0.2223 0.2301 0.0005  0.0107  -0.0124 105 SER   A CB  
791  O OG  A SER   A 99  ? 0.2510 0.2453 0.2608 0.0032  0.0101  -0.0137 105 SER   A OG  
792  O OG  B SER   A 99  ? 0.2355 0.2344 0.2494 0.0025  0.0161  -0.0131 105 SER   A OG  
793  N N   . GLU   A 100 ? 0.2399 0.2194 0.2182 -0.0051 0.0130  -0.0223 106 GLU   A N   
794  C CA  . GLU   A 100 ? 0.2559 0.2301 0.2291 -0.0070 0.0156  -0.0279 106 GLU   A CA  
795  C C   . GLU   A 100 ? 0.2590 0.2330 0.2390 -0.0043 0.0106  -0.0276 106 GLU   A C   
796  O O   . GLU   A 100 ? 0.2478 0.2248 0.2325 -0.0022 0.0048  -0.0233 106 GLU   A O   
797  C CB  . GLU   A 100 ? 0.2822 0.2498 0.2360 -0.0131 0.0132  -0.0293 106 GLU   A CB  
798  C CG  . GLU   A 100 ? 0.3247 0.2920 0.2705 -0.0168 0.0192  -0.0302 106 GLU   A CG  
799  C CD  . GLU   A 100 ? 0.3545 0.3148 0.2791 -0.0241 0.0167  -0.0306 106 GLU   A CD  
800  O OE1 . GLU   A 100 ? 0.4059 0.3607 0.3203 -0.0279 0.0142  -0.0336 106 GLU   A OE1 
801  O OE2 . GLU   A 100 ? 0.3408 0.3011 0.2582 -0.0268 0.0167  -0.0274 106 GLU   A OE2 
802  N N   . PRO   A 101 ? 0.2661 0.2363 0.2470 -0.0048 0.0131  -0.0324 107 PRO   A N   
803  C CA  . PRO   A 101 ? 0.2540 0.2245 0.2427 -0.0027 0.0087  -0.0319 107 PRO   A CA  
804  C C   . PRO   A 101 ? 0.2450 0.2164 0.2304 -0.0032 -0.0003 -0.0282 107 PRO   A C   
805  O O   . PRO   A 101 ? 0.2460 0.2214 0.2414 -0.0002 -0.0034 -0.0253 107 PRO   A O   
806  C CB  . PRO   A 101 ? 0.2827 0.2464 0.2668 -0.0055 0.0126  -0.0386 107 PRO   A CB  
807  C CG  . PRO   A 101 ? 0.3046 0.2671 0.2887 -0.0059 0.0221  -0.0423 107 PRO   A CG  
808  C CD  . PRO   A 101 ? 0.2807 0.2462 0.2574 -0.0074 0.0215  -0.0390 107 PRO   A CD  
809  N N   . GLY   A 102 ? 0.2443 0.2120 0.2162 -0.0074 -0.0045 -0.0283 108 GLY   A N   
810  C CA  . GLY   A 102 ? 0.2531 0.2217 0.2239 -0.0078 -0.0132 -0.0246 108 GLY   A CA  
811  C C   . GLY   A 102 ? 0.2365 0.2094 0.2138 -0.0044 -0.0155 -0.0195 108 GLY   A C   
812  O O   . GLY   A 102 ? 0.2470 0.2210 0.2273 -0.0036 -0.0218 -0.0165 108 GLY   A O   
813  N N   . ASP   A 103 ? 0.2180 0.1931 0.1976 -0.0029 -0.0102 -0.0187 109 ASP   A N   
814  C CA  . ASP   A 103 ? 0.2026 0.1812 0.1878 -0.0005 -0.0117 -0.0146 109 ASP   A CA  
815  C C   . ASP   A 103 ? 0.1969 0.1802 0.1948 0.0027  -0.0116 -0.0138 109 ASP   A C   
816  O O   . ASP   A 103 ? 0.1936 0.1792 0.1956 0.0039  -0.0131 -0.0113 109 ASP   A O   
817  C CB  . ASP   A 103 ? 0.1922 0.1722 0.1755 -0.0011 -0.0066 -0.0137 109 ASP   A CB  
818  C CG  . ASP   A 103 ? 0.2311 0.2064 0.2006 -0.0051 -0.0070 -0.0134 109 ASP   A CG  
819  O OD1 . ASP   A 103 ? 0.2464 0.2179 0.2095 -0.0066 -0.0130 -0.0114 109 ASP   A OD1 
820  O OD2 . ASP   A 103 ? 0.2353 0.2108 0.2011 -0.0069 -0.0011 -0.0149 109 ASP   A OD2 
821  N N   . CYS   A 104 ? 0.1929 0.1770 0.1966 0.0035  -0.0100 -0.0161 110 CYS   A N   
822  C CA  . CYS   A 104 ? 0.1906 0.1789 0.2052 0.0056  -0.0103 -0.0148 110 CYS   A CA  
823  C C   . CYS   A 104 ? 0.1892 0.1785 0.2060 0.0059  -0.0148 -0.0136 110 CYS   A C   
824  O O   . CYS   A 104 ? 0.2128 0.1997 0.2264 0.0050  -0.0190 -0.0144 110 CYS   A O   
825  C CB  . CYS   A 104 ? 0.1825 0.1699 0.2022 0.0059  -0.0086 -0.0171 110 CYS   A CB  
826  S SG  . CYS   A 104 ? 0.2143 0.2017 0.2387 0.0071  -0.0020 -0.0177 110 CYS   A SG  
827  N N   . GLY   A 105 ? 0.1693 0.1623 0.1922 0.0068  -0.0141 -0.0118 111 GLY   A N   
828  C CA  . GLY   A 105 ? 0.1755 0.1697 0.2028 0.0074  -0.0166 -0.0116 111 GLY   A CA  
829  C C   . GLY   A 105 ? 0.1865 0.1792 0.2107 0.0075  -0.0171 -0.0101 111 GLY   A C   
830  O O   . GLY   A 105 ? 0.1973 0.1911 0.2269 0.0082  -0.0174 -0.0102 111 GLY   A O   
831  N N   . GLY   A 106 ? 0.1903 0.1804 0.2066 0.0067  -0.0165 -0.0090 112 GLY   A N   
832  C CA  . GLY   A 106 ? 0.1807 0.1686 0.1939 0.0063  -0.0166 -0.0075 112 GLY   A CA  
833  C C   . GLY   A 106 ? 0.1649 0.1559 0.1819 0.0055  -0.0132 -0.0073 112 GLY   A C   
834  O O   . GLY   A 106 ? 0.1705 0.1653 0.1888 0.0046  -0.0107 -0.0069 112 GLY   A O   
835  N N   . ILE   A 107 ? 0.1589 0.1477 0.1777 0.0057  -0.0132 -0.0076 113 ILE   A N   
836  C CA  . ILE   A 107 ? 0.1673 0.1582 0.1878 0.0037  -0.0096 -0.0085 113 ILE   A CA  
837  C C   . ILE   A 107 ? 0.1701 0.1600 0.1838 0.0008  -0.0079 -0.0070 113 ILE   A C   
838  O O   . ILE   A 107 ? 0.1781 0.1634 0.1871 0.0008  -0.0091 -0.0060 113 ILE   A O   
839  C CB  . ILE   A 107 ? 0.1835 0.1725 0.2106 0.0048  -0.0088 -0.0108 113 ILE   A CB  
840  C CG1 . ILE   A 107 ? 0.2055 0.1985 0.2409 0.0063  -0.0093 -0.0123 113 ILE   A CG1 
841  C CG2 . ILE   A 107 ? 0.2199 0.2087 0.2451 0.0013  -0.0041 -0.0126 113 ILE   A CG2 
842  C CD1 . ILE   A 107 ? 0.2297 0.2219 0.2752 0.0080  -0.0080 -0.0150 113 ILE   A CD1 
843  N N   . LEU   A 108 ? 0.1604 0.1546 0.1734 -0.0023 -0.0056 -0.0064 114 LEU   A N   
844  C CA  . LEU   A 108 ? 0.1586 0.1533 0.1663 -0.0064 -0.0041 -0.0051 114 LEU   A CA  
845  C C   . LEU   A 108 ? 0.1607 0.1534 0.1675 -0.0094 -0.0015 -0.0077 114 LEU   A C   
846  O O   . LEU   A 108 ? 0.1651 0.1606 0.1749 -0.0104 -0.0001 -0.0090 114 LEU   A O   
847  C CB  . LEU   A 108 ? 0.1508 0.1526 0.1597 -0.0083 -0.0042 -0.0019 114 LEU   A CB  
848  C CG  . LEU   A 108 ? 0.1630 0.1675 0.1677 -0.0135 -0.0036 0.0002  114 LEU   A CG  
849  C CD1 . LEU   A 108 ? 0.1897 0.1913 0.1900 -0.0140 -0.0035 0.0008  114 LEU   A CD1 
850  C CD2 . LEU   A 108 ? 0.1701 0.1827 0.1792 -0.0152 -0.0048 0.0045  114 LEU   A CD2 
851  N N   . ARG   A 109 ? 0.1690 0.1562 0.1714 -0.0114 -0.0002 -0.0089 115 ARG   A N   
852  C CA  . ARG   A 109 ? 0.1855 0.1688 0.1867 -0.0146 0.0036  -0.0128 115 ARG   A CA  
853  C C   . ARG   A 109 ? 0.1916 0.1731 0.1847 -0.0207 0.0051  -0.0126 115 ARG   A C   
854  O O   . ARG   A 109 ? 0.2006 0.1808 0.1901 -0.0211 0.0033  -0.0100 115 ARG   A O   
855  C CB  . ARG   A 109 ? 0.2335 0.2091 0.2402 -0.0102 0.0041  -0.0154 115 ARG   A CB  
856  C CG  . ARG   A 109 ? 0.3237 0.3008 0.3402 -0.0048 0.0027  -0.0163 115 ARG   A CG  
857  C CD  . ARG   A 109 ? 0.3803 0.3499 0.4039 -0.0011 0.0028  -0.0179 115 ARG   A CD  
858  N NE  . ARG   A 109 ? 0.4637 0.4344 0.4979 0.0007  0.0063  -0.0221 115 ARG   A NE  
859  C CZ  . ARG   A 109 ? 0.5000 0.4744 0.5443 0.0050  0.0037  -0.0216 115 ARG   A CZ  
860  N NH1 . ARG   A 109 ? 0.5315 0.5077 0.5751 0.0076  -0.0027 -0.0173 115 ARG   A NH1 
861  N NH2 . ARG   A 109 ? 0.5363 0.5124 0.5915 0.0062  0.0077  -0.0256 115 ARG   A NH2 
862  N N   . CYS   A 110 ? 0.1928 0.1741 0.1818 -0.0264 0.0086  -0.0155 116 CYS   A N   
863  C CA  . CYS   A 110 ? 0.2164 0.1947 0.1963 -0.0337 0.0104  -0.0165 116 CYS   A CA  
864  C C   . CYS   A 110 ? 0.2434 0.2122 0.2228 -0.0351 0.0162  -0.0233 116 CYS   A C   
865  O O   . CYS   A 110 ? 0.2526 0.2186 0.2403 -0.0299 0.0183  -0.0264 116 CYS   A O   
866  C CB  . CYS   A 110 ? 0.2228 0.2088 0.1966 -0.0412 0.0093  -0.0139 116 CYS   A CB  
867  S SG  . CYS   A 110 ? 0.2211 0.2092 0.1934 -0.0452 0.0130  -0.0175 116 CYS   A SG  
868  N N   . GLN   A 111 ? 0.2783 0.2426 0.2486 -0.0428 0.0192  -0.0260 117 GLN   A N   
869  C CA  . GLN   A 111 ? 0.3105 0.2647 0.2803 -0.0448 0.0262  -0.0336 117 GLN   A CA  
870  C C   . GLN   A 111 ? 0.3137 0.2697 0.2861 -0.0460 0.0315  -0.0387 117 GLN   A C   
871  O O   . GLN   A 111 ? 0.3476 0.2961 0.3257 -0.0443 0.0380  -0.0454 117 GLN   A O   
872  C CB  . GLN   A 111 ? 0.3606 0.3094 0.3181 -0.0545 0.0287  -0.0360 117 GLN   A CB  
873  C CG  . GLN   A 111 ? 0.4282 0.3854 0.3747 -0.0643 0.0275  -0.0344 117 GLN   A CG  
874  C CD  . GLN   A 111 ? 0.5334 0.4860 0.4668 -0.0752 0.0293  -0.0367 117 GLN   A CD  
875  O OE1 . GLN   A 111 ? 0.5667 0.5258 0.4945 -0.0803 0.0239  -0.0310 117 GLN   A OE1 
876  N NE2 . GLN   A 111 ? 0.5372 0.4787 0.4663 -0.0793 0.0371  -0.0453 117 GLN   A NE2 
877  N N   . HIS   A 112 ? 0.2655 0.2311 0.2349 -0.0488 0.0292  -0.0356 118 HIS   A N   
878  C CA  . HIS   A 112 ? 0.2604 0.2286 0.2303 -0.0515 0.0340  -0.0395 118 HIS   A CA  
879  C C   . HIS   A 112 ? 0.2612 0.2329 0.2452 -0.0426 0.0333  -0.0390 118 HIS   A C   
880  O O   . HIS   A 112 ? 0.2828 0.2559 0.2696 -0.0441 0.0384  -0.0432 118 HIS   A O   
881  C CB  . HIS   A 112 ? 0.2720 0.2481 0.2304 -0.0605 0.0311  -0.0354 118 HIS   A CB  
882  C CG  . HIS   A 112 ? 0.2973 0.2715 0.2417 -0.0706 0.0307  -0.0352 118 HIS   A CG  
883  N ND1 . HIS   A 112 ? 0.3020 0.2820 0.2438 -0.0720 0.0233  -0.0277 118 HIS   A ND1 
884  C CD2 . HIS   A 112 ? 0.3370 0.3051 0.2695 -0.0807 0.0369  -0.0417 118 HIS   A CD2 
885  C CE1 . HIS   A 112 ? 0.3353 0.3124 0.2646 -0.0823 0.0244  -0.0294 118 HIS   A CE1 
886  N NE2 . HIS   A 112 ? 0.3593 0.3289 0.2813 -0.0883 0.0325  -0.0379 118 HIS   A NE2 
887  N N   . GLY   A 113 ? 0.2340 0.2073 0.2261 -0.0342 0.0272  -0.0341 119 GLY   A N   
888  C CA  . GLY   A 113 ? 0.2100 0.1872 0.2144 -0.0269 0.0255  -0.0332 119 GLY   A CA  
889  C C   . GLY   A 113 ? 0.2005 0.1840 0.2062 -0.0230 0.0180  -0.0263 119 GLY   A C   
890  O O   . GLY   A 113 ? 0.2169 0.2010 0.2171 -0.0239 0.0142  -0.0222 119 GLY   A O   
891  N N   . VAL   A 114 ? 0.1916 0.1796 0.2050 -0.0194 0.0168  -0.0255 120 VAL   A N   
892  C CA  . VAL   A 114 ? 0.1864 0.1795 0.2018 -0.0159 0.0109  -0.0202 120 VAL   A CA  
893  C C   . VAL   A 114 ? 0.1893 0.1879 0.1978 -0.0211 0.0093  -0.0161 120 VAL   A C   
894  O O   . VAL   A 114 ? 0.2014 0.2028 0.2068 -0.0264 0.0117  -0.0168 120 VAL   A O   
895  C CB  . VAL   A 114 ? 0.1892 0.1847 0.2150 -0.0112 0.0103  -0.0211 120 VAL   A CB  
896  C CG1 . VAL   A 114 ? 0.1951 0.1948 0.2219 -0.0087 0.0052  -0.0165 120 VAL   A CG1 
897  C CG2 . VAL   A 114 ? 0.2181 0.2091 0.2527 -0.0056 0.0100  -0.0235 120 VAL   A CG2 
898  N N   . VAL   A 115 ? 0.1643 0.1649 0.1710 -0.0199 0.0051  -0.0114 121 VAL   A N   
899  C CA  . VAL   A 115 ? 0.1671 0.1738 0.1707 -0.0239 0.0025  -0.0062 121 VAL   A CA  
900  C C   . VAL   A 115 ? 0.1826 0.1931 0.1935 -0.0196 -0.0003 -0.0032 121 VAL   A C   
901  O O   . VAL   A 115 ? 0.1844 0.1991 0.1959 -0.0224 -0.0014 0.0002  121 VAL   A O   
902  C CB  . VAL   A 115 ? 0.1759 0.1831 0.1758 -0.0251 0.0004  -0.0033 121 VAL   A CB  
903  C CG1 . VAL   A 115 ? 0.1897 0.2044 0.1904 -0.0280 -0.0030 0.0030  121 VAL   A CG1 
904  C CG2 . VAL   A 115 ? 0.2066 0.2091 0.1986 -0.0302 0.0032  -0.0065 121 VAL   A CG2 
905  N N   . GLY   A 116 ? 0.1702 0.1786 0.1860 -0.0133 -0.0015 -0.0040 122 GLY   A N   
906  C CA  . GLY   A 116 ? 0.1732 0.1838 0.1950 -0.0097 -0.0036 -0.0020 122 GLY   A CA  
907  C C   . GLY   A 116 ? 0.1560 0.1632 0.1803 -0.0044 -0.0047 -0.0040 122 GLY   A C   
908  O O   . GLY   A 116 ? 0.1667 0.1699 0.1889 -0.0032 -0.0046 -0.0062 122 GLY   A O   
909  N N   . ILE   A 117 ? 0.1522 0.1603 0.1807 -0.0017 -0.0060 -0.0030 123 ILE   A N   
910  C CA  . ILE   A 117 ? 0.1610 0.1656 0.1897 0.0019  -0.0073 -0.0050 123 ILE   A CA  
911  C C   . ILE   A 117 ? 0.1542 0.1592 0.1831 0.0032  -0.0071 -0.0036 123 ILE   A C   
912  O O   . ILE   A 117 ? 0.1551 0.1632 0.1884 0.0028  -0.0064 -0.0011 123 ILE   A O   
913  C CB  . ILE   A 117 ? 0.1732 0.1772 0.2067 0.0034  -0.0084 -0.0072 123 ILE   A CB  
914  C CG1 . ILE   A 117 ? 0.1845 0.1912 0.2227 0.0024  -0.0078 -0.0058 123 ILE   A CG1 
915  C CG2 . ILE   A 117 ? 0.2078 0.2109 0.2431 0.0033  -0.0081 -0.0095 123 ILE   A CG2 
916  C CD1 . ILE   A 117 ? 0.2027 0.2084 0.2456 0.0036  -0.0090 -0.0083 123 ILE   A CD1 
917  N N   . VAL   A 118 ? 0.1401 0.1416 0.1645 0.0044  -0.0074 -0.0051 124 VAL   A N   
918  C CA  . VAL   A 118 ? 0.1499 0.1513 0.1743 0.0053  -0.0056 -0.0051 124 VAL   A CA  
919  C C   . VAL   A 118 ? 0.1588 0.1601 0.1893 0.0067  -0.0049 -0.0062 124 VAL   A C   
920  O O   . VAL   A 118 ? 0.1546 0.1534 0.1850 0.0071  -0.0068 -0.0083 124 VAL   A O   
921  C CB  . VAL   A 118 ? 0.1562 0.1528 0.1725 0.0051  -0.0059 -0.0072 124 VAL   A CB  
922  C CG1 . VAL   A 118 ? 0.1711 0.1672 0.1872 0.0054  -0.0024 -0.0087 124 VAL   A CG1 
923  C CG2 . VAL   A 118 ? 0.1732 0.1690 0.1837 0.0035  -0.0063 -0.0056 124 VAL   A CG2 
924  N N   . SER   A 119 ? 0.1589 0.1625 0.1955 0.0075  -0.0025 -0.0045 125 SER   A N   
925  C CA  . SER   A 119 ? 0.1624 0.1647 0.2060 0.0089  -0.0015 -0.0052 125 SER   A CA  
926  C C   . SER   A 119 ? 0.1815 0.1828 0.2295 0.0106  0.0028  -0.0065 125 SER   A C   
927  O O   . SER   A 119 ? 0.1953 0.1923 0.2462 0.0117  0.0046  -0.0094 125 SER   A O   
928  C CB  . SER   A 119 ? 0.1701 0.1765 0.2208 0.0082  -0.0030 -0.0006 125 SER   A CB  
929  O OG  . SER   A 119 ? 0.1729 0.1775 0.2316 0.0095  -0.0022 -0.0001 125 SER   A OG  
930  N N   . THR   A 120 ? 0.1745 0.1793 0.2238 0.0106  0.0050  -0.0048 126 THR   A N   
931  C CA  . THR   A 120 ? 0.1816 0.1862 0.2373 0.0124  0.0105  -0.0066 126 THR   A CA  
932  C C   . THR   A 120 ? 0.2063 0.2117 0.2550 0.0108  0.0133  -0.0083 126 THR   A C   
933  O O   . THR   A 120 ? 0.1964 0.2027 0.2367 0.0086  0.0104  -0.0068 126 THR   A O   
934  C CB  . THR   A 120 ? 0.2075 0.2180 0.2793 0.0144  0.0109  -0.0011 126 THR   A CB  
935  O OG1 . THR   A 120 ? 0.2253 0.2432 0.2985 0.0128  0.0090  0.0038  126 THR   A OG1 
936  C CG2 . THR   A 120 ? 0.1988 0.2086 0.2767 0.0150  0.0076  0.0019  126 THR   A CG2 
937  N N   . GLY   A 121 ? 0.2369 0.2412 0.2890 0.0116  0.0197  -0.0117 127 GLY   A N   
938  C CA  . GLY   A 121 ? 0.2759 0.2810 0.3211 0.0094  0.0233  -0.0134 127 GLY   A CA  
939  C C   . GLY   A 121 ? 0.3306 0.3353 0.3827 0.0103  0.0319  -0.0177 127 GLY   A C   
940  O O   . GLY   A 121 ? 0.3584 0.3617 0.4219 0.0134  0.0351  -0.0193 127 GLY   A O   
941  N N   . GLY   A 122 ? 0.3609 0.3651 0.4038 0.0072  0.0359  -0.0203 128 GLY   A N   
942  C CA  . GLY   A 122 ? 0.3753 0.3794 0.4227 0.0069  0.0457  -0.0253 128 GLY   A CA  
943  C C   . GLY   A 122 ? 0.3642 0.3784 0.4250 0.0077  0.0487  -0.0213 128 GLY   A C   
944  O O   . GLY   A 122 ? 0.3493 0.3705 0.4171 0.0087  0.0426  -0.0144 128 GLY   A O   
945  N N   . ASN   A 123 ? 0.3669 0.3825 0.4320 0.0069  0.0585  -0.0259 129 ASN   A N   
946  C CA  . ASN   A 123 ? 0.3574 0.3839 0.4376 0.0074  0.0622  -0.0225 129 ASN   A CA  
947  C C   . ASN   A 123 ? 0.3223 0.3542 0.3951 0.0039  0.0554  -0.0162 129 ASN   A C   
948  O O   . ASN   A 123 ? 0.3142 0.3566 0.4021 0.0049  0.0540  -0.0105 129 ASN   A O   
949  C CB  . ASN   A 123 ? 0.3961 0.4305 0.5040 0.0135  0.0626  -0.0182 129 ASN   A CB  
950  C CG  . ASN   A 123 ? 0.4783 0.5107 0.6019 0.0173  0.0731  -0.0242 129 ASN   A CG  
951  O OD1 . ASN   A 123 ? 0.5254 0.5490 0.6373 0.0149  0.0811  -0.0332 129 ASN   A OD1 
952  N ND2 . ASN   A 123 ? 0.4785 0.5183 0.6290 0.0228  0.0733  -0.0193 129 ASN   A ND2 
953  N N   . GLY   A 124 ? 0.2926 0.3174 0.3434 -0.0003 0.0508  -0.0168 130 GLY   A N   
954  C CA  . GLY   A 124 ? 0.2681 0.2960 0.3118 -0.0037 0.0453  -0.0117 130 GLY   A CA  
955  C C   . GLY   A 124 ? 0.2246 0.2561 0.2735 -0.0020 0.0362  -0.0053 130 GLY   A C   
956  O O   . GLY   A 124 ? 0.2067 0.2417 0.2528 -0.0050 0.0325  -0.0012 130 GLY   A O   
957  N N   . LEU   A 125 ? 0.2090 0.2391 0.2644 0.0019  0.0331  -0.0047 131 LEU   A N   
958  C CA  . LEU   A 125 ? 0.2041 0.2369 0.2624 0.0024  0.0251  0.0008  131 LEU   A CA  
959  C C   . LEU   A 125 ? 0.2098 0.2336 0.2560 0.0029  0.0209  -0.0015 131 LEU   A C   
960  O O   . LEU   A 125 ? 0.2466 0.2635 0.2865 0.0037  0.0234  -0.0066 131 LEU   A O   
961  C CB  . LEU   A 125 ? 0.2211 0.2611 0.2993 0.0060  0.0243  0.0050  131 LEU   A CB  
962  C CG  . LEU   A 125 ? 0.2444 0.2952 0.3396 0.0063  0.0282  0.0080  131 LEU   A CG  
963  C CD1 . LEU   A 125 ? 0.2755 0.3317 0.3929 0.0110  0.0287  0.0115  131 LEU   A CD1 
964  C CD2 . LEU   A 125 ? 0.2307 0.2885 0.3238 0.0017  0.0234  0.0135  131 LEU   A CD2 
965  N N   . VAL   A 126 ? 0.1632 0.1874 0.2061 0.0018  0.0147  0.0019  132 VAL   A N   
966  C CA  . VAL   A 126 ? 0.1613 0.1792 0.1972 0.0026  0.0107  0.0005  132 VAL   A CA  
967  C C   . VAL   A 126 ? 0.1613 0.1837 0.2055 0.0032  0.0068  0.0048  132 VAL   A C   
968  O O   . VAL   A 126 ? 0.1718 0.2001 0.2190 0.0007  0.0047  0.0090  132 VAL   A O   
969  C CB  . VAL   A 126 ? 0.1863 0.1984 0.2078 0.0001  0.0078  -0.0006 132 VAL   A CB  
970  C CG1 . VAL   A 126 ? 0.2074 0.2226 0.2267 -0.0032 0.0062  0.0027  132 VAL   A CG1 
971  C CG2 . VAL   A 126 ? 0.1960 0.2031 0.2138 0.0013  0.0038  -0.0019 132 VAL   A CG2 
972  N N   . GLY   A 127 ? 0.1578 0.1776 0.2054 0.0055  0.0057  0.0038  133 GLY   A N   
973  C CA  . GLY   A 127 ? 0.1569 0.1802 0.2109 0.0052  0.0021  0.0081  133 GLY   A CA  
974  C C   . GLY   A 127 ? 0.1549 0.1736 0.2007 0.0041  -0.0009 0.0063  133 GLY   A C   
975  O O   . GLY   A 127 ? 0.1627 0.1756 0.2035 0.0055  -0.0004 0.0020  133 GLY   A O   
976  N N   . PHE   A 128 ? 0.1338 0.1554 0.1782 0.0010  -0.0038 0.0095  134 PHE   A N   
977  C CA  . PHE   A 128 ? 0.1459 0.1640 0.1840 -0.0003 -0.0053 0.0074  134 PHE   A CA  
978  C C   . PHE   A 128 ? 0.1501 0.1709 0.1927 -0.0020 -0.0071 0.0107  134 PHE   A C   
979  O O   . PHE   A 128 ? 0.1523 0.1783 0.1982 -0.0048 -0.0088 0.0159  134 PHE   A O   
980  C CB  . PHE   A 128 ? 0.1473 0.1651 0.1772 -0.0041 -0.0058 0.0071  134 PHE   A CB  
981  C CG  . PHE   A 128 ? 0.1470 0.1624 0.1720 -0.0036 -0.0045 0.0054  134 PHE   A CG  
982  C CD1 . PHE   A 128 ? 0.1494 0.1586 0.1690 -0.0019 -0.0044 0.0017  134 PHE   A CD1 
983  C CD2 . PHE   A 128 ? 0.1584 0.1782 0.1845 -0.0057 -0.0039 0.0082  134 PHE   A CD2 
984  C CE1 . PHE   A 128 ? 0.1580 0.1642 0.1717 -0.0023 -0.0037 0.0010  134 PHE   A CE1 
985  C CE2 . PHE   A 128 ? 0.1727 0.1898 0.1931 -0.0063 -0.0025 0.0068  134 PHE   A CE2 
986  C CZ  . PHE   A 128 ? 0.1651 0.1750 0.1787 -0.0047 -0.0024 0.0033  134 PHE   A CZ  
987  N N   . ALA   A 129 ? 0.1388 0.1562 0.1814 -0.0009 -0.0071 0.0080  135 ALA   A N   
988  C CA  . ALA   A 129 ? 0.1343 0.1534 0.1795 -0.0034 -0.0084 0.0109  135 ALA   A CA  
989  C C   . ALA   A 129 ? 0.1472 0.1673 0.1846 -0.0084 -0.0084 0.0103  135 ALA   A C   
990  O O   . ALA   A 129 ? 0.1585 0.1755 0.1918 -0.0081 -0.0068 0.0056  135 ALA   A O   
991  C CB  . ALA   A 129 ? 0.1485 0.1638 0.1964 -0.0012 -0.0079 0.0077  135 ALA   A CB  
992  N N   . ASP   A 130 ? 0.1463 0.1706 0.1821 -0.0136 -0.0100 0.0152  136 ASP   A N   
993  C CA  . ASP   A 130 ? 0.1563 0.1808 0.1830 -0.0197 -0.0090 0.0140  136 ASP   A CA  
994  C C   . ASP   A 130 ? 0.1616 0.1841 0.1868 -0.0215 -0.0070 0.0111  136 ASP   A C   
995  O O   . ASP   A 130 ? 0.1751 0.1981 0.2054 -0.0208 -0.0080 0.0134  136 ASP   A O   
996  C CB  . ASP   A 130 ? 0.1802 0.2100 0.2046 -0.0261 -0.0123 0.0209  136 ASP   A CB  
997  C CG  . ASP   A 130 ? 0.2191 0.2487 0.2317 -0.0342 -0.0110 0.0194  136 ASP   A CG  
998  O OD1 . ASP   A 130 ? 0.2168 0.2435 0.2241 -0.0345 -0.0082 0.0144  136 ASP   A OD1 
999  O OD2 . ASP   A 130 ? 0.2533 0.2852 0.2616 -0.0409 -0.0125 0.0232  136 ASP   A OD2 
1000 N N   . VAL   A 131 ? 0.1665 0.1869 0.1854 -0.0244 -0.0036 0.0060  137 VAL   A N   
1001 C CA  . VAL   A 131 ? 0.1671 0.1865 0.1852 -0.0271 -0.0003 0.0026  137 VAL   A CA  
1002 C C   . VAL   A 131 ? 0.1904 0.2101 0.1981 -0.0359 0.0027  0.0013  137 VAL   A C   
1003 O O   . VAL   A 131 ? 0.2002 0.2195 0.2062 -0.0394 0.0067  -0.0020 137 VAL   A O   
1004 C CB  . VAL   A 131 ? 0.1787 0.1950 0.2023 -0.0217 0.0024  -0.0039 137 VAL   A CB  
1005 C CG1 . VAL   A 131 ? 0.1951 0.2107 0.2265 -0.0149 -0.0007 -0.0030 137 VAL   A CG1 
1006 C CG2 . VAL   A 131 ? 0.1805 0.1935 0.2011 -0.0208 0.0045  -0.0079 137 VAL   A CG2 
1007 N N   . ARG   A 132 ? 0.1902 0.2107 0.1908 -0.0399 0.0013  0.0034  138 ARG   A N   
1008 C CA  . ARG   A 132 ? 0.1958 0.2154 0.1846 -0.0491 0.0045  0.0012  138 ARG   A CA  
1009 C C   . ARG   A 132 ? 0.2280 0.2506 0.2101 -0.0577 0.0037  0.0052  138 ARG   A C   
1010 O O   . ARG   A 132 ? 0.2570 0.2778 0.2281 -0.0662 0.0082  0.0014  138 ARG   A O   
1011 C CB  . ARG   A 132 ? 0.1902 0.2101 0.1729 -0.0522 0.0022  0.0031  138 ARG   A CB  
1012 C CG  . ARG   A 132 ? 0.1857 0.2014 0.1727 -0.0453 0.0037  -0.0013 138 ARG   A CG  
1013 C CD  . ARG   A 132 ? 0.1939 0.2105 0.1753 -0.0489 0.0012  0.0013  138 ARG   A CD  
1014 N NE  . ARG   A 132 ? 0.2089 0.2321 0.1962 -0.0471 -0.0048 0.0093  138 ARG   A NE  
1015 C CZ  . ARG   A 132 ? 0.2144 0.2409 0.2009 -0.0491 -0.0080 0.0131  138 ARG   A CZ  
1016 N NH1 . ARG   A 132 ? 0.2164 0.2400 0.1937 -0.0548 -0.0062 0.0101  138 ARG   A NH1 
1017 N NH2 . ARG   A 132 ? 0.2023 0.2350 0.1978 -0.0460 -0.0125 0.0198  138 ARG   A NH2 
1018 N N   . ASP   A 133 ? 0.2129 0.2391 0.2004 -0.0564 -0.0016 0.0127  139 ASP   A N   
1019 C CA  . ASP   A 133 ? 0.2212 0.2497 0.2021 -0.0650 -0.0033 0.0181  139 ASP   A CA  
1020 C C   . ASP   A 133 ? 0.2434 0.2700 0.2262 -0.0651 0.0016  0.0139  139 ASP   A C   
1021 O O   . ASP   A 133 ? 0.2693 0.2971 0.2448 -0.0735 0.0014  0.0175  139 ASP   A O   
1022 C CB  . ASP   A 133 ? 0.2387 0.2714 0.2265 -0.0636 -0.0115 0.0290  139 ASP   A CB  
1023 C CG  . ASP   A 133 ? 0.2893 0.3210 0.2917 -0.0536 -0.0125 0.0297  139 ASP   A CG  
1024 O OD1 . ASP   A 133 ? 0.2514 0.2805 0.2598 -0.0458 -0.0094 0.0232  139 ASP   A OD1 
1025 O OD2 . ASP   A 133 ? 0.3057 0.3387 0.3133 -0.0541 -0.0167 0.0371  139 ASP   A OD2 
1026 N N   . LEU   A 134 ? 0.2300 0.2543 0.2223 -0.0569 0.0056  0.0071  140 LEU   A N   
1027 C CA  . LEU   A 134 ? 0.2310 0.2549 0.2277 -0.0569 0.0098  0.0037  140 LEU   A CA  
1028 C C   . LEU   A 134 ? 0.2387 0.2610 0.2290 -0.0623 0.0183  -0.0047 140 LEU   A C   
1029 O O   . LEU   A 134 ? 0.2364 0.2570 0.2342 -0.0568 0.0230  -0.0122 140 LEU   A O   
1030 C CB  . LEU   A 134 ? 0.2104 0.2333 0.2212 -0.0460 0.0089  0.0012  140 LEU   A CB  
1031 C CG  . LEU   A 134 ? 0.2366 0.2599 0.2541 -0.0403 0.0021  0.0079  140 LEU   A CG  
1032 C CD1 . LEU   A 134 ? 0.2374 0.2589 0.2661 -0.0308 0.0018  0.0040  140 LEU   A CD1 
1033 C CD2 . LEU   A 134 ? 0.2629 0.2874 0.2808 -0.0444 -0.0011 0.0151  140 LEU   A CD2 
1034 N N   . LEU   A 135 ? 0.2388 0.2615 0.2149 -0.0738 0.0203  -0.0035 141 LEU   A N   
1035 C CA  . LEU   A 135 ? 0.2500 0.2702 0.2180 -0.0804 0.0297  -0.0124 141 LEU   A CA  
1036 C C   . LEU   A 135 ? 0.2814 0.3019 0.2578 -0.0789 0.0376  -0.0195 141 LEU   A C   
1037 O O   . LEU   A 135 ? 0.2932 0.3114 0.2717 -0.0787 0.0460  -0.0288 141 LEU   A O   
1038 C CB  . LEU   A 135 ? 0.2707 0.2909 0.2190 -0.0949 0.0304  -0.0099 141 LEU   A CB  
1039 C CG  . LEU   A 135 ? 0.3010 0.3224 0.2403 -0.0988 0.0220  -0.0019 141 LEU   A CG  
1040 C CD1 . LEU   A 135 ? 0.3239 0.3447 0.2420 -0.1148 0.0240  -0.0015 141 LEU   A CD1 
1041 C CD2 . LEU   A 135 ? 0.2989 0.3183 0.2429 -0.0917 0.0209  -0.0049 141 LEU   A CD2 
1042 N N   . TRP   A 136 ? 0.2712 0.2946 0.2542 -0.0775 0.0351  -0.0153 142 TRP   A N   
1043 C CA  . TRP   A 136 ? 0.2761 0.3011 0.2685 -0.0766 0.0417  -0.0208 142 TRP   A CA  
1044 C C   . TRP   A 136 ? 0.2739 0.2990 0.2837 -0.0653 0.0437  -0.0273 142 TRP   A C   
1045 O O   . TRP   A 136 ? 0.2821 0.3092 0.3014 -0.0646 0.0505  -0.0334 142 TRP   A O   
1046 C CB  . TRP   A 136 ? 0.2699 0.2972 0.2648 -0.0780 0.0372  -0.0138 142 TRP   A CB  
1047 C CG  . TRP   A 136 ? 0.2604 0.2875 0.2637 -0.0693 0.0276  -0.0067 142 TRP   A CG  
1048 C CD1 . TRP   A 136 ? 0.2619 0.2883 0.2599 -0.0703 0.0195  0.0026  142 TRP   A CD1 
1049 C CD2 . TRP   A 136 ? 0.2494 0.2767 0.2684 -0.0585 0.0254  -0.0088 142 TRP   A CD2 
1050 N NE1 . TRP   A 136 ? 0.2665 0.2923 0.2764 -0.0606 0.0138  0.0054  142 TRP   A NE1 
1051 C CE2 . TRP   A 136 ? 0.2567 0.2828 0.2780 -0.0541 0.0172  -0.0013 142 TRP   A CE2 
1052 C CE3 . TRP   A 136 ? 0.2575 0.2865 0.2895 -0.0531 0.0296  -0.0157 142 TRP   A CE3 
1053 C CZ2 . TRP   A 136 ? 0.2645 0.2898 0.2977 -0.0449 0.0137  -0.0018 142 TRP   A CZ2 
1054 C CZ3 . TRP   A 136 ? 0.2715 0.3003 0.3153 -0.0442 0.0246  -0.0151 142 TRP   A CZ3 
1055 C CH2 . TRP   A 136 ? 0.2606 0.2873 0.3037 -0.0406 0.0171  -0.0087 142 TRP   A CH2 
1056 N N   . LEU   A 137 ? 0.2794 0.3025 0.2938 -0.0568 0.0378  -0.0255 143 LEU   A N   
1057 C CA  . LEU   A 137 ? 0.2971 0.3197 0.3263 -0.0471 0.0387  -0.0305 143 LEU   A CA  
1058 C C   . LEU   A 137 ? 0.3593 0.3797 0.3903 -0.0486 0.0480  -0.0395 143 LEU   A C   
1059 O O   . LEU   A 137 ? 0.3781 0.3991 0.4243 -0.0417 0.0503  -0.0439 143 LEU   A O   
1060 C CB  . LEU   A 137 ? 0.2735 0.2937 0.3042 -0.0396 0.0311  -0.0268 143 LEU   A CB  
1061 C CG  . LEU   A 137 ? 0.2525 0.2739 0.2858 -0.0355 0.0229  -0.0198 143 LEU   A CG  
1062 C CD1 . LEU   A 137 ? 0.2671 0.2859 0.2987 -0.0303 0.0176  -0.0172 143 LEU   A CD1 
1063 C CD2 . LEU   A 137 ? 0.2532 0.2766 0.3005 -0.0295 0.0217  -0.0213 143 LEU   A CD2 
1064 N N   . ASP   A 138 ? 0.3872 0.4048 0.4030 -0.0578 0.0532  -0.0419 144 ASP   A N   
1065 C CA  . ASP   A 138 ? 0.4267 0.4404 0.4413 -0.0610 0.0633  -0.0512 144 ASP   A CA  
1066 C C   . ASP   A 138 ? 0.4631 0.4793 0.4819 -0.0663 0.0743  -0.0583 144 ASP   A C   
1067 O O   . ASP   A 138 ? 0.4718 0.4847 0.4925 -0.0684 0.0844  -0.0673 144 ASP   A O   
1068 C CB  . ASP   A 138 ? 0.4504 0.4598 0.4444 -0.0705 0.0642  -0.0509 144 ASP   A CB  
1069 C CG  . ASP   A 138 ? 0.4942 0.5007 0.4842 -0.0667 0.0562  -0.0462 144 ASP   A CG  
1070 O OD1 . ASP   A 138 ? 0.4950 0.5013 0.4976 -0.0561 0.0512  -0.0444 144 ASP   A OD1 
1071 O OD2 . ASP   A 138 ? 0.5212 0.5257 0.4946 -0.0751 0.0549  -0.0442 144 ASP   A OD2 
1072 N N   . GLU   A 139 ? 0.4826 0.5041 0.5024 -0.0694 0.0732  -0.0548 145 GLU   A N   
1073 C CA  . GLU   A 139 ? 0.5192 0.5439 0.5429 -0.0752 0.0838  -0.0611 145 GLU   A CA  
1074 C C   . GLU   A 139 ? 0.5318 0.5630 0.5719 -0.0698 0.0806  -0.0582 145 GLU   A C   
1075 O O   . GLU   A 139 ? 0.5500 0.5852 0.5933 -0.0753 0.0881  -0.0617 145 GLU   A O   
1076 C CB  . GLU   A 139 ? 0.5782 0.6020 0.5793 -0.0901 0.0877  -0.0601 145 GLU   A CB  
1077 C CG  . GLU   A 139 ? 0.6661 0.6917 0.6570 -0.0934 0.0768  -0.0483 145 GLU   A CG  
1078 C CD  . GLU   A 139 ? 0.7922 0.8147 0.7587 -0.1053 0.0746  -0.0439 145 GLU   A CD  
1079 O OE1 . GLU   A 139 ? 0.8224 0.8465 0.7777 -0.1137 0.0709  -0.0367 145 GLU   A OE1 
1080 O OE2 . GLU   A 139 ? 0.8371 0.8553 0.7957 -0.1069 0.0762  -0.0475 145 GLU   A OE2 
1081 N N1  . A1BN5 B .   ? 0.2728 0.2431 0.3230 0.0095  0.0114  -0.0285 201 A1BN5 A N1  
1082 C C4  . A1BN5 B .   ? 0.3268 0.3071 0.3521 0.0056  0.0351  -0.0345 201 A1BN5 A C4  
1083 C C5  . A1BN5 B .   ? 0.3077 0.2869 0.3403 0.0080  0.0310  -0.0330 201 A1BN5 A C5  
1084 C C6  . A1BN5 B .   ? 0.2972 0.2795 0.3285 0.0084  0.0226  -0.0277 201 A1BN5 A C6  
1085 C C7  . A1BN5 B .   ? 0.2828 0.2606 0.3160 0.0085  0.0148  -0.0277 201 A1BN5 A C7  
1086 C C8  . A1BN5 B .   ? 0.2678 0.2455 0.3117 0.0103  0.0131  -0.0258 201 A1BN5 A C8  
1087 C C10 . A1BN5 B .   ? 0.2655 0.2412 0.3266 0.0120  0.0101  -0.0221 201 A1BN5 A C10 
1088 C C13 . A1BN5 B .   ? 0.2595 0.2429 0.3149 0.0128  0.0115  -0.0195 201 A1BN5 A C13 
1089 O O1  . A1BN5 B .   ? 0.2791 0.2648 0.3622 0.0156  0.0073  -0.0079 201 A1BN5 A O1  
1090 C C12 . A1BN5 B .   ? 0.2614 0.2494 0.3357 0.0149  0.0074  -0.0099 201 A1BN5 A C12 
1091 N N2  . A1BN5 B .   ? 0.2308 0.2256 0.3038 0.0144  0.0053  -0.0054 201 A1BN5 A N2  
1092 C C11 . A1BN5 B .   ? 0.2547 0.2371 0.3184 0.0135  0.0098  -0.0174 201 A1BN5 A C11 
1093 C C9  . A1BN5 B .   ? 0.2840 0.2554 0.3254 0.0085  0.0127  -0.0300 201 A1BN5 A C9  
1094 O O   . A1BN5 B .   ? 0.2832 0.2579 0.3036 0.0052  0.0120  -0.0301 201 A1BN5 A O   
1095 N N   . A1BN5 B .   ? 0.2940 0.2757 0.3330 0.0102  0.0192  -0.0261 201 A1BN5 A N   
1096 C C1  . A1BN5 B .   ? 0.3050 0.2905 0.3281 0.0068  0.0183  -0.0243 201 A1BN5 A C1  
1097 C C   . A1BN5 B .   ? 0.2983 0.2864 0.3207 0.0070  0.0109  -0.0198 201 A1BN5 A C   
1098 C C3  . A1BN5 B .   ? 0.3213 0.3050 0.3381 0.0038  0.0303  -0.0304 201 A1BN5 A C3  
1099 C C2  . A1BN5 B .   ? 0.3136 0.2995 0.3297 0.0045  0.0220  -0.0254 201 A1BN5 A C2  
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